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HEADER    IMMUNE SYSTEM                           11-NOV-14   4WWK              
TITLE     CRYSTAL STRUCTURE OF HUMAN TCR ALPHA CHAIN-TRAV12-3, BETA CHAIN-TRBV6-
TITLE    2 5, ANTIGEN-PRESENTING MOLECULE CD1D, AND BETA-2-MICROGLOBULIN        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TCR ALPHA CHAIN-TRAV12-3;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TCR BETA CHAIN-TRBV6-5;                                    
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ANTIGEN-PRESENTING GLYCOPROTEIN CD1D;                      
COMPND  11 CHAIN: C;                                                            
COMPND  12 SYNONYM: R3G1;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND  16 CHAIN: D;                                                            
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: CD1D;                                                          
SOURCE  18 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL;                            
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  27 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL                             
KEYWDS    INNATE IMMUNITY, NKT, IMMUNE SYSTEM                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LE NOURS,T.PRAVEENA,D.G.PELLICCI,N.A.GHERARDIN,R.T.LIM,G.BESRA,     
AUTHOR   2 A.KESHIPEDDY,S.K.RICHARDSON,A.R.HOWELL,S.GRAS,D.I.GODFREY,           
AUTHOR   3 J.ROSSJOHN,A.P.ULDRICH                                               
REVDAT   5   29-JUL-20 4WWK    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   08-JAN-20 4WWK    1       REMARK                                   
REVDAT   3   04-APR-18 4WWK    1       JRNL                                     
REVDAT   2   20-SEP-17 4WWK    1       REMARK                                   
REVDAT   1   03-FEB-16 4WWK    0                                                
JRNL        AUTH   J.LE NOURS,T.PRAVEENA,D.G.PELLICCI,N.A.GHERARDIN,F.J.ROSS,   
JRNL        AUTH 2 R.T.LIM,G.S.BESRA,S.KESHIPEDDY,S.K.RICHARDSON,A.R.HOWELL,    
JRNL        AUTH 3 S.GRAS,D.I.GODFREY,J.ROSSJOHN,A.P.ULDRICH                    
JRNL        TITL   ATYPICAL NATURAL KILLER T-CELL RECEPTOR RECOGNITION OF       
JRNL        TITL 2 CD1D-LIPID ANTIGENS.                                         
JRNL        REF    NAT COMMUN                    V.   7 10570 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   26875526                                                     
JRNL        DOI    10.1038/NCOMMS10570                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19335                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.198                          
REMARK   3   R VALUE            (WORKING SET)  : 0.195                          
REMARK   3   FREE R VALUE                      : 0.256                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.210                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1007                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.10                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.27                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 93.00                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2729                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2245                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2566                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2202                   
REMARK   3   BIN FREE R VALUE                        : 0.2884                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.97                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 163                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5794                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 3                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.08200                                             
REMARK   3    B22 (A**2) : 2.20270                                              
REMARK   3    B33 (A**2) : -0.12080                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.576               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.441               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.895                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.810                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6044   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8280   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2610   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 117    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 919    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6044   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 822    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6154   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.98                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.20                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.60                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   25.1376   38.2692  364.4430           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1616 T22:    0.0647                                    
REMARK   3     T33:   -0.0654 T12:   -0.2312                                    
REMARK   3     T13:    0.0869 T23:    0.1591                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8134 L22:    0.0000                                    
REMARK   3     L33:    8.4003 L12:   -0.9266                                    
REMARK   3     L13:    3.0238 L23:   -1.2217                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0404 S12:   -0.9122 S13:   -0.2833                     
REMARK   3     S21:    0.2690 S22:    0.0017 S23:    0.3260                     
REMARK   3     S31:   -0.0682 S32:   -0.0366 S33:   -0.0421                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   43.3623   44.7899  358.9500           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3122 T22:   -0.0193                                    
REMARK   3     T33:   -0.1582 T12:   -0.1131                                    
REMARK   3     T13:   -0.1386 T23:    0.1400                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.5404 L22:    1.2958                                    
REMARK   3     L33:    5.7395 L12:   -0.1492                                    
REMARK   3     L13:    1.9960 L23:   -1.4882                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0935 S12:   -0.7778 S13:   -0.4553                     
REMARK   3     S21:    0.3844 S22:    0.0395 S23:   -0.3354                     
REMARK   3     S31:   -0.3197 S32:    0.8324 S33:   -0.1330                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   10.5112   43.1346  311.3960           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2231 T22:   -0.1956                                    
REMARK   3     T33:    0.1685 T12:    0.0700                                    
REMARK   3     T13:   -0.0384 T23:   -0.0592                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5915 L22:    2.1296                                    
REMARK   3     L33:    2.1644 L12:   -0.4155                                    
REMARK   3     L13:    0.3635 L23:   -0.0048                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2357 S12:    0.0670 S13:   -0.0669                     
REMARK   3     S21:   -0.3554 S22:   -0.2747 S23:    0.2590                     
REMARK   3     S31:   -0.1600 S32:   -0.3921 S33:    0.0389                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   18.1501   43.3402  293.7380           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0160 T22:   -0.2854                                    
REMARK   3     T33:    0.1407 T12:    0.2219                                    
REMARK   3     T13:    0.1125 T23:    0.0861                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8547 L22:    2.5697                                    
REMARK   3     L33:    6.5134 L12:    0.9605                                    
REMARK   3     L13:   -1.0189 L23:    0.6333                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2213 S12:    0.4612 S13:    0.1488                     
REMARK   3     S21:   -0.9880 S22:   -0.1883 S23:   -0.4727                     
REMARK   3     S31:   -0.8015 S32:    0.0765 S33:   -0.0331                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204387.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19363                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2PO6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG8000 0.1M CHES 9.5, PH 9.5,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.19000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      127.86000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.03500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      127.86000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.19000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.03500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     GLN A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASN A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     ILE A   210                                                      
REMARK 465     ILE A   211                                                      
REMARK 465     PRO A   212                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     ASP A   214                                                      
REMARK 465     THR A   215                                                      
REMARK 465     PHE A   216                                                      
REMARK 465     PHE A   217                                                      
REMARK 465     PRO A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     SER A   223                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ASN B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER C     0                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     SER D   -18                                                      
REMARK 465     ARG D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     VAL D   -15                                                      
REMARK 465     ALA D   -14                                                      
REMARK 465     LEU D   -13                                                      
REMARK 465     ALA D   -12                                                      
REMARK 465     VAL D   -11                                                      
REMARK 465     LEU D   -10                                                      
REMARK 465     ALA D    -9                                                      
REMARK 465     LEU D    -8                                                      
REMARK 465     LEU D    -7                                                      
REMARK 465     SER D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     SER D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     LEU D    -2                                                      
REMARK 465     GLU D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   5    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A  54    CG   SD   CE                                        
REMARK 470     GLU A  67    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  79    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  93    CG   OD1  OD2                                       
REMARK 470     LYS A 116    CG   CD   CE   NZ                                   
REMARK 470     ASP A 121    CG   OD1  OD2                                       
REMARK 470     ASN A 133    CG   OD1  ND2                                       
REMARK 470     VAL A 138    CG1  CG2                                            
REMARK 470     TYR A 139    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 140    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 141    CG   CD1  CD2                                       
REMARK 470     ARG A 142    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 143    CG   OD1  OD2                                       
REMARK 470     SER A 144    OG                                                  
REMARK 470     LYS A 145    CG   CD   CE   NZ                                   
REMARK 470     SER A 146    CB   OG                                             
REMARK 470     SER A 147    CB   OG                                             
REMARK 470     ASP A 148    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 149    CB   CG   CD   CE   NZ                              
REMARK 470     SER A 150    CB   OG                                             
REMARK 470     VAL A 151    CB   CG1  CG2                                       
REMARK 470     CYS A 152    CB   SG                                             
REMARK 470     LEU A 153    CG   CD1  CD2                                       
REMARK 470     PHE A 154    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 157    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 158    CG   OD1  OD2                                       
REMARK 470     GLN A 160    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 162    CG   OD1  ND2                                       
REMARK 470     VAL A 163    CG1  CG2                                            
REMARK 470     GLN A 165    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     ASP A 168    CG   OD1  OD2                                       
REMARK 470     SER A 169    OG                                                  
REMARK 470     ASP A 170    CG   OD1  OD2                                       
REMARK 470     VAL A 171    CG1  CG2                                            
REMARK 470     TYR A 172    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 173    CG1  CG2  CD1                                       
REMARK 470     ASP A 175    CG   OD1  OD2                                       
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     ARG A 182    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     ASN A 189    CG   OD1  ND2                                       
REMARK 470     TRP A 194    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 194    CZ3  CH2                                            
REMARK 470     ASN A 196    CG   OD1  ND2                                       
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     SER A 198    OG                                                  
REMARK 470     ASP A 199    CG   OD1  OD2                                       
REMARK 470     PHE A 200    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 204    CG   OD1  ND2                                       
REMARK 470     PHE A 206    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 207    CG   OD1  ND2                                       
REMARK 470     LYS B   9    CG   CD   CE   NZ                                   
REMARK 470     VAL B  12    CG1  CG2                                            
REMARK 470     LYS B  14    CG   CD   CE   NZ                                   
REMARK 470     SER B  18    OG                                                  
REMARK 470     MET B  48    CG   SD   CE                                        
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 124    CG1  CG2  CD1                                       
REMARK 470     GLU B 126    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 128    CG   CD1  CD2                                       
REMARK 470     LYS B 129    CG   CD   CE   NZ                                   
REMARK 470     ASN B 130    CG   OD1  ND2                                       
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 139    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 140    CG   CD   OE1  OE2                                  
REMARK 470     SER B 142    OG                                                  
REMARK 470     GLU B 143    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 145    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 146    CG1  CG2  CD1                                       
REMARK 470     SER B 147    OG                                                  
REMARK 470     HIS B 148    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 149    OG1  CG2                                            
REMARK 470     GLN B 150    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 151    CG   CD   CE   NZ                                   
REMARK 470     THR B 153    OG1  CG2                                            
REMARK 470     LEU B 154    CG   CD1  CD2                                       
REMARK 470     VAL B 155    CG1  CG2                                            
REMARK 470     LEU B 157    CG   CD1  CD2                                       
REMARK 470     THR B 159    OG1  CG2                                            
REMARK 470     LYS B 175    CG   CD   CE   NZ                                   
REMARK 470     GLU B 176    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 184    CG   OD1  OD2                                       
REMARK 470     LEU B 188    CG   CD1  CD2                                       
REMARK 470     LYS B 189    CG   CD   CE   NZ                                   
REMARK 470     GLU B 190    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 191    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 194    CG   CD1  CD2                                       
REMARK 470     ASN B 195    CG   OD1  ND2                                       
REMARK 470     ASP B 196    CG   OD1  OD2                                       
REMARK 470     ARG B 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 201    CG   CD1  CD2                                       
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 207    CG1  CG2                                            
REMARK 470     SER B 208    OG                                                  
REMARK 470     THR B 210    OG1  CG2                                            
REMARK 470     PHE B 211    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TRP B 212    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 212    CZ3  CH2                                            
REMARK 470     ASN B 214    CG   OD1  ND2                                       
REMARK 470     ARG B 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 217    CG   OD1  ND2                                       
REMARK 470     PHE B 219    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 222    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 228    CG   CD1  CD2                                       
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 231    CG   OD1  ND2                                       
REMARK 470     GLU B 233    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 236    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 237    CG   OD1  OD2                                       
REMARK 470     ARG B 238    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 240    CG   CD   CE   NZ                                   
REMARK 470     GLU B 249    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 255    CG   OD1  OD2                                       
REMARK 470     ASP C  45    CG   OD1  OD2                                       
REMARK 470     GLU C  64    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 108    CG   OD1  ND2                                       
REMARK 470     LYS C 121    CG   CD   CE   NZ                                   
REMARK 470     GLU C 132    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 135    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 136    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 152    CG   CD   CE   NZ                                   
REMARK 470     LYS C 178    CG   CD   CE   NZ                                   
REMARK 470     LYS C 182    CG   CD   CE   NZ                                   
REMARK 470     LYS C 183    CG   CD   CE   NZ                                   
REMARK 470     LYS C 186    CG   CD   CE   NZ                                   
REMARK 470     LYS C 188    CG   CD   CE   NZ                                   
REMARK 470     ARG C 193    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 219    CG   CD   CE   NZ                                   
REMARK 470     GLN C 225    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 255    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 262    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 271    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  19    CG   CD   CE   NZ                                   
REMARK 470     LYS D  41    CG   CD   CE   NZ                                   
REMARK 470     GLU D  44    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  47    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  75    CG   CD   CE   NZ                                   
REMARK 470     GLU D  77    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  91    CG   CD   CE   NZ                                   
REMARK 470     LYS D  94    CG   CD   CE   NZ                                   
REMARK 470     ARG D  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D  98    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A   8     -163.75   -100.02                                   
REMARK 500    ASP A  68       79.91   -159.47                                   
REMARK 500    ALA A 100     -177.58   -172.37                                   
REMARK 500    GLN A 132     -124.44     65.00                                   
REMARK 500    SER A 144      -76.42    -71.87                                   
REMARK 500    ASN A 196       55.58   -110.51                                   
REMARK 500    ASP A 199       84.73     62.40                                   
REMARK 500    LEU B  92      -77.39    -73.37                                   
REMARK 500    ASP B 196       49.36    -95.78                                   
REMARK 500    ASN C  20     -160.67   -160.95                                   
REMARK 500    SER C  22      -73.78    -92.82                                   
REMARK 500    ARG C  25      100.87   -160.65                                   
REMARK 500    PRO C  52       -9.37    -59.54                                   
REMARK 500    ASN C 108      -58.23   -151.35                                   
REMARK 500    PHE C 114       84.84   -155.92                                   
REMARK 500    ILE C 123      -45.86   -132.46                                   
REMARK 500    LEU C 249      117.94   -160.46                                   
REMARK 500    GLN D   2      -46.44   -144.95                                   
REMARK 500    PRO D  32     -174.51    -69.26                                   
REMARK 500    ASP D  59        3.86    -61.71                                   
REMARK 500    TRP D  60       -0.37     75.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4WWK A    0   223  PDB    4WWK     4WWK             0    223             
DBREF  4WWK B    0   255  PDB    4WWK     4WWK             0    255             
DBREF  4WWK C    3   277  UNP    P15813   CD1D_HUMAN      21    295             
DBREF  4WWK D  -19    99  UNP    P61769   B2MG_HUMAN       1    119             
SEQADV 4WWK SER C    0  UNP  P15813              EXPRESSION TAG                 
SEQADV 4WWK PRO C    1  UNP  P15813              EXPRESSION TAG                 
SEQADV 4WWK GLY C    2  UNP  P15813              EXPRESSION TAG                 
SEQRES   1 A  209  MET GLN LYS GLU VAL GLU GLN ASP PRO GLY PRO LEU SER          
SEQRES   2 A  209  VAL PRO GLU GLY ALA ILE VAL SER LEU ASN CYS THR TYR          
SEQRES   3 A  209  SER ASN SER ALA PHE GLN TYR PHE MET TRP TYR ARG GLN          
SEQRES   4 A  209  TYR SER ARG LYS GLY PRO GLU LEU LEU MET TYR THR TYR          
SEQRES   5 A  209  SER SER GLY ASN LYS GLU ASP GLY ARG PHE THR ALA GLN          
SEQRES   6 A  209  VAL ASP LYS SER SER LYS TYR ILE SER LEU PHE ILE ARG          
SEQRES   7 A  209  ASP SER GLN PRO SER ASP SER ALA THR TYR LEU CYS ALA          
SEQRES   8 A  209  MET SER GLY ASP LEU ASN THR ASN ALA GLY LYS SER THR          
SEQRES   9 A  209  PHE GLY ASP GLY THR THR LEU THR VAL LYS PRO ASN ILE          
SEQRES  10 A  209  GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER          
SEQRES  11 A  209  LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE          
SEQRES  12 A  209  ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP          
SEQRES  13 A  209  VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER          
SEQRES  14 A  209  MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN          
SEQRES  15 A  209  LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER          
SEQRES  16 A  209  ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER          
SEQRES  17 A  209  SER                                                          
SEQRES   1 B  243  MET ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL          
SEQRES   2 B  243  LEU LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN          
SEQRES   3 B  243  ASP MET ASN HIS GLU TYR MET SER TRP TYR ARG GLN ASP          
SEQRES   4 B  243  PRO GLY MET GLY LEU ARG LEU ILE HIS TYR SER VAL GLY          
SEQRES   5 B  243  ALA GLY ILE THR ASP GLN GLY GLU VAL PRO ASN GLY TYR          
SEQRES   6 B  243  ASN VAL SER ARG SER THR THR GLU ASP PHE PRO LEU ARG          
SEQRES   7 B  243  LEU LEU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE          
SEQRES   8 B  243  CYS ALA SER SER GLN GLY PRO PHE GLN PRO GLN HIS PHE          
SEQRES   9 B  243  GLY ASP GLY THR ARG LEU SER ILE LEU GLU ASP LEU LYS          
SEQRES  10 B  243  ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER          
SEQRES  11 B  243  GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL          
SEQRES  12 B  243  CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU          
SEQRES  13 B  243  SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL          
SEQRES  14 B  243  CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU          
SEQRES  15 B  243  ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL          
SEQRES  16 B  243  SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG          
SEQRES  17 B  243  CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU          
SEQRES  18 B  243  TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL          
SEQRES  19 B  243  SER ALA GLU ALA TRP GLY ARG ALA ASP                          
SEQRES   1 C  278  SER PRO GLY VAL PRO GLN ARG LEU PHE PRO LEU ARG CYS          
SEQRES   2 C  278  LEU GLN ILE SER SER PHE ALA ASN SER SER TRP THR ARG          
SEQRES   3 C  278  THR ASP GLY LEU ALA TRP LEU GLY GLU LEU GLN THR HIS          
SEQRES   4 C  278  SER TRP SER ASN ASP SER ASP THR VAL ARG SER LEU LYS          
SEQRES   5 C  278  PRO TRP SER GLN GLY THR PHE SER ASP GLN GLN TRP GLU          
SEQRES   6 C  278  THR LEU GLN HIS ILE PHE ARG VAL TYR ARG SER SER PHE          
SEQRES   7 C  278  THR ARG ASP VAL LYS GLU PHE ALA LYS MET LEU ARG LEU          
SEQRES   8 C  278  SER TYR PRO LEU GLU LEU GLN VAL SER ALA GLY CYS GLU          
SEQRES   9 C  278  VAL HIS PRO GLY ASN ALA SER ASN ASN PHE PHE HIS VAL          
SEQRES  10 C  278  ALA PHE GLN GLY LYS ASP ILE LEU SER PHE GLN GLY THR          
SEQRES  11 C  278  SER TRP GLU PRO THR GLN GLU ALA PRO LEU TRP VAL ASN          
SEQRES  12 C  278  LEU ALA ILE GLN VAL LEU ASN GLN ASP LYS TRP THR ARG          
SEQRES  13 C  278  GLU THR VAL GLN TRP LEU LEU ASN GLY THR CYS PRO GLN          
SEQRES  14 C  278  PHE VAL SER GLY LEU LEU GLU SER GLY LYS SER GLU LEU          
SEQRES  15 C  278  LYS LYS GLN VAL LYS PRO LYS ALA TRP LEU SER ARG GLY          
SEQRES  16 C  278  PRO SER PRO GLY PRO GLY ARG LEU LEU LEU VAL CYS HIS          
SEQRES  17 C  278  VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL LYS TRP          
SEQRES  18 C  278  MET ARG GLY GLU GLN GLU GLN GLN GLY THR GLN PRO GLY          
SEQRES  19 C  278  ASP ILE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU ARG          
SEQRES  20 C  278  ALA THR LEU ASP VAL VAL ALA GLY GLU ALA ALA GLY LEU          
SEQRES  21 C  278  SER CYS ARG VAL LYS HIS SER SER LEU GLU GLY GLN ASP          
SEQRES  22 C  278  ILE VAL LEU TYR TRP                                          
SEQRES   1 D  119  MET SER ARG SER VAL ALA LEU ALA VAL LEU ALA LEU LEU          
SEQRES   2 D  119  SER LEU SER GLY LEU GLU ALA ILE GLN ARG THR PRO LYS          
SEQRES   3 D  119  ILE GLN VAL TYR SER ARG HIS PRO ALA GLU ASN GLY LYS          
SEQRES   4 D  119  SER ASN PHE LEU ASN CYS TYR VAL SER GLY PHE HIS PRO          
SEQRES   5 D  119  SER ASP ILE GLU VAL ASP LEU LEU LYS ASN GLY GLU ARG          
SEQRES   6 D  119  ILE GLU LYS VAL GLU HIS SER ASP LEU SER PHE SER LYS          
SEQRES   7 D  119  ASP TRP SER PHE TYR LEU LEU TYR TYR THR GLU PHE THR          
SEQRES   8 D  119  PRO THR GLU LYS ASP GLU TYR ALA CYS ARG VAL ASN HIS          
SEQRES   9 D  119  VAL THR LEU SER GLN PRO LYS ILE VAL LYS TRP ASP ARG          
SEQRES  10 D  119  ASP MET                                                      
HET    NAG  C 301      14                                                       
HET    NAG  C 302      14                                                       
HET    JLS  C 303      58                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     JLS (15Z)-N-[(2S,3S,4R)-1-(ALPHA-D-GALACTOPYRANOSYLOXY)-3,           
HETNAM   2 JLS  4-DIHYDROXYOCTADECAN-2-YL]TETRACOS-15-ENAMIDE                   
HETSYN     JLS PBS-44                                                           
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   7  JLS    C48 H93 N O9                                                 
FORMUL   8  HOH   *3(H2 O)                                                      
HELIX    1 AA1 GLN A   95  SER A   99  5                                   5    
HELIX    2 AA2 THR A  112  LYS A  116  5                                   5    
HELIX    3 AA3 ALA A  201  PHE A  206  1                                   6    
HELIX    4 AA4 ALA B   95  THR B   99  5                                   5    
HELIX    5 AA5 ASP B  127  VAL B  131  5                                   5    
HELIX    6 AA6 SER B  142  THR B  149  1                                   8    
HELIX    7 AA7 ALA B  209  ASN B  214  1                                   6    
HELIX    8 AA8 SER C   59  ARG C   89  1                                  31    
HELIX    9 AA9 PRO C  138  ASP C  151  1                                  14    
HELIX   10 AB1 ASP C  151  GLY C  164  1                                  14    
HELIX   11 AB2 GLY C  164  GLY C  177  1                                  14    
HELIX   12 AB3 GLY C  177  LYS C  182  1                                   6    
SHEET    1 AA1 5 LEU A  11  PRO A  14  0                                        
SHEET    2 AA1 5 THR A 123  LYS A 128  1  O  THR A 126   N  VAL A  13           
SHEET    3 AA1 5 ALA A 100  SER A 107 -1  N  TYR A 102   O  THR A 123           
SHEET    4 AA1 5 TYR A  32  GLN A  44 -1  N  MET A  40   O  ALA A 105           
SHEET    5 AA1 5 GLU A  51  THR A  56 -1  O  THR A  56   N  PHE A  39           
SHEET    1 AA2 4 LEU A  11  PRO A  14  0                                        
SHEET    2 AA2 4 THR A 123  LYS A 128  1  O  THR A 126   N  VAL A  13           
SHEET    3 AA2 4 ALA A 100  SER A 107 -1  N  TYR A 102   O  THR A 123           
SHEET    4 AA2 4 THR A 118  PHE A 119 -1  O  THR A 118   N  MET A 106           
SHEET    1 AA3 4 VAL A  19  THR A  24  0                                        
SHEET    2 AA3 4 TYR A  86  ILE A  91 -1  O  LEU A  89   N  LEU A  21           
SHEET    3 AA3 4 PHE A  76  ASP A  81 -1  N  GLN A  79   O  SER A  88           
SHEET    4 AA3 4 GLU A  67  ASP A  68 -1  N  ASP A  68   O  PHE A  76           
SHEET    1 AA4 2 CYS A 177  ASP A 180  0                                        
SHEET    2 AA4 2 LYS A 187  SER A 190 -1  O  SER A 190   N  CYS A 177           
SHEET    1 AA5 4 VAL B   4  THR B   7  0                                        
SHEET    2 AA5 4 MET B  19  GLN B  25 -1  O  GLN B  22   N  THR B   7           
SHEET    3 AA5 4 LEU B  89  LEU B  91 -1  O  LEU B  89   N  LEU B  21           
SHEET    4 AA5 4 TYR B  76  VAL B  78 -1  N  ASN B  77   O  ARG B  90           
SHEET    1 AA6 6 PHE B  10  LYS B  14  0                                        
SHEET    2 AA6 6 THR B 120  LEU B 125  1  O  SER B 123   N  LEU B  13           
SHEET    3 AA6 6 VAL B 101  SER B 107 -1  N  TYR B 102   O  THR B 120           
SHEET    4 AA6 6 TYR B  31  ASP B  45 -1  N  TYR B  42   O  PHE B 103           
SHEET    5 AA6 6 GLY B  49  GLY B  58 -1  O  SER B  56   N  MET B  39           
SHEET    6 AA6 6 ILE B  61  GLN B  68 -1  O  ASP B  67   N  TYR B  55           
SHEET    1 AA7 4 PHE B  10  LYS B  14  0                                        
SHEET    2 AA7 4 THR B 120  LEU B 125  1  O  SER B 123   N  LEU B  13           
SHEET    3 AA7 4 VAL B 101  SER B 107 -1  N  TYR B 102   O  THR B 120           
SHEET    4 AA7 4 HIS B 115  PHE B 116 -1  O  HIS B 115   N  SER B 106           
SHEET    1 AA8 4 GLU B 135  PHE B 139  0                                        
SHEET    2 AA8 4 LYS B 151  PHE B 161 -1  O  THR B 159   N  GLU B 135           
SHEET    3 AA8 4 TYR B 199  SER B 208 -1  O  SER B 203   N  CYS B 156           
SHEET    4 AA8 4 VAL B 181  THR B 183 -1  N  CYS B 182   O  ARG B 204           
SHEET    1 AA9 4 GLU B 135  PHE B 139  0                                        
SHEET    2 AA9 4 LYS B 151  PHE B 161 -1  O  THR B 159   N  GLU B 135           
SHEET    3 AA9 4 TYR B 199  SER B 208 -1  O  SER B 203   N  CYS B 156           
SHEET    4 AA9 4 LEU B 188  LYS B 189 -1  N  LEU B 188   O  ALA B 200           
SHEET    1 AB1 4 LYS B 175  VAL B 177  0                                        
SHEET    2 AB1 4 VAL B 166  VAL B 172 -1  N  VAL B 172   O  LYS B 175           
SHEET    3 AB1 4 HIS B 218  PHE B 225 -1  O  ARG B 220   N  TRP B 171           
SHEET    4 AB1 4 ILE B 245  TRP B 251 -1  O  VAL B 246   N  VAL B 223           
SHEET    1 AB2 8 ARG C  48  SER C  49  0                                        
SHEET    2 AB2 8 LEU C  35  TRP C  40 -1  N  SER C  39   O  ARG C  48           
SHEET    3 AB2 8 ARG C  25  LEU C  32 -1  N  GLY C  28   O  TRP C  40           
SHEET    4 AB2 8 LEU C  10  PHE C  18 -1  N  LEU C  13   O  LEU C  29           
SHEET    5 AB2 8 LEU C  94  VAL C 104 -1  O  LEU C  96   N  SER C  16           
SHEET    6 AB2 8 SER C 110  PHE C 118 -1  O  HIS C 115   N  SER C  99           
SHEET    7 AB2 8 LYS C 121  GLN C 127 -1  O  LYS C 121   N  PHE C 118           
SHEET    8 AB2 8 SER C 130  PRO C 133 -1  O  GLU C 132   N  SER C 125           
SHEET    1 AB3 4 LYS C 188  ARG C 193  0                                        
SHEET    2 AB3 4 ARG C 201  SER C 209 -1  O  HIS C 207   N  TRP C 190           
SHEET    3 AB3 4 TRP C 243  VAL C 252 -1  O  LEU C 245   N  VAL C 208           
SHEET    4 AB3 4 LEU C 236  PRO C 237 -1  N  LEU C 236   O  TYR C 244           
SHEET    1 AB4 3 VAL C 216  MET C 221  0                                        
SHEET    2 AB4 3 SER C 260  HIS C 265 -1  O  SER C 260   N  MET C 221           
SHEET    3 AB4 3 ILE C 273  TYR C 276 -1  O  LEU C 275   N  CYS C 261           
SHEET    1 AB5 4 LYS D   6  SER D  11  0                                        
SHEET    2 AB5 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3 AB5 4 PHE D  62  PHE D  70 -1  O  PHE D  62   N  PHE D  30           
SHEET    4 AB5 4 GLU D  50  HIS D  51 -1  N  GLU D  50   O  TYR D  67           
SHEET    1 AB6 4 LYS D   6  SER D  11  0                                        
SHEET    2 AB6 4 ASN D  21  PHE D  30 -1  O  ASN D  24   N  TYR D  10           
SHEET    3 AB6 4 PHE D  62  PHE D  70 -1  O  PHE D  62   N  PHE D  30           
SHEET    4 AB6 4 SER D  55  PHE D  56 -1  N  SER D  55   O  TYR D  63           
SHEET    1 AB7 4 GLU D  44  ARG D  45  0                                        
SHEET    2 AB7 4 GLU D  36  LYS D  41 -1  N  LYS D  41   O  GLU D  44           
SHEET    3 AB7 4 TYR D  78  ASN D  83 -1  O  ALA D  79   N  LEU D  40           
SHEET    4 AB7 4 LYS D  91  LYS D  94 -1  O  LYS D  91   N  VAL D  82           
SSBOND   1 CYS A   23    CYS A  104                          1555   1555  2.04  
SSBOND   2 CYS B   23    CYS B  104                          1555   1555  2.03  
SSBOND   3 CYS C  102    CYS C  166                          1555   1555  2.05  
SSBOND   4 CYS D   25    CYS D   80                          1555   1555  2.05  
LINK         ND2 ASN C  20                 C1  NAG C 301     1555   1555  1.43  
LINK         ND2 ASN C  42                 C1  NAG C 302     1555   1555  1.44  
CISPEP   1 SER A   26    ASN A   27          0         4.12                     
CISPEP   2 THR B    7    PRO B    8          0        -4.20                     
CISPEP   3 TYR B  162    PRO B  163          0         1.19                     
CISPEP   4 TYR C   92    PRO C   93          0         2.72                     
CISPEP   5 PRO C  106    GLY C  107          0         1.30                     
CISPEP   6 TYR C  212    PRO C  213          0         5.59                     
CISPEP   7 HIS D   31    PRO D   32          0         0.97                     
CRYST1   56.380   76.070  255.720  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017737  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013146  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003911        0.00000                         
ATOM      1  N   GLU A   5      16.004  50.748 349.882  1.00 55.13           N  
ANISOU    1  N   GLU A   5     7758   5494   7695   -671    168   -599       N  
ATOM      2  CA  GLU A   5      15.680  49.373 350.270  1.00 54.10           C  
ANISOU    2  CA  GLU A   5     7172   5702   7681   -735    374   -461       C  
ATOM      3  C   GLU A   5      16.571  48.883 351.439  1.00 57.79           C  
ANISOU    3  C   GLU A   5     7643   6238   8075   -947    367   -372       C  
ATOM      4  O   GLU A   5      17.637  48.300 351.196  1.00 54.94           O  
ANISOU    4  O   GLU A   5     7236   5808   7829  -1257    310   -242       O  
ATOM      5  CB  GLU A   5      15.822  48.442 349.055  1.00 53.12           C  
ANISOU    5  CB  GLU A   5     6734   5597   7853   -926    431   -318       C  
ATOM      6  N   GLN A   6      16.117  49.093 352.705  1.00 57.45           N  
ANISOU    6  N   GLN A   6     7627   6392   7809   -751    427   -440       N  
ATOM      7  CA  GLN A   6      16.922  48.733 353.883  1.00 58.35           C  
ANISOU    7  CA  GLN A   6     7755   6591   7825   -920    422   -369       C  
ATOM      8  C   GLN A   6      16.222  47.831 354.946  1.00 63.18           C  
ANISOU    8  C   GLN A   6     8039   7611   8357   -816    608   -280       C  
ATOM      9  O   GLN A   6      15.052  47.459 354.810  1.00 62.52           O  
ANISOU    9  O   GLN A   6     7709   7788   8258   -619    735   -267       O  
ATOM     10  CB  GLN A   6      17.464  50.006 354.566  1.00 62.22           C  
ANISOU   10  CB  GLN A   6     8736   6854   8052   -856    221   -541       C  
ATOM     11  CG  GLN A   6      18.761  50.517 353.924  1.00 80.04           C  
ANISOU   11  CG  GLN A   6    11256   8784  10370  -1216      8   -488       C  
ATOM     12  CD  GLN A   6      19.317  51.817 354.478  1.00106.28           C  
ANISOU   12  CD  GLN A   6    15124  11825  13432  -1251   -256   -626       C  
ATOM     13  OE1 GLN A   6      20.066  52.535 353.796  1.00100.43           O  
ANISOU   13  OE1 GLN A   6    14679  10790  12690  -1514   -483   -597       O  
ATOM     14  NE2 GLN A   6      18.994  52.147 355.726  1.00103.98           N  
ANISOU   14  NE2 GLN A   6    14990  11625  12892  -1013   -261   -764       N  
ATOM     15  N   ASP A   7      17.029  47.450 355.973  1.00 60.72           N  
ANISOU   15  N   ASP A   7     7706   7384   7981   -991    613   -189       N  
ATOM     16  CA  ASP A   7      16.741  46.623 357.150  1.00 62.04           C  
ANISOU   16  CA  ASP A   7     7603   7918   8050   -974    754    -64       C  
ATOM     17  C   ASP A   7      17.039  47.440 358.451  1.00 69.55           C  
ANISOU   17  C   ASP A   7     8799   8945   8683   -820    695   -202       C  
ATOM     18  O   ASP A   7      17.657  48.503 358.336  1.00 70.02           O  
ANISOU   18  O   ASP A   7     9257   8697   8649   -828    515   -361       O  
ATOM     19  CB  ASP A   7      17.541  45.284 357.108  1.00 62.15           C  
ANISOU   19  CB  ASP A   7     7382   7954   8281  -1308    797    183       C  
ATOM     20  CG  ASP A   7      18.932  45.248 356.457  1.00 70.58           C  
ANISOU   20  CG  ASP A   7     8588   8758   9473  -1564    673    220       C  
ATOM     21  OD1 ASP A   7      19.451  46.324 356.089  1.00 72.82           O  
ANISOU   21  OD1 ASP A   7     9168   8830   9672  -1582    535     86       O  
ATOM     22  OD2 ASP A   7      19.503  44.136 356.332  1.00 71.78           O  
ANISOU   22  OD2 ASP A   7     8561   8941   9772  -1742    694    396       O  
ATOM     23  N   PRO A   8      16.632  47.003 359.682  1.00 68.58           N  
ANISOU   23  N   PRO A   8     8469   9220   8366   -692    815   -143       N  
ATOM     24  CA  PRO A   8      16.849  47.852 360.875  1.00 71.03           C  
ANISOU   24  CA  PRO A   8     9038   9604   8346   -485    739   -314       C  
ATOM     25  C   PRO A   8      18.060  47.502 361.768  1.00 74.44           C  
ANISOU   25  C   PRO A   8     9501  10030   8751   -757    710   -214       C  
ATOM     26  O   PRO A   8      18.968  46.783 361.361  1.00 71.46           O  
ANISOU   26  O   PRO A   8     9029   9521   8603  -1105    708    -41       O  
ATOM     27  CB  PRO A   8      15.546  47.661 361.658  1.00 75.46           C  
ANISOU   27  CB  PRO A   8     9311  10707   8652   -129    892   -310       C  
ATOM     28  CG  PRO A   8      15.032  46.289 361.231  1.00 78.54           C  
ANISOU   28  CG  PRO A   8     9220  11344   9278   -361   1057    -13       C  
ATOM     29  CD  PRO A   8      15.826  45.817 360.037  1.00 70.61           C  
ANISOU   29  CD  PRO A   8     8269   9903   8655   -718    996     82       C  
ATOM     30  N   GLY A   9      18.038  48.046 362.987  1.00 74.18           N  
ANISOU   30  N   GLY A   9     9606  10177   8400   -543    678   -342       N  
ATOM     31  CA  GLY A   9      19.046  47.913 364.023  1.00 74.72           C  
ANISOU   31  CA  GLY A   9     9731  10302   8358   -719    643   -294       C  
ATOM     32  C   GLY A   9      19.086  46.636 364.843  1.00 79.16           C  
ANISOU   32  C   GLY A   9     9866  11263   8950   -854    831    -27       C  
ATOM     33  O   GLY A   9      18.436  45.643 364.516  1.00 77.79           O  
ANISOU   33  O   GLY A   9     9333  11285   8937   -915    976    181       O  
ATOM     34  N   PRO A  10      20.015  46.667 365.866  1.00 76.97           N  
ANISOU   34  N   PRO A  10     9676  11042   8527   -971    786    -16       N  
ATOM     35  CA  PRO A  10      20.384  45.477 366.677  1.00 76.13           C  
ANISOU   35  CA  PRO A  10     9235  11243   8448  -1153    925    251       C  
ATOM     36  C   PRO A  10      19.325  44.515 367.217  1.00 80.34           C  
ANISOU   36  C   PRO A  10     9342  12234   8948  -1059   1114    467       C  
ATOM     37  O   PRO A  10      18.219  44.902 367.601  1.00 82.05           O  
ANISOU   37  O   PRO A  10     9460  12758   8957   -744   1173    382       O  
ATOM     38  CB  PRO A  10      21.128  46.078 367.882  1.00 79.73           C  
ANISOU   38  CB  PRO A  10     9888  11793   8611  -1104    844    128       C  
ATOM     39  CG  PRO A  10      21.095  47.574 367.698  1.00 85.94           C  
ANISOU   39  CG  PRO A  10    11158  12272   9223   -918    631   -206       C  
ATOM     40  CD  PRO A  10      20.887  47.798 366.238  1.00 79.85           C  
ANISOU   40  CD  PRO A  10    10489  11150   8702   -992    572   -233       C  
ATOM     41  N   LEU A  11      19.758  43.232 367.315  1.00 75.23           N  
ANISOU   41  N   LEU A  11     8452  11662   8471  -1344   1188    767       N  
ATOM     42  CA  LEU A  11      19.002  42.061 367.774  1.00 75.90           C  
ANISOU   42  CA  LEU A  11     8154  12121   8563  -1417   1319   1072       C  
ATOM     43  C   LEU A  11      19.852  41.136 368.651  1.00 78.90           C  
ANISOU   43  C   LEU A  11     8431  12622   8927  -1623   1346   1304       C  
ATOM     44  O   LEU A  11      21.022  40.897 368.342  1.00 76.97           O  
ANISOU   44  O   LEU A  11     8339  12088   8817  -1793   1272   1315       O  
ATOM     45  CB  LEU A  11      18.465  41.264 366.562  1.00 74.60           C  
ANISOU   45  CB  LEU A  11     7864  11777   8705  -1593   1320   1237       C  
ATOM     46  CG  LEU A  11      17.446  41.988 365.688  1.00 79.84           C  
ANISOU   46  CG  LEU A  11     8546  12412   9378  -1391   1321   1063       C  
ATOM     47  CD1 LEU A  11      17.073  41.148 364.485  1.00 78.36           C  
ANISOU   47  CD1 LEU A  11     8253  12017   9502  -1602   1301   1224       C  
ATOM     48  CD2 LEU A  11      16.200  42.359 366.481  1.00 85.81           C  
ANISOU   48  CD2 LEU A  11     9070  13731   9802  -1102   1422   1049       C  
ATOM     49  N   SER A  12      19.251  40.603 369.729  1.00 76.88           N  
ANISOU   49  N   SER A  12     7892  12844   8477  -1596   1448   1507       N  
ATOM     50  CA  SER A  12      19.892  39.680 370.670  1.00 76.97           C  
ANISOU   50  CA  SER A  12     7779  13027   8438  -1772   1479   1765       C  
ATOM     51  C   SER A  12      18.949  38.503 370.928  1.00 81.79           C  
ANISOU   51  C   SER A  12     8057  13951   9067  -1953   1537   2150       C  
ATOM     52  O   SER A  12      17.883  38.684 371.523  1.00 84.41           O  
ANISOU   52  O   SER A  12     8124  14790   9158  -1824   1624   2216       O  
ATOM     53  CB  SER A  12      20.257  40.397 371.968  1.00 82.49           C  
ANISOU   53  CB  SER A  12     8503  14045   8796  -1567   1514   1620       C  
ATOM     54  OG  SER A  12      21.018  41.569 371.722  1.00 89.86           O  
ANISOU   54  OG  SER A  12     9786  14666   9692  -1463   1411   1283       O  
ATOM     55  N   VAL A  13      19.316  37.309 370.430  1.00 76.14           N  
ANISOU   55  N   VAL A  13     7372  12944   8612  -2249   1461   2410       N  
ATOM     56  CA  VAL A  13      18.488  36.099 370.506  1.00 77.34           C  
ANISOU   56  CA  VAL A  13     7304  13258   8823  -2522   1438   2812       C  
ATOM     57  C   VAL A  13      19.244  34.967 371.254  1.00 81.41           C  
ANISOU   57  C   VAL A  13     7855  13726   9350  -2735   1378   3113       C  
ATOM     58  O   VAL A  13      20.402  34.724 370.927  1.00 78.78           O  
ANISOU   58  O   VAL A  13     7777  12995   9160  -2729   1298   3029       O  
ATOM     59  CB  VAL A  13      18.069  35.675 369.061  1.00 79.71           C  
ANISOU   59  CB  VAL A  13     7696  13159   9430  -2669   1335   2833       C  
ATOM     60  CG1 VAL A  13      17.383  34.315 369.031  1.00 81.69           C  
ANISOU   60  CG1 VAL A  13     7820  13451   9769  -3033   1236   3267       C  
ATOM     61  CG2 VAL A  13      17.182  36.731 368.403  1.00 79.23           C  
ANISOU   61  CG2 VAL A  13     7566  13212   9324  -2452   1402   2578       C  
ATOM     62  N   PRO A  14      18.619  34.240 372.225  1.00 81.18           N  
ANISOU   62  N   PRO A  14     7572  14124   9151  -2919   1400   3482       N  
ATOM     63  CA  PRO A  14      19.339  33.142 372.902  1.00 81.93           C  
ANISOU   63  CA  PRO A  14     7749  14127   9254  -3113   1316   3780       C  
ATOM     64  C   PRO A  14      19.534  31.918 371.996  1.00 85.59           C  
ANISOU   64  C   PRO A  14     8473  14032  10016  -3371   1099   3988       C  
ATOM     65  O   PRO A  14      18.823  31.775 371.000  1.00 85.01           O  
ANISOU   65  O   PRO A  14     8435  13743  10124  -3477   1021   3983       O  
ATOM     66  CB  PRO A  14      18.441  32.806 374.102  1.00 87.48           C  
ANISOU   66  CB  PRO A  14     8084  15484   9670  -3263   1387   4136       C  
ATOM     67  CG  PRO A  14      17.396  33.885 374.151  1.00 92.84           C  
ANISOU   67  CG  PRO A  14     8473  16669  10132  -3043   1534   3954       C  
ATOM     68  CD  PRO A  14      17.247  34.365 372.752  1.00 85.85           C  
ANISOU   68  CD  PRO A  14     7774  15348   9496  -2955   1491   3670       C  
ATOM     69  N   GLU A  15      20.497  31.037 372.355  1.00 82.33           N  
ANISOU   69  N   GLU A  15     8265  13388   9629  -3438    985   4159       N  
ATOM     70  CA  GLU A  15      20.891  29.823 371.622  1.00 82.24           C  
ANISOU   70  CA  GLU A  15     8593  12810   9844  -3588    733   4331       C  
ATOM     71  C   GLU A  15      19.713  28.914 371.245  1.00 88.76           C  
ANISOU   71  C   GLU A  15     9406  13554  10766  -3981    557   4695       C  
ATOM     72  O   GLU A  15      18.778  28.748 372.031  1.00 91.68           O  
ANISOU   72  O   GLU A  15     9480  14398  10958  -4231    604   5005       O  
ATOM     73  CB  GLU A  15      21.907  29.006 372.440  1.00 84.74           C  
ANISOU   73  CB  GLU A  15     9088  13046  10065  -3559    648   4505       C  
ATOM     74  CG  GLU A  15      22.878  28.205 371.587  1.00 94.38           C  
ANISOU   74  CG  GLU A  15    10732  13669  11458  -3436    422   4447       C  
ATOM     75  CD  GLU A  15      23.738  27.210 372.340  1.00117.33           C  
ANISOU   75  CD  GLU A  15    13856  16472  14251  -3406    285   4680       C  
ATOM     76  OE1 GLU A  15      24.565  27.645 373.173  1.00110.24           O  
ANISOU   76  OE1 GLU A  15    12853  15868  13166  -3208    434   4581       O  
ATOM     77  OE2 GLU A  15      23.611  25.994 372.070  1.00114.55           O  
ANISOU   77  OE2 GLU A  15    13814  15723  13987  -3573      4   4957       O  
ATOM     78  N   GLY A  16      19.798  28.339 370.044  1.00 84.26           N  
ANISOU   78  N   GLY A  16     9151  12418  10447  -4035    341   4662       N  
ATOM     79  CA  GLY A  16      18.830  27.400 369.484  1.00 86.77           C  
ANISOU   79  CA  GLY A  16     9565  12517  10888  -4431    100   4981       C  
ATOM     80  C   GLY A  16      17.439  27.937 369.217  1.00 91.18           C  
ANISOU   80  C   GLY A  16     9757  13475  11414  -4624    209   5028       C  
ATOM     81  O   GLY A  16      16.477  27.163 369.198  1.00 94.00           O  
ANISOU   81  O   GLY A  16    10056  13900  11760  -5060     40   5412       O  
ATOM     82  N   ALA A  17      17.320  29.257 368.997  1.00 84.89           N  
ANISOU   82  N   ALA A  17     8726  12953  10575  -4309    466   4652       N  
ATOM     83  CA  ALA A  17      16.038  29.902 368.721  1.00 85.40           C  
ANISOU   83  CA  ALA A  17     8437  13446  10564  -4374    590   4636       C  
ATOM     84  C   ALA A  17      15.988  30.422 367.285  1.00 86.03           C  
ANISOU   84  C   ALA A  17     8662  13144  10883  -4200    574   4292       C  
ATOM     85  O   ALA A  17      17.013  30.859 366.755  1.00 82.33           O  
ANISOU   85  O   ALA A  17     8441  12294  10549  -3898    589   3955       O  
ATOM     86  CB  ALA A  17      15.796  31.033 369.705  1.00 86.29           C  
ANISOU   86  CB  ALA A  17     8181  14234  10372  -4105    875   4490       C  
ATOM     87  N   ILE A  18      14.793  30.361 366.656  1.00 83.73           N  
ANISOU   87  N   ILE A  18     8189  13008  10618  -4408    538   4404       N  
ATOM     88  CA  ILE A  18      14.559  30.795 365.274  1.00 80.96           C  
ANISOU   88  CA  ILE A  18     7933  12349  10479  -4282    517   4123       C  
ATOM     89  C   ILE A  18      14.669  32.326 365.187  1.00 81.98           C  
ANISOU   89  C   ILE A  18     7919  12717  10513  -3829    777   3693       C  
ATOM     90  O   ILE A  18      13.958  33.046 365.894  1.00 83.22           O  
ANISOU   90  O   ILE A  18     7739  13481  10399  -3719    956   3695       O  
ATOM     91  CB  ILE A  18      13.211  30.251 364.716  1.00 86.73           C  
ANISOU   91  CB  ILE A  18     8489  13236  11228  -4675    390   4409       C  
ATOM     92  CG1 ILE A  18      13.282  28.723 364.499  1.00 89.87           C  
ANISOU   92  CG1 ILE A  18     9200  13176  11770  -5138     38   4788       C  
ATOM     93  CG2 ILE A  18      12.799  30.951 363.417  1.00 84.79           C  
ANISOU   93  CG2 ILE A  18     8247  12825  11144  -4494    428   4098       C  
ATOM     94  CD1 ILE A  18      12.630  27.881 365.596  1.00102.90           C  
ANISOU   94  CD1 ILE A  18    10635  15273  13190  -5618    -54   5329       C  
ATOM     95  N   VAL A  19      15.584  32.801 364.320  1.00 74.57           N  
ANISOU   95  N   VAL A  19     7259  11306   9769  -3562    766   3337       N  
ATOM     96  CA  VAL A  19      15.863  34.220 364.097  1.00 71.76           C  
ANISOU   96  CA  VAL A  19     6890  11020   9354  -3179    938   2931       C  
ATOM     97  C   VAL A  19      15.256  34.666 362.767  1.00 73.58           C  
ANISOU   97  C   VAL A  19     7125  11088   9743  -3110    923   2749       C  
ATOM     98  O   VAL A  19      15.546  34.073 361.727  1.00 71.83           O  
ANISOU   98  O   VAL A  19     7103  10419   9772  -3213    765   2750       O  
ATOM     99  CB  VAL A  19      17.382  34.540 364.142  1.00 73.14           C  
ANISOU   99  CB  VAL A  19     7340  10868   9584  -2974    928   2699       C  
ATOM    100  CG1 VAL A  19      17.616  36.042 364.268  1.00 71.52           C  
ANISOU  100  CG1 VAL A  19     7132  10801   9242  -2659   1074   2345       C  
ATOM    101  CG2 VAL A  19      18.084  33.789 365.271  1.00 74.27           C  
ANISOU  101  CG2 VAL A  19     7519  11084   9615  -3073    898   2916       C  
ATOM    102  N   SER A  20      14.442  35.728 362.802  1.00 70.28           N  
ANISOU  102  N   SER A  20     6508  11041   9156  -2890   1076   2576       N  
ATOM    103  CA  SER A  20      13.809  36.283 361.609  1.00 69.03           C  
ANISOU  103  CA  SER A  20     6336  10786   9106  -2779   1082   2391       C  
ATOM    104  C   SER A  20      14.409  37.656 361.259  1.00 69.72           C  
ANISOU  104  C   SER A  20     6614  10696   9179  -2405   1153   1980       C  
ATOM    105  O   SER A  20      14.163  38.645 361.956  1.00 70.62           O  
ANISOU  105  O   SER A  20     6664  11136   9034  -2136   1268   1821       O  
ATOM    106  CB  SER A  20      12.297  36.383 361.797  1.00 75.96           C  
ANISOU  106  CB  SER A  20     6837  12256   9769  -2820   1164   2549       C  
ATOM    107  OG  SER A  20      11.677  37.010 360.686  1.00 85.29           O  
ANISOU  107  OG  SER A  20     7995  13373  11037  -2691   1174   2371       O  
ATOM    108  N   LEU A  21      15.212  37.700 360.187  1.00 62.15           N  
ANISOU  108  N   LEU A  21     5911   9231   8473  -2391   1056   1820       N  
ATOM    109  CA  LEU A  21      15.833  38.927 359.684  1.00 59.12           C  
ANISOU  109  CA  LEU A  21     5735   8628   8099  -2135   1072   1485       C  
ATOM    110  C   LEU A  21      15.186  39.272 358.362  1.00 61.47           C  
ANISOU  110  C   LEU A  21     6031   8777   8545  -2068   1048   1363       C  
ATOM    111  O   LEU A  21      15.173  38.427 357.465  1.00 60.14           O  
ANISOU  111  O   LEU A  21     5875   8371   8605  -2239    949   1466       O  
ATOM    112  CB  LEU A  21      17.351  38.768 359.516  1.00 56.81           C  
ANISOU  112  CB  LEU A  21     5683   7982   7922  -2180    979   1428       C  
ATOM    113  CG  LEU A  21      18.139  38.428 360.758  1.00 62.02           C  
ANISOU  113  CG  LEU A  21     6359   8772   8435  -2234    996   1536       C  
ATOM    114  CD1 LEU A  21      18.552  36.979 360.739  1.00 62.38           C  
ANISOU  114  CD1 LEU A  21     6425   8660   8616  -2436    889   1784       C  
ATOM    115  CD2 LEU A  21      19.365  39.295 360.861  1.00 63.18           C  
ANISOU  115  CD2 LEU A  21     6706   8799   8500  -2129    977   1327       C  
ATOM    116  N   ASN A  22      14.626  40.483 358.228  1.00 57.99           N  
ANISOU  116  N   ASN A  22     5602   8472   7962  -1798   1119   1141       N  
ATOM    117  CA  ASN A  22      13.960  40.822 356.973  1.00 56.84           C  
ANISOU  117  CA  ASN A  22     5441   8220   7936  -1712   1105   1030       C  
ATOM    118  C   ASN A  22      14.398  42.168 356.371  1.00 56.65           C  
ANISOU  118  C   ASN A  22     5687   7945   7893  -1461   1075    722       C  
ATOM    119  O   ASN A  22      14.956  43.029 357.056  1.00 55.94           O  
ANISOU  119  O   ASN A  22     5788   7844   7623  -1313   1069    573       O  
ATOM    120  CB  ASN A  22      12.425  40.774 357.123  1.00 62.60           C  
ANISOU  120  CB  ASN A  22     5855   9440   8492  -1643   1199   1130       C  
ATOM    121  CG  ASN A  22      11.834  41.490 358.316  1.00 94.28           C  
ANISOU  121  CG  ASN A  22     9760  13939  12124  -1355   1310   1060       C  
ATOM    122  OD1 ASN A  22      12.532  42.099 359.142  1.00 91.73           O  
ANISOU  122  OD1 ASN A  22     9621  13573  11658  -1215   1313    933       O  
ATOM    123  ND2 ASN A  22      10.515  41.413 358.432  1.00 88.37           N  
ANISOU  123  ND2 ASN A  22     8694  13717  11168  -1249   1394   1146       N  
ATOM    124  N   CYS A  23      14.164  42.291 355.055  1.00 50.68           N  
ANISOU  124  N   CYS A  23     4965   6968   7322  -1445   1030    643       N  
ATOM    125  CA  CYS A  23      14.425  43.453 354.217  1.00 49.52           C  
ANISOU  125  CA  CYS A  23     5064   6564   7188  -1259    974    399       C  
ATOM    126  C   CYS A  23      13.162  43.801 353.444  1.00 52.91           C  
ANISOU  126  C   CYS A  23     5373   7123   7607  -1072   1020    327       C  
ATOM    127  O   CYS A  23      12.442  42.905 353.003  1.00 52.35           O  
ANISOU  127  O   CYS A  23     5056   7166   7667  -1210   1044    477       O  
ATOM    128  CB  CYS A  23      15.593  43.193 353.269  1.00 47.72           C  
ANISOU  128  CB  CYS A  23     4984   5957   7192  -1436    858    398       C  
ATOM    129  SG  CYS A  23      17.212  43.117 354.078  1.00 51.20           S  
ANISOU  129  SG  CYS A  23     5571   6305   7578  -1605    794    457       S  
ATOM    130  N   THR A  24      12.894  45.097 353.278  1.00 49.33           N  
ANISOU  130  N   THR A  24     5122   6642   6981   -758   1006     98       N  
ATOM    131  CA  THR A  24      11.741  45.583 352.521  1.00 49.56           C  
ANISOU  131  CA  THR A  24     5070   6803   6957   -507   1044     -2       C  
ATOM    132  C   THR A  24      12.271  46.439 351.388  1.00 51.40           C  
ANISOU  132  C   THR A  24     5616   6598   7316   -448    925   -174       C  
ATOM    133  O   THR A  24      13.242  47.173 351.594  1.00 50.71           O  
ANISOU  133  O   THR A  24     5865   6220   7181   -463    811   -277       O  
ATOM    134  CB  THR A  24      10.756  46.346 353.425  1.00 59.75           C  
ANISOU  134  CB  THR A  24     6321   8522   7859   -101   1118   -117       C  
ATOM    135  OG1 THR A  24      11.453  47.370 354.137  1.00 61.11           O  
ANISOU  135  OG1 THR A  24     6883   8501   7836     91   1026   -309       O  
ATOM    136  CG2 THR A  24      10.026  45.437 354.401  1.00 59.16           C  
ANISOU  136  CG2 THR A  24     5829   9016   7632   -183   1246    110       C  
ATOM    137  N   TYR A  25      11.672  46.335 350.187  1.00 46.48           N  
ANISOU  137  N   TYR A  25     4876   5941   6843   -421    934   -182       N  
ATOM    138  CA  TYR A  25      12.150  47.134 349.066  1.00 44.46           C  
ANISOU  138  CA  TYR A  25     4888   5306   6700   -379    818   -314       C  
ATOM    139  C   TYR A  25      11.056  47.986 348.429  1.00 50.78           C  
ANISOU  139  C   TYR A  25     5729   6192   7372    -16    836   -470       C  
ATOM    140  O   TYR A  25      11.209  48.424 347.288  1.00 49.74           O  
ANISOU  140  O   TYR A  25     5713   5813   7374     -6    763   -530       O  
ATOM    141  CB  TYR A  25      12.883  46.290 348.023  1.00 42.34           C  
ANISOU  141  CB  TYR A  25     4514   4823   6749   -688    769   -193       C  
ATOM    142  CG  TYR A  25      12.075  45.286 347.229  1.00 42.76           C  
ANISOU  142  CG  TYR A  25     4237   5032   6977   -764    832    -87       C  
ATOM    143  CD1 TYR A  25      11.879  43.990 347.702  1.00 44.74           C  
ANISOU  143  CD1 TYR A  25     4241   5462   7296   -979    874    103       C  
ATOM    144  CD2 TYR A  25      11.676  45.565 345.926  1.00 42.55           C  
ANISOU  144  CD2 TYR A  25     4182   4919   7066   -675    810   -157       C  
ATOM    145  CE1 TYR A  25      11.222  43.029 346.933  1.00 44.96           C  
ANISOU  145  CE1 TYR A  25     4030   5568   7485  -1112    871    214       C  
ATOM    146  CE2 TYR A  25      11.027  44.611 345.144  1.00 42.97           C  
ANISOU  146  CE2 TYR A  25     3958   5085   7283   -778    835    -63       C  
ATOM    147  CZ  TYR A  25      10.791  43.347 345.654  1.00 49.36           C  
ANISOU  147  CZ  TYR A  25     4556   6054   8146  -1008    853    121       C  
ATOM    148  OH  TYR A  25      10.132  42.422 344.879  1.00 47.29           O  
ANISOU  148  OH  TYR A  25     4079   5861   8030  -1150    826    219       O  
ATOM    149  N   SER A  26       9.995  48.298 349.188  1.00 50.45           N  
ANISOU  149  N   SER A  26     5603   6534   7030    320    922   -540       N  
ATOM    150  CA  SER A  26       8.966  49.210 348.701  1.00 52.39           C  
ANISOU  150  CA  SER A  26     5914   6919   7074    761    930   -711       C  
ATOM    151  C   SER A  26       9.533  50.631 348.816  1.00 57.11           C  
ANISOU  151  C   SER A  26     7095   7100   7502   1020    743   -945       C  
ATOM    152  O   SER A  26      10.044  50.979 349.882  1.00 59.06           O  
ANISOU  152  O   SER A  26     7586   7279   7573   1064    673  -1007       O  
ATOM    153  CB  SER A  26       7.668  49.052 349.490  1.00 59.65           C  
ANISOU  153  CB  SER A  26     6499   8499   7668   1065   1077   -690       C  
ATOM    154  OG  SER A  26       6.708  50.026 349.110  1.00 71.17           O  
ANISOU  154  OG  SER A  26     8013  10154   8875   1567   1083   -869       O  
ATOM    155  N   ASN A  27       9.547  51.424 347.733  1.00 51.67           N  
ANISOU  155  N   ASN A  27     6669   6094   6870   1144    630  -1057       N  
ATOM    156  CA  ASN A  27       8.983  51.087 346.433  1.00 49.12           C  
ANISOU  156  CA  ASN A  27     6083   5836   6745   1113    700  -1002       C  
ATOM    157  C   ASN A  27      10.066  51.099 345.336  1.00 46.57           C  
ANISOU  157  C   ASN A  27     5904   5049   6743    739    578   -929       C  
ATOM    158  O   ASN A  27      10.562  52.155 344.927  1.00 46.60           O  
ANISOU  158  O   ASN A  27     6346   4656   6705    781    392  -1025       O  
ATOM    159  CB  ASN A  27       7.822  52.030 346.089  1.00 55.74           C  
ANISOU  159  CB  ASN A  27     7043   6821   7313   1666    692  -1193       C  
ATOM    160  CG  ASN A  27       8.127  53.493 346.300  1.00 87.69           C  
ANISOU  160  CG  ASN A  27    11747  10452  11120   1993    462  -1419       C  
ATOM    161  OD1 ASN A  27       8.124  53.996 347.430  1.00 85.43           O  
ANISOU  161  OD1 ASN A  27    11718  10204  10540   2247    395  -1543       O  
ATOM    162  ND2 ASN A  27       8.432  54.196 345.217  1.00 79.99           N  
ANISOU  162  ND2 ASN A  27    11084   9056  10252   1983    309  -1470       N  
ATOM    163  N   SER A  28      10.440  49.891 344.895  1.00 37.79           N  
ANISOU  163  N   SER A  28     4428   4012   5917    372    659   -747       N  
ATOM    164  CA  SER A  28      11.406  49.573 343.836  1.00 33.56           C  
ANISOU  164  CA  SER A  28     3889   3198   5665     45    574   -652       C  
ATOM    165  C   SER A  28      11.001  48.236 343.224  1.00 33.96           C  
ANISOU  165  C   SER A  28     3497   3461   5946   -121    684   -522       C  
ATOM    166  O   SER A  28      10.176  47.540 343.813  1.00 35.19           O  
ANISOU  166  O   SER A  28     3378   3942   6049    -98    804   -461       O  
ATOM    167  CB  SER A  28      12.827  49.520 344.388  1.00 35.38           C  
ANISOU  167  CB  SER A  28     4299   3216   5929   -263    468   -573       C  
ATOM    168  OG  SER A  28      13.207  50.754 344.974  1.00 44.44           O  
ANISOU  168  OG  SER A  28     5909   4114   6864   -172    313   -683       O  
ATOM    169  N   ALA A  29      11.524  47.879 342.046  1.00 26.48           N  
ANISOU  169  N   ALA A  29     2485   2353   5223   -285    622   -474       N  
ATOM    170  CA  ALA A  29      11.126  46.623 341.407  1.00 23.99           C  
ANISOU  170  CA  ALA A  29     1824   2177   5113   -416    674   -380       C  
ATOM    171  C   ALA A  29      12.332  45.707 341.195  1.00 23.60           C  
ANISOU  171  C   ALA A  29     1739   1986   5242   -692    587   -271       C  
ATOM    172  O   ALA A  29      12.738  45.438 340.054  1.00 22.69           O  
ANISOU  172  O   ALA A  29     1635   1805   5180   -598    505   -273       O  
ATOM    173  CB  ALA A  29      10.415  46.904 340.090  1.00 24.44           C  
ANISOU  173  CB  ALA A  29     1796   2250   5241   -260    677   -451       C  
ATOM    174  N   PHE A  30      12.891  45.216 342.312  1.00 19.54           N  
ANISOU  174  N   PHE A  30     1392   1528   4503   -572    557   -217       N  
ATOM    175  CA  PHE A  30      14.036  44.322 342.295  1.00 18.98           C  
ANISOU  175  CA  PHE A  30     1373   1441   4397   -553    457   -134       C  
ATOM    176  C   PHE A  30      13.629  42.923 341.833  1.00 23.03           C  
ANISOU  176  C   PHE A  30     1621   1927   5204   -826    452    -42       C  
ATOM    177  O   PHE A  30      12.453  42.556 341.934  1.00 24.35           O  
ANISOU  177  O   PHE A  30     1638   2201   5414   -889    517    -12       O  
ATOM    178  CB  PHE A  30      14.714  44.289 343.659  1.00 20.39           C  
ANISOU  178  CB  PHE A  30     1588   1626   4533   -782    473    -68       C  
ATOM    179  CG  PHE A  30      15.408  45.591 343.990  1.00 21.37           C  
ANISOU  179  CG  PHE A  30     1891   1650   4578   -894    443   -113       C  
ATOM    180  CD1 PHE A  30      16.498  46.025 343.247  1.00 23.37           C  
ANISOU  180  CD1 PHE A  30     2212   1779   4888  -1070    331    -81       C  
ATOM    181  CD2 PHE A  30      15.002  46.357 345.072  1.00 23.38           C  
ANISOU  181  CD2 PHE A  30     2259   1831   4795  -1025    504   -162       C  
ATOM    182  CE1 PHE A  30      17.138  47.225 343.556  1.00 24.83           C  
ANISOU  182  CE1 PHE A  30     2656   1816   4963  -1225    239    -96       C  
ATOM    183  CE2 PHE A  30      15.651  47.543 345.390  1.00 27.08           C  
ANISOU  183  CE2 PHE A  30     3051   2136   5102  -1036    398   -226       C  
ATOM    184  CZ  PHE A  30      16.707  47.976 344.624  1.00 24.92           C  
ANISOU  184  CZ  PHE A  30     2895   1717   4858  -1211    257   -180       C  
ATOM    185  N   GLN A  31      14.587  42.162 341.279  1.00 20.32           N  
ANISOU  185  N   GLN A  31     1420   1562   4738   -546    314    -25       N  
ATOM    186  CA  GLN A  31      14.300  40.850 340.710  1.00 20.88           C  
ANISOU  186  CA  GLN A  31     1413   1588   4932   -558    231     25       C  
ATOM    187  C   GLN A  31      15.123  39.731 341.337  1.00 24.99           C  
ANISOU  187  C   GLN A  31     1836   2010   5648   -936    150    143       C  
ATOM    188  O   GLN A  31      14.622  38.604 341.460  1.00 25.98           O  
ANISOU  188  O   GLN A  31     1931   2075   5865  -1064     72    224       O  
ATOM    189  CB  GLN A  31      14.528  40.865 339.186  1.00 20.93           C  
ANISOU  189  CB  GLN A  31     1373   1532   5048   -449    168    -42       C  
ATOM    190  CG  GLN A  31      13.708  41.916 338.427  1.00 23.83           C  
ANISOU  190  CG  GLN A  31     1589   1889   5575   -576    260   -129       C  
ATOM    191  CD  GLN A  31      12.214  41.677 338.433  1.00 31.91           C  
ANISOU  191  CD  GLN A  31     2228   2988   6908   -992    353   -112       C  
ATOM    192  OE1 GLN A  31      11.732  40.547 338.412  1.00 26.75           O  
ANISOU  192  OE1 GLN A  31     1495   2328   6341  -1113    283    -47       O  
ATOM    193  NE2 GLN A  31      11.446  42.747 338.423  1.00 25.43           N  
ANISOU  193  NE2 GLN A  31     1391   2284   5987   -867    472   -175       N  
ATOM    194  N   TYR A  32      16.375  40.024 341.713  1.00 21.93           N  
ANISOU  194  N   TYR A  32     1619   1710   5004   -680    113    139       N  
ATOM    195  CA  TYR A  32      17.276  39.022 342.290  1.00 22.16           C  
ANISOU  195  CA  TYR A  32     1687   1727   5006   -725     16    224       C  
ATOM    196  C   TYR A  32      17.709  39.487 343.675  1.00 23.50           C  
ANISOU  196  C   TYR A  32     1884   1945   5099   -930     98    282       C  
ATOM    197  O   TYR A  32      18.046  40.659 343.858  1.00 22.77           O  
ANISOU  197  O   TYR A  32     1844   1925   4883   -908    163    233       O  
ATOM    198  CB  TYR A  32      18.477  38.755 341.364  1.00 22.76           C  
ANISOU  198  CB  TYR A  32     1723   1795   5131   -701    -91    205       C  
ATOM    199  CG  TYR A  32      18.130  38.757 339.887  1.00 23.90           C  
ANISOU  199  CG  TYR A  32     1754   1871   5457   -678   -143    121       C  
ATOM    200  CD1 TYR A  32      18.139  39.939 339.149  1.00 24.69           C  
ANISOU  200  CD1 TYR A  32     1795   2037   5548   -666    -78     63       C  
ATOM    201  CD2 TYR A  32      17.820  37.574 339.221  1.00 25.09           C  
ANISOU  201  CD2 TYR A  32     1876   1871   5785   -690   -294     94       C  
ATOM    202  CE1 TYR A  32      17.812  39.950 337.797  1.00 24.85           C  
ANISOU  202  CE1 TYR A  32     1743   2037   5661   -544   -122    -14       C  
ATOM    203  CE2 TYR A  32      17.510  37.570 337.862  1.00 25.79           C  
ANISOU  203  CE2 TYR A  32     1878   1925   5997   -606   -360     -7       C  
ATOM    204  CZ  TYR A  32      17.514  38.762 337.153  1.00 33.86           C  
ANISOU  204  CZ  TYR A  32     2702   3052   7112   -730   -272    -71       C  
ATOM    205  OH  TYR A  32      17.222  38.780 335.812  1.00 39.75           O  
ANISOU  205  OH  TYR A  32     3354   3821   7929   -579   -334   -167       O  
ATOM    206  N   PHE A  39      17.651  38.581 344.656  1.00 20.96           N  
ANISOU  206  N   PHE A  39     1671   1693   4601   -774     40    358       N  
ATOM    207  CA  PHE A  39      17.899  38.915 346.050  1.00 21.21           C  
ANISOU  207  CA  PHE A  39     1754   1812   4493   -865    107    404       C  
ATOM    208  C   PHE A  39      19.007  38.066 346.676  1.00 25.63           C  
ANISOU  208  C   PHE A  39     2259   2266   5215  -1232     67    543       C  
ATOM    209  O   PHE A  39      19.032  36.841 346.532  1.00 25.85           O  
ANISOU  209  O   PHE A  39     2317   2181   5324  -1230    -63    609       O  
ATOM    210  CB  PHE A  39      16.594  38.779 346.844  1.00 23.24           C  
ANISOU  210  CB  PHE A  39     1926   2077   4827  -1092    194    484       C  
ATOM    211  CG  PHE A  39      15.387  39.373 346.151  1.00 23.88           C  
ANISOU  211  CG  PHE A  39     1903   2166   5004  -1121    281    421       C  
ATOM    212  CD1 PHE A  39      15.066  40.715 346.306  1.00 25.73           C  
ANISOU  212  CD1 PHE A  39     2051   2439   5285  -1266    441    349       C  
ATOM    213  CD2 PHE A  39      14.585  38.595 345.324  1.00 25.31           C  
ANISOU  213  CD2 PHE A  39     1978   2273   5368  -1232    226    468       C  
ATOM    214  CE1 PHE A  39      13.958  41.265 345.656  1.00 26.33           C  
ANISOU  214  CE1 PHE A  39     2015   2564   5424  -1244    519    282       C  
ATOM    215  CE2 PHE A  39      13.485  39.148 344.667  1.00 27.22           C  
ANISOU  215  CE2 PHE A  39     2038   2557   5749  -1358    328    425       C  
ATOM    216  CZ  PHE A  39      13.166  40.474 344.853  1.00 25.61           C  
ANISOU  216  CZ  PHE A  39     1854   2472   5402  -1197    456    311       C  
ATOM    217  N   MET A  40      19.921  38.751 347.381  1.00 24.14           N  
ANISOU  217  N   MET A  40     2148   2234   4791  -1144     97    525       N  
ATOM    218  CA  MET A  40      21.101  38.185 348.033  1.00 24.64           C  
ANISOU  218  CA  MET A  40     2229   2348   4786  -1221     47    616       C  
ATOM    219  C   MET A  40      21.030  38.307 349.546  1.00 26.71           C  
ANISOU  219  C   MET A  40     2478   2649   5019  -1474    156    711       C  
ATOM    220  O   MET A  40      20.294  39.149 350.056  1.00 26.29           O  
ANISOU  220  O   MET A  40     2435   2649   4907  -1496    258    658       O  
ATOM    221  CB  MET A  40      22.371  38.920 347.540  1.00 26.11           C  
ANISOU  221  CB  MET A  40     2344   2645   4930  -1335     39    608       C  
ATOM    222  CG  MET A  40      22.859  38.478 346.180  1.00 28.99           C  
ANISOU  222  CG  MET A  40     2548   2982   5484  -1399    -46    602       C  
ATOM    223  SD  MET A  40      22.108  39.438 344.844  1.00 33.14           S  
ANISOU  223  SD  MET A  40     3007   3447   6135  -1398    -19    490       S  
ATOM    224  CE  MET A  40      23.469  40.491 344.398  1.00 30.24           C  
ANISOU  224  CE  MET A  40     2563   3387   5541  -1463    -61    524       C  
ATOM    225  N   TRP A  41      21.829  37.488 350.255  1.00 23.84           N  
ANISOU  225  N   TRP A  41     2205   2381   4473  -1311     58    774       N  
ATOM    226  CA  TRP A  41      22.001  37.506 351.708  1.00 24.46           C  
ANISOU  226  CA  TRP A  41     2300   2562   4433  -1428    121    854       C  
ATOM    227  C   TRP A  41      23.474  37.281 352.005  1.00 27.07           C  
ANISOU  227  C   TRP A  41     2557   2960   4769  -1650    136    969       C  
ATOM    228  O   TRP A  41      24.128  36.471 351.343  1.00 26.37           O  
ANISOU  228  O   TRP A  41     2468   2837   4713  -1552     24   1000       O  
ATOM    229  CB  TRP A  41      21.098  36.491 352.431  1.00 25.24           C  
ANISOU  229  CB  TRP A  41     2404   2600   4584  -1491     97    982       C  
ATOM    230  CG  TRP A  41      19.707  37.003 352.701  1.00 26.71           C  
ANISOU  230  CG  TRP A  41     2507   2817   4825  -1615    216    987       C  
ATOM    231  CD1 TRP A  41      18.559  36.660 352.041  1.00 29.16           C  
ANISOU  231  CD1 TRP A  41     2714   3006   5359  -1800    237   1050       C  
ATOM    232  CD2 TRP A  41      19.332  37.988 353.674  1.00 26.89           C  
ANISOU  232  CD2 TRP A  41     2488   3012   4718  -1665    358    953       C  
ATOM    233  NE1 TRP A  41      17.494  37.375 352.539  1.00 29.26           N  
ANISOU  233  NE1 TRP A  41     2624   3197   5295  -1830    365   1038       N  
ATOM    234  CE2 TRP A  41      17.941  38.203 353.540  1.00 30.20           C  
ANISOU  234  CE2 TRP A  41     2711   3452   5311  -1915    505   1026       C  
ATOM    235  CE3 TRP A  41      20.040  38.718 354.648  1.00 27.60           C  
ANISOU  235  CE3 TRP A  41     2580   3217   4690  -1769    455    948       C  
ATOM    236  CZ2 TRP A  41      17.242  39.105 354.352  1.00 30.29           C  
ANISOU  236  CZ2 TRP A  41     2633   3688   5189  -1919    655    994       C  
ATOM    237  CZ3 TRP A  41      19.346  39.609 355.452  1.00 29.14           C  
ANISOU  237  CZ3 TRP A  41     2687   3553   4831  -1890    623    937       C  
ATOM    238  CH2 TRP A  41      17.965  39.792 355.306  1.00 30.25           C  
ANISOU  238  CH2 TRP A  41     2684   3778   5031  -1921    721    951       C  
ATOM    239  N   TYR A  42      24.015  38.065 352.939  1.00 25.33           N  
ANISOU  239  N   TYR A  42     2385   2945   4294  -1614    169    932       N  
ATOM    240  CA  TYR A  42      25.428  38.040 353.301  1.00 25.14           C  
ANISOU  240  CA  TYR A  42     2323   3134   4095  -1653    138    998       C  
ATOM    241  C   TYR A  42      25.628  37.996 354.796  1.00 29.26           C  
ANISOU  241  C   TYR A  42     2776   3746   4598  -1945    283   1144       C  
ATOM    242  O   TYR A  42      24.796  38.482 355.562  1.00 28.47           O  
ANISOU  242  O   TYR A  42     2713   3608   4497  -2013    371   1115       O  
ATOM    243  CB  TYR A  42      26.155  39.279 352.741  1.00 25.54           C  
ANISOU  243  CB  TYR A  42     2340   3344   4019  -1749    121    937       C  
ATOM    244  CG  TYR A  42      26.271  39.326 351.234  1.00 26.19           C  
ANISOU  244  CG  TYR A  42     2328   3405   4216  -1714     65    908       C  
ATOM    245  CD1 TYR A  42      27.326  38.703 350.577  1.00 28.39           C  
ANISOU  245  CD1 TYR A  42     2432   3908   4446  -1661     -6    981       C  
ATOM    246  CD2 TYR A  42      25.370  40.059 350.469  1.00 26.15           C  
ANISOU  246  CD2 TYR A  42     2379   3226   4330  -1704     79    800       C  
ATOM    247  CE1 TYR A  42      27.441  38.745 349.185  1.00 29.01           C  
ANISOU  247  CE1 TYR A  42     2424   4038   4560  -1537    -87    932       C  
ATOM    248  CE2 TYR A  42      25.481  40.121 349.078  1.00 26.21           C  
ANISOU  248  CE2 TYR A  42     2302   3241   4417  -1644     17    770       C  
ATOM    249  CZ  TYR A  42      26.519  39.461 348.440  1.00 31.48           C  
ANISOU  249  CZ  TYR A  42     2765   4138   5058  -1624    -55    845       C  
ATOM    250  OH  TYR A  42      26.636  39.520 347.072  1.00 28.75           O  
ANISOU  250  OH  TYR A  42     2319   3865   4740  -1504   -131    803       O  
ATOM    251  N   ARG A  43      26.762  37.432 355.200  1.00 28.42           N  
ANISOU  251  N   ARG A  43     2645   3840   4312  -1870    229   1227       N  
ATOM    252  CA  ARG A  43      27.207  37.334 356.583  1.00 29.98           C  
ANISOU  252  CA  ARG A  43     2845   4207   4341  -1935    287   1317       C  
ATOM    253  C   ARG A  43      28.569  38.014 356.683  1.00 36.32           C  
ANISOU  253  C   ARG A  43     3569   5356   4876  -1987    256   1319       C  
ATOM    254  O   ARG A  43      29.410  37.853 355.789  1.00 35.72           O  
ANISOU  254  O   ARG A  43     3410   5462   4701  -1864    161   1329       O  
ATOM    255  CB  ARG A  43      27.261  35.863 357.027  1.00 30.54           C  
ANISOU  255  CB  ARG A  43     2976   4199   4427  -1791    226   1452       C  
ATOM    256  CG  ARG A  43      27.568  35.661 358.503  1.00 39.65           C  
ANISOU  256  CG  ARG A  43     4127   5516   5422  -1854    293   1566       C  
ATOM    257  CD  ARG A  43      27.246  34.256 358.968  1.00 51.20           C  
ANISOU  257  CD  ARG A  43     5703   6803   6947  -1776    218   1726       C  
ATOM    258  NE  ARG A  43      27.976  33.232 358.215  1.00 57.50           N  
ANISOU  258  NE  ARG A  43     6611   7536   7702  -1501     36   1744       N  
ATOM    259  CZ  ARG A  43      27.758  31.925 358.322  1.00 69.65           C  
ANISOU  259  CZ  ARG A  43     8349   8820   9294  -1390   -116   1864       C  
ATOM    260  NH1 ARG A  43      26.832  31.464 359.159  1.00 53.20           N  
ANISOU  260  NH1 ARG A  43     6336   6559   7317  -1601   -100   2020       N  
ATOM    261  NH2 ARG A  43      28.458  31.069 357.590  1.00 56.47           N  
ANISOU  261  NH2 ARG A  43     6826   7086   7542  -1062   -312   1838       N  
ATOM    262  N   GLN A  44      28.775  38.808 357.740  1.00 35.19           N  
ANISOU  262  N   GLN A  44     3443   5344   4585  -2173    321   1313       N  
ATOM    263  CA  GLN A  44      30.050  39.493 357.924  1.00 36.41           C  
ANISOU  263  CA  GLN A  44     3530   5845   4460  -2307    268   1342       C  
ATOM    264  C   GLN A  44      30.480  39.451 359.389  1.00 42.80           C  
ANISOU  264  C   GLN A  44     4342   6840   5080  -2377    326   1406       C  
ATOM    265  O   GLN A  44      29.850  40.067 360.257  1.00 41.84           O  
ANISOU  265  O   GLN A  44     4322   6603   4971  -2489    394   1345       O  
ATOM    266  CB  GLN A  44      29.995  40.936 357.398  1.00 37.32           C  
ANISOU  266  CB  GLN A  44     3720   5906   4552  -2546    215   1248       C  
ATOM    267  CG  GLN A  44      31.369  41.589 357.313  1.00 47.32           C  
ANISOU  267  CG  GLN A  44     4907   7555   5516  -2767    105   1326       C  
ATOM    268  CD  GLN A  44      31.298  43.029 356.895  1.00 66.33           C  
ANISOU  268  CD  GLN A  44     7469   9838   7895  -3059      0   1261       C  
ATOM    269  OE1 GLN A  44      30.396  43.782 357.284  1.00 63.29           O  
ANISOU  269  OE1 GLN A  44     7318   9125   7604  -3121     15   1132       O  
ATOM    270  NE2 GLN A  44      32.274  43.453 356.114  1.00 59.00           N  
ANISOU  270  NE2 GLN A  44     6422   9200   6796  -3235   -130   1362       N  
ATOM    271  N   TYR A  45      31.560  38.705 359.647  1.00 42.41           N  
ANISOU  271  N   TYR A  45     4174   7114   4826  -2266    292   1521       N  
ATOM    272  CA  TYR A  45      32.138  38.576 360.978  1.00 44.76           C  
ANISOU  272  CA  TYR A  45     4443   7656   4910  -2312    339   1599       C  
ATOM    273  C   TYR A  45      33.117  39.716 361.220  1.00 53.73           C  
ANISOU  273  C   TYR A  45     5528   9119   5766  -2593    281   1598       C  
ATOM    274  O   TYR A  45      33.667  40.273 360.261  1.00 53.90           O  
ANISOU  274  O   TYR A  45     5490   9278   5712  -2717    181   1598       O  
ATOM    275  CB  TYR A  45      32.852  37.216 361.147  1.00 46.40           C  
ANISOU  275  CB  TYR A  45     4569   8067   4996  -2024    312   1726       C  
ATOM    276  CG  TYR A  45      31.953  35.998 361.092  1.00 46.37           C  
ANISOU  276  CG  TYR A  45     4689   7698   5233  -1802    312   1764       C  
ATOM    277  CD1 TYR A  45      31.113  35.679 362.152  1.00 48.56           C  
ANISOU  277  CD1 TYR A  45     5046   7804   5601  -1858    396   1827       C  
ATOM    278  CD2 TYR A  45      32.013  35.111 360.022  1.00 46.27           C  
ANISOU  278  CD2 TYR A  45     4718   7546   5317  -1545    200   1756       C  
ATOM    279  CE1 TYR A  45      30.296  34.554 362.113  1.00 49.39           C  
ANISOU  279  CE1 TYR A  45     5275   7589   5903  -1741    357   1913       C  
ATOM    280  CE2 TYR A  45      31.214  33.972 359.981  1.00 46.96           C  
ANISOU  280  CE2 TYR A  45     4978   7257   5608  -1395    144   1806       C  
ATOM    281  CZ  TYR A  45      30.358  33.695 361.031  1.00 54.06           C  
ANISOU  281  CZ  TYR A  45     5959   7978   6605  -1528    216   1903       C  
ATOM    282  OH  TYR A  45      29.566  32.576 361.001  1.00 55.94           O  
ANISOU  282  OH  TYR A  45     6375   7858   7021  -1464    124   2001       O  
ATOM    283  N   SER A  46      33.350  40.054 362.500  1.00 53.57           N  
ANISOU  283  N   SER A  46     5537   9241   5577  -2721    322   1615       N  
ATOM    284  CA  SER A  46      34.300  41.094 362.890  1.00 55.74           C  
ANISOU  284  CA  SER A  46     5801   9819   5557  -3037    233   1629       C  
ATOM    285  C   SER A  46      35.696  40.744 362.353  1.00 61.13           C  
ANISOU  285  C   SER A  46     6231  11038   5958  -3036    148   1780       C  
ATOM    286  O   SER A  46      36.106  39.580 362.415  1.00 61.01           O  
ANISOU  286  O   SER A  46     6068  11240   5874  -2724    192   1869       O  
ATOM    287  CB  SER A  46      34.321  41.247 364.410  1.00 61.79           C  
ANISOU  287  CB  SER A  46     6628  10666   6185  -3099    296   1620       C  
ATOM    288  OG  SER A  46      35.007  42.422 364.816  1.00 75.11           O  
ANISOU  288  OG  SER A  46     8395  12529   7615  -3451    173   1598       O  
ATOM    289  N   ARG A  47      36.384  41.742 361.768  1.00 59.34           N  
ANISOU  289  N   ARG A  47     5965  11034   5547  -3369      5   1819       N  
ATOM    290  CA  ARG A  47      37.726  41.652 361.166  1.00 61.15           C  
ANISOU  290  CA  ARG A  47     5897  11897   5439  -3440    -97   1991       C  
ATOM    291  C   ARG A  47      37.735  40.726 359.908  1.00 64.03           C  
ANISOU  291  C   ARG A  47     6091  12346   5893  -3043    -84   2014       C  
ATOM    292  O   ARG A  47      38.778  40.156 359.562  1.00 65.41           O  
ANISOU  292  O   ARG A  47     5983  13100   5769  -2847   -120   2141       O  
ATOM    293  CB  ARG A  47      38.790  41.214 362.206  1.00 63.33           C  
ANISOU  293  CB  ARG A  47     5982  12729   5353  -3433    -78   2120       C  
ATOM    294  N   LYS A  48      36.582  40.625 359.205  1.00 57.39           N  
ANISOU  294  N   LYS A  48     5422  10956   5428  -2907    -49   1882       N  
ATOM    295  CA  LYS A  48      36.423  39.798 358.000  1.00 55.72           C  
ANISOU  295  CA  LYS A  48     5120  10710   5342  -2537    -60   1864       C  
ATOM    296  C   LYS A  48      35.559  40.517 356.942  1.00 56.42           C  
ANISOU  296  C   LYS A  48     5329  10405   5703  -2672    -97   1766       C  
ATOM    297  O   LYS A  48      34.942  41.544 357.240  1.00 55.48           O  
ANISOU  297  O   LYS A  48     5416   9957   5709  -2986   -103   1692       O  
ATOM    298  CB  LYS A  48      35.800  38.431 358.359  1.00 57.53           C  
ANISOU  298  CB  LYS A  48     5462  10622   5773  -2112     27   1812       C  
ATOM    299  CG  LYS A  48      36.721  37.473 359.112  1.00 73.40           C  
ANISOU  299  CG  LYS A  48     7346  13048   7493  -1825     27   1918       C  
ATOM    300  CD  LYS A  48      36.015  36.159 359.435  1.00 83.21           C  
ANISOU  300  CD  LYS A  48     8781  13886   8948  -1449     55   1889       C  
ATOM    301  CE  LYS A  48      36.888  35.201 360.210  1.00 94.46           C  
ANISOU  301  CE  LYS A  48    10147  15661  10081  -1139     36   1991       C  
ATOM    302  NZ  LYS A  48      36.206  33.902 360.455  1.00101.07           N  
ANISOU  302  NZ  LYS A  48    11242  16037  11123   -827     11   1991       N  
ATOM    303  N   GLY A  49      35.529  39.961 355.728  1.00 51.21           N  
ANISOU  303  N   GLY A  49     4558   9791   5107  -2394   -136   1755       N  
ATOM    304  CA  GLY A  49      34.759  40.484 354.604  1.00 49.17           C  
ANISOU  304  CA  GLY A  49     4376   9213   5093  -2458   -169   1670       C  
ATOM    305  C   GLY A  49      33.416  39.802 354.418  1.00 50.47           C  
ANISOU  305  C   GLY A  49     4741   8778   5657  -2209    -88   1523       C  
ATOM    306  O   GLY A  49      33.238  38.688 354.918  1.00 50.55           O  
ANISOU  306  O   GLY A  49     4805   8670   5731  -1936    -41   1515       O  
ATOM    307  N   PRO A  50      32.439  40.427 353.693  1.00 44.31           N  
ANISOU  307  N   PRO A  50     4079   7623   5134  -2310    -87   1423       N  
ATOM    308  CA  PRO A  50      31.121  39.780 353.514  1.00 41.80           C  
ANISOU  308  CA  PRO A  50     3915   6800   5168  -2109    -16   1305       C  
ATOM    309  C   PRO A  50      31.213  38.440 352.785  1.00 44.71           C  
ANISOU  309  C   PRO A  50     4220   7181   5585  -1712    -70   1302       C  
ATOM    310  O   PRO A  50      32.045  38.266 351.890  1.00 44.93           O  
ANISOU  310  O   PRO A  50     4077   7551   5441  -1553   -164   1333       O  
ATOM    311  CB  PRO A  50      30.322  40.806 352.699  1.00 42.26           C  
ANISOU  311  CB  PRO A  50     4064   6590   5405  -2284    -25   1213       C  
ATOM    312  CG  PRO A  50      31.013  42.091 352.905  1.00 47.72           C  
ANISOU  312  CG  PRO A  50     4761   7504   5866  -2640   -103   1275       C  
ATOM    313  CD  PRO A  50      32.466  41.750 353.039  1.00 45.40           C  
ANISOU  313  CD  PRO A  50     4230   7783   5237  -2631   -168   1429       C  
ATOM    314  N   GLU A  51      30.368  37.490 353.205  1.00 40.45           N  
ANISOU  314  N   GLU A  51     3831   6291   5246  -1552    -37   1276       N  
ATOM    315  CA  GLU A  51      30.309  36.123 352.692  1.00 40.79           C  
ANISOU  315  CA  GLU A  51     3939   6211   5349  -1187   -140   1267       C  
ATOM    316  C   GLU A  51      28.872  35.783 352.328  1.00 41.14           C  
ANISOU  316  C   GLU A  51     4140   5751   5740  -1203   -134   1196       C  
ATOM    317  O   GLU A  51      28.007  35.787 353.210  1.00 40.76           O  
ANISOU  317  O   GLU A  51     4186   5462   5838  -1386    -43   1223       O  
ATOM    318  CB  GLU A  51      30.857  35.159 353.768  1.00 44.26           C  
ANISOU  318  CB  GLU A  51     4453   6726   5638  -1030   -163   1362       C  
ATOM    319  CG  GLU A  51      30.860  33.678 353.415  1.00 60.91           C  
ANISOU  319  CG  GLU A  51     6724   8670   7749   -622   -331   1358       C  
ATOM    320  CD  GLU A  51      31.115  32.782 354.614  1.00 87.07           C  
ANISOU  320  CD  GLU A  51    10188  11932  10962   -515   -363   1466       C  
ATOM    321  OE1 GLU A  51      32.302  32.525 354.920  1.00 83.00           O  
ANISOU  321  OE1 GLU A  51     9582  11832  10124   -302   -399   1516       O  
ATOM    322  OE2 GLU A  51      30.131  32.367 355.268  1.00 80.64           O  
ANISOU  322  OE2 GLU A  51     9564  10706  10368   -659   -355   1523       O  
ATOM    323  N   LEU A  52      28.622  35.478 351.034  1.00 35.10           N  
ANISOU  323  N   LEU A  52     3380   4882   5076  -1006   -239   1115       N  
ATOM    324  CA  LEU A  52      27.291  35.138 350.511  1.00 32.94           C  
ANISOU  324  CA  LEU A  52     3234   4174   5109  -1027   -260   1052       C  
ATOM    325  C   LEU A  52      26.701  33.893 351.195  1.00 35.43           C  
ANISOU  325  C   LEU A  52     3766   4163   5531   -988   -336   1130       C  
ATOM    326  O   LEU A  52      27.331  32.834 351.210  1.00 36.06           O  
ANISOU  326  O   LEU A  52     3976   4240   5486   -719   -493   1164       O  
ATOM    327  CB  LEU A  52      27.331  34.947 348.978  1.00 32.50           C  
ANISOU  327  CB  LEU A  52     3139   4120   5088   -784   -386    947       C  
ATOM    328  CG  LEU A  52      26.052  34.435 348.290  1.00 36.23           C  
ANISOU  328  CG  LEU A  52     3745   4167   5853   -778   -448    877       C  
ATOM    329  CD1 LEU A  52      25.019  35.546 348.098  1.00 34.61           C  
ANISOU  329  CD1 LEU A  52     3452   3865   5833  -1065   -290    834       C  
ATOM    330  CD2 LEU A  52      26.381  33.801 346.965  1.00 38.31           C  
ANISOU  330  CD2 LEU A  52     4025   4449   6081   -425   -632    773       C  
ATOM    331  N   LEU A  53      25.499  34.053 351.779  1.00 30.37           N  
ANISOU  331  N   LEU A  53     3168   3283   5088  -1255   -242   1174       N  
ATOM    332  CA  LEU A  53      24.756  32.970 352.426  1.00 31.29           C  
ANISOU  332  CA  LEU A  53     3464   3115   5310  -1336   -321   1303       C  
ATOM    333  C   LEU A  53      23.883  32.304 351.397  1.00 37.08           C  
ANISOU  333  C   LEU A  53     4326   3513   6250  -1308   -477   1268       C  
ATOM    334  O   LEU A  53      24.110  31.140 351.059  1.00 38.77           O  
ANISOU  334  O   LEU A  53     4775   3498   6456  -1119   -714   1289       O  
ATOM    335  CB  LEU A  53      23.890  33.457 353.603  1.00 30.56           C  
ANISOU  335  CB  LEU A  53     3289   3067   5256  -1647   -141   1404       C  
ATOM    336  CG  LEU A  53      24.597  34.048 354.786  1.00 34.68           C  
ANISOU  336  CG  LEU A  53     3728   3873   5576  -1702     -8   1450       C  
ATOM    337  CD1 LEU A  53      23.693  34.984 355.501  1.00 34.48           C  
ANISOU  337  CD1 LEU A  53     3585   3945   5570  -1926    179   1449       C  
ATOM    338  CD2 LEU A  53      25.073  32.975 355.725  1.00 38.84           C  
ANISOU  338  CD2 LEU A  53     4387   4371   6000  -1653   -101   1614       C  
ATOM    339  N   MET A  54      22.896  33.062 350.875  1.00 33.12           N  
ANISOU  339  N   MET A  54     3695   2979   5908  -1475   -367   1203       N  
ATOM    340  CA  MET A  54      21.941  32.586 349.883  1.00 33.89           C  
ANISOU  340  CA  MET A  54     3869   2806   6202  -1501   -491   1169       C  
ATOM    341  C   MET A  54      21.637  33.658 348.821  1.00 34.71           C  
ANISOU  341  C   MET A  54     3796   3007   6384  -1464   -386   1004       C  
ATOM    342  O   MET A  54      21.801  34.862 349.056  1.00 32.46           O  
ANISOU  342  O   MET A  54     3349   2945   6039  -1530   -198    953       O  
ATOM    343  CB  MET A  54      20.642  32.107 350.564  1.00 37.90           C  
ANISOU  343  CB  MET A  54     4403   3175   6823  -1829   -485   1344       C  
ATOM    344  N   TYR A  55      21.218  33.176 347.636  1.00 30.50           N  
ANISOU  344  N   TYR A  55     3335   2280   5975  -1350   -540    922       N  
ATOM    345  CA  TYR A  55      20.851  33.947 346.452  1.00 27.97           C  
ANISOU  345  CA  TYR A  55     2873   2010   5745  -1292   -484    776       C  
ATOM    346  C   TYR A  55      19.600  33.313 345.862  1.00 33.61           C  
ANISOU  346  C   TYR A  55     3658   2461   6650  -1409   -595    789       C  
ATOM    347  O   TYR A  55      19.584  32.109 345.576  1.00 35.05           O  
ANISOU  347  O   TYR A  55     4070   2378   6870  -1335   -846    812       O  
ATOM    348  CB  TYR A  55      22.026  33.978 345.438  1.00 27.67           C  
ANISOU  348  CB  TYR A  55     2810   2116   5586   -958   -584    650       C  
ATOM    349  CG  TYR A  55      21.731  34.631 344.101  1.00 26.82           C  
ANISOU  349  CG  TYR A  55     2564   2064   5561   -878   -562    517       C  
ATOM    350  CD1 TYR A  55      21.345  35.966 344.024  1.00 27.37           C  
ANISOU  350  CD1 TYR A  55     2463   2279   5658  -1039   -365    489       C  
ATOM    351  CD2 TYR A  55      21.919  33.940 342.908  1.00 27.65           C  
ANISOU  351  CD2 TYR A  55     2738   2082   5687   -605   -759    412       C  
ATOM    352  CE1 TYR A  55      21.113  36.584 342.794  1.00 27.16           C  
ANISOU  352  CE1 TYR A  55     2322   2302   5696   -965   -354    384       C  
ATOM    353  CE2 TYR A  55      21.676  34.542 341.673  1.00 27.07           C  
ANISOU  353  CE2 TYR A  55     2517   2094   5676   -524   -735    298       C  
ATOM    354  CZ  TYR A  55      21.285  35.870 341.620  1.00 32.10           C  
ANISOU  354  CZ  TYR A  55     2968   2875   6353   -718   -526    297       C  
ATOM    355  OH  TYR A  55      21.058  36.485 340.410  1.00 29.44           O  
ANISOU  355  OH  TYR A  55     2498   2619   6069   -642   -510    203       O  
ATOM    356  N   THR A  56      18.528  34.102 345.746  1.00 29.79           N  
ANISOU  356  N   THR A  56     3004   2061   6253  -1586   -433    782       N  
ATOM    357  CA  THR A  56      17.269  33.607 345.199  1.00 31.02           C  
ANISOU  357  CA  THR A  56     3165   2083   6537  -1712   -520    813       C  
ATOM    358  C   THR A  56      16.631  34.711 344.362  1.00 32.43           C  
ANISOU  358  C   THR A  56     3135   2381   6807  -1713   -360    685       C  
ATOM    359  O   THR A  56      16.624  35.871 344.760  1.00 31.50           O  
ANISOU  359  O   THR A  56     2891   2495   6585  -1659   -156    638       O  
ATOM    360  CB  THR A  56      16.354  33.005 346.283  1.00 43.99           C  
ANISOU  360  CB  THR A  56     4819   3686   8208  -2089   -523   1046       C  
ATOM    361  OG1 THR A  56      15.120  32.588 345.689  1.00 50.00           O  
ANISOU  361  OG1 THR A  56     5541   4374   9082  -2292   -612   1105       O  
ATOM    362  CG2 THR A  56      16.119  33.936 347.471  1.00 40.72           C  
ANISOU  362  CG2 THR A  56     4211   3587   7675  -2195   -259   1111       C  
ATOM    363  N   TYR A  57      16.135  34.324 343.181  1.00 29.68           N  
ANISOU  363  N   TYR A  57     2814   2000   6465  -1501   -497    602       N  
ATOM    364  CA  TYR A  57      15.541  35.167 342.140  1.00 28.15           C  
ANISOU  364  CA  TYR A  57     2472   1941   6282  -1337   -397    471       C  
ATOM    365  C   TYR A  57      14.025  34.987 342.023  1.00 32.22           C  
ANISOU  365  C   TYR A  57     2863   2396   6982  -1712   -380    549       C  
ATOM    366  O   TYR A  57      13.350  35.883 341.526  1.00 31.50           O  
ANISOU  366  O   TYR A  57     2614   2483   6873  -1623   -233    468       O  
ATOM    367  CB  TYR A  57      16.192  34.855 340.776  1.00 27.91           C  
ANISOU  367  CB  TYR A  57     2481   1770   6354  -1156   -551    327       C  
ATOM    368  CG  TYR A  57      16.873  33.501 340.688  1.00 30.27           C  
ANISOU  368  CG  TYR A  57     3033   1726   6742  -1186   -838    331       C  
ATOM    369  CD1 TYR A  57      18.203  33.341 341.067  1.00 32.44           C  
ANISOU  369  CD1 TYR A  57     3396   2064   6867   -979   -882    324       C  
ATOM    370  CD2 TYR A  57      16.193  32.386 340.205  1.00 32.63           C  
ANISOU  370  CD2 TYR A  57     3515   1740   7143  -1252  -1090    340       C  
ATOM    371  CE1 TYR A  57      18.833  32.103 340.985  1.00 36.41           C  
ANISOU  371  CE1 TYR A  57     4174   2355   7307   -776  -1163    309       C  
ATOM    372  CE2 TYR A  57      16.811  31.139 340.127  1.00 35.31           C  
ANISOU  372  CE2 TYR A  57     4184   1796   7437  -1086  -1404    325       C  
ATOM    373  CZ  TYR A  57      18.134  31.003 340.517  1.00 45.51           C  
ANISOU  373  CZ  TYR A  57     5569   3158   8563   -812  -1436    300       C  
ATOM    374  OH  TYR A  57      18.768  29.785 340.442  1.00 51.37           O  
ANISOU  374  OH  TYR A  57     6668   3634   9218   -563  -1762    265       O  
ATOM    375  N   SER A  58      13.499  33.837 342.452  1.00 31.80           N  
ANISOU  375  N   SER A  58     2943   2291   6847  -1794   -564    707       N  
ATOM    376  CA  SER A  58      12.076  33.529 342.371  1.00 33.83           C  
ANISOU  376  CA  SER A  58     3096   2625   7132  -2071   -597    834       C  
ATOM    377  C   SER A  58      11.352  33.811 343.700  1.00 37.81           C  
ANISOU  377  C   SER A  58     3378   3351   7636  -2517   -416   1045       C  
ATOM    378  O   SER A  58      11.962  33.743 344.773  1.00 37.72           O  
ANISOU  378  O   SER A  58     3433   3357   7542  -2542   -373   1128       O  
ATOM    379  CB  SER A  58      11.887  32.070 341.957  1.00 39.31           C  
ANISOU  379  CB  SER A  58     4000   2833   8104  -2544   -940    946       C  
ATOM    380  OG  SER A  58      10.575  31.577 342.181  1.00 53.11           O  
ANISOU  380  OG  SER A  58     5633   4686   9859  -2945  -1013   1142       O  
ATOM    381  N   SER A  59      10.036  34.108 343.607  1.00 36.35           N  
ANISOU  381  N   SER A  59     3026   3525   7261  -2468   -347   1104       N  
ATOM    382  CA  SER A  59       9.145  34.360 344.745  1.00 37.77           C  
ANISOU  382  CA  SER A  59     2981   4111   7259  -2679   -202   1298       C  
ATOM    383  C   SER A  59       8.914  33.049 345.530  1.00 44.32           C  
ANISOU  383  C   SER A  59     3764   4816   8259  -3408   -372   1656       C  
ATOM    384  O   SER A  59       8.574  32.011 344.945  1.00 45.92           O  
ANISOU  384  O   SER A  59     4116   4778   8552  -3658   -650   1763       O  
ATOM    385  CB  SER A  59       7.824  34.956 344.263  1.00 39.96           C  
ANISOU  385  CB  SER A  59     2890   4764   7531  -2816    -50   1313       C  
ATOM    386  OG  SER A  59       7.333  35.932 345.167  1.00 44.44           O  
ANISOU  386  OG  SER A  59     3093   5809   7984  -2864    242   1354       O  
ATOM    387  N   GLY A  60       9.160  33.102 346.833  1.00 42.76           N  
ANISOU  387  N   GLY A  60     3595   4819   7832  -3338   -306   1775       N  
ATOM    388  CA  GLY A  60       9.031  31.940 347.701  1.00 45.99           C  
ANISOU  388  CA  GLY A  60     4086   5167   8221  -3792   -499   2110       C  
ATOM    389  C   GLY A  60      10.253  31.663 348.556  1.00 50.20           C  
ANISOU  389  C   GLY A  60     4823   5439   8811  -3795   -501   2138       C  
ATOM    390  O   GLY A  60      11.127  32.525 348.714  1.00 47.10           O  
ANISOU  390  O   GLY A  60     4442   5054   8401  -3432   -314   1914       O  
ATOM    391  N   ASN A  61      10.323  30.439 349.105  1.00 50.51           N  
ANISOU  391  N   ASN A  61     5081   5264   8848  -4136   -759   2414       N  
ATOM    392  CA  ASN A  61      11.388  30.010 350.010  1.00 50.69           C  
ANISOU  392  CA  ASN A  61     5342   5085   8832  -4072   -812   2473       C  
ATOM    393  C   ASN A  61      12.380  29.033 349.363  1.00 53.85           C  
ANISOU  393  C   ASN A  61     6232   4856   9373  -3934  -1138   2376       C  
ATOM    394  O   ASN A  61      12.024  28.286 348.442  1.00 54.58           O  
ANISOU  394  O   ASN A  61     6543   4617   9577  -4060  -1425   2384       O  
ATOM    395  CB  ASN A  61      10.779  29.371 351.264  1.00 56.91           C  
ANISOU  395  CB  ASN A  61     6030   6131   9461  -4522   -868   2879       C  
ATOM    396  CG  ASN A  61       9.899  30.304 352.067  1.00 87.89           C  
ANISOU  396  CG  ASN A  61     9458  10768  13166  -4561   -541   2969       C  
ATOM    397  OD1 ASN A  61       9.080  31.062 351.532  1.00 81.61           O  
ANISOU  397  OD1 ASN A  61     8363  10319  12326  -4487   -379   2872       O  
ATOM    398  ND2 ASN A  61      10.027  30.250 353.378  1.00 85.00           N  
ANISOU  398  ND2 ASN A  61     9000  10666  12630  -4642   -446   3154       N  
ATOM    399  N   LYS A  66      13.632  29.058 349.875  1.00 47.99           N  
ANISOU  399  N   LYS A  66     5660   3984   8588  -3646  -1103   2278       N  
ATOM    400  CA  LYS A  66      14.751  28.213 349.468  1.00 47.69           C  
ANISOU  400  CA  LYS A  66     6062   3459   8598  -3393  -1381   2172       C  
ATOM    401  C   LYS A  66      15.538  27.835 350.719  1.00 52.82           C  
ANISOU  401  C   LYS A  66     6845   4105   9118  -3378  -1386   2317       C  
ATOM    402  O   LYS A  66      15.984  28.712 351.459  1.00 49.87           O  
ANISOU  402  O   LYS A  66     6230   4075   8644  -3242  -1089   2262       O  
ATOM    403  CB  LYS A  66      15.629  28.929 348.419  1.00 46.55           C  
ANISOU  403  CB  LYS A  66     5900   3285   8503  -2899  -1283   1807       C  
ATOM    404  CG  LYS A  66      16.823  28.119 347.898  1.00 61.59           C  
ANISOU  404  CG  LYS A  66     8206   4802  10394  -2535  -1565   1666       C  
ATOM    405  CD  LYS A  66      18.151  28.727 348.370  1.00 72.45           C  
ANISOU  405  CD  LYS A  66     9508   6388  11632  -2171  -1382   1534       C  
ATOM    406  CE  LYS A  66      19.378  28.087 347.754  1.00 84.13           C  
ANISOU  406  CE  LYS A  66    11301   7636  13030  -1719  -1630   1372       C  
ATOM    407  NZ  LYS A  66      20.621  28.836 348.100  1.00 89.13           N  
ANISOU  407  NZ  LYS A  66    11769   8601  13494  -1399  -1429   1259       N  
ATOM    408  N   GLU A  67      15.670  26.530 350.976  1.00 54.34           N  
ANISOU  408  N   GLU A  67     7452   3895   9301  -3530  -1746   2509       N  
ATOM    409  CA  GLU A  67      16.389  26.031 352.141  1.00 56.40           C  
ANISOU  409  CA  GLU A  67     7886   4110   9432  -3523  -1797   2673       C  
ATOM    410  C   GLU A  67      17.844  25.700 351.786  1.00 62.59           C  
ANISOU  410  C   GLU A  67     9002   4617  10163  -2989  -1936   2441       C  
ATOM    411  O   GLU A  67      18.146  25.343 350.642  1.00 62.28           O  
ANISOU  411  O   GLU A  67     9227   4253  10182  -2716  -2169   2244       O  
ATOM    412  CB  GLU A  67      15.682  24.811 352.744  1.00 62.36           C  
ANISOU  412  CB  GLU A  67     8917   4610  10166  -4031  -2130   3068       C  
ATOM    413  N   ASP A  68      18.742  25.859 352.783  1.00 60.55           N  
ANISOU  413  N   ASP A  68     8696   4553   9758  -2818  -1787   2464       N  
ATOM    414  CA  ASP A  68      20.182  25.604 352.716  1.00 60.75           C  
ANISOU  414  CA  ASP A  68     8953   4475   9652  -2311  -1877   2291       C  
ATOM    415  C   ASP A  68      20.698  25.417 354.149  1.00 64.99           C  
ANISOU  415  C   ASP A  68     9503   5160  10030  -2371  -1807   2491       C  
ATOM    416  O   ASP A  68      21.216  26.346 354.773  1.00 62.16           O  
ANISOU  416  O   ASP A  68     8826   5223   9570  -2265  -1489   2425       O  
ATOM    417  CB  ASP A  68      20.914  26.749 351.977  1.00 59.69           C  
ANISOU  417  CB  ASP A  68     8522   4667   9492  -1919  -1617   1970       C  
ATOM    418  CG  ASP A  68      22.229  26.359 351.320  1.00 75.92           C  
ANISOU  418  CG  ASP A  68    10810   6632  11405  -1358  -1795   1760       C  
ATOM    419  OD1 ASP A  68      23.133  25.866 352.039  1.00 78.46           O  
ANISOU  419  OD1 ASP A  68    11292   6977  11543  -1151  -1865   1818       O  
ATOM    420  OD2 ASP A  68      22.379  26.609 350.098  1.00 82.16           O  
ANISOU  420  OD2 ASP A  68    11583   7399  12236  -1097  -1849   1538       O  
ATOM    421  N   GLY A  74      20.485  24.221 354.673  1.00 65.40           N  
ANISOU  421  N   GLY A  74     9942   4851  10058  -2585  -2126   2754       N  
ATOM    422  CA  GLY A  74      20.879  23.864 356.028  1.00 66.95           C  
ANISOU  422  CA  GLY A  74    10200   5134  10104  -2683  -2113   2992       C  
ATOM    423  C   GLY A  74      19.945  24.453 357.059  1.00 70.21           C  
ANISOU  423  C   GLY A  74    10192   5966  10518  -3174  -1833   3244       C  
ATOM    424  O   GLY A  74      18.753  24.130 357.074  1.00 71.97           O  
ANISOU  424  O   GLY A  74    10391   6132  10823  -3652  -1941   3487       O  
ATOM    425  N   ARG A  75      20.483  25.339 357.918  1.00 63.80           N  
ANISOU  425  N   ARG A  75     9035   5623   9583  -3049  -1484   3186       N  
ATOM    426  CA  ARG A  75      19.724  26.004 358.984  1.00 62.69           C  
ANISOU  426  CA  ARG A  75     8478   5961   9382  -3395  -1196   3376       C  
ATOM    427  C   ARG A  75      19.168  27.349 358.498  1.00 63.00           C  
ANISOU  427  C   ARG A  75     8093   6361   9484  -3374   -879   3157       C  
ATOM    428  O   ARG A  75      18.505  28.049 359.265  1.00 62.29           O  
ANISOU  428  O   ARG A  75     7648   6706   9313  -3572   -638   3255       O  
ATOM    429  CB  ARG A  75      20.600  26.203 360.237  1.00 60.64           C  
ANISOU  429  CB  ARG A  75     8126   5988   8927  -3255  -1027   3424       C  
ATOM    430  CG  ARG A  75      21.144  24.915 360.852  1.00 68.80           C  
ANISOU  430  CG  ARG A  75     9563   6714   9864  -3272  -1321   3671       C  
ATOM    431  CD  ARG A  75      21.864  25.152 362.168  1.00 75.57           C  
ANISOU  431  CD  ARG A  75    10260   7933  10521  -3197  -1123   3757       C  
ATOM    432  NE  ARG A  75      23.147  25.836 361.989  1.00 81.88           N  
ANISOU  432  NE  ARG A  75    10986   8908  11218  -2723   -957   3443       N  
ATOM    433  CZ  ARG A  75      23.363  27.116 362.280  1.00 90.10           C  
ANISOU  433  CZ  ARG A  75    11641  10398  12197  -2647   -618   3257       C  
ATOM    434  NH1 ARG A  75      22.385  27.866 362.774  1.00 74.83           N  
ANISOU  434  NH1 ARG A  75     9371   8780  10282  -2926   -398   3315       N  
ATOM    435  NH2 ARG A  75      24.557  27.655 362.078  1.00 71.82           N  
ANISOU  435  NH2 ARG A  75     9283   8238   9766  -2286   -522   3019       N  
ATOM    436  N   PHE A  76      19.394  27.679 357.213  1.00 57.34           N  
ANISOU  436  N   PHE A  76     7429   5473   8885  -3111   -902   2865       N  
ATOM    437  CA  PHE A  76      18.980  28.940 356.606  1.00 54.27           C  
ANISOU  437  CA  PHE A  76     6713   5352   8554  -3041   -643   2637       C  
ATOM    438  C   PHE A  76      17.864  28.777 355.573  1.00 58.30           C  
ANISOU  438  C   PHE A  76     7213   5708   9229  -3228   -754   2642       C  
ATOM    439  O   PHE A  76      17.993  27.985 354.636  1.00 58.33           O  
ANISOU  439  O   PHE A  76     7521   5299   9342  -3160  -1033   2597       O  
ATOM    440  CB  PHE A  76      20.188  29.619 355.933  1.00 53.30           C  
ANISOU  440  CB  PHE A  76     6602   5242   8409  -2615   -558   2316       C  
ATOM    441  CG  PHE A  76      21.337  29.932 356.856  1.00 54.36           C  
ANISOU  441  CG  PHE A  76     6701   5597   8355  -2437   -437   2291       C  
ATOM    442  CD1 PHE A  76      22.339  28.998 357.086  1.00 59.11           C  
ANISOU  442  CD1 PHE A  76     7574   6027   8860  -2233   -629   2337       C  
ATOM    443  CD2 PHE A  76      21.428  31.168 357.483  1.00 55.00           C  
ANISOU  443  CD2 PHE A  76     6504   6062   8333  -2448   -154   2208       C  
ATOM    444  CE1 PHE A  76      23.398  29.284 357.948  1.00 59.90           C  
ANISOU  444  CE1 PHE A  76     7611   6388   8762  -2075   -513   2324       C  
ATOM    445  CE2 PHE A  76      22.493  31.459 358.337  1.00 57.81           C  
ANISOU  445  CE2 PHE A  76     6832   6631   8502  -2319    -62   2189       C  
ATOM    446  CZ  PHE A  76      23.474  30.516 358.562  1.00 57.34           C  
ANISOU  446  CZ  PHE A  76     6988   6450   8350  -2146   -228   2255       C  
ATOM    447  N   THR A  77      16.792  29.577 355.727  1.00 54.94           N  
ANISOU  447  N   THR A  77     6436   5646   8791  -3420   -540   2677       N  
ATOM    448  CA  THR A  77      15.649  29.650 354.814  1.00 55.58           C  
ANISOU  448  CA  THR A  77     6408   5723   8988  -3597   -584   2680       C  
ATOM    449  C   THR A  77      15.541  31.094 354.314  1.00 57.70           C  
ANISOU  449  C   THR A  77     6396   6272   9255  -3350   -297   2392       C  
ATOM    450  O   THR A  77      15.470  32.012 355.131  1.00 57.43           O  
ANISOU  450  O   THR A  77     6123   6624   9074  -3290    -48   2363       O  
ATOM    451  CB  THR A  77      14.358  29.164 355.502  1.00 67.77           C  
ANISOU  451  CB  THR A  77     7783   7513  10452  -4082   -637   3054       C  
ATOM    452  OG1 THR A  77      14.481  27.777 355.830  1.00 72.43           O  
ANISOU  452  OG1 THR A  77     8711   7767  11043  -4339   -955   3338       O  
ATOM    453  CG2 THR A  77      13.122  29.367 354.640  1.00 66.57           C  
ANISOU  453  CG2 THR A  77     7470   7446  10378  -4291   -677   3082       C  
ATOM    454  N   ALA A  78      15.531  31.293 352.983  1.00 52.47           N  
ANISOU  454  N   ALA A  78     5794   5402   8740  -3191   -355   2178       N  
ATOM    455  CA  ALA A  78      15.432  32.620 352.373  1.00 49.34           C  
ANISOU  455  CA  ALA A  78     5194   5200   8352  -2962   -131   1915       C  
ATOM    456  C   ALA A  78      14.085  32.801 351.659  1.00 53.16           C  
ANISOU  456  C   ALA A  78     5489   5811   8898  -3109   -115   1936       C  
ATOM    457  O   ALA A  78      13.903  32.315 350.537  1.00 52.40           O  
ANISOU  457  O   ALA A  78     5514   5443   8954  -3122   -289   1882       O  
ATOM    458  CB  ALA A  78      16.584  32.831 351.408  1.00 47.87           C  
ANISOU  458  CB  ALA A  78     5178   4767   8245  -2638   -187   1659       C  
ATOM    459  N   GLN A  79      13.133  33.485 352.333  1.00 50.67           N  
ANISOU  459  N   GLN A  79     4870   5953   8431  -3190     89   2011       N  
ATOM    460  CA  GLN A  79      11.776  33.738 351.825  1.00 51.47           C  
ANISOU  460  CA  GLN A  79     4717   6328   8513  -3307    140   2055       C  
ATOM    461  C   GLN A  79      11.707  35.068 351.068  1.00 51.98           C  
ANISOU  461  C   GLN A  79     4691   6472   8585  -2961    316   1742       C  
ATOM    462  O   GLN A  79      12.223  36.083 351.540  1.00 49.76           O  
ANISOU  462  O   GLN A  79     4406   6306   8194  -2705    482   1575       O  
ATOM    463  CB  GLN A  79      10.735  33.713 352.960  1.00 55.71           C  
ANISOU  463  CB  GLN A  79     4938   7422   8809  -3533    251   2323       C  
ATOM    464  N   VAL A  80      11.075  35.042 349.883  1.00 47.84           N  
ANISOU  464  N   VAL A  80     4128   5864   8185  -2968    251   1671       N  
ATOM    465  CA  VAL A  80      10.918  36.192 348.989  1.00 45.27           C  
ANISOU  465  CA  VAL A  80     3740   5578   7883  -2664    381   1400       C  
ATOM    466  C   VAL A  80       9.437  36.382 348.644  1.00 51.01           C  
ANISOU  466  C   VAL A  80     4173   6685   8525  -2741    446   1468       C  
ATOM    467  O   VAL A  80       8.733  35.403 348.362  1.00 51.65           O  
ANISOU  467  O   VAL A  80     4184   6780   8661  -3062    293   1671       O  
ATOM    468  CB  VAL A  80      11.781  36.009 347.701  1.00 46.51           C  
ANISOU  468  CB  VAL A  80     4130   5281   8262  -2525    239   1215       C  
ATOM    469  CG1 VAL A  80      11.438  37.034 346.623  1.00 44.46           C  
ANISOU  469  CG1 VAL A  80     3787   5065   8039  -2285    335    991       C  
ATOM    470  CG2 VAL A  80      13.267  36.053 348.018  1.00 44.74           C  
ANISOU  470  CG2 VAL A  80     4124   4832   8043  -2378    214   1129       C  
ATOM    471  N   ASP A  81       8.983  37.653 348.654  1.00 48.17           N  
ANISOU  471  N   ASP A  81     3664   6633   8005  -2439    647   1298       N  
ATOM    472  CA  ASP A  81       7.639  38.040 348.239  1.00 50.13           C  
ANISOU  472  CA  ASP A  81     3619   7308   8120  -2390    735   1312       C  
ATOM    473  C   ASP A  81       7.736  39.253 347.310  1.00 52.92           C  
ANISOU  473  C   ASP A  81     4055   7550   8501  -1991    826   1000       C  
ATOM    474  O   ASP A  81       7.842  40.397 347.762  1.00 52.03           O  
ANISOU  474  O   ASP A  81     4002   7550   8218  -1667    954    831       O  
ATOM    475  CB  ASP A  81       6.677  38.294 349.414  1.00 55.00           C  
ANISOU  475  CB  ASP A  81     3923   8583   8391  -2388    880   1476       C  
ATOM    476  CG  ASP A  81       5.203  38.294 349.010  1.00 68.38           C  
ANISOU  476  CG  ASP A  81     5231  10850   9900  -2443    933   1599       C  
ATOM    477  OD1 ASP A  81       4.912  38.322 347.782  1.00 66.88           O  
ANISOU  477  OD1 ASP A  81     5035  10532   9845  -2397    893   1490       O  
ATOM    478  OD2 ASP A  81       4.340  38.244 349.915  1.00 78.85           O  
ANISOU  478  OD2 ASP A  81     6233  12809  10918  -2526   1014   1814       O  
ATOM    479  N   LYS A  82       7.707  38.977 345.998  1.00 48.99           N  
ANISOU  479  N   LYS A  82     3597   6803   8212  -2022    728    927       N  
ATOM    480  CA  LYS A  82       7.762  39.985 344.944  1.00 47.12           C  
ANISOU  480  CA  LYS A  82     3435   6442   8026  -1696    782    670       C  
ATOM    481  C   LYS A  82       6.472  40.838 344.937  1.00 55.74           C  
ANISOU  481  C   LYS A  82     4277   8033   8869  -1455    935    619       C  
ATOM    482  O   LYS A  82       6.525  42.018 344.568  1.00 54.91           O  
ANISOU  482  O   LYS A  82     4286   7882   8694  -1093   1009    396       O  
ATOM    483  CB  LYS A  82       7.992  39.319 343.579  1.00 46.89           C  
ANISOU  483  CB  LYS A  82     3483   6068   8266  -1797    627    627       C  
ATOM    484  CG  LYS A  82       9.395  38.747 343.401  1.00 46.26           C  
ANISOU  484  CG  LYS A  82     3680   5523   8374  -1850    481    592       C  
ATOM    485  CD  LYS A  82       9.703  38.442 341.940  1.00 48.11           C  
ANISOU  485  CD  LYS A  82     3990   5475   8813  -1803    343    483       C  
ATOM    486  CE  LYS A  82      11.187  38.409 341.676  1.00 52.70           C  
ANISOU  486  CE  LYS A  82     4804   5731   9490  -1698    245    392       C  
ATOM    487  NZ  LYS A  82      11.504  38.134 340.248  1.00 57.21           N  
ANISOU  487  NZ  LYS A  82     5418   6107  10212  -1591    112    277       N  
ATOM    488  N   SER A  83       5.328  40.252 345.376  1.00 56.28           N  
ANISOU  488  N   SER A  83     4012   8606   8768  -1653    964    841       N  
ATOM    489  CA  SER A  83       4.049  40.956 345.445  1.00 58.83           C  
ANISOU  489  CA  SER A  83     4027   9544   8781  -1401   1109    824       C  
ATOM    490  C   SER A  83       4.030  41.971 346.608  1.00 64.96           C  
ANISOU  490  C   SER A  83     4827  10627   9229  -1019   1253    721       C  
ATOM    491  O   SER A  83       3.759  43.152 346.369  1.00 64.93           O  
ANISOU  491  O   SER A  83     4900  10714   9055   -552   1336    487       O  
ATOM    492  CB  SER A  83       2.892  39.972 345.574  1.00 65.33           C  
ANISOU  492  CB  SER A  83     4448  10893   9483  -1786   1073   1139       C  
ATOM    493  OG  SER A  83       1.647  40.651 345.593  1.00 76.76           O  
ANISOU  493  OG  SER A  83     5543  13038  10583  -1511   1218   1130       O  
ATOM    494  N   SER A  84       4.336  41.518 347.853  1.00 62.69           N  
ANISOU  494  N   SER A  84     4511  10468   8839  -1196   1259    886       N  
ATOM    495  CA  SER A  84       4.354  42.369 349.056  1.00 63.71           C  
ANISOU  495  CA  SER A  84     4667  10901   8638   -847   1372    795       C  
ATOM    496  C   SER A  84       5.633  43.234 349.142  1.00 63.83           C  
ANISOU  496  C   SER A  84     5161  10324   8767   -602   1337    521       C  
ATOM    497  O   SER A  84       5.712  44.111 350.009  1.00 64.84           O  
ANISOU  497  O   SER A  84     5413  10601   8624   -251   1394    377       O  
ATOM    498  CB  SER A  84       4.209  41.527 350.321  1.00 69.07           C  
ANISOU  498  CB  SER A  84     5120  11955   9168  -1159   1382   1094       C  
ATOM    499  OG  SER A  84       3.009  40.770 350.316  1.00 80.26           O  
ANISOU  499  OG  SER A  84     6080  13986  10427  -1448   1388   1398       O  
ATOM    500  N   LYS A  85       6.609  42.997 348.225  1.00 55.53           N  
ANISOU  500  N   LYS A  85     4373   8645   8081   -785   1224    457       N  
ATOM    501  CA  LYS A  85       7.892  43.698 348.104  1.00 52.12           C  
ANISOU  501  CA  LYS A  85     4354   7672   7777   -671   1157    259       C  
ATOM    502  C   LYS A  85       8.669  43.662 349.436  1.00 56.18           C  
ANISOU  502  C   LYS A  85     4999   8158   8190   -734   1158    303       C  
ATOM    503  O   LYS A  85       8.978  44.702 350.023  1.00 56.26           O  
ANISOU  503  O   LYS A  85     5248   8114   8015   -458   1165    126       O  
ATOM    504  CB  LYS A  85       7.714  45.138 347.577  1.00 53.91           C  
ANISOU  504  CB  LYS A  85     4806   7807   7872   -233   1167    -15       C  
ATOM    505  CG  LYS A  85       7.447  45.214 346.079  1.00 57.87           C  
ANISOU  505  CG  LYS A  85     5281   8147   8559   -206   1133    -80       C  
ATOM    506  CD  LYS A  85       7.471  46.655 345.595  1.00 65.30           C  
ANISOU  506  CD  LYS A  85     6527   8906   9379    199   1104   -332       C  
ATOM    507  CE  LYS A  85       6.822  46.844 344.244  1.00 73.17           C  
ANISOU  507  CE  LYS A  85     7432   9891  10481    301   1103   -390       C  
ATOM    508  NZ  LYS A  85       7.657  46.319 343.132  1.00 78.82           N  
ANISOU  508  NZ  LYS A  85     8197  10198  11551      1   1007   -345       N  
ATOM    509  N   TYR A  86       8.959  42.440 349.912  1.00 53.10           N  
ANISOU  509  N   TYR A  86     4478   7788   7911  -1102   1126    542       N  
ATOM    510  CA  TYR A  86       9.701  42.184 351.150  1.00 53.31           C  
ANISOU  510  CA  TYR A  86     4588   7806   7863  -1209   1125    625       C  
ATOM    511  C   TYR A  86      10.346  40.793 351.102  1.00 53.76           C  
ANISOU  511  C   TYR A  86     4642   7620   8166  -1615   1016    843       C  
ATOM    512  O   TYR A  86       9.741  39.833 350.624  1.00 53.55           O  
ANISOU  512  O   TYR A  86     4447   7646   8254  -1858    956   1018       O  
ATOM    513  CB  TYR A  86       8.808  42.364 352.407  1.00 58.62           C  
ANISOU  513  CB  TYR A  86     5021   9078   8174  -1075   1244    712       C  
ATOM    514  CG  TYR A  86       8.196  41.104 352.985  1.00 63.57           C  
ANISOU  514  CG  TYR A  86     5309  10085   8762  -1436   1250   1059       C  
ATOM    515  CD1 TYR A  86       7.042  40.550 352.437  1.00 67.54           C  
ANISOU  515  CD1 TYR A  86     5494  10921   9248  -1599   1251   1232       C  
ATOM    516  CD2 TYR A  86       8.740  40.495 354.113  1.00 65.48           C  
ANISOU  516  CD2 TYR A  86     5545  10383   8950  -1635   1241   1234       C  
ATOM    517  CE1 TYR A  86       6.460  39.403 352.979  1.00 71.23           C  
ANISOU  517  CE1 TYR A  86     5669  11744   9651  -2009   1214   1596       C  
ATOM    518  CE2 TYR A  86       8.173  39.343 354.658  1.00 69.08           C  
ANISOU  518  CE2 TYR A  86     5719  11176   9354  -2009   1215   1590       C  
ATOM    519  CZ  TYR A  86       7.028  38.806 354.093  1.00 79.04           C  
ANISOU  519  CZ  TYR A  86     6686  12749  10598  -2218   1189   1781       C  
ATOM    520  OH  TYR A  86       6.461  37.679 354.635  1.00 83.65           O  
ANISOU  520  OH  TYR A  86     7010  13666  11106  -2663   1121   2176       O  
ATOM    521  N   ILE A  87      11.590  40.706 351.571  1.00 47.91           N  
ANISOU  521  N   ILE A  87     4120   6602   7482  -1673    966    826       N  
ATOM    522  CA  ILE A  87      12.354  39.462 351.600  1.00 46.66           C  
ANISOU  522  CA  ILE A  87     4026   6194   7507  -1961    843    999       C  
ATOM    523  C   ILE A  87      12.817  39.210 353.038  1.00 51.63           C  
ANISOU  523  C   ILE A  87     4660   6976   7981  -2040    879   1126       C  
ATOM    524  O   ILE A  87      12.922  40.157 353.817  1.00 51.29           O  
ANISOU  524  O   ILE A  87     4652   7107   7731  -1841    977   1008       O  
ATOM    525  CB  ILE A  87      13.520  39.448 350.565  1.00 46.76           C  
ANISOU  525  CB  ILE A  87     4272   5763   7732  -1928    728    866       C  
ATOM    526  CG1 ILE A  87      14.561  40.559 350.830  1.00 45.45           C  
ANISOU  526  CG1 ILE A  87     4305   5497   7468  -1757    757    688       C  
ATOM    527  CG2 ILE A  87      12.973  39.521 349.132  1.00 46.59           C  
ANISOU  527  CG2 ILE A  87     4212   5622   7868  -1873    683    775       C  
ATOM    528  CD1 ILE A  87      15.988  40.234 350.391  1.00 48.53           C  
ANISOU  528  CD1 ILE A  87     4857   5623   7961  -1816    643    681       C  
ATOM    529  N   SER A  88      13.060  37.939 353.396  1.00 49.43           N  
ANISOU  529  N   SER A  88     4377   6621   7785  -2317    778   1362       N  
ATOM    530  CA  SER A  88      13.449  37.567 354.754  1.00 50.91           C  
ANISOU  530  CA  SER A  88     4552   6963   7827  -2416    804   1519       C  
ATOM    531  C   SER A  88      14.372  36.338 354.786  1.00 55.22           C  
ANISOU  531  C   SER A  88     5276   7181   8524  -2618    634   1676       C  
ATOM    532  O   SER A  88      14.329  35.495 353.885  1.00 54.67           O  
ANISOU  532  O   SER A  88     5292   6839   8641  -2746    472   1739       O  
ATOM    533  CB  SER A  88      12.196  37.290 355.589  1.00 57.84           C  
ANISOU  533  CB  SER A  88     5124   8355   8497  -2549    882   1748       C  
ATOM    534  OG  SER A  88      12.433  37.337 356.987  1.00 67.88           O  
ANISOU  534  OG  SER A  88     6344   9878   9568  -2571    947   1864       O  
ATOM    535  N   LEU A  89      15.192  36.242 355.852  1.00 52.22           N  
ANISOU  535  N   LEU A  89     4971   6835   8035  -2614    656   1727       N  
ATOM    536  CA  LEU A  89      16.097  35.127 356.121  1.00 52.00           C  
ANISOU  536  CA  LEU A  89     5123   6556   8080  -2739    503   1877       C  
ATOM    537  C   LEU A  89      15.831  34.563 357.526  1.00 59.02           C  
ANISOU  537  C   LEU A  89     5908   7716   8803  -2929    530   2147       C  
ATOM    538  O   LEU A  89      15.942  35.289 358.520  1.00 58.70           O  
ANISOU  538  O   LEU A  89     5764   7976   8565  -2823    685   2102       O  
ATOM    539  CB  LEU A  89      17.568  35.544 355.967  1.00 49.53           C  
ANISOU  539  CB  LEU A  89     4997   6051   7771  -2533    491   1686       C  
ATOM    540  CG  LEU A  89      18.596  34.414 356.030  1.00 54.15           C  
ANISOU  540  CG  LEU A  89     5782   6390   8402  -2551    318   1793       C  
ATOM    541  CD1 LEU A  89      18.634  33.617 354.723  1.00 53.92           C  
ANISOU  541  CD1 LEU A  89     5909   6016   8562  -2514    116   1758       C  
ATOM    542  CD2 LEU A  89      19.967  34.955 356.357  1.00 54.87           C  
ANISOU  542  CD2 LEU A  89     5945   6532   8372  -2380    364   1668       C  
ATOM    543  N   PHE A  90      15.468  33.268 357.596  1.00 58.10           N  
ANISOU  543  N   PHE A  90     5841   7483   8752  -3218    353   2434       N  
ATOM    544  CA  PHE A  90      15.188  32.575 358.853  1.00 60.59           C  
ANISOU  544  CA  PHE A  90     6066   8041   8914  -3466    337   2755       C  
ATOM    545  C   PHE A  90      16.299  31.591 359.197  1.00 64.83           C  
ANISOU  545  C   PHE A  90     6904   8233   9495  -3494    159   2863       C  
ATOM    546  O   PHE A  90      16.669  30.758 358.364  1.00 64.17           O  
ANISOU  546  O   PHE A  90     7102   7701   9579  -3506    -72   2861       O  
ATOM    547  CB  PHE A  90      13.834  31.849 358.806  1.00 65.42           C  
ANISOU  547  CB  PHE A  90     6505   8843   9508  -3850    236   3073       C  
ATOM    548  CG  PHE A  90      12.685  32.673 358.280  1.00 67.07           C  
ANISOU  548  CG  PHE A  90     6414   9408   9662  -3803    377   2979       C  
ATOM    549  CD1 PHE A  90      12.249  33.805 358.960  1.00 70.36           C  
ANISOU  549  CD1 PHE A  90     6532  10371   9830  -3589    629   2882       C  
ATOM    550  CD2 PHE A  90      12.019  32.303 357.118  1.00 69.69           C  
ANISOU  550  CD2 PHE A  90     6775   9546  10158  -3944    241   2987       C  
ATOM    551  CE1 PHE A  90      11.184  34.567 358.471  1.00 71.77           C  
ANISOU  551  CE1 PHE A  90     6450  10905   9914  -3474    748   2785       C  
ATOM    552  CE2 PHE A  90      10.944  33.059 356.636  1.00 72.80           C  
ANISOU  552  CE2 PHE A  90     6873  10313  10474  -3878    375   2908       C  
ATOM    553  CZ  PHE A  90      10.535  34.186 357.316  1.00 71.06           C  
ANISOU  553  CZ  PHE A  90     6360  10645   9993  -3628    630   2808       C  
ATOM    554  N   ILE A  91      16.833  31.695 360.425  1.00 62.23           N  
ANISOU  554  N   ILE A  91     6526   8129   8991  -3462    258   2943       N  
ATOM    555  CA  ILE A  91      17.884  30.806 360.919  1.00 62.93           C  
ANISOU  555  CA  ILE A  91     6874   7969   9067  -3452    111   3057       C  
ATOM    556  C   ILE A  91      17.275  29.880 361.981  1.00 71.81           C  
ANISOU  556  C   ILE A  91     7945   9264  10076  -3806     23   3471       C  
ATOM    557  O   ILE A  91      16.985  30.329 363.091  1.00 73.05           O  
ANISOU  557  O   ILE A  91     7845   9880  10029  -3842    203   3571       O  
ATOM    558  CB  ILE A  91      19.130  31.571 361.445  1.00 63.66           C  
ANISOU  558  CB  ILE A  91     6979   8168   9041  -3146    263   2833       C  
ATOM    559  CG1 ILE A  91      19.653  32.573 360.400  1.00 61.06           C  
ANISOU  559  CG1 ILE A  91     6668   7740   8792  -2880    339   2475       C  
ATOM    560  CG2 ILE A  91      20.232  30.591 361.875  1.00 64.87           C  
ANISOU  560  CG2 ILE A  91     7397   8090   9160  -3084    100   2943       C  
ATOM    561  CD1 ILE A  91      20.455  33.727 360.970  1.00 68.52           C  
ANISOU  561  CD1 ILE A  91     7545   8913   9575  -2685    513   2269       C  
ATOM    562  N   ARG A  92      17.064  28.600 361.627  1.00 70.59           N  
ANISOU  562  N   ARG A  92     8051   8738  10033  -4071   -281   3717       N  
ATOM    563  CA  ARG A  92      16.501  27.594 362.529  1.00 74.58           C  
ANISOU  563  CA  ARG A  92     8573   9328  10437  -4491   -443   4168       C  
ATOM    564  C   ARG A  92      17.588  27.063 363.457  1.00 79.50           C  
ANISOU  564  C   ARG A  92     9415   9833  10959  -4380   -505   4261       C  
ATOM    565  O   ARG A  92      18.705  26.814 362.994  1.00 77.90           O  
ANISOU  565  O   ARG A  92     9548   9218  10831  -4075   -626   4067       O  
ATOM    566  CB  ARG A  92      15.867  26.442 361.728  1.00 77.82           C  
ANISOU  566  CB  ARG A  92     9271   9301  10997  -4846   -810   4393       C  
ATOM    567  CG  ARG A  92      14.538  26.800 361.075  1.00 88.27           C  
ANISOU  567  CG  ARG A  92    10303  10874  12361  -5086   -762   4426       C  
ATOM    568  CD  ARG A  92      14.208  25.888 359.908  1.00 98.58           C  
ANISOU  568  CD  ARG A  92    11968  11629  13860  -5310  -1131   4493       C  
ATOM    569  NE  ARG A  92      14.903  26.283 358.680  1.00102.13           N  
ANISOU  569  NE  ARG A  92    12633  11674  14497  -4871  -1142   4061       N  
ATOM    570  CZ  ARG A  92      15.944  25.638 358.161  1.00115.06           C  
ANISOU  570  CZ  ARG A  92    14742  12749  16227  -4598  -1378   3914       C  
ATOM    571  NH1 ARG A  92      16.425  24.551 358.753  1.00105.76           N  
ANISOU  571  NH1 ARG A  92    13927  11271  14984  -4698  -1640   4146       N  
ATOM    572  NH2 ARG A  92      16.505  26.069 357.039  1.00 97.38           N  
ANISOU  572  NH2 ARG A  92    12613  10273  14114  -4199  -1367   3540       N  
ATOM    573  N   ASP A  93      17.261  26.889 364.763  1.00 78.52           N  
ANISOU  573  N   ASP A  93     9073  10130  10632  -4604   -419   4564       N  
ATOM    574  CA  ASP A  93      18.157  26.395 365.824  1.00 79.43           C  
ANISOU  574  CA  ASP A  93     9328  10241  10610  -4539   -450   4706       C  
ATOM    575  C   ASP A  93      19.544  27.063 365.710  1.00 79.72           C  
ANISOU  575  C   ASP A  93     9451  10201  10640  -4026   -297   4307       C  
ATOM    576  O   ASP A  93      20.562  26.390 365.500  1.00 79.41           O  
ANISOU  576  O   ASP A  93     9777   9764  10632  -3820   -481   4256       O  
ATOM    577  CB  ASP A  93      18.258  24.856 365.791  1.00 84.84           C  
ANISOU  577  CB  ASP A  93    10486  10398  11350  -4803   -866   5041       C  
ATOM    578  N   SER A  94      19.548  28.411 365.792  1.00 73.24           N  
ANISOU  578  N   SER A  94     8302   9778   9748  -3817     15   4026       N  
ATOM    579  CA  SER A  94      20.726  29.268 365.655  1.00 69.50           C  
ANISOU  579  CA  SER A  94     7851   9317   9241  -3419    165   3663       C  
ATOM    580  C   SER A  94      21.780  28.984 366.718  1.00 73.61           C  
ANISOU  580  C   SER A  94     8443   9941   9586  -3301    182   3742       C  
ATOM    581  O   SER A  94      21.458  28.852 367.897  1.00 75.46           O  
ANISOU  581  O   SER A  94     8507  10508   9654  -3462    258   3977       O  
ATOM    582  CB  SER A  94      20.325  30.738 365.709  1.00 71.08           C  
ANISOU  582  CB  SER A  94     7735   9907   9364  -3300    441   3408       C  
ATOM    583  OG  SER A  94      19.703  31.064 366.941  1.00 82.16           O  
ANISOU  583  OG  SER A  94     8847  11821  10548  -3406    602   3566       O  
ATOM    584  N   GLN A  95      23.039  28.890 366.284  1.00 68.47           N  
ANISOU  584  N   GLN A  95     8015   9058   8942  -3006    110   3552       N  
ATOM    585  CA  GLN A  95      24.201  28.634 367.135  1.00 68.70           C  
ANISOU  585  CA  GLN A  95     8124   9191   8787  -2828    114   3588       C  
ATOM    586  C   GLN A  95      24.927  29.952 367.458  1.00 70.23           C  
ANISOU  586  C   GLN A  95     8097   9750   8836  -2634    358   3305       C  
ATOM    587  O   GLN A  95      24.804  30.891 366.667  1.00 67.53           O  
ANISOU  587  O   GLN A  95     7667   9416   8573  -2574    445   3051       O  
ATOM    588  CB  GLN A  95      25.168  27.647 366.435  1.00 70.49           C  
ANISOU  588  CB  GLN A  95     8735   8999   9049  -2581   -151   3565       C  
ATOM    589  CG  GLN A  95      24.553  26.305 366.017  1.00 82.07           C  
ANISOU  589  CG  GLN A  95    10548   9984  10653  -2753   -477   3813       C  
ATOM    590  CD  GLN A  95      23.918  25.537 367.156  1.00 98.78           C  
ANISOU  590  CD  GLN A  95    12706  12136  12688  -3082   -568   4222       C  
ATOM    591  OE1 GLN A  95      24.460  25.437 368.267  1.00 92.34           O  
ANISOU  591  OE1 GLN A  95    11848  11551  11684  -3021   -499   4338       O  
ATOM    592  NE2 GLN A  95      22.753  24.967 366.892  1.00 92.88           N  
ANISOU  592  NE2 GLN A  95    12039  11185  12066  -3467   -742   4473       N  
ATOM    593  N   PRO A  96      25.735  30.054 368.551  1.00 67.69           N  
ANISOU  593  N   PRO A  96     7714   9710   8295  -2544    444   3342       N  
ATOM    594  CA  PRO A  96      26.461  31.314 368.810  1.00 65.71           C  
ANISOU  594  CA  PRO A  96     7299   9773   7894  -2410    625   3077       C  
ATOM    595  C   PRO A  96      27.471  31.653 367.697  1.00 67.80           C  
ANISOU  595  C   PRO A  96     7665   9911   8186  -2201    560   2835       C  
ATOM    596  O   PRO A  96      27.981  32.775 367.648  1.00 65.84           O  
ANISOU  596  O   PRO A  96     7308   9871   7838  -2165    666   2622       O  
ATOM    597  CB  PRO A  96      27.163  31.053 370.150  1.00 68.92           C  
ANISOU  597  CB  PRO A  96     7653  10474   8058  -2372    679   3216       C  
ATOM    598  CG  PRO A  96      26.437  29.909 370.757  1.00 76.02           C  
ANISOU  598  CG  PRO A  96     8617  11284   8985  -2541    580   3569       C  
ATOM    599  CD  PRO A  96      26.032  29.058 369.600  1.00 71.97           C  
ANISOU  599  CD  PRO A  96     8349  10294   8702  -2578    361   3632       C  
ATOM    600  N   SER A  97      27.724  30.685 366.786  1.00 64.75           N  
ANISOU  600  N   SER A  97     7499   9194   7911  -2072    361   2878       N  
ATOM    601  CA  SER A  97      28.595  30.800 365.613  1.00 63.22           C  
ANISOU  601  CA  SER A  97     7381   8921   7718  -1835    271   2684       C  
ATOM    602  C   SER A  97      28.040  31.840 364.638  1.00 65.11           C  
ANISOU  602  C   SER A  97     7528   9087   8124  -1920    335   2476       C  
ATOM    603  O   SER A  97      28.806  32.557 363.995  1.00 63.26           O  
ANISOU  603  O   SER A  97     7246   8959   7833  -1803    337   2297       O  
ATOM    604  CB  SER A  97      28.709  29.449 364.904  1.00 68.29           C  
ANISOU  604  CB  SER A  97     8321   9203   8423  -1635     11   2780       C  
ATOM    605  OG  SER A  97      28.999  28.375 365.784  1.00 79.17           O  
ANISOU  605  OG  SER A  97     9856  10569   9654  -1549    -91   2993       O  
ATOM    606  N   ASP A  98      26.696  31.928 364.563  1.00 61.84           N  
ANISOU  606  N   ASP A  98     7074   8537   7886  -2129    382   2524       N  
ATOM    607  CA  ASP A  98      25.929  32.823 363.696  1.00 59.78           C  
ANISOU  607  CA  ASP A  98     6738   8193   7783  -2199    441   2349       C  
ATOM    608  C   ASP A  98      26.017  34.311 364.094  1.00 61.14           C  
ANISOU  608  C   ASP A  98     6757   8636   7836  -2240    613   2159       C  
ATOM    609  O   ASP A  98      25.551  35.148 363.319  1.00 59.57           O  
ANISOU  609  O   ASP A  98     6536   8361   7737  -2258    644   1992       O  
ATOM    610  CB  ASP A  98      24.452  32.386 363.665  1.00 62.69           C  
ANISOU  610  CB  ASP A  98     7088   8412   8318  -2398    424   2497       C  
ATOM    611  CG  ASP A  98      24.237  30.991 363.116  1.00 75.36           C  
ANISOU  611  CG  ASP A  98     8919   9656  10059  -2422    191   2677       C  
ATOM    612  OD1 ASP A  98      24.910  30.629 362.119  1.00 75.70           O  
ANISOU  612  OD1 ASP A  98     9133   9462  10166  -2223     41   2565       O  
ATOM    613  OD2 ASP A  98      23.394  30.264 363.672  1.00 84.13           O  
ANISOU  613  OD2 ASP A  98    10045  10732  11190  -2644    134   2937       O  
ATOM    614  N   SER A  99      26.597  34.646 365.274  1.00 56.99           N  
ANISOU  614  N   SER A  99     6163   8401   7089  -2249    699   2180       N  
ATOM    615  CA  SER A  99      26.748  36.035 365.719  1.00 55.52           C  
ANISOU  615  CA  SER A  99     5911   8429   6755  -2289    806   1995       C  
ATOM    616  C   SER A  99      27.658  36.785 364.746  1.00 56.74           C  
ANISOU  616  C   SER A  99     6118   8553   6886  -2264    740   1814       C  
ATOM    617  O   SER A  99      28.856  36.500 364.666  1.00 56.27           O  
ANISOU  617  O   SER A  99     6052   8645   6684  -2214    682   1841       O  
ATOM    618  CB  SER A  99      27.291  36.108 367.144  1.00 60.12           C  
ANISOU  618  CB  SER A  99     6430   9320   7091  -2303    877   2066       C  
ATOM    619  OG  SER A  99      26.385  35.549 368.079  1.00 69.99           O  
ANISOU  619  OG  SER A  99     7595  10665   8332  -2351    944   2251       O  
ATOM    620  N   ALA A 100      27.042  37.677 363.938  1.00 51.24           N  
ANISOU  620  N   ALA A 100     5459   7694   6315  -2296    738   1655       N  
ATOM    621  CA  ALA A 100      27.660  38.492 362.886  1.00 49.25           C  
ANISOU  621  CA  ALA A 100     5258   7391   6062  -2323    661   1507       C  
ATOM    622  C   ALA A 100      26.664  39.517 362.320  1.00 51.54           C  
ANISOU  622  C   ALA A 100     5621   7496   6466  -2355    678   1339       C  
ATOM    623  O   ALA A 100      25.521  39.601 362.785  1.00 50.88           O  
ANISOU  623  O   ALA A 100     5519   7380   6433  -2319    761   1328       O  
ATOM    624  CB  ALA A 100      28.162  37.594 361.760  1.00 49.28           C  
ANISOU  624  CB  ALA A 100     5248   7306   6170  -2209    559   1569       C  
ATOM    625  N   THR A 101      27.105  40.292 361.308  1.00 47.54           N  
ANISOU  625  N   THR A 101     5184   6914   5965  -2412    592   1224       N  
ATOM    626  CA  THR A 101      26.267  41.275 360.625  1.00 46.78           C  
ANISOU  626  CA  THR A 101     5197   6613   5965  -2419    577   1063       C  
ATOM    627  C   THR A 101      25.641  40.597 359.422  1.00 48.26           C  
ANISOU  627  C   THR A 101     5320   6612   6406  -2329    571   1087       C  
ATOM    628  O   THR A 101      26.324  39.854 358.710  1.00 47.45           O  
ANISOU  628  O   THR A 101     5153   6521   6354  -2294    504   1163       O  
ATOM    629  CB  THR A 101      27.060  42.527 360.244  1.00 57.34           C  
ANISOU  629  CB  THR A 101     6679   7949   7157  -2580    452    960       C  
ATOM    630  OG1 THR A 101      27.961  42.859 361.306  1.00 60.13           O  
ANISOU  630  OG1 THR A 101     7077   8512   7259  -2701    423    980       O  
ATOM    631  CG2 THR A 101      26.149  43.714 359.938  1.00 56.05           C  
ANISOU  631  CG2 THR A 101     6720   7545   7032  -2564    412    778       C  
ATOM    632  N   TYR A 102      24.341  40.826 359.212  1.00 43.48           N  
ANISOU  632  N   TYR A 102     4725   5870   5926  -2262    631   1017       N  
ATOM    633  CA  TYR A 102      23.609  40.209 358.117  1.00 41.66           C  
ANISOU  633  CA  TYR A 102     4433   5468   5929  -2200    621   1038       C  
ATOM    634  C   TYR A 102      23.154  41.281 357.138  1.00 44.12           C  
ANISOU  634  C   TYR A 102     4832   5629   6303  -2174    592    869       C  
ATOM    635  O   TYR A 102      22.243  42.059 357.427  1.00 44.37           O  
ANISOU  635  O   TYR A 102     4925   5650   6284  -2107    645    759       O  
ATOM    636  CB  TYR A 102      22.455  39.348 358.654  1.00 43.44           C  
ANISOU  636  CB  TYR A 102     4549   5724   6231  -2181    700   1160       C  
ATOM    637  CG  TYR A 102      22.952  38.067 359.296  1.00 45.96           C  
ANISOU  637  CG  TYR A 102     4825   6100   6536  -2222    673   1364       C  
ATOM    638  CD1 TYR A 102      23.432  38.057 360.603  1.00 48.95           C  
ANISOU  638  CD1 TYR A 102     5184   6690   6724  -2253    727   1437       C  
ATOM    639  CD2 TYR A 102      22.976  36.872 358.585  1.00 46.53           C  
ANISOU  639  CD2 TYR A 102     4918   5996   6767  -2207    566   1474       C  
ATOM    640  CE1 TYR A 102      23.930  36.890 361.183  1.00 49.95           C  
ANISOU  640  CE1 TYR A 102     5300   6856   6823  -2273    687   1632       C  
ATOM    641  CE2 TYR A 102      23.460  35.696 359.159  1.00 48.40           C  
ANISOU  641  CE2 TYR A 102     5192   6230   6967  -2211    496   1656       C  
ATOM    642  CZ  TYR A 102      23.941  35.711 360.458  1.00 54.80           C  
ANISOU  642  CZ  TYR A 102     5972   7259   7592  -2247    563   1742       C  
ATOM    643  OH  TYR A 102      24.429  34.556 361.019  1.00 54.48           O  
ANISOU  643  OH  TYR A 102     5993   7204   7504  -2235    483   1929       O  
ATOM    644  N   LEU A 103      23.852  41.345 355.991  1.00 39.22           N  
ANISOU  644  N   LEU A 103     4219   4927   5754  -2196    496    851       N  
ATOM    645  CA  LEU A 103      23.619  42.313 354.922  1.00 38.40           C  
ANISOU  645  CA  LEU A 103     4203   4680   5706  -2197    441    724       C  
ATOM    646  C   LEU A 103      22.789  41.720 353.796  1.00 42.54           C  
ANISOU  646  C   LEU A 103     4633   5068   6463  -2093    448    720       C  
ATOM    647  O   LEU A 103      23.042  40.591 353.382  1.00 41.39           O  
ANISOU  647  O   LEU A 103     4390   4924   6412  -2052    411    813       O  
ATOM    648  CB  LEU A 103      24.960  42.810 354.347  1.00 38.04           C  
ANISOU  648  CB  LEU A 103     4195   4718   5539  -2335    313    742       C  
ATOM    649  CG  LEU A 103      25.811  43.712 355.228  1.00 43.28           C  
ANISOU  649  CG  LEU A 103     4996   5497   5952  -2514    251    738       C  
ATOM    650  CD1 LEU A 103      26.908  42.923 355.918  1.00 43.68           C  
ANISOU  650  CD1 LEU A 103     4908   5827   5863  -2561    252    879       C  
ATOM    651  CD2 LEU A 103      26.420  44.821 354.416  1.00 44.96           C  
ANISOU  651  CD2 LEU A 103     5346   5667   6069  -2706     94    710       C  
ATOM    652  N   CYS A 104      21.823  42.494 353.273  1.00 40.52           N  
ANISOU  652  N   CYS A 104     4432   4689   6274  -2029    473    601       N  
ATOM    653  CA  CYS A 104      21.003  42.078 352.140  1.00 40.04           C  
ANISOU  653  CA  CYS A 104     4280   4516   6418  -1944    476    583       C  
ATOM    654  C   CYS A 104      21.192  43.053 350.968  1.00 40.02           C  
ANISOU  654  C   CYS A 104     4360   4404   6440  -1939    397    480       C  
ATOM    655  O   CYS A 104      21.327  44.266 351.163  1.00 39.45           O  
ANISOU  655  O   CYS A 104     4469   4279   6241  -1972    360    390       O  
ATOM    656  CB  CYS A 104      19.533  41.917 352.522  1.00 42.50           C  
ANISOU  656  CB  CYS A 104     4516   4858   6774  -1863    583    572       C  
ATOM    657  SG  CYS A 104      18.594  43.468 352.621  1.00 48.57           S  
ANISOU  657  SG  CYS A 104     5431   5637   7386  -1711    633    383       S  
ATOM    658  N   ALA A 105      21.266  42.496 349.759  1.00 33.91           N  
ANISOU  658  N   ALA A 105     3481   3593   5812  -1899    343    503       N  
ATOM    659  CA  ALA A 105      21.434  43.255 348.527  1.00 32.27           C  
ANISOU  659  CA  ALA A 105     3298   3326   5636  -1895    267    441       C  
ATOM    660  C   ALA A 105      20.419  42.796 347.517  1.00 33.34           C  
ANISOU  660  C   ALA A 105     3336   3359   5973  -1763    295    391       C  
ATOM    661  O   ALA A 105      20.023  41.630 347.541  1.00 33.18           O  
ANISOU  661  O   ALA A 105     3211   3328   6069  -1713    309    444       O  
ATOM    662  CB  ALA A 105      22.840  43.083 347.980  1.00 32.82           C  
ANISOU  662  CB  ALA A 105     3289   3562   5620  -1959    156    528       C  
ATOM    663  N   MET A 106      19.973  43.708 346.645  1.00 27.89           N  
ANISOU  663  N   MET A 106     2708   2583   5308  -1711    280    297       N  
ATOM    664  CA  MET A 106      18.958  43.404 345.638  1.00 26.95           C  
ANISOU  664  CA  MET A 106     2514   2426   5301  -1492    299    229       C  
ATOM    665  C   MET A 106      19.355  43.981 344.270  1.00 30.75           C  
ANISOU  665  C   MET A 106     2958   2845   5883  -1574    224    207       C  
ATOM    666  O   MET A 106      19.900  45.085 344.207  1.00 30.19           O  
ANISOU  666  O   MET A 106     3033   2748   5688  -1663    158    199       O  
ATOM    667  CB  MET A 106      17.592  43.941 346.089  1.00 29.15           C  
ANISOU  667  CB  MET A 106     2805   2646   5624  -1494    417    157       C  
ATOM    668  CG  MET A 106      17.141  43.423 347.451  1.00 33.26           C  
ANISOU  668  CG  MET A 106     3277   3284   6076  -1514    508    218       C  
ATOM    669  SD  MET A 106      15.509  44.013 347.941  1.00 38.39           S  
ANISOU  669  SD  MET A 106     3887   4074   6627  -1333    634    136       S  
ATOM    670  CE  MET A 106      15.652  43.980 349.698  1.00 36.42           C  
ANISOU  670  CE  MET A 106     3674   3993   6170  -1360    696    188       C  
ATOM    671  N   SER A 107      19.111  43.207 343.184  1.00 28.22           N  
ANISOU  671  N   SER A 107     2512   2557   5655  -1386    190    194       N  
ATOM    672  CA  SER A 107      19.424  43.541 341.778  1.00 28.02           C  
ANISOU  672  CA  SER A 107     2422   2563   5661  -1324    113    173       C  
ATOM    673  C   SER A 107      18.179  43.446 340.894  1.00 32.70           C  
ANISOU  673  C   SER A 107     2904   3039   6483  -1285    165     88       C  
ATOM    674  O   SER A 107      17.105  43.111 341.395  1.00 34.59           O  
ANISOU  674  O   SER A 107     3126   3229   6788  -1257    250     63       O  
ATOM    675  CB  SER A 107      20.478  42.579 341.232  1.00 31.05           C  
ANISOU  675  CB  SER A 107     2629   3083   6084  -1364     17    242       C  
ATOM    676  OG  SER A 107      21.664  42.562 342.007  1.00 44.96           O  
ANISOU  676  OG  SER A 107     4414   5005   7663  -1472    -22    339       O  
ATOM    677  N   GLY A 108      18.341  43.685 339.590  1.00 27.59           N  
ANISOU  677  N   GLY A 108     2192   2433   5857  -1185    103     60       N  
ATOM    678  CA  GLY A 108      17.270  43.533 338.613  1.00 26.59           C  
ANISOU  678  CA  GLY A 108     1974   2255   5874  -1043    132    -25       C  
ATOM    679  C   GLY A 108      16.471  44.771 338.283  1.00 30.94           C  
ANISOU  679  C   GLY A 108     2595   2732   6428  -1029    184    -93       C  
ATOM    680  O   GLY A 108      15.833  44.819 337.225  1.00 31.00           O  
ANISOU  680  O   GLY A 108     2506   2748   6526   -915    183   -149       O  
ATOM    681  N   ASP A 109      16.459  45.766 339.185  1.00 27.78           N  
ANISOU  681  N   ASP A 109     2406   2256   5894  -1081    213   -103       N  
ATOM    682  CA  ASP A 109      15.713  46.995 338.922  1.00 28.19           C  
ANISOU  682  CA  ASP A 109     2627   2203   5881   -972    222   -188       C  
ATOM    683  C   ASP A 109      16.576  47.907 338.059  1.00 31.88           C  
ANISOU  683  C   ASP A 109     3207   2622   6285  -1075     81   -130       C  
ATOM    684  O   ASP A 109      17.520  48.525 338.560  1.00 32.29           O  
ANISOU  684  O   ASP A 109     3441   2634   6195  -1269    -23    -49       O  
ATOM    685  CB  ASP A 109      15.267  47.688 340.227  1.00 31.35           C  
ANISOU  685  CB  ASP A 109     3264   2528   6121   -925    265   -246       C  
ATOM    686  CG  ASP A 109      14.247  48.807 340.065  1.00 41.69           C  
ANISOU  686  CG  ASP A 109     4766   3748   7328   -686    277   -375       C  
ATOM    687  OD1 ASP A 109      13.988  49.223 338.908  1.00 42.04           O  
ANISOU  687  OD1 ASP A 109     4802   3745   7426   -600    240   -403       O  
ATOM    688  OD2 ASP A 109      13.709  49.268 341.093  1.00 49.10           O  
ANISOU  688  OD2 ASP A 109     5868   4684   8105   -547    316   -454       O  
ATOM    689  N   LEU A 110      16.244  47.993 336.753  1.00 27.04           N  
ANISOU  689  N   LEU A 110     2475   2041   5760   -975     66   -151       N  
ATOM    690  CA  LEU A 110      16.976  48.815 335.784  1.00 26.51           C  
ANISOU  690  CA  LEU A 110     2463   1983   5625  -1085    -74    -60       C  
ATOM    691  C   LEU A 110      16.893  50.298 336.089  1.00 30.88           C  
ANISOU  691  C   LEU A 110     3418   2294   6023  -1147   -182    -63       C  
ATOM    692  O   LEU A 110      17.588  51.082 335.446  1.00 32.01           O  
ANISOU  692  O   LEU A 110     3671   2416   6074  -1329   -342     60       O  
ATOM    693  CB  LEU A 110      16.466  48.569 334.370  1.00 25.57           C  
ANISOU  693  CB  LEU A 110     2118   1965   5633   -923    -52    -96       C  
ATOM    694  CG  LEU A 110      17.434  47.840 333.487  1.00 29.61           C  
ANISOU  694  CG  LEU A 110     2356   2739   6154   -979   -127      5       C  
ATOM    695  CD1 LEU A 110      16.710  46.897 332.602  1.00 28.98           C  
ANISOU  695  CD1 LEU A 110     2018   2751   6241   -754    -66    -97       C  
ATOM    696  CD2 LEU A 110      18.263  48.792 332.676  1.00 32.59           C  
ANISOU  696  CD2 LEU A 110     2777   3209   6396  -1141   -271    153       C  
ATOM    697  N   ASN A 111      16.063  50.686 337.066  1.00 26.69           N  
ANISOU  697  N   ASN A 111     3118   1592   5430   -993   -123   -192       N  
ATOM    698  CA  ASN A 111      15.918  52.082 337.441  1.00 28.31           C  
ANISOU  698  CA  ASN A 111     3792   1512   5454   -968   -262   -241       C  
ATOM    699  C   ASN A 111      16.712  52.386 338.718  1.00 32.41           C  
ANISOU  699  C   ASN A 111     4576   1924   5814  -1178   -361   -201       C  
ATOM    700  O   ASN A 111      17.157  53.527 338.885  1.00 34.95           O  
ANISOU  700  O   ASN A 111     5330   1984   5965  -1311   -576   -174       O  
ATOM    701  CB  ASN A 111      14.453  52.453 337.561  1.00 30.17           C  
ANISOU  701  CB  ASN A 111     4126   1680   5656   -565   -158   -435       C  
ATOM    702  CG  ASN A 111      13.669  52.084 336.312  1.00 44.95           C  
ANISOU  702  CG  ASN A 111     5704   3699   7677   -376    -54   -469       C  
ATOM    703  OD1 ASN A 111      12.860  51.145 336.316  1.00 41.43           O  
ANISOU  703  OD1 ASN A 111     4920   3477   7344   -237    124   -523       O  
ATOM    704  ND2 ASN A 111      13.949  52.759 335.197  1.00 28.08           N  
ANISOU  704  ND2 ASN A 111     3675   1454   5538   -416   -182   -413       N  
ATOM    705  N   THR A 112      16.963  51.360 339.572  1.00 25.73           N  
ANISOU  705  N   THR A 112     3483   1305   4988  -1203   -234   -178       N  
ATOM    706  CA  THR A 112      17.787  51.522 340.775  1.00 25.64           C  
ANISOU  706  CA  THR A 112     3642   1316   4784  -1354   -307   -124       C  
ATOM    707  C   THR A 112      19.183  50.982 340.448  1.00 26.49           C  
ANISOU  707  C   THR A 112     3534   1657   4874  -1646   -374     75       C  
ATOM    708  O   THR A 112      19.356  49.786 340.224  1.00 24.81           O  
ANISOU  708  O   THR A 112     2966   1724   4738  -1530   -252    110       O  
ATOM    709  CB  THR A 112      17.139  50.885 342.014  1.00 31.22           C  
ANISOU  709  CB  THR A 112     4308   1998   5554  -1245   -141   -245       C  
ATOM    710  OG1 THR A 112      15.781  51.318 342.095  1.00 35.08           O  
ANISOU  710  OG1 THR A 112     4899   2428   6002   -884    -65   -415       O  
ATOM    711  CG2 THR A 112      17.860  51.264 343.310  1.00 28.44           C  
ANISOU  711  CG2 THR A 112     4218   1571   5018  -1402   -231   -232       C  
ATOM    712  N   ASN A 113      20.160  51.900 340.371  1.00 25.14           N  
ANISOU  712  N   ASN A 113     3572   1601   4379  -1766   -592    225       N  
ATOM    713  CA  ASN A 113      21.575  51.690 340.033  1.00 25.29           C  
ANISOU  713  CA  ASN A 113     3440   1944   4225  -1988   -707    447       C  
ATOM    714  C   ASN A 113      21.698  50.887 338.717  1.00 27.83           C  
ANISOU  714  C   ASN A 113     3365   2407   4803  -2072   -642    513       C  
ATOM    715  O   ASN A 113      22.549  50.004 338.582  1.00 27.15           O  
ANISOU  715  O   ASN A 113     2995   2652   4668  -2113   -623    624       O  
ATOM    716  CB  ASN A 113      22.355  51.054 341.188  1.00 22.51           C  
ANISOU  716  CB  ASN A 113     3026   1863   3666  -1909   -661    484       C  
ATOM    717  CG  ASN A 113      22.103  51.696 342.529  1.00 44.96           C  
ANISOU  717  CG  ASN A 113     6244   3998   6842  -2603   -719    383       C  
ATOM    718  OD1 ASN A 113      21.756  51.023 343.500  1.00 46.08           O  
ANISOU  718  OD1 ASN A 113     6330   4154   7025  -2419   -564    272       O  
ATOM    719  ND2 ASN A 113      22.231  53.012 342.617  1.00 37.17           N  
ANISOU  719  ND2 ASN A 113     5697   2746   5681  -2834   -968    422       N  
ATOM    720  N   ALA A 114      20.821  51.226 337.744  1.00 25.48           N  
ANISOU  720  N   ALA A 114     3080   2083   4518  -1734   -617    437       N  
ATOM    721  CA  ALA A 114      20.726  50.638 336.412  1.00 24.49           C  
ANISOU  721  CA  ALA A 114     2660   2159   4485  -1548   -566    464       C  
ATOM    722  C   ALA A 114      20.821  49.077 336.412  1.00 26.51           C  
ANISOU  722  C   ALA A 114     2544   2551   4979  -1510   -414    412       C  
ATOM    723  O   ALA A 114      21.418  48.485 335.512  1.00 25.94           O  
ANISOU  723  O   ALA A 114     2238   2744   4874  -1437   -436    491       O  
ATOM    724  CB  ALA A 114      21.787  51.240 335.509  1.00 26.32           C  
ANISOU  724  CB  ALA A 114     2851   2572   4580  -1896   -762    706       C  
ATOM    725  N   GLY A 115      20.210  48.439 337.406  1.00 23.74           N  
ANISOU  725  N   GLY A 115     2259   2147   4616  -1217   -284    282       N  
ATOM    726  CA  GLY A 115      20.186  46.984 337.502  1.00 22.94           C  
ANISOU  726  CA  GLY A 115     1963   2141   4613  -1026   -187    236       C  
ATOM    727  C   GLY A 115      21.114  46.369 338.526  1.00 26.91           C  
ANISOU  727  C   GLY A 115     2343   2714   5167  -1378   -198    314       C  
ATOM    728  O   GLY A 115      20.797  45.309 339.075  1.00 25.66           O  
ANISOU  728  O   GLY A 115     2130   2541   5079  -1213   -121    256       O  
ATOM    729  N   LYS A 116      22.276  47.024 338.778  1.00 26.32           N  
ANISOU  729  N   LYS A 116     2382   2807   4814  -1550   -319    460       N  
ATOM    730  CA  LYS A 116      23.310  46.582 339.726  1.00 26.88           C  
ANISOU  730  CA  LYS A 116     2417   3058   4738  -1693   -345    554       C  
ATOM    731  C   LYS A 116      22.753  46.532 341.158  1.00 31.15           C  
ANISOU  731  C   LYS A 116     3014   3313   5510  -1963   -238    469       C  
ATOM    732  O   LYS A 116      21.799  47.252 341.474  1.00 31.02           O  
ANISOU  732  O   LYS A 116     3217   3011   5560  -1933   -197    360       O  
ATOM    733  CB  LYS A 116      24.542  47.493 339.646  1.00 30.22           C  
ANISOU  733  CB  LYS A 116     2813   3695   4974  -2163   -507    761       C  
ATOM    734  N   SER A 117      23.325  45.645 342.003  1.00 29.25           N  
ANISOU  734  N   SER A 117     2728   3243   5143  -1855   -211    506       N  
ATOM    735  CA  SER A 117      22.881  45.411 343.382  1.00 29.04           C  
ANISOU  735  CA  SER A 117     2827   3076   5130  -1838   -119    446       C  
ATOM    736  C   SER A 117      22.982  46.655 344.280  1.00 31.32           C  
ANISOU  736  C   SER A 117     3351   3171   5379  -2205   -157    451       C  
ATOM    737  O   SER A 117      23.956  47.414 344.222  1.00 31.31           O  
ANISOU  737  O   SER A 117     3455   3299   5142  -2391   -305    558       O  
ATOM    738  CB  SER A 117      23.635  44.248 344.019  1.00 32.92           C  
ANISOU  738  CB  SER A 117     3108   3742   5658  -1965    -94    535       C  
ATOM    739  OG  SER A 117      24.927  44.621 344.468  1.00 47.11           O  
ANISOU  739  OG  SER A 117     4863   5829   7207  -2166   -195    675       O  
ATOM    740  N   THR A 118      21.926  46.835 345.095  1.00 28.04           N  
ANISOU  740  N   THR A 118     3135   2627   4894  -1890    -73    309       N  
ATOM    741  CA  THR A 118      21.716  47.897 346.076  1.00 28.34           C  
ANISOU  741  CA  THR A 118     3479   2488   4803  -1989   -113    244       C  
ATOM    742  C   THR A 118      21.793  47.243 347.437  1.00 31.12           C  
ANISOU  742  C   THR A 118     3776   2838   5210  -2129     -9    257       C  
ATOM    743  O   THR A 118      21.028  46.319 347.694  1.00 30.40           O  
ANISOU  743  O   THR A 118     3517   2791   5245  -1955    134    230       O  
ATOM    744  CB  THR A 118      20.349  48.571 345.818  1.00 32.82           C  
ANISOU  744  CB  THR A 118     4207   2725   5538  -1921    -72     89       C  
ATOM    745  OG1 THR A 118      20.276  49.012 344.466  1.00 30.30           O  
ANISOU  745  OG1 THR A 118     3862   2351   5301  -1919   -141    103       O  
ATOM    746  CG2 THR A 118      20.071  49.738 346.751  1.00 34.33           C  
ANISOU  746  CG2 THR A 118     4815   2699   5530  -1905   -173    -22       C  
ATOM    747  N   PHE A 119      22.709  47.686 348.297  1.00 29.56           N  
ANISOU  747  N   PHE A 119     3727   2727   4777  -2279   -105    312       N  
ATOM    748  CA  PHE A 119      22.865  47.093 349.623  1.00 30.05           C  
ANISOU  748  CA  PHE A 119     3740   2872   4804  -2329    -16    333       C  
ATOM    749  C   PHE A 119      22.068  47.830 350.689  1.00 37.27           C  
ANISOU  749  C   PHE A 119     4922   3632   5605  -2213      3    187       C  
ATOM    750  O   PHE A 119      22.005  49.060 350.667  1.00 37.68           O  
ANISOU  750  O   PHE A 119     5311   3472   5534  -2244   -141     94       O  
ATOM    751  CB  PHE A 119      24.349  47.062 350.033  1.00 32.59           C  
ANISOU  751  CB  PHE A 119     4026   3412   4944  -2600   -119    480       C  
ATOM    752  CG  PHE A 119      25.136  45.901 349.475  1.00 33.24           C  
ANISOU  752  CG  PHE A 119     3775   3783   5072  -2580    -86    616       C  
ATOM    753  CD1 PHE A 119      25.751  45.989 348.230  1.00 36.30           C  
ANISOU  753  CD1 PHE A 119     4022   4318   5454  -2643   -179    700       C  
ATOM    754  CD2 PHE A 119      25.278  44.723 350.201  1.00 35.06           C  
ANISOU  754  CD2 PHE A 119     3848   4154   5318  -2468     17    661       C  
ATOM    755  CE1 PHE A 119      26.479  44.909 347.711  1.00 36.55           C  
ANISOU  755  CE1 PHE A 119     3760   4653   5475  -2531   -169    796       C  
ATOM    756  CE2 PHE A 119      26.016  43.649 349.689  1.00 37.24           C  
ANISOU  756  CE2 PHE A 119     3883   4669   5596  -2376      7    761       C  
ATOM    757  CZ  PHE A 119      26.604  43.748 348.443  1.00 35.21           C  
ANISOU  757  CZ  PHE A 119     3490   4573   5314  -2377    -85    813       C  
ATOM    758  N   GLY A 120      21.493  47.063 351.621  1.00 36.36           N  
ANISOU  758  N   GLY A 120     4672   3640   5503  -2069    156    178       N  
ATOM    759  CA  GLY A 120      20.800  47.576 352.800  1.00 39.10           C  
ANISOU  759  CA  GLY A 120     5194   3971   5691  -1907    195     55       C  
ATOM    760  C   GLY A 120      21.842  48.030 353.817  1.00 48.46           C  
ANISOU  760  C   GLY A 120     6576   5180   6657  -2092     86     70       C  
ATOM    761  O   GLY A 120      23.041  47.768 353.627  1.00 49.14           O  
ANISOU  761  O   GLY A 120     6605   5347   6720  -2361      3    204       O  
ATOM    762  N   ASP A 121      21.420  48.730 354.896  1.00 47.52           N  
ANISOU  762  N   ASP A 121     6679   5036   6340  -1934     75    -68       N  
ATOM    763  CA  ASP A 121      22.348  49.245 355.921  1.00 48.88           C  
ANISOU  763  CA  ASP A 121     7080   5212   6281  -2098    -51    -80       C  
ATOM    764  C   ASP A 121      23.047  48.111 356.684  1.00 50.70           C  
ANISOU  764  C   ASP A 121     7002   5740   6520  -2232     72     89       C  
ATOM    765  O   ASP A 121      24.263  48.167 356.856  1.00 49.71           O  
ANISOU  765  O   ASP A 121     6912   5682   6295  -2511    -35    188       O  
ATOM    766  CB  ASP A 121      21.633  50.182 356.902  1.00 53.67           C  
ANISOU  766  CB  ASP A 121     8004   5738   6652  -1807   -100   -300       C  
ATOM    767  N   GLY A 122      22.281  47.100 357.102  1.00 46.95           N  
ANISOU  767  N   GLY A 122     6232   5461   6147  -2049    276    142       N  
ATOM    768  CA  GLY A 122      22.789  45.937 357.823  1.00 46.39           C  
ANISOU  768  CA  GLY A 122     5897   5639   6092  -2134    385    312       C  
ATOM    769  C   GLY A 122      22.172  45.709 359.188  1.00 52.34           C  
ANISOU  769  C   GLY A 122     6591   6595   6702  -1972    501    294       C  
ATOM    770  O   GLY A 122      21.777  46.666 359.861  1.00 53.53           O  
ANISOU  770  O   GLY A 122     6969   6722   6646  -1823    453    126       O  
ATOM    771  N   THR A 123      22.094  44.428 359.604  1.00 49.71           N  
ANISOU  771  N   THR A 123     5970   6465   6452  -1988    632    473       N  
ATOM    772  CA  THR A 123      21.535  44.005 360.895  1.00 51.78           C  
ANISOU  772  CA  THR A 123     6103   6997   6576  -1877    752    526       C  
ATOM    773  C   THR A 123      22.590  43.239 361.705  1.00 57.46           C  
ANISOU  773  C   THR A 123     6724   7868   7239  -2036    766    692       C  
ATOM    774  O   THR A 123      23.118  42.229 361.230  1.00 56.32           O  
ANISOU  774  O   THR A 123     6444   7704   7251  -2143    767    857       O  
ATOM    775  CB  THR A 123      20.258  43.142 360.709  1.00 58.58           C  
ANISOU  775  CB  THR A 123     6704   7995   7557  -1775    878    633       C  
ATOM    776  OG1 THR A 123      19.410  43.715 359.713  1.00 58.14           O  
ANISOU  776  OG1 THR A 123     6710   7806   7575  -1638    861    495       O  
ATOM    777  CG2 THR A 123      19.473  42.962 362.012  1.00 58.88           C  
ANISOU  777  CG2 THR A 123     6585   8401   7385  -1646    993    690       C  
ATOM    778  N   THR A 124      22.881  43.708 362.929  1.00 56.11           N  
ANISOU  778  N   THR A 124     6643   7851   6824  -2014    761    635       N  
ATOM    779  CA  THR A 124      23.830  43.022 363.800  1.00 56.20           C  
ANISOU  779  CA  THR A 124     6557   8051   6748  -2139    783    787       C  
ATOM    780  C   THR A 124      23.049  42.028 364.675  1.00 61.44           C  
ANISOU  780  C   THR A 124     6976   8973   7397  -2059    928    958       C  
ATOM    781  O   THR A 124      21.981  42.358 365.205  1.00 62.65           O  
ANISOU  781  O   THR A 124     7077   9294   7435  -1889   1001    898       O  
ATOM    782  CB  THR A 124      24.724  43.998 364.587  1.00 65.63           C  
ANISOU  782  CB  THR A 124     7967   9286   7682  -2212    680    664       C  
ATOM    783  OG1 THR A 124      25.602  43.244 365.428  1.00 65.21           O  
ANISOU  783  OG1 THR A 124     7776   9468   7533  -2313    721    824       O  
ATOM    784  CG2 THR A 124      23.936  45.034 365.403  1.00 66.98           C  
ANISOU  784  CG2 THR A 124     8329   9491   7630  -2000    661    449       C  
ATOM    785  N   LEU A 125      23.570  40.797 364.776  1.00 57.27           N  
ANISOU  785  N   LEU A 125     6302   8499   6960  -2171    950   1184       N  
ATOM    786  CA  LEU A 125      22.953  39.715 365.535  1.00 57.89           C  
ANISOU  786  CA  LEU A 125     6175   8784   7035  -2178   1041   1412       C  
ATOM    787  C   LEU A 125      23.948  39.108 366.525  1.00 63.28           C  
ANISOU  787  C   LEU A 125     6823   9637   7585  -2245   1047   1557       C  
ATOM    788  O   LEU A 125      25.106  38.868 366.178  1.00 61.68           O  
ANISOU  788  O   LEU A 125     6691   9342   7402  -2302    971   1574       O  
ATOM    789  CB  LEU A 125      22.417  38.642 364.561  1.00 56.80           C  
ANISOU  789  CB  LEU A 125     5957   8464   7159  -2252   1011   1578       C  
ATOM    790  CG  LEU A 125      21.940  37.309 365.143  1.00 62.45           C  
ANISOU  790  CG  LEU A 125     6519   9309   7902  -2358   1032   1880       C  
ATOM    791  CD1 LEU A 125      20.644  37.467 365.922  1.00 64.60           C  
ANISOU  791  CD1 LEU A 125     6590   9929   8027  -2332   1144   1946       C  
ATOM    792  CD2 LEU A 125      21.781  36.282 364.061  1.00 63.66           C  
ANISOU  792  CD2 LEU A 125     6712   9169   8306  -2453    921   2011       C  
ATOM    793  N   THR A 126      23.478  38.867 367.760  1.00 62.59           N  
ANISOU  793  N   THR A 126     6598   9854   7328  -2215   1139   1669       N  
ATOM    794  CA  THR A 126      24.242  38.256 368.847  1.00 63.70           C  
ANISOU  794  CA  THR A 126     6680  10202   7321  -2262   1161   1827       C  
ATOM    795  C   THR A 126      23.423  37.090 369.410  1.00 70.04           C  
ANISOU  795  C   THR A 126     7294  11168   8150  -2336   1211   2137       C  
ATOM    796  O   THR A 126      22.282  37.286 369.841  1.00 70.80           O  
ANISOU  796  O   THR A 126     7227  11522   8152  -2300   1293   2179       O  
ATOM    797  CB  THR A 126      24.638  39.296 369.910  1.00 73.13           C  
ANISOU  797  CB  THR A 126     7920  11639   8227  -2176   1195   1653       C  
ATOM    798  OG1 THR A 126      23.566  40.221 370.110  1.00 73.42           O  
ANISOU  798  OG1 THR A 126     7936  11815   8146  -2014   1247   1501       O  
ATOM    799  CG2 THR A 126      25.901  40.056 369.532  1.00 71.49           C  
ANISOU  799  CG2 THR A 126     7922  11275   7966  -2229   1087   1455       C  
ATOM    800  N   VAL A 127      23.989  35.870 369.341  1.00 67.90           N  
ANISOU  800  N   VAL A 127     7057  10759   7984  -2435   1134   2363       N  
ATOM    801  CA  VAL A 127      23.345  34.636 369.802  1.00 70.22           C  
ANISOU  801  CA  VAL A 127     7250  11122   8309  -2575   1113   2705       C  
ATOM    802  C   VAL A 127      24.015  34.197 371.113  1.00 77.25           C  
ANISOU  802  C   VAL A 127     8085  12280   8987  -2578   1151   2866       C  
ATOM    803  O   VAL A 127      25.105  33.612 371.106  1.00 76.44           O  
ANISOU  803  O   VAL A 127     8113  12053   8876  -2539   1076   2907       O  
ATOM    804  CB  VAL A 127      23.317  33.510 368.724  1.00 73.60           C  
ANISOU  804  CB  VAL A 127     7835  11140   8991  -2672    944   2857       C  
ATOM    805  CG1 VAL A 127      22.647  32.242 369.257  1.00 76.04           C  
ANISOU  805  CG1 VAL A 127     8102  11479   9311  -2888    865   3244       C  
ATOM    806  CG2 VAL A 127      22.622  33.981 367.447  1.00 71.80           C  
ANISOU  806  CG2 VAL A 127     7639  10680   8961  -2663    916   2688       C  
ATOM    807  N   LYS A 128      23.346  34.518 372.238  1.00 76.93           N  
ANISOU  807  N   LYS A 128     7829  12663   8740  -2586   1269   2951       N  
ATOM    808  CA  LYS A 128      23.782  34.228 373.606  1.00 79.06           C  
ANISOU  808  CA  LYS A 128     7992  13271   8775  -2584   1328   3109       C  
ATOM    809  C   LYS A 128      23.857  32.704 373.835  1.00 86.68           C  
ANISOU  809  C   LYS A 128     9002  14120   9814  -2767   1216   3504       C  
ATOM    810  O   LYS A 128      22.927  31.994 373.443  1.00 87.50           O  
ANISOU  810  O   LYS A 128     9083  14113  10049  -2960   1134   3734       O  
ATOM    811  CB  LYS A 128      22.842  34.898 374.626  1.00 83.44           C  
ANISOU  811  CB  LYS A 128     8279  14351   9073  -2517   1469   3110       C  
ATOM    812  CG  LYS A 128      22.866  36.432 374.594  1.00 92.24           C  
ANISOU  812  CG  LYS A 128     9441  15563  10043  -2273   1534   2698       C  
ATOM    813  CD  LYS A 128      21.770  37.056 375.464  1.00104.15           C  
ANISOU  813  CD  LYS A 128    10699  17603  11269  -2112   1647   2674       C  
ATOM    814  CE  LYS A 128      20.457  37.247 374.734  1.00114.60           C  
ANISOU  814  CE  LYS A 128    11924  18956  12662  -2073   1659   2639       C  
ATOM    815  NZ  LYS A 128      19.394  37.772 375.631  1.00124.97           N  
ANISOU  815  NZ  LYS A 128    12949  20903  13630  -1854   1767   2632       N  
ATOM    816  N   PRO A 129      24.960  32.179 374.429  1.00 85.15           N  
ANISOU  816  N   PRO A 129     8901  13931   9522  -2718   1181   3592       N  
ATOM    817  CA  PRO A 129      25.078  30.718 374.600  1.00 87.37           C  
ANISOU  817  CA  PRO A 129     9313  14025   9858  -2854   1027   3958       C  
ATOM    818  C   PRO A 129      24.212  30.137 375.716  1.00 96.01           C  
ANISOU  818  C   PRO A 129    10201  15473  10805  -3069   1055   4336       C  
ATOM    819  O   PRO A 129      23.811  30.855 376.634  1.00 96.18           O  
ANISOU  819  O   PRO A 129     9941  15996  10608  -3030   1227   4299       O  
ATOM    820  CB  PRO A 129      26.560  30.527 374.929  1.00 88.40           C  
ANISOU  820  CB  PRO A 129     9585  14129   9872  -2660   1000   3887       C  
ATOM    821  CG  PRO A 129      26.954  31.790 375.600  1.00 91.63           C  
ANISOU  821  CG  PRO A 129     9813  14929  10073  -2540   1181   3626       C  
ATOM    822  CD  PRO A 129      26.169  32.876 374.921  1.00 85.71           C  
ANISOU  822  CD  PRO A 129     8991  14166   9409  -2540   1251   3369       C  
ATOM    823  N   ASN A 130      23.954  28.816 375.636  1.00 96.59           N  
ANISOU  823  N   ASN A 130    10437  15292  10971  -3293    856   4711       N  
ATOM    824  CA  ASN A 130      23.192  28.067 376.636  1.00100.94           C  
ANISOU  824  CA  ASN A 130    10822  16156  11376  -3580    826   5159       C  
ATOM    825  C   ASN A 130      24.129  27.771 377.809  1.00108.12           C  
ANISOU  825  C   ASN A 130    11731  17281  12067  -3458    870   5261       C  
ATOM    826  O   ASN A 130      24.829  26.753 377.820  1.00108.40           O  
ANISOU  826  O   ASN A 130    12078  16971  12137  -3436    686   5419       O  
ATOM    827  CB  ASN A 130      22.587  26.794 376.030  1.00103.07           C  
ANISOU  827  CB  ASN A 130    11339  16001  11823  -3920    538   5532       C  
ATOM    828  CG  ASN A 130      21.539  26.156 376.901  1.00127.80           C  
ANISOU  828  CG  ASN A 130    14245  19516  14799  -4328    489   6038       C  
ATOM    829  OD1 ASN A 130      20.434  26.680 377.074  1.00121.29           O  
ANISOU  829  OD1 ASN A 130    13032  19183  13870  -4484    622   6112       O  
ATOM    830  ND2 ASN A 130      21.856  24.999 377.460  1.00123.55           N  
ANISOU  830  ND2 ASN A 130    13943  18791  14211  -4507    280   6417       N  
ATOM    831  N   ILE A 131      24.175  28.727 378.760  1.00106.66           N  
ANISOU  831  N   ILE A 131    11221  17668  11639  -3325   1105   5127       N  
ATOM    832  CA  ILE A 131      25.012  28.771 379.967  1.00108.23           C  
ANISOU  832  CA  ILE A 131    11334  18203  11587  -3179   1203   5153       C  
ATOM    833  C   ILE A 131      25.113  27.427 380.699  1.00117.23           C  
ANISOU  833  C   ILE A 131    12570  19320  12651  -3374   1054   5635       C  
ATOM    834  O   ILE A 131      26.241  27.041 381.026  1.00116.72           O  
ANISOU  834  O   ILE A 131    12687  19145  12515  -3199   1012   5624       O  
ATOM    835  CB  ILE A 131      24.516  29.884 380.949  1.00112.10           C  
ANISOU  835  CB  ILE A 131    11427  19367  11800  -3071   1440   5011       C  
ATOM    836  CG1 ILE A 131      25.476  30.144 382.142  1.00112.95           C  
ANISOU  836  CG1 ILE A 131    11448  19831  11637  -2880   1551   4947       C  
ATOM    837  CG2 ILE A 131      23.086  29.649 381.426  1.00116.33           C  
ANISOU  837  CG2 ILE A 131    11634  20350  12216  -3315   1471   5350       C  
ATOM    838  CD1 ILE A 131      25.240  31.474 382.917  1.00119.80           C  
ANISOU  838  CD1 ILE A 131    12038  21251  12230  -2664   1749   4649       C  
ATOM    839  N   GLN A 132      23.956  26.737 380.986  1.00118.27           N  
ANISOU  839  N   GLN A 132    12575  19598  12765  -3744    963   6075       N  
ATOM    840  CA  GLN A 132      23.956  25.552 381.788  1.00122.50           C  
ANISOU  840  CA  GLN A 132    13191  20160  13192  -3987    805   6574       C  
ATOM    841  C   GLN A 132      24.400  26.031 383.148  1.00128.79           C  
ANISOU  841  C   GLN A 132    13680  21579  13675  -3809   1025   6556       C  
ATOM    842  O   GLN A 132      23.751  26.852 383.795  1.00128.94           O  
ANISOU  842  O   GLN A 132    13272  22230  13489  -3783   1235   6498       O  
ATOM    843  CB  GLN A 132      24.776  24.382 381.180  1.00124.22           C  
ANISOU  843  CB  GLN A 132    13974  19641  13584  -3965    500   6687       C  
ATOM    844  CG  GLN A 132      24.114  23.721 379.966  1.00137.43           C  
ANISOU  844  CG  GLN A 132    15967  20719  15532  -4215    224   6800       C  
ATOM    845  CD  GLN A 132      22.922  22.864 380.332  1.00157.23           C  
ANISOU  845  CD  GLN A 132    18430  23308  18002  -4770     27   7376       C  
ATOM    846  OE1 GLN A 132      21.769  23.308 380.299  1.00152.39           O  
ANISOU  846  OE1 GLN A 132    17440  23105  17355  -5044    126   7485       O  
ATOM    847  NE2 GLN A 132      23.171  21.610 380.677  1.00151.34           N  
ANISOU  847  NE2 GLN A 132    18077  22193  17232  -4953   -280   7773       N  
ATOM    848  N   ASN A 133      25.479  25.407 383.672  1.00127.20           N  
ANISOU  848  N   ASN A 133    13698  21239  13393  -3675    953   6649       N  
ATOM    849  CA  ASN A 133      26.010  25.630 385.017  1.00128.59           C  
ANISOU  849  CA  ASN A 133    13628  21968  13263  -3529   1121   6695       C  
ATOM    850  C   ASN A 133      26.691  27.007 385.194  1.00130.32           C  
ANISOU  850  C   ASN A 133    13662  22493  13361  -3154   1372   6161       C  
ATOM    851  O   ASN A 133      27.780  27.228 384.655  1.00126.79           O  
ANISOU  851  O   ASN A 133    13453  21729  12993  -2906   1353   5848       O  
ATOM    852  CB  ASN A 133      26.980  24.510 385.395  1.00131.20           C  
ANISOU  852  CB  ASN A 133    14292  22010  13546  -3477    942   6947       C  
ATOM    853  N   PRO A 134      26.085  27.925 385.995  1.00129.00           N  
ANISOU  853  N   PRO A 134    13079  22976  12958  -3104   1583   6069       N  
ATOM    854  CA  PRO A 134      26.722  29.234 386.228  1.00126.86           C  
ANISOU  854  CA  PRO A 134    12709  22945  12546  -2772   1762   5569       C  
ATOM    855  C   PRO A 134      27.647  29.224 387.456  1.00133.22           C  
ANISOU  855  C   PRO A 134    13417  24132  13067  -2613   1849   5593       C  
ATOM    856  O   PRO A 134      27.361  28.529 388.437  1.00136.12           O  
ANISOU  856  O   PRO A 134    13609  24854  13257  -2736   1855   5991       O  
ATOM    857  CB  PRO A 134      25.526  30.168 386.443  1.00129.38           C  
ANISOU  857  CB  PRO A 134    12691  23742  12726  -2744   1898   5448       C  
ATOM    858  CG  PRO A 134      24.376  29.264 386.866  1.00137.49           C  
ANISOU  858  CG  PRO A 134    13476  25081  13682  -3066   1850   5991       C  
ATOM    859  CD  PRO A 134      24.798  27.826 386.717  1.00134.13           C  
ANISOU  859  CD  PRO A 134    13339  24205  13421  -3331   1642   6413       C  
ATOM    860  N   ASP A 135      28.751  29.997 387.414  1.00128.24           N  
ANISOU  860  N   ASP A 135    12889  23461  12376  -2368   1906   5189       N  
ATOM    861  CA  ASP A 135      29.692  30.054 388.537  1.00129.32           C  
ANISOU  861  CA  ASP A 135    12931  23975  12230  -2215   1985   5175       C  
ATOM    862  C   ASP A 135      30.187  31.497 388.810  1.00132.57           C  
ANISOU  862  C   ASP A 135    13277  24633  12461  -2007   2091   4680       C  
ATOM    863  O   ASP A 135      30.923  32.060 387.993  1.00129.22           O  
ANISOU  863  O   ASP A 135    13065  23883  12148  -1950   2038   4362       O  
ATOM    864  CB  ASP A 135      30.874  29.093 388.319  1.00130.68           C  
ANISOU  864  CB  ASP A 135    13373  23817  12463  -2168   1865   5310       C  
ATOM    865  CG  ASP A 135      30.495  27.632 388.475  1.00142.09           C  
ANISOU  865  CG  ASP A 135    14933  25075  13982  -2344   1722   5830       C  
ATOM    866  OD1 ASP A 135      30.287  27.191 389.629  1.00145.35           O  
ANISOU  866  OD1 ASP A 135    15159  25892  14177  -2403   1765   6148       O  
ATOM    867  OD2 ASP A 135      30.393  26.932 387.445  1.00146.70           O  
ANISOU  867  OD2 ASP A 135    15816  25097  14827  -2431   1542   5925       O  
ATOM    868  N   PRO A 136      29.790  32.109 389.959  1.00132.13           N  
ANISOU  868  N   PRO A 136    12945  25160  12099  -1897   2214   4618       N  
ATOM    869  CA  PRO A 136      30.245  33.479 390.255  1.00131.44           C  
ANISOU  869  CA  PRO A 136    12880  25244  11816  -1701   2255   4138       C  
ATOM    870  C   PRO A 136      31.681  33.478 390.790  1.00135.80           C  
ANISOU  870  C   PRO A 136    13485  25925  12186  -1638   2255   4062       C  
ATOM    871  O   PRO A 136      31.907  33.231 391.982  1.00137.50           O  
ANISOU  871  O   PRO A 136    13495  26618  12131  -1566   2334   4215       O  
ATOM    872  CB  PRO A 136      29.223  33.987 391.294  1.00135.98           C  
ANISOU  872  CB  PRO A 136    13154  26411  12102  -1554   2359   4119       C  
ATOM    873  CG  PRO A 136      28.258  32.836 391.544  1.00142.64           C  
ANISOU  873  CG  PRO A 136    13742  27495  12961  -1724   2393   4657       C  
ATOM    874  CD  PRO A 136      28.920  31.597 391.038  1.00137.19           C  
ANISOU  874  CD  PRO A 136    13253  26351  12523  -1941   2294   4983       C  
ATOM    875  N   ALA A 137      32.657  33.728 389.888  1.00130.53           N  
ANISOU  875  N   ALA A 137    13065  24883  11647  -1672   2165   3850       N  
ATOM    876  CA  ALA A 137      34.088  33.740 390.216  1.00130.49           C  
ANISOU  876  CA  ALA A 137    13096  25031  11454  -1636   2149   3780       C  
ATOM    877  C   ALA A 137      34.867  34.814 389.441  1.00132.59           C  
ANISOU  877  C   ALA A 137    13568  25071  11739  -1691   2048   3397       C  
ATOM    878  O   ALA A 137      34.602  35.044 388.257  1.00130.28           O  
ANISOU  878  O   ALA A 137    13447  24347  11708  -1767   1971   3297       O  
ATOM    879  CB  ALA A 137      34.695  32.373 389.939  1.00131.38           C  
ANISOU  879  CB  ALA A 137    13252  25017  11651  -1641   2116   4139       C  
ATOM    880  N   VAL A 138      35.847  35.446 390.121  1.00129.90           N  
ANISOU  880  N   VAL A 138    13205  25047  11103  -1683   2033   3207       N  
ATOM    881  CA  VAL A 138      36.730  36.481 389.576  1.00128.66           C  
ANISOU  881  CA  VAL A 138    13226  24776  10882  -1814   1904   2893       C  
ATOM    882  C   VAL A 138      38.117  36.353 390.233  1.00133.60           C  
ANISOU  882  C   VAL A 138    13748  25809  11204  -1839   1899   2942       C  
ATOM    883  O   VAL A 138      38.472  37.142 391.115  1.00134.76           O  
ANISOU  883  O   VAL A 138    13866  26281  11057  -1860   1877   2764       O  
ATOM    884  CB  VAL A 138      36.132  37.899 389.742  1.00133.18           C  
ANISOU  884  CB  VAL A 138    13956  25282  11366  -1829   1823   2511       C  
ATOM    885  N   TYR A 139      38.884  35.328 389.811  1.00129.71           N  
ANISOU  885  N   TYR A 139    13206  25319  10757  -1803   1905   3184       N  
ATOM    886  CA  TYR A 139      40.226  35.029 390.325  1.00130.83           C  
ANISOU  886  CA  TYR A 139    13216  25899  10594  -1775   1908   3276       C  
ATOM    887  C   TYR A 139      41.280  35.985 389.755  1.00134.84           C  
ANISOU  887  C   TYR A 139    13786  26502  10944  -1995   1769   3049       C  
ATOM    888  O   TYR A 139      41.142  36.446 388.619  1.00132.98           O  
ANISOU  888  O   TYR A 139    13707  25912  10906  -2128   1668   2923       O  
ATOM    889  CB  TYR A 139      40.610  33.576 390.007  1.00131.87           C  
ANISOU  889  CB  TYR A 139    13314  25994  10798  -1578   1936   3610       C  
ATOM    890  N   GLN A 140      42.334  36.274 390.547  1.00133.32           N  
ANISOU  890  N   GLN A 140    13458  26821  10377  -2061   1754   3021       N  
ATOM    891  CA  GLN A 140      43.438  37.156 390.155  1.00133.83           C  
ANISOU  891  CA  GLN A 140    13538  27100  10211  -2345   1599   2865       C  
ATOM    892  C   GLN A 140      44.531  36.362 389.429  1.00137.88           C  
ANISOU  892  C   GLN A 140    13901  27863  10625  -2265   1590   3072       C  
ATOM    893  O   GLN A 140      44.885  35.267 389.870  1.00138.07           O  
ANISOU  893  O   GLN A 140    13770  28145  10546  -1975   1698   3309       O  
ATOM    894  CB  GLN A 140      44.017  37.876 391.381  1.00137.66           C  
ANISOU  894  CB  GLN A 140    13945  28055  10304  -2479   1563   2744       C  
ATOM    895  N   LEU A 141      45.059  36.912 388.316  1.00134.20           N  
ANISOU  895  N   LEU A 141    13488  27344  10159  -2497   1445   2988       N  
ATOM    896  CA  LEU A 141      46.093  36.262 387.506  1.00134.44           C  
ANISOU  896  CA  LEU A 141    13350  27687  10042  -2390   1417   3161       C  
ATOM    897  C   LEU A 141      47.365  37.123 387.395  1.00140.75           C  
ANISOU  897  C   LEU A 141    13994  29051  10436  -2754   1269   3118       C  
ATOM    898  O   LEU A 141      47.317  38.235 386.861  1.00140.45           O  
ANISOU  898  O   LEU A 141    14105  28831  10430  -3164   1105   2948       O  
ATOM    899  CB  LEU A 141      45.542  35.942 386.108  1.00132.23           C  
ANISOU  899  CB  LEU A 141    13220  26897  10123  -2298   1378   3165       C  
ATOM    900  N   ARG A 142      48.500  36.598 387.906  1.00139.46           N  
ANISOU  900  N   ARG A 142    13535  29589   9865  -2616   1310   3293       N  
ATOM    901  CA  ARG A 142      49.808  37.263 387.877  1.00141.85           C  
ANISOU  901  CA  ARG A 142    13605  30592   9701  -2962   1176   3322       C  
ATOM    902  C   ARG A 142      50.519  36.964 386.559  1.00146.13           C  
ANISOU  902  C   ARG A 142    13983  31400  10140  -2907   1103   3448       C  
ATOM    903  O   ARG A 142      50.472  35.824 386.093  1.00144.90           O  
ANISOU  903  O   ARG A 142    13786  31191  10078  -2406   1198   3575       O  
ATOM    904  CB  ARG A 142      50.670  36.821 389.069  1.00144.63           C  
ANISOU  904  CB  ARG A 142    13676  31656   9620  -2809   1267   3455       C  
ATOM    905  N   ASP A 143      51.167  37.985 385.955  1.00144.10           N  
ANISOU  905  N   ASP A 143    13651  31433   9668  -3422    908   3423       N  
ATOM    906  CA  ASP A 143      51.860  37.866 384.667  1.00144.49           C  
ANISOU  906  CA  ASP A 143    13496  31842   9562  -3433    818   3552       C  
ATOM    907  C   ASP A 143      53.122  36.998 384.769  1.00151.40           C  
ANISOU  907  C   ASP A 143    13930  33678   9917  -3075    883   3785       C  
ATOM    908  O   ASP A 143      53.707  36.880 385.849  1.00153.32           O  
ANISOU  908  O   ASP A 143    13993  34438   9826  -3058    938   3849       O  
ATOM    909  CB  ASP A 143      52.191  39.247 384.084  1.00147.60           C  
ANISOU  909  CB  ASP A 143    13930  32314   9837  -4156    566   3502       C  
ATOM    910  N   SER A 144      53.514  36.373 383.638  1.00148.48           N  
ANISOU  910  N   SER A 144    13395  33558   9461  -2735    873   3900       N  
ATOM    911  CA  SER A 144      54.649  35.452 383.531  1.00151.17           C  
ANISOU  911  CA  SER A 144    13341  34806   9289  -2241    921   4103       C  
ATOM    912  C   SER A 144      56.020  36.160 383.626  1.00156.13           C  
ANISOU  912  C   SER A 144    13832  35906   9583  -2579    814   4116       C  
ATOM    913  O   SER A 144      56.670  36.061 384.671  1.00155.67           O  
ANISOU  913  O   SER A 144    13774  36019   9354  -2491    875   4105       O  
ATOM    914  CB  SER A 144      54.558  34.643 382.239  1.00153.70           C  
ANISOU  914  CB  SER A 144    13684  34995   9720  -1695    916   4137       C  
ATOM    915  N   LYS A 145      56.462  36.842 382.539  1.00153.34           N  
ANISOU  915  N   LYS A 145    13351  35786   9125  -2963    649   4165       N  
ATOM    916  CA  LYS A 145      57.753  37.538 382.440  1.00152.82           C  
ANISOU  916  CA  LYS A 145    13331  35799   8933  -3244    525   4142       C  
ATOM    917  C   LYS A 145      57.891  38.646 383.491  1.00155.69           C  
ANISOU  917  C   LYS A 145    14039  35638   9477  -3784    436   3988       C  
ATOM    918  O   LYS A 145      58.934  38.738 384.140  1.00155.28           O  
ANISOU  918  O   LYS A 145    14035  35668   9295  -3742    433   3971       O  
ATOM    919  CB  LYS A 145      57.953  38.118 381.031  1.00154.01           C  
ANISOU  919  CB  LYS A 145    13550  35727   9239  -3483    366   4135       C  
ATOM    920  N   SER A 146      56.839  39.466 383.670  1.00153.83           N  
ANISOU  920  N   SER A 146    13806  35384   9258  -4399    329   3982       N  
ATOM    921  CA  SER A 146      56.833  40.538 384.640  1.00154.18           C  
ANISOU  921  CA  SER A 146    14103  35153   9325  -4953    189   3862       C  
ATOM    922  C   SER A 146      55.986  40.005 385.775  1.00156.76           C  
ANISOU  922  C   SER A 146    14511  35289   9762  -4657    375   3763       C  
ATOM    923  O   SER A 146      54.810  39.687 385.596  1.00155.96           O  
ANISOU  923  O   SER A 146    14407  35026   9823  -4564    455   3747       O  
ATOM    924  N   SER A 147      56.593  39.904 386.947  1.00154.41           N  
ANISOU  924  N   SER A 147    14126  35334   9210  -4603    431   3774       N  
ATOM    925  CA  SER A 147      55.906  39.342 388.118  1.00154.50           C  
ANISOU  925  CA  SER A 147    14105  35387   9210  -4324    614   3735       C  
ATOM    926  C   SER A 147      55.385  40.426 389.074  1.00157.92           C  
ANISOU  926  C   SER A 147    14927  35270   9806  -4753    485   3498       C  
ATOM    927  O   SER A 147      55.064  40.149 390.231  1.00157.55           O  
ANISOU  927  O   SER A 147    14884  35262   9718  -4561    611   3441       O  
ATOM    928  N   ASP A 148      55.288  41.675 388.569  1.00155.78           N  
ANISOU  928  N   ASP A 148    14829  34857   9502  -5448    192   3432       N  
ATOM    929  CA  ASP A 148      54.813  42.842 389.318  1.00156.76           C  
ANISOU  929  CA  ASP A 148    15347  34546   9669  -5921    -24   3203       C  
ATOM    930  C   ASP A 148      53.401  43.286 388.909  1.00159.40           C  
ANISOU  930  C   ASP A 148    15973  34304  10289  -6082    -86   3034       C  
ATOM    931  O   ASP A 148      52.648  43.759 389.762  1.00159.37           O  
ANISOU  931  O   ASP A 148    16253  33937  10362  -6109   -118   2811       O  
ATOM    932  N   LYS A 149      53.053  43.146 387.608  1.00153.79           N  
ANISOU  932  N   LYS A 149    15240  33423   9771  -6115   -103   3111       N  
ATOM    933  CA  LYS A 149      51.750  43.525 387.046  1.00150.10           C  
ANISOU  933  CA  LYS A 149    15235  31957   9839  -6034   -130   2883       C  
ATOM    934  C   LYS A 149      50.700  42.427 387.223  1.00149.12           C  
ANISOU  934  C   LYS A 149    15136  31394  10129  -5300    201   2814       C  
ATOM    935  O   LYS A 149      51.028  41.242 387.115  1.00147.53           O  
ANISOU  935  O   LYS A 149    14594  31580   9882  -4836    432   3004       O  
ATOM    936  N   SER A 150      49.437  42.826 387.482  1.00143.61           N  
ANISOU  936  N   SER A 150    14855  29906   9804  -5197    197   2553       N  
ATOM    937  CA  SER A 150      48.314  41.904 387.684  1.00140.33           C  
ANISOU  937  CA  SER A 150    14480  29067   9771  -4597    473   2506       C  
ATOM    938  C   SER A 150      47.008  42.393 387.046  1.00141.40           C  
ANISOU  938  C   SER A 150    15000  28364  10363  -4551    431   2303       C  
ATOM    939  O   SER A 150      46.745  43.598 387.023  1.00141.95           O  
ANISOU  939  O   SER A 150    15429  28072  10435  -4915    182   2091       O  
ATOM    940  N   VAL A 151      46.189  41.443 386.545  1.00134.95           N  
ANISOU  940  N   VAL A 151    14130  27234   9909  -4099    652   2372       N  
ATOM    941  CA  VAL A 151      44.890  41.690 385.907  1.00132.40           C  
ANISOU  941  CA  VAL A 151    14099  26185  10022  -3983    658   2219       C  
ATOM    942  C   VAL A 151      43.990  40.457 386.036  1.00133.95           C  
ANISOU  942  C   VAL A 151    14191  26194  10508  -3470    926   2325       C  
ATOM    943  O   VAL A 151      44.261  39.439 385.396  1.00132.54           O  
ANISOU  943  O   VAL A 151    13803  26172  10384  -3234   1042   2545       O  
ATOM    944  N   CYS A 152      42.927  40.551 386.864  1.00129.89           N  
ANISOU  944  N   CYS A 152    13836  25374  10142  -3295    997   2180       N  
ATOM    945  CA  CYS A 152      41.976  39.461 387.126  1.00128.11           C  
ANISOU  945  CA  CYS A 152    13515  25000  10161  -2894   1220   2312       C  
ATOM    946  C   CYS A 152      40.763  39.464 386.189  1.00129.29           C  
ANISOU  946  C   CYS A 152    13840  24564  10721  -2807   1233   2254       C  
ATOM    947  O   CYS A 152      40.268  40.530 385.823  1.00128.57           O  
ANISOU  947  O   CYS A 152    14003  24134  10715  -2980   1090   2020       O  
ATOM    948  N   LEU A 153      40.271  38.261 385.831  1.00124.33           N  
ANISOU  948  N   LEU A 153    13102  23806  10330  -2542   1382   2473       N  
ATOM    949  CA  LEU A 153      39.127  38.079 384.933  1.00122.08           C  
ANISOU  949  CA  LEU A 153    12947  23010  10430  -2460   1402   2462       C  
ATOM    950  C   LEU A 153      37.926  37.452 385.646  1.00126.06           C  
ANISOU  950  C   LEU A 153    13392  23439  11065  -2240   1549   2570       C  
ATOM    951  O   LEU A 153      38.088  36.475 386.379  1.00126.58           O  
ANISOU  951  O   LEU A 153    13289  23769  11038  -2089   1656   2806       O  
ATOM    952  CB  LEU A 153      39.526  37.210 383.733  1.00120.66           C  
ANISOU  952  CB  LEU A 153    12728  22704  10414  -2388   1388   2639       C  
ATOM    953  N   PHE A 154      36.718  38.010 385.407  1.00122.05           N  
ANISOU  953  N   PHE A 154    13014  22612  10747  -2226   1543   2418       N  
ATOM    954  CA  PHE A 154      35.450  37.549 385.983  1.00122.38           C  
ANISOU  954  CA  PHE A 154    12960  22656  10883  -2053   1669   2531       C  
ATOM    955  C   PHE A 154      34.773  36.539 385.033  1.00124.67           C  
ANISOU  955  C   PHE A 154    13251  22602  11517  -2019   1699   2756       C  
ATOM    956  O   PHE A 154      33.747  36.838 384.415  1.00123.24           O  
ANISOU  956  O   PHE A 154    13153  22126  11547  -2023   1687   2670       O  
ATOM    957  CB  PHE A 154      34.529  38.744 386.295  1.00125.04           C  
ANISOU  957  CB  PHE A 154    13416  22941  11153  -2001   1634   2233       C  
ATOM    958  N   THR A 155      35.371  35.336 384.929  1.00121.36           N  
ANISOU  958  N   THR A 155    12764  22219  11127  -1969   1716   3037       N  
ATOM    959  CA  THR A 155      34.928  34.227 384.074  1.00120.35           C  
ANISOU  959  CA  THR A 155    12701  21740  11287  -1930   1690   3267       C  
ATOM    960  C   THR A 155      33.630  33.569 384.593  1.00126.02           C  
ANISOU  960  C   THR A 155    13331  22441  12110  -1919   1762   3508       C  
ATOM    961  O   THR A 155      33.207  33.830 385.723  1.00127.41           O  
ANISOU  961  O   THR A 155    13341  22978  12092  -1892   1856   3539       O  
ATOM    962  CB  THR A 155      36.059  33.181 383.919  1.00128.13           C  
ANISOU  962  CB  THR A 155    13703  22785  12195  -1815   1638   3465       C  
ATOM    963  OG1 THR A 155      35.627  32.146 383.032  1.00126.97           O  
ANISOU  963  OG1 THR A 155    13705  22218  12319  -1755   1557   3636       O  
ATOM    964  CG2 THR A 155      36.510  32.570 385.252  1.00128.81           C  
ANISOU  964  CG2 THR A 155    13647  23269  12026  -1710   1712   3690       C  
ATOM    965  N   ASP A 156      33.020  32.703 383.741  1.00122.38           N  
ANISOU  965  N   ASP A 156    12976  21593  11932  -1952   1698   3692       N  
ATOM    966  CA  ASP A 156      31.791  31.920 383.962  1.00123.85           C  
ANISOU  966  CA  ASP A 156    13100  21713  12245  -2031   1712   3988       C  
ATOM    967  C   ASP A 156      30.590  32.826 384.334  1.00128.70           C  
ANISOU  967  C   ASP A 156    13546  22540  12815  -2068   1810   3852       C  
ATOM    968  O   ASP A 156      29.751  32.456 385.163  1.00130.47           O  
ANISOU  968  O   ASP A 156    13568  23075  12930  -2104   1880   4085       O  
ATOM    969  CB  ASP A 156      32.011  30.814 385.020  1.00128.15           C  
ANISOU  969  CB  ASP A 156    13566  22494  12632  -2013   1722   4364       C  
ATOM    970  CG  ASP A 156      33.196  29.909 384.742  1.00136.57           C  
ANISOU  970  CG  ASP A 156    14825  23379  13685  -1887   1608   4488       C  
ATOM    971  OD1 ASP A 156      33.199  29.240 383.682  1.00136.04           O  
ANISOU  971  OD1 ASP A 156    14993  22855  13840  -1881   1460   4582       O  
ATOM    972  OD2 ASP A 156      34.109  29.852 385.592  1.00143.02           O  
ANISOU  972  OD2 ASP A 156    15565  24535  14242  -1763   1655   4486       O  
ATOM    973  N   PHE A 157      30.503  33.998 383.673  1.00123.81           N  
ANISOU  973  N   PHE A 157    13018  21771  12255  -2043   1797   3486       N  
ATOM    974  CA  PHE A 157      29.461  35.008 383.866  1.00124.26           C  
ANISOU  974  CA  PHE A 157    12990  21983  12241  -1986   1855   3275       C  
ATOM    975  C   PHE A 157      28.092  34.521 383.374  1.00128.62           C  
ANISOU  975  C   PHE A 157    13457  22426  12984  -2065   1862   3468       C  
ATOM    976  O   PHE A 157      28.008  33.517 382.660  1.00127.22           O  
ANISOU  976  O   PHE A 157    13372  21911  13055  -2202   1785   3697       O  
ATOM    977  CB  PHE A 157      29.849  36.308 383.140  1.00124.33           C  
ANISOU  977  CB  PHE A 157    13211  21761  12267  -1951   1783   2848       C  
ATOM    978  N   ASP A 158      27.022  35.238 383.764  1.00127.23           N  
ANISOU  978  N   ASP A 158    13114  22568  12660  -1960   1937   3370       N  
ATOM    979  CA  ASP A 158      25.652  34.914 383.369  1.00128.26           C  
ANISOU  979  CA  ASP A 158    13094  22743  12897  -2032   1954   3551       C  
ATOM    980  C   ASP A 158      25.272  35.618 382.066  1.00130.43           C  
ANISOU  980  C   ASP A 158    13557  22610  13393  -2001   1895   3265       C  
ATOM    981  O   ASP A 158      25.736  36.734 381.810  1.00128.81           O  
ANISOU  981  O   ASP A 158    13542  22260  13140  -1855   1862   2874       O  
ATOM    982  CB  ASP A 158      24.658  35.272 384.481  1.00133.33           C  
ANISOU  982  CB  ASP A 158    13401  24061  13199  -1881   2068   3611       C  
ATOM    983  N   SER A 159      24.431  34.956 381.241  1.00126.92           N  
ANISOU  983  N   SER A 159    13073  21973  13179  -2166   1858   3479       N  
ATOM    984  CA  SER A 159      23.934  35.496 379.970  1.00124.82           C  
ANISOU  984  CA  SER A 159    12948  21346  13132  -2149   1808   3260       C  
ATOM    985  C   SER A 159      23.027  36.699 380.232  1.00130.25           C  
ANISOU  985  C   SER A 159    13522  22375  13593  -1887   1879   2987       C  
ATOM    986  O   SER A 159      23.066  37.669 379.473  1.00128.15           O  
ANISOU  986  O   SER A 159    13468  21818  13405  -1757   1830   2641       O  
ATOM    987  CB  SER A 159      23.186  34.425 379.181  1.00128.24           C  
ANISOU  987  CB  SER A 159    13344  21557  13822  -2403   1740   3590       C  
ATOM    988  OG  SER A 159      24.066  33.419 378.706  1.00135.13           O  
ANISOU  988  OG  SER A 159    14427  22012  14903  -2564   1623   3772       O  
ATOM    989  N   GLN A 160      22.247  36.642 381.338  1.00130.29           N  
ANISOU  989  N   GLN A 160    13200  23021  13284  -1783   1978   3146       N  
ATOM    990  CA  GLN A 160      21.341  37.698 381.796  1.00132.39           C  
ANISOU  990  CA  GLN A 160    13321  23752  13231  -1435   2042   2902       C  
ATOM    991  C   GLN A 160      22.116  38.899 382.376  1.00136.29           C  
ANISOU  991  C   GLN A 160    14056  24235  13494  -1127   2009   2460       C  
ATOM    992  O   GLN A 160      21.573  40.006 382.413  1.00137.03           O  
ANISOU  992  O   GLN A 160    14245  24431  13388   -787   1983   2113       O  
ATOM    993  CB  GLN A 160      20.364  37.143 382.843  1.00137.74           C  
ANISOU  993  CB  GLN A 160    13524  25214  13596  -1423   2150   3260       C  
ATOM    994  N   THR A 161      23.378  38.676 382.825  1.00131.77           N  
ANISOU  994  N   THR A 161    13604  23538  12923  -1241   1985   2476       N  
ATOM    995  CA  THR A 161      24.267  39.703 383.386  1.00131.50           C  
ANISOU  995  CA  THR A 161    13818  23471  12674  -1052   1919   2105       C  
ATOM    996  C   THR A 161      25.025  40.401 382.244  1.00131.75           C  
ANISOU  996  C   THR A 161    14266  22844  12947  -1152   1772   1810       C  
ATOM    997  O   THR A 161      25.657  39.734 381.421  1.00128.67           O  
ANISOU  997  O   THR A 161    13948  22076  12867  -1427   1743   1967       O  
ATOM    998  CB  THR A 161      25.221  39.083 384.432  1.00139.25           C  
ANISOU  998  CB  THR A 161    14687  24697  13524  -1159   1964   2298       C  
ATOM    999  OG1 THR A 161      24.448  38.462 385.460  1.00141.61           O  
ANISOU  999  OG1 THR A 161    14581  25623  13602  -1099   2092   2617       O  
ATOM   1000  CG2 THR A 161      26.158  40.111 385.062  1.00138.30           C  
ANISOU 1000  CG2 THR A 161    14802  24603  13144  -1000   1880   1937       C  
ATOM   1001  N   ASN A 162      24.950  41.742 382.203  1.00128.66           N  
ANISOU 1001  N   ASN A 162    14166  22335  12385   -916   1656   1390       N  
ATOM   1002  CA  ASN A 162      25.607  42.562 381.188  1.00126.20           C  
ANISOU 1002  CA  ASN A 162    14268  21439  12245  -1032   1483   1115       C  
ATOM   1003  C   ASN A 162      26.872  43.202 381.747  1.00129.97           C  
ANISOU 1003  C   ASN A 162    15004  21841  12539  -1117   1347    922       C  
ATOM   1004  O   ASN A 162      26.865  43.690 382.879  1.00132.07           O  
ANISOU 1004  O   ASN A 162    15285  22435  12462   -899   1327    775       O  
ATOM   1005  CB  ASN A 162      24.654  43.633 380.663  1.00128.09           C  
ANISOU 1005  CB  ASN A 162    14727  21520  12421   -749   1391    800       C  
ATOM   1006  N   VAL A 163      27.956  43.195 380.946  1.00124.15           N  
ANISOU 1006  N   VAL A 163    14450  20720  12001  -1437   1243    933       N  
ATOM   1007  CA  VAL A 163      29.258  43.763 381.302  1.00124.46           C  
ANISOU 1007  CA  VAL A 163    14711  20708  11872  -1620   1091    800       C  
ATOM   1008  C   VAL A 163      29.169  45.291 381.314  1.00130.39           C  
ANISOU 1008  C   VAL A 163    15918  21205  12417  -1512    848    391       C  
ATOM   1009  O   VAL A 163      28.970  45.910 380.265  1.00129.03           O  
ANISOU 1009  O   VAL A 163    16014  20611  12400  -1569    715    248       O  
ATOM   1010  CB  VAL A 163      30.377  43.267 380.355  1.00125.72           C  
ANISOU 1010  CB  VAL A 163    14869  20639  12258  -1981   1051    971       C  
ATOM   1011  N   SER A 164      29.292  45.887 382.513  1.00130.01           N  
ANISOU 1011  N   SER A 164    15988  21403  12007  -1336    768    200       N  
ATOM   1012  CA  SER A 164      29.210  47.333 382.722  1.00132.72           C  
ANISOU 1012  CA  SER A 164    16844  21495  12089  -1184    482   -211       C  
ATOM   1013  C   SER A 164      30.572  48.007 382.524  1.00136.88           C  
ANISOU 1013  C   SER A 164    17724  21737  12548  -1617    212   -298       C  
ATOM   1014  O   SER A 164      31.575  47.549 383.079  1.00136.09           O  
ANISOU 1014  O   SER A 164    17433  21903  12370  -1864    258   -126       O  
ATOM   1015  CB  SER A 164      28.672  47.638 384.118  1.00139.93           C  
ANISOU 1015  CB  SER A 164    17732  22833  12603   -742    496   -390       C  
ATOM   1016  OG  SER A 164      27.414  47.021 384.338  1.00148.95           O  
ANISOU 1016  OG  SER A 164    18508  24342  13745   -362    730   -283       O  
ATOM   1017  N   GLN A 165      30.599  49.097 381.726  1.00134.38           N  
ANISOU 1017  N   GLN A 165    17920  20904  12234  -1723    -85   -543       N  
ATOM   1018  CA  GLN A 165      31.805  49.885 381.442  1.00135.19           C  
ANISOU 1018  CA  GLN A 165    18410  20717  12241  -2201   -406   -610       C  
ATOM   1019  C   GLN A 165      32.223  50.683 382.683  1.00142.91           C  
ANISOU 1019  C   GLN A 165    19702  21800  12796  -2144   -636   -851       C  
ATOM   1020  O   GLN A 165      31.360  51.192 383.405  1.00145.31           O  
ANISOU 1020  O   GLN A 165    20209  22136  12866  -1653   -693  -1131       O  
ATOM   1021  CB  GLN A 165      31.574  50.822 380.248  1.00136.74           C  
ANISOU 1021  CB  GLN A 165    19089  20311  12556  -2332   -679   -775       C  
ATOM   1022  N   SER A 166      33.541  50.776 382.935  1.00139.79           N  
ANISOU 1022  N   SER A 166    19330  21511  12271  -2623   -774   -741       N  
ATOM   1023  CA  SER A 166      34.096  51.474 384.097  1.00143.42           C  
ANISOU 1023  CA  SER A 166    20079  22086  12329  -2663  -1015   -939       C  
ATOM   1024  C   SER A 166      33.916  52.993 384.003  1.00151.08           C  
ANISOU 1024  C   SER A 166    21853  22475  13074  -2674  -1504  -1323       C  
ATOM   1025  O   SER A 166      34.076  53.572 382.925  1.00150.33           O  
ANISOU 1025  O   SER A 166    22099  21907  13115  -3021  -1743  -1320       O  
ATOM   1026  CB  SER A 166      35.573  51.135 384.278  1.00146.62           C  
ANISOU 1026  CB  SER A 166    20258  22797  12652  -3222  -1036   -679       C  
ATOM   1027  OG  SER A 166      36.340  51.505 383.144  1.00154.99           O  
ANISOU 1027  OG  SER A 166    21486  23573  13830  -3784  -1249   -549       O  
ATOM   1028  N   LYS A 167      33.574  53.624 385.147  1.00151.42           N  
ANISOU 1028  N   LYS A 167    22220  22559  12753  -2272  -1672  -1654       N  
ATOM   1029  CA  LYS A 167      33.377  55.071 385.290  1.00155.89           C  
ANISOU 1029  CA  LYS A 167    23642  22561  13028  -2174  -2189  -2071       C  
ATOM   1030  C   LYS A 167      34.701  55.769 385.629  1.00161.96           C  
ANISOU 1030  C   LYS A 167    24821  23165  13551  -2827  -2609  -2078       C  
ATOM   1031  O   LYS A 167      34.924  56.901 385.193  1.00164.57           O  
ANISOU 1031  O   LYS A 167    25867  22882  13781  -3130  -3095  -2247       O  
ATOM   1032  CB  LYS A 167      32.323  55.372 386.366  1.00161.85           C  
ANISOU 1032  CB  LYS A 167    24553  23493  13452  -1367  -2192  -2438       C  
ATOM   1033  N   ASP A 168      35.571  55.089 386.407  1.00157.25           N  
ANISOU 1033  N   ASP A 168    23778  23128  12841  -3065  -2438  -1874       N  
ATOM   1034  CA  ASP A 168      36.890  55.586 386.802  1.00159.50           C  
ANISOU 1034  CA  ASP A 168    24316  23422  12864  -3718  -2787  -1822       C  
ATOM   1035  C   ASP A 168      37.880  55.440 385.643  1.00159.93           C  
ANISOU 1035  C   ASP A 168    24221  23414  13132  -4495  -2844  -1454       C  
ATOM   1036  O   ASP A 168      37.899  54.401 384.976  1.00154.58           O  
ANISOU 1036  O   ASP A 168    22930  23023  12782  -4507  -2441  -1142       O  
ATOM   1037  CB  ASP A 168      37.399  54.839 388.045  1.00161.30           C  
ANISOU 1037  CB  ASP A 168    24040  24355  12892  -3642  -2536  -1713       C  
ATOM   1038  N   SER A 169      38.700  56.484 385.408  1.00159.43           N  
ANISOU 1038  N   SER A 169    24730  22996  12849  -5144  -3372  -1484       N  
ATOM   1039  CA  SER A 169      39.710  56.526 384.345  1.00157.74           C  
ANISOU 1039  CA  SER A 169    24415  22783  12737  -5947  -3510  -1126       C  
ATOM   1040  C   SER A 169      40.826  55.494 384.567  1.00157.62           C  
ANISOU 1040  C   SER A 169    23617  23577  12694  -6297  -3193   -724       C  
ATOM   1041  O   SER A 169      41.393  54.998 383.591  1.00154.41           O  
ANISOU 1041  O   SER A 169    22803  23396  12468  -6668  -3054   -377       O  
ATOM   1042  CB  SER A 169      40.313  57.922 384.242  1.00166.71           C  
ANISOU 1042  CB  SER A 169    26387  23385  13571  -6587  -4204  -1242       C  
ATOM   1043  N   ASP A 170      41.131  55.173 385.844  1.00154.11           N  
ANISOU 1043  N   ASP A 170    22965  23593  11996  -6134  -3086   -777       N  
ATOM   1044  CA  ASP A 170      42.158  54.206 386.241  1.00151.62           C  
ANISOU 1044  CA  ASP A 170    21941  24076  11592  -6371  -2796   -433       C  
ATOM   1045  C   ASP A 170      41.733  52.767 385.913  1.00148.02           C  
ANISOU 1045  C   ASP A 170    20742  24013  11487  -5900  -2195   -205       C  
ATOM   1046  O   ASP A 170      42.528  52.017 385.346  1.00145.07           O  
ANISOU 1046  O   ASP A 170    19852  24084  11185  -6182  -2005    151       O  
ATOM   1047  CB  ASP A 170      42.475  54.340 387.739  1.00156.63           C  
ANISOU 1047  CB  ASP A 170    22625  25036  11850  -6269  -2870   -594       C  
ATOM   1048  N   VAL A 171      40.484  52.392 386.258  1.00141.62           N  
ANISOU 1048  N   VAL A 171    19893  23059  10859  -5186  -1929   -402       N  
ATOM   1049  CA  VAL A 171      39.926  51.058 386.023  1.00136.29           C  
ANISOU 1049  CA  VAL A 171    18599  22678  10506  -4742  -1410   -197       C  
ATOM   1050  C   VAL A 171      39.594  50.848 384.541  1.00135.97           C  
ANISOU 1050  C   VAL A 171    18509  22315  10839  -4814  -1339    -63       C  
ATOM   1051  O   VAL A 171      39.090  51.765 383.887  1.00136.81           O  
ANISOU 1051  O   VAL A 171    19120  21845  11016  -4865  -1607   -263       O  
ATOM   1052  CB  VAL A 171      38.677  50.825 386.897  1.00140.16           C  
ANISOU 1052  CB  VAL A 171    19065  23182  11008  -4026  -1195   -423       C  
ATOM   1053  N   TYR A 172      39.867  49.631 384.021  1.00127.80           N  
ANISOU 1053  N   TYR A 172    16892  21642  10026  -4784   -993    265       N  
ATOM   1054  CA  TYR A 172      39.599  49.250 382.628  1.00123.81           C  
ANISOU 1054  CA  TYR A 172    16262  20909   9869  -4812   -890    415       C  
ATOM   1055  C   TYR A 172      39.050  47.814 382.554  1.00122.28           C  
ANISOU 1055  C   TYR A 172    15550  20957   9955  -4362   -445    605       C  
ATOM   1056  O   TYR A 172      39.730  46.871 382.961  1.00120.82           O  
ANISOU 1056  O   TYR A 172    14936  21276   9692  -4343   -244    840       O  
ATOM   1057  CB  TYR A 172      40.862  49.402 381.763  1.00125.33           C  
ANISOU 1057  CB  TYR A 172    16356  21291   9972  -5420  -1067    663       C  
ATOM   1058  N   ILE A 173      37.810  47.665 382.047  1.00116.00           N  
ANISOU 1058  N   ILE A 173    14821  19795   9458  -4004   -319    509       N  
ATOM   1059  CA  ILE A 173      37.113  46.381 381.909  1.00112.30           C  
ANISOU 1059  CA  ILE A 173    13945  19457   9267  -3622     43    688       C  
ATOM   1060  C   ILE A 173      36.704  46.134 380.449  1.00112.29           C  
ANISOU 1060  C   ILE A 173    13927  19124   9615  -3645     81    771       C  
ATOM   1061  O   ILE A 173      36.342  47.078 379.740  1.00112.14           O  
ANISOU 1061  O   ILE A 173    14271  18675   9663  -3756   -127    592       O  
ATOM   1062  CB  ILE A 173      35.885  46.331 382.844  1.00116.15           C  
ANISOU 1062  CB  ILE A 173    14455  19941   9736  -3146    179    524       C  
ATOM   1063  N   THR A 174      36.752  44.856 380.014  1.00105.50           N  
ANISOU 1063  N   THR A 174    12676  18446   8963  -3519    326   1036       N  
ATOM   1064  CA  THR A 174      36.420  44.424 378.649  1.00102.30           C  
ANISOU 1064  CA  THR A 174    12210  17775   8882  -3505    377   1133       C  
ATOM   1065  C   THR A 174      34.985  43.906 378.542  1.00104.16           C  
ANISOU 1065  C   THR A 174    12398  17786   9392  -3133    564   1109       C  
ATOM   1066  O   THR A 174      34.416  43.453 379.536  1.00104.51           O  
ANISOU 1066  O   THR A 174    12310  18023   9376  -2881    715   1131       O  
ATOM   1067  CB  THR A 174      37.397  43.339 378.161  1.00107.84           C  
ANISOU 1067  CB  THR A 174    12568  18804   9604  -3573    474   1423       C  
ATOM   1068  OG1 THR A 174      37.333  42.207 379.031  1.00106.52           O  
ANISOU 1068  OG1 THR A 174    12125  18943   9405  -3309    689   1588       O  
ATOM   1069  CG2 THR A 174      38.829  43.847 378.033  1.00107.84           C  
ANISOU 1069  CG2 THR A 174    12550  19114   9311  -3975    282   1487       C  
ATOM   1070  N   ASP A 175      34.422  43.942 377.315  1.00 98.59           N  
ANISOU 1070  N   ASP A 175    11769  16725   8967  -3121    549   1092       N  
ATOM   1071  CA  ASP A 175      33.069  43.478 376.993  1.00 97.01           C  
ANISOU 1071  CA  ASP A 175    11511  16320   9028  -2832    700   1091       C  
ATOM   1072  C   ASP A 175      32.945  41.955 377.142  1.00 99.66           C  
ANISOU 1072  C   ASP A 175    11502  16855   9509  -2683    915   1382       C  
ATOM   1073  O   ASP A 175      33.961  41.258 377.210  1.00 98.81           O  
ANISOU 1073  O   ASP A 175    11231  16983   9329  -2766    937   1564       O  
ATOM   1074  CB  ASP A 175      32.694  43.901 375.563  1.00 97.21           C  
ANISOU 1074  CB  ASP A 175    11711  15930   9293  -2904    602   1006       C  
ATOM   1075  N   LYS A 176      31.695  41.446 377.199  1.00 96.14           N  
ANISOU 1075  N   LYS A 176    10964  16330   9236  -2467   1049   1436       N  
ATOM   1076  CA  LYS A 176      31.393  40.017 377.324  1.00 95.51           C  
ANISOU 1076  CA  LYS A 176    10630  16357   9300  -2367   1202   1730       C  
ATOM   1077  C   LYS A 176      31.916  39.246 376.105  1.00 98.07           C  
ANISOU 1077  C   LYS A 176    10935  16481   9847  -2441   1163   1872       C  
ATOM   1078  O   LYS A 176      31.654  39.635 374.963  1.00 96.32           O  
ANISOU 1078  O   LYS A 176    10830  15955   9811  -2489   1092   1769       O  
ATOM   1079  CB  LYS A 176      29.884  39.786 377.506  1.00 98.34           C  
ANISOU 1079  CB  LYS A 176    10904  16692   9770  -2199   1308   1767       C  
ATOM   1080  N   CYS A 177      32.691  38.180 376.366  1.00 95.15           N  
ANISOU 1080  N   CYS A 177    10428  16299   9424  -2411   1196   2098       N  
ATOM   1081  CA  CYS A 177      33.313  37.318 375.358  1.00 93.99           C  
ANISOU 1081  CA  CYS A 177    10267  16037   9406  -2383   1141   2232       C  
ATOM   1082  C   CYS A 177      33.005  35.849 375.658  1.00 98.25           C  
ANISOU 1082  C   CYS A 177    10733  16561  10034  -2233   1195   2508       C  
ATOM   1083  O   CYS A 177      33.057  35.445 376.817  1.00 99.44           O  
ANISOU 1083  O   CYS A 177    10789  16971  10024  -2189   1266   2641       O  
ATOM   1084  CB  CYS A 177      34.817  37.571 375.305  1.00 94.89           C  
ANISOU 1084  CB  CYS A 177    10338  16440   9274  -2464   1061   2216       C  
ATOM   1085  SG  CYS A 177      35.285  39.109 374.470  1.00 98.68           S  
ANISOU 1085  SG  CYS A 177    10959  16862   9671  -2742    913   1964       S  
ATOM   1086  N   VAL A 178      32.692  35.049 374.621  1.00 93.67           N  
ANISOU 1086  N   VAL A 178    10228  15664   9699  -2166   1135   2600       N  
ATOM   1087  CA  VAL A 178      32.354  33.631 374.788  1.00 94.30           C  
ANISOU 1087  CA  VAL A 178    10336  15618   9877  -2060   1114   2870       C  
ATOM   1088  C   VAL A 178      33.370  32.732 374.040  1.00 98.07           C  
ANISOU 1088  C   VAL A 178    10906  16030  10325  -1869    987   2948       C  
ATOM   1089  O   VAL A 178      33.504  32.822 372.816  1.00 96.28           O  
ANISOU 1089  O   VAL A 178    10756  15602  10225  -1820    900   2843       O  
ATOM   1090  CB  VAL A 178      30.887  33.337 374.356  1.00 97.85           C  
ANISOU 1090  CB  VAL A 178    10834  15739  10606  -2139   1111   2939       C  
ATOM   1091  CG1 VAL A 178      30.567  31.846 374.431  1.00 99.22           C  
ANISOU 1091  CG1 VAL A 178    11099  15726  10873  -2107   1023   3251       C  
ATOM   1092  CG2 VAL A 178      29.892  34.136 375.195  1.00 98.21           C  
ANISOU 1092  CG2 VAL A 178    10749  15967  10600  -2239   1237   2873       C  
ATOM   1093  N   LEU A 179      34.065  31.859 374.799  1.00 96.32           N  
ANISOU 1093  N   LEU A 179    10679  16006   9912  -1720    970   3132       N  
ATOM   1094  CA  LEU A 179      35.051  30.890 374.300  1.00 97.11           C  
ANISOU 1094  CA  LEU A 179    10887  16108   9903  -1435    836   3216       C  
ATOM   1095  C   LEU A 179      34.413  29.502 374.183  1.00102.91           C  
ANISOU 1095  C   LEU A 179    11868  16427  10806  -1323    699   3445       C  
ATOM   1096  O   LEU A 179      33.600  29.145 375.033  1.00103.64           O  
ANISOU 1096  O   LEU A 179    11969  16443  10967  -1481    737   3631       O  
ATOM   1097  CB  LEU A 179      36.305  30.840 375.208  1.00 98.63           C  
ANISOU 1097  CB  LEU A 179    10943  16809   9724  -1303    878   3267       C  
ATOM   1098  CG  LEU A 179      36.104  30.636 376.722  1.00104.71           C  
ANISOU 1098  CG  LEU A 179    11629  17790  10366  -1381    987   3425       C  
ATOM   1099  CD1 LEU A 179      36.424  29.216 377.130  1.00107.13           C  
ANISOU 1099  CD1 LEU A 179    12087  18036  10580  -1130    888   3686       C  
ATOM   1100  CD2 LEU A 179      36.957  31.599 377.520  1.00107.21           C  
ANISOU 1100  CD2 LEU A 179    11721  18633  10379  -1470   1094   3307       C  
ATOM   1101  N   ASP A 180      34.784  28.721 373.152  1.00100.45           N  
ANISOU 1101  N   ASP A 180    11769  15866  10533  -1055    513   3442       N  
ATOM   1102  CA  ASP A 180      34.230  27.378 372.942  1.00102.48           C  
ANISOU 1102  CA  ASP A 180    12360  15641  10938   -951    307   3644       C  
ATOM   1103  C   ASP A 180      35.330  26.327 372.730  1.00109.05           C  
ANISOU 1103  C   ASP A 180    13422  16476  11534   -486    109   3700       C  
ATOM   1104  O   ASP A 180      36.343  26.608 372.085  1.00108.30           O  
ANISOU 1104  O   ASP A 180    13237  16664  11246   -203     94   3527       O  
ATOM   1105  CB  ASP A 180      33.253  27.373 371.753  1.00103.18           C  
ANISOU 1105  CB  ASP A 180    12587  15264  11351  -1064    210   3562       C  
ATOM   1106  CG  ASP A 180      32.414  26.113 371.637  1.00116.82           C  
ANISOU 1106  CG  ASP A 180    14668  16457  13262  -1112    -20   3798       C  
ATOM   1107  OD1 ASP A 180      31.412  25.993 372.382  1.00118.34           O  
ANISOU 1107  OD1 ASP A 180    14817  16577  13569  -1454     27   4002       O  
ATOM   1108  OD2 ASP A 180      32.749  25.253 370.794  1.00124.30           O  
ANISOU 1108  OD2 ASP A 180    15941  17077  14210   -813   -269   3785       O  
ATOM   1109  N   MET A 181      35.108  25.112 373.274  1.00108.58           N  
ANISOU 1109  N   MET A 181    13669  16124  11463   -401    -63   3956       N  
ATOM   1110  CA  MET A 181      36.013  23.961 373.182  1.00111.39           C  
ANISOU 1110  CA  MET A 181    14349  16395  11579     94   -303   4029       C  
ATOM   1111  C   MET A 181      35.485  22.981 372.131  1.00116.87           C  
ANISOU 1111  C   MET A 181    15521  16414  12469    243   -630   4050       C  
ATOM   1112  O   MET A 181      34.311  22.613 372.174  1.00116.94           O  
ANISOU 1112  O   MET A 181    15711  15962  12760   -121   -723   4217       O  
ATOM   1113  CB  MET A 181      36.170  23.291 374.557  1.00116.45           C  
ANISOU 1113  CB  MET A 181    15068  17139  12038     99   -313   4305       C  
ATOM   1114  CG  MET A 181      36.874  24.192 375.558  1.00119.11           C  
ANISOU 1114  CG  MET A 181    14957  18174  12125     33    -21   4255       C  
ATOM   1115  SD  MET A 181      36.990  23.499 377.228  1.00126.57           S  
ANISOU 1115  SD  MET A 181    15934  19294  12862      4      2   4585       S  
ATOM   1116  CE  MET A 181      38.226  22.207 376.977  1.00126.98           C  
ANISOU 1116  CE  MET A 181    16388  19283  12574    703   -289   4631       C  
ATOM   1117  N   ARG A 182      36.339  22.601 371.162  1.00114.44           N  
ANISOU 1117  N   ARG A 182    15399  16100  11984    776   -814   3878       N  
ATOM   1118  CA  ARG A 182      35.973  21.717 370.049  1.00116.03           C  
ANISOU 1118  CA  ARG A 182    16083  15683  12319   1015  -1157   3835       C  
ATOM   1119  C   ARG A 182      35.825  20.244 370.461  1.00124.64           C  
ANISOU 1119  C   ARG A 182    17784  16220  13354   1200  -1524   4081       C  
ATOM   1120  O   ARG A 182      35.062  19.515 369.819  1.00125.91           O  
ANISOU 1120  O   ARG A 182    18399  15712  13728   1134  -1828   4138       O  
ATOM   1121  CB  ARG A 182      37.003  21.827 368.918  1.00116.31           C  
ANISOU 1121  CB  ARG A 182    16074  16002  12114   1591  -1229   3552       C  
ATOM   1122  N   SER A 183      36.554  19.806 371.508  1.00123.43           N  
ANISOU 1122  N   SER A 183    17672  16323  12901   1421  -1523   4233       N  
ATOM   1123  CA  SER A 183      36.529  18.421 371.982  1.00127.90           C  
ANISOU 1123  CA  SER A 183    18857  16375  13366   1625  -1895   4484       C  
ATOM   1124  C   SER A 183      35.556  18.215 373.152  1.00132.19           C  
ANISOU 1124  C   SER A 183    19418  16716  14093    994  -1857   4863       C  
ATOM   1125  O   SER A 183      34.711  17.321 373.079  1.00134.72           O  
ANISOU 1125  O   SER A 183    20242  16359  14586    761  -2190   5100       O  
ATOM   1126  CB  SER A 183      37.930  17.967 372.385  1.00134.13           C  
ANISOU 1126  CB  SER A 183    19723  17567  13673   2318  -1957   4436       C  
ATOM   1127  OG  SER A 183      38.449  18.752 373.446  1.00141.06           O  
ANISOU 1127  OG  SER A 183    20045  19177  14376   2168  -1581   4481       O  
ATOM   1128  N   MET A 184      35.677  19.031 374.221  1.00126.28           N  
ANISOU 1128  N   MET A 184    18128  16575  13277    711  -1478   4932       N  
ATOM   1129  CA  MET A 184      34.855  18.924 375.434  1.00126.99           C  
ANISOU 1129  CA  MET A 184    18129  16655  13466    164  -1397   5290       C  
ATOM   1130  C   MET A 184      33.454  19.560 375.272  1.00128.33           C  
ANISOU 1130  C   MET A 184    18056  16704  14001   -497  -1265   5360       C  
ATOM   1131  O   MET A 184      32.606  19.372 376.150  1.00129.34           O  
ANISOU 1131  O   MET A 184    18151  16781  14211   -972  -1265   5699       O  
ATOM   1132  CB  MET A 184      35.584  19.542 376.641  1.00128.26           C  
ANISOU 1132  CB  MET A 184    17810  17555  13366    193  -1057   5305       C  
ATOM   1133  CG  MET A 184      36.860  18.805 377.034  1.00135.01           C  
ANISOU 1133  CG  MET A 184    18900  18570  13829    780  -1195   5342       C  
ATOM   1134  SD  MET A 184      36.599  17.348 378.075  1.00144.83           S  
ANISOU 1134  SD  MET A 184    20715  19319  14997    706  -1541   5826       S  
ATOM   1135  CE  MET A 184      38.280  16.803 378.287  1.00144.20           C  
ANISOU 1135  CE  MET A 184    20814  19572  14404   1552  -1637   5728       C  
ATOM   1136  N   ASP A 185      33.214  20.288 374.151  1.00121.61           N  
ANISOU 1136  N   ASP A 185    17022  15849  13334   -512  -1161   5058       N  
ATOM   1137  CA  ASP A 185      31.954  20.968 373.790  1.00119.14           C  
ANISOU 1137  CA  ASP A 185    16466  15464  13339  -1034  -1029   5054       C  
ATOM   1138  C   ASP A 185      31.467  21.918 374.918  1.00121.10           C  
ANISOU 1138  C   ASP A 185    16174  16270  13568  -1434   -665   5153       C  
ATOM   1139  O   ASP A 185      30.264  22.017 375.182  1.00121.36           O  
ANISOU 1139  O   ASP A 185    16094  16255  13762  -1911   -637   5372       O  
ATOM   1140  CB  ASP A 185      30.858  19.947 373.402  1.00124.06           C  
ANISOU 1140  CB  ASP A 185    17551  15402  14185  -1354  -1392   5326       C  
ATOM   1141  CG  ASP A 185      31.136  19.187 372.118  1.00135.23           C  
ANISOU 1141  CG  ASP A 185    19515  16223  15645   -972  -1769   5171       C  
ATOM   1142  OD1 ASP A 185      32.033  18.316 372.126  1.00138.86           O  
ANISOU 1142  OD1 ASP A 185    20404  16479  15879   -495  -2029   5183       O  
ATOM   1143  OD2 ASP A 185      30.425  19.431 371.118  1.00138.91           O  
ANISOU 1143  OD2 ASP A 185    20003  16427  16351  -1125  -1822   5039       O  
ATOM   1144  N   PHE A 186      32.417  22.629 375.558  1.00115.40           N  
ANISOU 1144  N   PHE A 186    15113  16118  12615  -1220   -401   4986       N  
ATOM   1145  CA  PHE A 186      32.146  23.562 376.653  1.00113.53           C  
ANISOU 1145  CA  PHE A 186    14403  16432  12302  -1493    -77   5017       C  
ATOM   1146  C   PHE A 186      32.292  25.020 376.193  1.00112.30           C  
ANISOU 1146  C   PHE A 186    13872  16610  12186  -1507    188   4647       C  
ATOM   1147  O   PHE A 186      33.252  25.361 375.500  1.00110.27           O  
ANISOU 1147  O   PHE A 186    13618  16430  11852  -1208    189   4383       O  
ATOM   1148  CB  PHE A 186      33.085  23.272 377.842  1.00117.03           C  
ANISOU 1148  CB  PHE A 186    14783  17257  12424  -1289    -14   5138       C  
ATOM   1149  CG  PHE A 186      32.785  24.036 379.113  1.00118.10           C  
ANISOU 1149  CG  PHE A 186    14487  17940  12446  -1548    272   5212       C  
ATOM   1150  CD1 PHE A 186      31.894  23.531 380.053  1.00123.71           C  
ANISOU 1150  CD1 PHE A 186    15161  18671  13169  -1884    252   5581       C  
ATOM   1151  CD2 PHE A 186      33.421  25.242 379.387  1.00117.76           C  
ANISOU 1151  CD2 PHE A 186    14084  18414  12245  -1456    533   4925       C  
ATOM   1152  CE1 PHE A 186      31.623  24.234 381.232  1.00124.54           C  
ANISOU 1152  CE1 PHE A 186    14851  19343  13126  -2059    512   5633       C  
ATOM   1153  CE2 PHE A 186      33.146  25.947 380.562  1.00120.57           C  
ANISOU 1153  CE2 PHE A 186    14088  19254  12470  -1647    764   4962       C  
ATOM   1154  CZ  PHE A 186      32.252  25.436 381.478  1.00121.11           C  
ANISOU 1154  CZ  PHE A 186    14100  19373  12544  -1912    762   5303       C  
ATOM   1155  N   LYS A 187      31.344  25.874 376.613  1.00106.79           N  
ANISOU 1155  N   LYS A 187    12861  16142  11572  -1844    392   4645       N  
ATOM   1156  CA  LYS A 187      31.319  27.306 376.314  1.00103.11           C  
ANISOU 1156  CA  LYS A 187    12097  15948  11133  -1892    613   4316       C  
ATOM   1157  C   LYS A 187      31.387  28.115 377.615  1.00106.72           C  
ANISOU 1157  C   LYS A 187    12225  16948  11374  -1980    847   4300       C  
ATOM   1158  O   LYS A 187      30.795  27.700 378.613  1.00108.53           O  
ANISOU 1158  O   LYS A 187    12364  17330  11542  -2146    880   4569       O  
ATOM   1159  CB  LYS A 187      30.062  27.667 375.511  1.00104.39           C  
ANISOU 1159  CB  LYS A 187    12239  15851  11573  -2133    607   4269       C  
ATOM   1160  N   SER A 188      32.113  29.256 377.616  1.00101.07           N  
ANISOU 1160  N   SER A 188    11340  16540  10522  -1885    984   4000       N  
ATOM   1161  CA  SER A 188      32.253  30.089 378.818  1.00101.18           C  
ANISOU 1161  CA  SER A 188    11093  17045  10306  -1942   1170   3935       C  
ATOM   1162  C   SER A 188      32.298  31.591 378.504  1.00101.93           C  
ANISOU 1162  C   SER A 188    11071  17271  10387  -1995   1270   3578       C  
ATOM   1163  O   SER A 188      33.143  32.040 377.726  1.00 99.96           O  
ANISOU 1163  O   SER A 188    10885  16960  10136  -1923   1217   3380       O  
ATOM   1164  CB  SER A 188      33.503  29.692 379.602  1.00106.93           C  
ANISOU 1164  CB  SER A 188    11799  18082  10748  -1758   1174   4011       C  
ATOM   1165  OG  SER A 188      33.609  30.399 380.828  1.00118.03           O  
ANISOU 1165  OG  SER A 188    12967  19956  11921  -1818   1335   3965       O  
ATOM   1166  N   ASN A 189      31.399  32.365 379.145  1.00 98.13           N  
ANISOU 1166  N   ASN A 189    10430  16994   9860  -2108   1392   3508       N  
ATOM   1167  CA  ASN A 189      31.320  33.819 379.005  1.00 96.34           C  
ANISOU 1167  CA  ASN A 189    10164  16855   9584  -2140   1449   3169       C  
ATOM   1168  C   ASN A 189      32.293  34.470 380.001  1.00100.72           C  
ANISOU 1168  C   ASN A 189    10636  17810   9822  -2105   1500   3046       C  
ATOM   1169  O   ASN A 189      32.021  34.494 381.204  1.00102.16           O  
ANISOU 1169  O   ASN A 189    10677  18323   9817  -2083   1590   3128       O  
ATOM   1170  CB  ASN A 189      29.884  34.314 379.204  1.00 96.70           C  
ANISOU 1170  CB  ASN A 189    10116  16935   9691  -2195   1523   3132       C  
ATOM   1171  N   SER A 190      33.446  34.958 379.497  1.00 95.79           N  
ANISOU 1171  N   SER A 190    10081  17199   9115  -2115   1431   2874       N  
ATOM   1172  CA  SER A 190      34.505  35.563 380.310  1.00 96.29           C  
ANISOU 1172  CA  SER A 190    10077  17647   8861  -2139   1441   2772       C  
ATOM   1173  C   SER A 190      34.737  37.040 379.984  1.00 99.79           C  
ANISOU 1173  C   SER A 190    10623  18063   9229  -2289   1368   2454       C  
ATOM   1174  O   SER A 190      34.649  37.442 378.825  1.00 97.70           O  
ANISOU 1174  O   SER A 190    10481  17497   9144  -2362   1287   2334       O  
ATOM   1175  CB  SER A 190      35.814  34.801 380.122  1.00 99.70           C  
ANISOU 1175  CB  SER A 190    10476  18245   9162  -2053   1390   2907       C  
ATOM   1176  OG  SER A 190      35.641  33.401 380.272  1.00108.47           O  
ANISOU 1176  OG  SER A 190    11581  19307  10326  -1891   1404   3196       O  
ATOM   1177  N   ALA A 191      35.066  37.835 381.016  1.00 98.60           N  
ANISOU 1177  N   ALA A 191    10451  18216   8798  -2343   1371   2325       N  
ATOM   1178  CA  ALA A 191      35.375  39.264 380.909  1.00 99.25           C  
ANISOU 1178  CA  ALA A 191    10703  18267   8741  -2516   1243   2033       C  
ATOM   1179  C   ALA A 191      36.626  39.584 381.737  1.00105.84           C  
ANISOU 1179  C   ALA A 191    11474  19517   9222  -2636   1193   2023       C  
ATOM   1180  O   ALA A 191      36.694  39.209 382.910  1.00106.92           O  
ANISOU 1180  O   ALA A 191    11468  19977   9179  -2524   1290   2117       O  
ATOM   1181  CB  ALA A 191      34.191  40.097 381.371  1.00100.88           C  
ANISOU 1181  CB  ALA A 191    11028  18361   8940  -2426   1252   1826       C  
ATOM   1182  N   VAL A 192      37.624  40.245 381.116  1.00102.96           N  
ANISOU 1182  N   VAL A 192    11192  19185   8742  -2888   1034   1939       N  
ATOM   1183  CA  VAL A 192      38.915  40.577 381.737  1.00104.75           C  
ANISOU 1183  CA  VAL A 192    11338  19855   8607  -3078    953   1956       C  
ATOM   1184  C   VAL A 192      38.950  42.060 382.162  1.00110.49           C  
ANISOU 1184  C   VAL A 192    12335  20510   9136  -3331    759   1683       C  
ATOM   1185  O   VAL A 192      38.439  42.925 381.449  1.00109.62           O  
ANISOU 1185  O   VAL A 192    12496  20001   9154  -3461    614   1503       O  
ATOM   1186  CB  VAL A 192      40.106  40.223 380.789  1.00108.36           C  
ANISOU 1186  CB  VAL A 192    11651  20533   8988  -3210    884   2111       C  
ATOM   1187  CG1 VAL A 192      41.458  40.431 381.470  1.00110.38           C  
ANISOU 1187  CG1 VAL A 192    11735  21379   8826  -3378    830   2190       C  
ATOM   1188  CG2 VAL A 192      39.998  38.791 380.268  1.00106.64           C  
ANISOU 1188  CG2 VAL A 192    11280  20262   8975  -2898   1015   2326       C  
ATOM   1189  N   ALA A 193      39.566  42.334 383.326  1.00109.54           N  
ANISOU 1189  N   ALA A 193    12172  20759   8688  -3391    734   1651       N  
ATOM   1190  CA  ALA A 193      39.741  43.673 383.888  1.00111.97           C  
ANISOU 1190  CA  ALA A 193    12779  21018   8746  -3626    504   1393       C  
ATOM   1191  C   ALA A 193      41.177  43.854 384.415  1.00118.25           C  
ANISOU 1191  C   ALA A 193    13456  22314   9159  -3938    390   1479       C  
ATOM   1192  O   ALA A 193      41.689  42.984 385.124  1.00118.03           O  
ANISOU 1192  O   ALA A 193    13119  22747   8981  -3791    556   1654       O  
ATOM   1193  CB  ALA A 193      38.730  43.912 384.998  1.00113.89           C  
ANISOU 1193  CB  ALA A 193    13127  21207   8940  -3317    573   1211       C  
ATOM   1194  N   TRP A 194      41.833  44.969 384.039  1.00116.88           N  
ANISOU 1194  N   TRP A 194    13531  22065   8812  -4393     90   1379       N  
ATOM   1195  CA  TRP A 194      43.210  45.276 384.445  1.00119.37           C  
ANISOU 1195  CA  TRP A 194    13739  22886   8729  -4793    -69   1479       C  
ATOM   1196  C   TRP A 194      43.419  46.780 384.637  1.00126.87           C  
ANISOU 1196  C   TRP A 194    15162  23591   9453  -5236   -458   1246       C  
ATOM   1197  O   TRP A 194      42.812  47.585 383.926  1.00126.43           O  
ANISOU 1197  O   TRP A 194    15500  22977   9562  -5349   -652   1077       O  
ATOM   1198  CB  TRP A 194      44.211  44.736 383.412  1.00117.27           C  
ANISOU 1198  CB  TRP A 194    13156  22978   8424  -5003    -60   1761       C  
ATOM   1199  N   SER A 195      44.288  47.151 385.600  1.00126.78           N  
ANISOU 1199  N   SER A 195    15138  23986   9047  -5491   -596   1241       N  
ATOM   1200  CA  SER A 195      44.622  48.543 385.926  1.00130.74           C  
ANISOU 1200  CA  SER A 195    16127  24282   9266  -5960  -1022   1037       C  
ATOM   1201  C   SER A 195      46.027  48.660 386.539  1.00137.68           C  
ANISOU 1201  C   SER A 195    16795  25824   9693  -6419  -1163   1209       C  
ATOM   1202  O   SER A 195      46.517  47.710 387.158  1.00136.28           O  
ANISOU 1202  O   SER A 195    16142  26247   9390  -6200   -892   1386       O  
ATOM   1203  CB  SER A 195      43.587  49.134 386.879  1.00135.93           C  
ANISOU 1203  CB  SER A 195    17194  24539   9914  -5600  -1085    673       C  
ATOM   1204  OG  SER A 195      43.833  50.510 387.124  1.00149.20           O  
ANISOU 1204  OG  SER A 195    19459  25905  11323  -6009  -1555    437       O  
ATOM   1205  N   ASN A 196      46.660  49.839 386.372  1.00137.92           N  
ANISOU 1205  N   ASN A 196    17199  25745   9460  -7074  -1610   1169       N  
ATOM   1206  CA  ASN A 196      47.996  50.142 386.893  1.00141.46           C  
ANISOU 1206  CA  ASN A 196    17497  26818   9435  -7637  -1824   1340       C  
ATOM   1207  C   ASN A 196      47.902  51.181 388.037  1.00149.64           C  
ANISOU 1207  C   ASN A 196    19075  27591  10191  -7808  -2170   1032       C  
ATOM   1208  O   ASN A 196      48.544  52.236 387.988  1.00153.58           O  
ANISOU 1208  O   ASN A 196    19967  27982  10406  -8487  -2644   1020       O  
ATOM   1209  CB  ASN A 196      48.914  50.623 385.760  1.00143.67           C  
ANISOU 1209  CB  ASN A 196    17732  27285   9570  -8350  -2103   1611       C  
ATOM   1210  N   LYS A 197      47.095  50.862 389.070  1.00145.27           N  
ANISOU 1210  N   LYS A 197    18548  26951   9698  -7191  -1952    793       N  
ATOM   1211  CA  LYS A 197      46.869  51.717 390.239  1.00148.91           C  
ANISOU 1211  CA  LYS A 197    19492  27195   9890  -7167  -2231    456       C  
ATOM   1212  C   LYS A 197      47.410  51.072 391.515  1.00153.24           C  
ANISOU 1212  C   LYS A 197    19608  28458  10158  -6979  -2008    528       C  
ATOM   1213  O   LYS A 197      47.385  49.844 391.638  1.00149.06           O  
ANISOU 1213  O   LYS A 197    18473  28405   9760  -6586  -1554    751       O  
ATOM   1214  CB  LYS A 197      45.373  52.020 390.399  1.00150.61           C  
ANISOU 1214  CB  LYS A 197    20144  26721  10359  -6543  -2202     76       C  
ATOM   1215  N   SER A 198      47.889  51.910 392.467  1.00154.48           N  
ANISOU 1215  N   SER A 198    20114  28662   9919  -7254  -2356    335       N  
ATOM   1216  CA  SER A 198      48.442  51.482 393.757  1.00155.72           C  
ANISOU 1216  CA  SER A 198    19929  29482   9755  -7121  -2209    366       C  
ATOM   1217  C   SER A 198      47.378  50.739 394.566  1.00157.63           C  
ANISOU 1217  C   SER A 198    19973  29739  10181  -6257  -1798    211       C  
ATOM   1218  O   SER A 198      46.376  51.336 394.969  1.00158.48           O  
ANISOU 1218  O   SER A 198    20546  29333  10335  -5881  -1922   -153       O  
ATOM   1219  CB  SER A 198      48.985  52.677 394.538  1.00164.61           C  
ANISOU 1219  CB  SER A 198    21591  30520  10433  -7604  -2737    139       C  
ATOM   1220  N   ASP A 199      47.586  49.412 394.741  1.00151.30           N  
ANISOU 1220  N   ASP A 199    18478  29548   9462  -5939  -1324    511       N  
ATOM   1221  CA  ASP A 199      46.711  48.449 395.425  1.00148.48           C  
ANISOU 1221  CA  ASP A 199    17796  29346   9276  -5203   -892    505       C  
ATOM   1222  C   ASP A 199      45.348  48.347 394.697  1.00149.05           C  
ANISOU 1222  C   ASP A 199    18047  28800   9786  -4777   -760    386       C  
ATOM   1223  O   ASP A 199      44.391  49.041 395.056  1.00149.74           O  
ANISOU 1223  O   ASP A 199    18555  28466   9874  -4484   -900     43       O  
ATOM   1224  CB  ASP A 199      46.543  48.775 396.925  1.00153.47           C  
ANISOU 1224  CB  ASP A 199    18538  30198   9576  -4945   -951    255       C  
ATOM   1225  N   PHE A 200      45.289  47.495 393.648  1.00141.76           N  
ANISOU 1225  N   PHE A 200    16807  27854   9199  -4731   -510    664       N  
ATOM   1226  CA  PHE A 200      44.090  47.256 392.838  1.00138.54           C  
ANISOU 1226  CA  PHE A 200    16494  26926   9218  -4384   -364    615       C  
ATOM   1227  C   PHE A 200      43.352  46.013 393.346  1.00139.98           C  
ANISOU 1227  C   PHE A 200    16246  27362   9578  -3802     70    774       C  
ATOM   1228  O   PHE A 200      43.929  44.922 393.376  1.00138.19           O  
ANISOU 1228  O   PHE A 200    15559  27585   9362  -3754    321   1096       O  
ATOM   1229  CB  PHE A 200      44.453  47.111 391.351  1.00138.01           C  
ANISOU 1229  CB  PHE A 200    16385  26652   9401  -4708   -395    815       C  
ATOM   1230  N   ALA A 201      42.086  46.190 393.770  1.00136.44           N  
ANISOU 1230  N   ALA A 201    15958  26654   9229  -3359    132    560       N  
ATOM   1231  CA  ALA A 201      41.241  45.126 394.322  1.00134.51           C  
ANISOU 1231  CA  ALA A 201    15335  26653   9121  -2853    499    722       C  
ATOM   1232  C   ALA A 201      40.322  44.515 393.265  1.00135.01           C  
ANISOU 1232  C   ALA A 201    15323  26351   9621  -2692    672    862       C  
ATOM   1233  O   ALA A 201      39.869  45.219 392.361  1.00134.07           O  
ANISOU 1233  O   ALA A 201    15547  25719   9676  -2792    497    684       O  
ATOM   1234  CB  ALA A 201      40.413  45.667 395.475  1.00138.00           C  
ANISOU 1234  CB  ALA A 201    15921  27182   9332  -2457    463    436       C  
ATOM   1235  N   CYS A 202      40.037  43.203 393.399  1.00129.64           N  
ANISOU 1235  N   CYS A 202    14223  25925   9108  -2452    992   1189       N  
ATOM   1236  CA  CYS A 202      39.185  42.438 392.486  1.00126.48           C  
ANISOU 1236  CA  CYS A 202    13720  25226   9109  -2312   1160   1372       C  
ATOM   1237  C   CYS A 202      37.707  42.829 392.639  1.00130.74           C  
ANISOU 1237  C   CYS A 202    14381  25557   9735  -1982   1188   1189       C  
ATOM   1238  O   CYS A 202      37.069  43.159 391.638  1.00128.85           O  
ANISOU 1238  O   CYS A 202    14333  24867   9756  -1993   1131   1103       O  
ATOM   1239  CB  CYS A 202      39.384  40.937 392.689  1.00125.38           C  
ANISOU 1239  CB  CYS A 202    13168  25405   9066  -2186   1426   1784       C  
ATOM   1240  SG  CYS A 202      41.040  40.339 392.258  1.00128.73           S  
ANISOU 1240  SG  CYS A 202    13420  26124   9370  -2458   1407   2014       S  
ATOM   1241  N   ALA A 203      37.172  42.787 393.884  1.00129.45           N  
ANISOU 1241  N   ALA A 203    14076  25783   9325  -1668   1280   1140       N  
ATOM   1242  CA  ALA A 203      35.775  43.096 394.217  1.00130.48           C  
ANISOU 1242  CA  ALA A 203    14230  25916   9431  -1282   1325    990       C  
ATOM   1243  C   ALA A 203      35.407  44.564 393.948  1.00136.38           C  
ANISOU 1243  C   ALA A 203    15485  26278  10054  -1211   1031    517       C  
ATOM   1244  O   ALA A 203      34.292  44.833 393.491  1.00135.66           O  
ANISOU 1244  O   ALA A 203    15493  25981  10071   -960   1033    397       O  
ATOM   1245  CB  ALA A 203      35.498  42.754 395.673  1.00133.71           C  
ANISOU 1245  CB  ALA A 203    14324  26949   9529   -973   1479   1072       C  
ATOM   1246  N   ASN A 204      36.336  45.503 394.230  1.00135.39           N  
ANISOU 1246  N   ASN A 204    15698  26061   9681  -1436    755    261       N  
ATOM   1247  CA  ASN A 204      36.143  46.943 394.031  1.00137.95           C  
ANISOU 1247  CA  ASN A 204    16616  25953   9846  -1413    394   -191       C  
ATOM   1248  C   ASN A 204      36.076  47.314 392.546  1.00140.01           C  
ANISOU 1248  C   ASN A 204    17184  25583  10430  -1688    245   -229       C  
ATOM   1249  O   ASN A 204      35.356  48.248 392.189  1.00141.06           O  
ANISOU 1249  O   ASN A 204    17757  25307  10533  -1514     25   -551       O  
ATOM   1250  CB  ASN A 204      37.260  47.731 394.710  1.00142.26           C  
ANISOU 1250  CB  ASN A 204    17447  26574  10032  -1675    106   -392       C  
ATOM   1251  N   ALA A 205      36.825  46.583 391.691  1.00133.61           N  
ANISOU 1251  N   ALA A 205    16151  24718   9897  -2076    354     91       N  
ATOM   1252  CA  ALA A 205      36.895  46.794 390.240  1.00131.22           C  
ANISOU 1252  CA  ALA A 205    16058  23900   9898  -2366    240    113       C  
ATOM   1253  C   ALA A 205      35.566  46.477 389.536  1.00132.84           C  
ANISOU 1253  C   ALA A 205    16205  23856  10412  -2048    399    130       C  
ATOM   1254  O   ALA A 205      35.192  47.193 388.605  1.00132.07           O  
ANISOU 1254  O   ALA A 205    16469  23264  10446  -2100    215    -56       O  
ATOM   1255  CB  ALA A 205      38.008  45.947 389.643  1.00129.48           C  
ANISOU 1255  CB  ALA A 205    15534  23837   9825  -2758    343    463       C  
ATOM   1256  N   PHE A 206      34.863  45.411 389.975  1.00128.08           N  
ANISOU 1256  N   PHE A 206    15153  23607   9905  -1749    722    373       N  
ATOM   1257  CA  PHE A 206      33.584  44.990 389.401  1.00126.17           C  
ANISOU 1257  CA  PHE A 206    14780  23236   9921  -1486    886    449       C  
ATOM   1258  C   PHE A 206      32.446  45.893 389.887  1.00132.26           C  
ANISOU 1258  C   PHE A 206    15760  24027  10464  -1035    798    114       C  
ATOM   1259  O   PHE A 206      32.286  46.090 391.096  1.00134.52           O  
ANISOU 1259  O   PHE A 206    15960  24739  10412   -751    820     15       O  
ATOM   1260  CB  PHE A 206      33.291  43.521 389.743  1.00126.45           C  
ANISOU 1260  CB  PHE A 206    14288  23661  10098  -1403   1209    871       C  
ATOM   1261  N   ASN A 207      31.673  46.454 388.933  1.00127.89           N  
ANISOU 1261  N   ASN A 207    15484  23044  10066   -933    691    -69       N  
ATOM   1262  CA  ASN A 207      30.539  47.344 389.193  1.00153.32           C  
ANISOU 1262  CA  ASN A 207    18941  26257  13058   -438    585   -409       C  
ATOM   1263  C   ASN A 207      29.501  47.233 388.082  1.00165.28           C  
ANISOU 1263  C   ASN A 207    20448  27494  14856   -318    652   -382       C  
ATOM   1264  O   ASN A 207      29.024  46.139 387.789  1.00119.54           O  
ANISOU 1264  O   ASN A 207    14216  21883   9320   -369    918    -35       O  
ATOM   1265  CB  ASN A 207      31.007  48.792 389.331  1.00157.18           C  
ANISOU 1265  CB  ASN A 207    20082  26380  13261   -429    181   -857       C  
TER    1266      ASN A 207                                                      
ATOM   1267  N   GLY B   3      38.960  33.258 343.950  1.00 47.76           N  
ANISOU 1267  N   GLY B   3     5348   4108   8690    911  -2046   -126       N  
ATOM   1268  CA  GLY B   3      38.449  34.332 344.796  1.00 44.46           C  
ANISOU 1268  CA  GLY B   3     4852   3882   8159    583  -1885    183       C  
ATOM   1269  C   GLY B   3      39.057  35.707 344.562  1.00 46.43           C  
ANISOU 1269  C   GLY B   3     4902   4607   8133    493  -1600    104       C  
ATOM   1270  O   GLY B   3      39.862  35.896 343.640  1.00 46.81           O  
ANISOU 1270  O   GLY B   3     4839   4894   8052    644  -1502   -169       O  
ATOM   1271  N   VAL B   4      38.660  36.685 345.409  1.00 40.44           N  
ANISOU 1271  N   VAL B   4     4101   3994   7271    242  -1478    351       N  
ATOM   1272  CA  VAL B   4      39.132  38.077 345.367  1.00 38.36           C  
ANISOU 1272  CA  VAL B   4     3700   4109   6766     98  -1249    324       C  
ATOM   1273  C   VAL B   4      40.192  38.280 346.461  1.00 44.23           C  
ANISOU 1273  C   VAL B   4     4288   5069   7448    137  -1247    417       C  
ATOM   1274  O   VAL B   4      39.965  37.920 347.624  1.00 44.48           O  
ANISOU 1274  O   VAL B   4     4357   4990   7555    104  -1343    641       O  
ATOM   1275  CB  VAL B   4      37.967  39.098 345.481  1.00 39.09           C  
ANISOU 1275  CB  VAL B   4     3892   4193   6766   -186  -1125    486       C  
ATOM   1276  CG1 VAL B   4      38.474  40.541 345.573  1.00 37.21           C  
ANISOU 1276  CG1 VAL B   4     3565   4268   6307   -341   -935    474       C  
ATOM   1277  CG2 VAL B   4      37.006  38.949 344.311  1.00 38.57           C  
ANISOU 1277  CG2 VAL B   4     3941   3977   6737   -232  -1126    399       C  
ATOM   1278  N   THR B   5      41.351  38.843 346.070  1.00 41.36           N  
ANISOU 1278  N   THR B   5     3731   5055   6929    192  -1145    263       N  
ATOM   1279  CA  THR B   5      42.482  39.101 346.958  1.00 42.02           C  
ANISOU 1279  CA  THR B   5     3629   5414   6922    206  -1147    335       C  
ATOM   1280  C   THR B   5      42.936  40.538 346.778  1.00 43.59           C  
ANISOU 1280  C   THR B   5     3725   5953   6884    -44   -978    317       C  
ATOM   1281  O   THR B   5      43.518  40.881 345.748  1.00 43.51           O  
ANISOU 1281  O   THR B   5     3590   6179   6762    -32   -885    158       O  
ATOM   1282  CB  THR B   5      43.632  38.087 346.711  1.00 56.22           C  
ANISOU 1282  CB  THR B   5     5254   7323   8786    558  -1249    197       C  
ATOM   1283  OG1 THR B   5      43.792  37.867 345.305  1.00 58.17           O  
ANISOU 1283  OG1 THR B   5     5452   7661   8990    722  -1191    -69       O  
ATOM   1284  CG2 THR B   5      43.411  36.754 347.430  1.00 56.40           C  
ANISOU 1284  CG2 THR B   5     5390   6983   9058    775  -1470    301       C  
ATOM   1285  N   GLN B   6      42.650  41.384 347.774  1.00 38.87           N  
ANISOU 1285  N   GLN B   6     3193   5376   6200   -277   -952    482       N  
ATOM   1286  CA  GLN B   6      43.030  42.794 347.738  1.00 38.24           C  
ANISOU 1286  CA  GLN B   6     3078   5537   5916   -549   -840    481       C  
ATOM   1287  C   GLN B   6      44.321  43.025 348.548  1.00 46.28           C  
ANISOU 1287  C   GLN B   6     3893   6874   6819   -595   -892    527       C  
ATOM   1288  O   GLN B   6      44.543  42.375 349.575  1.00 46.43           O  
ANISOU 1288  O   GLN B   6     3881   6868   6893   -492  -1000    630       O  
ATOM   1289  CB  GLN B   6      41.882  43.713 348.198  1.00 36.95           C  
ANISOU 1289  CB  GLN B   6     3157   5175   5707   -765   -784    587       C  
ATOM   1290  CG  GLN B   6      41.349  43.436 349.598  1.00 41.00           C  
ANISOU 1290  CG  GLN B   6     3773   5550   6256   -746   -863    751       C  
ATOM   1291  CD  GLN B   6      40.065  44.165 349.869  1.00 50.21           C  
ANISOU 1291  CD  GLN B   6     5160   6546   7371   -870   -792    831       C  
ATOM   1292  OE1 GLN B   6      38.992  43.574 349.887  1.00 46.27           O  
ANISOU 1292  OE1 GLN B   6     4755   5849   6978   -795   -804    922       O  
ATOM   1293  NE2 GLN B   6      40.144  45.447 350.164  1.00 40.31           N  
ANISOU 1293  NE2 GLN B   6     3996   5371   5950  -1056   -735    809       N  
ATOM   1294  N   THR B   7      45.180  43.935 348.048  1.00 45.48           N  
ANISOU 1294  N   THR B   7     3634   7097   6550   -768   -827    475       N  
ATOM   1295  CA  THR B   7      46.484  44.271 348.626  1.00 48.00           C  
ANISOU 1295  CA  THR B   7     3718   7789   6729   -869   -881    527       C  
ATOM   1296  C   THR B   7      46.530  45.762 349.026  1.00 52.71           C  
ANISOU 1296  C   THR B   7     4430   8438   7160  -1274   -870    593       C  
ATOM   1297  O   THR B   7      46.176  46.596 348.196  1.00 52.22           O  
ANISOU 1297  O   THR B   7     4461   8338   7044  -1461   -788    562       O  
ATOM   1298  CB  THR B   7      47.591  43.951 347.593  1.00 60.20           C  
ANISOU 1298  CB  THR B   7     4933   9738   8205   -729   -843    431       C  
ATOM   1299  OG1 THR B   7      47.327  42.700 346.952  1.00 61.17           O  
ANISOU 1299  OG1 THR B   7     5041   9720   8483   -338   -851    305       O  
ATOM   1300  CG2 THR B   7      48.992  43.955 348.196  1.00 61.66           C  
ANISOU 1300  CG2 THR B   7     4804  10360   8265   -750   -919    508       C  
ATOM   1301  N   PRO B   8      46.997  46.149 350.241  1.00 50.13           N  
ANISOU 1301  N   PRO B   8     4112   8194   6743  -1421   -968    680       N  
ATOM   1302  CA  PRO B   8      47.434  45.313 351.369  1.00 51.04           C  
ANISOU 1302  CA  PRO B   8     4116   8386   6889  -1249  -1081    759       C  
ATOM   1303  C   PRO B   8      46.249  44.966 352.282  1.00 53.84           C  
ANISOU 1303  C   PRO B   8     4737   8385   7335  -1154  -1105    822       C  
ATOM   1304  O   PRO B   8      45.097  45.150 351.880  1.00 51.82           O  
ANISOU 1304  O   PRO B   8     4700   7835   7156  -1137  -1025    791       O  
ATOM   1305  CB  PRO B   8      48.480  46.206 352.052  1.00 54.43           C  
ANISOU 1305  CB  PRO B   8     4428   9137   7116  -1551  -1169    818       C  
ATOM   1306  CG  PRO B   8      48.039  47.632 351.755  1.00 57.88           C  
ANISOU 1306  CG  PRO B   8     5118   9423   7449  -1905  -1132    779       C  
ATOM   1307  CD  PRO B   8      47.050  47.578 350.605  1.00 51.54           C  
ANISOU 1307  CD  PRO B   8     4450   8370   6764  -1805   -995    706       C  
ATOM   1308  N   LYS B   9      46.522  44.440 353.487  1.00 50.96           N  
ANISOU 1308  N   LYS B   9     4324   8093   6946  -1092  -1217    936       N  
ATOM   1309  CA  LYS B   9      45.474  44.106 354.450  1.00 49.28           C  
ANISOU 1309  CA  LYS B   9     4310   7643   6773  -1021  -1247   1042       C  
ATOM   1310  C   LYS B   9      45.266  45.296 355.378  1.00 51.39           C  
ANISOU 1310  C   LYS B   9     4747   7961   6819  -1275  -1265   1041       C  
ATOM   1311  O   LYS B   9      44.135  45.575 355.780  1.00 49.26           O  
ANISOU 1311  O   LYS B   9     4705   7495   6516  -1274  -1224   1065       O  
ATOM   1312  CB  LYS B   9      45.834  42.835 355.237  1.00 53.44           C  
ANISOU 1312  CB  LYS B   9     4679   8217   7408   -777  -1373   1193       C  
ATOM   1313  N   PHE B  10      46.377  45.992 355.711  1.00 48.66           N  
ANISOU 1313  N   PHE B  10     4283   7900   6306  -1486  -1337   1009       N  
ATOM   1314  CA  PHE B  10      46.435  47.171 356.578  1.00 48.91           C  
ANISOU 1314  CA  PHE B  10     4483   7991   6109  -1755  -1401    967       C  
ATOM   1315  C   PHE B  10      47.426  48.185 356.029  1.00 55.13           C  
ANISOU 1315  C   PHE B  10     5204   8957   6785  -2070  -1441    888       C  
ATOM   1316  O   PHE B  10      48.390  47.787 355.368  1.00 56.55           O  
ANISOU 1316  O   PHE B  10     5081   9401   7005  -2061  -1453    925       O  
ATOM   1317  CB  PHE B  10      46.874  46.774 357.995  1.00 52.09           C  
ANISOU 1317  CB  PHE B  10     4781   8618   6392  -1719  -1534   1081       C  
ATOM   1318  CG  PHE B  10      45.976  45.837 358.761  1.00 52.62           C  
ANISOU 1318  CG  PHE B  10     4905   8565   6522  -1472  -1528   1217       C  
ATOM   1319  CD1 PHE B  10      46.126  44.459 358.650  1.00 55.52           C  
ANISOU 1319  CD1 PHE B  10     5071   8938   7087  -1210  -1563   1371       C  
ATOM   1320  CD2 PHE B  10      45.036  46.329 359.657  1.00 54.22           C  
ANISOU 1320  CD2 PHE B  10     5356   8675   6569  -1500  -1508   1206       C  
ATOM   1321  CE1 PHE B  10      45.325  43.592 359.393  1.00 56.14           C  
ANISOU 1321  CE1 PHE B  10     5195   8910   7227  -1037  -1591   1552       C  
ATOM   1322  CE2 PHE B  10      44.235  45.461 360.401  1.00 56.66           C  
ANISOU 1322  CE2 PHE B  10     5671   8952   6906  -1303  -1507   1382       C  
ATOM   1323  CZ  PHE B  10      44.385  44.099 360.264  1.00 54.90           C  
ANISOU 1323  CZ  PHE B  10     5244   8718   6897  -1101  -1556   1575       C  
ATOM   1324  N   GLN B  11      47.226  49.487 356.339  1.00 51.71           N  
ANISOU 1324  N   GLN B  11     5050   8395   6201  -2347  -1478    791       N  
ATOM   1325  CA  GLN B  11      48.130  50.575 355.940  1.00 53.00           C  
ANISOU 1325  CA  GLN B  11     5200   8686   6253  -2726  -1563    749       C  
ATOM   1326  C   GLN B  11      47.911  51.814 356.805  1.00 58.43           C  
ANISOU 1326  C   GLN B  11     6240   9208   6751  -2988  -1686    639       C  
ATOM   1327  O   GLN B  11      46.775  52.272 356.952  1.00 56.86           O  
ANISOU 1327  O   GLN B  11     6382   8673   6550  -2894  -1624    540       O  
ATOM   1328  CB  GLN B  11      47.964  50.940 354.449  1.00 53.00           C  
ANISOU 1328  CB  GLN B  11     5202   8568   6366  -2790  -1448    728       C  
ATOM   1329  CG  GLN B  11      49.016  51.916 353.914  1.00 64.15           C  
ANISOU 1329  CG  GLN B  11     6517  10184   7674  -3205  -1544    760       C  
ATOM   1330  CD  GLN B  11      50.323  51.240 353.583  1.00 79.71           C  
ANISOU 1330  CD  GLN B  11     8007  12664   9616  -3216  -1575    875       C  
ATOM   1331  OE1 GLN B  11      50.402  50.370 352.706  1.00 73.23           O  
ANISOU 1331  OE1 GLN B  11     6930  11991   8903  -2965  -1451    901       O  
ATOM   1332  NE2 GLN B  11      51.386  51.659 354.251  1.00 71.89           N  
ANISOU 1332  NE2 GLN B  11     6884  11972   8461  -3502  -1750    938       N  
ATOM   1333  N   VAL B  12      49.006  52.360 357.355  1.00 57.86           N  
ANISOU 1333  N   VAL B  12     6085   9389   6511  -3309  -1871    651       N  
ATOM   1334  CA  VAL B  12      49.007  53.597 358.136  1.00 59.71           C  
ANISOU 1334  CA  VAL B  12     6663   9475   6549  -3612  -2044    520       C  
ATOM   1335  C   VAL B  12      49.795  54.616 357.339  1.00 65.30           C  
ANISOU 1335  C   VAL B  12     7378  10197   7237  -4059  -2160    542       C  
ATOM   1336  O   VAL B  12      50.967  54.369 357.041  1.00 66.70           O  
ANISOU 1336  O   VAL B  12     7175  10776   7392  -4247  -2225    687       O  
ATOM   1337  CB  VAL B  12      49.571  53.406 359.560  1.00 65.83           C  
ANISOU 1337  CB  VAL B  12     7365  10529   7117  -3657  -2208    523       C  
ATOM   1338  N   LEU B  13      49.150  55.726 356.936  1.00 61.78           N  
ANISOU 1338  N   LEU B  13     7338   9332   6803  -4215  -2186    428       N  
ATOM   1339  CA  LEU B  13      49.805  56.767 356.132  1.00 63.87           C  
ANISOU 1339  CA  LEU B  13     7650   9552   7067  -4676  -2317    489       C  
ATOM   1340  C   LEU B  13      49.551  58.191 356.683  1.00 69.01           C  
ANISOU 1340  C   LEU B  13     8835   9783   7604  -4975  -2539    319       C  
ATOM   1341  O   LEU B  13      48.614  58.398 357.455  1.00 67.71           O  
ANISOU 1341  O   LEU B  13     9032   9318   7378  -4730  -2527    120       O  
ATOM   1342  CB  LEU B  13      49.355  56.671 354.648  1.00 61.83           C  
ANISOU 1342  CB  LEU B  13     7312   9185   6997  -4581  -2123    579       C  
ATOM   1343  CG  LEU B  13      47.854  56.799 354.349  1.00 63.91           C  
ANISOU 1343  CG  LEU B  13     7924   8979   7378  -4259  -1958    462       C  
ATOM   1344  CD1 LEU B  13      47.409  58.256 354.288  1.00 66.68           C  
ANISOU 1344  CD1 LEU B  13     8770   8862   7702  -4508  -2099    362       C  
ATOM   1345  CD2 LEU B  13      47.508  56.121 353.058  1.00 62.19           C  
ANISOU 1345  CD2 LEU B  13     7469   8831   7329  -4054  -1739    567       C  
ATOM   1346  N   LYS B  14      50.365  59.170 356.240  1.00 68.21           N  
ANISOU 1346  N   LYS B  14     8781   9664   7472  -5495  -2749    406       N  
ATOM   1347  CA  LYS B  14      50.224  60.578 356.621  1.00 71.35           C  
ANISOU 1347  CA  LYS B  14     9715   9606   7791  -5835  -3013    258       C  
ATOM   1348  C   LYS B  14      49.320  61.303 355.612  1.00 74.24           C  
ANISOU 1348  C   LYS B  14    10414   9473   8322  -5798  -2940    247       C  
ATOM   1349  O   LYS B  14      49.169  60.831 354.484  1.00 71.20           O  
ANISOU 1349  O   LYS B  14     9758   9213   8083  -5691  -2736    417       O  
ATOM   1350  CB  LYS B  14      51.597  61.264 356.725  1.00 78.42           C  
ANISOU 1350  CB  LYS B  14    10490  10736   8569  -6479  -3329    397       C  
ATOM   1351  N   THR B  15      48.723  62.444 356.016  1.00 73.21           N  
ANISOU 1351  N   THR B  15    10875   8786   8156  -5866  -3117     39       N  
ATOM   1352  CA  THR B  15      47.814  63.259 355.194  1.00 73.10           C  
ANISOU 1352  CA  THR B  15    11249   8237   8290  -5808  -3088     15       C  
ATOM   1353  C   THR B  15      48.515  63.764 353.905  1.00 79.32           C  
ANISOU 1353  C   THR B  15    11880   9066   9193  -6299  -3183    314       C  
ATOM   1354  O   THR B  15      49.713  64.050 353.926  1.00 82.65           O  
ANISOU 1354  O   THR B  15    12159   9708   9535  -6831  -3426    458       O  
ATOM   1355  CB  THR B  15      47.255  64.429 356.033  1.00 84.52           C  
ANISOU 1355  CB  THR B  15    13371   9097   9644  -5796  -3321   -290       C  
ATOM   1356  OG1 THR B  15      46.790  63.927 357.287  1.00 82.71           O  
ANISOU 1356  OG1 THR B  15    13210   8967   9249  -5378  -3237   -541       O  
ATOM   1357  CG2 THR B  15      46.114  65.176 355.339  1.00 83.29           C  
ANISOU 1357  CG2 THR B  15    13641   8366   9639  -5594  -3269   -345       C  
ATOM   1358  N   GLY B  16      47.754  63.835 352.809  1.00 73.80           N  
ANISOU 1358  N   GLY B  16    11178   8204   8657  -6121  -2991    424       N  
ATOM   1359  CA  GLY B  16      48.211  64.298 351.500  1.00 75.01           C  
ANISOU 1359  CA  GLY B  16    11181   8412   8909  -6520  -3039    725       C  
ATOM   1360  C   GLY B  16      49.216  63.401 350.800  1.00 78.36           C  
ANISOU 1360  C   GLY B  16    10926   9545   9303  -6670  -2910    990       C  
ATOM   1361  O   GLY B  16      49.986  63.879 349.961  1.00 80.75           O  
ANISOU 1361  O   GLY B  16    11041  10038   9603  -7142  -3027   1266       O  
ATOM   1362  N   GLN B  17      49.204  62.093 351.124  1.00 71.70           N  
ANISOU 1362  N   GLN B  17     9707   9106   8429  -6255  -2672    919       N  
ATOM   1363  CA  GLN B  17      50.112  61.082 350.572  1.00 70.51           C  
ANISOU 1363  CA  GLN B  17     8914   9635   8242  -6261  -2530   1112       C  
ATOM   1364  C   GLN B  17      49.359  60.105 349.639  1.00 69.88           C  
ANISOU 1364  C   GLN B  17     8608   9662   8282  -5796  -2197   1128       C  
ATOM   1365  O   GLN B  17      48.282  59.616 349.993  1.00 66.31           O  
ANISOU 1365  O   GLN B  17     8366   8920   7910  -5343  -2042    948       O  
ATOM   1366  CB  GLN B  17      50.784  60.319 351.729  1.00 71.86           C  
ANISOU 1366  CB  GLN B  17     8841  10171   8293  -6146  -2561   1023       C  
ATOM   1367  CG  GLN B  17      52.069  59.579 351.377  1.00 87.22           C  
ANISOU 1367  CG  GLN B  17    10148  12840  10152  -6287  -2533   1238       C  
ATOM   1368  CD  GLN B  17      52.326  58.413 352.310  1.00106.33           C  
ANISOU 1368  CD  GLN B  17    12302  15587  12511  -5948  -2466   1146       C  
ATOM   1369  OE1 GLN B  17      52.114  58.480 353.532  1.00 99.48           O  
ANISOU 1369  OE1 GLN B  17    11676  14554  11567  -5922  -2596    990       O  
ATOM   1370  NE2 GLN B  17      52.795  57.309 351.751  1.00100.98           N  
ANISOU 1370  NE2 GLN B  17    11122  15390  11856  -5668  -2272   1240       N  
ATOM   1371  N   SER B  18      49.947  59.827 348.454  1.00 66.13           N  
ANISOU 1371  N   SER B  18     7693   9639   7796  -5920  -2100   1346       N  
ATOM   1372  CA  SER B  18      49.419  58.910 347.440  1.00 62.24           C  
ANISOU 1372  CA  SER B  18     6952   9314   7384  -5529  -1814   1358       C  
ATOM   1373  C   SER B  18      49.438  57.466 347.943  1.00 64.01           C  
ANISOU 1373  C   SER B  18     6894   9806   7620  -5050  -1648   1221       C  
ATOM   1374  O   SER B  18      50.373  57.061 348.641  1.00 64.93           O  
ANISOU 1374  O   SER B  18     6745  10283   7641  -5106  -1727   1239       O  
ATOM   1375  CB  SER B  18      50.214  59.024 346.143  1.00 66.83           C  
ANISOU 1375  CB  SER B  18     7130  10369   7893  -5810  -1780   1617       C  
ATOM   1376  N   MET B  19      48.386  56.700 347.606  1.00 57.39           N  
ANISOU 1376  N   MET B  19     6126   8776   6903  -4592  -1440   1103       N  
ATOM   1377  CA  MET B  19      48.232  55.307 348.012  1.00 55.07           C  
ANISOU 1377  CA  MET B  19     5629   8637   6660  -4130  -1303    989       C  
ATOM   1378  C   MET B  19      47.328  54.583 347.029  1.00 57.95           C  
ANISOU 1378  C   MET B  19     5947   8931   7142  -3780  -1090    949       C  
ATOM   1379  O   MET B  19      46.167  54.965 346.847  1.00 56.66           O  
ANISOU 1379  O   MET B  19     6106   8362   7060  -3698  -1036    907       O  
ATOM   1380  CB  MET B  19      47.680  55.221 349.459  1.00 56.31           C  
ANISOU 1380  CB  MET B  19     6086   8479   6828  -3962  -1368    843       C  
ATOM   1381  CG  MET B  19      47.114  53.860 349.873  1.00 57.05           C  
ANISOU 1381  CG  MET B  19     6076   8588   7012  -3478  -1231    757       C  
ATOM   1382  SD  MET B  19      48.253  52.457 349.790  1.00 61.77           S  
ANISOU 1382  SD  MET B  19     6131   9738   7598  -3284  -1200    811       S  
ATOM   1383  CE  MET B  19      47.308  51.251 350.641  1.00 55.73           C  
ANISOU 1383  CE  MET B  19     5456   8753   6968  -2798  -1116    724       C  
ATOM   1384  N   THR B  20      47.862  53.525 346.409  1.00 54.61           N  
ANISOU 1384  N   THR B  20     5124   8909   6716  -3558   -981    952       N  
ATOM   1385  CA  THR B  20      47.112  52.681 345.486  1.00 52.18           C  
ANISOU 1385  CA  THR B  20     4753   8568   6504  -3217   -805    883       C  
ATOM   1386  C   THR B  20      46.938  51.327 346.157  1.00 53.97           C  
ANISOU 1386  C   THR B  20     4882   8797   6826  -2794   -763    766       C  
ATOM   1387  O   THR B  20      47.938  50.655 346.430  1.00 55.76           O  
ANISOU 1387  O   THR B  20     4781   9399   7007  -2687   -784    768       O  
ATOM   1388  CB  THR B  20      47.812  52.607 344.107  1.00 61.99           C  
ANISOU 1388  CB  THR B  20     5651  10259   7645  -3312   -729    968       C  
ATOM   1389  OG1 THR B  20      47.703  53.877 343.464  1.00 66.31           O  
ANISOU 1389  OG1 THR B  20     6327  10745   8120  -3738   -791   1125       O  
ATOM   1390  CG2 THR B  20      47.223  51.532 343.192  1.00 56.99           C  
ANISOU 1390  CG2 THR B  20     4944   9628   7081  -2947   -565    859       C  
ATOM   1391  N   LEU B  21      45.690  50.944 346.473  1.00 46.76           N  
ANISOU 1391  N   LEU B  21     4245   7479   6043  -2559   -720    691       N  
ATOM   1392  CA  LEU B  21      45.469  49.626 347.051  1.00 45.10           C  
ANISOU 1392  CA  LEU B  21     3962   7232   5942  -2191   -705    624       C  
ATOM   1393  C   LEU B  21      44.980  48.714 345.912  1.00 47.99           C  
ANISOU 1393  C   LEU B  21     4235   7593   6405  -1923   -593    551       C  
ATOM   1394  O   LEU B  21      44.041  49.059 345.197  1.00 46.18           O  
ANISOU 1394  O   LEU B  21     4179   7154   6211  -1946   -520    544       O  
ATOM   1395  CB  LEU B  21      44.586  49.600 348.328  1.00 43.61           C  
ANISOU 1395  CB  LEU B  21     4057   6704   5808  -2101   -750    621       C  
ATOM   1396  CG  LEU B  21      43.155  50.112 348.312  1.00 46.59           C  
ANISOU 1396  CG  LEU B  21     4770   6695   6236  -2076   -690    614       C  
ATOM   1397  CD1 LEU B  21      42.237  49.048 347.809  1.00 45.82           C  
ANISOU 1397  CD1 LEU B  21     4659   6466   6284  -1787   -607    597       C  
ATOM   1398  CD2 LEU B  21      42.689  50.459 349.702  1.00 48.08           C  
ANISOU 1398  CD2 LEU B  21     5187   6709   6373  -2071   -755    617       C  
ATOM   1399  N   GLN B  22      45.720  47.621 345.672  1.00 46.13           N  
ANISOU 1399  N   GLN B  22     3716   7620   6192  -1675   -594    490       N  
ATOM   1400  CA  GLN B  22      45.505  46.666 344.585  1.00 45.96           C  
ANISOU 1400  CA  GLN B  22     3586   7642   6235  -1392   -521    372       C  
ATOM   1401  C   GLN B  22      44.367  45.678 344.856  1.00 48.35           C  
ANISOU 1401  C   GLN B  22     4094   7543   6734  -1123   -541    318       C  
ATOM   1402  O   GLN B  22      44.004  45.456 346.016  1.00 47.68           O  
ANISOU 1402  O   GLN B  22     4143   7245   6730  -1092   -613    390       O  
ATOM   1403  CB  GLN B  22      46.802  45.878 344.309  1.00 49.92           C  
ANISOU 1403  CB  GLN B  22     3713   8585   6670  -1186   -535    306       C  
ATOM   1404  CG  GLN B  22      47.878  46.655 343.552  1.00 67.96           C  
ANISOU 1404  CG  GLN B  22     5707  11379   8734  -1420   -487    364       C  
ATOM   1405  CD  GLN B  22      47.491  47.038 342.137  1.00 95.80           C  
ANISOU 1405  CD  GLN B  22     9224  14997  12180  -1485   -372    325       C  
ATOM   1406  OE1 GLN B  22      46.720  46.347 341.446  1.00 90.60           O  
ANISOU 1406  OE1 GLN B  22     8650  14171  11601  -1225   -319    181       O  
ATOM   1407  NE2 GLN B  22      48.040  48.153 341.671  1.00 93.05           N  
ANISOU 1407  NE2 GLN B  22     8769  14926  11661  -1859   -352    470       N  
ATOM   1408  N   CYS B  23      43.821  45.077 343.764  1.00 43.71           N  
ANISOU 1408  N   CYS B  23     3519   6884   6206   -946   -489    204       N  
ATOM   1409  CA  CYS B  23      42.760  44.068 343.793  1.00 41.43           C  
ANISOU 1409  CA  CYS B  23     3406   6230   6103   -725   -534    159       C  
ATOM   1410  C   CYS B  23      42.919  43.069 342.650  1.00 46.14           C  
ANISOU 1410  C   CYS B  23     3897   6903   6732   -450   -535    -37       C  
ATOM   1411  O   CYS B  23      43.016  43.460 341.486  1.00 46.49           O  
ANISOU 1411  O   CYS B  23     3855   7163   6648   -499   -443   -122       O  
ATOM   1412  CB  CYS B  23      41.380  44.708 343.762  1.00 38.99           C  
ANISOU 1412  CB  CYS B  23     3362   5622   5829   -889   -488    249       C  
ATOM   1413  SG  CYS B  23      40.023  43.527 343.957  1.00 41.76           S  
ANISOU 1413  SG  CYS B  23     3906   5565   6396   -699   -571    268       S  
ATOM   1414  N   ALA B  24      42.891  41.778 342.991  1.00 42.61           N  
ANISOU 1414  N   ALA B  24     3478   6259   6453   -161   -656   -105       N  
ATOM   1415  CA  ALA B  24      43.008  40.677 342.045  1.00 43.82           C  
ANISOU 1415  CA  ALA B  24     3592   6394   6663    157   -706   -330       C  
ATOM   1416  C   ALA B  24      41.734  39.843 342.011  1.00 45.04           C  
ANISOU 1416  C   ALA B  24     4019   6071   7021    221   -816   -340       C  
ATOM   1417  O   ALA B  24      41.021  39.743 343.012  1.00 42.88           O  
ANISOU 1417  O   ALA B  24     3902   5507   6881    117   -889   -148       O  
ATOM   1418  CB  ALA B  24      44.190  39.800 342.416  1.00 47.49           C  
ANISOU 1418  CB  ALA B  24     3868   7010   7165    475   -797   -412       C  
ATOM   1419  N   GLN B  25      41.469  39.232 340.850  1.00 41.75           N  
ANISOU 1419  N   GLN B  25     3645   5611   6607    385   -837   -560       N  
ATOM   1420  CA  GLN B  25      40.325  38.370 340.573  1.00 40.80           C  
ANISOU 1420  CA  GLN B  25     3773   5065   6663    429   -971   -603       C  
ATOM   1421  C   GLN B  25      40.739  37.360 339.496  1.00 48.83           C  
ANISOU 1421  C   GLN B  25     4783   6095   7675    765  -1053   -941       C  
ATOM   1422  O   GLN B  25      41.163  37.767 338.407  1.00 49.32           O  
ANISOU 1422  O   GLN B  25     4700   6520   7520    810   -924  -1122       O  
ATOM   1423  CB  GLN B  25      39.122  39.233 340.145  1.00 38.95           C  
ANISOU 1423  CB  GLN B  25     3659   4775   6367    119   -873   -478       C  
ATOM   1424  CG  GLN B  25      37.924  38.466 339.612  1.00 41.11           C  
ANISOU 1424  CG  GLN B  25     4149   4697   6774    110  -1003   -514       C  
ATOM   1425  CD  GLN B  25      37.854  38.588 338.121  1.00 49.57           C  
ANISOU 1425  CD  GLN B  25     5195   5952   7688    139   -938   -743       C  
ATOM   1426  OE1 GLN B  25      38.362  37.745 337.380  1.00 46.80           O  
ANISOU 1426  OE1 GLN B  25     4835   5622   7323    405  -1021  -1032       O  
ATOM   1427  NE2 GLN B  25      37.287  39.679 337.653  1.00 37.48           N  
ANISOU 1427  NE2 GLN B  25     3643   4584   6012   -111   -789   -627       N  
ATOM   1428  N   ASP B  26      40.654  36.050 339.813  1.00 48.38           N  
ANISOU 1428  N   ASP B  26     4884   5653   7845   1010  -1279  -1023       N  
ATOM   1429  CA  ASP B  26      41.037  34.973 338.885  1.00 52.39           C  
ANISOU 1429  CA  ASP B  26     5446   6085   8373   1390  -1405  -1384       C  
ATOM   1430  C   ASP B  26      39.812  34.285 338.247  1.00 56.95           C  
ANISOU 1430  C   ASP B  26     6333   6212   9094   1328  -1586  -1474       C  
ATOM   1431  O   ASP B  26      39.965  33.539 337.277  1.00 60.41           O  
ANISOU 1431  O   ASP B  26     6867   6567   9519   1606  -1698  -1816       O  
ATOM   1432  CB  ASP B  26      41.940  33.924 339.580  1.00 57.56           C  
ANISOU 1432  CB  ASP B  26     6073   6610   9185   1770  -1571  -1451       C  
ATOM   1433  CG  ASP B  26      41.352  33.251 340.813  1.00 71.86           C  
ANISOU 1433  CG  ASP B  26     8088   7915  11301   1687  -1792  -1177       C  
ATOM   1434  OD1 ASP B  26      41.418  33.853 341.907  1.00 71.50           O  
ANISOU 1434  OD1 ASP B  26     7947   7963  11257   1462  -1720   -864       O  
ATOM   1435  OD2 ASP B  26      40.901  32.088 340.699  1.00 80.55           O  
ANISOU 1435  OD2 ASP B  26     9442   8535  12627   1853  -2052  -1277       O  
ATOM   1436  N   MET B  27      38.607  34.577 338.760  1.00 49.64           N  
ANISOU 1436  N   MET B  27     5549   5036   8276    964  -1614  -1176       N  
ATOM   1437  CA  MET B  27      37.333  33.982 338.352  1.00 49.38           C  
ANISOU 1437  CA  MET B  27     5781   4595   8386    814  -1800  -1161       C  
ATOM   1438  C   MET B  27      36.847  34.399 336.940  1.00 52.02           C  
ANISOU 1438  C   MET B  27     6126   5122   8517    726  -1706  -1364       C  
ATOM   1439  O   MET B  27      35.847  33.849 336.468  1.00 52.19           O  
ANISOU 1439  O   MET B  27     6357   4843   8631    602  -1876  -1386       O  
ATOM   1440  CB  MET B  27      36.262  34.322 339.396  1.00 49.04           C  
ANISOU 1440  CB  MET B  27     5804   4357   8472    461  -1823   -729       C  
ATOM   1441  CG  MET B  27      36.551  33.726 340.760  1.00 53.37           C  
ANISOU 1441  CG  MET B  27     6368   4689   9222    525  -1961   -506       C  
ATOM   1442  SD  MET B  27      35.758  34.635 342.101  1.00 54.23           S  
ANISOU 1442  SD  MET B  27     6416   4862   9326    165  -1852    -18       S  
ATOM   1443  CE  MET B  27      34.450  33.488 342.520  1.00 52.55           C  
ANISOU 1443  CE  MET B  27     6440   4144   9383    -13  -2168    229       C  
ATOM   1444  N   ASN B  28      37.561  35.332 336.266  1.00 47.45           N  
ANISOU 1444  N   ASN B  28     5313   5059   7656    770  -1456  -1491       N  
ATOM   1445  CA  ASN B  28      37.272  35.865 334.920  1.00 46.88           C  
ANISOU 1445  CA  ASN B  28     5191   5284   7338    692  -1333  -1655       C  
ATOM   1446  C   ASN B  28      35.938  36.689 334.886  1.00 46.20           C  
ANISOU 1446  C   ASN B  28     5174   5135   7244    283  -1271  -1359       C  
ATOM   1447  O   ASN B  28      35.284  36.783 333.836  1.00 46.19           O  
ANISOU 1447  O   ASN B  28     5231   5188   7131    187  -1281  -1457       O  
ATOM   1448  CB  ASN B  28      37.280  34.750 333.854  1.00 51.69           C  
ANISOU 1448  CB  ASN B  28     5953   5760   7928    973  -1515  -2072       C  
ATOM   1449  CG  ASN B  28      37.800  35.195 332.510  1.00 79.69           C  
ANISOU 1449  CG  ASN B  28     9326   9824  11128   1081  -1345  -2345       C  
ATOM   1450  OD1 ASN B  28      38.938  35.674 332.375  1.00 74.80           O  
ANISOU 1450  OD1 ASN B  28     8433   9686  10302   1248  -1159  -2423       O  
ATOM   1451  ND2 ASN B  28      36.985  35.020 331.477  1.00 72.95           N  
ANISOU 1451  ND2 ASN B  28     8609   8921  10186    978  -1416  -2481       N  
ATOM   1452  N   HIS B  29      35.592  37.337 336.026  1.00 38.23           N  
ANISOU 1452  N   HIS B  29     4140   4061   6327     67  -1201  -1003       N  
ATOM   1453  CA  HIS B  29      34.407  38.188 336.193  1.00 34.36           C  
ANISOU 1453  CA  HIS B  29     3689   3543   5825   -258  -1125   -700       C  
ATOM   1454  C   HIS B  29      34.541  39.505 335.438  1.00 34.45           C  
ANISOU 1454  C   HIS B  29     3548   3962   5579   -390   -887   -671       C  
ATOM   1455  O   HIS B  29      35.598  40.133 335.482  1.00 34.13           O  
ANISOU 1455  O   HIS B  29     3340   4222   5408   -335   -744   -709       O  
ATOM   1456  CB  HIS B  29      34.176  38.493 337.679  1.00 33.17           C  
ANISOU 1456  CB  HIS B  29     3549   3244   5812   -374  -1117   -374       C  
ATOM   1457  CG  HIS B  29      33.740  37.320 338.492  1.00 37.64           C  
ANISOU 1457  CG  HIS B  29     4264   3406   6632   -342  -1359   -275       C  
ATOM   1458  ND1 HIS B  29      33.771  37.360 339.870  1.00 38.21           N  
ANISOU 1458  ND1 HIS B  29     4323   3382   6812   -388  -1375    -12       N  
ATOM   1459  CD2 HIS B  29      33.255  36.119 338.097  1.00 41.79           C  
ANISOU 1459  CD2 HIS B  29     4960   3608   7310   -294  -1609   -389       C  
ATOM   1460  CE1 HIS B  29      33.309  36.189 340.269  1.00 39.48           C  
ANISOU 1460  CE1 HIS B  29     4624   3185   7191   -376  -1626     61       C  
ATOM   1461  NE2 HIS B  29      32.987  35.409 339.238  1.00 42.03           N  
ANISOU 1461  NE2 HIS B  29     5076   3329   7563   -329  -1787   -160       N  
ATOM   1462  N   GLU B  30      33.464  39.940 334.770  1.00 28.12           N  
ANISOU 1462  N   GLU B  30     2798   3178   4709   -585   -860   -569       N  
ATOM   1463  CA  GLU B  30      33.483  41.190 334.012  1.00 26.12           C  
ANISOU 1463  CA  GLU B  30     2423   3275   4227   -726   -663   -499       C  
ATOM   1464  C   GLU B  30      33.423  42.386 334.960  1.00 27.32           C  
ANISOU 1464  C   GLU B  30     2545   3450   4385   -886   -524   -198       C  
ATOM   1465  O   GLU B  30      34.278  43.273 334.884  1.00 27.45           O  
ANISOU 1465  O   GLU B  30     2439   3731   4259   -931   -383   -176       O  
ATOM   1466  CB  GLU B  30      32.332  41.230 332.987  1.00 27.48           C  
ANISOU 1466  CB  GLU B  30     2658   3461   4323   -861   -700   -481       C  
ATOM   1467  CG  GLU B  30      32.679  41.893 331.660  1.00 38.80           C  
ANISOU 1467  CG  GLU B  30     3954   5308   5480   -895   -565   -581       C  
ATOM   1468  CD  GLU B  30      33.924  41.417 330.925  1.00 66.23           C  
ANISOU 1468  CD  GLU B  30     7309   9062   8793   -666   -555   -931       C  
ATOM   1469  OE1 GLU B  30      33.903  40.292 330.373  1.00 50.56           O  
ANISOU 1469  OE1 GLU B  30     5418   6964   6827   -495   -714  -1220       O  
ATOM   1470  OE2 GLU B  30      34.909  42.189 330.869  1.00 67.65           O  
ANISOU 1470  OE2 GLU B  30     7300   9593   8813   -659   -398   -915       O  
ATOM   1471  N   TYR B  31      32.451  42.366 335.891  1.00 21.25           N  
ANISOU 1471  N   TYR B  31     1958   2414   3703   -867   -550     53       N  
ATOM   1472  CA  TYR B  31      32.163  43.416 336.864  1.00 19.37           C  
ANISOU 1472  CA  TYR B  31     1879   2186   3294   -728   -431    325       C  
ATOM   1473  C   TYR B  31      33.066  43.366 338.083  1.00 22.13           C  
ANISOU 1473  C   TYR B  31     2026   2467   3916   -950   -468    307       C  
ATOM   1474  O   TYR B  31      33.285  42.293 338.644  1.00 22.50           O  
ANISOU 1474  O   TYR B  31     2064   2344   4139   -885   -606    247       O  
ATOM   1475  CB  TYR B  31      30.698  43.314 337.307  1.00 19.21           C  
ANISOU 1475  CB  TYR B  31     1948   2067   3282   -686   -517    539       C  
ATOM   1476  CG  TYR B  31      29.722  43.866 336.297  1.00 19.57           C  
ANISOU 1476  CG  TYR B  31     2023   2225   3186   -749   -491    609       C  
ATOM   1477  CD1 TYR B  31      29.563  43.267 335.050  1.00 22.13           C  
ANISOU 1477  CD1 TYR B  31     2267   2550   3590   -965   -526    481       C  
ATOM   1478  CD2 TYR B  31      28.931  44.969 336.596  1.00 19.27           C  
ANISOU 1478  CD2 TYR B  31     1998   2276   3048   -735   -465    770       C  
ATOM   1479  CE1 TYR B  31      28.676  43.783 334.105  1.00 23.19           C  
ANISOU 1479  CE1 TYR B  31     2309   2791   3713  -1233   -505    568       C  
ATOM   1480  CE2 TYR B  31      28.021  45.479 335.670  1.00 20.37           C  
ANISOU 1480  CE2 TYR B  31     2110   2502   3129   -866   -448    861       C  
ATOM   1481  CZ  TYR B  31      27.897  44.884 334.423  1.00 25.90           C  
ANISOU 1481  CZ  TYR B  31     2555   3149   4138  -1485   -395    842       C  
ATOM   1482  OH  TYR B  31      27.000  45.375 333.505  1.00 24.85           O  
ANISOU 1482  OH  TYR B  31     2446   3172   3823  -1467   -387    951       O  
ATOM   1483  N   MET B  39      33.580  44.542 338.491  1.00 19.84           N  
ANISOU 1483  N   MET B  39     1843   2319   3378   -818   -340    392       N  
ATOM   1484  CA  MET B  39      34.440  44.743 339.667  1.00 20.48           C  
ANISOU 1484  CA  MET B  39     1882   2397   3502   -823   -339    415       C  
ATOM   1485  C   MET B  39      34.087  46.080 340.335  1.00 24.11           C  
ANISOU 1485  C   MET B  39     2284   2832   4044  -1169   -254    591       C  
ATOM   1486  O   MET B  39      33.779  47.041 339.627  1.00 24.07           O  
ANISOU 1486  O   MET B  39     2347   2910   3887  -1204   -184    633       O  
ATOM   1487  CB  MET B  39      35.933  44.674 339.308  1.00 22.99           C  
ANISOU 1487  CB  MET B  39     1883   2957   3896  -1000   -324    232       C  
ATOM   1488  CG  MET B  39      36.438  43.259 339.169  1.00 28.62           C  
ANISOU 1488  CG  MET B  39     2531   3646   4697   -778   -439     34       C  
ATOM   1489  SD  MET B  39      38.176  43.117 338.712  1.00 35.55           S  
ANISOU 1489  SD  MET B  39     3165   4894   5449   -645   -405   -163       S  
ATOM   1490  CE  MET B  39      38.924  42.975 340.328  1.00 32.20           C  
ANISOU 1490  CE  MET B  39     2727   4378   5129   -607   -471    -49       C  
ATOM   1491  N   SER B  40      34.090  46.124 341.693  1.00 21.82           N  
ANISOU 1491  N   SER B  40     2128   2477   3685   -964   -306    663       N  
ATOM   1492  CA  SER B  40      33.701  47.294 342.484  1.00 21.31           C  
ANISOU 1492  CA  SER B  40     2176   2401   3519   -981   -268    763       C  
ATOM   1493  C   SER B  40      34.557  47.523 343.718  1.00 25.84           C  
ANISOU 1493  C   SER B  40     2682   2919   4217  -1225   -244    804       C  
ATOM   1494  O   SER B  40      35.206  46.607 344.221  1.00 25.78           O  
ANISOU 1494  O   SER B  40     2578   2943   4274  -1149   -321    755       O  
ATOM   1495  CB  SER B  40      32.259  47.151 342.945  1.00 23.23           C  
ANISOU 1495  CB  SER B  40     2447   2496   3884  -1047   -245    944       C  
ATOM   1496  OG  SER B  40      31.398  46.898 341.852  1.00 35.32           O  
ANISOU 1496  OG  SER B  40     3947   3973   5500  -1187   -197   1015       O  
ATOM   1497  N   TRP B  41      34.494  48.759 344.231  1.00 23.75           N  
ANISOU 1497  N   TRP B  41     2555   2629   3839  -1285   -203    846       N  
ATOM   1498  CA  TRP B  41      35.178  49.220 345.424  1.00 24.63           C  
ANISOU 1498  CA  TRP B  41     2716   2747   3896  -1337   -235    833       C  
ATOM   1499  C   TRP B  41      34.191  49.841 346.382  1.00 29.23           C  
ANISOU 1499  C   TRP B  41     3477   3213   4415  -1257   -207    919       C  
ATOM   1500  O   TRP B  41      33.540  50.834 346.051  1.00 29.81           O  
ANISOU 1500  O   TRP B  41     3700   3192   4435  -1265   -150    952       O  
ATOM   1501  CB  TRP B  41      36.278  50.226 345.070  1.00 24.95           C  
ANISOU 1501  CB  TRP B  41     2766   2869   3843  -1536   -241    766       C  
ATOM   1502  CG  TRP B  41      37.574  49.572 344.710  1.00 27.30           C  
ANISOU 1502  CG  TRP B  41     2835   3389   4149  -1582   -282    683       C  
ATOM   1503  CD1 TRP B  41      38.148  49.513 343.476  1.00 31.04           C  
ANISOU 1503  CD1 TRP B  41     3158   4041   4594  -1661   -251    637       C  
ATOM   1504  CD2 TRP B  41      38.436  48.844 345.591  1.00 27.99           C  
ANISOU 1504  CD2 TRP B  41     2791   3589   4255  -1514   -356    644       C  
ATOM   1505  NE1 TRP B  41      39.315  48.787 343.530  1.00 31.52           N  
ANISOU 1505  NE1 TRP B  41     2995   4333   4649  -1618   -293    557       N  
ATOM   1506  CE2 TRP B  41      39.517  48.366 344.817  1.00 32.79           C  
ANISOU 1506  CE2 TRP B  41     3167   4440   4851  -1528   -363    565       C  
ATOM   1507  CE3 TRP B  41      38.392  48.533 346.960  1.00 29.28           C  
ANISOU 1507  CE3 TRP B  41     2994   3705   4427  -1429   -416    681       C  
ATOM   1508  CZ2 TRP B  41      40.542  47.601 345.363  1.00 33.12           C  
ANISOU 1508  CZ2 TRP B  41     3022   4655   4907  -1437   -433    520       C  
ATOM   1509  CZ3 TRP B  41      39.396  47.751 347.496  1.00 31.67           C  
ANISOU 1509  CZ3 TRP B  41     3118   4164   4752  -1368   -494    654       C  
ATOM   1510  CH2 TRP B  41      40.447  47.277 346.697  1.00 33.24           C  
ANISOU 1510  CH2 TRP B  41     3092   4578   4958  -1359   -503    573       C  
ATOM   1511  N   TYR B  42      34.065  49.242 347.560  1.00 25.53           N  
ANISOU 1511  N   TYR B  42     2986   2774   3940  -1156   -249    964       N  
ATOM   1512  CA  TYR B  42      33.193  49.715 348.623  1.00 25.84           C  
ANISOU 1512  CA  TYR B  42     3156   2789   3874  -1041   -218   1038       C  
ATOM   1513  C   TYR B  42      34.021  50.139 349.817  1.00 32.44           C  
ANISOU 1513  C   TYR B  42     4058   3680   4588  -1069   -277    959       C  
ATOM   1514  O   TYR B  42      35.097  49.590 350.033  1.00 32.96           O  
ANISOU 1514  O   TYR B  42     4000   3837   4687  -1146   -353    915       O  
ATOM   1515  CB  TYR B  42      32.222  48.600 349.055  1.00 26.65           C  
ANISOU 1515  CB  TYR B  42     3146   2943   4035   -911   -224   1209       C  
ATOM   1516  CG  TYR B  42      31.244  48.152 347.994  1.00 27.36           C  
ANISOU 1516  CG  TYR B  42     3182   2988   4227   -899   -192   1305       C  
ATOM   1517  CD1 TYR B  42      29.999  48.756 347.869  1.00 29.20           C  
ANISOU 1517  CD1 TYR B  42     3482   3226   4388   -814   -106   1412       C  
ATOM   1518  CD2 TYR B  42      31.535  47.076 347.159  1.00 27.80           C  
ANISOU 1518  CD2 TYR B  42     3114   3011   4439   -953   -261   1286       C  
ATOM   1519  CE1 TYR B  42      29.086  48.335 346.903  1.00 30.61           C  
ANISOU 1519  CE1 TYR B  42     3589   3396   4646   -826    -92   1519       C  
ATOM   1520  CE2 TYR B  42      30.632  46.648 346.186  1.00 28.17           C  
ANISOU 1520  CE2 TYR B  42     3124   3017   4563   -964   -258   1358       C  
ATOM   1521  CZ  TYR B  42      29.408  47.283 346.059  1.00 36.41           C  
ANISOU 1521  CZ  TYR B  42     4217   4086   5531   -922   -175   1488       C  
ATOM   1522  OH  TYR B  42      28.514  46.874 345.097  1.00 37.85           O  
ANISOU 1522  OH  TYR B  42     4345   4260   5775   -956   -185   1576       O  
ATOM   1523  N   ARG B  43      33.518  51.078 350.616  1.00 30.76           N  
ANISOU 1523  N   ARG B  43     4037   3430   4221   -986   -248    934       N  
ATOM   1524  CA  ARG B  43      34.171  51.476 351.861  1.00 32.42           C  
ANISOU 1524  CA  ARG B  43     4336   3702   4278   -999   -317    843       C  
ATOM   1525  C   ARG B  43      33.144  51.299 352.980  1.00 39.36           C  
ANISOU 1525  C   ARG B  43     5238   4699   5018   -773   -270    930       C  
ATOM   1526  O   ARG B  43      31.961  51.552 352.743  1.00 38.89           O  
ANISOU 1526  O   ARG B  43     5238   4614   4926   -616   -177    998       O  
ATOM   1527  CB  ARG B  43      34.774  52.892 351.792  1.00 32.21           C  
ANISOU 1527  CB  ARG B  43     4556   3522   4159  -1141   -368    676       C  
ATOM   1528  CG  ARG B  43      33.789  54.058 351.718  1.00 33.39           C  
ANISOU 1528  CG  ARG B  43     4980   3478   4227  -1013   -313    629       C  
ATOM   1529  CD  ARG B  43      34.502  55.386 351.862  1.00 35.31           C  
ANISOU 1529  CD  ARG B  43     5508   3520   4388  -1176   -424    462       C  
ATOM   1530  NE  ARG B  43      35.065  55.600 353.201  1.00 38.20           N  
ANISOU 1530  NE  ARG B  43     5980   3954   4580  -1179   -523    331       N  
ATOM   1531  CZ  ARG B  43      35.426  56.790 353.677  1.00 55.51           C  
ANISOU 1531  CZ  ARG B  43     8481   5955   6657  -1283   -651    155       C  
ATOM   1532  NH1 ARG B  43      35.277  57.883 352.937  1.00 49.37           N  
ANISOU 1532  NH1 ARG B  43     7944   4877   5938  -1395   -701    115       N  
ATOM   1533  NH2 ARG B  43      35.920  56.900 354.902  1.00 40.31           N  
ANISOU 1533  NH2 ARG B  43     6638   4126   4553  -1286   -749     26       N  
ATOM   1534  N   GLN B  44      33.559  50.786 354.153  1.00 39.05           N  
ANISOU 1534  N   GLN B  44     5111   4839   4889   -751   -333    961       N  
ATOM   1535  CA  GLN B  44      32.607  50.531 355.237  1.00 41.58           C  
ANISOU 1535  CA  GLN B  44     5399   5356   5044   -549   -288   1081       C  
ATOM   1536  C   GLN B  44      32.986  51.240 356.539  1.00 52.82           C  
ANISOU 1536  C   GLN B  44     6974   6891   6205   -499   -335    930       C  
ATOM   1537  O   GLN B  44      34.033  50.975 357.141  1.00 53.28           O  
ANISOU 1537  O   GLN B  44     6983   7028   6232   -630   -444    879       O  
ATOM   1538  CB  GLN B  44      32.433  49.025 355.485  1.00 42.14           C  
ANISOU 1538  CB  GLN B  44     5200   5585   5228   -548   -327   1329       C  
ATOM   1539  CG  GLN B  44      31.074  48.659 356.077  1.00 51.90           C  
ANISOU 1539  CG  GLN B  44     6342   7020   6358   -373   -253   1558       C  
ATOM   1540  CD  GLN B  44      30.931  47.181 356.356  1.00 71.01           C  
ANISOU 1540  CD  GLN B  44     8518   9553   8908   -424   -334   1842       C  
ATOM   1541  OE1 GLN B  44      31.344  46.323 355.568  1.00 63.47           O  
ANISOU 1541  OE1 GLN B  44     7477   8431   8208   -540   -410   1890       O  
ATOM   1542  NE2 GLN B  44      30.303  46.847 357.472  1.00 68.11           N  
ANISOU 1542  NE2 GLN B  44     8043   9475   8363   -331   -330   2045       N  
ATOM   1543  N   ASP B  45      32.088  52.127 356.977  1.00 54.30           N  
ANISOU 1543  N   ASP B  45     7343   7100   6187   -285   -257    853       N  
ATOM   1544  CA  ASP B  45      32.211  52.903 358.205  1.00 58.12           C  
ANISOU 1544  CA  ASP B  45     8020   7688   6375   -169   -294    668       C  
ATOM   1545  C   ASP B  45      31.044  52.585 359.148  1.00 65.95           C  
ANISOU 1545  C   ASP B  45     8903   9021   7132    128   -187    811       C  
ATOM   1546  O   ASP B  45      29.943  52.300 358.654  1.00 64.97           O  
ANISOU 1546  O   ASP B  45     8662   8956   7068    264    -72    994       O  
ATOM   1547  CB  ASP B  45      32.247  54.403 357.872  1.00 61.50           C  
ANISOU 1547  CB  ASP B  45     8820   7803   6745   -146   -318    392       C  
ATOM   1548  CG  ASP B  45      33.498  54.870 357.156  1.00 71.38           C  
ANISOU 1548  CG  ASP B  45    10184   8781   8157   -478   -450    264       C  
ATOM   1549  OD1 ASP B  45      34.500  54.126 357.171  1.00 70.90           O  
ANISOU 1549  OD1 ASP B  45     9921   8828   8191   -701   -528    333       O  
ATOM   1550  OD2 ASP B  45      33.469  55.971 356.574  1.00 79.11           O  
ANISOU 1550  OD2 ASP B  45    11439   9456   9163   -513   -481    119       O  
ATOM   1551  N   PRO B  46      31.235  52.630 360.496  1.00 66.15           N  
ANISOU 1551  N   PRO B  46     8939   9325   6869    223   -225    751       N  
ATOM   1552  CA  PRO B  46      30.111  52.321 361.401  1.00 68.17           C  
ANISOU 1552  CA  PRO B  46     9044   9994   6864    507   -113    921       C  
ATOM   1553  C   PRO B  46      28.933  53.295 361.221  1.00 74.37           C  
ANISOU 1553  C   PRO B  46    10002  10767   7488    842     26    807       C  
ATOM   1554  O   PRO B  46      29.092  54.513 361.364  1.00 76.16           O  
ANISOU 1554  O   PRO B  46    10569  10809   7559    978     -2    473       O  
ATOM   1555  CB  PRO B  46      30.739  52.415 362.800  1.00 72.26           C  
ANISOU 1555  CB  PRO B  46     9589  10789   7076    526   -198    811       C  
ATOM   1556  CG  PRO B  46      32.208  52.269 362.576  1.00 75.19           C  
ANISOU 1556  CG  PRO B  46    10002  10936   7631    192   -366    710       C  
ATOM   1557  CD  PRO B  46      32.463  52.932 361.263  1.00 68.98           C  
ANISOU 1557  CD  PRO B  46     9413   9694   7103     67   -375    553       C  
ATOM   1558  N   GLY B  47      27.779  52.737 360.845  1.00 70.01           N  
ANISOU 1558  N   GLY B  47     9219  10391   6993    963    152   1093       N  
ATOM   1559  CA  GLY B  47      26.545  53.482 360.625  1.00 71.18           C  
ANISOU 1559  CA  GLY B  47     9442  10606   6997   1309    298   1062       C  
ATOM   1560  C   GLY B  47      26.043  53.453 359.194  1.00 72.39           C  
ANISOU 1560  C   GLY B  47     9565  10491   7447   1239    346   1182       C  
ATOM   1561  O   GLY B  47      24.961  52.918 358.924  1.00 72.14           O  
ANISOU 1561  O   GLY B  47     9281  10711   7418   1341    450   1471       O  
ATOM   1562  N   MET B  48      26.833  54.033 358.267  1.00 66.12           N  
ANISOU 1562  N   MET B  48     9013   9221   6889   1043    262    980       N  
ATOM   1563  CA  MET B  48      26.507  54.143 356.840  1.00 62.94           C  
ANISOU 1563  CA  MET B  48     8617   8546   6753    956    292   1057       C  
ATOM   1564  C   MET B  48      26.557  52.791 356.074  1.00 60.76           C  
ANISOU 1564  C   MET B  48     8026   8309   6750    674    269   1351       C  
ATOM   1565  O   MET B  48      25.929  52.682 355.016  1.00 59.44           O  
ANISOU 1565  O   MET B  48     7783   8062   6741    652    317   1484       O  
ATOM   1566  CB  MET B  48      27.435  55.163 356.161  1.00 65.04           C  
ANISOU 1566  CB  MET B  48     9222   8337   7154    800    192    777       C  
ATOM   1567  N   GLY B  49      27.281  51.798 356.600  1.00 53.41           N  
ANISOU 1567  N   GLY B  49     6935   7491   5869    478    180   1440       N  
ATOM   1568  CA  GLY B  49      27.415  50.485 355.970  1.00 49.67           C  
ANISOU 1568  CA  GLY B  49     6212   7006   5656    238    119   1681       C  
ATOM   1569  C   GLY B  49      28.274  50.505 354.717  1.00 47.72           C  
ANISOU 1569  C   GLY B  49     6046   6403   5683      3     51   1553       C  
ATOM   1570  O   GLY B  49      29.276  51.230 354.668  1.00 48.13           O  
ANISOU 1570  O   GLY B  49     6293   6263   5732    -82     -2   1308       O  
ATOM   1571  N   LEU B  50      27.886  49.719 353.686  1.00 38.35           N  
ANISOU 1571  N   LEU B  50     4705   5151   4715   -113     42   1721       N  
ATOM   1572  CA  LEU B  50      28.630  49.640 352.423  1.00 34.52           C  
ANISOU 1572  CA  LEU B  50     4259   4398   4460   -311    -10   1610       C  
ATOM   1573  C   LEU B  50      28.217  50.744 351.443  1.00 36.44           C  
ANISOU 1573  C   LEU B  50     4666   4475   4704   -264     68   1509       C  
ATOM   1574  O   LEU B  50      27.050  50.834 351.041  1.00 36.19           O  
ANISOU 1574  O   LEU B  50     4584   4516   4653   -147    146   1651       O  
ATOM   1575  CB  LEU B  50      28.478  48.261 351.756  1.00 32.99           C  
ANISOU 1575  CB  LEU B  50     3857   4192   4484   -446    -82   1794       C  
ATOM   1576  CG  LEU B  50      29.260  47.098 352.370  1.00 36.97           C  
ANISOU 1576  CG  LEU B  50     4232   4735   5080   -540   -210   1864       C  
ATOM   1577  CD1 LEU B  50      28.913  45.804 351.689  1.00 35.95           C  
ANISOU 1577  CD1 LEU B  50     3951   4544   5162   -638   -304   2051       C  
ATOM   1578  CD2 LEU B  50      30.762  47.324 352.276  1.00 39.71           C  
ANISOU 1578  CD2 LEU B  50     4645   4957   5488   -642   -274   1633       C  
ATOM   1579  N   ARG B  51      29.191  51.584 351.061  1.00 31.51           N  
ANISOU 1579  N   ARG B  51     4226   3645   4101   -373     32   1292       N  
ATOM   1580  CA  ARG B  51      28.985  52.688 350.124  1.00 30.50           C  
ANISOU 1580  CA  ARG B  51     4277   3321   3990   -372     72   1211       C  
ATOM   1581  C   ARG B  51      29.846  52.468 348.887  1.00 29.70           C  
ANISOU 1581  C   ARG B  51     4122   3098   4063   -624     21   1166       C  
ATOM   1582  O   ARG B  51      31.054  52.266 349.030  1.00 29.18           O  
ANISOU 1582  O   ARG B  51     4034   3022   4031   -789    -57   1062       O  
ATOM   1583  CB  ARG B  51      29.305  54.033 350.792  1.00 33.15           C  
ANISOU 1583  CB  ARG B  51     4912   3515   4169   -289     50   1015       C  
ATOM   1584  CG  ARG B  51      28.298  54.448 351.864  1.00 45.12           C  
ANISOU 1584  CG  ARG B  51     6512   5165   5469     42    124   1021       C  
ATOM   1585  CD  ARG B  51      28.435  55.912 352.221  1.00 56.26           C  
ANISOU 1585  CD  ARG B  51     8286   6344   6747    162     86    793       C  
ATOM   1586  NE  ARG B  51      29.611  56.161 353.055  1.00 64.62           N  
ANISOU 1586  NE  ARG B  51     9481   7345   7725     17    -36    597       N  
ATOM   1587  CZ  ARG B  51      29.954  57.350 353.539  1.00 81.03           C  
ANISOU 1587  CZ  ARG B  51    11906   9198   9685     57   -126    365       C  
ATOM   1588  NH1 ARG B  51      29.216  58.423 353.271  1.00 71.61           N  
ANISOU 1588  NH1 ARG B  51    10980   7777   8450    273   -107    292       N  
ATOM   1589  NH2 ARG B  51      31.034  57.478 354.295  1.00 67.64           N  
ANISOU 1589  NH2 ARG B  51    10303   7488   7910   -117   -255    206       N  
ATOM   1590  N   LEU B  52      29.226  52.459 347.676  1.00 23.48           N  
ANISOU 1590  N   LEU B  52     3158   2440   3323   -531     -3   1050       N  
ATOM   1591  CA  LEU B  52      29.957  52.218 346.423  1.00 21.14           C  
ANISOU 1591  CA  LEU B  52     2724   2243   3066   -587   -112    882       C  
ATOM   1592  C   LEU B  52      30.821  53.422 346.038  1.00 22.41           C  
ANISOU 1592  C   LEU B  52     3134   2169   3212   -812    -91    894       C  
ATOM   1593  O   LEU B  52      30.300  54.522 345.884  1.00 22.73           O  
ANISOU 1593  O   LEU B  52     3366   2056   3215   -784    -50    918       O  
ATOM   1594  CB  LEU B  52      29.001  51.854 345.269  1.00 20.19           C  
ANISOU 1594  CB  LEU B  52     2448   2227   2999   -496   -116    910       C  
ATOM   1595  CG  LEU B  52      29.645  51.566 343.903  1.00 22.55           C  
ANISOU 1595  CG  LEU B  52     2736   2475   3355   -667   -131    956       C  
ATOM   1596  CD1 LEU B  52      30.397  50.247 343.901  1.00 22.09           C  
ANISOU 1596  CD1 LEU B  52     2555   2496   3340   -662   -215    915       C  
ATOM   1597  CD2 LEU B  52      28.615  51.559 342.811  1.00 22.74           C  
ANISOU 1597  CD2 LEU B  52     2694   2541   3407   -629   -110   1034       C  
ATOM   1598  N   ILE B  53      32.132  53.207 345.877  1.00 18.20           N  
ANISOU 1598  N   ILE B  53     2498   1825   2591   -824   -222    714       N  
ATOM   1599  CA  ILE B  53      33.048  54.279 345.479  1.00 18.68           C  
ANISOU 1599  CA  ILE B  53     2708   1792   2596  -1026   -262    693       C  
ATOM   1600  C   ILE B  53      33.052  54.371 343.947  1.00 22.46           C  
ANISOU 1600  C   ILE B  53     3157   2159   3217  -1284   -189    856       C  
ATOM   1601  O   ILE B  53      32.690  55.403 343.379  1.00 21.92           O  
ANISOU 1601  O   ILE B  53     3222   1986   3121  -1312   -193    894       O  
ATOM   1602  CB  ILE B  53      34.489  54.095 346.045  1.00 20.59           C  
ANISOU 1602  CB  ILE B  53     2943   2029   2853  -1262   -309    694       C  
ATOM   1603  CG1 ILE B  53      34.509  53.918 347.566  1.00 20.81           C  
ANISOU 1603  CG1 ILE B  53     3045   2006   2855  -1224   -323    664       C  
ATOM   1604  CG2 ILE B  53      35.370  55.242 345.631  1.00 21.48           C  
ANISOU 1604  CG2 ILE B  53     3178   2066   2918  -1534   -376    700       C  
ATOM   1605  CD1 ILE B  53      35.687  53.069 348.065  1.00 23.95           C  
ANISOU 1605  CD1 ILE B  53     3293   2379   3430  -1548   -321    734       C  
ATOM   1606  N   HIS B  54      33.502  53.288 343.297  1.00 20.50           N  
ANISOU 1606  N   HIS B  54     2690   2137   2961  -1224   -212    810       N  
ATOM   1607  CA  HIS B  54      33.627  53.163 341.852  1.00 21.20           C  
ANISOU 1607  CA  HIS B  54     2679   2310   3067  -1331   -185    859       C  
ATOM   1608  C   HIS B  54      33.437  51.726 341.416  1.00 24.67           C  
ANISOU 1608  C   HIS B  54     2930   2797   3645  -1350   -122    887       C  
ATOM   1609  O   HIS B  54      33.711  50.808 342.190  1.00 23.85           O  
ANISOU 1609  O   HIS B  54     2758   2714   3591  -1269   -150    836       O  
ATOM   1610  CB  HIS B  54      35.001  53.638 341.393  1.00 23.10           C  
ANISOU 1610  CB  HIS B  54     2872   2604   3300  -1676   -189    897       C  
ATOM   1611  CG  HIS B  54      35.195  55.116 341.423  1.00 27.46           C  
ANISOU 1611  CG  HIS B  54     3615   2898   3922  -2060   -182   1045       C  
ATOM   1612  ND1 HIS B  54      35.898  55.725 342.443  1.00 30.31           N  
ANISOU 1612  ND1 HIS B  54     4112   3102   4303  -2264   -250   1030       N  
ATOM   1613  CD2 HIS B  54      34.829  56.054 340.520  1.00 29.89           C  
ANISOU 1613  CD2 HIS B  54     4027   3061   4268  -2255   -151   1212       C  
ATOM   1614  CE1 HIS B  54      35.915  57.015 342.149  1.00 31.65           C  
ANISOU 1614  CE1 HIS B  54     4499   3077   4450  -2437   -317   1117       C  
ATOM   1615  NE2 HIS B  54      35.287  57.262 341.000  1.00 31.83           N  
ANISOU 1615  NE2 HIS B  54     4508   3096   4489  -2432   -259   1242       N  
ATOM   1616  N   TYR B  55      33.001  51.535 340.161  1.00 22.79           N  
ANISOU 1616  N   TYR B  55     2645   2684   3332  -1231   -139    866       N  
ATOM   1617  CA  TYR B  55      32.757  50.222 339.586  1.00 22.43           C  
ANISOU 1617  CA  TYR B  55     2488   2717   3318  -1113   -154    813       C  
ATOM   1618  C   TYR B  55      33.207  50.156 338.133  1.00 25.17           C  
ANISOU 1618  C   TYR B  55     2709   3204   3651  -1320    -91    811       C  
ATOM   1619  O   TYR B  55      33.139  51.144 337.401  1.00 25.53           O  
ANISOU 1619  O   TYR B  55     2785   3310   3605  -1431    -73    884       O  
ATOM   1620  CB  TYR B  55      31.268  49.835 339.705  1.00 23.19           C  
ANISOU 1620  CB  TYR B  55     2587   2719   3505  -1035   -148    913       C  
ATOM   1621  CG  TYR B  55      30.337  50.644 338.825  1.00 25.42           C  
ANISOU 1621  CG  TYR B  55     2891   2964   3804  -1181    -66   1073       C  
ATOM   1622  CD1 TYR B  55      29.757  51.823 339.288  1.00 27.21           C  
ANISOU 1622  CD1 TYR B  55     3249   3035   4056  -1247     15   1232       C  
ATOM   1623  CD2 TYR B  55      30.008  50.214 337.539  1.00 26.20           C  
ANISOU 1623  CD2 TYR B  55     2901   3156   3896  -1266    -52   1098       C  
ATOM   1624  CE1 TYR B  55      28.887  52.565 338.488  1.00 28.33           C  
ANISOU 1624  CE1 TYR B  55     3434   3144   4184  -1300     77   1402       C  
ATOM   1625  CE2 TYR B  55      29.157  50.960 336.723  1.00 27.28           C  
ANISOU 1625  CE2 TYR B  55     3053   3311   4003  -1341     -2   1252       C  
ATOM   1626  CZ  TYR B  55      28.584  52.125 337.208  1.00 34.33           C  
ANISOU 1626  CZ  TYR B  55     4080   3995   4968  -1480    136   1514       C  
ATOM   1627  OH  TYR B  55      27.749  52.870 336.409  1.00 35.91           O  
ANISOU 1627  OH  TYR B  55     4310   4217   5115  -1484    168   1680       O  
ATOM   1628  N   SER B  56      33.618  48.966 337.718  1.00 22.09           N  
ANISOU 1628  N   SER B  56     2306   2926   3160  -1063   -156    647       N  
ATOM   1629  CA  SER B  56      34.049  48.684 336.365  1.00 22.44           C  
ANISOU 1629  CA  SER B  56     2245   3165   3116  -1142   -114    573       C  
ATOM   1630  C   SER B  56      33.216  47.559 335.817  1.00 24.37           C  
ANISOU 1630  C   SER B  56     2347   3357   3556  -1241   -103    537       C  
ATOM   1631  O   SER B  56      33.176  46.483 336.421  1.00 23.95           O  
ANISOU 1631  O   SER B  56     2272   3174   3652  -1153   -165    455       O  
ATOM   1632  CB  SER B  56      35.525  48.319 336.346  1.00 26.17           C  
ANISOU 1632  CB  SER B  56     2425   3844   3675  -1357    -50    470       C  
ATOM   1633  OG  SER B  56      35.912  47.983 335.026  1.00 37.26           O  
ANISOU 1633  OG  SER B  56     3486   5581   5089  -1555     18    377       O  
ATOM   1634  N   VAL B  57      32.535  47.799 334.693  1.00 20.93           N  
ANISOU 1634  N   VAL B  57     2027   3009   2919  -1136   -124    560       N  
ATOM   1635  CA  VAL B  57      31.667  46.785 334.100  1.00 20.57           C  
ANISOU 1635  CA  VAL B  57     1988   2921   2908  -1085   -171    509       C  
ATOM   1636  C   VAL B  57      32.462  45.882 333.152  1.00 25.79           C  
ANISOU 1636  C   VAL B  57     2246   3801   3754  -1379   -153    268       C  
ATOM   1637  O   VAL B  57      32.007  44.787 332.844  1.00 28.56           O  
ANISOU 1637  O   VAL B  57     2636   4052   4166  -1291   -268    128       O  
ATOM   1638  CB  VAL B  57      30.398  47.362 333.429  1.00 23.06           C  
ANISOU 1638  CB  VAL B  57     2255   3279   3228  -1269   -157    685       C  
ATOM   1639  CG1 VAL B  57      29.631  48.256 334.391  1.00 22.21           C  
ANISOU 1639  CG1 VAL B  57     2262   3034   3142  -1171   -185    869       C  
ATOM   1640  CG2 VAL B  57      30.716  48.102 332.137  1.00 23.76           C  
ANISOU 1640  CG2 VAL B  57     2247   3645   3138  -1413    -88    697       C  
ATOM   1641  N   GLY B  58      33.628  46.335 332.723  1.00 22.77           N  
ANISOU 1641  N   GLY B  58     1860   3672   3120  -1273    -76    189       N  
ATOM   1642  CA  GLY B  58      34.507  45.588 331.840  1.00 23.98           C  
ANISOU 1642  CA  GLY B  58     1721   4151   3239  -1264    -84    -86       C  
ATOM   1643  C   GLY B  58      35.806  46.337 331.689  1.00 31.20           C  
ANISOU 1643  C   GLY B  58     2442   5423   3992  -1325     20    -70       C  
ATOM   1644  O   GLY B  58      35.946  47.431 332.244  1.00 30.02           O  
ANISOU 1644  O   GLY B  58     2317   5230   3861  -1501     72    153       O  
ATOM   1645  N   ALA B  59      36.765  45.763 330.938  1.00 31.74           N  
ANISOU 1645  N   ALA B  59     2315   5860   3884  -1179     40   -305       N  
ATOM   1646  CA  ALA B  59      38.069  46.383 330.694  1.00 33.87           C  
ANISOU 1646  CA  ALA B  59     2331   6580   3958  -1240    137   -275       C  
ATOM   1647  C   ALA B  59      37.902  47.729 330.002  1.00 40.25           C  
ANISOU 1647  C   ALA B  59     3073   7624   4596  -1549    226      3       C  
ATOM   1648  O   ALA B  59      37.066  47.854 329.096  1.00 40.43           O  
ANISOU 1648  O   ALA B  59     3127   7714   4521  -1604    238     33       O  
ATOM   1649  CB  ALA B  59      38.940  45.464 329.855  1.00 37.64           C  
ANISOU 1649  CB  ALA B  59     2596   7459   4246   -967    147   -594       C  
ATOM   1650  N   GLY B  60      38.646  48.727 330.487  1.00 38.33           N  
ANISOU 1650  N   GLY B  60     2761   7470   4333  -1766    262    220       N  
ATOM   1651  CA  GLY B  60      38.639  50.097 329.971  1.00 39.54           C  
ANISOU 1651  CA  GLY B  60     2877   7791   4357  -2096    309    528       C  
ATOM   1652  C   GLY B  60      37.363  50.893 330.203  1.00 42.50           C  
ANISOU 1652  C   GLY B  60     3535   7735   4879  -2244    279    755       C  
ATOM   1653  O   GLY B  60      37.110  51.879 329.503  1.00 43.19           O  
ANISOU 1653  O   GLY B  60     3619   7929   4862  -2474    300   1000       O  
ATOM   1654  N   ILE B  61      36.543  50.471 331.176  1.00 37.22           N  
ANISOU 1654  N   ILE B  61     3098   6601   4444  -2101    225    696       N  
ATOM   1655  CA  ILE B  61      35.284  51.134 331.518  1.00 35.76           C  
ANISOU 1655  CA  ILE B  61     3164   6032   4392  -2169    204    894       C  
ATOM   1656  C   ILE B  61      35.220  51.299 333.040  1.00 40.72           C  
ANISOU 1656  C   ILE B  61     3978   6277   5217  -2129    161    919       C  
ATOM   1657  O   ILE B  61      35.309  50.317 333.771  1.00 40.24           O  
ANISOU 1657  O   ILE B  61     3926   6095   5266  -1946    125    750       O  
ATOM   1658  CB  ILE B  61      34.042  50.366 330.957  1.00 37.45           C  
ANISOU 1658  CB  ILE B  61     3440   6153   4636  -2030    186    827       C  
ATOM   1659  CG1 ILE B  61      34.081  50.256 329.424  1.00 39.70           C  
ANISOU 1659  CG1 ILE B  61     3544   6852   4690  -2060    219    768       C  
ATOM   1660  CG2 ILE B  61      32.739  51.021 331.406  1.00 35.62           C  
ANISOU 1660  CG2 ILE B  61     3420   5597   4517  -2074    177   1061       C  
ATOM   1661  CD1 ILE B  61      33.825  48.888 328.895  1.00 48.98           C  
ANISOU 1661  CD1 ILE B  61     4672   8094   5845  -1846    170    464       C  
ATOM   1662  N   THR B  66      35.084  52.538 333.507  1.00 38.51           N  
ANISOU 1662  N   THR B  66     3857   5805   4970  -2297    149   1128       N  
ATOM   1663  CA  THR B  66      34.965  52.878 334.926  1.00 38.06           C  
ANISOU 1663  CA  THR B  66     4003   5402   5056  -2263    105   1150       C  
ATOM   1664  C   THR B  66      33.900  53.956 335.090  1.00 43.08           C  
ANISOU 1664  C   THR B  66     4887   5735   5744  -2293     98   1346       C  
ATOM   1665  O   THR B  66      33.757  54.822 334.213  1.00 44.46           O  
ANISOU 1665  O   THR B  66     5080   5970   5844  -2447    102   1520       O  
ATOM   1666  CB  THR B  66      36.316  53.336 335.534  1.00 48.40           C  
ANISOU 1666  CB  THR B  66     5260   6803   6328  -2429     64   1147       C  
ATOM   1667  OG1 THR B  66      36.882  54.406 334.765  1.00 47.91           O  
ANISOU 1667  OG1 THR B  66     5139   6925   6139  -2713     54   1327       O  
ATOM   1668  CG2 THR B  66      37.318  52.196 335.698  1.00 48.07           C  
ANISOU 1668  CG2 THR B  66     4986   7016   6263  -2311     65    943       C  
ATOM   1669  N   ASP B  67      33.147  53.901 336.202  1.00 38.09           N  
ANISOU 1669  N   ASP B  67     4438   4804   5229  -2126     84   1332       N  
ATOM   1670  CA  ASP B  67      32.119  54.897 336.503  1.00 38.15           C  
ANISOU 1670  CA  ASP B  67     4685   4534   5277  -2070     82   1488       C  
ATOM   1671  C   ASP B  67      32.078  55.210 337.996  1.00 40.18           C  
ANISOU 1671  C   ASP B  67     5143   4525   5599  -1961     48   1436       C  
ATOM   1672  O   ASP B  67      32.585  54.438 338.816  1.00 39.00           O  
ANISOU 1672  O   ASP B  67     4926   4411   5481  -1898     35   1299       O  
ATOM   1673  CB  ASP B  67      30.732  54.459 336.013  1.00 40.04           C  
ANISOU 1673  CB  ASP B  67     4896   4781   5535  -1904    128   1559       C  
ATOM   1674  CG  ASP B  67      30.679  54.023 334.563  1.00 61.31           C  
ANISOU 1674  CG  ASP B  67     7401   7753   8141  -1992    151   1584       C  
ATOM   1675  OD1 ASP B  67      30.765  54.908 333.668  1.00 64.53           O  
ANISOU 1675  OD1 ASP B  67     7818   8234   8468  -2146    152   1737       O  
ATOM   1676  OD2 ASP B  67      30.587  52.792 334.316  1.00 69.62           O  
ANISOU 1676  OD2 ASP B  67     8308   8946   9198  -1913    151   1451       O  
ATOM   1677  N   GLN B  68      31.480  56.362 338.336  1.00 35.97           N  
ANISOU 1677  N   GLN B  68     4863   3728   5075  -1921     25   1543       N  
ATOM   1678  CA  GLN B  68      31.321  56.839 339.703  1.00 35.32           C  
ANISOU 1678  CA  GLN B  68     5013   3392   5013  -1784    -10   1478       C  
ATOM   1679  C   GLN B  68      30.272  56.027 340.465  1.00 36.37           C  
ANISOU 1679  C   GLN B  68     5110   3540   5168  -1490     57   1449       C  
ATOM   1680  O   GLN B  68      29.313  55.536 339.874  1.00 34.90           O  
ANISOU 1680  O   GLN B  68     4806   3460   4994  -1385    115   1542       O  
ATOM   1681  CB  GLN B  68      30.910  58.317 339.694  1.00 38.61           C  
ANISOU 1681  CB  GLN B  68     5735   3509   5427  -1782    -68   1584       C  
ATOM   1682  CG  GLN B  68      32.012  59.276 339.256  1.00 56.82           C  
ANISOU 1682  CG  GLN B  68     8140   5729   7719  -2120   -186   1636       C  
ATOM   1683  CD  GLN B  68      31.634  60.733 339.410  1.00 73.92           C  
ANISOU 1683  CD  GLN B  68    10675   7502   9909  -2114   -292   1727       C  
ATOM   1684  OE1 GLN B  68      30.654  61.098 340.078  1.00 68.57           O  
ANISOU 1684  OE1 GLN B  68    10221   6590   9244  -1806   -280   1684       O  
ATOM   1685  NE2 GLN B  68      32.429  61.607 338.809  1.00 65.23           N  
ANISOU 1685  NE2 GLN B  68     9648   6324   8810  -2449   -412   1860       N  
ATOM   1686  N   GLY B  69      30.451  55.929 341.773  1.00 32.47           N  
ANISOU 1686  N   GLY B  69     4709   2967   4662  -1382     35   1343       N  
ATOM   1687  CA  GLY B  69      29.507  55.261 342.653  1.00 31.65           C  
ANISOU 1687  CA  GLY B  69     4565   2912   4550  -1123     89   1350       C  
ATOM   1688  C   GLY B  69      28.664  56.263 343.416  1.00 37.67           C  
ANISOU 1688  C   GLY B  69     5573   3499   5241   -885    106   1364       C  
ATOM   1689  O   GLY B  69      28.139  57.213 342.829  1.00 39.09           O  
ANISOU 1689  O   GLY B  69     5911   3528   5413   -835    106   1442       O  
ATOM   1690  N   GLU B  70      28.564  56.075 344.737  1.00 34.06           N  
ANISOU 1690  N   GLU B  70     5153   3070   4717   -718    112   1286       N  
ATOM   1691  CA  GLU B  70      27.798  56.909 345.661  1.00 35.87           C  
ANISOU 1691  CA  GLU B  70     5604   3192   4833   -429    134   1250       C  
ATOM   1692  C   GLU B  70      28.674  58.019 346.265  1.00 41.09           C  
ANISOU 1692  C   GLU B  70     6581   3587   5446   -507     22   1069       C  
ATOM   1693  O   GLU B  70      28.216  59.157 346.420  1.00 42.70           O  
ANISOU 1693  O   GLU B  70     7072   3554   5599   -339     -7   1027       O  
ATOM   1694  CB  GLU B  70      27.219  56.020 346.775  1.00 37.25           C  
ANISOU 1694  CB  GLU B  70     5627   3604   4921   -223    195   1272       C  
ATOM   1695  CG  GLU B  70      25.990  56.591 347.465  1.00 52.15           C  
ANISOU 1695  CG  GLU B  70     7618   5538   6659    157    273   1306       C  
ATOM   1696  CD  GLU B  70      25.679  55.970 348.812  1.00 73.56           C  
ANISOU 1696  CD  GLU B  70    10206   8514   9229    339    318   1314       C  
ATOM   1697  OE1 GLU B  70      25.605  54.721 348.894  1.00 62.31           O  
ANISOU 1697  OE1 GLU B  70     8498   7318   7858    237    332   1457       O  
ATOM   1698  OE2 GLU B  70      25.509  56.736 349.789  1.00 70.49           O  
ANISOU 1698  OE2 GLU B  70    10014   8103   8668    587    327   1180       O  
ATOM   1699  N   VAL B  71      29.922  57.667 346.627  1.00 36.98           N  
ANISOU 1699  N   VAL B  71     6010   3100   4939   -754    -59    962       N  
ATOM   1700  CA  VAL B  71      30.928  58.554 347.227  1.00 38.52           C  
ANISOU 1700  CA  VAL B  71     6464   3084   5086   -915   -200    800       C  
ATOM   1701  C   VAL B  71      32.251  58.404 346.413  1.00 41.08           C  
ANISOU 1701  C   VAL B  71     6654   3453   5500  -1324   -281    827       C  
ATOM   1702  O   VAL B  71      33.199  57.749 346.859  1.00 39.84           O  
ANISOU 1702  O   VAL B  71     6337   3467   5333  -1471   -320    766       O  
ATOM   1703  CB  VAL B  71      31.097  58.312 348.759  1.00 43.02           C  
ANISOU 1703  CB  VAL B  71     7097   3732   5518   -776   -226    643       C  
ATOM   1704  CG1 VAL B  71      29.993  59.011 349.541  1.00 45.09           C  
ANISOU 1704  CG1 VAL B  71     7610   3885   5639   -391   -189    564       C  
ATOM   1705  CG2 VAL B  71      31.145  56.824 349.111  1.00 40.43           C  
ANISOU 1705  CG2 VAL B  71     6423   3740   5198   -748   -152    712       C  
ATOM   1706  N   PRO B  72      32.308  58.970 345.184  1.00 37.36           N  
ANISOU 1706  N   PRO B  72     6216   2879   5102  -1496   -303    944       N  
ATOM   1707  CA  PRO B  72      33.497  58.764 344.343  1.00 36.45           C  
ANISOU 1707  CA  PRO B  72     5912   2907   5031  -1862   -357    998       C  
ATOM   1708  C   PRO B  72      34.619  59.793 344.517  1.00 41.17           C  
ANISOU 1708  C   PRO B  72     6710   3329   5603  -2189   -537    964       C  
ATOM   1709  O   PRO B  72      35.705  59.579 343.975  1.00 39.98           O  
ANISOU 1709  O   PRO B  72     6353   3384   5454  -2495   -583   1014       O  
ATOM   1710  CB  PRO B  72      32.924  58.830 342.928  1.00 37.80           C  
ANISOU 1710  CB  PRO B  72     5986   3118   5258  -1886   -287   1171       C  
ATOM   1711  CG  PRO B  72      31.705  59.683 343.036  1.00 43.55           C  
ANISOU 1711  CG  PRO B  72     6982   3581   5985  -1622   -268   1217       C  
ATOM   1712  CD  PRO B  72      31.276  59.753 344.468  1.00 39.81           C  
ANISOU 1712  CD  PRO B  72     6690   2997   5440  -1350   -272   1059       C  
ATOM   1713  N   ASN B  74      34.371  60.890 345.257  1.00 40.08           N  
ANISOU 1713  N   ASN B  74     6966   2829   5432  -2124   -652    882       N  
ATOM   1714  CA  ASN B  74      35.339  61.968 345.453  1.00 42.83           C  
ANISOU 1714  CA  ASN B  74     7576   2930   5766  -2459   -872    853       C  
ATOM   1715  C   ASN B  74      36.504  61.575 346.367  1.00 47.56           C  
ANISOU 1715  C   ASN B  74     8069   3711   6290  -2659   -963    728       C  
ATOM   1716  O   ASN B  74      36.307  61.001 347.448  1.00 45.62           O  
ANISOU 1716  O   ASN B  74     7798   3565   5971  -2425   -912    576       O  
ATOM   1717  CB  ASN B  74      34.660  63.225 345.973  1.00 44.54           C  
ANISOU 1717  CB  ASN B  74     8287   2668   5968  -2274   -989    753       C  
ATOM   1718  CG  ASN B  74      33.856  63.956 344.925  1.00 63.48           C  
ANISOU 1718  CG  ASN B  74    10843   4820   8455  -2196   -983    924       C  
ATOM   1719  OD1 ASN B  74      33.738  63.529 343.766  1.00 53.51           O  
ANISOU 1719  OD1 ASN B  74     9308   3771   7252  -2277   -876   1128       O  
ATOM   1720  ND2 ASN B  74      33.295  65.092 345.310  1.00 58.07           N  
ANISOU 1720  ND2 ASN B  74    10615   3678   7772  -2020  -1111    838       N  
ATOM   1721  N   GLY B  75      37.707  61.913 345.895  1.00 46.23           N  
ANISOU 1721  N   GLY B  75     7816   3624   6128  -3104  -1101    827       N  
ATOM   1722  CA  GLY B  75      38.977  61.638 346.557  1.00 46.57           C  
ANISOU 1722  CA  GLY B  75     7711   3887   6094  -3367  -1211    763       C  
ATOM   1723  C   GLY B  75      39.646  60.379 346.058  1.00 46.88           C  
ANISOU 1723  C   GLY B  75     7243   4438   6131  -3401  -1076    833       C  
ATOM   1724  O   GLY B  75      40.767  60.071 346.465  1.00 47.10           O  
ANISOU 1724  O   GLY B  75     7084   4716   6094  -3587  -1151    804       O  
ATOM   1725  N   TYR B  76      38.959  59.651 345.161  1.00 40.33           N  
ANISOU 1725  N   TYR B  76     6195   3765   5366  -3207   -889    918       N  
ATOM   1726  CA  TYR B  76      39.422  58.375 344.623  1.00 37.58           C  
ANISOU 1726  CA  TYR B  76     5404   3855   5021  -3159   -761    945       C  
ATOM   1727  C   TYR B  76      39.437  58.326 343.088  1.00 42.30           C  
ANISOU 1727  C   TYR B  76     5789   4645   5637  -3277   -683   1106       C  
ATOM   1728  O   TYR B  76      38.602  58.935 342.405  1.00 42.03           O  
ANISOU 1728  O   TYR B  76     5920   4405   5643  -3247   -656   1201       O  
ATOM   1729  CB  TYR B  76      38.566  57.212 345.145  1.00 34.76           C  
ANISOU 1729  CB  TYR B  76     4962   3543   4703  -2750   -617    844       C  
ATOM   1730  CG  TYR B  76      38.247  57.248 346.626  1.00 35.19           C  
ANISOU 1730  CG  TYR B  76     5218   3443   4711  -2572   -663    709       C  
ATOM   1731  CD1 TYR B  76      39.104  56.669 347.559  1.00 36.89           C  
ANISOU 1731  CD1 TYR B  76     5291   3857   4869  -2611   -723    634       C  
ATOM   1732  CD2 TYR B  76      37.048  57.784 347.088  1.00 35.43           C  
ANISOU 1732  CD2 TYR B  76     5548   3183   4732  -2328   -634    662       C  
ATOM   1733  CE1 TYR B  76      38.786  56.648 348.917  1.00 36.38           C  
ANISOU 1733  CE1 TYR B  76     5388   3706   4729  -2442   -760    520       C  
ATOM   1734  CE2 TYR B  76      36.713  57.753 348.440  1.00 36.06           C  
ANISOU 1734  CE2 TYR B  76     5779   3199   4725  -2128   -657    533       C  
ATOM   1735  CZ  TYR B  76      37.586  57.187 349.350  1.00 39.67           C  
ANISOU 1735  CZ  TYR B  76     6098   3858   5115  -2200   -722    464       C  
ATOM   1736  OH  TYR B  76      37.249  57.173 350.674  1.00 37.39           O  
ANISOU 1736  OH  TYR B  76     5948   3548   4709  -2010   -746    348       O  
ATOM   1737  N   ASN B  77      40.391  57.539 342.578  1.00 38.61           N  
ANISOU 1737  N   ASN B  77     4938   4609   5122  -3376   -642   1130       N  
ATOM   1738  CA  ASN B  77      40.683  57.272 341.176  1.00 38.09           C  
ANISOU 1738  CA  ASN B  77     4586   4871   5016  -3471   -559   1249       C  
ATOM   1739  C   ASN B  77      40.686  55.752 340.942  1.00 39.05           C  
ANISOU 1739  C   ASN B  77     4394   5296   5147  -3170   -420   1124       C  
ATOM   1740  O   ASN B  77      41.092  55.001 341.836  1.00 37.82           O  
ANISOU 1740  O   ASN B  77     4149   5213   5007  -3028   -432   1003       O  
ATOM   1741  CB  ASN B  77      42.061  57.877 340.851  1.00 40.93           C  
ANISOU 1741  CB  ASN B  77     4766   5521   5265  -3898   -675   1396       C  
ATOM   1742  CG  ASN B  77      42.316  58.229 339.410  1.00 72.06           C  
ANISOU 1742  CG  ASN B  77     8505   9748   9126  -4106   -632   1594       C  
ATOM   1743  OD1 ASN B  77      41.666  57.736 338.482  1.00 71.13           O  
ANISOU 1743  OD1 ASN B  77     8289   9727   9011  -3904   -493   1587       O  
ATOM   1744  ND2 ASN B  77      43.304  59.085 339.193  1.00 67.70           N  
ANISOU 1744  ND2 ASN B  77     7870   9371   8482  -4542   -765   1793       N  
ATOM   1745  N   VAL B  78      40.236  55.294 339.761  1.00 34.28           N  
ANISOU 1745  N   VAL B  78     3657   4858   4511  -3040   -316   1146       N  
ATOM   1746  CA  VAL B  78      40.232  53.864 339.425  1.00 32.39           C  
ANISOU 1746  CA  VAL B  78     3181   4858   4270  -2734   -220   1000       C  
ATOM   1747  C   VAL B  78      40.689  53.627 337.984  1.00 36.67           C  
ANISOU 1747  C   VAL B  78     3406   5808   4720  -2848   -136   1047       C  
ATOM   1748  O   VAL B  78      40.543  54.512 337.135  1.00 36.24           O  
ANISOU 1748  O   VAL B  78     3387   5787   4596  -3064   -134   1214       O  
ATOM   1749  CB  VAL B  78      38.876  53.173 339.673  1.00 33.38           C  
ANISOU 1749  CB  VAL B  78     3435   4695   4552  -2476   -150    929       C  
ATOM   1750  CG1 VAL B  78      38.677  52.840 341.147  1.00 32.06           C  
ANISOU 1750  CG1 VAL B  78     3405   4306   4471  -2323   -198    851       C  
ATOM   1751  CG2 VAL B  78      37.713  53.982 339.102  1.00 32.81           C  
ANISOU 1751  CG2 VAL B  78     3581   4384   4499  -2511   -122   1054       C  
ATOM   1752  N   SER B  79      41.222  52.412 337.718  1.00 34.13           N  
ANISOU 1752  N   SER B  79     2808   5799   4361  -2631    -83    889       N  
ATOM   1753  CA  SER B  79      41.693  51.971 336.400  1.00 35.94           C  
ANISOU 1753  CA  SER B  79     2739   6483   4436  -2595     -4    854       C  
ATOM   1754  C   SER B  79      41.323  50.508 336.132  1.00 40.28           C  
ANISOU 1754  C   SER B  79     3208   7059   5038  -2207     42    608       C  
ATOM   1755  O   SER B  79      41.337  49.693 337.049  1.00 38.53           O  
ANISOU 1755  O   SER B  79     3029   6668   4944  -2000     -2    484       O  
ATOM   1756  CB  SER B  79      43.207  52.141 336.282  1.00 42.10           C  
ANISOU 1756  CB  SER B  79     3192   7761   5044  -2774    -19    916       C  
ATOM   1757  OG  SER B  79      43.587  53.471 335.967  1.00 51.31           O  
ANISOU 1757  OG  SER B  79     4392   8977   6126  -3198    -79   1178       O  
ATOM   1758  N   ARG B  80      41.015  50.175 334.874  1.00 38.95           N  
ANISOU 1758  N   ARG B  80     2934   7099   4766  -2120    111    544       N  
ATOM   1759  CA  ARG B  80      40.717  48.803 334.468  1.00 39.27           C  
ANISOU 1759  CA  ARG B  80     2922   7161   4839  -1770    123    286       C  
ATOM   1760  C   ARG B  80      41.463  48.519 333.151  1.00 48.24           C  
ANISOU 1760  C   ARG B  80     3749   8857   5722  -1704    197    182       C  
ATOM   1761  O   ARG B  80      40.854  48.459 332.076  1.00 48.70           O  
ANISOU 1761  O   ARG B  80     3813   9010   5683  -1690    239    150       O  
ATOM   1762  CB  ARG B  80      39.195  48.554 334.362  1.00 36.03           C  
ANISOU 1762  CB  ARG B  80     2780   6338   4572  -1689    103    274       C  
ATOM   1763  CG  ARG B  80      38.810  47.072 334.276  1.00 41.26           C  
ANISOU 1763  CG  ARG B  80     3465   6879   5332  -1364     50     20       C  
ATOM   1764  CD  ARG B  80      38.689  46.414 335.640  1.00 44.52           C  
ANISOU 1764  CD  ARG B  80     4018   6930   5969  -1230    -40     -5       C  
ATOM   1765  NE  ARG B  80      38.451  44.971 335.560  1.00 48.49           N  
ANISOU 1765  NE  ARG B  80     4548   7296   6581   -942   -129   -227       N  
ATOM   1766  CZ  ARG B  80      37.250  44.405 335.470  1.00 58.58           C  
ANISOU 1766  CZ  ARG B  80     6009   8266   7985   -890   -201   -244       C  
ATOM   1767  NH1 ARG B  80      36.157  45.153 335.412  1.00 44.13           N  
ANISOU 1767  NH1 ARG B  80     4314   6284   6168  -1073   -168    -54       N  
ATOM   1768  NH2 ARG B  80      37.136  43.085 335.426  1.00 44.60           N  
ANISOU 1768  NH2 ARG B  80     4285   6336   6325   -656   -323   -441       N  
ATOM   1769  N   SER B  81      42.803  48.403 333.246  1.00 47.79           N  
ANISOU 1769  N   SER B  81     3398   9227   5532  -1669    215    144       N  
ATOM   1770  CA  SER B  81      43.685  48.129 332.108  1.00 51.23           C  
ANISOU 1770  CA  SER B  81     3477  10304   5683  -1566    299     44       C  
ATOM   1771  C   SER B  81      43.455  46.709 331.597  1.00 56.70           C  
ANISOU 1771  C   SER B  81     4167  10996   6379  -1114    295   -320       C  
ATOM   1772  O   SER B  81      43.431  46.483 330.387  1.00 57.80           O  
ANISOU 1772  O   SER B  81     4169  11492   6301  -1008    359   -447       O  
ATOM   1773  CB  SER B  81      45.143  48.330 332.505  1.00 57.87           C  
ANISOU 1773  CB  SER B  81     3990  11606   6392  -1629    309    122       C  
ATOM   1774  OG  SER B  81      45.389  49.679 332.871  1.00 68.25           O  
ANISOU 1774  OG  SER B  81     5334  12895   7703  -2088    273    455       O  
ATOM   1775  N   THR B  83      43.259  45.765 332.537  1.00 53.19           N  
ANISOU 1775  N   THR B  83     3894  10136   6179   -857    200   -482       N  
ATOM   1776  CA  THR B  83      42.968  44.352 332.288  1.00 54.18           C  
ANISOU 1776  CA  THR B  83     4106  10095   6386   -439    132   -820       C  
ATOM   1777  C   THR B  83      41.664  43.989 332.995  1.00 55.33           C  
ANISOU 1777  C   THR B  83     4629   9559   6835   -454     19   -798       C  
ATOM   1778  O   THR B  83      41.183  44.767 333.821  1.00 52.71           O  
ANISOU 1778  O   THR B  83     4447   8941   6641   -707      7   -552       O  
ATOM   1779  CB  THR B  83      44.128  43.450 332.737  1.00 66.38           C  
ANISOU 1779  CB  THR B  83     5452  11841   7929    -89     98  -1009       C  
ATOM   1780  OG1 THR B  83      44.448  43.727 334.104  1.00 65.74           O  
ANISOU 1780  OG1 THR B  83     5411  11545   8023   -219     44   -817       O  
ATOM   1781  CG2 THR B  83      45.357  43.584 331.845  1.00 68.95           C  
ANISOU 1781  CG2 THR B  83     5356  12933   7909     20    216  -1080       C  
ATOM   1782  N   THR B  84      41.103  42.807 332.682  1.00 52.28           N  
ANISOU 1782  N   THR B  84     4395   8928   6540   -183    -78  -1054       N  
ATOM   1783  CA  THR B  84      39.843  42.312 333.244  1.00 49.57           C  
ANISOU 1783  CA  THR B  84     4376   7991   6468   -204   -208  -1020       C  
ATOM   1784  C   THR B  84      40.102  41.451 334.526  1.00 53.18           C  
ANISOU 1784  C   THR B  84     4925   8106   7176    -10   -341  -1051       C  
ATOM   1785  O   THR B  84      39.222  40.695 334.939  1.00 52.12           O  
ANISOU 1785  O   THR B  84     5024   7519   7258     52   -486  -1074       O  
ATOM   1786  CB  THR B  84      39.025  41.584 332.134  1.00 55.78           C  
ANISOU 1786  CB  THR B  84     5290   8692   7213    -92   -277  -1240       C  
ATOM   1787  OG1 THR B  84      37.819  41.037 332.669  1.00 50.67           O  
ANISOU 1787  OG1 THR B  84     4925   7508   6818   -159   -418  -1162       O  
ATOM   1788  CG2 THR B  84      39.818  40.503 331.404  1.00 58.60           C  
ANISOU 1788  CG2 THR B  84     5560   9239   7467    309   -338  -1635       C  
ATOM   1789  N   GLU B  85      41.277  41.621 335.178  1.00 50.61           N  
ANISOU 1789  N   GLU B  85     4404   8013   6815     49   -302  -1008       N  
ATOM   1790  CA  GLU B  85      41.657  40.889 336.400  1.00 50.77           C  
ANISOU 1790  CA  GLU B  85     4466   7784   7041    226   -422  -1001       C  
ATOM   1791  C   GLU B  85      41.990  41.831 337.563  1.00 53.59           C  
ANISOU 1791  C   GLU B  85     4777   8161   7422    -27   -377   -721       C  
ATOM   1792  O   GLU B  85      41.725  41.500 338.722  1.00 51.86           O  
ANISOU 1792  O   GLU B  85     4699   7606   7398    -25   -475   -607       O  
ATOM   1793  CB  GLU B  85      42.871  39.970 336.152  1.00 55.59           C  
ANISOU 1793  CB  GLU B  85     4868   8673   7579    629   -454  -1261       C  
ATOM   1794  CG  GLU B  85      42.621  38.793 335.222  1.00 68.35           C  
ANISOU 1794  CG  GLU B  85     6597  10158   9215    977   -560  -1604       C  
ATOM   1795  CD  GLU B  85      42.706  39.066 333.730  1.00 86.29           C  
ANISOU 1795  CD  GLU B  85     8737  12856  11194   1016   -444  -1801       C  
ATOM   1796  OE1 GLU B  85      43.627  39.799 333.297  1.00 72.12           O  
ANISOU 1796  OE1 GLU B  85     6623  11649   9131    966   -280  -1757       O  
ATOM   1797  OE2 GLU B  85      41.876  38.495 332.986  1.00 79.59           O  
ANISOU 1797  OE2 GLU B  85     8092  11777  10371   1095   -532  -1995       O  
ATOM   1798  N   ASP B  86      42.615  42.978 337.256  1.00 50.93           N  
ANISOU 1798  N   ASP B  86     4242   8233   6875   -252   -248   -606       N  
ATOM   1799  CA  ASP B  86      43.044  43.937 338.266  1.00 49.71           C  
ANISOU 1799  CA  ASP B  86     4054   8122   6713   -516   -229   -371       C  
ATOM   1800  C   ASP B  86      42.215  45.215 338.242  1.00 49.54           C  
ANISOU 1800  C   ASP B  86     4199   7963   6660   -882   -168   -163       C  
ATOM   1801  O   ASP B  86      42.019  45.809 337.178  1.00 49.75           O  
ANISOU 1801  O   ASP B  86     4187   8167   6548  -1008    -87   -149       O  
ATOM   1802  CB  ASP B  86      44.532  44.276 338.081  1.00 54.78           C  
ANISOU 1802  CB  ASP B  86     4343   9320   7150   -528   -174   -365       C  
ATOM   1803  CG  ASP B  86      45.461  43.093 338.272  1.00 72.77           C  
ANISOU 1803  CG  ASP B  86     6432  11767   9451   -127   -234   -549       C  
ATOM   1804  OD1 ASP B  86      45.729  42.381 337.274  1.00 76.30           O  
ANISOU 1804  OD1 ASP B  86     6751  12438   9799    168   -207   -781       O  
ATOM   1805  OD2 ASP B  86      45.933  42.885 339.416  1.00 79.88           O  
ANISOU 1805  OD2 ASP B  86     7310  12587  10453    -87   -314   -468       O  
ATOM   1806  N   PHE B  87      41.752  45.645 339.430  1.00 42.26           N  
ANISOU 1806  N   PHE B  87     3461   6741   5855  -1029   -213     -2       N  
ATOM   1807  CA  PHE B  87      40.996  46.881 339.605  1.00 39.69           C  
ANISOU 1807  CA  PHE B  87     3328   6240   5513  -1320   -175    181       C  
ATOM   1808  C   PHE B  87      41.569  47.663 340.816  1.00 43.55           C  
ANISOU 1808  C   PHE B  87     3855   6698   5993  -1502   -220    310       C  
ATOM   1809  O   PHE B  87      41.081  47.539 341.942  1.00 41.80           O  
ANISOU 1809  O   PHE B  87     3805   6193   5885  -1456   -275    355       O  
ATOM   1810  CB  PHE B  87      39.482  46.615 339.727  1.00 39.03           C  
ANISOU 1810  CB  PHE B  87     3498   5759   5571  -1259   -190    211       C  
ATOM   1811  CG  PHE B  87      38.586  47.833 339.634  1.00 38.81           C  
ANISOU 1811  CG  PHE B  87     3661   5569   5515  -1478   -140    378       C  
ATOM   1812  CD1 PHE B  87      38.741  48.756 338.605  1.00 42.17           C  
ANISOU 1812  CD1 PHE B  87     4042   6179   5802  -1672    -73    444       C  
ATOM   1813  CD2 PHE B  87      37.532  48.010 340.520  1.00 39.34           C  
ANISOU 1813  CD2 PHE B  87     3946   5315   5688  -1464   -164    480       C  
ATOM   1814  CE1 PHE B  87      37.912  49.878 338.516  1.00 42.07           C  
ANISOU 1814  CE1 PHE B  87     4226   5976   5781  -1839    -47    606       C  
ATOM   1815  CE2 PHE B  87      36.684  49.121 340.414  1.00 41.28           C  
ANISOU 1815  CE2 PHE B  87     4370   5412   5901  -1599   -118    617       C  
ATOM   1816  CZ  PHE B  87      36.882  50.048 339.413  1.00 39.76           C  
ANISOU 1816  CZ  PHE B  87     4160   5350   5598  -1778    -68    675       C  
ATOM   1817  N   PRO B  88      42.638  48.460 340.602  1.00 41.64           N  
ANISOU 1817  N   PRO B  88     3442   6781   5598  -1721   -211    377       N  
ATOM   1818  CA  PRO B  88      43.226  49.190 341.730  1.00 41.57           C  
ANISOU 1818  CA  PRO B  88     3480   6746   5568  -1919   -287    480       C  
ATOM   1819  C   PRO B  88      42.515  50.507 342.046  1.00 42.95           C  
ANISOU 1819  C   PRO B  88     3949   6631   5738  -2189   -305    609       C  
ATOM   1820  O   PRO B  88      42.117  51.256 341.142  1.00 42.71           O  
ANISOU 1820  O   PRO B  88     3983   6587   5657  -2346   -259    684       O  
ATOM   1821  CB  PRO B  88      44.663  49.439 341.271  1.00 46.24           C  
ANISOU 1821  CB  PRO B  88     3738   7841   5992  -2058   -291    512       C  
ATOM   1822  CG  PRO B  88      44.581  49.511 339.778  1.00 51.65           C  
ANISOU 1822  CG  PRO B  88     4276   8784   6564  -2073   -194    499       C  
ATOM   1823  CD  PRO B  88      43.380  48.714 339.344  1.00 45.27           C  
ANISOU 1823  CD  PRO B  88     3638   7686   5876  -1816   -145    376       C  
ATOM   1824  N   LEU B  89      42.374  50.782 343.353  1.00 37.03           N  
ANISOU 1824  N   LEU B  89     3381   5660   5030  -2222   -382    630       N  
ATOM   1825  CA  LEU B  89      41.798  52.013 343.883  1.00 35.65           C  
ANISOU 1825  CA  LEU B  89     3518   5189   4840  -2420   -425    706       C  
ATOM   1826  C   LEU B  89      42.948  52.917 344.264  1.00 42.86           C  
ANISOU 1826  C   LEU B  89     4390   6259   5638  -2747   -536    770       C  
ATOM   1827  O   LEU B  89      43.875  52.465 344.942  1.00 44.30           O  
ANISOU 1827  O   LEU B  89     4405   6644   5783  -2743   -601    743       O  
ATOM   1828  CB  LEU B  89      40.874  51.736 345.088  1.00 33.50           C  
ANISOU 1828  CB  LEU B  89     3471   4613   4645  -2223   -442    669       C  
ATOM   1829  CG  LEU B  89      40.106  52.937 345.648  1.00 37.17           C  
ANISOU 1829  CG  LEU B  89     4285   4756   5083  -2315   -471    701       C  
ATOM   1830  CD1 LEU B  89      38.870  53.232 344.835  1.00 35.76           C  
ANISOU 1830  CD1 LEU B  89     4250   4376   4961  -2207   -378    744       C  
ATOM   1831  CD2 LEU B  89      39.695  52.694 347.062  1.00 39.02           C  
ANISOU 1831  CD2 LEU B  89     4653   4867   5306  -2174   -516    656       C  
ATOM   1832  N   ARG B  90      42.921  54.173 343.800  1.00 40.23           N  
ANISOU 1832  N   ARG B  90     4197   5840   5248  -3048   -577    875       N  
ATOM   1833  CA  ARG B  90      43.984  55.126 344.092  1.00 42.53           C  
ANISOU 1833  CA  ARG B  90     4475   6249   5435  -3434   -722    968       C  
ATOM   1834  C   ARG B  90      43.438  56.324 344.840  1.00 48.30           C  
ANISOU 1834  C   ARG B  90     5642   6530   6179  -3594   -844    971       C  
ATOM   1835  O   ARG B  90      42.376  56.843 344.496  1.00 47.27           O  
ANISOU 1835  O   ARG B  90     5778   6071   6110  -3523   -805    985       O  
ATOM   1836  CB  ARG B  90      44.699  55.576 342.805  1.00 43.14           C  
ANISOU 1836  CB  ARG B  90     4310   6666   5415  -3716   -712   1128       C  
ATOM   1837  N   LEU B  91      44.168  56.742 345.881  1.00 47.16           N  
ANISOU 1837  N   LEU B  91     5570   6380   5968  -3787  -1002    944       N  
ATOM   1838  CA  LEU B  91      43.908  57.921 346.708  1.00 48.25           C  
ANISOU 1838  CA  LEU B  91     6135   6112   6084  -3961  -1167    903       C  
ATOM   1839  C   LEU B  91      44.999  58.925 346.399  1.00 55.67           C  
ANISOU 1839  C   LEU B  91     7058   7150   6945  -4479  -1361   1052       C  
ATOM   1840  O   LEU B  91      46.172  58.606 346.602  1.00 56.96           O  
ANISOU 1840  O   LEU B  91     6911   7712   7019  -4672  -1429   1108       O  
ATOM   1841  CB  LEU B  91      43.908  57.546 348.208  1.00 47.89           C  
ANISOU 1841  CB  LEU B  91     6190   6011   5994  -3788  -1222    742       C  
ATOM   1842  CG  LEU B  91      42.603  57.008 348.797  1.00 49.96           C  
ANISOU 1842  CG  LEU B  91     6624   6045   6313  -3347  -1093    619       C  
ATOM   1843  CD1 LEU B  91      42.469  55.507 348.585  1.00 47.36           C  
ANISOU 1843  CD1 LEU B  91     5952   5989   6052  -3041   -934    629       C  
ATOM   1844  CD2 LEU B  91      42.535  57.292 350.275  1.00 53.51           C  
ANISOU 1844  CD2 LEU B  91     7322   6345   6663  -3291  -1205    478       C  
ATOM   1845  N   LEU B  92      44.651  60.103 345.856  1.00 54.08           N  
ANISOU 1845  N   LEU B  92     7156   6615   6777  -4716  -1458   1152       N  
ATOM   1846  CA  LEU B  92      45.684  61.089 345.532  1.00 58.06           C  
ANISOU 1846  CA  LEU B  92     7656   7188   7216  -5272  -1678   1345       C  
ATOM   1847  C   LEU B  92      46.221  61.733 346.841  1.00 63.57           C  
ANISOU 1847  C   LEU B  92     8632   7671   7849  -5504  -1935   1234       C  
ATOM   1848  O   LEU B  92      47.295  61.346 347.305  1.00 63.34           O  
ANISOU 1848  O   LEU B  92     8318   8030   7718  -5681  -2009   1255       O  
ATOM   1849  CB  LEU B  92      45.189  62.137 344.502  1.00 59.80           C  
ANISOU 1849  CB  LEU B  92     8113   7107   7503  -5480  -1733   1528       C  
ATOM   1850  CG  LEU B  92      46.183  63.237 344.144  1.00 69.69           C  
ANISOU 1850  CG  LEU B  92     9390   8387   8703  -6110  -1996   1783       C  
ATOM   1851  CD1 LEU B  92      47.376  62.672 343.415  1.00 70.94           C  
ANISOU 1851  CD1 LEU B  92     8950   9270   8734  -6358  -1937   1997       C  
ATOM   1852  CD2 LEU B  92      45.526  64.337 343.324  1.00 74.70           C  
ANISOU 1852  CD2 LEU B  92    10363   8589   9432  -6276  -2087   1958       C  
ATOM   1853  N   SER B  93      45.470  62.670 347.438  1.00 61.66           N  
ANISOU 1853  N   SER B  93     8937   6837   7652  -5472  -2070   1102       N  
ATOM   1854  CA  SER B  93      45.844  63.305 348.697  1.00 64.42           C  
ANISOU 1854  CA  SER B  93     9622   6931   7923  -5647  -2325    939       C  
ATOM   1855  C   SER B  93      44.950  62.721 349.775  1.00 65.84           C  
ANISOU 1855  C   SER B  93     9971   6967   8078  -5120  -2197    652       C  
ATOM   1856  O   SER B  93      43.793  63.129 349.909  1.00 65.21           O  
ANISOU 1856  O   SER B  93    10266   6461   8051  -4811  -2148    521       O  
ATOM   1857  CB  SER B  93      45.727  64.827 348.608  1.00 72.06           C  
ANISOU 1857  CB  SER B  93    11110   7331   8937  -5990  -2607    978       C  
ATOM   1858  OG  SER B  93      44.403  65.235 348.301  1.00 79.20           O  
ANISOU 1858  OG  SER B  93    12365   7772   9953  -5638  -2508    908       O  
ATOM   1859  N   ALA B  94      45.455  61.695 350.474  1.00 60.74           N  
ANISOU 1859  N   ALA B  94     9002   6730   7347  -4992  -2126    588       N  
ATOM   1860  CA  ALA B  94      44.711  60.986 351.512  1.00 58.43           C  
ANISOU 1860  CA  ALA B  94     8778   6416   7009  -4526  -2003    375       C  
ATOM   1861  C   ALA B  94      44.428  61.894 352.699  1.00 65.62           C  
ANISOU 1861  C   ALA B  94    10184   6947   7803  -4535  -2207    140       C  
ATOM   1862  O   ALA B  94      45.310  62.631 353.133  1.00 69.29           O  
ANISOU 1862  O   ALA B  94    10776   7378   8176  -4944  -2475    119       O  
ATOM   1863  CB  ALA B  94      45.475  59.759 351.951  1.00 57.71           C  
ANISOU 1863  CB  ALA B  94     8217   6850   6859  -4448  -1923    412       C  
ATOM   1864  N   ALA B  95      43.181  61.879 353.183  1.00 60.81           N  
ANISOU 1864  N   ALA B  95     9857   6065   7183  -4086  -2092    -37       N  
ATOM   1865  CA  ALA B  95      42.740  62.729 354.288  1.00 63.52           C  
ANISOU 1865  CA  ALA B  95    10694   6052   7387  -3976  -2253   -308       C  
ATOM   1866  C   ALA B  95      42.111  61.896 355.415  1.00 65.21           C  
ANISOU 1866  C   ALA B  95    10831   6485   7461  -3524  -2100   -463       C  
ATOM   1867  O   ALA B  95      41.696  60.764 355.144  1.00 61.29           O  
ANISOU 1867  O   ALA B  95     9977   6276   7035  -3253  -1856   -339       O  
ATOM   1868  CB  ALA B  95      41.742  63.754 353.768  1.00 65.55           C  
ANISOU 1868  CB  ALA B  95    11404   5772   7730  -3825  -2271   -372       C  
ATOM   1869  N   PRO B  96      41.982  62.430 356.666  1.00 63.88           N  
ANISOU 1869  N   PRO B  96    10998   6188   7084  -3430  -2247   -726       N  
ATOM   1870  CA  PRO B  96      41.364  61.638 357.754  1.00 62.36           C  
ANISOU 1870  CA  PRO B  96    10697   6272   6725  -3007  -2096   -834       C  
ATOM   1871  C   PRO B  96      39.906  61.234 357.487  1.00 63.44           C  
ANISOU 1871  C   PRO B  96    10828   6364   6914  -2492  -1821   -813       C  
ATOM   1872  O   PRO B  96      39.375  60.353 358.165  1.00 61.16           O  
ANISOU 1872  O   PRO B  96    10347   6372   6517  -2168  -1666   -806       O  
ATOM   1873  CB  PRO B  96      41.452  62.571 358.963  1.00 68.43           C  
ANISOU 1873  CB  PRO B  96    11907   6856   7239  -3024  -2331  -1149       C  
ATOM   1874  CG  PRO B  96      42.536  63.520 358.631  1.00 76.10           C  
ANISOU 1874  CG  PRO B  96    13080   7579   8256  -3581  -2641  -1155       C  
ATOM   1875  CD  PRO B  96      42.416  63.748 357.165  1.00 70.04           C  
ANISOU 1875  CD  PRO B  96    12268   6589   7754  -3716  -2573   -936       C  
ATOM   1876  N   SER B  97      39.275  61.865 356.480  1.00 59.89           N  
ANISOU 1876  N   SER B  97    10559   5573   6626  -2443  -1773   -763       N  
ATOM   1877  CA  SER B  97      37.913  61.585 356.026  1.00 57.38           C  
ANISOU 1877  CA  SER B  97    10216   5210   6375  -2007  -1530   -703       C  
ATOM   1878  C   SER B  97      37.875  60.245 355.280  1.00 57.30           C  
ANISOU 1878  C   SER B  97     9693   5551   6526  -1980  -1315   -432       C  
ATOM   1879  O   SER B  97      36.792  59.701 355.055  1.00 55.88           O  
ANISOU 1879  O   SER B  97     9396   5455   6381  -1636  -1112   -350       O  
ATOM   1880  CB  SER B  97      37.412  62.706 355.111  1.00 62.15           C  
ANISOU 1880  CB  SER B  97    11169   5339   7106  -2014  -1584   -712       C  
ATOM   1881  OG  SER B  97      37.787  64.008 355.539  1.00 74.49           O  
ANISOU 1881  OG  SER B  97    13245   6488   8569  -2125  -1847   -953       O  
ATOM   1882  N   GLN B  98      39.060  59.722 354.888  1.00 51.80           N  
ANISOU 1882  N   GLN B  98     8695   5066   5918  -2339  -1376   -297       N  
ATOM   1883  CA  GLN B  98      39.205  58.474 354.139  1.00 47.73           C  
ANISOU 1883  CA  GLN B  98     7724   4857   5556  -2327  -1214    -81       C  
ATOM   1884  C   GLN B  98      39.760  57.339 355.023  1.00 50.51           C  
ANISOU 1884  C   GLN B  98     7761   5598   5832  -2283  -1204    -48       C  
ATOM   1885  O   GLN B  98      40.078  56.261 354.509  1.00 48.16           O  
ANISOU 1885  O   GLN B  98     7098   5544   5658  -2286  -1117    107       O  
ATOM   1886  CB  GLN B  98      40.078  58.694 352.889  1.00 48.92           C  
ANISOU 1886  CB  GLN B  98     7733   5004   5850  -2696  -1269     57       C  
ATOM   1887  CG  GLN B  98      39.373  59.536 351.816  1.00 63.69           C  
ANISOU 1887  CG  GLN B  98     9832   6540   7829  -2701  -1241    106       C  
ATOM   1888  CD  GLN B  98      40.272  60.030 350.708  1.00 81.51           C  
ANISOU 1888  CD  GLN B  98    12009   8788  10172  -3124  -1342    249       C  
ATOM   1889  OE1 GLN B  98      41.400  60.490 350.930  1.00 76.74           O  
ANISOU 1889  OE1 GLN B  98    11435   8212   9509  -3500  -1540    246       O  
ATOM   1890  NE2 GLN B  98      39.762  59.996 349.487  1.00 73.86           N  
ANISOU 1890  NE2 GLN B  98    10940   7795   9327  -3090  -1219    395       N  
ATOM   1891  N   THR B  99      39.831  57.570 356.357  1.00 48.27           N  
ANISOU 1891  N   THR B  99     7632   5369   5338  -2214  -1299   -197       N  
ATOM   1892  CA  THR B  99      40.255  56.573 357.348  1.00 47.14           C  
ANISOU 1892  CA  THR B  99     7224   5593   5093  -2148  -1304   -151       C  
ATOM   1893  C   THR B  99      39.072  55.619 357.464  1.00 47.49           C  
ANISOU 1893  C   THR B  99     7115   5754   5174  -1763  -1100    -34       C  
ATOM   1894  O   THR B  99      38.039  55.989 358.034  1.00 47.69           O  
ANISOU 1894  O   THR B  99     7343   5718   5057  -1493  -1038   -121       O  
ATOM   1895  CB  THR B  99      40.662  57.269 358.659  1.00 58.52           C  
ANISOU 1895  CB  THR B  99     8913   7055   6268  -2222  -1486   -355       C  
ATOM   1896  OG1 THR B  99      41.614  58.299 358.379  1.00 60.04           O  
ANISOU 1896  OG1 THR B  99     9286   7071   6455  -2629  -1701   -443       O  
ATOM   1897  CG2 THR B  99      41.226  56.308 359.688  1.00 57.67           C  
ANISOU 1897  CG2 THR B  99     8526   7354   6032  -2185  -1514   -285       C  
ATOM   1898  N   SER B 100      39.180  54.437 356.819  1.00 40.96           N  
ANISOU 1898  N   SER B 100     5941   5084   4540  -1738  -1005    164       N  
ATOM   1899  CA  SER B 100      38.075  53.478 356.716  1.00 38.38           C  
ANISOU 1899  CA  SER B 100     5461   4829   4293  -1445   -843    316       C  
ATOM   1900  C   SER B 100      38.540  52.022 356.536  1.00 39.95           C  
ANISOU 1900  C   SER B 100     5288   5240   4650  -1441   -831    503       C  
ATOM   1901  O   SER B 100      39.700  51.692 356.781  1.00 40.00           O  
ANISOU 1901  O   SER B 100     5131   5400   4668  -1608   -935    510       O  
ATOM   1902  CB  SER B 100      37.219  53.875 355.511  1.00 41.07           C  
ANISOU 1902  CB  SER B 100     5910   4924   4770  -1374   -727    335       C  
ATOM   1903  OG  SER B 100      36.006  53.152 355.394  1.00 50.18           O  
ANISOU 1903  OG  SER B 100     6949   6135   5981  -1117   -587    481       O  
ATOM   1904  N   VAL B 101      37.594  51.156 356.125  1.00 34.95           N  
ANISOU 1904  N   VAL B 101     4531   4612   4137  -1240   -718    658       N  
ATOM   1905  CA  VAL B 101      37.745  49.741 355.773  1.00 33.33           C  
ANISOU 1905  CA  VAL B 101     4037   4505   4122  -1190   -716    831       C  
ATOM   1906  C   VAL B 101      37.270  49.608 354.317  1.00 35.09           C  
ANISOU 1906  C   VAL B 101     4240   4550   4541  -1183   -627    852       C  
ATOM   1907  O   VAL B 101      36.109  49.902 354.018  1.00 33.74           O  
ANISOU 1907  O   VAL B 101     4179   4270   4369  -1069   -531    888       O  
ATOM   1908  CB  VAL B 101      37.003  48.759 356.722  1.00 37.30           C  
ANISOU 1908  CB  VAL B 101     4425   5161   4584  -1006   -710   1024       C  
ATOM   1909  CG1 VAL B 101      37.410  47.322 356.427  1.00 36.39           C  
ANISOU 1909  CG1 VAL B 101     4056   5080   4689   -979   -767   1192       C  
ATOM   1910  CG2 VAL B 101      37.245  49.094 358.194  1.00 39.22           C  
ANISOU 1910  CG2 VAL B 101     4717   5616   4569   -996   -781    992       C  
ATOM   1911  N   TYR B 102      38.169  49.199 353.416  1.00 30.70           N  
ANISOU 1911  N   TYR B 102     3534   4006   4124  -1294   -657    825       N  
ATOM   1912  CA  TYR B 102      37.864  49.107 351.993  1.00 28.72           C  
ANISOU 1912  CA  TYR B 102     3256   3636   4023  -1304   -583    817       C  
ATOM   1913  C   TYR B 102      37.671  47.675 351.542  1.00 31.60           C  
ANISOU 1913  C   TYR B 102     3426   4010   4571  -1173   -591    914       C  
ATOM   1914  O   TYR B 102      38.445  46.794 351.911  1.00 30.77           O  
ANISOU 1914  O   TYR B 102     3153   4018   4520  -1133   -677    943       O  
ATOM   1915  CB  TYR B 102      38.961  49.798 351.170  1.00 30.29           C  
ANISOU 1915  CB  TYR B 102     3425   3875   4209  -1519   -608    711       C  
ATOM   1916  CG  TYR B 102      38.930  51.302 351.336  1.00 32.61           C  
ANISOU 1916  CG  TYR B 102     3976   4050   4365  -1681   -624    627       C  
ATOM   1917  CD1 TYR B 102      38.295  52.112 350.402  1.00 34.18           C  
ANISOU 1917  CD1 TYR B 102     4336   4064   4588  -1724   -557    615       C  
ATOM   1918  CD2 TYR B 102      39.462  51.909 352.469  1.00 34.65           C  
ANISOU 1918  CD2 TYR B 102     4343   4356   4466  -1780   -727    561       C  
ATOM   1919  CE1 TYR B 102      38.222  53.492 350.572  1.00 36.18           C  
ANISOU 1919  CE1 TYR B 102     4870   4140   4736  -1852   -603    542       C  
ATOM   1920  CE2 TYR B 102      39.372  53.283 352.662  1.00 36.74           C  
ANISOU 1920  CE2 TYR B 102     4902   4444   4612  -1916   -778    458       C  
ATOM   1921  CZ  TYR B 102      38.760  54.073 351.707  1.00 42.71           C  
ANISOU 1921  CZ  TYR B 102     5834   4975   5420  -1946   -721    451       C  
ATOM   1922  OH  TYR B 102      38.692  55.429 351.889  1.00 44.08           O  
ANISOU 1922  OH  TYR B 102     6333   4917   5498  -2069   -803    353       O  
ATOM   1923  N   PHE B 103      36.616  47.451 350.746  1.00 28.30           N  
ANISOU 1923  N   PHE B 103     3045   3459   4249  -1102   -521    965       N  
ATOM   1924  CA  PHE B 103      36.272  46.142 350.211  1.00 28.35           C  
ANISOU 1924  CA  PHE B 103     2926   3409   4438   -999   -557   1040       C  
ATOM   1925  C   PHE B 103      36.235  46.152 348.713  1.00 32.35           C  
ANISOU 1925  C   PHE B 103     3412   3850   5028  -1030   -508    948       C  
ATOM   1926  O   PHE B 103      35.683  47.062 348.100  1.00 31.41           O  
ANISOU 1926  O   PHE B 103     3404   3678   4852  -1094   -420    928       O  
ATOM   1927  CB  PHE B 103      34.927  45.634 350.763  1.00 29.99           C  
ANISOU 1927  CB  PHE B 103     3168   3556   4670   -904   -556   1234       C  
ATOM   1928  CG  PHE B 103      35.020  45.218 352.210  1.00 32.68           C  
ANISOU 1928  CG  PHE B 103     3470   4015   4934   -853   -623   1367       C  
ATOM   1929  CD1 PHE B 103      35.591  44.002 352.566  1.00 36.89           C  
ANISOU 1929  CD1 PHE B 103     3866   4563   5587   -805   -754   1458       C  
ATOM   1930  CD2 PHE B 103      34.585  46.064 353.221  1.00 35.07           C  
ANISOU 1930  CD2 PHE B 103     3876   4422   5028   -833   -563   1397       C  
ATOM   1931  CE1 PHE B 103      35.722  43.639 353.909  1.00 38.94           C  
ANISOU 1931  CE1 PHE B 103     4074   4963   5760   -772   -824   1612       C  
ATOM   1932  CE2 PHE B 103      34.703  45.693 354.562  1.00 39.22           C  
ANISOU 1932  CE2 PHE B 103     4348   5114   5440   -785   -623   1520       C  
ATOM   1933  CZ  PHE B 103      35.273  44.484 354.898  1.00 38.11           C  
ANISOU 1933  CZ  PHE B 103     4052   5008   5420   -772   -752   1645       C  
ATOM   1934  N   CYS B 104      36.844  45.134 348.129  1.00 30.29           N  
ANISOU 1934  N   CYS B 104     3012   3603   4893   -961   -574    888       N  
ATOM   1935  CA  CYS B 104      36.846  44.907 346.703  1.00 30.72           C  
ANISOU 1935  CA  CYS B 104     3026   3637   5011   -952   -543    778       C  
ATOM   1936  C   CYS B 104      35.862  43.804 346.435  1.00 31.54           C  
ANISOU 1936  C   CYS B 104     3157   3559   5268   -855   -610    853       C  
ATOM   1937  O   CYS B 104      35.853  42.812 347.172  1.00 31.94           O  
ANISOU 1937  O   CYS B 104     3179   3529   5428   -764   -729    941       O  
ATOM   1938  CB  CYS B 104      38.238  44.549 346.203  1.00 33.83           C  
ANISOU 1938  CB  CYS B 104     3244   4205   5406   -907   -576    627       C  
ATOM   1939  SG  CYS B 104      38.418  44.689 344.409  1.00 39.03           S  
ANISOU 1939  SG  CYS B 104     3831   4970   6027   -926   -498    465       S  
ATOM   1940  N   ALA B 105      35.009  43.972 345.416  1.00 24.55           N  
ANISOU 1940  N   ALA B 105     2332   2608   4390   -898   -556    844       N  
ATOM   1941  CA  ALA B 105      34.017  42.958 345.097  1.00 23.57           C  
ANISOU 1941  CA  ALA B 105     2241   2313   4400   -858   -642    923       C  
ATOM   1942  C   ALA B 105      33.951  42.714 343.611  1.00 27.64           C  
ANISOU 1942  C   ALA B 105     2745   2819   4938   -854   -639    760       C  
ATOM   1943  O   ALA B 105      33.922  43.664 342.837  1.00 27.28           O  
ANISOU 1943  O   ALA B 105     2700   2894   4772   -934   -520    700       O  
ATOM   1944  CB  ALA B 105      32.658  43.371 345.624  1.00 23.59           C  
ANISOU 1944  CB  ALA B 105     2324   2313   4328   -871   -604   1127       C  
ATOM   1945  N   SER B 106      33.948  41.443 343.208  1.00 25.30           N  
ANISOU 1945  N   SER B 106     2450   2376   4788   -761   -787    685       N  
ATOM   1946  CA  SER B 106      33.843  41.084 341.800  1.00 26.16           C  
ANISOU 1946  CA  SER B 106     2566   2476   4899   -734   -809    496       C  
ATOM   1947  C   SER B 106      32.601  40.210 341.574  1.00 31.30           C  
ANISOU 1947  C   SER B 106     3318   2891   5681   -787   -956    600       C  
ATOM   1948  O   SER B 106      32.230  39.391 342.422  1.00 31.51           O  
ANISOU 1948  O   SER B 106     3390   2724   5857   -782  -1106    755       O  
ATOM   1949  CB  SER B 106      35.110  40.399 341.303  1.00 32.16           C  
ANISOU 1949  CB  SER B 106     3245   3300   5676   -544   -868    232       C  
ATOM   1950  OG  SER B 106      35.171  39.030 341.664  1.00 45.24           O  
ANISOU 1950  OG  SER B 106     4963   4699   7527   -396  -1076    202       O  
ATOM   1951  N   SER B 107      31.941  40.423 340.440  1.00 27.87           N  
ANISOU 1951  N   SER B 107     2911   2498   5183   -868   -922    547       N  
ATOM   1952  CA  SER B 107      30.726  39.710 340.084  1.00 28.20           C  
ANISOU 1952  CA  SER B 107     3034   2361   5319   -970  -1066    653       C  
ATOM   1953  C   SER B 107      30.750  39.328 338.618  1.00 30.85           C  
ANISOU 1953  C   SER B 107     3403   2702   5616   -944  -1125    392       C  
ATOM   1954  O   SER B 107      31.248  40.091 337.796  1.00 29.51           O  
ANISOU 1954  O   SER B 107     3162   2771   5279   -914   -976    231       O  
ATOM   1955  CB  SER B 107      29.505  40.575 340.385  1.00 31.72           C  
ANISOU 1955  CB  SER B 107     3461   2911   5680  -1126   -953    935       C  
ATOM   1956  OG  SER B 107      28.309  39.814 340.367  1.00 46.09           O  
ANISOU 1956  OG  SER B 107     5318   4602   7590  -1255  -1106   1114       O  
ATOM   1957  N   GLN B 108      30.205  38.146 338.295  1.00 27.76           N  
ANISOU 1957  N   GLN B 108     3125   2056   5367   -973  -1359    359       N  
ATOM   1958  CA  GLN B 108      30.103  37.629 336.935  1.00 28.86           C  
ANISOU 1958  CA  GLN B 108     3334   2169   5464   -951  -1460     89       C  
ATOM   1959  C   GLN B 108      29.298  38.606 336.067  1.00 30.56           C  
ANISOU 1959  C   GLN B 108     3483   2636   5491  -1116  -1312    171       C  
ATOM   1960  O   GLN B 108      29.742  38.960 334.975  1.00 30.86           O  
ANISOU 1960  O   GLN B 108     3474   2891   5359  -1058  -1221    -57       O  
ATOM   1961  CB  GLN B 108      29.452  36.240 336.956  1.00 32.78           C  
ANISOU 1961  CB  GLN B 108     4004   2280   6171  -1011  -1784     96       C  
ATOM   1962  CG  GLN B 108      30.011  35.279 335.925  1.00 52.34           C  
ANISOU 1962  CG  GLN B 108     6613   4611   8663   -831  -1959   -322       C  
ATOM   1963  CD  GLN B 108      29.506  33.884 336.184  1.00 80.24           C  
ANISOU 1963  CD  GLN B 108    10367   7669  12450   -886  -2325   -304       C  
ATOM   1964  OE1 GLN B 108      28.469  33.461 335.653  1.00 76.28           O  
ANISOU 1964  OE1 GLN B 108     9975   7025  11982  -1106  -2509   -248       O  
ATOM   1965  NE2 GLN B 108      30.211  33.147 337.037  1.00 76.23           N  
ANISOU 1965  NE2 GLN B 108     9932   6901  12133   -708  -2460   -325       N  
ATOM   1966  N   GLY B 109      28.167  39.074 336.597  1.00 25.45           N  
ANISOU 1966  N   GLY B 109     2823   2057   4791  -1197  -1264    533       N  
ATOM   1967  CA  GLY B 109      27.291  40.040 335.942  1.00 24.38           C  
ANISOU 1967  CA  GLY B 109     2655   2197   4411  -1207  -1122    685       C  
ATOM   1968  C   GLY B 109      26.671  41.048 336.897  1.00 24.71           C  
ANISOU 1968  C   GLY B 109     2636   2400   4353  -1168   -994    981       C  
ATOM   1969  O   GLY B 109      26.897  40.977 338.111  1.00 24.33           O  
ANISOU 1969  O   GLY B 109     2565   2300   4379  -1104  -1004   1080       O  
ATOM   1970  N   PRO B 110      25.862  42.004 336.386  1.00 20.01           N  
ANISOU 1970  N   PRO B 110     2079   2135   3391   -897   -925   1072       N  
ATOM   1971  CA  PRO B 110      25.252  43.007 337.286  1.00 19.06           C  
ANISOU 1971  CA  PRO B 110     1885   2198   3161   -758   -890   1221       C  
ATOM   1972  C   PRO B 110      24.148  42.471 338.214  1.00 23.04           C  
ANISOU 1972  C   PRO B 110     2258   2603   3892  -1042   -971   1533       C  
ATOM   1973  O   PRO B 110      23.717  43.191 339.114  1.00 22.20           O  
ANISOU 1973  O   PRO B 110     2059   2651   3727   -916   -927   1630       O  
ATOM   1974  CB  PRO B 110      24.662  44.036 336.317  1.00 20.15           C  
ANISOU 1974  CB  PRO B 110     1995   2461   3199   -867   -790   1274       C  
ATOM   1975  CG  PRO B 110      24.443  43.302 335.049  1.00 24.28           C  
ANISOU 1975  CG  PRO B 110     2496   2870   3859  -1253   -805   1277       C  
ATOM   1976  CD  PRO B 110      25.500  42.242 334.974  1.00 21.25           C  
ANISOU 1976  CD  PRO B 110     2236   2353   3484  -1079   -886   1026       C  
ATOM   1977  N   PHE B 111      23.681  41.227 337.985  1.00 22.34           N  
ANISOU 1977  N   PHE B 111     2196   2407   3885  -1148  -1177   1594       N  
ATOM   1978  CA  PHE B 111      22.584  40.600 338.722  1.00 23.34           C  
ANISOU 1978  CA  PHE B 111     2222   2563   4085  -1263  -1346   1878       C  
ATOM   1979  C   PHE B 111      23.045  39.410 339.538  1.00 29.22           C  
ANISOU 1979  C   PHE B 111     3005   2882   5216  -1617  -1444   2005       C  
ATOM   1980  O   PHE B 111      22.323  38.949 340.424  1.00 31.02           O  
ANISOU 1980  O   PHE B 111     3143   3114   5530  -1757  -1532   2317       O  
ATOM   1981  CB  PHE B 111      21.484  40.145 337.745  1.00 25.45           C  
ANISOU 1981  CB  PHE B 111     2477   2800   4393  -1571  -1463   2052       C  
ATOM   1982  CG  PHE B 111      20.922  41.189 336.807  1.00 25.72           C  
ANISOU 1982  CG  PHE B 111     2453   3041   4279  -1603  -1312   2083       C  
ATOM   1983  CD1 PHE B 111      20.801  42.519 337.206  1.00 26.43           C  
ANISOU 1983  CD1 PHE B 111     2422   3298   4321  -1550  -1074   2208       C  
ATOM   1984  CD2 PHE B 111      20.451  40.834 335.553  1.00 28.29           C  
ANISOU 1984  CD2 PHE B 111     2793   3298   4656  -1920  -1360   2069       C  
ATOM   1985  CE1 PHE B 111      20.264  43.480 336.348  1.00 26.43           C  
ANISOU 1985  CE1 PHE B 111     2364   3483   4195  -1551   -959   2259       C  
ATOM   1986  CE2 PHE B 111      19.903  41.797 334.699  1.00 29.28           C  
ANISOU 1986  CE2 PHE B 111     2775   3593   4756  -2152  -1174   2190       C  
ATOM   1987  CZ  PHE B 111      19.808  43.111 335.105  1.00 26.97           C  
ANISOU 1987  CZ  PHE B 111     2459   3587   4200  -1700  -1053   2224       C  
ATOM   1988  N   GLN B 112      24.221  38.887 339.229  1.00 26.73           N  
ANISOU 1988  N   GLN B 112     2819   2386   4952  -1476  -1509   1692       N  
ATOM   1989  CA  GLN B 112      24.753  37.736 339.941  1.00 27.88           C  
ANISOU 1989  CA  GLN B 112     3029   2235   5329  -1519  -1701   1688       C  
ATOM   1990  C   GLN B 112      25.333  38.198 341.302  1.00 29.19           C  
ANISOU 1990  C   GLN B 112     3128   2418   5546  -1477  -1555   1800       C  
ATOM   1991  O   GLN B 112      25.588  39.392 341.465  1.00 26.75           O  
ANISOU 1991  O   GLN B 112     2751   2395   5018  -1269  -1334   1713       O  
ATOM   1992  CB  GLN B 112      25.786  37.000 339.066  1.00 29.53           C  
ANISOU 1992  CB  GLN B 112     3406   2072   5743  -1576  -1794   1321       C  
ATOM   1993  CG  GLN B 112      25.130  36.162 337.954  1.00 43.22           C  
ANISOU 1993  CG  GLN B 112     5264   3544   7614  -1844  -2035   1221       C  
ATOM   1994  CD  GLN B 112      25.169  36.799 336.576  1.00 65.36           C  
ANISOU 1994  CD  GLN B 112     8053   6554  10226  -1804  -1908    953       C  
ATOM   1995  OE1 GLN B 112      25.614  36.184 335.605  1.00 64.58           O  
ANISOU 1995  OE1 GLN B 112     8070   6345  10124  -1698  -2011    584       O  
ATOM   1996  NE2 GLN B 112      24.663  38.020 336.432  1.00 54.93           N  
ANISOU 1996  NE2 GLN B 112     6591   5550   8731  -1874  -1691   1135       N  
ATOM   1997  N   PRO B 113      25.470  37.315 342.321  1.00 28.23           N  
ANISOU 1997  N   PRO B 113     2987   2211   5531  -1447  -1738   1932       N  
ATOM   1998  CA  PRO B 113      26.003  37.782 343.610  1.00 27.32           C  
ANISOU 1998  CA  PRO B 113     2775   2246   5359  -1317  -1618   2001       C  
ATOM   1999  C   PRO B 113      27.479  38.153 343.519  1.00 29.94           C  
ANISOU 1999  C   PRO B 113     3250   2271   5853  -1359  -1437   1799       C  
ATOM   2000  O   PRO B 113      28.201  37.637 342.661  1.00 31.12           O  
ANISOU 2000  O   PRO B 113     3485   2259   6080  -1280  -1526   1501       O  
ATOM   2001  CB  PRO B 113      25.776  36.591 344.538  1.00 30.50           C  
ANISOU 2001  CB  PRO B 113     3203   2379   6007  -1522  -1845   2310       C  
ATOM   2002  CG  PRO B 113      25.786  35.409 343.646  1.00 35.96           C  
ANISOU 2002  CG  PRO B 113     4131   2512   7021  -1770  -2087   2278       C  
ATOM   2003  CD  PRO B 113      25.178  35.864 342.356  1.00 31.93           C  
ANISOU 2003  CD  PRO B 113     3580   2241   6310  -1729  -2047   2099       C  
ATOM   2004  N   GLN B 114      27.914  39.070 344.383  1.00 26.54           N  
ANISOU 2004  N   GLN B 114     2699   2192   5192  -1125  -1286   1761       N  
ATOM   2005  CA  GLN B 114      29.296  39.537 344.398  1.00 25.59           C  
ANISOU 2005  CA  GLN B 114     2603   2077   5042   -997  -1168   1518       C  
ATOM   2006  C   GLN B 114      30.150  38.653 345.289  1.00 31.69           C  
ANISOU 2006  C   GLN B 114     3414   2603   6024  -1015  -1284   1585       C  
ATOM   2007  O   GLN B 114      29.623  37.992 346.185  1.00 32.22           O  
ANISOU 2007  O   GLN B 114     3462   2615   6165  -1081  -1404   1866       O  
ATOM   2008  CB  GLN B 114      29.381  41.007 344.848  1.00 24.80           C  
ANISOU 2008  CB  GLN B 114     2466   2233   4725   -940   -938   1520       C  
ATOM   2009  CG  GLN B 114      28.843  41.967 343.799  1.00 30.83           C  
ANISOU 2009  CG  GLN B 114     3278   2978   5458  -1121   -757   1533       C  
ATOM   2010  CD  GLN B 114      29.175  43.405 344.080  1.00 47.62           C  
ANISOU 2010  CD  GLN B 114     5420   5261   7412  -1074   -560   1492       C  
ATOM   2011  OE1 GLN B 114      28.611  44.025 344.985  1.00 44.76           O  
ANISOU 2011  OE1 GLN B 114     5059   4993   6954  -1044   -483   1660       O  
ATOM   2012  NE2 GLN B 114      30.061  43.984 343.270  1.00 35.51           N  
ANISOU 2012  NE2 GLN B 114     3902   3765   5823  -1070   -487   1270       N  
ATOM   2013  N   HIS B 115      31.471  38.620 345.004  1.00 29.51           N  
ANISOU 2013  N   HIS B 115     3136   2313   5761   -864  -1274   1306       N  
ATOM   2014  CA  HIS B 115      32.501  37.891 345.749  1.00 30.70           C  
ANISOU 2014  CA  HIS B 115     3268   2380   6018   -730  -1394   1284       C  
ATOM   2015  C   HIS B 115      33.425  38.949 346.335  1.00 33.09           C  
ANISOU 2015  C   HIS B 115     3478   2946   6148   -674  -1212   1218       C  
ATOM   2016  O   HIS B 115      34.059  39.694 345.587  1.00 31.06           O  
ANISOU 2016  O   HIS B 115     3185   2836   5779   -640  -1081    992       O  
ATOM   2017  CB  HIS B 115      33.227  36.866 344.851  1.00 33.59           C  
ANISOU 2017  CB  HIS B 115     3694   2534   6535   -568  -1558   1013       C  
ATOM   2018  CG  HIS B 115      32.284  35.876 344.241  1.00 39.04           C  
ANISOU 2018  CG  HIS B 115     4520   2925   7389   -653  -1771   1049       C  
ATOM   2019  ND1 HIS B 115      31.693  36.108 343.010  1.00 40.73           N  
ANISOU 2019  ND1 HIS B 115     4780   3157   7537   -732  -1728    907       N  
ATOM   2020  CD2 HIS B 115      31.780  34.731 344.754  1.00 43.50           C  
ANISOU 2020  CD2 HIS B 115     5182   3179   8168   -709  -2041   1246       C  
ATOM   2021  CE1 HIS B 115      30.891  35.076 342.791  1.00 42.34           C  
ANISOU 2021  CE1 HIS B 115     5114   3060   7914   -833  -1978    990       C  
ATOM   2022  NE2 HIS B 115      30.902  34.226 343.814  1.00 44.47           N  
ANISOU 2022  NE2 HIS B 115     5426   3107   8366   -835  -2181   1204       N  
ATOM   2023  N   PHE B 116      33.413  39.079 347.673  1.00 30.56           N  
ANISOU 2023  N   PHE B 116     3117   2711   5784   -698  -1211   1437       N  
ATOM   2024  CA  PHE B 116      34.135  40.118 348.411  1.00 30.02           C  
ANISOU 2024  CA  PHE B 116     2989   2883   5535   -686  -1069   1402       C  
ATOM   2025  C   PHE B 116      35.530  39.722 348.911  1.00 35.68           C  
ANISOU 2025  C   PHE B 116     3620   3653   6286   -561  -1145   1309       C  
ATOM   2026  O   PHE B 116      35.759  38.589 349.338  1.00 37.19           O  
ANISOU 2026  O   PHE B 116     3797   3690   6642   -466  -1325   1390       O  
ATOM   2027  CB  PHE B 116      33.289  40.563 349.617  1.00 31.71           C  
ANISOU 2027  CB  PHE B 116     3203   3217   5629   -760  -1021   1669       C  
ATOM   2028  CG  PHE B 116      32.152  41.492 349.252  1.00 32.41           C  
ANISOU 2028  CG  PHE B 116     3345   3380   5589   -838   -871   1719       C  
ATOM   2029  CD1 PHE B 116      30.918  40.986 348.849  1.00 36.21           C  
ANISOU 2029  CD1 PHE B 116     3835   3780   6144   -907   -920   1893       C  
ATOM   2030  CD2 PHE B 116      32.319  42.874 349.295  1.00 33.05           C  
ANISOU 2030  CD2 PHE B 116     3471   3607   5478   -844   -701   1603       C  
ATOM   2031  CE1 PHE B 116      29.875  41.848 348.486  1.00 35.96           C  
ANISOU 2031  CE1 PHE B 116     3825   3854   5986   -947   -780   1953       C  
ATOM   2032  CE2 PHE B 116      31.274  43.735 348.941  1.00 34.87           C  
ANISOU 2032  CE2 PHE B 116     3762   3885   5600   -869   -575   1650       C  
ATOM   2033  CZ  PHE B 116      30.062  43.217 348.539  1.00 33.38           C  
ANISOU 2033  CZ  PHE B 116     3551   3657   5476   -904   -604   1827       C  
ATOM   2034  N   GLY B 117      36.427  40.702 348.906  1.00 31.95           N  
ANISOU 2034  N   GLY B 117     3088   3398   5652   -574  -1020   1166       N  
ATOM   2035  CA  GLY B 117      37.780  40.559 349.426  1.00 33.64           C  
ANISOU 2035  CA  GLY B 117     3180   3756   5845   -483  -1069   1095       C  
ATOM   2036  C   GLY B 117      37.797  40.593 350.945  1.00 39.75           C  
ANISOU 2036  C   GLY B 117     3928   4620   6554   -509  -1120   1305       C  
ATOM   2037  O   GLY B 117      36.773  40.890 351.573  1.00 39.26           O  
ANISOU 2037  O   GLY B 117     3940   4547   6430   -592  -1092   1487       O  
ATOM   2038  N   ASP B 118      38.961  40.299 351.555  1.00 38.11           N  
ANISOU 2038  N   ASP B 118     3593   4553   6333   -427  -1194   1288       N  
ATOM   2039  CA  ASP B 118      39.099  40.254 353.013  1.00 39.15           C  
ANISOU 2039  CA  ASP B 118     3679   4814   6384   -445  -1262   1486       C  
ATOM   2040  C   ASP B 118      39.091  41.656 353.653  1.00 43.20           C  
ANISOU 2040  C   ASP B 118     4237   5544   6632   -605  -1135   1459       C  
ATOM   2041  O   ASP B 118      38.982  41.776 354.876  1.00 43.81           O  
ANISOU 2041  O   ASP B 118     4311   5745   6588   -635  -1168   1614       O  
ATOM   2042  CB  ASP B 118      40.368  39.480 353.410  1.00 43.31           C  
ANISOU 2042  CB  ASP B 118     4042   5436   6978   -294  -1394   1483       C  
ATOM   2043  CG  ASP B 118      40.275  37.956 353.301  1.00 58.17           C  
ANISOU 2043  CG  ASP B 118     5921   7056   9124   -104  -1588   1596       C  
ATOM   2044  OD1 ASP B 118      39.194  37.443 352.908  1.00 58.11           O  
ANISOU 2044  OD1 ASP B 118     6045   6774   9260   -125  -1636   1674       O  
ATOM   2045  OD2 ASP B 118      41.279  37.274 353.624  1.00 66.94           O  
ANISOU 2045  OD2 ASP B 118     6904   8228  10301     63  -1710   1617       O  
ATOM   2046  N   GLY B 119      39.167  42.692 352.825  1.00 39.07           N  
ANISOU 2046  N   GLY B 119     3769   5059   6017   -705  -1009   1266       N  
ATOM   2047  CA  GLY B 119      39.169  44.076 353.279  1.00 38.39           C  
ANISOU 2047  CA  GLY B 119     3783   5100   5705   -857   -920   1204       C  
ATOM   2048  C   GLY B 119      40.547  44.662 353.492  1.00 42.73           C  
ANISOU 2048  C   GLY B 119     4236   5867   6131   -960   -950   1089       C  
ATOM   2049  O   GLY B 119      41.537  43.924 353.569  1.00 43.53           O  
ANISOU 2049  O   GLY B 119     4149   6094   6296   -882  -1040   1099       O  
ATOM   2050  N   THR B 120      40.611  46.006 353.578  1.00 38.59           N  
ANISOU 2050  N   THR B 120     3845   5387   5431  -1137   -892    989       N  
ATOM   2051  CA  THR B 120      41.837  46.767 353.825  1.00 39.70           C  
ANISOU 2051  CA  THR B 120     3927   5730   5429  -1317   -945    899       C  
ATOM   2052  C   THR B 120      41.534  47.890 354.811  1.00 44.16           C  
ANISOU 2052  C   THR B 120     4711   6286   5781  -1448   -957    859       C  
ATOM   2053  O   THR B 120      40.643  48.700 354.556  1.00 43.30           O  
ANISOU 2053  O   THR B 120     4825   5996   5630  -1474   -877    801       O  
ATOM   2054  CB  THR B 120      42.453  47.302 352.515  1.00 47.54           C  
ANISOU 2054  CB  THR B 120     4856   6763   6445  -1449   -895    786       C  
ATOM   2055  OG1 THR B 120      42.620  46.231 351.592  1.00 47.23           O  
ANISOU 2055  OG1 THR B 120     4645   6724   6576  -1272   -872    781       O  
ATOM   2056  CG2 THR B 120      43.800  47.965 352.732  1.00 48.08           C  
ANISOU 2056  CG2 THR B 120     4793   7098   6376  -1665   -977    747       C  
ATOM   2057  N   ARG B 121      42.272  47.941 355.930  1.00 42.18           N  
ANISOU 2057  N   ARG B 121     4404   6237   5386  -1508  -1066    880       N  
ATOM   2058  CA  ARG B 121      42.105  48.991 356.935  1.00 43.19           C  
ANISOU 2058  CA  ARG B 121     4754   6377   5278  -1620  -1107    798       C  
ATOM   2059  C   ARG B 121      43.103  50.121 356.657  1.00 47.96           C  
ANISOU 2059  C   ARG B 121     5419   7024   5779  -1919  -1188    663       C  
ATOM   2060  O   ARG B 121      44.302  49.864 356.511  1.00 48.37           O  
ANISOU 2060  O   ARG B 121     5236   7303   5840  -2043  -1271    694       O  
ATOM   2061  CB  ARG B 121      42.266  48.429 358.351  1.00 45.56           C  
ANISOU 2061  CB  ARG B 121     4970   6894   5446  -1538  -1197    902       C  
ATOM   2062  CG  ARG B 121      41.548  49.258 359.404  1.00 61.18           C  
ANISOU 2062  CG  ARG B 121     7205   8875   7165  -1538  -1204    814       C  
ATOM   2063  CD  ARG B 121      41.692  48.639 360.777  1.00 77.48           C  
ANISOU 2063  CD  ARG B 121     9151  11212   9077  -1447  -1283    947       C  
ATOM   2064  NE  ARG B 121      41.415  49.610 361.834  1.00 90.24           N  
ANISOU 2064  NE  ARG B 121    10999  12910  10378  -1469  -1317    805       N  
ATOM   2065  CZ  ARG B 121      40.230  49.774 362.409  1.00106.39           C  
ANISOU 2065  CZ  ARG B 121    13186  14957  12280  -1276  -1225    812       C  
ATOM   2066  NH1 ARG B 121      39.195  49.027 362.038  1.00 91.77           N  
ANISOU 2066  NH1 ARG B 121    11253  13034  10582  -1091  -1101    991       N  
ATOM   2067  NH2 ARG B 121      40.068  50.681 363.361  1.00 97.34           N  
ANISOU 2067  NH2 ARG B 121    12258  13909  10818  -1262  -1264    638       N  
ATOM   2068  N   LEU B 122      42.593  51.363 356.536  1.00 44.74           N  
ANISOU 2068  N   LEU B 122     5322   6397   5280  -2033  -1173    530       N  
ATOM   2069  CA  LEU B 122      43.390  52.553 356.210  1.00 46.25           C  
ANISOU 2069  CA  LEU B 122     5638   6545   5390  -2363  -1278    423       C  
ATOM   2070  C   LEU B 122      43.408  53.547 357.372  1.00 51.79           C  
ANISOU 2070  C   LEU B 122     6635   7186   5855  -2474  -1410    277       C  
ATOM   2071  O   LEU B 122      42.352  53.891 357.900  1.00 51.42           O  
ANISOU 2071  O   LEU B 122     6837   6979   5720  -2275  -1354    196       O  
ATOM   2072  CB  LEU B 122      42.844  53.229 354.927  1.00 45.25           C  
ANISOU 2072  CB  LEU B 122     5663   6150   5380  -2422  -1189    393       C  
ATOM   2073  CG  LEU B 122      43.348  52.696 353.596  1.00 49.40           C  
ANISOU 2073  CG  LEU B 122     5910   6791   6070  -2471  -1120    486       C  
ATOM   2074  CD1 LEU B 122      42.887  51.273 353.370  1.00 48.06           C  
ANISOU 2074  CD1 LEU B 122     5519   6693   6048  -2158  -1007    572       C  
ATOM   2075  CD2 LEU B 122      42.878  53.566 352.460  1.00 51.59           C  
ANISOU 2075  CD2 LEU B 122     6362   6832   6408  -2585  -1063    469       C  
ATOM   2076  N   SER B 123      44.612  53.995 357.772  1.00 50.12           N  
ANISOU 2076  N   SER B 123     6387   7132   5524  -2787  -1592    241       N  
ATOM   2077  CA  SER B 123      44.801  54.962 358.854  1.00 52.81           C  
ANISOU 2077  CA  SER B 123     7024   7416   5625  -2944  -1766     72       C  
ATOM   2078  C   SER B 123      45.517  56.217 358.347  1.00 58.87           C  
ANISOU 2078  C   SER B 123     7979   8022   6369  -3370  -1940     -4       C  
ATOM   2079  O   SER B 123      46.732  56.202 358.124  1.00 59.74           O  
ANISOU 2079  O   SER B 123     7844   8385   6468  -3683  -2065     93       O  
ATOM   2080  CB  SER B 123      45.569  54.340 360.018  1.00 57.94           C  
ANISOU 2080  CB  SER B 123     7465   8440   6112  -2955  -1877    118       C  
ATOM   2081  OG  SER B 123      44.715  53.533 360.810  1.00 65.87           O  
ANISOU 2081  OG  SER B 123     8406   9539   7084  -2590  -1758    179       O  
ATOM   2082  N   ILE B 124      44.745  57.296 358.143  1.00 56.20           N  
ANISOU 2082  N   ILE B 124     8064   7267   6023  -3380  -1957   -152       N  
ATOM   2083  CA  ILE B 124      45.264  58.580 357.689  1.00 58.89           C  
ANISOU 2083  CA  ILE B 124     8666   7353   6358  -3790  -2154   -212       C  
ATOM   2084  C   ILE B 124      45.428  59.482 358.916  1.00 67.06           C  
ANISOU 2084  C   ILE B 124    10081   8247   7150  -3926  -2395   -448       C  
ATOM   2085  O   ILE B 124      44.444  59.847 359.568  1.00 67.11           O  
ANISOU 2085  O   ILE B 124    10440   8013   7047  -3633  -2365   -654       O  
ATOM   2086  CB  ILE B 124      44.377  59.205 356.589  1.00 60.88           C  
ANISOU 2086  CB  ILE B 124     9158   7200   6772  -3719  -2054   -209       C  
ATOM   2087  N   LEU B 125      46.689  59.784 359.255  1.00 66.77           N  
ANISOU 2087  N   LEU B 125     9949   8412   7009  -4356  -2636   -420       N  
ATOM   2088  CA  LEU B 125      47.064  60.592 360.413  1.00 70.88           C  
ANISOU 2088  CA  LEU B 125    10801   8848   7281  -4562  -2913   -643       C  
ATOM   2089  C   LEU B 125      47.642  61.945 359.999  1.00 79.47           C  
ANISOU 2089  C   LEU B 125    12235   9578   8384  -5071  -3207   -697       C  
ATOM   2090  O   LEU B 125      48.448  62.007 359.068  1.00 79.33           O  
ANISOU 2090  O   LEU B 125    11975   9663   8504  -5438  -3255   -463       O  
ATOM   2091  CB  LEU B 125      48.102  59.835 361.258  1.00 71.78           C  
ANISOU 2091  CB  LEU B 125    10534   9500   7238  -4701  -3009   -551       C  
ATOM   2092  CG  LEU B 125      47.625  58.580 361.975  1.00 73.64           C  
ANISOU 2092  CG  LEU B 125    10508  10069   7404  -4246  -2809   -512       C  
ATOM   2093  CD1 LEU B 125      48.112  57.333 361.273  1.00 70.59           C  
ANISOU 2093  CD1 LEU B 125     9560  10053   7210  -4151  -2631   -214       C  
ATOM   2094  CD2 LEU B 125      48.140  58.560 363.373  1.00 79.32           C  
ANISOU 2094  CD2 LEU B 125    11241  11070   7827  -4340  -3004   -618       C  
ATOM   2095  N   GLU B 126      47.251  63.023 360.705  1.00 80.08           N  
ANISOU 2095  N   GLU B 126    12877   9246   8304  -5096  -3420  -1001       N  
ATOM   2096  CA  GLU B 126      47.772  64.367 360.450  1.00 84.86           C  
ANISOU 2096  CA  GLU B 126    13900   9425   8919  -5597  -3765  -1077       C  
ATOM   2097  C   GLU B 126      49.249  64.410 360.861  1.00 93.12           C  
ANISOU 2097  C   GLU B 126    14722  10825   9833  -6173  -4057   -969       C  
ATOM   2098  O   GLU B 126      50.079  64.963 360.136  1.00 94.95           O  
ANISOU 2098  O   GLU B 126    14939  10982  10156  -6720  -4274   -789       O  
ATOM   2099  CB  GLU B 126      46.946  65.424 361.196  1.00 89.57           C  
ANISOU 2099  CB  GLU B 126    15192   9467   9372  -5383  -3920  -1479       C  
ATOM   2100  N   ASP B 127      49.563  63.763 362.007  1.00 90.72           N  
ANISOU 2100  N   ASP B 127    14204  10959   9308  -6050  -4056  -1041       N  
ATOM   2101  CA  ASP B 127      50.893  63.598 362.598  1.00 93.60           C  
ANISOU 2101  CA  ASP B 127    14284  11775   9506  -6507  -4302   -936       C  
ATOM   2102  C   ASP B 127      51.138  62.094 362.820  1.00 94.53           C  
ANISOU 2102  C   ASP B 127    13763  12550   9606  -6216  -4046   -723       C  
ATOM   2103  O   ASP B 127      50.280  61.405 363.389  1.00 91.61           O  
ANISOU 2103  O   ASP B 127    13381  12259   9168  -5698  -3831   -830       O  
ATOM   2104  CB  ASP B 127      51.003  64.395 363.916  1.00100.26           C  
ANISOU 2104  CB  ASP B 127    15614  12432  10048  -6649  -4633  -1290       C  
ATOM   2105  CG  ASP B 127      52.389  64.928 364.256  1.00114.34           C  
ANISOU 2105  CG  ASP B 127    17327  14429  11687  -7344  -5036  -1210       C  
ATOM   2106  OD1 ASP B 127      53.005  65.588 363.387  1.00116.88           O  
ANISOU 2106  OD1 ASP B 127    17659  14593  12156  -7872  -5229  -1018       O  
ATOM   2107  OD2 ASP B 127      52.812  64.775 365.422  1.00121.28           O  
ANISOU 2107  OD2 ASP B 127    18169  15624  12289  -7384  -5183  -1340       O  
ATOM   2108  N   LEU B 128      52.289  61.584 362.332  1.00 91.21           N  
ANISOU 2108  N   LEU B 128    12805  12602   9250  -6536  -4072   -403       N  
ATOM   2109  CA  LEU B 128      52.670  60.168 362.427  1.00 88.07           C  
ANISOU 2109  CA  LEU B 128    11788  12807   8869  -6272  -3861   -176       C  
ATOM   2110  C   LEU B 128      53.379  59.836 363.763  1.00 93.79           C  
ANISOU 2110  C   LEU B 128    12357  13963   9316  -6344  -4036   -210       C  
ATOM   2111  O   LEU B 128      53.763  58.684 363.980  1.00 91.18           O  
ANISOU 2111  O   LEU B 128    11535  14121   8986  -6116  -3898    -17       O  
ATOM   2112  CB  LEU B 128      53.560  59.776 361.236  1.00 87.59           C  
ANISOU 2112  CB  LEU B 128    11212  13098   8972  -6528  -3808    164       C  
ATOM   2113  N   LYS B 129      53.515  60.835 364.666  1.00 94.62           N  
ANISOU 2113  N   LYS B 129    12898  13872   9180  -6637  -4349   -462       N  
ATOM   2114  CA  LYS B 129      54.125  60.681 365.990  1.00 97.41           C  
ANISOU 2114  CA  LYS B 129    13171  14615   9225  -6742  -4553   -530       C  
ATOM   2115  C   LYS B 129      53.227  59.845 366.914  1.00 99.47           C  
ANISOU 2115  C   LYS B 129    13439  14994   9361  -6141  -4334   -651       C  
ATOM   2116  O   LYS B 129      53.700  59.320 367.924  1.00 99.88           O  
ANISOU 2116  O   LYS B 129    13263  15500   9187  -6122  -4418   -609       O  
ATOM   2117  CB  LYS B 129      54.399  62.056 366.614  1.00105.31           C  
ANISOU 2117  CB  LYS B 129    14713  15299  10002  -7221  -4966   -813       C  
ATOM   2118  N   ASN B 130      51.937  59.707 366.543  1.00 93.83           N  
ANISOU 2118  N   ASN B 130    12954  13910   8786  -5669  -4060   -763       N  
ATOM   2119  CA  ASN B 130      50.923  58.948 367.272  1.00 91.99           C  
ANISOU 2119  CA  ASN B 130    12728  13773   8452  -5104  -3833   -837       C  
ATOM   2120  C   ASN B 130      51.081  57.418 367.091  1.00 93.51           C  
ANISOU 2120  C   ASN B 130    12319  14414   8797  -4808  -3590   -489       C  
ATOM   2121  O   ASN B 130      50.482  56.664 367.862  1.00 92.07           O  
ANISOU 2121  O   ASN B 130    12057  14421   8506  -4420  -3454   -470       O  
ATOM   2122  CB  ASN B 130      49.526  59.390 366.832  1.00 90.29           C  
ANISOU 2122  CB  ASN B 130    12936  13030   8338  -4741  -3641  -1042       C  
ATOM   2123  N   VAL B 131      51.894  56.966 366.103  1.00 89.35           N  
ANISOU 2123  N   VAL B 131    11376  14066   8505  -4983  -3551   -214       N  
ATOM   2124  CA  VAL B 131      52.123  55.540 365.811  1.00 86.59           C  
ANISOU 2124  CA  VAL B 131    10486  14088   8328  -4692  -3351     93       C  
ATOM   2125  C   VAL B 131      52.993  54.890 366.916  1.00 94.09           C  
ANISOU 2125  C   VAL B 131    11096  15593   9060  -4739  -3500    235       C  
ATOM   2126  O   VAL B 131      54.074  55.396 367.225  1.00 97.31           O  
ANISOU 2126  O   VAL B 131    11416  16250   9306  -5170  -3759    250       O  
ATOM   2127  CB  VAL B 131      52.723  55.303 364.393  1.00 88.67           C  
ANISOU 2127  CB  VAL B 131    10424  14391   8874  -4816  -3261    301       C  
ATOM   2128  CG1 VAL B 131      52.792  53.815 364.058  1.00 85.54           C  
ANISOU 2128  CG1 VAL B 131     9549  14284   8668  -4424  -3051    554       C  
ATOM   2129  CG2 VAL B 131      51.915  56.031 363.327  1.00 86.73           C  
ANISOU 2129  CG2 VAL B 131    10518  13622   8812  -4820  -3146    178       C  
ATOM   2130  N   PHE B 132      52.496  53.771 367.508  1.00 89.65           N  
ANISOU 2130  N   PHE B 132    10342  15227   8493  -4314  -3353    364       N  
ATOM   2131  CA  PHE B 132      53.163  53.007 368.571  1.00 91.81           C  
ANISOU 2131  CA  PHE B 132    10284  16023   8578  -4281  -3471    542       C  
ATOM   2132  C   PHE B 132      52.841  51.493 368.504  1.00 94.01           C  
ANISOU 2132  C   PHE B 132    10196  16466   9059  -3822  -3270    832       C  
ATOM   2133  O   PHE B 132      51.676  51.139 368.315  1.00 90.78           O  
ANISOU 2133  O   PHE B 132     9942  15771   8778  -3486  -3065    813       O  
ATOM   2134  CB  PHE B 132      52.774  53.551 369.958  1.00 96.44           C  
ANISOU 2134  CB  PHE B 132    11192  16673   8776  -4310  -3615    325       C  
ATOM   2135  CG  PHE B 132      53.421  54.865 370.321  1.00102.23           C  
ANISOU 2135  CG  PHE B 132    12228  17358   9258  -4804  -3913     68       C  
ATOM   2136  CD1 PHE B 132      54.730  54.910 370.792  1.00108.93           C  
ANISOU 2136  CD1 PHE B 132    12805  18651   9931  -5187  -4179    183       C  
ATOM   2137  CD2 PHE B 132      52.722  56.059 370.199  1.00105.25           C  
ANISOU 2137  CD2 PHE B 132    13175  17237   9577  -4889  -3951   -283       C  
ATOM   2138  CE1 PHE B 132      55.331  56.127 371.121  1.00114.22           C  
ANISOU 2138  CE1 PHE B 132    13773  19254  10373  -5696  -4494    -45       C  
ATOM   2139  CE2 PHE B 132      53.324  57.277 370.525  1.00112.60           C  
ANISOU 2139  CE2 PHE B 132    14434  18054  10294  -5365  -4270   -527       C  
ATOM   2140  CZ  PHE B 132      54.623  57.303 370.989  1.00114.25           C  
ANISOU 2140  CZ  PHE B 132    14378  18699  10334  -5788  -4548   -406       C  
ATOM   2141  N   PRO B 133      53.841  50.588 368.691  1.00 92.73           N  
ANISOU 2141  N   PRO B 133     9555  16754   8923  -3800  -3347   1112       N  
ATOM   2142  CA  PRO B 133      53.551  49.139 368.654  1.00 91.00           C  
ANISOU 2142  CA  PRO B 133     9033  16627   8914  -3360  -3201   1387       C  
ATOM   2143  C   PRO B 133      52.922  48.634 369.969  1.00 97.45           C  
ANISOU 2143  C   PRO B 133     9905  17597   9524  -3146  -3221   1472       C  
ATOM   2144  O   PRO B 133      52.958  49.371 370.957  1.00100.00           O  
ANISOU 2144  O   PRO B 133    10418  18080   9497  -3350  -3370   1320       O  
ATOM   2145  CB  PRO B 133      54.935  48.504 368.410  1.00 94.42           C  
ANISOU 2145  CB  PRO B 133     8956  17499   9419  -3417  -3309   1633       C  
ATOM   2146  CG  PRO B 133      55.903  49.642 368.266  1.00101.47           C  
ANISOU 2146  CG  PRO B 133     9861  18562  10132  -3925  -3496   1508       C  
ATOM   2147  CD  PRO B 133      55.275  50.821 368.928  1.00 97.96           C  
ANISOU 2147  CD  PRO B 133     9925  17863   9432  -4167  -3585   1207       C  
ATOM   2148  N   PRO B 134      52.355  47.400 370.044  1.00 93.06           N  
ANISOU 2148  N   PRO B 134     9192  17013   9153  -2757  -3096   1718       N  
ATOM   2149  CA  PRO B 134      51.736  46.963 371.306  1.00 94.33           C  
ANISOU 2149  CA  PRO B 134     9386  17366   9087  -2594  -3123   1843       C  
ATOM   2150  C   PRO B 134      52.685  46.264 372.274  1.00102.19           C  
ANISOU 2150  C   PRO B 134    10017  18883   9928  -2604  -3315   2125       C  
ATOM   2151  O   PRO B 134      53.554  45.495 371.861  1.00101.63           O  
ANISOU 2151  O   PRO B 134     9587  18963  10065  -2532  -3366   2346       O  
ATOM   2152  CB  PRO B 134      50.639  45.995 370.852  1.00 93.09           C  
ANISOU 2152  CB  PRO B 134     9237  16910   9224  -2227  -2926   2016       C  
ATOM   2153  CG  PRO B 134      50.994  45.598 369.452  1.00 95.37           C  
ANISOU 2153  CG  PRO B 134     9365  16963   9909  -2145  -2846   2058       C  
ATOM   2154  CD  PRO B 134      52.187  46.377 368.991  1.00 92.07           C  
ANISOU 2154  CD  PRO B 134     8880  16666   9436  -2462  -2942   1888       C  
ATOM   2155  N   GLU B 135      52.482  46.519 373.578  1.00102.87           N  
ANISOU 2155  N   GLU B 135    10191  19268   9628  -2661  -3418   2119       N  
ATOM   2156  CA  GLU B 135      53.245  45.902 374.662  1.00106.84           C  
ANISOU 2156  CA  GLU B 135    10371  20302   9921  -2671  -3607   2402       C  
ATOM   2157  C   GLU B 135      52.517  44.621 375.070  1.00111.29           C  
ANISOU 2157  C   GLU B 135    10786  20887  10613  -2311  -3529   2774       C  
ATOM   2158  O   GLU B 135      51.479  44.674 375.737  1.00111.11           O  
ANISOU 2158  O   GLU B 135    10952  20879  10387  -2213  -3457   2769       O  
ATOM   2159  CB  GLU B 135      53.425  46.877 375.840  1.00111.83           C  
ANISOU 2159  CB  GLU B 135    11185  21271  10033  -2950  -3781   2183       C  
ATOM   2160  N   VAL B 136      53.034  43.473 374.603  1.00107.95           N  
ANISOU 2160  N   VAL B 136    10032  20448  10536  -2103  -3546   3098       N  
ATOM   2161  CA  VAL B 136      52.436  42.156 374.818  1.00107.46           C  
ANISOU 2161  CA  VAL B 136     9833  20312  10686  -1777  -3513   3489       C  
ATOM   2162  C   VAL B 136      53.028  41.492 376.073  1.00115.47           C  
ANISOU 2162  C   VAL B 136    10551  21851  11470  -1755  -3717   3855       C  
ATOM   2163  O   VAL B 136      54.249  41.373 376.209  1.00117.40           O  
ANISOU 2163  O   VAL B 136    10510  22421  11675  -1831  -3881   3950       O  
ATOM   2164  CB  VAL B 136      52.581  41.260 373.554  1.00109.13           C  
ANISOU 2164  CB  VAL B 136     9909  20136  11418  -1526  -3439   3609       C  
ATOM   2165  CG1 VAL B 136      51.882  39.914 373.732  1.00108.76           C  
ANISOU 2165  CG1 VAL B 136     9795  19909  11621  -1219  -3437   3999       C  
ATOM   2166  CG2 VAL B 136      52.042  41.973 372.317  1.00105.33           C  
ANISOU 2166  CG2 VAL B 136     9698  19199  11124  -1577  -3247   3250       C  
ATOM   2167  N   ALA B 137      52.132  41.072 376.985  1.00113.15           N  
ANISOU 2167  N   ALA B 137    10307  21677  11009  -1654  -3707   4083       N  
ATOM   2168  CA  ALA B 137      52.437  40.383 378.240  1.00116.83           C  
ANISOU 2168  CA  ALA B 137    10513  22638  11239  -1620  -3887   4487       C  
ATOM   2169  C   ALA B 137      51.356  39.337 378.527  1.00120.55           C  
ANISOU 2169  C   ALA B 137    10975  22976  11852  -1392  -3836   4887       C  
ATOM   2170  O   ALA B 137      50.165  39.655 378.480  1.00118.29           O  
ANISOU 2170  O   ALA B 137    10937  22522  11486  -1379  -3671   4770       O  
ATOM   2171  CB  ALA B 137      52.538  41.383 379.385  1.00120.35           C  
ANISOU 2171  CB  ALA B 137    11053  23581  11092  -1877  -3970   4279       C  
ATOM   2172  N   VAL B 138      51.771  38.086 378.788  1.00119.42           N  
ANISOU 2172  N   VAL B 138    10542  22896  11935  -1212  -3990   5376       N  
ATOM   2173  CA  VAL B 138      50.858  36.973 379.056  1.00119.83           C  
ANISOU 2173  CA  VAL B 138    10561  22798  12170  -1033  -4003   5839       C  
ATOM   2174  C   VAL B 138      50.761  36.745 380.574  1.00128.47           C  
ANISOU 2174  C   VAL B 138    11486  24505  12821  -1109  -4141   6208       C  
ATOM   2175  O   VAL B 138      51.784  36.585 381.244  1.00131.09           O  
ANISOU 2175  O   VAL B 138    11565  25263  12979  -1150  -4332   6374       O  
ATOM   2176  CB  VAL B 138      51.273  35.682 378.288  1.00123.67           C  
ANISOU 2176  CB  VAL B 138    10893  22869  13228   -766  -4111   6152       C  
ATOM   2177  CG1 VAL B 138      50.384  34.496 378.652  1.00124.64           C  
ANISOU 2177  CG1 VAL B 138    10999  22809  13549   -633  -4184   6677       C  
ATOM   2178  CG2 VAL B 138      51.247  35.910 376.780  1.00119.72           C  
ANISOU 2178  CG2 VAL B 138    10562  21810  13116   -679  -3959   5771       C  
ATOM   2179  N   PHE B 139      49.517  36.741 381.099  1.00125.90           N  
ANISOU 2179  N   PHE B 139    11276  24266  12292  -1125  -4040   6346       N  
ATOM   2180  CA  PHE B 139      49.203  36.509 382.509  1.00129.94           C  
ANISOU 2180  CA  PHE B 139    11628  25393  12351  -1188  -4138   6720       C  
ATOM   2181  C   PHE B 139      48.973  35.013 382.755  1.00137.30           C  
ANISOU 2181  C   PHE B 139    12344  26234  13590  -1053  -4297   7421       C  
ATOM   2182  O   PHE B 139      48.175  34.390 382.048  1.00134.85           O  
ANISOU 2182  O   PHE B 139    12140  25424  13674   -955  -4233   7582       O  
ATOM   2183  CB  PHE B 139      47.981  37.334 382.943  1.00131.14           C  
ANISOU 2183  CB  PHE B 139    11993  25765  12069  -1259  -3936   6494       C  
ATOM   2184  N   GLU B 140      49.695  34.440 383.745  1.00138.72           N  
ANISOU 2184  N   GLU B 140    12230  26880  13597  -1061  -4531   7847       N  
ATOM   2185  CA  GLU B 140      49.629  33.021 384.118  1.00141.75           C  
ANISOU 2185  CA  GLU B 140    12397  27213  14247   -947  -4743   8566       C  
ATOM   2186  C   GLU B 140      48.255  32.648 384.721  1.00147.16           C  
ANISOU 2186  C   GLU B 140    13099  28062  14753  -1018  -4687   8965       C  
ATOM   2187  O   GLU B 140      47.680  33.467 385.443  1.00146.90           O  
ANISOU 2187  O   GLU B 140    13107  28543  14165  -1146  -4546   8786       O  
ATOM   2188  CB  GLU B 140      50.754  32.669 385.106  1.00147.67           C  
ANISOU 2188  CB  GLU B 140    12822  28518  14770   -956  -5000   8901       C  
ATOM   2189  N   PRO B 141      47.719  31.425 384.449  1.00144.79           N  
ANISOU 2189  N   PRO B 141    12768  27349  14898   -938  -4806   9506       N  
ATOM   2190  CA  PRO B 141      46.405  31.054 385.011  1.00146.15           C  
ANISOU 2190  CA  PRO B 141    12918  27718  14894  -1051  -4764   9941       C  
ATOM   2191  C   PRO B 141      46.421  30.883 386.535  1.00155.20           C  
ANISOU 2191  C   PRO B 141    13778  29709  15484  -1171  -4892  10429       C  
ATOM   2192  O   PRO B 141      47.403  30.394 387.100  1.00154.63           O  
ANISOU 2192  O   PRO B 141    13833  29414  15504   -991  -5046  10267       O  
ATOM   2193  CB  PRO B 141      46.079  29.731 384.313  1.00148.09           C  
ANISOU 2193  CB  PRO B 141    13204  27257  15805   -966  -4937  10412       C  
ATOM   2194  CG  PRO B 141      47.399  29.162 383.938  1.00153.44           C  
ANISOU 2194  CG  PRO B 141    13809  27614  16876   -772  -5158  10440       C  
ATOM   2195  CD  PRO B 141      48.261  30.341 383.599  1.00146.33           C  
ANISOU 2195  CD  PRO B 141    12960  26870  15768   -740  -4996   9733       C  
ATOM   2196  N   SER B 142      45.318  31.293 387.188  1.00152.56           N  
ANISOU 2196  N   SER B 142    13454  29827  14684  -1280  -4723  10472       N  
ATOM   2197  CA  SER B 142      45.130  31.232 388.639  1.00152.62           C  
ANISOU 2197  CA  SER B 142    13750  29939  14299  -1166  -4678  10189       C  
ATOM   2198  C   SER B 142      44.906  29.800 389.140  1.00156.04           C  
ANISOU 2198  C   SER B 142    14480  29686  15121   -997  -4822  10380       C  
ATOM   2199  O   SER B 142      44.294  28.986 388.444  1.00155.07           O  
ANISOU 2199  O   SER B 142    14359  29122  15440  -1022  -4882  10762       O  
ATOM   2200  CB  SER B 142      43.952  32.107 389.055  1.00154.91           C  
ANISOU 2200  CB  SER B 142    14229  30516  14114  -1182  -4383   9826       C  
ATOM   2201  N   GLU B 143      45.387  29.511 390.369  1.00154.83           N  
ANISOU 2201  N   GLU B 143    14395  29725  14709   -921  -4934  10372       N  
ATOM   2202  CA  GLU B 143      45.254  28.212 391.037  1.00155.34           C  
ANISOU 2202  CA  GLU B 143    14693  29324  15004   -786  -5093  10603       C  
ATOM   2203  C   GLU B 143      43.799  27.943 391.454  1.00157.79           C  
ANISOU 2203  C   GLU B 143    15346  29386  15219   -777  -4903  10501       C  
ATOM   2204  O   GLU B 143      43.403  26.780 391.553  1.00157.73           O  
ANISOU 2204  O   GLU B 143    15502  28929  15498   -730  -5019  10800       O  
ATOM   2205  CB  GLU B 143      46.176  28.141 392.262  1.00157.40           C  
ANISOU 2205  CB  GLU B 143    15136  29635  15033   -626  -5204  10301       C  
ATOM   2206  N   ALA B 144      43.014  29.021 391.688  1.00155.05           N  
ANISOU 2206  N   ALA B 144    14861  29685  14365   -916  -4672  10407       N  
ATOM   2207  CA  ALA B 144      41.604  28.979 392.087  1.00154.53           C  
ANISOU 2207  CA  ALA B 144    14936  29688  14090   -958  -4484  10454       C  
ATOM   2208  C   ALA B 144      40.715  28.404 390.980  1.00155.94           C  
ANISOU 2208  C   ALA B 144    15214  29292  14745  -1000  -4428  10603       C  
ATOM   2209  O   ALA B 144      39.816  27.617 391.278  1.00155.71           O  
ANISOU 2209  O   ALA B 144    15338  29050  14775  -1028  -4409  10818       O  
ATOM   2210  CB  ALA B 144      41.126  30.374 392.466  1.00154.96           C  
ANISOU 2210  CB  ALA B 144    15001  30314  13564   -962  -4215  10011       C  
ATOM   2211  N   GLU B 145      40.972  28.788 389.712  1.00152.60           N  
ANISOU 2211  N   GLU B 145    14442  28975  14563  -1131  -4471  10850       N  
ATOM   2212  CA  GLU B 145      40.218  28.317 388.547  1.00151.45           C  
ANISOU 2212  CA  GLU B 145    14229  28452  14862  -1252  -4482  11193       C  
ATOM   2213  C   GLU B 145      40.617  26.882 388.156  1.00154.12           C  
ANISOU 2213  C   GLU B 145    14877  27833  15849  -1126  -4725  11294       C  
ATOM   2214  O   GLU B 145      39.872  26.222 387.430  1.00153.32           O  
ANISOU 2214  O   GLU B 145    14836  27309  16110  -1220  -4770  11583       O  
ATOM   2215  CB  GLU B 145      40.420  29.268 387.358  1.00151.38           C  
ANISOU 2215  CB  GLU B 145    14014  28560  14942  -1316  -4384  11043       C  
ATOM   2216  N   ILE B 146      41.781  26.405 388.643  1.00152.59           N  
ANISOU 2216  N   ILE B 146    14639  27611  15728  -1014  -4957  11401       N  
ATOM   2217  CA  ILE B 146      42.308  25.066 388.369  1.00153.13           C  
ANISOU 2217  CA  ILE B 146    14897  26963  16323   -873  -5234  11620       C  
ATOM   2218  C   ILE B 146      41.931  24.062 389.477  1.00156.34           C  
ANISOU 2218  C   ILE B 146    15790  26989  16624   -702  -5245  11445       C  
ATOM   2219  O   ILE B 146      42.016  22.853 389.247  1.00156.56           O  
ANISOU 2219  O   ILE B 146    16046  26408  17031   -591  -5441  11641       O  
ATOM   2220  CB  ILE B 146      43.840  25.133 388.187  1.00155.95           C  
ANISOU 2220  CB  ILE B 146    15246  27154  16854   -646  -5371  11331       C  
ATOM   2221  N   SER B 147      41.515  24.556 390.663  1.00154.18           N  
ANISOU 2221  N   SER B 147    15446  27334  15802   -786  -5119  11437       N  
ATOM   2222  CA  SER B 147      41.138  23.720 391.810  1.00155.02           C  
ANISOU 2222  CA  SER B 147    15859  27302  15739   -705  -5154  11468       C  
ATOM   2223  C   SER B 147      39.614  23.601 391.996  1.00157.60           C  
ANISOU 2223  C   SER B 147    16424  27521  15935   -798  -4928  11399       C  
ATOM   2224  O   SER B 147      39.163  22.646 392.631  1.00157.91           O  
ANISOU 2224  O   SER B 147    16739  27277  15983   -759  -4982  11529       O  
ATOM   2225  CB  SER B 147      41.763  24.262 393.092  1.00157.94           C  
ANISOU 2225  CB  SER B 147    16383  27964  15665   -546  -5082  10979       C  
ATOM   2226  N   HIS B 148      38.831  24.563 391.461  1.00154.67           N  
ANISOU 2226  N   HIS B 148    15694  27694  15379  -1028  -4751  11564       N  
ATOM   2227  CA  HIS B 148      37.369  24.586 391.583  1.00154.25           C  
ANISOU 2227  CA  HIS B 148    15695  27759  15156  -1166  -4554  11655       C  
ATOM   2228  C   HIS B 148      36.657  24.157 390.291  1.00156.95           C  
ANISOU 2228  C   HIS B 148    16122  27552  15961  -1262  -4545  11762       C  
ATOM   2229  O   HIS B 148      35.573  23.575 390.367  1.00156.64           O  
ANISOU 2229  O   HIS B 148    16243  27317  15957  -1356  -4493  11925       O  
ATOM   2230  CB  HIS B 148      36.887  25.984 391.996  1.00154.25           C  
ANISOU 2230  CB  HIS B 148    15550  28441  14619  -1179  -4261  11323       C  
ATOM   2231  N   THR B 149      37.249  24.458 389.117  1.00154.59           N  
ANISOU 2231  N   THR B 149    15472  27292  15975  -1371  -4674  12033       N  
ATOM   2232  CA  THR B 149      36.680  24.135 387.803  1.00153.84           C  
ANISOU 2232  CA  THR B 149    15333  26776  16343  -1529  -4732  12295       C  
ATOM   2233  C   THR B 149      37.504  23.078 387.039  1.00157.09           C  
ANISOU 2233  C   THR B 149    16016  26301  17371  -1385  -4999  12289       C  
ATOM   2234  O   THR B 149      36.980  22.478 386.094  1.00156.55           O  
ANISOU 2234  O   THR B 149    16053  25705  17725  -1492  -5094  12495       O  
ATOM   2235  CB  THR B 149      36.561  25.411 386.963  1.00158.74           C  
ANISOU 2235  CB  THR B 149    15870  27545  16898  -1503  -4478  11828       C  
ATOM   2236  N   GLN B 150      38.783  22.859 387.448  1.00155.36           N  
ANISOU 2236  N   GLN B 150    15675  26164  17190  -1257  -5220  12417       N  
ATOM   2237  CA  GLN B 150      39.757  21.928 386.848  1.00155.89           C  
ANISOU 2237  CA  GLN B 150    15877  25567  17786  -1088  -5520  12530       C  
ATOM   2238  C   GLN B 150      39.954  22.247 385.341  1.00157.29           C  
ANISOU 2238  C   GLN B 150    15957  25374  18431  -1108  -5557  12463       C  
ATOM   2239  O   GLN B 150      40.035  21.348 384.499  1.00157.25           O  
ANISOU 2239  O   GLN B 150    16155  24637  18957  -1036  -5764  12582       O  
ATOM   2240  CB  GLN B 150      39.363  20.454 387.084  1.00157.81           C  
ANISOU 2240  CB  GLN B 150    16616  25102  18243   -971  -5640  12585       C  
ATOM   2241  N   LYS B 151      40.027  23.554 385.029  1.00153.63           N  
ANISOU 2241  N   LYS B 151    14977  25627  17768  -1317  -5450  12610       N  
ATOM   2242  CA  LYS B 151      40.218  24.110 383.691  1.00152.33           C  
ANISOU 2242  CA  LYS B 151    14595  25310  17973  -1398  -5477  12645       C  
ATOM   2243  C   LYS B 151      40.932  25.455 383.817  1.00154.00           C  
ANISOU 2243  C   LYS B 151    14569  26156  17786  -1339  -5266  12246       C  
ATOM   2244  O   LYS B 151      40.411  26.370 384.462  1.00153.17           O  
ANISOU 2244  O   LYS B 151    14327  26762  17109  -1441  -5020  12123       O  
ATOM   2245  CB  LYS B 151      38.872  24.253 382.961  1.00152.82           C  
ANISOU 2245  CB  LYS B 151    14766  25145  18152  -1585  -5326  12621       C  
ATOM   2246  N   ALA B 152      42.141  25.558 383.242  1.00152.23           N  
ANISOU 2246  N   ALA B 152    13995  25981  17864  -1322  -5493  12527       N  
ATOM   2247  CA  ALA B 152      42.962  26.766 383.316  1.00149.18           C  
ANISOU 2247  CA  ALA B 152    13553  26027  17104  -1200  -5265  11905       C  
ATOM   2248  C   ALA B 152      42.766  27.668 382.101  1.00145.87           C  
ANISOU 2248  C   ALA B 152    13407  25203  16813  -1111  -4969  11126       C  
ATOM   2249  O   ALA B 152      42.814  27.195 380.963  1.00143.28           O  
ANISOU 2249  O   ALA B 152    13295  24100  17046  -1005  -5031  10975       O  
ATOM   2250  CB  ALA B 152      44.428  26.391 383.453  1.00151.72           C  
ANISOU 2250  CB  ALA B 152    13788  26253  17604   -988  -5482  11901       C  
ATOM   2251  N   THR B 153      42.557  28.972 382.351  1.00139.22           N  
ANISOU 2251  N   THR B 153    12570  24886  15442  -1147  -4661  10628       N  
ATOM   2252  CA  THR B 153      42.369  29.975 381.305  1.00133.37           C  
ANISOU 2252  CA  THR B 153    12080  23846  14748  -1078  -4373   9895       C  
ATOM   2253  C   THR B 153      43.474  31.041 381.398  1.00134.86           C  
ANISOU 2253  C   THR B 153    12282  24309  14649   -985  -4258   9295       C  
ATOM   2254  O   THR B 153      43.516  31.808 382.364  1.00136.06           O  
ANISOU 2254  O   THR B 153    12328  25150  14217  -1056  -4164   9193       O  
ATOM   2255  CB  THR B 153      40.962  30.585 381.384  1.00138.49           C  
ANISOU 2255  CB  THR B 153    12770  24779  15072  -1208  -4123   9853       C  
ATOM   2256  N   LEU B 154      44.387  31.058 380.406  1.00127.90           N  
ANISOU 2256  N   LEU B 154    11522  22907  14165   -834  -4285   8916       N  
ATOM   2257  CA  LEU B 154      45.483  32.026 380.322  1.00125.75           C  
ANISOU 2257  CA  LEU B 154    11258  22830  13692   -782  -4203   8369       C  
ATOM   2258  C   LEU B 154      45.054  33.194 379.424  1.00124.15           C  
ANISOU 2258  C   LEU B 154    11315  22430  13426   -805  -3909   7707       C  
ATOM   2259  O   LEU B 154      44.754  32.991 378.243  1.00120.88           O  
ANISOU 2259  O   LEU B 154    11078  21410  13439   -733  -3841   7530       O  
ATOM   2260  CB  LEU B 154      46.766  31.361 379.804  1.00126.31           C  
ANISOU 2260  CB  LEU B 154    11257  22540  14194   -595  -4401   8380       C  
ATOM   2261  N   VAL B 155      44.974  34.407 380.005  1.00119.39           N  
ANISOU 2261  N   VAL B 155    10749  22332  12280   -903  -3751   7350       N  
ATOM   2262  CA  VAL B 155      44.543  35.615 379.301  1.00114.95           C  
ANISOU 2262  CA  VAL B 155    10450  21624  11603   -927  -3492   6735       C  
ATOM   2263  C   VAL B 155      45.730  36.517 378.976  1.00116.47           C  
ANISOU 2263  C   VAL B 155    10705  21818  11729   -952  -3486   6218       C  
ATOM   2264  O   VAL B 155      46.597  36.728 379.826  1.00118.41           O  
ANISOU 2264  O   VAL B 155    10798  22524  11667  -1017  -3615   6240       O  
ATOM   2265  CB  VAL B 155      43.473  36.384 380.102  1.00119.80           C  
ANISOU 2265  CB  VAL B 155    11115  22741  11661   -992  -3322   6668       C  
ATOM   2266  N   CYS B 156      45.752  37.055 377.742  1.00108.91           N  
ANISOU 2266  N   CYS B 156     9960  20372  11050   -925  -3348   5776       N  
ATOM   2267  CA  CYS B 156      46.799  37.950 377.247  1.00107.27           C  
ANISOU 2267  CA  CYS B 156     9820  20120  10816   -988  -3333   5295       C  
ATOM   2268  C   CYS B 156      46.268  39.373 377.091  1.00107.39           C  
ANISOU 2268  C   CYS B 156    10123  20144  10535  -1091  -3132   4768       C  
ATOM   2269  O   CYS B 156      45.117  39.567 376.697  1.00104.44           O  
ANISOU 2269  O   CYS B 156     9926  19552  10206  -1040  -2959   4698       O  
ATOM   2270  CB  CYS B 156      47.383  37.436 375.936  1.00105.66           C  
ANISOU 2270  CB  CYS B 156     9604  19385  11156   -871  -3359   5228       C  
ATOM   2271  SG  CYS B 156      48.761  38.428 375.301  1.00108.78           S  
ANISOU 2271  SG  CYS B 156    10003  19805  11523   -976  -3357   4731       S  
ATOM   2272  N   LEU B 157      47.130  40.364 377.375  1.00104.17           N  
ANISOU 2272  N   LEU B 157     9767  19973   9839  -1239  -3175   4405       N  
ATOM   2273  CA  LEU B 157      46.801  41.780 377.276  1.00102.62           C  
ANISOU 2273  CA  LEU B 157     9881  19749   9361  -1346  -3039   3880       C  
ATOM   2274  C   LEU B 157      47.896  42.553 376.535  1.00105.18           C  
ANISOU 2274  C   LEU B 157    10280  19897   9788  -1509  -3088   3498       C  
ATOM   2275  O   LEU B 157      49.047  42.595 376.981  1.00106.76           O  
ANISOU 2275  O   LEU B 157    10300  20400   9865  -1638  -3268   3531       O  
ATOM   2276  CB  LEU B 157      46.569  42.382 378.670  1.00106.02           C  
ANISOU 2276  CB  LEU B 157    10355  20747   9181  -1409  -3072   3812       C  
ATOM   2277  N   ALA B 158      47.524  43.142 375.386  1.00 98.62           N  
ANISOU 2277  N   ALA B 158     9691  18601   9179  -1515  -2935   3173       N  
ATOM   2278  CA  ALA B 158      48.383  43.976 374.546  1.00 97.34           C  
ANISOU 2278  CA  ALA B 158     9627  18241   9118  -1696  -2958   2817       C  
ATOM   2279  C   ALA B 158      47.899  45.418 374.659  1.00100.46           C  
ANISOU 2279  C   ALA B 158    10403  18564   9203  -1829  -2887   2356       C  
ATOM   2280  O   ALA B 158      46.808  45.745 374.176  1.00 97.66           O  
ANISOU 2280  O   ALA B 158    10286  17902   8919  -1711  -2705   2215       O  
ATOM   2281  CB  ALA B 158      48.347  43.493 373.101  1.00 94.83           C  
ANISOU 2281  CB  ALA B 158     9279  17443   9308  -1590  -2855   2836       C  
ATOM   2282  N   THR B 159      48.675  46.261 375.364  1.00 99.30           N  
ANISOU 2282  N   THR B 159    10322  18710   8696  -2064  -3049   2133       N  
ATOM   2283  CA  THR B 159      48.307  47.651 375.629  1.00 99.78           C  
ANISOU 2283  CA  THR B 159    10786  18699   8427  -2189  -3042   1673       C  
ATOM   2284  C   THR B 159      49.226  48.658 374.936  1.00102.75           C  
ANISOU 2284  C   THR B 159    11306  18876   8856  -2512  -3164   1356       C  
ATOM   2285  O   THR B 159      50.381  48.349 374.637  1.00102.81           O  
ANISOU 2285  O   THR B 159    11038  19031   8995  -2687  -3302   1502       O  
ATOM   2286  CB  THR B 159      48.308  47.900 377.143  1.00111.07           C  
ANISOU 2286  CB  THR B 159    12244  20645   9314  -2203  -3158   1640       C  
ATOM   2287  N   GLY B 160      48.680  49.851 374.700  1.00 98.48           N  
ANISOU 2287  N   GLY B 160    11190  18019   8209  -2583  -3120    947       N  
ATOM   2288  CA  GLY B 160      49.374  50.990 374.113  1.00 98.91           C  
ANISOU 2288  CA  GLY B 160    11466  17835   8281  -2927  -3257    632       C  
ATOM   2289  C   GLY B 160      49.815  50.848 372.674  1.00 99.15           C  
ANISOU 2289  C   GLY B 160    11383  17523   8764  -3017  -3184    704       C  
ATOM   2290  O   GLY B 160      51.006  50.976 372.384  1.00 99.80           O  
ANISOU 2290  O   GLY B 160    11299  17712   8907  -3319  -3344    733       O  
ATOM   2291  N   PHE B 161      48.858  50.624 371.757  1.00 91.82           N  
ANISOU 2291  N   PHE B 161    10536  16224   8129  -2767  -2948    733       N  
ATOM   2292  CA  PHE B 161      49.153  50.523 370.328  1.00 88.48           C  
ANISOU 2292  CA  PHE B 161    10030  15478   8110  -2822  -2859    775       C  
ATOM   2293  C   PHE B 161      48.268  51.458 369.515  1.00 89.74           C  
ANISOU 2293  C   PHE B 161    10595  15145   8358  -2800  -2729    496       C  
ATOM   2294  O   PHE B 161      47.068  51.566 369.774  1.00 88.72           O  
ANISOU 2294  O   PHE B 161    10692  14890   8128  -2550  -2596    404       O  
ATOM   2295  CB  PHE B 161      49.040  49.080 369.802  1.00 87.59           C  
ANISOU 2295  CB  PHE B 161     9557  15388   8337  -2543  -2722   1132       C  
ATOM   2296  CG  PHE B 161      47.689  48.411 369.895  1.00 87.01           C  
ANISOU 2296  CG  PHE B 161     9542  15182   8335  -2196  -2533   1257       C  
ATOM   2297  CD1 PHE B 161      47.331  47.686 371.025  1.00 91.45           C  
ANISOU 2297  CD1 PHE B 161     9972  16070   8704  -2030  -2558   1479       C  
ATOM   2298  CD2 PHE B 161      46.799  48.451 368.828  1.00 86.10           C  
ANISOU 2298  CD2 PHE B 161     9579  14655   8482  -2057  -2342   1196       C  
ATOM   2299  CE1 PHE B 161      46.086  47.059 371.107  1.00 90.96           C  
ANISOU 2299  CE1 PHE B 161     9931  15930   8701  -1754  -2399   1645       C  
ATOM   2300  CE2 PHE B 161      45.553  47.826 368.910  1.00 87.39           C  
ANISOU 2300  CE2 PHE B 161     9768  14734   8703  -1774  -2185   1343       C  
ATOM   2301  CZ  PHE B 161      45.208  47.126 370.046  1.00 87.08           C  
ANISOU 2301  CZ  PHE B 161     9590  15028   8468  -1634  -2217   1577       C  
ATOM   2302  N   TYR B 162      48.870  52.135 368.533  1.00 85.30           N  
ANISOU 2302  N   TYR B 162    10098  14340   7973  -3060  -2772    388       N  
ATOM   2303  CA  TYR B 162      48.154  53.039 367.642  1.00 83.54           C  
ANISOU 2303  CA  TYR B 162    10238  13633   7870  -3074  -2674    162       C  
ATOM   2304  C   TYR B 162      48.791  53.002 366.248  1.00 84.36           C  
ANISOU 2304  C   TYR B 162    10173  13587   8293  -3258  -2645    255       C  
ATOM   2305  O   TYR B 162      50.016  53.092 366.153  1.00 85.50           O  
ANISOU 2305  O   TYR B 162    10106  13961   8418  -3567  -2810    324       O  
ATOM   2306  CB  TYR B 162      48.100  54.470 368.203  1.00 88.36           C  
ANISOU 2306  CB  TYR B 162    11317  14071   8183  -3286  -2847   -199       C  
ATOM   2307  CG  TYR B 162      47.064  55.346 367.528  1.00 89.54           C  
ANISOU 2307  CG  TYR B 162    11892  13711   8420  -3177  -2734   -431       C  
ATOM   2308  CD1 TYR B 162      45.706  55.188 367.794  1.00 90.48           C  
ANISOU 2308  CD1 TYR B 162    12169  13729   8480  -2764  -2535   -488       C  
ATOM   2309  CD2 TYR B 162      47.440  56.338 366.629  1.00 90.95           C  
ANISOU 2309  CD2 TYR B 162    12298  13533   8727  -3492  -2838   -565       C  
ATOM   2310  CE1 TYR B 162      44.747  55.988 367.171  1.00 90.73           C  
ANISOU 2310  CE1 TYR B 162    12570  13318   8587  -2629  -2433   -688       C  
ATOM   2311  CE2 TYR B 162      46.492  57.151 366.010  1.00 91.15           C  
ANISOU 2311  CE2 TYR B 162    12719  13075   8838  -3377  -2751   -757       C  
ATOM   2312  CZ  TYR B 162      45.146  56.969 366.278  1.00 97.43           C  
ANISOU 2312  CZ  TYR B 162    13662  13778   9579  -2927  -2544   -826       C  
ATOM   2313  OH  TYR B 162      44.213  57.768 365.660  1.00 97.97           O  
ANISOU 2313  OH  TYR B 162    14099  13396   9730  -2782  -2459  -1002       O  
ATOM   2314  N   PRO B 163      48.003  52.817 365.159  1.00 76.74           N  
ANISOU 2314  N   PRO B 163     9256  12301   7602  -3072  -2438    280       N  
ATOM   2315  CA  PRO B 163      46.539  52.660 365.115  1.00 74.08           C  
ANISOU 2315  CA  PRO B 163     9116  11715   7317  -2718  -2234    242       C  
ATOM   2316  C   PRO B 163      46.102  51.222 365.415  1.00 76.74           C  
ANISOU 2316  C   PRO B 163     9145  12260   7754  -2392  -2111    516       C  
ATOM   2317  O   PRO B 163      46.952  50.354 365.627  1.00 76.95           O  
ANISOU 2317  O   PRO B 163     8828  12585   7823  -2413  -2187    720       O  
ATOM   2318  CB  PRO B 163      46.209  53.072 363.679  1.00 73.46           C  
ANISOU 2318  CB  PRO B 163     9146  11262   7503  -2760  -2118    197       C  
ATOM   2319  CG  PRO B 163      47.395  52.604 362.886  1.00 77.63           C  
ANISOU 2319  CG  PRO B 163     9317  11970   8207  -2963  -2171    358       C  
ATOM   2320  CD  PRO B 163      48.588  52.756 363.802  1.00 76.64           C  
ANISOU 2320  CD  PRO B 163     9062  12203   7856  -3229  -2401    368       C  
ATOM   2321  N   ASP B 164      44.780  50.971 365.429  1.00 72.06           N  
ANISOU 2321  N   ASP B 164     8670  11511   7199  -2097  -1936    541       N  
ATOM   2322  CA  ASP B 164      44.211  49.644 365.669  1.00 70.79           C  
ANISOU 2322  CA  ASP B 164     8259  11490   7148  -1822  -1838    828       C  
ATOM   2323  C   ASP B 164      44.443  48.750 364.420  1.00 72.19           C  
ANISOU 2323  C   ASP B 164     8196  11522   7711  -1772  -1768    997       C  
ATOM   2324  O   ASP B 164      43.503  48.427 363.682  1.00 69.72           O  
ANISOU 2324  O   ASP B 164     7924  10970   7594  -1606  -1620   1050       O  
ATOM   2325  CB  ASP B 164      42.713  49.766 366.032  1.00 72.18           C  
ANISOU 2325  CB  ASP B 164     8630  11585   7211  -1566  -1688    809       C  
ATOM   2326  CG  ASP B 164      42.029  48.460 366.397  1.00 82.01           C  
ANISOU 2326  CG  ASP B 164     9633  13001   8524  -1335  -1617   1143       C  
ATOM   2327  OD1 ASP B 164      42.714  47.557 366.931  1.00 83.43           O  
ANISOU 2327  OD1 ASP B 164     9541  13426   8731  -1353  -1726   1370       O  
ATOM   2328  OD2 ASP B 164      40.809  48.341 366.151  1.00 86.69           O  
ANISOU 2328  OD2 ASP B 164    10303  13491   9143  -1146  -1470   1199       O  
ATOM   2329  N   HIS B 165      45.721  48.394 364.178  1.00 68.92           N  
ANISOU 2329  N   HIS B 165     7527  11278   7381  -1911  -1881   1068       N  
ATOM   2330  CA  HIS B 165      46.179  47.596 363.038  1.00 67.00           C  
ANISOU 2330  CA  HIS B 165     7038  10966   7452  -1846  -1839   1182       C  
ATOM   2331  C   HIS B 165      47.000  46.399 363.534  1.00 71.79           C  
ANISOU 2331  C   HIS B 165     7295  11865   8116  -1732  -1948   1426       C  
ATOM   2332  O   HIS B 165      48.176  46.262 363.180  1.00 72.82           O  
ANISOU 2332  O   HIS B 165     7186  12185   8297  -1818  -2030   1450       O  
ATOM   2333  CB  HIS B 165      47.016  48.482 362.084  1.00 68.10           C  
ANISOU 2333  CB  HIS B 165     7189  11063   7623  -2113  -1865   1019       C  
ATOM   2334  CG  HIS B 165      46.227  49.411 361.208  1.00 69.93           C  
ANISOU 2334  CG  HIS B 165     7721  10941   7910  -2178  -1749    841       C  
ATOM   2335  ND1 HIS B 165      46.706  49.801 359.970  1.00 70.97           N  
ANISOU 2335  ND1 HIS B 165     7795  10977   8195  -2305  -1706    794       N  
ATOM   2336  CD2 HIS B 165      45.031  50.014 361.420  1.00 70.96           C  
ANISOU 2336  CD2 HIS B 165     8185  10832   7944  -2115  -1675    716       C  
ATOM   2337  CE1 HIS B 165      45.786  50.610 359.468  1.00 69.18           C  
ANISOU 2337  CE1 HIS B 165     7878  10428   7980  -2332  -1617    660       C  
ATOM   2338  NE2 HIS B 165      44.760  50.767 360.305  1.00 69.50           N  
ANISOU 2338  NE2 HIS B 165     8163  10365   7879  -2203  -1594    602       N  
ATOM   2339  N   VAL B 166      46.383  45.539 364.370  1.00 67.85           N  
ANISOU 2339  N   VAL B 166     6753  11428   7599  -1535  -1958   1631       N  
ATOM   2340  CA  VAL B 166      47.053  44.368 364.953  1.00 68.82           C  
ANISOU 2340  CA  VAL B 166     6574  11793   7781  -1403  -2083   1903       C  
ATOM   2341  C   VAL B 166      46.324  43.051 364.599  1.00 71.03           C  
ANISOU 2341  C   VAL B 166     6786  11845   8358  -1128  -2041   2134       C  
ATOM   2342  O   VAL B 166      45.156  43.069 364.203  1.00 68.56           O  
ANISOU 2342  O   VAL B 166     6657  11270   8121  -1062  -1921   2120       O  
ATOM   2343  CB  VAL B 166      47.267  44.492 366.491  1.00 75.07           C  
ANISOU 2343  CB  VAL B 166     7332  12949   8243  -1475  -2211   2004       C  
ATOM   2344  CG1 VAL B 166      48.217  45.636 366.832  1.00 76.95           C  
ANISOU 2344  CG1 VAL B 166     7597  13429   8212  -1770  -2320   1797       C  
ATOM   2345  CG2 VAL B 166      45.948  44.627 367.249  1.00 74.41           C  
ANISOU 2345  CG2 VAL B 166     7463  12831   7979  -1400  -2130   2030       C  
ATOM   2346  N   GLU B 167      47.039  41.916 364.743  1.00 69.11           N  
ANISOU 2346  N   GLU B 167     6280  11699   8281   -971  -2162   2354       N  
ATOM   2347  CA  GLU B 167      46.549  40.556 364.502  1.00 68.85           C  
ANISOU 2347  CA  GLU B 167     6184  11428   8547   -720  -2196   2596       C  
ATOM   2348  C   GLU B 167      47.108  39.616 365.583  1.00 75.81           C  
ANISOU 2348  C   GLU B 167     6844  12555   9406   -614  -2384   2921       C  
ATOM   2349  O   GLU B 167      48.296  39.279 365.559  1.00 77.01           O  
ANISOU 2349  O   GLU B 167     6764  12894   9600   -543  -2492   2954       O  
ATOM   2350  CB  GLU B 167      46.926  40.068 363.091  1.00 69.31           C  
ANISOU 2350  CB  GLU B 167     6183  11229   8921   -568  -2159   2477       C  
ATOM   2351  CG  GLU B 167      46.120  40.700 361.968  1.00 78.35           C  
ANISOU 2351  CG  GLU B 167     7549  12076  10143   -631  -1984   2242       C  
ATOM   2352  CD  GLU B 167      46.343  40.095 360.595  1.00101.73           C  
ANISOU 2352  CD  GLU B 167    10461  14793  13397   -453  -1952   2138       C  
ATOM   2353  OE1 GLU B 167      47.518  39.882 360.217  1.00 96.03           O  
ANISOU 2353  OE1 GLU B 167     9530  14250  12709   -378  -1993   2064       O  
ATOM   2354  OE2 GLU B 167      45.339  39.852 359.886  1.00 97.51           O  
ANISOU 2354  OE2 GLU B 167    10088  13923  13038   -385  -1887   2127       O  
ATOM   2355  N   LEU B 168      46.249  39.224 366.545  1.00 73.40           N  
ANISOU 2355  N   LEU B 168     6587  12294   9007   -606  -2423   3181       N  
ATOM   2356  CA  LEU B 168      46.602  38.359 367.674  1.00 76.29           C  
ANISOU 2356  CA  LEU B 168     6757  12903   9326   -529  -2608   3546       C  
ATOM   2357  C   LEU B 168      46.389  36.879 367.337  1.00 81.29           C  
ANISOU 2357  C   LEU B 168     7328  13205  10352   -295  -2730   3836       C  
ATOM   2358  O   LEU B 168      45.336  36.506 366.808  1.00 79.16           O  
ANISOU 2358  O   LEU B 168     7217  12570  10288   -255  -2673   3868       O  
ATOM   2359  CB  LEU B 168      45.770  38.743 368.909  1.00 77.24           C  
ANISOU 2359  CB  LEU B 168     6946  13294   9109   -651  -2592   3704       C  
ATOM   2360  CG  LEU B 168      46.359  38.394 370.273  1.00 85.61           C  
ANISOU 2360  CG  LEU B 168     7796  14795   9936   -668  -2767   3998       C  
ATOM   2361  CD1 LEU B 168      45.924  39.397 371.316  1.00 86.79           C  
ANISOU 2361  CD1 LEU B 168     8034  15336   9605   -838  -2708   3901       C  
ATOM   2362  CD2 LEU B 168      45.995  36.981 370.702  1.00 90.03           C  
ANISOU 2362  CD2 LEU B 168     8239  15261  10707   -525  -2916   4485       C  
ATOM   2363  N   SER B 169      47.380  36.038 367.692  1.00 80.85           N  
ANISOU 2363  N   SER B 169     7048  13276  10395   -142  -2921   4057       N  
ATOM   2364  CA  SER B 169      47.350  34.594 367.452  1.00 82.36           C  
ANISOU 2364  CA  SER B 169     7196  13130  10968    112  -3093   4336       C  
ATOM   2365  C   SER B 169      47.889  33.811 368.643  1.00 89.78           C  
ANISOU 2365  C   SER B 169     7926  14330  11858    189  -3321   4755       C  
ATOM   2366  O   SER B 169      48.826  34.261 369.307  1.00 90.87           O  
ANISOU 2366  O   SER B 169     7869  14920  11738    135  -3360   4743       O  
ATOM   2367  CB  SER B 169      48.167  34.243 366.212  1.00 86.07           C  
ANISOU 2367  CB  SER B 169     7617  13364  11720    349  -3094   4088       C  
ATOM   2368  OG  SER B 169      47.840  35.057 365.097  1.00 93.25           O  
ANISOU 2368  OG  SER B 169     8702  14059  12670    276  -2892   3723       O  
ATOM   2369  N   TRP B 170      47.304  32.624 368.894  1.00 87.97           N  
ANISOU 2369  N   TRP B 170     7735  13810  11878    295  -3493   5145       N  
ATOM   2370  CA  TRP B 170      47.714  31.703 369.954  1.00 91.48           C  
ANISOU 2370  CA  TRP B 170     8001  14421  12338    383  -3743   5617       C  
ATOM   2371  C   TRP B 170      48.403  30.489 369.336  1.00 97.81           C  
ANISOU 2371  C   TRP B 170     8763  14825  13576    738  -3951   5712       C  
ATOM   2372  O   TRP B 170      47.842  29.839 368.451  1.00 96.79           O  
ANISOU 2372  O   TRP B 170     8833  14144  13800    858  -3991   5673       O  
ATOM   2373  CB  TRP B 170      46.518  31.274 370.815  1.00 91.08           C  
ANISOU 2373  CB  TRP B 170     8017  14372  12219    210  -3814   6056       C  
ATOM   2374  CG  TRP B 170      46.110  32.285 371.842  1.00 91.41           C  
ANISOU 2374  CG  TRP B 170     8010  14972  11751    -54  -3674   6058       C  
ATOM   2375  CD1 TRP B 170      45.084  33.176 371.749  1.00 91.62           C  
ANISOU 2375  CD1 TRP B 170     8194  15062  11555   -239  -3449   5849       C  
ATOM   2376  CD2 TRP B 170      46.715  32.502 373.124  1.00 93.87           C  
ANISOU 2376  CD2 TRP B 170     8105  15865  11694   -131  -3759   6264       C  
ATOM   2377  NE1 TRP B 170      45.007  33.933 372.894  1.00 92.03           N  
ANISOU 2377  NE1 TRP B 170     8162  15684  11121   -401  -3389   5884       N  
ATOM   2378  CE2 TRP B 170      45.998  33.542 373.756  1.00 96.59           C  
ANISOU 2378  CE2 TRP B 170     8513  16598  11591   -357  -3578   6134       C  
ATOM   2379  CE3 TRP B 170      47.806  31.926 373.798  1.00 98.65           C  
ANISOU 2379  CE3 TRP B 170     8469  16721  12291    -15  -3978   6538       C  
ATOM   2380  CZ2 TRP B 170      46.329  34.013 375.032  1.00 98.16           C  
ANISOU 2380  CZ2 TRP B 170     8557  17417  11322   -479  -3613   6245       C  
ATOM   2381  CZ3 TRP B 170      48.133  32.395 375.062  1.00102.22           C  
ANISOU 2381  CZ3 TRP B 170     8746  17805  12286   -164  -4012   6683       C  
ATOM   2382  CH2 TRP B 170      47.402  33.428 375.665  1.00101.65           C  
ANISOU 2382  CH2 TRP B 170     8758  18105  11760   -399  -3834   6523       C  
ATOM   2383  N   TRP B 171      49.627  30.204 369.783  1.00 97.62           N  
ANISOU 2383  N   TRP B 171     8487  15090  13516    920  -4089   5818       N  
ATOM   2384  CA  TRP B 171      50.426  29.091 369.276  1.00100.71           C  
ANISOU 2384  CA  TRP B 171     8810  15172  14283   1331  -4292   5891       C  
ATOM   2385  C   TRP B 171      50.796  28.137 370.409  1.00110.08           C  
ANISOU 2385  C   TRP B 171     9837  16471  15518   1444  -4586   6438       C  
ATOM   2386  O   TRP B 171      51.352  28.573 371.420  1.00111.10           O  
ANISOU 2386  O   TRP B 171     9727  17177  15307   1314  -4605   6602       O  
ATOM   2387  CB  TRP B 171      51.701  29.609 368.586  1.00 99.17           C  
ANISOU 2387  CB  TRP B 171     8410  15252  14019   1521  -4186   5502       C  
ATOM   2388  CG  TRP B 171      51.478  30.582 367.463  1.00 95.82           C  
ANISOU 2388  CG  TRP B 171     8110  14766  13533   1404  -3912   4994       C  
ATOM   2389  CD1 TRP B 171      51.192  31.910 367.575  1.00 95.54           C  
ANISOU 2389  CD1 TRP B 171     8104  15044  13151   1041  -3692   4761       C  
ATOM   2390  CD2 TRP B 171      51.658  30.327 366.065  1.00 94.76           C  
ANISOU 2390  CD2 TRP B 171     8067  14264  13671   1671  -3846   4655       C  
ATOM   2391  NE1 TRP B 171      51.136  32.489 366.331  1.00 92.12           N  
ANISOU 2391  NE1 TRP B 171     7780  14442  12780   1042  -3497   4338       N  
ATOM   2392  CE2 TRP B 171      51.420  31.540 365.384  1.00 94.79           C  
ANISOU 2392  CE2 TRP B 171     8143  14396  13479   1420  -3577   4265       C  
ATOM   2393  CE3 TRP B 171      51.987  29.185 365.316  1.00 98.49           C  
ANISOU 2393  CE3 TRP B 171     8588  14307  14528   2115  -3998   4633       C  
ATOM   2394  CZ2 TRP B 171      51.481  31.640 363.990  1.00 92.54           C  
ANISOU 2394  CZ2 TRP B 171     7944  13867  13350   1573  -3446   3887       C  
ATOM   2395  CZ3 TRP B 171      52.045  29.284 363.936  1.00 98.47           C  
ANISOU 2395  CZ3 TRP B 171     8684  14066  14666   2290  -3864   4215       C  
ATOM   2396  CH2 TRP B 171      51.797  30.500 363.287  1.00 95.12           C  
ANISOU 2396  CH2 TRP B 171     8296  13823  14021   2010  -3585   3861       C  
ATOM   2397  N   VAL B 172      50.485  26.840 370.246  1.00109.88           N  
ANISOU 2397  N   VAL B 172     9954  15883  15910   1671  -4837   6730       N  
ATOM   2398  CA  VAL B 172      50.798  25.813 371.245  1.00114.69           C  
ANISOU 2398  CA  VAL B 172    10445  16500  16633   1800  -5158   7298       C  
ATOM   2399  C   VAL B 172      51.707  24.767 370.593  1.00122.11           C  
ANISOU 2399  C   VAL B 172    11376  17036  17984   2331  -5374   7261       C  
ATOM   2400  O   VAL B 172      51.318  24.144 369.599  1.00121.60           O  
ANISOU 2400  O   VAL B 172    11582  16322  18299   2531  -5438   7088       O  
ATOM   2401  CB  VAL B 172      49.527  25.185 371.887  1.00119.85           C  
ANISOU 2401  CB  VAL B 172    11279  16873  17384   1541  -5318   7801       C  
ATOM   2402  CG1 VAL B 172      49.887  24.047 372.838  1.00125.29           C  
ANISOU 2402  CG1 VAL B 172    11858  17509  18237   1685  -5686   8423       C  
ATOM   2403  CG2 VAL B 172      48.699  26.237 372.619  1.00116.84           C  
ANISOU 2403  CG2 VAL B 172    10856  17005  16535   1084  -5094   7837       C  
ATOM   2404  N   ASN B 173      52.926  24.602 371.157  1.00122.07           N  
ANISOU 2404  N   ASN B 173    11054  17447  17880   2572  -5489   7408       N  
ATOM   2405  CA  ASN B 173      53.985  23.674 370.727  1.00126.19           C  
ANISOU 2405  CA  ASN B 173    11481  17751  18716   3141  -5694   7402       C  
ATOM   2406  C   ASN B 173      54.357  23.866 369.228  1.00128.71           C  
ANISOU 2406  C   ASN B 173    11879  17836  19189   3451  -5516   6788       C  
ATOM   2407  O   ASN B 173      54.563  22.889 368.500  1.00131.56           O  
ANISOU 2407  O   ASN B 173    12390  17653  19943   3915  -5689   6705       O  
ATOM   2408  CB  ASN B 173      53.600  22.213 371.027  1.00130.52           C  
ANISOU 2408  CB  ASN B 173    12238  17650  19702   3358  -6084   7888       C  
ATOM   2409  CG  ASN B 173      53.606  21.873 372.495  1.00152.63           C  
ANISOU 2409  CG  ASN B 173    14864  20772  22357   3174  -6305   8546       C  
ATOM   2410  OD1 ASN B 173      54.658  21.691 373.113  1.00150.69           O  
ANISOU 2410  OD1 ASN B 173    14300  20962  21992   3389  -6418   8750       O  
ATOM   2411  ND2 ASN B 173      52.428  21.745 373.078  1.00142.65           N  
ANISOU 2411  ND2 ASN B 173    13781  19329  21090   2777  -6380   8920       N  
ATOM   2412  N   GLY B 174      54.452  25.127 368.803  1.00120.63           N  
ANISOU 2412  N   GLY B 174    10756  17239  17838   3197  -5186   6371       N  
ATOM   2413  CA  GLY B 174      54.810  25.498 367.437  1.00118.32           C  
ANISOU 2413  CA  GLY B 174    10484  16871  17600   3410  -4980   5812       C  
ATOM   2414  C   GLY B 174      53.650  25.663 366.474  1.00118.11           C  
ANISOU 2414  C   GLY B 174    10836  16308  17732   3249  -4842   5513       C  
ATOM   2415  O   GLY B 174      53.777  26.400 365.492  1.00114.78           O  
ANISOU 2415  O   GLY B 174    10411  15986  17216   3242  -4597   5052       O  
ATOM   2416  N   LYS B 175      52.517  24.974 366.732  1.00114.79           N  
ANISOU 2416  N   LYS B 175    10728  15342  17546   3103  -5010   5800       N  
ATOM   2417  CA  LYS B 175      51.327  25.017 365.874  1.00111.45           C  
ANISOU 2417  CA  LYS B 175    10665  14393  17289   2929  -4923   5585       C  
ATOM   2418  C   LYS B 175      50.270  25.999 366.398  1.00110.78           C  
ANISOU 2418  C   LYS B 175    10638  14551  16903   2358  -4725   5667       C  
ATOM   2419  O   LYS B 175      50.003  26.040 367.601  1.00111.21           O  
ANISOU 2419  O   LYS B 175    10591  14891  16774   2111  -4801   6081       O  
ATOM   2420  CB  LYS B 175      50.714  23.615 365.733  1.00117.47           C  
ANISOU 2420  CB  LYS B 175    11743  14372  18519   3122  -5264   5848       C  
ATOM   2421  N   GLU B 176      49.663  26.778 365.476  1.00102.84           N  
ANISOU 2421  N   GLU B 176     9792  13447  15835   2178  -4474   5272       N  
ATOM   2422  CA  GLU B 176      48.616  27.759 365.771  1.00 98.53           C  
ANISOU 2422  CA  GLU B 176     9328  13092  15015   1704  -4264   5274       C  
ATOM   2423  C   GLU B 176      47.327  27.047 366.170  1.00103.45           C  
ANISOU 2423  C   GLU B 176    10177  13309  15819   1503  -4433   5672       C  
ATOM   2424  O   GLU B 176      46.945  26.064 365.529  1.00104.69           O  
ANISOU 2424  O   GLU B 176    10564  12855  16359   1661  -4619   5700       O  
ATOM   2425  CB  GLU B 176      48.374  28.675 364.562  1.00 95.63           C  
ANISOU 2425  CB  GLU B 176     9064  12701  14569   1623  -3974   4751       C  
ATOM   2426  N   VAL B 177      46.671  27.528 367.239  1.00 99.37           N  
ANISOU 2426  N   VAL B 177     9591  13155  15011   1152  -4382   5985       N  
ATOM   2427  CA  VAL B 177      45.438  26.928 367.762  1.00100.20           C  
ANISOU 2427  CA  VAL B 177     9834  13026  15209    907  -4528   6437       C  
ATOM   2428  C   VAL B 177      44.245  27.889 367.600  1.00 99.51           C  
ANISOU 2428  C   VAL B 177     9846  13084  14881    565  -4259   6295       C  
ATOM   2429  O   VAL B 177      44.438  29.105 367.521  1.00 95.88           O  
ANISOU 2429  O   VAL B 177     9311  13026  14093    475  -3982   5948       O  
ATOM   2430  CB  VAL B 177      45.585  26.436 369.234  1.00107.85           C  
ANISOU 2430  CB  VAL B 177    10615  14320  16045    818  -4735   7028       C  
ATOM   2431  CG1 VAL B 177      46.570  25.272 369.333  1.00112.36           C  
ANISOU 2431  CG1 VAL B 177    11145  14593  16952   1172  -5067   7266       C  
ATOM   2432  CG2 VAL B 177      45.980  27.566 370.185  1.00106.41           C  
ANISOU 2432  CG2 VAL B 177    10180  14909  15343    661  -4532   6973       C  
ATOM   2433  N   HIS B 178      43.018  27.330 367.545  1.00 96.41           N  
ANISOU 2433  N   HIS B 178     9619  12357  14656    375  -4364   6581       N  
ATOM   2434  CA  HIS B 178      41.768  28.088 367.402  1.00 93.11           C  
ANISOU 2434  CA  HIS B 178     9278  12064  14035     76  -4141   6523       C  
ATOM   2435  C   HIS B 178      40.751  27.704 368.478  1.00 99.55           C  
ANISOU 2435  C   HIS B 178    10022  13076  14728   -207  -4259   7127       C  
ATOM   2436  O   HIS B 178      39.914  28.531 368.844  1.00 97.01           O  
ANISOU 2436  O   HIS B 178     9646  13146  14068   -429  -4041   7142       O  
ATOM   2437  CB  HIS B 178      41.156  27.881 366.009  1.00 91.94           C  
ANISOU 2437  CB  HIS B 178     9384  11354  14195    101  -4121   6234       C  
ATOM   2438  CG  HIS B 178      42.012  28.401 364.899  1.00 92.80           C  
ANISOU 2438  CG  HIS B 178     9539  11371  14350    342  -3954   5634       C  
ATOM   2439  ND1 HIS B 178      41.914  29.711 364.467  1.00 90.47           N  
ANISOU 2439  ND1 HIS B 178     9227  11380  13769    248  -3624   5232       N  
ATOM   2440  CD2 HIS B 178      42.965  27.770 364.174  1.00 95.96           C  
ANISOU 2440  CD2 HIS B 178     9991  11434  15035    677  -4082   5402       C  
ATOM   2441  CE1 HIS B 178      42.801  29.834 363.494  1.00 88.99           C  
ANISOU 2441  CE1 HIS B 178     9062  11056  13696    486  -3562   4803       C  
ATOM   2442  NE2 HIS B 178      43.458  28.692 363.283  1.00 92.57           N  
ANISOU 2442  NE2 HIS B 178     9544  11152  14475    766  -3819   4875       N  
ATOM   2443  N   SER B 179      40.814  26.448 368.969  1.00100.99           N  
ANISOU 2443  N   SER B 179    10199  12998  15175   -188  -4610   7637       N  
ATOM   2444  CA  SER B 179      39.925  25.929 370.008  1.00104.08           C  
ANISOU 2444  CA  SER B 179    10494  13577  15476   -473  -4774   8303       C  
ATOM   2445  C   SER B 179      40.273  26.545 371.363  1.00108.96           C  
ANISOU 2445  C   SER B 179    10825  14971  15602   -543  -4664   8506       C  
ATOM   2446  O   SER B 179      41.455  26.707 371.685  1.00109.19           O  
ANISOU 2446  O   SER B 179    10736  15197  15555   -339  -4690   8392       O  
ATOM   2447  CB  SER B 179      40.011  24.407 370.077  1.00113.01           C  
ANISOU 2447  CB  SER B 179    11733  14136  17070   -425  -5218   8778       C  
ATOM   2448  OG  SER B 179      39.089  23.864 371.010  1.00126.21           O  
ANISOU 2448  OG  SER B 179    13313  15964  18678   -756  -5400   9472       O  
ATOM   2449  N   GLY B 180      39.237  26.903 372.123  1.00105.65           N  
ANISOU 2449  N   GLY B 180    10288  15022  14832   -822  -4541   8792       N  
ATOM   2450  CA  GLY B 180      39.360  27.519 373.442  1.00106.32           C  
ANISOU 2450  CA  GLY B 180    10114  15897  14384   -907  -4423   8976       C  
ATOM   2451  C   GLY B 180      39.939  28.919 373.409  1.00105.72           C  
ANISOU 2451  C   GLY B 180    10011  16227  13932   -793  -4101   8362       C  
ATOM   2452  O   GLY B 180      40.408  29.426 374.430  1.00105.98           O  
ANISOU 2452  O   GLY B 180     9859  16857  13550   -804  -4043   8408       O  
ATOM   2453  N   VAL B 181      39.900  29.549 372.227  1.00 98.07           N  
ANISOU 2453  N   VAL B 181     9232  14929  13100   -703  -3910   7794       N  
ATOM   2454  CA  VAL B 181      40.424  30.885 371.982  1.00 94.39           C  
ANISOU 2454  CA  VAL B 181     8791  14726  12349   -623  -3629   7192       C  
ATOM   2455  C   VAL B 181      39.258  31.852 371.824  1.00 94.78           C  
ANISOU 2455  C   VAL B 181     8915  14982  12115   -758  -3347   6992       C  
ATOM   2456  O   VAL B 181      38.270  31.531 371.159  1.00 92.90           O  
ANISOU 2456  O   VAL B 181     8793  14413  12092   -832  -3331   7055       O  
ATOM   2457  CB  VAL B 181      41.360  30.895 370.736  1.00 96.40           C  
ANISOU 2457  CB  VAL B 181     9180  14496  12952   -410  -3627   6722       C  
ATOM   2458  CG1 VAL B 181      41.866  32.299 370.411  1.00 92.96           C  
ANISOU 2458  CG1 VAL B 181     8772  14311  12236   -386  -3356   6139       C  
ATOM   2459  CG2 VAL B 181      42.534  29.933 370.916  1.00 99.42           C  
ANISOU 2459  CG2 VAL B 181     9466  14713  13596   -211  -3902   6915       C  
ATOM   2460  N   CYS B 182      39.373  33.027 372.459  1.00 90.76           N  
ANISOU 2460  N   CYS B 182     8346  15020  11117   -780  -3145   6750       N  
ATOM   2461  CA  CYS B 182      38.403  34.108 372.354  1.00 88.64           C  
ANISOU 2461  CA  CYS B 182     8161  14980  10536   -839  -2869   6496       C  
ATOM   2462  C   CYS B 182      39.101  35.448 372.548  1.00 91.33           C  
ANISOU 2462  C   CYS B 182     8560  15627  10515   -785  -2689   5974       C  
ATOM   2463  O   CYS B 182      39.640  35.726 373.622  1.00 93.20           O  
ANISOU 2463  O   CYS B 182     8672  16350  10390   -799  -2724   6032       O  
ATOM   2464  CB  CYS B 182      37.237  33.938 373.321  1.00 91.50           C  
ANISOU 2464  CB  CYS B 182     8371  15800  10595   -963  -2853   6967       C  
ATOM   2465  SG  CYS B 182      35.879  35.103 373.035  1.00 93.30           S  
ANISOU 2465  SG  CYS B 182     8688  16266  10496   -970  -2523   6698       S  
ATOM   2466  N   THR B 183      39.100  36.265 371.484  1.00 84.42           N  
ANISOU 2466  N   THR B 183     7882  14452   9740   -742  -2520   5475       N  
ATOM   2467  CA  THR B 183      39.699  37.596 371.448  1.00 82.74           C  
ANISOU 2467  CA  THR B 183     7784  14404   9251   -728  -2368   4954       C  
ATOM   2468  C   THR B 183      38.581  38.636 371.385  1.00 86.01           C  
ANISOU 2468  C   THR B 183     8347  14940   9394   -727  -2130   4724       C  
ATOM   2469  O   THR B 183      37.580  38.408 370.702  1.00 83.86           O  
ANISOU 2469  O   THR B 183     8130  14424   9309   -722  -2054   4813       O  
ATOM   2470  CB  THR B 183      40.651  37.707 370.237  1.00 86.89           C  
ANISOU 2470  CB  THR B 183     8404  14498  10113   -682  -2382   4600       C  
ATOM   2471  OG1 THR B 183      41.454  36.529 370.138  1.00 86.42           O  
ANISOU 2471  OG1 THR B 183     8204  14254  10377   -613  -2602   4862       O  
ATOM   2472  CG2 THR B 183      41.545  38.938 370.297  1.00 85.03           C  
ANISOU 2472  CG2 THR B 183     8240  14454   9616   -726  -2310   4154       C  
ATOM   2473  N   ASP B 184      38.747  39.768 372.097  1.00 84.56           N  
ANISOU 2473  N   ASP B 184     8235  15129   8765   -720  -2029   4426       N  
ATOM   2474  CA  ASP B 184      37.785  40.873 372.087  1.00 84.25           C  
ANISOU 2474  CA  ASP B 184     8365  15216   8432   -659  -1811   4149       C  
ATOM   2475  C   ASP B 184      37.714  41.441 370.659  1.00 85.93           C  
ANISOU 2475  C   ASP B 184     8801  14914   8934   -645  -1693   3773       C  
ATOM   2476  O   ASP B 184      38.768  41.695 370.072  1.00 84.23           O  
ANISOU 2476  O   ASP B 184     8666  14453   8886   -698  -1744   3497       O  
ATOM   2477  CB  ASP B 184      38.185  41.952 373.106  1.00 88.22           C  
ANISOU 2477  CB  ASP B 184     8945  16155   8419   -640  -1782   3852       C  
ATOM   2478  N   PRO B 185      36.517  41.547 370.036  1.00 82.34           N  
ANISOU 2478  N   PRO B 185     8415  14317   8552   -587  -1546   3799       N  
ATOM   2479  CA  PRO B 185      36.458  42.009 368.635  1.00 79.31           C  
ANISOU 2479  CA  PRO B 185     8227  13457   8449   -582  -1446   3480       C  
ATOM   2480  C   PRO B 185      36.744  43.499 368.491  1.00 83.27           C  
ANISOU 2480  C   PRO B 185     8976  13942   8721   -556  -1337   2971       C  
ATOM   2481  O   PRO B 185      37.507  43.881 367.603  1.00 80.86           O  
ANISOU 2481  O   PRO B 185     8790  13308   8625   -627  -1353   2696       O  
ATOM   2482  CB  PRO B 185      35.028  41.664 368.196  1.00 80.54           C  
ANISOU 2482  CB  PRO B 185     8352  13571   8677   -534  -1336   3705       C  
ATOM   2483  CG  PRO B 185      34.439  40.838 369.313  1.00 87.82           C  
ANISOU 2483  CG  PRO B 185     9030  14894   9444   -554  -1417   4212       C  
ATOM   2484  CD  PRO B 185      35.169  41.240 370.548  1.00 85.71           C  
ANISOU 2484  CD  PRO B 185     8714  15050   8800   -536  -1470   4150       C  
ATOM   2485  N   GLN B 186      36.144  44.329 369.362  1.00 82.70           N  
ANISOU 2485  N   GLN B 186     8984  14229   8210   -452  -1242   2852       N  
ATOM   2486  CA  GLN B 186      36.343  45.774 369.359  1.00 83.20           C  
ANISOU 2486  CA  GLN B 186     9333  14251   8030   -414  -1174   2364       C  
ATOM   2487  C   GLN B 186      37.297  46.176 370.498  1.00 90.47           C  
ANISOU 2487  C   GLN B 186    10265  15498   8612   -479  -1305   2228       C  
ATOM   2488  O   GLN B 186      36.946  46.024 371.673  1.00 93.04           O  
ANISOU 2488  O   GLN B 186    10482  16296   8572   -390  -1307   2379       O  
ATOM   2489  CB  GLN B 186      35.004  46.521 369.464  1.00 85.25           C  
ANISOU 2489  CB  GLN B 186     9726  14636   8027   -199   -985   2248       C  
ATOM   2490  CG  GLN B 186      34.496  47.043 368.128  1.00 96.41           C  
ANISOU 2490  CG  GLN B 186    11300  15611   9722   -161   -864   2097       C  
ATOM   2491  CD  GLN B 186      33.588  48.235 368.301  1.00118.15           C  
ANISOU 2491  CD  GLN B 186    14281  18438  12173     72   -708   1816       C  
ATOM   2492  OE1 GLN B 186      32.460  48.127 368.796  1.00114.98           O  
ANISOU 2492  OE1 GLN B 186    13767  18375  11545    272   -585   1993       O  
ATOM   2493  NE2 GLN B 186      34.059  49.402 367.884  1.00111.00           N  
ANISOU 2493  NE2 GLN B 186    13696  17225  11255     56   -720   1384       N  
ATOM   2494  N   PRO B 187      38.515  46.670 370.172  1.00 86.62           N  
ANISOU 2494  N   PRO B 187     9883  14809   8218   -649  -1422   1965       N  
ATOM   2495  CA  PRO B 187      39.466  47.054 371.231  1.00 89.38           C  
ANISOU 2495  CA  PRO B 187    10238  15481   8241   -750  -1572   1840       C  
ATOM   2496  C   PRO B 187      39.113  48.402 371.860  1.00 95.39           C  
ANISOU 2496  C   PRO B 187    11312  16364   8569   -666  -1532   1431       C  
ATOM   2497  O   PRO B 187      38.642  49.306 371.161  1.00 93.89           O  
ANISOU 2497  O   PRO B 187    11402  15839   8433   -612  -1439   1128       O  
ATOM   2498  CB  PRO B 187      40.813  47.118 370.496  1.00 89.96           C  
ANISOU 2498  CB  PRO B 187    10298  15293   8590   -975  -1707   1723       C  
ATOM   2499  CG  PRO B 187      40.539  46.605 369.095  1.00 90.86           C  
ANISOU 2499  CG  PRO B 187    10375  14977   9169   -957  -1618   1812       C  
ATOM   2500  CD  PRO B 187      39.105  46.884 368.839  1.00 85.36           C  
ANISOU 2500  CD  PRO B 187     9815  14179   8436   -777  -1432   1793       C  
ATOM   2501  N   LEU B 188      39.345  48.529 373.184  1.00 95.08           N  
ANISOU 2501  N   LEU B 188    11235  16801   8091   -640  -1615   1419       N  
ATOM   2502  CA  LEU B 188      39.039  49.731 373.966  1.00 97.82           C  
ANISOU 2502  CA  LEU B 188    11886  17318   7962   -521  -1605   1009       C  
ATOM   2503  C   LEU B 188      40.214  50.706 374.036  1.00102.99           C  
ANISOU 2503  C   LEU B 188    12796  17807   8529   -766  -1803    612       C  
ATOM   2504  O   LEU B 188      41.370  50.281 374.109  1.00102.69           O  
ANISOU 2504  O   LEU B 188    12579  17833   8606  -1017  -1972    740       O  
ATOM   2505  CB  LEU B 188      38.616  49.344 375.387  1.00101.39           C  
ANISOU 2505  CB  LEU B 188    12158  18428   7937   -363  -1598   1195       C  
ATOM   2506  N   LYS B 189      39.904  52.016 374.037  1.00100.93           N  
ANISOU 2506  N   LYS B 189    12953  17340   8055   -690  -1800    141       N  
ATOM   2507  CA  LYS B 189      40.887  53.095 374.135  1.00102.83           C  
ANISOU 2507  CA  LYS B 189    13507  17380   8183   -945  -2018   -265       C  
ATOM   2508  C   LYS B 189      41.147  53.445 375.604  1.00112.12           C  
ANISOU 2508  C   LYS B 189    14766  19034   8803   -922  -2162   -455       C  
ATOM   2509  O   LYS B 189      40.220  53.398 376.418  1.00113.96           O  
ANISOU 2509  O   LYS B 189    14993  19640   8668   -602  -2041   -463       O  
ATOM   2510  CB  LYS B 189      40.405  54.332 373.364  1.00104.83           C  
ANISOU 2510  CB  LYS B 189    14216  17092   8521   -883  -1979   -669       C  
ATOM   2511  N   GLU B 190      42.407  53.790 375.941  1.00110.86           N  
ANISOU 2511  N   GLU B 190    14662  18904   8557  -1267  -2423   -598       N  
ATOM   2512  CA  GLU B 190      42.825  54.157 377.299  1.00115.59           C  
ANISOU 2512  CA  GLU B 190    15350  19945   8624  -1315  -2609   -802       C  
ATOM   2513  C   GLU B 190      42.231  55.509 377.722  1.00123.47           C  
ANISOU 2513  C   GLU B 190    16884  20792   9238  -1117  -2639  -1370       C  
ATOM   2514  O   GLU B 190      41.838  55.663 378.879  1.00126.82           O  
ANISOU 2514  O   GLU B 190    17362  21676   9146   -901  -2650  -1518       O  
ATOM   2515  CB  GLU B 190      44.356  54.193 377.405  1.00118.13           C  
ANISOU 2515  CB  GLU B 190    15587  20300   8996  -1776  -2898   -797       C  
ATOM   2516  N   GLN B 191      42.160  56.474 376.782  1.00119.65           N  
ANISOU 2516  N   GLN B 191    16797  19670   8994  -1173  -2662  -1684       N  
ATOM   2517  CA  GLN B 191      41.606  57.808 377.011  1.00123.28           C  
ANISOU 2517  CA  GLN B 191    17827  19849   9167   -964  -2714  -2241       C  
ATOM   2518  C   GLN B 191      40.378  58.037 376.109  1.00124.74           C  
ANISOU 2518  C   GLN B 191    18152  19652   9591   -606  -2452  -2266       C  
ATOM   2519  O   GLN B 191      40.514  57.982 374.885  1.00120.29           O  
ANISOU 2519  O   GLN B 191    17558  18633   9514   -780  -2408  -2116       O  
ATOM   2520  CB  GLN B 191      42.672  58.891 376.772  1.00127.21           C  
ANISOU 2520  CB  GLN B 191    18738  19891   9705  -1396  -3053  -2613       C  
ATOM   2521  N   PRO B 192      39.170  58.270 376.679  1.00123.89           N  
ANISOU 2521  N   PRO B 192    18165  19772   9134    -96  -2271  -2433       N  
ATOM   2522  CA  PRO B 192      37.988  58.479 375.819  1.00121.56           C  
ANISOU 2522  CA  PRO B 192    17966  19161   9060    254  -2023  -2426       C  
ATOM   2523  C   PRO B 192      37.909  59.889 375.221  1.00127.26           C  
ANISOU 2523  C   PRO B 192    19298  19183   9874    284  -2148  -2916       C  
ATOM   2524  O   PRO B 192      37.193  60.088 374.236  1.00124.07           O  
ANISOU 2524  O   PRO B 192    18968  18396   9778    447  -1990  -2864       O  
ATOM   2525  CB  PRO B 192      36.814  58.212 376.761  1.00125.82           C  
ANISOU 2525  CB  PRO B 192    18361  20309   9134    783  -1800  -2402       C  
ATOM   2526  CG  PRO B 192      37.329  58.548 378.117  1.00135.55           C  
ANISOU 2526  CG  PRO B 192    19728  21966   9811    780  -1991  -2696       C  
ATOM   2527  CD  PRO B 192      38.822  58.350 378.115  1.00130.41           C  
ANISOU 2527  CD  PRO B 192    19014  21209   9328    199  -2276  -2620       C  
ATOM   2528  N   ALA B 193      38.635  60.862 375.818  1.00128.71           N  
ANISOU 2528  N   ALA B 193    19924  19188   9791    118  -2450  -3377       N  
ATOM   2529  CA  ALA B 193      38.670  62.261 375.385  1.00131.40           C  
ANISOU 2529  CA  ALA B 193    20909  18822  10194    108  -2644  -3862       C  
ATOM   2530  C   ALA B 193      39.543  62.449 374.132  1.00132.05           C  
ANISOU 2530  C   ALA B 193    21041  18305  10827   -427  -2795  -3709       C  
ATOM   2531  O   ALA B 193      39.090  63.071 373.166  1.00130.85           O  
ANISOU 2531  O   ALA B 193    21168  17589  10958   -343  -2759  -3797       O  
ATOM   2532  CB  ALA B 193      39.174  63.147 376.517  1.00138.65           C  
ANISOU 2532  CB  ALA B 193    22281  19772  10629     69  -2955  -4390       C  
ATOM   2533  N   LEU B 194      40.781  61.904 374.149  1.00126.78           N  
ANISOU 2533  N   LEU B 194    20079  17801  10292   -960  -2959  -3460       N  
ATOM   2534  CA  LEU B 194      41.742  61.996 373.048  1.00123.83           C  
ANISOU 2534  CA  LEU B 194    19667  17001  10380  -1494  -3106  -3279       C  
ATOM   2535  C   LEU B 194      41.283  61.195 371.822  1.00121.34           C  
ANISOU 2535  C   LEU B 194    18959  16619  10526  -1426  -2814  -2839       C  
ATOM   2536  O   LEU B 194      40.877  60.038 371.954  1.00117.73           O  
ANISOU 2536  O   LEU B 194    18027  16621  10084  -1234  -2579  -2492       O  
ATOM   2537  CB  LEU B 194      43.120  61.505 373.511  1.00124.58           C  
ANISOU 2537  CB  LEU B 194    19489  17426  10421  -2010  -3342  -3122       C  
ATOM   2538  N   ASN B 195      41.335  61.826 370.635  1.00116.52           N  
ANISOU 2538  N   ASN B 195    18562  15428  10283  -1601  -2851  -2851       N  
ATOM   2539  CA  ASN B 195      40.960  61.204 369.361  1.00111.03           C  
ANISOU 2539  CA  ASN B 195    17552  14610  10023  -1575  -2610  -2482       C  
ATOM   2540  C   ASN B 195      42.049  60.221 368.909  1.00111.17           C  
ANISOU 2540  C   ASN B 195    17065  14883  10291  -1989  -2634  -2090       C  
ATOM   2541  O   ASN B 195      41.730  59.135 368.415  1.00106.35           O  
ANISOU 2541  O   ASN B 195    16026  14489   9893  -1858  -2400  -1738       O  
ATOM   2542  CB  ASN B 195      40.713  62.269 368.290  1.00112.46           C  
ANISOU 2542  CB  ASN B 195    18138  14120  10470  -1641  -2669  -2627       C  
ATOM   2543  N   ASP B 196      43.333  60.604 369.100  1.00109.73           N  
ANISOU 2543  N   ASP B 196    16938  14682  10072  -2478  -2933  -2156       N  
ATOM   2544  CA  ASP B 196      44.510  59.798 368.763  1.00107.25           C  
ANISOU 2544  CA  ASP B 196    16154  14651   9946  -2869  -2993  -1819       C  
ATOM   2545  C   ASP B 196      44.992  59.034 370.016  1.00111.55           C  
ANISOU 2545  C   ASP B 196    16411  15789  10183  -2868  -3060  -1740       C  
ATOM   2546  O   ASP B 196      46.181  59.055 370.351  1.00113.40           O  
ANISOU 2546  O   ASP B 196    16531  16217  10339  -3272  -3301  -1708       O  
ATOM   2547  CB  ASP B 196      45.621  60.691 368.173  1.00111.02           C  
ANISOU 2547  CB  ASP B 196    16812  14808  10563  -3431  -3282  -1881       C  
ATOM   2548  N   SER B 197      44.047  58.355 370.700  1.00106.16           N  
ANISOU 2548  N   SER B 197    15589  15429   9318  -2421  -2849  -1675       N  
ATOM   2549  CA  SER B 197      44.289  57.586 371.923  1.00106.93           C  
ANISOU 2549  CA  SER B 197    15407  16118   9104  -2354  -2881  -1560       C  
ATOM   2550  C   SER B 197      44.694  56.147 371.612  1.00105.61           C  
ANISOU 2550  C   SER B 197    14650  16286   9190  -2371  -2753  -1072       C  
ATOM   2551  O   SER B 197      44.142  55.533 370.696  1.00101.23           O  
ANISOU 2551  O   SER B 197    13919  15585   8960  -2196  -2531   -847       O  
ATOM   2552  CB  SER B 197      43.046  57.593 372.807  1.00112.05           C  
ANISOU 2552  CB  SER B 197    16202  16978   9393  -1869  -2730  -1718       C  
ATOM   2553  OG  SER B 197      43.262  56.928 374.041  1.00122.39           O  
ANISOU 2553  OG  SER B 197    17259  18889  10353  -1821  -2778  -1606       O  
ATOM   2554  N   ARG B 198      45.650  55.612 372.398  1.00102.69           N  
ANISOU 2554  N   ARG B 198    13992  16360   8665  -2570  -2911   -918       N  
ATOM   2555  CA  ARG B 198      46.173  54.249 372.274  1.00 99.51           C  
ANISOU 2555  CA  ARG B 198    13047  16294   8471  -2574  -2846   -467       C  
ATOM   2556  C   ARG B 198      45.090  53.214 372.596  1.00100.40           C  
ANISOU 2556  C   ARG B 198    12948  16629   8572  -2155  -2608   -210       C  
ATOM   2557  O   ARG B 198      44.254  53.453 373.470  1.00102.26           O  
ANISOU 2557  O   ARG B 198    13346  17049   8459  -1913  -2556   -347       O  
ATOM   2558  CB  ARG B 198      47.384  54.055 373.196  1.00102.36           C  
ANISOU 2558  CB  ARG B 198    13188  17106   8599  -2853  -3095   -387       C  
ATOM   2559  N   TYR B 199      45.104  52.075 371.874  1.00 92.08           N  
ANISOU 2559  N   TYR B 199    11535  15563   7887  -2075  -2476    161       N  
ATOM   2560  CA  TYR B 199      44.146  50.979 372.036  1.00 89.42           C  
ANISOU 2560  CA  TYR B 199    10972  15392   7613  -1748  -2285    475       C  
ATOM   2561  C   TYR B 199      44.706  49.840 372.908  1.00 92.74           C  
ANISOU 2561  C   TYR B 199    10996  16293   7947  -1748  -2379    840       C  
ATOM   2562  O   TYR B 199      45.920  49.742 373.102  1.00 93.27           O  
ANISOU 2562  O   TYR B 199    10904  16535   7998  -1987  -2566    884       O  
ATOM   2563  CB  TYR B 199      43.737  50.417 370.663  1.00 86.53           C  
ANISOU 2563  CB  TYR B 199    10502  14657   7718  -1658  -2114    649       C  
ATOM   2564  CG  TYR B 199      42.895  51.346 369.818  1.00 87.02           C  
ANISOU 2564  CG  TYR B 199    10911  14281   7870  -1583  -1984    378       C  
ATOM   2565  CD1 TYR B 199      41.517  51.431 370.002  1.00 88.57           C  
ANISOU 2565  CD1 TYR B 199    11229  14457   7965  -1274  -1801    366       C  
ATOM   2566  CD2 TYR B 199      43.463  52.090 368.787  1.00 87.04           C  
ANISOU 2566  CD2 TYR B 199    11086  13917   8070  -1819  -2044    179       C  
ATOM   2567  CE1 TYR B 199      40.731  52.265 369.208  1.00 88.28           C  
ANISOU 2567  CE1 TYR B 199    11494  14029   8019  -1175  -1684    140       C  
ATOM   2568  CE2 TYR B 199      42.687  52.926 367.985  1.00 86.88           C  
ANISOU 2568  CE2 TYR B 199    11380  13482   8147  -1748  -1938    -33       C  
ATOM   2569  CZ  TYR B 199      41.320  53.010 368.199  1.00 94.05           C  
ANISOU 2569  CZ  TYR B 199    12420  14359   8956  -1410  -1758    -60       C  
ATOM   2570  OH  TYR B 199      40.545  53.827 367.410  1.00 94.13           O  
ANISOU 2570  OH  TYR B 199    12728  13975   9064  -1312  -1657   -252       O  
ATOM   2571  N   ALA B 200      43.800  48.981 373.426  1.00 88.29           N  
ANISOU 2571  N   ALA B 200    10260  15959   7327  -1489  -2257   1133       N  
ATOM   2572  CA  ALA B 200      44.108  47.806 374.248  1.00 88.91           C  
ANISOU 2572  CA  ALA B 200     9967  16465   7348  -1452  -2337   1551       C  
ATOM   2573  C   ALA B 200      43.151  46.647 373.907  1.00 89.77           C  
ANISOU 2573  C   ALA B 200     9874  16505   7729  -1234  -2187   1951       C  
ATOM   2574  O   ALA B 200      41.929  46.840 373.876  1.00 88.43           O  
ANISOU 2574  O   ALA B 200     9833  16283   7485  -1050  -2017   1921       O  
ATOM   2575  CB  ALA B 200      44.026  48.154 375.727  1.00 93.62           C  
ANISOU 2575  CB  ALA B 200    10601  17578   7391  -1423  -2419   1482       C  
ATOM   2576  N   LEU B 201      43.716  45.458 373.616  1.00 84.99           N  
ANISOU 2576  N   LEU B 201     8960  15886   7447  -1253  -2266   2322       N  
ATOM   2577  CA  LEU B 201      42.954  44.262 373.245  1.00 82.95           C  
ANISOU 2577  CA  LEU B 201     8522  15499   7495  -1095  -2188   2723       C  
ATOM   2578  C   LEU B 201      43.307  43.068 374.141  1.00 88.99           C  
ANISOU 2578  C   LEU B 201     8964  16622   8228  -1072  -2338   3198       C  
ATOM   2579  O   LEU B 201      44.487  42.823 374.410  1.00 89.98           O  
ANISOU 2579  O   LEU B 201     8930  16913   8343  -1172  -2508   3252       O  
ATOM   2580  CB  LEU B 201      43.202  43.909 371.773  1.00 79.63           C  
ANISOU 2580  CB  LEU B 201     8098  14571   7585  -1101  -2150   2699       C  
ATOM   2581  N   SER B 202      42.269  42.323 374.588  1.00 85.86           N  
ANISOU 2581  N   SER B 202     8453  16358   7811   -950  -2286   3571       N  
ATOM   2582  CA  SER B 202      42.391  41.148 375.459  1.00 87.92           C  
ANISOU 2582  CA  SER B 202     8417  16939   8048   -934  -2435   4095       C  
ATOM   2583  C   SER B 202      41.999  39.857 374.734  1.00 89.19           C  
ANISOU 2583  C   SER B 202     8455  16731   8704   -867  -2470   4497       C  
ATOM   2584  O   SER B 202      41.009  39.844 373.996  1.00 86.84           O  
ANISOU 2584  O   SER B 202     8274  16129   8591   -815  -2332   4473       O  
ATOM   2585  CB  SER B 202      41.528  41.315 376.707  1.00 94.83           C  
ANISOU 2585  CB  SER B 202     9241  18371   8419   -888  -2386   4255       C  
ATOM   2586  OG  SER B 202      40.143  41.245 376.404  1.00104.00           O  
ANISOU 2586  OG  SER B 202    10461  19457   9597   -784  -2209   4350       O  
ATOM   2587  N   SER B 203      42.760  38.771 374.972  1.00 86.20           N  
ANISOU 2587  N   SER B 203     7848  16375   8528   -863  -2675   4872       N  
ATOM   2588  CA  SER B 203      42.516  37.454 374.378  1.00 85.18           C  
ANISOU 2588  CA  SER B 203     7625  15861   8877   -793  -2775   5265       C  
ATOM   2589  C   SER B 203      42.670  36.359 375.425  1.00 92.46           C  
ANISOU 2589  C   SER B 203     8293  17081   9754   -795  -2990   5840       C  
ATOM   2590  O   SER B 203      43.639  36.377 376.182  1.00 94.25           O  
ANISOU 2590  O   SER B 203     8374  17650   9786   -815  -3119   5886       O  
ATOM   2591  CB  SER B 203      43.463  37.209 373.212  1.00 86.28           C  
ANISOU 2591  CB  SER B 203     7801  15528   9455   -728  -2828   5054       C  
ATOM   2592  OG  SER B 203      43.149  36.004 372.534  1.00 93.96           O  
ANISOU 2592  OG  SER B 203     8749  16061  10892   -633  -2929   5355       O  
ATOM   2593  N   ARG B 204      41.720  35.405 375.463  1.00 89.97           N  
ANISOU 2593  N   ARG B 204     7921  16644   9621   -797  -3046   6304       N  
ATOM   2594  CA  ARG B 204      41.708  34.321 376.446  1.00 93.67           C  
ANISOU 2594  CA  ARG B 204     8157  17366  10067   -828  -3268   6929       C  
ATOM   2595  C   ARG B 204      41.851  32.931 375.811  1.00 98.28           C  
ANISOU 2595  C   ARG B 204     8725  17381  11237   -766  -3490   7291       C  
ATOM   2596  O   ARG B 204      41.124  32.599 374.869  1.00 95.75           O  
ANISOU 2596  O   ARG B 204     8553  16575  11252   -762  -3450   7266       O  
ATOM   2597  CB  ARG B 204      40.417  34.380 377.280  1.00 95.29           C  
ANISOU 2597  CB  ARG B 204     8278  18029   9900   -926  -3183   7258       C  
ATOM   2598  N   LEU B 205      42.786  32.118 376.356  1.00 98.07           N  
ANISOU 2598  N   LEU B 205     8525  17417  11319   -706  -3743   7627       N  
ATOM   2599  CA  LEU B 205      43.039  30.733 375.946  1.00 99.60           C  
ANISOU 2599  CA  LEU B 205     8710  17087  12047   -604  -4011   8004       C  
ATOM   2600  C   LEU B 205      42.711  29.787 377.105  1.00108.15           C  
ANISOU 2600  C   LEU B 205     9597  18447  13046   -707  -4245   8733       C  
ATOM   2601  O   LEU B 205      43.367  29.852 378.146  1.00110.50           O  
ANISOU 2601  O   LEU B 205     9689  19255  13039   -712  -4336   8925       O  
ATOM   2602  CB  LEU B 205      44.495  30.531 375.468  1.00 99.68           C  
ANISOU 2602  CB  LEU B 205     8686  16882  12308   -386  -4125   7768       C  
ATOM   2603  CG  LEU B 205      44.941  29.076 375.228  1.00107.18           C  
ANISOU 2603  CG  LEU B 205     9616  17337  13770   -201  -4439   8150       C  
ATOM   2604  CD1 LEU B 205      44.605  28.609 373.826  1.00105.31           C  
ANISOU 2604  CD1 LEU B 205     9626  16357  14030    -78  -4436   7916       C  
ATOM   2605  CD2 LEU B 205      46.413  28.914 375.481  1.00111.77           C  
ANISOU 2605  CD2 LEU B 205    10014  18089  14365      2  -4578   8117       C  
ATOM   2606  N   ARG B 206      41.702  28.916 376.926  1.00106.24           N  
ANISOU 2606  N   ARG B 206     9413  17891  13064   -815  -4357   9161       N  
ATOM   2607  CA  ARG B 206      41.300  27.953 377.950  1.00111.03           C  
ANISOU 2607  CA  ARG B 206     9839  18721  13627   -961  -4603   9925       C  
ATOM   2608  C   ARG B 206      41.669  26.536 377.525  1.00118.63           C  
ANISOU 2608  C   ARG B 206    10875  19005  15193   -862  -4968  10308       C  
ATOM   2609  O   ARG B 206      41.266  26.080 376.451  1.00116.67           O  
ANISOU 2609  O   ARG B 206    10857  18071  15400   -824  -5024  10188       O  
ATOM   2610  CB  ARG B 206      39.800  28.055 378.262  1.00111.18           C  
ANISOU 2610  CB  ARG B 206     9827  18990  13428  -1208  -4490  10221       C  
ATOM   2611  N   VAL B 207      42.461  25.858 378.373  1.00120.15           N  
ANISOU 2611  N   VAL B 207    10884  19389  15377   -805  -5229  10753       N  
ATOM   2612  CA  VAL B 207      42.929  24.485 378.180  1.00123.96           C  
ANISOU 2612  CA  VAL B 207    11427  19272  16401   -670  -5620  11170       C  
ATOM   2613  C   VAL B 207      42.746  23.687 379.479  1.00133.68           C  
ANISOU 2613  C   VAL B 207    12435  20863  17496   -851  -5897  12010       C  
ATOM   2614  O   VAL B 207      42.937  24.239 380.566  1.00134.12           O  
ANISOU 2614  O   VAL B 207    12232  21723  17004   -959  -5793  12153       O  
ATOM   2615  CB  VAL B 207      44.396  24.459 377.703  1.00127.69           C  
ANISOU 2615  CB  VAL B 207    11903  19536  17077   -303  -5678  10786       C  
ATOM   2616  N   SER B 208      42.381  22.390 379.359  1.00134.34           N  
ANISOU 2616  N   SER B 208    12629  20343  18070   -890  -6270  12565       N  
ATOM   2617  CA  SER B 208      42.143  21.466 380.479  1.00140.18           C  
ANISOU 2617  CA  SER B 208    13186  21296  18779  -1088  -6599  13453       C  
ATOM   2618  C   SER B 208      43.335  21.394 381.442  1.00145.53           C  
ANISOU 2618  C   SER B 208    13837  22334  19125   -779  -6584  13250       C  
ATOM   2619  O   SER B 208      44.476  21.607 381.023  1.00145.84           O  
ANISOU 2619  O   SER B 208    13665  22386  19362   -582  -6672  13169       O  
ATOM   2620  CB  SER B 208      41.824  20.069 379.959  1.00143.97           C  
ANISOU 2620  CB  SER B 208    14213  20730  19760   -911  -6823  13382       C  
ATOM   2621  N   ALA B 209      43.056  21.092 382.730  1.00143.90           N  
ANISOU 2621  N   ALA B 209    13674  22521  18481   -834  -6567  13441       N  
ATOM   2622  CA  ALA B 209      44.024  20.998 383.834  1.00145.28           C  
ANISOU 2622  CA  ALA B 209    13785  23109  18307   -623  -6600  13381       C  
ATOM   2623  C   ALA B 209      45.242  20.117 383.512  1.00149.89           C  
ANISOU 2623  C   ALA B 209    14660  23023  19268   -135  -6803  13089       C  
ATOM   2624  O   ALA B 209      46.349  20.445 383.942  1.00150.18           O  
ANISOU 2624  O   ALA B 209    14496  23439  19124     50  -6826  12971       O  
ATOM   2625  CB  ALA B 209      43.334  20.475 385.083  1.00146.27           C  
ANISOU 2625  CB  ALA B 209    14184  23399  17992   -657  -6518  13388       C  
ATOM   2626  N   THR B 210      45.038  19.018 382.752  1.00148.19           N  
ANISOU 2626  N   THR B 210    14738  21949  19619    -16  -7045  13259       N  
ATOM   2627  CA  THR B 210      46.084  18.073 382.349  1.00149.93           C  
ANISOU 2627  CA  THR B 210    15205  21526  20235    465  -7282  13106       C  
ATOM   2628  C   THR B 210      47.109  18.714 381.394  1.00152.21           C  
ANISOU 2628  C   THR B 210    15269  21792  20771    693  -7247  12752       C  
ATOM   2629  O   THR B 210      48.276  18.315 381.408  1.00153.58           O  
ANISOU 2629  O   THR B 210    15451  21865  21038   1108  -7370  12588       O  
ATOM   2630  CB  THR B 210      45.453  16.837 381.703  1.00156.12           C  
ANISOU 2630  CB  THR B 210    16795  21275  21248    756  -7248  12645       C  
ATOM   2631  N   PHE B 211      46.676  19.703 380.581  1.00146.68           N  
ANISOU 2631  N   PHE B 211    14226  21270  20236    358  -7152  12868       N  
ATOM   2632  CA  PHE B 211      47.524  20.408 379.614  1.00145.04           C  
ANISOU 2632  CA  PHE B 211    13742  21086  20279    496  -7105  12620       C  
ATOM   2633  C   PHE B 211      48.398  21.489 380.277  1.00146.98           C  
ANISOU 2633  C   PHE B 211    13667  22228  19952    515  -6856  12326       C  
ATOM   2634  O   PHE B 211      49.578  21.602 379.932  1.00146.32           O  
ANISOU 2634  O   PHE B 211    13504  22149  19943    853  -6839  11966       O  
ATOM   2635  CB  PHE B 211      46.672  21.037 378.499  1.00141.20           C  
ANISOU 2635  CB  PHE B 211    13522  20259  19868    378  -6817  12054       C  
ATOM   2636  N   TRP B 212      47.820  22.283 381.210  1.00142.48           N  
ANISOU 2636  N   TRP B 212    12912  22427  18799    158  -6671  12467       N  
ATOM   2637  CA  TRP B 212      48.501  23.380 381.913  1.00140.82           C  
ANISOU 2637  CA  TRP B 212    12436  23077  17993    110  -6454  12182       C  
ATOM   2638  C   TRP B 212      49.588  22.883 382.859  1.00148.06           C  
ANISOU 2638  C   TRP B 212    13200  24290  18767    325  -6662  12385       C  
ATOM   2639  O   TRP B 212      50.667  23.477 382.904  1.00148.37           O  
ANISOU 2639  O   TRP B 212    12922  24823  18630    404  -6634  12264       O  
ATOM   2640  CB  TRP B 212      47.493  24.230 382.699  1.00138.16           C  
ANISOU 2640  CB  TRP B 212    12019  23411  17064   -276  -6217  12229       C  
ATOM   2641  N   GLN B 213      49.298  21.806 383.617  1.00145.86           N  
ANISOU 2641  N   GLN B 213    13238  23675  18508    449  -6830  12550       N  
ATOM   2642  CA  GLN B 213      50.201  21.193 384.595  1.00147.59           C  
ANISOU 2642  CA  GLN B 213    13522  24002  18552    731  -6991  12535       C  
ATOM   2643  C   GLN B 213      51.423  20.535 383.940  1.00152.43           C  
ANISOU 2643  C   GLN B 213    14252  24098  19568   1253  -7157  12250       C  
ATOM   2644  O   GLN B 213      52.481  20.475 384.572  1.00153.16           O  
ANISOU 2644  O   GLN B 213    14278  24464  19453   1497  -7228  12082       O  
ATOM   2645  CB  GLN B 213      49.444  20.158 385.439  1.00148.94           C  
ANISOU 2645  CB  GLN B 213    14187  23793  18611    790  -7055  12570       C  
ATOM   2646  CG  GLN B 213      49.196  20.600 386.877  1.00153.30           C  
ANISOU 2646  CG  GLN B 213    15348  24523  18375    905  -6669  11516       C  
ATOM   2647  CD  GLN B 213      48.105  21.633 386.996  1.00160.52           C  
ANISOU 2647  CD  GLN B 213    16735  25386  18870    786  -6158  10544       C  
ATOM   2648  OE1 GLN B 213      46.912  21.321 386.937  1.00155.70           O  
ANISOU 2648  OE1 GLN B 213    16158  24699  18301    554  -6135  10940       O  
ATOM   2649  NE2 GLN B 213      48.495  22.884 387.188  1.00153.48           N  
ANISOU 2649  NE2 GLN B 213    15215  25387  17713    472  -6133  10846       N  
ATOM   2650  N   ASN B 214      51.275  20.042 382.687  1.00150.11           N  
ANISOU 2650  N   ASN B 214    13976  23160  19901   1369  -7295  12434       N  
ATOM   2651  CA  ASN B 214      52.340  19.386 381.924  1.00152.02           C  
ANISOU 2651  CA  ASN B 214    14255  22921  20585   1884  -7480  12279       C  
ATOM   2652  C   ASN B 214      53.459  20.392 381.573  1.00154.52           C  
ANISOU 2652  C   ASN B 214    14234  23753  20724   2006  -7294  11838       C  
ATOM   2653  O   ASN B 214      53.206  21.350 380.836  1.00152.56           O  
ANISOU 2653  O   ASN B 214    13628  23789  20550   1699  -7140  11952       O  
ATOM   2654  CB  ASN B 214      51.780  18.725 380.661  1.00152.88           C  
ANISOU 2654  CB  ASN B 214    14595  22139  21355   1992  -7620  12369       C  
ATOM   2655  N   PRO B 215      54.694  20.204 382.107  1.00154.67           N  
ANISOU 2655  N   PRO B 215    14013  24120  20635   2295  -7439  11890       N  
ATOM   2656  CA  PRO B 215      55.774  21.166 381.823  1.00154.16           C  
ANISOU 2656  CA  PRO B 215    13505  24672  20398   2335  -7299  11652       C  
ATOM   2657  C   PRO B 215      56.427  20.977 380.448  1.00158.11           C  
ANISOU 2657  C   PRO B 215    13976  24729  21369   2744  -7289  11359       C  
ATOM   2658  O   PRO B 215      57.260  21.800 380.060  1.00157.55           O  
ANISOU 2658  O   PRO B 215    13469  25208  21183   2725  -7144  11252       O  
ATOM   2659  CB  PRO B 215      56.785  20.913 382.957  1.00157.69           C  
ANISOU 2659  CB  PRO B 215    13959  25462  20496   2578  -7420  11485       C  
ATOM   2660  CG  PRO B 215      56.140  19.891 383.875  1.00161.73           C  
ANISOU 2660  CG  PRO B 215    15088  25459  20902   2700  -7541  11387       C  
ATOM   2661  CD  PRO B 215      55.164  19.153 383.027  1.00158.53           C  
ANISOU 2661  CD  PRO B 215    14829  24385  21019   2665  -7654  11834       C  
ATOM   2662  N   ARG B 216      56.052  19.910 379.712  1.00158.17           N  
ANISOU 2662  N   ARG B 216    14184  23917  21995   3025  -7526  11638       N  
ATOM   2663  CA  ARG B 216      56.576  19.602 378.379  1.00159.09           C  
ANISOU 2663  CA  ARG B 216    14301  23528  22618   3467  -7552  11387       C  
ATOM   2664  C   ARG B 216      55.920  20.480 377.296  1.00156.59           C  
ANISOU 2664  C   ARG B 216    14224  23016  22255   3267  -7184  10703       C  
ATOM   2665  O   ARG B 216      56.609  20.920 376.372  1.00154.30           O  
ANISOU 2665  O   ARG B 216    13872  22770  21985   3532  -6996  10148       O  
ATOM   2666  CB  ARG B 216      56.379  18.115 378.051  1.00162.52           C  
ANISOU 2666  CB  ARG B 216    15227  22978  23547   3915  -7861  11439       C  
ATOM   2667  N   ASN B 217      54.598  20.728 377.407  1.00149.79           N  
ANISOU 2667  N   ASN B 217    13613  21976  21325   2810  -7086  10771       N  
ATOM   2668  CA  ASN B 217      53.841  21.549 376.461  1.00143.45           C  
ANISOU 2668  CA  ASN B 217    13048  20984  20473   2589  -6754  10192       C  
ATOM   2669  C   ASN B 217      54.201  23.031 376.617  1.00143.52           C  
ANISOU 2669  C   ASN B 217    12827  21774  19930   2326  -6399   9754       C  
ATOM   2670  O   ASN B 217      54.409  23.500 377.740  1.00143.87           O  
ANISOU 2670  O   ASN B 217    12616  22511  19537   2074  -6395  10003       O  
ATOM   2671  CB  ASN B 217      52.342  21.336 376.648  1.00142.21           C  
ANISOU 2671  CB  ASN B 217    13170  20490  20372   2186  -6778  10471       C  
ATOM   2672  N   HIS B 218      54.289  23.756 375.485  1.00136.12           N  
ANISOU 2672  N   HIS B 218    11992  20717  19011   2379  -6124   9107       N  
ATOM   2673  CA  HIS B 218      54.642  25.178 375.444  1.00132.18           C  
ANISOU 2673  CA  HIS B 218    11332  20843  18048   2125  -5809   8649       C  
ATOM   2674  C   HIS B 218      53.485  26.021 374.914  1.00130.06           C  
ANISOU 2674  C   HIS B 218    11346  20401  17668   1769  -5526   8290       C  
ATOM   2675  O   HIS B 218      52.782  25.605 373.990  1.00128.02           O  
ANISOU 2675  O   HIS B 218    11383  19495  17765   1858  -5506   8146       O  
ATOM   2676  CB  HIS B 218      55.902  25.393 374.577  1.00133.36           C  
ANISOU 2676  CB  HIS B 218    11291  21114  18264   2479  -5728   8225       C  
ATOM   2677  CG  HIS B 218      56.255  26.832 374.333  1.00133.26           C  
ANISOU 2677  CG  HIS B 218    11154  21641  17836   2191  -5429   7744       C  
ATOM   2678  ND1 HIS B 218      55.934  27.463 373.142  1.00130.91           N  
ANISOU 2678  ND1 HIS B 218    11044  21087  17611   2156  -5176   7206       N  
ATOM   2679  CD2 HIS B 218      56.874  27.722 375.143  1.00135.43           C  
ANISOU 2679  CD2 HIS B 218    11165  22663  17630   1904  -5377   7751       C  
ATOM   2680  CE1 HIS B 218      56.379  28.704 373.260  1.00128.33           C  
ANISOU 2680  CE1 HIS B 218    10563  21329  16868   1851  -4988   6923       C  
ATOM   2681  NE2 HIS B 218      56.950  28.908 374.448  1.00131.28           N  
ANISOU 2681  NE2 HIS B 218    10677  22304  16899   1685  -5106   7218       N  
ATOM   2682  N   PHE B 219      53.312  27.218 375.496  1.00123.63           N  
ANISOU 2682  N   PHE B 219    10449  20173  16353   1383  -5322   8134       N  
ATOM   2683  CA  PHE B 219      52.292  28.182 375.098  1.00118.41           C  
ANISOU 2683  CA  PHE B 219    10026  19449  15516   1060  -5043   7779       C  
ATOM   2684  C   PHE B 219      52.959  29.482 374.634  1.00118.58           C  
ANISOU 2684  C   PHE B 219     9968  19841  15246    946  -4800   7218       C  
ATOM   2685  O   PHE B 219      53.827  30.018 375.329  1.00119.37           O  
ANISOU 2685  O   PHE B 219     9811  20542  15002    851  -4826   7224       O  
ATOM   2686  CB  PHE B 219      51.309  28.443 376.249  1.00120.48           C  
ANISOU 2686  CB  PHE B 219    10312  20036  15429    706  -5036   8112       C  
ATOM   2687  N   ARG B 220      52.569  29.961 373.440  1.00111.04           N  
ANISOU 2687  N   ARG B 220     9231  18523  14437    939  -4587   6759       N  
ATOM   2688  CA  ARG B 220      53.074  31.188 372.819  1.00107.94           C  
ANISOU 2688  CA  ARG B 220     8808  18380  13822    804  -4361   6236       C  
ATOM   2689  C   ARG B 220      51.921  32.054 372.322  1.00107.28           C  
ANISOU 2689  C   ARG B 220     9031  18077  13653    543  -4114   5911       C  
ATOM   2690  O   ARG B 220      50.902  31.525 371.869  1.00105.63           O  
ANISOU 2690  O   ARG B 220     9053  17372  13710    589  -4096   5979       O  
ATOM   2691  CB  ARG B 220      54.021  30.862 371.656  1.00108.56           C  
ANISOU 2691  CB  ARG B 220     8779  18274  14193   1147  -4358   5986       C  
ATOM   2692  N   CYS B 221      52.086  33.383 372.395  1.00101.54           N  
ANISOU 2692  N   CYS B 221     8311  17710  12559    266  -3944   5566       N  
ATOM   2693  CA  CYS B 221      51.072  34.338 371.952  1.00 97.15           C  
ANISOU 2693  CA  CYS B 221     8041  16984  11889     36  -3711   5234       C  
ATOM   2694  C   CYS B 221      51.732  35.462 371.137  1.00 98.11           C  
ANISOU 2694  C   CYS B 221     8164  17209  11905    -79  -3558   4755       C  
ATOM   2695  O   CYS B 221      52.457  36.284 371.702  1.00 98.99           O  
ANISOU 2695  O   CYS B 221     8145  17788  11677   -281  -3580   4649       O  
ATOM   2696  CB  CYS B 221      50.292  34.883 373.145  1.00 97.72           C  
ANISOU 2696  CB  CYS B 221     8188  17386  11554   -226  -3682   5360       C  
ATOM   2697  SG  CYS B 221      48.947  36.009 372.700  1.00 97.51           S  
ANISOU 2697  SG  CYS B 221     8514  17149  11386   -433  -3407   5000       S  
ATOM   2698  N   GLN B 222      51.485  35.479 369.808  1.00 90.80           N  
ANISOU 2698  N   GLN B 222     7380  15856  11262     29  -3425   4484       N  
ATOM   2699  CA  GLN B 222      52.050  36.460 368.876  1.00 88.11           C  
ANISOU 2699  CA  GLN B 222     7038  15578  10863    -79  -3281   4070       C  
ATOM   2700  C   GLN B 222      51.022  37.506 368.437  1.00 86.79           C  
ANISOU 2700  C   GLN B 222     7188  15198  10592   -317  -3072   3766       C  
ATOM   2701  O   GLN B 222      49.855  37.176 368.214  1.00 84.59           O  
ANISOU 2701  O   GLN B 222     7125  14545  10470   -263  -3003   3816       O  
ATOM   2702  CB  GLN B 222      52.627  35.753 367.641  1.00 89.60           C  
ANISOU 2702  CB  GLN B 222     7118  15516  11409    244  -3280   3977       C  
ATOM   2703  N   VAL B 223      51.469  38.772 368.316  1.00 81.44           N  
ANISOU 2703  N   VAL B 223     6535  14758   9650   -588  -2993   3469       N  
ATOM   2704  CA  VAL B 223      50.655  39.911 367.870  1.00 77.86           C  
ANISOU 2704  CA  VAL B 223     6387  14116   9082   -810  -2814   3155       C  
ATOM   2705  C   VAL B 223      51.381  40.572 366.691  1.00 79.39           C  
ANISOU 2705  C   VAL B 223     6540  14284   9343   -897  -2731   2860       C  
ATOM   2706  O   VAL B 223      52.449  41.167 366.880  1.00 81.03           O  
ANISOU 2706  O   VAL B 223     6573  14859   9356  -1081  -2807   2790       O  
ATOM   2707  CB  VAL B 223      50.329  40.921 369.011  1.00 82.57           C  
ANISOU 2707  CB  VAL B 223     7128  14992   9254  -1085  -2827   3086       C  
ATOM   2708  CG1 VAL B 223      49.630  42.170 368.475  1.00 79.86           C  
ANISOU 2708  CG1 VAL B 223     7111  14430   8804  -1277  -2662   2730       C  
ATOM   2709  CG2 VAL B 223      49.483  40.273 370.099  1.00 83.53           C  
ANISOU 2709  CG2 VAL B 223     7269  15188   9279   -992  -2881   3395       C  
ATOM   2710  N   GLN B 224      50.818  40.438 365.475  1.00 71.78           N  
ANISOU 2710  N   GLN B 224     5713  12920   8640   -781  -2590   2714       N  
ATOM   2711  CA  GLN B 224      51.405  41.014 364.266  1.00 70.03           C  
ANISOU 2711  CA  GLN B 224     5447  12681   8481   -852  -2495   2461       C  
ATOM   2712  C   GLN B 224      50.936  42.461 364.134  1.00 71.98           C  
ANISOU 2712  C   GLN B 224     5967  12865   8518  -1193  -2392   2203       C  
ATOM   2713  O   GLN B 224      49.752  42.711 363.922  1.00 69.32           O  
ANISOU 2713  O   GLN B 224     5916  12198   8224  -1193  -2275   2120       O  
ATOM   2714  CB  GLN B 224      51.054  40.165 363.028  1.00 69.54           C  
ANISOU 2714  CB  GLN B 224     5404  12246   8773   -553  -2407   2420       C  
ATOM   2715  CG  GLN B 224      51.394  40.798 361.681  1.00 75.74           C  
ANISOU 2715  CG  GLN B 224     6165  13010   9605   -618  -2279   2160       C  
ATOM   2716  CD  GLN B 224      52.840  40.667 361.310  1.00 94.18           C  
ANISOU 2716  CD  GLN B 224     8124  15751  11910   -543  -2340   2167       C  
ATOM   2717  OE1 GLN B 224      53.267  39.655 360.752  1.00 91.72           O  
ANISOU 2717  OE1 GLN B 224     7626  15420  11803   -183  -2365   2212       O  
ATOM   2718  NE2 GLN B 224      53.615  41.706 361.575  1.00 86.44           N  
ANISOU 2718  NE2 GLN B 224     7028  15151  10666   -878  -2374   2115       N  
ATOM   2719  N   PHE B 225      51.864  43.409 364.311  1.00 70.22           N  
ANISOU 2719  N   PHE B 225     5654  12961   8064  -1487  -2458   2094       N  
ATOM   2720  CA  PHE B 225      51.590  44.842 364.223  1.00 69.38           C  
ANISOU 2720  CA  PHE B 225     5823  12781   7759  -1836  -2416   1849       C  
ATOM   2721  C   PHE B 225      51.954  45.351 362.837  1.00 72.84           C  
ANISOU 2721  C   PHE B 225     6231  13130   8315  -1947  -2324   1690       C  
ATOM   2722  O   PHE B 225      52.916  44.866 362.237  1.00 73.71           O  
ANISOU 2722  O   PHE B 225     6012  13479   8515  -1866  -2346   1760       O  
ATOM   2723  CB  PHE B 225      52.361  45.607 365.316  1.00 74.14           C  
ANISOU 2723  CB  PHE B 225     6383  13766   8020  -2146  -2595   1838       C  
ATOM   2724  CG  PHE B 225      52.244  47.116 365.292  1.00 75.82           C  
ANISOU 2724  CG  PHE B 225     6901  13884   8021  -2530  -2616   1575       C  
ATOM   2725  CD1 PHE B 225      51.085  47.748 365.730  1.00 77.74           C  
ANISOU 2725  CD1 PHE B 225     7547  13847   8143  -2548  -2557   1413       C  
ATOM   2726  CD2 PHE B 225      53.304  47.904 364.858  1.00 79.44           C  
ANISOU 2726  CD2 PHE B 225     7243  14545   8395  -2869  -2713   1503       C  
ATOM   2727  CE1 PHE B 225      50.983  49.143 365.715  1.00 79.25           C  
ANISOU 2727  CE1 PHE B 225     8063  13895   8154  -2866  -2604   1152       C  
ATOM   2728  CE2 PHE B 225      53.201  49.298 364.845  1.00 82.78           C  
ANISOU 2728  CE2 PHE B 225     7989  14819   8646  -3248  -2777   1276       C  
ATOM   2729  CZ  PHE B 225      52.041  49.908 365.271  1.00 79.84           C  
ANISOU 2729  CZ  PHE B 225     8058  14103   8176  -3227  -2728   1087       C  
ATOM   2730  N   TYR B 226      51.176  46.321 362.330  1.00 67.84           N  
ANISOU 2730  N   TYR B 226     5929  12183   7665  -2113  -2221   1489       N  
ATOM   2731  CA  TYR B 226      51.388  46.926 361.018  1.00 66.96           C  
ANISOU 2731  CA  TYR B 226     5827  11970   7644  -2256  -2133   1357       C  
ATOM   2732  C   TYR B 226      51.659  48.426 361.185  1.00 73.72           C  
ANISOU 2732  C   TYR B 226     6893  12844   8274  -2704  -2222   1206       C  
ATOM   2733  O   TYR B 226      50.727  49.209 361.387  1.00 72.59           O  
ANISOU 2733  O   TYR B 226     7136  12382   8063  -2789  -2188   1055       O  
ATOM   2734  CB  TYR B 226      50.182  46.657 360.096  1.00 64.49           C  
ANISOU 2734  CB  TYR B 226     5722  11224   7557  -2039  -1946   1285       C  
ATOM   2735  CG  TYR B 226      49.979  45.191 359.774  1.00 64.82           C  
ANISOU 2735  CG  TYR B 226     5583  11199   7848  -1637  -1895   1416       C  
ATOM   2736  CD1 TYR B 226      50.657  44.588 358.718  1.00 67.19           C  
ANISOU 2736  CD1 TYR B 226     5625  11598   8307  -1478  -1851   1414       C  
ATOM   2737  CD2 TYR B 226      49.100  44.408 360.517  1.00 64.53           C  
ANISOU 2737  CD2 TYR B 226     5641  11003   7876  -1416  -1906   1544       C  
ATOM   2738  CE1 TYR B 226      50.471  43.240 358.413  1.00 67.43           C  
ANISOU 2738  CE1 TYR B 226     5540  11508   8572  -1087  -1838   1498       C  
ATOM   2739  CE2 TYR B 226      48.907  43.058 360.223  1.00 65.00           C  
ANISOU 2739  CE2 TYR B 226     5574  10937   8186  -1077  -1905   1677       C  
ATOM   2740  CZ  TYR B 226      49.589  42.480 359.163  1.00 72.49           C  
ANISOU 2740  CZ  TYR B 226     6314  11921   9308   -904  -1879   1633       C  
ATOM   2741  OH  TYR B 226      49.421  41.149 358.868  1.00 73.15           O  
ANISOU 2741  OH  TYR B 226     6320  11829   9644   -550  -1909   1728       O  
ATOM   2742  N   GLY B 227      52.943  48.790 361.145  1.00 73.81           N  
ANISOU 2742  N   GLY B 227     6644  13235   8163  -2978  -2356   1258       N  
ATOM   2743  CA  GLY B 227      53.413  50.165 361.290  1.00 76.10           C  
ANISOU 2743  CA  GLY B 227     7099  13569   8246  -3468  -2503   1152       C  
ATOM   2744  C   GLY B 227      54.142  50.694 360.071  1.00 81.58           C  
ANISOU 2744  C   GLY B 227     7626  14380   8989  -3732  -2492   1174       C  
ATOM   2745  O   GLY B 227      54.051  50.106 358.989  1.00 79.50           O  
ANISOU 2745  O   GLY B 227     7207  14080   8919  -3506  -2323   1207       O  
ATOM   2746  N   LEU B 228      54.870  51.816 360.241  1.00 81.75           N  
ANISOU 2746  N   LEU B 228     7683  14557   8821  -4233  -2688   1162       N  
ATOM   2747  CA  LEU B 228      55.633  52.474 359.172  1.00 83.32           C  
ANISOU 2747  CA  LEU B 228     7711  14924   9021  -4587  -2719   1234       C  
ATOM   2748  C   LEU B 228      56.749  51.572 358.652  1.00 89.16           C  
ANISOU 2748  C   LEU B 228     7838  16257   9780  -4454  -2681   1447       C  
ATOM   2749  O   LEU B 228      57.420  50.911 359.445  1.00 90.28           O  
ANISOU 2749  O   LEU B 228     7692  16784   9826  -4363  -2780   1560       O  
ATOM   2750  CB  LEU B 228      56.218  53.806 359.664  1.00 86.89           C  
ANISOU 2750  CB  LEU B 228     8366  15389   9259  -5195  -2993   1199       C  
ATOM   2751  N   SER B 229      56.926  51.525 357.319  1.00 86.06           N  
ANISOU 2751  N   SER B 229     7240  15961   9498  -4408  -2535   1500       N  
ATOM   2752  CA  SER B 229      57.962  50.713 356.676  1.00 88.11           C  
ANISOU 2752  CA  SER B 229     6910  16812   9757  -4222  -2472   1671       C  
ATOM   2753  C   SER B 229      59.340  51.326 356.909  1.00 98.36           C  
ANISOU 2753  C   SER B 229     7848  18704  10819  -4712  -2683   1864       C  
ATOM   2754  O   SER B 229      59.433  52.532 357.155  1.00 99.79           O  
ANISOU 2754  O   SER B 229     8279  18762  10874  -5263  -2869   1857       O  
ATOM   2755  CB  SER B 229      57.690  50.577 355.179  1.00 89.74           C  
ANISOU 2755  CB  SER B 229     7028  16971  10099  -4048  -2257   1645       C  
ATOM   2756  OG  SER B 229      57.912  51.792 354.480  1.00 98.73           O  
ANISOU 2756  OG  SER B 229     8302  18044  11167  -4547  -2303   1672       O  
ATOM   2757  N   GLU B 230      60.410  50.508 356.805  1.00 98.47           N  
ANISOU 2757  N   GLU B 230     7277  19365  10773  -4506  -2669   2041       N  
ATOM   2758  CA  GLU B 230      61.801  50.954 356.968  1.00103.51           C  
ANISOU 2758  CA  GLU B 230     7457  20699  11175  -4927  -2856   2274       C  
ATOM   2759  C   GLU B 230      62.178  51.985 355.874  1.00110.01           C  
ANISOU 2759  C   GLU B 230     8202  21684  11911  -5446  -2879   2379       C  
ATOM   2760  O   GLU B 230      63.204  52.663 355.991  1.00113.87           O  
ANISOU 2760  O   GLU B 230     8430  22644  12193  -5979  -3088   2584       O  
ATOM   2761  CB  GLU B 230      62.759  49.752 356.949  1.00107.01           C  
ANISOU 2761  CB  GLU B 230     7269  21800  11591  -4468  -2789   2432       C  
ATOM   2762  N   ASN B 231      61.312  52.113 354.837  1.00103.89           N  
ANISOU 2762  N   ASN B 231     7660  20521  11291  -5315  -2681   2262       N  
ATOM   2763  CA  ASN B 231      61.421  53.052 353.721  1.00105.01           C  
ANISOU 2763  CA  ASN B 231     7790  20728  11382  -5761  -2679   2366       C  
ATOM   2764  C   ASN B 231      60.983  54.470 354.141  1.00109.34           C  
ANISOU 2764  C   ASN B 231     8900  20736  11907  -6378  -2905   2315       C  
ATOM   2765  O   ASN B 231      61.360  55.439 353.480  1.00111.54           O  
ANISOU 2765  O   ASN B 231     9155  21120  12104  -6919  -3016   2477       O  
ATOM   2766  CB  ASN B 231      60.580  52.567 352.538  1.00102.46           C  
ANISOU 2766  CB  ASN B 231     7526  20175  11229  -5342  -2390   2247       C  
ATOM   2767  N   ASP B 232      60.197  54.588 355.234  1.00103.76           N  
ANISOU 2767  N   ASP B 232     8697  19464  11263  -6286  -2983   2097       N  
ATOM   2768  CA  ASP B 232      59.704  55.865 355.763  1.00104.16           C  
ANISOU 2768  CA  ASP B 232     9342  18948  11287  -6758  -3202   1978       C  
ATOM   2769  C   ASP B 232      60.674  56.452 356.785  1.00112.26           C  
ANISOU 2769  C   ASP B 232    10304  20262  12087  -7288  -3544   2078       C  
ATOM   2770  O   ASP B 232      61.296  55.705 357.543  1.00113.03           O  
ANISOU 2770  O   ASP B 232    10063  20805  12080  -7120  -3587   2142       O  
ATOM   2771  CB  ASP B 232      58.314  55.695 356.404  1.00102.09           C  
ANISOU 2771  CB  ASP B 232     9633  17995  11161  -6353  -3102   1678       C  
ATOM   2772  CG  ASP B 232      57.245  55.101 355.500  1.00108.25           C  
ANISOU 2772  CG  ASP B 232    10515  18452  12164  -5852  -2791   1574       C  
ATOM   2773  OD1 ASP B 232      57.219  55.452 354.296  1.00108.41           O  
ANISOU 2773  OD1 ASP B 232    10516  18431  12245  -5998  -2709   1646       O  
ATOM   2774  OD2 ASP B 232      56.410  54.316 356.005  1.00111.42           O  
ANISOU 2774  OD2 ASP B 232    11028  18639  12670  -5345  -2648   1435       O  
ATOM   2775  N   GLU B 233      60.784  57.793 356.814  1.00111.48           N  
ANISOU 2775  N   GLU B 233    10552  19888  11919  -7932  -3810   2095       N  
ATOM   2776  CA  GLU B 233      61.665  58.524 357.731  1.00116.07           C  
ANISOU 2776  CA  GLU B 233    11154  20666  12283  -8539  -4191   2175       C  
ATOM   2777  C   GLU B 233      61.120  58.509 359.165  1.00119.39           C  
ANISOU 2777  C   GLU B 233    12011  20720  12632  -8388  -4315   1887       C  
ATOM   2778  O   GLU B 233      59.907  58.385 359.370  1.00115.22           O  
ANISOU 2778  O   GLU B 233    11955  19595  12228  -7992  -4168   1612       O  
ATOM   2779  CB  GLU B 233      61.862  59.970 357.254  1.00120.85           C  
ANISOU 2779  CB  GLU B 233    12067  20986  12866  -9274  -4462   2271       C  
ATOM   2780  N   TRP B 234      62.030  58.629 360.153  1.00119.75           N  
ANISOU 2780  N   TRP B 234    11869  21179  12451  -8709  -4588   1967       N  
ATOM   2781  CA  TRP B 234      61.717  58.633 361.583  1.00120.05           C  
ANISOU 2781  CA  TRP B 234    12246  21020  12347  -8630  -4746   1727       C  
ATOM   2782  C   TRP B 234      62.697  59.564 362.326  1.00130.58           C  
ANISOU 2782  C   TRP B 234    13613  22577  13424  -9376  -5195   1802       C  
ATOM   2783  O   TRP B 234      63.770  59.133 362.765  1.00133.06           O  
ANISOU 2783  O   TRP B 234    13390  23600  13568  -9541  -5315   2039       O  
ATOM   2784  CB  TRP B 234      61.753  57.195 362.136  1.00116.32           C  
ANISOU 2784  CB  TRP B 234    11374  20952  11869  -8002  -4534   1764       C  
ATOM   2785  CG  TRP B 234      61.401  57.079 363.588  1.00117.59           C  
ANISOU 2785  CG  TRP B 234    11829  20985  11867  -7868  -4660   1554       C  
ATOM   2786  CD1 TRP B 234      62.257  56.839 364.620  1.00123.77           C  
ANISOU 2786  CD1 TRP B 234    12331  22284  12411  -8014  -4870   1656       C  
ATOM   2787  CD2 TRP B 234      60.096  57.197 364.165  1.00114.70           C  
ANISOU 2787  CD2 TRP B 234    12058  19988  11534  -7545  -4576   1222       C  
ATOM   2788  NE1 TRP B 234      61.566  56.794 365.807  1.00122.64           N  
ANISOU 2788  NE1 TRP B 234    12584  21873  12143  -7809  -4923   1403       N  
ATOM   2789  CE2 TRP B 234      60.237  57.015 365.559  1.00120.53           C  
ANISOU 2789  CE2 TRP B 234    12849  20916  12030  -7514  -4740   1133       C  
ATOM   2790  CE3 TRP B 234      58.815  57.440 363.641  1.00112.35           C  
ANISOU 2790  CE3 TRP B 234    12232  19028  11427  -7273  -4377   1004       C  
ATOM   2791  CZ2 TRP B 234      59.145  57.055 366.434  1.00118.37           C  
ANISOU 2791  CZ2 TRP B 234    13069  20224  11683  -7208  -4699    833       C  
ATOM   2792  CZ3 TRP B 234      57.735  57.493 364.510  1.00112.31           C  
ANISOU 2792  CZ3 TRP B 234    12710  18604  11360  -6967  -4339    712       C  
ATOM   2793  CH2 TRP B 234      57.904  57.300 365.888  1.00114.98           C  
ANISOU 2793  CH2 TRP B 234    13078  19171  11439  -6932  -4493    626       C  
ATOM   2794  N   THR B 235      62.322  60.854 362.437  1.00129.64           N  
ANISOU 2794  N   THR B 235    14134  21840  13282  -9831  -5460   1603       N  
ATOM   2795  CA  THR B 235      63.126  61.906 363.076  1.00135.78           C  
ANISOU 2795  CA  THR B 235    15087  22666  13838 -10607  -5942   1628       C  
ATOM   2796  C   THR B 235      63.061  61.847 364.610  1.00141.26           C  
ANISOU 2796  C   THR B 235    16036  23350  14287 -10551  -6143   1363       C  
ATOM   2797  O   THR B 235      63.945  62.400 365.267  1.00146.04           O  
ANISOU 2797  O   THR B 235    16620  24208  14660 -11147  -6538   1423       O  
ATOM   2798  CB  THR B 235      62.701  63.301 362.584  1.00146.91           C  
ANISOU 2798  CB  THR B 235    17134  23339  15346 -11092  -6171   1510       C  
ATOM   2799  OG1 THR B 235      61.282  63.435 362.687  1.00143.95           O  
ANISOU 2799  OG1 THR B 235    17393  22193  15107 -10589  -5991   1123       O  
ATOM   2800  CG2 THR B 235      63.163  63.591 361.161  1.00146.31           C  
ANISOU 2800  CG2 THR B 235    16730  23437  15424 -11414  -6108   1876       C  
ATOM   2801  N   GLN B 236      62.023  61.196 365.175  1.00133.87           N  
ANISOU 2801  N   GLN B 236    15327  22155  13381  -9864  -5886   1089       N  
ATOM   2802  CA  GLN B 236      61.837  61.064 366.624  1.00135.21           C  
ANISOU 2802  CA  GLN B 236    15729  22346  13297  -9724  -6026    835       C  
ATOM   2803  C   GLN B 236      62.979  60.261 367.260  1.00141.42           C  
ANISOU 2803  C   GLN B 236    15858  23994  13882  -9792  -6114   1111       C  
ATOM   2804  O   GLN B 236      63.489  59.323 366.641  1.00139.17           O  
ANISOU 2804  O   GLN B 236    14928  24238  13711  -9557  -5890   1435       O  
ATOM   2805  CB  GLN B 236      60.485  60.409 366.941  1.00131.47           C  
ANISOU 2805  CB  GLN B 236    15540  21500  12914  -8955  -5685    569       C  
ATOM   2806  N   ASP B 237      63.392  60.655 368.483  1.00142.40           N  
ANISOU 2806  N   ASP B 237    16155  24260  13690 -10099  -6453    971       N  
ATOM   2807  CA  ASP B 237      64.473  60.014 369.241  1.00145.22           C  
ANISOU 2807  CA  ASP B 237    15943  25428  13807 -10216  -6599   1216       C  
ATOM   2808  C   ASP B 237      64.086  58.599 369.682  1.00145.19           C  
ANISOU 2808  C   ASP B 237    15597  25737  13830  -9453  -6267   1283       C  
ATOM   2809  O   ASP B 237      64.952  57.724 369.738  1.00146.04           O  
ANISOU 2809  O   ASP B 237    15050  26557  13884  -9371  -6245   1613       O  
ATOM   2810  CB  ASP B 237      64.857  60.861 370.463  1.00152.75           C  
ANISOU 2810  CB  ASP B 237    17266  26371  14399 -10744  -7065    995       C  
ATOM   2811  N   ARG B 238      62.785  58.377 369.971  1.00137.26           N  
ANISOU 2811  N   ARG B 238    15028  24211  12913  -8898  -6022    995       N  
ATOM   2812  CA  ARG B 238      62.216  57.093 370.396  1.00133.34           C  
ANISOU 2812  CA  ARG B 238    14301  23897  12463  -8190  -5721   1054       C  
ATOM   2813  C   ARG B 238      62.341  56.027 369.296  1.00133.48           C  
ANISOU 2813  C   ARG B 238    13779  24131  12806  -7772  -5381   1365       C  
ATOM   2814  O   ARG B 238      62.589  56.368 368.139  1.00132.87           O  
ANISOU 2814  O   ARG B 238    13577  23997  12912  -7978  -5330   1478       O  
ATOM   2815  CB  ARG B 238      60.740  57.275 370.786  1.00130.75           C  
ANISOU 2815  CB  ARG B 238    14593  22945  12143  -7778  -5560    682       C  
ATOM   2816  N   ALA B 239      62.179  54.739 369.662  1.00127.27           N  
ANISOU 2816  N   ALA B 239    12684  23596  12079  -7189  -5167   1506       N  
ATOM   2817  CA  ALA B 239      62.271  53.609 368.733  1.00123.75           C  
ANISOU 2817  CA  ALA B 239    11764  23324  11929  -6713  -4866   1762       C  
ATOM   2818  C   ALA B 239      61.150  53.650 367.678  1.00122.60           C  
ANISOU 2818  C   ALA B 239    11939  22552  12092  -6434  -4575   1604       C  
ATOM   2819  O   ALA B 239      60.001  53.961 368.006  1.00120.35           O  
ANISOU 2819  O   ALA B 239    12181  21731  11815  -6282  -4500   1334       O  
ATOM   2820  CB  ALA B 239      62.226  52.298 369.502  1.00123.46           C  
ANISOU 2820  CB  ALA B 239    11448  23578  11884  -6178  -4762   1919       C  
ATOM   2821  N   LYS B 240      61.504  53.355 366.412  1.00117.22           N  
ANISOU 2821  N   LYS B 240    10916  21985  11636  -6367  -4414   1776       N  
ATOM   2822  CA  LYS B 240      60.589  53.370 365.267  1.00112.54           C  
ANISOU 2822  CA  LYS B 240    10548  20886  11327  -6135  -4148   1666       C  
ATOM   2823  C   LYS B 240      59.560  52.227 365.323  1.00111.17           C  
ANISOU 2823  C   LYS B 240    10430  20450  11358  -5449  -3862   1629       C  
ATOM   2824  O   LYS B 240      59.933  51.085 365.607  1.00110.29           O  
ANISOU 2824  O   LYS B 240     9914  20698  11293  -5082  -3800   1826       O  
ATOM   2825  CB  LYS B 240      61.371  53.299 363.945  1.00115.59           C  
ANISOU 2825  CB  LYS B 240    10490  21589  11839  -6255  -4070   1878       C  
ATOM   2826  N   PRO B 241      58.267  52.518 365.017  1.00104.29           N  
ANISOU 2826  N   PRO B 241    10051  18956  10618  -5275  -3703   1400       N  
ATOM   2827  CA  PRO B 241      57.234  51.464 365.040  1.00 99.91           C  
ANISOU 2827  CA  PRO B 241     9550  18156  10256  -4679  -3454   1393       C  
ATOM   2828  C   PRO B 241      57.048  50.817 363.658  1.00 99.32           C  
ANISOU 2828  C   PRO B 241     9272  17975  10489  -4380  -3207   1472       C  
ATOM   2829  O   PRO B 241      56.251  51.288 362.841  1.00 96.28           O  
ANISOU 2829  O   PRO B 241     9183  17155  10242  -4382  -3073   1330       O  
ATOM   2830  CB  PRO B 241      55.977  52.222 365.497  1.00100.31           C  
ANISOU 2830  CB  PRO B 241    10209  17666  10239  -4679  -3431   1112       C  
ATOM   2831  CG  PRO B 241      56.297  53.709 365.287  1.00107.57           C  
ANISOU 2831  CG  PRO B 241    11435  18414  11022  -5238  -3631    942       C  
ATOM   2832  CD  PRO B 241      57.665  53.821 364.681  1.00105.84           C  
ANISOU 2832  CD  PRO B 241    10781  18643  10791  -5609  -3762   1153       C  
ATOM   2833  N   VAL B 242      57.808  49.742 363.398  1.00 95.59           N  
ANISOU 2833  N   VAL B 242     8294  17917  10109  -4106  -3159   1693       N  
ATOM   2834  CA  VAL B 242      57.798  49.007 362.127  1.00 93.22           C  
ANISOU 2834  CA  VAL B 242     7749  17604  10066  -3773  -2948   1755       C  
ATOM   2835  C   VAL B 242      56.797  47.847 362.156  1.00 93.74           C  
ANISOU 2835  C   VAL B 242     7910  17348  10358  -3207  -2776   1752       C  
ATOM   2836  O   VAL B 242      56.170  47.599 363.190  1.00 93.15           O  
ANISOU 2836  O   VAL B 242     8033  17131  10227  -3092  -2820   1750       O  
ATOM   2837  CB  VAL B 242      59.212  48.500 361.733  1.00100.25           C  
ANISOU 2837  CB  VAL B 242     8029  19144  10917  -3762  -2998   1974       C  
ATOM   2838  CG1 VAL B 242      60.088  49.638 361.220  1.00103.01           C  
ANISOU 2838  CG1 VAL B 242     8259  19786  11092  -4345  -3128   2009       C  
ATOM   2839  CG2 VAL B 242      59.892  47.745 362.878  1.00102.58           C  
ANISOU 2839  CG2 VAL B 242     8011  19862  11102  -3592  -3141   2161       C  
ATOM   2840  N   THR B 243      56.651  47.139 361.012  1.00 87.88           N  
ANISOU 2840  N   THR B 243     7024  16508   9857  -2872  -2594   1759       N  
ATOM   2841  CA  THR B 243      55.793  45.961 360.891  1.00 84.95           C  
ANISOU 2841  CA  THR B 243     6726  15819   9731  -2360  -2461   1771       C  
ATOM   2842  C   THR B 243      56.529  44.850 361.650  1.00 90.09           C  
ANISOU 2842  C   THR B 243     7022  16820  10388  -2061  -2570   1986       C  
ATOM   2843  O   THR B 243      57.481  44.260 361.129  1.00 91.63           O  
ANISOU 2843  O   THR B 243     6824  17334  10657  -1828  -2559   2079       O  
ATOM   2844  CB  THR B 243      55.476  45.658 359.409  1.00 92.18           C  
ANISOU 2844  CB  THR B 243     7622  16534  10868  -2145  -2269   1677       C  
ATOM   2845  OG1 THR B 243      54.922  46.826 358.801  1.00 91.03           O  
ANISOU 2845  OG1 THR B 243     7772  16136  10679  -2484  -2203   1522       O  
ATOM   2846  CG2 THR B 243      54.507  44.492 359.238  1.00 88.03           C  
ANISOU 2846  CG2 THR B 243     7240  15604  10605  -1676  -2161   1669       C  
ATOM   2847  N   GLN B 244      56.142  44.652 362.924  1.00 85.82           N  
ANISOU 2847  N   GLN B 244     6609  16261   9739  -2073  -2684   2069       N  
ATOM   2848  CA  GLN B 244      56.788  43.706 363.832  1.00 87.55           C  
ANISOU 2848  CA  GLN B 244     6523  16811   9929  -1842  -2822   2309       C  
ATOM   2849  C   GLN B 244      55.801  42.753 364.508  1.00 88.90           C  
ANISOU 2849  C   GLN B 244     6878  16652  10246  -1510  -2810   2420       C  
ATOM   2850  O   GLN B 244      54.632  43.093 364.711  1.00 86.02           O  
ANISOU 2850  O   GLN B 244     6892  15902   9890  -1568  -2730   2315       O  
ATOM   2851  CB  GLN B 244      57.601  44.463 364.906  1.00 91.89           C  
ANISOU 2851  CB  GLN B 244     6965  17809  10140  -2240  -3026   2377       C  
ATOM   2852  CG  GLN B 244      56.800  45.449 365.765  1.00101.63           C  
ANISOU 2852  CG  GLN B 244     8636  18821  11157  -2564  -3075   2225       C  
ATOM   2853  CD  GLN B 244      57.690  46.299 366.633  1.00122.84           C  
ANISOU 2853  CD  GLN B 244    11241  21932  13500  -3005  -3297   2232       C  
ATOM   2854  OE1 GLN B 244      58.219  45.851 367.656  1.00120.80           O  
ANISOU 2854  OE1 GLN B 244    10767  22046  13085  -2971  -3452   2417       O  
ATOM   2855  NE2 GLN B 244      57.859  47.554 366.252  1.00115.15           N  
ANISOU 2855  NE2 GLN B 244    10454  20899  12399  -3447  -3340   2041       N  
ATOM   2856  N   ILE B 245      56.301  41.563 364.880  1.00 86.47           N  
ANISOU 2856  N   ILE B 245     6286  16525  10045  -1164  -2904   2660       N  
ATOM   2857  CA  ILE B 245      55.538  40.529 365.576  1.00 85.12           C  
ANISOU 2857  CA  ILE B 245     6227  16094  10019   -867  -2944   2851       C  
ATOM   2858  C   ILE B 245      56.023  40.511 367.037  1.00 90.79           C  
ANISOU 2858  C   ILE B 245     6803  17216  10476   -989  -3136   3076       C  
ATOM   2859  O   ILE B 245      57.063  39.921 367.345  1.00 93.14           O  
ANISOU 2859  O   ILE B 245     6737  17884  10769   -824  -3271   3287       O  
ATOM   2860  CB  ILE B 245      55.633  39.134 364.878  1.00 88.37           C  
ANISOU 2860  CB  ILE B 245     6488  16300  10788   -355  -2935   2961       C  
ATOM   2861  CG1 ILE B 245      55.461  39.233 363.349  1.00 86.55           C  
ANISOU 2861  CG1 ILE B 245     6313  15826  10747   -248  -2761   2710       C  
ATOM   2862  CG2 ILE B 245      54.630  38.145 365.470  1.00 88.25           C  
ANISOU 2862  CG2 ILE B 245     6675  15895  10961   -123  -2984   3161       C  
ATOM   2863  CD1 ILE B 245      56.722  38.987 362.569  1.00 95.33           C  
ANISOU 2863  CD1 ILE B 245     7020  17322  11878    -54  -2767   2689       C  
ATOM   2864  N   VAL B 246      55.285  41.218 367.916  1.00 86.08           N  
ANISOU 2864  N   VAL B 246     6487  16585   9637  -1269  -3148   3016       N  
ATOM   2865  CA  VAL B 246      55.574  41.326 369.351  1.00 88.28           C  
ANISOU 2865  CA  VAL B 246     6685  17251   9607  -1418  -3322   3189       C  
ATOM   2866  C   VAL B 246      54.890  40.143 370.052  1.00 91.88           C  
ANISOU 2866  C   VAL B 246     7151  17565  10195  -1106  -3365   3497       C  
ATOM   2867  O   VAL B 246      53.659  40.066 370.069  1.00 89.15           O  
ANISOU 2867  O   VAL B 246     7096  16847   9928  -1050  -3257   3471       O  
ATOM   2868  CB  VAL B 246      55.149  42.702 369.947  1.00 91.78           C  
ANISOU 2868  CB  VAL B 246     7437  17744   9691  -1836  -3327   2946       C  
ATOM   2869  CG1 VAL B 246      55.597  42.836 371.399  1.00 95.05           C  
ANISOU 2869  CG1 VAL B 246     7731  18642   9740  -2004  -3528   3093       C  
ATOM   2870  CG2 VAL B 246      55.688  43.865 369.116  1.00 91.14           C  
ANISOU 2870  CG2 VAL B 246     7420  17662   9548  -2165  -3292   2655       C  
ATOM   2871  N   SER B 247      55.690  39.208 370.593  1.00 91.14           N  
ANISOU 2871  N   SER B 247     6723  17772  10133   -903  -3533   3816       N  
ATOM   2872  CA  SER B 247      55.176  38.007 371.248  1.00 91.77           C  
ANISOU 2872  CA  SER B 247     6783  17722  10362   -619  -3620   4173       C  
ATOM   2873  C   SER B 247      55.716  37.827 372.670  1.00 99.96           C  
ANISOU 2873  C   SER B 247     7602  19276  11105   -698  -3825   4476       C  
ATOM   2874  O   SER B 247      56.885  38.120 372.939  1.00102.36           O  
ANISOU 2874  O   SER B 247     7621  20052  11222   -810  -3943   4494       O  
ATOM   2875  CB  SER B 247      55.489  36.769 370.414  1.00 95.34           C  
ANISOU 2875  CB  SER B 247     7079  17901  11244   -181  -3646   4315       C  
ATOM   2876  OG  SER B 247      56.820  36.775 369.924  1.00106.91           O  
ANISOU 2876  OG  SER B 247     8179  19732  12709    -75  -3720   4315       O  
ATOM   2877  N   ALA B 248      54.848  37.330 373.574  1.00 97.09           N  
ANISOU 2877  N   ALA B 248     7349  18856  10684   -651  -3873   4740       N  
ATOM   2878  CA  ALA B 248      55.170  37.055 374.976  1.00100.47           C  
ANISOU 2878  CA  ALA B 248     7585  19767  10822   -709  -4065   5076       C  
ATOM   2879  C   ALA B 248      54.985  35.559 375.284  1.00105.81           C  
ANISOU 2879  C   ALA B 248     8134  20279  11791   -366  -4200   5560       C  
ATOM   2880  O   ALA B 248      53.947  34.979 374.949  1.00103.19           O  
ANISOU 2880  O   ALA B 248     8014  19476  11717   -233  -4132   5653       O  
ATOM   2881  CB  ALA B 248      54.306  37.906 375.894  1.00100.79           C  
ANISOU 2881  CB  ALA B 248     7866  19985  10445   -999  -4013   4969       C  
ATOM   2882  N   GLU B 249      56.014  34.941 375.902  1.00106.33           N  
ANISOU 2882  N   GLU B 249     7852  20724  11824   -233  -4413   5884       N  
ATOM   2883  CA  GLU B 249      56.061  33.512 376.235  1.00108.67           C  
ANISOU 2883  CA  GLU B 249     8005  20879  12408    107  -4596   6377       C  
ATOM   2884  C   GLU B 249      55.605  33.209 377.666  1.00114.41           C  
ANISOU 2884  C   GLU B 249     8682  21938  12850    -16  -4741   6801       C  
ATOM   2885  O   GLU B 249      55.802  34.020 378.574  1.00114.72           O  
ANISOU 2885  O   GLU B 249     8651  22524  12414   -308  -4764   6745       O  
ATOM   2886  CB  GLU B 249      57.483  32.965 376.032  1.00113.33           C  
ANISOU 2886  CB  GLU B 249     8219  21692  13147    390  -4751   6506       C  
ATOM   2887  N   ALA B 250      55.009  32.013 377.849  1.00112.36           N  
ANISOU 2887  N   ALA B 250     8463  21350  12879    201  -4857   7234       N  
ATOM   2888  CA  ALA B 250      54.521  31.486 379.125  1.00115.18           C  
ANISOU 2888  CA  ALA B 250     8748  21986  13029    119  -5013   7742       C  
ATOM   2889  C   ALA B 250      54.642  29.960 379.147  1.00122.38           C  
ANISOU 2889  C   ALA B 250     9562  22559  14379    461  -5254   8275       C  
ATOM   2890  O   ALA B 250      54.131  29.281 378.250  1.00120.30           O  
ANISOU 2890  O   ALA B 250     9501  21634  14575    664  -5241   8269       O  
ATOM   2891  CB  ALA B 250      53.079  31.910 379.360  1.00113.49           C  
ANISOU 2891  CB  ALA B 250     8816  21678  12626   -119  -4849   7687       C  
ATOM   2892  N   TRP B 251      55.349  29.431 380.164  1.00123.95           N  
ANISOU 2892  N   TRP B 251     9461  23199  14434    525  -5496   8732       N  
ATOM   2893  CA  TRP B 251      55.598  28.000 380.346  1.00127.67           C  
ANISOU 2893  CA  TRP B 251     9822  23393  15294    856  -5777   9289       C  
ATOM   2894  C   TRP B 251      54.708  27.399 381.426  1.00132.61           C  
ANISOU 2894  C   TRP B 251    10473  24107  15804    697  -5922   9875       C  
ATOM   2895  O   TRP B 251      54.601  27.959 382.521  1.00132.84           O  
ANISOU 2895  O   TRP B 251    10382  24778  15312    405  -5905   9992       O  
ATOM   2896  CB  TRP B 251      57.067  27.757 380.698  1.00130.75           C  
ANISOU 2896  CB  TRP B 251     9824  24222  15632   1077  -5971   9456       C  
ATOM   2897  CG  TRP B 251      57.945  27.587 379.500  1.00131.45           C  
ANISOU 2897  CG  TRP B 251     9850  24022  16073   1440  -5936   9126       C  
ATOM   2898  CD1 TRP B 251      58.772  28.521 378.950  1.00132.90           C  
ANISOU 2898  CD1 TRP B 251     9884  24539  16071   1383  -5783   8658       C  
ATOM   2899  CD2 TRP B 251      58.071  26.411 378.691  1.00132.97           C  
ANISOU 2899  CD2 TRP B 251    10125  23555  16844   1922  -6065   9240       C  
ATOM   2900  NE1 TRP B 251      59.418  27.995 377.856  1.00132.91           N  
ANISOU 2900  NE1 TRP B 251     9828  24199  16474   1813  -5787   8490       N  
ATOM   2901  CE2 TRP B 251      59.008  26.699 377.675  1.00136.23           C  
ANISOU 2901  CE2 TRP B 251    10403  23993  17364   2175  -5958   8811       C  
ATOM   2902  CE3 TRP B 251      57.486  25.133 378.729  1.00136.66           C  
ANISOU 2902  CE3 TRP B 251    10777  23406  17744   2160  -6282   9668       C  
ATOM   2903  CZ2 TRP B 251      59.376  25.758 376.706  1.00137.14           C  
ANISOU 2903  CZ2 TRP B 251    10561  23568  17977   2707  -6040   8757       C  
ATOM   2904  CZ3 TRP B 251      57.851  24.201 377.769  1.00139.83           C  
ANISOU 2904  CZ3 TRP B 251    11262  23196  18669   2666  -6392   9606       C  
ATOM   2905  CH2 TRP B 251      58.786  24.515 376.773  1.00139.75           C  
ANISOU 2905  CH2 TRP B 251    11114  23253  18731   2960  -6262   9136       C  
ATOM   2906  N   GLY B 252      54.104  26.253 381.106  1.00129.83           N  
ANISOU 2906  N   GLY B 252    10276  23125  15928    887  -6080  10243       N  
ATOM   2907  CA  GLY B 252      53.224  25.509 382.003  1.00132.04           C  
ANISOU 2907  CA  GLY B 252    10578  23405  16185    738  -6256  10883       C  
ATOM   2908  C   GLY B 252      53.960  24.868 383.162  1.00139.90           C  
ANISOU 2908  C   GLY B 252    11247  24883  17026    803  -6551  11487       C  
ATOM   2909  O   GLY B 252      55.007  24.246 382.964  1.00141.94           O  
ANISOU 2909  O   GLY B 252    11342  25046  17543   1148  -6742  11594       O  
ATOM   2910  N   ARG B 253      53.421  25.031 384.382  1.00137.50           N  
ANISOU 2910  N   ARG B 253    10827  25144  16274    491  -6587  11890       N  
ATOM   2911  CA  ARG B 253      54.009  24.494 385.611  1.00140.60           C  
ANISOU 2911  CA  ARG B 253    11120  25873  16427    579  -6798  12169       C  
ATOM   2912  C   ARG B 253      53.040  23.566 386.342  1.00143.61           C  
ANISOU 2912  C   ARG B 253    11909  25828  16830    585  -6879  12334       C  
ATOM   2913  O   ARG B 253      51.824  23.768 386.284  1.00141.87           O  
ANISOU 2913  O   ARG B 253    11759  25620  16524    294  -6753  12493       O  
ATOM   2914  CB  ARG B 253      54.440  25.637 386.540  1.00140.41           C  
ANISOU 2914  CB  ARG B 253    10929  26717  15706    339  -6658  11861       C  
ATOM   2915  N   ALA B 254      53.586  22.553 387.034  1.00142.89           N  
ANISOU 2915  N   ALA B 254    11902  25555  16837    851  -7142  12563       N  
ATOM   2916  CA  ALA B 254      52.806  21.587 387.809  1.00143.22           C  
ANISOU 2916  CA  ALA B 254    12344  25213  16859    886  -7241  12720       C  
ATOM   2917  C   ALA B 254      52.422  22.151 389.186  1.00145.08           C  
ANISOU 2917  C   ALA B 254    12749  25944  16429    689  -7061  12395       C  
ATOM   2918  O   ALA B 254      51.433  21.705 389.772  1.00144.36           O  
ANISOU 2918  O   ALA B 254    12900  25737  16214    567  -7034  12561       O  
ATOM   2919  CB  ALA B 254      53.589  20.295 387.971  1.00145.96           C  
ANISOU 2919  CB  ALA B 254    13013  24944  17499   1389  -7506  12636       C  
ATOM   2920  N   ASP B 255      53.198  23.135 389.692  1.00142.42           N  
ANISOU 2920  N   ASP B 255    12048  26390  15674    561  -7016  12296       N  
ATOM   2921  CA  ASP B 255      52.971  23.786 390.985  1.00157.45           C  
ANISOU 2921  CA  ASP B 255    15299  27447  17076    883  -6542  10193       C  
ATOM   2922  C   ASP B 255      53.261  25.289 390.906  1.00167.18           C  
ANISOU 2922  C   ASP B 255    17086  28304  18130    952  -6154   8729       C  
ATOM   2923  O   ASP B 255      54.253  25.707 390.310  1.00137.28           O  
ANISOU 2923  O   ASP B 255    11478  26504  14178    383  -6589  10836       O  
ATOM   2924  CB  ASP B 255      53.830  23.133 392.078  1.00160.28           C  
ANISOU 2924  CB  ASP B 255    15925  27641  17332   1171  -6726   9952       C  
TER    2925      ASP B 255                                                      
ATOM   2926  N   PHE C   8       2.784  51.723 316.857  1.00 30.55           N  
ANISOU 2926  N   PHE C   8     2040   3272   6297   1541   -176   -950       N  
ATOM   2927  CA  PHE C   8       4.244  51.659 316.703  1.00 28.79           C  
ANISOU 2927  CA  PHE C   8     2002   2894   6041   1421   -159   -868       C  
ATOM   2928  C   PHE C   8       4.878  50.527 317.530  1.00 30.54           C  
ANISOU 2928  C   PHE C   8     2145   3129   6329   1188    -95   -823       C  
ATOM   2929  O   PHE C   8       5.478  50.798 318.573  1.00 30.17           O  
ANISOU 2929  O   PHE C   8     2168   3031   6265   1102     -8   -787       O  
ATOM   2930  CB  PHE C   8       4.912  52.995 317.081  1.00 30.25           C  
ANISOU 2930  CB  PHE C   8     2426   2934   6135   1485   -109   -830       C  
ATOM   2931  CG  PHE C   8       4.591  54.162 316.186  1.00 32.59           C  
ANISOU 2931  CG  PHE C   8     2859   3176   6348   1710   -175   -859       C  
ATOM   2932  CD1 PHE C   8       5.089  54.224 314.893  1.00 35.72           C  
ANISOU 2932  CD1 PHE C   8     3397   3477   6697   1759   -242   -826       C  
ATOM   2933  CD2 PHE C   8       3.828  55.221 316.651  1.00 35.93           C  
ANISOU 2933  CD2 PHE C   8     3286   3637   6730   1882   -164   -917       C  
ATOM   2934  CE1 PHE C   8       4.802  55.310 314.071  1.00 38.02           C  
ANISOU 2934  CE1 PHE C   8     3840   3705   6900   1970   -306   -848       C  
ATOM   2935  CE2 PHE C   8       3.547  56.310 315.831  1.00 40.18           C  
ANISOU 2935  CE2 PHE C   8     3968   4112   7184   2102   -234   -944       C  
ATOM   2936  CZ  PHE C   8       4.036  56.349 314.546  1.00 38.19           C  
ANISOU 2936  CZ  PHE C   8     3867   3759   6885   2141   -308   -907       C  
ATOM   2937  N   PRO C   9       4.815  49.266 317.067  1.00 25.44           N  
ANISOU 2937  N   PRO C   9     1375   2539   5753   1085   -146   -826       N  
ATOM   2938  CA  PRO C   9       5.398  48.169 317.855  1.00 24.10           C  
ANISOU 2938  CA  PRO C   9     1146   2371   5638    872    -93   -783       C  
ATOM   2939  C   PRO C   9       6.903  48.011 317.649  1.00 26.54           C  
ANISOU 2939  C   PRO C   9     1621   2541   5924    779    -77   -706       C  
ATOM   2940  O   PRO C   9       7.411  48.313 316.568  1.00 27.20           O  
ANISOU 2940  O   PRO C   9     1820   2548   5969    849   -126   -687       O  
ATOM   2941  CB  PRO C   9       4.657  46.932 317.333  1.00 26.31           C  
ANISOU 2941  CB  PRO C   9     1250   2751   5997    816   -171   -820       C  
ATOM   2942  CG  PRO C   9       3.566  47.462 316.401  1.00 32.24           C  
ANISOU 2942  CG  PRO C   9     1940   3572   6739   1004   -266   -891       C  
ATOM   2943  CD  PRO C   9       4.121  48.739 315.883  1.00 27.63           C  
ANISOU 2943  CD  PRO C   9     1564   2876   6056   1158   -266   -873       C  
ATOM   2944  N   LEU C  10       7.609  47.504 318.680  1.00 20.93           N  
ANISOU 2944  N   LEU C  10      978   1787   5189    563    -17   -655       N  
ATOM   2945  CA  LEU C  10       9.044  47.227 318.624  1.00 19.18           C  
ANISOU 2945  CA  LEU C  10      916   1445   4925    408     -9   -578       C  
ATOM   2946  C   LEU C  10       9.262  45.764 318.273  1.00 22.56           C  
ANISOU 2946  C   LEU C  10     1163   1913   5495    407    -34   -575       C  
ATOM   2947  O   LEU C  10       8.781  44.885 318.983  1.00 23.54           O  
ANISOU 2947  O   LEU C  10     1170   2107   5667    305    -23   -590       O  
ATOM   2948  CB  LEU C  10       9.723  47.572 319.955  1.00 18.47           C  
ANISOU 2948  CB  LEU C  10      888   1307   4824    315     64   -538       C  
ATOM   2949  CG  LEU C  10      11.237  47.370 320.043  1.00 20.86           C  
ANISOU 2949  CG  LEU C  10     1190   1519   5216    314     92   -473       C  
ATOM   2950  CD1 LEU C  10      11.993  48.618 319.604  1.00 20.42           C  
ANISOU 2950  CD1 LEU C  10     1292   1355   5111    381     99   -438       C  
ATOM   2951  CD2 LEU C  10      11.638  47.034 321.453  1.00 23.38           C  
ANISOU 2951  CD2 LEU C  10     1505   1831   5548    182    136   -449       C  
ATOM   2952  N   ARG C  11       9.950  45.491 317.170  1.00 18.98           N  
ANISOU 2952  N   ARG C  11      903   1368   4942    317    -88   -544       N  
ATOM   2953  CA  ARG C  11      10.215  44.108 316.799  1.00 18.56           C  
ANISOU 2953  CA  ARG C  11      844   1291   4915    226   -128   -538       C  
ATOM   2954  C   ARG C  11      11.707  43.882 316.769  1.00 21.41           C  
ANISOU 2954  C   ARG C  11     1146   1610   5381    276    -88   -469       C  
ATOM   2955  O   ARG C  11      12.401  44.492 315.953  1.00 20.36           O  
ANISOU 2955  O   ARG C  11     1119   1410   5207    350    -80   -438       O  
ATOM   2956  CB  ARG C  11       9.577  43.747 315.453  1.00 19.07           C  
ANISOU 2956  CB  ARG C  11      891   1390   4963    310   -219   -586       C  
ATOM   2957  CG  ARG C  11       8.080  43.525 315.505  1.00 30.62           C  
ANISOU 2957  CG  ARG C  11     2043   3015   6576    463   -273   -663       C  
ATOM   2958  CD  ARG C  11       7.461  43.747 314.142  1.00 47.72           C  
ANISOU 2958  CD  ARG C  11     4225   5198   8710    609   -378   -715       C  
ATOM   2959  NE  ARG C  11       7.362  45.176 313.835  1.00 71.66           N  
ANISOU 2959  NE  ARG C  11     7344   8210  11675    771   -364   -721       N  
ATOM   2960  CZ  ARG C  11       6.235  45.883 313.882  1.00 94.22           C  
ANISOU 2960  CZ  ARG C  11    10119  11150  14531    883   -397   -780       C  
ATOM   2961  NH1 ARG C  11       5.085  45.295 314.190  1.00 85.97           N  
ANISOU 2961  NH1 ARG C  11     8880  10226  13558    843   -440   -838       N  
ATOM   2962  NH2 ARG C  11       6.248  47.179 313.599  1.00 82.10           N  
ANISOU 2962  NH2 ARG C  11     8696   9574  12924   1036   -388   -781       N  
ATOM   2963  N   CYS C  12      12.206  43.054 317.705  1.00 19.36           N  
ANISOU 2963  N   CYS C  12      970   1290   5096     87    -67   -439       N  
ATOM   2964  CA  CYS C  12      13.611  42.660 317.803  1.00 18.94           C  
ANISOU 2964  CA  CYS C  12      946   1172   5078     43    -44   -375       C  
ATOM   2965  C   CYS C  12      13.772  41.330 317.063  1.00 20.30           C  
ANISOU 2965  C   CYS C  12     1087   1344   5282     36    -96   -381       C  
ATOM   2966  O   CYS C  12      13.209  40.302 317.461  1.00 20.50           O  
ANISOU 2966  O   CYS C  12     1063   1393   5331    -20   -126   -404       O  
ATOM   2967  CB  CYS C  12      14.065  42.570 319.257  1.00 19.68           C  
ANISOU 2967  CB  CYS C  12      980   1276   5221    -44     -2   -343       C  
ATOM   2968  SG  CYS C  12      13.825  44.100 320.201  1.00 24.40           S  
ANISOU 2968  SG  CYS C  12     1594   1881   5795    -24     53   -344       S  
ATOM   2969  N   LEU C  13      14.464  41.388 315.936  1.00 15.82           N  
ANISOU 2969  N   LEU C  13      778    806   4428      9   -100   -333       N  
ATOM   2970  CA  LEU C  13      14.682  40.262 315.054  1.00 15.37           C  
ANISOU 2970  CA  LEU C  13      754    779   4306     13   -141   -332       C  
ATOM   2971  C   LEU C  13      16.087  39.674 315.266  1.00 17.72           C  
ANISOU 2971  C   LEU C  13     1054   1072   4607      8   -107   -271       C  
ATOM   2972  O   LEU C  13      17.045  40.430 315.431  1.00 17.70           O  
ANISOU 2972  O   LEU C  13     1049   1062   4615      3    -52   -221       O  
ATOM   2973  CB  LEU C  13      14.513  40.751 313.606  1.00 16.11           C  
ANISOU 2973  CB  LEU C  13      893    920   4307     17   -172   -347       C  
ATOM   2974  CG  LEU C  13      13.099  40.849 313.023  1.00 19.48           C  
ANISOU 2974  CG  LEU C  13     1160   1269   4972    177   -265   -461       C  
ATOM   2975  CD1 LEU C  13      12.293  41.958 313.644  1.00 19.59           C  
ANISOU 2975  CD1 LEU C  13     1131   1315   4998    233   -244   -482       C  
ATOM   2976  CD2 LEU C  13      13.162  41.129 311.553  1.00 21.29           C  
ANISOU 2976  CD2 LEU C  13     1384   1447   5257    506   -295   -479       C  
ATOM   2977  N   GLN C  14      16.208  38.337 315.241  1.00 13.29           N  
ANISOU 2977  N   GLN C  14      567    582   3899     10   -135   -259       N  
ATOM   2978  CA  GLN C  14      17.479  37.633 315.387  1.00 13.00           C  
ANISOU 2978  CA  GLN C  14      574    583   3783      7   -114   -206       C  
ATOM   2979  C   GLN C  14      17.640  36.611 314.262  1.00 14.98           C  
ANISOU 2979  C   GLN C  14      683    692   4315     12   -177   -256       C  
ATOM   2980  O   GLN C  14      16.696  35.884 313.994  1.00 15.58           O  
ANISOU 2980  O   GLN C  14      737    746   4436     21   -251   -310       O  
ATOM   2981  CB  GLN C  14      17.538  36.951 316.765  1.00 13.21           C  
ANISOU 2981  CB  GLN C  14      551    559   3909      7   -122   -199       C  
ATOM   2982  CG  GLN C  14      18.570  35.818 316.901  1.00 15.05           C  
ANISOU 2982  CG  GLN C  14      698    701   4320      7   -144   -179       C  
ATOM   2983  CD  GLN C  14      18.758  35.353 318.325  1.00 29.82           C  
ANISOU 2983  CD  GLN C  14     2342   2323   6668   -256   -195   -198       C  
ATOM   2984  OE1 GLN C  14      18.220  35.922 319.273  1.00 29.69           O  
ANISOU 2984  OE1 GLN C  14     2291   2336   6654   -332   -179   -202       O  
ATOM   2985  NE2 GLN C  14      19.523  34.296 318.514  1.00 19.32           N  
ANISOU 2985  NE2 GLN C  14     1063   1001   5275   -153   -218   -165       N  
ATOM   2986  N   ILE C  15      18.800  36.556 313.596  1.00 12.64           N  
ANISOU 2986  N   ILE C  15      512    520   3772      8   -126   -198       N  
ATOM   2987  CA  ILE C  15      19.019  35.554 312.559  1.00 13.25           C  
ANISOU 2987  CA  ILE C  15      555    561   3920     11   -170   -227       C  
ATOM   2988  C   ILE C  15      20.297  34.801 312.905  1.00 18.43           C  
ANISOU 2988  C   ILE C  15     1065   1045   4893     27   -159   -209       C  
ATOM   2989  O   ILE C  15      21.397  35.345 312.756  1.00 19.11           O  
ANISOU 2989  O   ILE C  15     1168   1072   5019     97    -70   -156       O  
ATOM   2990  CB  ILE C  15      19.020  36.081 311.099  1.00 16.08           C  
ANISOU 2990  CB  ILE C  15      900    910   4300     12   -163   -245       C  
ATOM   2991  CG1 ILE C  15      17.775  36.903 310.790  1.00 16.34           C  
ANISOU 2991  CG1 ILE C  15      920    928   4361     24   -213   -299       C  
ATOM   2992  CG2 ILE C  15      19.128  34.911 310.106  1.00 16.80           C  
ANISOU 2992  CG2 ILE C  15     1044    902   4435    156   -213   -285       C  
ATOM   2993  CD1 ILE C  15      18.063  38.273 310.429  1.00 27.79           C  
ANISOU 2993  CD1 ILE C  15     2407   2070   6082    478   -112   -287       C  
ATOM   2994  N   SER C  16      20.139  33.541 313.340  1.00 15.85           N  
ANISOU 2994  N   SER C  16      771    771   4479     13   -224   -221       N  
ATOM   2995  CA  SER C  16      21.217  32.658 313.756  1.00 15.98           C  
ANISOU 2995  CA  SER C  16      776    773   4521     11   -222   -190       C  
ATOM   2996  C   SER C  16      21.511  31.574 312.717  1.00 20.82           C  
ANISOU 2996  C   SER C  16     1550   1004   5358    291   -262   -240       C  
ATOM   2997  O   SER C  16      20.729  30.632 312.551  1.00 21.75           O  
ANISOU 2997  O   SER C  16     1741   1060   5462    284   -357   -297       O  
ATOM   2998  CB  SER C  16      20.863  32.007 315.086  1.00 18.67           C  
ANISOU 2998  CB  SER C  16     1093   1082   4919     13   -276   -187       C  
ATOM   2999  OG  SER C  16      20.681  32.971 316.105  1.00 21.54           O  
ANISOU 2999  OG  SER C  16     1436   1154   5595    -46   -254   -188       O  
ATOM   3000  N   SER C  17      22.653  31.691 312.039  1.00 18.73           N  
ANISOU 3000  N   SER C  17     1258    901   4957    260   -185   -195       N  
ATOM   3001  CA  SER C  17      23.045  30.712 311.044  1.00 19.73           C  
ANISOU 3001  CA  SER C  17     1502    965   5032    403   -199   -219       C  
ATOM   3002  C   SER C  17      24.124  29.784 311.614  1.00 22.74           C  
ANISOU 3002  C   SER C  17     1919   1141   5581    579   -199   -197       C  
ATOM   3003  O   SER C  17      25.076  30.245 312.254  1.00 23.01           O  
ANISOU 3003  O   SER C  17     1851   1212   5681    559   -133   -136       O  
ATOM   3004  CB  SER C  17      23.528  31.406 309.776  1.00 25.10           C  
ANISOU 3004  CB  SER C  17     2262   1498   5775    705    -88   -208       C  
ATOM   3005  OG  SER C  17      23.756  30.466 308.737  1.00 41.32           O  
ANISOU 3005  OG  SER C  17     4446   3502   7750    852   -100   -240       O  
ATOM   3006  N   PHE C  18      23.954  28.470 311.403  1.00 19.67           N  
ANISOU 3006  N   PHE C  18     1580    886   5007    445   -293   -235       N  
ATOM   3007  CA  PHE C  18      24.878  27.436 311.870  1.00 19.10           C  
ANISOU 3007  CA  PHE C  18     1516    826   4916    438   -320   -219       C  
ATOM   3008  C   PHE C  18      25.198  26.535 310.702  1.00 22.15           C  
ANISOU 3008  C   PHE C  18     2108    965   5344    760   -329   -264       C  
ATOM   3009  O   PHE C  18      24.461  25.580 310.472  1.00 22.69           O  
ANISOU 3009  O   PHE C  18     2311    932   5377    770   -442   -325       O  
ATOM   3010  CB  PHE C  18      24.255  26.638 313.035  1.00 19.66           C  
ANISOU 3010  CB  PHE C  18     1616    771   5085    381   -437   -236       C  
ATOM   3011  CG  PHE C  18      23.967  27.442 314.279  1.00 19.77           C  
ANISOU 3011  CG  PHE C  18     1525    774   5212    272   -424   -200       C  
ATOM   3012  CD1 PHE C  18      22.787  28.179 314.397  1.00 21.74           C  
ANISOU 3012  CD1 PHE C  18     1792    923   5544    235   -428   -226       C  
ATOM   3013  CD2 PHE C  18      24.862  27.453 315.341  1.00 20.64           C  
ANISOU 3013  CD2 PHE C  18     1601    812   5430    277   -414   -150       C  
ATOM   3014  CE1 PHE C  18      22.516  28.920 315.549  1.00 21.27           C  
ANISOU 3014  CE1 PHE C  18     1636    910   5537    101   -409   -194       C  
ATOM   3015  CE2 PHE C  18      24.590  28.191 316.491  1.00 22.45           C  
ANISOU 3015  CE2 PHE C  18     1767   1017   5744    165   -408   -120       C  
ATOM   3016  CZ  PHE C  18      23.419  28.921 316.587  1.00 20.19           C  
ANISOU 3016  CZ  PHE C  18     1452    770   5450     65   -400   -142       C  
ATOM   3017  N   ALA C  19      26.253  26.859 309.923  1.00 19.67           N  
ANISOU 3017  N   ALA C  19     1733    912   4829    686   -214   -221       N  
ATOM   3018  CA  ALA C  19      26.629  26.065 308.740  1.00 20.52           C  
ANISOU 3018  CA  ALA C  19     1989    984   4825    860   -203   -253       C  
ATOM   3019  C   ALA C  19      26.991  24.605 309.091  1.00 22.73           C  
ANISOU 3019  C   ALA C  19     2392   1037   5207   1062   -291   -288       C  
ATOM   3020  O   ALA C  19      26.650  23.695 308.338  1.00 22.78           O  
ANISOU 3020  O   ALA C  19     2563   1000   5092   1129   -362   -346       O  
ATOM   3021  CB  ALA C  19      27.791  26.719 308.008  1.00 21.60           C  
ANISOU 3021  CB  ALA C  19     2095   1136   4976   1027    -29   -197       C  
ATOM   3022  N   ASN C  20      27.672  24.406 310.234  1.00 20.07           N  
ANISOU 3022  N   ASN C  20     1911    891   4823    824   -302   -240       N  
ATOM   3023  CA  ASN C  20      28.155  23.129 310.754  1.00 20.73           C  
ANISOU 3023  CA  ASN C  20     2067    897   4913    882   -389   -255       C  
ATOM   3024  C   ASN C  20      28.456  23.232 312.270  1.00 23.32           C  
ANISOU 3024  C   ASN C  20     2333    993   5535    974   -427   -212       C  
ATOM   3025  O   ASN C  20      27.962  24.152 312.930  1.00 22.47           O  
ANISOU 3025  O   ASN C  20     2112    945   5479    810   -415   -187       O  
ATOM   3026  CB  ASN C  20      29.397  22.683 309.967  1.00 21.65           C  
ANISOU 3026  CB  ASN C  20     2231   1030   4967   1072   -304   -244       C  
ATOM   3027  CG  ASN C  20      30.503  23.703 309.875  1.00 34.82           C  
ANISOU 3027  CG  ASN C  20     3769   2445   7017   1545   -131   -181       C  
ATOM   3028  OD1 ASN C  20      30.740  24.487 310.800  1.00 25.32           O  
ANISOU 3028  OD1 ASN C  20     2389   1349   5882   1365   -111   -125       O  
ATOM   3029  ND2 ASN C  20      31.203  23.681 308.740  1.00 30.87           N  
ANISOU 3029  ND2 ASN C  20     3298   1977   6454   1747    -10   -181       N  
ATOM   3030  N   SER C  21      29.264  22.302 312.817  1.00 21.62           N  
ANISOU 3030  N   SER C  21     2107    894   5215    889   -477   -205       N  
ATOM   3031  CA  SER C  21      29.637  22.308 314.235  1.00 21.18           C  
ANISOU 3031  CA  SER C  21     1959    834   5253    789   -529   -164       C  
ATOM   3032  C   SER C  21      30.595  23.488 314.593  1.00 24.27           C  
ANISOU 3032  C   SER C  21     2190   1102   5929   1013   -426    -86       C  
ATOM   3033  O   SER C  21      30.629  23.901 315.755  1.00 23.18           O  
ANISOU 3033  O   SER C  21     1957   1019   5833    839   -464    -52       O  
ATOM   3034  CB  SER C  21      30.263  20.973 314.637  1.00 23.86           C  
ANISOU 3034  CB  SER C  21     2454    928   5686   1026   -631   -169       C  
ATOM   3035  OG  SER C  21      31.486  20.693 313.973  1.00 29.18           O  
ANISOU 3035  OG  SER C  21     3134   1488   6466   1389   -565   -154       O  
ATOM   3036  N   SER C  22      31.357  24.015 313.601  1.00 22.85           N  
ANISOU 3036  N   SER C  22     1920   1116   5644   1005   -288    -72       N  
ATOM   3037  CA  SER C  22      32.318  25.101 313.783  1.00 23.11           C  
ANISOU 3037  CA  SER C  22     1755   1234   5793   1019   -178     -3       C  
ATOM   3038  C   SER C  22      31.684  26.449 313.507  1.00 28.25           C  
ANISOU 3038  C   SER C  22     2320   1850   6565   1074    -93     20       C  
ATOM   3039  O   SER C  22      31.402  27.204 314.435  1.00 28.61           O  
ANISOU 3039  O   SER C  22     2270   1929   6673    912   -113     50       O  
ATOM   3040  CB  SER C  22      33.521  24.914 312.861  1.00 27.60           C  
ANISOU 3040  CB  SER C  22     2244   1758   6486   1411    -69     22       C  
ATOM   3041  OG  SER C  22      34.213  23.702 313.101  1.00 40.49           O  
ANISOU 3041  OG  SER C  22     3928   3334   8122   1542   -150      7       O  
ATOM   3042  N   TRP C  23      31.452  26.735 312.219  1.00 25.63           N  
ANISOU 3042  N   TRP C  23     2053   1532   6154   1168     -1     -1       N  
ATOM   3043  CA  TRP C  23      30.916  27.969 311.665  1.00 24.75           C  
ANISOU 3043  CA  TRP C  23     1906   1475   6023   1104     92     13       C  
ATOM   3044  C   TRP C  23      29.546  28.346 312.223  1.00 29.65           C  
ANISOU 3044  C   TRP C  23     2574   2062   6630    924      1    -18       C  
ATOM   3045  O   TRP C  23      28.622  27.526 312.222  1.00 28.66           O  
ANISOU 3045  O   TRP C  23     2584   1858   6447    897   -108    -77       O  
ATOM   3046  CB  TRP C  23      30.826  27.833 310.146  1.00 24.32           C  
ANISOU 3046  CB  TRP C  23     1981   1462   5800   1182    176    -13       C  
ATOM   3047  CG  TRP C  23      30.810  29.141 309.429  1.00 24.84           C  
ANISOU 3047  CG  TRP C  23     1988   1579   5870   1201    314     27       C  
ATOM   3048  CD1 TRP C  23      31.879  29.793 308.890  1.00 28.14           C  
ANISOU 3048  CD1 TRP C  23     2285   2050   6357   1340    482     89       C  
ATOM   3049  CD2 TRP C  23      29.665  29.961 309.171  1.00 23.91           C  
ANISOU 3049  CD2 TRP C  23     1927   1469   5687   1084    300      8       C  
ATOM   3050  NE1 TRP C  23      31.470  30.956 308.291  1.00 27.23           N  
ANISOU 3050  NE1 TRP C  23     2177   1966   6205   1298    572    114       N  
ATOM   3051  CE2 TRP C  23      30.114  31.094 308.463  1.00 27.61           C  
ANISOU 3051  CE2 TRP C  23     2327   1960   6203   1199    460     59       C  
ATOM   3052  CE3 TRP C  23      28.297  29.856 309.482  1.00 23.91           C  
ANISOU 3052  CE3 TRP C  23     2004   1388   5693   1034    175    -55       C  
ATOM   3053  CZ2 TRP C  23      29.242  32.114 308.054  1.00 26.24           C  
ANISOU 3053  CZ2 TRP C  23     2201   1789   5978   1141    481     56       C  
ATOM   3054  CZ3 TRP C  23      27.436  30.860 309.065  1.00 24.45           C  
ANISOU 3054  CZ3 TRP C  23     2094   1460   5735   1006    199    -63       C  
ATOM   3055  CH2 TRP C  23      27.910  31.970 308.356  1.00 25.27           C  
ANISOU 3055  CH2 TRP C  23     2159   1619   5822   1055    345     -9       C  
ATOM   3056  N   THR C  24      29.431  29.622 312.668  1.00 27.58           N  
ANISOU 3056  N   THR C  24     2197   1862   6421    802     52     23       N  
ATOM   3057  CA  THR C  24      28.230  30.286 313.198  1.00 26.93           C  
ANISOU 3057  CA  THR C  24     2127   1773   6332    644     -1      2       C  
ATOM   3058  C   THR C  24      28.266  31.786 312.887  1.00 32.43           C  
ANISOU 3058  C   THR C  24     2744   2534   7043    606    105     43       C  
ATOM   3059  O   THR C  24      29.356  32.366 312.795  1.00 33.48           O  
ANISOU 3059  O   THR C  24     2770   2719   7232    633    201    104       O  
ATOM   3060  CB  THR C  24      28.104  30.102 314.720  1.00 37.48           C  
ANISOU 3060  CB  THR C  24     3419   3089   7733    498    -99     12       C  
ATOM   3061  OG1 THR C  24      27.977  28.721 315.061  1.00 45.72           O  
ANISOU 3061  OG1 THR C  24     4560   4057   8755    517   -205    -22       O  
ATOM   3062  CG2 THR C  24      26.973  30.918 315.295  1.00 33.72           C  
ANISOU 3062  CG2 THR C  24     2936   2623   7252    348   -125     -3       C  
ATOM   3063  N   ARG C  25      27.068  32.421 312.799  1.00 28.17           N  
ANISOU 3063  N   ARG C  25     2253   1990   6459    536     83     10       N  
ATOM   3064  CA  ARG C  25      26.867  33.854 312.587  1.00 26.97           C  
ANISOU 3064  CA  ARG C  25     2060   1880   6308    493    161     39       C  
ATOM   3065  C   ARG C  25      25.444  34.256 313.020  1.00 31.96           C  
ANISOU 3065  C   ARG C  25     2729   2503   6914    394     87     -8       C  
ATOM   3066  O   ARG C  25      24.493  34.013 312.273  1.00 32.43           O  
ANISOU 3066  O   ARG C  25     2878   2546   6900    443     53    -63       O  
ATOM   3067  CB  ARG C  25      27.129  34.232 311.118  1.00 24.55           C  
ANISOU 3067  CB  ARG C  25     1809   1587   5930    631    272     52       C  
ATOM   3068  CG  ARG C  25      27.195  35.721 310.891  1.00 33.90           C  
ANISOU 3068  CG  ARG C  25     2950   2805   7124    592    371    105       C  
ATOM   3069  CD  ARG C  25      27.673  36.094 309.505  1.00 45.41           C  
ANISOU 3069  CD  ARG C  25     4466   4276   8512    724    501    136       C  
ATOM   3070  NE  ARG C  25      27.723  37.546 309.327  1.00 54.24           N  
ANISOU 3070  NE  ARG C  25     5573   5409   9629    675    588    186       N  
ATOM   3071  CZ  ARG C  25      28.742  38.320 309.695  1.00 76.92           C  
ANISOU 3071  CZ  ARG C  25     8335   8311  12582    607    680    266       C  
ATOM   3072  NH1 ARG C  25      29.817  37.789 310.268  1.00 66.43           N  
ANISOU 3072  NH1 ARG C  25     6877   7014  11350    587    695    303       N  
ATOM   3073  NH2 ARG C  25      28.693  39.631 309.495  1.00 70.80           N  
ANISOU 3073  NH2 ARG C  25     7579   7528  11793    557    748    309       N  
ATOM   3074  N   THR C  26      25.292  34.851 314.227  1.00 28.65           N  
ANISOU 3074  N   THR C  26     2239   2095   6551    260     59      9       N  
ATOM   3075  CA  THR C  26      23.986  35.342 314.699  1.00 28.36           C  
ANISOU 3075  CA  THR C  26     2219   2064   6494    174     11    -32       C  
ATOM   3076  C   THR C  26      24.007  36.859 314.636  1.00 31.35           C  
ANISOU 3076  C   THR C  26     2570   2469   6874    156     84      0       C  
ATOM   3077  O   THR C  26      24.853  37.496 315.273  1.00 31.95           O  
ANISOU 3077  O   THR C  26     2582   2551   7006    100    122     54       O  
ATOM   3078  CB  THR C  26      23.580  34.801 316.096  1.00 41.58           C  
ANISOU 3078  CB  THR C  26     3870   3724   8205     48    -71    -45       C  
ATOM   3079  OG1 THR C  26      23.465  33.371 316.049  1.00 43.04           O  
ANISOU 3079  OG1 THR C  26     4108   3868   8377     66   -143    -75       O  
ATOM   3080  CG2 THR C  26      22.293  35.452 316.660  1.00 40.65           C  
ANISOU 3080  CG2 THR C  26     3747   3629   8070    -37    -94    -80       C  
ATOM   3081  N   ASP C  27      23.094  37.429 313.828  1.00 25.93           N  
ANISOU 3081  N   ASP C  27     1941   1790   6122    207     92    -35       N  
ATOM   3082  CA  ASP C  27      22.953  38.871 313.645  1.00 24.29           C  
ANISOU 3082  CA  ASP C  27     1741   1592   5897    208    153    -11       C  
ATOM   3083  C   ASP C  27      21.573  39.294 314.018  1.00 26.80           C  
ANISOU 3083  C   ASP C  27     2071   1923   6187    173     96    -66       C  
ATOM   3084  O   ASP C  27      20.606  38.607 313.709  1.00 26.15           O  
ANISOU 3084  O   ASP C  27     2012   1851   6072    200     30   -127       O  
ATOM   3085  CB  ASP C  27      23.254  39.298 312.206  1.00 26.32           C  
ANISOU 3085  CB  ASP C  27     2070   1842   6089    333    230      7       C  
ATOM   3086  CG  ASP C  27      24.582  38.802 311.694  1.00 37.40           C  
ANISOU 3086  CG  ASP C  27     3453   3244   7513    386    307     62       C  
ATOM   3087  OD1 ASP C  27      24.654  37.616 311.288  1.00 38.21           O  
ANISOU 3087  OD1 ASP C  27     3582   3339   7595    455    277     34       O  
ATOM   3088  OD2 ASP C  27      25.558  39.590 311.712  1.00 43.07           O  
ANISOU 3088  OD2 ASP C  27     4126   3968   8272    359    397    132       O  
ATOM   3089  N   GLY C  28      21.493  40.429 314.680  1.00 23.94           N  
ANISOU 3089  N   GLY C  28     1692   1563   5840    114    121    -46       N  
ATOM   3090  CA  GLY C  28      20.236  41.019 315.109  1.00 23.63           C  
ANISOU 3090  CA  GLY C  28     1657   1545   5776     95     84    -95       C  
ATOM   3091  C   GLY C  28      19.979  42.387 314.507  1.00 26.58           C  
ANISOU 3091  C   GLY C  28     2092   1906   6100    160    129    -86       C  
ATOM   3092  O   GLY C  28      20.873  42.994 313.903  1.00 26.65           O  
ANISOU 3092  O   GLY C  28     2142   1883   6101    191    198    -30       O  
ATOM   3093  N   LEU C  29      18.734  42.860 314.662  1.00 21.08           N  
ANISOU 3093  N   LEU C  29     1404   1236   5371    185     91   -141       N  
ATOM   3094  CA  LEU C  29      18.242  44.158 314.218  1.00 20.76           C  
ANISOU 3094  CA  LEU C  29     1434   1181   5275    260    112   -147       C  
ATOM   3095  C   LEU C  29      16.884  44.427 314.885  1.00 22.78           C  
ANISOU 3095  C   LEU C  29     1652   1484   5521    264     62   -214       C  
ATOM   3096  O   LEU C  29      16.188  43.475 315.253  1.00 22.92           O  
ANISOU 3096  O   LEU C  29     1593   1553   5562    232     10   -261       O  
ATOM   3097  CB  LEU C  29      18.177  44.291 312.675  1.00 21.52           C  
ANISOU 3097  CB  LEU C  29     1619   1259   5300    393    123   -148       C  
ATOM   3098  CG  LEU C  29      17.174  43.465 311.874  1.00 26.68           C  
ANISOU 3098  CG  LEU C  29     2273   1950   5914    477     43   -218       C  
ATOM   3099  CD1 LEU C  29      16.892  44.134 310.565  1.00 27.11           C  
ANISOU 3099  CD1 LEU C  29     2444   1979   5876    619     44   -225       C  
ATOM   3100  CD2 LEU C  29      17.697  42.048 311.607  1.00 30.77           C  
ANISOU 3100  CD2 LEU C  29     2767   2468   6455    457     26   -216       C  
ATOM   3101  N   ALA C  30      16.547  45.717 315.093  1.00 17.02           N  
ANISOU 3101  N   ALA C  30      970    813   4684    197     77   -205       N  
ATOM   3102  CA  ALA C  30      15.329  46.139 315.763  1.00 16.06           C  
ANISOU 3102  CA  ALA C  30      830    753   4520    172     42   -261       C  
ATOM   3103  C   ALA C  30      14.586  47.182 314.946  1.00 20.03           C  
ANISOU 3103  C   ALA C  30     1399   1156   5055    469     39   -305       C  
ATOM   3104  O   ALA C  30      15.213  48.018 314.303  1.00 21.05           O  
ANISOU 3104  O   ALA C  30     1644   1212   5141    518     74   -260       O  
ATOM   3105  CB  ALA C  30      15.665  46.690 317.137  1.00 16.16           C  
ANISOU 3105  CB  ALA C  30      826    746   4568    109     76   -242       C  
ATOM   3106  N   TRP C  31      13.248  47.139 314.977  1.00 16.90           N  
ANISOU 3106  N   TRP C  31      972    913   4536    369    -29   -363       N  
ATOM   3107  CA  TRP C  31      12.386  48.069 314.253  1.00 17.10           C  
ANISOU 3107  CA  TRP C  31     1063    969   4465    479    -68   -399       C  
ATOM   3108  C   TRP C  31      11.322  48.704 315.154  1.00 20.18           C  
ANISOU 3108  C   TRP C  31     1354   1313   4999    734    -54   -475       C  
ATOM   3109  O   TRP C  31      10.594  47.981 315.839  1.00 20.70           O  
ANISOU 3109  O   TRP C  31     1280   1468   5116    674    -65   -516       O  
ATOM   3110  CB  TRP C  31      11.648  47.342 313.115  1.00 16.54           C  
ANISOU 3110  CB  TRP C  31      992    972   4321    473   -159   -446       C  
ATOM   3111  CG  TRP C  31      12.487  46.554 312.163  1.00 16.89           C  
ANISOU 3111  CG  TRP C  31     1071    982   4366    485   -157   -412       C  
ATOM   3112  CD1 TRP C  31      12.903  45.264 312.312  1.00 18.30           C  
ANISOU 3112  CD1 TRP C  31     1159   1099   4695    529   -152   -415       C  
ATOM   3113  CD2 TRP C  31      12.881  46.954 310.845  1.00 17.14           C  
ANISOU 3113  CD2 TRP C  31     1223    989   4300    582   -158   -384       C  
ATOM   3114  NE1 TRP C  31      13.590  44.855 311.191  1.00 17.88           N  
ANISOU 3114  NE1 TRP C  31     1192   1033   4568    534   -152   -383       N  
ATOM   3115  CE2 TRP C  31      13.579  45.868 310.267  1.00 19.38           C  
ANISOU 3115  CE2 TRP C  31     1495   1157   4711    721   -140   -375       C  
ATOM   3116  CE3 TRP C  31      12.720  48.134 310.095  1.00 18.64           C  
ANISOU 3116  CE3 TRP C  31     1533   1104   4445    785   -154   -381       C  
ATOM   3117  CZ2 TRP C  31      14.120  45.926 308.978  1.00 19.06           C  
ANISOU 3117  CZ2 TRP C  31     1586   1097   4559    774   -125   -339       C  
ATOM   3118  CZ3 TRP C  31      13.275  48.197 308.826  1.00 19.93           C  
ANISOU 3118  CZ3 TRP C  31     1828   1172   4575    938   -134   -351       C  
ATOM   3119  CH2 TRP C  31      13.970  47.105 308.283  1.00 20.10           C  
ANISOU 3119  CH2 TRP C  31     1848   1172   4617    920   -114   -328       C  
ATOM   3120  N   LEU C  32      11.181  50.028 315.106  1.00 17.32           N  
ANISOU 3120  N   LEU C  32     1147   1009   4426    617    -63   -451       N  
ATOM   3121  CA  LEU C  32      10.108  50.717 315.808  1.00 17.89           C  
ANISOU 3121  CA  LEU C  32     1188   1113   4495    715    -67   -511       C  
ATOM   3122  C   LEU C  32       9.194  51.221 314.718  1.00 23.98           C  
ANISOU 3122  C   LEU C  32     1942   1821   5350   1110   -117   -587       C  
ATOM   3123  O   LEU C  32       9.544  52.157 313.999  1.00 24.57           O  
ANISOU 3123  O   LEU C  32     2186   1799   5349   1210   -122   -561       O  
ATOM   3124  CB  LEU C  32      10.611  51.827 316.739  1.00 17.81           C  
ANISOU 3124  CB  LEU C  32     1276   1034   4457    708     -7   -478       C  
ATOM   3125  CG  LEU C  32       9.545  52.739 317.350  1.00 22.55           C  
ANISOU 3125  CG  LEU C  32     1847   1572   5149   1016     19   -569       C  
ATOM   3126  CD1 LEU C  32       8.801  52.051 318.492  1.00 23.07           C  
ANISOU 3126  CD1 LEU C  32     1748   1751   5268    936     54   -607       C  
ATOM   3127  CD2 LEU C  32      10.158  54.011 317.842  1.00 25.73           C  
ANISOU 3127  CD2 LEU C  32     2443   1845   5487   1039     53   -539       C  
ATOM   3128  N   GLY C  33       8.074  50.531 314.542  1.00 22.26           N  
ANISOU 3128  N   GLY C  33     1570   1733   5156   1126   -183   -653       N  
ATOM   3129  CA  GLY C  33       7.155  50.790 313.448  1.00 23.35           C  
ANISOU 3129  CA  GLY C  33     1705   1908   5261   1307   -280   -710       C  
ATOM   3130  C   GLY C  33       7.789  50.224 312.192  1.00 27.53           C  
ANISOU 3130  C   GLY C  33     2315   2373   5774   1326   -325   -680       C  
ATOM   3131  O   GLY C  33       8.166  49.048 312.171  1.00 27.18           O  
ANISOU 3131  O   GLY C  33     2191   2352   5782   1203   -330   -668       O  
ATOM   3132  N   GLU C  34       7.992  51.074 311.175  1.00 24.53           N  
ANISOU 3132  N   GLU C  34     2121   1902   5299   1463   -349   -660       N  
ATOM   3133  CA  GLU C  34       8.602  50.697 309.895  1.00 24.69           C  
ANISOU 3133  CA  GLU C  34     2263   1858   5259   1484   -379   -625       C  
ATOM   3134  C   GLU C  34      10.092  51.070 309.842  1.00 28.43           C  
ANISOU 3134  C   GLU C  34     2898   2202   5704   1406   -266   -523       C  
ATOM   3135  O   GLU C  34      10.804  50.606 308.946  1.00 29.07           O  
ANISOU 3135  O   GLU C  34     3060   2234   5751   1397   -255   -482       O  
ATOM   3136  CB  GLU C  34       7.846  51.346 308.716  1.00 27.52           C  
ANISOU 3136  CB  GLU C  34     2731   2197   5528   1705   -482   -668       C  
ATOM   3137  CG  GLU C  34       7.756  52.864 308.783  1.00 42.67           C  
ANISOU 3137  CG  GLU C  34     4813   4036   7366   1834   -458   -653       C  
ATOM   3138  CD  GLU C  34       6.773  53.466 307.802  1.00 72.95           C  
ANISOU 3138  CD  GLU C  34     8725   7875  11116   2062   -582   -712       C  
ATOM   3139  OE1 GLU C  34       7.197  53.778 306.665  1.00 79.08           O  
ANISOU 3139  OE1 GLU C  34     9704   8554  11789   2151   -604   -675       O  
ATOM   3140  OE2 GLU C  34       5.581  53.611 308.160  1.00 63.74           O  
ANISOU 3140  OE2 GLU C  34     7417   6814   9987   2158   -658   -794       O  
ATOM   3141  N   LEU C  35      10.554  51.909 310.791  1.00 23.61           N  
ANISOU 3141  N   LEU C  35     2333   1599   5039   1254   -192   -475       N  
ATOM   3142  CA  LEU C  35      11.934  52.386 310.867  1.00 22.25           C  
ANISOU 3142  CA  LEU C  35     2281   1364   4809   1104    -96   -371       C  
ATOM   3143  C   LEU C  35      12.819  51.447 311.660  1.00 25.46           C  
ANISOU 3143  C   LEU C  35     2581   1678   5414   1056    -26   -348       C  
ATOM   3144  O   LEU C  35      12.433  51.054 312.761  1.00 25.55           O  
ANISOU 3144  O   LEU C  35     2459   1758   5491    979    -30   -383       O  
ATOM   3145  CB  LEU C  35      11.983  53.770 311.525  1.00 22.14           C  
ANISOU 3145  CB  LEU C  35     2376   1297   4739   1106    -61   -349       C  
ATOM   3146  CG  LEU C  35      11.175  54.901 310.914  1.00 25.56           C  
ANISOU 3146  CG  LEU C  35     2972   1542   5196   1471   -104   -405       C  
ATOM   3147  CD1 LEU C  35      10.984  55.991 311.923  1.00 25.78           C  
ANISOU 3147  CD1 LEU C  35     3064   1520   5211   1483    -81   -415       C  
ATOM   3148  CD2 LEU C  35      11.856  55.463 309.681  1.00 27.12           C  
ANISOU 3148  CD2 LEU C  35     3386   1620   5297   1537    -85   -338       C  
ATOM   3149  N   GLN C  36      14.015  51.107 311.110  1.00 21.88           N  
ANISOU 3149  N   GLN C  36     2172   1246   4897    901     28   -264       N  
ATOM   3150  CA  GLN C  36      15.039  50.270 311.754  1.00 20.30           C  
ANISOU 3150  CA  GLN C  36     1868   1091   4755    699     80   -214       C  
ATOM   3151  C   GLN C  36      15.819  51.150 312.717  1.00 23.70           C  
ANISOU 3151  C   GLN C  36     2364   1338   5302    716    150   -173       C  
ATOM   3152  O   GLN C  36      16.439  52.122 312.278  1.00 24.83           O  
ANISOU 3152  O   GLN C  36     2649   1385   5400    727    199   -113       O  
ATOM   3153  CB  GLN C  36      15.964  49.643 310.704  1.00 20.95           C  
ANISOU 3153  CB  GLN C  36     1993   1118   4848    729    124   -165       C  
ATOM   3154  CG  GLN C  36      16.648  48.368 311.174  1.00 25.96           C  
ANISOU 3154  CG  GLN C  36     2517   1711   5636    689    148   -156       C  
ATOM   3155  CD  GLN C  36      17.843  47.994 310.331  1.00 38.61           C  
ANISOU 3155  CD  GLN C  36     4167   3274   7227    680    221    -86       C  
ATOM   3156  OE1 GLN C  36      17.868  48.169 309.102  1.00 33.91           O  
ANISOU 3156  OE1 GLN C  36     3689   2648   6549    790    239    -72       O  
ATOM   3157  NE2 GLN C  36      18.860  47.445 310.977  1.00 28.63           N  
ANISOU 3157  NE2 GLN C  36     2818   2016   6045    558    267    -41       N  
ATOM   3158  N   THR C  37      15.744  50.860 314.024  1.00 19.67           N  
ANISOU 3158  N   THR C  37     1723    963   4786    528    137   -184       N  
ATOM   3159  CA  THR C  37      16.374  51.690 315.059  1.00 19.44           C  
ANISOU 3159  CA  THR C  37     1732    880   4773    438    174   -147       C  
ATOM   3160  C   THR C  37      17.726  51.164 315.516  1.00 23.73           C  
ANISOU 3160  C   THR C  37     2264   1288   5466    359    219    -88       C  
ATOM   3161  O   THR C  37      18.552  51.943 315.991  1.00 23.81           O  
ANISOU 3161  O   THR C  37     2345   1215   5488    278    250    -33       O  
ATOM   3162  CB  THR C  37      15.461  51.822 316.279  1.00 19.96           C  
ANISOU 3162  CB  THR C  37     1782    884   4919    515    147   -222       C  
ATOM   3163  OG1 THR C  37      15.164  50.515 316.770  1.00 20.95           O  
ANISOU 3163  OG1 THR C  37     1748   1107   5104    451    128   -254       O  
ATOM   3164  CG2 THR C  37      14.193  52.587 315.979  1.00 15.50           C  
ANISOU 3164  CG2 THR C  37     1190    635   4063    407     91   -246       C  
ATOM   3165  N   HIS C  38      17.933  49.853 315.440  1.00 20.83           N  
ANISOU 3165  N   HIS C  38     1773    989   5152    312    209    -92       N  
ATOM   3166  CA  HIS C  38      19.182  49.252 315.886  1.00 20.82           C  
ANISOU 3166  CA  HIS C  38     1709    976   5226    181    237    -33       C  
ATOM   3167  C   HIS C  38      19.675  48.204 314.902  1.00 25.68           C  
ANISOU 3167  C   HIS C  38     2276   1623   5859    205    257    -11       C  
ATOM   3168  O   HIS C  38      18.895  47.622 314.149  1.00 25.20           O  
ANISOU 3168  O   HIS C  38     2207   1607   5760    300    226    -58       O  
ATOM   3169  CB  HIS C  38      19.018  48.621 317.289  1.00 21.22           C  
ANISOU 3169  CB  HIS C  38     1667   1068   5329     82    199    -62       C  
ATOM   3170  CG  HIS C  38      18.559  49.577 318.350  1.00 24.92           C  
ANISOU 3170  CG  HIS C  38     2192   1507   5771     63    184    -88       C  
ATOM   3171  ND1 HIS C  38      17.222  49.918 318.484  1.00 27.01           N  
ANISOU 3171  ND1 HIS C  38     2469   1813   5982    160    165   -159       N  
ATOM   3172  CD2 HIS C  38      19.269  50.219 319.304  1.00 26.73           C  
ANISOU 3172  CD2 HIS C  38     2468   1669   6018    -34    184    -56       C  
ATOM   3173  CE1 HIS C  38      17.165  50.770 319.493  1.00 26.54           C  
ANISOU 3173  CE1 HIS C  38     2476   1709   5901    130    164   -167       C  
ATOM   3174  NE2 HIS C  38      18.370  50.980 320.022  1.00 26.82           N  
ANISOU 3174  NE2 HIS C  38     2544   1673   5975     11    168   -108       N  
ATOM   3175  N   SER C  39      20.986  47.989 314.907  1.00 23.63           N  
ANISOU 3175  N   SER C  39     1987   1338   5655    124    304     60       N  
ATOM   3176  CA  SER C  39      21.696  46.991 314.123  1.00 24.11           C  
ANISOU 3176  CA  SER C  39     1999   1425   5738    144    338     89       C  
ATOM   3177  C   SER C  39      22.638  46.278 315.068  1.00 29.69           C  
ANISOU 3177  C   SER C  39     2596   2148   6538     26    327    118       C  
ATOM   3178  O   SER C  39      23.158  46.893 316.003  1.00 28.32           O  
ANISOU 3178  O   SER C  39     2410   1941   6411    -76    321    148       O  
ATOM   3179  CB  SER C  39      22.439  47.638 312.960  1.00 29.32           C  
ANISOU 3179  CB  SER C  39     2739   2038   6362    189    429    158       C  
ATOM   3180  OG  SER C  39      23.221  46.702 312.237  1.00 40.07           O  
ANISOU 3180  OG  SER C  39     4057   3430   7739    222    476    187       O  
ATOM   3181  N   TRP C  40      22.816  44.971 314.859  1.00 29.65           N  
ANISOU 3181  N   TRP C  40     2524   2185   6556     46    310    104       N  
ATOM   3182  CA  TRP C  40      23.647  44.118 315.704  1.00 30.39           C  
ANISOU 3182  CA  TRP C  40     2521   2295   6732    -41    285    125       C  
ATOM   3183  C   TRP C  40      24.358  43.075 314.855  1.00 33.04           C  
ANISOU 3183  C   TRP C  40     2820   2652   7081     20    318    146       C  
ATOM   3184  O   TRP C  40      23.763  42.053 314.508  1.00 32.82           O  
ANISOU 3184  O   TRP C  40     2802   2648   7022     83    278     97       O  
ATOM   3185  CB  TRP C  40      22.766  43.454 316.771  1.00 29.60           C  
ANISOU 3185  CB  TRP C  40     2392   2220   6636    -88    200     65       C  
ATOM   3186  CG  TRP C  40      23.486  42.864 317.947  1.00 31.42           C  
ANISOU 3186  CG  TRP C  40     2554   2447   6935   -190    159     85       C  
ATOM   3187  CD1 TRP C  40      24.666  43.288 318.498  1.00 34.88           C  
ANISOU 3187  CD1 TRP C  40     2955   2861   7438   -267    167    143       C  
ATOM   3188  CD2 TRP C  40      22.984  41.832 318.812  1.00 31.26           C  
ANISOU 3188  CD2 TRP C  40     2508   2447   6923   -233     91     46       C  
ATOM   3189  NE1 TRP C  40      24.956  42.544 319.620  1.00 34.78           N  
ANISOU 3189  NE1 TRP C  40     2897   2851   7468   -340    100    140       N  
ATOM   3190  CE2 TRP C  40      23.938  41.641 319.834  1.00 36.03           C  
ANISOU 3190  CE2 TRP C  40     3071   3032   7586   -320     58     84       C  
ATOM   3191  CE3 TRP C  40      21.820  41.036 318.812  1.00 32.19           C  
ANISOU 3191  CE3 TRP C  40     2632   2594   7005   -212     52    -14       C  
ATOM   3192  CZ2 TRP C  40      23.766  40.675 320.844  1.00 35.20           C  
ANISOU 3192  CZ2 TRP C  40     2954   2929   7492   -377     -8     65       C  
ATOM   3193  CZ3 TRP C  40      21.650  40.092 319.813  1.00 33.35           C  
ANISOU 3193  CZ3 TRP C  40     2758   2744   7169   -284     -2    -28       C  
ATOM   3194  CH2 TRP C  40      22.615  39.915 320.810  1.00 34.11           C  
ANISOU 3194  CH2 TRP C  40     2836   2814   7311   -361    -30     12       C  
ATOM   3195  N   SER C  41      25.620  43.359 314.491  1.00 28.25           N  
ANISOU 3195  N   SER C  41     2175   2038   6521      5    395    220       N  
ATOM   3196  CA  SER C  41      26.456  42.480 313.686  1.00 27.78           C  
ANISOU 3196  CA  SER C  41     2074   2004   6476     76    449    248       C  
ATOM   3197  C   SER C  41      27.214  41.518 314.588  1.00 29.96           C  
ANISOU 3197  C   SER C  41     2242   2300   6839     20    397    256       C  
ATOM   3198  O   SER C  41      27.586  41.909 315.698  1.00 28.46           O  
ANISOU 3198  O   SER C  41     1998   2101   6715    -93    354    275       O  
ATOM   3199  CB  SER C  41      27.430  43.306 312.856  1.00 33.36           C  
ANISOU 3199  CB  SER C  41     2782   2702   7191     88    575    329       C  
ATOM   3200  OG  SER C  41      27.979  42.553 311.788  1.00 46.63           O  
ANISOU 3200  OG  SER C  41     4447   4414   8858    192    650    350       O  
ATOM   3201  N   ASN C  42      27.455  40.263 314.109  1.00 26.30           N  
ANISOU 3201  N   ASN C  42     1765   1859   6370    106    394    240       N  
ATOM   3202  CA  ASN C  42      28.191  39.206 314.824  1.00 25.46           C  
ANISOU 3202  CA  ASN C  42     1574   1766   6335     86    340    245       C  
ATOM   3203  C   ASN C  42      29.604  39.682 315.242  1.00 29.27           C  
ANISOU 3203  C   ASN C  42     1932   2269   6921     23    383    321       C  
ATOM   3204  O   ASN C  42      30.124  39.230 316.267  1.00 28.36           O  
ANISOU 3204  O   ASN C  42     1743   2155   6877    -41    305    327       O  
ATOM   3205  CB  ASN C  42      28.292  37.924 313.971  1.00 23.76           C  
ANISOU 3205  CB  ASN C  42     1392   1558   6080    217    346    218       C  
ATOM   3206  CG  ASN C  42      28.940  36.758 314.697  1.00 39.85           C  
ANISOU 3206  CG  ASN C  42     3368   3596   8176    215    276    216       C  
ATOM   3207  OD1 ASN C  42      28.374  36.231 315.663  1.00 30.65           O  
ANISOU 3207  OD1 ASN C  42     2224   2406   7017    147    170    179       O  
ATOM   3208  ND2 ASN C  42      30.148  36.345 314.250  1.00 35.14           N  
ANISOU 3208  ND2 ASN C  42     2698   3029   7624    295    340    258       N  
ATOM   3209  N   ASP C  43      30.203  40.602 314.461  1.00 26.78           N  
ANISOU 3209  N   ASP C  43     1595   1965   6614     37    502    380       N  
ATOM   3210  CA  ASP C  43      31.537  41.148 314.734  1.00 28.17           C  
ANISOU 3210  CA  ASP C  43     1637   2168   6900    -35    554    458       C  
ATOM   3211  C   ASP C  43      31.529  42.134 315.910  1.00 31.20           C  
ANISOU 3211  C   ASP C  43     2000   2516   7338   -196    483    472       C  
ATOM   3212  O   ASP C  43      32.435  42.073 316.736  1.00 31.18           O  
ANISOU 3212  O   ASP C  43     1878   2528   7439   -277    437    506       O  
ATOM   3213  CB  ASP C  43      32.154  41.819 313.492  1.00 31.75           C  
ANISOU 3213  CB  ASP C  43     2083   2642   7339     16    719    524       C  
ATOM   3214  CG  ASP C  43      31.282  41.806 312.252  1.00 47.43           C  
ANISOU 3214  CG  ASP C  43     4225   4607   9188    137    783    494       C  
ATOM   3215  OD1 ASP C  43      31.055  40.703 311.696  1.00 47.25           O  
ANISOU 3215  OD1 ASP C  43     4248   4597   9106    264    774    449       O  
ATOM   3216  OD2 ASP C  43      30.827  42.899 311.836  1.00 57.88           O  
ANISOU 3216  OD2 ASP C  43     5636   5894  10461    108    833    514       O  
ATOM   3217  N   SER C  44      30.525  43.029 315.990  1.00 27.22           N  
ANISOU 3217  N   SER C  44     1616   1964   6762   -233    467    444       N  
ATOM   3218  CA  SER C  44      30.408  44.026 317.058  1.00 27.24           C  
ANISOU 3218  CA  SER C  44     1637   1920   6793   -368    401    448       C  
ATOM   3219  C   SER C  44      30.116  43.402 318.409  1.00 30.76           C  
ANISOU 3219  C   SER C  44     2073   2358   7255   -423    265    400       C  
ATOM   3220  O   SER C  44      29.393  42.419 318.485  1.00 29.63           O  
ANISOU 3220  O   SER C  44     1966   2228   7064   -360    222    346       O  
ATOM   3221  CB  SER C  44      29.303  45.029 316.739  1.00 31.80           C  
ANISOU 3221  CB  SER C  44     2360   2450   7275   -357    424    423       C  
ATOM   3222  OG  SER C  44      29.693  45.974 315.758  1.00 45.59           O  
ANISOU 3222  OG  SER C  44     4138   4179   9006   -341    542    482       O  
ATOM   3223  N   ASP C  45      30.665  43.994 319.473  1.00 29.52           N  
ANISOU 3223  N   ASP C  45     1881   2171   7162   -548    197    422       N  
ATOM   3224  CA  ASP C  45      30.439  43.605 320.867  1.00 30.02           C  
ANISOU 3224  CA  ASP C  45     1961   2214   7230   -613     68    384       C  
ATOM   3225  C   ASP C  45      29.411  44.572 321.467  1.00 36.36           C  
ANISOU 3225  C   ASP C  45     2896   2962   7957   -664     38    345       C  
ATOM   3226  O   ASP C  45      29.008  44.443 322.624  1.00 35.38           O  
ANISOU 3226  O   ASP C  45     2819   2815   7808   -712    -51    309       O  
ATOM   3227  CB  ASP C  45      31.758  43.623 321.660  1.00 32.67           C  
ANISOU 3227  CB  ASP C  45     2180   2552   7681   -706     -4    430       C  
ATOM   3228  N   THR C  46      28.984  45.540 320.645  1.00 35.86           N  
ANISOU 3228  N   THR C  46     2901   2875   7848   -640    119    354       N  
ATOM   3229  CA  THR C  46      28.024  46.583 320.993  1.00 37.03           C  
ANISOU 3229  CA  THR C  46     3181   2969   7919   -659    106    318       C  
ATOM   3230  C   THR C  46      26.845  46.568 320.003  1.00 42.40           C  
ANISOU 3230  C   THR C  46     3936   3668   8507   -538    173    280       C  
ATOM   3231  O   THR C  46      26.986  46.096 318.869  1.00 42.67           O  
ANISOU 3231  O   THR C  46     3942   3733   8539   -460    247    302       O  
ATOM   3232  CB  THR C  46      28.724  47.953 321.028  1.00 51.37           C  
ANISOU 3232  CB  THR C  46     5030   4716   9771   -756    116    369       C  
ATOM   3233  OG1 THR C  46      29.441  48.144 319.807  1.00 54.70           O  
ANISOU 3233  OG1 THR C  46     5406   5149  10228   -735    221    432       O  
ATOM   3234  CG2 THR C  46      29.683  48.101 322.216  1.00 51.76           C  
ANISOU 3234  CG2 THR C  46     5020   4739   9906   -887     16    393       C  
ATOM   3235  N   VAL C  47      25.677  47.064 320.454  1.00 38.55           N  
ANISOU 3235  N   VAL C  47     3543   3164   7941   -515    144    220       N  
ATOM   3236  CA  VAL C  47      24.445  47.127 319.663  1.00 37.37           C  
ANISOU 3236  CA  VAL C  47     3457   3035   7706   -400    183    173       C  
ATOM   3237  C   VAL C  47      24.398  48.515 319.039  1.00 39.92           C  
ANISOU 3237  C   VAL C  47     3880   3296   7991   -380    234    199       C  
ATOM   3238  O   VAL C  47      24.230  49.503 319.759  1.00 41.07           O  
ANISOU 3238  O   VAL C  47     4105   3381   8118   -431    205    194       O  
ATOM   3239  CB  VAL C  47      23.192  46.786 320.520  1.00 40.59           C  
ANISOU 3239  CB  VAL C  47     3892   3470   8059   -380    133     98       C  
ATOM   3240  CG1 VAL C  47      21.912  46.925 319.707  1.00 40.20           C  
ANISOU 3240  CG1 VAL C  47     3887   3452   7937   -261    160     48       C  
ATOM   3241  CG2 VAL C  47      23.300  45.380 321.116  1.00 39.93           C  
ANISOU 3241  CG2 VAL C  47     3730   3433   8010   -415     86     83       C  
ATOM   3242  N   ARG C  48      24.614  48.587 317.711  1.00 34.01           N  
ANISOU 3242  N   ARG C  48     3145   2553   7224   -305    308    231       N  
ATOM   3243  CA  ARG C  48      24.690  49.838 316.957  1.00 33.45           C  
ANISOU 3243  CA  ARG C  48     3185   2414   7110   -283    367    269       C  
ATOM   3244  C   ARG C  48      23.334  50.538 316.883  1.00 36.17           C  
ANISOU 3244  C   ARG C  48     3653   2736   7355   -187    344    207       C  
ATOM   3245  O   ARG C  48      22.339  49.916 316.520  1.00 35.94           O  
ANISOU 3245  O   ARG C  48     3612   2765   7278    -84    324    146       O  
ATOM   3246  CB  ARG C  48      25.259  49.599 315.546  1.00 32.28           C  
ANISOU 3246  CB  ARG C  48     3026   2284   6956   -220    462    323       C  
ATOM   3247  CG  ARG C  48      25.902  50.846 314.933  1.00 41.93           C  
ANISOU 3247  CG  ARG C  48     4342   3426   8165   -253    540    398       C  
ATOM   3248  CD  ARG C  48      26.750  50.572 313.699  1.00 47.06           C  
ANISOU 3248  CD  ARG C  48     4959   4097   8823   -220    655    469       C  
ATOM   3249  NE  ARG C  48      25.979  49.973 312.606  1.00 57.30           N  
ANISOU 3249  NE  ARG C  48     6313   5432  10025    -57    679    430       N  
ATOM   3250  CZ  ARG C  48      25.334  50.656 311.663  1.00 71.76           C  
ANISOU 3250  CZ  ARG C  48     8298   7219  11750     44    715    430       C  
ATOM   3251  NH1 ARG C  48      25.353  51.986 311.664  1.00 57.48           N  
ANISOU 3251  NH1 ARG C  48     6612   5318   9909      1    740    470       N  
ATOM   3252  NH2 ARG C  48      24.663  50.015 310.713  1.00 57.15           N  
ANISOU 3252  NH2 ARG C  48     6494   5405   9816    190    716    388       N  
ATOM   3253  N   SER C  49      23.307  51.829 317.261  1.00 31.89           N  
ANISOU 3253  N   SER C  49     3227   2106   6784   -222    338    219       N  
ATOM   3254  CA  SER C  49      22.117  52.683 317.238  1.00 31.18           C  
ANISOU 3254  CA  SER C  49     3268   1982   6599   -121    316    164       C  
ATOM   3255  C   SER C  49      22.093  53.455 315.924  1.00 34.17           C  
ANISOU 3255  C   SER C  49     3769   2304   6910    -34    376    201       C  
ATOM   3256  O   SER C  49      23.044  54.176 315.615  1.00 35.44           O  
ANISOU 3256  O   SER C  49     3994   2384   7089   -110    425    278       O  
ATOM   3257  CB  SER C  49      22.101  53.623 318.439  1.00 34.80           C  
ANISOU 3257  CB  SER C  49     3810   2363   7050   -195    268    150       C  
ATOM   3258  OG  SER C  49      21.659  52.956 319.611  1.00 41.52           O  
ANISOU 3258  OG  SER C  49     4587   3272   7916   -222    212     93       O  
ATOM   3259  N   LEU C  50      21.025  53.263 315.134  1.00 28.33           N  
ANISOU 3259  N   LEU C  50     3060   1608   6095    121    369    149       N  
ATOM   3260  CA  LEU C  50      20.860  53.842 313.800  1.00 27.62           C  
ANISOU 3260  CA  LEU C  50     3100   1471   5922    232    414    176       C  
ATOM   3261  C   LEU C  50      20.191  55.219 313.802  1.00 31.41           C  
ANISOU 3261  C   LEU C  50     3762   1856   6315    306    391    159       C  
ATOM   3262  O   LEU C  50      20.397  55.996 312.862  1.00 32.31           O  
ANISOU 3262  O   LEU C  50     4024   1887   6364    352    438    210       O  
ATOM   3263  CB  LEU C  50      20.043  52.891 312.912  1.00 26.86           C  
ANISOU 3263  CB  LEU C  50     2958   1465   5783    371    394    123       C  
ATOM   3264  CG  LEU C  50      20.563  51.469 312.747  1.00 30.54           C  
ANISOU 3264  CG  LEU C  50     3279   2013   6313    332    411    132       C  
ATOM   3265  CD1 LEU C  50      19.484  50.587 312.244  1.00 30.52           C  
ANISOU 3265  CD1 LEU C  50     3226   2093   6276    445    348     51       C  
ATOM   3266  CD2 LEU C  50      21.735  51.407 311.798  1.00 32.90           C  
ANISOU 3266  CD2 LEU C  50     3612   2282   6608    322    509    218       C  
ATOM   3267  N   LYS C  51      19.373  55.514 314.819  1.00 26.28           N  
ANISOU 3267  N   LYS C  51     3115   1217   5654    330    326     87       N  
ATOM   3268  CA  LYS C  51      18.682  56.802 314.882  1.00 26.05           C  
ANISOU 3268  CA  LYS C  51     3263   1098   5537    424    298     60       C  
ATOM   3269  C   LYS C  51      19.205  57.626 316.063  1.00 27.95           C  
ANISOU 3269  C   LYS C  51     3574   1244   5803    298    282     78       C  
ATOM   3270  O   LYS C  51      19.592  57.034 317.068  1.00 26.49           O  
ANISOU 3270  O   LYS C  51     3268   1103   5695    177    266     73       O  
ATOM   3271  CB  LYS C  51      17.156  56.604 314.955  1.00 27.93           C  
ANISOU 3271  CB  LYS C  51     3466   1424   5724    591    236    -45       C  
ATOM   3272  CG  LYS C  51      16.544  55.846 313.767  1.00 32.26           C  
ANISOU 3272  CG  LYS C  51     3959   2056   6241    721    223    -73       C  
ATOM   3273  CD  LYS C  51      16.936  56.423 312.408  1.00 38.33           C  
ANISOU 3273  CD  LYS C  51     4893   2737   6933    794    259    -13       C  
ATOM   3274  CE  LYS C  51      16.139  55.821 311.284  1.00 44.23           C  
ANISOU 3274  CE  LYS C  51     5622   3557   7627    948    221    -56       C  
ATOM   3275  NZ  LYS C  51      14.809  56.466 311.151  1.00 49.22           N  
ANISOU 3275  NZ  LYS C  51     6312   4205   8186   1130    140   -139       N  
ATOM   3276  N   PRO C  52      19.231  58.981 315.977  1.00 24.49           N  
ANISOU 3276  N   PRO C  52     3334    688   5284    319    277     97       N  
ATOM   3277  CA  PRO C  52      19.785  59.785 317.092  1.00 24.64           C  
ANISOU 3277  CA  PRO C  52     3418    641   5302    188    249    110       C  
ATOM   3278  C   PRO C  52      19.079  59.601 318.445  1.00 26.87           C  
ANISOU 3278  C   PRO C  52     3687    910   5611    219    190     22       C  
ATOM   3279  O   PRO C  52      19.597  60.051 319.469  1.00 27.08           O  
ANISOU 3279  O   PRO C  52     3773    860   5656    107    157     27       O  
ATOM   3280  CB  PRO C  52      19.620  61.226 316.601  1.00 27.42           C  
ANISOU 3280  CB  PRO C  52     4063    766   5590    259    247    136       C  
ATOM   3281  CG  PRO C  52      19.549  61.121 315.118  1.00 32.04           C  
ANISOU 3281  CG  PRO C  52     4683   1364   6128    362    299    174       C  
ATOM   3282  CD  PRO C  52      18.827  59.844 314.848  1.00 26.50           C  
ANISOU 3282  CD  PRO C  52     3787    838   5445    465    289    110       C  
ATOM   3283  N   TRP C  53      17.932  58.897 318.441  1.00 21.83           N  
ANISOU 3283  N   TRP C  53     2834    626   4835    312    179    -50       N  
ATOM   3284  CA  TRP C  53      17.044  58.634 319.570  1.00 20.42           C  
ANISOU 3284  CA  TRP C  53     2552    613   4593    331    146   -125       C  
ATOM   3285  C   TRP C  53      16.872  57.125 319.858  1.00 22.40           C  
ANISOU 3285  C   TRP C  53     2689    774   5048    348    156   -161       C  
ATOM   3286  O   TRP C  53      15.938  56.741 320.570  1.00 22.19           O  
ANISOU 3286  O   TRP C  53     2595    822   5015    408    147   -232       O  
ATOM   3287  CB  TRP C  53      15.676  59.261 319.260  1.00 19.58           C  
ANISOU 3287  CB  TRP C  53     2484    631   4323    474    124   -181       C  
ATOM   3288  CG  TRP C  53      15.205  59.051 317.846  1.00 19.81           C  
ANISOU 3288  CG  TRP C  53     2516    669   4341    586    127   -181       C  
ATOM   3289  CD1 TRP C  53      15.420  59.875 316.783  1.00 22.54           C  
ANISOU 3289  CD1 TRP C  53     3114    716   4734    743    137   -157       C  
ATOM   3290  CD2 TRP C  53      14.453  57.938 317.343  1.00 19.18           C  
ANISOU 3290  CD2 TRP C  53     2260    751   4275    612    115   -216       C  
ATOM   3291  NE1 TRP C  53      14.838  59.356 315.653  1.00 21.85           N  
ANISOU 3291  NE1 TRP C  53     2946    764   4592    821    127   -168       N  
ATOM   3292  CE2 TRP C  53      14.214  58.180 315.971  1.00 22.23           C  
ANISOU 3292  CE2 TRP C  53     2818    877   4752    866    114   -230       C  
ATOM   3293  CE3 TRP C  53      13.925  56.771 317.927  1.00 19.20           C  
ANISOU 3293  CE3 TRP C  53     2098    813   4383    609    111   -269       C  
ATOM   3294  CZ2 TRP C  53      13.508  57.276 315.159  1.00 21.68           C  
ANISOU 3294  CZ2 TRP C  53     2610    967   4663    912     84   -262       C  
ATOM   3295  CZ3 TRP C  53      13.221  55.880 317.125  1.00 19.96           C  
ANISOU 3295  CZ3 TRP C  53     2105    931   4547    720     92   -312       C  
ATOM   3296  CH2 TRP C  53      13.023  56.131 315.757  1.00 20.93           C  
ANISOU 3296  CH2 TRP C  53     2312   1001   4638    859     72   -309       C  
ATOM   3297  N   SER C  54      17.773  56.277 319.335  1.00 18.62           N  
ANISOU 3297  N   SER C  54     1941    658   4476    176    176    -87       N  
ATOM   3298  CA  SER C  54      17.701  54.824 319.522  1.00 17.22           C  
ANISOU 3298  CA  SER C  54     1538    669   4335    117    176    -97       C  
ATOM   3299  C   SER C  54      17.933  54.376 320.987  1.00 19.87           C  
ANISOU 3299  C   SER C  54     1940    764   4845     77    156   -125       C  
ATOM   3300  O   SER C  54      17.519  53.275 321.350  1.00 19.53           O  
ANISOU 3300  O   SER C  54     1768    815   4838     65    153   -155       O  
ATOM   3301  CB  SER C  54      18.689  54.120 318.602  1.00 18.26           C  
ANISOU 3301  CB  SER C  54     1680    640   4619    100    208    -42       C  
ATOM   3302  OG  SER C  54      18.439  54.444 317.246  1.00 23.27           O  
ANISOU 3302  OG  SER C  54     2515    978   5350    256    233    -36       O  
ATOM   3303  N   GLN C  55      18.580  55.206 321.820  1.00 17.28           N  
ANISOU 3303  N   GLN C  55     1566    648   4351      3    135    -93       N  
ATOM   3304  CA  GLN C  55      18.806  54.871 323.226  1.00 16.76           C  
ANISOU 3304  CA  GLN C  55     1454    637   4276    -47    104   -106       C  
ATOM   3305  C   GLN C  55      17.588  55.294 324.057  1.00 21.11           C  
ANISOU 3305  C   GLN C  55     2299    750   4973     12    104   -203       C  
ATOM   3306  O   GLN C  55      17.449  54.879 325.207  1.00 21.08           O  
ANISOU 3306  O   GLN C  55     2272    772   4964    -33     94   -230       O  
ATOM   3307  CB  GLN C  55      20.097  55.524 323.750  1.00 17.87           C  
ANISOU 3307  CB  GLN C  55     1709    622   4460   -139     63    -61       C  
ATOM   3308  CG  GLN C  55      20.588  54.926 325.062  1.00 18.87           C  
ANISOU 3308  CG  GLN C  55     1934    464   4772   -294     13    -67       C  
ATOM   3309  CD  GLN C  55      21.998  55.314 325.388  1.00 34.69           C  
ANISOU 3309  CD  GLN C  55     4084   2133   6964   -523    -44     -9       C  
ATOM   3310  OE1 GLN C  55      22.915  55.183 324.567  1.00 35.65           O  
ANISOU 3310  OE1 GLN C  55     4132   2247   7166   -589    -27     59       O  
ATOM   3311  NE2 GLN C  55      22.217  55.728 326.625  1.00 21.33           N  
ANISOU 3311  NE2 GLN C  55     2416    544   5144   -520   -111    -27       N  
ATOM   3312  N   GLY C  56      16.720  56.106 323.460  1.00 20.06           N  
ANISOU 3312  N   GLY C  56     2206    690   4724    140    119   -231       N  
ATOM   3313  CA  GLY C  56      15.505  56.604 324.092  1.00 21.02           C  
ANISOU 3313  CA  GLY C  56     2423    761   4801    275    130   -314       C  
ATOM   3314  C   GLY C  56      15.768  57.454 325.317  1.00 25.97           C  
ANISOU 3314  C   GLY C  56     3268   1175   5423    262    108   -343       C  
ATOM   3315  O   GLY C  56      16.592  58.370 325.266  1.00 26.39           O  
ANISOU 3315  O   GLY C  56     3480   1082   5464    203     70   -304       O  
ATOM   3316  N   THR C  57      15.083  57.117 326.436  1.00 22.33           N  
ANISOU 3316  N   THR C  57     2778    785   4922    286    129   -398       N  
ATOM   3317  CA  THR C  57      15.163  57.799 327.733  1.00 22.31           C  
ANISOU 3317  CA  THR C  57     2935    708   4834    266    109   -424       C  
ATOM   3318  C   THR C  57      16.124  57.035 328.681  1.00 23.70           C  
ANISOU 3318  C   THR C  57     3082    859   5063     82     73   -389       C  
ATOM   3319  O   THR C  57      16.395  57.510 329.787  1.00 24.08           O  
ANISOU 3319  O   THR C  57     3276    825   5049     41     38   -406       O  
ATOM   3320  CB  THR C  57      13.743  57.961 328.320  1.00 34.54           C  
ANISOU 3320  CB  THR C  57     4493   2330   6299    440    171   -512       C  
ATOM   3321  OG1 THR C  57      12.867  58.415 327.289  1.00 34.71           O  
ANISOU 3321  OG1 THR C  57     4477   2402   6308    612    196   -543       O  
ATOM   3322  CG2 THR C  57      13.681  58.971 329.467  1.00 37.50           C  
ANISOU 3322  CG2 THR C  57     5102   2589   6560    487    155   -554       C  
ATOM   3323  N   PHE C  58      16.674  55.886 328.229  1.00 18.89           N  
ANISOU 3323  N   PHE C  58     2144    627   4405    -18     71   -303       N  
ATOM   3324  CA  PHE C  58      17.621  55.089 329.016  1.00 17.91           C  
ANISOU 3324  CA  PHE C  58     1913    626   4265   -125     30   -256       C  
ATOM   3325  C   PHE C  58      18.966  55.776 329.149  1.00 20.33           C  
ANISOU 3325  C   PHE C  58     2407    641   4678   -252    -55   -224       C  
ATOM   3326  O   PHE C  58      19.561  56.152 328.136  1.00 20.70           O  
ANISOU 3326  O   PHE C  58     2437    656   4771   -267    -62   -180       O  
ATOM   3327  CB  PHE C  58      17.841  53.696 328.401  1.00 18.08           C  
ANISOU 3327  CB  PHE C  58     1775    671   4425   -165     49   -234       C  
ATOM   3328  CG  PHE C  58      16.769  52.659 328.634  1.00 18.41           C  
ANISOU 3328  CG  PHE C  58     1748    732   4515   -149    106   -281       C  
ATOM   3329  CD1 PHE C  58      16.088  52.596 329.844  1.00 21.22           C  
ANISOU 3329  CD1 PHE C  58     2269    889   4906   -180    132   -347       C  
ATOM   3330  CD2 PHE C  58      16.499  51.694 327.676  1.00 18.62           C  
ANISOU 3330  CD2 PHE C  58     1671    732   4672   -158    131   -285       C  
ATOM   3331  CE1 PHE C  58      15.122  51.618 330.069  1.00 22.05           C  
ANISOU 3331  CE1 PHE C  58     2250   1122   5004   -159    197   -374       C  
ATOM   3332  CE2 PHE C  58      15.530  50.721 327.900  1.00 21.10           C  
ANISOU 3332  CE2 PHE C  58     1916   1068   5032   -162    177   -327       C  
ATOM   3333  CZ  PHE C  58      14.856  50.680 329.098  1.00 20.25           C  
ANISOU 3333  CZ  PHE C  58     1850    990   4854   -159    215   -362       C  
ATOM   3334  N   SER C  59      19.466  55.899 330.391  1.00 17.34           N  
ANISOU 3334  N   SER C  59     1952    565   4070   -233   -113   -194       N  
ATOM   3335  CA  SER C  59      20.772  56.491 330.685  1.00 17.71           C  
ANISOU 3335  CA  SER C  59     2067    551   4112   -313   -213   -149       C  
ATOM   3336  C   SER C  59      21.888  55.619 330.111  1.00 22.18           C  
ANISOU 3336  C   SER C  59     2648    764   5017   -529   -249   -113       C  
ATOM   3337  O   SER C  59      21.640  54.446 329.786  1.00 21.86           O  
ANISOU 3337  O   SER C  59     2449    837   5020   -501   -203   -108       O  
ATOM   3338  CB  SER C  59      20.954  56.656 332.193  1.00 19.34           C  
ANISOU 3338  CB  SER C  59     2501    516   4330   -415   -289   -187       C  
ATOM   3339  OG  SER C  59      21.138  55.434 332.893  1.00 20.63           O  
ANISOU 3339  OG  SER C  59     2672    544   4624   -526   -307   -200       O  
ATOM   3340  N   ASP C  60      23.122  56.164 330.003  1.00 20.73           N  
ANISOU 3340  N   ASP C  60     2390    730   4757   -524   -321    -48       N  
ATOM   3341  CA  ASP C  60      24.256  55.381 329.499  1.00 20.15           C  
ANISOU 3341  CA  ASP C  60     2133    755   4767   -545   -346     17       C  
ATOM   3342  C   ASP C  60      24.465  54.113 330.324  1.00 22.00           C  
ANISOU 3342  C   ASP C  60     2370    838   5152   -690   -391      8       C  
ATOM   3343  O   ASP C  60      24.763  53.080 329.737  1.00 21.54           O  
ANISOU 3343  O   ASP C  60     2153    863   5167   -670   -364     39       O  
ATOM   3344  CB  ASP C  60      25.543  56.208 329.469  1.00 22.50           C  
ANISOU 3344  CB  ASP C  60     2528    825   5198   -731   -430     66       C  
ATOM   3345  CG  ASP C  60      25.744  57.041 328.214  1.00 30.69           C  
ANISOU 3345  CG  ASP C  60     3802   1262   6596  -1052   -374     92       C  
ATOM   3346  OD1 ASP C  60      24.823  57.070 327.359  1.00 30.99           O  
ANISOU 3346  OD1 ASP C  60     3849   1347   6578   -912   -277     71       O  
ATOM   3347  OD2 ASP C  60      26.828  57.658 328.079  1.00 35.83           O  
ANISOU 3347  OD2 ASP C  60     4465   1824   7325  -1189   -425    150       O  
ATOM   3348  N   GLN C  61      24.239  54.178 331.663  1.00 19.53           N  
ANISOU 3348  N   GLN C  61     2089    717   4614   -574   -445    -13       N  
ATOM   3349  CA  GLN C  61      24.392  53.052 332.592  1.00 19.18           C  
ANISOU 3349  CA  GLN C  61     2005    732   4550   -576   -489    -10       C  
ATOM   3350  C   GLN C  61      23.362  51.958 332.313  1.00 20.13           C  
ANISOU 3350  C   GLN C  61     2093    789   4765   -605   -389    -49       C  
ATOM   3351  O   GLN C  61      23.733  50.781 332.240  1.00 19.82           O  
ANISOU 3351  O   GLN C  61     1930    845   4755   -580   -399    -19       O  
ATOM   3352  CB  GLN C  61      24.315  53.498 334.066  1.00 21.04           C  
ANISOU 3352  CB  GLN C  61     2476    758   4760   -706   -575    -54       C  
ATOM   3353  CG  GLN C  61      25.495  54.352 334.541  1.00 40.01           C  
ANISOU 3353  CG  GLN C  61     5189   2482   7530  -1160   -743    -88       C  
ATOM   3354  CD  GLN C  61      25.353  55.839 334.284  1.00 63.27           C  
ANISOU 3354  CD  GLN C  61     8298   5310  10432  -1147   -746   -106       C  
ATOM   3355  OE1 GLN C  61      24.345  56.295 333.729  1.00 58.69           O  
ANISOU 3355  OE1 GLN C  61     7764   4750   9787  -1023   -635   -137       O  
ATOM   3356  NE2 GLN C  61      26.366  56.622 334.645  1.00 61.16           N  
ANISOU 3356  NE2 GLN C  61     8121   4913  10205  -1275   -879    -86       N  
ATOM   3357  N   GLN C  62      22.078  52.346 332.149  1.00 16.12           N  
ANISOU 3357  N   GLN C  62     1513    598   4014   -361   -285    -76       N  
ATOM   3358  CA  GLN C  62      20.965  51.437 331.836  1.00 13.94           C  
ANISOU 3358  CA  GLN C  62     1101    525   3670   -229   -181    -96       C  
ATOM   3359  C   GLN C  62      21.235  50.758 330.530  1.00 16.39           C  
ANISOU 3359  C   GLN C  62     1359    635   4233   -337   -158    -86       C  
ATOM   3360  O   GLN C  62      21.097  49.542 330.435  1.00 15.59           O  
ANISOU 3360  O   GLN C  62     1159    626   4140   -289   -136    -79       O  
ATOM   3361  CB  GLN C  62      19.631  52.193 331.760  1.00 14.07           C  
ANISOU 3361  CB  GLN C  62     1195    491   3660   -223    -98   -156       C  
ATOM   3362  CG  GLN C  62      19.139  52.700 333.100  1.00 15.88           C  
ANISOU 3362  CG  GLN C  62     1664    495   3876   -316   -104   -212       C  
ATOM   3363  CD  GLN C  62      17.884  53.525 332.983  1.00 25.71           C  
ANISOU 3363  CD  GLN C  62     3232   1199   5338   -388    -30   -335       C  
ATOM   3364  OE1 GLN C  62      17.787  54.464 332.186  1.00 18.22           O  
ANISOU 3364  OE1 GLN C  62     2200    466   4256   -260    -22   -311       O  
ATOM   3365  NE2 GLN C  62      16.910  53.231 333.828  1.00 23.88           N  
ANISOU 3365  NE2 GLN C  62     3016   1040   5018   -329     44   -378       N  
ATOM   3366  N   TRP C  63      21.686  51.543 329.537  1.00 15.55           N  
ANISOU 3366  N   TRP C  63     1184    645   4079   -240   -155    -56       N  
ATOM   3367  CA  TRP C  63      22.009  51.064 328.205  1.00 15.93           C  
ANISOU 3367  CA  TRP C  63     1127    700   4227   -213   -121    -30       C  
ATOM   3368  C   TRP C  63      23.175  50.070 328.206  1.00 19.69           C  
ANISOU 3368  C   TRP C  63     1613    899   4969   -455   -177     11       C  
ATOM   3369  O   TRP C  63      23.138  49.120 327.422  1.00 19.47           O  
ANISOU 3369  O   TRP C  63     1484    921   4991   -413   -141     21       O  
ATOM   3370  CB  TRP C  63      22.305  52.228 327.266  1.00 15.88           C  
ANISOU 3370  CB  TRP C  63     1135    689   4209   -197   -105    -12       C  
ATOM   3371  CG  TRP C  63      22.264  51.848 325.816  1.00 16.45           C  
ANISOU 3371  CG  TRP C  63     1141    724   4384   -189    -45      2       C  
ATOM   3372  CD1 TRP C  63      23.271  51.978 324.909  1.00 18.81           C  
ANISOU 3372  CD1 TRP C  63     1471    807   4868   -330    -38     56       C  
ATOM   3373  CD2 TRP C  63      21.158  51.265 325.107  1.00 15.98           C  
ANISOU 3373  CD2 TRP C  63     1015    741   4316   -113     17    -33       C  
ATOM   3374  NE1 TRP C  63      22.861  51.529 323.675  1.00 18.09           N  
ANISOU 3374  NE1 TRP C  63     1305    789   4780   -244     28     55       N  
ATOM   3375  CE2 TRP C  63      21.571  51.077 323.769  1.00 18.54           C  
ANISOU 3375  CE2 TRP C  63     1385    808   4853   -240     51     -1       C  
ATOM   3376  CE3 TRP C  63      19.856  50.880 325.474  1.00 16.62           C  
ANISOU 3376  CE3 TRP C  63     1123    775   4418   -129     45    -90       C  
ATOM   3377  CZ2 TRP C  63      20.735  50.516 322.800  1.00 17.64           C  
ANISOU 3377  CZ2 TRP C  63     1187    806   4707   -137     96    -26       C  
ATOM   3378  CZ3 TRP C  63      19.030  50.323 324.513  1.00 17.32           C  
ANISOU 3378  CZ3 TRP C  63     1175    820   4587   -119     87   -116       C  
ATOM   3379  CH2 TRP C  63      19.470  50.146 323.194  1.00 17.71           C  
ANISOU 3379  CH2 TRP C  63     1186    850   4694   -108    104    -85       C  
ATOM   3380  N   GLU C  64      24.183  50.260 329.085  1.00 17.96           N  
ANISOU 3380  N   GLU C  64     1381    819   4623   -371   -265     46       N  
ATOM   3381  CA  GLU C  64      25.315  49.338 329.186  1.00 18.15           C  
ANISOU 3381  CA  GLU C  64     1332    849   4717   -385   -329     94       C  
ATOM   3382  C   GLU C  64      24.848  47.978 329.771  1.00 21.89           C  
ANISOU 3382  C   GLU C  64     1836   1093   5388   -648   -339     65       C  
ATOM   3383  O   GLU C  64      25.279  46.919 329.297  1.00 22.40           O  
ANISOU 3383  O   GLU C  64     1803   1163   5544   -666   -342     91       O  
ATOM   3384  CB  GLU C  64      26.444  49.945 330.031  1.00 19.95           C  
ANISOU 3384  CB  GLU C  64     1630    927   5022   -558   -445    122       C  
ATOM   3385  N   THR C  65      23.941  48.020 330.769  1.00 18.62           N  
ANISOU 3385  N   THR C  65     1470    883   4720   -449   -325     33       N  
ATOM   3386  CA  THR C  65      23.384  46.846 331.429  1.00 18.03           C  
ANISOU 3386  CA  THR C  65     1393    868   4589   -420   -315     21       C  
ATOM   3387  C   THR C  65      22.632  45.995 330.407  1.00 20.55           C  
ANISOU 3387  C   THR C  65     1662   1026   5121   -588   -238     -7       C  
ATOM   3388  O   THR C  65      22.866  44.784 330.356  1.00 20.48           O  
ANISOU 3388  O   THR C  65     1595   1044   5141   -587   -256     13       O  
ATOM   3389  CB  THR C  65      22.510  47.286 332.616  1.00 23.39           C  
ANISOU 3389  CB  THR C  65     2285   1189   5412   -766   -314    -49       C  
ATOM   3390  OG1 THR C  65      23.363  47.513 333.742  1.00 25.00           O  
ANISOU 3390  OG1 THR C  65     2594   1319   5585   -833   -426    -36       O  
ATOM   3391  CG2 THR C  65      21.414  46.275 332.982  1.00 19.64           C  
ANISOU 3391  CG2 THR C  65     1770    902   4789   -636   -253    -58       C  
ATOM   3392  N   LEU C  66      21.753  46.622 329.582  1.00 17.46           N  
ANISOU 3392  N   LEU C  66     1223    844   4567   -330   -152    -29       N  
ATOM   3393  CA  LEU C  66      20.985  45.888 328.571  1.00 16.33           C  
ANISOU 3393  CA  LEU C  66      998    802   4406   -199    -85    -45       C  
ATOM   3394  C   LEU C  66      21.913  45.303 327.538  1.00 19.84           C  
ANISOU 3394  C   LEU C  66     1388   1025   5125   -440   -110    -13       C  
ATOM   3395  O   LEU C  66      21.756  44.133 327.179  1.00 19.85           O  
ANISOU 3395  O   LEU C  66     1336   1054   5153   -423   -102    -13       O  
ATOM   3396  CB  LEU C  66      19.935  46.761 327.902  1.00 15.76           C  
ANISOU 3396  CB  LEU C  66      917    772   4300   -130    -16    -86       C  
ATOM   3397  CG  LEU C  66      18.793  47.202 328.784  1.00 18.87           C  
ANISOU 3397  CG  LEU C  66     1420    940   4809   -374     20   -148       C  
ATOM   3398  CD1 LEU C  66      18.033  48.308 328.126  1.00 18.69           C  
ANISOU 3398  CD1 LEU C  66     1432    875   4794   -336     64   -186       C  
ATOM   3399  CD2 LEU C  66      17.865  46.043 329.107  1.00 20.09           C  
ANISOU 3399  CD2 LEU C  66     1545   1004   5083   -547     56   -182       C  
ATOM   3400  N   GLN C  67      22.935  46.090 327.123  1.00 17.36           N  
ANISOU 3400  N   GLN C  67     1053    858   4684   -221   -130     29       N  
ATOM   3401  CA  GLN C  67      23.955  45.677 326.163  1.00 16.89           C  
ANISOU 3401  CA  GLN C  67      928    823   4667   -142   -135     73       C  
ATOM   3402  C   GLN C  67      24.647  44.390 326.631  1.00 18.44           C  
ANISOU 3402  C   GLN C  67     1093    924   4988   -285   -194     97       C  
ATOM   3403  O   GLN C  67      24.885  43.507 325.808  1.00 17.88           O  
ANISOU 3403  O   GLN C  67      977    889   4930   -191   -177    110       O  
ATOM   3404  CB  GLN C  67      24.976  46.799 325.956  1.00 18.28           C  
ANISOU 3404  CB  GLN C  67     1108    876   4963   -296   -152    111       C  
ATOM   3405  CG  GLN C  67      25.516  46.844 324.543  1.00 36.66           C  
ANISOU 3405  CG  GLN C  67     3374   2865   7691   -732    -89    154       C  
ATOM   3406  CD  GLN C  67      25.303  48.192 323.919  1.00 57.52           C  
ANISOU 3406  CD  GLN C  67     6095   5459  10302   -709    -37    161       C  
ATOM   3407  OE1 GLN C  67      24.225  48.509 323.405  1.00 50.07           O  
ANISOU 3407  OE1 GLN C  67     5207   4531   9288   -618     12    123       O  
ATOM   3408  NE2 GLN C  67      26.340  49.008 323.939  1.00 57.31           N  
ANISOU 3408  NE2 GLN C  67     6076   5370  10329   -793    -55    212       N  
ATOM   3409  N   HIS C  68      24.916  44.273 327.957  1.00 15.63           N  
ANISOU 3409  N   HIS C  68      792    752   4393    -47   -260    112       N  
ATOM   3410  CA  HIS C  68      25.537  43.109 328.599  1.00 15.14           C  
ANISOU 3410  CA  HIS C  68      743    719   4288    -13   -324    140       C  
ATOM   3411  C   HIS C  68      24.625  41.895 328.522  1.00 15.69           C  
ANISOU 3411  C   HIS C  68      804    760   4397    -53   -296    113       C  
ATOM   3412  O   HIS C  68      25.103  40.794 328.276  1.00 15.26           O  
ANISOU 3412  O   HIS C  68      781    758   4261    -11   -311    129       O  
ATOM   3413  CB  HIS C  68      25.888  43.412 330.069  1.00 15.90           C  
ANISOU 3413  CB  HIS C  68      881    740   4418   -166   -416    150       C  
ATOM   3414  CG  HIS C  68      26.578  42.281 330.773  1.00 18.50           C  
ANISOU 3414  CG  HIS C  68     1207    915   4906   -389   -513    168       C  
ATOM   3415  ND1 HIS C  68      25.877  41.389 331.563  1.00 19.55           N  
ANISOU 3415  ND1 HIS C  68     1400   1000   5028   -499   -523    145       N  
ATOM   3416  CD2 HIS C  68      27.888  41.929 330.777  1.00 19.91           C  
ANISOU 3416  CD2 HIS C  68     1325    995   5245   -503   -602    205       C  
ATOM   3417  CE1 HIS C  68      26.777  40.533 332.026  1.00 19.24           C  
ANISOU 3417  CE1 HIS C  68     1353    956   5002   -484   -616    181       C  
ATOM   3418  NE2 HIS C  68      28.000  40.821 331.587  1.00 19.68           N  
ANISOU 3418  NE2 HIS C  68     1332    968   5178   -500   -671    214       N  
ATOM   3419  N   ILE C  69      23.317  42.098 328.736  1.00 14.15           N  
ANISOU 3419  N   ILE C  69      754    741   3879     -4   -212     64       N  
ATOM   3420  CA  ILE C  69      22.311  41.036 328.688  1.00 13.82           C  
ANISOU 3420  CA  ILE C  69      737    728   3786     -2   -176     40       C  
ATOM   3421  C   ILE C  69      22.341  40.379 327.288  1.00 16.02           C  
ANISOU 3421  C   ILE C  69      909    901   4276     -2   -166     39       C  
ATOM   3422  O   ILE C  69      22.540  39.171 327.213  1.00 15.63           O  
ANISOU 3422  O   ILE C  69      874    864   4201     -3   -190     51       O  
ATOM   3423  CB  ILE C  69      20.907  41.573 329.102  1.00 15.06           C  
ANISOU 3423  CB  ILE C  69      830    825   4068      0   -125     -3       C  
ATOM   3424  CG1 ILE C  69      20.903  41.946 330.601  1.00 15.30           C  
ANISOU 3424  CG1 ILE C  69      901    829   4083    -93   -150     -3       C  
ATOM   3425  CG2 ILE C  69      19.790  40.567 328.773  1.00 14.99           C  
ANISOU 3425  CG2 ILE C  69      804    802   4089      1    -81    -32       C  
ATOM   3426  CD1 ILE C  69      19.822  42.916 331.030  1.00 22.29           C  
ANISOU 3426  CD1 ILE C  69     1838   1317   5313   -668    -97    -75       C  
ATOM   3427  N   PHE C  70      22.232  41.180 326.204  1.00 13.75           N  
ANISOU 3427  N   PHE C  70      675    671   3879     -1   -115     24       N  
ATOM   3428  CA  PHE C  70      22.281  40.698 324.823  1.00 13.44           C  
ANISOU 3428  CA  PHE C  70      597    594   3917     -1    -95     20       C  
ATOM   3429  C   PHE C  70      23.614  40.027 324.501  1.00 16.35           C  
ANISOU 3429  C   PHE C  70      828    824   4559     -2   -141     64       C  
ATOM   3430  O   PHE C  70      23.617  39.016 323.815  1.00 16.45           O  
ANISOU 3430  O   PHE C  70      809    804   4637     -2   -142     60       O  
ATOM   3431  CB  PHE C  70      22.016  41.835 323.826  1.00 14.90           C  
ANISOU 3431  CB  PHE C  70      722    722   4216      0    -51      7       C  
ATOM   3432  CG  PHE C  70      20.768  42.664 324.072  1.00 16.58           C  
ANISOU 3432  CG  PHE C  70      900    900   4501      0    -18    -35       C  
ATOM   3433  CD1 PHE C  70      19.527  42.051 324.263  1.00 19.13           C  
ANISOU 3433  CD1 PHE C  70     1149   1127   4992   -110     -7    -82       C  
ATOM   3434  CD2 PHE C  70      20.819  44.056 324.038  1.00 18.26           C  
ANISOU 3434  CD2 PHE C  70     1067   1067   4806      0      2    -36       C  
ATOM   3435  CE1 PHE C  70      18.374  42.817 324.486  1.00 19.96           C  
ANISOU 3435  CE1 PHE C  70     1256   1229   5101   -155     30   -128       C  
ATOM   3436  CE2 PHE C  70      19.664  44.822 324.248  1.00 20.49           C  
ANISOU 3436  CE2 PHE C  70     1350   1258   5176   -153     33    -84       C  
ATOM   3437  CZ  PHE C  70      18.452  44.196 324.482  1.00 19.35           C  
ANISOU 3437  CZ  PHE C  70     1207   1178   4968    -80     51   -128       C  
ATOM   3438  N   ARG C  71      24.739  40.555 325.017  1.00 14.34           N  
ANISOU 3438  N   ARG C  71      605    600   4244     -5   -171     99       N  
ATOM   3439  CA  ARG C  71      26.080  39.998 324.792  1.00 14.22           C  
ANISOU 3439  CA  ARG C  71      561    555   4289     -8   -204    138       C  
ATOM   3440  C   ARG C  71      26.148  38.555 325.305  1.00 18.29           C  
ANISOU 3440  C   ARG C  71      943    913   5093   -110   -284    152       C  
ATOM   3441  O   ARG C  71      26.554  37.642 324.569  1.00 18.70           O  
ANISOU 3441  O   ARG C  71      948    923   5233   -129   -286    158       O  
ATOM   3442  CB  ARG C  71      27.153  40.871 325.457  1.00 12.33           C  
ANISOU 3442  CB  ARG C  71      411    404   3868    -11   -226    162       C  
ATOM   3443  CG  ARG C  71      28.342  41.096 324.545  1.00 16.07           C  
ANISOU 3443  CG  ARG C  71      623    621   4861    -13   -242    231       C  
ATOM   3444  CD  ARG C  71      29.380  42.049 325.105  1.00 23.28           C  
ANISOU 3444  CD  ARG C  71     1289   1304   6253   -709   -293    270       C  
ATOM   3445  NE  ARG C  71      28.890  43.428 325.152  1.00 34.93           N  
ANISOU 3445  NE  ARG C  71     2818   2722   7732   -817   -260    262       N  
ATOM   3446  CZ  ARG C  71      28.620  44.086 326.273  1.00 49.22           C  
ANISOU 3446  CZ  ARG C  71     4721   4481   9500   -891   -325    242       C  
ATOM   3447  NH1 ARG C  71      28.807  43.506 327.453  1.00 44.36           N  
ANISOU 3447  NH1 ARG C  71     4135   3845   8875   -936   -427    231       N  
ATOM   3448  NH2 ARG C  71      28.169  45.330 326.224  1.00 29.18           N  
ANISOU 3448  NH2 ARG C  71     2264   1901   6920   -913   -291    231       N  
ATOM   3449  N   VAL C  72      25.681  38.357 326.553  1.00 16.10           N  
ANISOU 3449  N   VAL C  72      784    763   4571    -12   -314    145       N  
ATOM   3450  CA  VAL C  72      25.607  37.071 327.245  1.00 15.73           C  
ANISOU 3450  CA  VAL C  72      790    761   4426    -15   -361    149       C  
ATOM   3451  C   VAL C  72      24.567  36.213 326.526  1.00 17.80           C  
ANISOU 3451  C   VAL C  72      976    913   4876   -106   -343    118       C  
ATOM   3452  O   VAL C  72      24.832  35.048 326.267  1.00 17.52           O  
ANISOU 3452  O   VAL C  72      933    867   4855    -89   -381    126       O  
ATOM   3453  CB  VAL C  72      25.286  37.276 328.753  1.00 17.25           C  
ANISOU 3453  CB  VAL C  72      969    858   4727   -162   -428    156       C  
ATOM   3454  CG1 VAL C  72      24.804  35.995 329.427  1.00 17.10           C  
ANISOU 3454  CG1 VAL C  72     1001    844   4651   -201   -460    155       C  
ATOM   3455  CG2 VAL C  72      26.472  37.872 329.492  1.00 17.23           C  
ANISOU 3455  CG2 VAL C  72      962    824   4761   -191   -510    193       C  
ATOM   3456  N   TYR C  73      23.408  36.797 326.167  1.00 16.42           N  
ANISOU 3456  N   TYR C  73      897    881   4459     -6   -255     79       N  
ATOM   3457  CA  TYR C  73      22.342  36.069 325.481  1.00 16.26           C  
ANISOU 3457  CA  TYR C  73      880    866   4431     -3   -226     46       C  
ATOM   3458  C   TYR C  73      22.885  35.459 324.211  1.00 18.49           C  
ANISOU 3458  C   TYR C  73     1030    986   5011    -94   -249     43       C  
ATOM   3459  O   TYR C  73      22.796  34.244 324.068  1.00 19.56           O  
ANISOU 3459  O   TYR C  73     1160   1065   5207   -191   -288     33       O  
ATOM   3460  CB  TYR C  73      21.110  36.956 325.208  1.00 16.87           C  
ANISOU 3460  CB  TYR C  73      947    939   4523      0   -166      6       C  
ATOM   3461  CG  TYR C  73      20.101  36.344 324.263  1.00 17.36           C  
ANISOU 3461  CG  TYR C  73      964    958   4673      1   -151    -32       C  
ATOM   3462  CD1 TYR C  73      19.262  35.314 324.677  1.00 19.04           C  
ANISOU 3462  CD1 TYR C  73     1151   1109   4973   -204   -172    -55       C  
ATOM   3463  CD2 TYR C  73      19.969  36.809 322.960  1.00 17.48           C  
ANISOU 3463  CD2 TYR C  73      970    966   4707      2   -124    -55       C  
ATOM   3464  CE1 TYR C  73      18.340  34.736 323.801  1.00 19.69           C  
ANISOU 3464  CE1 TYR C  73     1195   1162   5124   -286   -175    -97       C  
ATOM   3465  CE2 TYR C  73      19.041  36.251 322.082  1.00 17.75           C  
ANISOU 3465  CE2 TYR C  73      979    977   4789      3   -127    -95       C  
ATOM   3466  CZ  TYR C  73      18.233  35.206 322.502  1.00 20.24           C  
ANISOU 3466  CZ  TYR C  73     1222   1217   5251   -257   -165   -126       C  
ATOM   3467  OH  TYR C  73      17.342  34.628 321.630  1.00 15.22           O  
ANISOU 3467  OH  TYR C  73      788    787   4210      6   -147   -133       O  
ATOM   3468  N   ARG C  74      23.538  36.263 323.360  1.00 15.44           N  
ANISOU 3468  N   ARG C  74      713    703   4452     -3   -197     51       N  
ATOM   3469  CA  ARG C  74      24.135  35.817 322.106  1.00 15.21           C  
ANISOU 3469  CA  ARG C  74      644    636   4501     -2   -184     52       C  
ATOM   3470  C   ARG C  74      25.056  34.592 322.327  1.00 19.44           C  
ANISOU 3470  C   ARG C  74     1036    990   5359   -109   -263     75       C  
ATOM   3471  O   ARG C  74      24.786  33.530 321.761  1.00 19.44           O  
ANISOU 3471  O   ARG C  74     1045    988   5355    -83   -282     54       O  
ATOM   3472  CB  ARG C  74      24.893  36.970 321.435  1.00 14.30           C  
ANISOU 3472  CB  ARG C  74      541    538   4352     -2   -128     71       C  
ATOM   3473  CG  ARG C  74      25.290  36.677 319.998  1.00 18.58           C  
ANISOU 3473  CG  ARG C  74      879    881   5300    -32    -98     79       C  
ATOM   3474  CD  ARG C  74      25.660  37.946 319.267  1.00 25.60           C  
ANISOU 3474  CD  ARG C  74     1654   1722   6350   -225    -16    108       C  
ATOM   3475  NE  ARG C  74      26.974  38.439 319.664  1.00 30.78           N  
ANISOU 3475  NE  ARG C  74     2238   2376   7079   -265     -7    167       N  
ATOM   3476  CZ  ARG C  74      27.507  39.574 319.234  1.00 46.45           C  
ANISOU 3476  CZ  ARG C  74     4192   4367   9088   -272     61    207       C  
ATOM   3477  NH1 ARG C  74      26.843  40.347 318.386  1.00 36.68           N  
ANISOU 3477  NH1 ARG C  74     3007   3134   7797   -227    128    195       N  
ATOM   3478  NH2 ARG C  74      28.709  39.946 319.649  1.00 36.05           N  
ANISOU 3478  NH2 ARG C  74     2795   3051   7852   -327     56    260       N  
ATOM   3479  N   SER C  75      26.080  34.717 323.195  1.00 17.82           N  
ANISOU 3479  N   SER C  75      830    799   5140    -60   -305    118       N  
ATOM   3480  CA  SER C  75      27.016  33.628 323.513  1.00 18.45           C  
ANISOU 3480  CA  SER C  75      886    833   5292    -88   -377    141       C  
ATOM   3481  C   SER C  75      26.319  32.333 323.981  1.00 19.34           C  
ANISOU 3481  C   SER C  75     1056    890   5403   -200   -442    116       C  
ATOM   3482  O   SER C  75      26.649  31.250 323.499  1.00 18.65           O  
ANISOU 3482  O   SER C  75      968    807   5311   -129   -476    113       O  
ATOM   3483  CB  SER C  75      27.975  34.074 324.607  1.00 23.54           C  
ANISOU 3483  CB  SER C  75     1443   1309   6194   -456   -448    165       C  
ATOM   3484  OG  SER C  75      27.269  34.323 325.812  1.00 41.57           O  
ANISOU 3484  OG  SER C  75     3805   3565   8425   -563   -486    154       O  
ATOM   3485  N   SER C  76      25.376  32.474 324.939  1.00 16.11           N  
ANISOU 3485  N   SER C  76      714    671   4734    -13   -437    122       N  
ATOM   3486  CA  SER C  76      24.607  31.414 325.584  1.00 15.65           C  
ANISOU 3486  CA  SER C  76      716    653   4579    -25   -478    118       C  
ATOM   3487  C   SER C  76      23.727  30.693 324.602  1.00 17.98           C  
ANISOU 3487  C   SER C  76     1038    770   5023   -243   -469     63       C  
ATOM   3488  O   SER C  76      23.803  29.467 324.533  1.00 17.33           O  
ANISOU 3488  O   SER C  76      995    690   4898   -213   -525     65       O  
ATOM   3489  CB  SER C  76      23.752  31.995 326.697  1.00 17.38           C  
ANISOU 3489  CB  SER C  76     1000    753   4849   -274   -467    104       C  
ATOM   3490  OG  SER C  76      24.546  32.710 327.627  1.00 23.38           O  
ANISOU 3490  OG  SER C  76     1766   1208   5911   -708   -520    104       O  
ATOM   3491  N   PHE C  77      22.901  31.454 323.831  1.00 15.97           N  
ANISOU 3491  N   PHE C  77      748    679   4639    -47   -390     45       N  
ATOM   3492  CA  PHE C  77      22.004  30.930 322.798  1.00 15.91           C  
ANISOU 3492  CA  PHE C  77      745    671   4628    -46   -381      4       C  
ATOM   3493  C   PHE C  77      22.797  30.058 321.820  1.00 18.18           C  
ANISOU 3493  C   PHE C  77     1044    757   5109   -202   -432    -21       C  
ATOM   3494  O   PHE C  77      22.364  28.942 321.561  1.00 18.13           O  
ANISOU 3494  O   PHE C  77     1097    710   5081   -226   -483    -43       O  
ATOM   3495  CB  PHE C  77      21.269  32.069 322.061  1.00 17.06           C  
ANISOU 3495  CB  PHE C  77      864    761   4857   -128   -318    -38       C  
ATOM   3496  CG  PHE C  77      20.254  31.657 321.011  1.00 18.94           C  
ANISOU 3496  CG  PHE C  77     1102    903   5192   -274   -335   -101       C  
ATOM   3497  CD1 PHE C  77      20.656  31.334 319.715  1.00 21.78           C  
ANISOU 3497  CD1 PHE C  77     1473   1111   5691   -365   -359   -140       C  
ATOM   3498  CD2 PHE C  77      18.893  31.667 321.293  1.00 21.19           C  
ANISOU 3498  CD2 PHE C  77     1373   1132   5546   -483   -342   -147       C  
ATOM   3499  CE1 PHE C  77      19.717  30.976 318.741  1.00 22.79           C  
ANISOU 3499  CE1 PHE C  77     1623   1244   5794   -340   -386   -194       C  
ATOM   3500  CE2 PHE C  77      17.956  31.291 320.321  1.00 23.72           C  
ANISOU 3500  CE2 PHE C  77     1679   1417   5918   -555   -377   -209       C  
ATOM   3501  CZ  PHE C  77      18.375  30.951 319.052  1.00 21.84           C  
ANISOU 3501  CZ  PHE C  77     1476   1153   5668   -439   -404   -229       C  
ATOM   3502  N   THR C  78      23.971  30.529 321.329  1.00 15.19           N  
ANISOU 3502  N   THR C  78      579    541   4652     -1   -397     12       N  
ATOM   3503  CA  THR C  78      24.797  29.760 320.394  1.00 15.39           C  
ANISOU 3503  CA  THR C  78      575    534   4738      0   -417      2       C  
ATOM   3504  C   THR C  78      25.261  28.416 321.014  1.00 21.03           C  
ANISOU 3504  C   THR C  78     1505    813   5674   -184   -517     -7       C  
ATOM   3505  O   THR C  78      25.040  27.377 320.384  1.00 21.77           O  
ANISOU 3505  O   THR C  78     1688    850   5734   -127   -557    -37       O  
ATOM   3506  CB  THR C  78      25.973  30.579 319.876  1.00 18.41           C  
ANISOU 3506  CB  THR C  78      987    614   5394    -94   -360     21       C  
ATOM   3507  OG1 THR C  78      25.476  31.759 319.256  1.00 17.21           O  
ANISOU 3507  OG1 THR C  78      736    643   5159    -29   -280     16       O  
ATOM   3508  CG2 THR C  78      26.817  29.809 318.868  1.00 17.48           C  
ANISOU 3508  CG2 THR C  78      871    505   5265     54   -348     21       C  
ATOM   3509  N   ARG C  79      25.860  28.420 322.235  1.00 19.61           N  
ANISOU 3509  N   ARG C  79     1247    791   5414   -150   -558     40       N  
ATOM   3510  CA  ARG C  79      26.305  27.170 322.870  1.00 20.54           C  
ANISOU 3510  CA  ARG C  79     1475    787   5543   -176   -655     49       C  
ATOM   3511  C   ARG C  79      25.104  26.242 323.197  1.00 24.82           C  
ANISOU 3511  C   ARG C  79     2212   1115   6102   -339   -702     18       C  
ATOM   3512  O   ARG C  79      25.280  25.027 323.189  1.00 24.69           O  
ANISOU 3512  O   ARG C  79     2314   1008   6060   -307   -776     14       O  
ATOM   3513  CB  ARG C  79      27.204  27.412 324.104  1.00 21.73           C  
ANISOU 3513  CB  ARG C  79     1624    873   5758   -224   -706     93       C  
ATOM   3514  CG  ARG C  79      26.510  27.671 325.446  1.00 35.92           C  
ANISOU 3514  CG  ARG C  79     3502   2578   7568   -417   -726    103       C  
ATOM   3515  CD  ARG C  79      27.515  27.810 326.580  1.00 50.24           C  
ANISOU 3515  CD  ARG C  79     5315   4370   9403   -424   -802    144       C  
ATOM   3516  NE  ARG C  79      28.325  29.028 326.465  1.00 63.95           N  
ANISOU 3516  NE  ARG C  79     6906   6183  11209   -396   -771    164       N  
ATOM   3517  CZ  ARG C  79      28.058  30.170 327.093  1.00 85.79           C  
ANISOU 3517  CZ  ARG C  79     9638   8984  13974   -490   -746    172       C  
ATOM   3518  NH1 ARG C  79      27.006  30.263 327.899  1.00 82.45           N  
ANISOU 3518  NH1 ARG C  79     9308   8540  13481   -603   -737    161       N  
ATOM   3519  NH2 ARG C  79      28.842  31.227 326.923  1.00 69.57           N  
ANISOU 3519  NH2 ARG C  79     7461   6985  11987   -471   -726    192       N  
ATOM   3520  N   ASP C  80      23.894  26.813 323.414  1.00 22.91           N  
ANISOU 3520  N   ASP C  80     1918   1001   5786   -401   -654      7       N  
ATOM   3521  CA  ASP C  80      22.657  26.066 323.672  1.00 23.99           C  
ANISOU 3521  CA  ASP C  80     2150   1080   5884   -523   -679    -15       C  
ATOM   3522  C   ASP C  80      22.191  25.322 322.406  1.00 25.52           C  
ANISOU 3522  C   ASP C  80     2422   1159   6115   -522   -708    -70       C  
ATOM   3523  O   ASP C  80      21.898  24.132 322.496  1.00 25.72           O  
ANISOU 3523  O   ASP C  80     2573   1088   6110   -561   -779    -79       O  
ATOM   3524  CB  ASP C  80      21.529  26.988 324.195  1.00 26.51           C  
ANISOU 3524  CB  ASP C  80     2429   1396   6248   -705   -615    -31       C  
ATOM   3525  CG  ASP C  80      21.564  27.277 325.693  1.00 49.80           C  
ANISOU 3525  CG  ASP C  80     5405   4341   9177   -809   -609      9       C  
ATOM   3526  OD1 ASP C  80      21.555  26.305 326.491  1.00 54.36           O  
ANISOU 3526  OD1 ASP C  80     6101   4833   9719   -875   -665     34       O  
ATOM   3527  OD2 ASP C  80      21.509  28.471 326.070  1.00 56.53           O  
ANISOU 3527  OD2 ASP C  80     6177   5266  10036   -828   -549     14       O  
ATOM   3528  N   VAL C  81      22.145  26.012 321.234  1.00 20.75           N  
ANISOU 3528  N   VAL C  81     1661    816   5405   -310   -650    -79       N  
ATOM   3529  CA  VAL C  81      21.752  25.441 319.934  1.00 20.36           C  
ANISOU 3529  CA  VAL C  81     1655    749   5333   -251   -678   -128       C  
ATOM   3530  C   VAL C  81      22.726  24.314 319.573  1.00 24.87           C  
ANISOU 3530  C   VAL C  81     2428   1019   6003   -229   -747   -149       C  
ATOM   3531  O   VAL C  81      22.307  23.258 319.091  1.00 26.04           O  
ANISOU 3531  O   VAL C  81     2703   1079   6114   -228   -819   -184       O  
ATOM   3532  CB  VAL C  81      21.689  26.508 318.808  1.00 22.30           C  
ANISOU 3532  CB  VAL C  81     1897    877   5700   -251   -612   -174       C  
ATOM   3533  CG1 VAL C  81      21.225  25.906 317.486  1.00 22.56           C  
ANISOU 3533  CG1 VAL C  81     2009    870   5691   -163   -652   -230       C  
ATOM   3534  CG2 VAL C  81      20.789  27.668 319.194  1.00 21.44           C  
ANISOU 3534  CG2 VAL C  81     1685    855   5605   -349   -558   -180       C  
ATOM   3535  N   LYS C  82      24.019  24.537 319.845  1.00 21.22           N  
ANISOU 3535  N   LYS C  82     1858    700   5504   -106   -723   -101       N  
ATOM   3536  CA  LYS C  82      25.068  23.563 319.598  1.00 21.64           C  
ANISOU 3536  CA  LYS C  82     2002    666   5556     12   -774    -99       C  
ATOM   3537  C   LYS C  82      24.884  22.323 320.510  1.00 27.25           C  
ANISOU 3537  C   LYS C  82     2921   1141   6292    -68   -881    -94       C  
ATOM   3538  O   LYS C  82      24.961  21.190 320.016  1.00 27.58           O  
ANISOU 3538  O   LYS C  82     3107   1080   6293      4   -949   -122       O  
ATOM   3539  CB  LYS C  82      26.448  24.209 319.779  1.00 22.15           C  
ANISOU 3539  CB  LYS C  82     2000    685   5731    118   -725    -56       C  
ATOM   3540  CG  LYS C  82      26.809  25.122 318.623  1.00 21.88           C  
ANISOU 3540  CG  LYS C  82     1854    745   5714    227   -619    -61       C  
ATOM   3541  CD  LYS C  82      28.211  25.679 318.750  1.00 29.46           C  
ANISOU 3541  CD  LYS C  82     2686   1768   6739    328   -570    -12       C  
ATOM   3542  CE  LYS C  82      28.637  26.499 317.554  1.00 35.71           C  
ANISOU 3542  CE  LYS C  82     3378   2648   7544    427   -448     -7       C  
ATOM   3543  NZ  LYS C  82      28.645  25.704 316.291  1.00 45.31           N  
ANISOU 3543  NZ  LYS C  82     4690   3828   8695    584   -428    -47       N  
ATOM   3544  N   GLU C  83      24.593  22.543 321.816  1.00 24.23           N  
ANISOU 3544  N   GLU C  83     2528    759   5918   -217   -893    -57       N  
ATOM   3545  CA  GLU C  83      24.361  21.467 322.788  1.00 25.31           C  
ANISOU 3545  CA  GLU C  83     2822    777   6017   -314   -981    -38       C  
ATOM   3546  C   GLU C  83      23.077  20.701 322.467  1.00 29.38           C  
ANISOU 3546  C   GLU C  83     3451   1220   6493   -432  -1016    -76       C  
ATOM   3547  O   GLU C  83      23.001  19.500 322.729  1.00 29.91           O  
ANISOU 3547  O   GLU C  83     3692   1155   6519   -456  -1103    -75       O  
ATOM   3548  CB  GLU C  83      24.308  22.009 324.228  1.00 26.64           C  
ANISOU 3548  CB  GLU C  83     2958    973   6191   -445   -969     10       C  
ATOM   3549  CG  GLU C  83      25.665  22.068 324.922  1.00 42.56           C  
ANISOU 3549  CG  GLU C  83     4961   2982   8229   -352  -1013     53       C  
ATOM   3550  CD  GLU C  83      26.375  20.747 325.188  1.00 78.09           C  
ANISOU 3550  CD  GLU C  83     9626   7350  12694   -268  -1125     66       C  
ATOM   3551  OE1 GLU C  83      25.692  19.739 325.488  1.00 73.41           O  
ANISOU 3551  OE1 GLU C  83     9208   6642  12044   -358  -1181     63       O  
ATOM   3552  OE2 GLU C  83      27.626  20.729 325.113  1.00 77.87           O  
ANISOU 3552  OE2 GLU C  83     9552   7335  12702   -113  -1159     80       O  
ATOM   3553  N   PHE C  84      22.079  21.395 321.897  1.00 24.87           N  
ANISOU 3553  N   PHE C  84     2754    794   5901   -478   -956   -102       N  
ATOM   3554  CA  PHE C  84      20.809  20.799 321.513  1.00 25.04           C  
ANISOU 3554  CA  PHE C  84     2829    801   5883   -578   -991   -136       C  
ATOM   3555  C   PHE C  84      20.976  20.016 320.255  1.00 28.16           C  
ANISOU 3555  C   PHE C  84     3372   1024   6303   -496  -1060   -200       C  
ATOM   3556  O   PHE C  84      20.301  19.013 320.106  1.00 29.08           O  
ANISOU 3556  O   PHE C  84     3624   1034   6392   -580  -1141   -226       O  
ATOM   3557  CB  PHE C  84      19.706  21.856 321.342  1.00 26.10           C  
ANISOU 3557  CB  PHE C  84     2843    984   6090   -708   -918   -168       C  
ATOM   3558  CG  PHE C  84      19.025  22.288 322.622  1.00 27.41           C  
ANISOU 3558  CG  PHE C  84     2960   1178   6277   -895   -867   -133       C  
ATOM   3559  CD1 PHE C  84      18.624  21.351 323.568  1.00 31.48           C  
ANISOU 3559  CD1 PHE C  84     3595   1600   6765  -1047   -907   -103       C  
ATOM   3560  CD2 PHE C  84      18.735  23.624 322.856  1.00 28.52           C  
ANISOU 3560  CD2 PHE C  84     2942   1450   6443   -909   -774   -128       C  
ATOM   3561  CE1 PHE C  84      17.993  21.753 324.746  1.00 32.32           C  
ANISOU 3561  CE1 PHE C  84     3658   1753   6868  -1202   -842    -66       C  
ATOM   3562  CE2 PHE C  84      18.099  24.023 324.035  1.00 31.25           C  
ANISOU 3562  CE2 PHE C  84     3249   1839   6786  -1056   -718    -98       C  
ATOM   3563  CZ  PHE C  84      17.732  23.085 324.970  1.00 30.13           C  
ANISOU 3563  CZ  PHE C  84     3221   1613   6614  -1199   -746    -66       C  
ATOM   3564  N   ALA C  85      21.879  20.442 319.356  1.00 24.47           N  
ANISOU 3564  N   ALA C  85     2853    609   5835   -297  -1025   -214       N  
ATOM   3565  CA  ALA C  85      22.153  19.714 318.112  1.00 25.63           C  
ANISOU 3565  CA  ALA C  85     3120    678   5942   -145  -1075   -266       C  
ATOM   3566  C   ALA C  85      22.735  18.327 318.405  1.00 31.93           C  
ANISOU 3566  C   ALA C  85     4117   1317   6698    -93  -1175   -260       C  
ATOM   3567  O   ALA C  85      22.318  17.359 317.772  1.00 32.80           O  
ANISOU 3567  O   ALA C  85     4390   1312   6759    -77  -1261   -308       O  
ATOM   3568  CB  ALA C  85      23.108  20.501 317.234  1.00 25.97           C  
ANISOU 3568  CB  ALA C  85     3063    812   5991     56   -990   -268       C  
ATOM   3569  N   LYS C  86      23.662  18.234 319.385  1.00 28.88           N  
ANISOU 3569  N   LYS C  86     3729    917   6329    -68  -1176   -205       N  
ATOM   3570  CA  LYS C  86      24.319  16.996 319.811  1.00 30.52           C  
ANISOU 3570  CA  LYS C  86     4124    977   6497     -3  -1274   -191       C  
ATOM   3571  C   LYS C  86      23.347  16.074 320.559  1.00 37.16           C  
ANISOU 3571  C   LYS C  86     5127   1686   7305   -212  -1359   -182       C  
ATOM   3572  O   LYS C  86      23.284  14.875 320.259  1.00 38.50           O  
ANISOU 3572  O   LYS C  86     5509   1698   7421   -187  -1460   -206       O  
ATOM   3573  CB  LYS C  86      25.531  17.301 320.718  1.00 33.30           C  
ANISOU 3573  CB  LYS C  86     4400   1370   6883     82  -1257   -133       C  
ATOM   3574  CG  LYS C  86      26.672  18.064 320.057  1.00 53.22           C  
ANISOU 3574  CG  LYS C  86     6760   4013   9448    284  -1175   -131       C  
ATOM   3575  CD  LYS C  86      27.638  18.643 321.099  1.00 63.22           C  
ANISOU 3575  CD  LYS C  86     7903   5347  10771    305  -1161    -72       C  
ATOM   3576  CE  LYS C  86      28.627  19.617 320.494  1.00 70.36           C  
ANISOU 3576  CE  LYS C  86     8607   6391  11737    455  -1063    -62       C  
ATOM   3577  NZ  LYS C  86      29.556  20.175 321.514  1.00 73.85           N  
ANISOU 3577  NZ  LYS C  86     8921   6896  12244    460  -1069     -7       N  
ATOM   3578  N   MET C  87      22.619  16.641 321.549  1.00 33.64           N  
ANISOU 3578  N   MET C  87     4590   1304   6888   -415  -1313   -145       N  
ATOM   3579  CA  MET C  87      21.651  15.978 322.432  1.00 34.40           C  
ANISOU 3579  CA  MET C  87     4801   1310   6962   -645  -1354   -120       C  
ATOM   3580  C   MET C  87      20.445  15.441 321.658  1.00 39.05           C  
ANISOU 3580  C   MET C  87     5458   1840   7540   -760  -1401   -173       C  
ATOM   3581  O   MET C  87      20.084  14.283 321.845  1.00 40.32           O  
ANISOU 3581  O   MET C  87     5820   1839   7660   -846  -1495   -173       O  
ATOM   3582  CB  MET C  87      21.193  16.988 323.503  1.00 36.12           C  
ANISOU 3582  CB  MET C  87     4861   1650   7212   -799  -1259    -74       C  
ATOM   3583  CG  MET C  87      20.318  16.433 324.626  1.00 40.86           C  
ANISOU 3583  CG  MET C  87     5567   2174   7783  -1028  -1270    -29       C  
ATOM   3584  SD  MET C  87      19.319  17.734 325.453  1.00 44.15           S  
ANISOU 3584  SD  MET C  87     5777   2761   8235  -1209  -1133     -2       S  
ATOM   3585  CE  MET C  87      20.624  18.838 326.098  1.00 39.96           C  
ANISOU 3585  CE  MET C  87     5159   2314   7712  -1069  -1092     40       C  
ATOM   3586  N   LEU C  88      19.824  16.271 320.803  1.00 35.64           N  
ANISOU 3586  N   LEU C  88     4866   1531   7144   -763  -1347   -219       N  
ATOM   3587  CA  LEU C  88      18.621  15.901 320.046  1.00 36.95           C  
ANISOU 3587  CA  LEU C  88     5063   1665   7313   -875  -1401   -275       C  
ATOM   3588  C   LEU C  88      18.946  15.184 318.714  1.00 42.88           C  
ANISOU 3588  C   LEU C  88     5962   2313   8016   -707  -1495   -342       C  
ATOM   3589  O   LEU C  88      18.023  14.692 318.050  1.00 43.40           O  
ANISOU 3589  O   LEU C  88     6100   2316   8074   -795  -1575   -394       O  
ATOM   3590  CB  LEU C  88      17.731  17.143 319.782  1.00 36.03           C  
ANISOU 3590  CB  LEU C  88     4712   1727   7251   -942  -1314   -297       C  
ATOM   3591  CG  LEU C  88      17.217  17.909 321.019  1.00 40.00           C  
ANISOU 3591  CG  LEU C  88     5061   2343   7794  -1098  -1211   -243       C  
ATOM   3592  CD1 LEU C  88      17.005  19.379 320.721  1.00 38.51           C  
ANISOU 3592  CD1 LEU C  88     4651   2334   7645  -1039  -1113   -260       C  
ATOM   3593  CD2 LEU C  88      15.939  17.344 321.508  1.00 43.21           C  
ANISOU 3593  CD2 LEU C  88     5485   2716   8218  -1348  -1230   -234       C  
ATOM   3594  N   ARG C  89      20.247  15.107 318.344  1.00 39.90           N  
ANISOU 3594  N   ARG C  89     5632   1921   7608   -466  -1485   -341       N  
ATOM   3595  CA  ARG C  89      20.767  14.485 317.112  1.00 41.06           C  
ANISOU 3595  CA  ARG C  89     5925   1979   7695   -258  -1549   -400       C  
ATOM   3596  C   ARG C  89      20.140  15.142 315.848  1.00 44.18           C  
ANISOU 3596  C   ARG C  89     6234   2464   8089   -210  -1529   -466       C  
ATOM   3597  O   ARG C  89      19.455  14.478 315.057  1.00 44.35           O  
ANISOU 3597  O   ARG C  89     6392   2388   8070   -231  -1630   -529       O  
ATOM   3598  CB  ARG C  89      20.582  12.954 317.108  1.00 45.42           C  
ANISOU 3598  CB  ARG C  89     6761   2310   8187   -300  -1695   -422       C  
ATOM   3599  CG  ARG C  89      21.380  12.219 318.187  1.00 64.76           C  
ANISOU 3599  CG  ARG C  89     9340   4650  10616   -290  -1728   -362       C  
ATOM   3600  CD  ARG C  89      20.685  10.940 318.631  1.00 85.12           C  
ANISOU 3600  CD  ARG C  89    12160   7025  13155   -470  -1854   -359       C  
ATOM   3601  NE  ARG C  89      19.530  11.223 319.490  1.00100.42           N  
ANISOU 3601  NE  ARG C  89    14004   9008  15144   -770  -1823   -320       N  
ATOM   3602  CZ  ARG C  89      18.604  10.332 319.834  1.00116.36           C  
ANISOU 3602  CZ  ARG C  89    16176  10885  17150   -994  -1906   -313       C  
ATOM   3603  NH1 ARG C  89      18.680   9.079 319.396  1.00101.49           N  
ANISOU 3603  NH1 ARG C  89    14573   8788  15201   -959  -2043   -344       N  
ATOM   3604  NH2 ARG C  89      17.593  10.687 320.617  1.00104.93           N  
ANISOU 3604  NH2 ARG C  89    14608   9506  15754  -1255  -1850   -273       N  
ATOM   3605  N   LEU C  90      20.391  16.469 315.689  1.00 38.74           N  
ANISOU 3605  N   LEU C  90     5327   1952   7440   -148  -1405   -449       N  
ATOM   3606  CA  LEU C  90      19.952  17.309 314.567  1.00 37.06           C  
ANISOU 3606  CA  LEU C  90     5020   1840   7222    -81  -1367   -499       C  
ATOM   3607  C   LEU C  90      21.124  17.636 313.634  1.00 39.15           C  
ANISOU 3607  C   LEU C  90     5292   2140   7442    190  -1299   -508       C  
ATOM   3608  O   LEU C  90      22.215  17.988 314.098  1.00 37.49           O  
ANISOU 3608  O   LEU C  90     5005   1982   7256    289  -1215   -456       O  
ATOM   3609  CB  LEU C  90      19.314  18.597 315.078  1.00 35.62           C  
ANISOU 3609  CB  LEU C  90     4604   1821   7108   -209  -1274   -471       C  
ATOM   3610  CG  LEU C  90      17.904  18.463 315.580  1.00 40.53           C  
ANISOU 3610  CG  LEU C  90     5184   2445   7770   -455  -1325   -482       C  
ATOM   3611  CD1 LEU C  90      17.596  19.554 316.564  1.00 39.58           C  
ANISOU 3611  CD1 LEU C  90     4862   2462   7713   -572  -1218   -431       C  
ATOM   3612  CD2 LEU C  90      16.907  18.474 314.425  1.00 43.85           C  
ANISOU 3612  CD2 LEU C  90     5610   2876   8177   -465  -1397   -559       C  
ATOM   3613  N   SER C  91      20.897  17.500 312.323  1.00 36.24           N  
ANISOU 3613  N   SER C  91     5019   1743   7009    306  -1336   -575       N  
ATOM   3614  CA  SER C  91      21.929  17.711 311.313  1.00 36.47           C  
ANISOU 3614  CA  SER C  91     5082   1797   6976    568  -1263   -589       C  
ATOM   3615  C   SER C  91      21.952  19.151 310.809  1.00 39.09           C  
ANISOU 3615  C   SER C  91     5228   2295   7328    618  -1134   -573       C  
ATOM   3616  O   SER C  91      20.903  19.789 310.645  1.00 38.32           O  
ANISOU 3616  O   SER C  91     5052   2257   7250    499  -1150   -595       O  
ATOM   3617  CB  SER C  91      21.771  16.735 310.145  1.00 41.72           C  
ANISOU 3617  CB  SER C  91     5988   2328   7537    688  -1370   -670       C  
ATOM   3618  OG  SER C  91      20.484  16.764 309.547  1.00 50.52           O  
ANISOU 3618  OG  SER C  91     7133   3427   8636    567  -1465   -731       O  
ATOM   3619  N   TYR C  92      23.174  19.654 310.568  1.00 34.52           N  
ANISOU 3619  N   TYR C  92     4581   1788   6747    797  -1007   -533       N  
ATOM   3620  CA  TYR C  92      23.421  21.002 310.075  1.00 32.85           C  
ANISOU 3620  CA  TYR C  92     4215   1720   6549    862   -869   -506       C  
ATOM   3621  C   TYR C  92      23.154  21.067 308.560  1.00 36.88           C  
ANISOU 3621  C   TYR C  92     4843   2215   6953   1012   -868   -566       C  
ATOM   3622  O   TYR C  92      23.117  20.004 307.932  1.00 37.50           O  
ANISOU 3622  O   TYR C  92     5125   2174   6950   1106   -958   -623       O  
ATOM   3623  CB  TYR C  92      24.851  21.444 310.424  1.00 33.31           C  
ANISOU 3623  CB  TYR C  92     4151   1853   6651    978   -737   -435       C  
ATOM   3624  CG  TYR C  92      25.062  21.671 311.905  1.00 33.42           C  
ANISOU 3624  CG  TYR C  92     4031   1901   6766    829   -736   -374       C  
ATOM   3625  CD1 TYR C  92      24.689  22.869 312.507  1.00 33.58           C  
ANISOU 3625  CD1 TYR C  92     3875   2031   6854    695   -672   -334       C  
ATOM   3626  CD2 TYR C  92      25.641  20.692 312.705  1.00 35.00           C  
ANISOU 3626  CD2 TYR C  92     4300   2016   6982    833   -805   -358       C  
ATOM   3627  CE1 TYR C  92      24.876  23.082 313.872  1.00 33.20           C  
ANISOU 3627  CE1 TYR C  92     3725   2007   6883    565   -676   -282       C  
ATOM   3628  CE2 TYR C  92      25.856  20.902 314.067  1.00 35.40           C  
ANISOU 3628  CE2 TYR C  92     4248   2093   7111    705   -812   -302       C  
ATOM   3629  CZ  TYR C  92      25.464  22.097 314.648  1.00 41.17           C  
ANISOU 3629  CZ  TYR C  92     4806   2932   7904    569   -747   -265       C  
ATOM   3630  OH  TYR C  92      25.653  22.293 315.993  1.00 41.57           O  
ANISOU 3630  OH  TYR C  92     4778   3000   8016    448   -760   -215       O  
ATOM   3631  N   PRO C  93      22.919  22.265 307.947  1.00 32.70           N  
ANISOU 3631  N   PRO C  93     4220   1792   6413   1040   -778   -558       N  
ATOM   3632  CA  PRO C  93      22.930  23.615 308.538  1.00 30.74           C  
ANISOU 3632  CA  PRO C  93     3759   1676   6245    947   -672   -497       C  
ATOM   3633  C   PRO C  93      21.648  23.932 309.283  1.00 33.54           C  
ANISOU 3633  C   PRO C  93     4031   2053   6659    728   -753   -512       C  
ATOM   3634  O   PRO C  93      20.606  23.365 308.973  1.00 34.36           O  
ANISOU 3634  O   PRO C  93     4228   2096   6733    663   -879   -576       O  
ATOM   3635  CB  PRO C  93      23.118  24.541 307.324  1.00 32.61           C  
ANISOU 3635  CB  PRO C  93     4003   1977   6411   1094   -567   -497       C  
ATOM   3636  CG  PRO C  93      23.201  23.660 306.105  1.00 38.60           C  
ANISOU 3636  CG  PRO C  93     4979   2642   7045   1275   -611   -558       C  
ATOM   3637  CD  PRO C  93      22.630  22.338 306.505  1.00 34.97           C  
ANISOU 3637  CD  PRO C  93     4645   2058   6584   1188   -784   -614       C  
ATOM   3638  N   LEU C  94      21.733  24.815 310.280  1.00 28.62           N  
ANISOU 3638  N   LEU C  94     3234   1517   6122    614   -683   -454       N  
ATOM   3639  CA  LEU C  94      20.568  25.207 311.063  1.00 27.91           C  
ANISOU 3639  CA  LEU C  94     3049   1465   6089    419   -732   -462       C  
ATOM   3640  C   LEU C  94      20.325  26.702 310.938  1.00 31.84           C  
ANISOU 3640  C   LEU C  94     3414   2077   6606    414   -639   -439       C  
ATOM   3641  O   LEU C  94      21.267  27.500 310.978  1.00 31.65           O  
ANISOU 3641  O   LEU C  94     3316   2110   6600    480   -522   -383       O  
ATOM   3642  CB  LEU C  94      20.699  24.790 312.541  1.00 27.51           C  
ANISOU 3642  CB  LEU C  94     2946   1396   6112    271   -751   -420       C  
ATOM   3643  CG  LEU C  94      20.883  23.281 312.805  1.00 33.29           C  
ANISOU 3643  CG  LEU C  94     3825   1999   6825    259   -851   -434       C  
ATOM   3644  CD1 LEU C  94      21.181  22.996 314.268  1.00 32.90           C  
ANISOU 3644  CD1 LEU C  94     3730   1936   6836    135   -852   -380       C  
ATOM   3645  CD2 LEU C  94      19.675  22.483 312.363  1.00 37.18           C  
ANISOU 3645  CD2 LEU C  94     4430   2410   7285    175   -984   -504       C  
ATOM   3646  N   GLU C  95      19.052  27.068 310.739  1.00 27.57           N  
ANISOU 3646  N   GLU C  95     2844   1568   6063    338   -699   -485       N  
ATOM   3647  CA  GLU C  95      18.582  28.443 310.610  1.00 25.93           C  
ANISOU 3647  CA  GLU C  95     2529   1457   5865    335   -635   -475       C  
ATOM   3648  C   GLU C  95      17.589  28.724 311.734  1.00 26.11           C  
ANISOU 3648  C   GLU C  95     2429   1530   5960    153   -662   -476       C  
ATOM   3649  O   GLU C  95      16.530  28.080 311.801  1.00 25.81           O  
ANISOU 3649  O   GLU C  95     2400   1473   5935     57   -767   -526       O  
ATOM   3650  CB  GLU C  95      17.954  28.669 309.221  1.00 28.31           C  
ANISOU 3650  CB  GLU C  95     2912   1758   6086    446   -683   -535       C  
ATOM   3651  CG  GLU C  95      18.977  28.915 308.123  1.00 43.88           C  
ANISOU 3651  CG  GLU C  95     4984   3714   7975    640   -599   -516       C  
ATOM   3652  CD  GLU C  95      19.349  30.373 307.925  1.00 66.31           C  
ANISOU 3652  CD  GLU C  95     7753   6631  10809    698   -469   -465       C  
ATOM   3653  OE1 GLU C  95      20.536  30.722 308.128  1.00 57.01           O  
ANISOU 3653  OE1 GLU C  95     6544   5469   9647    749   -346   -397       O  
ATOM   3654  OE2 GLU C  95      18.448  31.169 307.574  1.00 58.60           O  
ANISOU 3654  OE2 GLU C  95     6751   5698   9817    691   -495   -491       O  
ATOM   3655  N   LEU C  96      17.982  29.609 312.677  1.00 19.75           N  
ANISOU 3655  N   LEU C  96     1509    795   5200    100   -568   -417       N  
ATOM   3656  CA  LEU C  96      17.153  29.972 313.830  1.00 19.23           C  
ANISOU 3656  CA  LEU C  96     1254    946   5105     -2   -563   -381       C  
ATOM   3657  C   LEU C  96      16.894  31.461 313.835  1.00 19.22           C  
ANISOU 3657  C   LEU C  96     1238    878   5188    -20   -493   -397       C  
ATOM   3658  O   LEU C  96      17.808  32.253 313.625  1.00 19.16           O  
ANISOU 3658  O   LEU C  96     1193    952   5134     48   -410   -347       O  
ATOM   3659  CB  LEU C  96      17.764  29.501 315.173  1.00 19.45           C  
ANISOU 3659  CB  LEU C  96     1274    950   5165    -64   -537   -327       C  
ATOM   3660  CG  LEU C  96      17.423  28.065 315.551  1.00 25.25           C  
ANISOU 3660  CG  LEU C  96     2160   1424   6009   -256   -642   -380       C  
ATOM   3661  CD1 LEU C  96      18.026  27.081 314.570  1.00 27.03           C  
ANISOU 3661  CD1 LEU C  96     2523   1560   6188   -140   -700   -403       C  
ATOM   3662  CD2 LEU C  96      17.832  27.760 316.974  1.00 27.88           C  
ANISOU 3662  CD2 LEU C  96     2482   1736   6377   -368   -622   -327       C  
ATOM   3663  N   GLN C  97      15.626  31.835 313.984  1.00 15.98           N  
ANISOU 3663  N   GLN C  97      790    767   4515     46   -474   -370       N  
ATOM   3664  CA  GLN C  97      15.207  33.230 314.020  1.00 14.75           C  
ANISOU 3664  CA  GLN C  97      635    627   4342     42   -415   -378       C  
ATOM   3665  C   GLN C  97      14.360  33.464 315.239  1.00 17.63           C  
ANISOU 3665  C   GLN C  97      921    920   4860     39   -399   -392       C  
ATOM   3666  O   GLN C  97      13.490  32.651 315.558  1.00 18.11           O  
ANISOU 3666  O   GLN C  97      934    955   4994    -48   -461   -425       O  
ATOM   3667  CB  GLN C  97      14.434  33.641 312.761  1.00 16.68           C  
ANISOU 3667  CB  GLN C  97      921    913   4503     55   -466   -431       C  
ATOM   3668  CG  GLN C  97      15.164  33.464 311.445  1.00 16.29           C  
ANISOU 3668  CG  GLN C  97      844    682   4664    138   -537   -491       C  
ATOM   3669  CD  GLN C  97      14.199  32.961 310.407  1.00 29.05           C  
ANISOU 3669  CD  GLN C  97     2546   2194   6298    254   -655   -578       C  
ATOM   3670  OE1 GLN C  97      13.808  31.779 310.393  1.00 27.84           O  
ANISOU 3670  OE1 GLN C  97     2427   1996   6155    196   -753   -617       O  
ATOM   3671  NE2 GLN C  97      13.773  33.854 309.536  1.00 14.19           N  
ANISOU 3671  NE2 GLN C  97      640    530   4221    173   -672   -585       N  
ATOM   3672  N   VAL C  98      14.610  34.562 315.927  1.00 14.32           N  
ANISOU 3672  N   VAL C  98      583    591   4267     28   -299   -343       N  
ATOM   3673  CA  VAL C  98      13.889  34.906 317.143  1.00 14.61           C  
ANISOU 3673  CA  VAL C  98      630    643   4279     23   -253   -336       C  
ATOM   3674  C   VAL C  98      13.252  36.257 316.924  1.00 18.50           C  
ANISOU 3674  C   VAL C  98      907   1062   5061    -57   -266   -413       C  
ATOM   3675  O   VAL C  98      13.966  37.216 316.640  1.00 18.39           O  
ANISOU 3675  O   VAL C  98      952   1013   5023      4   -221   -389       O  
ATOM   3676  CB  VAL C  98      14.840  34.892 318.375  1.00 16.24           C  
ANISOU 3676  CB  VAL C  98      782    792   4596     16   -215   -292       C  
ATOM   3677  CG1 VAL C  98      14.112  35.291 319.657  1.00 15.76           C  
ANISOU 3677  CG1 VAL C  98      709    726   4554     11   -168   -297       C  
ATOM   3678  CG2 VAL C  98      15.547  33.547 318.529  1.00 15.93           C  
ANISOU 3678  CG2 VAL C  98      753    753   4545     17   -254   -257       C  
ATOM   3679  N   SER C  99      11.923  36.337 317.047  1.00 17.69           N  
ANISOU 3679  N   SER C  99      792    994   4937    -55   -280   -461       N  
ATOM   3680  CA  SER C  99      11.167  37.577 316.877  1.00 18.42           C  
ANISOU 3680  CA  SER C  99      801   1147   5052    -55   -272   -504       C  
ATOM   3681  C   SER C  99      10.481  37.953 318.188  1.00 22.99           C  
ANISOU 3681  C   SER C  99     1040   1906   5790   -239   -243   -513       C  
ATOM   3682  O   SER C  99       9.397  37.448 318.485  1.00 24.87           O  
ANISOU 3682  O   SER C  99     1172   2211   6067   -316   -263   -548       O  
ATOM   3683  CB  SER C  99      10.150  37.433 315.747  1.00 22.56           C  
ANISOU 3683  CB  SER C  99     1036   1825   5709    -84   -404   -582       C  
ATOM   3684  OG  SER C  99       9.178  38.466 315.789  1.00 34.22           O  
ANISOU 3684  OG  SER C  99     2436   3384   7181     -4   -393   -619       O  
ATOM   3685  N   ALA C 100      11.118  38.815 318.979  1.00 19.23           N  
ANISOU 3685  N   ALA C 100      794   1329   5183   -143   -144   -468       N  
ATOM   3686  CA  ALA C 100      10.558  39.236 320.255  1.00 19.69           C  
ANISOU 3686  CA  ALA C 100      798   1442   5240   -198    -76   -467       C  
ATOM   3687  C   ALA C 100      10.297  40.726 320.262  1.00 26.23           C  
ANISOU 3687  C   ALA C 100     1448   2380   6139   -172    -47   -489       C  
ATOM   3688  O   ALA C 100      10.882  41.453 319.459  1.00 26.58           O  
ANISOU 3688  O   ALA C 100     1571   2377   6153    -66    -61   -480       O  
ATOM   3689  CB  ALA C 100      11.502  38.867 321.377  1.00 19.75           C  
ANISOU 3689  CB  ALA C 100      869   1404   5232   -265    -35   -406       C  
ATOM   3690  N   GLY C 101       9.425  41.176 321.159  1.00 24.60           N  
ANISOU 3690  N   GLY C 101     1172   2246   5927   -185     12   -510       N  
ATOM   3691  CA  GLY C 101       9.094  42.590 321.275  1.00 25.37           C  
ANISOU 3691  CA  GLY C 101     1291   2368   5982    -64     55   -532       C  
ATOM   3692  C   GLY C 101       7.780  42.885 321.956  1.00 32.45           C  
ANISOU 3692  C   GLY C 101     2065   3380   6883    -47    107   -579       C  
ATOM   3693  O   GLY C 101       7.218  42.023 322.631  1.00 32.49           O  
ANISOU 3693  O   GLY C 101     1972   3448   6926   -162    134   -582       O  
ATOM   3694  N   CYS C 102       7.294  44.121 321.793  1.00 32.20           N  
ANISOU 3694  N   CYS C 102     2045   3378   6813     99    127   -614       N  
ATOM   3695  CA  CYS C 102       6.044  44.598 322.378  1.00 34.74           C  
ANISOU 3695  CA  CYS C 102     2250   3818   7133    159    185   -664       C  
ATOM   3696  C   CYS C 102       5.560  45.852 321.677  1.00 39.16           C  
ANISOU 3696  C   CYS C 102     2829   4395   7655    361    158   -711       C  
ATOM   3697  O   CYS C 102       6.304  46.483 320.926  1.00 36.97           O  
ANISOU 3697  O   CYS C 102     2688   4019   7338    440    111   -694       O  
ATOM   3698  CB  CYS C 102       6.190  44.840 323.883  1.00 36.14           C  
ANISOU 3698  CB  CYS C 102     2473   3991   7267     93    295   -640       C  
ATOM   3699  SG  CYS C 102       7.176  46.295 324.320  1.00 40.07           S  
ANISOU 3699  SG  CYS C 102     3194   4360   7672    178    321   -615       S  
ATOM   3700  N   GLU C 103       4.308  46.223 321.976  1.00 38.62           N  
ANISOU 3700  N   GLU C 103     2625   4452   7596    446    194   -768       N  
ATOM   3701  CA  GLU C 103       3.636  47.429 321.513  1.00 39.87           C  
ANISOU 3701  CA  GLU C 103     2787   4646   7718    657    173   -822       C  
ATOM   3702  C   GLU C 103       2.931  48.071 322.689  1.00 45.26           C  
ANISOU 3702  C   GLU C 103     3421   5408   8367    718    286   -852       C  
ATOM   3703  O   GLU C 103       2.250  47.379 323.444  1.00 44.75           O  
ANISOU 3703  O   GLU C 103     3197   5457   8347    627    357   -860       O  
ATOM   3704  CB  GLU C 103       2.663  47.159 320.347  1.00 42.35           C  
ANISOU 3704  CB  GLU C 103     2951   5053   8089    743     66   -879       C  
ATOM   3705  CG  GLU C 103       1.669  46.028 320.536  1.00 54.80           C  
ANISOU 3705  CG  GLU C 103     4286   6770   9764    627     62   -905       C  
ATOM   3706  CD  GLU C 103       0.836  45.763 319.299  1.00 81.20           C  
ANISOU 3706  CD  GLU C 103     7496  10191  13165    710    -72   -965       C  
ATOM   3707  OE1 GLU C 103       1.246  44.909 318.479  1.00 79.82           O  
ANISOU 3707  OE1 GLU C 103     7346   9964  13019    630   -171   -952       O  
ATOM   3708  OE2 GLU C 103      -0.213  46.429 319.136  1.00 72.64           O  
ANISOU 3708  OE2 GLU C 103     6292   9216  12091    867    -87  -1026       O  
ATOM   3709  N   VAL C 104       3.141  49.378 322.871  1.00 43.84           N  
ANISOU 3709  N   VAL C 104     3396   5159   8101    867    308   -863       N  
ATOM   3710  CA  VAL C 104       2.524  50.150 323.946  1.00 45.69           C  
ANISOU 3710  CA  VAL C 104     3625   5452   8281    960    415   -897       C  
ATOM   3711  C   VAL C 104       1.265  50.776 323.384  1.00 53.28           C  
ANISOU 3711  C   VAL C 104     4449   6538   9259   1170    386   -974       C  
ATOM   3712  O   VAL C 104       1.313  51.526 322.405  1.00 52.32           O  
ANISOU 3712  O   VAL C 104     4411   6360   9109   1321    293   -996       O  
ATOM   3713  CB  VAL C 104       3.488  51.184 324.590  1.00 49.10           C  
ANISOU 3713  CB  VAL C 104     4320   5729   8607    999    449   -869       C  
ATOM   3714  CG1 VAL C 104       2.763  52.104 325.573  1.00 50.27           C  
ANISOU 3714  CG1 VAL C 104     4486   5930   8682   1130    551   -916       C  
ATOM   3715  CG2 VAL C 104       4.631  50.474 325.292  1.00 47.60           C  
ANISOU 3715  CG2 VAL C 104     4234   5437   8415    789    468   -797       C  
ATOM   3716  N   HIS C 105       0.136  50.424 323.997  1.00 53.99           N  
ANISOU 3716  N   HIS C 105     4320   6799   9394   1174    468  -1013       N  
ATOM   3717  CA  HIS C 105      -1.193  50.884 323.623  1.00 56.88           C  
ANISOU 3717  CA  HIS C 105     4501   7319   9794   1367    452  -1091       C  
ATOM   3718  C   HIS C 105      -1.543  52.217 324.300  1.00 64.06           C  
ANISOU 3718  C   HIS C 105     5511   8226  10603   1577    536  -1131       C  
ATOM   3719  O   HIS C 105      -1.149  52.437 325.450  1.00 62.90           O  
ANISOU 3719  O   HIS C 105     5477   8036  10387   1524    654  -1107       O  
ATOM   3720  CB  HIS C 105      -2.240  49.820 324.008  1.00 59.00           C  
ANISOU 3720  CB  HIS C 105     4459   7785  10173   1255    510  -1109       C  
ATOM   3721  CG  HIS C 105      -2.170  48.564 323.200  1.00 61.80           C  
ANISOU 3721  CG  HIS C 105     4699   8151  10630   1082    404  -1087       C  
ATOM   3722  ND1 HIS C 105      -3.027  48.343 322.137  1.00 64.77           N  
ANISOU 3722  ND1 HIS C 105     4890   8628  11091   1154    279  -1141       N  
ATOM   3723  CD2 HIS C 105      -1.363  47.488 323.342  1.00 62.17           C  
ANISOU 3723  CD2 HIS C 105     4806   8115  10700    853    398  -1023       C  
ATOM   3724  CE1 HIS C 105      -2.711  47.148 321.663  1.00 63.38           C  
ANISOU 3724  CE1 HIS C 105     4678   8421  10983    963    203  -1109       C  
ATOM   3725  NE2 HIS C 105      -1.711  46.599 322.351  1.00 62.16           N  
ANISOU 3725  NE2 HIS C 105     4668   8156  10794    783    274  -1037       N  
ATOM   3726  N   PRO C 106      -2.312  53.107 323.630  1.00 64.65           N  
ANISOU 3726  N   PRO C 106     5558   8344  10660   1826    472  -1197       N  
ATOM   3727  CA  PRO C 106      -2.742  54.338 324.310  1.00 66.62           C  
ANISOU 3727  CA  PRO C 106     5906   8594  10810   2043    554  -1243       C  
ATOM   3728  C   PRO C 106      -3.937  54.040 325.238  1.00 73.67           C  
ANISOU 3728  C   PRO C 106     6536   9707  11747   2078    698  -1287       C  
ATOM   3729  O   PRO C 106      -4.933  53.475 324.778  1.00 74.32           O  
ANISOU 3729  O   PRO C 106     6329   9969  11942   2101    667  -1326       O  
ATOM   3730  CB  PRO C 106      -3.103  55.286 323.158  1.00 69.15           C  
ANISOU 3730  CB  PRO C 106     6297   8876  11100   2294    420  -1293       C  
ATOM   3731  CG  PRO C 106      -3.359  54.406 321.973  1.00 73.22           C  
ANISOU 3731  CG  PRO C 106     6647   9451  11723   2230    282  -1294       C  
ATOM   3732  CD  PRO C 106      -2.886  53.009 322.269  1.00 67.32           C  
ANISOU 3732  CD  PRO C 106     5782   8736  11062   1935    318  -1238       C  
ATOM   3733  N   GLY C 107      -3.836  54.361 326.534  1.00 71.60           N  
ANISOU 3733  N   GLY C 107     6369   9435  11402   2069    854  -1278       N  
ATOM   3734  CA  GLY C 107      -2.690  55.006 327.175  1.00 70.30           C  
ANISOU 3734  CA  GLY C 107     6541   9060  11109   2031    879  -1236       C  
ATOM   3735  C   GLY C 107      -2.344  54.417 328.529  1.00 73.59           C  
ANISOU 3735  C   GLY C 107     6989   9482  11490   1848   1028  -1191       C  
ATOM   3736  O   GLY C 107      -2.063  55.160 329.474  1.00 73.37           O  
ANISOU 3736  O   GLY C 107     7161   9378  11340   1920   1112  -1199       O  
ATOM   3737  N   ASN C 108      -2.369  53.070 328.629  1.00 69.39           N  
ANISOU 3737  N   ASN C 108     6278   9030  11056   1611   1053  -1145       N  
ATOM   3738  CA  ASN C 108      -2.051  52.324 329.850  1.00 68.63           C  
ANISOU 3738  CA  ASN C 108     6207   8939  10931   1415   1184  -1093       C  
ATOM   3739  C   ASN C 108      -1.485  50.933 329.514  1.00 69.45           C  
ANISOU 3739  C   ASN C 108     6227   9027  11134   1142   1128  -1026       C  
ATOM   3740  O   ASN C 108      -0.354  50.618 329.902  1.00 67.90           O  
ANISOU 3740  O   ASN C 108     6217   8688  10895    983   1115   -965       O  
ATOM   3741  CB  ASN C 108      -3.289  52.199 330.749  1.00 71.85           C  
ANISOU 3741  CB  ASN C 108     6412   9551  11338   1479   1369  -1129       C  
ATOM   3742  N   ALA C 109      -2.270  50.122 328.771  1.00 64.47           N  
ANISOU 3742  N   ALA C 109     5322   8537  10636   1094   1084  -1041       N  
ATOM   3743  CA  ALA C 109      -1.954  48.746 328.371  1.00 62.10           C  
ANISOU 3743  CA  ALA C 109     4922   8236  10437    851   1025   -989       C  
ATOM   3744  C   ALA C 109      -0.774  48.645 327.394  1.00 60.24           C  
ANISOU 3744  C   ALA C 109     4854   7826  10209    798    858   -956       C  
ATOM   3745  O   ALA C 109      -0.365  49.641 326.791  1.00 59.12           O  
ANISOU 3745  O   ALA C 109     4856   7591  10018    957    774   -979       O  
ATOM   3746  CB  ALA C 109      -3.186  48.102 327.746  1.00 64.48           C  
ANISOU 3746  CB  ALA C 109     4891   8733  10875    838   1009  -1026       C  
ATOM   3747  N   SER C 110      -0.227  47.418 327.264  1.00 53.31           N  
ANISOU 3747  N   SER C 110     3964   6903   9388    574    818   -899       N  
ATOM   3748  CA  SER C 110       0.868  47.039 326.367  1.00 50.12           C  
ANISOU 3748  CA  SER C 110     3687   6353   9003    498    678   -862       C  
ATOM   3749  C   SER C 110       0.997  45.516 326.303  1.00 51.05           C  
ANISOU 3749  C   SER C 110     3711   6482   9204    267    654   -817       C  
ATOM   3750  O   SER C 110       1.132  44.879 327.348  1.00 51.00           O  
ANISOU 3750  O   SER C 110     3725   6473   9179    118    750   -773       O  
ATOM   3751  CB  SER C 110       2.193  47.665 326.808  1.00 52.35           C  
ANISOU 3751  CB  SER C 110     4251   6455   9185    499    674   -819       C  
ATOM   3752  OG  SER C 110       2.738  47.047 327.963  1.00 61.22           O  
ANISOU 3752  OG  SER C 110     5455   7538  10268    344    762   -768       O  
ATOM   3753  N   ASN C 111       0.950  44.929 325.096  1.00 45.20           N  
ANISOU 3753  N   ASN C 111     2888   5744   8543    243    524   -829       N  
ATOM   3754  CA  ASN C 111       1.122  43.481 324.939  1.00 43.81           C  
ANISOU 3754  CA  ASN C 111     2650   5556   8440     33    480   -792       C  
ATOM   3755  C   ASN C 111       2.544  43.165 324.432  1.00 43.31           C  
ANISOU 3755  C   ASN C 111     2788   5319   8350    -22    387   -744       C  
ATOM   3756  O   ASN C 111       3.117  43.977 323.713  1.00 42.33           O  
ANISOU 3756  O   ASN C 111     2779   5118   8189    110    317   -754       O  
ATOM   3757  CB  ASN C 111       0.055  42.879 324.016  1.00 46.09           C  
ANISOU 3757  CB  ASN C 111     2705   5967   8839     23    396   -841       C  
ATOM   3758  CG  ASN C 111       0.157  43.265 322.558  1.00 67.44           C  
ANISOU 3758  CG  ASN C 111     5433   8636  11555    167    238   -883       C  
ATOM   3759  OD1 ASN C 111      -0.573  44.136 322.083  1.00 65.58           O  
ANISOU 3759  OD1 ASN C 111     5130   8474  11314    355    212   -940       O  
ATOM   3760  ND2 ASN C 111       1.011  42.577 321.799  1.00 54.03           N  
ANISOU 3760  ND2 ASN C 111     3833   6827   9869     90    128   -857       N  
ATOM   3761  N   ASN C 112       3.100  41.998 324.793  1.00 37.28           N  
ANISOU 3761  N   ASN C 112     2065   4494   7605   -211    389   -690       N  
ATOM   3762  CA  ASN C 112       4.440  41.591 324.353  1.00 34.53           C  
ANISOU 3762  CA  ASN C 112     1886   3994   7240   -265    309   -643       C  
ATOM   3763  C   ASN C 112       4.425  40.191 323.710  1.00 35.56           C  
ANISOU 3763  C   ASN C 112     1957   4110   7443   -397    220   -634       C  
ATOM   3764  O   ASN C 112       3.430  39.473 323.830  1.00 36.68           O  
ANISOU 3764  O   ASN C 112     1939   4349   7649   -491    232   -652       O  
ATOM   3765  CB  ASN C 112       5.454  41.655 325.503  1.00 33.58           C  
ANISOU 3765  CB  ASN C 112     1929   3777   7051   -343    380   -583       C  
ATOM   3766  CG  ASN C 112       5.125  40.773 326.668  1.00 53.23           C  
ANISOU 3766  CG  ASN C 112     4376   6306   9542   -504    470   -552       C  
ATOM   3767  OD1 ASN C 112       5.386  39.567 326.647  1.00 50.12           O  
ANISOU 3767  OD1 ASN C 112     3985   5873   9186   -651    435   -517       O  
ATOM   3768  ND2 ASN C 112       4.569  41.361 327.717  1.00 42.62           N  
ANISOU 3768  ND2 ASN C 112     3010   5033   8149   -474    592   -561       N  
ATOM   3769  N   PHE C 113       5.526  39.817 323.027  1.00 27.92           N  
ANISOU 3769  N   PHE C 113     1120   3021   6466   -403    133   -606       N  
ATOM   3770  CA  PHE C 113       5.676  38.533 322.335  1.00 26.43           C  
ANISOU 3770  CA  PHE C 113      923   2790   6328   -503     37   -600       C  
ATOM   3771  C   PHE C 113       7.152  38.100 322.297  1.00 25.71           C  
ANISOU 3771  C   PHE C 113     1009   2555   6204   -542      8   -543       C  
ATOM   3772  O   PHE C 113       8.037  38.933 322.484  1.00 24.56           O  
ANISOU 3772  O   PHE C 113      975   2349   6007   -469     39   -517       O  
ATOM   3773  CB  PHE C 113       5.076  38.613 320.909  1.00 28.82           C  
ANISOU 3773  CB  PHE C 113     1154   3131   6666   -398    -78   -660       C  
ATOM   3774  CG  PHE C 113       5.753  39.579 319.967  1.00 30.24           C  
ANISOU 3774  CG  PHE C 113     1451   3247   6792   -224   -123   -668       C  
ATOM   3775  CD1 PHE C 113       5.471  40.943 320.019  1.00 34.58           C  
ANISOU 3775  CD1 PHE C 113     2000   3838   7302    -74    -83   -692       C  
ATOM   3776  CD2 PHE C 113       6.672  39.131 319.026  1.00 32.39           C  
ANISOU 3776  CD2 PHE C 113     1845   3415   7048   -207   -201   -649       C  
ATOM   3777  CE1 PHE C 113       6.127  41.847 319.168  1.00 35.08           C  
ANISOU 3777  CE1 PHE C 113     2191   3829   7309     74   -119   -690       C  
ATOM   3778  CE2 PHE C 113       7.326  40.032 318.176  1.00 35.13           C  
ANISOU 3778  CE2 PHE C 113     2305   3703   7339    -57   -224   -646       C  
ATOM   3779  CZ  PHE C 113       7.049  41.385 318.255  1.00 33.56           C  
ANISOU 3779  CZ  PHE C 113     2111   3538   7102     75   -184   -664       C  
ATOM   3780  N   PHE C 114       7.407  36.790 322.099  1.00 21.46           N  
ANISOU 3780  N   PHE C 114      753   1864   5535   -491    -32   -517       N  
ATOM   3781  CA  PHE C 114       8.747  36.180 321.996  1.00 19.72           C  
ANISOU 3781  CA  PHE C 114      748   1511   5233   -430    -58   -461       C  
ATOM   3782  C   PHE C 114       8.631  34.871 321.201  1.00 22.39           C  
ANISOU 3782  C   PHE C 114      940   1861   5705   -599   -167   -477       C  
ATOM   3783  O   PHE C 114       8.467  33.806 321.788  1.00 22.68           O  
ANISOU 3783  O   PHE C 114      980   1886   5753   -722   -168   -453       O  
ATOM   3784  CB  PHE C 114       9.375  35.933 323.392  1.00 20.54           C  
ANISOU 3784  CB  PHE C 114      865   1607   5331   -546      4   -405       C  
ATOM   3785  CG  PHE C 114      10.880  35.766 323.432  1.00 20.79           C  
ANISOU 3785  CG  PHE C 114      980   1557   5364   -552    -24   -354       C  
ATOM   3786  CD1 PHE C 114      11.500  34.707 322.772  1.00 22.42           C  
ANISOU 3786  CD1 PHE C 114     1098   1709   5711   -740   -116   -348       C  
ATOM   3787  CD2 PHE C 114      11.674  36.634 324.179  1.00 21.83           C  
ANISOU 3787  CD2 PHE C 114     1062   1679   5554   -650     15   -330       C  
ATOM   3788  CE1 PHE C 114      12.892  34.554 322.813  1.00 22.39           C  
ANISOU 3788  CE1 PHE C 114     1174   1617   5715   -750   -140   -305       C  
ATOM   3789  CE2 PHE C 114      13.071  36.485 324.214  1.00 22.83           C  
ANISOU 3789  CE2 PHE C 114     1215   1719   5741   -739    -23   -288       C  
ATOM   3790  CZ  PHE C 114      13.669  35.444 323.538  1.00 21.41           C  
ANISOU 3790  CZ  PHE C 114     1159   1487   5489   -612    -83   -265       C  
ATOM   3791  N   HIS C 115       8.671  34.946 319.876  1.00 19.11           N  
ANISOU 3791  N   HIS C 115      770   1353   5137   -314   -210   -494       N  
ATOM   3792  CA  HIS C 115       8.539  33.738 319.080  1.00 19.70           C  
ANISOU 3792  CA  HIS C 115      843   1401   5240   -344   -305   -507       C  
ATOM   3793  C   HIS C 115       9.864  33.366 318.490  1.00 21.18           C  
ANISOU 3793  C   HIS C 115      985   1540   5523   -440   -380   -494       C  
ATOM   3794  O   HIS C 115      10.621  34.249 318.081  1.00 19.73           O  
ANISOU 3794  O   HIS C 115      882   1325   5288   -302   -347   -479       O  
ATOM   3795  CB  HIS C 115       7.489  33.893 317.968  1.00 21.40           C  
ANISOU 3795  CB  HIS C 115      883   1688   5562   -393   -408   -591       C  
ATOM   3796  CG  HIS C 115       6.211  34.517 318.427  1.00 25.19           C  
ANISOU 3796  CG  HIS C 115      979   2369   6223   -579   -418   -650       C  
ATOM   3797  ND1 HIS C 115       5.284  33.805 319.166  1.00 27.91           N  
ANISOU 3797  ND1 HIS C 115     1104   2811   6689   -807   -422   -661       N  
ATOM   3798  CD2 HIS C 115       5.759  35.781 318.257  1.00 26.98           C  
ANISOU 3798  CD2 HIS C 115     1040   2716   6494   -507   -404   -687       C  
ATOM   3799  CE1 HIS C 115       4.300  34.651 319.419  1.00 28.41           C  
ANISOU 3799  CE1 HIS C 115     1008   3006   6779   -762   -372   -694       C  
ATOM   3800  NE2 HIS C 115       4.536  35.849 318.887  1.00 28.17           N  
ANISOU 3800  NE2 HIS C 115     1010   2991   6702   -576   -366   -714       N  
ATOM   3801  N   VAL C 116      10.163  32.054 318.480  1.00 19.05           N  
ANISOU 3801  N   VAL C 116      899   1205   5135   -333   -396   -448       N  
ATOM   3802  CA  VAL C 116      11.379  31.509 317.900  1.00 18.47           C  
ANISOU 3802  CA  VAL C 116      913   1070   5037   -263   -436   -418       C  
ATOM   3803  C   VAL C 116      10.941  30.470 316.860  1.00 23.14           C  
ANISOU 3803  C   VAL C 116     1358   1597   5838   -577   -627   -518       C  
ATOM   3804  O   VAL C 116       9.970  29.733 317.073  1.00 24.02           O  
ANISOU 3804  O   VAL C 116     1426   1726   5975   -681   -671   -539       O  
ATOM   3805  CB  VAL C 116      12.388  30.963 318.956  1.00 21.37           C  
ANISOU 3805  CB  VAL C 116     1228   1375   5518   -518   -442   -385       C  
ATOM   3806  CG1 VAL C 116      13.585  30.276 318.311  1.00 20.96           C  
ANISOU 3806  CG1 VAL C 116     1274   1247   5444   -446   -491   -365       C  
ATOM   3807  CG2 VAL C 116      12.828  32.028 319.952  1.00 21.10           C  
ANISOU 3807  CG2 VAL C 116     1184   1375   5460   -494   -342   -346       C  
ATOM   3808  N   ALA C 117      11.605  30.486 315.694  1.00 21.09           N  
ANISOU 3808  N   ALA C 117     1222   1300   5490   -368   -653   -515       N  
ATOM   3809  CA  ALA C 117      11.344  29.554 314.593  1.00 21.57           C  
ANISOU 3809  CA  ALA C 117     1334   1303   5560   -380   -786   -571       C  
ATOM   3810  C   ALA C 117      12.586  28.760 314.254  1.00 22.22           C  
ANISOU 3810  C   ALA C 117     1539   1234   5671   -437   -836   -580       C  
ATOM   3811  O   ALA C 117      13.698  29.203 314.550  1.00 21.07           O  
ANISOU 3811  O   ALA C 117     1426   1110   5470   -309   -737   -513       O  
ATOM   3812  CB  ALA C 117      10.872  30.301 313.371  1.00 22.33           C  
ANISOU 3812  CB  ALA C 117     1376   1415   5696   -357   -867   -658       C  
ATOM   3813  N   PHE C 118      12.388  27.592 313.630  1.00 19.85           N  
ANISOU 3813  N   PHE C 118     1336    988   5219   -247   -895   -541       N  
ATOM   3814  CA  PHE C 118      13.442  26.650 313.253  1.00 19.50           C  
ANISOU 3814  CA  PHE C 118     1407    887   5114   -188   -935   -521       C  
ATOM   3815  C   PHE C 118      13.219  26.111 311.834  1.00 22.64           C  
ANISOU 3815  C   PHE C 118     1983   1018   5601   -286  -1098   -676       C  
ATOM   3816  O   PHE C 118      12.199  25.465 311.556  1.00 22.62           O  
ANISOU 3816  O   PHE C 118     1984    994   5616   -376  -1221   -732       O  
ATOM   3817  CB  PHE C 118      13.482  25.502 314.272  1.00 21.18           C  
ANISOU 3817  CB  PHE C 118     1687    980   5381   -373   -973   -510       C  
ATOM   3818  CG  PHE C 118      14.441  24.377 313.996  1.00 22.18           C  
ANISOU 3818  CG  PHE C 118     1988    939   5499   -379  -1041   -525       C  
ATOM   3819  CD1 PHE C 118      15.748  24.432 314.456  1.00 23.57           C  
ANISOU 3819  CD1 PHE C 118     2254    953   5748   -404   -982   -514       C  
ATOM   3820  CD2 PHE C 118      14.021  23.233 313.337  1.00 24.18           C  
ANISOU 3820  CD2 PHE C 118     2424    951   5812   -505  -1197   -627       C  
ATOM   3821  CE1 PHE C 118      16.630  23.386 314.221  1.00 24.90           C  
ANISOU 3821  CE1 PHE C 118     2584   1002   5874   -324  -1028   -510       C  
ATOM   3822  CE2 PHE C 118      14.904  22.187 313.098  1.00 27.59           C  
ANISOU 3822  CE2 PHE C 118     3041   1249   6192   -428  -1243   -625       C  
ATOM   3823  CZ  PHE C 118      16.200  22.266 313.547  1.00 25.17           C  
ANISOU 3823  CZ  PHE C 118     2765    928   5872   -331  -1154   -566       C  
ATOM   3824  N   GLN C 119      14.200  26.384 310.948  1.00 19.61           N  
ANISOU 3824  N   GLN C 119     1612    785   5053    -27  -1043   -615       N  
ATOM   3825  CA  GLN C 119      14.246  25.980 309.535  1.00 19.94           C  
ANISOU 3825  CA  GLN C 119     1798    766   5013     81  -1135   -677       C  
ATOM   3826  C   GLN C 119      13.013  26.518 308.749  1.00 23.51           C  
ANISOU 3826  C   GLN C 119     2293   1096   5542     61  -1233   -796       C  
ATOM   3827  O   GLN C 119      12.465  25.825 307.884  1.00 23.68           O  
ANISOU 3827  O   GLN C 119     2424   1053   5521     85  -1374   -865       O  
ATOM   3828  CB  GLN C 119      14.413  24.441 309.388  1.00 21.72           C  
ANISOU 3828  CB  GLN C 119     2228    783   5242     47  -1246   -724       C  
ATOM   3829  CG  GLN C 119      15.646  23.857 310.102  1.00 24.52           C  
ANISOU 3829  CG  GLN C 119     2702    961   5653     43  -1177   -695       C  
ATOM   3830  CD  GLN C 119      16.987  24.092 309.430  1.00 43.61           C  
ANISOU 3830  CD  GLN C 119     5208   3363   8000    259  -1084   -670       C  
ATOM   3831  OE1 GLN C 119      17.365  25.207 309.046  1.00 37.95           O  
ANISOU 3831  OE1 GLN C 119     4421   2730   7266    361   -976   -643       O  
ATOM   3832  NE2 GLN C 119      17.781  23.044 309.355  1.00 41.03           N  
ANISOU 3832  NE2 GLN C 119     5030   2927   7632    329  -1113   -671       N  
ATOM   3833  N   GLY C 120      12.632  27.763 309.052  1.00 20.09           N  
ANISOU 3833  N   GLY C 120     1707    780   5146     54  -1161   -778       N  
ATOM   3834  CA  GLY C 120      11.523  28.457 308.408  1.00 20.66           C  
ANISOU 3834  CA  GLY C 120     1712    924   5215     85  -1238   -837       C  
ATOM   3835  C   GLY C 120      10.218  28.497 309.169  1.00 25.41           C  
ANISOU 3835  C   GLY C 120     2128   1608   5917    -88  -1290   -861       C  
ATOM   3836  O   GLY C 120       9.535  29.520 309.149  1.00 24.33           O  
ANISOU 3836  O   GLY C 120     1866   1576   5803    -61  -1269   -873       O  
ATOM   3837  N   LYS C 121       9.843  27.378 309.808  1.00 24.41           N  
ANISOU 3837  N   LYS C 121     1992   1435   5850   -262  -1357   -869       N  
ATOM   3838  CA  LYS C 121       8.577  27.225 310.541  1.00 25.70           C  
ANISOU 3838  CA  LYS C 121     1977   1674   6115   -452  -1400   -887       C  
ATOM   3839  C   LYS C 121       8.739  27.512 312.038  1.00 29.05           C  
ANISOU 3839  C   LYS C 121     2285   2152   6600   -574  -1253   -814       C  
ATOM   3840  O   LYS C 121       9.829  27.310 312.564  1.00 28.84           O  
ANISOU 3840  O   LYS C 121     2348   2063   6546   -559  -1167   -755       O  
ATOM   3841  CB  LYS C 121       8.028  25.798 310.335  1.00 29.61           C  
ANISOU 3841  CB  LYS C 121     2540   2074   6635   -592  -1557   -933       C  
ATOM   3842  N   ASP C 122       7.661  27.954 312.726  1.00 25.25           N  
ANISOU 3842  N   ASP C 122     1608   1788   6199   -689  -1227   -820       N  
ATOM   3843  CA  ASP C 122       7.687  28.209 314.177  1.00 25.15           C  
ANISOU 3843  CA  ASP C 122     1505   1833   6220   -786  -1081   -749       C  
ATOM   3844  C   ASP C 122       7.915  26.909 314.960  1.00 29.45           C  
ANISOU 3844  C   ASP C 122     2111   2278   6801   -988  -1100   -719       C  
ATOM   3845  O   ASP C 122       7.528  25.834 314.484  1.00 30.54           O  
ANISOU 3845  O   ASP C 122     2314   2338   6952  -1070  -1229   -756       O  
ATOM   3846  CB  ASP C 122       6.375  28.843 314.665  1.00 27.99           C  
ANISOU 3846  CB  ASP C 122     1625   2341   6668   -884  -1063   -780       C  
ATOM   3847  CG  ASP C 122       5.911  30.048 313.889  1.00 42.87           C  
ANISOU 3847  CG  ASP C 122     3432   4320   8536   -715  -1084   -828       C  
ATOM   3848  OD1 ASP C 122       5.256  29.858 312.838  1.00 45.83           O  
ANISOU 3848  OD1 ASP C 122     3811   4693   8910   -664  -1228   -896       O  
ATOM   3849  OD2 ASP C 122       6.155  31.183 314.357  1.00 49.18           O  
ANISOU 3849  OD2 ASP C 122     4175   5190   9321   -634   -966   -800       O  
ATOM   3850  N   ILE C 123       8.519  26.999 316.165  1.00 24.76           N  
ANISOU 3850  N   ILE C 123     1596   1714   6098   -873   -924   -601       N  
ATOM   3851  CA  ILE C 123       8.745  25.804 316.987  1.00 24.48           C  
ANISOU 3851  CA  ILE C 123     1673   1624   6004   -927   -906   -530       C  
ATOM   3852  C   ILE C 123       8.305  26.045 318.429  1.00 26.24           C  
ANISOU 3852  C   ILE C 123     1772   1892   6307  -1147   -808   -504       C  
ATOM   3853  O   ILE C 123       7.623  25.189 318.998  1.00 27.27           O  
ANISOU 3853  O   ILE C 123     1888   2015   6460  -1306   -820   -488       O  
ATOM   3854  CB  ILE C 123      10.187  25.247 316.914  1.00 25.50           C  
ANISOU 3854  CB  ILE C 123     1935   1594   6158   -984   -951   -529       C  
ATOM   3855  CG1 ILE C 123      11.247  26.362 316.976  1.00 23.60           C  
ANISOU 3855  CG1 ILE C 123     1700   1414   5852   -774   -839   -486       C  
ATOM   3856  CG2 ILE C 123      10.347  24.356 315.674  1.00 26.76           C  
ANISOU 3856  CG2 ILE C 123     2218   1600   6350  -1024  -1120   -610       C  
ATOM   3857  CD1 ILE C 123      12.361  26.060 317.873  1.00 25.32           C  
ANISOU 3857  CD1 ILE C 123     1976   1487   6157   -954   -821   -465       C  
ATOM   3858  N   LEU C 124       8.678  27.195 319.019  1.00 21.81           N  
ANISOU 3858  N   LEU C 124     1306   1460   5523   -751   -619   -414       N  
ATOM   3859  CA  LEU C 124       8.281  27.522 320.385  1.00 21.86           C  
ANISOU 3859  CA  LEU C 124     1278   1529   5499   -804   -499   -375       C  
ATOM   3860  C   LEU C 124       8.267  29.044 320.629  1.00 24.83           C  
ANISOU 3860  C   LEU C 124     1441   1949   6044   -968   -454   -430       C  
ATOM   3861  O   LEU C 124       8.869  29.823 319.882  1.00 23.97           O  
ANISOU 3861  O   LEU C 124     1354   1832   5922   -825   -467   -448       O  
ATOM   3862  CB  LEU C 124       9.138  26.790 321.446  1.00 21.54           C  
ANISOU 3862  CB  LEU C 124     1354   1449   5382   -826   -466   -300       C  
ATOM   3863  CG  LEU C 124      10.627  27.102 321.518  1.00 23.17           C  
ANISOU 3863  CG  LEU C 124     1574   1556   5674   -900   -491   -298       C  
ATOM   3864  CD1 LEU C 124      10.938  27.883 322.759  1.00 22.87           C  
ANISOU 3864  CD1 LEU C 124     1536   1569   5583   -864   -378   -256       C  
ATOM   3865  CD2 LEU C 124      11.437  25.837 321.547  1.00 24.87           C  
ANISOU 3865  CD2 LEU C 124     1894   1620   5935  -1048   -583   -282       C  
ATOM   3866  N   SER C 125       7.549  29.445 321.686  1.00 23.10           N  
ANISOU 3866  N   SER C 125     1263   1817   5697   -850   -321   -394       N  
ATOM   3867  CA  SER C 125       7.383  30.822 322.120  1.00 22.25           C  
ANISOU 3867  CA  SER C 125     1130   1772   5552   -740   -223   -406       C  
ATOM   3868  C   SER C 125       7.230  30.890 323.629  1.00 23.82           C  
ANISOU 3868  C   SER C 125     1228   2014   5808   -960   -128   -377       C  
ATOM   3869  O   SER C 125       6.743  29.945 324.240  1.00 24.46           O  
ANISOU 3869  O   SER C 125     1314   2100   5880  -1082   -110   -351       O  
ATOM   3870  CB  SER C 125       6.162  31.440 321.443  1.00 26.59           C  
ANISOU 3870  CB  SER C 125     1306   2440   6356   -987   -286   -503       C  
ATOM   3871  OG  SER C 125       4.999  30.645 321.612  1.00 36.93           O  
ANISOU 3871  OG  SER C 125     2282   3846   7903  -1376   -339   -542       O  
ATOM   3872  N   PHE C 126       7.629  32.009 324.227  1.00 20.25           N  
ANISOU 3872  N   PHE C 126      968   1568   5159   -666    -30   -355       N  
ATOM   3873  CA  PHE C 126       7.499  32.235 325.662  1.00 20.33           C  
ANISOU 3873  CA  PHE C 126      992   1614   5119   -727     71   -326       C  
ATOM   3874  C   PHE C 126       6.073  32.660 325.965  1.00 23.95           C  
ANISOU 3874  C   PHE C 126     1094   2205   5801  -1039    138   -372       C  
ATOM   3875  O   PHE C 126       5.592  33.635 325.394  1.00 23.47           O  
ANISOU 3875  O   PHE C 126      957   2201   5758   -932    142   -424       O  
ATOM   3876  CB  PHE C 126       8.512  33.289 326.138  1.00 20.34           C  
ANISOU 3876  CB  PHE C 126     1022   1592   5113   -692    104   -311       C  
ATOM   3877  CG  PHE C 126       8.732  33.296 327.627  1.00 21.57           C  
ANISOU 3877  CG  PHE C 126     1169   1757   5268   -850    183   -271       C  
ATOM   3878  CD1 PHE C 126       9.561  32.355 328.228  1.00 23.73           C  
ANISOU 3878  CD1 PHE C 126     1457   1950   5607  -1070    153   -214       C  
ATOM   3879  CD2 PHE C 126       8.114  34.241 328.431  1.00 23.52           C  
ANISOU 3879  CD2 PHE C 126     1250   2079   5608  -1010    291   -287       C  
ATOM   3880  CE1 PHE C 126       9.754  32.352 329.609  1.00 24.67           C  
ANISOU 3880  CE1 PHE C 126     1619   2050   5704  -1206    226   -172       C  
ATOM   3881  CE2 PHE C 126       8.315  34.243 329.814  1.00 25.90           C  
ANISOU 3881  CE2 PHE C 126     1505   2373   5962  -1251    382   -240       C  
ATOM   3882  CZ  PHE C 126       9.144  33.307 330.391  1.00 24.49           C  
ANISOU 3882  CZ  PHE C 126     1549   2103   5652  -1203    339   -187       C  
ATOM   3883  N   GLN C 127       5.394  31.906 326.829  1.00 23.70           N  
ANISOU 3883  N   GLN C 127     1119   2195   5690  -1084    201   -345       N  
ATOM   3884  CA  GLN C 127       4.003  32.126 327.223  1.00 25.87           C  
ANISOU 3884  CA  GLN C 127     1152   2605   6071  -1241    291   -373       C  
ATOM   3885  C   GLN C 127       3.886  32.208 328.743  1.00 31.03           C  
ANISOU 3885  C   GLN C 127     1549   3346   6896  -1634    457   -316       C  
ATOM   3886  O   GLN C 127       4.144  31.219 329.438  1.00 31.69           O  
ANISOU 3886  O   GLN C 127     1735   3353   6952  -1788    477   -257       O  
ATOM   3887  CB  GLN C 127       3.117  30.990 326.673  1.00 28.40           C  
ANISOU 3887  CB  GLN C 127     1261   2972   6556  -1481    230   -386       C  
ATOM   3888  CG  GLN C 127       1.901  31.455 325.875  1.00 36.26           C  
ANISOU 3888  CG  GLN C 127     1722   4185   7868  -1723    212   -457       C  
ATOM   3889  CD  GLN C 127       2.253  32.198 324.608  1.00 40.94           C  
ANISOU 3889  CD  GLN C 127     2318   4768   8469  -1527     82   -521       C  
ATOM   3890  OE1 GLN C 127       3.178  31.839 323.864  1.00 30.82           O  
ANISOU 3890  OE1 GLN C 127     1182   3360   7169  -1492    -40   -522       O  
ATOM   3891  NE2 GLN C 127       1.518  33.265 324.349  1.00 31.68           N  
ANISOU 3891  NE2 GLN C 127      993   3729   7315  -1385    110   -574       N  
ATOM   3892  N   GLY C 128       3.513  33.388 329.238  1.00 29.30           N  
ANISOU 3892  N   GLY C 128     1348   3204   6580  -1452    558   -342       N  
ATOM   3893  CA  GLY C 128       3.367  33.660 330.665  1.00 30.11           C  
ANISOU 3893  CA  GLY C 128     1460   3350   6632  -1537    721   -299       C  
ATOM   3894  C   GLY C 128       4.684  33.605 331.416  1.00 33.62           C  
ANISOU 3894  C   GLY C 128     2044   3674   7057  -1644    729   -234       C  
ATOM   3895  O   GLY C 128       5.395  34.614 331.497  1.00 32.26           O  
ANISOU 3895  O   GLY C 128     1962   3473   6824  -1499    723   -248       O  
ATOM   3896  N   THR C 129       5.029  32.405 331.947  1.00 31.09           N  
ANISOU 3896  N   THR C 129     1870   3249   6693  -1779    711   -174       N  
ATOM   3897  CA  THR C 129       6.262  32.173 332.719  1.00 29.87           C  
ANISOU 3897  CA  THR C 129     1966   2953   6432  -1774    683   -120       C  
ATOM   3898  C   THR C 129       7.167  31.115 332.104  1.00 30.99           C  
ANISOU 3898  C   THR C 129     2193   2947   6635  -1873    535    -91       C  
ATOM   3899  O   THR C 129       8.243  30.873 332.639  1.00 29.81           O  
ANISOU 3899  O   THR C 129     2229   2677   6419  -1860    486    -52       O  
ATOM   3900  CB  THR C 129       5.936  31.756 334.174  1.00 42.33           C  
ANISOU 3900  CB  THR C 129     3605   4527   7951  -1952    831    -53       C  
ATOM   3901  OG1 THR C 129       5.161  30.553 334.207  1.00 47.05           O  
ANISOU 3901  OG1 THR C 129     4143   5135   8600  -2145    862    -19       O  
ATOM   3902  CG2 THR C 129       5.208  32.868 334.943  1.00 40.60           C  
ANISOU 3902  CG2 THR C 129     3316   4437   7672  -1875    998    -73       C  
ATOM   3903  N   SER C 130       6.759  30.486 331.005  1.00 28.26           N  
ANISOU 3903  N   SER C 130     1843   2627   6269  -1756    441   -128       N  
ATOM   3904  CA  SER C 130       7.561  29.405 330.443  1.00 27.91           C  
ANISOU 3904  CA  SER C 130     1935   2463   6207  -1743    302   -107       C  
ATOM   3905  C   SER C 130       7.476  29.303 328.923  1.00 29.54           C  
ANISOU 3905  C   SER C 130     1984   2653   6588  -1796    187   -162       C  
ATOM   3906  O   SER C 130       6.599  29.890 328.295  1.00 29.32           O  
ANISOU 3906  O   SER C 130     1783   2739   6618  -1748    205   -216       O  
ATOM   3907  CB  SER C 130       7.136  28.070 331.060  1.00 32.13           C  
ANISOU 3907  CB  SER C 130     2428   2896   6882  -2171    333    -45       C  
ATOM   3908  OG  SER C 130       5.724  27.922 331.105  1.00 41.74           O  
ANISOU 3908  OG  SER C 130     3455   4234   8171  -2298    417    -59       O  
ATOM   3909  N   TRP C 131       8.396  28.523 328.349  1.00 26.14           N  
ANISOU 3909  N   TRP C 131     1809   2161   5961  -1482     65   -148       N  
ATOM   3910  CA  TRP C 131       8.472  28.250 326.928  1.00 25.77           C  
ANISOU 3910  CA  TRP C 131     1742   2100   5949  -1370    -45   -189       C  
ATOM   3911  C   TRP C 131       7.401  27.250 326.563  1.00 30.93           C  
ANISOU 3911  C   TRP C 131     2154   2693   6905  -1874   -101   -221       C  
ATOM   3912  O   TRP C 131       7.418  26.148 327.106  1.00 32.33           O  
ANISOU 3912  O   TRP C 131     2418   2774   7090  -2057   -116   -177       O  
ATOM   3913  CB  TRP C 131       9.861  27.693 326.579  1.00 24.05           C  
ANISOU 3913  CB  TRP C 131     1711   1809   5619  -1167   -138   -155       C  
ATOM   3914  CG  TRP C 131      10.983  28.604 326.953  1.00 23.68           C  
ANISOU 3914  CG  TRP C 131     1709   1749   5539  -1065   -117   -137       C  
ATOM   3915  CD1 TRP C 131      11.817  28.486 328.027  1.00 25.53           C  
ANISOU 3915  CD1 TRP C 131     1999   1883   5819  -1251   -109    -93       C  
ATOM   3916  CD2 TRP C 131      11.354  29.812 326.284  1.00 22.63           C  
ANISOU 3916  CD2 TRP C 131     1543   1653   5402   -884   -109   -167       C  
ATOM   3917  NE1 TRP C 131      12.702  29.539 328.056  1.00 24.19           N  
ANISOU 3917  NE1 TRP C 131     1855   1745   5589  -1062   -100    -90       N  
ATOM   3918  CE2 TRP C 131      12.439  30.369 326.997  1.00 24.76           C  
ANISOU 3918  CE2 TRP C 131     1807   1837   5763  -1038   -104   -142       C  
ATOM   3919  CE3 TRP C 131      10.872  30.481 325.144  1.00 23.26           C  
ANISOU 3919  CE3 TRP C 131     1508   1752   5578   -866   -127   -226       C  
ATOM   3920  CZ2 TRP C 131      13.071  31.548 326.590  1.00 23.57           C  
ANISOU 3920  CZ2 TRP C 131     1655   1717   5585   -860    -94   -154       C  
ATOM   3921  CZ3 TRP C 131      11.500  31.644 324.741  1.00 23.52           C  
ANISOU 3921  CZ3 TRP C 131     1502   1778   5657   -808   -121   -243       C  
ATOM   3922  CH2 TRP C 131      12.580  32.172 325.463  1.00 23.49           C  
ANISOU 3922  CH2 TRP C 131     1556   1740   5629   -796    -99   -204       C  
ATOM   3923  N   GLU C 132       6.462  27.620 325.673  1.00 28.73           N  
ANISOU 3923  N   GLU C 132     1802   2539   6574  -1661   -115   -275       N  
ATOM   3924  CA  GLU C 132       5.392  26.728 325.220  1.00 30.17           C  
ANISOU 3924  CA  GLU C 132     1876   2738   6850  -1830   -173   -300       C  
ATOM   3925  C   GLU C 132       5.603  26.386 323.740  1.00 33.03           C  
ANISOU 3925  C   GLU C 132     2144   3013   7393  -1966   -361   -373       C  
ATOM   3926  O   GLU C 132       5.940  27.284 322.966  1.00 31.50           O  
ANISOU 3926  O   GLU C 132     1932   2856   7181  -1768   -392   -415       O  
ATOM   3927  CB  GLU C 132       4.007  27.352 325.456  1.00 32.17           C  
ANISOU 3927  CB  GLU C 132     1851   3155   7218  -1953    -88   -337       C  
ATOM   3928  N   PRO C 133       5.449  25.105 323.319  1.00 31.84           N  
ANISOU 3928  N   PRO C 133     2135   2779   7185  -1969   -454   -361       N  
ATOM   3929  CA  PRO C 133       5.659  24.775 321.894  1.00 31.56           C  
ANISOU 3929  CA  PRO C 133     2142   2673   7175  -1895   -619   -421       C  
ATOM   3930  C   PRO C 133       4.435  25.025 321.023  1.00 38.18           C  
ANISOU 3930  C   PRO C 133     2723   3604   8178  -2029   -712   -515       C  
ATOM   3931  O   PRO C 133       3.315  25.059 321.539  1.00 40.79           O  
ANISOU 3931  O   PRO C 133     2868   4054   8578  -2162   -648   -514       O  
ATOM   3932  CB  PRO C 133       5.954  23.279 321.928  1.00 33.26           C  
ANISOU 3932  CB  PRO C 133     2505   2713   7419  -2100   -719   -401       C  
ATOM   3933  CG  PRO C 133       5.208  22.779 323.116  1.00 38.46           C  
ANISOU 3933  CG  PRO C 133     3080   3383   8152  -2400   -629   -355       C  
ATOM   3934  CD  PRO C 133       5.051  23.913 324.096  1.00 34.12           C  
ANISOU 3934  CD  PRO C 133     2453   2994   7516  -2253   -442   -314       C  
ATOM   3935  N   THR C 134       4.635  25.119 319.697  1.00 33.82           N  
ANISOU 3935  N   THR C 134     2217   3016   7617  -1887   -849   -579       N  
ATOM   3936  CA  THR C 134       3.529  25.244 318.742  1.00 34.72           C  
ANISOU 3936  CA  THR C 134     2172   3218   7803  -1885   -959   -658       C  
ATOM   3937  C   THR C 134       2.902  23.843 318.575  1.00 40.38           C  
ANISOU 3937  C   THR C 134     2914   3849   8578  -2103  -1082   -670       C  
ATOM   3938  O   THR C 134       3.570  22.857 318.875  1.00 39.76           O  
ANISOU 3938  O   THR C 134     3032   3614   8460  -2189  -1106   -629       O  
ATOM   3939  CB  THR C 134       4.009  25.865 317.433  1.00 41.84           C  
ANISOU 3939  CB  THR C 134     3137   4105   8654  -1647  -1054   -717       C  
ATOM   3940  OG1 THR C 134       5.203  25.208 317.007  1.00 43.85           O  
ANISOU 3940  OG1 THR C 134     3638   4193   8832  -1576  -1111   -702       O  
ATOM   3941  CG2 THR C 134       4.264  27.353 317.564  1.00 37.41           C  
ANISOU 3941  CG2 THR C 134     2497   3657   8061  -1464   -939   -713       C  
ATOM   3942  N   GLN C 135       1.623  23.748 318.157  1.00 39.23           N  
ANISOU 3942  N   GLN C 135     2572   3802   8529  -2198  -1162   -725       N  
ATOM   3943  CA  GLN C 135       0.915  22.459 318.021  1.00 41.13           C  
ANISOU 3943  CA  GLN C 135     2812   3971   8843  -2433  -1287   -739       C  
ATOM   3944  C   GLN C 135       1.581  21.511 317.020  1.00 45.16           C  
ANISOU 3944  C   GLN C 135     3584   4281   9296  -2394  -1473   -775       C  
ATOM   3945  O   GLN C 135       1.684  20.318 317.305  1.00 45.26           O  
ANISOU 3945  O   GLN C 135     3740   4148   9308  -2571  -1522   -744       O  
ATOM   3946  CB  GLN C 135      -0.554  22.667 317.622  1.00 44.31           C  
ANISOU 3946  CB  GLN C 135     2933   4534   9368  -2509  -1360   -804       C  
ATOM   3947  N   GLU C 136       2.048  22.042 315.868  1.00 41.33           N  
ANISOU 3947  N   GLU C 136     3177   3779   8749  -2157  -1569   -838       N  
ATOM   3948  CA  GLU C 136       2.664  21.252 314.795  1.00 41.28           C  
ANISOU 3948  CA  GLU C 136     3420   3594   8672  -2079  -1740   -883       C  
ATOM   3949  C   GLU C 136       4.198  21.129 314.939  1.00 42.94           C  
ANISOU 3949  C   GLU C 136     3880   3672   8765  -1930  -1671   -834       C  
ATOM   3950  O   GLU C 136       4.864  20.661 314.007  1.00 42.50           O  
ANISOU 3950  O   GLU C 136     4031   3486   8632  -1802  -1784   -872       O  
ATOM   3951  CB  GLU C 136       2.298  21.846 313.422  1.00 42.95           C  
ANISOU 3951  CB  GLU C 136     3591   3858   8871  -1901  -1883   -977       C  
ATOM   3952  N   ALA C 137       4.748  21.502 316.108  1.00 37.92           N  
ANISOU 3952  N   ALA C 137     3227   3068   8114  -1946  -1492   -752       N  
ATOM   3953  CA  ALA C 137       6.186  21.405 316.375  1.00 36.05           C  
ANISOU 3953  CA  ALA C 137     3194   2723   7782  -1817  -1426   -701       C  
ATOM   3954  C   ALA C 137       6.650  19.935 316.463  1.00 39.42           C  
ANISOU 3954  C   ALA C 137     3858   2945   8173  -1918  -1517   -682       C  
ATOM   3955  O   ALA C 137       5.887  19.086 316.942  1.00 39.86           O  
ANISOU 3955  O   ALA C 137     3901   2958   8285  -2151  -1556   -668       O  
ATOM   3956  CB  ALA C 137       6.533  22.137 317.661  1.00 35.75           C  
ANISOU 3956  CB  ALA C 137     3071   2770   7742  -1831  -1234   -624       C  
ATOM   3957  N   PRO C 138       7.893  19.618 316.009  1.00 35.00           N  
ANISOU 3957  N   PRO C 138     3519   2258   7523  -1746  -1547   -680       N  
ATOM   3958  CA  PRO C 138       8.368  18.220 316.077  1.00 35.79           C  
ANISOU 3958  CA  PRO C 138     3862   2155   7581  -1818  -1639   -665       C  
ATOM   3959  C   PRO C 138       8.526  17.745 317.519  1.00 40.09           C  
ANISOU 3959  C   PRO C 138     4439   2657   8137  -1988  -1543   -576       C  
ATOM   3960  O   PRO C 138       8.836  18.546 318.398  1.00 39.08           O  
ANISOU 3960  O   PRO C 138     4201   2634   8014  -1968  -1392   -521       O  
ATOM   3961  CB  PRO C 138       9.709  18.250 315.333  1.00 36.26           C  
ANISOU 3961  CB  PRO C 138     4104   2130   7542  -1556  -1655   -679       C  
ATOM   3962  CG  PRO C 138      10.139  19.653 315.358  1.00 38.82           C  
ANISOU 3962  CG  PRO C 138     4278   2609   7861  -1393  -1520   -662       C  
ATOM   3963  CD  PRO C 138       8.914  20.507 315.414  1.00 34.74           C  
ANISOU 3963  CD  PRO C 138     3520   2258   7421  -1480  -1495   -688       C  
ATOM   3964  N   LEU C 139       8.310  16.448 317.757  1.00 37.79           N  
ANISOU 3964  N   LEU C 139     4317   2201   7842  -2154  -1635   -562       N  
ATOM   3965  CA  LEU C 139       8.346  15.831 319.082  1.00 38.21           C  
ANISOU 3965  CA  LEU C 139     4440   2183   7893  -2338  -1563   -476       C  
ATOM   3966  C   LEU C 139       9.626  16.108 319.884  1.00 42.44           C  
ANISOU 3966  C   LEU C 139     5065   2701   8361  -2198  -1453   -408       C  
ATOM   3967  O   LEU C 139       9.597  15.996 321.114  1.00 43.44           O  
ANISOU 3967  O   LEU C 139     5187   2831   8486  -2329  -1354   -333       O  
ATOM   3968  CB  LEU C 139       8.130  14.323 318.970  1.00 39.92           C  
ANISOU 3968  CB  LEU C 139     4890   2184   8094  -2492  -1708   -479       C  
ATOM   3969  CG  LEU C 139       6.710  13.887 318.634  1.00 46.18           C  
ANISOU 3969  CG  LEU C 139     5586   2984   8977  -2738  -1803   -516       C  
ATOM   3970  CD1 LEU C 139       6.676  12.424 318.255  1.00 48.07           C  
ANISOU 3970  CD1 LEU C 139     6097   2983   9183  -2831  -1986   -542       C  
ATOM   3971  CD2 LEU C 139       5.748  14.176 319.787  1.00 49.26           C  
ANISOU 3971  CD2 LEU C 139     5792   3481   9442  -2995  -1667   -444       C  
ATOM   3972  N   TRP C 140      10.726  16.496 319.218  1.00 37.28           N  
ANISOU 3972  N   TRP C 140     4482   2033   7649  -1938  -1467   -434       N  
ATOM   3973  CA  TRP C 140      11.965  16.783 319.920  1.00 35.55           C  
ANISOU 3973  CA  TRP C 140     4325   1804   7378  -1801  -1379   -376       C  
ATOM   3974  C   TRP C 140      11.917  18.165 320.567  1.00 38.20           C  
ANISOU 3974  C   TRP C 140     4441   2329   7744  -1777  -1224   -343       C  
ATOM   3975  O   TRP C 140      12.674  18.408 321.505  1.00 37.28           O  
ANISOU 3975  O   TRP C 140     4355   2213   7599  -1745  -1144   -282       O  
ATOM   3976  CB  TRP C 140      13.183  16.628 319.003  1.00 34.00           C  
ANISOU 3976  CB  TRP C 140     4267   1533   7118  -1541  -1437   -409       C  
ATOM   3977  CG  TRP C 140      13.210  17.514 317.793  1.00 34.61           C  
ANISOU 3977  CG  TRP C 140     4234   1717   7200  -1365  -1437   -474       C  
ATOM   3978  CD1 TRP C 140      12.963  17.142 316.503  1.00 38.44           C  
ANISOU 3978  CD1 TRP C 140     4796   2147   7661  -1289  -1553   -551       C  
ATOM   3979  CD2 TRP C 140      13.623  18.888 317.743  1.00 32.97           C  
ANISOU 3979  CD2 TRP C 140     3857   1666   7002  -1227  -1319   -464       C  
ATOM   3980  NE1 TRP C 140      13.157  18.212 315.657  1.00 37.02           N  
ANISOU 3980  NE1 TRP C 140     4503   2087   7474  -1113  -1508   -586       N  
ATOM   3981  CE2 TRP C 140      13.550  19.299 316.394  1.00 36.86           C  
ANISOU 3981  CE2 TRP C 140     4330   2198   7479  -1078  -1363   -532       C  
ATOM   3982  CE3 TRP C 140      14.014  19.826 318.714  1.00 33.19           C  
ANISOU 3982  CE3 TRP C 140     3762   1801   7048  -1221  -1186   -405       C  
ATOM   3983  CZ2 TRP C 140      13.824  20.609 315.997  1.00 35.05           C  
ANISOU 3983  CZ2 TRP C 140     3960   2106   7251   -934  -1272   -537       C  
ATOM   3984  CZ3 TRP C 140      14.303  21.119 318.319  1.00 33.68           C  
ANISOU 3984  CZ3 TRP C 140     3685   1995   7118  -1080  -1104   -414       C  
ATOM   3985  CH2 TRP C 140      14.199  21.503 316.976  1.00 34.36           C  
ANISOU 3985  CH2 TRP C 140     3751   2114   7188   -942  -1143   -476       C  
ATOM   3986  N   VAL C 141      11.043  19.077 320.073  1.00 35.05           N  
ANISOU 3986  N   VAL C 141     3835   2084   7400  -1784  -1192   -387       N  
ATOM   3987  CA  VAL C 141      10.886  20.433 320.630  1.00 34.04           C  
ANISOU 3987  CA  VAL C 141     3507   2130   7297  -1755  -1051   -365       C  
ATOM   3988  C   VAL C 141      10.396  20.290 322.082  1.00 39.11           C  
ANISOU 3988  C   VAL C 141     4116   2792   7951  -1956   -954   -297       C  
ATOM   3989  O   VAL C 141      10.938  20.961 322.966  1.00 37.24           O  
ANISOU 3989  O   VAL C 141     3857   2605   7688  -1914   -848   -248       O  
ATOM   3990  CB  VAL C 141       9.984  21.356 319.754  1.00 37.86           C  
ANISOU 3990  CB  VAL C 141     3793   2761   7830  -1709  -1053   -432       C  
ATOM   3991  CG1 VAL C 141       9.509  22.596 320.510  1.00 36.94           C  
ANISOU 3991  CG1 VAL C 141     3479   2814   7742  -1718   -909   -408       C  
ATOM   3992  CG2 VAL C 141      10.717  21.770 318.484  1.00 36.78           C  
ANISOU 3992  CG2 VAL C 141     3707   2611   7655  -1477  -1112   -483       C  
ATOM   3993  N   ASN C 142       9.462  19.332 322.329  1.00 38.19           N  
ANISOU 3993  N   ASN C 142     4024   2620   7868  -2176   -997   -290       N  
ATOM   3994  CA  ASN C 142       8.926  18.992 323.654  1.00 39.49           C  
ANISOU 3994  CA  ASN C 142     4184   2784   8036  -2390   -903   -219       C  
ATOM   3995  C   ASN C 142      10.056  18.608 324.615  1.00 44.43           C  
ANISOU 3995  C   ASN C 142     5011   3292   8578  -2356   -874   -146       C  
ATOM   3996  O   ASN C 142      10.057  19.024 325.777  1.00 43.65           O  
ANISOU 3996  O   ASN C 142     4887   3244   8453  -2417   -753    -86       O  
ATOM   3997  CB  ASN C 142       7.913  17.852 323.550  1.00 42.90           C  
ANISOU 3997  CB  ASN C 142     4648   3138   8515  -2628   -978   -222       C  
ATOM   3998  CG  ASN C 142       6.679  18.195 322.753  1.00 77.55           C  
ANISOU 3998  CG  ASN C 142     8815   7655  12998  -2694  -1013   -290       C  
ATOM   3999  OD1 ASN C 142       6.542  17.812 321.584  1.00 76.70           O  
ANISOU 3999  OD1 ASN C 142     8738   7493  12910  -2648  -1161   -360       O  
ATOM   4000  ND2 ASN C 142       5.741  18.913 323.371  1.00 69.77           N  
ANISOU 4000  ND2 ASN C 142     7603   6840  12068  -2795   -883   -273       N  
ATOM   4001  N   LEU C 143      11.039  17.854 324.099  1.00 42.46           N  
ANISOU 4001  N   LEU C 143     4963   2887   8282  -2239   -990   -156       N  
ATOM   4002  CA  LEU C 143      12.219  17.413 324.830  1.00 42.54           C  
ANISOU 4002  CA  LEU C 143     5171   2776   8217  -2168   -997    -98       C  
ATOM   4003  C   LEU C 143      13.142  18.602 325.182  1.00 42.23           C  
ANISOU 4003  C   LEU C 143     5046   2842   8158  -1987   -913    -83       C  
ATOM   4004  O   LEU C 143      13.708  18.619 326.275  1.00 41.28           O  
ANISOU 4004  O   LEU C 143     5005   2691   7989  -1995   -866    -21       O  
ATOM   4005  CB  LEU C 143      12.968  16.358 323.997  1.00 43.82           C  
ANISOU 4005  CB  LEU C 143     5547   2760   8343  -2063  -1148   -128       C  
ATOM   4006  CG  LEU C 143      14.264  15.825 324.570  1.00 49.69           C  
ANISOU 4006  CG  LEU C 143     6495   3371   9013  -1951  -1183    -80       C  
ATOM   4007  CD1 LEU C 143      13.992  15.098 325.860  1.00 51.66           C  
ANISOU 4007  CD1 LEU C 143     6885   3523   9222  -2146  -1159     -1       C  
ATOM   4008  CD2 LEU C 143      15.006  14.911 323.567  1.00 53.41           C  
ANISOU 4008  CD2 LEU C 143     7153   3690   9451  -1798  -1325   -124       C  
ATOM   4009  N   ALA C 144      13.283  19.584 324.271  1.00 36.54           N  
ANISOU 4009  N   ALA C 144     4175   2237   7471  -1831   -900   -138       N  
ATOM   4010  CA  ALA C 144      14.109  20.778 324.498  1.00 34.50           C  
ANISOU 4010  CA  ALA C 144     3827   2077   7203  -1673   -824   -127       C  
ATOM   4011  C   ALA C 144      13.437  21.759 325.474  1.00 36.04           C  
ANISOU 4011  C   ALA C 144     3880   2404   7408  -1767   -692    -98       C  
ATOM   4012  O   ALA C 144      14.148  22.432 326.218  1.00 34.24           O  
ANISOU 4012  O   ALA C 144     3654   2205   7150  -1702   -635    -62       O  
ATOM   4013  CB  ALA C 144      14.407  21.477 323.183  1.00 34.55           C  
ANISOU 4013  CB  ALA C 144     3738   2153   7236  -1494   -846   -190       C  
ATOM   4014  N   ILE C 145      12.074  21.837 325.468  1.00 32.57           N  
ANISOU 4014  N   ILE C 145     3320   2079   6978  -1868   -643   -110       N  
ATOM   4015  CA  ILE C 145      11.266  22.680 326.375  1.00 31.80           C  
ANISOU 4015  CA  ILE C 145     3092   2149   6840  -1889   -502    -83       C  
ATOM   4016  C   ILE C 145      11.504  22.193 327.815  1.00 33.46           C  
ANISOU 4016  C   ILE C 145     3430   2221   7062  -2119   -455    -15       C  
ATOM   4017  O   ILE C 145      11.643  23.019 328.721  1.00 32.60           O  
ANISOU 4017  O   ILE C 145     3289   2188   6907  -2088   -355     16       O  
ATOM   4018  CB  ILE C 145       9.750  22.683 325.980  1.00 34.94           C  
ANISOU 4018  CB  ILE C 145     3306   2579   7389  -2141   -488   -134       C  
ATOM   4019  CG1 ILE C 145       9.557  23.362 324.635  1.00 34.32           C  
ANISOU 4019  CG1 ILE C 145     3097   2582   7359  -1998   -544   -212       C  
ATOM   4020  CG2 ILE C 145       8.858  23.371 327.014  1.00 35.70           C  
ANISOU 4020  CG2 ILE C 145     3265   2809   7490  -2246   -334   -106       C  
ATOM   4021  CD1 ILE C 145       8.277  23.213 324.093  1.00 41.24           C  
ANISOU 4021  CD1 ILE C 145     3830   3533   8307  -2101   -569   -258       C  
ATOM   4022  N   GLN C 146      11.612  20.856 328.001  1.00 30.36           N  
ANISOU 4022  N   GLN C 146     3220   1857   6460  -1964   -515     38       N  
ATOM   4023  CA  GLN C 146      11.892  20.223 329.284  1.00 30.59           C  
ANISOU 4023  CA  GLN C 146     3414   1815   6393  -2048   -488    113       C  
ATOM   4024  C   GLN C 146      13.192  20.797 329.887  1.00 29.88           C  
ANISOU 4024  C   GLN C 146     3397   1683   6273  -1938   -492    136       C  
ATOM   4025  O   GLN C 146      13.207  21.143 331.062  1.00 29.60           O  
ANISOU 4025  O   GLN C 146     3400   1691   6154  -1956   -411    182       O  
ATOM   4026  CB  GLN C 146      11.972  18.691 329.116  1.00 33.09           C  
ANISOU 4026  CB  GLN C 146     3930   1881   6763  -2250   -605    129       C  
ATOM   4027  CG  GLN C 146      12.121  17.928 330.427  1.00 55.83           C  
ANISOU 4027  CG  GLN C 146     7032   4487   9695  -2571   -584    204       C  
ATOM   4028  CD  GLN C 146      11.990  16.445 330.208  1.00 88.31           C  
ANISOU 4028  CD  GLN C 146    11344   8414  13795  -2692   -692    222       C  
ATOM   4029  OE1 GLN C 146      11.696  15.988 329.098  1.00 86.27           O  
ANISOU 4029  OE1 GLN C 146    11062   8122  13595  -2691   -786    166       O  
ATOM   4030  NE2 GLN C 146      12.218  15.660 331.260  1.00 87.72           N  
ANISOU 4030  NE2 GLN C 146    11492   8202  13634  -2793   -688    301       N  
ATOM   4031  N   VAL C 147      14.246  20.942 329.070  1.00 25.56           N  
ANISOU 4031  N   VAL C 147     2824   1336   5551  -1493   -569    126       N  
ATOM   4032  CA  VAL C 147      15.555  21.478 329.470  1.00 23.91           C  
ANISOU 4032  CA  VAL C 147     2633   1177   5273  -1303   -590    148       C  
ATOM   4033  C   VAL C 147      15.450  23.001 329.709  1.00 25.73           C  
ANISOU 4033  C   VAL C 147     2744   1370   5660  -1424   -496    117       C  
ATOM   4034  O   VAL C 147      15.866  23.484 330.768  1.00 25.85           O  
ANISOU 4034  O   VAL C 147     2802   1390   5628  -1427   -462    150       O  
ATOM   4035  CB  VAL C 147      16.642  21.133 328.407  1.00 25.52           C  
ANISOU 4035  CB  VAL C 147     2890   1161   5645  -1323   -710    110       C  
ATOM   4036  CG1 VAL C 147      17.986  21.786 328.729  1.00 24.18           C  
ANISOU 4036  CG1 VAL C 147     2711   1032   5445  -1158   -731    130       C  
ATOM   4037  CG2 VAL C 147      16.802  19.620 328.238  1.00 26.40           C  
ANISOU 4037  CG2 VAL C 147     3179   1115   5735  -1384   -818    121       C  
ATOM   4038  N   LEU C 148      14.899  23.740 328.717  1.00 21.83           N  
ANISOU 4038  N   LEU C 148     2084   1161   5049  -1114   -447     82       N  
ATOM   4039  CA  LEU C 148      14.710  25.190 328.736  1.00 20.24           C  
ANISOU 4039  CA  LEU C 148     1767   1102   4821   -972   -357     59       C  
ATOM   4040  C   LEU C 148      13.911  25.672 329.941  1.00 24.51           C  
ANISOU 4040  C   LEU C 148     2290   1497   5524  -1375   -257     59       C  
ATOM   4041  O   LEU C 148      14.301  26.662 330.550  1.00 24.23           O  
ANISOU 4041  O   LEU C 148     2237   1498   5469  -1329   -209     63       O  
ATOM   4042  CB  LEU C 148      14.004  25.678 327.455  1.00 19.58           C  
ANISOU 4042  CB  LEU C 148     1568   1082   4790   -881   -343      5       C  
ATOM   4043  CG  LEU C 148      14.781  25.686 326.135  1.00 21.62           C  
ANISOU 4043  CG  LEU C 148     1791   1173   5250   -974   -435    -39       C  
ATOM   4044  CD1 LEU C 148      13.890  26.133 325.004  1.00 21.42           C  
ANISOU 4044  CD1 LEU C 148     1668   1187   5283   -954   -436    -97       C  
ATOM   4045  CD2 LEU C 148      16.007  26.584 326.193  1.00 21.71           C  
ANISOU 4045  CD2 LEU C 148     1772   1153   5323   -931   -427    -38       C  
ATOM   4046  N   ASN C 149      12.791  25.004 330.274  1.00 23.98           N  
ANISOU 4046  N   ASN C 149     2242   1506   5364  -1406   -210     72       N  
ATOM   4047  CA  ASN C 149      11.925  25.411 331.381  1.00 24.77           C  
ANISOU 4047  CA  ASN C 149     2324   1647   5440  -1542    -84     86       C  
ATOM   4048  C   ASN C 149      12.543  25.152 332.747  1.00 28.05           C  
ANISOU 4048  C   ASN C 149     2884   1834   5939  -1861    -68    151       C  
ATOM   4049  O   ASN C 149      12.142  25.800 333.715  1.00 27.72           O  
ANISOU 4049  O   ASN C 149     2843   1864   5824  -1876     42    166       O  
ATOM   4050  CB  ASN C 149      10.567  24.731 331.295  1.00 27.06           C  
ANISOU 4050  CB  ASN C 149     2542   1913   5825  -1793    -34     81       C  
ATOM   4051  CG  ASN C 149       9.595  25.404 330.361  1.00 50.83           C  
ANISOU 4051  CG  ASN C 149     5249   4843   9220  -2200     -2     18       C  
ATOM   4052  OD1 ASN C 149       9.844  26.478 329.796  1.00 39.71           O  
ANISOU 4052  OD1 ASN C 149     3744   3510   7833  -2042     -7    -28       O  
ATOM   4053  ND2 ASN C 149       8.442  24.789 330.197  1.00 51.51           N  
ANISOU 4053  ND2 ASN C 149     5241   4971   9360  -2355     26     13       N  
ATOM   4054  N   GLN C 150      13.502  24.210 332.835  1.00 26.72           N  
ANISOU 4054  N   GLN C 150     2876   1620   5655  -1729   -184    184       N  
ATOM   4055  CA  GLN C 150      14.181  23.877 334.089  1.00 27.59           C  
ANISOU 4055  CA  GLN C 150     3173   1606   5703  -1817   -200    244       C  
ATOM   4056  C   GLN C 150      14.937  25.074 334.592  1.00 29.58           C  
ANISOU 4056  C   GLN C 150     3428   1719   6092  -1926   -184    246       C  
ATOM   4057  O   GLN C 150      14.922  25.369 335.793  1.00 29.79           O  
ANISOU 4057  O   GLN C 150     3559   1725   6033  -1977   -129    285       O  
ATOM   4058  CB  GLN C 150      15.140  22.697 333.910  1.00 28.97           C  
ANISOU 4058  CB  GLN C 150     3521   1556   5932  -1886   -344    275       C  
ATOM   4059  CG  GLN C 150      14.479  21.342 334.108  1.00 47.99           C  
ANISOU 4059  CG  GLN C 150     6094   3683   8459  -2254   -346    320       C  
ATOM   4060  CD  GLN C 150      15.494  20.231 334.195  1.00 71.24           C  
ANISOU 4060  CD  GLN C 150     9262   6444  11363  -2213   -491    352       C  
ATOM   4061  OE1 GLN C 150      15.330  19.281 334.968  1.00 70.49           O  
ANISOU 4061  OE1 GLN C 150     9364   6228  11191  -2334   -496    413       O  
ATOM   4062  NE2 GLN C 150      16.569  20.319 333.411  1.00 61.27           N  
ANISOU 4062  NE2 GLN C 150     7980   5154  10145  -2035   -607    313       N  
ATOM   4063  N   ASP C 151      15.562  25.801 333.657  1.00 25.75           N  
ANISOU 4063  N   ASP C 151     2803   1468   5512  -1551   -234    195       N  
ATOM   4064  CA  ASP C 151      16.294  26.986 334.034  1.00 24.30           C  
ANISOU 4064  CA  ASP C 151     2592   1367   5275  -1396   -233    186       C  
ATOM   4065  C   ASP C 151      15.248  28.046 334.308  1.00 26.46           C  
ANISOU 4065  C   ASP C 151     2770   1639   5644  -1568    -94    160       C  
ATOM   4066  O   ASP C 151      14.600  28.574 333.404  1.00 27.34           O  
ANISOU 4066  O   ASP C 151     2725   1808   5854  -1574    -50    113       O  
ATOM   4067  CB  ASP C 151      17.229  27.316 332.856  1.00 24.57           C  
ANISOU 4067  CB  ASP C 151     2541   1341   5454  -1330   -319    157       C  
ATOM   4068  CG  ASP C 151      17.756  28.720 332.671  1.00 36.74           C  
ANISOU 4068  CG  ASP C 151     4015   2751   7193  -1464   -312    131       C  
ATOM   4069  OD1 ASP C 151      17.838  29.469 333.675  1.00 38.59           O  
ANISOU 4069  OD1 ASP C 151     4308   2992   7363  -1478   -281    148       O  
ATOM   4070  OD2 ASP C 151      18.220  29.027 331.550  1.00 42.56           O  
ANISOU 4070  OD2 ASP C 151     4650   3517   8003  -1361   -347    100       O  
ATOM   4071  N   LYS C 152      15.090  28.356 335.601  1.00 22.75           N  
ANISOU 4071  N   LYS C 152     2391   1379   4873  -1336    -36    175       N  
ATOM   4072  CA  LYS C 152      14.143  29.356 336.073  1.00 22.23           C  
ANISOU 4072  CA  LYS C 152     2270   1413   4765  -1329     99    144       C  
ATOM   4073  C   LYS C 152      14.718  30.772 335.965  1.00 23.56           C  
ANISOU 4073  C   LYS C 152     2384   1536   5033  -1328     95    119       C  
ATOM   4074  O   LYS C 152      13.961  31.706 335.702  1.00 23.15           O  
ANISOU 4074  O   LYS C 152     2230   1568   4998  -1289    186     76       O  
ATOM   4075  CB  LYS C 152      13.714  29.060 337.514  1.00 24.87           C  
ANISOU 4075  CB  LYS C 152     2743   1588   5116  -1643    197    201       C  
ATOM   4076  N   TRP C 153      16.043  30.939 336.168  1.00 20.67           N  
ANISOU 4076  N   TRP C 153     2080   1302   4473  -1004    -28    128       N  
ATOM   4077  CA  TRP C 153      16.713  32.250 336.108  1.00 19.57           C  
ANISOU 4077  CA  TRP C 153     1900   1228   4305   -846    -53    106       C  
ATOM   4078  C   TRP C 153      16.416  32.977 334.788  1.00 21.02           C  
ANISOU 4078  C   TRP C 153     1939   1364   4684   -887    -25     64       C  
ATOM   4079  O   TRP C 153      16.037  34.147 334.828  1.00 21.09           O  
ANISOU 4079  O   TRP C 153     1908   1399   4705   -868     38     30       O  
ATOM   4080  CB  TRP C 153      18.231  32.121 336.316  1.00 18.32           C  
ANISOU 4080  CB  TRP C 153     1782   1104   4075   -709   -195    143       C  
ATOM   4081  CG  TRP C 153      18.912  33.422 336.618  1.00 18.43           C  
ANISOU 4081  CG  TRP C 153     1794   1105   4104   -682   -223    133       C  
ATOM   4082  CD1 TRP C 153      19.172  33.945 337.851  1.00 20.78           C  
ANISOU 4082  CD1 TRP C 153     2234   1223   4438   -894   -236    143       C  
ATOM   4083  CD2 TRP C 153      19.416  34.369 335.666  1.00 17.61           C  
ANISOU 4083  CD2 TRP C 153     1577   1057   4057   -542   -244    115       C  
ATOM   4084  NE1 TRP C 153      19.784  35.172 337.729  1.00 19.83           N  
ANISOU 4084  NE1 TRP C 153     2069   1158   4308   -783   -274    126       N  
ATOM   4085  CE2 TRP C 153      19.960  35.452 336.399  1.00 20.15           C  
ANISOU 4085  CE2 TRP C 153     1973   1191   4492   -745   -277    109       C  
ATOM   4086  CE3 TRP C 153      19.454  34.415 334.260  1.00 17.73           C  
ANISOU 4086  CE3 TRP C 153     1479   1065   4193   -488   -241     98       C  
ATOM   4087  CZ2 TRP C 153      20.566  36.547 335.775  1.00 18.97           C  
ANISOU 4087  CZ2 TRP C 153     1739   1111   4357   -606   -305     97       C  
ATOM   4088  CZ3 TRP C 153      20.047  35.505 333.645  1.00 18.11           C  
ANISOU 4088  CZ3 TRP C 153     1464   1082   4335   -462   -259     85       C  
ATOM   4089  CH2 TRP C 153      20.588  36.558 334.399  1.00 18.59           C  
ANISOU 4089  CH2 TRP C 153     1570   1102   4393   -512   -289     86       C  
ATOM   4090  N   THR C 154      16.552  32.282 333.636  1.00 17.04           N  
ANISOU 4090  N   THR C 154     1380   1052   4042   -545    -73     61       N  
ATOM   4091  CA  THR C 154      16.271  32.836 332.309  1.00 15.58           C  
ANISOU 4091  CA  THR C 154     1103    926   3891   -380    -54     23       C  
ATOM   4092  C   THR C 154      14.766  33.084 332.171  1.00 20.15           C  
ANISOU 4092  C   THR C 154     1586   1357   4712   -764     52    -22       C  
ATOM   4093  O   THR C 154      14.373  34.146 331.686  1.00 19.54           O  
ANISOU 4093  O   THR C 154     1448   1322   4655   -681     95    -63       O  
ATOM   4094  CB  THR C 154      16.803  31.905 331.235  1.00 13.88           C  
ANISOU 4094  CB  THR C 154      854    682   3739   -343   -130     40       C  
ATOM   4095  OG1 THR C 154      18.202  31.722 331.435  1.00 13.23           O  
ANISOU 4095  OG1 THR C 154      788    600   3638   -282   -221     81       O  
ATOM   4096  CG2 THR C 154      16.540  32.402 329.831  1.00 10.31           C  
ANISOU 4096  CG2 THR C 154      395    391   3133      0   -104     11       C  
ATOM   4097  N   ARG C 155      13.925  32.125 332.637  1.00 19.42           N  
ANISOU 4097  N   ARG C 155     1545   1329   4505   -748     92    -13       N  
ATOM   4098  CA  ARG C 155      12.462  32.251 332.599  1.00 19.96           C  
ANISOU 4098  CA  ARG C 155     1544   1435   4604   -829    194    -50       C  
ATOM   4099  C   ARG C 155      12.001  33.512 333.343  1.00 24.02           C  
ANISOU 4099  C   ARG C 155     1946   1863   5316  -1168    310    -60       C  
ATOM   4100  O   ARG C 155      10.979  34.095 332.978  1.00 24.18           O  
ANISOU 4100  O   ARG C 155     1849   1963   5377  -1156    386   -104       O  
ATOM   4101  CB  ARG C 155      11.775  31.013 333.204  1.00 18.95           C  
ANISOU 4101  CB  ARG C 155     1474   1326   4397   -908    222    -25       C  
ATOM   4102  CG  ARG C 155      11.799  29.779 332.323  1.00 21.18           C  
ANISOU 4102  CG  ARG C 155     1689   1474   4885  -1171    147     -1       C  
ATOM   4103  CD  ARG C 155      10.646  28.836 332.607  1.00 25.10           C  
ANISOU 4103  CD  ARG C 155     2104   1882   5549  -1577    214     21       C  
ATOM   4104  NE  ARG C 155      10.619  28.362 333.991  1.00 29.50           N  
ANISOU 4104  NE  ARG C 155     2721   2245   6245  -2042    298    103       N  
ATOM   4105  CZ  ARG C 155       9.526  28.288 334.745  1.00 44.80           C  
ANISOU 4105  CZ  ARG C 155     4616   4255   8149  -2160    441    124       C  
ATOM   4106  NH1 ARG C 155       8.348  28.662 334.259  1.00 30.19           N  
ANISOU 4106  NH1 ARG C 155     2572   2564   6335  -2126    520     77       N  
ATOM   4107  NH2 ARG C 155       9.601  27.844 335.992  1.00 35.50           N  
ANISOU 4107  NH2 ARG C 155     3607   3013   6869  -2258    503    190       N  
ATOM   4108  N   GLU C 156      12.770  33.929 334.372  1.00 21.87           N  
ANISOU 4108  N   GLU C 156     1836   1614   4862  -1007    294    -42       N  
ATOM   4109  CA  GLU C 156      12.486  35.095 335.198  1.00 22.20           C  
ANISOU 4109  CA  GLU C 156     1893   1660   4881  -1039    380    -60       C  
ATOM   4110  C   GLU C 156      13.019  36.387 334.535  1.00 23.29           C  
ANISOU 4110  C   GLU C 156     1955   1740   5155  -1055    346    -87       C  
ATOM   4111  O   GLU C 156      12.322  37.411 334.535  1.00 22.30           O  
ANISOU 4111  O   GLU C 156     1782   1683   5007   -975    422   -131       O  
ATOM   4112  CB  GLU C 156      13.086  34.893 336.599  1.00 23.79           C  
ANISOU 4112  CB  GLU C 156     2246   1738   5055  -1226    382     -5       C  
ATOM   4113  CG  GLU C 156      12.422  35.715 337.689  1.00 36.25           C  
ANISOU 4113  CG  GLU C 156     3851   3238   6683  -1454    531      6       C  
ATOM   4114  CD  GLU C 156      11.138  35.123 338.231  1.00 63.68           C  
ANISOU 4114  CD  GLU C 156     7282   6794  10120  -1552    687     23       C  
ATOM   4115  OE1 GLU C 156      10.051  35.567 337.796  1.00 68.92           O  
ANISOU 4115  OE1 GLU C 156     7777   7584  10824  -1519    792    -18       O  
ATOM   4116  OE2 GLU C 156      11.219  34.223 339.099  1.00 56.17           O  
ANISOU 4116  OE2 GLU C 156     6462   5779   9099  -1663    704     80       O  
ATOM   4117  N   THR C 157      14.241  36.320 333.965  1.00 20.18           N  
ANISOU 4117  N   THR C 157     1636   1416   4615   -730    217    -78       N  
ATOM   4118  CA  THR C 157      14.925  37.416 333.270  1.00 19.14           C  
ANISOU 4118  CA  THR C 157     1479   1300   4492   -578    172    -96       C  
ATOM   4119  C   THR C 157      14.137  37.826 332.016  1.00 22.08           C  
ANISOU 4119  C   THR C 157     1681   1608   5099   -751    211   -139       C  
ATOM   4120  O   THR C 157      13.951  39.023 331.817  1.00 22.33           O  
ANISOU 4120  O   THR C 157     1680   1643   5162   -727    244   -171       O  
ATOM   4121  CB  THR C 157      16.365  37.010 332.947  1.00 23.43           C  
ANISOU 4121  CB  THR C 157     1988   1581   5332   -944     52    -53       C  
ATOM   4122  OG1 THR C 157      17.005  36.631 334.165  1.00 23.70           O  
ANISOU 4122  OG1 THR C 157     2153   1549   5304  -1012      6    -13       O  
ATOM   4123  CG2 THR C 157      17.160  38.121 332.294  1.00 22.36           C  
ANISOU 4123  CG2 THR C 157     1834   1467   5195   -795     10    -63       C  
ATOM   4124  N   VAL C 158      13.653  36.855 331.196  1.00 19.47           N  
ANISOU 4124  N   VAL C 158     1369   1377   4653   -514    193   -146       N  
ATOM   4125  CA  VAL C 158      12.835  37.114 329.993  1.00 19.12           C  
ANISOU 4125  CA  VAL C 158     1251   1355   4660   -439    208   -192       C  
ATOM   4126  C   VAL C 158      11.512  37.757 330.424  1.00 23.37           C  
ANISOU 4126  C   VAL C 158     1556   1900   5425   -807    320   -230       C  
ATOM   4127  O   VAL C 158      11.068  38.717 329.792  1.00 23.28           O  
ANISOU 4127  O   VAL C 158     1477   1926   5443   -727    337   -273       O  
ATOM   4128  CB  VAL C 158      12.580  35.833 329.137  1.00 21.92           C  
ANISOU 4128  CB  VAL C 158     1472   1660   5194   -669    162   -186       C  
ATOM   4129  CG1 VAL C 158      11.605  36.102 327.989  1.00 21.68           C  
ANISOU 4129  CG1 VAL C 158     1353   1674   5210   -609    170   -239       C  
ATOM   4130  CG2 VAL C 158      13.879  35.252 328.597  1.00 21.33           C  
ANISOU 4130  CG2 VAL C 158     1459   1536   5110   -585     67   -149       C  
ATOM   4131  N   GLN C 159      10.906  37.242 331.522  1.00 22.06           N  
ANISOU 4131  N   GLN C 159     1475   1778   5130   -787    389   -220       N  
ATOM   4132  CA  GLN C 159       9.629  37.710 332.058  1.00 22.72           C  
ANISOU 4132  CA  GLN C 159     1453   1942   5237   -867    513   -250       C  
ATOM   4133  C   GLN C 159       9.641  39.198 332.421  1.00 24.72           C  
ANISOU 4133  C   GLN C 159     1594   2207   5590   -973    584   -265       C  
ATOM   4134  O   GLN C 159       8.693  39.875 332.030  1.00 25.73           O  
ANISOU 4134  O   GLN C 159     1604   2436   5736   -884    641   -314       O  
ATOM   4135  CB  GLN C 159       9.187  36.884 333.273  1.00 24.84           C  
ANISOU 4135  CB  GLN C 159     1690   2218   5532  -1122    611   -202       C  
ATOM   4136  CG  GLN C 159       7.662  36.823 333.449  1.00 39.25           C  
ANISOU 4136  CG  GLN C 159     3282   4179   7454  -1277    758   -214       C  
ATOM   4137  CD  GLN C 159       7.183  36.092 334.694  1.00 55.27           C  
ANISOU 4137  CD  GLN C 159     5373   6216   9412  -1413    875   -164       C  
ATOM   4138  OE1 GLN C 159       7.928  35.379 335.394  1.00 46.32           O  
ANISOU 4138  OE1 GLN C 159     4403   4971   8226  -1508    840   -107       O  
ATOM   4139  NE2 GLN C 159       5.902  36.257 334.994  1.00 48.30           N  
ANISOU 4139  NE2 GLN C 159     4358   5469   8523  -1422   1022   -182       N  
ATOM   4140  N   TRP C 160      10.665  39.719 333.147  1.00 20.47           N  
ANISOU 4140  N   TRP C 160     1335   1595   4849   -762    534   -256       N  
ATOM   4141  CA  TRP C 160      10.617  41.147 333.487  1.00 19.77           C  
ANISOU 4141  CA  TRP C 160     1279   1501   4730   -698    575   -287       C  
ATOM   4142  C   TRP C 160      11.074  42.013 332.343  1.00 20.79           C  
ANISOU 4142  C   TRP C 160     1304   1589   5007   -725    512   -303       C  
ATOM   4143  O   TRP C 160      10.649  43.163 332.273  1.00 21.33           O  
ANISOU 4143  O   TRP C 160     1376   1687   5042   -610    551   -345       O  
ATOM   4144  CB  TRP C 160      11.342  41.534 334.792  1.00 18.95           C  
ANISOU 4144  CB  TRP C 160     1358   1335   4508   -703    574   -262       C  
ATOM   4145  CG  TRP C 160      12.798  41.211 334.881  1.00 19.33           C  
ANISOU 4145  CG  TRP C 160     1500   1286   4559   -745    449   -214       C  
ATOM   4146  CD1 TRP C 160      13.360  40.180 335.570  1.00 21.92           C  
ANISOU 4146  CD1 TRP C 160     1886   1503   4939   -966    414   -158       C  
ATOM   4147  CD2 TRP C 160      13.889  41.999 334.379  1.00 18.72           C  
ANISOU 4147  CD2 TRP C 160     1465   1168   4481   -649    349   -211       C  
ATOM   4148  NE1 TRP C 160      14.731  40.258 335.508  1.00 21.28           N  
ANISOU 4148  NE1 TRP C 160     1888   1364   4834   -905    283   -132       N  
ATOM   4149  CE2 TRP C 160      15.083  41.355 334.766  1.00 21.73           C  
ANISOU 4149  CE2 TRP C 160     1912   1380   4966   -868    250   -158       C  
ATOM   4150  CE3 TRP C 160      13.975  43.158 333.588  1.00 18.96           C  
ANISOU 4150  CE3 TRP C 160     1462   1160   4583   -613    335   -241       C  
ATOM   4151  CZ2 TRP C 160      16.342  41.826 334.389  1.00 20.67           C  
ANISOU 4151  CZ2 TRP C 160     1810   1225   4818   -772    139   -140       C  
ATOM   4152  CZ3 TRP C 160      15.222  43.623 333.220  1.00 19.44           C  
ANISOU 4152  CZ3 TRP C 160     1567   1136   4683   -617    232   -217       C  
ATOM   4153  CH2 TRP C 160      16.386  42.961 333.615  1.00 20.01           C  
ANISOU 4153  CH2 TRP C 160     1693   1152   4757   -680    139   -167       C  
ATOM   4154  N   LEU C 161      11.901  41.484 331.439  1.00 17.40           N  
ANISOU 4154  N   LEU C 161     1015   1151   4446   -444    396   -292       N  
ATOM   4155  CA  LEU C 161      12.360  42.258 330.292  1.00 16.96           C  
ANISOU 4155  CA  LEU C 161      944   1065   4434   -344    340   -304       C  
ATOM   4156  C   LEU C 161      11.208  42.582 329.332  1.00 21.22           C  
ANISOU 4156  C   LEU C 161     1180   1665   5219   -555    382   -350       C  
ATOM   4157  O   LEU C 161      11.187  43.675 328.766  1.00 20.82           O  
ANISOU 4157  O   LEU C 161     1143   1607   5159   -438    372   -378       O  
ATOM   4158  CB  LEU C 161      13.468  41.517 329.547  1.00 16.69           C  
ANISOU 4158  CB  LEU C 161      932   1002   4406   -294    248   -260       C  
ATOM   4159  CG  LEU C 161      14.888  41.798 330.018  1.00 20.38           C  
ANISOU 4159  CG  LEU C 161     1381   1330   5031   -580    185   -213       C  
ATOM   4160  CD1 LEU C 161      15.836  40.707 329.565  1.00 20.07           C  
ANISOU 4160  CD1 LEU C 161     1345   1274   5006   -565    110   -170       C  
ATOM   4161  CD2 LEU C 161      15.387  43.155 329.514  1.00 23.74           C  
ANISOU 4161  CD2 LEU C 161     1809   1658   5553   -639    163   -224       C  
ATOM   4162  N   LEU C 162      10.240  41.647 329.180  1.00 20.03           N  
ANISOU 4162  N   LEU C 162     1017   1577   5017   -492    404   -369       N  
ATOM   4163  CA  LEU C 162       9.089  41.797 328.288  1.00 20.34           C  
ANISOU 4163  CA  LEU C 162      913   1704   5111   -441    415   -421       C  
ATOM   4164  C   LEU C 162       7.924  42.574 328.932  1.00 26.46           C  
ANISOU 4164  C   LEU C 162     1501   2629   5923   -454    533   -460       C  
ATOM   4165  O   LEU C 162       7.281  43.367 328.239  1.00 26.69           O  
ANISOU 4165  O   LEU C 162     1459   2718   5965   -321    531   -509       O  
ATOM   4166  CB  LEU C 162       8.583  40.429 327.793  1.00 20.66           C  
ANISOU 4166  CB  LEU C 162      896   1770   5184   -495    382   -419       C  
ATOM   4167  CG  LEU C 162       9.487  39.598 326.855  1.00 23.45           C  
ANISOU 4167  CG  LEU C 162     1098   2103   5708   -669    287   -386       C  
ATOM   4168  CD1 LEU C 162       8.879  38.229 326.611  1.00 24.49           C  
ANISOU 4168  CD1 LEU C 162     1154   2263   5889   -778    262   -384       C  
ATOM   4169  CD2 LEU C 162       9.712  40.274 325.499  1.00 23.95           C  
ANISOU 4169  CD2 LEU C 162     1152   2154   5795   -537    219   -414       C  
ATOM   4170  N   ASN C 163       7.641  42.338 330.234  1.00 24.72           N  
ANISOU 4170  N   ASN C 163     1314   2432   5647   -530    629   -442       N  
ATOM   4171  CA  ASN C 163       6.537  42.982 330.969  1.00 25.99           C  
ANISOU 4171  CA  ASN C 163     1418   2700   5757   -462    755   -479       C  
ATOM   4172  C   ASN C 163       6.913  44.384 331.473  1.00 28.99           C  
ANISOU 4172  C   ASN C 163     1953   3022   6039   -332    779   -499       C  
ATOM   4173  O   ASN C 163       6.030  45.233 331.594  1.00 29.26           O  
ANISOU 4173  O   ASN C 163     1938   3141   6039   -205    856   -549       O  
ATOM   4174  CB  ASN C 163       6.074  42.104 332.153  1.00 28.69           C  
ANISOU 4174  CB  ASN C 163     1745   3088   6068   -603    862   -445       C  
ATOM   4175  CG  ASN C 163       4.834  42.594 332.887  1.00 56.62           C  
ANISOU 4175  CG  ASN C 163     5193   6759   9561   -543   1018   -478       C  
ATOM   4176  OD1 ASN C 163       3.707  42.147 332.636  1.00 52.95           O  
ANISOU 4176  OD1 ASN C 163     4520   6433   9166   -556   1073   -503       O  
ATOM   4177  ND2 ASN C 163       5.016  43.497 333.842  1.00 48.90           N  
ANISOU 4177  ND2 ASN C 163     4370   5746   8465   -477   1091   -481       N  
ATOM   4178  N   GLY C 164       8.189  44.607 331.781  1.00 24.72           N  
ANISOU 4178  N   GLY C 164     1595   2341   5457   -364    711   -463       N  
ATOM   4179  CA  GLY C 164       8.644  45.885 332.319  1.00 25.07           C  
ANISOU 4179  CA  GLY C 164     1811   2306   5409   -268    714   -479       C  
ATOM   4180  C   GLY C 164       9.526  46.756 331.446  1.00 28.53           C  
ANISOU 4180  C   GLY C 164     2336   2640   5866   -198    608   -479       C  
ATOM   4181  O   GLY C 164       9.195  47.922 331.199  1.00 27.89           O  
ANISOU 4181  O   GLY C 164     2294   2554   5748    -57    617   -522       O  
ATOM   4182  N   THR C 165      10.667  46.207 331.002  1.00 25.15           N  
ANISOU 4182  N   THR C 165     1942   2123   5490   -293    512   -430       N  
ATOM   4183  CA  THR C 165      11.671  46.929 330.224  1.00 25.09           C  
ANISOU 4183  CA  THR C 165     2014   2011   5506   -256    421   -414       C  
ATOM   4184  C   THR C 165      11.254  47.235 328.789  1.00 30.68           C  
ANISOU 4184  C   THR C 165     2628   2760   6270   -152    396   -441       C  
ATOM   4185  O   THR C 165      11.551  48.339 328.340  1.00 30.12           O  
ANISOU 4185  O   THR C 165     2645   2624   6177    -63    368   -449       O  
ATOM   4186  CB  THR C 165      12.999  46.193 330.221  1.00 33.65           C  
ANISOU 4186  CB  THR C 165     3137   3012   6638   -382    339   -353       C  
ATOM   4187  OG1 THR C 165      13.116  45.449 331.435  1.00 36.47           O  
ANISOU 4187  OG1 THR C 165     3549   3357   6950   -485    359   -330       O  
ATOM   4188  CG2 THR C 165      14.183  47.144 330.060  1.00 29.85           C  
ANISOU 4188  CG2 THR C 165     2773   2410   6159   -373    265   -328       C  
ATOM   4189  N   CYS C 166      10.633  46.285 328.054  1.00 29.34           N  
ANISOU 4189  N   CYS C 166     2299   2683   6167   -166    397   -451       N  
ATOM   4190  CA  CYS C 166      10.219  46.545 326.671  1.00 30.50           C  
ANISOU 4190  CA  CYS C 166     2365   2866   6357    -62    358   -479       C  
ATOM   4191  C   CYS C 166       9.237  47.730 326.605  1.00 30.65           C  
ANISOU 4191  C   CYS C 166     2382   2936   6327    103    399   -539       C  
ATOM   4192  O   CYS C 166       9.510  48.644 325.827  1.00 29.49           O  
ANISOU 4192  O   CYS C 166     2310   2729   6164    205    357   -545       O  
ATOM   4193  CB  CYS C 166       9.641  45.307 325.990  1.00 33.07           C  
ANISOU 4193  CB  CYS C 166     2532   3275   6757   -115    337   -486       C  
ATOM   4194  SG  CYS C 166       9.103  45.592 324.272  1.00 38.41           S  
ANISOU 4194  SG  CYS C 166     3130   3990   7475     19    268   -525       S  
ATOM   4195  N   PRO C 167       8.120  47.767 327.385  1.00 25.78           N  
ANISOU 4195  N   PRO C 167     1687   2426   5682    140    483   -581       N  
ATOM   4196  CA  PRO C 167       7.205  48.919 327.297  1.00 25.53           C  
ANISOU 4196  CA  PRO C 167     1654   2443   5604    324    517   -641       C  
ATOM   4197  C   PRO C 167       7.861  50.228 327.725  1.00 25.68           C  
ANISOU 4197  C   PRO C 167     1890   2334   5533    399    512   -639       C  
ATOM   4198  O   PRO C 167       7.650  51.245 327.066  1.00 24.86           O  
ANISOU 4198  O   PRO C 167     1842   2202   5401    550    485   -671       O  
ATOM   4199  CB  PRO C 167       6.062  48.534 328.237  1.00 28.72           C  
ANISOU 4199  CB  PRO C 167     1931   2985   5996    320    627   -674       C  
ATOM   4200  CG  PRO C 167       6.132  47.043 328.318  1.00 33.40           C  
ANISOU 4200  CG  PRO C 167     2412   3621   6659    138    629   -635       C  
ATOM   4201  CD  PRO C 167       7.598  46.777 328.348  1.00 27.68           C  
ANISOU 4201  CD  PRO C 167     1838   2750   5930     27    559   -573       C  
ATOM   4202  N   GLN C 168       8.696  50.184 328.789  1.00 20.05           N  
ANISOU 4202  N   GLN C 168     1311   1533   4775    290    525   -601       N  
ATOM   4203  CA  GLN C 168       9.458  51.323 329.313  1.00 18.90           C  
ANISOU 4203  CA  GLN C 168     1385   1247   4549    320    502   -594       C  
ATOM   4204  C   GLN C 168      10.327  51.912 328.214  1.00 20.76           C  
ANISOU 4204  C   GLN C 168     1701   1372   4815    340    412   -566       C  
ATOM   4205  O   GLN C 168      10.349  53.128 328.038  1.00 20.91           O  
ANISOU 4205  O   GLN C 168     1858   1312   4777    450    395   -586       O  
ATOM   4206  CB  GLN C 168      10.311  50.877 330.508  1.00 19.76           C  
ANISOU 4206  CB  GLN C 168     1595   1286   4626    169    502   -552       C  
ATOM   4207  CG  GLN C 168      11.286  51.926 331.039  1.00 35.20           C  
ANISOU 4207  CG  GLN C 168     3781   3085   6510    164    451   -541       C  
ATOM   4208  CD  GLN C 168      11.952  51.512 332.329  1.00 58.19           C  
ANISOU 4208  CD  GLN C 168     6791   5943   9374     38    447   -513       C  
ATOM   4209  OE1 GLN C 168      12.199  52.347 333.202  1.00 55.09           O  
ANISOU 4209  OE1 GLN C 168     6579   5472   8883     68    449   -533       O  
ATOM   4210  NE2 GLN C 168      12.270  50.221 332.484  1.00 49.73           N  
ANISOU 4210  NE2 GLN C 168     5628   4905   8364    -99    433   -468       N  
ATOM   4211  N   PHE C 169      10.997  51.038 327.448  1.00 16.33           N  
ANISOU 4211  N   PHE C 169     1055    841   4311    200    353   -507       N  
ATOM   4212  CA  PHE C 169      11.857  51.402 326.330  1.00 15.94           C  
ANISOU 4212  CA  PHE C 169     1017    826   4216    112    273   -438       C  
ATOM   4213  C   PHE C 169      11.040  51.995 325.187  1.00 17.99           C  
ANISOU 4213  C   PHE C 169     1295    965   4575    411    286   -523       C  
ATOM   4214  O   PHE C 169      11.392  53.078 324.735  1.00 18.41           O  
ANISOU 4214  O   PHE C 169     1477    960   4556    442    252   -503       O  
ATOM   4215  CB  PHE C 169      12.687  50.197 325.849  1.00 16.45           C  
ANISOU 4215  CB  PHE C 169      995    853   4403     44    248   -402       C  
ATOM   4216  CG  PHE C 169      13.689  50.476 324.750  1.00 17.62           C  
ANISOU 4216  CG  PHE C 169     1234    815   4645     96    208   -376       C  
ATOM   4217  CD1 PHE C 169      14.513  51.598 324.800  1.00 20.70           C  
ANISOU 4217  CD1 PHE C 169     1790   1061   5016    100    189   -351       C  
ATOM   4218  CD2 PHE C 169      13.842  49.592 323.688  1.00 20.53           C  
ANISOU 4218  CD2 PHE C 169     1513   1202   5085     90    186   -360       C  
ATOM   4219  CE1 PHE C 169      15.451  51.845 323.798  1.00 21.57           C  
ANISOU 4219  CE1 PHE C 169     1938   1097   5160     79    163   -297       C  
ATOM   4220  CE2 PHE C 169      14.789  49.835 322.686  1.00 23.31           C  
ANISOU 4220  CE2 PHE C 169     1915   1479   5461     86    162   -311       C  
ATOM   4221  CZ  PHE C 169      15.580  50.965 322.745  1.00 21.30           C  
ANISOU 4221  CZ  PHE C 169     1801   1112   5181     77    158   -276       C  
ATOM   4222  N   VAL C 170       9.943  51.327 324.758  1.00 15.59           N  
ANISOU 4222  N   VAL C 170      877    891   4154    231    252   -511       N  
ATOM   4223  CA  VAL C 170       9.053  51.782 323.675  1.00 16.52           C  
ANISOU 4223  CA  VAL C 170      968   1045   4264    390    224   -559       C  
ATOM   4224  C   VAL C 170       8.549  53.226 323.955  1.00 20.23           C  
ANISOU 4224  C   VAL C 170     1485   1399   4801    800    294   -654       C  
ATOM   4225  O   VAL C 170       8.713  54.095 323.091  1.00 20.06           O  
ANISOU 4225  O   VAL C 170     1581   1311   4729    882    245   -647       O  
ATOM   4226  CB  VAL C 170       7.882  50.792 323.441  1.00 20.12           C  
ANISOU 4226  CB  VAL C 170     1122   1589   4935    647    281   -655       C  
ATOM   4227  CG1 VAL C 170       6.833  51.366 322.488  1.00 20.90           C  
ANISOU 4227  CG1 VAL C 170     1179   1749   5013    815    233   -708       C  
ATOM   4228  CG2 VAL C 170       8.399  49.458 322.916  1.00 19.24           C  
ANISOU 4228  CG2 VAL C 170      928   1489   4895    492    243   -613       C  
ATOM   4229  N   SER C 171       8.012  53.478 325.180  1.00 17.71           N  
ANISOU 4229  N   SER C 171     1215   1193   4320    635    319   -641       N  
ATOM   4230  CA  SER C 171       7.536  54.780 325.647  1.00 18.49           C  
ANISOU 4230  CA  SER C 171     1433   1263   4329    803    346   -685       C  
ATOM   4231  C   SER C 171       8.617  55.839 325.480  1.00 22.23           C  
ANISOU 4231  C   SER C 171     2127   1461   4857    979    340   -699       C  
ATOM   4232  O   SER C 171       8.330  56.932 324.997  1.00 23.27           O  
ANISOU 4232  O   SER C 171     2382   1530   4928   1139    316   -728       O  
ATOM   4233  CB  SER C 171       7.109  54.697 327.105  1.00 21.47           C  
ANISOU 4233  CB  SER C 171     1773   1615   4770    961    482   -763       C  
ATOM   4234  OG  SER C 171       6.134  53.683 327.300  1.00 33.03           O  
ANISOU 4234  OG  SER C 171     3000   3258   6290    943    543   -790       O  
ATOM   4235  N   GLY C 172       9.854  55.479 325.812  1.00 19.08           N  
ANISOU 4235  N   GLY C 172     1779   1050   4420    704    300   -603       N  
ATOM   4236  CA  GLY C 172      11.022  56.340 325.666  1.00 19.17           C  
ANISOU 4236  CA  GLY C 172     1976    919   4389    647    251   -551       C  
ATOM   4237  C   GLY C 172      11.327  56.701 324.225  1.00 22.66           C  
ANISOU 4237  C   GLY C 172     2497   1184   4931    795    221   -555       C  
ATOM   4238  O   GLY C 172      11.413  57.887 323.902  1.00 22.75           O  
ANISOU 4238  O   GLY C 172     2687   1079   4876    890    197   -559       O  
ATOM   4239  N   LEU C 173      11.472  55.675 323.347  1.00 19.52           N  
ANISOU 4239  N   LEU C 173     1915    958   4542    650    195   -499       N  
ATOM   4240  CA  LEU C 173      11.732  55.809 321.906  1.00 19.57           C  
ANISOU 4240  CA  LEU C 173     1935    962   4538    667    156   -462       C  
ATOM   4241  C   LEU C 173      10.680  56.687 321.226  1.00 25.73           C  
ANISOU 4241  C   LEU C 173     2811   1618   5347   1004    153   -550       C  
ATOM   4242  O   LEU C 173      11.030  57.537 320.399  1.00 26.57           O  
ANISOU 4242  O   LEU C 173     3071   1613   5410   1068    125   -522       O  
ATOM   4243  CB  LEU C 173      11.747  54.436 321.211  1.00 18.58           C  
ANISOU 4243  CB  LEU C 173     1631    949   4480    574    144   -442       C  
ATOM   4244  CG  LEU C 173      12.935  53.513 321.446  1.00 21.58           C  
ANISOU 4244  CG  LEU C 173     1995   1164   5040    524    168   -412       C  
ATOM   4245  CD1 LEU C 173      12.667  52.159 320.861  1.00 21.18           C  
ANISOU 4245  CD1 LEU C 173     1764   1229   5054    489    160   -420       C  
ATOM   4246  CD2 LEU C 173      14.186  54.046 320.804  1.00 25.06           C  
ANISOU 4246  CD2 LEU C 173     2550   1483   5489    468    157   -338       C  
ATOM   4247  N   LEU C 174       9.389  56.475 321.582  1.00 22.43           N  
ANISOU 4247  N   LEU C 174     2265   1336   4923   1121    170   -626       N  
ATOM   4248  CA  LEU C 174       8.246  57.222 321.053  1.00 23.29           C  
ANISOU 4248  CA  LEU C 174     2389   1491   4969   1339    144   -689       C  
ATOM   4249  C   LEU C 174       8.325  58.704 321.399  1.00 31.10           C  
ANISOU 4249  C   LEU C 174     3620   2332   5863   1462    145   -704       C  
ATOM   4250  O   LEU C 174       7.920  59.531 320.588  1.00 31.30           O  
ANISOU 4250  O   LEU C 174     3753   2307   5831   1633    101   -725       O  
ATOM   4251  CB  LEU C 174       6.923  56.655 321.589  1.00 23.27           C  
ANISOU 4251  CB  LEU C 174     2171   1685   4984   1395    173   -760       C  
ATOM   4252  CG  LEU C 174       6.465  55.315 321.053  1.00 25.03           C  
ANISOU 4252  CG  LEU C 174     2151   2038   5322   1364    158   -775       C  
ATOM   4253  CD1 LEU C 174       5.363  54.781 321.893  1.00 25.24           C  
ANISOU 4253  CD1 LEU C 174     1971   2234   5386   1373    215   -831       C  
ATOM   4254  CD2 LEU C 174       6.020  55.417 319.623  1.00 26.18           C  
ANISOU 4254  CD2 LEU C 174     2281   2201   5466   1504     73   -795       C  
ATOM   4255  N   GLU C 175       8.828  59.031 322.606  1.00 30.35           N  
ANISOU 4255  N   GLU C 175     3627   2165   5740   1369    182   -694       N  
ATOM   4256  CA  GLU C 175       8.985  60.403 323.095  1.00 31.97           C  
ANISOU 4256  CA  GLU C 175     4087   2218   5844   1452    174   -708       C  
ATOM   4257  C   GLU C 175      10.154  61.101 322.406  1.00 34.65           C  
ANISOU 4257  C   GLU C 175     4637   2363   6167   1369    127   -631       C  
ATOM   4258  O   GLU C 175       9.993  62.225 321.936  1.00 35.05           O  
ANISOU 4258  O   GLU C 175     4890   2291   6135   1501     95   -640       O  
ATOM   4259  CB  GLU C 175       9.167  60.422 324.625  1.00 33.98           C  
ANISOU 4259  CB  GLU C 175     4383   2461   6069   1371    221   -726       C  
ATOM   4260  CG  GLU C 175       7.853  60.252 325.379  1.00 51.06           C  
ANISOU 4260  CG  GLU C 175     6417   4782   8202   1514    287   -810       C  
ATOM   4261  CD  GLU C 175       7.879  59.557 326.732  1.00 80.26           C  
ANISOU 4261  CD  GLU C 175    10053   8541  11900   1395    355   -817       C  
ATOM   4262  OE1 GLU C 175       8.953  59.517 327.378  1.00 80.02           O  
ANISOU 4262  OE1 GLU C 175    10153   8392  11859   1232    336   -770       O  
ATOM   4263  OE2 GLU C 175       6.808  59.063 327.155  1.00 75.81           O  
ANISOU 4263  OE2 GLU C 175     9311   8147  11345   1467    428   -868       O  
ATOM   4264  N   SER C 176      11.308  60.428 322.316  1.00 30.67           N  
ANISOU 4264  N   SER C 176     4083   1831   5740   1154    127   -555       N  
ATOM   4265  CA  SER C 176      12.523  60.976 321.708  1.00 31.24           C  
ANISOU 4265  CA  SER C 176     4318   1737   5817   1042    100   -471       C  
ATOM   4266  C   SER C 176      12.492  60.993 320.160  1.00 35.13           C  
ANISOU 4266  C   SER C 176     4820   2219   6309   1117     84   -436       C  
ATOM   4267  O   SER C 176      13.111  61.871 319.559  1.00 34.32           O  
ANISOU 4267  O   SER C 176     4910   1962   6168   1101     70   -381       O  
ATOM   4268  CB  SER C 176      13.758  60.221 322.197  1.00 35.09           C  
ANISOU 4268  CB  SER C 176     4729   2213   6391    797    108   -404       C  
ATOM   4269  OG  SER C 176      13.691  58.833 321.913  1.00 45.33           O  
ANISOU 4269  OG  SER C 176     5791   3660   7773    740    128   -395       O  
ATOM   4270  N   GLY C 177      11.783  60.052 319.540  1.00 32.67           N  
ANISOU 4270  N   GLY C 177     4317   2063   6035   1194     85   -468       N  
ATOM   4271  CA  GLY C 177      11.701  59.972 318.084  1.00 33.47           C  
ANISOU 4271  CA  GLY C 177     4431   2162   6124   1276     62   -443       C  
ATOM   4272  C   GLY C 177      10.403  60.418 317.439  1.00 40.54           C  
ANISOU 4272  C   GLY C 177     5325   3120   6958   1524     18   -517       C  
ATOM   4273  O   GLY C 177      10.250  60.264 316.224  1.00 40.01           O  
ANISOU 4273  O   GLY C 177     5238   3080   6883   1599    -15   -509       O  
ATOM   4274  N   LYS C 178       9.470  60.985 318.245  1.00 40.03           N  
ANISOU 4274  N   LYS C 178     5289   3078   6844   1662     13   -593       N  
ATOM   4275  CA  LYS C 178       8.119  61.458 317.885  1.00 41.60           C  
ANISOU 4275  CA  LYS C 178     5464   3352   6988   1919    -31   -677       C  
ATOM   4276  C   LYS C 178       8.056  62.087 316.496  1.00 47.35           C  
ANISOU 4276  C   LYS C 178     6352   3992   7649   2061    -93   -656       C  
ATOM   4277  O   LYS C 178       7.329  61.584 315.635  1.00 46.76           O  
ANISOU 4277  O   LYS C 178     6154   4026   7586   2177   -144   -693       O  
ATOM   4278  CB  LYS C 178       7.596  62.461 318.933  1.00 45.06           C  
ANISOU 4278  CB  LYS C 178     6017   3750   7354   2045    -16   -738       C  
ATOM   4279  N   SER C 179       8.853  63.151 316.281  1.00 45.74           N  
ANISOU 4279  N   SER C 179     6426   3582   7370   2037    -93   -594       N  
ATOM   4280  CA  SER C 179       8.956  63.921 315.041  1.00 47.08           C  
ANISOU 4280  CA  SER C 179     6814   3624   7453   2154   -139   -557       C  
ATOM   4281  C   SER C 179       9.325  63.046 313.826  1.00 50.67           C  
ANISOU 4281  C   SER C 179     7184   4126   7942   2095   -145   -505       C  
ATOM   4282  O   SER C 179       8.687  63.171 312.777  1.00 51.83           O  
ANISOU 4282  O   SER C 179     7383   4281   8029   2270   -208   -526       O  
ATOM   4283  CB  SER C 179       9.991  65.027 315.205  1.00 51.77           C  
ANISOU 4283  CB  SER C 179     7702   3985   7984   2059   -115   -481       C  
ATOM   4284  OG  SER C 179      11.295  64.504 315.394  1.00 63.79           O  
ANISOU 4284  OG  SER C 179     9183   5469   9584   1789    -55   -392       O  
ATOM   4285  N   GLU C 180      10.344  62.170 313.977  1.00 44.62           N  
ANISOU 4285  N   GLU C 180     6300   3388   7266   1862    -85   -442       N  
ATOM   4286  CA  GLU C 180      10.830  61.281 312.923  1.00 43.66           C  
ANISOU 4286  CA  GLU C 180     6105   3307   7175   1796    -77   -392       C  
ATOM   4287  C   GLU C 180       9.787  60.221 312.577  1.00 45.70           C  
ANISOU 4287  C   GLU C 180     6130   3755   7477   1894   -134   -471       C  
ATOM   4288  O   GLU C 180       9.729  59.775 311.428  1.00 45.26           O  
ANISOU 4288  O   GLU C 180     6078   3720   7399   1951   -170   -459       O  
ATOM   4289  CB  GLU C 180      12.151  60.614 313.356  1.00 44.23           C  
ANISOU 4289  CB  GLU C 180     6104   3363   7337   1534      2   -311       C  
ATOM   4290  CG  GLU C 180      13.003  60.096 312.201  1.00 56.97           C  
ANISOU 4290  CG  GLU C 180     7764   4936   8945   1468     38   -227       C  
ATOM   4291  CD  GLU C 180      14.496  59.929 312.445  1.00 76.76           C  
ANISOU 4291  CD  GLU C 180    10262   7383  11522   1232    123   -129       C  
ATOM   4292  OE1 GLU C 180      15.076  60.700 313.247  1.00 63.47           O  
ANISOU 4292  OE1 GLU C 180     8671   5595   9849   1124    147    -96       O  
ATOM   4293  OE2 GLU C 180      15.100  59.066 311.769  1.00 70.20           O  
ANISOU 4293  OE2 GLU C 180     9341   6601  10729   1164    160    -86       O  
ATOM   4294  N   LEU C 181       8.978  59.814 313.575  1.00 40.99           N  
ANISOU 4294  N   LEU C 181     5340   3294   6940   1908   -142   -548       N  
ATOM   4295  CA  LEU C 181       7.918  58.815 313.425  1.00 40.33           C  
ANISOU 4295  CA  LEU C 181     5010   3397   6914   1978   -196   -626       C  
ATOM   4296  C   LEU C 181       6.655  59.444 312.822  1.00 45.40           C  
ANISOU 4296  C   LEU C 181     5684   4076   7489   2245   -289   -703       C  
ATOM   4297  O   LEU C 181       5.830  58.729 312.238  1.00 45.56           O  
ANISOU 4297  O   LEU C 181     5545   4224   7541   2326   -365   -757       O  
ATOM   4298  CB  LEU C 181       7.586  58.166 314.784  1.00 39.66           C  
ANISOU 4298  CB  LEU C 181     4710   3440   6919   1876   -150   -669       C  
ATOM   4299  CG  LEU C 181       8.671  57.309 315.440  1.00 42.59           C  
ANISOU 4299  CG  LEU C 181     5007   3807   7369   1623    -79   -607       C  
ATOM   4300  CD1 LEU C 181       8.536  57.319 316.953  1.00 42.13           C  
ANISOU 4300  CD1 LEU C 181     4873   3793   7342   1549    -23   -634       C  
ATOM   4301  CD2 LEU C 181       8.645  55.882 314.911  1.00 45.20           C  
ANISOU 4301  CD2 LEU C 181     5151   4247   7776   1539   -101   -607       C  
ATOM   4302  N   LYS C 182       6.512  60.783 312.966  1.00 41.74           N  
ANISOU 4302  N   LYS C 182     5430   3496   6933   2383   -296   -710       N  
ATOM   4303  CA  LYS C 182       5.372  61.549 312.464  1.00 42.61           C  
ANISOU 4303  CA  LYS C 182     5603   3621   6968   2660   -388   -782       C  
ATOM   4304  C   LYS C 182       5.705  62.334 311.169  1.00 45.72           C  
ANISOU 4304  C   LYS C 182     6285   3847   7240   2774   -442   -731       C  
ATOM   4305  O   LYS C 182       4.851  63.084 310.686  1.00 47.01           O  
ANISOU 4305  O   LYS C 182     6556   3985   7319   3017   -527   -781       O  
ATOM   4306  CB  LYS C 182       4.859  62.506 313.555  1.00 46.10           C  
ANISOU 4306  CB  LYS C 182     6092   4048   7377   2770   -362   -836       C  
ATOM   4307  N   LYS C 183       6.917  62.134 310.592  1.00 39.96           N  
ANISOU 4307  N   LYS C 183     5676   3007   6499   2607   -389   -630       N  
ATOM   4308  CA  LYS C 183       7.360  62.812 309.363  1.00 39.83           C  
ANISOU 4308  CA  LYS C 183     5942   2828   6364   2682   -413   -564       C  
ATOM   4309  C   LYS C 183       6.522  62.394 308.153  1.00 44.35           C  
ANISOU 4309  C   LYS C 183     6480   3478   6893   2866   -529   -611       C  
ATOM   4310  O   LYS C 183       5.979  61.283 308.116  1.00 43.09           O  
ANISOU 4310  O   LYS C 183     6064   3489   6819   2846   -572   -666       O  
ATOM   4311  CB  LYS C 183       8.849  62.562 309.085  1.00 40.51           C  
ANISOU 4311  CB  LYS C 183     6117   2809   6464   2445   -307   -444       C  
ATOM   4312  N   GLN C 184       6.388  63.320 307.186  1.00 42.58           N  
ANISOU 4312  N   GLN C 184     6529   3118   6530   3046   -589   -591       N  
ATOM   4313  CA  GLN C 184       5.619  63.151 305.948  1.00 43.30           C  
ANISOU 4313  CA  GLN C 184     6653   3250   6549   3250   -720   -634       C  
ATOM   4314  C   GLN C 184       6.467  63.555 304.733  1.00 48.12           C  
ANISOU 4314  C   GLN C 184     7573   3684   7028   3251   -696   -533       C  
ATOM   4315  O   GLN C 184       6.943  64.693 304.674  1.00 49.02           O  
ANISOU 4315  O   GLN C 184     7970   3612   7045   3269   -649   -466       O  
ATOM   4316  CB  GLN C 184       4.318  63.992 305.985  1.00 46.04           C  
ANISOU 4316  CB  GLN C 184     7033   3622   6839   3542   -848   -732       C  
ATOM   4317  CG  GLN C 184       3.356  63.684 307.139  1.00 52.87           C  
ANISOU 4317  CG  GLN C 184     7587   4678   7825   3577   -866   -837       C  
ATOM   4318  CD  GLN C 184       2.495  62.468 306.912  1.00 68.89           C  
ANISOU 4318  CD  GLN C 184     9293   6926   9957   3591   -954   -916       C  
ATOM   4319  OE1 GLN C 184       2.377  61.952 305.798  1.00 66.44           O  
ANISOU 4319  OE1 GLN C 184     9001   6629   9614   3633  -1042   -915       O  
ATOM   4320  NE2 GLN C 184       1.864  61.988 307.971  1.00 57.99           N  
ANISOU 4320  NE2 GLN C 184     7617   5717   8699   3554   -932   -987       N  
ATOM   4321  N   VAL C 185       6.671  62.630 303.779  1.00 44.01           N  
ANISOU 4321  N   VAL C 185     7009   3215   6498   3227   -721   -518       N  
ATOM   4322  CA  VAL C 185       7.434  62.905 302.554  1.00 44.41           C  
ANISOU 4322  CA  VAL C 185     7344   3116   6412   3239   -687   -423       C  
ATOM   4323  C   VAL C 185       6.494  62.711 301.354  1.00 50.89           C  
ANISOU 4323  C   VAL C 185     8226   3977   7134   3482   -857   -489       C  
ATOM   4324  O   VAL C 185       5.974  61.609 301.149  1.00 51.34           O  
ANISOU 4324  O   VAL C 185     8051   4193   7264   3491   -942   -562       O  
ATOM   4325  CB  VAL C 185       8.731  62.063 302.433  1.00 46.47           C  
ANISOU 4325  CB  VAL C 185     7555   3373   6727   2987   -540   -329       C  
ATOM   4326  CG1 VAL C 185       9.562  62.508 301.230  1.00 47.15           C  
ANISOU 4326  CG1 VAL C 185     7956   3297   6662   3002   -474   -220       C  
ATOM   4327  CG2 VAL C 185       9.564  62.144 303.710  1.00 44.92           C  
ANISOU 4327  CG2 VAL C 185     7256   3163   6648   2749   -403   -280       C  
ATOM   4328  N   LYS C 186       6.263  63.789 300.586  1.00 48.78           N  
ANISOU 4328  N   LYS C 186     8280   3555   6699   3677   -915   -463       N  
ATOM   4329  CA  LYS C 186       5.351  63.805 299.441  1.00 50.24           C  
ANISOU 4329  CA  LYS C 186     8575   3749   6764   3936  -1094   -523       C  
ATOM   4330  C   LYS C 186       5.807  62.866 298.308  1.00 53.86           C  
ANISOU 4330  C   LYS C 186     9082   4217   7166   3890  -1091   -485       C  
ATOM   4331  O   LYS C 186       6.972  62.911 297.913  1.00 53.21           O  
ANISOU 4331  O   LYS C 186     9175   4017   7024   3748   -935   -367       O  
ATOM   4332  CB  LYS C 186       5.176  65.236 298.900  1.00 54.68           C  
ANISOU 4332  CB  LYS C 186     9515   4114   7146   4144  -1142   -488       C  
ATOM   4333  N   PRO C 187       4.908  62.017 297.759  1.00 50.86           N  
ANISOU 4333  N   PRO C 187     8552   3973   6801   4012  -1261   -584       N  
ATOM   4334  CA  PRO C 187       5.324  61.144 296.656  1.00 50.78           C  
ANISOU 4334  CA  PRO C 187     8619   3958   6717   3986  -1268   -556       C  
ATOM   4335  C   PRO C 187       5.202  61.798 295.280  1.00 57.22           C  
ANISOU 4335  C   PRO C 187     9814   4624   7304   4207  -1354   -524       C  
ATOM   4336  O   PRO C 187       4.315  62.624 295.048  1.00 58.33           O  
ANISOU 4336  O   PRO C 187    10085   4719   7359   4438  -1498   -572       O  
ATOM   4337  CB  PRO C 187       4.358  59.962 296.762  1.00 52.11           C  
ANISOU 4337  CB  PRO C 187     8457   4331   7010   4007  -1430   -684       C  
ATOM   4338  CG  PRO C 187       3.144  60.499 297.449  1.00 57.14           C  
ANISOU 4338  CG  PRO C 187     8919   5065   7727   4148  -1559   -787       C  
ATOM   4339  CD  PRO C 187       3.483  61.812 298.098  1.00 53.10           C  
ANISOU 4339  CD  PRO C 187     8589   4421   7168   4177  -1456   -727       C  
ATOM   4340  N   LYS C 188       6.086  61.400 294.359  1.00 54.47           N  
ANISOU 4340  N   LYS C 188     9646   4201   6848   4145  -1265   -444       N  
ATOM   4341  CA  LYS C 188       6.043  61.827 292.963  1.00 56.56           C  
ANISOU 4341  CA  LYS C 188    10283   4328   6880   4340  -1332   -406       C  
ATOM   4342  C   LYS C 188       5.473  60.652 292.163  1.00 61.92           C  
ANISOU 4342  C   LYS C 188    10876   5116   7537   4429  -1502   -498       C  
ATOM   4343  O   LYS C 188       5.943  59.518 292.318  1.00 60.21           O  
ANISOU 4343  O   LYS C 188    10477   4988   7413   4259  -1429   -498       O  
ATOM   4344  CB  LYS C 188       7.429  62.265 292.459  1.00 58.95           C  
ANISOU 4344  CB  LYS C 188    10879   4459   7061   4212  -1090   -242       C  
ATOM   4345  N   ALA C 189       4.412  60.897 291.382  1.00 60.72           N  
ANISOU 4345  N   ALA C 189    10836   4959   7274   4695  -1746   -584       N  
ATOM   4346  CA  ALA C 189       3.755  59.839 290.618  1.00 61.11           C  
ANISOU 4346  CA  ALA C 189    10810   5107   7303   4793  -1949   -685       C  
ATOM   4347  C   ALA C 189       3.815  60.092 289.120  1.00 67.49           C  
ANISOU 4347  C   ALA C 189    12030   5769   7843   4995  -2032   -653       C  
ATOM   4348  O   ALA C 189       3.785  61.248 288.691  1.00 69.43           O  
ANISOU 4348  O   ALA C 189    12591   5863   7925   5155  -2038   -599       O  
ATOM   4349  CB  ALA C 189       2.308  59.706 291.062  1.00 62.43           C  
ANISOU 4349  CB  ALA C 189    10689   5434   7598   4926  -2203   -838       C  
ATOM   4350  N   TRP C 190       3.887  59.012 288.323  1.00 63.86           N  
ANISOU 4350  N   TRP C 190    11587   5346   7330   4994  -2100   -687       N  
ATOM   4351  CA  TRP C 190       3.914  59.080 286.858  1.00 65.87           C  
ANISOU 4351  CA  TRP C 190    12231   5475   7323   5187  -2191   -668       C  
ATOM   4352  C   TRP C 190       3.311  57.805 286.244  1.00 69.55           C  
ANISOU 4352  C   TRP C 190    12581   6047   7799   5233  -2406   -787       C  
ATOM   4353  O   TRP C 190       3.314  56.756 286.890  1.00 67.48           O  
ANISOU 4353  O   TRP C 190    11980   5927   7733   5050  -2391   -840       O  
ATOM   4354  CB  TRP C 190       5.341  59.335 286.331  1.00 64.79           C  
ANISOU 4354  CB  TRP C 190    12413   5178   7027   5087  -1898   -502       C  
ATOM   4355  CG  TRP C 190       6.298  58.198 286.519  1.00 64.22           C  
ANISOU 4355  CG  TRP C 190    12181   5172   7047   4854  -1708   -463       C  
ATOM   4356  CD1 TRP C 190       6.625  57.244 285.601  1.00 67.63           C  
ANISOU 4356  CD1 TRP C 190    12735   5596   7365   4874  -1711   -469       C  
ATOM   4357  CD2 TRP C 190       7.064  57.905 287.695  1.00 61.85           C  
ANISOU 4357  CD2 TRP C 190    11588   4949   6963   4581  -1491   -413       C  
ATOM   4358  NE1 TRP C 190       7.530  56.360 286.140  1.00 65.27           N  
ANISOU 4358  NE1 TRP C 190    12225   5369   7204   4636  -1509   -428       N  
ATOM   4359  CE2 TRP C 190       7.836  56.755 287.417  1.00 64.90           C  
ANISOU 4359  CE2 TRP C 190    11924   5375   7361   4451  -1372   -390       C  
ATOM   4360  CE3 TRP C 190       7.177  58.505 288.961  1.00 61.80           C  
ANISOU 4360  CE3 TRP C 190    11369   4978   7134   4441  -1391   -388       C  
ATOM   4361  CZ2 TRP C 190       8.694  56.180 288.365  1.00 61.96           C  
ANISOU 4361  CZ2 TRP C 190    11283   5081   7179   4192  -1169   -345       C  
ATOM   4362  CZ3 TRP C 190       8.027  57.932 289.899  1.00 61.01           C  
ANISOU 4362  CZ3 TRP C 190    11011   4953   7217   4177  -1193   -343       C  
ATOM   4363  CH2 TRP C 190       8.785  56.794 289.593  1.00 60.73           C  
ANISOU 4363  CH2 TRP C 190    10923   4958   7194   4056  -1085   -320       C  
ATOM   4364  N   LEU C 191       2.794  57.903 284.999  1.00 67.86           N  
ANISOU 4364  N   LEU C 191    12663   5753   7368   5476  -2613   -829       N  
ATOM   4365  CA  LEU C 191       2.169  56.779 284.287  1.00 68.13           C  
ANISOU 4365  CA  LEU C 191    12644   5862   7380   5546  -2856   -949       C  
ATOM   4366  C   LEU C 191       3.101  56.147 283.230  1.00 72.52           C  
ANISOU 4366  C   LEU C 191    13515   6309   7731   5537  -2740   -881       C  
ATOM   4367  O   LEU C 191       4.109  56.751 282.853  1.00 71.58           O  
ANISOU 4367  O   LEU C 191    13707   6043   7446   5531  -2500   -741       O  
ATOM   4368  CB  LEU C 191       0.852  57.225 283.613  1.00 70.38           C  
ANISOU 4368  CB  LEU C 191    13026   6147   7569   5841  -3215  -1064       C  
ATOM   4369  CG  LEU C 191      -0.264  57.802 284.488  1.00 74.65           C  
ANISOU 4369  CG  LEU C 191    13266   6806   8291   5913  -3372  -1150       C  
ATOM   4370  CD1 LEU C 191      -1.456  58.121 283.655  1.00 77.47           C  
ANISOU 4370  CD1 LEU C 191    13775   7142   8517   6227  -3713  -1249       C  
ATOM   4371  CD2 LEU C 191      -0.707  56.833 285.559  1.00 75.64           C  
ANISOU 4371  CD2 LEU C 191    12875   7149   8715   5723  -3430  -1251       C  
ATOM   4372  N   SER C 192       2.748  54.927 282.754  1.00 70.64           N  
ANISOU 4372  N   SER C 192    13197   6139   7503   5534  -2911   -982       N  
ATOM   4373  CA  SER C 192       3.495  54.185 281.728  1.00 72.08           C  
ANISOU 4373  CA  SER C 192    13665   6231   7490   5549  -2837   -946       C  
ATOM   4374  C   SER C 192       2.647  53.083 281.068  1.00 79.02           C  
ANISOU 4374  C   SER C 192    14507   7169   8350   5639  -3161  -1099       C  
ATOM   4375  O   SER C 192       1.630  52.660 281.624  1.00 78.16           O  
ANISOU 4375  O   SER C 192    14052   7202   8444   5605  -3392  -1225       O  
ATOM   4376  CB  SER C 192       4.765  53.565 282.316  1.00 73.90           C  
ANISOU 4376  CB  SER C 192    13768   6487   7826   5287  -2503   -850       C  
ATOM   4377  OG  SER C 192       4.488  52.422 283.109  1.00 81.00           O  
ANISOU 4377  OG  SER C 192    14248   7545   8984   5102  -2566   -939       O  
ATOM   4378  N   ARG C 193       3.102  52.599 279.895  1.00 78.95           N  
ANISOU 4378  N   ARG C 193    14856   7048   8094   5745  -3168  -1086       N  
ATOM   4379  CA  ARG C 193       2.460  51.527 279.138  1.00 81.33           C  
ANISOU 4379  CA  ARG C 193    15198   7369   8335   5832  -3465  -1223       C  
ATOM   4380  C   ARG C 193       3.156  50.182 279.427  1.00 86.30           C  
ANISOU 4380  C   ARG C 193    15676   8049   9065   5622  -3329  -1229       C  
ATOM   4381  O   ARG C 193       4.309  49.973 279.036  1.00 85.94           O  
ANISOU 4381  O   ARG C 193    15859   7916   8878   5588  -3060  -1125       O  
ATOM   4382  CB  ARG C 193       2.473  51.845 277.634  1.00 84.45           C  
ANISOU 4382  CB  ARG C 193    16120   7597   8372   6107  -3582  -1214       C  
ATOM   4383  N   GLY C 194       2.454  49.301 280.135  1.00 83.51           N  
ANISOU 4383  N   GLY C 194    14933   7838   8958   5484  -3507  -1347       N  
ATOM   4384  CA  GLY C 194       2.964  47.982 280.493  1.00 82.69           C  
ANISOU 4384  CA  GLY C 194    14661   7786   8973   5283  -3420  -1369       C  
ATOM   4385  C   GLY C 194       2.953  47.004 279.334  1.00 90.57           C  
ANISOU 4385  C   GLY C 194    15940   8699   9774   5392  -3589  -1445       C  
ATOM   4386  O   GLY C 194       2.309  47.279 278.315  1.00 92.87           O  
ANISOU 4386  O   GLY C 194    16519   8910   9856   5623  -3830  -1502       O  
ATOM   4387  N   PRO C 195       3.648  45.841 279.453  1.00 87.68           N  
ANISOU 4387  N   PRO C 195    15512   8343   9461   5241  -3482  -1451       N  
ATOM   4388  CA  PRO C 195       3.652  44.863 278.346  1.00 90.08           C  
ANISOU 4388  CA  PRO C 195    16105   8556   9567   5351  -3647  -1531       C  
ATOM   4389  C   PRO C 195       2.244  44.335 278.051  1.00 98.27           C  
ANISOU 4389  C   PRO C 195    17041   9636  10661   5411  -4103  -1708       C  
ATOM   4390  O   PRO C 195       1.618  43.705 278.907  1.00 96.77           O  
ANISOU 4390  O   PRO C 195    16452   9573  10744   5229  -4237  -1788       O  
ATOM   4391  CB  PRO C 195       4.590  43.758 278.849  1.00 89.80           C  
ANISOU 4391  CB  PRO C 195    15939   8543   9637   5149  -3428  -1502       C  
ATOM   4392  CG  PRO C 195       5.395  44.395 279.923  1.00 91.31           C  
ANISOU 4392  CG  PRO C 195    15888   8803  10001   4978  -3085  -1369       C  
ATOM   4393  CD  PRO C 195       4.470  45.362 280.580  1.00 86.50           C  
ANISOU 4393  CD  PRO C 195    15048   8277   9539   4978  -3214  -1389       C  
ATOM   4394  N   SER C 196       1.741  44.655 276.842  1.00 99.66           N  
ANISOU 4394  N   SER C 196    17581   9708  10579   5665  -4343  -1763       N  
ATOM   4395  CA  SER C 196       0.401  44.321 276.356  1.00102.83           C  
ANISOU 4395  CA  SER C 196    17949  10133  10990   5767  -4805  -1929       C  
ATOM   4396  C   SER C 196       0.177  42.798 276.262  1.00109.07           C  
ANISOU 4396  C   SER C 196    18646  10934  11862   5639  -4998  -2050       C  
ATOM   4397  O   SER C 196       0.770  42.146 275.397  1.00109.89           O  
ANISOU 4397  O   SER C 196    19093  10913  11748   5711  -4965  -2054       O  
ATOM   4398  CB  SER C 196       0.151  44.977 275.001  1.00109.90           C  
ANISOU 4398  CB  SER C 196    19325  10886  11545   6080  -4980  -1943       C  
ATOM   4399  OG  SER C 196       1.056  44.497 274.020  1.00121.04           O  
ANISOU 4399  OG  SER C 196    21176  12146  12669   6177  -4846  -1902       O  
ATOM   4400  N   PRO C 197      -0.693  42.216 277.127  1.00106.21           N  
ANISOU 4400  N   PRO C 197    17837  10714  11804   5452  -5202  -2150       N  
ATOM   4401  CA  PRO C 197      -0.924  40.759 277.072  1.00106.73           C  
ANISOU 4401  CA  PRO C 197    17819  10778  11955   5309  -5393  -2263       C  
ATOM   4402  C   PRO C 197      -1.963  40.342 276.012  1.00114.08           C  
ANISOU 4402  C   PRO C 197    18949  11644  12751   5468  -5856  -2419       C  
ATOM   4403  O   PRO C 197      -2.244  39.148 275.865  1.00114.72           O  
ANISOU 4403  O   PRO C 197    19019  11697  12872   5367  -6053  -2522       O  
ATOM   4404  CB  PRO C 197      -1.401  40.420 278.497  1.00106.63           C  
ANISOU 4404  CB  PRO C 197    17243  10946  12327   5031  -5390  -2287       C  
ATOM   4405  CG  PRO C 197      -1.451  41.752 279.258  1.00109.74           C  
ANISOU 4405  CG  PRO C 197    17437  11438  12823   5055  -5213  -2196       C  
ATOM   4406  CD  PRO C 197      -1.469  42.826 278.222  1.00106.95           C  
ANISOU 4406  CD  PRO C 197    17484  10974  12178   5354  -5250  -2161       C  
ATOM   4407  N   GLY C 198      -2.500  41.317 275.277  1.00112.25           N  
ANISOU 4407  N   GLY C 198    18913  11380  12356   5715  -6032  -2436       N  
ATOM   4408  CA  GLY C 198      -3.482  41.101 274.219  1.00115.28           C  
ANISOU 4408  CA  GLY C 198    19509  11700  12591   5900  -6485  -2580       C  
ATOM   4409  C   GLY C 198      -3.219  41.933 272.975  1.00120.70           C  
ANISOU 4409  C   GLY C 198    20733  12230  12897   6226  -6499  -2538       C  
ATOM   4410  O   GLY C 198      -2.569  42.982 273.070  1.00119.35           O  
ANISOU 4410  O   GLY C 198    20684  12034  12628   6311  -6193  -2400       O  
ATOM   4411  N   PRO C 199      -3.722  41.506 271.785  1.00119.58           N  
ANISOU 4411  N   PRO C 199    20935  11972  12527   6411  -6858  -2656       N  
ATOM   4412  CA  PRO C 199      -3.480  42.289 270.554  1.00121.14           C  
ANISOU 4412  CA  PRO C 199    21685  12008  12335   6734  -6877  -2614       C  
ATOM   4413  C   PRO C 199      -4.174  43.660 270.549  1.00124.30           C  
ANISOU 4413  C   PRO C 199    22042  12457  12729   6914  -6988  -2594       C  
ATOM   4414  O   PRO C 199      -3.608  44.627 270.037  1.00124.19           O  
ANISOU 4414  O   PRO C 199    22392  12336  12459   7111  -6799  -2482       O  
ATOM   4415  CB  PRO C 199      -4.025  41.388 269.441  1.00126.20           C  
ANISOU 4415  CB  PRO C 199    22637  12533  12783   6858  -7288  -2769       C  
ATOM   4416  CG  PRO C 199      -5.006  40.496 270.109  1.00130.90           C  
ANISOU 4416  CG  PRO C 199    22762  13262  13713   6635  -7605  -2913       C  
ATOM   4417  CD  PRO C 199      -4.499  40.281 271.502  1.00122.91           C  
ANISOU 4417  CD  PRO C 199    21282  12391  13025   6330  -7261  -2828       C  
ATOM   4418  N   GLY C 200      -5.375  43.724 271.121  1.00120.08           N  
ANISOU 4418  N   GLY C 200    21068  12081  12477   6845  -7284  -2698       N  
ATOM   4419  CA  GLY C 200      -6.160  44.948 271.234  1.00120.25           C  
ANISOU 4419  CA  GLY C 200    20980  12171  12537   7012  -7422  -2698       C  
ATOM   4420  C   GLY C 200      -6.354  45.388 272.672  1.00119.95           C  
ANISOU 4420  C   GLY C 200    20398  12325  12853   6816  -7225  -2645       C  
ATOM   4421  O   GLY C 200      -7.278  46.151 272.967  1.00120.36           O  
ANISOU 4421  O   GLY C 200    20238  12476  13016   6919  -7395  -2680       O  
ATOM   4422  N   ARG C 201      -5.481  44.896 273.577  1.00112.21           N  
ANISOU 4422  N   ARG C 201    19197  11396  12044   6544  -6868  -2563       N  
ATOM   4423  CA  ARG C 201      -5.488  45.192 275.011  1.00108.64           C  
ANISOU 4423  CA  ARG C 201    18247  11115  11917   6330  -6637  -2504       C  
ATOM   4424  C   ARG C 201      -4.184  45.848 275.448  1.00108.61           C  
ANISOU 4424  C   ARG C 201    18375  11052  11840   6281  -6139  -2319       C  
ATOM   4425  O   ARG C 201      -3.112  45.452 274.987  1.00108.00           O  
ANISOU 4425  O   ARG C 201    18617  10847  11571   6270  -5914  -2245       O  
ATOM   4426  CB  ARG C 201      -5.713  43.909 275.831  1.00106.94           C  
ANISOU 4426  CB  ARG C 201    17600  11026  12008   6018  -6680  -2577       C  
ATOM   4427  CG  ARG C 201      -7.164  43.471 275.907  1.00118.98           C  
ANISOU 4427  CG  ARG C 201    18786  12682  13738   5991  -7129  -2745       C  
ATOM   4428  CD  ARG C 201      -7.403  42.568 277.100  1.00127.21           C  
ANISOU 4428  CD  ARG C 201    19322  13879  15135   5653  -7089  -2781       C  
ATOM   4429  NE  ARG C 201      -8.814  42.203 277.234  1.00139.92           N  
ANISOU 4429  NE  ARG C 201    20569  15631  16963   5610  -7500  -2933       N  
ATOM   4430  CZ  ARG C 201      -9.714  42.903 277.920  1.00155.13           C  
ANISOU 4430  CZ  ARG C 201    22087  17739  19117   5613  -7573  -2957       C  
ATOM   4431  NH1 ARG C 201      -9.363  44.023 278.540  1.00140.29           N  
ANISOU 4431  NH1 ARG C 201    20128  15909  17267   5661  -7270  -2844       N  
ATOM   4432  NH2 ARG C 201     -10.974  42.496 277.979  1.00144.64           N  
ANISOU 4432  NH2 ARG C 201    20426  16544  17987   5569  -7949  -3097       N  
ATOM   4433  N   LEU C 202      -4.277  46.836 276.354  1.00102.09           N  
ANISOU 4433  N   LEU C 202    17293  10323  11173   6249  -5970  -2248       N  
ATOM   4434  CA  LEU C 202      -3.122  47.537 276.916  1.00 98.60           C  
ANISOU 4434  CA  LEU C 202    16918   9840  10704   6178  -5515  -2075       C  
ATOM   4435  C   LEU C 202      -3.209  47.534 278.443  1.00 97.43           C  
ANISOU 4435  C   LEU C 202    16245   9867  10906   5926  -5341  -2051       C  
ATOM   4436  O   LEU C 202      -4.267  47.853 278.991  1.00 97.72           O  
ANISOU 4436  O   LEU C 202    15953  10041  11137   5939  -5532  -2125       O  
ATOM   4437  CB  LEU C 202      -3.024  48.988 276.369  1.00 99.87           C  
ANISOU 4437  CB  LEU C 202    17427   9890  10628   6440  -5459  -1990       C  
ATOM   4438  CG  LEU C 202      -1.897  49.884 276.906  1.00102.45           C  
ANISOU 4438  CG  LEU C 202    17840  10163  10923   6374  -5012  -1808       C  
ATOM   4439  CD1 LEU C 202      -0.538  49.314 276.550  1.00101.43           C  
ANISOU 4439  CD1 LEU C 202    17973   9924  10641   6278  -4699  -1705       C  
ATOM   4440  CD2 LEU C 202      -2.026  51.338 276.413  1.00106.47           C  
ANISOU 4440  CD2 LEU C 202    18660  10566  11226   6631  -5016  -1741       C  
ATOM   4441  N   LEU C 203      -2.101  47.170 279.125  1.00 89.09           N  
ANISOU 4441  N   LEU C 203    15113   8811   9928   5706  -4981  -1948       N  
ATOM   4442  CA  LEU C 203      -2.032  47.184 280.587  1.00 85.33           C  
ANISOU 4442  CA  LEU C 203    14184   8482   9757   5463  -4783  -1910       C  
ATOM   4443  C   LEU C 203      -1.534  48.557 281.040  1.00 86.53           C  
ANISOU 4443  C   LEU C 203    14395   8607   9876   5520  -4515  -1780       C  
ATOM   4444  O   LEU C 203      -0.369  48.903 280.825  1.00 85.40           O  
ANISOU 4444  O   LEU C 203    14518   8349   9581   5513  -4212  -1649       O  
ATOM   4445  CB  LEU C 203      -1.148  46.043 281.154  1.00 83.08           C  
ANISOU 4445  CB  LEU C 203    13771   8211   9584   5197  -4559  -1873       C  
ATOM   4446  CG  LEU C 203      -0.946  46.009 282.676  1.00 84.83           C  
ANISOU 4446  CG  LEU C 203    13559   8570  10101   4940  -4333  -1824       C  
ATOM   4447  CD1 LEU C 203      -2.250  45.788 283.404  1.00 85.65           C  
ANISOU 4447  CD1 LEU C 203    13226   8848  10470   4859  -4580  -1940       C  
ATOM   4448  CD2 LEU C 203       0.057  44.953 283.062  1.00 84.52           C  
ANISOU 4448  CD2 LEU C 203    13480   8514  10121   4720  -4110  -1776       C  
ATOM   4449  N   LEU C 204      -2.438  49.347 281.637  1.00 81.93           N  
ANISOU 4449  N   LEU C 204    13570   8128   9431   5584  -4635  -1820       N  
ATOM   4450  CA  LEU C 204      -2.146  50.690 282.131  1.00 80.02           C  
ANISOU 4450  CA  LEU C 204    13369   7862   9175   5647  -4426  -1716       C  
ATOM   4451  C   LEU C 204      -1.420  50.579 283.456  1.00 78.87           C  
ANISOU 4451  C   LEU C 204    12928   7794   9245   5375  -4098  -1631       C  
ATOM   4452  O   LEU C 204      -1.744  49.699 284.258  1.00 77.06           O  
ANISOU 4452  O   LEU C 204    12310   7708   9260   5179  -4137  -1695       O  
ATOM   4453  CB  LEU C 204      -3.437  51.498 282.255  1.00 81.78           C  
ANISOU 4453  CB  LEU C 204    13437   8170   9465   5833  -4693  -1803       C  
ATOM   4454  CG  LEU C 204      -3.855  52.252 280.993  1.00 89.82           C  
ANISOU 4454  CG  LEU C 204    14868   9057  10204   6162  -4911  -1822       C  
ATOM   4455  CD1 LEU C 204      -4.454  51.324 279.942  1.00 92.33           C  
ANISOU 4455  CD1 LEU C 204    15318   9352  10412   6265  -5253  -1944       C  
ATOM   4456  CD2 LEU C 204      -4.861  53.339 281.322  1.00 94.97           C  
ANISOU 4456  CD2 LEU C 204    15373   9781  10928   6344  -5074  -1869       C  
ATOM   4457  N   VAL C 205      -0.375  51.403 283.649  1.00 72.66           N  
ANISOU 4457  N   VAL C 205    12344   6904   8360   5350  -3775  -1484       N  
ATOM   4458  CA  VAL C 205       0.470  51.344 284.847  1.00 68.84           C  
ANISOU 4458  CA  VAL C 205    11631   6471   8053   5097  -3453  -1391       C  
ATOM   4459  C   VAL C 205       0.608  52.738 285.490  1.00 69.84           C  
ANISOU 4459  C   VAL C 205    11763   6575   8198   5139  -3293  -1307       C  
ATOM   4460  O   VAL C 205       0.827  53.732 284.793  1.00 69.91           O  
ANISOU 4460  O   VAL C 205    12121   6447   7994   5326  -3271  -1244       O  
ATOM   4461  CB  VAL C 205       1.870  50.727 284.532  1.00 71.46           C  
ANISOU 4461  CB  VAL C 205    12169   6704   8278   4973  -3184  -1288       C  
ATOM   4462  CG1 VAL C 205       2.667  50.462 285.802  1.00 68.31           C  
ANISOU 4462  CG1 VAL C 205    11490   6377   8089   4700  -2898  -1213       C  
ATOM   4463  CG2 VAL C 205       1.758  49.444 283.714  1.00 72.29           C  
ANISOU 4463  CG2 VAL C 205    12360   6796   8312   4982  -3355  -1373       C  
ATOM   4464  N   CYS C 206       0.494  52.779 286.833  1.00 63.49           N  
ANISOU 4464  N   CYS C 206    10588   5895   7640   4960  -3181  -1304       N  
ATOM   4465  CA  CYS C 206       0.639  53.972 287.659  1.00 62.04           C  
ANISOU 4465  CA  CYS C 206    10366   5700   7506   4962  -3021  -1233       C  
ATOM   4466  C   CYS C 206       1.774  53.752 288.645  1.00 61.53           C  
ANISOU 4466  C   CYS C 206    10164   5645   7568   4694  -2696  -1130       C  
ATOM   4467  O   CYS C 206       1.688  52.866 289.495  1.00 58.45           O  
ANISOU 4467  O   CYS C 206     9433   5386   7388   4499  -2674  -1172       O  
ATOM   4468  CB  CYS C 206      -0.670  54.309 288.373  1.00 63.11           C  
ANISOU 4468  CB  CYS C 206    10186   5981   7810   5039  -3219  -1341       C  
ATOM   4469  SG  CYS C 206      -0.563  55.714 289.522  1.00 66.13           S  
ANISOU 4469  SG  CYS C 206    10518   6352   8258   5054  -3036  -1270       S  
ATOM   4470  N   HIS C 207       2.835  54.557 288.520  1.00 58.19           N  
ANISOU 4470  N   HIS C 207    10011   5081   7016   4681  -2452   -993       N  
ATOM   4471  CA  HIS C 207       4.008  54.504 289.390  1.00 56.35           C  
ANISOU 4471  CA  HIS C 207     9684   4842   6886   4440  -2144   -883       C  
ATOM   4472  C   HIS C 207       3.927  55.584 290.446  1.00 59.19           C  
ANISOU 4472  C   HIS C 207     9932   5211   7347   4407  -2048   -847       C  
ATOM   4473  O   HIS C 207       3.647  56.734 290.114  1.00 60.24           O  
ANISOU 4473  O   HIS C 207    10280   5251   7356   4587  -2095   -827       O  
ATOM   4474  CB  HIS C 207       5.302  54.683 288.581  1.00 57.70           C  
ANISOU 4474  CB  HIS C 207    10205   4855   6862   4427  -1922   -750       C  
ATOM   4475  CG  HIS C 207       5.516  53.664 287.513  1.00 62.08           C  
ANISOU 4475  CG  HIS C 207    10908   5385   7293   4467  -1981   -776       C  
ATOM   4476  ND1 HIS C 207       6.400  52.617 287.689  1.00 62.63           N  
ANISOU 4476  ND1 HIS C 207    10866   5492   7437   4280  -1828   -747       N  
ATOM   4477  CD2 HIS C 207       4.971  53.579 286.278  1.00 66.14           C  
ANISOU 4477  CD2 HIS C 207    11689   5834   7607   4683  -2180   -829       C  
ATOM   4478  CE1 HIS C 207       6.354  51.919 286.566  1.00 63.50           C  
ANISOU 4478  CE1 HIS C 207    11179   5557   7390   4390  -1932   -785       C  
ATOM   4479  NE2 HIS C 207       5.505  52.459 285.689  1.00 65.97           N  
ANISOU 4479  NE2 HIS C 207    11727   5808   7533   4628  -2147   -836       N  
ATOM   4480  N   VAL C 208       4.148  55.220 291.718  1.00 53.72           N  
ANISOU 4480  N   VAL C 208     8920   4623   6870   4188  -1922   -842       N  
ATOM   4481  CA  VAL C 208       4.139  56.160 292.846  1.00 52.94           C  
ANISOU 4481  CA  VAL C 208     8703   4535   6876   4133  -1815   -810       C  
ATOM   4482  C   VAL C 208       5.348  55.848 293.722  1.00 55.64           C  
ANISOU 4482  C   VAL C 208     8940   4873   7326   3864  -1547   -713       C  
ATOM   4483  O   VAL C 208       5.464  54.726 294.213  1.00 54.13           O  
ANISOU 4483  O   VAL C 208     8505   4789   7274   3700  -1526   -744       O  
ATOM   4484  CB  VAL C 208       2.824  56.159 293.675  1.00 56.73           C  
ANISOU 4484  CB  VAL C 208     8853   5176   7525   4179  -1989   -934       C  
ATOM   4485  CG1 VAL C 208       2.700  57.440 294.494  1.00 56.48           C  
ANISOU 4485  CG1 VAL C 208     8821   5114   7525   4215  -1908   -904       C  
ATOM   4486  CG2 VAL C 208       1.592  55.962 292.799  1.00 58.48           C  
ANISOU 4486  CG2 VAL C 208     9087   5448   7684   4408  -2289  -1052       C  
ATOM   4487  N   SER C 209       6.256  56.818 293.900  1.00 52.58           N  
ANISOU 4487  N   SER C 209     8743   4359   6876   3818  -1351   -594       N  
ATOM   4488  CA  SER C 209       7.464  56.598 294.699  1.00 50.75           C  
ANISOU 4488  CA  SER C 209     8421   4117   6745   3567  -1105   -497       C  
ATOM   4489  C   SER C 209       7.857  57.816 295.523  1.00 54.13           C  
ANISOU 4489  C   SER C 209     8898   4467   7201   3508   -974   -425       C  
ATOM   4490  O   SER C 209       7.555  58.953 295.148  1.00 54.93           O  
ANISOU 4490  O   SER C 209     9233   4459   7179   3668  -1017   -406       O  
ATOM   4491  CB  SER C 209       8.636  56.193 293.808  1.00 54.40           C  
ANISOU 4491  CB  SER C 209     9101   4485   7083   3516   -952   -396       C  
ATOM   4492  OG  SER C 209       8.950  57.195 292.855  1.00 64.72           O  
ANISOU 4492  OG  SER C 209    10777   5630   8185   3651   -905   -314       O  
ATOM   4493  N   GLY C 210       8.566  57.544 296.617  1.00 48.97           N  
ANISOU 4493  N   GLY C 210     8045   3860   6703   3280   -820   -384       N  
ATOM   4494  CA  GLY C 210       9.087  58.543 297.541  1.00 48.29           C  
ANISOU 4494  CA  GLY C 210     7980   3702   6665   3178   -688   -316       C  
ATOM   4495  C   GLY C 210       8.094  58.990 298.585  1.00 51.12           C  
ANISOU 4495  C   GLY C 210     8162   4136   7123   3233   -792   -405       C  
ATOM   4496  O   GLY C 210       8.003  60.183 298.879  1.00 52.01           O  
ANISOU 4496  O   GLY C 210     8429   4151   7182   3309   -783   -382       O  
ATOM   4497  N   PHE C 211       7.352  58.042 299.155  1.00 45.73           N  
ANISOU 4497  N   PHE C 211     7166   3625   6583   3195   -885   -506       N  
ATOM   4498  CA  PHE C 211       6.359  58.375 300.157  1.00 45.42           C  
ANISOU 4498  CA  PHE C 211     6928   3684   6646   3248   -970   -594       C  
ATOM   4499  C   PHE C 211       6.695  57.798 301.528  1.00 46.76           C  
ANISOU 4499  C   PHE C 211     6817   3954   6995   3022   -865   -597       C  
ATOM   4500  O   PHE C 211       7.008  56.607 301.670  1.00 44.58           O  
ANISOU 4500  O   PHE C 211     6369   3762   6809   2874   -836   -601       O  
ATOM   4501  CB  PHE C 211       4.945  57.942 299.721  1.00 48.27           C  
ANISOU 4501  CB  PHE C 211     7156   4170   7014   3435  -1195   -722       C  
ATOM   4502  CG  PHE C 211       4.756  56.510 299.276  1.00 49.03           C  
ANISOU 4502  CG  PHE C 211     7079   4378   7171   3368  -1274   -774       C  
ATOM   4503  CD1 PHE C 211       4.973  56.141 297.952  1.00 52.65           C  
ANISOU 4503  CD1 PHE C 211     7734   4773   7499   3447  -1335   -759       C  
ATOM   4504  CD2 PHE C 211       4.285  55.548 300.160  1.00 49.85           C  
ANISOU 4504  CD2 PHE C 211     6843   4647   7452   3240  -1300   -843       C  
ATOM   4505  CE1 PHE C 211       4.774  54.821 297.534  1.00 53.11           C  
ANISOU 4505  CE1 PHE C 211     7654   4921   7604   3392  -1423   -814       C  
ATOM   4506  CE2 PHE C 211       4.082  54.230 299.740  1.00 52.26           C  
ANISOU 4506  CE2 PHE C 211     7007   5039   7809   3173  -1385   -892       C  
ATOM   4507  CZ  PHE C 211       4.329  53.875 298.430  1.00 50.97           C  
ANISOU 4507  CZ  PHE C 211     7046   4803   7516   3252  -1452   -880       C  
ATOM   4508  N   TYR C 212       6.638  58.677 302.537  1.00 42.36           N  
ANISOU 4508  N   TYR C 212     6241   3376   6479   3007   -812   -594       N  
ATOM   4509  CA  TYR C 212       6.801  58.323 303.941  1.00 40.38           C  
ANISOU 4509  CA  TYR C 212     5753   3211   6380   2825   -726   -604       C  
ATOM   4510  C   TYR C 212       5.616  58.951 304.701  1.00 42.88           C  
ANISOU 4510  C   TYR C 212     5962   3600   6731   2963   -803   -693       C  
ATOM   4511  O   TYR C 212       5.329  60.131 304.477  1.00 43.56           O  
ANISOU 4511  O   TYR C 212     6253   3584   6714   3129   -835   -691       O  
ATOM   4512  CB  TYR C 212       8.175  58.726 304.520  1.00 40.88           C  
ANISOU 4512  CB  TYR C 212     5925   3154   6453   2628   -547   -490       C  
ATOM   4513  CG  TYR C 212       8.318  58.384 305.989  1.00 42.00           C  
ANISOU 4513  CG  TYR C 212     5846   3374   6736   2452   -472   -503       C  
ATOM   4514  CD1 TYR C 212       8.380  57.060 306.416  1.00 43.23           C  
ANISOU 4514  CD1 TYR C 212     5754   3659   7013   2301   -456   -524       C  
ATOM   4515  CD2 TYR C 212       8.364  59.382 306.955  1.00 43.27           C  
ANISOU 4515  CD2 TYR C 212     6069   3471   6900   2443   -425   -494       C  
ATOM   4516  CE1 TYR C 212       8.442  56.736 307.771  1.00 43.82           C  
ANISOU 4516  CE1 TYR C 212     5642   3802   7204   2150   -394   -536       C  
ATOM   4517  CE2 TYR C 212       8.446  59.072 308.312  1.00 43.52           C  
ANISOU 4517  CE2 TYR C 212     5918   3573   7045   2295   -363   -510       C  
ATOM   4518  CZ  TYR C 212       8.481  57.748 308.715  1.00 51.75           C  
ANISOU 4518  CZ  TYR C 212     6712   4748   8203   2148   -346   -529       C  
ATOM   4519  OH  TYR C 212       8.556  57.438 310.050  1.00 53.72           O  
ANISOU 4519  OH  TYR C 212     6801   5058   8550   2007   -287   -541       O  
ATOM   4520  N   PRO C 213       4.839  58.182 305.504  1.00 36.83           N  
ANISOU 4520  N   PRO C 213     4887   3010   6098   2917   -838   -775       N  
ATOM   4521  CA  PRO C 213       5.018  56.767 305.875  1.00 34.44           C  
ANISOU 4521  CA  PRO C 213     4332   2830   5922   2724   -813   -787       C  
ATOM   4522  C   PRO C 213       4.536  55.777 304.800  1.00 37.29           C  
ANISOU 4522  C   PRO C 213     4629   3263   6278   2780   -946   -835       C  
ATOM   4523  O   PRO C 213       4.137  56.172 303.700  1.00 37.93           O  
ANISOU 4523  O   PRO C 213     4865   3297   6249   2969  -1061   -857       O  
ATOM   4524  CB  PRO C 213       4.217  56.660 307.175  1.00 36.11           C  
ANISOU 4524  CB  PRO C 213     4287   3183   6251   2697   -804   -857       C  
ATOM   4525  CG  PRO C 213       3.093  57.622 306.979  1.00 42.72           C  
ANISOU 4525  CG  PRO C 213     5166   4036   7028   2952   -906   -928       C  
ATOM   4526  CD  PRO C 213       3.687  58.776 306.212  1.00 39.02           C  
ANISOU 4526  CD  PRO C 213     5050   3370   6406   3062   -894   -860       C  
ATOM   4527  N   LYS C 214       4.607  54.476 305.127  1.00 31.87           N  
ANISOU 4527  N   LYS C 214     3730   2677   5701   2610   -937   -850       N  
ATOM   4528  CA  LYS C 214       4.237  53.377 304.247  1.00 31.68           C  
ANISOU 4528  CA  LYS C 214     3633   2715   5688   2619  -1059   -897       C  
ATOM   4529  C   LYS C 214       2.731  53.366 303.819  1.00 37.37           C  
ANISOU 4529  C   LYS C 214     4226   3551   6423   2802  -1258  -1011       C  
ATOM   4530  O   LYS C 214       2.496  53.054 302.644  1.00 37.51           O  
ANISOU 4530  O   LYS C 214     4343   3546   6365   2906  -1390  -1038       O  
ATOM   4531  CB  LYS C 214       4.609  52.030 304.890  1.00 32.36           C  
ANISOU 4531  CB  LYS C 214     3514   2879   5901   2387  -1002   -891       C  
ATOM   4532  CG  LYS C 214       4.830  50.910 303.870  1.00 44.90           C  
ANISOU 4532  CG  LYS C 214     5130   4462   7468   2356  -1082   -900       C  
ATOM   4533  CD  LYS C 214       5.219  49.590 304.515  1.00 51.92           C  
ANISOU 4533  CD  LYS C 214     5841   5411   8477   2134  -1028   -892       C  
ATOM   4534  CE  LYS C 214       5.370  48.494 303.494  1.00 61.89           C  
ANISOU 4534  CE  LYS C 214     7146   6659   9709   2120  -1120   -912       C  
ATOM   4535  NZ  LYS C 214       5.940  47.261 304.095  1.00 71.02           N  
ANISOU 4535  NZ  LYS C 214     8169   7846  10967   1910  -1059   -895       N  
ATOM   4536  N   PRO C 215       1.708  53.658 304.685  1.00 34.27           N  
ANISOU 4536  N   PRO C 215     3615   3286   6122   2849  -1290  -1081       N  
ATOM   4537  CA  PRO C 215       0.310  53.516 304.229  1.00 35.59           C  
ANISOU 4537  CA  PRO C 215     3624   3579   6320   3012  -1485  -1189       C  
ATOM   4538  C   PRO C 215      -0.065  54.454 303.086  1.00 41.05           C  
ANISOU 4538  C   PRO C 215     4549   4186   6863   3280  -1619  -1210       C  
ATOM   4539  O   PRO C 215       0.088  55.670 303.202  1.00 42.08           O  
ANISOU 4539  O   PRO C 215     4862   4222   6904   3406  -1565  -1178       O  
ATOM   4540  CB  PRO C 215      -0.512  53.798 305.491  1.00 37.55           C  
ANISOU 4540  CB  PRO C 215     3615   3967   6684   3011  -1440  -1240       C  
ATOM   4541  CG  PRO C 215       0.401  54.545 306.391  1.00 40.53           C  
ANISOU 4541  CG  PRO C 215     4123   4246   7032   2935  -1247  -1161       C  
ATOM   4542  CD  PRO C 215       1.752  53.997 306.124  1.00 34.65           C  
ANISOU 4542  CD  PRO C 215     3528   3382   6254   2752  -1152  -1069       C  
ATOM   4543  N   VAL C 216      -0.531  53.867 301.968  1.00 37.79           N  
ANISOU 4543  N   VAL C 216     4150   3793   6414   3363  -1802  -1262       N  
ATOM   4544  CA  VAL C 216      -0.928  54.592 300.762  1.00 39.65           C  
ANISOU 4544  CA  VAL C 216     4616   3949   6499   3622  -1960  -1287       C  
ATOM   4545  C   VAL C 216      -2.109  53.868 300.093  1.00 48.51           C  
ANISOU 4545  C   VAL C 216     5556   5202   7675   3716  -2209  -1401       C  
ATOM   4546  O   VAL C 216      -2.270  52.656 300.275  1.00 48.45           O  
ANISOU 4546  O   VAL C 216     5331   5292   7786   3544  -2244  -1434       O  
ATOM   4547  CB  VAL C 216       0.275  54.803 299.796  1.00 42.32           C  
ANISOU 4547  CB  VAL C 216     5328   4090   6664   3624  -1892  -1190       C  
ATOM   4548  CG1 VAL C 216       0.585  53.554 298.975  1.00 41.59           C  
ANISOU 4548  CG1 VAL C 216     5248   3994   6561   3525  -1956  -1195       C  
ATOM   4549  CG2 VAL C 216       0.062  56.012 298.892  1.00 43.81           C  
ANISOU 4549  CG2 VAL C 216     5817   4156   6672   3893  -1984  -1184       C  
ATOM   4550  N   TRP C 217      -2.935  54.630 299.343  1.00 48.81           N  
ANISOU 4550  N   TRP C 217     5686   5234   7625   3986  -2389  -1460       N  
ATOM   4551  CA  TRP C 217      -4.115  54.171 298.611  1.00 51.72           C  
ANISOU 4551  CA  TRP C 217     5907   5716   8028   4117  -2658  -1572       C  
ATOM   4552  C   TRP C 217      -3.981  54.598 297.156  1.00 57.10           C  
ANISOU 4552  C   TRP C 217     6944   6249   8501   4328  -2809  -1567       C  
ATOM   4553  O   TRP C 217      -4.116  55.784 296.852  1.00 57.83           O  
ANISOU 4553  O   TRP C 217     7251   6254   8468   4553  -2836  -1554       O  
ATOM   4554  CB  TRP C 217      -5.396  54.756 299.243  1.00 53.00           C  
ANISOU 4554  CB  TRP C 217     5793   6044   8301   4269  -2745  -1662       C  
ATOM   4555  CG  TRP C 217      -6.676  54.191 298.699  1.00 57.02           C  
ANISOU 4555  CG  TRP C 217     6063   6708   8896   4365  -3017  -1783       C  
ATOM   4556  CD1 TRP C 217      -7.354  53.108 299.172  1.00 60.49           C  
ANISOU 4556  CD1 TRP C 217     6127   7326   9529   4192  -3075  -1846       C  
ATOM   4557  CD2 TRP C 217      -7.448  54.699 297.597  1.00 59.53           C  
ANISOU 4557  CD2 TRP C 217     6497   7011   9112   4651  -3277  -1854       C  
ATOM   4558  NE1 TRP C 217      -8.498  52.903 298.431  1.00 62.75           N  
ANISOU 4558  NE1 TRP C 217     6274   7717   9852   4342  -3359  -1954       N  
ATOM   4559  CE2 TRP C 217      -8.579  53.864 297.457  1.00 65.34           C  
ANISOU 4559  CE2 TRP C 217     6898   7931   9999   4632  -3494  -1964       C  
ATOM   4560  CE3 TRP C 217      -7.293  55.778 296.710  1.00 62.02           C  
ANISOU 4560  CE3 TRP C 217     7177   7169   9219   4919  -3353  -1833       C  
ATOM   4561  CZ2 TRP C 217      -9.541  54.064 296.460  1.00 67.29           C  
ANISOU 4561  CZ2 TRP C 217     7152   8215  10201   4877  -3795  -2059       C  
ATOM   4562  CZ3 TRP C 217      -8.252  55.982 295.729  1.00 66.23           C  
ANISOU 4562  CZ3 TRP C 217     7735   7733   9695   5172  -3647  -1925       C  
ATOM   4563  CH2 TRP C 217      -9.357  55.129 295.607  1.00 68.47           C  
ANISOU 4563  CH2 TRP C 217     7671   8207  10137   5153  -3870  -2039       C  
ATOM   4564  N   VAL C 218      -3.665  53.645 296.262  1.00 53.34           N  
ANISOU 4564  N   VAL C 218     6563   5728   7975   4258  -2899  -1571       N  
ATOM   4565  CA  VAL C 218      -3.496  53.919 294.826  1.00 53.89           C  
ANISOU 4565  CA  VAL C 218     6991   5653   7830   4448  -3040  -1564       C  
ATOM   4566  C   VAL C 218      -4.464  53.026 294.040  1.00 57.60           C  
ANISOU 4566  C   VAL C 218     7329   6218   8339   4501  -3333  -1681       C  
ATOM   4567  O   VAL C 218      -4.257  51.811 293.974  1.00 57.27           O  
ANISOU 4567  O   VAL C 218     7176   6212   8372   4307  -3345  -1696       O  
ATOM   4568  CB  VAL C 218      -2.015  53.729 294.376  1.00 56.15           C  
ANISOU 4568  CB  VAL C 218     7600   5760   7974   4331  -2845  -1444       C  
ATOM   4569  CG1 VAL C 218      -1.835  54.017 292.886  1.00 57.51           C  
ANISOU 4569  CG1 VAL C 218     8159   5782   7909   4530  -2973  -1432       C  
ATOM   4570  CG2 VAL C 218      -1.065  54.590 295.206  1.00 54.32           C  
ANISOU 4570  CG2 VAL C 218     7475   5440   7725   4258  -2570  -1331       C  
ATOM   4571  N   LYS C 219      -5.522  53.616 293.464  1.00 54.39           N  
ANISOU 4571  N   LYS C 219     6932   5848   7884   4762  -3578  -1766       N  
ATOM   4572  CA  LYS C 219      -6.510  52.848 292.701  1.00 55.61           C  
ANISOU 4572  CA  LYS C 219     6957   6094   8077   4830  -3891  -1885       C  
ATOM   4573  C   LYS C 219      -6.962  53.585 291.440  1.00 60.37           C  
ANISOU 4573  C   LYS C 219     7861   6601   8477   5151  -4130  -1924       C  
ATOM   4574  O   LYS C 219      -7.194  54.795 291.489  1.00 61.08           O  
ANISOU 4574  O   LYS C 219     8064   6652   8490   5364  -4124  -1911       O  
ATOM   4575  CB  LYS C 219      -7.723  52.509 293.578  1.00 59.01           C  
ANISOU 4575  CB  LYS C 219     6895   6764   8762   4775  -3992  -1985       C  
ATOM   4576  N   TRP C 220      -7.079  52.849 290.311  1.00 56.80           N  
ANISOU 4576  N   TRP C 220     7555   6098   7928   5190  -4346  -1975       N  
ATOM   4577  CA  TRP C 220      -7.518  53.381 289.015  1.00 58.71           C  
ANISOU 4577  CA  TRP C 220     8102   6242   7962   5489  -4605  -2019       C  
ATOM   4578  C   TRP C 220      -8.987  53.782 289.076  1.00 66.60           C  
ANISOU 4578  C   TRP C 220     8829   7403   9073   5691  -4885  -2144       C  
ATOM   4579  O   TRP C 220      -9.778  53.133 289.764  1.00 66.19           O  
ANISOU 4579  O   TRP C 220     8337   7550   9260   5564  -4970  -2227       O  
ATOM   4580  CB  TRP C 220      -7.283  52.370 287.876  1.00 57.53           C  
ANISOU 4580  CB  TRP C 220     8162   6007   7691   5459  -4766  -2049       C  
ATOM   4581  CG  TRP C 220      -5.851  52.264 287.440  1.00 56.24           C  
ANISOU 4581  CG  TRP C 220     8384   5649   7336   5375  -4522  -1925       C  
ATOM   4582  CD1 TRP C 220      -4.920  51.381 287.900  1.00 56.66           C  
ANISOU 4582  CD1 TRP C 220     8382   5689   7458   5102  -4296  -1862       C  
ATOM   4583  CD2 TRP C 220      -5.184  53.079 286.464  1.00 56.58           C  
ANISOU 4583  CD2 TRP C 220     8921   5486   7089   5572  -4473  -1845       C  
ATOM   4584  NE1 TRP C 220      -3.714  51.596 287.275  1.00 55.15           N  
ANISOU 4584  NE1 TRP C 220     8598   5310   7047   5119  -4106  -1750       N  
ATOM   4585  CE2 TRP C 220      -3.848  52.629 286.385  1.00 58.42           C  
ANISOU 4585  CE2 TRP C 220     9357   5604   7237   5397  -4203  -1734       C  
ATOM   4586  CE3 TRP C 220      -5.584  54.154 285.650  1.00 59.86           C  
ANISOU 4586  CE3 TRP C 220     9636   5804   7306   5882  -4630  -1852       C  
ATOM   4587  CZ2 TRP C 220      -2.910  53.215 285.523  1.00 58.01           C  
ANISOU 4587  CZ2 TRP C 220     9778   5350   6914   5511  -4071  -1628       C  
ATOM   4588  CZ3 TRP C 220      -4.651  54.749 284.813  1.00 61.32           C  
ANISOU 4588  CZ3 TRP C 220    10312   5775   7212   5991  -4500  -1744       C  
ATOM   4589  CH2 TRP C 220      -3.333  54.279 284.751  1.00 60.09           C  
ANISOU 4589  CH2 TRP C 220    10334   5516   6983   5801  -4218  -1633       C  
ATOM   4590  N   MET C 221      -9.335  54.885 288.394  1.00 66.60           N  
ANISOU 4590  N   MET C 221     9088   7317   8901   6007  -5013  -2152       N  
ATOM   4591  CA  MET C 221     -10.685  55.454 288.380  1.00 69.99           C  
ANISOU 4591  CA  MET C 221     9305   7882   9404   6258  -5279  -2264       C  
ATOM   4592  C   MET C 221     -11.136  55.834 286.972  1.00 78.22           C  
ANISOU 4592  C   MET C 221    10686   8812  10222   6568  -5595  -2318       C  
ATOM   4593  O   MET C 221     -10.309  56.223 286.146  1.00 78.24           O  
ANISOU 4593  O   MET C 221    11170   8595   9963   6660  -5528  -2233       O  
ATOM   4594  CB  MET C 221     -10.756  56.730 289.257  1.00 72.12           C  
ANISOU 4594  CB  MET C 221     9533   8168   9702   6380  -5100  -2221       C  
ATOM   4595  CG  MET C 221      -9.949  56.689 290.548  1.00 72.91           C  
ANISOU 4595  CG  MET C 221     9470   8297   9934   6107  -4732  -2130       C  
ATOM   4596  SD  MET C 221     -10.745  55.763 291.878  1.00 77.03           S  
ANISOU 4596  SD  MET C 221     9336   9118  10814   5864  -4707  -2213       S  
ATOM   4597  CE  MET C 221     -11.973  56.966 292.420  1.00 76.31           C  
ANISOU 4597  CE  MET C 221     9016   9174  10805   6167  -4808  -2292       C  
ATOM   4598  N   ARG C 222     -12.453  55.773 286.716  1.00 77.87           N  
ANISOU 4598  N   ARG C 222    10388   8920  10277   6737  -5937  -2455       N  
ATOM   4599  CA  ARG C 222     -13.036  56.232 285.456  1.00 80.94           C  
ANISOU 4599  CA  ARG C 222    11065   9222  10467   7066  -6277  -2521       C  
ATOM   4600  C   ARG C 222     -13.322  57.719 285.649  1.00 87.23           C  
ANISOU 4600  C   ARG C 222    11981   9983  11181   7369  -6262  -2503       C  
ATOM   4601  O   ARG C 222     -12.934  58.553 284.829  1.00 88.29           O  
ANISOU 4601  O   ARG C 222    12587   9915  11044   7609  -6313  -2455       O  
ATOM   4602  CB  ARG C 222     -14.297  55.413 285.093  1.00 82.98           C  
ANISOU 4602  CB  ARG C 222    10980   9663  10884   7093  -6670  -2681       C  
ATOM   4603  CG  ARG C 222     -15.119  55.914 283.885  1.00 90.17           C  
ANISOU 4603  CG  ARG C 222    12111  10523  11625   7460  -7075  -2773       C  
ATOM   4604  CD  ARG C 222     -14.398  55.895 282.538  1.00 89.95           C  
ANISOU 4604  CD  ARG C 222    12678  10238  11263   7568  -7157  -2726       C  
ATOM   4605  NE  ARG C 222     -14.006  54.548 282.121  1.00 91.31           N  
ANISOU 4605  NE  ARG C 222    12853  10393  11448   7331  -7227  -2754       N  
ATOM   4606  CZ  ARG C 222     -13.406  54.265 280.968  1.00102.39           C  
ANISOU 4606  CZ  ARG C 222    14729  11592  12581   7384  -7296  -2726       C  
ATOM   4607  NH1 ARG C 222     -13.138  55.231 280.096  1.00 86.19           N  
ANISOU 4607  NH1 ARG C 222    13186   9337  10223   7656  -7303  -2664       N  
ATOM   4608  NH2 ARG C 222     -13.076  53.014 280.676  1.00 88.63           N  
ANISOU 4608  NH2 ARG C 222    12968   9842  10866   7168  -7357  -2760       N  
ATOM   4609  N   GLY C 223     -13.947  58.016 286.781  1.00 84.02           N  
ANISOU 4609  N   GLY C 223    11154   9765  11004   7344  -6171  -2535       N  
ATOM   4610  CA  GLY C 223     -14.271  59.349 287.263  1.00 84.92           C  
ANISOU 4610  CA  GLY C 223    11292   9880  11094   7598  -6121  -2526       C  
ATOM   4611  C   GLY C 223     -14.312  59.239 288.767  1.00 87.28           C  
ANISOU 4611  C   GLY C 223    11158  10355  11649   7393  -5855  -2513       C  
ATOM   4612  O   GLY C 223     -13.272  59.054 289.407  1.00 83.60           O  
ANISOU 4612  O   GLY C 223    10776   9807  11180   7155  -5522  -2402       O  
ATOM   4613  N   GLU C 224     -15.523  59.253 289.326  1.00 86.46           N  
ANISOU 4613  N   GLU C 224    10574  10503  11772   7472  -6007  -2629       N  
ATOM   4614  CA  GLU C 224     -15.743  59.055 290.754  1.00 85.33           C  
ANISOU 4614  CA  GLU C 224     9974  10562  11887   7286  -5779  -2633       C  
ATOM   4615  C   GLU C 224     -15.748  57.551 291.053  1.00 88.14           C  
ANISOU 4615  C   GLU C 224     9967  11066  12455   6921  -5758  -2658       C  
ATOM   4616  O   GLU C 224     -15.335  57.134 292.138  1.00 85.01           O  
ANISOU 4616  O   GLU C 224     9347  10746  12208   6651  -5478  -2607       O  
ATOM   4617  CB  GLU C 224     -17.064  59.714 291.189  1.00 89.63           C  
ANISOU 4617  CB  GLU C 224    10174  11312  12567   7564  -5932  -2741       C  
ATOM   4618  CG  GLU C 224     -16.912  61.168 291.603  1.00 99.85           C  
ANISOU 4618  CG  GLU C 224    11704  12500  13735   7816  -5780  -2692       C  
ATOM   4619  CD  GLU C 224     -16.597  61.388 293.071  1.00114.67           C  
ANISOU 4619  CD  GLU C 224    13376  14448  15744   7636  -5419  -2634       C  
ATOM   4620  OE1 GLU C 224     -17.485  61.899 293.791  1.00115.93           O  
ANISOU 4620  OE1 GLU C 224    13202  14797  16050   7784  -5415  -2703       O  
ATOM   4621  OE2 GLU C 224     -15.466  61.060 293.502  1.00 95.80           O  
ANISOU 4621  OE2 GLU C 224    11163  11927  13309   7358  -5142  -2521       O  
ATOM   4622  N   GLN C 225     -16.193  56.746 290.058  1.00 86.86           N  
ANISOU 4622  N   GLN C 225     9777  10929  12295   6914  -6065  -2737       N  
ATOM   4623  CA  GLN C 225     -16.311  55.290 290.111  1.00 86.39           C  
ANISOU 4623  CA  GLN C 225     9418  10988  12419   6591  -6115  -2776       C  
ATOM   4624  C   GLN C 225     -14.950  54.596 290.082  1.00 87.67           C  
ANISOU 4624  C   GLN C 225     9864  10968  12477   6304  -5878  -2663       C  
ATOM   4625  O   GLN C 225     -14.139  54.859 289.190  1.00 86.53           O  
ANISOU 4625  O   GLN C 225    10207  10594  12075   6396  -5875  -2600       O  
ATOM   4626  CB  GLN C 225     -17.177  54.783 288.949  1.00 90.80           C  
ANISOU 4626  CB  GLN C 225     9916  11601  12982   6710  -6549  -2900       C  
ATOM   4627  N   GLU C 226     -14.721  53.694 291.058  1.00 83.05           N  
ANISOU 4627  N   GLU C 226     8970  10493  12094   5961  -5679  -2638       N  
ATOM   4628  CA  GLU C 226     -13.500  52.892 291.203  1.00 80.29           C  
ANISOU 4628  CA  GLU C 226     8807  10007  11692   5665  -5450  -2540       C  
ATOM   4629  C   GLU C 226     -13.409  51.810 290.126  1.00 85.46           C  
ANISOU 4629  C   GLU C 226     9598  10590  12284   5577  -5683  -2585       C  
ATOM   4630  O   GLU C 226     -14.441  51.333 289.636  1.00 87.56           O  
ANISOU 4630  O   GLU C 226     9640  10977  12650   5625  -6002  -2704       O  
ATOM   4631  CB  GLU C 226     -13.451  52.227 292.591  1.00 79.74           C  
ANISOU 4631  CB  GLU C 226     8342  10090  11867   5345  -5195  -2510       C  
ATOM   4632  CG  GLU C 226     -12.837  53.087 293.683  1.00 89.03           C  
ANISOU 4632  CG  GLU C 226     9537  11249  13040   5346  -4860  -2419       C  
ATOM   4633  CD  GLU C 226     -12.834  52.490 295.080  1.00108.23           C  
ANISOU 4633  CD  GLU C 226    11595  13831  15698   5052  -4615  -2391       C  
ATOM   4634  OE1 GLU C 226     -13.019  53.263 296.047  1.00104.59           O  
ANISOU 4634  OE1 GLU C 226    10968  13461  15309   5117  -4453  -2379       O  
ATOM   4635  OE2 GLU C 226     -12.637  51.260 295.214  1.00 99.20           O  
ANISOU 4635  OE2 GLU C 226    10342  12704  14647   4764  -4583  -2381       O  
ATOM   4636  N   GLN C 227     -12.175  51.409 289.773  1.00 80.27           N  
ANISOU 4636  N   GLN C 227     9300   9736  11464   5446  -5524  -2494       N  
ATOM   4637  CA  GLN C 227     -11.961  50.342 288.801  1.00 80.92           C  
ANISOU 4637  CA  GLN C 227     9553   9728  11466   5356  -5707  -2529       C  
ATOM   4638  C   GLN C 227     -11.785  49.028 289.545  1.00 84.27           C  
ANISOU 4638  C   GLN C 227     9687  10239  12094   4987  -5595  -2526       C  
ATOM   4639  O   GLN C 227     -10.927  48.922 290.423  1.00 80.82           O  
ANISOU 4639  O   GLN C 227     9237   9774  11696   4793  -5269  -2427       O  
ATOM   4640  CB  GLN C 227     -10.778  50.631 287.861  1.00 81.14           C  
ANISOU 4640  CB  GLN C 227    10152   9494  11183   5455  -5615  -2438       C  
ATOM   4641  CG  GLN C 227     -11.102  51.619 286.740  1.00 95.34           C  
ANISOU 4641  CG  GLN C 227    12294  11184  12748   5823  -5822  -2462       C  
ATOM   4642  CD  GLN C 227     -12.308  51.223 285.914  1.00115.52           C  
ANISOU 4642  CD  GLN C 227    14769  13808  15315   5972  -6261  -2606       C  
ATOM   4643  OE1 GLN C 227     -12.420  50.091 285.422  1.00110.07           O  
ANISOU 4643  OE1 GLN C 227    14098  13097  14625   5850  -6430  -2661       O  
ATOM   4644  NE2 GLN C 227     -13.245  52.149 285.758  1.00109.21           N  
ANISOU 4644  NE2 GLN C 227    13879  13090  14525   6247  -6466  -2675       N  
ATOM   4645  N   GLN C 228     -12.649  48.050 289.226  1.00 83.74           N  
ANISOU 4645  N   GLN C 228     9380  10276  12162   4892  -5879  -2637       N  
ATOM   4646  CA  GLN C 228     -12.676  46.725 289.848  1.00 82.94           C  
ANISOU 4646  CA  GLN C 228     8990  10258  12264   4545  -5834  -2651       C  
ATOM   4647  C   GLN C 228     -11.377  45.939 289.577  1.00 84.27           C  
ANISOU 4647  C   GLN C 228     9490  10235  12296   4370  -5671  -2572       C  
ATOM   4648  O   GLN C 228     -10.805  45.373 290.513  1.00 81.72           O  
ANISOU 4648  O   GLN C 228     9016   9938  12097   4098  -5438  -2514       O  
ATOM   4649  CB  GLN C 228     -13.921  45.913 289.402  1.00 87.51           C  
ANISOU 4649  CB  GLN C 228     9275  10971  13001   4502  -6216  -2792       C  
ATOM   4650  CG  GLN C 228     -14.193  45.856 287.888  1.00104.04           C  
ANISOU 4650  CG  GLN C 228    11685  12946  14901   4721  -6582  -2875       C  
ATOM   4651  CD  GLN C 228     -15.163  44.760 287.513  1.00123.25           C  
ANISOU 4651  CD  GLN C 228    13853  15480  17497   4590  -6935  -3003       C  
ATOM   4652  OE1 GLN C 228     -16.358  45.001 287.303  1.00121.48           O  
ANISOU 4652  OE1 GLN C 228    13347  15413  17397   4713  -7213  -3107       O  
ATOM   4653  NE2 GLN C 228     -14.665  43.533 287.393  1.00111.01           N  
ANISOU 4653  NE2 GLN C 228    12393  13837  15949   4341  -6939  -3001       N  
ATOM   4654  N   GLY C 229     -10.905  45.973 288.328  1.00 81.08           N  
ANISOU 4654  N   GLY C 229     9535   9641  11630   4540  -5786  -2568       N  
ATOM   4655  CA  GLY C 229      -9.708  45.270 287.879  1.00 79.07           C  
ANISOU 4655  CA  GLY C 229     9626   9200  11216   4425  -5653  -2502       C  
ATOM   4656  C   GLY C 229      -8.372  45.878 288.262  1.00 79.57           C  
ANISOU 4656  C   GLY C 229     9946   9141  11148   4420  -5270  -2355       C  
ATOM   4657  O   GLY C 229      -7.348  45.507 287.676  1.00 78.41           O  
ANISOU 4657  O   GLY C 229    10155   8823  10813   4410  -5172  -2297       O  
ATOM   4658  N   THR C 230      -8.360  46.808 289.247  1.00 73.95           N  
ANISOU 4658  N   THR C 230     9052   8513  10531   4423  -5049  -2295       N  
ATOM   4659  CA  THR C 230      -7.140  47.466 289.725  1.00 70.69           C  
ANISOU 4659  CA  THR C 230     8845   7994  10018   4402  -4691  -2156       C  
ATOM   4660  C   THR C 230      -6.289  46.421 290.448  1.00 71.15           C  
ANISOU 4660  C   THR C 230     8808   8046  10181   4092  -4462  -2095       C  
ATOM   4661  O   THR C 230      -6.751  45.795 291.406  1.00 70.20           O  
ANISOU 4661  O   THR C 230     8311   8071  10293   3884  -4427  -2121       O  
ATOM   4662  CB  THR C 230      -7.466  48.697 290.596  1.00 77.08           C  
ANISOU 4662  CB  THR C 230     9499   8891  10898   4508  -4563  -2125       C  
ATOM   4663  OG1 THR C 230      -8.376  49.540 289.891  1.00 78.44           O  
ANISOU 4663  OG1 THR C 230     9732   9082  10991   4803  -4820  -2200       O  
ATOM   4664  CG2 THR C 230      -6.224  49.502 290.963  1.00 72.41           C  
ANISOU 4664  CG2 THR C 230     9167   8166  10179   4511  -4230  -1985       C  
ATOM   4665  N   GLN C 231      -5.067  46.207 289.934  1.00 65.68           N  
ANISOU 4665  N   GLN C 231     8464   7181   9309   4069  -4313  -2015       N  
ATOM   4666  CA  GLN C 231      -4.108  45.233 290.443  1.00 62.71           C  
ANISOU 4666  CA  GLN C 231     8065   6769   8992   3813  -4101  -1953       C  
ATOM   4667  C   GLN C 231      -2.908  45.936 291.100  1.00 62.10           C  
ANISOU 4667  C   GLN C 231     8101   6627   8869   3771  -3741  -1814       C  
ATOM   4668  O   GLN C 231      -1.956  46.323 290.415  1.00 59.94           O  
ANISOU 4668  O   GLN C 231     8184   6202   8388   3877  -3623  -1737       O  
ATOM   4669  CB  GLN C 231      -3.657  44.279 289.320  1.00 64.88           C  
ANISOU 4669  CB  GLN C 231     8632   6909   9111   3816  -4213  -1977       C  
ATOM   4670  CG  GLN C 231      -4.584  43.086 289.117  1.00 84.50           C  
ANISOU 4670  CG  GLN C 231    10929   9462  11715   3714  -4511  -2103       C  
ATOM   4671  CD  GLN C 231      -4.298  41.998 290.122  1.00108.42           C  
ANISOU 4671  CD  GLN C 231    13697  12553  14944   3406  -4389  -2090       C  
ATOM   4672  OE1 GLN C 231      -4.828  41.991 291.238  1.00104.64           O  
ANISOU 4672  OE1 GLN C 231    12845  12226  14689   3259  -4343  -2099       O  
ATOM   4673  NE2 GLN C 231      -3.424  41.070 289.760  1.00101.93           N  
ANISOU 4673  NE2 GLN C 231    13081  11610  14038   3310  -4323  -2064       N  
ATOM   4674  N   PRO C 232      -2.948  46.109 292.443  1.00 57.93           N  
ANISOU 4674  N   PRO C 232     7270   6210   8530   3613  -3565  -1779       N  
ATOM   4675  CA  PRO C 232      -1.824  46.767 293.129  1.00 55.64           C  
ANISOU 4675  CA  PRO C 232     7078   5856   8205   3561  -3242  -1652       C  
ATOM   4676  C   PRO C 232      -0.621  45.848 293.310  1.00 57.57           C  
ANISOU 4676  C   PRO C 232     7403   6026   8445   3361  -3049  -1579       C  
ATOM   4677  O   PRO C 232      -0.764  44.622 293.383  1.00 57.14           O  
ANISOU 4677  O   PRO C 232     7212   6010   8490   3201  -3124  -1626       O  
ATOM   4678  CB  PRO C 232      -2.415  47.152 294.486  1.00 56.83           C  
ANISOU 4678  CB  PRO C 232     6875   6160   8558   3475  -3162  -1659       C  
ATOM   4679  CG  PRO C 232      -3.474  46.139 294.741  1.00 62.41           C  
ANISOU 4679  CG  PRO C 232     7250   7013   9449   3357  -3357  -1765       C  
ATOM   4680  CD  PRO C 232      -4.011  45.717 293.396  1.00 60.06           C  
ANISOU 4680  CD  PRO C 232     7104   6668   9049   3473  -3646  -1851       C  
ATOM   4681  N   GLY C 233       0.551  46.464 293.393  1.00 52.60           N  
ANISOU 4681  N   GLY C 233     6993   5287   7704   3374  -2804  -1464       N  
ATOM   4682  CA  GLY C 233       1.807  45.766 293.616  1.00 50.39           C  
ANISOU 4682  CA  GLY C 233     6791   4938   7415   3209  -2592  -1382       C  
ATOM   4683  C   GLY C 233       2.205  45.793 295.077  1.00 51.36           C  
ANISOU 4683  C   GLY C 233     6667   5134   7714   3005  -2380  -1323       C  
ATOM   4684  O   GLY C 233       1.419  46.199 295.940  1.00 50.57           O  
ANISOU 4684  O   GLY C 233     6312   5150   7753   2973  -2408  -1358       O  
ATOM   4685  N   ASP C 234       3.423  45.334 295.363  1.00 46.08           N  
ANISOU 4685  N   ASP C 234     6069   4402   7037   2871  -2169  -1237       N  
ATOM   4686  CA  ASP C 234       3.971  45.332 296.714  1.00 43.72           C  
ANISOU 4686  CA  ASP C 234     5574   4153   6885   2678  -1964  -1173       C  
ATOM   4687  C   ASP C 234       4.521  46.715 297.008  1.00 45.10           C  
ANISOU 4687  C   ASP C 234     5852   4280   7005   2743  -1789  -1084       C  
ATOM   4688  O   ASP C 234       4.984  47.393 296.085  1.00 45.28           O  
ANISOU 4688  O   ASP C 234     6154   4194   6856   2890  -1753  -1036       O  
ATOM   4689  CB  ASP C 234       5.073  44.262 296.859  1.00 44.85           C  
ANISOU 4689  CB  ASP C 234     5752   4245   7043   2520  -1830  -1121       C  
ATOM   4690  CG  ASP C 234       4.726  42.864 296.361  1.00 59.99           C  
ANISOU 4690  CG  ASP C 234     7639   6170   8983   2462  -1996  -1200       C  
ATOM   4691  OD1 ASP C 234       3.524  42.499 296.387  1.00 62.29           O  
ANISOU 4691  OD1 ASP C 234     7747   6550   9371   2440  -2195  -1297       O  
ATOM   4692  OD2 ASP C 234       5.662  42.118 295.985  1.00 66.15           O  
ANISOU 4692  OD2 ASP C 234     8572   6869   9694   2432  -1923  -1166       O  
ATOM   4693  N   ILE C 235       4.455  47.146 298.273  1.00 39.52           N  
ANISOU 4693  N   ILE C 235     4938   3645   6434   2633  -1682  -1062       N  
ATOM   4694  CA  ILE C 235       4.972  48.456 298.681  1.00 38.57           C  
ANISOU 4694  CA  ILE C 235     4912   3471   6272   2674  -1521   -981       C  
ATOM   4695  C   ILE C 235       6.460  48.238 299.012  1.00 41.55           C  
ANISOU 4695  C   ILE C 235     5373   3772   6644   2527  -1294   -871       C  
ATOM   4696  O   ILE C 235       6.822  47.933 300.155  1.00 40.35           O  
ANISOU 4696  O   ILE C 235     5041   3668   6622   2350  -1182   -843       O  
ATOM   4697  CB  ILE C 235       4.140  49.107 299.830  1.00 41.37           C  
ANISOU 4697  CB  ILE C 235     5034   3931   6755   2654  -1523  -1016       C  
ATOM   4698  CG1 ILE C 235       2.620  49.085 299.532  1.00 43.58           C  
ANISOU 4698  CG1 ILE C 235     5167   4318   7072   2784  -1757  -1135       C  
ATOM   4699  CG2 ILE C 235       4.595  50.529 300.101  1.00 41.59           C  
ANISOU 4699  CG2 ILE C 235     5211   3878   6712   2729  -1393   -943       C  
ATOM   4700  CD1 ILE C 235       1.840  47.876 300.138  1.00 52.18           C  
ANISOU 4700  CD1 ILE C 235     5932   5554   8341   2628  -1839  -1210       C  
ATOM   4701  N   LEU C 236       7.299  48.317 297.953  1.00 37.77           N  
ANISOU 4701  N   LEU C 236     5164   3178   6009   2608  -1235   -811       N  
ATOM   4702  CA  LEU C 236       8.752  48.094 297.928  1.00 35.81           C  
ANISOU 4702  CA  LEU C 236     5023   2855   5730   2506  -1029   -707       C  
ATOM   4703  C   LEU C 236       9.527  49.280 298.530  1.00 39.37           C  
ANISOU 4703  C   LEU C 236     5530   3248   6181   2460   -839   -604       C  
ATOM   4704  O   LEU C 236       9.102  50.420 298.348  1.00 40.31           O  
ANISOU 4704  O   LEU C 236     5765   3325   6227   2583   -867   -598       O  
ATOM   4705  CB  LEU C 236       9.201  47.845 296.482  1.00 36.69           C  
ANISOU 4705  CB  LEU C 236     5408   2873   5660   2636  -1042   -688       C  
ATOM   4706  CG  LEU C 236       8.369  46.840 295.679  1.00 42.13           C  
ANISOU 4706  CG  LEU C 236     6104   3591   6312   2714  -1261   -797       C  
ATOM   4707  CD1 LEU C 236       8.583  47.010 294.207  1.00 43.89           C  
ANISOU 4707  CD1 LEU C 236     6647   3711   6317   2904  -1304   -788       C  
ATOM   4708  CD2 LEU C 236       8.662  45.426 296.089  1.00 43.54           C  
ANISOU 4708  CD2 LEU C 236     6134   3812   6595   2557  -1252   -820       C  
ATOM   4709  N   PRO C 237      10.656  49.051 299.249  1.00 34.33           N  
ANISOU 4709  N   PRO C 237     4816   2602   5624   2286   -659   -525       N  
ATOM   4710  CA  PRO C 237      11.348  50.177 299.903  1.00 33.69           C  
ANISOU 4710  CA  PRO C 237     4776   2466   5558   2223   -500   -434       C  
ATOM   4711  C   PRO C 237      12.457  50.842 299.104  1.00 38.74           C  
ANISOU 4711  C   PRO C 237     5668   2985   6067   2259   -347   -322       C  
ATOM   4712  O   PRO C 237      13.002  50.245 298.183  1.00 39.65           O  
ANISOU 4712  O   PRO C 237     5910   3067   6088   2311   -320   -302       O  
ATOM   4713  CB  PRO C 237      11.953  49.533 301.148  1.00 33.90           C  
ANISOU 4713  CB  PRO C 237     4580   2553   5748   2011   -405   -411       C  
ATOM   4714  CG  PRO C 237      12.077  48.067 300.826  1.00 37.78           C  
ANISOU 4714  CG  PRO C 237     4997   3091   6269   1969   -451   -450       C  
ATOM   4715  CD  PRO C 237      11.288  47.760 299.594  1.00 34.71           C  
ANISOU 4715  CD  PRO C 237     4732   2693   5764   2139   -610   -522       C  
ATOM   4716  N   ASN C 238      12.825  52.065 299.505  1.00 35.47           N  
ANISOU 4716  N   ASN C 238     5327   2503   5648   2223   -239   -247       N  
ATOM   4717  CA  ASN C 238      13.937  52.800 298.905  1.00 36.55           C  
ANISOU 4717  CA  ASN C 238     5684   2522   5681   2219    -70   -126       C  
ATOM   4718  C   ASN C 238      15.097  52.834 299.901  1.00 41.20           C  
ANISOU 4718  C   ASN C 238     6149   3109   6395   2007    102    -39       C  
ATOM   4719  O   ASN C 238      14.901  52.448 301.060  1.00 39.08           O  
ANISOU 4719  O   ASN C 238     5657   2918   6273   1889     72    -80       O  
ATOM   4720  CB  ASN C 238      13.511  54.206 298.491  1.00 38.24           C  
ANISOU 4720  CB  ASN C 238     6124   2634   5771   2355   -102   -105       C  
ATOM   4721  CG  ASN C 238      12.459  54.245 297.408  1.00 63.28           C  
ANISOU 4721  CG  ASN C 238     9440   5798   8807   2581   -280   -184       C  
ATOM   4722  OD1 ASN C 238      12.546  53.557 296.381  1.00 55.54           O  
ANISOU 4722  OD1 ASN C 238     8567   4809   7725   2665   -307   -194       O  
ATOM   4723  ND2 ASN C 238      11.464  55.101 297.592  1.00 57.53           N  
ANISOU 4723  ND2 ASN C 238     8729   5066   8064   2696   -410   -244       N  
ATOM   4724  N   ALA C 239      16.307  53.254 299.450  1.00 40.52           N  
ANISOU 4724  N   ALA C 239     6204   2938   6252   1955    280     81       N  
ATOM   4725  CA  ALA C 239      17.508  53.356 300.297  1.00 40.88           C  
ANISOU 4725  CA  ALA C 239     6141   2976   6415   1753    442    172       C  
ATOM   4726  C   ALA C 239      17.233  54.308 301.465  1.00 45.94           C  
ANISOU 4726  C   ALA C 239     6716   3596   7143   1669    408    164       C  
ATOM   4727  O   ALA C 239      17.507  53.968 302.616  1.00 44.88           O  
ANISOU 4727  O   ALA C 239     6377   3522   7153   1522    418    152       O  
ATOM   4728  CB  ALA C 239      18.700  53.827 299.479  1.00 43.08           C  
ANISOU 4728  CB  ALA C 239     6605   3160   6603   1733    628    302       C  
ATOM   4729  N   ASP C 240      16.623  55.466 301.163  1.00 44.40           N  
ANISOU 4729  N   ASP C 240     6709   3314   6848   1781    355    160       N  
ATOM   4730  CA  ASP C 240      16.106  56.421 302.139  1.00 44.76           C  
ANISOU 4730  CA  ASP C 240     6736   3330   6940   1758    297    132       C  
ATOM   4731  C   ASP C 240      14.824  55.800 302.683  1.00 49.98           C  
ANISOU 4731  C   ASP C 240     7218   4112   7660   1836    131     -2       C  
ATOM   4732  O   ASP C 240      14.224  54.977 301.995  1.00 51.22           O  
ANISOU 4732  O   ASP C 240     7348   4336   7779   1944     41    -66       O  
ATOM   4733  CB  ASP C 240      15.861  57.794 301.492  1.00 48.33           C  
ANISOU 4733  CB  ASP C 240     7477   3638   7248   1878    294    173       C  
ATOM   4734  CG  ASP C 240      15.305  57.747 300.075  1.00 63.29           C  
ANISOU 4734  CG  ASP C 240     9572   5501   8973   2091    225    152       C  
ATOM   4735  OD1 ASP C 240      16.027  57.267 299.162  1.00 64.81           O  
ANISOU 4735  OD1 ASP C 240     9842   5683   9099   2093    314    209       O  
ATOM   4736  OD2 ASP C 240      14.184  58.247 299.865  1.00 70.61           O  
ANISOU 4736  OD2 ASP C 240    10597   6407   9826   2264     86     83       O  
ATOM   4737  N   GLU C 241      14.394  56.150 303.890  1.00 45.78           N  
ANISOU 4737  N   GLU C 241     6564   3610   7218   1781     89    -46       N  
ATOM   4738  CA  GLU C 241      13.230  55.534 304.505  1.00 44.82           C  
ANISOU 4738  CA  GLU C 241     6244   3617   7169   1830    -42   -164       C  
ATOM   4739  C   GLU C 241      11.974  56.127 303.889  1.00 48.25           C  
ANISOU 4739  C   GLU C 241     6787   4045   7501   2055   -179   -237       C  
ATOM   4740  O   GLU C 241      11.149  56.753 304.555  1.00 50.01           O  
ANISOU 4740  O   GLU C 241     6974   4285   7741   2122   -245   -295       O  
ATOM   4741  CB  GLU C 241      13.288  55.625 306.036  1.00 45.48           C  
ANISOU 4741  CB  GLU C 241     6162   3740   7377   1689    -17   -179       C  
ATOM   4742  CG  GLU C 241      14.160  54.520 306.616  1.00 56.23           C  
ANISOU 4742  CG  GLU C 241     7337   5169   8859   1499     52   -152       C  
ATOM   4743  CD  GLU C 241      15.169  54.890 307.688  1.00 77.02           C  
ANISOU 4743  CD  GLU C 241     9936   7755  11573   1314    153    -84       C  
ATOM   4744  OE1 GLU C 241      15.752  55.997 307.615  1.00 63.07           O  
ANISOU 4744  OE1 GLU C 241     8336   5868   9760   1293    215    -14       O  
ATOM   4745  OE2 GLU C 241      15.437  54.028 308.557  1.00 74.72           O  
ANISOU 4745  OE2 GLU C 241     9459   7540  11391   1182    166    -95       O  
ATOM   4746  N   THR C 242      11.762  55.756 302.599  1.00 41.62           N  
ANISOU 4746  N   THR C 242     6060   3196   6559   2183   -234   -247       N  
ATOM   4747  CA  THR C 242      10.620  56.059 301.720  1.00 41.03           C  
ANISOU 4747  CA  THR C 242     6094   3121   6374   2414   -389   -319       C  
ATOM   4748  C   THR C 242      10.175  54.744 301.060  1.00 41.36           C  
ANISOU 4748  C   THR C 242     6027   3264   6426   2452   -492   -387       C  
ATOM   4749  O   THR C 242      10.759  53.703 301.363  1.00 39.95           O  
ANISOU 4749  O   THR C 242     5708   3139   6332   2303   -429   -373       O  
ATOM   4750  CB  THR C 242      10.950  57.152 300.687  1.00 46.48           C  
ANISOU 4750  CB  THR C 242     7118   3651   6890   2536   -353   -244       C  
ATOM   4751  OG1 THR C 242      12.206  56.874 300.075  1.00 41.45           O  
ANISOU 4751  OG1 THR C 242     6592   2950   6208   2438   -207   -141       O  
ATOM   4752  CG2 THR C 242      10.920  58.554 301.276  1.00 45.20           C  
ANISOU 4752  CG2 THR C 242     7085   3382   6705   2545   -312   -206       C  
ATOM   4753  N   TRP C 243       9.133  54.769 300.200  1.00 36.66           N  
ANISOU 4753  N   TRP C 243     5493   2689   5746   2651   -661   -466       N  
ATOM   4754  CA  TRP C 243       8.603  53.554 299.571  1.00 35.93           C  
ANISOU 4754  CA  TRP C 243     5306   2683   5661   2688   -788   -542       C  
ATOM   4755  C   TRP C 243       8.229  53.762 298.089  1.00 41.19           C  
ANISOU 4755  C   TRP C 243     6222   3280   6148   2900   -903   -559       C  
ATOM   4756  O   TRP C 243       8.255  54.888 297.599  1.00 42.21           O  
ANISOU 4756  O   TRP C 243     6588   3300   6149   3029   -892   -516       O  
ATOM   4757  CB  TRP C 243       7.379  53.045 300.354  1.00 34.43           C  
ANISOU 4757  CB  TRP C 243     4827   2646   5609   2682   -929   -658       C  
ATOM   4758  CG  TRP C 243       7.640  52.750 301.803  1.00 33.87           C  
ANISOU 4758  CG  TRP C 243     4522   2648   5700   2484   -827   -648       C  
ATOM   4759  CD1 TRP C 243       7.513  53.612 302.853  1.00 36.48           C  
ANISOU 4759  CD1 TRP C 243     4799   2979   6082   2457   -766   -638       C  
ATOM   4760  CD2 TRP C 243       8.116  51.516 302.350  1.00 32.43           C  
ANISOU 4760  CD2 TRP C 243     4155   2533   5634   2294   -774   -645       C  
ATOM   4761  NE1 TRP C 243       7.882  52.991 304.024  1.00 34.46           N  
ANISOU 4761  NE1 TRP C 243     4338   2791   5964   2259   -679   -628       N  
ATOM   4762  CE2 TRP C 243       8.265  51.705 303.744  1.00 35.41           C  
ANISOU 4762  CE2 TRP C 243     4373   2952   6128   2155   -683   -630       C  
ATOM   4763  CE3 TRP C 243       8.413  50.258 301.802  1.00 33.17           C  
ANISOU 4763  CE3 TRP C 243     4217   2649   5736   2235   -804   -656       C  
ATOM   4764  CZ2 TRP C 243       8.692  50.678 304.595  1.00 33.37           C  
ANISOU 4764  CZ2 TRP C 243     3928   2759   5994   1961   -623   -622       C  
ATOM   4765  CZ3 TRP C 243       8.848  49.250 302.644  1.00 33.20           C  
ANISOU 4765  CZ3 TRP C 243     4035   2713   5867   2044   -742   -650       C  
ATOM   4766  CH2 TRP C 243       8.983  49.462 304.021  1.00 32.87           C  
ANISOU 4766  CH2 TRP C 243     3839   2713   5939   1909   -653   -631       C  
ATOM   4767  N   TYR C 244       7.892  52.666 297.381  1.00 37.84           N  
ANISOU 4767  N   TYR C 244     5763   2908   5708   2934  -1019   -621       N  
ATOM   4768  CA  TYR C 244       7.529  52.661 295.966  1.00 39.60           C  
ANISOU 4768  CA  TYR C 244     6218   3071   5757   3129  -1149   -649       C  
ATOM   4769  C   TYR C 244       6.410  51.656 295.697  1.00 44.68           C  
ANISOU 4769  C   TYR C 244     6698   3826   6453   3185  -1382   -780       C  
ATOM   4770  O   TYR C 244       6.505  50.499 296.110  1.00 43.45           O  
ANISOU 4770  O   TYR C 244     6341   3751   6416   3037  -1384   -812       O  
ATOM   4771  CB  TYR C 244       8.768  52.341 295.098  1.00 41.36           C  
ANISOU 4771  CB  TYR C 244     6665   3193   5857   3099   -998   -554       C  
ATOM   4772  CG  TYR C 244       8.468  51.953 293.662  1.00 45.90           C  
ANISOU 4772  CG  TYR C 244     7467   3718   6255   3278  -1129   -592       C  
ATOM   4773  CD1 TYR C 244       8.276  52.923 292.681  1.00 49.88           C  
ANISOU 4773  CD1 TYR C 244     8275   4112   6566   3479  -1178   -568       C  
ATOM   4774  CD2 TYR C 244       8.422  50.616 293.275  1.00 46.90           C  
ANISOU 4774  CD2 TYR C 244     7532   3893   6395   3247  -1204   -649       C  
ATOM   4775  CE1 TYR C 244       8.017  52.573 291.355  1.00 52.44           C  
ANISOU 4775  CE1 TYR C 244     8831   4383   6711   3650  -1305   -603       C  
ATOM   4776  CE2 TYR C 244       8.149  50.254 291.956  1.00 49.75           C  
ANISOU 4776  CE2 TYR C 244     8122   4199   6581   3416  -1335   -689       C  
ATOM   4777  CZ  TYR C 244       7.952  51.236 290.997  1.00 59.95           C  
ANISOU 4777  CZ  TYR C 244     9713   5387   7678   3619  -1384   -666       C  
ATOM   4778  OH  TYR C 244       7.696  50.886 289.695  1.00 63.54           O  
ANISOU 4778  OH  TYR C 244    10417   5781   7945   3792  -1519   -706       O  
ATOM   4779  N   LEU C 245       5.374  52.095 294.962  1.00 43.39           N  
ANISOU 4779  N   LEU C 245     6634   3658   6195   3398  -1584   -852       N  
ATOM   4780  CA  LEU C 245       4.222  51.287 294.560  1.00 44.14           C  
ANISOU 4780  CA  LEU C 245     6598   3849   6326   3474  -1839   -980       C  
ATOM   4781  C   LEU C 245       3.976  51.448 293.051  1.00 49.97           C  
ANISOU 4781  C   LEU C 245     7644   4491   6849   3696  -1990  -1003       C  
ATOM   4782  O   LEU C 245       4.273  52.499 292.477  1.00 49.82           O  
ANISOU 4782  O   LEU C 245     7907   4354   6669   3837  -1938   -938       O  
ATOM   4783  CB  LEU C 245       2.963  51.650 295.382  1.00 44.76           C  
ANISOU 4783  CB  LEU C 245     6406   4058   6543   3516  -1974  -1071       C  
ATOM   4784  CG  LEU C 245       1.673  50.915 295.016  1.00 51.36           C  
ANISOU 4784  CG  LEU C 245     7066   5009   7439   3588  -2249  -1205       C  
ATOM   4785  CD1 LEU C 245       1.793  49.452 295.289  1.00 50.56           C  
ANISOU 4785  CD1 LEU C 245     6772   4980   7460   3387  -2261  -1238       C  
ATOM   4786  CD2 LEU C 245       0.485  51.471 295.779  1.00 56.13           C  
ANISOU 4786  CD2 LEU C 245     7414   5742   8169   3655  -2352  -1281       C  
ATOM   4787  N   ARG C 246       3.442  50.387 292.420  1.00 48.29           N  
ANISOU 4787  N   ARG C 246     7392   4324   6633   3720  -2182  -1093       N  
ATOM   4788  CA  ARG C 246       3.177  50.302 290.989  1.00 50.21           C  
ANISOU 4788  CA  ARG C 246     7917   4484   6677   3919  -2356  -1132       C  
ATOM   4789  C   ARG C 246       1.827  49.586 290.735  1.00 56.06           C  
ANISOU 4789  C   ARG C 246     8471   5335   7495   3979  -2673  -1281       C  
ATOM   4790  O   ARG C 246       1.803  48.369 290.537  1.00 55.91           O  
ANISOU 4790  O   ARG C 246     8354   5354   7535   3870  -2750  -1334       O  
ATOM   4791  CB  ARG C 246       4.358  49.557 290.330  1.00 49.90           C  
ANISOU 4791  CB  ARG C 246     8089   4348   6520   3856  -2214  -1065       C  
ATOM   4792  CG  ARG C 246       4.431  49.644 288.820  1.00 63.95           C  
ANISOU 4792  CG  ARG C 246    10249   6006   8045   4066  -2315  -1068       C  
ATOM   4793  CD  ARG C 246       5.547  48.776 288.269  1.00 79.54           C  
ANISOU 4793  CD  ARG C 246    12396   7907   9920   4000  -2162  -1011       C  
ATOM   4794  NE  ARG C 246       5.245  47.345 288.363  1.00 92.75           N  
ANISOU 4794  NE  ARG C 246    13895   9651  11696   3895  -2292  -1104       N  
ATOM   4795  CZ  ARG C 246       6.129  46.408 288.697  1.00109.24           C  
ANISOU 4795  CZ  ARG C 246    15911  11746  13851   3729  -2131  -1067       C  
ATOM   4796  NH1 ARG C 246       7.384  46.739 288.983  1.00 94.73           N  
ANISOU 4796  NH1 ARG C 246    14133   9863  11999   3645  -1833   -939       N  
ATOM   4797  NH2 ARG C 246       5.765  45.135 288.753  1.00 98.73           N  
ANISOU 4797  NH2 ARG C 246    14446  10463  12604   3644  -2274  -1157       N  
ATOM   4798  N   ALA C 247       0.706  50.342 290.753  1.00 54.44           N  
ANISOU 4798  N   ALA C 247     8210   5180   7297   4149  -2860  -1350       N  
ATOM   4799  CA  ALA C 247      -0.642  49.793 290.515  1.00 56.08           C  
ANISOU 4799  CA  ALA C 247     8216   5503   7589   4217  -3174  -1493       C  
ATOM   4800  C   ALA C 247      -0.946  49.708 289.018  1.00 62.44           C  
ANISOU 4800  C   ALA C 247     9328   6214   8184   4428  -3406  -1545       C  
ATOM   4801  O   ALA C 247      -0.672  50.661 288.282  1.00 62.61           O  
ANISOU 4801  O   ALA C 247     9687   6106   7995   4619  -3381  -1490       O  
ATOM   4802  CB  ALA C 247      -1.696  50.636 291.216  1.00 57.54           C  
ANISOU 4802  CB  ALA C 247     8172   5802   7891   4311  -3263  -1544       C  
ATOM   4803  N   THR C 248      -1.511  48.561 288.575  1.00 60.71           N  
ANISOU 4803  N   THR C 248     9002   6050   8015   4390  -3638  -1652       N  
ATOM   4804  CA  THR C 248      -1.834  48.278 287.165  1.00 62.99           C  
ANISOU 4804  CA  THR C 248     9574   6250   8108   4573  -3888  -1718       C  
ATOM   4805  C   THR C 248      -3.346  48.003 286.934  1.00 69.22           C  
ANISOU 4805  C   THR C 248    10148   7158   8995   4666  -4264  -1870       C  
ATOM   4806  O   THR C 248      -4.094  47.825 287.897  1.00 68.10           O  
ANISOU 4806  O   THR C 248     9602   7181   9093   4548  -4312  -1924       O  
ATOM   4807  CB  THR C 248      -0.990  47.092 286.654  1.00 71.19           C  
ANISOU 4807  CB  THR C 248    10766   7208   9075   4452  -3830  -1703       C  
ATOM   4808  OG1 THR C 248      -1.229  45.940 287.463  1.00 69.74           O  
ANISOU 4808  OG1 THR C 248    10231   7141   9127   4201  -3835  -1750       O  
ATOM   4809  CG2 THR C 248       0.500  47.400 286.614  1.00 68.50           C  
ANISOU 4809  CG2 THR C 248    10706   6735   8586   4425  -3495  -1557       C  
ATOM   4810  N   LEU C 249      -3.782  47.991 285.647  1.00 68.94           N  
ANISOU 4810  N   LEU C 249    10389   7039   8767   4882  -4528  -1935       N  
ATOM   4811  CA  LEU C 249      -5.162  47.730 285.199  1.00 71.84           C  
ANISOU 4811  CA  LEU C 249    10611   7496   9190   4999  -4923  -2083       C  
ATOM   4812  C   LEU C 249      -5.161  47.327 283.718  1.00 79.94           C  
ANISOU 4812  C   LEU C 249    12024   8382   9969   5163  -5154  -2135       C  
ATOM   4813  O   LEU C 249      -4.727  48.122 282.880  1.00 80.45           O  
ANISOU 4813  O   LEU C 249    12496   8299   9774   5374  -5112  -2075       O  
ATOM   4814  CB  LEU C 249      -6.066  48.965 285.429  1.00 73.03           C  
ANISOU 4814  CB  LEU C 249    10657   7722   9370   5207  -5029  -2110       C  
ATOM   4815  CG  LEU C 249      -7.451  48.959 284.775  1.00 80.62           C  
ANISOU 4815  CG  LEU C 249    11520   8762  10350   5394  -5450  -2256       C  
ATOM   4816  CD1 LEU C 249      -8.505  48.414 285.716  1.00 80.99           C  
ANISOU 4816  CD1 LEU C 249    11020   9036  10718   5231  -5576  -2352       C  
ATOM   4817  CD2 LEU C 249      -7.834  50.344 284.341  1.00 84.91           C  
ANISOU 4817  CD2 LEU C 249    12255   9259  10746   5706  -5536  -2249       C  
ATOM   4818  N   ASP C 250      -5.619  46.088 283.404  1.00 78.86           N  
ANISOU 4818  N   ASP C 250    11777   8280   9904   5060  -5391  -2242       N  
ATOM   4819  CA  ASP C 250      -5.663  45.558 282.034  1.00 81.48           C  
ANISOU 4819  CA  ASP C 250    12468   8481  10011   5200  -5638  -2309       C  
ATOM   4820  C   ASP C 250      -7.020  45.849 281.392  1.00 88.10           C  
ANISOU 4820  C   ASP C 250    13259   9374  10840   5408  -6062  -2442       C  
ATOM   4821  O   ASP C 250      -8.040  45.315 281.833  1.00 88.13           O  
ANISOU 4821  O   ASP C 250    12873   9533  11080   5299  -6290  -2550       O  
ATOM   4822  CB  ASP C 250      -5.350  44.045 282.016  1.00 83.56           C  
ANISOU 4822  CB  ASP C 250    12683   8726  10340   4974  -5665  -2351       C  
ATOM   4823  CG  ASP C 250      -5.248  43.435 280.624  1.00 99.84           C  
ANISOU 4823  CG  ASP C 250    15164  10627  12143   5111  -5874  -2409       C  
ATOM   4824  OD1 ASP C 250      -4.221  43.668 279.946  1.00100.63           O  
ANISOU 4824  OD1 ASP C 250    15682  10569  11984   5226  -5678  -2319       O  
ATOM   4825  OD2 ASP C 250      -6.185  42.705 280.225  1.00108.10           O  
ANISOU 4825  OD2 ASP C 250    16121  11704  13246   5097  -6230  -2545       O  
ATOM   4826  N   VAL C 251      -7.022  46.716 280.358  1.00 87.12           N  
ANISOU 4826  N   VAL C 251    13533   9125  10445   5706  -6163  -2429       N  
ATOM   4827  CA  VAL C 251      -8.230  47.145 279.632  1.00 90.56           C  
ANISOU 4827  CA  VAL C 251    13995   9589  10825   5956  -6570  -2547       C  
ATOM   4828  C   VAL C 251      -7.991  47.193 278.102  1.00 97.16           C  
ANISOU 4828  C   VAL C 251    15394  10221  11300   6204  -6742  -2561       C  
ATOM   4829  O   VAL C 251      -6.844  47.249 277.652  1.00 95.63           O  
ANISOU 4829  O   VAL C 251    15587   9866  10881   6222  -6484  -2454       O  
ATOM   4830  CB  VAL C 251      -8.789  48.513 280.141  1.00 94.74           C  
ANISOU 4830  CB  VAL C 251    14371  10206  11419   6124  -6550  -2524       C  
ATOM   4831  CG1 VAL C 251      -9.480  48.376 281.497  1.00 93.67           C  
ANISOU 4831  CG1 VAL C 251    13637  10305  11649   5933  -6531  -2568       C  
ATOM   4832  CG2 VAL C 251      -7.714  49.599 280.177  1.00 92.75           C  
ANISOU 4832  CG2 VAL C 251    14434   9822  10986   6207  -6184  -2363       C  
ATOM   4833  N   VAL C 252      -9.092  47.194 277.320  1.00 97.49           N  
ANISOU 4833  N   VAL C 252    15474  10278  11289   6399  -7177  -2694       N  
ATOM   4834  CA  VAL C 252      -9.109  47.288 275.850  1.00100.08           C  
ANISOU 4834  CA  VAL C 252    16325  10426  11277   6666  -7415  -2731       C  
ATOM   4835  C   VAL C 252      -8.696  48.728 275.444  1.00104.25           C  
ANISOU 4835  C   VAL C 252    17229  10830  11552   6934  -7253  -2618       C  
ATOM   4836  O   VAL C 252      -9.134  49.688 276.082  1.00103.15           O  
ANISOU 4836  O   VAL C 252    16874  10784  11535   6997  -7196  -2590       O  
ATOM   4837  CB  VAL C 252     -10.506  46.888 275.274  1.00107.40           C  
ANISOU 4837  CB  VAL C 252    17118  11426  12262   6782  -7955  -2915       C  
ATOM   4838  CG1 VAL C 252     -10.536  46.961 273.747  1.00110.05           C  
ANISOU 4838  CG1 VAL C 252    18016  11566  12232   7059  -8221  -2961       C  
ATOM   4839  CG2 VAL C 252     -10.923  45.497 275.745  1.00106.97           C  
ANISOU 4839  CG2 VAL C 252    16660  11497  12486   6486  -8101  -3018       C  
ATOM   4840  N   ALA C 253      -7.857  48.857 274.384  1.00101.69           N  
ANISOU 4840  N   ALA C 253    17474  10290  10871   7088  -7173  -2551       N  
ATOM   4841  CA  ALA C 253      -7.294  50.098 273.820  1.00102.01           C  
ANISOU 4841  CA  ALA C 253    17968  10172  10621   7327  -7000  -2429       C  
ATOM   4842  C   ALA C 253      -8.280  51.293 273.761  1.00107.96           C  
ANISOU 4842  C   ALA C 253    18689  10964  11367   7592  -7237  -2469       C  
ATOM   4843  O   ALA C 253      -7.859  52.431 273.981  1.00106.73           O  
ANISOU 4843  O   ALA C 253    18680  10746  11126   7689  -7005  -2352       O  
ATOM   4844  CB  ALA C 253      -6.747  49.829 272.428  1.00104.53           C  
ANISOU 4844  CB  ALA C 253    18882  10276  10557   7494  -7049  -2412       C  
ATOM   4845  N   GLY C 254      -9.552  51.022 273.464  1.00107.18           N  
ANISOU 4845  N   GLY C 254    18403  10962  11358   7704  -7694  -2633       N  
ATOM   4846  CA  GLY C 254     -10.600  52.036 273.389  1.00109.21           C  
ANISOU 4846  CA  GLY C 254    18588  11277  11630   7970  -7968  -2694       C  
ATOM   4847  C   GLY C 254     -11.027  52.588 274.738  1.00111.13           C  
ANISOU 4847  C   GLY C 254    18305  11718  12201   7866  -7838  -2684       C  
ATOM   4848  O   GLY C 254     -11.437  53.749 274.831  1.00111.37           O  
ANISOU 4848  O   GLY C 254    18369  11750  12196   8086  -7873  -2664       O  
ATOM   4849  N   GLU C 255     -10.931  51.753 275.796  1.00105.25           N  
ANISOU 4849  N   GLU C 255    17089  11136  11768   7537  -7686  -2697       N  
ATOM   4850  CA  GLU C 255     -11.305  52.094 277.174  1.00103.13           C  
ANISOU 4850  CA  GLU C 255    16290  11069  11826   7398  -7540  -2690       C  
ATOM   4851  C   GLU C 255     -10.211  52.902 277.898  1.00103.10           C  
ANISOU 4851  C   GLU C 255    16390  10996  11789   7323  -7064  -2518       C  
ATOM   4852  O   GLU C 255     -10.484  53.462 278.962  1.00101.36           O  
ANISOU 4852  O   GLU C 255    15831  10906  11774   7283  -6941  -2502       O  
ATOM   4853  CB  GLU C 255     -11.632  50.819 277.971  1.00103.29           C  
ANISOU 4853  CB  GLU C 255    15802  11272  12170   7067  -7562  -2766       C  
ATOM   4854  N   ALA C 256      -8.992  52.981 277.312  1.00 97.97           N  
ANISOU 4854  N   ALA C 256    16206  10142  10877   7310  -6803  -2393       N  
ATOM   4855  CA  ALA C 256      -7.841  53.712 277.863  1.00 94.83           C  
ANISOU 4855  CA  ALA C 256    15953   9654  10425   7223  -6353  -2221       C  
ATOM   4856  C   ALA C 256      -8.129  55.215 278.017  1.00 98.14           C  
ANISOU 4856  C   ALA C 256    16489  10030  10769   7459  -6327  -2171       C  
ATOM   4857  O   ALA C 256      -7.643  55.829 278.967  1.00 95.44           O  
ANISOU 4857  O   ALA C 256    16031   9705  10529   7349  -6017  -2072       O  
ATOM   4858  CB  ALA C 256      -6.617  53.504 276.983  1.00 95.07           C  
ANISOU 4858  CB  ALA C 256    16487   9474  10162   7209  -6141  -2112       C  
ATOM   4859  N   ALA C 257      -8.924  55.794 277.098  1.00 97.03           N  
ANISOU 4859  N   ALA C 257    16592   9827  10450   7785  -6660  -2240       N  
ATOM   4860  CA  ALA C 257      -9.307  57.206 277.132  1.00 97.79           C  
ANISOU 4860  CA  ALA C 257    16834   9867  10454   8048  -6687  -2205       C  
ATOM   4861  C   ALA C 257     -10.246  57.485 278.305  1.00100.24           C  
ANISOU 4861  C   ALA C 257    16597  10404  11087   8033  -6763  -2286       C  
ATOM   4862  O   ALA C 257     -11.181  56.716 278.548  1.00100.71           O  
ANISOU 4862  O   ALA C 257    16246  10655  11364   7992  -7032  -2427       O  
ATOM   4863  CB  ALA C 257      -9.973  57.604 275.822  1.00102.23           C  
ANISOU 4863  CB  ALA C 257    17803  10304  10737   8404  -7053  -2268       C  
ATOM   4864  N   GLY C 258      -9.962  58.567 279.028  1.00 94.82           N  
ANISOU 4864  N   GLY C 258    15910   9689  10426   8059  -6517  -2194       N  
ATOM   4865  CA  GLY C 258     -10.739  59.005 280.184  1.00 93.93           C  
ANISOU 4865  CA  GLY C 258    15330   9771  10587   8068  -6532  -2252       C  
ATOM   4866  C   GLY C 258     -10.265  58.447 281.512  1.00 93.07           C  
ANISOU 4866  C   GLY C 258    14793   9808  10761   7715  -6221  -2213       C  
ATOM   4867  O   GLY C 258     -10.464  59.083 282.551  1.00 92.14           O  
ANISOU 4867  O   GLY C 258    14410   9789  10809   7707  -6097  -2206       O  
ATOM   4868  N   LEU C 259      -9.640  57.253 281.492  1.00 86.34           N  
ANISOU 4868  N   LEU C 259    13883   8964   9959   7432  -6097  -2192       N  
ATOM   4869  CA  LEU C 259      -9.142  56.593 282.693  1.00 82.32           C  
ANISOU 4869  CA  LEU C 259    12992   8581   9704   7086  -5813  -2154       C  
ATOM   4870  C   LEU C 259      -8.021  57.384 283.343  1.00 83.59           C  
ANISOU 4870  C   LEU C 259    13319   8628   9815   6983  -5405  -1996       C  
ATOM   4871  O   LEU C 259      -7.188  57.997 282.667  1.00 82.37           O  
ANISOU 4871  O   LEU C 259    13636   8260   9401   7070  -5271  -1887       O  
ATOM   4872  CB  LEU C 259      -8.687  55.158 282.414  1.00 80.94           C  
ANISOU 4872  CB  LEU C 259    12768   8420   9568   6837  -5804  -2171       C  
ATOM   4873  CG  LEU C 259      -9.797  54.111 282.305  1.00 86.90           C  
ANISOU 4873  CG  LEU C 259    13156   9353  10509   6792  -6145  -2332       C  
ATOM   4874  CD1 LEU C 259      -9.238  52.785 281.846  1.00 86.49           C  
ANISOU 4874  CD1 LEU C 259    13204   9245  10411   6600  -6157  -2341       C  
ATOM   4875  CD2 LEU C 259     -10.536  53.926 283.630  1.00 87.65           C  
ANISOU 4875  CD2 LEU C 259    12656   9692  10954   6619  -6101  -2386       C  
ATOM   4876  N   SER C 260      -8.042  57.378 284.675  1.00 79.16           N  
ANISOU 4876  N   SER C 260    12361   8211   9507   6793  -5213  -1986       N  
ATOM   4877  CA  SER C 260      -7.121  58.084 285.553  1.00 77.01           C  
ANISOU 4877  CA  SER C 260    12147   7867   9246   6665  -4844  -1855       C  
ATOM   4878  C   SER C 260      -6.781  57.223 286.776  1.00 78.34           C  
ANISOU 4878  C   SER C 260    11898   8186   9681   6322  -4627  -1844       C  
ATOM   4879  O   SER C 260      -7.478  56.242 287.042  1.00 77.64           O  
ANISOU 4879  O   SER C 260    11447   8270   9781   6211  -4778  -1946       O  
ATOM   4880  CB  SER C 260      -7.760  59.400 285.993  1.00 82.27           C  
ANISOU 4880  CB  SER C 260    12805   8539   9915   6894  -4876  -1865       C  
ATOM   4881  OG  SER C 260      -6.873  60.175 286.779  1.00 91.09           O  
ANISOU 4881  OG  SER C 260    14030   9559  11020   6783  -4540  -1738       O  
ATOM   4882  N   CYS C 261      -5.721  57.586 287.524  1.00 73.15           N  
ANISOU 4882  N   CYS C 261    11297   7458   9038   6149  -4282  -1720       N  
ATOM   4883  CA  CYS C 261      -5.362  56.856 288.733  1.00 70.74           C  
ANISOU 4883  CA  CYS C 261    10624   7283   8972   5836  -4071  -1703       C  
ATOM   4884  C   CYS C 261      -5.176  57.807 289.906  1.00 71.98           C  
ANISOU 4884  C   CYS C 261    10679   7454   9218   5800  -3847  -1644       C  
ATOM   4885  O   CYS C 261      -4.278  58.650 289.878  1.00 71.08           O  
ANISOU 4885  O   CYS C 261    10875   7169   8963   5804  -3641  -1526       O  
ATOM   4886  CB  CYS C 261      -4.128  55.994 288.523  1.00 69.83           C  
ANISOU 4886  CB  CYS C 261    10651   7079   8804   5599  -3874  -1616       C  
ATOM   4887  SG  CYS C 261      -3.819  54.844 289.884  1.00 71.56           S  
ANISOU 4887  SG  CYS C 261    10412   7464   9313   5225  -3684  -1617       S  
ATOM   4888  N   ARG C 262      -6.035  57.668 290.933  1.00 67.06           N  
ANISOU 4888  N   ARG C 262     9624   7031   8825   5762  -3890  -1727       N  
ATOM   4889  CA  ARG C 262      -6.000  58.498 292.135  1.00 65.25           C  
ANISOU 4889  CA  ARG C 262     9258   6839   8695   5738  -3700  -1693       C  
ATOM   4890  C   ARG C 262      -5.081  57.874 293.182  1.00 65.01           C  
ANISOU 4890  C   ARG C 262     9075   6831   8795   5401  -3405  -1614       C  
ATOM   4891  O   ARG C 262      -5.032  56.646 293.324  1.00 63.90           O  
ANISOU 4891  O   ARG C 262     8709   6791   8780   5190  -3406  -1640       O  
ATOM   4892  CB  ARG C 262      -7.409  58.721 292.702  1.00 66.94           C  
ANISOU 4892  CB  ARG C 262     9083   7266   9086   5873  -3874  -1819       C  
ATOM   4893  N   VAL C 263      -4.320  58.736 293.886  1.00 58.49           N  
ANISOU 4893  N   VAL C 263     8393   5899   7930   5355  -3164  -1515       N  
ATOM   4894  CA  VAL C 263      -3.355  58.367 294.922  1.00 54.44           C  
ANISOU 4894  CA  VAL C 263     7777   5386   7523   5057  -2881  -1431       C  
ATOM   4895  C   VAL C 263      -3.685  59.149 296.186  1.00 57.24           C  
ANISOU 4895  C   VAL C 263     7950   5809   7990   5066  -2769  -1440       C  
ATOM   4896  O   VAL C 263      -3.657  60.374 296.159  1.00 57.62           O  
ANISOU 4896  O   VAL C 263     8233   5736   7922   5233  -2737  -1404       O  
ATOM   4897  CB  VAL C 263      -1.890  58.623 294.467  1.00 56.55           C  
ANISOU 4897  CB  VAL C 263     8432   5435   7619   4963  -2682  -1289       C  
ATOM   4898  CG1 VAL C 263      -0.892  58.235 295.556  1.00 53.79           C  
ANISOU 4898  CG1 VAL C 263     7958   5091   7388   4662  -2406  -1206       C  
ATOM   4899  CG2 VAL C 263      -1.572  57.902 293.163  1.00 56.69           C  
ANISOU 4899  CG2 VAL C 263     8653   5383   7503   4981  -2782  -1282       C  
ATOM   4900  N   LYS C 264      -3.982  58.447 297.288  1.00 52.30           N  
ANISOU 4900  N   LYS C 264     6927   5367   7579   4888  -2708  -1485       N  
ATOM   4901  CA  LYS C 264      -4.281  59.065 298.586  1.00 51.30           C  
ANISOU 4901  CA  LYS C 264     6607   5321   7564   4878  -2585  -1497       C  
ATOM   4902  C   LYS C 264      -3.134  58.768 299.575  1.00 52.54           C  
ANISOU 4902  C   LYS C 264     6734   5439   7790   4579  -2312  -1402       C  
ATOM   4903  O   LYS C 264      -2.799  57.603 299.812  1.00 50.74           O  
ANISOU 4903  O   LYS C 264     6318   5289   7671   4346  -2261  -1396       O  
ATOM   4904  CB  LYS C 264      -5.637  58.575 299.143  1.00 54.16           C  
ANISOU 4904  CB  LYS C 264     6529   5935   8116   4923  -2719  -1623       C  
ATOM   4905  CG  LYS C 264      -6.862  59.025 298.352  1.00 63.06           C  
ANISOU 4905  CG  LYS C 264     7643   7121   9198   5246  -2989  -1725       C  
ATOM   4906  CD  LYS C 264      -8.159  58.539 299.006  1.00 68.56           C  
ANISOU 4906  CD  LYS C 264     7862   8083  10103   5268  -3093  -1842       C  
ATOM   4907  CE  LYS C 264      -9.400  59.213 298.469  1.00 72.19           C  
ANISOU 4907  CE  LYS C 264     8277   8616  10535   5611  -3345  -1945       C  
ATOM   4908  NZ  LYS C 264      -9.797  58.673 297.145  1.00 80.85           N  
ANISOU 4908  NZ  LYS C 264     9448   9701  11569   5702  -3617  -1997       N  
ATOM   4909  N   HIS C 265      -2.516  59.823 300.122  1.00 48.41           N  
ANISOU 4909  N   HIS C 265     6412   4785   7197   4589  -2150  -1329       N  
ATOM   4910  CA  HIS C 265      -1.413  59.698 301.077  1.00 45.97           C  
ANISOU 4910  CA  HIS C 265     6099   4424   6942   4325  -1906  -1238       C  
ATOM   4911  C   HIS C 265      -1.506  60.791 302.146  1.00 50.37           C  
ANISOU 4911  C   HIS C 265     6675   4955   7510   4386  -1799  -1233       C  
ATOM   4912  O   HIS C 265      -1.953  61.900 301.858  1.00 51.54           O  
ANISOU 4912  O   HIS C 265     7005   5026   7550   4634  -1877  -1255       O  
ATOM   4913  CB  HIS C 265      -0.057  59.752 300.349  1.00 45.63           C  
ANISOU 4913  CB  HIS C 265     6391   4181   6765   4218  -1797  -1117       C  
ATOM   4914  CG  HIS C 265       1.102  59.286 301.176  1.00 46.76           C  
ANISOU 4914  CG  HIS C 265     6482   4298   6986   3922  -1577  -1031       C  
ATOM   4915  ND1 HIS C 265       2.212  60.084 301.374  1.00 47.94           N  
ANISOU 4915  ND1 HIS C 265     6867   4282   7066   3848  -1409   -928       N  
ATOM   4916  CD2 HIS C 265       1.286  58.117 301.831  1.00 46.89           C  
ANISOU 4916  CD2 HIS C 265     6246   4428   7143   3694  -1515  -1035       C  
ATOM   4917  CE1 HIS C 265       3.028  59.387 302.148  1.00 45.34           C  
ANISOU 4917  CE1 HIS C 265     6405   3981   6840   3585  -1257   -877       C  
ATOM   4918  NE2 HIS C 265       2.518  58.192 302.438  1.00 45.07           N  
ANISOU 4918  NE2 HIS C 265     6087   4109   6929   3490  -1312   -937       N  
ATOM   4919  N   SER C 266      -1.074  60.470 303.377  1.00 45.97           N  
ANISOU 4919  N   SER C 266     5946   4451   7070   4166  -1626  -1206       N  
ATOM   4920  CA  SER C 266      -1.079  61.369 304.537  1.00 46.12           C  
ANISOU 4920  CA  SER C 266     5972   4447   7104   4188  -1510  -1203       C  
ATOM   4921  C   SER C 266      -0.295  62.668 304.284  1.00 50.31           C  
ANISOU 4921  C   SER C 266     6912   4733   7469   4265  -1447  -1119       C  
ATOM   4922  O   SER C 266      -0.615  63.694 304.887  1.00 51.13           O  
ANISOU 4922  O   SER C 266     7099   4793   7535   4408  -1431  -1142       O  
ATOM   4923  CB  SER C 266      -0.534  60.657 305.775  1.00 48.90           C  
ANISOU 4923  CB  SER C 266     6112   4875   7592   3908  -1338  -1174       C  
ATOM   4924  OG  SER C 266       0.623  59.874 305.519  1.00 56.24           O  
ANISOU 4924  OG  SER C 266     7118   5727   8525   3666  -1244  -1083       O  
ATOM   4925  N   SER C 267       0.712  62.623 303.388  1.00 46.29           N  
ANISOU 4925  N   SER C 267     6664   4066   6860   4174  -1409  -1023       N  
ATOM   4926  CA  SER C 267       1.517  63.782 303.006  1.00 46.75           C  
ANISOU 4926  CA  SER C 267     7120   3882   6759   4218  -1346   -929       C  
ATOM   4927  C   SER C 267       0.718  64.691 302.069  1.00 54.20           C  
ANISOU 4927  C   SER C 267     8289   4748   7554   4543  -1514   -971       C  
ATOM   4928  O   SER C 267       0.867  65.910 302.144  1.00 54.86           O  
ANISOU 4928  O   SER C 267     8647   4668   7529   4658  -1492   -938       O  
ATOM   4929  CB  SER C 267       2.827  63.346 302.356  1.00 48.45           C  
ANISOU 4929  CB  SER C 267     7508   3978   6924   4016  -1240   -812       C  
ATOM   4930  OG  SER C 267       2.602  62.670 301.132  1.00 55.28           O  
ANISOU 4930  OG  SER C 267     8411   4866   7726   4100  -1358   -827       O  
ATOM   4931  N   LEU C 268      -0.132  64.098 301.193  1.00 52.89           N  
ANISOU 4931  N   LEU C 268     8020   4693   7383   4692  -1694  -1045       N  
ATOM   4932  CA  LEU C 268      -1.023  64.836 300.285  1.00 55.80           C  
ANISOU 4932  CA  LEU C 268     8567   5014   7621   5021  -1890  -1101       C  
ATOM   4933  C   LEU C 268      -2.117  65.443 301.149  1.00 63.72           C  
ANISOU 4933  C   LEU C 268     9396   6125   8689   5214  -1950  -1201       C  
ATOM   4934  O   LEU C 268      -2.949  64.707 301.691  1.00 63.67           O  
ANISOU 4934  O   LEU C 268     9003   6346   8844   5193  -1989  -1292       O  
ATOM   4935  CB  LEU C 268      -1.598  63.916 299.189  1.00 56.29           C  
ANISOU 4935  CB  LEU C 268     8535   5177   7675   5102  -2076  -1158       C  
ATOM   4936  CG  LEU C 268      -0.593  63.196 298.302  1.00 59.75           C  
ANISOU 4936  CG  LEU C 268     9149   5517   8035   4940  -2019  -1068       C  
ATOM   4937  CD1 LEU C 268      -1.258  62.096 297.524  1.00 60.17           C  
ANISOU 4937  CD1 LEU C 268     9017   5712   8132   4967  -2192  -1146       C  
ATOM   4938  CD2 LEU C 268       0.128  64.158 297.376  1.00 63.46           C  
ANISOU 4938  CD2 LEU C 268    10095   5737   8278   5056  -2002   -972       C  
ATOM   4939  N   GLU C 269      -2.069  66.771 301.351  1.00 62.80           N  
ANISOU 4939  N   GLU C 269     9566   5846   8451   5387  -1940  -1181       N  
ATOM   4940  CA  GLU C 269      -2.934  67.464 302.288  1.00 64.80           C  
ANISOU 4940  CA  GLU C 269     9698   6173   8750   5566  -1959  -1266       C  
ATOM   4941  C   GLU C 269      -4.299  67.584 301.650  1.00 71.26           C  
ANISOU 4941  C   GLU C 269    10411   7113   9553   5896  -2195  -1382       C  
ATOM   4942  O   GLU C 269      -4.738  68.654 301.227  1.00 73.34           O  
ANISOU 4942  O   GLU C 269    10927   7259   9679   6185  -2306  -1404       O  
ATOM   4943  CB  GLU C 269      -2.337  68.834 302.679  1.00 67.15           C  
ANISOU 4943  CB  GLU C 269    10372   6227   8915   5618  -1863  -1198       C  
ATOM   4944  CG  GLU C 269      -1.070  68.752 303.518  1.00 79.36           C  
ANISOU 4944  CG  GLU C 269    11990   7667  10498   5287  -1639  -1092       C  
ATOM   4945  CD  GLU C 269      -1.260  68.185 304.912  1.00110.63           C  
ANISOU 4945  CD  GLU C 269    15615  11793  14627   5133  -1520  -1137       C  
ATOM   4946  OE1 GLU C 269      -1.969  68.825 305.725  1.00112.65           O  
ANISOU 4946  OE1 GLU C 269    15841  12075  14886   5298  -1523  -1205       O  
ATOM   4947  OE2 GLU C 269      -0.701  67.098 305.190  1.00104.16           O  
ANISOU 4947  OE2 GLU C 269    14579  11071  13927   4855  -1422  -1104       O  
ATOM   4948  N   GLY C 270      -4.986  66.440 301.600  1.00 67.14           N  
ANISOU 4948  N   GLY C 270     9506   6827   9178   5848  -2282  -1459       N  
ATOM   4949  CA  GLY C 270      -6.307  66.285 301.002  1.00 69.06           C  
ANISOU 4949  CA  GLY C 270     9564   7228   9448   6118  -2523  -1577       C  
ATOM   4950  C   GLY C 270      -6.273  66.166 299.488  1.00 73.48           C  
ANISOU 4950  C   GLY C 270    10357   7692   9872   6228  -2707  -1562       C  
ATOM   4951  O   GLY C 270      -7.084  65.438 298.904  1.00 74.11           O  
ANISOU 4951  O   GLY C 270    10204   7932  10022   6283  -2887  -1642       O  
ATOM   4952  N   GLN C 271      -5.326  66.888 298.844  1.00 69.16           N  
ANISOU 4952  N   GLN C 271    10279   6876   9123   6256  -2663  -1459       N  
ATOM   4953  CA  GLN C 271      -5.147  66.949 297.398  1.00 69.43           C  
ANISOU 4953  CA  GLN C 271    10623   6774   8983   6371  -2809  -1425       C  
ATOM   4954  C   GLN C 271      -4.459  65.688 296.876  1.00 69.65           C  
ANISOU 4954  C   GLN C 271    10578   6835   9050   6099  -2759  -1376       C  
ATOM   4955  O   GLN C 271      -3.229  65.575 296.882  1.00 67.37           O  
ANISOU 4955  O   GLN C 271    10464   6413   8719   5860  -2562  -1260       O  
ATOM   4956  CB  GLN C 271      -4.376  68.219 296.988  1.00 71.53           C  
ANISOU 4956  CB  GLN C 271    11416   6738   9023   6467  -2744  -1319       C  
ATOM   4957  N   ASP C 272      -5.283  64.743 296.416  1.00 65.47           N  
ANISOU 4957  N   ASP C 272     9781   6487   8607   6141  -2947  -1472       N  
ATOM   4958  CA  ASP C 272      -4.860  63.470 295.843  1.00 63.33           C  
ANISOU 4958  CA  ASP C 272     9421   6266   8376   5927  -2951  -1454       C  
ATOM   4959  C   ASP C 272      -4.264  63.700 294.466  1.00 65.86           C  
ANISOU 4959  C   ASP C 272    10176   6382   8465   6011  -3013  -1383       C  
ATOM   4960  O   ASP C 272      -4.690  64.622 293.770  1.00 68.00           O  
ANISOU 4960  O   ASP C 272    10715   6546   8575   6297  -3167  -1400       O  
ATOM   4961  CB  ASP C 272      -6.062  62.506 295.752  1.00 66.40           C  
ANISOU 4961  CB  ASP C 272     9395   6907   8929   5968  -3162  -1589       C  
ATOM   4962  CG  ASP C 272      -6.930  62.453 297.001  1.00 81.41           C  
ANISOU 4962  CG  ASP C 272    10869   9025  11040   5962  -3134  -1673       C  
ATOM   4963  OD1 ASP C 272      -6.367  62.335 298.115  1.00 81.57           O  
ANISOU 4963  OD1 ASP C 272    10774   9062  11155   5746  -2901  -1623       O  
ATOM   4964  OD2 ASP C 272      -8.172  62.542 296.866  1.00 89.87           O  
ANISOU 4964  OD2 ASP C 272    11722  10249  12175   6180  -3344  -1789       O  
ATOM   4965  N   ILE C 273      -3.279  62.881 294.068  1.00 58.93           N  
ANISOU 4965  N   ILE C 273     9381   5448   7563   5774  -2890  -1303       N  
ATOM   4966  CA  ILE C 273      -2.679  63.010 292.740  1.00 58.62           C  
ANISOU 4966  CA  ILE C 273     9752   5223   7299   5840  -2922  -1230       C  
ATOM   4967  C   ILE C 273      -3.596  62.293 291.765  1.00 62.71           C  
ANISOU 4967  C   ILE C 273    10191   5840   7795   5996  -3210  -1339       C  
ATOM   4968  O   ILE C 273      -3.803  61.087 291.891  1.00 61.54           O  
ANISOU 4968  O   ILE C 273     9744   5848   7792   5840  -3254  -1396       O  
ATOM   4969  CB  ILE C 273      -1.213  62.506 292.641  1.00 59.52           C  
ANISOU 4969  CB  ILE C 273    10003   5232   7379   5552  -2669  -1100       C  
ATOM   4970  CG1 ILE C 273      -0.382  62.881 293.879  1.00 58.11           C  
ANISOU 4970  CG1 ILE C 273     9762   5017   7299   5336  -2399  -1016       C  
ATOM   4971  CG2 ILE C 273      -0.554  63.014 291.349  1.00 61.28           C  
ANISOU 4971  CG2 ILE C 273    10713   5233   7337   5656  -2659  -1005       C  
ATOM   4972  CD1 ILE C 273       0.665  61.835 294.278  1.00 64.40           C  
ANISOU 4972  CD1 ILE C 273    10431   5843   8196   5003  -2183   -942       C  
ATOM   4973  N   VAL C 274      -4.187  63.038 290.830  1.00 60.70           N  
ANISOU 4973  N   VAL C 274    10204   5495   7365   6305  -3420  -1372       N  
ATOM   4974  CA  VAL C 274      -5.096  62.458 289.850  1.00 62.10           C  
ANISOU 4974  CA  VAL C 274    10347   5749   7501   6487  -3729  -1479       C  
ATOM   4975  C   VAL C 274      -4.436  62.624 288.468  1.00 67.46           C  
ANISOU 4975  C   VAL C 274    11525   6207   7898   6581  -3754  -1399       C  
ATOM   4976  O   VAL C 274      -4.384  63.723 287.921  1.00 68.87           O  
ANISOU 4976  O   VAL C 274    12082   6210   7876   6796  -3783  -1349       O  
ATOM   4977  CB  VAL C 274      -6.522  63.062 289.983  1.00 67.81           C  
ANISOU 4977  CB  VAL C 274    10904   6585   8276   6789  -3987  -1606       C  
ATOM   4978  CG1 VAL C 274      -7.436  62.629 288.846  1.00 69.90           C  
ANISOU 4978  CG1 VAL C 274    11164   6913   8483   6995  -4334  -1716       C  
ATOM   4979  CG2 VAL C 274      -7.143  62.677 291.323  1.00 66.58           C  
ANISOU 4979  CG2 VAL C 274    10235   6662   8400   6673  -3930  -1680       C  
ATOM   4980  N   LEU C 275      -3.856  61.528 287.959  1.00 63.37           N  
ANISOU 4980  N   LEU C 275    11025   5692   7361   6408  -3718  -1377       N  
ATOM   4981  CA  LEU C 275      -3.150  61.502 286.680  1.00 64.48           C  
ANISOU 4981  CA  LEU C 275    11619   5641   7238   6469  -3708  -1298       C  
ATOM   4982  C   LEU C 275      -3.942  60.733 285.625  1.00 69.68           C  
ANISOU 4982  C   LEU C 275    12293   6355   7828   6624  -4027  -1410       C  
ATOM   4983  O   LEU C 275      -4.092  59.509 285.730  1.00 68.65           O  
ANISOU 4983  O   LEU C 275    11881   6364   7839   6466  -4087  -1478       O  
ATOM   4984  CB  LEU C 275      -1.745  60.875 286.842  1.00 62.44           C  
ANISOU 4984  CB  LEU C 275    11424   5320   6981   6165  -3394  -1175       C  
ATOM   4985  CG  LEU C 275      -0.618  61.780 287.341  1.00 66.19           C  
ANISOU 4985  CG  LEU C 275    12096   5645   7409   6043  -3078  -1023       C  
ATOM   4986  CD1 LEU C 275       0.510  60.952 287.898  1.00 63.52           C  
ANISOU 4986  CD1 LEU C 275    11599   5343   7193   5709  -2800   -945       C  
ATOM   4987  CD2 LEU C 275      -0.083  62.682 286.224  1.00 70.97           C  
ANISOU 4987  CD2 LEU C 275    13250   6004   7711   6204  -3036   -914       C  
ATOM   4988  N   TYR C 276      -4.433  61.456 284.600  1.00 67.60           N  
ANISOU 4988  N   TYR C 276    12376   5968   7339   6932  -4239  -1429       N  
ATOM   4989  CA  TYR C 276      -5.204  60.897 283.488  1.00 68.84           C  
ANISOU 4989  CA  TYR C 276    12618   6147   7391   7123  -4575  -1535       C  
ATOM   4990  C   TYR C 276      -4.270  60.277 282.432  1.00 70.74           C  
ANISOU 4990  C   TYR C 276    13216   6243   7418   7054  -4494  -1461       C  
ATOM   4991  O   TYR C 276      -3.089  60.629 282.383  1.00 69.18           O  
ANISOU 4991  O   TYR C 276    13304   5890   7093   6947  -4197  -1313       O  
ATOM   4992  CB  TYR C 276      -6.090  61.988 282.870  1.00 72.84           C  
ANISOU 4992  CB  TYR C 276    13366   6574   7735   7498  -4836  -1582       C  
ATOM   4993  CG  TYR C 276      -7.252  62.405 283.748  1.00 75.23           C  
ANISOU 4993  CG  TYR C 276    13269   7060   8256   7616  -4995  -1696       C  
ATOM   4994  CD1 TYR C 276      -7.079  63.325 284.780  1.00 76.07           C  
ANISOU 4994  CD1 TYR C 276    13299   7157   8447   7595  -4796  -1642       C  
ATOM   4995  CD2 TYR C 276      -8.539  61.931 283.507  1.00 78.06           C  
ANISOU 4995  CD2 TYR C 276    13331   7598   8729   7758  -5348  -1858       C  
ATOM   4996  CE1 TYR C 276      -8.151  63.739 285.569  1.00 77.48           C  
ANISOU 4996  CE1 TYR C 276    13120   7507   8814   7722  -4927  -1748       C  
ATOM   4997  CE2 TYR C 276      -9.618  62.330 284.297  1.00 79.92           C  
ANISOU 4997  CE2 TYR C 276    13180   8017   9169   7874  -5480  -1961       C  
ATOM   4998  CZ  TYR C 276      -9.419  63.233 285.330  1.00 85.79           C  
ANISOU 4998  CZ  TYR C 276    13857   8752   9986   7863  -5261  -1906       C  
ATOM   4999  OH  TYR C 276     -10.480  63.633 286.108  1.00 86.65           O  
ANISOU 4999  OH  TYR C 276    13592   9046  10286   7995  -5376  -2008       O  
ATOM   5000  N   TRP C 277      -4.795  59.360 281.594  1.00 67.05           N  
ANISOU 5000  N   TRP C 277    12730   5830   6914   7115  -4756  -1564       N  
ATOM   5001  CA  TRP C 277      -4.006  58.679 280.567  1.00 88.69           C  
ANISOU 5001  CA  TRP C 277    15800   8448   9450   7072  -4708  -1515       C  
ATOM   5002  C   TRP C 277      -3.697  59.605 279.377  1.00 99.70           C  
ANISOU 5002  C   TRP C 277    17785   9611  10487   7341  -4757  -1444       C  
ATOM   5003  O   TRP C 277      -4.552  59.880 278.537  1.00 63.60           O  
ANISOU 5003  O   TRP C 277    13343   5132   5692   7440  -5009  -1626       O  
ATOM   5004  CB  TRP C 277      -4.717  57.396 280.107  1.00 88.31           C  
ANISOU 5004  CB  TRP C 277    15537   8530   9488   7046  -4993  -1660       C  
ATOM   5005  CG  TRP C 277      -3.890  56.504 279.227  1.00 89.28           C  
ANISOU 5005  CG  TRP C 277    15942   8547   9433   6971  -4925  -1622       C  
ATOM   5006  CD1 TRP C 277      -4.121  56.211 277.915  1.00 94.69           C  
ANISOU 5006  CD1 TRP C 277    16978   9128   9872   7169  -5164  -1672       C  
ATOM   5007  CD2 TRP C 277      -2.710  55.778 279.601  1.00 86.61           C  
ANISOU 5007  CD2 TRP C 277    15566   8198   9145   6691  -4598  -1531       C  
ATOM   5008  NE1 TRP C 277      -3.163  55.339 277.449  1.00 93.34           N  
ANISOU 5008  NE1 TRP C 277    16993   8882   9589   7033  -4997  -1618       N  
ATOM   5009  CE2 TRP C 277      -2.278  55.066 278.459  1.00 91.75           C  
ANISOU 5009  CE2 TRP C 277    16552   8739   9570   6743  -4648  -1531       C  
ATOM   5010  CE3 TRP C 277      -1.971  55.659 280.793  1.00 84.98           C  
ANISOU 5010  CE3 TRP C 277    15079   8063   9148   6410  -4274  -1452       C  
ATOM   5011  CZ2 TRP C 277      -1.142  54.244 278.474  1.00 89.43           C  
ANISOU 5011  CZ2 TRP C 277    16310   8410   9258   6533  -4378  -1455       C  
ATOM   5012  CZ3 TRP C 277      -0.844  54.849 280.804  1.00 84.85           C  
ANISOU 5012  CZ3 TRP C 277    15108   8012   9118   6198  -4020  -1376       C  
ATOM   5013  CH2 TRP C 277      -0.446  54.144 279.658  1.00 86.68           C  
ANISOU 5013  CH2 TRP C 277    15664   8142   9130   6264  -4070  -1379       C  
TER    5014      TRP C 277                                                      
ATOM   5015  N   ILE D   1      16.885  24.813 301.253  1.00 51.23           N  
ANISOU 5015  N   ILE D   1     7176   3215   9073   1892    238   -172       N  
ATOM   5016  CA  ILE D   1      15.916  24.940 300.163  1.00 50.78           C  
ANISOU 5016  CA  ILE D   1     7260   3265   8768   1719    285   -356       C  
ATOM   5017  C   ILE D   1      14.505  24.752 300.752  1.00 52.97           C  
ANISOU 5017  C   ILE D   1     7627   3647   8852   1342    109   -486       C  
ATOM   5018  O   ILE D   1      14.141  23.643 301.159  1.00 55.10           O  
ANISOU 5018  O   ILE D   1     8199   3715   9020   1182     99   -553       O  
ATOM   5019  CB  ILE D   1      16.258  23.979 298.976  1.00 56.82           C  
ANISOU 5019  CB  ILE D   1     8373   3803   9414   1852    516   -460       C  
ATOM   5020  CG1 ILE D   1      15.098  23.835 297.956  1.00 57.55           C  
ANISOU 5020  CG1 ILE D   1     8674   4007   9188   1596    534   -675       C  
ATOM   5021  CG2 ILE D   1      16.785  22.620 299.472  1.00 61.12           C  
ANISOU 5021  CG2 ILE D   1     9246   3976  10000   1960    586   -435       C  
ATOM   5022  CD1 ILE D   1      15.514  23.496 296.516  1.00 67.20           C  
ANISOU 5022  CD1 ILE D   1    10102   5139  10293   1746    770   -763       C  
ATOM   5023  N   GLN D   2      13.745  25.862 300.855  1.00 45.28           N  
ANISOU 5023  N   GLN D   2     6388   2990   7827   1206    -20   -519       N  
ATOM   5024  CA  GLN D   2      12.392  25.874 301.414  1.00 43.24           C  
ANISOU 5024  CA  GLN D   2     6111   2927   7392    869   -183   -652       C  
ATOM   5025  C   GLN D   2      11.511  26.901 300.669  1.00 45.17           C  
ANISOU 5025  C   GLN D   2     6154   3520   7491    829   -246   -740       C  
ATOM   5026  O   GLN D   2      10.386  26.554 300.292  1.00 46.93           O  
ANISOU 5026  O   GLN D   2     6459   3915   7456    592   -298   -921       O  
ATOM   5027  CB  GLN D   2      12.433  26.158 302.934  1.00 42.76           C  
ANISOU 5027  CB  GLN D   2     5879   2885   7482    779   -328   -550       C  
ATOM   5028  CG  GLN D   2      11.203  25.690 303.723  1.00 59.68           C  
ANISOU 5028  CG  GLN D   2     8099   5137   9439    396   -451   -695       C  
ATOM   5029  CD  GLN D   2      11.179  24.196 304.013  1.00 85.97           C  
ANISOU 5029  CD  GLN D   2    11841   8163  12660    226   -397   -746       C  
ATOM   5030  OE1 GLN D   2      10.904  23.366 303.137  1.00 85.16           O  
ANISOU 5030  OE1 GLN D   2    12038   7955  12364    130   -292   -885       O  
ATOM   5031  NE2 GLN D   2      11.401  23.817 305.269  1.00 75.70           N  
ANISOU 5031  NE2 GLN D   2    10602   6708  11452    162   -469   -639       N  
ATOM   5032  N   ARG D   3      12.019  28.140 300.438  1.00 37.54           N  
ANISOU 5032  N   ARG D   3     4936   2659   6668   1056   -240   -611       N  
ATOM   5033  CA  ARG D   3      11.282  29.217 299.765  1.00 35.99           C  
ANISOU 5033  CA  ARG D   3     4579   2753   6341   1089   -302   -653       C  
ATOM   5034  C   ARG D   3      12.154  29.951 298.743  1.00 40.07           C  
ANISOU 5034  C   ARG D   3     5079   3225   6922   1362   -166   -539       C  
ATOM   5035  O   ARG D   3      13.230  30.441 299.085  1.00 38.57           O  
ANISOU 5035  O   ARG D   3     4781   2912   6963   1517    -95   -382       O  
ATOM   5036  CB  ARG D   3      10.720  30.209 300.792  1.00 33.24           C  
ANISOU 5036  CB  ARG D   3     3961   2603   6065   1031   -460   -624       C  
ATOM   5037  CG  ARG D   3       9.429  29.734 301.427  1.00 43.00           C  
ANISOU 5037  CG  ARG D   3     5172   4042   7122    737   -596   -799       C  
ATOM   5038  CD  ARG D   3       8.923  30.678 302.497  1.00 54.39           C  
ANISOU 5038  CD  ARG D   3     6354   5665   8647    696   -721   -781       C  
ATOM   5039  NE  ARG D   3       9.159  30.141 303.838  1.00 66.06           N  
ANISOU 5039  NE  ARG D   3     7854   6995  10250    520   -752   -748       N  
ATOM   5040  CZ  ARG D   3       8.606  30.617 304.949  1.00 80.33           C  
ANISOU 5040  CZ  ARG D   3     9488   8940  12094    391   -851   -770       C  
ATOM   5041  NH1 ARG D   3       7.769  31.648 304.895  1.00 70.80           N  
ANISOU 5041  NH1 ARG D   3     8061   8016  10824    449   -919   -833       N  
ATOM   5042  NH2 ARG D   3       8.881  30.064 306.124  1.00 62.60           N  
ANISOU 5042  NH2 ARG D   3     7302   6548   9935    221   -878   -729       N  
ATOM   5043  N   THR D   4      11.679  30.026 297.485  1.00 38.39           N  
ANISOU 5043  N   THR D   4     4974   3135   6478   1390   -130   -623       N  
ATOM   5044  CA  THR D   4      12.393  30.656 296.367  1.00 38.71           C  
ANISOU 5044  CA  THR D   4     5056   3143   6508   1609     14   -534       C  
ATOM   5045  C   THR D   4      12.231  32.202 296.423  1.00 41.31           C  
ANISOU 5045  C   THR D   4     5190   3628   6876   1735    -62   -418       C  
ATOM   5046  O   THR D   4      11.150  32.682 296.774  1.00 40.38           O  
ANISOU 5046  O   THR D   4     4955   3732   6657   1674   -237   -473       O  
ATOM   5047  CB  THR D   4      11.962  30.031 295.022  1.00 48.12           C  
ANISOU 5047  CB  THR D   4     6487   4394   7404   1567     80   -671       C  
ATOM   5048  OG1 THR D   4      12.775  30.545 293.967  1.00 46.19           O  
ANISOU 5048  OG1 THR D   4     6313   4094   7144   1765    246   -580       O  
ATOM   5049  CG2 THR D   4      10.475  30.218 294.706  1.00 49.29           C  
ANISOU 5049  CG2 THR D   4     6589   4877   7260   1415   -115   -810       C  
ATOM   5050  N   PRO D   5      13.297  32.990 296.112  1.00 37.57           N  
ANISOU 5050  N   PRO D   5     4691   3040   6542   1906     81   -264       N  
ATOM   5051  CA  PRO D   5      13.186  34.457 296.228  1.00 36.40           C  
ANISOU 5051  CA  PRO D   5     4432   2975   6423   2004     31   -151       C  
ATOM   5052  C   PRO D   5      12.408  35.147 295.101  1.00 41.21           C  
ANISOU 5052  C   PRO D   5     5150   3751   6759   2113    -14   -161       C  
ATOM   5053  O   PRO D   5      12.323  34.636 293.982  1.00 43.19           O  
ANISOU 5053  O   PRO D   5     5569   4032   6808   2129     52   -220       O  
ATOM   5054  CB  PRO D   5      14.643  34.916 296.208  1.00 38.05           C  
ANISOU 5054  CB  PRO D   5     4613   3003   6840   2088    227     -1       C  
ATOM   5055  CG  PRO D   5      15.353  33.880 295.417  1.00 43.96           C  
ANISOU 5055  CG  PRO D   5     5494   3642   7568   2123    403    -43       C  
ATOM   5056  CD  PRO D   5      14.670  32.585 295.729  1.00 39.78           C  
ANISOU 5056  CD  PRO D   5     5038   3113   6964   2005    306   -192       C  
ATOM   5057  N   LYS D   6      11.880  36.341 295.410  1.00 35.59           N  
ANISOU 5057  N   LYS D   6     4356   3135   6031   2204   -122    -95       N  
ATOM   5058  CA  LYS D   6      11.141  37.218 294.508  1.00 36.07           C  
ANISOU 5058  CA  LYS D   6     4513   3347   5845   2374   -193    -62       C  
ATOM   5059  C   LYS D   6      12.051  38.404 294.174  1.00 38.58           C  
ANISOU 5059  C   LYS D   6     4953   3471   6232   2508    -35    123       C  
ATOM   5060  O   LYS D   6      12.355  39.207 295.055  1.00 37.71           O  
ANISOU 5060  O   LYS D   6     4765   3251   6310   2505    -20    204       O  
ATOM   5061  CB  LYS D   6       9.827  37.663 295.186  1.00 38.49           C  
ANISOU 5061  CB  LYS D   6     4650   3896   6077   2411   -422   -132       C  
ATOM   5062  CG  LYS D   6       8.798  38.331 294.274  1.00 51.38           C  
ANISOU 5062  CG  LYS D   6     6337   5782   7403   2612   -558   -134       C  
ATOM   5063  CD  LYS D   6       7.494  38.578 295.037  1.00 57.98           C  
ANISOU 5063  CD  LYS D   6     6938   6907   8185   2656   -775   -232       C  
ATOM   5064  CE  LYS D   6       6.291  38.711 294.136  1.00 68.70           C  
ANISOU 5064  CE  LYS D   6     8266   8628   9207   2831   -956   -283       C  
ATOM   5065  NZ  LYS D   6       6.119  40.098 293.638  1.00 79.41           N  
ANISOU 5065  NZ  LYS D   6     9781   9924  10466   3183   -961   -102       N  
ATOM   5066  N   ILE D   7      12.514  38.490 292.920  1.00 34.81           N  
ANISOU 5066  N   ILE D   7     4691   2946   5591   2585    100    181       N  
ATOM   5067  CA  ILE D   7      13.429  39.543 292.466  1.00 34.59           C  
ANISOU 5067  CA  ILE D   7     4827   2729   5587   2660    288    350       C  
ATOM   5068  C   ILE D   7      12.661  40.659 291.706  1.00 37.61           C  
ANISOU 5068  C   ILE D   7     5412   3176   5700   2871    198    444       C  
ATOM   5069  O   ILE D   7      12.041  40.383 290.680  1.00 38.46           O  
ANISOU 5069  O   ILE D   7     5635   3449   5526   2958    116    405       O  
ATOM   5070  CB  ILE D   7      14.554  38.918 291.592  1.00 38.86           C  
ANISOU 5070  CB  ILE D   7     5482   3160   6121   2595    538    356       C  
ATOM   5071  CG1 ILE D   7      15.207  37.694 292.276  1.00 37.48           C  
ANISOU 5071  CG1 ILE D   7     5124   2934   6182   2460    605    260       C  
ATOM   5072  CG2 ILE D   7      15.603  39.959 291.235  1.00 41.69           C  
ANISOU 5072  CG2 ILE D   7     5978   3342   6519   2601    763    515       C  
ATOM   5073  CD1 ILE D   7      15.585  36.615 291.356  1.00 40.90           C  
ANISOU 5073  CD1 ILE D   7     5678   3355   6508   2443    750    168       C  
ATOM   5074  N   GLN D   8      12.713  41.911 292.216  1.00 32.90           N  
ANISOU 5074  N   GLN D   8     4876   2493   5131   2893    217    560       N  
ATOM   5075  CA  GLN D   8      12.046  43.081 291.619  1.00 34.13           C  
ANISOU 5075  CA  GLN D   8     5271   2630   5066   3167    141    678       C  
ATOM   5076  C   GLN D   8      13.038  44.248 291.495  1.00 38.99           C  
ANISOU 5076  C   GLN D   8     6161   2902   5752   3193    362    862       C  
ATOM   5077  O   GLN D   8      13.600  44.674 292.506  1.00 38.24           O  
ANISOU 5077  O   GLN D   8     5985   2646   5896   3062    445    883       O  
ATOM   5078  CB  GLN D   8      10.826  43.502 292.452  1.00 34.91           C  
ANISOU 5078  CB  GLN D   8     5213   2891   5161   3308    -94    622       C  
ATOM   5079  CG  GLN D   8       9.730  42.451 292.549  1.00 41.40           C  
ANISOU 5079  CG  GLN D   8     5779   4031   5920   3363   -332    455       C  
ATOM   5080  CD  GLN D   8       9.039  42.491 293.888  1.00 49.67           C  
ANISOU 5080  CD  GLN D   8     6549   5201   7122   3350   -481    351       C  
ATOM   5081  OE1 GLN D   8       7.918  42.992 294.016  1.00 39.46           O  
ANISOU 5081  OE1 GLN D   8     5176   4126   5690   3572   -664    323       O  
ATOM   5082  NE2 GLN D   8       9.682  41.929 294.912  1.00 43.48           N  
ANISOU 5082  NE2 GLN D   8     5601   4303   6616   3099   -407    290       N  
ATOM   5083  N   VAL D   9      13.267  44.749 290.259  1.00 36.77           N  
ANISOU 5083  N   VAL D   9     6214   2550   5208   3280    470    981       N  
ATOM   5084  CA  VAL D   9      14.244  45.811 289.969  1.00 37.63           C  
ANISOU 5084  CA  VAL D   9     6637   2364   5299   3210    719   1144       C  
ATOM   5085  C   VAL D   9      13.526  47.110 289.585  1.00 43.97           C  
ANISOU 5085  C   VAL D   9     7806   3033   5868   3514    632   1302       C  
ATOM   5086  O   VAL D   9      12.678  47.103 288.687  1.00 46.05           O  
ANISOU 5086  O   VAL D   9     8193   3461   5844   3768    463   1331       O  
ATOM   5087  CB  VAL D   9      15.256  45.382 288.871  1.00 42.49           C  
ANISOU 5087  CB  VAL D   9     7408   2918   5820   3067    970   1178       C  
ATOM   5088  CG1 VAL D   9      16.463  46.308 288.836  1.00 43.33           C  
ANISOU 5088  CG1 VAL D   9     7726   2746   5991   2871   1268   1302       C  
ATOM   5089  CG2 VAL D   9      15.705  43.938 289.060  1.00 40.53           C  
ANISOU 5089  CG2 VAL D   9     6829   2826   5743   2899   1009   1012       C  
ATOM   5090  N   TYR D  10      13.893  48.231 290.245  1.00 40.28           N  
ANISOU 5090  N   TYR D  10     7503   2353   5450   3416    764   1375       N  
ATOM   5091  CA  TYR D  10      13.276  49.544 290.022  1.00 42.32           C  
ANISOU 5091  CA  TYR D  10     8147   2457   5474   3673    728   1508       C  
ATOM   5092  C   TYR D  10      14.218  50.710 290.393  1.00 46.04           C  
ANISOU 5092  C   TYR D  10     8997   2401   6096   3567    978   1672       C  
ATOM   5093  O   TYR D  10      15.111  50.550 291.218  1.00 43.24           O  
ANISOU 5093  O   TYR D  10     8422   2012   5995   3210   1130   1590       O  
ATOM   5094  CB  TYR D  10      11.951  49.653 290.816  1.00 42.90           C  
ANISOU 5094  CB  TYR D  10     8010   2727   5563   3932    452   1419       C  
ATOM   5095  CG  TYR D  10      12.080  49.343 292.292  1.00 41.46           C  
ANISOU 5095  CG  TYR D  10     7452   2584   5717   3711    434   1275       C  
ATOM   5096  CD1 TYR D  10      11.954  48.041 292.766  1.00 40.15           C  
ANISOU 5096  CD1 TYR D  10     6850   2651   5756   3605    307   1123       C  
ATOM   5097  CD2 TYR D  10      12.321  50.353 293.217  1.00 42.58           C  
ANISOU 5097  CD2 TYR D  10     7729   2454   5994   3658    536   1310       C  
ATOM   5098  CE1 TYR D  10      12.113  47.745 294.118  1.00 38.16           C  
ANISOU 5098  CE1 TYR D  10     6275   2467   5757   3350    296    994       C  
ATOM   5099  CE2 TYR D  10      12.457  50.072 294.575  1.00 40.94           C  
ANISOU 5099  CE2 TYR D  10     7186   2306   6063   3427    515   1177       C  
ATOM   5100  CZ  TYR D  10      12.362  48.766 295.018  1.00 41.87           C  
ANISOU 5100  CZ  TYR D  10     6901   2542   6465   3440    366   1073       C  
ATOM   5101  OH  TYR D  10      12.495  48.494 296.352  1.00 39.63           O  
ANISOU 5101  OH  TYR D  10     6322   2296   6440   3230    338    956       O  
ATOM   5102  N   SER D  11      13.988  51.884 289.775  1.00 47.26           N  
ANISOU 5102  N   SER D  11     9658   2348   5952   3739   1044   1826       N  
ATOM   5103  CA  SER D  11      14.720  53.143 289.980  1.00 49.20           C  
ANISOU 5103  CA  SER D  11    10351   2157   6184   3572   1306   1950       C  
ATOM   5104  C   SER D  11      14.082  53.988 291.106  1.00 54.37           C  
ANISOU 5104  C   SER D  11    11122   2563   6974   3793   1209   1968       C  
ATOM   5105  O   SER D  11      12.877  53.858 291.349  1.00 54.08           O  
ANISOU 5105  O   SER D  11    10935   2712   6902   4191    938   1928       O  
ATOM   5106  CB  SER D  11      14.750  53.944 288.683  1.00 55.09           C  
ANISOU 5106  CB  SER D  11    11744   2598   6588   3743   1418   2193       C  
ATOM   5107  OG  SER D  11      13.453  54.040 288.116  1.00 61.25           O  
ANISOU 5107  OG  SER D  11    12676   3490   7107   4268   1144   2278       O  
ATOM   5108  N   ARG D  12      14.884  54.851 291.788  1.00 52.23           N  
ANISOU 5108  N   ARG D  12    11046   2026   6772   3450   1458   1957       N  
ATOM   5109  CA  ARG D  12      14.398  55.701 292.891  1.00 52.75           C  
ANISOU 5109  CA  ARG D  12    11207   1954   6881   3527   1439   1899       C  
ATOM   5110  C   ARG D  12      13.436  56.771 292.387  1.00 60.96           C  
ANISOU 5110  C   ARG D  12    12888   2559   7717   4124   1353   2128       C  
ATOM   5111  O   ARG D  12      12.321  56.879 292.898  1.00 60.70           O  
ANISOU 5111  O   ARG D  12    12731   2639   7694   4536   1131   2077       O  
ATOM   5112  CB  ARG D  12      15.559  56.374 293.653  1.00 51.64           C  
ANISOU 5112  CB  ARG D  12    11199   1562   6859   3009   1734   1860       C  
ATOM   5113  CG  ARG D  12      15.482  56.263 295.178  1.00 52.95           C  
ANISOU 5113  CG  ARG D  12    11099   1584   7436   2930   1647   1764       C  
ATOM   5114  CD  ARG D  12      14.264  56.911 295.815  1.00 57.75           C  
ANISOU 5114  CD  ARG D  12    11870   2056   8015   3348   1502   1741       C  
ATOM   5115  NE  ARG D  12      14.474  58.327 296.107  1.00 73.34           N  
ANISOU 5115  NE  ARG D  12    14483   3509   9873   3285   1732   1825       N  
ATOM   5116  CZ  ARG D  12      13.545  59.134 296.616  1.00 88.53           C  
ANISOU 5116  CZ  ARG D  12    16702   5199  11737   3657   1684   1824       C  
ATOM   5117  NH1 ARG D  12      12.331  58.673 296.888  1.00 72.19           N  
ANISOU 5117  NH1 ARG D  12    14293   3421   9714   4118   1407   1742       N  
ATOM   5118  NH2 ARG D  12      13.824  60.410 296.855  1.00 76.56           N  
ANISOU 5118  NH2 ARG D  12    15830   3158  10103   3563   1927   1896       N  
ATOM   5119  N   HIS D  13      13.880  57.569 291.407  1.00 62.21           N  
ANISOU 5119  N   HIS D  13    13657   2382   7598   4100   1553   2321       N  
ATOM   5120  CA  HIS D  13      13.118  58.661 290.803  1.00 67.01           C  
ANISOU 5120  CA  HIS D  13    14914   2661   7885   4594   1519   2526       C  
ATOM   5121  C   HIS D  13      12.720  58.276 289.368  1.00 73.68           C  
ANISOU 5121  C   HIS D  13    15860   3712   8422   4887   1378   2667       C  
ATOM   5122  O   HIS D  13      13.333  57.348 288.832  1.00 71.69           O  
ANISOU 5122  O   HIS D  13    15314   3725   8202   4578   1421   2612       O  
ATOM   5123  CB  HIS D  13      13.963  59.948 290.814  1.00 71.26           C  
ANISOU 5123  CB  HIS D  13    16179   2597   8301   4308   1874   2657       C  
ATOM   5124  CG  HIS D  13      14.438  60.350 292.175  1.00 73.39           C  
ANISOU 5124  CG  HIS D  13    16392   2661   8831   3963   2027   2513       C  
ATOM   5125  ND1 HIS D  13      15.656  59.917 292.670  1.00 72.73           N  
ANISOU 5125  ND1 HIS D  13    16017   2650   8967   3297   2233   2388       N  
ATOM   5126  CD2 HIS D  13      13.842  61.133 293.102  1.00 76.25           C  
ANISOU 5126  CD2 HIS D  13    16948   2776   9248   4209   1999   2473       C  
ATOM   5127  CE1 HIS D  13      15.762  60.449 293.875  1.00 71.90           C  
ANISOU 5127  CE1 HIS D  13    15945   2345   9028   3128   2309   2280       C  
ATOM   5128  NE2 HIS D  13      14.695  61.190 294.179  1.00 74.31           N  
ANISOU 5128  NE2 HIS D  13    16557   2435   9243   3654   2187   2320       N  
ATOM   5129  N   PRO D  14      11.722  58.933 288.713  1.00 74.48           N  
ANISOU 5129  N   PRO D  14    16369   3716   8212   5485   1208   2845       N  
ATOM   5130  CA  PRO D  14      11.381  58.540 287.333  1.00 76.35           C  
ANISOU 5130  CA  PRO D  14    16701   4184   8125   5727   1059   2980       C  
ATOM   5131  C   PRO D  14      12.582  58.684 286.403  1.00 82.52           C  
ANISOU 5131  C   PRO D  14    17892   4731   8731   5281   1369   3099       C  
ATOM   5132  O   PRO D  14      13.291  59.693 286.456  1.00 84.31           O  
ANISOU 5132  O   PRO D  14    18696   4453   8883   5049   1669   3213       O  
ATOM   5133  CB  PRO D  14      10.235  59.484 286.952  1.00 82.88           C  
ANISOU 5133  CB  PRO D  14    18001   4845   8645   6435    868   3182       C  
ATOM   5134  CG  PRO D  14      10.324  60.612 287.905  1.00 88.98           C  
ANISOU 5134  CG  PRO D  14    19176   5105   9529   6465   1054   3202       C  
ATOM   5135  CD  PRO D  14      10.870  60.047 289.174  1.00 79.48           C  
ANISOU 5135  CD  PRO D  14    17399   4040   8759   5987   1142   2933       C  
ATOM   5136  N   ALA D  15      12.846  57.627 285.616  1.00 78.51           N  
ANISOU 5136  N   ALA D  15    17062   4602   8165   5115   1319   3045       N  
ATOM   5137  CA  ALA D  15      13.974  57.514 284.695  1.00 79.76           C  
ANISOU 5137  CA  ALA D  15    17476   4658   8172   4678   1610   3111       C  
ATOM   5138  C   ALA D  15      14.064  58.693 283.708  1.00 90.04           C  
ANISOU 5138  C   ALA D  15    19664   5504   9042   4810   1767   3401       C  
ATOM   5139  O   ALA D  15      13.064  59.080 283.093  1.00 92.50           O  
ANISOU 5139  O   ALA D  15    20293   5816   9039   5355   1530   3575       O  
ATOM   5140  CB  ALA D  15      13.891  56.200 283.933  1.00 78.53           C  
ANISOU 5140  CB  ALA D  15    16877   5000   7961   4647   1466   3011       C  
ATOM   5141  N   GLU D  16      15.279  59.272 283.609  1.00 88.78           N  
ANISOU 5141  N   GLU D  16    19899   4967   8865   4294   2171   3449       N  
ATOM   5142  CA  GLU D  16      15.661  60.389 282.736  1.00 94.29           C  
ANISOU 5142  CA  GLU D  16    21491   5167   9167   4239   2421   3707       C  
ATOM   5143  C   GLU D  16      17.110  60.155 282.298  1.00 98.07           C  
ANISOU 5143  C   GLU D  16    22000   5618   9644   3533   2827   3654       C  
ATOM   5144  O   GLU D  16      18.002  60.026 283.144  1.00 95.08           O  
ANISOU 5144  O   GLU D  16    21296   5242   9587   3039   3046   3482       O  
ATOM   5145  CB  GLU D  16      15.473  61.749 283.452  1.00 98.62           C  
ANISOU 5145  CB  GLU D  16    22614   5152   9704   4369   2522   3814       C  
ATOM   5146  CG  GLU D  16      15.803  62.983 282.616  1.00116.11           C  
ANISOU 5146  CG  GLU D  16    25860   6775  11482   4353   2775   4099       C  
ATOM   5147  CD  GLU D  16      14.792  63.457 281.583  1.00140.93           C  
ANISOU 5147  CD  GLU D  16    29546   9826  14175   5027   2527   4379       C  
ATOM   5148  OE1 GLU D  16      13.614  63.035 281.649  1.00138.05           O  
ANISOU 5148  OE1 GLU D  16    28803   9809  13838   5636   2117   4363       O  
ATOM   5149  OE2 GLU D  16      15.174  64.290 280.729  1.00135.07           O  
ANISOU 5149  OE2 GLU D  16    29624   8663  13032   4940   2746   4618       O  
ATOM   5150  N   ASN D  17      17.322  60.055 280.974  1.00 97.73           N  
ANISOU 5150  N   ASN D  17    22308   5596   9230   3496   2917   3793       N  
ATOM   5151  CA  ASN D  17      18.614  59.773 280.349  1.00 98.44           C  
ANISOU 5151  CA  ASN D  17    22427   5718   9257   2875   3305   3745       C  
ATOM   5152  C   ASN D  17      19.616  60.916 280.561  1.00106.65           C  
ANISOU 5152  C   ASN D  17    24063   6243  10217   2377   3734   3828       C  
ATOM   5153  O   ASN D  17      19.430  62.015 280.030  1.00111.71           O  
ANISOU 5153  O   ASN D  17    25553   6407  10484   2512   3822   4075       O  
ATOM   5154  CB  ASN D  17      18.431  59.484 278.851  1.00101.69           C  
ANISOU 5154  CB  ASN D  17    23136   6265   9237   3013   3275   3884       C  
ATOM   5155  CG  ASN D  17      17.553  58.286 278.558  1.00121.27           C  
ANISOU 5155  CG  ASN D  17    25040   9279  11756   3405   2885   3777       C  
ATOM   5156  OD1 ASN D  17      16.356  58.260 278.869  1.00113.53           O  
ANISOU 5156  OD1 ASN D  17    23954   8407  10773   3958   2493   3817       O  
ATOM   5157  ND2 ASN D  17      18.126  57.272 277.932  1.00112.46           N  
ANISOU 5157  ND2 ASN D  17    23553   8517  10661   3119   2998   3630       N  
ATOM   5158  N   GLY D  18      20.656  60.639 281.351  1.00101.09           N  
ANISOU 5158  N   GLY D  18    22911   5648   9850   1803   3989   3620       N  
ATOM   5159  CA  GLY D  18      21.714  61.598 281.654  1.00104.12           C  
ANISOU 5159  CA  GLY D  18    23726   5642  10195   1209   4412   3639       C  
ATOM   5160  C   GLY D  18      21.884  61.929 283.123  1.00106.23           C  
ANISOU 5160  C   GLY D  18    23726   5807  10830   1023   4420   3492       C  
ATOM   5161  O   GLY D  18      23.000  61.846 283.645  1.00105.20           O  
ANISOU 5161  O   GLY D  18    23285   5782  10904    409   4697   3333       O  
ATOM   5162  N   LYS D  19      20.780  62.337 283.794  1.00102.13           N  
ANISOU 5162  N   LYS D  19    23326   5102  10378   1551   4119   3543       N  
ATOM   5163  CA  LYS D  19      20.755  62.699 285.217  1.00 99.96           C  
ANISOU 5163  CA  LYS D  19    22858   4702  10421   1455   4092   3408       C  
ATOM   5164  C   LYS D  19      21.004  61.473 286.104  1.00 98.26           C  
ANISOU 5164  C   LYS D  19    21615   5047  10674   1308   3941   3138       C  
ATOM   5165  O   LYS D  19      20.656  60.350 285.719  1.00 94.54           O  
ANISOU 5165  O   LYS D  19    20610   5022  10289   1563   3715   3075       O  
ATOM   5166  CB  LYS D  19      19.417  63.357 285.583  1.00103.29           C  
ANISOU 5166  CB  LYS D  19    23651   4827  10767   2143   3801   3528       C  
ATOM   5167  N   SER D  20      21.617  61.692 287.288  1.00 93.79           N  
ANISOU 5167  N   SER D  20    20808   4445  10385    887   4068   2982       N  
ATOM   5168  CA  SER D  20      21.937  60.622 288.241  1.00 88.55           C  
ANISOU 5168  CA  SER D  20    19225   4267  10153    716   3939   2742       C  
ATOM   5169  C   SER D  20      20.674  60.051 288.891  1.00 87.41           C  
ANISOU 5169  C   SER D  20    18681   4318  10211   1308   3510   2679       C  
ATOM   5170  O   SER D  20      19.733  60.795 289.189  1.00 88.40           O  
ANISOU 5170  O   SER D  20    19210   4132  10246   1705   3374   2762       O  
ATOM   5171  CB  SER D  20      22.900  61.116 289.317  1.00 93.18           C  
ANISOU 5171  CB  SER D  20    19732   4751  10921    102   4178   2614       C  
ATOM   5172  OG  SER D  20      23.409  60.031 290.078  1.00 98.46           O  
ANISOU 5172  OG  SER D  20    19519   5922  11970   -101   4077   2405       O  
ATOM   5173  N   ASN D  21      20.671  58.724 289.108  1.00 78.14           N  
ANISOU 5173  N   ASN D  21    16724   3661   9305   1361   3316   2524       N  
ATOM   5174  CA  ASN D  21      19.558  57.980 289.696  1.00 73.55           C  
ANISOU 5174  CA  ASN D  21    15673   3350   8922   1832   2927   2433       C  
ATOM   5175  C   ASN D  21      20.091  56.838 290.589  1.00 72.37           C  
ANISOU 5175  C   ASN D  21    14704   3632   9162   1567   2857   2216       C  
ATOM   5176  O   ASN D  21      21.307  56.646 290.686  1.00 72.10           O  
ANISOU 5176  O   ASN D  21    14455   3708   9233   1073   3096   2149       O  
ATOM   5177  CB  ASN D  21      18.663  57.434 288.563  1.00 72.86           C  
ANISOU 5177  CB  ASN D  21    15627   3442   8615   2337   2699   2525       C  
ATOM   5178  CG  ASN D  21      17.189  57.280 288.880  1.00 86.63           C  
ANISOU 5178  CG  ASN D  21    17234   5301  10380   2931   2316   2514       C  
ATOM   5179  OD1 ASN D  21      16.763  57.175 290.037  1.00 80.00           O  
ANISOU 5179  OD1 ASN D  21    16039   4553   9805   2984   2169   2380       O  
ATOM   5180  ND2 ASN D  21      16.374  57.213 287.836  1.00 75.82           N  
ANISOU 5180  ND2 ASN D  21    16110   3979   8718   3381   2142   2646       N  
ATOM   5181  N   PHE D  22      19.181  56.096 291.249  1.00 64.75           N  
ANISOU 5181  N   PHE D  22    13290   2917   8396   1896   2532   2109       N  
ATOM   5182  CA  PHE D  22      19.515  54.972 292.123  1.00 60.00           C  
ANISOU 5182  CA  PHE D  22    11962   2695   8139   1717   2423   1922       C  
ATOM   5183  C   PHE D  22      18.765  53.715 291.683  1.00 60.13           C  
ANISOU 5183  C   PHE D  22    11581   3079   8186   2063   2156   1861       C  
ATOM   5184  O   PHE D  22      17.544  53.763 291.515  1.00 59.39           O  
ANISOU 5184  O   PHE D  22    11580   3005   7981   2504   1910   1890       O  
ATOM   5185  CB  PHE D  22      19.188  55.317 293.583  1.00 60.22           C  
ANISOU 5185  CB  PHE D  22    11847   2653   8382   1679   2314   1825       C  
ATOM   5186  CG  PHE D  22      20.350  55.845 294.386  1.00 62.62           C  
ANISOU 5186  CG  PHE D  22    12142   2838   8812   1124   2559   1774       C  
ATOM   5187  CD1 PHE D  22      20.802  57.147 294.212  1.00 69.77           C  
ANISOU 5187  CD1 PHE D  22    13665   3320   9524    894   2820   1869       C  
ATOM   5188  CD2 PHE D  22      20.970  55.053 295.343  1.00 62.22           C  
ANISOU 5188  CD2 PHE D  22    11483   3102   9054    823   2522   1630       C  
ATOM   5189  CE1 PHE D  22      21.868  57.641 294.968  1.00 71.87           C  
ANISOU 5189  CE1 PHE D  22    13914   3512   9883    323   3046   1802       C  
ATOM   5190  CE2 PHE D  22      22.037  55.547 296.098  1.00 66.28           C  
ANISOU 5190  CE2 PHE D  22    11952   3568   9664    296   2724   1578       C  
ATOM   5191  CZ  PHE D  22      22.478  56.838 295.906  1.00 68.21           C  
ANISOU 5191  CZ  PHE D  22    12788   3421   9708     25   2988   1654       C  
ATOM   5192  N   LEU D  23      19.500  52.605 291.464  1.00 54.16           N  
ANISOU 5192  N   LEU D  23    10395   2621   7562   1862   2214   1772       N  
ATOM   5193  CA  LEU D  23      18.922  51.335 291.024  1.00 51.57           C  
ANISOU 5193  CA  LEU D  23     9718   2620   7256   2111   2005   1692       C  
ATOM   5194  C   LEU D  23      18.732  50.406 292.225  1.00 52.70           C  
ANISOU 5194  C   LEU D  23     9302   3004   7719   2090   1806   1531       C  
ATOM   5195  O   LEU D  23      19.699  50.090 292.925  1.00 51.65           O  
ANISOU 5195  O   LEU D  23     8868   2937   7820   1769   1917   1461       O  
ATOM   5196  CB  LEU D  23      19.796  50.673 289.932  1.00 52.22           C  
ANISOU 5196  CB  LEU D  23     9736   2842   7262   1942   2212   1688       C  
ATOM   5197  CG  LEU D  23      19.307  49.341 289.323  1.00 54.73           C  
ANISOU 5197  CG  LEU D  23     9787   3456   7551   2162   2048   1599       C  
ATOM   5198  CD1 LEU D  23      18.280  49.561 288.227  1.00 56.34           C  
ANISOU 5198  CD1 LEU D  23    10379   3629   7397   2495   1923   1700       C  
ATOM   5199  CD2 LEU D  23      20.469  48.549 288.762  1.00 57.30           C  
ANISOU 5199  CD2 LEU D  23     9887   3938   7946   1920   2287   1531       C  
ATOM   5200  N   ASN D  24      17.478  49.980 292.455  1.00 47.26           N  
ANISOU 5200  N   ASN D  24     8475   2465   7018   2424   1510   1473       N  
ATOM   5201  CA  ASN D  24      17.102  49.103 293.557  1.00 43.51           C  
ANISOU 5201  CA  ASN D  24     7526   2207   6798   2420   1306   1324       C  
ATOM   5202  C   ASN D  24      16.673  47.732 293.049  1.00 46.39           C  
ANISOU 5202  C   ASN D  24     7611   2867   7148   2556   1151   1226       C  
ATOM   5203  O   ASN D  24      15.834  47.649 292.154  1.00 46.52           O  
ANISOU 5203  O   ASN D  24     7790   2961   6927   2822   1030   1253       O  
ATOM   5204  CB  ASN D  24      15.949  49.718 294.380  1.00 41.35           C  
ANISOU 5204  CB  ASN D  24     7312   1870   6528   2643   1107   1305       C  
ATOM   5205  CG  ASN D  24      16.158  51.116 294.911  1.00 60.55           C  
ANISOU 5205  CG  ASN D  24    10114   3961   8931   2569   1248   1391       C  
ATOM   5206  OD1 ASN D  24      17.067  51.385 295.692  1.00 56.20           O  
ANISOU 5206  OD1 ASN D  24     9512   3301   8539   2216   1409   1372       O  
ATOM   5207  ND2 ASN D  24      15.251  52.019 294.586  1.00 54.21           N  
ANISOU 5207  ND2 ASN D  24     9683   2995   7919   2912   1175   1477       N  
ATOM   5208  N   CYS D  25      17.245  46.663 293.632  1.00 41.95           N  
ANISOU 5208  N   CYS D  25     6648   2467   6823   2372   1150   1115       N  
ATOM   5209  CA  CYS D  25      16.901  45.255 293.393  1.00 40.79           C  
ANISOU 5209  CA  CYS D  25     6240   2560   6699   2446   1020    997       C  
ATOM   5210  C   CYS D  25      16.467  44.725 294.747  1.00 38.57           C  
ANISOU 5210  C   CYS D  25     5628   2388   6640   2402    828    887       C  
ATOM   5211  O   CYS D  25      17.253  44.756 295.695  1.00 37.06           O  
ANISOU 5211  O   CYS D  25     5241   2163   6677   2189    895    875       O  
ATOM   5212  CB  CYS D  25      18.074  44.475 292.793  1.00 42.94           C  
ANISOU 5212  CB  CYS D  25     6409   2877   7029   2290   1236    979       C  
ATOM   5213  SG  CYS D  25      17.853  42.667 292.726  1.00 46.19           S  
ANISOU 5213  SG  CYS D  25     6542   3509   7501   2345   1124    820       S  
ATOM   5214  N   TYR D  26      15.177  44.386 294.875  1.00 33.31           N  
ANISOU 5214  N   TYR D  26     4870   2039   5747   2416    604    785       N  
ATOM   5215  CA  TYR D  26      14.594  43.948 296.135  1.00 30.89           C  
ANISOU 5215  CA  TYR D  26     4268   1989   5480   2196    434    653       C  
ATOM   5216  C   TYR D  26      14.262  42.469 296.079  1.00 33.14           C  
ANISOU 5216  C   TYR D  26     4375   2314   5901   2320    310    550       C  
ATOM   5217  O   TYR D  26      13.240  42.079 295.500  1.00 33.35           O  
ANISOU 5217  O   TYR D  26     4440   2482   5751   2482    172    485       O  
ATOM   5218  CB  TYR D  26      13.357  44.793 296.473  1.00 31.61           C  
ANISOU 5218  CB  TYR D  26     4450   2109   5454   2393    275    635       C  
ATOM   5219  CG  TYR D  26      12.682  44.441 297.782  1.00 30.60           C  
ANISOU 5219  CG  TYR D  26     4067   2117   5443   2291    108    509       C  
ATOM   5220  CD1 TYR D  26      13.302  44.699 299.002  1.00 30.93           C  
ANISOU 5220  CD1 TYR D  26     3997   1996   5759   2157    151    518       C  
ATOM   5221  CD2 TYR D  26      11.397  43.912 297.804  1.00 30.57           C  
ANISOU 5221  CD2 TYR D  26     3953   2338   5326   2417    -98    390       C  
ATOM   5222  CE1 TYR D  26      12.671  44.403 300.211  1.00 29.49           C  
ANISOU 5222  CE1 TYR D  26     3608   1957   5642   2025      9    399       C  
ATOM   5223  CE2 TYR D  26      10.753  43.622 299.006  1.00 29.79           C  
ANISOU 5223  CE2 TYR D  26     3640   2362   5317   2307   -229    267       C  
ATOM   5224  CZ  TYR D  26      11.395  43.870 300.207  1.00 31.28           C  
ANISOU 5224  CZ  TYR D  26     3731   2276   5879   2327   -190    300       C  
ATOM   5225  OH  TYR D  26      10.767  43.582 301.390  1.00 28.37           O  
ANISOU 5225  OH  TYR D  26     3172   2088   5519   2117   -302    169       O  
ATOM   5226  N   VAL D  27      15.167  41.649 296.679  1.00 29.41           N  
ANISOU 5226  N   VAL D  27     3679   2034   5461   1872    388    501       N  
ATOM   5227  CA  VAL D  27      15.113  40.184 296.792  1.00 27.87           C  
ANISOU 5227  CA  VAL D  27     3340   1996   5254   1718    323    394       C  
ATOM   5228  C   VAL D  27      14.275  39.853 298.036  1.00 28.75           C  
ANISOU 5228  C   VAL D  27     3294   2125   5505   1719    118    298       C  
ATOM   5229  O   VAL D  27      14.738  39.985 299.167  1.00 27.99           O  
ANISOU 5229  O   VAL D  27     3055   2026   5556   1513    115    310       O  
ATOM   5230  CB  VAL D  27      16.534  39.588 296.834  1.00 30.38           C  
ANISOU 5230  CB  VAL D  27     3563   2078   5904   1817    492    451       C  
ATOM   5231  CG1 VAL D  27      16.496  38.075 296.668  1.00 30.17           C  
ANISOU 5231  CG1 VAL D  27     3474   2107   5884   1791    454    353       C  
ATOM   5232  CG2 VAL D  27      17.414  40.215 295.761  1.00 31.56           C  
ANISOU 5232  CG2 VAL D  27     3874   2087   6031   1939    723    550       C  
ATOM   5233  N   SER D  28      13.024  39.463 297.799  1.00 25.50           N  
ANISOU 5233  N   SER D  28     2917   2006   4764   1567    -33    175       N  
ATOM   5234  CA  SER D  28      11.982  39.263 298.789  1.00 24.51           C  
ANISOU 5234  CA  SER D  28     2680   2012   4620   1451   -212     53       C  
ATOM   5235  C   SER D  28      11.577  37.812 298.985  1.00 25.56           C  
ANISOU 5235  C   SER D  28     2722   2117   4872   1524   -313    -63       C  
ATOM   5236  O   SER D  28      11.696  37.002 298.070  1.00 25.38           O  
ANISOU 5236  O   SER D  28     2787   2102   4755   1559   -271    -90       O  
ATOM   5237  CB  SER D  28      10.754  40.053 298.329  1.00 29.71           C  
ANISOU 5237  CB  SER D  28     3361   2630   5297   1986   -347     41       C  
ATOM   5238  OG  SER D  28       9.612  39.990 299.170  1.00 39.34           O  
ANISOU 5238  OG  SER D  28     4331   3835   6782   2369   -547    -46       O  
ATOM   5239  N   GLY D  29      11.032  37.528 300.168  1.00 22.37           N  
ANISOU 5239  N   GLY D  29     2229   1859   4411   1179   -417   -163       N  
ATOM   5240  CA  GLY D  29      10.433  36.236 300.511  1.00 21.47           C  
ANISOU 5240  CA  GLY D  29     2070   1796   4289   1073   -517   -298       C  
ATOM   5241  C   GLY D  29      11.109  34.874 300.353  1.00 24.73           C  
ANISOU 5241  C   GLY D  29     2479   1956   4961   1280   -466   -293       C  
ATOM   5242  O   GLY D  29      10.542  33.994 299.705  1.00 26.33           O  
ANISOU 5242  O   GLY D  29     2748   2150   5106   1398   -494   -403       O  
ATOM   5243  N   PHE D  30      12.371  34.752 300.794  1.00 21.09           N  
ANISOU 5243  N   PHE D  30     2022   1531   4462    907   -353   -187       N  
ATOM   5244  CA  PHE D  30      13.150  33.524 300.599  1.00 20.49           C  
ANISOU 5244  CA  PHE D  30     1990   1378   4416    860   -271   -169       C  
ATOM   5245  C   PHE D  30      13.563  32.830 301.913  1.00 24.08           C  
ANISOU 5245  C   PHE D  30     2366   1543   5239   1018   -323   -145       C  
ATOM   5246  O   PHE D  30      13.538  33.435 302.986  1.00 23.81           O  
ANISOU 5246  O   PHE D  30     2206   1555   5286    896   -396   -115       O  
ATOM   5247  CB  PHE D  30      14.402  33.827 299.756  1.00 21.72           C  
ANISOU 5247  CB  PHE D  30     2179   1420   4653   1025    -80    -46       C  
ATOM   5248  CG  PHE D  30      15.372  34.838 300.320  1.00 21.62           C  
ANISOU 5248  CG  PHE D  30     2041   1375   4797    994     -7     81       C  
ATOM   5249  CD1 PHE D  30      16.408  34.442 301.153  1.00 23.15           C  
ANISOU 5249  CD1 PHE D  30     2113   1405   5279   1070     28    159       C  
ATOM   5250  CD2 PHE D  30      15.294  36.174 299.960  1.00 22.73           C  
ANISOU 5250  CD2 PHE D  30     2198   1486   4953   1137     26    136       C  
ATOM   5251  CE1 PHE D  30      17.327  35.372 301.648  1.00 23.62           C  
ANISOU 5251  CE1 PHE D  30     2040   1428   5507   1061     89    270       C  
ATOM   5252  CE2 PHE D  30      16.203  37.108 300.466  1.00 24.33           C  
ANISOU 5252  CE2 PHE D  30     2301   1556   5388   1216    103    252       C  
ATOM   5253  CZ  PHE D  30      17.211  36.701 301.310  1.00 22.77           C  
ANISOU 5253  CZ  PHE D  30     1961   1384   5307   1010    137    303       C  
ATOM   5254  N   HIS D  31      13.978  31.558 301.806  1.00 22.73           N  
ANISOU 5254  N   HIS D  31     2283   1375   4978    893   -274   -159       N  
ATOM   5255  CA  HIS D  31      14.450  30.756 302.929  1.00 22.71           C  
ANISOU 5255  CA  HIS D  31     2253   1279   5098    823   -316   -121       C  
ATOM   5256  C   HIS D  31      15.276  29.568 302.419  1.00 27.17           C  
ANISOU 5256  C   HIS D  31     3036   1410   5879   1208   -189    -88       C  
ATOM   5257  O   HIS D  31      14.795  28.878 301.520  1.00 27.24           O  
ANISOU 5257  O   HIS D  31     3253   1368   5730   1227   -128   -195       O  
ATOM   5258  CB  HIS D  31      13.278  30.272 303.797  1.00 22.36           C  
ANISOU 5258  CB  HIS D  31     2250   1212   5033    722   -474   -231       C  
ATOM   5259  CG  HIS D  31      13.595  30.269 305.255  1.00 24.55           C  
ANISOU 5259  CG  HIS D  31     2468   1303   5555    750   -570   -155       C  
ATOM   5260  ND1 HIS D  31      14.396  29.287 305.817  1.00 27.02           N  
ANISOU 5260  ND1 HIS D  31     2908   1343   6015    860   -563    -66       N  
ATOM   5261  CD2 HIS D  31      13.216  31.135 306.223  1.00 24.82           C  
ANISOU 5261  CD2 HIS D  31     2353   1396   5680    676   -675   -147       C  
ATOM   5262  CE1 HIS D  31      14.492  29.596 307.100  1.00 26.03           C  
ANISOU 5262  CE1 HIS D  31     2648   1290   5953    715   -677     -5       C  
ATOM   5263  NE2 HIS D  31      13.789  30.693 307.395  1.00 24.85           N  
ANISOU 5263  NE2 HIS D  31     2339   1317   5785    599   -739    -59       N  
ATOM   5264  N   PRO D  32      16.512  29.287 302.921  1.00 26.60           N  
ANISOU 5264  N   PRO D  32     2862   1356   5889   1196   -132     39       N  
ATOM   5265  CA  PRO D  32      17.289  29.969 303.990  1.00 26.41           C  
ANISOU 5265  CA  PRO D  32     2604   1397   6034   1139   -192    163       C  
ATOM   5266  C   PRO D  32      17.811  31.379 303.644  1.00 29.84           C  
ANISOU 5266  C   PRO D  32     2873   1734   6731   1414   -131    255       C  
ATOM   5267  O   PRO D  32      17.517  31.923 302.582  1.00 28.30           O  
ANISOU 5267  O   PRO D  32     2729   1639   6384   1391    -32    207       O  
ATOM   5268  CB  PRO D  32      18.471  29.013 304.216  1.00 29.20           C  
ANISOU 5268  CB  PRO D  32     2995   1523   6577   1406   -135    272       C  
ATOM   5269  CG  PRO D  32      18.631  28.299 302.921  1.00 33.32           C  
ANISOU 5269  CG  PRO D  32     3747   1729   7183   1804     37    230       C  
ATOM   5270  CD  PRO D  32      17.235  28.100 302.423  1.00 29.15           C  
ANISOU 5270  CD  PRO D  32     3385   1401   6289   1462      3     58       C  
ATOM   5271  N   SER D  33      18.611  31.951 304.566  1.00 29.64           N  
ANISOU 5271  N   SER D  33     2641   1789   6831   1318   -174    362       N  
ATOM   5272  CA  SER D  33      19.206  33.293 304.501  1.00 30.18           C  
ANISOU 5272  CA  SER D  33     2533   1918   7016   1334   -113    441       C  
ATOM   5273  C   SER D  33      20.290  33.467 303.437  1.00 37.45           C  
ANISOU 5273  C   SER D  33     3352   2655   8221   1839     73    532       C  
ATOM   5274  O   SER D  33      20.453  34.584 302.951  1.00 37.80           O  
ANISOU 5274  O   SER D  33     3350   2764   8249   1798    169    550       O  
ATOM   5275  CB  SER D  33      19.808  33.668 305.852  1.00 32.18           C  
ANISOU 5275  CB  SER D  33     2565   2135   7527   1383   -243    557       C  
ATOM   5276  OG  SER D  33      20.806  32.746 306.261  1.00 41.30           O  
ANISOU 5276  OG  SER D  33     3596   3190   8907   1670   -274    677       O  
ATOM   5277  N   ASP D  34      21.064  32.405 303.123  1.00 38.06           N  
ANISOU 5277  N   ASP D  34     3434   2663   8364   2032    161    559       N  
ATOM   5278  CA  ASP D  34      22.178  32.459 302.168  1.00 40.79           C  
ANISOU 5278  CA  ASP D  34     3681   3045   8774   2210    388    598       C  
ATOM   5279  C   ASP D  34      21.720  32.827 300.776  1.00 44.38           C  
ANISOU 5279  C   ASP D  34     4330   3468   9065   2232    547    511       C  
ATOM   5280  O   ASP D  34      21.011  32.066 300.113  1.00 44.25           O  
ANISOU 5280  O   ASP D  34     4569   3344   8902   2282    559    407       O  
ATOM   5281  CB  ASP D  34      22.979  31.149 302.145  1.00 45.88           C  
ANISOU 5281  CB  ASP D  34     4318   3606   9508   2463    452    628       C  
ATOM   5282  CG  ASP D  34      23.822  30.961 303.377  1.00 65.88           C  
ANISOU 5282  CG  ASP D  34     6585   6233  12214   2499    321    758       C  
ATOM   5283  OD1 ASP D  34      24.060  31.968 304.091  1.00 67.33           O  
ANISOU 5283  OD1 ASP D  34     6538   6586  12460   2307    233    822       O  
ATOM   5284  OD2 ASP D  34      24.321  29.827 303.586  1.00 77.91           O  
ANISOU 5284  OD2 ASP D  34     8137   7665  13800   2733    317    799       O  
ATOM   5285  N   ILE D  35      22.127  34.030 300.354  1.00 40.83           N  
ANISOU 5285  N   ILE D  35     3780   3118   8617   2165    665    557       N  
ATOM   5286  CA  ILE D  35      21.786  34.609 299.064  1.00 40.77           C  
ANISOU 5286  CA  ILE D  35     3960   3093   8438   2175    813    510       C  
ATOM   5287  C   ILE D  35      22.993  35.406 298.524  1.00 46.31           C  
ANISOU 5287  C   ILE D  35     4510   3887   9200   2163   1042    585       C  
ATOM   5288  O   ILE D  35      23.743  36.002 299.303  1.00 45.98           O  
ANISOU 5288  O   ILE D  35     4224   3950   9297   2044   1030    666       O  
ATOM   5289  CB  ILE D  35      20.470  35.455 299.189  1.00 41.97           C  
ANISOU 5289  CB  ILE D  35     4264   3242   8440   2044    658    474       C  
ATOM   5290  CG1 ILE D  35      19.878  35.839 297.822  1.00 43.14           C  
ANISOU 5290  CG1 ILE D  35     4659   3373   8361   2103    757    426       C  
ATOM   5291  CG2 ILE D  35      20.633  36.677 300.113  1.00 41.83           C  
ANISOU 5291  CG2 ILE D  35     4103   3279   8510   1877    589    552       C  
ATOM   5292  CD1 ILE D  35      19.379  34.666 297.049  1.00 54.74           C  
ANISOU 5292  CD1 ILE D  35     6312   4795   9691   2203    775    314       C  
ATOM   5293  N   GLU D  36      23.203  35.354 297.195  1.00 44.78           N  
ANISOU 5293  N   GLU D  36     4462   3669   8884   2258   1260    548       N  
ATOM   5294  CA  GLU D  36      24.288  36.059 296.508  1.00 47.08           C  
ANISOU 5294  CA  GLU D  36     4650   4051   9188   2219   1519    599       C  
ATOM   5295  C   GLU D  36      23.676  36.957 295.436  1.00 50.28           C  
ANISOU 5295  C   GLU D  36     5356   4393   9355   2152   1608    592       C  
ATOM   5296  O   GLU D  36      23.194  36.463 294.413  1.00 50.65           O  
ANISOU 5296  O   GLU D  36     5642   4378   9227   2264   1676    522       O  
ATOM   5297  CB  GLU D  36      25.312  35.070 295.915  1.00 51.32           C  
ANISOU 5297  CB  GLU D  36     5069   4633   9798   2419   1738    564       C  
ATOM   5298  CG  GLU D  36      26.630  35.709 295.502  1.00 66.24           C  
ANISOU 5298  CG  GLU D  36     6716   6697  11754   2354   2000    613       C  
ATOM   5299  CD  GLU D  36      27.611  34.769 294.827  1.00 91.69           C  
ANISOU 5299  CD  GLU D  36     9811   9992  15036   2586   2248    561       C  
ATOM   5300  OE1 GLU D  36      27.367  34.398 293.656  1.00 94.88           O  
ANISOU 5300  OE1 GLU D  36    10477  10301  15271   2678   2427    480       O  
ATOM   5301  OE2 GLU D  36      28.637  34.421 295.457  1.00 82.94           O  
ANISOU 5301  OE2 GLU D  36     8335   9049  14130   2687   2268    598       O  
ATOM   5302  N   VAL D  37      23.650  38.276 295.707  1.00 45.03           N  
ANISOU 5302  N   VAL D  37     4713   3733   8664   1969   1595    667       N  
ATOM   5303  CA  VAL D  37      23.059  39.273 294.821  1.00 44.18           C  
ANISOU 5303  CA  VAL D  37     4925   3539   8323   1925   1656    695       C  
ATOM   5304  C   VAL D  37      24.142  40.206 294.293  1.00 50.13           C  
ANISOU 5304  C   VAL D  37     5670   4324   9052   1766   1935    765       C  
ATOM   5305  O   VAL D  37      24.881  40.810 295.077  1.00 50.07           O  
ANISOU 5305  O   VAL D  37     5454   4385   9186   1576   1970    816       O  
ATOM   5306  CB  VAL D  37      21.926  40.061 295.519  1.00 45.64           C  
ANISOU 5306  CB  VAL D  37     5238   3650   8453   1872   1421    718       C  
ATOM   5307  CG1 VAL D  37      21.128  40.892 294.516  1.00 46.23           C  
ANISOU 5307  CG1 VAL D  37     5677   3631   8259   1926   1447    751       C  
ATOM   5308  CG2 VAL D  37      21.004  39.134 296.299  1.00 43.14           C  
ANISOU 5308  CG2 VAL D  37     4849   3353   8191   1958   1158    638       C  
ATOM   5309  N   ASP D  38      24.228  40.316 292.958  1.00 48.60           N  
ANISOU 5309  N   ASP D  38     5718   4094   8655   1812   2138    761       N  
ATOM   5310  CA  ASP D  38      25.174  41.182 292.256  1.00 51.26           C  
ANISOU 5310  CA  ASP D  38     6115   4452   8909   1636   2439    819       C  
ATOM   5311  C   ASP D  38      24.439  42.011 291.204  1.00 55.73           C  
ANISOU 5311  C   ASP D  38     7149   4864   9162   1643   2489    874       C  
ATOM   5312  O   ASP D  38      23.871  41.445 290.270  1.00 54.86           O  
ANISOU 5312  O   ASP D  38     7240   4734   8871   1808   2497    828       O  
ATOM   5313  CB  ASP D  38      26.306  40.370 291.580  1.00 55.89           C  
ANISOU 5313  CB  ASP D  38     6492   5189   9555   1689   2710    756       C  
ATOM   5314  CG  ASP D  38      26.948  39.263 292.396  1.00 70.22           C  
ANISOU 5314  CG  ASP D  38     7875   7155  11649   1800   2654    705       C  
ATOM   5315  OD1 ASP D  38      27.707  39.584 293.337  1.00 72.26           O  
ANISOU 5315  OD1 ASP D  38     7814   7549  12091   1646   2639    748       O  
ATOM   5316  OD2 ASP D  38      26.776  38.076 292.026  1.00 76.02           O  
ANISOU 5316  OD2 ASP D  38     8609   7877  12400   2037   2643    622       O  
ATOM   5317  N   LEU D  39      24.433  43.346 291.352  1.00 54.01           N  
ANISOU 5317  N   LEU D  39     7135   4527   8860   1466   2520    973       N  
ATOM   5318  CA  LEU D  39      23.823  44.221 290.350  1.00 55.66           C  
ANISOU 5318  CA  LEU D  39     7828   4565   8754   1495   2575   1056       C  
ATOM   5319  C   LEU D  39      24.809  44.350 289.206  1.00 64.26           C  
ANISOU 5319  C   LEU D  39     9031   5688   9699   1359   2931   1072       C  
ATOM   5320  O   LEU D  39      26.010  44.473 289.455  1.00 65.41           O  
ANISOU 5320  O   LEU D  39     8933   5942   9979   1124   3156   1062       O  
ATOM   5321  CB  LEU D  39      23.429  45.597 290.914  1.00 55.79           C  
ANISOU 5321  CB  LEU D  39     8094   4388   8714   1384   2505   1161       C  
ATOM   5322  CG  LEU D  39      22.364  45.626 292.013  1.00 57.71           C  
ANISOU 5322  CG  LEU D  39     8269   4593   9066   1521   2175   1141       C  
ATOM   5323  CD1 LEU D  39      22.238  47.012 292.613  1.00 58.58           C  
ANISOU 5323  CD1 LEU D  39     8618   4496   9142   1381   2180   1227       C  
ATOM   5324  CD2 LEU D  39      21.027  45.171 291.483  1.00 59.47           C  
ANISOU 5324  CD2 LEU D  39     8657   4824   9115   1834   1947   1117       C  
ATOM   5325  N   LEU D  40      24.321  44.255 287.962  1.00 62.99           N  
ANISOU 5325  N   LEU D  40     9208   5473   9253   1496   2982   1085       N  
ATOM   5326  CA  LEU D  40      25.186  44.284 286.789  1.00 66.21           C  
ANISOU 5326  CA  LEU D  40     9753   5919   9487   1373   3331   1085       C  
ATOM   5327  C   LEU D  40      24.895  45.483 285.849  1.00 71.22           C  
ANISOU 5327  C   LEU D  40    10950   6350   9762   1294   3438   1228       C  
ATOM   5328  O   LEU D  40      23.756  45.945 285.755  1.00 70.25           O  
ANISOU 5328  O   LEU D  40    11142   6079   9473   1470   3198   1311       O  
ATOM   5329  CB  LEU D  40      25.101  42.933 286.028  1.00 66.73           C  
ANISOU 5329  CB  LEU D  40     9738   6112   9506   1572   3365    958       C  
ATOM   5330  CG  LEU D  40      23.771  42.456 285.421  1.00 71.31           C  
ANISOU 5330  CG  LEU D  40    10594   6647   9854   1822   3121    934       C  
ATOM   5331  CD1 LEU D  40      23.513  43.106 284.081  1.00 74.66           C  
ANISOU 5331  CD1 LEU D  40    11510   6983   9876   1807   3246   1022       C  
ATOM   5332  CD2 LEU D  40      23.719  40.954 285.307  1.00 72.28           C  
ANISOU 5332  CD2 LEU D  40    10505   6891  10068   1977   3093    769       C  
ATOM   5333  N   LYS D  41      25.950  45.964 285.158  1.00 69.54           N  
ANISOU 5333  N   LYS D  41    10855   6146   9423   1035   3808   1255       N  
ATOM   5334  CA  LYS D  41      25.923  47.049 284.175  1.00 71.61           C  
ANISOU 5334  CA  LYS D  41    11681   6207   9319    904   3988   1394       C  
ATOM   5335  C   LYS D  41      26.489  46.515 282.852  1.00 77.29           C  
ANISOU 5335  C   LYS D  41    12501   7041   9824    856   4289   1338       C  
ATOM   5336  O   LYS D  41      27.711  46.448 282.684  1.00 79.21           O  
ANISOU 5336  O   LYS D  41    12528   7428  10140    593   4633   1274       O  
ATOM   5337  CB  LYS D  41      26.713  48.267 284.681  1.00 75.52           C  
ANISOU 5337  CB  LYS D  41    12269   6578   9848    530   4189   1477       C  
ATOM   5338  N   ASN D  42      25.582  46.084 281.939  1.00 72.77           N  
ANISOU 5338  N   ASN D  42    12224   6442   8985   1111   4154   1345       N  
ATOM   5339  CA  ASN D  42      25.857  45.484 280.619  1.00 74.28           C  
ANISOU 5339  CA  ASN D  42    12576   6728   8919   1113   4388   1280       C  
ATOM   5340  C   ASN D  42      26.567  44.123 280.763  1.00 76.80           C  
ANISOU 5340  C   ASN D  42    12380   7294   9505   1150   4533   1069       C  
ATOM   5341  O   ASN D  42      27.402  43.762 279.930  1.00 79.30           O  
ANISOU 5341  O   ASN D  42    12685   7722   9722   1029   4886    988       O  
ATOM   5342  CB  ASN D  42      26.659  46.431 279.697  1.00 76.99           C  
ANISOU 5342  CB  ASN D  42    13319   6972   8962    803   4770   1383       C  
ATOM   5343  CG  ASN D  42      25.843  47.515 279.040  1.00 90.78           C  
ANISOU 5343  CG  ASN D  42    15727   8449  10317    851   4652   1596       C  
ATOM   5344  OD1 ASN D  42      24.880  47.259 278.309  1.00 82.11           O  
ANISOU 5344  OD1 ASN D  42    14926   7329   8942   1107   4444   1639       O  
ATOM   5345  ND2 ASN D  42      26.250  48.755 279.241  1.00 82.80           N  
ANISOU 5345  ND2 ASN D  42    14983   7232   9247    594   4798   1734       N  
ATOM   5346  N   GLY D  43      26.204  43.377 281.805  1.00 69.51           N  
ANISOU 5346  N   GLY D  43    11064   6444   8902   1334   4265    984       N  
ATOM   5347  CA  GLY D  43      26.771  42.062 282.077  1.00 68.65           C  
ANISOU 5347  CA  GLY D  43    10504   6521   9058   1436   4352    804       C  
ATOM   5348  C   GLY D  43      27.767  42.028 283.217  1.00 71.86           C  
ANISOU 5348  C   GLY D  43    10390   7055   9858   1329   4412    775       C  
ATOM   5349  O   GLY D  43      27.731  41.103 284.032  1.00 69.32           O  
ANISOU 5349  O   GLY D  43     9716   6806   9815   1504   4229    693       O  
ATOM   5350  N   GLU D  44      28.683  43.016 283.271  1.00 70.63           N  
ANISOU 5350  N   GLU D  44    10192   6940   9703   1020   4673    841       N  
ATOM   5351  CA  GLU D  44      29.711  43.116 284.316  1.00 70.29           C  
ANISOU 5351  CA  GLU D  44     9640   7076   9991    855   4745    816       C  
ATOM   5352  C   GLU D  44      29.093  43.649 285.608  1.00 69.86           C  
ANISOU 5352  C   GLU D  44     9537   6904  10104    842   4396    904       C  
ATOM   5353  O   GLU D  44      28.328  44.612 285.558  1.00 68.70           O  
ANISOU 5353  O   GLU D  44     9812   6527   9766    786   4267   1025       O  
ATOM   5354  CB  GLU D  44      30.874  44.011 283.856  1.00 75.72           C  
ANISOU 5354  CB  GLU D  44    10324   7873  10574    462   5152    841       C  
ATOM   5355  N   ARG D  45      29.418  43.020 286.759  1.00 64.07           N  
ANISOU 5355  N   ARG D  45     8304   6326   9714    914   4246    846       N  
ATOM   5356  CA  ARG D  45      28.859  43.395 288.067  1.00 60.54           C  
ANISOU 5356  CA  ARG D  45     7763   5798   9442    899   3921    905       C  
ATOM   5357  C   ARG D  45      29.416  44.727 288.590  1.00 63.91           C  
ANISOU 5357  C   ARG D  45     8222   6199   9862    509   4030    990       C  
ATOM   5358  O   ARG D  45      30.615  44.987 288.490  1.00 66.34           O  
ANISOU 5358  O   ARG D  45     8314   6698  10192    233   4331    964       O  
ATOM   5359  CB  ARG D  45      29.043  42.282 289.126  1.00 59.39           C  
ANISOU 5359  CB  ARG D  45     7107   5825   9633   1084   3731    825       C  
ATOM   5360  CG  ARG D  45      30.488  41.871 289.428  1.00 74.44           C  
ANISOU 5360  CG  ARG D  45     8488   8047  11749    999   3964    759       C  
ATOM   5361  CD  ARG D  45      30.626  41.285 290.823  1.00 84.87           C  
ANISOU 5361  CD  ARG D  45     9352   9508  13385   1106   3716    744       C  
ATOM   5362  NE  ARG D  45      30.993  42.296 291.818  1.00 96.73           N  
ANISOU 5362  NE  ARG D  45    10692  11083  14979    781   3647    810       N  
ATOM   5363  CZ  ARG D  45      30.155  42.827 292.706  1.00113.02           C  
ANISOU 5363  CZ  ARG D  45    12898  12975  17070    726   3358    868       C  
ATOM   5364  NH1 ARG D  45      28.881  42.449 292.737  1.00 99.37           N  
ANISOU 5364  NH1 ARG D  45    11440  11025  15292    978   3101    871       N  
ATOM   5365  NH2 ARG D  45      30.584  43.736 293.571  1.00102.12           N  
ANISOU 5365  NH2 ARG D  45    11384  11661  15754    400   3334    909       N  
ATOM   5366  N   ILE D  46      28.522  45.556 289.155  1.00 57.57           N  
ANISOU 5366  N   ILE D  46     7689   5166   9019    482   3792   1078       N  
ATOM   5367  CA  ILE D  46      28.825  46.864 289.740  1.00 58.29           C  
ANISOU 5367  CA  ILE D  46     7914   5151   9083    122   3860   1154       C  
ATOM   5368  C   ILE D  46      29.515  46.626 291.093  1.00 62.25           C  
ANISOU 5368  C   ILE D  46     7864   5888   9901    -29   3768   1096       C  
ATOM   5369  O   ILE D  46      28.939  45.989 291.977  1.00 59.12           O  
ANISOU 5369  O   ILE D  46     7256   5513   9694    190   3463   1069       O  
ATOM   5370  CB  ILE D  46      27.535  47.733 289.852  1.00 59.66           C  
ANISOU 5370  CB  ILE D  46     8616   4970   9083    226   3643   1260       C  
ATOM   5371  CG1 ILE D  46      26.827  47.867 288.483  1.00 60.81           C  
ANISOU 5371  CG1 ILE D  46     9280   4932   8895    427   3691   1330       C  
ATOM   5372  CG2 ILE D  46      27.832  49.114 290.460  1.00 62.12           C  
ANISOU 5372  CG2 ILE D  46     9146   5110   9348   -150   3743   1330       C  
ATOM   5373  CD1 ILE D  46      25.309  47.944 288.543  1.00 64.22           C  
ANISOU 5373  CD1 ILE D  46    10002   5175   9225    783   3348   1383       C  
ATOM   5374  N   GLU D  47      30.759  47.115 291.227  1.00 62.61           N  
ANISOU 5374  N   GLU D  47     7673   6135   9980   -422   4034   1076       N  
ATOM   5375  CA  GLU D  47      31.617  46.946 292.402  1.00 62.98           C  
ANISOU 5375  CA  GLU D  47     7158   6482  10288   -617   3977   1023       C  
ATOM   5376  C   GLU D  47      31.070  47.651 293.657  1.00 65.33           C  
ANISOU 5376  C   GLU D  47     7563   6610  10648   -760   3726   1064       C  
ATOM   5377  O   GLU D  47      30.896  46.994 294.688  1.00 62.09           O  
ANISOU 5377  O   GLU D  47     6810   6320  10461   -611   3453   1035       O  
ATOM   5378  CB  GLU D  47      33.041  47.443 292.095  1.00 68.87           C  
ANISOU 5378  CB  GLU D  47     7657   7517  10992  -1057   4349    984       C  
ATOM   5379  N   LYS D  48      30.814  48.977 293.567  1.00 64.02           N  
ANISOU 5379  N   LYS D  48     7906   6148  10271  -1043   3831   1131       N  
ATOM   5380  CA  LYS D  48      30.322  49.809 294.671  1.00 63.03           C  
ANISOU 5380  CA  LYS D  48     7969   5814  10165  -1207   3654   1158       C  
ATOM   5381  C   LYS D  48      28.800  49.662 294.862  1.00 63.89           C  
ANISOU 5381  C   LYS D  48     8386   5630  10259   -777   3338   1198       C  
ATOM   5382  O   LYS D  48      28.035  50.568 294.515  1.00 64.34           O  
ANISOU 5382  O   LYS D  48     9011   5329  10107   -729   3348   1274       O  
ATOM   5383  CB  LYS D  48      30.693  51.289 294.445  1.00 69.04           C  
ANISOU 5383  CB  LYS D  48     9206   6340  10688  -1678   3928   1207       C  
ATOM   5384  CG  LYS D  48      32.097  51.679 294.883  1.00 84.62           C  
ANISOU 5384  CG  LYS D  48    10809   8636  12709  -2238   4161   1139       C  
ATOM   5385  CD  LYS D  48      32.322  53.173 294.653  1.00 97.14           C  
ANISOU 5385  CD  LYS D  48    12955   9928  14027  -2745   4438   1179       C  
ATOM   5386  CE  LYS D  48      33.724  53.616 294.985  1.00110.99           C  
ANISOU 5386  CE  LYS D  48    14335  12043  15792  -3372   4686   1093       C  
ATOM   5387  NZ  LYS D  48      33.919  55.066 294.723  1.00122.17           N  
ANISOU 5387  NZ  LYS D  48    16365  13138  16918  -3919   4984   1123       N  
ATOM   5388  N   VAL D  49      28.368  48.517 295.416  1.00 57.09           N  
ANISOU 5388  N   VAL D  49     7148   4935   9610   -462   3063   1147       N  
ATOM   5389  CA  VAL D  49      26.954  48.244 295.701  1.00 53.37           C  
ANISOU 5389  CA  VAL D  49     6856   4277   9144    -88   2755   1155       C  
ATOM   5390  C   VAL D  49      26.765  48.092 297.212  1.00 54.03           C  
ANISOU 5390  C   VAL D  49     6659   4436   9434   -149   2505   1111       C  
ATOM   5391  O   VAL D  49      27.494  47.335 297.865  1.00 53.59           O  
ANISOU 5391  O   VAL D  49     6112   4672   9579   -234   2456   1065       O  
ATOM   5392  CB  VAL D  49      26.333  47.041 294.925  1.00 55.60           C  
ANISOU 5392  CB  VAL D  49     7066   4631   9428    331   2647   1127       C  
ATOM   5393  CG1 VAL D  49      26.030  47.409 293.481  1.00 56.91           C  
ANISOU 5393  CG1 VAL D  49     7681   4626   9315    447   2810   1184       C  
ATOM   5394  CG2 VAL D  49      27.206  45.788 294.995  1.00 55.79           C  
ANISOU 5394  CG2 VAL D  49     6563   4981   9652    374   2690   1058       C  
ATOM   5395  N   GLU D  50      25.800  48.837 297.762  1.00 47.78           N  
ANISOU 5395  N   GLU D  50     6190   3387   8576    -92   2354   1128       N  
ATOM   5396  CA  GLU D  50      25.461  48.778 299.179  1.00 44.73           C  
ANISOU 5396  CA  GLU D  50     5615   3036   8345   -147   2122   1079       C  
ATOM   5397  C   GLU D  50      24.200  47.956 299.361  1.00 44.01           C  
ANISOU 5397  C   GLU D  50     5499   2925   8296    254   1838   1046       C  
ATOM   5398  O   GLU D  50      23.471  47.721 298.394  1.00 42.70           O  
ANISOU 5398  O   GLU D  50     5558   2667   7998    550   1819   1067       O  
ATOM   5399  CB  GLU D  50      25.274  50.184 299.749  1.00 47.43           C  
ANISOU 5399  CB  GLU D  50     6334   3109   8577   -410   2190   1095       C  
ATOM   5400  CG  GLU D  50      26.572  50.909 300.034  1.00 62.55           C  
ANISOU 5400  CG  GLU D  50     8178   5106  10483   -929   2427   1089       C  
ATOM   5401  CD  GLU D  50      26.393  52.400 300.230  1.00 93.65           C  
ANISOU 5401  CD  GLU D  50    12635   8695  14251  -1204   2563   1106       C  
ATOM   5402  OE1 GLU D  50      25.706  52.795 301.201  1.00 93.37           O  
ANISOU 5402  OE1 GLU D  50    12692   8529  14253  -1198   2404   1063       O  
ATOM   5403  OE2 GLU D  50      26.931  53.175 299.406  1.00 93.37           O  
ANISOU 5403  OE2 GLU D  50    12945   8500  14032  -1433   2846   1157       O  
ATOM   5404  N   HIS D  51      23.952  47.496 300.586  1.00 38.72           N  
ANISOU 5404  N   HIS D  51     4553   2368   7790    239   1617    991       N  
ATOM   5405  CA  HIS D  51      22.751  46.736 300.896  1.00 36.25           C  
ANISOU 5405  CA  HIS D  51     4200   2060   7511    548   1356    942       C  
ATOM   5406  C   HIS D  51      22.339  46.948 302.335  1.00 38.95           C  
ANISOU 5406  C   HIS D  51     4453   2401   7946    426   1176    891       C  
ATOM   5407  O   HIS D  51      23.185  47.176 303.202  1.00 39.08           O  
ANISOU 5407  O   HIS D  51     4272   2517   8060    119   1200    886       O  
ATOM   5408  CB  HIS D  51      22.935  45.243 300.610  1.00 36.31           C  
ANISOU 5408  CB  HIS D  51     3886   2280   7628    735   1276    915       C  
ATOM   5409  CG  HIS D  51      23.897  44.561 301.527  1.00 40.21           C  
ANISOU 5409  CG  HIS D  51     3950   3002   8325    577   1222    904       C  
ATOM   5410  ND1 HIS D  51      23.462  43.886 302.655  1.00 40.24           N  
ANISOU 5410  ND1 HIS D  51     3761   3083   8444    612    978    865       N  
ATOM   5411  CD2 HIS D  51      25.246  44.475 301.456  1.00 44.40           C  
ANISOU 5411  CD2 HIS D  51     4210   3718   8940    396   1378    933       C  
ATOM   5412  CE1 HIS D  51      24.552  43.400 303.223  1.00 40.83           C  
ANISOU 5412  CE1 HIS D  51     3477   3370   8666    479    975    888       C  
ATOM   5413  NE2 HIS D  51      25.651  43.728 302.536  1.00 43.72           N  
ANISOU 5413  NE2 HIS D  51     3755   3831   9025    356   1207    924       N  
ATOM   5414  N   SER D  52      21.033  46.826 302.588  1.00 34.51           N  
ANISOU 5414  N   SER D  52     4011   1764   7339    659    993    843       N  
ATOM   5415  CA  SER D  52      20.413  46.942 303.908  1.00 33.21           C  
ANISOU 5415  CA  SER D  52     3780   1602   7237    585    820    774       C  
ATOM   5416  C   SER D  52      20.781  45.749 304.803  1.00 34.19           C  
ANISOU 5416  C   SER D  52     3497   1962   7533    518    652    741       C  
ATOM   5417  O   SER D  52      21.452  44.815 304.356  1.00 33.29           O  
ANISOU 5417  O   SER D  52     3169   1990   7490    583    667    770       O  
ATOM   5418  CB  SER D  52      18.899  46.998 303.748  1.00 37.09           C  
ANISOU 5418  CB  SER D  52     4473   2003   7617    888    691    722       C  
ATOM   5419  OG  SER D  52      18.412  45.745 303.287  1.00 48.35           O  
ANISOU 5419  OG  SER D  52     5742   3582   9045   1119    560    690       O  
ATOM   5420  N   ASP D  53      20.322  45.773 306.057  1.00 29.40           N  
ANISOU 5420  N   ASP D  53     2812   1384   6976    404    499    681       N  
ATOM   5421  CA  ASP D  53      20.531  44.652 306.963  1.00 28.01           C  
ANISOU 5421  CA  ASP D  53     2314   1401   6927    353    317    662       C  
ATOM   5422  C   ASP D  53      19.545  43.547 306.587  1.00 28.37           C  
ANISOU 5422  C   ASP D  53     2350   1482   6947    637    182    615       C  
ATOM   5423  O   ASP D  53      18.356  43.835 306.380  1.00 27.91           O  
ANISOU 5423  O   ASP D  53     2446   1461   6699    692    147    534       O  
ATOM   5424  CB  ASP D  53      20.354  45.076 308.437  1.00 30.13           C  
ANISOU 5424  CB  ASP D  53     2543   1685   7221    107    207    610       C  
ATOM   5425  CG  ASP D  53      21.557  45.760 309.061  1.00 46.18           C  
ANISOU 5425  CG  ASP D  53     4488   3769   9290   -255    296    647       C  
ATOM   5426  OD1 ASP D  53      22.702  45.312 308.801  1.00 48.19           O  
ANISOU 5426  OD1 ASP D  53     4490   4195   9626   -334    339    717       O  
ATOM   5427  OD2 ASP D  53      21.353  46.710 309.855  1.00 54.62           O  
ANISOU 5427  OD2 ASP D  53     5722   4730  10300   -467    320    592       O  
ATOM   5428  N   LEU D  54      20.040  42.298 306.455  1.00 24.23           N  
ANISOU 5428  N   LEU D  54     1597   1305   6304    429    153    601       N  
ATOM   5429  CA  LEU D  54      19.190  41.154 306.115  1.00 23.31           C  
ANISOU 5429  CA  LEU D  54     1531   1326   6001    414     63    521       C  
ATOM   5430  C   LEU D  54      18.112  41.008 307.215  1.00 23.83           C  
ANISOU 5430  C   LEU D  54     1601   1380   6074    396   -122    433       C  
ATOM   5431  O   LEU D  54      18.442  41.000 308.404  1.00 23.66           O  
ANISOU 5431  O   LEU D  54     1471   1379   6141    214   -207    440       O  
ATOM   5432  CB  LEU D  54      20.062  39.884 305.938  1.00 23.64           C  
ANISOU 5432  CB  LEU D  54     1464   1380   6139    457     66    574       C  
ATOM   5433  CG  LEU D  54      19.428  38.507 305.627  1.00 25.67           C  
ANISOU 5433  CG  LEU D  54     1749   1574   6429    736    -33    532       C  
ATOM   5434  CD1 LEU D  54      18.694  38.531 304.323  1.00 25.75           C  
ANISOU 5434  CD1 LEU D  54     1936   1583   6264    874     43    477       C  
ATOM   5435  CD2 LEU D  54      20.387  37.328 305.803  1.00 27.20           C  
ANISOU 5435  CD2 LEU D  54     1789   1732   6813    908    -53    606       C  
ATOM   5436  N   SER D  55      16.829  41.034 306.808  1.00 19.74           N  
ANISOU 5436  N   SER D  55     1219   1146   5134    122   -132    292       N  
ATOM   5437  CA  SER D  55      15.686  40.971 307.714  1.00 18.08           C  
ANISOU 5437  CA  SER D  55     1043   1032   4794    -12   -263    170       C  
ATOM   5438  C   SER D  55      14.644  39.946 307.240  1.00 20.65           C  
ANISOU 5438  C   SER D  55     1430   1288   5128    231   -367    100       C  
ATOM   5439  O   SER D  55      14.730  39.462 306.114  1.00 20.92           O  
ANISOU 5439  O   SER D  55     1523   1342   5082    335   -313    118       O  
ATOM   5440  CB  SER D  55      15.056  42.352 307.824  1.00 19.12           C  
ANISOU 5440  CB  SER D  55     1233   1060   4972    190   -245    160       C  
ATOM   5441  OG  SER D  55      13.919  42.349 308.666  1.00 22.58           O  
ANISOU 5441  OG  SER D  55     1688   1287   5607    522   -388     81       O  
ATOM   5442  N   PHE D  56      13.655  39.620 308.096  1.00 18.35           N  
ANISOU 5442  N   PHE D  56     1224   1165   4585      4   -451    -29       N  
ATOM   5443  CA  PHE D  56      12.610  38.656 307.753  1.00 17.94           C  
ANISOU 5443  CA  PHE D  56     1255   1176   4385     22   -522   -135       C  
ATOM   5444  C   PHE D  56      11.195  39.173 308.046  1.00 21.24           C  
ANISOU 5444  C   PHE D  56     1586   1494   4990    333   -649   -247       C  
ATOM   5445  O   PHE D  56      10.979  39.841 309.052  1.00 20.54           O  
ANISOU 5445  O   PHE D  56     1476   1393   4937    241   -664   -281       O  
ATOM   5446  CB  PHE D  56      12.836  37.313 308.466  1.00 18.10           C  
ANISOU 5446  CB  PHE D  56     1224   1124   4531     23   -599   -133       C  
ATOM   5447  CG  PHE D  56      12.958  37.337 309.971  1.00 17.77           C  
ANISOU 5447  CG  PHE D  56     1116    995   4639     21   -674   -112       C  
ATOM   5448  CD1 PHE D  56      14.202  37.420 310.580  1.00 20.03           C  
ANISOU 5448  CD1 PHE D  56     1305   1188   5116     -2   -676     10       C  
ATOM   5449  CD2 PHE D  56      11.839  37.179 310.779  1.00 19.12           C  
ANISOU 5449  CD2 PHE D  56     1327   1185   4753     43   -742   -209       C  
ATOM   5450  CE1 PHE D  56      14.318  37.410 311.973  1.00 21.07           C  
ANISOU 5450  CE1 PHE D  56     1443   1305   5258     -8   -740     42       C  
ATOM   5451  CE2 PHE D  56      11.955  37.172 312.172  1.00 22.08           C  
ANISOU 5451  CE2 PHE D  56     1719   1563   5108     36   -762   -169       C  
ATOM   5452  CZ  PHE D  56      13.194  37.268 312.759  1.00 19.85           C  
ANISOU 5452  CZ  PHE D  56     1361   1198   4985      9   -788    -43       C  
ATOM   5453  N   SER D  57      10.232  38.837 307.163  1.00 20.63           N  
ANISOU 5453  N   SER D  57     1605   1550   4683    356   -673   -348       N  
ATOM   5454  CA  SER D  57       8.814  39.189 307.299  1.00 21.38           C  
ANISOU 5454  CA  SER D  57     1670   1755   4697    529   -748   -489       C  
ATOM   5455  C   SER D  57       8.151  38.314 308.376  1.00 24.56           C  
ANISOU 5455  C   SER D  57     1857   2186   5288    610   -860   -598       C  
ATOM   5456  O   SER D  57       8.810  37.406 308.893  1.00 24.02           O  
ANISOU 5456  O   SER D  57     1863   1990   5275    377   -858   -560       O  
ATOM   5457  CB  SER D  57       8.099  39.025 305.963  1.00 25.38           C  
ANISOU 5457  CB  SER D  57     2032   2371   5241   1053   -812   -505       C  
ATOM   5458  OG  SER D  57       8.582  39.922 304.972  1.00 39.94           O  
ANISOU 5458  OG  SER D  57     3794   4041   7339   1694   -776   -341       O  
ATOM   5459  N   LYS D  58       6.859  38.579 308.721  1.00 22.52           N  
ANISOU 5459  N   LYS D  58     1596   2108   4854    586   -886   -772       N  
ATOM   5460  CA  LYS D  58       6.106  37.821 309.737  1.00 22.36           C  
ANISOU 5460  CA  LYS D  58     1549   2159   4788    431   -904   -919       C  
ATOM   5461  C   LYS D  58       6.207  36.317 309.484  1.00 25.91           C  
ANISOU 5461  C   LYS D  58     1602   2812   5432    441  -1075   -900       C  
ATOM   5462  O   LYS D  58       6.595  35.584 310.394  1.00 26.59           O  
ANISOU 5462  O   LYS D  58     1728   2799   5574    184  -1099   -880       O  
ATOM   5463  CB  LYS D  58       4.629  38.252 309.785  1.00 25.53           C  
ANISOU 5463  CB  LYS D  58     1560   3001   5140    633   -995  -1093       C  
ATOM   5464  CG  LYS D  58       3.805  37.563 310.880  1.00 45.27           C  
ANISOU 5464  CG  LYS D  58     3626   5870   7705    406  -1121  -1252       C  
ATOM   5465  CD  LYS D  58       2.351  38.041 310.952  1.00 68.16           C  
ANISOU 5465  CD  LYS D  58     6266   9188  10444    500  -1145  -1462       C  
ATOM   5466  CE  LYS D  58       1.547  37.330 312.025  1.00 90.61           C  
ANISOU 5466  CE  LYS D  58     8974  12277  13178    112  -1154  -1656       C  
ATOM   5467  NZ  LYS D  58       0.126  37.795 312.098  1.00106.51           N  
ANISOU 5467  NZ  LYS D  58    10675  14762  15034    210  -1164  -1880       N  
ATOM   5468  N   ASP D  59       5.931  35.875 308.229  1.00 23.81           N  
ANISOU 5468  N   ASP D  59     1642   2492   4913    460   -990   -946       N  
ATOM   5469  CA  ASP D  59       5.956  34.476 307.780  1.00 23.03           C  
ANISOU 5469  CA  ASP D  59     1657   2355   4738    339   -983   -976       C  
ATOM   5470  C   ASP D  59       7.350  33.807 307.901  1.00 22.10           C  
ANISOU 5470  C   ASP D  59     1740   1880   4777    268   -939   -811       C  
ATOM   5471  O   ASP D  59       7.495  32.660 307.484  1.00 21.28           O  
ANISOU 5471  O   ASP D  59     1631   1764   4691    244   -976   -811       O  
ATOM   5472  CB  ASP D  59       5.447  34.381 306.322  1.00 25.41           C  
ANISOU 5472  CB  ASP D  59     1677   2986   4992    530  -1113  -1030       C  
ATOM   5473  CG  ASP D  59       6.406  34.843 305.230  1.00 41.81           C  
ANISOU 5473  CG  ASP D  59     3879   4858   7148    827  -1041   -864       C  
ATOM   5474  OD1 ASP D  59       7.212  35.777 305.490  1.00 42.15           O  
ANISOU 5474  OD1 ASP D  59     3924   4733   7357   1003   -990   -722       O  
ATOM   5475  OD2 ASP D  59       6.313  34.312 304.096  1.00 50.94           O  
ANISOU 5475  OD2 ASP D  59     5143   6033   8178    858  -1025   -889       O  
ATOM   5476  N   TRP D  60       8.352  34.525 308.465  1.00 18.51           N  
ANISOU 5476  N   TRP D  60     1492   1402   4139    159   -774   -586       N  
ATOM   5477  CA  TRP D  60       9.752  34.130 308.705  1.00 17.13           C  
ANISOU 5477  CA  TRP D  60     1283   1147   4078    109   -766   -424       C  
ATOM   5478  C   TRP D  60      10.611  34.136 307.429  1.00 19.84           C  
ANISOU 5478  C   TRP D  60     1605   1473   4458     92   -737   -378       C  
ATOM   5479  O   TRP D  60      11.799  33.819 307.526  1.00 19.70           O  
ANISOU 5479  O   TRP D  60     1488   1347   4652     63   -741   -283       O  
ATOM   5480  CB  TRP D  60       9.880  32.756 309.400  1.00 15.88           C  
ANISOU 5480  CB  TRP D  60     1141    975   3917    101   -800   -376       C  
ATOM   5481  CG  TRP D  60       9.167  32.668 310.711  1.00 16.96           C  
ANISOU 5481  CG  TRP D  60     1313   1144   3987    108   -801   -389       C  
ATOM   5482  CD1 TRP D  60       7.930  32.151 310.935  1.00 20.51           C  
ANISOU 5482  CD1 TRP D  60     1816   1687   4290    136   -760   -481       C  
ATOM   5483  CD2 TRP D  60       9.628  33.166 311.971  1.00 16.92           C  
ANISOU 5483  CD2 TRP D  60     1299   1110   4018     84   -807   -307       C  
ATOM   5484  NE1 TRP D  60       7.596  32.277 312.260  1.00 19.55           N  
ANISOU 5484  NE1 TRP D  60     1687   1557   4184    134   -762   -477       N  
ATOM   5485  CE2 TRP D  60       8.621  32.894 312.922  1.00 20.51           C  
ANISOU 5485  CE2 TRP D  60     1779   1598   4417    103   -809   -365       C  
ATOM   5486  CE3 TRP D  60      10.807  33.803 312.397  1.00 17.34           C  
ANISOU 5486  CE3 TRP D  60     1261   1048   4280     56   -859   -213       C  
ATOM   5487  CZ2 TRP D  60       8.752  33.235 314.271  1.00 20.26           C  
ANISOU 5487  CZ2 TRP D  60     1761   1560   4378     87   -815   -304       C  
ATOM   5488  CZ3 TRP D  60      10.933  34.146 313.733  1.00 19.16           C  
ANISOU 5488  CZ3 TRP D  60     1500   1268   4510     43   -882   -157       C  
ATOM   5489  CH2 TRP D  60       9.913  33.867 314.653  1.00 20.77           C  
ANISOU 5489  CH2 TRP D  60     1795   1568   4529     56   -846   -196       C  
ATOM   5490  N   SER D  61      10.045  34.477 306.247  1.00 16.11           N  
ANISOU 5490  N   SER D  61     1290   1190   3641    102   -641   -402       N  
ATOM   5491  CA  SER D  61      10.850  34.505 305.025  1.00 15.88           C  
ANISOU 5491  CA  SER D  61     1301   1214   3518     80   -561   -334       C  
ATOM   5492  C   SER D  61      11.715  35.775 305.017  1.00 16.70           C  
ANISOU 5492  C   SER D  61     1238   1139   3969    106   -574   -278       C  
ATOM   5493  O   SER D  61      11.313  36.777 305.602  1.00 16.95           O  
ANISOU 5493  O   SER D  61     1262   1165   4015    117   -596   -297       O  
ATOM   5494  CB  SER D  61       9.979  34.396 303.781  1.00 16.13           C  
ANISOU 5494  CB  SER D  61     1298   1202   3628    188   -687   -493       C  
ATOM   5495  OG  SER D  61       9.183  35.548 303.589  1.00 22.71           O  
ANISOU 5495  OG  SER D  61     1887   1934   4808    963   -771   -495       O  
ATOM   5496  N   PHE D  62      12.910  35.721 304.399  1.00 14.41           N  
ANISOU 5496  N   PHE D  62     1039    983   3451     24   -400   -148       N  
ATOM   5497  CA  PHE D  62      13.870  36.827 304.383  1.00 14.07           C  
ANISOU 5497  CA  PHE D  62      964    929   3452      5   -298    -46       C  
ATOM   5498  C   PHE D  62      13.679  37.817 303.234  1.00 17.45           C  
ANISOU 5498  C   PHE D  62     1342   1128   4159    435   -280      7       C  
ATOM   5499  O   PHE D  62      13.121  37.452 302.197  1.00 18.57           O  
ANISOU 5499  O   PHE D  62     1576   1289   4192    615   -290    -33       O  
ATOM   5500  CB  PHE D  62      15.295  36.274 304.325  1.00 14.68           C  
ANISOU 5500  CB  PHE D  62      901    884   3792     -4   -226     52       C  
ATOM   5501  CG  PHE D  62      15.696  35.456 305.524  1.00 15.20           C  
ANISOU 5501  CG  PHE D  62      938    912   3928     -6   -287     61       C  
ATOM   5502  CD1 PHE D  62      16.071  36.071 306.711  1.00 16.21           C  
ANISOU 5502  CD1 PHE D  62      964    933   4264    -11   -337    109       C  
ATOM   5503  CD2 PHE D  62      15.696  34.074 305.469  1.00 15.64           C  
ANISOU 5503  CD2 PHE D  62      906    864   4174      4   -349     37       C  
ATOM   5504  CE1 PHE D  62      16.412  35.319 307.825  1.00 16.69           C  
ANISOU 5504  CE1 PHE D  62      979    934   4428    -16   -419    133       C  
ATOM   5505  CE2 PHE D  62      16.061  33.321 306.579  1.00 17.61           C  
ANISOU 5505  CE2 PHE D  62     1089    953   4650    119   -444     82       C  
ATOM   5506  CZ  PHE D  62      16.426  33.951 307.748  1.00 16.76           C  
ANISOU 5506  CZ  PHE D  62      992    937   4437    -15   -455    115       C  
ATOM   5507  N   TYR D  63      14.158  39.072 303.421  1.00 15.62           N  
ANISOU 5507  N   TYR D  63     1111    984   3841    234   -188     70       N  
ATOM   5508  CA  TYR D  63      14.099  40.141 302.415  1.00 16.53           C  
ANISOU 5508  CA  TYR D  63     1329   1057   3894    479   -101    136       C  
ATOM   5509  C   TYR D  63      15.328  41.058 302.497  1.00 21.59           C  
ANISOU 5509  C   TYR D  63     1922   1360   4919    818     31    295       C  
ATOM   5510  O   TYR D  63      15.805  41.365 303.593  1.00 20.99           O  
ANISOU 5510  O   TYR D  63     1729   1275   4971    640     22    309       O  
ATOM   5511  CB  TYR D  63      12.794  40.961 302.503  1.00 17.39           C  
ANISOU 5511  CB  TYR D  63     1523   1187   3896    642   -198     69       C  
ATOM   5512  CG  TYR D  63      12.579  41.750 303.780  1.00 17.14           C  
ANISOU 5512  CG  TYR D  63     1429   1123   3959    561   -237     48       C  
ATOM   5513  CD1 TYR D  63      13.071  43.045 303.912  1.00 18.81           C  
ANISOU 5513  CD1 TYR D  63     1681   1192   4272    705   -137    142       C  
ATOM   5514  CD2 TYR D  63      11.782  41.251 304.804  1.00 16.80           C  
ANISOU 5514  CD2 TYR D  63     1315   1106   3964    474   -371    -68       C  
ATOM   5515  CE1 TYR D  63      12.862  43.783 305.076  1.00 19.57           C  
ANISOU 5515  CE1 TYR D  63     1740   1215   4479    692   -165    117       C  
ATOM   5516  CE2 TYR D  63      11.552  41.985 305.967  1.00 17.35           C  
ANISOU 5516  CE2 TYR D  63     1333   1125   4134    452   -400    -94       C  
ATOM   5517  CZ  TYR D  63      12.092  43.253 306.099  1.00 23.95           C  
ANISOU 5517  CZ  TYR D  63     2176   1570   5354   1002   -326     33       C  
ATOM   5518  OH  TYR D  63      11.870  43.983 307.246  1.00 24.96           O  
ANISOU 5518  OH  TYR D  63     2283   1568   5632   1062   -342     -1       O  
ATOM   5519  N   LEU D  64      15.825  41.504 301.333  1.00 21.84           N  
ANISOU 5519  N   LEU D  64     2070   1358   4869    925    180    376       N  
ATOM   5520  CA  LEU D  64      17.012  42.353 301.235  1.00 23.37           C  
ANISOU 5520  CA  LEU D  64     2272   1357   5248    999    354    498       C  
ATOM   5521  C   LEU D  64      16.883  43.397 300.137  1.00 30.73           C  
ANISOU 5521  C   LEU D  64     3538   1787   6352   1604    454    612       C  
ATOM   5522  O   LEU D  64      16.388  43.073 299.056  1.00 32.03           O  
ANISOU 5522  O   LEU D  64     3833   1965   6374   1808    444    604       O  
ATOM   5523  CB  LEU D  64      18.235  41.469 300.928  1.00 23.50           C  
ANISOU 5523  CB  LEU D  64     2158   1354   5416    966    460    549       C  
ATOM   5524  CG  LEU D  64      19.380  41.459 301.939  1.00 26.48           C  
ANISOU 5524  CG  LEU D  64     2346   1494   6221   1066    484    626       C  
ATOM   5525  CD1 LEU D  64      20.357  40.365 301.608  1.00 26.98           C  
ANISOU 5525  CD1 LEU D  64     2250   1589   6412   1113    551    655       C  
ATOM   5526  CD2 LEU D  64      20.122  42.795 301.961  1.00 29.16           C  
ANISOU 5526  CD2 LEU D  64     2809   1483   6787   1239    638    730       C  
ATOM   5527  N   LEU D  65      17.367  44.630 300.385  1.00 30.12           N  
ANISOU 5527  N   LEU D  65     3588   1557   6299   1520    579    685       N  
ATOM   5528  CA  LEU D  65      17.363  45.685 299.369  1.00 32.40           C  
ANISOU 5528  CA  LEU D  65     4245   1580   6487   1718    721    786       C  
ATOM   5529  C   LEU D  65      18.796  46.017 298.933  1.00 40.07           C  
ANISOU 5529  C   LEU D  65     5279   2384   7560   1570    966    883       C  
ATOM   5530  O   LEU D  65      19.568  46.594 299.707  1.00 40.42           O  
ANISOU 5530  O   LEU D  65     5257   2380   7719   1310   1048    900       O  
ATOM   5531  CB  LEU D  65      16.631  46.960 299.835  1.00 33.22           C  
ANISOU 5531  CB  LEU D  65     4585   1530   6507   1787    689    796       C  
ATOM   5532  CG  LEU D  65      16.737  48.180 298.892  1.00 39.90           C  
ANISOU 5532  CG  LEU D  65     5902   2037   7224   1951    851    929       C  
ATOM   5533  CD1 LEU D  65      15.632  48.185 297.862  1.00 41.03           C  
ANISOU 5533  CD1 LEU D  65     6234   2217   7137   2324    745    952       C  
ATOM   5534  CD2 LEU D  65      16.731  49.473 299.668  1.00 43.24           C  
ANISOU 5534  CD2 LEU D  65     6555   2224   7649   1857    919    946       C  
ATOM   5535  N   TYR D  66      19.135  45.655 297.688  1.00 39.18           N  
ANISOU 5535  N   TYR D  66     5264   2288   7336   1653   1094    924       N  
ATOM   5536  CA  TYR D  66      20.432  45.958 297.091  1.00 41.72           C  
ANISOU 5536  CA  TYR D  66     5621   2572   7658   1455   1362    992       C  
ATOM   5537  C   TYR D  66      20.271  47.233 296.245  1.00 49.75           C  
ANISOU 5537  C   TYR D  66     7103   3360   8440   1479   1514   1094       C  
ATOM   5538  O   TYR D  66      19.367  47.306 295.403  1.00 49.98           O  
ANISOU 5538  O   TYR D  66     7384   3342   8265   1745   1447   1123       O  
ATOM   5539  CB  TYR D  66      20.970  44.758 296.280  1.00 42.99           C  
ANISOU 5539  CB  TYR D  66     5602   2892   7840   1521   1440    961       C  
ATOM   5540  CG  TYR D  66      21.867  43.840 297.090  1.00 44.12           C  
ANISOU 5540  CG  TYR D  66     5321   3209   8235   1396   1428    911       C  
ATOM   5541  CD1 TYR D  66      21.333  42.812 297.864  1.00 43.86           C  
ANISOU 5541  CD1 TYR D  66     5068   3271   8326   1493   1200    836       C  
ATOM   5542  CD2 TYR D  66      23.248  44.015 297.102  1.00 46.75           C  
ANISOU 5542  CD2 TYR D  66     5472   3626   8665   1180   1643    943       C  
ATOM   5543  CE1 TYR D  66      22.153  41.982 298.632  1.00 43.76           C  
ANISOU 5543  CE1 TYR D  66     4703   3397   8525   1416   1173    815       C  
ATOM   5544  CE2 TYR D  66      24.078  43.184 297.857  1.00 47.36           C  
ANISOU 5544  CE2 TYR D  66     5136   3895   8964   1117   1610    912       C  
ATOM   5545  CZ  TYR D  66      23.526  42.172 298.625  1.00 52.43           C  
ANISOU 5545  CZ  TYR D  66     5604   4594   9724   1254   1368    859       C  
ATOM   5546  OH  TYR D  66      24.346  41.349 299.364  1.00 53.87           O  
ANISOU 5546  OH  TYR D  66     5416   4946  10105   1230   1323    852       O  
ATOM   5547  N   TYR D  67      21.100  48.262 296.524  1.00 48.65           N  
ANISOU 5547  N   TYR D  67     7098   3078   8308   1192   1707   1150       N  
ATOM   5548  CA  TYR D  67      21.023  49.555 295.838  1.00 51.22           C  
ANISOU 5548  CA  TYR D  67     7935   3124   8401   1171   1877   1257       C  
ATOM   5549  C   TYR D  67      22.403  50.125 295.475  1.00 57.70           C  
ANISOU 5549  C   TYR D  67     8833   3898   9193    787   2199   1307       C  
ATOM   5550  O   TYR D  67      23.397  49.824 296.143  1.00 56.72           O  
ANISOU 5550  O   TYR D  67     8337   3954   9261    495   2267   1251       O  
ATOM   5551  CB  TYR D  67      20.241  50.579 296.695  1.00 52.43           C  
ANISOU 5551  CB  TYR D  67     8343   3051   8527   1219   1779   1266       C  
ATOM   5552  CG  TYR D  67      20.902  50.948 298.007  1.00 53.70           C  
ANISOU 5552  CG  TYR D  67     8327   3206   8872    862   1816   1208       C  
ATOM   5553  CD1 TYR D  67      20.689  50.191 299.155  1.00 53.12           C  
ANISOU 5553  CD1 TYR D  67     7831   3337   9014    847   1608   1105       C  
ATOM   5554  CD2 TYR D  67      21.710  52.074 298.109  1.00 57.23           C  
ANISOU 5554  CD2 TYR D  67     9064   3434   9246    516   2057   1255       C  
ATOM   5555  CE1 TYR D  67      21.296  50.524 300.365  1.00 54.09           C  
ANISOU 5555  CE1 TYR D  67     7798   3477   9277    508   1625   1055       C  
ATOM   5556  CE2 TYR D  67      22.324  52.417 299.312  1.00 58.37           C  
ANISOU 5556  CE2 TYR D  67     9049   3600   9530    148   2084   1190       C  
ATOM   5557  CZ  TYR D  67      22.110  51.642 300.441  1.00 63.50           C  
ANISOU 5557  CZ  TYR D  67     9256   4479  10393    157   1858   1092       C  
ATOM   5558  OH  TYR D  67      22.723  51.971 301.627  1.00 65.40           O  
ANISOU 5558  OH  TYR D  67     9340   4763  10744   -217   1870   1031       O  
ATOM   5559  N   THR D  68      22.441  50.974 294.424  1.00 57.57           N  
ANISOU 5559  N   THR D  68     9304   3655   8916    782   2394   1414       N  
ATOM   5560  CA  THR D  68      23.649  51.659 293.954  1.00 61.09           C  
ANISOU 5560  CA  THR D  68     9923   4023   9265    388   2735   1465       C  
ATOM   5561  C   THR D  68      23.297  52.905 293.141  1.00 68.21           C  
ANISOU 5561  C   THR D  68    11528   4543   9845    429   2882   1604       C  
ATOM   5562  O   THR D  68      22.270  52.938 292.459  1.00 67.77           O  
ANISOU 5562  O   THR D  68    11760   4377   9613    830   2739   1674       O  
ATOM   5563  CB  THR D  68      24.589  50.722 293.154  1.00 73.83           C  
ANISOU 5563  CB  THR D  68    11212   5922  10917    300   2899   1428       C  
ATOM   5564  OG1 THR D  68      25.815  51.404 292.879  1.00 79.68           O  
ANISOU 5564  OG1 THR D  68    12045   6647  11583   -142   3239   1453       O  
ATOM   5565  CG2 THR D  68      23.976  50.203 291.846  1.00 73.18           C  
ANISOU 5565  CG2 THR D  68    11321   5845  10639    643   2869   1467       C  
ATOM   5566  N   GLU D  69      24.172  53.922 293.212  1.00 68.13           N  
ANISOU 5566  N   GLU D  69    11800   4344   9743      2   3167   1644       N  
ATOM   5567  CA  GLU D  69      24.045  55.161 292.450  1.00 71.84           C  
ANISOU 5567  CA  GLU D  69    13005   4404   9887    -34   3362   1788       C  
ATOM   5568  C   GLU D  69      24.515  54.886 291.018  1.00 78.80           C  
ANISOU 5568  C   GLU D  69    14030   5354  10558    -52   3565   1856       C  
ATOM   5569  O   GLU D  69      25.582  54.293 290.823  1.00 78.88           O  
ANISOU 5569  O   GLU D  69    13652   5654  10666   -349   3748   1780       O  
ATOM   5570  CB  GLU D  69      24.858  56.286 293.114  1.00 75.95           C  
ANISOU 5570  CB  GLU D  69    13785   4695  10379   -558   3612   1782       C  
ATOM   5571  CG  GLU D  69      24.603  57.668 292.534  1.00 91.38           C  
ANISOU 5571  CG  GLU D  69    16599   6123  11997   -568   3790   1932       C  
ATOM   5572  CD  GLU D  69      25.142  58.839 293.336  1.00114.95           C  
ANISOU 5572  CD  GLU D  69    19932   8806  14938  -1056   4007   1911       C  
ATOM   5573  OE1 GLU D  69      24.445  59.877 293.404  1.00110.61           O  
ANISOU 5573  OE1 GLU D  69    20031   7786  14208   -887   4012   2000       O  
ATOM   5574  OE2 GLU D  69      26.260  58.726 293.890  1.00108.59           O  
ANISOU 5574  OE2 GLU D  69    18763   8237  14261  -1605   4175   1801       O  
ATOM   5575  N   PHE D  70      23.701  55.272 290.022  1.00 77.25           N  
ANISOU 5575  N   PHE D  70    14364   4920  10065    291   3524   1996       N  
ATOM   5576  CA  PHE D  70      24.016  55.047 288.610  1.00 79.19           C  
ANISOU 5576  CA  PHE D  70    14816   5210  10060    300   3699   2070       C  
ATOM   5577  C   PHE D  70      23.499  56.209 287.726  1.00 88.56           C  
ANISOU 5577  C   PHE D  70    16847   5960  10842    444   3785   2276       C  
ATOM   5578  O   PHE D  70      23.019  57.222 288.246  1.00 89.38           O  
ANISOU 5578  O   PHE D  70    17374   5709  10877    532   3733   2355       O  
ATOM   5579  CB  PHE D  70      23.440  53.685 288.152  1.00 77.52           C  
ANISOU 5579  CB  PHE D  70    14189   5341   9925    687   3458   2000       C  
ATOM   5580  CG  PHE D  70      21.978  53.650 287.759  1.00 78.01           C  
ANISOU 5580  CG  PHE D  70    14503   5321   9816   1235   3142   2082       C  
ATOM   5581  CD1 PHE D  70      20.982  53.923 288.690  1.00 78.99           C  
ANISOU 5581  CD1 PHE D  70    14596   5364  10055   1515   2858   2071       C  
ATOM   5582  CD2 PHE D  70      21.598  53.302 286.470  1.00 81.35           C  
ANISOU 5582  CD2 PHE D  70    15159   5796   9955   1464   3124   2157       C  
ATOM   5583  CE1 PHE D  70      19.632  53.884 288.325  1.00 79.52           C  
ANISOU 5583  CE1 PHE D  70    14833   5424   9956   2027   2564   2136       C  
ATOM   5584  CE2 PHE D  70      20.246  53.253 286.110  1.00 83.73           C  
ANISOU 5584  CE2 PHE D  70    15642   6090  10080   1961   2809   2228       C  
ATOM   5585  CZ  PHE D  70      19.273  53.539 287.042  1.00 80.00           C  
ANISOU 5585  CZ  PHE D  70    15098   5566   9731   2246   2529   2216       C  
ATOM   5586  N   THR D  71      23.644  56.060 286.393  1.00 88.33           N  
ANISOU 5586  N   THR D  71    17085   5945  10531    466   3932   2363       N  
ATOM   5587  CA  THR D  71      23.201  57.011 285.371  1.00 92.38           C  
ANISOU 5587  CA  THR D  71    18406   6081  10615    625   4007   2579       C  
ATOM   5588  C   THR D  71      22.574  56.215 284.204  1.00 96.19           C  
ANISOU 5588  C   THR D  71    18876   6775  10896   1014   3844   2623       C  
ATOM   5589  O   THR D  71      23.264  55.381 283.610  1.00 95.39           O  
ANISOU 5589  O   THR D  71    18474   6961  10808    820   4001   2533       O  
ATOM   5590  CB  THR D  71      24.355  57.932 284.920  1.00105.06           C  
ANISOU 5590  CB  THR D  71    20491   7430  11998     60   4461   2652       C  
ATOM   5591  OG1 THR D  71      25.569  57.183 284.834  1.00104.66           O  
ANISOU 5591  OG1 THR D  71    19924   7755  12086   -365   4711   2502       O  
ATOM   5592  CG2 THR D  71      24.553  59.118 285.848  1.00105.22           C  
ANISOU 5592  CG2 THR D  71    20823   7090  12067   -244   4589   2666       C  
ATOM   5593  N   PRO D  72      21.268  56.408 283.886  1.00 93.33           N  
ANISOU 5593  N   PRO D  72    18796   6313  10350   1564   3524   2744       N  
ATOM   5594  CA  PRO D  72      20.660  55.625 282.794  1.00 93.03           C  
ANISOU 5594  CA  PRO D  72    18723   6525  10100   1894   3349   2770       C  
ATOM   5595  C   PRO D  72      20.890  56.225 281.403  1.00101.37           C  
ANISOU 5595  C   PRO D  72    20460   7372  10685   1835   3562   2964       C  
ATOM   5596  O   PRO D  72      20.939  57.446 281.243  1.00104.58           O  
ANISOU 5596  O   PRO D  72    21537   7350  10849   1778   3709   3149       O  
ATOM   5597  CB  PRO D  72      19.173  55.612 283.150  1.00 93.45           C  
ANISOU 5597  CB  PRO D  72    18746   6613  10149   2479   2910   2810       C  
ATOM   5598  CG  PRO D  72      18.959  56.841 283.981  1.00 99.62           C  
ANISOU 5598  CG  PRO D  72    19917   6983  10953   2526   2930   2910       C  
ATOM   5599  CD  PRO D  72      20.286  57.328 284.501  1.00 95.73           C  
ANISOU 5599  CD  PRO D  72    19442   6309  10622   1920   3309   2849       C  
ATOM   5600  N   THR D  73      21.037  55.341 280.398  1.00 97.88           N  
ANISOU 5600  N   THR D  73    19872   7220  10097   1836   3590   2915       N  
ATOM   5601  CA  THR D  73      21.249  55.672 278.981  1.00101.84           C  
ANISOU 5601  CA  THR D  73    20952   7609  10132   1771   3781   3072       C  
ATOM   5602  C   THR D  73      20.419  54.695 278.110  1.00104.97           C  
ANISOU 5602  C   THR D  73    21201   8342  10342   2138   3502   3045       C  
ATOM   5603  O   THR D  73      20.031  53.619 278.585  1.00100.51           O  
ANISOU 5603  O   THR D  73    20014   8122  10054   2285   3276   2856       O  
ATOM   5604  CB  THR D  73      22.760  55.643 278.618  1.00108.28           C  
ANISOU 5604  CB  THR D  73    21740   8448  10952   1157   4277   2991       C  
ATOM   5605  OG1 THR D  73      23.554  56.111 279.713  1.00104.10           O  
ANISOU 5605  OG1 THR D  73    20992   7817  10745    778   4470   2904       O  
ATOM   5606  CG2 THR D  73      23.088  56.455 277.366  1.00111.89           C  
ANISOU 5606  CG2 THR D  73    22988   8623  10903    977   4559   3197       C  
ATOM   5607  N   GLU D  74      20.145  55.080 276.843  1.00105.34           N  
ANISOU 5607  N   GLU D  74    21847   8282   9894   2259   3522   3235       N  
ATOM   5608  CA  GLU D  74      19.384  54.283 275.876  1.00105.25           C  
ANISOU 5608  CA  GLU D  74    21798   8580   9614   2559   3275   3228       C  
ATOM   5609  C   GLU D  74      20.131  52.999 275.481  1.00106.78           C  
ANISOU 5609  C   GLU D  74    21527   9123   9920   2257   3479   2988       C  
ATOM   5610  O   GLU D  74      19.491  51.974 275.231  1.00104.59           O  
ANISOU 5610  O   GLU D  74    20930   9182   9628   2469   3234   2864       O  
ATOM   5611  CB  GLU D  74      19.082  55.116 274.623  1.00112.12           C  
ANISOU 5611  CB  GLU D  74    23484   9220   9895   2710   3284   3511       C  
ATOM   5612  N   LYS D  75      21.479  53.060 275.436  1.00103.48           N  
ANISOU 5612  N   LYS D  75    21078   8636   9605   1762   3936   2913       N  
ATOM   5613  CA  LYS D  75      22.348  51.942 275.063  1.00101.94           C  
ANISOU 5613  CA  LYS D  75    20467   8742   9522   1478   4200   2686       C  
ATOM   5614  C   LYS D  75      22.611  50.970 276.237  1.00 99.54           C  
ANISOU 5614  C   LYS D  75    19362   8683   9775   1440   4142   2433       C  
ATOM   5615  O   LYS D  75      22.515  49.754 276.046  1.00 96.86           O  
ANISOU 5615  O   LYS D  75    18625   8642   9535   1511   4088   2245       O  
ATOM   5616  CB  LYS D  75      23.683  52.473 274.509  1.00108.12           C  
ANISOU 5616  CB  LYS D  75    21550   9385  10146    976   4729   2717       C  
ATOM   5617  N   ASP D  76      22.947  51.508 277.435  1.00 93.59           N  
ANISOU 5617  N   ASP D  76    18414   7789   9357   1319   4161   2432       N  
ATOM   5618  CA  ASP D  76      23.289  50.744 278.643  1.00 88.77           C  
ANISOU 5618  CA  ASP D  76    17089   7380   9259   1258   4110   2226       C  
ATOM   5619  C   ASP D  76      22.073  50.044 279.278  1.00 87.53           C  
ANISOU 5619  C   ASP D  76    16601   7380   9279   1673   3645   2154       C  
ATOM   5620  O   ASP D  76      21.032  50.677 279.476  1.00 87.48           O  
ANISOU 5620  O   ASP D  76    16864   7236   9140   1975   3347   2292       O  
ATOM   5621  CB  ASP D  76      23.967  51.655 279.686  1.00 90.55           C  
ANISOU 5621  CB  ASP D  76    17276   7406   9722    967   4266   2261       C  
ATOM   5622  CG  ASP D  76      25.267  52.287 279.218  1.00104.07           C  
ANISOU 5622  CG  ASP D  76    19215   9024  11304    467   4752   2289       C  
ATOM   5623  OD1 ASP D  76      26.254  51.544 279.025  1.00104.50           O  
ANISOU 5623  OD1 ASP D  76    18870   9348  11486    226   5021   2125       O  
ATOM   5624  OD2 ASP D  76      25.308  53.527 279.079  1.00113.40           O  
ANISOU 5624  OD2 ASP D  76    20969   9863  12256    311   4874   2467       O  
ATOM   5625  N   GLU D  77      22.232  48.738 279.615  1.00 79.54           N  
ANISOU 5625  N   GLU D  77    15007   6656   8559   1685   3599   1936       N  
ATOM   5626  CA  GLU D  77      21.220  47.879 280.247  1.00 74.99           C  
ANISOU 5626  CA  GLU D  77    14064   6260   8167   1991   3207   1826       C  
ATOM   5627  C   GLU D  77      21.669  47.439 281.645  1.00 73.68           C  
ANISOU 5627  C   GLU D  77    13329   6173   8492   1890   3183   1688       C  
ATOM   5628  O   GLU D  77      22.841  47.115 281.844  1.00 73.73           O  
ANISOU 5628  O   GLU D  77    13062   6250   8703   1623   3472   1596       O  
ATOM   5629  CB  GLU D  77      20.929  46.645 279.378  1.00 76.30           C  
ANISOU 5629  CB  GLU D  77    14138   6674   8180   2100   3157   1689       C  
ATOM   5630  N   TYR D  78      20.737  47.422 282.608  1.00 65.68           N  
ANISOU 5630  N   TYR D  78    12127   5176   7652   2108   2838   1675       N  
ATOM   5631  CA  TYR D  78      21.025  47.052 283.994  1.00 61.44           C  
ANISOU 5631  CA  TYR D  78    11094   4706   7546   2030   2767   1562       C  
ATOM   5632  C   TYR D  78      20.095  45.929 284.458  1.00 61.22           C  
ANISOU 5632  C   TYR D  78    10722   4889   7652   2261   2444   1420       C  
ATOM   5633  O   TYR D  78      18.981  45.806 283.946  1.00 60.86           O  
ANISOU 5633  O   TYR D  78    10843   4911   7368   2506   2202   1439       O  
ATOM   5634  CB  TYR D  78      20.903  48.278 284.919  1.00 62.41           C  
ANISOU 5634  CB  TYR D  78    11351   4600   7761   1989   2709   1677       C  
ATOM   5635  CG  TYR D  78      21.849  49.417 284.590  1.00 67.34           C  
ANISOU 5635  CG  TYR D  78    12337   4988   8261   1690   3044   1804       C  
ATOM   5636  CD1 TYR D  78      21.516  50.374 283.633  1.00 72.67           C  
ANISOU 5636  CD1 TYR D  78    13632   5432   8547   1761   3106   1985       C  
ATOM   5637  CD2 TYR D  78      23.045  49.579 285.283  1.00 67.99           C  
ANISOU 5637  CD2 TYR D  78    12157   5083   8595   1323   3289   1747       C  
ATOM   5638  CE1 TYR D  78      22.378  51.429 283.331  1.00 76.36           C  
ANISOU 5638  CE1 TYR D  78    14490   5652   8872   1442   3435   2100       C  
ATOM   5639  CE2 TYR D  78      23.907  50.641 285.003  1.00 72.12           C  
ANISOU 5639  CE2 TYR D  78    13013   5406   8981    983   3612   1845       C  
ATOM   5640  CZ  TYR D  78      23.570  51.562 284.023  1.00 82.18           C  
ANISOU 5640  CZ  TYR D  78    14946   6415   9862   1029   3696   2019       C  
ATOM   5641  OH  TYR D  78      24.416  52.607 283.741  1.00 86.21           O  
ANISOU 5641  OH  TYR D  78    15842   6702  10213    652   4034   2115       O  
ATOM   5642  N   ALA D  79      20.572  45.099 285.413  1.00 54.87           N  
ANISOU 5642  N   ALA D  79     9440   4201   7207   2168   2443   1281       N  
ATOM   5643  CA  ALA D  79      19.870  43.942 285.992  1.00 51.67           C  
ANISOU 5643  CA  ALA D  79     8701   3970   6961   2314   2183   1133       C  
ATOM   5644  C   ALA D  79      20.568  43.466 287.269  1.00 53.49           C  
ANISOU 5644  C   ALA D  79     8483   4244   7598   2184   2202   1049       C  
ATOM   5645  O   ALA D  79      21.649  43.972 287.575  1.00 53.06           O  
ANISOU 5645  O   ALA D  79     8346   4130   7684   1976   2425   1093       O  
ATOM   5646  CB  ALA D  79      19.832  42.804 284.977  1.00 53.12           C  
ANISOU 5646  CB  ALA D  79     8904   4294   6985   2365   2245   1015       C  
ATOM   5647  N   CYS D  80      19.962  42.500 288.017  1.00 48.77           N  
ANISOU 5647  N   CYS D  80     7601   3764   7167   2283   1969    929       N  
ATOM   5648  CA  CYS D  80      20.603  41.919 289.199  1.00 47.49           C  
ANISOU 5648  CA  CYS D  80     7034   3649   7361   2186   1966    858       C  
ATOM   5649  C   CYS D  80      20.597  40.397 289.136  1.00 50.65           C  
ANISOU 5649  C   CYS D  80     7241   4162   7843   2260   1943    709       C  
ATOM   5650  O   CYS D  80      19.565  39.765 288.897  1.00 49.71           O  
ANISOU 5650  O   CYS D  80     7197   4101   7590   2377   1750    628       O  
ATOM   5651  CB  CYS D  80      20.038  42.432 290.522  1.00 46.27           C  
ANISOU 5651  CB  CYS D  80     6747   3463   7370   2183   1726    882       C  
ATOM   5652  SG  CYS D  80      18.291  42.067 290.813  1.00 49.02           S  
ANISOU 5652  SG  CYS D  80     7152   3894   7580   2401   1353    822       S  
ATOM   5653  N   ARG D  81      21.798  39.832 289.324  1.00 47.39           N  
ANISOU 5653  N   ARG D  81     6585   3785   7637   2187   2155    670       N  
ATOM   5654  CA  ARG D  81      22.135  38.410 289.321  1.00 46.58           C  
ANISOU 5654  CA  ARG D  81     6309   3740   7649   2275   2201    541       C  
ATOM   5655  C   ARG D  81      21.920  37.866 290.723  1.00 47.50           C  
ANISOU 5655  C   ARG D  81     6145   3874   8028   2291   1974    510       C  
ATOM   5656  O   ARG D  81      22.689  38.186 291.633  1.00 46.86           O  
ANISOU 5656  O   ARG D  81     5798   3824   8183   2205   1999    565       O  
ATOM   5657  CB  ARG D  81      23.599  38.254 288.867  1.00 47.69           C  
ANISOU 5657  CB  ARG D  81     6309   3930   7880   2229   2552    532       C  
ATOM   5658  CG  ARG D  81      24.050  36.852 288.555  1.00 53.85           C  
ANISOU 5658  CG  ARG D  81     7008   4736   8716   2376   2678    398       C  
ATOM   5659  CD  ARG D  81      25.041  36.865 287.406  1.00 66.52           C  
ANISOU 5659  CD  ARG D  81     8657   6391  10225   2359   3059    371       C  
ATOM   5660  NE  ARG D  81      26.326  37.481 287.756  1.00 73.47           N  
ANISOU 5660  NE  ARG D  81     9239   7387  11291   2230   3261    442       N  
ATOM   5661  CZ  ARG D  81      27.330  37.654 286.899  1.00 92.25           C  
ANISOU 5661  CZ  ARG D  81    11595   9857  13599   2151   3615    430       C  
ATOM   5662  NH1 ARG D  81      27.209  37.270 285.633  1.00 76.10           N  
ANISOU 5662  NH1 ARG D  81     9839   7776  11300   2204   3813    356       N  
ATOM   5663  NH2 ARG D  81      28.462  38.219 287.300  1.00 85.75           N  
ANISOU 5663  NH2 ARG D  81    10459   9185  12938   1991   3781    482       N  
ATOM   5664  N   VAL D  82      20.854  37.079 290.905  1.00 42.12           N  
ANISOU 5664  N   VAL D  82     5532   3191   7280   2369   1746    420       N  
ATOM   5665  CA  VAL D  82      20.497  36.516 292.206  1.00 39.79           C  
ANISOU 5665  CA  VAL D  82     5033   2904   7183   2362   1521    385       C  
ATOM   5666  C   VAL D  82      20.678  34.994 292.184  1.00 44.42           C  
ANISOU 5666  C   VAL D  82     5594   3457   7828   2450   1556    266       C  
ATOM   5667  O   VAL D  82      20.133  34.331 291.301  1.00 45.16           O  
ANISOU 5667  O   VAL D  82     5915   3532   7710   2494   1580    162       O  
ATOM   5668  CB  VAL D  82      19.047  36.919 292.591  1.00 42.37           C  
ANISOU 5668  CB  VAL D  82     5456   3264   7379   2347   1233    371       C  
ATOM   5669  CG1 VAL D  82      18.615  36.289 293.905  1.00 40.09           C  
ANISOU 5669  CG1 VAL D  82     4976   2990   7266   2304   1017    322       C  
ATOM   5670  CG2 VAL D  82      18.880  38.439 292.644  1.00 42.53           C  
ANISOU 5670  CG2 VAL D  82     5556   3267   7337   2312   1216    494       C  
ATOM   5671  N   ASN D  83      21.442  34.446 293.157  1.00 40.67           N  
ANISOU 5671  N   ASN D  83     4866   2967   7619   2477   1558    283       N  
ATOM   5672  CA  ASN D  83      21.645  33.002 293.294  1.00 40.62           C  
ANISOU 5672  CA  ASN D  83     4869   2881   7685   2596   1590    191       C  
ATOM   5673  C   ASN D  83      21.360  32.532 294.730  1.00 40.87           C  
ANISOU 5673  C   ASN D  83     4753   2882   7891   2567   1354    206       C  
ATOM   5674  O   ASN D  83      21.969  32.994 295.695  1.00 39.20           O  
ANISOU 5674  O   ASN D  83     4277   2731   7887   2534   1301    307       O  
ATOM   5675  CB  ASN D  83      23.035  32.558 292.846  1.00 43.99           C  
ANISOU 5675  CB  ASN D  83     5167   3310   8236   2742   1882    200       C  
ATOM   5676  CG  ASN D  83      23.103  31.098 292.429  1.00 69.24           C  
ANISOU 5676  CG  ASN D  83     8532   6375  11402   2916   1998     78       C  
ATOM   5677  OD1 ASN D  83      22.296  30.242 292.826  1.00 57.28           O  
ANISOU 5677  OD1 ASN D  83     7179   4739   9843   2915   1841      1       O  
ATOM   5678  ND2 ASN D  83      24.083  30.778 291.608  1.00 67.51           N  
ANISOU 5678  ND2 ASN D  83     8293   6166  11193   3059   2301     47       N  
ATOM   5679  N   HIS D  84      20.419  31.598 294.833  1.00 37.05           N  
ANISOU 5679  N   HIS D  84     4464   2361   7254   2487   1214    106       N  
ATOM   5680  CA  HIS D  84      19.927  30.953 296.051  1.00 36.01           C  
ANISOU 5680  CA  HIS D  84     4288   2231   7163   2353    995    100       C  
ATOM   5681  C   HIS D  84      20.058  29.425 295.892  1.00 39.73           C  
ANISOU 5681  C   HIS D  84     4966   2417   7711   2595   1088    -10       C  
ATOM   5682  O   HIS D  84      20.330  28.944 294.788  1.00 40.56           O  
ANISOU 5682  O   HIS D  84     5257   2452   7702   2697   1295    -90       O  
ATOM   5683  CB  HIS D  84      18.450  31.368 296.261  1.00 34.88           C  
ANISOU 5683  CB  HIS D  84     4236   2155   6864   2200    770     28       C  
ATOM   5684  CG  HIS D  84      17.900  31.129 297.633  1.00 35.93           C  
ANISOU 5684  CG  HIS D  84     4278   2209   7166   2178    554     24       C  
ATOM   5685  ND1 HIS D  84      16.929  30.172 297.860  1.00 37.68           N  
ANISOU 5685  ND1 HIS D  84     4673   2378   7267   2062    438    -98       N  
ATOM   5686  CD2 HIS D  84      18.170  31.760 298.796  1.00 36.13           C  
ANISOU 5686  CD2 HIS D  84     4070   2290   7367   2119    441    129       C  
ATOM   5687  CE1 HIS D  84      16.656  30.237 299.151  1.00 35.64           C  
ANISOU 5687  CE1 HIS D  84     4279   2144   7118   1950    265    -56       C  
ATOM   5688  NE2 HIS D  84      17.377  31.179 299.756  1.00 35.11           N  
ANISOU 5688  NE2 HIS D  84     3966   2151   7222   1976    255     79       N  
ATOM   5689  N   VAL D  85      19.846  28.670 296.983  1.00 36.83           N  
ANISOU 5689  N   VAL D  85     4584   2106   7305   2388    924     21       N  
ATOM   5690  CA  VAL D  85      19.904  27.197 297.003  1.00 38.44           C  
ANISOU 5690  CA  VAL D  85     5041   2066   7496   2509    987    -56       C  
ATOM   5691  C   VAL D  85      18.692  26.597 296.213  1.00 40.29           C  
ANISOU 5691  C   VAL D  85     5670   2091   7546   2481    989   -270       C  
ATOM   5692  O   VAL D  85      18.754  25.454 295.747  1.00 41.30           O  
ANISOU 5692  O   VAL D  85     6108   2004   7578   2539   1118   -376       O  
ATOM   5693  CB  VAL D  85      20.002  26.674 298.468  1.00 41.04           C  
ANISOU 5693  CB  VAL D  85     5328   2157   8108   2671    831     10       C  
ATOM   5694  CG1 VAL D  85      18.838  27.160 299.328  1.00 38.60           C  
ANISOU 5694  CG1 VAL D  85     4990   1991   7687   2328    569     -9       C  
ATOM   5695  CG2 VAL D  85      20.159  25.157 298.534  1.00 43.30           C  
ANISOU 5695  CG2 VAL D  85     5924   2147   8380   2830    922    -36       C  
ATOM   5696  N   THR D  86      17.618  27.391 296.052  1.00 35.14           N  
ANISOU 5696  N   THR D  86     4936   1787   6628   2134    822   -287       N  
ATOM   5697  CA  THR D  86      16.425  26.993 295.310  1.00 34.31           C  
ANISOU 5697  CA  THR D  86     5114   1641   6283   2023    785   -482       C  
ATOM   5698  C   THR D  86      16.660  27.171 293.806  1.00 38.81           C  
ANISOU 5698  C   THR D  86     5843   2188   6716   2154    987   -557       C  
ATOM   5699  O   THR D  86      16.164  26.372 293.014  1.00 40.28           O  
ANISOU 5699  O   THR D  86     6328   2323   6655   2049   1048   -720       O  
ATOM   5700  CB  THR D  86      15.192  27.776 295.786  1.00 36.82           C  
ANISOU 5700  CB  THR D  86     5296   2153   6539   1854    540   -516       C  
ATOM   5701  OG1 THR D  86      15.394  29.174 295.584  1.00 33.89           O  
ANISOU 5701  OG1 THR D  86     4682   1948   6245   1952    522   -392       O  
ATOM   5702  CG2 THR D  86      14.837  27.493 297.241  1.00 33.24           C  
ANISOU 5702  CG2 THR D  86     4766   1670   6194   1708    362   -501       C  
ATOM   5703  N   LEU D  87      17.417  28.204 293.414  1.00 34.77           N  
ANISOU 5703  N   LEU D  87     5124   1820   6266   2255   1085   -415       N  
ATOM   5704  CA  LEU D  87      17.688  28.490 292.007  1.00 35.79           C  
ANISOU 5704  CA  LEU D  87     5403   1935   6262   2379   1291   -470       C  
ATOM   5705  C   LEU D  87      18.771  27.551 291.414  1.00 43.25           C  
ANISOU 5705  C   LEU D  87     6498   2672   7264   2567   1590   -516       C  
ATOM   5706  O   LEU D  87      19.937  27.598 291.826  1.00 43.36           O  
ANISOU 5706  O   LEU D  87     6309   2628   7539   2758   1712   -408       O  
ATOM   5707  CB  LEU D  87      18.086  29.965 291.828  1.00 34.73           C  
ANISOU 5707  CB  LEU D  87     5040   1984   6171   2406   1299   -309       C  
ATOM   5708  CG  LEU D  87      17.034  30.998 292.215  1.00 37.01           C  
ANISOU 5708  CG  LEU D  87     5235   2440   6387   2311   1049   -274       C  
ATOM   5709  CD1 LEU D  87      17.678  32.315 292.583  1.00 36.20           C  
ANISOU 5709  CD1 LEU D  87     4906   2390   6460   2367   1065   -100       C  
ATOM   5710  CD2 LEU D  87      16.006  31.188 291.114  1.00 40.33           C  
ANISOU 5710  CD2 LEU D  87     5865   3004   6455   2247   1000   -363       C  
ATOM   5711  N   SER D  88      18.376  26.724 290.419  1.00 42.19           N  
ANISOU 5711  N   SER D  88     6712   2449   6869   2515   1714   -687       N  
ATOM   5712  CA  SER D  88      19.272  25.778 289.738  1.00 45.48           C  
ANISOU 5712  CA  SER D  88     7338   2649   7294   2701   2027   -768       C  
ATOM   5713  C   SER D  88      20.268  26.504 288.824  1.00 51.26           C  
ANISOU 5713  C   SER D  88     7948   3472   8054   2862   2280   -702       C  
ATOM   5714  O   SER D  88      21.249  25.905 288.361  1.00 53.11           O  
ANISOU 5714  O   SER D  88     8227   3574   8379   3079   2564   -734       O  
ATOM   5715  CB  SER D  88      18.472  24.752 288.937  1.00 51.32           C  
ANISOU 5715  CB  SER D  88     8524   3268   7707   2541   2088   -991       C  
ATOM   5716  OG  SER D  88      17.715  25.348 287.898  1.00 59.77           O  
ANISOU 5716  OG  SER D  88     9692   4557   8462   2366   2043  -1056       O  
ATOM   5717  N   GLN D  89      20.005  27.796 288.577  1.00 46.94           N  
ANISOU 5717  N   GLN D  89     7264   3151   7419   2759   2187   -611       N  
ATOM   5718  CA  GLN D  89      20.813  28.683 287.747  1.00 48.32           C  
ANISOU 5718  CA  GLN D  89     7350   3432   7577   2833   2402   -532       C  
ATOM   5719  C   GLN D  89      20.576  30.127 288.204  1.00 50.23           C  
ANISOU 5719  C   GLN D  89     7350   3855   7881   2744   2212   -362       C  
ATOM   5720  O   GLN D  89      19.410  30.513 288.351  1.00 48.09           O  
ANISOU 5720  O   GLN D  89     7135   3677   7461   2606   1948   -364       O  
ATOM   5721  CB  GLN D  89      20.442  28.491 286.272  1.00 52.11           C  
ANISOU 5721  CB  GLN D  89     8181   3929   7691   2761   2555   -664       C  
ATOM   5722  CG  GLN D  89      21.532  28.870 285.298  1.00 74.68           C  
ANISOU 5722  CG  GLN D  89    11035   6821  10520   2862   2893   -635       C  
ATOM   5723  CD  GLN D  89      21.136  28.451 283.909  1.00101.85           C  
ANISOU 5723  CD  GLN D  89    14868  10250  13582   2784   3050   -789       C  
ATOM   5724  OE1 GLN D  89      20.282  29.075 283.263  1.00 98.91           O  
ANISOU 5724  OE1 GLN D  89    14650  10020  12913   2633   2917   -772       O  
ATOM   5725  NE2 GLN D  89      21.726  27.363 283.433  1.00 96.00           N  
ANISOU 5725  NE2 GLN D  89    14310   9338  12827   2899   3332   -943       N  
ATOM   5726  N   PRO D  90      21.640  30.933 288.463  1.00 47.02           N  
ANISOU 5726  N   PRO D  90     6674   3508   7684   2812   2343   -224       N  
ATOM   5727  CA  PRO D  90      21.419  32.318 288.936  1.00 44.93           C  
ANISOU 5727  CA  PRO D  90     6240   3364   7465   2706   2182    -71       C  
ATOM   5728  C   PRO D  90      20.466  33.107 288.032  1.00 48.94           C  
ANISOU 5728  C   PRO D  90     6994   3954   7647   2609   2100    -58       C  
ATOM   5729  O   PRO D  90      20.710  33.236 286.831  1.00 50.67           O  
ANISOU 5729  O   PRO D  90     7408   4187   7659   2613   2307    -75       O  
ATOM   5730  CB  PRO D  90      22.829  32.931 288.964  1.00 47.84           C  
ANISOU 5730  CB  PRO D  90     6356   3785   8033   2751   2425     33       C  
ATOM   5731  CG  PRO D  90      23.693  31.989 288.184  1.00 55.04           C  
ANISOU 5731  CG  PRO D  90     7334   4648   8929   2896   2741    -73       C  
ATOM   5732  CD  PRO D  90      23.081  30.633 288.346  1.00 50.49           C  
ANISOU 5732  CD  PRO D  90     6946   3923   8315   2978   2651   -212       C  
ATOM   5733  N   LYS D  91      19.337  33.564 288.613  1.00 43.61           N  
ANISOU 5733  N   LYS D  91     6315   3345   6909   2537   1791    -34       N  
ATOM   5734  CA  LYS D  91      18.291  34.319 287.917  1.00 43.24           C  
ANISOU 5734  CA  LYS D  91     6465   3409   6556   2498   1645    -10       C  
ATOM   5735  C   LYS D  91      18.723  35.767 287.691  1.00 47.78           C  
ANISOU 5735  C   LYS D  91     7043   3991   7119   2503   1719    165       C  
ATOM   5736  O   LYS D  91      19.155  36.433 288.638  1.00 45.40           O  
ANISOU 5736  O   LYS D  91     6533   3659   7058   2479   1690    266       O  
ATOM   5737  CB  LYS D  91      16.971  34.263 288.702  1.00 42.89           C  
ANISOU 5737  CB  LYS D  91     6358   3465   6473   2448   1303    -54       C  
ATOM   5738  N   ILE D  92      18.627  36.244 286.431  1.00 47.75           N  
ANISOU 5738  N   ILE D  92     7312   4017   6815   2513   1823    198       N  
ATOM   5739  CA  ILE D  92      18.979  37.623 286.065  1.00 49.34           C  
ANISOU 5739  CA  ILE D  92     7625   4187   6935   2502   1915    368       C  
ATOM   5740  C   ILE D  92      17.694  38.364 285.611  1.00 53.79           C  
ANISOU 5740  C   ILE D  92     8416   4835   7187   2574   1665    432       C  
ATOM   5741  O   ILE D  92      17.171  38.121 284.517  1.00 54.95           O  
ANISOU 5741  O   ILE D  92     8804   5067   7007   2603   1646    385       O  
ATOM   5742  CB  ILE D  92      20.173  37.743 285.046  1.00 55.48           C  
ANISOU 5742  CB  ILE D  92     8535   4913   7632   2452   2293    390       C  
ATOM   5743  CG1 ILE D  92      19.921  37.022 283.698  1.00 58.49           C  
ANISOU 5743  CG1 ILE D  92     9179   5336   7708   2471   2406    265       C  
ATOM   5744  CG2 ILE D  92      21.503  37.293 285.673  1.00 55.66           C  
ANISOU 5744  CG2 ILE D  92     8246   4902   8002   2411   2523    371       C  
ATOM   5745  CD1 ILE D  92      19.656  37.985 282.505  1.00 68.07           C  
ANISOU 5745  CD1 ILE D  92    10762   6568   8533   2453   2476    364       C  
ATOM   5746  N   VAL D  93      17.153  39.217 286.503  1.00 49.22           N  
ANISOU 5746  N   VAL D  93     7748   4249   6704   2619   1461    530       N  
ATOM   5747  CA  VAL D  93      15.934  39.985 286.232  1.00 49.77           C  
ANISOU 5747  CA  VAL D  93     7986   4412   6513   2754   1209    602       C  
ATOM   5748  C   VAL D  93      16.346  41.356 285.704  1.00 56.74           C  
ANISOU 5748  C   VAL D  93     9148   5148   7262   2792   1344    800       C  
ATOM   5749  O   VAL D  93      16.976  42.125 286.432  1.00 56.06           O  
ANISOU 5749  O   VAL D  93     9001   4909   7389   2729   1438    893       O  
ATOM   5750  CB  VAL D  93      14.994  40.071 287.466  1.00 51.04           C  
ANISOU 5750  CB  VAL D  93     7905   4660   6827   2810    913    568       C  
ATOM   5751  CG1 VAL D  93      13.841  41.043 287.223  1.00 51.89           C  
ANISOU 5751  CG1 VAL D  93     8160   4869   6687   3009    678    662       C  
ATOM   5752  CG2 VAL D  93      14.457  38.693 287.839  1.00 49.53           C  
ANISOU 5752  CG2 VAL D  93     7515   4616   6687   2737    780    371       C  
ATOM   5753  N   LYS D  94      16.005  41.643 284.429  1.00 56.46           N  
ANISOU 5753  N   LYS D  94     9446   5153   6851   2871   1360    861       N  
ATOM   5754  CA  LYS D  94      16.336  42.893 283.741  1.00 59.15           C  
ANISOU 5754  CA  LYS D  94    10152   5334   6988   2906   1496   1059       C  
ATOM   5755  C   LYS D  94      15.525  44.076 284.285  1.00 65.33           C  
ANISOU 5755  C   LYS D  94    11039   6056   7728   3103   1268   1203       C  
ATOM   5756  O   LYS D  94      14.373  43.903 284.693  1.00 63.95           O  
ANISOU 5756  O   LYS D  94    10725   6065   7508   3279    958   1151       O  
ATOM   5757  CB  LYS D  94      16.115  42.749 282.227  1.00 64.16           C  
ANISOU 5757  CB  LYS D  94    11130   6048   7198   2942   1552   1080       C  
ATOM   5758  N   TRP D  95      16.138  45.277 284.294  1.00 65.15           N  
ANISOU 5758  N   TRP D  95    11268   5777   7710   3064   1441   1373       N  
ATOM   5759  CA  TRP D  95      15.486  46.512 284.737  1.00 66.50           C  
ANISOU 5759  CA  TRP D  95    11634   5808   7827   3263   1288   1523       C  
ATOM   5760  C   TRP D  95      14.726  47.127 283.578  1.00 74.12           C  
ANISOU 5760  C   TRP D  95    13032   6785   8346   3522   1170   1676       C  
ATOM   5761  O   TRP D  95      15.317  47.447 282.546  1.00 75.83           O  
ANISOU 5761  O   TRP D  95    13613   6879   8321   3435   1386   1782       O  
ATOM   5762  CB  TRP D  95      16.500  47.515 285.320  1.00 65.86           C  
ANISOU 5762  CB  TRP D  95    11681   5414   7927   3064   1546   1626       C  
ATOM   5763  CG  TRP D  95      15.955  48.895 285.569  1.00 68.70           C  
ANISOU 5763  CG  TRP D  95    12391   5538   8174   3256   1467   1797       C  
ATOM   5764  CD1 TRP D  95      14.916  49.236 286.387  1.00 70.68           C  
ANISOU 5764  CD1 TRP D  95    12538   5814   8501   3508   1201   1791       C  
ATOM   5765  CD2 TRP D  95      16.475  50.125 285.047  1.00 71.87           C  
ANISOU 5765  CD2 TRP D  95    13325   5613   8370   3198   1690   1993       C  
ATOM   5766  NE1 TRP D  95      14.731  50.601 286.376  1.00 72.66           N  
ANISOU 5766  NE1 TRP D  95    13239   5761   8605   3659   1238   1972       N  
ATOM   5767  CE2 TRP D  95      15.683  51.173 285.572  1.00 76.63           C  
ANISOU 5767  CE2 TRP D  95    14162   6024   8930   3460   1536   2104       C  
ATOM   5768  CE3 TRP D  95      17.536  50.447 284.182  1.00 75.63           C  
ANISOU 5768  CE3 TRP D  95    14125   5933   8678   2942   2022   2079       C  
ATOM   5769  CZ2 TRP D  95      15.917  52.516 285.260  1.00 79.31           C  
ANISOU 5769  CZ2 TRP D  95    15094   5980   9061   3480   1700   2308       C  
ATOM   5770  CZ3 TRP D  95      17.762  51.779 283.868  1.00 80.44           C  
ANISOU 5770  CZ3 TRP D  95    15306   6189   9071   2919   2184   2279       C  
ATOM   5771  CH2 TRP D  95      16.957  52.795 284.401  1.00 82.01           C  
ANISOU 5771  CH2 TRP D  95    15775   6160   9226   3190   2021   2397       C  
ATOM   5772  N   ASP D  96      13.411  47.280 283.756  1.00 72.17           N  
ANISOU 5772  N   ASP D  96    12729   6715   7978   3842    827   1685       N  
ATOM   5773  CA  ASP D  96      12.506  47.856 282.764  1.00 76.20           C  
ANISOU 5773  CA  ASP D  96    13592   7305   8057   4166    637   1837       C  
ATOM   5774  C   ASP D  96      12.140  49.296 283.156  1.00 82.72           C  
ANISOU 5774  C   ASP D  96    14725   7870   8835   4448    574   2036       C  
ATOM   5775  O   ASP D  96      11.819  49.563 284.322  1.00 80.77           O  
ANISOU 5775  O   ASP D  96    14244   7596   8848   4535    471   1984       O  
ATOM   5776  CB  ASP D  96      11.241  46.976 282.626  1.00 77.88           C  
ANISOU 5776  CB  ASP D  96    13493   7969   8130   4344    283   1695       C  
ATOM   5777  CG  ASP D  96      10.289  47.298 281.478  1.00 93.10           C  
ANISOU 5777  CG  ASP D  96    15698  10100   9574   4662     47   1823       C  
ATOM   5778  OD1 ASP D  96      10.570  48.253 280.712  1.00 97.25           O  
ANISOU 5778  OD1 ASP D  96    16728  10393   9830   4746    173   2039       O  
ATOM   5779  OD2 ASP D  96       9.268  46.589 281.341  1.00 98.85           O  
ANISOU 5779  OD2 ASP D  96    16146  11241  10173   4805   -263   1708       O  
ATOM   5780  N   ARG D  97      12.201  50.219 282.178  1.00 82.91           N  
ANISOU 5780  N   ARG D  97    15313   7679   8511   4588    654   2264       N  
ATOM   5781  CA  ARG D  97      11.862  51.625 282.385  1.00 85.34           C  
ANISOU 5781  CA  ARG D  97    16042   7673   8710   4890    622   2480       C  
ATOM   5782  C   ARG D  97      10.349  51.772 282.584  1.00 90.38           C  
ANISOU 5782  C   ARG D  97    16535   8592   9215   5404    209   2497       C  
ATOM   5783  O   ARG D  97       9.918  52.396 283.557  1.00 89.43           O  
ANISOU 5783  O   ARG D  97    16382   8344   9255   5627    128   2518       O  
ATOM   5784  CB  ARG D  97      12.351  52.482 281.203  1.00 89.90           C  
ANISOU 5784  CB  ARG D  97    17308   7942   8906   4888    823   2726       C  
ATOM   5785  N   ASP D  98       9.555  51.152 281.683  1.00 88.86           N  
ANISOU 5785  N   ASP D  98    16227   8813   8725   5572    -43   2468       N  
ATOM   5786  CA  ASP D  98       8.089  51.176 281.688  1.00 90.61           C  
ANISOU 5786  CA  ASP D  98    16240   9423   8764   6042   -455   2467       C  
ATOM   5787  C   ASP D  98       7.497  50.399 282.868  1.00 90.60           C  
ANISOU 5787  C   ASP D  98    15581   9734   9109   5996   -622   2210       C  
ATOM   5788  O   ASP D  98       6.415  50.752 283.332  1.00 91.65           O  
ANISOU 5788  O   ASP D  98    15543  10047   9234   6384   -874   2213       O  
ATOM   5789  CB  ASP D  98       7.534  50.618 280.367  1.00 95.13           C  
ANISOU 5789  CB  ASP D  98    16851  10391   8902   6127   -657   2483       C  
ATOM   5790  N   MET D  99       8.187  49.343 283.342  1.00 82.53           N  
ANISOU 5790  N   MET D  99    14202   8781   8373   5541   -476   1990       N  
ATOM   5791  CA  MET D  99       7.722  48.519 284.459  1.00101.33           C  
ANISOU 5791  CA  MET D  99    16004  11429  11069   5431   -606   1747       C  
ATOM   5792  C   MET D  99       8.904  47.895 285.207  1.00135.24           C  
ANISOU 5792  C   MET D  99    20129  15493  15762   4967   -318   1617       C  
ATOM   5793  O   MET D  99       9.259  48.339 286.300  1.00 96.31           O  
ANISOU 5793  O   MET D  99    15138  10324  11132   4913   -216   1614       O  
ATOM   5794  CB  MET D  99       6.768  47.425 283.954  1.00103.89           C  
ANISOU 5794  CB  MET D  99    15976  12308  11190   5428   -879   1575       C  
ATOM   5795  CG  MET D  99       5.701  47.068 284.950  1.00105.99           C  
ANISOU 5795  CG  MET D  99    15720  12929  11621   5510  -1123   1385       C  
ATOM   5796  SD  MET D  99       4.605  45.762 284.366  1.00111.41           S  
ANISOU 5796  SD  MET D  99    16019  14300  12011   5457  -1443   1175       S  
ATOM   5797  CE  MET D  99       3.734  45.377 285.883  1.00105.69           C  
ANISOU 5797  CE  MET D  99    14705  13873  11579   5447  -1614    948       C  
TER    5798      MET D  99                                                      
HETATM 5799  C1  NAG C 301      32.308  24.556 308.482  1.00 31.63           C  
ANISOU 5799  C1  NAG C 301     3208   2200   6610   1822    167   -109       C  
HETATM 5800  C2  NAG C 301      33.581  23.744 308.237  1.00 33.13           C  
ANISOU 5800  C2  NAG C 301     3379   2404   6806   2041    224    -99       C  
HETATM 5801  C3  NAG C 301      34.723  24.619 307.721  1.00 34.33           C  
ANISOU 5801  C3  NAG C 301     3337   2698   7009   2134    434    -25       C  
HETATM 5802  C4  NAG C 301      34.260  25.449 306.522  1.00 35.24           C  
ANISOU 5802  C4  NAG C 301     3524   2840   7025   2159    563    -23       C  
HETATM 5803  C5  NAG C 301      32.991  26.231 306.857  1.00 32.93           C  
ANISOU 5803  C5  NAG C 301     3262   2520   6730   1940    480    -35       C  
HETATM 5804  C6  NAG C 301      32.409  26.934 305.651  1.00 34.81           C  
ANISOU 5804  C6  NAG C 301     3609   2765   6853   1979    573    -44       C  
HETATM 5805  C7  NAG C 301      33.596  21.746 309.684  1.00 33.94           C  
ANISOU 5805  C7  NAG C 301     3619   2339   6938   2045    -50   -151       C  
HETATM 5806  C8  NAG C 301      34.131  21.143 310.947  1.00 34.18           C  
ANISOU 5806  C8  NAG C 301     3585   2342   7059   2004   -163   -129       C  
HETATM 5807  N2  NAG C 301      33.992  23.006 309.422  1.00 32.45           N  
ANISOU 5807  N2  NAG C 301     3243   2283   6805   2004    102    -92       N  
HETATM 5808  O3  NAG C 301      35.806  23.773 307.345  1.00 34.20           O  
ANISOU 5808  O3  NAG C 301     3316   2697   6982   2367    495    -26       O  
HETATM 5809  O4  NAG C 301      35.282  26.347 306.097  1.00 37.15           O  
ANISOU 5809  O4  NAG C 301     3582   3212   7321   2212    769     59       O  
HETATM 5810  O5  NAG C 301      31.972  25.332 307.327  1.00 31.94           O  
ANISOU 5810  O5  NAG C 301     3295   2276   6565   1868    282   -110       O  
HETATM 5811  O6  NAG C 301      31.060  27.332 305.868  1.00 35.27           O  
ANISOU 5811  O6  NAG C 301     3726   2782   6894   1808    464    -77       O  
HETATM 5812  O7  NAG C 301      32.843  21.124 308.935  1.00 34.55           O  
ANISOU 5812  O7  NAG C 301     3919   2315   6894   2111   -102   -219       O  
HETATM 5813  C1  NAG C 302      30.887  35.276 314.863  1.00 36.28           C  
ANISOU 5813  C1  NAG C 302     2782   3175   7826    320    275    260       C  
HETATM 5814  C2  NAG C 302      32.066  34.834 313.993  1.00 38.68           C  
ANISOU 5814  C2  NAG C 302     3020   3523   8155    459    375    297       C  
HETATM 5815  C3  NAG C 302      33.022  33.896 314.733  1.00 41.08           C  
ANISOU 5815  C3  NAG C 302     3235   3836   8537    490    304    307       C  
HETATM 5816  C4  NAG C 302      33.420  34.479 316.087  1.00 42.63           C  
ANISOU 5816  C4  NAG C 302     3323   4041   8834    338    224    339       C  
HETATM 5817  C5  NAG C 302      32.169  34.863 316.875  1.00 39.27           C  
ANISOU 5817  C5  NAG C 302     3000   3562   8360    206    135    300       C  
HETATM 5818  C6  NAG C 302      32.459  35.552 318.189  1.00 39.10           C  
ANISOU 5818  C6  NAG C 302     2905   3536   8413     59     58    326       C  
HETATM 5819  C7  NAG C 302      31.575  34.844 311.579  1.00 40.64           C  
ANISOU 5819  C7  NAG C 302     3432   3773   8236    678    550    278       C  
HETATM 5820  C8  NAG C 302      31.090  34.030 310.418  1.00 39.49           C  
ANISOU 5820  C8  NAG C 302     3441   3596   7969    834    565    224       C  
HETATM 5821  N2  NAG C 302      31.600  34.215 312.763  1.00 39.16           N  
ANISOU 5821  N2  NAG C 302     3208   3565   8108    602    420    256       N  
HETATM 5822  O3  NAG C 302      34.186  33.699 313.937  1.00 42.61           O  
ANISOU 5822  O3  NAG C 302     3334   4088   8766    620    416    348       O  
HETATM 5823  O4  NAG C 302      34.219  33.543 316.814  1.00 45.25           O  
ANISOU 5823  O4  NAG C 302     3590   4374   9228    377    134    342       O  
HETATM 5824  O5  NAG C 302      31.383  35.785 316.104  1.00 37.52           O  
ANISOU 5824  O5  NAG C 302     2842   3339   8074    191    217    293       O  
HETATM 5825  O6  NAG C 302      31.251  35.840 318.891  1.00 37.86           O  
ANISOU 5825  O6  NAG C 302     2854   3334   8198    -43     -7    287       O  
HETATM 5826  O7  NAG C 302      31.918  36.018 311.452  1.00 42.98           O  
ANISOU 5826  O7  NAG C 302     3657   4104   8569    620    647    338       O  
HETATM 5827  CAA JLS C 303      20.036  34.625 329.258  1.00 26.33           C  
ANISOU 5827  CAA JLS C 303     2194   1696   6113   -971   -267      8       C  
HETATM 5828  CAB JLS C 303      18.805  35.395 329.688  1.00 24.30           C  
ANISOU 5828  CAB JLS C 303     1925   1500   5806  -1002   -178    -23       C  
HETATM 5829  CAC JLS C 303      17.874  35.656 328.508  1.00 23.30           C  
ANISOU 5829  CAC JLS C 303     1696   1447   5710   -953   -125    -67       C  
HETATM 5830  CAD JLS C 303      17.308  37.066 328.479  1.00 24.81           C  
ANISOU 5830  CAD JLS C 303     1848   1695   5883   -899    -61    -97       C  
HETATM 5831  CAE JLS C 303      16.711  37.355 327.102  1.00 27.86           C  
ANISOU 5831  CAE JLS C 303     2142   2136   6309   -817    -44   -135       C  
HETATM 5832  CAF JLS C 303      17.006  38.775 326.610  1.00 30.50           C  
ANISOU 5832  CAF JLS C 303     2468   2480   6643   -728    -22   -146       C  
HETATM 5833  CAG JLS C 303      17.508  38.804 325.168  1.00 32.92           C  
ANISOU 5833  CAG JLS C 303     2735   2779   6994   -643    -46   -146       C  
HETATM 5834  CAH JLS C 303      16.560  39.593 324.266  1.00 36.97           C  
ANISOU 5834  CAH JLS C 303     3199   3352   7497   -557    -10   -192       C  
HETATM 5835  CAI JLS C 303      16.031  38.744 323.108  1.00 39.82           C  
ANISOU 5835  CAI JLS C 303     3508   3739   7882   -523    -39   -219       C  
HETATM 5836  CAJ JLS C 303      15.894  39.540 321.807  1.00 40.38           C  
ANISOU 5836  CAJ JLS C 303     3566   3828   7949   -402    -35   -242       C  
HETATM 5837  CAK JLS C 303      16.530  38.808 320.624  1.00 40.48           C  
ANISOU 5837  CAK JLS C 303     3594   3806   7982   -353    -73   -230       C  
HETATM 5838  CAL JLS C 303      16.547  39.685 319.373  1.00 41.96           C  
ANISOU 5838  CAL JLS C 303     3798   3998   8147   -230    -59   -242       C  
HETATM 5839  CAM JLS C 303      17.951  40.176 319.006  1.00 43.14           C  
ANISOU 5839  CAM JLS C 303     3995   4093   8304   -196    -29   -185       C  
HETATM 5840  CAN JLS C 303      18.238  41.598 319.501  1.00 43.62           C  
ANISOU 5840  CAN JLS C 303     4085   4136   8352   -196     15   -161       C  
HETATM 5841  CAO JLS C 303      17.822  42.638 318.476  1.00 44.34           C  
ANISOU 5841  CAO JLS C 303     4213   4234   8400    -86     39   -180       C  
HETATM 5842  CAP JLS C 303      18.136  43.947 318.499  1.00 44.79           C  
ANISOU 5842  CAP JLS C 303     4327   4256   8435    -60     77   -157       C  
HETATM 5843  CAQ JLS C 303      18.980  44.672 319.532  1.00 44.15           C  
ANISOU 5843  CAQ JLS C 303     4277   4124   8373   -142     96   -112       C  
HETATM 5844  CAR JLS C 303      18.176  44.981 320.793  1.00 45.19           C  
ANISOU 5844  CAR JLS C 303     4411   4275   8485   -188     86   -148       C  
HETATM 5845  CAS JLS C 303      17.582  46.387 320.813  1.00 47.25           C  
ANISOU 5845  CAS JLS C 303     4742   4521   8691   -118    109   -173       C  
HETATM 5846  CAT JLS C 303      17.224  46.834 322.234  1.00 49.75           C  
ANISOU 5846  CAT JLS C 303     5090   4832   8982   -169    111   -193       C  
HETATM 5847  CAU JLS C 303      15.850  46.315 322.687  1.00 51.90           C  
ANISOU 5847  CAU JLS C 303     5296   5193   9232   -148    119   -254       C  
HETATM 5848  CAV JLS C 303      15.595  46.501 324.186  1.00 51.23           C  
ANISOU 5848  CAV JLS C 303     5242   5106   9116   -212    136   -265       C  
HETATM 5849  CAW JLS C 303      14.863  45.302 324.786  1.00 49.19           C  
ANISOU 5849  CAW JLS C 303     4895   4927   8869   -270    146   -288       C  
HETATM 5850  CAX JLS C 303      14.544  45.535 326.246  1.00 48.38           C  
ANISOU 5850  CAX JLS C 303     4837   4832   8713   -309    183   -303       C  
HETATM 5851  OAA JLS C 303      20.977  35.237 328.760  1.00 30.48           O  
ANISOU 5851  OAA JLS C 303     2679   2216   6684   -906   -292     17       O  
HETATM 5852  C1  JLS C 303      22.173  32.441 330.137  1.00 29.51           C  
ANISOU 5852  C1  JLS C 303     2750   1932   6531   -985   -469     88       C  
HETATM 5853  C1A JLS C 303      22.557  31.064 332.080  1.00 33.49           C  
ANISOU 5853  C1A JLS C 303     3477   2310   6937  -1083   -577    143       C  
HETATM 5854  O1A JLS C 303      21.627  31.837 331.311  1.00 32.45           O  
ANISOU 5854  O1A JLS C 303     3242   2264   6825  -1079   -473    105       O  
HETATM 5855  C2  JLS C 303      21.132  32.433 329.017  1.00 25.86           C  
ANISOU 5855  C2  JLS C 303     2212   1529   6087   -969   -396     48       C  
HETATM 5856  C2A JLS C 303      21.776  30.097 332.985  1.00 34.35           C  
ANISOU 5856  C2A JLS C 303     3728   2364   6960  -1183   -569    163       C  
HETATM 5857  N2  JLS C 303      20.023  33.297 329.430  1.00 24.73           N  
ANISOU 5857  N2  JLS C 303     2047   1446   5902  -1016   -310     24       N  
HETATM 5858  O2A JLS C 303      20.784  29.416 332.215  1.00 35.53           O  
ANISOU 5858  O2A JLS C 303     3846   2530   7124  -1217   -516    144       O  
HETATM 5859  C3  JLS C 303      20.618  31.015 328.730  1.00 25.57           C  
ANISOU 5859  C3  JLS C 303     2224   1452   6040  -1007   -420     44       C  
HETATM 5860  C3A JLS C 303      21.062  30.817 334.138  1.00 33.70           C  
ANISOU 5860  C3A JLS C 303     3711   2303   6788  -1263   -497    166       C  
HETATM 5861  O3  JLS C 303      21.682  30.100 328.435  1.00 26.50           O  
ANISOU 5861  O3  JLS C 303     2382   1501   6185   -945   -506     64       O  
HETATM 5862  O3A JLS C 303      20.408  29.873 335.001  1.00 32.13           O  
ANISOU 5862  O3A JLS C 303     3653   2051   6504  -1362   -478    196       O  
HETATM 5863  C4  JLS C 303      19.521  30.931 327.670  1.00 24.84           C  
ANISOU 5863  C4  JLS C 303     2060   1430   5948   -981   -367      1       C  
HETATM 5864  C4A JLS C 303      21.940  31.856 334.866  1.00 34.94           C  
ANISOU 5864  C4A JLS C 303     3897   2449   6928  -1230   -552    174       C  
HETATM 5865  O4  JLS C 303      19.039  29.579 327.646  1.00 27.19           O  
ANISOU 5865  O4  JLS C 303     2425   1659   6248  -1074   -402      0       O  
HETATM 5866  O4A JLS C 303      22.954  31.215 335.653  1.00 36.44           O  
ANISOU 5866  O4A JLS C 303     4207   2547   7089  -1224   -679    211       O  
HETATM 5867  C5  JLS C 303      19.915  31.394 326.263  1.00 23.67           C  
ANISOU 5867  C5  JLS C 303     1832   1373   5787   -769   -359    -17       C  
HETATM 5868  C5M JLS C 303      22.606  32.745 333.806  1.00 34.82           C  
ANISOU 5868  C5M JLS C 303     3730   2486   7014  -1142   -565    151       C  
HETATM 5869  O6A JLS C 303      24.178  34.476 333.217  1.00 33.55           O  
ANISOU 5869  O6A JLS C 303     3428   2363   6957  -1055   -614    141       O  
HETATM 5870  C6  JLS C 303      18.872  31.081 325.185  1.00 23.50           C  
ANISOU 5870  C6  JLS C 303     1772   1387   5768   -746   -343    -61       C  
HETATM 5871  C6A JLS C 303      23.525  33.847 334.325  1.00 35.29           C  
ANISOU 5871  C6A JLS C 303     3794   2533   7081  -1120   -629    156       C  
HETATM 5872  O5A JLS C 303      23.368  31.933 332.891  1.00 34.48           O  
ANISOU 5872  O5A JLS C 303     3623   2425   7052  -1074   -626    158       O  
HETATM 5873  C7  JLS C 303      17.489  31.692 325.441  1.00 23.37           C  
ANISOU 5873  C7  JLS C 303     1707   1456   5717   -774   -273    -91       C  
HETATM 5874  C8  JLS C 303      16.551  31.542 324.246  1.00 22.76           C  
ANISOU 5874  C8  JLS C 303     1579   1424   5644   -714   -274   -139       C  
HETATM 5875  C9  JLS C 303      15.745  30.249 324.321  1.00 22.36           C  
ANISOU 5875  C9  JLS C 303     1568   1376   5552   -757   -304   -144       C  
HETATM 5876  C10 JLS C 303      15.091  29.921 322.987  1.00 21.95           C  
ANISOU 5876  C10 JLS C 303     1487   1332   5521   -704   -348   -190       C  
HETATM 5877  C11 JLS C 303      15.929  28.901 322.228  1.00 21.95           C  
ANISOU 5877  C11 JLS C 303     1561   1244   5535   -680   -433   -183       C  
HETATM 5878  C12 JLS C 303      15.112  27.675 321.829  1.00 22.61           C  
ANISOU 5878  C12 JLS C 303     1675   1274   5642   -783   -505   -216       C  
HETATM 5879  C13 JLS C 303      15.652  27.067 320.539  1.00 23.26           C  
ANISOU 5879  C13 JLS C 303     1813   1251   5775   -755   -593   -256       C  
HETATM 5880  C14 JLS C 303      16.623  25.922 320.798  1.00 25.01           C  
ANISOU 5880  C14 JLS C 303     2177   1272   6054   -868   -668   -246       C  
HETATM 5881  C15 JLS C 303      16.411  24.800 319.785  1.00 29.43           C  
ANISOU 5881  C15 JLS C 303     2838   1745   6600   -844   -768   -290       C  
HETATM 5882  C16 JLS C 303      17.734  24.380 319.149  1.00 30.89           C  
ANISOU 5882  C16 JLS C 303     3125   1854   6756   -678   -799   -283       C  
HETATM 5883  C17 JLS C 303      17.523  23.459 317.951  1.00 32.00           C  
ANISOU 5883  C17 JLS C 303     3380   1912   6867   -619   -895   -338       C  
HETATM 5884  C18 JLS C 303      18.854  22.887 317.517  1.00 32.83           C  
ANISOU 5884  C18 JLS C 303     3588   1949   6939   -439   -909   -329       C  
HETATM 5885  O   HOH C 401      24.598  28.274 328.651  1.00 14.00           O  
HETATM 5886  O   HOH C 402      19.355  25.454 329.902  1.00 18.74           O  
HETATM 5887  O   HOH D 101      24.305  30.700 297.362  1.00 11.65           O  
CONECT  129  657                                                                
CONECT  657  129                                                                
CONECT 1413 1939                                                                
CONECT 1939 1413                                                                
CONECT 3029 5799                                                                
CONECT 3208 5813                                                                
CONECT 3699 4194                                                                
CONECT 4194 3699                                                                
CONECT 5213 5652                                                                
CONECT 5652 5213                                                                
CONECT 5799 3029 5800 5810                                                      
CONECT 5800 5799 5801 5807                                                      
CONECT 5801 5800 5802 5808                                                      
CONECT 5802 5801 5803 5809                                                      
CONECT 5803 5802 5804 5810                                                      
CONECT 5804 5803 5811                                                           
CONECT 5805 5806 5807 5812                                                      
CONECT 5806 5805                                                                
CONECT 5807 5800 5805                                                           
CONECT 5808 5801                                                                
CONECT 5809 5802                                                                
CONECT 5810 5799 5803                                                           
CONECT 5811 5804                                                                
CONECT 5812 5805                                                                
CONECT 5813 3208 5814 5824                                                      
CONECT 5814 5813 5815 5821                                                      
CONECT 5815 5814 5816 5822                                                      
CONECT 5816 5815 5817 5823                                                      
CONECT 5817 5816 5818 5824                                                      
CONECT 5818 5817 5825                                                           
CONECT 5819 5820 5821 5826                                                      
CONECT 5820 5819                                                                
CONECT 5821 5814 5819                                                           
CONECT 5822 5815                                                                
CONECT 5823 5816                                                                
CONECT 5824 5813 5817                                                           
CONECT 5825 5818                                                                
CONECT 5826 5819                                                                
CONECT 5827 5828 5851 5857                                                      
CONECT 5828 5827 5829                                                           
CONECT 5829 5828 5830                                                           
CONECT 5830 5829 5831                                                           
CONECT 5831 5830 5832                                                           
CONECT 5832 5831 5833                                                           
CONECT 5833 5832 5834                                                           
CONECT 5834 5833 5835                                                           
CONECT 5835 5834 5836                                                           
CONECT 5836 5835 5837                                                           
CONECT 5837 5836 5838                                                           
CONECT 5838 5837 5839                                                           
CONECT 5839 5838 5840                                                           
CONECT 5840 5839 5841                                                           
CONECT 5841 5840 5842                                                           
CONECT 5842 5841 5843                                                           
CONECT 5843 5842 5844                                                           
CONECT 5844 5843 5845                                                           
CONECT 5845 5844 5846                                                           
CONECT 5846 5845 5847                                                           
CONECT 5847 5846 5848                                                           
CONECT 5848 5847 5849                                                           
CONECT 5849 5848 5850                                                           
CONECT 5850 5849                                                                
CONECT 5851 5827                                                                
CONECT 5852 5854 5855                                                           
CONECT 5853 5854 5856 5872                                                      
CONECT 5854 5852 5853                                                           
CONECT 5855 5852 5857 5859                                                      
CONECT 5856 5853 5858 5860                                                      
CONECT 5857 5827 5855                                                           
CONECT 5858 5856                                                                
CONECT 5859 5855 5861 5863                                                      
CONECT 5860 5856 5862 5864                                                      
CONECT 5861 5859                                                                
CONECT 5862 5860                                                                
CONECT 5863 5859 5865 5867                                                      
CONECT 5864 5860 5866 5868                                                      
CONECT 5865 5863                                                                
CONECT 5866 5864                                                                
CONECT 5867 5863 5870                                                           
CONECT 5868 5864 5871 5872                                                      
CONECT 5869 5871                                                                
CONECT 5870 5867 5873                                                           
CONECT 5871 5868 5869                                                           
CONECT 5872 5853 5868                                                           
CONECT 5873 5870 5874                                                           
CONECT 5874 5873 5875                                                           
CONECT 5875 5874 5876                                                           
CONECT 5876 5875 5877                                                           
CONECT 5877 5876 5878                                                           
CONECT 5878 5877 5879                                                           
CONECT 5879 5878 5880                                                           
CONECT 5880 5879 5881                                                           
CONECT 5881 5880 5882                                                           
CONECT 5882 5881 5883                                                           
CONECT 5883 5882 5884                                                           
CONECT 5884 5883                                                                
MASTER      527    0    3   12   68    0    0    6 5883    4   96   68          
END

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Related entries of code: 4wwk

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
5whk	RCSB PDB PDBbind	119aa, >5WHK_4\|Chain... at 100%
6o9c	RCSB PDB PDBbind	119aa, >6O9C_2\|Chain... at 100%
6o9b	RCSB PDB PDBbind	119aa, >6O9B_2\|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
4ww2	RCSB PDB PDBbind	CD1d-alpha-GalCer

Entry Information

PDB ID	4wwk
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	9B2 TCR
Ligand Name	CD1d-alpha-GalCer
EC.Number	E.C.-.-.-.-
Resolution	3.1(Å)
Affinity (Kd/Ki/IC50)	Kd=4.0uM
Release Year	2016
Protein/NA Sequence	Check fasta file
Primary Reference	(2016) Nat Commun Vol. 7: pp. 10570-10570

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): A0A0K0K1A5 P15813 A0A0B4J271 P01848 A0A5B9 P61769
Entrez Gene ID	NCBI Entrez Gene ID: 912 567
ASD	Information of known allosteric effects of PDB entries

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