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HEADER    HYDROLASE/IMMUNE SYSTEM                 29-JUN-10   3NPS              
TITLE     CRYSTAL STRUCTURE OF MEMBRANE-TYPE SERINE PROTEASE 1 (MT-SP1) IN      
TITLE    2 COMPLEX WITH THE FAB INHIBITOR S4                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF TUMORIGENICITY 14 PROTEIN;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PEPTIDASE S1 DOMAIN (UNP RESIDUES 615-855);                
COMPND   5 SYNONYM: SERINE PROTEASE 14, MATRIPTASE, MEMBRANE-TYPE SERINE        
COMPND   6 PROTEASE 1, MT-SP1, PROSTAMIN, SERINE PROTEASE TADG-15, TUMOR-       
COMPND   7 ASSOCIATED DIFFERENTIALLY-EXPRESSED GENE 15 PROTEIN;                 
COMPND   8 EC: 3.4.21.109;                                                      
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: S4 FAB HEAVY CHAIN;                                        
COMPND  13 CHAIN: B;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: S4 FAB LIGHT CHAIN;                                        
COMPND  17 CHAIN: C;                                                            
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRSS14, SNC19, ST14, TADG15;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE30;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PMX7FH;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  26 EXPRESSION_SYSTEM_PLASMID: PMX7FH                                    
KEYWDS    HYDROLASE, ANTIBODY-PROTEASE COMPLEX, PROTEIN-PROTEIN COMPLEX,        
KEYWDS   2 ENZYME-INHIBITOR COMPLEX, DISEASE MUTATION, GLYCOPROTEIN, MEMBRANE,  
KEYWDS   3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE, HYDROLASE - IMMUNE    
KEYWDS   4 SYSTEM COMPLEX, HYDROLASE-IMMUNE SYSTEM COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BAHARUDDIN                                                          
REVDAT   5   08-NOV-17 3NPS    1       REMARK                                   
REVDAT   4   29-FEB-12 3NPS    1       JRNL                                     
REVDAT   3   21-DEC-11 3NPS    1                                                
REVDAT   2   07-DEC-11 3NPS    1       VERSN                                    
REVDAT   1   06-JUL-11 3NPS    0                                                
JRNL        AUTH   E.L.SCHNEIDER,M.S.LEE,A.BAHARUDDIN,D.H.GOETZ,C.J.FARADY,     
JRNL        AUTH 2 M.WARD,C.I.WANG,C.S.CRAIK                                    
JRNL        TITL   A REVERSE BINDING MOTIF THAT CONTRIBUTES TO SPECIFIC         
JRNL        TITL 2 PROTEASE INHIBITION BY ANTIBODIES.                           
JRNL        REF    J.MOL.BIOL.                   V. 415   699 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22154938                                                     
JRNL        DOI    10.1016/J.JMB.2011.11.036                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 88531                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4447                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6314                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 331                          
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5157                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 676                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.098         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.661         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5449 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7437 ; 1.606 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   727 ; 6.638 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   220 ;37.266 ;24.045       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   868 ;13.609 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;13.004 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   825 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4146 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3438 ; 0.952 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5580 ; 1.632 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2011 ; 2.452 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1831 ; 3.758 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    16        A   244                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.3462  27.2210  76.4011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0302 T22:   0.0162                                     
REMARK   3      T33:   0.0103 T12:  -0.0185                                     
REMARK   3      T13:   0.0039 T23:  -0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3799 L22:   0.3708                                     
REMARK   3      L33:   0.3744 L12:   0.0578                                     
REMARK   3      L13:  -0.1043 L23:  -0.0202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0337 S12:   0.0387 S13:  -0.0292                       
REMARK   3      S21:   0.0361 S22:   0.0160 S23:  -0.0066                       
REMARK   3      S31:   0.0447 S32:  -0.0377 S33:   0.0177                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): -60.7125  33.2225  32.7444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0448 T22:   0.0155                                     
REMARK   3      T33:   0.0191 T12:   0.0115                                     
REMARK   3      T13:  -0.0026 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2208 L22:   0.1784                                     
REMARK   3      L33:   0.4099 L12:   0.1253                                     
REMARK   3      L13:   0.1431 L23:   0.2617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:  -0.0200 S13:   0.0265                       
REMARK   3      S21:  -0.0352 S22:  -0.0165 S23:   0.0230                       
REMARK   3      S31:  -0.0655 S32:  -0.0366 S33:   0.0205                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   212                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.6826  19.1915  26.6593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0349 T22:   0.0175                                     
REMARK   3      T33:   0.0160 T12:   0.0000                                     
REMARK   3      T13:  -0.0043 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2307 L22:   0.0145                                     
REMARK   3      L33:   0.4091 L12:   0.0037                                     
REMARK   3      L13:   0.2140 L23:   0.0580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:   0.0338 S13:   0.0224                       
REMARK   3      S21:  -0.0047 S22:   0.0005 S23:  -0.0085                       
REMARK   3      S31:  -0.0219 S32:   0.0334 S33:  -0.0079                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY           
REMARK   4                                                                      
REMARK   4 3NPS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060127.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : KOHZU DOUBLE CRYSTAL SI (111)      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88531                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.393                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.5                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: PDB ENTRIES: 3BN9, 2JB5, 3KDM                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS, 100 MM NACL, 5% GLYCEROL,    
REMARK 280  NO BUFFER WAS ADDED FOR CRYSTALLIZATION, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.99400            
REMARK 290   SMTRY3   2  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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A    90     O    HOH A   350              1.87            
REMARK 500   O    HOH B   356     O    HOH C   357              2.08            
REMARK 500   O    HOH C   522     O    HOH C   533              2.09            
REMARK 500   O    HOH C   249     O    HOH C   673              2.14            
REMARK 500   O    HOH A   625     O    HOH B   358              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A    84     O    HOH B   234     2246     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A  42   CA  -  CB  -  SG  ANGL. DEV. =  11.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    SER B  30     -136.93     49.95                                   
REMARK 500    SER B  31       38.57    -98.72                                   
REMARK 500    SER B  76       53.48     33.69                                   
REMARK 500    SER B  76       48.99     39.11                                   
REMARK 500    TYR B 100E     -28.86   -153.14                                   
REMARK 500    ASN C  27B     -94.57   -109.65                                   
REMARK 500    ASN C  51      -47.79     77.63                                   
REMARK 500    ASN C  52       12.07   -144.80                                   
REMARK 500    ILE C  93      -92.31     57.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 213  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C 177   OG                                                     
REMARK 620 2 GLU C 161   OE2 110.9                                              
REMARK 620 3 HOH C 524   O    98.9  97.9                                        
REMARK 620 4 VAL C 146   O   131.8  94.1 118.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 245                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 246                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 213                  
DBREF  3NPS A   16   244  UNP    Q9Y5Y6   ST14_HUMAN     615    855             
DBREF  3NPS B    1   214  PDB    3NPS     3NPS             1    214             
DBREF  3NPS C    3   212  PDB    3NPS     3NPS             3    212             
SEQADV 3NPS SER A  122  UNP  Q9Y5Y6    CYS   731 ENGINEERED MUTATION            
SEQRES   1 A  241  VAL VAL GLY GLY THR ASP ALA ASP GLU GLY GLU TRP PRO          
SEQRES   2 A  241  TRP GLN VAL SER LEU HIS ALA LEU GLY GLN GLY HIS ILE          
SEQRES   3 A  241  CYS GLY ALA SER LEU ILE SER PRO ASN TRP LEU VAL SER          
SEQRES   4 A  241  ALA ALA HIS CYS TYR ILE ASP ASP ARG GLY PHE ARG TYR          
SEQRES   5 A  241  SER ASP PRO THR GLN TRP THR ALA PHE LEU GLY LEU HIS          
SEQRES   6 A  241  ASP GLN SER GLN ARG SER ALA PRO GLY VAL GLN GLU ARG          
SEQRES   7 A  241  ARG LEU LYS ARG ILE ILE SER HIS PRO PHE PHE ASN ASP          
SEQRES   8 A  241  PHE THR PHE ASP TYR ASP ILE ALA LEU LEU GLU LEU GLU          
SEQRES   9 A  241  LYS PRO ALA GLU TYR SER SER MET VAL ARG PRO ILE SER          
SEQRES  10 A  241  LEU PRO ASP ALA SER HIS VAL PHE PRO ALA GLY LYS ALA          
SEQRES  11 A  241  ILE TRP VAL THR GLY TRP GLY HIS THR GLN TYR GLY GLY          
SEQRES  12 A  241  THR GLY ALA LEU ILE LEU GLN LYS GLY GLU ILE ARG VAL          
SEQRES  13 A  241  ILE ASN GLN THR THR CYS GLU ASN LEU LEU PRO GLN GLN          
SEQRES  14 A  241  ILE THR PRO ARG MET MET CYS VAL GLY PHE LEU SER GLY          
SEQRES  15 A  241  GLY VAL ASP SER CYS GLN GLY ASP SER GLY GLY PRO LEU          
SEQRES  16 A  241  SER SER VAL GLU ALA ASP GLY ARG ILE PHE GLN ALA GLY          
SEQRES  17 A  241  VAL VAL SER TRP GLY ASP GLY CYS ALA GLN ARG ASN LYS          
SEQRES  18 A  241  PRO GLY VAL TYR THR ARG LEU PRO LEU PHE ARG ASP TRP          
SEQRES  19 A  241  ILE LYS GLU ASN THR GLY VAL                                  
SEQRES   1 B  226  GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 B  226  PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 B  226  GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN          
SEQRES   4 B  226  ALA GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE PRO          
SEQRES   5 B  226  ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN GLY          
SEQRES   6 B  226  ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR ALA          
SEQRES   7 B  226  TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR ALA          
SEQRES   8 B  226  VAL TYR TYR CYS ALA ARG THR PHE HIS ILE ARG ARG TYR          
SEQRES   9 B  226  ARG SER GLY TYR TYR ASP LYS MET ASP HIS TRP GLY GLN          
SEQRES  10 B  226  GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY          
SEQRES  11 B  226  PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR          
SEQRES  12 B  226  SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP          
SEQRES  13 B  226  TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY          
SEQRES  14 B  226  ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU          
SEQRES  15 B  226  GLU SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR          
SEQRES  16 B  226  VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS          
SEQRES  17 B  226  ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS          
SEQRES  18 B  226  LYS VAL GLU PRO LYS                                          
SEQRES   1 C  211  VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA PRO GLY          
SEQRES   2 C  211  GLN ARG VAL THR ILE SER CYS SER GLY SER SER SER ASN          
SEQRES   3 C  211  ILE GLY SER ASN TYR VAL SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 C  211  GLY THR ALA PRO LYS LEU LEU ILE TYR ASP ASN ASN GLN          
SEQRES   5 C  211  ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SER LYS          
SEQRES   6 C  211  SER GLY THR SER ALA VAL LEU ALA ILE THR GLY LEU GLN          
SEQRES   7 C  211  SER GLU ASP GLU ALA ASP TYR TYR CYS GLN SER ARG ASP          
SEQRES   8 C  211  ILE SER GLN TYR VAL PHE GLY GLY GLY THR LYS LEU THR          
SEQRES   9 C  211  VAL LEU ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE          
SEQRES  10 C  211  PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER          
SEQRES  11 C  211  VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA          
SEQRES  12 C  211  LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY          
SEQRES  13 C  211  ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP          
SEQRES  14 C  211  SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS          
SEQRES  15 C  211  ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL          
SEQRES  16 C  211  THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE          
SEQRES  17 C  211  ASN ARG GLY                                                  
HET    EDO  A   1       4                                                       
HET    EDO  A   2       4                                                       
HET    EDO  A   3       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   6       4                                                       
HET    EDO  A   7       4                                                       
HET     NA  A 245       1                                                       
HET     NA  A 246       1                                                       
HET     CL  A 247       1                                                       
HET    EDO  B 215       4                                                       
HET    EDO  B 216       4                                                       
HET    EDO  B 217       4                                                       
HET     NA  B 218       1                                                       
HET     NA  B 219       1                                                       
HET    EDO  C  10       4                                                       
HET     NA  C 213       1                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   4  EDO    10(C2 H6 O2)                                                 
FORMUL  10   NA    5(NA 1+)                                                     
FORMUL  12   CL    CL 1-                                                        
FORMUL  20  HOH   *676(H2 O)                                                    
HELIX    1   1 ALA A   55  ILE A   60  5                                   6    
HELIX    2   2 ASP A   60I THR A   62  5                                   3    
HELIX    3   3 ASN A  164  LEU A  172  1                                   9    
HELIX    4   4 PHE A  234  GLY A  243  1                                  10    
HELIX    5   5 GLN B   61  GLN B   64  5                                   4    
HELIX    6   6 GLU B   73  THR B   75  5                                   3    
HELIX    7   7 ARG B   83  THR B   87  5                                   5    
HELIX    8   8 SER B  156  ALA B  158  5                                   3    
HELIX    9   9 SER B  187  LEU B  189  5                                   3    
HELIX   10  10 LYS B  201  ASN B  204  5                                   4    
HELIX   11  11 ASN C   27B ASN C   31  5                                   5    
HELIX   12  12 GLN C   79  GLU C   83  5                                   5    
HELIX   13  13 SER C  121  GLY C  128  1                                   8    
HELIX   14  14 LYS C  183  GLU C  187  1                                   5    
SHEET    1   A 8 THR A  20  ASP A  21  0                                        
SHEET    2   A 8 GLN A 156  VAL A 162 -1  O  LYS A 157   N  THR A  20           
SHEET    3   A 8 MET A 180  GLY A 184 -1  O  GLY A 184   N  ARG A 161           
SHEET    4   A 8 GLY A 226  ARG A 230 -1  O  TYR A 228   N  MET A 181           
SHEET    5   A 8 ILE A 207  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    6   A 8 PRO A 198  VAL A 202 -1  N  SER A 201   O  PHE A 208           
SHEET    7   A 8 ALA A 135  GLY A 140 -1  N  TRP A 137   O  SER A 200           
SHEET    8   A 8 GLN A 156  VAL A 162 -1  O  ILE A 160   N  ILE A 136           
SHEET    1   B 7 GLN A  30  ALA A  35  0                                        
SHEET    2   B 7 GLY A  39  LEU A  46 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 ALA A 104  LEU A 108 -1  O  ALA A 104   N  SER A  54           
SHEET    5   B 7 GLN A  81  SER A  90 -1  N  LYS A  86   O  GLU A 107           
SHEET    6   B 7 TRP A  64  LEU A  68 -1  N  LEU A  68   O  GLN A  81           
SHEET    7   B 7 GLN A  30  ALA A  35 -1  N  HIS A  34   O  THR A  65           
SHEET    1   C 4 LEU B   4  GLN B   6  0                                        
SHEET    2   C 4 VAL B  18  ALA B  24 -1  O  LYS B  23   N  VAL B   5           
SHEET    3   C 4 THR B  77  LEU B  82 -1  O  ALA B  78   N  CYS B  22           
SHEET    4   C 4 VAL B  67  ASP B  72 -1  N  THR B  70   O  TYR B  79           
SHEET    1   D 6 GLU B  10  LYS B  12  0                                        
SHEET    2   D 6 THR B 107  VAL B 111  1  O  THR B 110   N  GLU B  10           
SHEET    3   D 6 ALA B  88  HIS B  97 -1  N  TYR B  90   O  THR B 107           
SHEET    4   D 6 TYR B  32  GLN B  39 -1  N  VAL B  37   O  TYR B  91           
SHEET    5   D 6 LEU B  45  ILE B  51 -1  O  GLY B  49   N  TRP B  36           
SHEET    6   D 6 ASN B  58  TYR B  59 -1  O  ASN B  58   N  GLY B  50           
SHEET    1   E 4 GLU B  10  LYS B  12  0                                        
SHEET    2   E 4 THR B 107  VAL B 111  1  O  THR B 110   N  GLU B  10           
SHEET    3   E 4 ALA B  88  HIS B  97 -1  N  TYR B  90   O  THR B 107           
SHEET    4   E 4 MET B 100I TRP B 103 -1  O  HIS B 102   N  ARG B  94           
SHEET    1   F 4 SER B 120  LEU B 124  0                                        
SHEET    2   F 4 THR B 135  TYR B 145 -1  O  GLY B 139   N  LEU B 124           
SHEET    3   F 4 TYR B 176  PRO B 185 -1  O  TYR B 176   N  TYR B 145           
SHEET    4   F 4 VAL B 163  THR B 165 -1  N  HIS B 164   O  VAL B 181           
SHEET    1   G 4 SER B 120  LEU B 124  0                                        
SHEET    2   G 4 THR B 135  TYR B 145 -1  O  GLY B 139   N  LEU B 124           
SHEET    3   G 4 TYR B 176  PRO B 185 -1  O  TYR B 176   N  TYR B 145           
SHEET    4   G 4 VAL B 169  LEU B 170 -1  N  VAL B 169   O  SER B 177           
SHEET    1   H 3 THR B 151  TRP B 154  0                                        
SHEET    2   H 3 TYR B 194  HIS B 200 -1  O  ASN B 197   N  SER B 153           
SHEET    3   H 3 THR B 205  VAL B 211 -1  O  VAL B 207   N  VAL B 198           
SHEET    1   I 5 SER C   9  GLY C  13  0                                        
SHEET    2   I 5 THR C 102  VAL C 106  1  O  THR C 105   N  VAL C  11           
SHEET    3   I 5 ALA C  84  ASP C  92 -1  N  ALA C  84   O  LEU C 104           
SHEET    4   I 5 VAL C  33  GLN C  38 -1  N  GLN C  38   O  ASP C  85           
SHEET    5   I 5 LYS C  45  ILE C  48 -1  O  LEU C  47   N  TRP C  35           
SHEET    1   J 4 SER C   9  GLY C  13  0                                        
SHEET    2   J 4 THR C 102  VAL C 106  1  O  THR C 105   N  VAL C  11           
SHEET    3   J 4 ALA C  84  ASP C  92 -1  N  ALA C  84   O  LEU C 104           
SHEET    4   J 4 GLN C  95  PHE C  98 -1  O  GLN C  95   N  ASP C  92           
SHEET    1   K 3 ARG C  18  SER C  24  0                                        
SHEET    2   K 3 SER C  70  THR C  76 -1  O  ILE C  75   N  VAL C  19           
SHEET    3   K 3 PHE C  62  SER C  67 -1  N  SER C  63   O  ALA C  74           
SHEET    1   L 4 SER C 114  PHE C 118  0                                        
SHEET    2   L 4 THR C 129  PHE C 139 -1  O  LEU C 135   N  PHE C 116           
SHEET    3   L 4 TYR C 173  SER C 182 -1  O  LEU C 179   N  VAL C 132           
SHEET    4   L 4 SER C 159  VAL C 163 -1  N  GLN C 160   O  THR C 178           
SHEET    1   M 4 ALA C 153  LEU C 154  0                                        
SHEET    2   M 4 LYS C 145  VAL C 150 -1  N  VAL C 150   O  ALA C 153           
SHEET    3   M 4 VAL C 191  THR C 197 -1  O  GLU C 195   N  GLN C 147           
SHEET    4   M 4 VAL C 205  ASN C 210 -1  O  VAL C 205   N  VAL C 196           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.06  
SSBOND   2 CYS A  168    CYS A  182                          1555   1555  2.07  
SSBOND   3 CYS A  191    CYS A  220                          1555   1555  2.06  
SSBOND   4 CYS B   22    CYS B   92                          1555   1555  2.04  
SSBOND   5 CYS B  140    CYS B  196                          1555   1555  2.05  
SSBOND   6 CYS C   23    CYS C   88                          1555   1555  2.07  
SSBOND   7 CYS C  134    CYS C  194                          1555   1555  2.07  
LINK         OG  SER C 177                NA    NA C 213     1555   1555  2.58  
LINK         OE2 GLU C 161                NA    NA C 213     1555   1555  2.70  
LINK        NA    NA C 213                 O   HOH C 524     1555   1555  2.80  
LINK         O   VAL C 146                NA    NA C 213     1555   1555  3.09  
CISPEP   1 PHE B  146    PRO B  147          0        -3.92                     
CISPEP   2 GLU B  148    PRO B  149          0        -1.15                     
CISPEP   3 TYR C  140    PRO C  141          0         2.95                     
SITE     1 AC1  5 PHE A 130  ALA A 132  ILE A 163  GLN A 165                    
SITE     2 AC1  5 ARG A 230                                                     
SITE     1 AC2  3 GLU A  26  TRP A  27  HOH A 649                               
SITE     1 AC3 10 ASP A  23  GLU A  24  GLY A  25  GLU A  26                    
SITE     2 AC3 10 TRP A  27  PRO A  28  LEU A  70  HIS A  71                    
SITE     3 AC3 10 LEU A 155  HOH A 384                                          
SITE     1 AC4  5 HIS A 143  HOH A 382  GLN C  53  HOH C 360                    
SITE     2 AC4  5 HOH C 479                                                     
SITE     1 AC5  5 HIS A  91  PHE A  93  PHE A 234  TRP A 237                    
SITE     2 AC5  5 HOH A 468                                                     
SITE     1 AC6  5 HIS A  57  CYS A  58  ILE A  60  TYR A  60G                   
SITE     2 AC6  5 ARG B 100                                                     
SITE     1 AC7  2 ILE A  88  SER A  90                                          
SITE     1 AC8  2 TRP A 141  GLY A 193                                          
SITE     1 AC9  5 GLY B 100D TYR B 100E TYR B 100F HOH B 294                    
SITE     2 AC9  5 TYR C  96                                                     
SITE     1 BC1  3 LYS B  19  SER B  21  TYR B  79                               
SITE     1 BC2  5 HOH B 318  THR C   5  GLN C   6  PRO C   7                    
SITE     2 BC2  5 HOH C 395                                                     
SITE     1 BC3  6 THR B 191  PRO C 141  GLN C 199  HOH C 263                    
SITE     2 BC3  6 HOH C 264  HOH C 537                                          
SITE     1 BC4  4 VAL C 146  GLU C 161  SER C 177  HOH C 524                    
CRYST1   39.161   83.988  101.394  90.00  91.45  90.00 P 1 21 1      2          
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      0.025536  0.000000  0.000646        0.00000                         
SCALE2      0.000000  0.011906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009866        0.00000                         
ATOM      1  N   VAL A  16     -37.593  23.779  68.997  1.00 16.03           N  
ANISOU    1  N   VAL A  16     2090   2005   1996   -195    104   -145       N  
ATOM      2  CA  VAL A  16     -36.506  24.680  69.506  1.00 15.98           C  
ANISOU    2  CA  VAL A  16     2070   1996   2005   -177     89   -128       C  
ATOM      3  C   VAL A  16     -35.282  24.637  68.570  1.00 17.19           C  
ANISOU    3  C   VAL A  16     2208   2156   2168   -174    104   -136       C  
ATOM      4  O   VAL A  16     -34.744  23.558  68.297  1.00 17.90           O  
ANISOU    4  O   VAL A  16     2299   2231   2270   -168    123   -152       O  
ATOM      5  CB  VAL A  16     -36.098  24.297  70.937  1.00 16.03           C  
ANISOU    5  CB  VAL A  16     2085   1975   2031   -156     78   -117       C  
ATOM      6  CG1 VAL A  16     -34.987  25.179  71.451  1.00 17.41           C  
ANISOU    6  CG1 VAL A  16     2244   2150   2220   -141     60   -102       C  
ATOM      7  CG2 VAL A  16     -37.314  24.295  71.886  1.00 16.09           C  
ANISOU    7  CG2 VAL A  16     2110   1976   2027   -160     67   -110       C  
ATOM      8  N   VAL A  17     -34.895  25.803  68.060  1.00 17.22           N  
ANISOU    8  N   VAL A  17     2195   2180   2166   -179     98   -126       N  
ATOM      9  CA  VAL A  17     -33.709  25.945  67.168  1.00 18.85           C  
ANISOU    9  CA  VAL A  17     2384   2397   2381   -178    113   -131       C  
ATOM     10  C   VAL A  17     -32.499  26.283  68.037  1.00 19.29           C  
ANISOU   10  C   VAL A  17     2424   2438   2465   -158    100   -118       C  
ATOM     11  O   VAL A  17     -32.619  27.109  68.945  1.00 19.03           O  
ANISOU   11  O   VAL A  17     2392   2403   2436   -154     76   -101       O  
ATOM     12  CB  VAL A  17     -33.944  27.043  66.123  1.00 18.13           C  
ANISOU   12  CB  VAL A  17     2285   2337   2268   -196    113   -123       C  
ATOM     13  CG1 VAL A  17     -32.711  27.178  65.211  1.00 17.05           C  
ANISOU   13  CG1 VAL A  17     2129   2210   2139   -197    132   -128       C  
ATOM     14  CG2 VAL A  17     -35.182  26.677  65.286  1.00 20.24           C  
ANISOU   14  CG2 VAL A  17     2564   2621   2504   -216    122   -135       C  
ATOM     15  N   GLY A  18     -31.350  25.666  67.760  1.00 19.19           N  
ANISOU   15  N   GLY A  18     2397   2419   2474   -146    116   -127       N  
ATOM     16  CA  GLY A  18     -30.119  25.979  68.492  1.00 19.84           C  
ANISOU   16  CA  GLY A  18     2460   2493   2586   -128    103   -115       C  
ATOM     17  C   GLY A  18     -30.093  25.431  69.888  1.00 20.72           C  
ANISOU   17  C   GLY A  18     2581   2580   2712   -108     83   -108       C  
ATOM     18  O   GLY A  18     -29.321  25.871  70.718  1.00 22.27           O  
ANISOU   18  O   GLY A  18     2763   2773   2926    -96     63    -95       O  
ATOM     19  N   GLY A  19     -30.912  24.418  70.137  1.00 19.31           N  
ANISOU   19  N   GLY A  19     2425   2385   2526   -106     91   -116       N  
ATOM     20  CA  GLY A  19     -30.897  23.773  71.443  1.00 20.44           C  
ANISOU   20  CA  GLY A  19     2581   2504   2683    -86     75   -107       C  
ATOM     21  C   GLY A  19     -30.208  22.417  71.427  1.00 20.53           C  
ANISOU   21  C   GLY A  19     2592   2492   2718    -66     94   -116       C  
ATOM     22  O   GLY A  19     -29.314  22.133  70.585  1.00 21.83           O  
ANISOU   22  O   GLY A  19     2736   2660   2898    -60    114   -127       O  
ATOM     23  N   THR A  20     -30.578  21.602  72.399  1.00 20.22           N  
ANISOU   23  N   THR A  20     2572   2427   2682    -53     87   -110       N  
ATOM     24  CA  THR A  20     -30.007  20.262  72.517  1.00 21.39           C  
ANISOU   24  CA  THR A  20     2725   2548   2856    -31    103   -115       C  
ATOM     25  C   THR A  20     -31.006  19.338  73.198  1.00 20.49           C  
ANISOU   25  C   THR A  20     2644   2407   2734    -31    106   -113       C  
ATOM     26  O   THR A  20     -31.992  19.802  73.791  1.00 20.69           O  
ANISOU   26  O   THR A  20     2686   2438   2737    -44     91   -105       O  
ATOM     27  CB  THR A  20     -28.642  20.278  73.306  1.00 21.83           C  
ANISOU   27  CB  THR A  20     2756   2597   2941      0     84    -97       C  
ATOM     28  OG1 THR A  20     -28.018  18.981  73.242  1.00 25.53           O  
ANISOU   28  OG1 THR A  20     3225   3038   3437     25    104   -102       O  
ATOM     29  CG2 THR A  20     -28.807  20.655  74.769  1.00 23.40           C  
ANISOU   29  CG2 THR A  20     2965   2792   3133      8     48    -73       C  
ATOM     30  N   ASP A  21     -30.750  18.029  73.152  1.00 20.86           N  
ANISOU   30  N   ASP A  21     2701   2424   2801    -15    127   -120       N  
ATOM     31  CA  ASP A  21     -31.640  17.121  73.811  1.00 20.52           C  
ANISOU   31  CA  ASP A  21     2691   2353   2753    -16    132   -117       C  
ATOM     32  C   ASP A  21     -31.692  17.380  75.324  1.00 20.45           C  
ANISOU   32  C   ASP A  21     2692   2338   2741     -2    100    -88       C  
ATOM     33  O   ASP A  21     -30.655  17.564  75.985  1.00 22.67           O  
ANISOU   33  O   ASP A  21     2956   2618   3038     23     80    -69       O  
ATOM     34  CB  ASP A  21     -31.194  15.653  73.615  1.00 20.85           C  
ANISOU   34  CB  ASP A  21     2743   2356   2823      3    160   -127       C  
ATOM     35  CG  ASP A  21     -31.306  15.143  72.182  1.00 25.21           C  
ANISOU   35  CG  ASP A  21     3296   2908   3376    -14    196   -161       C  
ATOM     36  OD1 ASP A  21     -31.732  15.838  71.262  1.00 26.03           O  
ANISOU   36  OD1 ASP A  21     3392   3042   3457    -40    201   -177       O  
ATOM     37  OD2 ASP A  21     -30.925  13.957  71.956  1.00 30.98           O  
ANISOU   37  OD2 ASP A  21     4036   3604   4130      2    223   -173       O  
ATOM     38  N   ALA A  22     -32.915  17.355  75.855  1.00 19.91           N  
ANISOU   38  N   ALA A  22     2648   2265   2650    -19     97    -84       N  
ATOM     39  CA  ALA A  22     -33.116  17.378  77.304  1.00 21.32           C  
ANISOU   39  CA  ALA A  22     2844   2434   2822     -7     73    -58       C  
ATOM     40  C   ALA A  22     -32.633  16.052  77.863  1.00 23.31           C  
ANISOU   40  C   ALA A  22     3112   2648   3098     19     82    -46       C  
ATOM     41  O   ALA A  22     -32.638  15.039  77.166  1.00 24.78           O  
ANISOU   41  O   ALA A  22     3305   2810   3299     19    111    -62       O  
ATOM     42  CB  ALA A  22     -34.605  17.544  77.634  1.00 21.71           C  
ANISOU   42  CB  ALA A  22     2917   2488   2843    -33     76    -59       C  
ATOM     43  N   ASP A  23     -32.241  16.061  79.144  1.00 24.45           N  
ANISOU   43  N   ASP A  23     3263   2785   3242     41     56    -18       N  
ATOM     44  CA  ASP A  23     -31.977  14.808  79.864  1.00 26.78           C  
ANISOU   44  CA  ASP A  23     3579   3042   3555     66     61      0       C  
ATOM     45  C   ASP A  23     -33.341  14.247  80.218  1.00 26.74           C  
ANISOU   45  C   ASP A  23     3611   3019   3531     44     78      0       C  
ATOM     46  O   ASP A  23     -34.280  15.015  80.439  1.00 26.38           O  
ANISOU   46  O   ASP A  23     3571   2995   3457     20     71     -2       O  
ATOM     47  CB  ASP A  23     -31.192  15.061  81.167  1.00 28.14           C  
ANISOU   47  CB  ASP A  23     3748   3218   3727     93     25     33       C  
ATOM     48  CG  ASP A  23     -29.774  15.571  80.923  1.00 32.66           C  
ANISOU   48  CG  ASP A  23     4280   3809   4320    115      6     36       C  
ATOM     49  OD1 ASP A  23     -29.038  14.984  80.105  1.00 39.78           O  
ANISOU   49  OD1 ASP A  23     5163   4698   5252    130     25     25       O  
ATOM     50  OD2 ASP A  23     -29.395  16.591  81.546  1.00 37.92           O  
ANISOU   50  OD2 ASP A  23     4931   4502   4973    115    -28     47       O  
ATOM     51  N   GLU A  24     -33.484  12.921  80.259  1.00 26.62           N  
ANISOU   51  N   GLU A  24     3619   2962   3533     52    102      2       N  
ATOM     52  CA  GLU A  24     -34.753  12.326  80.670  1.00 26.75           C  
ANISOU   52  CA  GLU A  24     3671   2959   3535     31    119      4       C  
ATOM     53  C   GLU A  24     -35.144  12.767  82.074  1.00 26.63           C  
ANISOU   53  C   GLU A  24     3673   2953   3494     34     93     34       C  
ATOM     54  O   GLU A  24     -34.359  12.618  83.020  1.00 27.00           O  
ANISOU   54  O   GLU A  24     3722   2991   3545     64     72     62       O  
ATOM     55  CB  GLU A  24     -34.680  10.799  80.630  1.00 27.90           C  
ANISOU   55  CB  GLU A  24     3840   3053   3706     43    148      6       C  
ATOM     56  CG  GLU A  24     -34.671  10.191  79.241  1.00 31.06           C  
ANISOU   56  CG  GLU A  24     4235   3440   4128     30    182    -30       C  
ATOM     57  CD  GLU A  24     -35.135   8.740  79.243  1.00 35.12           C  
ANISOU   57  CD  GLU A  24     4784   3901   4660     26    215    -34       C  
ATOM     58  OE1 GLU A  24     -34.812   8.022  78.277  1.00 40.15           O  
ANISOU   58  OE1 GLU A  24     5420   4516   5321     27    244    -60       O  
ATOM     59  OE2 GLU A  24     -35.824   8.331  80.202  1.00 39.46           O  
ANISOU   59  OE2 GLU A  24     5363   4432   5200     21    215    -12       O  
ATOM     60  N   GLY A  25     -36.350  13.312  82.198  1.00 24.90           N  
ANISOU   60  N   GLY A  25     3462   2751   3247      3     96     26       N  
ATOM     61  CA  GLY A  25     -36.852  13.717  83.496  1.00 23.91           C  
ANISOU   61  CA  GLY A  25     3357   2635   3094      3     79     51       C  
ATOM     62  C   GLY A  25     -36.399  15.109  83.916  1.00 23.62           C  
ANISOU   62  C   GLY A  25     3299   2636   3039      9     44     57       C  
ATOM     63  O   GLY A  25     -36.657  15.525  85.054  1.00 23.08           O  
ANISOU   63  O   GLY A  25     3247   2577   2947     11     26     76       O  
ATOM     64  N   GLU A  26     -35.731  15.818  83.017  1.00 22.51           N  
ANISOU   64  N   GLU A  26     3126   2517   2910     10     36     40       N  
ATOM     65  CA  GLU A  26     -35.207  17.157  83.304  1.00 22.20           C  
ANISOU   65  CA  GLU A  26     3066   2512   2858     14      5     43       C  
ATOM     66  C   GLU A  26     -36.291  18.228  83.368  1.00 21.71           C  
ANISOU   66  C   GLU A  26     3006   2475   2767    -13      3     33       C  
ATOM     67  O   GLU A  26     -36.148  19.224  84.070  1.00 21.65           O  
ANISOU   67  O   GLU A  26     2996   2487   2742    -11    -22     41       O  
ATOM     68  CB  GLU A  26     -34.150  17.534  82.255  1.00 22.81           C  
ANISOU   68  CB  GLU A  26     3108   2602   2958     21      1     28       C  
ATOM     69  CG  GLU A  26     -33.314  18.741  82.643  1.00 24.11           C  
ANISOU   69  CG  GLU A  26     3249   2794   3116     29    -33     35       C  
ATOM     70  CD  GLU A  26     -32.220  19.041  81.656  1.00 28.81           C  
ANISOU   70  CD  GLU A  26     3809   3401   3737     36    -34     23       C  
ATOM     71  OE1 GLU A  26     -32.351  18.624  80.489  1.00 23.87           O  
ANISOU   71  OE1 GLU A  26     3175   2770   3125     28     -6      4       O  
ATOM     72  OE2 GLU A  26     -31.227  19.705  82.057  1.00 33.57           O  
ANISOU   72  OE2 GLU A  26     4390   4020   4345     49    -62     32       O  
ATOM     73  N   TRP A  27     -37.387  18.014  82.642  1.00 19.40           N  
ANISOU   73  N   TRP A  27     2719   2182   2471    -37     29     15       N  
ATOM     74  CA  TRP A  27     -38.456  19.010  82.557  1.00 17.31           C  
ANISOU   74  CA  TRP A  27     2451   1943   2184    -61     30      6       C  
ATOM     75  C   TRP A  27     -39.759  18.279  82.777  1.00 17.92           C  
ANISOU   75  C   TRP A  27     2550   2006   2251    -79     55      5       C  
ATOM     76  O   TRP A  27     -40.558  18.145  81.853  1.00 19.13           O  
ANISOU   76  O   TRP A  27     2697   2166   2406   -102     75    -14       O  
ATOM     77  CB  TRP A  27     -38.444  19.659  81.169  1.00 18.36           C  
ANISOU   77  CB  TRP A  27     2555   2097   2323    -75     36    -17       C  
ATOM     78  CG  TRP A  27     -37.081  20.152  80.825  1.00 19.53           C  
ANISOU   78  CG  TRP A  27     2680   2254   2486    -58     18    -16       C  
ATOM     79  CD1 TRP A  27     -36.164  19.515  80.038  1.00 21.26           C  
ANISOU   79  CD1 TRP A  27     2885   2463   2730    -47     27    -24       C  
ATOM     80  CD2 TRP A  27     -36.463  21.362  81.277  1.00 20.39           C  
ANISOU   80  CD2 TRP A  27     2776   2382   2589    -50    -10     -9       C  
ATOM     81  NE1 TRP A  27     -35.003  20.261  79.961  1.00 24.33           N  
ANISOU   81  NE1 TRP A  27     3250   2866   3128    -34      6    -20       N  
ATOM     82  CE2 TRP A  27     -35.161  21.400  80.714  1.00 21.93           C  
ANISOU   82  CE2 TRP A  27     2947   2581   2806    -37    -18    -11       C  
ATOM     83  CE3 TRP A  27     -36.878  22.411  82.106  1.00 24.82           C  
ANISOU   83  CE3 TRP A  27     3343   2958   3128    -55    -27     -2       C  
ATOM     84  CZ2 TRP A  27     -34.282  22.465  80.947  1.00 24.86           C  
ANISOU   84  CZ2 TRP A  27     3298   2968   3178    -30    -43     -7       C  
ATOM     85  CZ3 TRP A  27     -36.015  23.465  82.337  1.00 25.11           C  
ANISOU   85  CZ3 TRP A  27     3365   3011   3166    -48    -53      1       C  
ATOM     86  CH2 TRP A  27     -34.727  23.478  81.768  1.00 24.71           C  
ANISOU   86  CH2 TRP A  27     3288   2962   3137    -37    -62     -1       C  
ATOM     87  N   PRO A  28     -40.000  17.822  84.014  1.00 17.38           N  
ANISOU   87  N   PRO A  28     2511   1923   2172    -72     53     26       N  
ATOM     88  CA  PRO A  28     -41.117  16.872  84.184  1.00 18.16           C  
ANISOU   88  CA  PRO A  28     2632   2002   2267    -90     82     26       C  
ATOM     89  C   PRO A  28     -42.520  17.551  84.168  1.00 17.38           C  
ANISOU   89  C   PRO A  28     2530   1926   2149   -116     92     16       C  
ATOM     90  O   PRO A  28     -43.548  16.882  84.267  1.00 17.84           O  
ANISOU   90  O   PRO A  28     2601   1973   2203   -135    116     14       O  
ATOM     91  CB  PRO A  28     -40.822  16.256  85.548  1.00 18.83           C  
ANISOU   91  CB  PRO A  28     2747   2064   2344    -71     75     55       C  
ATOM     92  CG  PRO A  28     -40.066  17.340  86.268  1.00 19.26           C  
ANISOU   92  CG  PRO A  28     2793   2140   2382    -53     41     66       C  
ATOM     93  CD  PRO A  28     -39.129  17.854  85.215  1.00 18.40           C  
ANISOU   93  CD  PRO A  28     2652   2045   2293    -46     29     51       C  
ATOM     94  N   TRP A  29     -42.544  18.889  84.026  1.00 16.69           N  
ANISOU   94  N   TRP A  29     2423   1870   2050   -117     75     10       N  
ATOM     95  CA  TRP A  29     -43.792  19.637  83.779  1.00 16.87           C  
ANISOU   95  CA  TRP A  29     2434   1916   2058   -138     85     -1       C  
ATOM     96  C   TRP A  29     -44.178  19.787  82.286  1.00 16.64           C  
ANISOU   96  C   TRP A  29     2378   1903   2040   -156     94    -24       C  
ATOM     97  O   TRP A  29     -45.287  20.234  81.973  1.00 17.02           O  
ANISOU   97  O   TRP A  29     2416   1971   2080   -175    103    -33       O  
ATOM     98  CB  TRP A  29     -43.709  21.050  84.392  1.00 17.93           C  
ANISOU   98  CB  TRP A  29     2564   2073   2176   -128     64      3       C  
ATOM     99  CG  TRP A  29     -42.358  21.659  84.206  1.00 20.01           C  
ANISOU   99  CG  TRP A  29     2815   2342   2447   -110     38      4       C  
ATOM    100  CD1 TRP A  29     -41.933  22.479  83.164  1.00 20.49           C  
ANISOU  100  CD1 TRP A  29     2848   2421   2518   -112     29     -9       C  
ATOM    101  CD2 TRP A  29     -41.236  21.508  85.069  1.00 18.10           C  
ANISOU  101  CD2 TRP A  29     2585   2088   2204    -88     17     20       C  
ATOM    102  NE1 TRP A  29     -40.624  22.841  83.349  1.00 19.42           N  
ANISOU  102  NE1 TRP A  29     2706   2284   2389    -94      5     -3       N  
ATOM    103  CE2 TRP A  29     -40.160  22.273  84.504  1.00 19.47           C  
ANISOU  103  CE2 TRP A  29     2734   2273   2389    -79     -4     14       C  
ATOM    104  CE3 TRP A  29     -41.028  20.827  86.279  1.00 19.92           C  
ANISOU  104  CE3 TRP A  29     2844   2301   2424    -76     13     40       C  
ATOM    105  CZ2 TRP A  29     -38.914  22.353  85.096  1.00 18.60           C  
ANISOU  105  CZ2 TRP A  29     2625   2160   2283    -59    -29     26       C  
ATOM    106  CZ3 TRP A  29     -39.766  20.916  86.879  1.00 21.02           C  
ANISOU  106  CZ3 TRP A  29     2985   2438   2565    -54    -15     53       C  
ATOM    107  CH2 TRP A  29     -38.728  21.668  86.278  1.00 19.62           C  
ANISOU  107  CH2 TRP A  29     2779   2274   2401    -46    -36     45       C  
ATOM    108  N   GLN A  30     -43.261  19.430  81.397  1.00 16.71           N  
ANISOU  108  N   GLN A  30     2378   1906   2067   -151     92    -33       N  
ATOM    109  CA  GLN A  30     -43.542  19.597  79.974  1.00 16.52           C  
ANISOU  109  CA  GLN A  30     2330   1900   2048   -168     99    -55       C  
ATOM    110  C   GLN A  30     -44.543  18.561  79.544  1.00 16.88           C  
ANISOU  110  C   GLN A  30     2382   1935   2095   -194    125    -67       C  
ATOM    111  O   GLN A  30     -44.349  17.375  79.797  1.00 18.62           O  
ANISOU  111  O   GLN A  30     2623   2125   2327   -193    139    -65       O  
ATOM    112  CB  GLN A  30     -42.246  19.461  79.182  1.00 16.03           C  
ANISOU  112  CB  GLN A  30     2257   1833   2002   -155     93    -62       C  
ATOM    113  CG  GLN A  30     -42.437  19.416  77.654  1.00 17.42           C  
ANISOU  113  CG  GLN A  30     2413   2024   2181   -174    104    -85       C  
ATOM    114  CD  GLN A  30     -42.720  20.782  77.032  1.00 18.05           C  
ANISOU  114  CD  GLN A  30     2470   2141   2249   -181     91    -88       C  
ATOM    115  OE1 GLN A  30     -43.708  20.963  76.298  1.00 19.49           O  
ANISOU  115  OE1 GLN A  30     2642   2343   2421   -203     98    -99       O  
ATOM    116  NE2 GLN A  30     -41.828  21.728  77.273  1.00 17.38           N  
ANISOU  116  NE2 GLN A  30     2375   2062   2164   -163     72    -78       N  
ATOM    117  N   VAL A  31     -45.580  19.017  78.863  1.00 17.79           N  
ANISOU  117  N   VAL A  31     2481   2078   2202   -216    130    -79       N  
ATOM    118  CA  VAL A  31     -46.605  18.120  78.342  1.00 17.88           C  
ANISOU  118  CA  VAL A  31     2494   2086   2215   -246    152    -94       C  
ATOM    119  C   VAL A  31     -46.624  18.272  76.814  1.00 19.16           C  
ANISOU  119  C   VAL A  31     2633   2270   2377   -262    152   -117       C  
ATOM    120  O   VAL A  31     -46.284  19.359  76.281  1.00 18.28           O  
ANISOU  120  O   VAL A  31     2501   2184   2258   -254    135   -116       O  
ATOM    121  CB  VAL A  31     -47.985  18.476  78.985  1.00 19.27           C  
ANISOU  121  CB  VAL A  31     2667   2277   2378   -261    158    -88       C  
ATOM    122  CG1 VAL A  31     -49.086  17.514  78.528  1.00 20.55           C  
ANISOU  122  CG1 VAL A  31     2828   2437   2543   -295    180   -103       C  
ATOM    123  CG2 VAL A  31     -47.873  18.417  80.511  1.00 20.87           C  
ANISOU  123  CG2 VAL A  31     2894   2460   2576   -243    158    -65       C  
ATOM    124  N   SER A  32     -47.024  17.192  76.143  1.00 19.28           N  
ANISOU  124  N   SER A  32     2654   2275   2398   -286    171   -137       N  
ATOM    125  CA  SER A  32     -47.265  17.196  74.689  1.00 19.00           C  
ANISOU  125  CA  SER A  32     2600   2263   2357   -309    173   -161       C  
ATOM    126  C   SER A  32     -48.746  17.045  74.418  1.00 19.92           C  
ANISOU  126  C   SER A  32     2705   2400   2464   -343    181   -171       C  
ATOM    127  O   SER A  32     -49.351  16.105  74.933  1.00 20.79           O  
ANISOU  127  O   SER A  32     2831   2488   2582   -359    198   -174       O  
ATOM    128  CB  SER A  32     -46.517  16.025  74.044  1.00 19.73           C  
ANISOU  128  CB  SER A  32     2707   2326   2464   -313    190   -181       C  
ATOM    129  OG  SER A  32     -46.806  15.953  72.632  1.00 19.00           O  
ANISOU  129  OG  SER A  32     2600   2258   2362   -338    194   -208       O  
ATOM    130  N   LEU A  33     -49.335  17.964  73.651  1.00 19.40           N  
ANISOU  130  N   LEU A  33     2612   2377   2383   -353    167   -175       N  
ATOM    131  CA ALEU A  33     -50.742  17.875  73.282  0.50 20.01           C  
ANISOU  131  CA ALEU A  33     2672   2480   2451   -385    171   -185       C  
ATOM    132  CA BLEU A  33     -50.748  17.905  73.271  0.50 19.60           C  
ANISOU  132  CA BLEU A  33     2619   2428   2399   -385    171   -184       C  
ATOM    133  C   LEU A  33     -50.887  17.436  71.831  1.00 20.46           C  
ANISOU  133  C   LEU A  33     2719   2555   2500   -414    173   -213       C  
ATOM    134  O   LEU A  33     -50.406  18.101  70.897  1.00 20.77           O  
ANISOU  134  O   LEU A  33     2744   2619   2527   -408    160   -216       O  
ATOM    135  CB ALEU A  33     -51.479  19.193  73.553  0.50 19.70           C  
ANISOU  135  CB ALEU A  33     2608   2476   2402   -376    155   -166       C  
ATOM    136  CB BLEU A  33     -51.401  19.282  73.399  0.50 18.72           C  
ANISOU  136  CB BLEU A  33     2482   2355   2276   -376    153   -167       C  
ATOM    137  CG ALEU A  33     -52.069  19.194  74.971  0.50 20.14           C  
ANISOU  137  CG ALEU A  33     2674   2517   2463   -369    163   -148       C  
ATOM    138  CG BLEU A  33     -51.828  19.773  74.778  0.50 17.85           C  
ANISOU  138  CG BLEU A  33     2375   2237   2169   -359    153   -144       C  
ATOM    139  CD1ALEU A  33     -51.960  20.550  75.570  0.50 23.15           C  
ANISOU  139  CD1ALEU A  33     3045   2912   2839   -340    148   -127       C  
ATOM    140  CD1BLEU A  33     -51.094  19.100  75.927  0.50 13.99           C  
ANISOU  140  CD1BLEU A  33     1920   1705   1691   -342    164   -135       C  
ATOM    141  CD2ALEU A  33     -53.524  18.680  75.022  0.50 18.21           C  
ANISOU  141  CD2ALEU A  33     2416   2285   2218   -401    177   -156       C  
ATOM    142  CD2BLEU A  33     -51.494  21.223  74.767  0.50 18.94           C  
ANISOU  142  CD2BLEU A  33     2500   2397   2301   -333    133   -129       C  
ATOM    143  N   HIS A  34     -51.527  16.280  71.671  1.00 21.22           N  
ANISOU  143  N   HIS A  34     2824   2638   2601   -446    192   -233       N  
ATOM    144  CA  HIS A  34     -51.787  15.728  70.346  1.00 22.80           C  
ANISOU  144  CA  HIS A  34     3017   2855   2790   -479    195   -264       C  
ATOM    145  C   HIS A  34     -53.231  15.950  69.948  1.00 23.34           C  
ANISOU  145  C   HIS A  34     3058   2965   2846   -512    187   -270       C  
ATOM    146  O   HIS A  34     -54.160  15.689  70.738  1.00 24.65           O  
ANISOU  146  O   HIS A  34     3221   3126   3020   -524    196   -263       O  
ATOM    147  CB  HIS A  34     -51.524  14.219  70.345  1.00 22.99           C  
ANISOU  147  CB  HIS A  34     3071   2834   2831   -497    222   -287       C  
ATOM    148  CG  HIS A  34     -50.079  13.846  70.436  1.00 24.82           C  
ANISOU  148  CG  HIS A  34     3328   3028   3077   -467    231   -287       C  
ATOM    149  ND1 HIS A  34     -49.570  12.712  69.840  1.00 27.03           N  
ANISOU  149  ND1 HIS A  34     3629   3277   3366   -480    252   -315       N  
ATOM    150  CD2 HIS A  34     -49.042  14.433  71.081  1.00 27.07           C  
ANISOU  150  CD2 HIS A  34     3617   3299   3369   -426    222   -263       C  
ATOM    151  CE1 HIS A  34     -48.278  12.624  70.103  1.00 28.78           C  
ANISOU  151  CE1 HIS A  34     3865   3469   3602   -445    256   -307       C  
ATOM    152  NE2 HIS A  34     -47.935  13.649  70.864  1.00 26.32           N  
ANISOU  152  NE2 HIS A  34     3543   3168   3288   -413    237   -275       N  
ATOM    153  N   ALA A  35     -53.446  16.369  68.706  1.00 24.44           N  
ANISOU  153  N   ALA A  35     3176   3146   2964   -527    173   -283       N  
ATOM    154  CA  ALA A  35     -54.789  16.468  68.176  1.00 26.66           C  
ANISOU  154  CA  ALA A  35     3427   3469   3232   -561    163   -292       C  
ATOM    155  C   ALA A  35     -55.084  15.230  67.345  1.00 28.63           C  
ANISOU  155  C   ALA A  35     3687   3714   3477   -606    176   -330       C  
ATOM    156  O   ALA A  35     -54.180  14.603  66.767  1.00 27.93           O  
ANISOU  156  O   ALA A  35     3622   3602   3388   -608    188   -352       O  
ATOM    157  CB  ALA A  35     -54.994  17.746  67.372  1.00 27.31           C  
ANISOU  157  CB  ALA A  35     3479   3605   3293   -552    135   -279       C  
ATOM    158  N   LEU A  36     -56.353  14.855  67.334  1.00 30.58           N  
ANISOU  158  N   LEU A  36     3915   3980   3723   -642    177   -340       N  
ATOM    159  CA  LEU A  36     -56.785  13.579  66.776  1.00 32.78           C  
ANISOU  159  CA  LEU A  36     4204   4247   4002   -690    193   -378       C  
ATOM    160  C   LEU A  36     -56.292  13.443  65.339  1.00 33.24           C  
ANISOU  160  C   LEU A  36     4267   4327   4036   -706    185   -407       C  
ATOM    161  O   LEU A  36     -56.498  14.346  64.522  1.00 34.08           O  
ANISOU  161  O   LEU A  36     4346   4485   4116   -705    160   -401       O  
ATOM    162  CB  LEU A  36     -58.312  13.520  66.829  1.00 33.82           C  
ANISOU  162  CB  LEU A  36     4304   4414   4133   -727    186   -380       C  
ATOM    163  CG  LEU A  36     -59.069  12.332  67.437  1.00 36.83           C  
ANISOU  163  CG  LEU A  36     4695   4763   4534   -765    212   -395       C  
ATOM    164  CD1 LEU A  36     -58.237  11.406  68.322  1.00 38.38           C  
ANISOU  164  CD1 LEU A  36     4938   4888   4756   -751    243   -395       C  
ATOM    165  CD2 LEU A  36     -60.300  12.858  68.187  1.00 37.14           C  
ANISOU  165  CD2 LEU A  36     4699   4831   4581   -769    206   -372       C  
ATOM    166  N   GLY A  37     -55.611  12.328  65.064  1.00 33.85           N  
ANISOU  166  N   GLY A  37     4378   4361   4121   -719    210   -437       N  
ATOM    167  CA  GLY A  37     -55.098  12.034  63.730  1.00 34.10           C  
ANISOU  167  CA  GLY A  37     4420   4407   4130   -737    210   -471       C  
ATOM    168  C   GLY A  37     -53.917  12.870  63.269  1.00 33.39           C  
ANISOU  168  C   GLY A  37     4333   4327   4027   -698    201   -458       C  
ATOM    169  O   GLY A  37     -53.504  12.771  62.112  1.00 34.56           O  
ANISOU  169  O   GLY A  37     4487   4494   4152   -711    200   -484       O  
ATOM    170  N   GLN A  38     -53.366  13.703  64.157  1.00 32.84           N  
ANISOU  170  N   GLN A  38     4260   4245   3971   -651    195   -420       N  
ATOM    171  CA  GLN A  38     -52.327  14.673  63.751  1.00 31.55           C  
ANISOU  171  CA  GLN A  38     4094   4097   3796   -616    183   -403       C  
ATOM    172  C   GLN A  38     -51.019  14.585  64.528  1.00 30.54           C  
ANISOU  172  C   GLN A  38     3990   3920   3695   -574    198   -389       C  
ATOM    173  O   GLN A  38     -50.008  15.193  64.128  1.00 29.64           O  
ANISOU  173  O   GLN A  38     3876   3812   3575   -548    194   -381       O  
ATOM    174  CB  GLN A  38     -52.860  16.108  63.818  1.00 31.38           C  
ANISOU  174  CB  GLN A  38     4039   4124   3762   -599    152   -369       C  
ATOM    175  CG  GLN A  38     -54.028  16.389  62.898  1.00 32.85           C  
ANISOU  175  CG  GLN A  38     4196   4367   3919   -634    131   -377       C  
ATOM    176  CD  GLN A  38     -54.758  17.649  63.274  1.00 34.13           C  
ANISOU  176  CD  GLN A  38     4324   4566   4077   -616    105   -340       C  
ATOM    177  OE1 GLN A  38     -55.942  17.609  63.627  1.00 38.68           O  
ANISOU  177  OE1 GLN A  38     4879   5160   4658   -634     99   -336       O  
ATOM    178  NE2 GLN A  38     -54.067  18.781  63.222  1.00 33.31           N  
ANISOU  178  NE2 GLN A  38     4215   4472   3968   -580     93   -313       N  
ATOM    179  N   GLY A  39     -51.024  13.867  65.645  1.00 29.12           N  
ANISOU  179  N   GLY A  39     3828   3693   3544   -567    215   -383       N  
ATOM    180  CA  GLY A  39     -49.832  13.800  66.478  1.00 27.19           C  
ANISOU  180  CA  GLY A  39     3603   3404   3323   -525    226   -366       C  
ATOM    181  C   GLY A  39     -49.629  15.098  67.234  1.00 25.08           C  
ANISOU  181  C   GLY A  39     3319   3153   3056   -489    204   -326       C  
ATOM    182  O   GLY A  39     -50.564  15.866  67.418  1.00 23.98           O  
ANISOU  182  O   GLY A  39     3157   3047   2906   -495    186   -310       O  
ATOM    183  N   HIS A  40     -48.398  15.322  67.676  1.00 24.04           N  
ANISOU  183  N   HIS A  40     3199   2997   2940   -452    206   -311       N  
ATOM    184  CA  HIS A  40     -48.082  16.498  68.508  1.00 23.12           C  
ANISOU  184  CA  HIS A  40     3070   2888   2826   -418    187   -275       C  
ATOM    185  C   HIS A  40     -48.307  17.813  67.797  1.00 23.11           C  
ANISOU  185  C   HIS A  40     3043   2937   2802   -417    164   -265       C  
ATOM    186  O   HIS A  40     -47.786  18.040  66.685  1.00 23.17           O  
ANISOU  186  O   HIS A  40     3044   2964   2795   -421    162   -277       O  
ATOM    187  CB  HIS A  40     -46.659  16.409  69.035  1.00 21.82           C  
ANISOU  187  CB  HIS A  40     2922   2689   2682   -382    192   -265       C  
ATOM    188  CG  HIS A  40     -46.163  17.709  69.584  1.00 20.58           C  
ANISOU  188  CG  HIS A  40     2751   2546   2524   -351    171   -235       C  
ATOM    189  ND1 HIS A  40     -46.165  17.986  70.936  1.00 20.33           N  
ANISOU  189  ND1 HIS A  40     2726   2496   2503   -330    164   -209       N  
ATOM    190  CD2 HIS A  40     -45.669  18.809  68.968  1.00 22.29           C  
ANISOU  190  CD2 HIS A  40     2950   2792   2729   -340    156   -227       C  
ATOM    191  CE1 HIS A  40     -45.699  19.212  71.129  1.00 18.86           C  
ANISOU  191  CE1 HIS A  40     2526   2327   2313   -308    145   -189       C  
ATOM    192  NE2 HIS A  40     -45.393  19.731  69.951  1.00 19.73           N  
ANISOU  192  NE2 HIS A  40     2622   2465   2411   -314    140   -198       N  
ATOM    193  N   ILE A  41     -49.068  18.697  68.430  1.00 22.06           N  
ANISOU  193  N   ILE A  41     2894   2823   2666   -410    148   -241       N  
ATOM    194  CA  ILE A  41     -49.354  20.006  67.871  1.00 21.59           C  
ANISOU  194  CA  ILE A  41     2808   2806   2587   -405    126   -226       C  
ATOM    195  C   ILE A  41     -48.782  21.122  68.741  1.00 21.34           C  
ANISOU  195  C   ILE A  41     2775   2768   2566   -369    113   -196       C  
ATOM    196  O   ILE A  41     -48.126  22.051  68.272  1.00 20.39           O  
ANISOU  196  O   ILE A  41     2645   2662   2438   -354    102   -185       O  
ATOM    197  CB  ILE A  41     -50.887  20.238  67.741  1.00 22.14           C  
ANISOU  197  CB  ILE A  41     2856   2911   2645   -429    116   -224       C  
ATOM    198  CG1 ILE A  41     -51.498  19.247  66.758  1.00 24.99           C  
ANISOU  198  CG1 ILE A  41     3216   3286   2993   -470    124   -256       C  
ATOM    199  CG2 ILE A  41     -51.237  21.704  67.359  1.00 22.68           C  
ANISOU  199  CG2 ILE A  41     2897   3020   2699   -416     92   -201       C  
ATOM    200  CD1 ILE A  41     -51.007  19.421  65.357  1.00 24.36           C  
ANISOU  200  CD1 ILE A  41     3133   3234   2891   -479    119   -270       C  
ATOM    201  N   CYS A  42     -49.042  21.041  70.035  1.00 21.15           N  
ANISOU  201  N   CYS A  42     2759   2721   2556   -357    116   -182       N  
ATOM    202  CA ACYS A  42     -48.739  22.113  70.981  0.50 20.05           C  
ANISOU  202  CA ACYS A  42     2618   2577   2422   -327    104   -156       C  
ATOM    203  CA BCYS A  42     -48.465  22.060  70.861  0.50 21.21           C  
ANISOU  203  CA BCYS A  42     2767   2722   2571   -325    104   -158       C  
ATOM    204  C   CYS A  42     -48.117  21.558  72.238  1.00 19.89           C  
ANISOU  204  C   CYS A  42     2622   2516   2420   -309    112   -149       C  
ATOM    205  O   CYS A  42     -48.342  20.397  72.557  1.00 19.74           O  
ANISOU  205  O   CYS A  42     2619   2474   2408   -322    129   -160       O  
ATOM    206  CB ACYS A  42     -50.018  22.886  71.332  0.50 19.86           C  
ANISOU  206  CB ACYS A  42     2575   2578   2392   -330     95   -142       C  
ATOM    207  CB BCYS A  42     -49.220  23.423  70.729  0.50 21.24           C  
ANISOU  207  CB BCYS A  42     2748   2760   2564   -320     87   -140       C  
ATOM    208  SG ACYS A  42     -50.274  24.228  70.117  0.50 20.87           S  
ANISOU  208  SG ACYS A  42     2675   2753   2503   -329     74   -132       S  
ATOM    209  SG BCYS A  42     -50.269  24.199  72.016  0.50 28.20           S  
ANISOU  209  SG BCYS A  42     3622   3644   3449   -307     82   -118       S  
ATOM    210  N   GLY A  43     -47.390  22.387  72.972  1.00 18.10           N  
ANISOU  210  N   GLY A  43     2399   2281   2198   -282    101   -131       N  
ATOM    211  CA  GLY A  43     -46.936  22.040  74.319  1.00 17.54           C  
ANISOU  211  CA  GLY A  43     2349   2177   2139   -263    104   -119       C  
ATOM    212  C   GLY A  43     -47.906  22.584  75.340  1.00 16.02           C  
ANISOU  212  C   GLY A  43     2157   1990   1942   -260    102   -105       C  
ATOM    213  O   GLY A  43     -48.863  23.299  75.016  1.00 15.24           O  
ANISOU  213  O   GLY A  43     2038   1918   1834   -268     97   -103       O  
ATOM    214  N   ALA A  44     -47.629  22.255  76.592  1.00 14.88           N  
ANISOU  214  N   ALA A  44     2034   1819   1802   -246    105    -95       N  
ATOM    215  CA  ALA A  44     -48.391  22.714  77.761  1.00 14.30           C  
ANISOU  215  CA  ALA A  44     1965   1745   1723   -240    106    -81       C  
ATOM    216  C   ALA A  44     -47.515  22.428  78.953  1.00 14.33           C  
ANISOU  216  C   ALA A  44     1995   1719   1729   -220    103    -69       C  
ATOM    217  O   ALA A  44     -46.483  21.775  78.837  1.00 16.25           O  
ANISOU  217  O   ALA A  44     2249   1943   1982   -212    102    -71       O  
ATOM    218  CB  ALA A  44     -49.728  21.971  77.923  1.00 15.43           C  
ANISOU  218  CB  ALA A  44     2108   1891   1864   -264    125    -86       C  
ATOM    219  N   SER A  45     -47.962  22.882  80.110  1.00 15.48           N  
ANISOU  219  N   SER A  45     2151   1864   1866   -211    104    -56       N  
ATOM    220  CA  SER A  45     -47.217  22.659  81.317  1.00 16.68           C  
ANISOU  220  CA  SER A  45     2329   1992   2016   -193     99    -43       C  
ATOM    221  C   SER A  45     -48.161  22.246  82.430  1.00 17.40           C  
ANISOU  221  C   SER A  45     2439   2075   2097   -199    115    -35       C  
ATOM    222  O   SER A  45     -49.302  22.738  82.525  1.00 16.97           O  
ANISOU  222  O   SER A  45     2373   2039   2036   -209    125    -36       O  
ATOM    223  CB  SER A  45     -46.438  23.918  81.733  1.00 17.47           C  
ANISOU  223  CB  SER A  45     2427   2099   2111   -172     76    -36       C  
ATOM    224  OG  SER A  45     -47.337  24.980  82.027  1.00 20.52           O  
ANISOU  224  OG  SER A  45     2805   2503   2487   -172     77    -35       O  
ATOM    225  N   LEU A  46     -47.660  21.319  83.239  1.00 17.80           N  
ANISOU  225  N   LEU A  46     2517   2099   2149   -193    120    -25       N  
ATOM    226  CA  LEU A  46     -48.422  20.745  84.345  1.00 17.88           C  
ANISOU  226  CA  LEU A  46     2550   2097   2148   -199    138    -14       C  
ATOM    227  C   LEU A  46     -48.314  21.663  85.532  1.00 17.47           C  
ANISOU  227  C   LEU A  46     2510   2050   2076   -181    128     -2       C  
ATOM    228  O   LEU A  46     -47.186  21.897  85.995  1.00 16.93           O  
ANISOU  228  O   LEU A  46     2455   1974   2005   -161    107      6       O  
ATOM    229  CB  LEU A  46     -47.838  19.377  84.728  1.00 17.76           C  
ANISOU  229  CB  LEU A  46     2561   2047   2139   -196    146     -4       C  
ATOM    230  CG  LEU A  46     -48.645  18.633  85.812  1.00 17.36           C  
ANISOU  230  CG  LEU A  46     2536   1981   2078   -206    169     10       C  
ATOM    231  CD1 LEU A  46     -50.060  18.321  85.398  1.00 20.49           C  
ANISOU  231  CD1 LEU A  46     2920   2388   2478   -236    195     -1       C  
ATOM    232  CD2 LEU A  46     -47.905  17.359  86.138  1.00 18.97           C  
ANISOU  232  CD2 LEU A  46     2768   2149   2292   -199    173     22       C  
ATOM    233  N   ILE A  47     -49.447  22.233  85.982  1.00 16.63           N  
ANISOU  233  N   ILE A  47     2400   1960   1958   -189    141     -2       N  
ATOM    234  CA  ILE A  47     -49.412  23.097  87.199  1.00 16.70           C  
ANISOU  234  CA  ILE A  47     2426   1974   1946   -173    135      6       C  
ATOM    235  C   ILE A  47     -50.040  22.531  88.453  1.00 18.03           C  
ANISOU  235  C   ILE A  47     2623   2132   2096   -177    156     19       C  
ATOM    236  O   ILE A  47     -49.836  23.083  89.536  1.00 18.84           O  
ANISOU  236  O   ILE A  47     2746   2235   2177   -164    151     27       O  
ATOM    237  CB  ILE A  47     -49.947  24.527  86.933  1.00 17.47           C  
ANISOU  237  CB  ILE A  47     2500   2095   2041   -169    131     -3       C  
ATOM    238  CG1 ILE A  47     -51.429  24.487  86.519  1.00 17.59           C  
ANISOU  238  CG1 ILE A  47     2494   2128   2062   -187    156    -10       C  
ATOM    239  CG2 ILE A  47     -49.027  25.217  85.875  1.00 17.82           C  
ANISOU  239  CG2 ILE A  47     2524   2148   2100   -161    106    -11       C  
ATOM    240  CD1 ILE A  47     -52.136  25.831  86.685  1.00 15.08           C  
ANISOU  240  CD1 ILE A  47     2160   1830   1739   -178    159    -14       C  
ATOM    241  N   SER A  48     -50.758  21.418  88.337  1.00 18.08           N  
ANISOU  241  N   SER A  48     2632   2128   2109   -197    181     22       N  
ATOM    242  CA  SER A  48     -51.323  20.749  89.505  1.00 19.25           C  
ANISOU  242  CA  SER A  48     2809   2263   2240   -203    204     37       C  
ATOM    243  C   SER A  48     -51.708  19.360  89.020  1.00 19.49           C  
ANISOU  243  C   SER A  48     2842   2275   2288   -226    225     38       C  
ATOM    244  O   SER A  48     -51.522  19.068  87.848  1.00 19.68           O  
ANISOU  244  O   SER A  48     2845   2298   2333   -234    219     24       O  
ATOM    245  CB  SER A  48     -52.555  21.524  90.021  1.00 19.47           C  
ANISOU  245  CB  SER A  48     2828   2313   2255   -209    225     32       C  
ATOM    246  OG  SER A  48     -53.733  21.278  89.232  1.00 20.99           O  
ANISOU  246  OG  SER A  48     2991   2519   2465   -233    247     22       O  
ATOM    247  N   PRO A  49     -52.342  18.529  89.861  1.00 20.29           N  
ANISOU  247  N   PRO A  49     2967   2361   2380   -238    252     51       N  
ATOM    248  CA  PRO A  49     -52.711  17.229  89.331  1.00 20.83           C  
ANISOU  248  CA  PRO A  49     3038   2409   2469   -263    272     50       C  
ATOM    249  C   PRO A  49     -53.778  17.287  88.237  1.00 20.62           C  
ANISOU  249  C   PRO A  49     2972   2403   2460   -290    286     28       C  
ATOM    250  O   PRO A  49     -53.914  16.327  87.480  1.00 22.43           O  
ANISOU  250  O   PRO A  49     3197   2617   2708   -311    296     19       O  
ATOM    251  CB  PRO A  49     -53.258  16.502  90.556  1.00 21.04           C  
ANISOU  251  CB  PRO A  49     3098   2418   2479   -271    300     71       C  
ATOM    252  CG  PRO A  49     -52.560  17.146  91.721  1.00 21.08           C  
ANISOU  252  CG  PRO A  49     3129   2426   2455   -243    283     88       C  
ATOM    253  CD  PRO A  49     -52.558  18.598  91.324  1.00 20.78           C  
ANISOU  253  CD  PRO A  49     3061   2420   2414   -231    263     70       C  
ATOM    254  N   ASN A  50     -54.507  18.396  88.161  1.00 19.60           N  
ANISOU  254  N   ASN A  50     2816   2307   2324   -289    286     19       N  
ATOM    255  CA  ASN A  50     -55.727  18.498  87.342  1.00 21.71           C  
ANISOU  255  CA  ASN A  50     3046   2600   2605   -316    300      3       C  
ATOM    256  C   ASN A  50     -55.651  19.506  86.186  1.00 20.41           C  
ANISOU  256  C   ASN A  50     2843   2464   2449   -309    276    -13       C  
ATOM    257  O   ASN A  50     -56.528  19.513  85.335  1.00 21.27           O  
ANISOU  257  O   ASN A  50     2918   2594   2570   -330    283    -26       O  
ATOM    258  CB  ASN A  50     -56.900  18.912  88.213  1.00 22.75           C  
ANISOU  258  CB  ASN A  50     3172   2749   2725   -322    326      9       C  
ATOM    259  CG  ASN A  50     -57.060  18.039  89.434  1.00 25.50           C  
ANISOU  259  CG  ASN A  50     3558   3071   3059   -329    352     28       C  
ATOM    260  OD1 ASN A  50     -57.428  16.866  89.328  1.00 29.96           O  
ANISOU  260  OD1 ASN A  50     4130   3616   3635   -355    372     30       O  
ATOM    261  ND2 ASN A  50     -56.776  18.587  90.588  1.00 23.32           N  
ANISOU  261  ND2 ASN A  50     3308   2795   2759   -307    351     41       N  
ATOM    262  N   TRP A  51     -54.627  20.355  86.179  1.00 19.59           N  
ANISOU  262  N   TRP A  51     2744   2361   2339   -280    250    -12       N  
ATOM    263  CA  TRP A  51     -54.604  21.502  85.292  1.00 18.41           C  
ANISOU  263  CA  TRP A  51     2561   2238   2194   -271    230    -22       C  
ATOM    264  C   TRP A  51     -53.276  21.668  84.595  1.00 17.66           C  
ANISOU  264  C   TRP A  51     2469   2136   2104   -256    202    -26       C  
ATOM    265  O   TRP A  51     -52.206  21.496  85.175  1.00 16.98           O  
ANISOU  265  O   TRP A  51     2410   2028   2012   -239    191    -17       O  
ATOM    266  CB  TRP A  51     -54.893  22.773  86.059  1.00 19.13           C  
ANISOU  266  CB  TRP A  51     2651   2346   2273   -251    228    -17       C  
ATOM    267  CG  TRP A  51     -56.296  22.891  86.484  1.00 18.49           C  
ANISOU  267  CG  TRP A  51     2555   2282   2190   -263    255    -17       C  
ATOM    268  CD1 TRP A  51     -56.809  22.603  87.741  1.00 20.22           C  
ANISOU  268  CD1 TRP A  51     2796   2492   2394   -265    281     -7       C  
ATOM    269  CD2 TRP A  51     -57.392  23.320  85.695  1.00 18.17           C  
ANISOU  269  CD2 TRP A  51     2471   2270   2161   -274    261    -25       C  
ATOM    270  NE1 TRP A  51     -58.136  22.839  87.752  1.00 18.31           N  
ANISOU  270  NE1 TRP A  51     2526   2272   2157   -277    304    -10       N  
ATOM    271  CE2 TRP A  51     -58.536  23.305  86.524  1.00 20.34           C  
ANISOU  271  CE2 TRP A  51     2742   2554   2431   -282    291    -21       C  
ATOM    272  CE3 TRP A  51     -57.522  23.744  84.355  1.00 18.31           C  
ANISOU  272  CE3 TRP A  51     2453   2311   2192   -279    244    -35       C  
ATOM    273  CZ2 TRP A  51     -59.817  23.694  86.060  1.00 19.39           C  
ANISOU  273  CZ2 TRP A  51     2579   2465   2323   -293    303    -26       C  
ATOM    274  CZ3 TRP A  51     -58.764  24.132  83.909  1.00 20.25           C  
ANISOU  274  CZ3 TRP A  51     2659   2587   2446   -289    253    -39       C  
ATOM    275  CH2 TRP A  51     -59.906  24.096  84.748  1.00 18.29           C  
ANISOU  275  CH2 TRP A  51     2404   2348   2198   -295    282    -35       C  
ATOM    276  N   LEU A  52     -53.385  22.021  83.320  1.00 16.29           N  
ANISOU  276  N   LEU A  52     2266   1983   1942   -263    191    -39       N  
ATOM    277  CA  LEU A  52     -52.229  22.435  82.524  1.00 16.39           C  
ANISOU  277  CA  LEU A  52     2273   1995   1958   -249    166    -43       C  
ATOM    278  C   LEU A  52     -52.391  23.891  82.091  1.00 15.88           C  
ANISOU  278  C   LEU A  52     2184   1958   1892   -236    151    -44       C  
ATOM    279  O   LEU A  52     -53.522  24.366  81.934  1.00 17.09           O  
ANISOU  279  O   LEU A  52     2314   2133   2045   -244    159    -45       O  
ATOM    280  CB  LEU A  52     -52.106  21.655  81.221  1.00 15.60           C  
ANISOU  280  CB  LEU A  52     2161   1897   1871   -269    166    -58       C  
ATOM    281  CG  LEU A  52     -52.414  20.156  81.266  1.00 15.61           C  
ANISOU  281  CG  LEU A  52     2177   1875   1879   -293    187    -63       C  
ATOM    282  CD1 LEU A  52     -52.205  19.604  79.888  1.00 18.49           C  
ANISOU  282  CD1 LEU A  52     2527   2244   2253   -310    184    -82       C  
ATOM    283  CD2 LEU A  52     -51.519  19.497  82.202  1.00 18.27           C  
ANISOU  283  CD2 LEU A  52     2549   2177   2216   -278    189    -51       C  
ATOM    284  N   VAL A  53     -51.266  24.559  81.847  1.00 15.36           N  
ANISOU  284  N   VAL A  53     2120   1888   1827   -218    129    -43       N  
ATOM    285  CA  VAL A  53     -51.244  25.905  81.243  1.00 15.52           C  
ANISOU  285  CA  VAL A  53     2118   1930   1849   -207    114    -43       C  
ATOM    286  C   VAL A  53     -50.729  25.739  79.799  1.00 14.48           C  
ANISOU  286  C   VAL A  53     1970   1809   1725   -216    102    -51       C  
ATOM    287  O   VAL A  53     -49.756  25.025  79.558  1.00 14.40           O  
ANISOU  287  O   VAL A  53     1971   1782   1719   -216     98    -55       O  
ATOM    288  CB  VAL A  53     -50.289  26.853  82.003  1.00 16.92           C  
ANISOU  288  CB  VAL A  53     2312   2096   2021   -183     98    -36       C  
ATOM    289  CG1 VAL A  53     -50.078  28.185  81.252  1.00 19.10           C  
ANISOU  289  CG1 VAL A  53     2567   2388   2301   -173     82    -36       C  
ATOM    290  CG2 VAL A  53     -50.817  27.105  83.424  1.00 17.40           C  
ANISOU  290  CG2 VAL A  53     2392   2150   2069   -174    110    -30       C  
ATOM    291  N   SER A  54     -51.394  26.408  78.871  1.00 14.21           N  
ANISOU  291  N   SER A  54     1907   1802   1692   -221     98    -53       N  
ATOM    292  CA  SER A  54     -50.964  26.380  77.456  1.00 14.94           C  
ANISOU  292  CA  SER A  54     1983   1908   1786   -230     87    -61       C  
ATOM    293  C   SER A  54     -51.284  27.720  76.791  1.00 15.08           C  
ANISOU  293  C   SER A  54     1976   1951   1802   -221     74    -53       C  
ATOM    294  O   SER A  54     -51.569  28.698  77.468  1.00 14.31           O  
ANISOU  294  O   SER A  54     1878   1853   1705   -204     73    -43       O  
ATOM    295  CB  SER A  54     -51.624  25.152  76.778  1.00 16.76           C  
ANISOU  295  CB  SER A  54     2206   2145   2016   -259    100    -74       C  
ATOM    296  OG  SER A  54     -51.155  24.911  75.432  1.00 16.98           O  
ANISOU  296  OG  SER A  54     2224   2186   2044   -270     92    -85       O  
ATOM    297  N   ALA A  55     -51.194  27.806  75.446  1.00 14.96           N  
ANISOU  297  N   ALA A  55     1943   1956   1784   -231     66    -57       N  
ATOM    298  CA  ALA A  55     -51.511  29.071  74.752  1.00 14.81           C  
ANISOU  298  CA  ALA A  55     1902   1961   1764   -222     53    -45       C  
ATOM    299  C   ALA A  55     -52.908  29.000  74.176  1.00 16.06           C  
ANISOU  299  C   ALA A  55     2033   2151   1919   -237     55    -45       C  
ATOM    300  O   ALA A  55     -53.258  27.981  73.564  1.00 18.21           O  
ANISOU  300  O   ALA A  55     2299   2435   2186   -262     60    -58       O  
ATOM    301  CB  ALA A  55     -50.502  29.286  73.607  1.00 14.67           C  
ANISOU  301  CB  ALA A  55     1881   1950   1743   -224     41    -47       C  
ATOM    302  N   ALA A  56     -53.695  30.056  74.311  1.00 16.02           N  
ANISOU  302  N   ALA A  56     2010   2161   1917   -223     52    -31       N  
ATOM    303  CA  ALA A  56     -55.032  30.072  73.741  1.00 17.28           C  
ANISOU  303  CA  ALA A  56     2138   2354   2074   -234     51    -28       C  
ATOM    304  C   ALA A  56     -55.027  29.817  72.231  1.00 17.74           C  
ANISOU  304  C   ALA A  56     2178   2441   2120   -253     38    -32       C  
ATOM    305  O   ALA A  56     -55.938  29.164  71.731  1.00 19.41           O  
ANISOU  305  O   ALA A  56     2370   2678   2326   -276     39    -40       O  
ATOM    306  CB  ALA A  56     -55.718  31.390  74.023  1.00 17.50           C  
ANISOU  306  CB  ALA A  56     2148   2392   2110   -209     48    -10       C  
ATOM    307  N   HIS A  57     -54.006  30.287  71.509  1.00 17.67           N  
ANISOU  307  N   HIS A  57     2178   2431   2106   -247     26    -28       N  
ATOM    308  CA  HIS A  57     -54.067  30.224  70.039  1.00 17.94           C  
ANISOU  308  CA  HIS A  57     2194   2497   2123   -263     13    -29       C  
ATOM    309  C   HIS A  57     -54.047  28.777  69.514  1.00 19.94           C  
ANISOU  309  C   HIS A  57     2453   2756   2368   -296     20    -54       C  
ATOM    310  O   HIS A  57     -54.363  28.536  68.340  1.00 21.98           O  
ANISOU  310  O   HIS A  57     2696   3046   2609   -316     11    -60       O  
ATOM    311  CB  HIS A  57     -52.913  31.057  69.420  1.00 18.13           C  
ANISOU  311  CB  HIS A  57     2228   2516   2143   -250      2    -18       C  
ATOM    312  CG  HIS A  57     -51.591  30.365  69.431  1.00 18.63           C  
ANISOU  312  CG  HIS A  57     2317   2555   2207   -255      9    -33       C  
ATOM    313  ND1 HIS A  57     -50.561  30.729  70.282  1.00 18.29           N  
ANISOU  313  ND1 HIS A  57     2295   2479   2177   -237     13    -30       N  
ATOM    314  CD2 HIS A  57     -51.105  29.359  68.665  1.00 19.49           C  
ANISOU  314  CD2 HIS A  57     2432   2667   2305   -277     14    -53       C  
ATOM    315  CE1 HIS A  57     -49.509  29.958  70.050  1.00 19.84           C  
ANISOU  315  CE1 HIS A  57     2506   2660   2372   -245     18    -45       C  
ATOM    316  NE2 HIS A  57     -49.823  29.101  69.086  1.00 19.35           N  
ANISOU  316  NE2 HIS A  57     2437   2619   2297   -268     21    -59       N  
ATOM    317  N   CYS A  58     -53.619  27.850  70.349  1.00 20.23           N  
ANISOU  317  N   CYS A  58     2513   2761   2413   -300     36    -69       N  
ATOM    318  CA  CYS A  58     -53.580  26.405  69.991  1.00 20.10           C  
ANISOU  318  CA  CYS A  58     2506   2739   2391   -330     47    -94       C  
ATOM    319  C   CYS A  58     -54.987  25.804  69.876  1.00 20.75           C  
ANISOU  319  C   CYS A  58     2567   2846   2471   -356     50   -103       C  
ATOM    320  O   CYS A  58     -55.164  24.730  69.278  1.00 21.18           O  
ANISOU  320  O   CYS A  58     2623   2906   2518   -387     56   -125       O  
ATOM    321  CB  CYS A  58     -52.809  25.569  71.012  1.00 20.96           C  
ANISOU  321  CB  CYS A  58     2646   2805   2514   -325     63   -104       C  
ATOM    322  SG  CYS A  58     -51.027  25.871  71.108  1.00 24.34           S  
ANISOU  322  SG  CYS A  58     3098   3203   2946   -302     60   -100       S  
ATOM    323  N   TYR A  59     -55.966  26.468  70.483  1.00 20.79           N  
ANISOU  323  N   TYR A  59     2552   2863   2484   -345     49    -87       N  
ATOM    324  CA  TYR A  59     -57.292  25.843  70.731  1.00 21.81           C  
ANISOU  324  CA  TYR A  59     2661   3008   2617   -368     58    -94       C  
ATOM    325  C   TYR A  59     -58.389  26.620  70.024  1.00 23.89           C  
ANISOU  325  C   TYR A  59     2883   3319   2874   -368     40    -81       C  
ATOM    326  O   TYR A  59     -59.521  26.684  70.484  1.00 23.56           O  
ANISOU  326  O   TYR A  59     2818   3293   2842   -371     45    -76       O  
ATOM    327  CB  TYR A  59     -57.583  25.661  72.266  1.00 20.39           C  
ANISOU  327  CB  TYR A  59     2495   2799   2453   -357     78    -90       C  
ATOM    328  CG  TYR A  59     -56.425  24.998  72.896  1.00 21.05           C  
ANISOU  328  CG  TYR A  59     2618   2839   2541   -352     90    -98       C  
ATOM    329  CD1 TYR A  59     -56.158  23.640  72.674  1.00 19.32           C  
ANISOU  329  CD1 TYR A  59     2416   2603   2321   -379    102   -119       C  
ATOM    330  CD2 TYR A  59     -55.461  25.744  73.567  1.00 18.06           C  
ANISOU  330  CD2 TYR A  59     2259   2436   2166   -320     87    -85       C  
ATOM    331  CE1 TYR A  59     -54.982  23.030  73.170  1.00 20.21           C  
ANISOU  331  CE1 TYR A  59     2565   2675   2440   -370    111   -124       C  
ATOM    332  CE2 TYR A  59     -54.315  25.151  74.072  1.00 17.08           C  
ANISOU  332  CE2 TYR A  59     2169   2276   2046   -314     94    -90       C  
ATOM    333  CZ  TYR A  59     -54.061  23.807  73.867  1.00 18.99           C  
ANISOU  333  CZ  TYR A  59     2427   2501   2289   -337    106   -108       C  
ATOM    334  OH  TYR A  59     -52.922  23.250  74.345  1.00 19.81           O  
ANISOU  334  OH  TYR A  59     2560   2568   2397   -327    112   -111       O  
ATOM    335  N   ILE A  60     -58.030  27.190  68.877  1.00 25.78           N  
ANISOU  335  N   ILE A  60     3114   3582   3098   -366     20    -75       N  
ATOM    336  CA  ILE A  60     -58.978  27.940  68.058  1.00 28.52           C  
ANISOU  336  CA  ILE A  60     3423   3978   3437   -365     -1    -59       C  
ATOM    337  C   ILE A  60     -59.250  27.081  66.827  1.00 29.33           C  
ANISOU  337  C   ILE A  60     3514   4113   3517   -404    -11    -80       C  
ATOM    338  O   ILE A  60     -58.312  26.496  66.241  1.00 29.69           O  
ANISOU  338  O   ILE A  60     3585   4146   3549   -418     -9    -97       O  
ATOM    339  CB  ILE A  60     -58.409  29.318  67.669  1.00 28.75           C  
ANISOU  339  CB  ILE A  60     3451   4010   3462   -332    -16    -33       C  
ATOM    340  CG1 ILE A  60     -57.925  30.077  68.925  1.00 28.73           C  
ANISOU  340  CG1 ILE A  60     3468   3968   3480   -297     -4    -19       C  
ATOM    341  CG2 ILE A  60     -59.409  30.141  66.850  1.00 30.31           C  
ANISOU  341  CG2 ILE A  60     3609   4256   3652   -327    -39    -11       C  
ATOM    342  CD1 ILE A  60     -59.014  30.531  69.900  1.00 29.61           C  
ANISOU  342  CD1 ILE A  60     3559   4082   3611   -281      5     -7       C  
ATOM    343  N   ASP A  60A    -60.527  26.959  66.470  1.00 31.19           N  
ANISOU  343  N   ASP A  60A    3712   4388   3749   -423    -22    -79       N  
ATOM    344  CA  ASP A  60A    -60.921  26.151  65.316  1.00 32.84           C  
ANISOU  344  CA  ASP A  60A    3909   4633   3936   -465    -34   -101       C  
ATOM    345  C   ASP A  60A    -60.312  26.748  64.052  1.00 33.77           C  
ANISOU  345  C   ASP A  60A    4029   4777   4026   -460    -56    -92       C  
ATOM    346  O   ASP A  60A    -60.132  27.965  63.969  1.00 33.27           O  
ANISOU  346  O   ASP A  60A    3958   4720   3963   -426    -69    -62       O  
ATOM    347  CB  ASP A  60A    -62.445  26.150  65.140  1.00 33.36           C  
ANISOU  347  CB  ASP A  60A    3926   4745   4003   -482    -47    -97       C  
ATOM    348  CG  ASP A  60A    -63.180  25.572  66.323  1.00 35.23           C  
ANISOU  348  CG  ASP A  60A    4157   4964   4267   -490    -23   -104       C  
ATOM    349  OD1 ASP A  60A    -62.621  24.737  67.066  1.00 36.14           O  
ANISOU  349  OD1 ASP A  60A    4306   5033   4392   -499      2   -122       O  
ATOM    350  OD2 ASP A  60A    -64.347  25.959  66.494  1.00 39.26           O  
ANISOU  350  OD2 ASP A  60A    4625   5505   4787   -488    -30    -90       O  
ATOM    351  N   ASP A  60B    -60.003  25.870  63.093  1.00 35.41           N  
ANISOU  351  N   ASP A  60B    4248   4997   4209   -495    -59   -120       N  
ATOM    352  CA  ASP A  60B    -59.832  26.266  61.680  1.00 37.30           C  
ANISOU  352  CA  ASP A  60B    4480   5278   4414   -504    -83   -115       C  
ATOM    353  C   ASP A  60B    -60.794  25.467  60.787  1.00 38.37           C  
ANISOU  353  C   ASP A  60B    4592   5461   4526   -550    -98   -138       C  
ATOM    354  O   ASP A  60B    -61.606  24.692  61.304  1.00 38.65           O  
ANISOU  354  O   ASP A  60B    4614   5495   4576   -574    -90   -156       O  
ATOM    355  CB  ASP A  60B    -58.366  26.217  61.217  1.00 37.73           C  
ANISOU  355  CB  ASP A  60B    4573   5308   4455   -497    -74   -124       C  
ATOM    356  CG  ASP A  60B    -57.799  24.811  61.145  1.00 39.31           C  
ANISOU  356  CG  ASP A  60B    4804   5481   4652   -529    -51   -166       C  
ATOM    357  OD1 ASP A  60B    -58.549  23.820  61.271  1.00 40.77           O  
ANISOU  357  OD1 ASP A  60B    4982   5670   4841   -562    -46   -191       O  
ATOM    358  OD2 ASP A  60B    -56.573  24.694  60.934  1.00 41.02           O  
ANISOU  358  OD2 ASP A  60B    5050   5671   4864   -521    -39   -174       O  
ATOM    359  N   ARG A  60C    -60.699  25.644  59.468  1.00 39.28           N  
ANISOU  359  N   ARG A  60C    4703   5618   4604   -565   -120   -139       N  
ATOM    360  CA  ARG A  60C    -61.670  25.070  58.533  1.00 40.02           C  
ANISOU  360  CA  ARG A  60C    4769   5765   4670   -608   -142   -157       C  
ATOM    361  C   ARG A  60C    -61.685  23.543  58.473  1.00 39.98           C  
ANISOU  361  C   ARG A  60C    4783   5745   4662   -656   -123   -207       C  
ATOM    362  O   ARG A  60C    -62.691  22.939  58.059  1.00 41.03           O  
ANISOU  362  O   ARG A  60C    4891   5916   4784   -696   -136   -227       O  
ATOM    363  CB  ARG A  60C    -61.479  25.644  57.111  1.00 41.09           C  
ANISOU  363  CB  ARG A  60C    4901   5951   4761   -612   -170   -145       C  
ATOM    364  CG  ARG A  60C    -60.026  25.813  56.663  1.00 42.81           C  
ANISOU  364  CG  ARG A  60C    5161   6143   4962   -599   -156   -148       C  
ATOM    365  CD  ARG A  60C    -59.904  26.052  55.149  1.00 47.96           C  
ANISOU  365  CD  ARG A  60C    5813   6848   5562   -616   -180   -146       C  
ATOM    366  NE  ARG A  60C    -59.637  24.797  54.446  1.00 51.18           N  
ANISOU  366  NE  ARG A  60C    6244   7260   5943   -663   -169   -196       N  
ATOM    367  CZ  ARG A  60C    -60.579  23.984  53.969  1.00 53.45           C  
ANISOU  367  CZ  ARG A  60C    6513   7583   6212   -709   -183   -225       C  
ATOM    368  NH1 ARG A  60C    -60.236  22.854  53.364  1.00 53.49           N  
ANISOU  368  NH1 ARG A  60C    6544   7585   6194   -750   -169   -273       N  
ATOM    369  NH2 ARG A  60C    -61.868  24.296  54.097  1.00 55.11           N  
ANISOU  369  NH2 ARG A  60C    6677   7833   6427   -713   -210   -207       N  
ATOM    370  N   GLY A  60D    -60.576  22.918  58.854  1.00 38.62           N  
ANISOU  370  N   GLY A  60D    4655   5519   4501   -654    -93   -229       N  
ATOM    371  CA  GLY A  60D    -60.492  21.461  58.815  1.00 37.88           C  
ANISOU  371  CA  GLY A  60D    4583   5401   4407   -696    -71   -276       C  
ATOM    372  C   GLY A  60D    -60.727  20.740  60.132  1.00 37.38           C  
ANISOU  372  C   GLY A  60D    4528   5290   4385   -698    -44   -285       C  
ATOM    373  O   GLY A  60D    -60.950  19.513  60.138  1.00 37.61           O  
ANISOU  373  O   GLY A  60D    4570   5303   4418   -738    -28   -322       O  
ATOM    374  N   PHE A  60E    -60.681  21.472  61.246  1.00 35.83           N  
ANISOU  374  N   PHE A  60E    4327   5069   4218   -657    -37   -253       N  
ATOM    375  CA  PHE A  60E    -60.575  20.834  62.559  1.00 34.15           C  
ANISOU  375  CA  PHE A  60E    4133   4802   4040   -652     -7   -259       C  
ATOM    376  C   PHE A  60E    -60.977  21.752  63.734  1.00 33.41           C  
ANISOU  376  C   PHE A  60E    4022   4699   3974   -613     -6   -223       C  
ATOM    377  O   PHE A  60E    -60.603  22.930  63.794  1.00 32.76           O  
ANISOU  377  O   PHE A  60E    3934   4622   3890   -573    -18   -192       O  
ATOM    378  CB  PHE A  60E    -59.144  20.290  62.718  1.00 34.08           C  
ANISOU  378  CB  PHE A  60E    4173   4740   4037   -641     17   -275       C  
ATOM    379  CG  PHE A  60E    -58.999  19.218  63.748  1.00 32.98           C  
ANISOU  379  CG  PHE A  60E    4060   4546   3925   -650     48   -292       C  
ATOM    380  CD1 PHE A  60E    -58.704  19.556  65.068  1.00 31.22           C  
ANISOU  380  CD1 PHE A  60E    3848   4285   3730   -614     62   -268       C  
ATOM    381  CD2 PHE A  60E    -59.126  17.873  63.407  1.00 29.32           C  
ANISOU  381  CD2 PHE A  60E    3613   4068   3460   -693     64   -331       C  
ATOM    382  CE1 PHE A  60E    -58.553  18.587  66.034  1.00 30.50           C  
ANISOU  382  CE1 PHE A  60E    3782   4145   3662   -621     89   -279       C  
ATOM    383  CE2 PHE A  60E    -58.976  16.881  64.383  1.00 31.70           C  
ANISOU  383  CE2 PHE A  60E    3941   4315   3789   -699     94   -342       C  
ATOM    384  CZ  PHE A  60E    -58.684  17.251  65.708  1.00 30.41           C  
ANISOU  384  CZ  PHE A  60E    3787   4116   3651   -662    106   -314       C  
ATOM    385  N   ARG A  60F    -61.769  21.193  64.645  1.00 32.57           N  
ANISOU  385  N   ARG A  60F    3905   4578   3890   -626     10   -227       N  
ATOM    386  CA  ARG A  60F    -62.251  21.900  65.838  1.00 31.05           C  
ANISOU  386  CA  ARG A  60F    3697   4376   3722   -595     17   -198       C  
ATOM    387  C   ARG A  60F    -61.252  21.843  67.006  1.00 29.66           C  
ANISOU  387  C   ARG A  60F    3563   4140   3566   -564     42   -192       C  
ATOM    388  O   ARG A  60F    -61.449  21.123  67.979  1.00 27.96           O  
ANISOU  388  O   ARG A  60F    3361   3893   3370   -573     66   -199       O  
ATOM    389  CB  ARG A  60F    -63.647  21.373  66.253  1.00 32.20           C  
ANISOU  389  CB  ARG A  60F    3811   4542   3883   -625     23   -205       C  
ATOM    390  CG  ARG A  60F    -64.796  21.949  65.391  1.00 35.98           C  
ANISOU  390  CG  ARG A  60F    4235   5088   4349   -637     -8   -195       C  
ATOM    391  CD  ARG A  60F    -66.211  21.692  65.962  1.00 39.62           C  
ANISOU  391  CD  ARG A  60F    4653   5570   4829   -657     -1   -194       C  
ATOM    392  NE  ARG A  60F    -66.343  22.057  67.382  1.00 45.17           N  
ANISOU  392  NE  ARG A  60F    5360   6241   5561   -625     24   -174       N  
ATOM    393  CZ  ARG A  60F    -66.513  23.297  67.837  1.00 44.24           C  
ANISOU  393  CZ  ARG A  60F    5225   6132   5454   -580     18   -141       C  
ATOM    394  NH1 ARG A  60F    -66.562  24.328  67.001  1.00 44.67           N  
ANISOU  394  NH1 ARG A  60F    5255   6225   5494   -558    -12   -121       N  
ATOM    395  NH2 ARG A  60F    -66.613  23.510  69.142  1.00 45.23           N  
ANISOU  395  NH2 ARG A  60F    5357   6225   5601   -556     45   -129       N  
ATOM    396  N   TYR A  60G    -60.181  22.634  66.917  1.00 27.81           N  
ANISOU  396  N   TYR A  60G    3347   3892   3327   -529     36   -176       N  
ATOM    397  CA  TYR A  60G    -59.169  22.634  67.965  1.00 26.02           C  
ANISOU  397  CA  TYR A  60G    3158   3614   3117   -501     55   -170       C  
ATOM    398  C   TYR A  60G    -59.721  23.168  69.281  1.00 25.52           C  
ANISOU  398  C   TYR A  60G    3086   3537   3074   -476     65   -148       C  
ATOM    399  O   TYR A  60G    -59.125  22.931  70.324  1.00 23.89           O  
ANISOU  399  O   TYR A  60G    2909   3289   2881   -461     84   -146       O  
ATOM    400  CB  TYR A  60G    -57.907  23.435  67.546  1.00 26.20           C  
ANISOU  400  CB  TYR A  60G    3198   3628   3130   -470     44   -158       C  
ATOM    401  CG  TYR A  60G    -57.162  22.806  66.380  1.00 26.25           C  
ANISOU  401  CG  TYR A  60G    3220   3638   3117   -492     42   -182       C  
ATOM    402  CD1 TYR A  60G    -56.248  21.762  66.596  1.00 26.00           C  
ANISOU  402  CD1 TYR A  60G    3223   3563   3092   -499     62   -204       C  
ATOM    403  CD2 TYR A  60G    -57.390  23.230  65.066  1.00 30.04           C  
ANISOU  403  CD2 TYR A  60G    3679   4164   3570   -504     20   -182       C  
ATOM    404  CE1 TYR A  60G    -55.560  21.165  65.524  1.00 26.89           C  
ANISOU  404  CE1 TYR A  60G    3351   3678   3188   -518     64   -228       C  
ATOM    405  CE2 TYR A  60G    -56.711  22.642  63.998  1.00 28.72           C  
ANISOU  405  CE2 TYR A  60G    3529   4001   3382   -525     20   -206       C  
ATOM    406  CZ  TYR A  60G    -55.808  21.607  64.236  1.00 29.07           C  
ANISOU  406  CZ  TYR A  60G    3608   4001   3435   -532     44   -231       C  
ATOM    407  OH  TYR A  60G    -55.131  20.999  63.190  1.00 30.52           O  
ANISOU  407  OH  TYR A  60G    3809   4187   3600   -551     49   -257       O  
ATOM    408  N   SER A  60H    -60.847  23.877  69.234  1.00 24.83           N  
ANISOU  408  N   SER A  60H    2958   3487   2988   -473     54   -133       N  
ATOM    409  CA  SER A  60H    -61.487  24.358  70.474  1.00 25.52           C  
ANISOU  409  CA  SER A  60H    3036   3566   3095   -451     68   -115       C  
ATOM    410  C   SER A  60H    -62.287  23.308  71.220  1.00 25.40           C  
ANISOU  410  C   SER A  60H    3018   3539   3092   -480     92   -128       C  
ATOM    411  O   SER A  60H    -62.741  23.540  72.348  1.00 25.45           O  
ANISOU  411  O   SER A  60H    3023   3533   3114   -465    110   -116       O  
ATOM    412  CB  SER A  60H    -62.399  25.547  70.206  1.00 26.83           C  
ANISOU  412  CB  SER A  60H    3158   3773   3262   -432     50    -92       C  
ATOM    413  OG  SER A  60H    -63.604  25.149  69.583  1.00 28.72           O  
ANISOU  413  OG  SER A  60H    3356   4056   3499   -464     41    -99       O  
ATOM    414  N   ASP A  60I    -62.434  22.124  70.635  1.00 24.91           N  
ANISOU  414  N   ASP A  60I    2960   3479   3025   -522     96   -154       N  
ATOM    415  CA  ASP A  60I    -63.271  21.100  71.260  1.00 24.81           C  
ANISOU  415  CA  ASP A  60I    2943   3457   3026   -555    119   -167       C  
ATOM    416  C   ASP A  60I    -62.369  20.165  72.095  1.00 24.08           C  
ANISOU  416  C   ASP A  60I    2903   3306   2942   -556    145   -176       C  
ATOM    417  O   ASP A  60I    -61.493  19.495  71.556  1.00 23.26           O  
ANISOU  417  O   ASP A  60I    2827   3180   2830   -567    145   -194       O  
ATOM    418  CB  ASP A  60I    -64.052  20.372  70.149  1.00 25.71           C  
ANISOU  418  CB  ASP A  60I    3029   3608   3130   -604    108   -191       C  
ATOM    419  CG  ASP A  60I    -64.906  19.223  70.669  1.00 27.63           C  
ANISOU  419  CG  ASP A  60I    3268   3840   3388   -646    133   -208       C  
ATOM    420  OD1 ASP A  60I    -64.808  18.822  71.849  1.00 27.12           O  
ANISOU  420  OD1 ASP A  60I    3229   3736   3340   -639    161   -202       O  
ATOM    421  OD2 ASP A  60I    -65.663  18.709  69.842  1.00 32.85           O  
ANISOU  421  OD2 ASP A  60I    3902   4535   4044   -687    123   -227       O  
ATOM    422  N   PRO A  61     -62.552  20.155  73.438  1.00 24.04           N  
ANISOU  422  N   PRO A  61     2910   3275   2951   -541    169   -163       N  
ATOM    423  CA  PRO A  61     -61.604  19.407  74.267  1.00 23.48           C  
ANISOU  423  CA  PRO A  61     2889   3149   2885   -535    189   -165       C  
ATOM    424  C   PRO A  61     -61.561  17.910  73.919  1.00 24.04           C  
ANISOU  424  C   PRO A  61     2979   3196   2959   -577    204   -191       C  
ATOM    425  O   PRO A  61     -60.569  17.242  74.194  1.00 24.60           O  
ANISOU  425  O   PRO A  61     3091   3223   3032   -572    215   -196       O  
ATOM    426  CB  PRO A  61     -62.137  19.624  75.704  1.00 23.21           C  
ANISOU  426  CB  PRO A  61     2857   3100   2861   -520    212   -146       C  
ATOM    427  CG  PRO A  61     -63.575  20.024  75.538  1.00 26.09           C  
ANISOU  427  CG  PRO A  61     3172   3511   3231   -535    211   -143       C  
ATOM    428  CD  PRO A  61     -63.673  20.722  74.224  1.00 24.44           C  
ANISOU  428  CD  PRO A  61     2930   3345   3012   -533    179   -146       C  
ATOM    429  N   THR A  62     -62.626  17.397  73.293  1.00 25.30           N  
ANISOU  429  N   THR A  62     3108   3384   3120   -620    205   -208       N  
ATOM    430  CA  THR A  62     -62.666  15.983  72.906  1.00 25.89           C  
ANISOU  430  CA  THR A  62     3201   3437   3199   -665    220   -236       C  
ATOM    431  C   THR A  62     -61.694  15.606  71.774  1.00 26.70           C  
ANISOU  431  C   THR A  62     3324   3531   3289   -671    207   -259       C  
ATOM    432  O   THR A  62     -61.485  14.417  71.501  1.00 27.86           O  
ANISOU  432  O   THR A  62     3495   3649   3441   -702    222   -284       O  
ATOM    433  CB  THR A  62     -64.102  15.551  72.424  1.00 25.83           C  
ANISOU  433  CB  THR A  62     3151   3468   3195   -714    220   -252       C  
ATOM    434  OG1 THR A  62     -64.395  16.141  71.155  1.00 29.21           O  
ANISOU  434  OG1 THR A  62     3543   3949   3606   -722    188   -261       O  
ATOM    435  CG2 THR A  62     -65.169  15.915  73.438  1.00 25.33           C  
ANISOU  435  CG2 THR A  62     3060   3418   3145   -711    235   -232       C  
ATOM    436  N   GLN A  63     -61.109  16.615  71.122  1.00 26.44           N  
ANISOU  436  N   GLN A  63     3282   3523   3241   -642    181   -250       N  
ATOM    437  CA  GLN A  63     -60.220  16.400  69.964  1.00 26.79           C  
ANISOU  437  CA  GLN A  63     3341   3568   3270   -647    169   -271       C  
ATOM    438  C   GLN A  63     -58.749  16.213  70.363  1.00 25.78           C  
ANISOU  438  C   GLN A  63     3258   3391   3148   -615    179   -267       C  
ATOM    439  O   GLN A  63     -57.878  16.074  69.507  1.00 26.35           O  
ANISOU  439  O   GLN A  63     3344   3459   3209   -613    173   -282       O  
ATOM    440  CB  GLN A  63     -60.388  17.547  68.951  1.00 26.79           C  
ANISOU  440  CB  GLN A  63     3307   3624   3249   -636    136   -263       C  
ATOM    441  CG  GLN A  63     -61.824  17.702  68.399  1.00 27.76           C  
ANISOU  441  CG  GLN A  63     3382   3802   3365   -668    121   -267       C  
ATOM    442  CD  GLN A  63     -62.308  16.426  67.681  1.00 32.08           C  
ANISOU  442  CD  GLN A  63     3929   4352   3908   -725    128   -305       C  
ATOM    443  OE1 GLN A  63     -61.908  16.149  66.558  1.00 32.80           O  
ANISOU  443  OE1 GLN A  63     4028   4456   3979   -743    117   -328       O  
ATOM    444  NE2 GLN A  63     -63.153  15.654  68.346  1.00 32.78           N  
ANISOU  444  NE2 GLN A  63     4013   4427   4015   -755    148   -312       N  
ATOM    445  N   TRP A  64     -58.484  16.200  71.674  1.00 24.98           N  
ANISOU  445  N   TRP A  64     3177   3253   3062   -590    195   -246       N  
ATOM    446  CA  TRP A  64     -57.125  16.259  72.190  1.00 25.43           C  
ANISOU  446  CA  TRP A  64     3269   3270   3124   -554    199   -235       C  
ATOM    447  C   TRP A  64     -56.768  15.128  73.120  1.00 25.70           C  
ANISOU  447  C   TRP A  64     3341   3249   3176   -556    226   -236       C  
ATOM    448  O   TRP A  64     -57.642  14.547  73.807  1.00 26.27           O  
ANISOU  448  O   TRP A  64     3414   3311   3258   -578    244   -234       O  
ATOM    449  CB  TRP A  64     -56.942  17.553  72.973  1.00 24.97           C  
ANISOU  449  CB  TRP A  64     3202   3222   3064   -512    186   -204       C  
ATOM    450  CG  TRP A  64     -56.968  18.772  72.130  1.00 23.61           C  
ANISOU  450  CG  TRP A  64     3001   3093   2877   -498    160   -197       C  
ATOM    451  CD1 TRP A  64     -58.047  19.571  71.881  1.00 24.02           C  
ANISOU  451  CD1 TRP A  64     3014   3190   2923   -503    147   -188       C  
ATOM    452  CD2 TRP A  64     -55.875  19.344  71.404  1.00 22.01           C  
ANISOU  452  CD2 TRP A  64     2804   2895   2665   -477    144   -197       C  
ATOM    453  NE1 TRP A  64     -57.699  20.618  71.072  1.00 23.50           N  
ANISOU  453  NE1 TRP A  64     2932   3153   2844   -484    123   -180       N  
ATOM    454  CE2 TRP A  64     -56.370  20.514  70.764  1.00 21.45           C  
ANISOU  454  CE2 TRP A  64     2700   2870   2581   -470    121   -185       C  
ATOM    455  CE3 TRP A  64     -54.527  19.011  71.252  1.00 22.22           C  
ANISOU  455  CE3 TRP A  64     2858   2890   2693   -462    147   -203       C  
ATOM    456  CZ2 TRP A  64     -55.560  21.354  69.971  1.00 21.87           C  
ANISOU  456  CZ2 TRP A  64     2750   2939   2623   -451    103   -179       C  
ATOM    457  CZ3 TRP A  64     -53.721  19.848  70.455  1.00 22.00           C  
ANISOU  457  CZ3 TRP A  64     2824   2880   2654   -444    130   -199       C  
ATOM    458  CH2 TRP A  64     -54.255  21.006  69.828  1.00 22.35           C  
ANISOU  458  CH2 TRP A  64     2838   2970   2685   -440    108   -187       C  
ATOM    459  N   THR A  65     -55.479  14.833  73.157  1.00 25.33           N  
ANISOU  459  N   THR A  65     3324   3167   3133   -534    229   -236       N  
ATOM    460  CA  THR A  65     -54.901  13.922  74.106  1.00 25.89           C  
ANISOU  460  CA  THR A  65     3433   3184   3220   -524    250   -230       C  
ATOM    461  C   THR A  65     -53.657  14.621  74.639  1.00 23.77           C  
ANISOU  461  C   THR A  65     3178   2901   2951   -476    238   -208       C  
ATOM    462  O   THR A  65     -52.821  15.093  73.866  1.00 23.49           O  
ANISOU  462  O   THR A  65     3138   2878   2911   -461    223   -214       O  
ATOM    463  CB  THR A  65     -54.487  12.584  73.437  1.00 27.38           C  
ANISOU  463  CB  THR A  65     3645   3338   3419   -548    268   -258       C  
ATOM    464  OG1 THR A  65     -55.631  11.978  72.827  1.00 30.43           O  
ANISOU  464  OG1 THR A  65     4017   3740   3804   -597    277   -283       O  
ATOM    465  CG2 THR A  65     -53.906  11.634  74.435  1.00 29.02           C  
ANISOU  465  CG2 THR A  65     3893   3488   3647   -535    290   -247       C  
ATOM    466  N   ALA A  66     -53.540  14.670  75.954  1.00 21.90           N  
ANISOU  466  N   ALA A  66     2959   2641   2720   -455    244   -183       N  
ATOM    467  CA  ALA A  66     -52.327  15.119  76.615  1.00 22.10           C  
ANISOU  467  CA  ALA A  66     3002   2647   2747   -413    234   -163       C  
ATOM    468  C   ALA A  66     -51.419  13.959  76.998  1.00 21.49           C  
ANISOU  468  C   ALA A  66     2961   2518   2685   -404    249   -162       C  
ATOM    469  O   ALA A  66     -51.907  12.942  77.517  1.00 23.48           O  
ANISOU  469  O   ALA A  66     3233   2741   2947   -422    272   -162       O  
ATOM    470  CB  ALA A  66     -52.690  15.956  77.868  1.00 21.65           C  
ANISOU  470  CB  ALA A  66     2944   2599   2682   -393    229   -136       C  
ATOM    471  N   PHE A  67     -50.107  14.093  76.747  1.00 20.66           N  
ANISOU  471  N   PHE A  67     2864   2402   2586   -375    238   -161       N  
ATOM    472  CA  PHE A  67     -49.099  13.109  77.172  1.00 22.19           C  
ANISOU  472  CA  PHE A  67     3089   2546   2796   -357    250   -155       C  
ATOM    473  C   PHE A  67     -48.180  13.772  78.185  1.00 22.23           C  
ANISOU  473  C   PHE A  67     3102   2546   2799   -316    232   -126       C  
ATOM    474  O   PHE A  67     -47.464  14.718  77.843  1.00 22.24           O  
ANISOU  474  O   PHE A  67     3086   2568   2795   -296    211   -125       O  
ATOM    475  CB  PHE A  67     -48.282  12.526  75.980  1.00 22.39           C  
ANISOU  475  CB  PHE A  67     3115   2559   2832   -360    255   -181       C  
ATOM    476  CG  PHE A  67     -49.101  11.683  75.044  1.00 23.73           C  
ANISOU  476  CG  PHE A  67     3285   2728   3005   -402    275   -213       C  
ATOM    477  CD1 PHE A  67     -49.181  10.305  75.234  1.00 25.17           C  
ANISOU  477  CD1 PHE A  67     3496   2864   3206   -417    302   -222       C  
ATOM    478  CD2 PHE A  67     -49.796  12.260  73.986  1.00 25.63           C  
ANISOU  478  CD2 PHE A  67     3496   3014   3227   -428    265   -234       C  
ATOM    479  CE1 PHE A  67     -49.964   9.518  74.383  1.00 27.12           C  
ANISOU  479  CE1 PHE A  67     3742   3108   3454   -461    320   -255       C  
ATOM    480  CE2 PHE A  67     -50.562  11.485  73.131  1.00 26.90           C  
ANISOU  480  CE2 PHE A  67     3656   3177   3388   -470    280   -264       C  
ATOM    481  CZ  PHE A  67     -50.645  10.093  73.341  1.00 29.40           C  
ANISOU  481  CZ  PHE A  67     4002   3446   3724   -488    308   -277       C  
ATOM    482  N   LEU A  68     -48.246  13.305  79.423  1.00 21.63           N  
ANISOU  482  N   LEU A  68     3052   2442   2726   -307    240   -104       N  
ATOM    483  CA ALEU A  68     -47.378  13.745  80.509  0.50 21.58           C  
ANISOU  483  CA ALEU A  68     3058   2427   2716   -270    224    -76       C  
ATOM    484  CA BLEU A  68     -47.360  13.757  80.499  0.50 21.77           C  
ANISOU  484  CA BLEU A  68     3081   2451   2739   -270    223    -76       C  
ATOM    485  C   LEU A  68     -46.202  12.775  80.635  1.00 21.72           C  
ANISOU  485  C   LEU A  68     3099   2402   2753   -248    228    -69       C  
ATOM    486  O   LEU A  68     -46.347  11.555  80.382  1.00 23.15           O  
ANISOU  486  O   LEU A  68     3297   2549   2950   -262    252    -78       O  
ATOM    487  CB ALEU A  68     -48.174  13.711  81.817  0.50 21.25           C  
ANISOU  487  CB ALEU A  68     3034   2380   2661   -274    232    -53       C  
ATOM    488  CB BLEU A  68     -48.133  13.830  81.829  0.50 21.52           C  
ANISOU  488  CB BLEU A  68     3066   2417   2694   -271    229    -53       C  
ATOM    489  CG ALEU A  68     -49.568  14.336  81.979  0.50 20.82           C  
ANISOU  489  CG ALEU A  68     2962   2357   2591   -298    238    -56       C  
ATOM    490  CG BLEU A  68     -48.977  15.078  82.136  0.50 22.05           C  
ANISOU  490  CG BLEU A  68     3112   2524   2740   -276    220    -49       C  
ATOM    491  CD1ALEU A  68     -50.612  13.927  80.950  0.50 20.96           C  
ANISOU  491  CD1ALEU A  68     2961   2387   2615   -337    254    -82       C  
ATOM    492  CD1BLEU A  68     -50.039  15.291  81.121  0.50 21.88           C  
ANISOU  492  CD1BLEU A  68     3064   2532   2719   -308    227    -72       C  
ATOM    493  CD2ALEU A  68     -50.090  13.975  83.366  0.50 20.80           C  
ANISOU  493  CD2ALEU A  68     2987   2338   2580   -298    253    -32       C  
ATOM    494  CD2BLEU A  68     -49.625  15.023  83.508  0.50 20.79           C  
ANISOU  494  CD2BLEU A  68     2974   2358   2568   -276    230    -27       C  
ATOM    495  N   GLY A  69     -45.040  13.268  81.056  1.00 22.84           N  
ANISOU  495  N   GLY A  69     3240   2544   2896   -212    206    -53       N  
ATOM    496  CA  GLY A  69     -43.884  12.387  81.306  1.00 22.82           C  
ANISOU  496  CA  GLY A  69     3256   2503   2913   -185    208    -41       C  
ATOM    497  C   GLY A  69     -43.255  11.876  80.030  1.00 23.01           C  
ANISOU  497  C   GLY A  69     3269   2516   2958   -187    218    -67       C  
ATOM    498  O   GLY A  69     -42.488  10.904  80.050  1.00 25.38           O  
ANISOU  498  O   GLY A  69     3585   2778   3281   -169    228    -64       O  
ATOM    499  N   LEU A  70     -43.616  12.488  78.909  1.00 21.39           N  
ANISOU  499  N   LEU A  70     3039   2344   2746   -207    217    -93       N  
ATOM    500  CA  LEU A  70     -43.089  12.075  77.629  1.00 21.18           C  
ANISOU  500  CA  LEU A  70     3002   2312   2733   -212    228   -121       C  
ATOM    501  C   LEU A  70     -41.712  12.666  77.349  1.00 20.50           C  
ANISOU  501  C   LEU A  70     2898   2236   2655   -180    210   -117       C  
ATOM    502  O   LEU A  70     -41.503  13.874  77.535  1.00 21.52           O  
ANISOU  502  O   LEU A  70     3008   2398   2770   -170    185   -107       O  
ATOM    503  CB  LEU A  70     -44.072  12.444  76.531  1.00 20.20           C  
ANISOU  503  CB  LEU A  70     2859   2221   2594   -249    233   -149       C  
ATOM    504  CG  LEU A  70     -43.652  12.065  75.127  1.00 20.22           C  
ANISOU  504  CG  LEU A  70     2853   2225   2604   -260    246   -182       C  
ATOM    505  CD1 LEU A  70     -43.532  10.504  75.115  1.00 20.87           C  
ANISOU  505  CD1 LEU A  70     2965   2255   2710   -264    276   -193       C  
ATOM    506  CD2 LEU A  70     -44.644  12.602  74.138  1.00 19.83           C  
ANISOU  506  CD2 LEU A  70     2784   2218   2534   -295    244   -204       C  
ATOM    507  N   HIS A  71     -40.794  11.819  76.897  1.00 21.61           N  
ANISOU  507  N   HIS A  71     3045   2347   2820   -164    224   -126       N  
ATOM    508  CA  HIS A  71     -39.444  12.211  76.516  1.00 21.06           C  
ANISOU  508  CA  HIS A  71     2955   2284   2762   -135    212   -126       C  
ATOM    509  C   HIS A  71     -39.273  12.199  75.002  1.00 21.36           C  
ANISOU  509  C   HIS A  71     2977   2336   2801   -151    228   -160       C  
ATOM    510  O   HIS A  71     -38.729  13.157  74.428  1.00 21.78           O  
ANISOU  510  O   HIS A  71     3005   2422   2847   -146    214   -164       O  
ATOM    511  CB  HIS A  71     -38.396  11.298  77.168  1.00 22.22           C  
ANISOU  511  CB  HIS A  71     3117   2388   2937    -99    216   -107       C  
ATOM    512  CG  HIS A  71     -36.982  11.671  76.837  1.00 25.17           C  
ANISOU  512  CG  HIS A  71     3467   2770   3327    -68    205   -105       C  
ATOM    513  ND1 HIS A  71     -36.393  12.823  77.305  1.00 23.84           N  
ANISOU  513  ND1 HIS A  71     3276   2632   3149    -52    173    -87       N  
ATOM    514  CD2 HIS A  71     -36.050  11.059  76.069  1.00 27.60           C  
ANISOU  514  CD2 HIS A  71     3767   3059   3660    -52    222   -121       C  
ATOM    515  CE1 HIS A  71     -35.157  12.907  76.847  1.00 25.92           C  
ANISOU  515  CE1 HIS A  71     3519   2898   3433    -28    171    -89       C  
ATOM    516  NE2 HIS A  71     -34.916  11.837  76.107  1.00 28.10           N  
ANISOU  516  NE2 HIS A  71     3802   3144   3730    -26    201   -109       N  
ATOM    517  N   ASP A  72     -39.776  11.130  74.382  1.00 22.21           N  
ANISOU  517  N   ASP A  72     3102   2420   2917   -173    257   -186       N  
ATOM    518  CA  ASP A  72     -39.513  10.818  72.962  1.00 21.37           C  
ANISOU  518  CA  ASP A  72     2989   2318   2814   -187    277   -222       C  
ATOM    519  C   ASP A  72     -40.860  10.563  72.288  1.00 21.29           C  
ANISOU  519  C   ASP A  72     2984   2320   2784   -234    291   -249       C  
ATOM    520  O   ASP A  72     -41.576   9.639  72.722  1.00 22.05           O  
ANISOU  520  O   ASP A  72     3106   2385   2888   -250    307   -251       O  
ATOM    521  CB  ASP A  72     -38.675   9.517  72.959  1.00 21.03           C  
ANISOU  521  CB  ASP A  72     2964   2221   2804   -165    303   -228       C  
ATOM    522  CG  ASP A  72     -38.298   9.048  71.590  1.00 22.76           C  
ANISOU  522  CG  ASP A  72     3180   2438   3030   -175    330   -268       C  
ATOM    523  OD1 ASP A  72     -38.938   9.435  70.588  1.00 24.21           O  
ANISOU  523  OD1 ASP A  72     3355   2655   3188   -209    333   -294       O  
ATOM    524  OD2 ASP A  72     -37.345   8.252  71.547  1.00 25.38           O  
ANISOU  524  OD2 ASP A  72     3519   2732   3391   -147    348   -271       O  
ATOM    525  N   GLN A  73     -41.204  11.342  71.245  1.00 21.00           N  
ANISOU  525  N   GLN A  73     2928   2329   2724   -256    284   -268       N  
ATOM    526  CA  GLN A  73     -42.492  11.255  70.524  1.00 22.52           C  
ANISOU  526  CA  GLN A  73     3120   2544   2894   -302    290   -293       C  
ATOM    527  C   GLN A  73     -42.666   9.880  69.859  1.00 24.04           C  
ANISOU  527  C   GLN A  73     3335   2701   3098   -324    323   -328       C  
ATOM    528  O   GLN A  73     -43.797   9.447  69.606  1.00 25.64           O  
ANISOU  528  O   GLN A  73     3545   2907   3290   -363    332   -346       O  
ATOM    529  CB  GLN A  73     -42.612  12.318  69.437  1.00 20.77           C  
ANISOU  529  CB  GLN A  73     2871   2376   2645   -316    276   -304       C  
ATOM    530  CG  GLN A  73     -42.822  13.762  69.920  1.00 22.27           C  
ANISOU  530  CG  GLN A  73     3038   2605   2818   -305    245   -275       C  
ATOM    531  CD  GLN A  73     -44.162  14.029  70.582  1.00 24.13           C  
ANISOU  531  CD  GLN A  73     3273   2854   3041   -325    234   -262       C  
ATOM    532  OE1 GLN A  73     -45.122  13.282  70.435  1.00 23.69           O  
ANISOU  532  OE1 GLN A  73     3228   2792   2983   -356    248   -279       O  
ATOM    533  NE2 GLN A  73     -44.243  15.153  71.301  1.00 23.66           N  
ANISOU  533  NE2 GLN A  73     3200   2815   2974   -309    210   -234       N  
ATOM    534  N   SER A  74     -41.543   9.220  69.572  1.00 24.60           N  
ANISOU  534  N   SER A  74     3415   2739   3192   -301    343   -338       N  
ATOM    535  CA  SER A  74     -41.598   7.846  69.048  1.00 25.61           C  
ANISOU  535  CA  SER A  74     3570   2825   3337   -317    378   -372       C  
ATOM    536  C   SER A  74     -41.801   6.777  70.137  1.00 26.86           C  
ANISOU  536  C   SER A  74     3759   2926   3523   -310    392   -356       C  
ATOM    537  O   SER A  74     -41.898   5.586  69.824  1.00 27.39           O  
ANISOU  537  O   SER A  74     3851   2949   3607   -324    423   -382       O  
ATOM    538  CB  SER A  74     -40.388   7.525  68.160  1.00 26.02           C  
ANISOU  538  CB  SER A  74     3621   2865   3402   -297    398   -395       C  
ATOM    539  OG  SER A  74     -39.230   7.217  68.922  1.00 25.48           O  
ANISOU  539  OG  SER A  74     3555   2758   3367   -249    401   -370       O  
ATOM    540  N   GLN A  75     -41.850   7.184  71.410  1.00 26.34           N  
ANISOU  540  N   GLN A  75     3692   2857   3460   -288    372   -315       N  
ATOM    541  CA  GLN A  75     -42.008   6.230  72.510  1.00 26.78           C  
ANISOU  541  CA  GLN A  75     3777   2860   3539   -279    384   -293       C  
ATOM    542  C   GLN A  75     -43.099   6.705  73.489  1.00 26.50           C  
ANISOU  542  C   GLN A  75     3741   2842   3485   -295    367   -267       C  
ATOM    543  O   GLN A  75     -42.829   6.978  74.654  1.00 24.31           O  
ANISOU  543  O   GLN A  75     3469   2558   3212   -267    351   -229       O  
ATOM    544  CB  GLN A  75     -40.686   5.982  73.267  1.00 27.05           C  
ANISOU  544  CB  GLN A  75     3818   2860   3602   -225    381   -264       C  
ATOM    545  CG  GLN A  75     -39.502   5.425  72.432  1.00 29.17           C  
ANISOU  545  CG  GLN A  75     4085   3104   3895   -201    402   -286       C  
ATOM    546  CD  GLN A  75     -38.308   5.086  73.319  1.00 33.28           C  
ANISOU  546  CD  GLN A  75     4610   3588   4446   -147    399   -252       C  
ATOM    547  OE1 GLN A  75     -38.283   4.054  73.991  1.00 33.53           O  
ANISOU  547  OE1 GLN A  75     4671   3566   4502   -134    415   -238       O  
ATOM    548  NE2 GLN A  75     -37.315   5.964  73.320  1.00 33.61           N  
ANISOU  548  NE2 GLN A  75     4622   3660   4487   -115    376   -238       N  
ATOM    549  N   ARG A  76     -44.328   6.772  73.008  1.00 27.34           N  
ANISOU  549  N   ARG A  76     3843   2973   3572   -341    370   -288       N  
ATOM    550  CA  ARG A  76     -45.438   7.257  73.823  1.00 28.88           C  
ANISOU  550  CA  ARG A  76     4033   3190   3751   -359    357   -267       C  
ATOM    551  C   ARG A  76     -45.964   6.283  74.848  1.00 28.92           C  
ANISOU  551  C   ARG A  76     4069   3148   3772   -367    376   -250       C  
ATOM    552  O   ARG A  76     -46.787   6.645  75.683  1.00 29.75           O  
ANISOU  552  O   ARG A  76     4172   3267   3864   -377    368   -228       O  
ATOM    553  CB  ARG A  76     -46.557   7.799  72.943  1.00 28.79           C  
ANISOU  553  CB  ARG A  76     3999   3228   3713   -403    350   -293       C  
ATOM    554  CG  ARG A  76     -46.111   9.003  72.118  1.00 32.29           C  
ANISOU  554  CG  ARG A  76     4410   3723   4136   -392    327   -298       C  
ATOM    555  CD  ARG A  76     -47.317   9.716  71.545  1.00 37.23           C  
ANISOU  555  CD  ARG A  76     5010   4401   4734   -429    313   -310       C  
ATOM    556  NE  ARG A  76     -47.930   8.978  70.454  1.00 40.93           N  
ANISOU  556  NE  ARG A  76     5482   4873   5197   -472    330   -351       N  
ATOM    557  CZ  ARG A  76     -47.517   9.024  69.190  1.00 41.70           C  
ANISOU  557  CZ  ARG A  76     5573   4989   5283   -481    332   -381       C  
ATOM    558  NH1 ARG A  76     -46.467   9.768  68.842  1.00 41.96           N  
ANISOU  558  NH1 ARG A  76     5593   5038   5311   -449    321   -373       N  
ATOM    559  NH2 ARG A  76     -48.155   8.312  68.272  1.00 43.31           N  
ANISOU  559  NH2 ARG A  76     5782   5195   5479   -524    347   -419       N  
ATOM    560  N   SER A  77     -45.473   5.049  74.794  1.00 31.01           N  
ANISOU  560  N   SER A  77     4363   3356   4064   -361    403   -259       N  
ATOM    561  CA  SER A  77     -45.841   4.030  75.764  1.00 32.54           C  
ANISOU  561  CA  SER A  77     4591   3498   4276   -365    423   -240       C  
ATOM    562  C   SER A  77     -44.667   3.630  76.654  1.00 32.69           C  
ANISOU  562  C   SER A  77     4629   3472   4317   -313    423   -205       C  
ATOM    563  O   SER A  77     -44.678   2.551  77.254  1.00 33.92           O  
ANISOU  563  O   SER A  77     4820   3573   4496   -309    445   -191       O  
ATOM    564  CB  SER A  77     -46.357   2.787  75.038  1.00 33.76           C  
ANISOU  564  CB  SER A  77     4768   3612   4448   -405    459   -277       C  
ATOM    565  OG  SER A  77     -47.453   3.111  74.202  1.00 36.41           O  
ANISOU  565  OG  SER A  77     5083   3991   4761   -455    457   -310       O  
ATOM    566  N   ALA A  77A    -43.635   4.475  76.710  1.00 32.14           N  
ANISOU  566  N   ALA A  77A    4539   3428   4244   -272    397   -190       N  
ATOM    567  CA  ALA A  77A    -42.515   4.256  77.606  1.00 32.72           C  
ANISOU  567  CA  ALA A  77A    4625   3471   4336   -221    389   -153       C  
ATOM    568  C   ALA A  77A    -43.003   4.262  79.053  1.00 33.00           C  
ANISOU  568  C   ALA A  77A    4679   3498   4362   -216    380   -111       C  
ATOM    569  O   ALA A  77A    -43.979   4.934  79.370  1.00 32.56           O  
ANISOU  569  O   ALA A  77A    4614   3478   4280   -241    370   -107       O  
ATOM    570  CB  ALA A  77A    -41.420   5.325  77.387  1.00 31.57           C  
ANISOU  570  CB  ALA A  77A    4447   3364   4184   -185    359   -147       C  
ATOM    571  N   PRO A  78     -42.328   3.506  79.935  1.00 34.98           N  
ANISOU  571  N   PRO A  78     4956   3701   4632   -181    385    -78       N  
ATOM    572  CA  PRO A  78     -42.718   3.559  81.346  1.00 35.19           C  
ANISOU  572  CA  PRO A  78     5002   3722   4645   -174    375    -35       C  
ATOM    573  C   PRO A  78     -42.709   5.001  81.847  1.00 35.23           C  
ANISOU  573  C   PRO A  78     4981   3787   4617   -164    338    -19       C  
ATOM    574  O   PRO A  78     -41.797   5.774  81.524  1.00 36.50           O  
ANISOU  574  O   PRO A  78     5116   3977   4777   -138    314    -21       O  
ATOM    575  CB  PRO A  78     -41.650   2.712  82.049  1.00 36.14           C  
ANISOU  575  CB  PRO A  78     5148   3791   4792   -128    378     -1       C  
ATOM    576  CG  PRO A  78     -41.094   1.804  80.954  1.00 36.87           C  
ANISOU  576  CG  PRO A  78     5244   3844   4921   -124    405    -33       C  
ATOM    577  CD  PRO A  78     -41.182   2.606  79.688  1.00 35.53           C  
ANISOU  577  CD  PRO A  78     5039   3722   4739   -146    399    -78       C  
ATOM    578  N   GLY A  79     -43.739   5.379  82.594  1.00 34.57           N  
ANISOU  578  N   GLY A  79     4904   3723   4509   -187    336     -5       N  
ATOM    579  CA  GLY A  79     -43.801   6.739  83.110  1.00 32.32           C  
ANISOU  579  CA  GLY A  79     4596   3490   4192   -178    305      8       C  
ATOM    580  C   GLY A  79     -44.591   7.720  82.269  1.00 30.91           C  
ANISOU  580  C   GLY A  79     4385   3362   3996   -210    299    -23       C  
ATOM    581  O   GLY A  79     -45.028   8.761  82.773  1.00 29.44           O  
ANISOU  581  O   GLY A  79     4186   3215   3784   -212    281    -13       O  
ATOM    582  N   VAL A  80     -44.785   7.418  80.984  1.00 29.34           N  
ANISOU  582  N   VAL A  80     4175   3165   3810   -234    314    -60       N  
ATOM    583  CA  VAL A  80     -45.689   8.236  80.168  1.00 27.91           C  
ANISOU  583  CA  VAL A  80     3963   3030   3610   -267    310    -88       C  
ATOM    584  C   VAL A  80     -47.129   8.071  80.651  1.00 27.63           C  
ANISOU  584  C   VAL A  80     3935   3000   3562   -304    326    -85       C  
ATOM    585  O   VAL A  80     -47.590   6.955  80.874  1.00 28.21           O  
ANISOU  585  O   VAL A  80     4034   3034   3649   -323    353    -85       O  
ATOM    586  CB  VAL A  80     -45.629   7.886  78.662  1.00 26.84           C  
ANISOU  586  CB  VAL A  80     3815   2897   3486   -288    323   -129       C  
ATOM    587  CG1 VAL A  80     -46.657   8.710  77.880  1.00 26.66           C  
ANISOU  587  CG1 VAL A  80     3763   2926   3442   -323    316   -153       C  
ATOM    588  CG2 VAL A  80     -44.282   8.208  78.093  1.00 27.79           C  
ANISOU  588  CG2 VAL A  80     3922   3021   3616   -254    309   -134       C  
ATOM    589  N   GLN A  81     -47.837   9.182  80.802  1.00 25.79           N  
ANISOU  589  N   GLN A  81     3679   2815   3306   -314    310    -83       N  
ATOM    590  CA  GLN A  81     -49.236   9.173  81.218  1.00 26.13           C  
ANISOU  590  CA  GLN A  81     3721   2870   3337   -348    325    -82       C  
ATOM    591  C   GLN A  81     -50.054   9.858  80.149  1.00 26.23           C  
ANISOU  591  C   GLN A  81     3697   2929   3340   -377    319   -111       C  
ATOM    592  O   GLN A  81     -49.804  11.041  79.803  1.00 26.74           O  
ANISOU  592  O   GLN A  81     3735   3034   3391   -363    294   -113       O  
ATOM    593  CB  GLN A  81     -49.433   9.897  82.560  1.00 25.98           C  
ANISOU  593  CB  GLN A  81     3708   2866   3298   -329    314    -48       C  
ATOM    594  CG  GLN A  81     -48.684   9.250  83.724  1.00 26.10           C  
ANISOU  594  CG  GLN A  81     3761   2840   3317   -300    316    -14       C  
ATOM    595  CD  GLN A  81     -48.855   9.963  85.029  1.00 27.60           C  
ANISOU  595  CD  GLN A  81     3959   3046   3482   -284    305     16       C  
ATOM    596  OE1 GLN A  81     -49.895  10.578  85.315  1.00 28.75           O  
ANISOU  596  OE1 GLN A  81     4092   3222   3610   -303    310     14       O  
ATOM    597  NE2 GLN A  81     -47.817   9.900  85.840  1.00 25.84           N  
ANISOU  597  NE2 GLN A  81     3757   2805   3256   -247    289     43       N  
ATOM    598  N   GLU A  82     -51.050   9.148  79.648  1.00 26.44           N  
ANISOU  598  N   GLU A  82     3723   2951   3373   -420    341   -132       N  
ATOM    599  CA AGLU A  82     -51.979   9.702  78.676  0.50 26.52           C  
ANISOU  599  CA AGLU A  82     3697   3007   3372   -452    336   -158       C  
ATOM    600  CA BGLU A  82     -51.987   9.683  78.674  0.50 26.03           C  
ANISOU  600  CA BGLU A  82     3635   2944   3310   -453    336   -159       C  
ATOM    601  C   GLU A  82     -53.276  10.158  79.364  1.00 26.39           C  
ANISOU  601  C   GLU A  82     3666   3018   3343   -472    340   -146       C  
ATOM    602  O   GLU A  82     -53.843   9.444  80.204  1.00 25.51           O  
ANISOU  602  O   GLU A  82     3574   2880   3237   -487    363   -133       O  
ATOM    603  CB AGLU A  82     -52.237   8.702  77.533  0.50 27.98           C  
ANISOU  603  CB AGLU A  82     3884   3177   3570   -489    353   -195       C  
ATOM    604  CB BGLU A  82     -52.287   8.618  77.612  0.50 27.34           C  
ANISOU  604  CB BGLU A  82     3805   3092   3490   -491    356   -194       C  
ATOM    605  CG AGLU A  82     -52.884   7.386  77.958  0.50 30.63           C  
ANISOU  605  CG AGLU A  82     4246   3468   3922   -521    386   -198       C  
ATOM    606  CG BGLU A  82     -53.267   9.060  76.545  0.50 26.83           C  
ANISOU  606  CG BGLU A  82     3705   3077   3414   -528    348   -222       C  
ATOM    607  CD AGLU A  82     -52.443   6.211  77.118  0.50 32.76           C  
ANISOU  607  CD AGLU A  82     4538   3697   4213   -537    406   -227       C  
ATOM    608  CD BGLU A  82     -53.509   8.005  75.486  0.50 28.78           C  
ANISOU  608  CD BGLU A  82     3958   3307   3671   -568    366   -261       C  
ATOM    609  OE1AGLU A  82     -51.813   6.433  76.056  0.50 33.94           O  
ANISOU  609  OE1AGLU A  82     4676   3861   4360   -531    394   -251       O  
ATOM    610  OE1BGLU A  82     -52.753   7.019  75.432  0.50 30.17           O  
ANISOU  610  OE1BGLU A  82     4165   3432   3865   -562    384   -268       O  
ATOM    611  OE2AGLU A  82     -52.719   5.056  77.523  0.50 33.82           O  
ANISOU  611  OE2AGLU A  82     4701   3782   4365   -557    434   -226       O  
ATOM    612  OE2BGLU A  82     -54.463   8.169  74.710  0.50 30.31           O  
ANISOU  612  OE2BGLU A  82     4125   3538   3855   -606    362   -284       O  
ATOM    613  N   ARG A  83     -53.743  11.364  79.033  1.00 25.11           N  
ANISOU  613  N   ARG A  83     3468   2908   3165   -470    320   -149       N  
ATOM    614  CA  ARG A  83     -54.965  11.890  79.634  1.00 25.65           C  
ANISOU  614  CA  ARG A  83     3518   3005   3224   -485    325   -138       C  
ATOM    615  C   ARG A  83     -55.848  12.569  78.587  1.00 26.20           C  
ANISOU  615  C   ARG A  83     3543   3126   3285   -509    313   -159       C  
ATOM    616  O   ARG A  83     -55.349  13.271  77.702  1.00 25.31           O  
ANISOU  616  O   ARG A  83     3412   3038   3166   -496    290   -169       O  
ATOM    617  CB  ARG A  83     -54.625  12.940  80.716  1.00 25.78           C  
ANISOU  617  CB  ARG A  83     3537   3032   3225   -446    312   -109       C  
ATOM    618  CG  ARG A  83     -53.990  12.392  81.976  1.00 24.34           C  
ANISOU  618  CG  ARG A  83     3396   2808   3045   -424    322    -82       C  
ATOM    619  CD  ARG A  83     -54.929  11.389  82.699  1.00 22.24           C  
ANISOU  619  CD  ARG A  83     3148   2517   2784   -454    355    -74       C  
ATOM    620  NE  ARG A  83     -54.310  10.952  83.938  1.00 24.39           N  
ANISOU  620  NE  ARG A  83     3461   2752   3053   -430    363    -45       N  
ATOM    621  CZ  ARG A  83     -53.477   9.921  84.056  1.00 23.88           C  
ANISOU  621  CZ  ARG A  83     3431   2640   3003   -421    370    -38       C  
ATOM    622  NH1 ARG A  83     -53.129   9.170  83.011  1.00 26.55           N  
ANISOU  622  NH1 ARG A  83     3770   2958   3361   -434    374    -61       N  
ATOM    623  NH2 ARG A  83     -52.942   9.656  85.237  1.00 25.40           N  
ANISOU  623  NH2 ARG A  83     3658   2806   3189   -396    373     -6       N  
ATOM    624  N   ARG A  84     -57.164  12.417  78.710  1.00 25.68           N  
ANISOU  624  N   ARG A  84     3458   3079   3221   -543    327   -163       N  
ATOM    625  CA  ARG A  84     -58.083  13.227  77.959  1.00 26.23           C  
ANISOU  625  CA  ARG A  84     3481   3202   3281   -558    313   -174       C  
ATOM    626  C   ARG A  84     -58.267  14.586  78.620  1.00 24.89           C  
ANISOU  626  C   ARG A  84     3294   3062   3100   -526    299   -151       C  
ATOM    627  O   ARG A  84     -57.978  14.744  79.826  1.00 25.62           O  
ANISOU  627  O   ARG A  84     3409   3134   3190   -502    308   -128       O  
ATOM    628  CB  ARG A  84     -59.434  12.538  77.898  1.00 26.53           C  
ANISOU  628  CB  ARG A  84     3502   3249   3328   -607    333   -187       C  
ATOM    629  CG  ARG A  84     -59.434  11.326  77.004  1.00 30.10           C  
ANISOU  629  CG  ARG A  84     3966   3681   3791   -646    344   -217       C  
ATOM    630  CD  ARG A  84     -60.851  10.804  76.897  1.00 35.75           C  
ANISOU  630  CD  ARG A  84     4657   4415   4514   -697    361   -230       C  
ATOM    631  NE  ARG A  84     -60.828   9.371  76.646  1.00 43.81           N  
ANISOU  631  NE  ARG A  84     5705   5392   5550   -735    384   -252       N  
ATOM    632  CZ  ARG A  84     -60.950   8.443  77.586  1.00 42.98           C  
ANISOU  632  CZ  ARG A  84     5631   5239   5459   -746    415   -240       C  
ATOM    633  NH1 ARG A  84     -61.144   8.778  78.858  1.00 46.55           N  
ANISOU  633  NH1 ARG A  84     6092   5686   5910   -725    427   -207       N  
ATOM    634  NH2 ARG A  84     -60.896   7.175  77.238  1.00 46.05           N  
ANISOU  634  NH2 ARG A  84     6046   5587   5863   -780    436   -262       N  
ATOM    635  N   LEU A  85     -58.807  15.535  77.866  1.00 25.21           N  
ANISOU  635  N   LEU A  85     3294   3152   3134   -527    280   -157       N  
ATOM    636  CA  LEU A  85     -59.158  16.847  78.400  1.00 24.96           C  
ANISOU  636  CA  LEU A  85     3241   3148   3093   -500    270   -138       C  
ATOM    637  C   LEU A  85     -60.649  16.916  78.681  1.00 25.83           C  
ANISOU  637  C   LEU A  85     3320   3288   3209   -524    285   -136       C  
ATOM    638  O   LEU A  85     -61.479  16.509  77.850  1.00 27.85           O  
ANISOU  638  O   LEU A  85     3547   3567   3469   -560    285   -154       O  
ATOM    639  CB  LEU A  85     -58.815  17.975  77.434  1.00 24.41           C  
ANISOU  639  CB  LEU A  85     3146   3113   3015   -480    239   -140       C  
ATOM    640  CG  LEU A  85     -57.350  18.178  77.025  1.00 22.48           C  
ANISOU  640  CG  LEU A  85     2924   2851   2766   -454    222   -141       C  
ATOM    641  CD1 LEU A  85     -57.220  19.476  76.283  1.00 22.61           C  
ANISOU  641  CD1 LEU A  85     2913   2904   2774   -435    195   -137       C  
ATOM    642  CD2 LEU A  85     -56.455  18.174  78.246  1.00 24.00           C  
ANISOU  642  CD2 LEU A  85     3153   3006   2960   -424    228   -123       C  
ATOM    643  N   LYS A  86     -60.978  17.478  79.834  1.00 25.62           N  
ANISOU  643  N   LYS A  86     3295   3260   3178   -503    296   -116       N  
ATOM    644  CA  LYS A  86     -62.337  17.721  80.221  1.00 26.07           C  
ANISOU  644  CA  LYS A  86     3320   3345   3241   -518    313   -112       C  
ATOM    645  C   LYS A  86     -62.806  19.090  79.754  1.00 26.08           C  
ANISOU  645  C   LYS A  86     3278   3392   3238   -497    292   -107       C  
ATOM    646  O   LYS A  86     -63.975  19.287  79.440  1.00 27.73           O  
ANISOU  646  O   LYS A  86     3444   3637   3454   -515    295   -110       O  
ATOM    647  CB  LYS A  86     -62.458  17.588  81.754  1.00 26.37           C  
ANISOU  647  CB  LYS A  86     3386   3358   3276   -506    341    -93       C  
ATOM    648  CG  LYS A  86     -63.743  18.138  82.340  1.00 30.19           C  
ANISOU  648  CG  LYS A  86     3836   3872   3762   -510    359    -85       C  
ATOM    649  CD  LYS A  86     -63.906  17.876  83.859  1.00 34.05           C  
ANISOU  649  CD  LYS A  86     4356   4335   4245   -504    392    -67       C  
ATOM    650  CE  LYS A  86     -62.600  17.565  84.580  1.00 33.78           C  
ANISOU  650  CE  LYS A  86     4379   4257   4199   -480    390    -56       C  
ATOM    651  NZ  LYS A  86     -62.841  17.522  86.060  1.00 37.89           N  
ANISOU  651  NZ  LYS A  86     4927   4762   4707   -471    419    -37       N  
ATOM    652  N   ARG A  87     -61.890  20.056  79.702  1.00 24.43           N  
ANISOU  652  N   ARG A  87     3079   3181   3021   -459    270    -99       N  
ATOM    653  CA  ARG A  87     -62.304  21.439  79.505  1.00 24.28           C  
ANISOU  653  CA  ARG A  87     3026   3197   3000   -433    255    -89       C  
ATOM    654  C   ARG A  87     -61.111  22.269  79.039  1.00 22.84           C  
ANISOU  654  C   ARG A  87     2858   3010   2810   -401    227    -85       C  
ATOM    655  O   ARG A  87     -59.954  22.014  79.443  1.00 22.97           O  
ANISOU  655  O   ARG A  87     2914   2992   2821   -387    226    -84       O  
ATOM    656  CB  ARG A  87     -62.852  22.037  80.825  1.00 24.64           C  
ANISOU  656  CB  ARG A  87     3075   3242   3047   -412    277    -74       C  
ATOM    657  CG  ARG A  87     -63.523  23.377  80.660  1.00 27.28           C  
ANISOU  657  CG  ARG A  87     3369   3610   3384   -388    268    -65       C  
ATOM    658  CD  ARG A  87     -64.178  23.881  81.919  1.00 30.37           C  
ANISOU  658  CD  ARG A  87     3760   4001   3777   -371    295    -54       C  
ATOM    659  NE  ARG A  87     -64.864  25.149  81.646  1.00 32.50           N  
ANISOU  659  NE  ARG A  87     3990   4304   4055   -347    287    -47       N  
ATOM    660  CZ  ARG A  87     -65.363  25.944  82.583  1.00 35.71           C  
ANISOU  660  CZ  ARG A  87     4392   4712   4463   -322    307    -38       C  
ATOM    661  NH1 ARG A  87     -65.252  25.602  83.861  1.00 36.89           N  
ANISOU  661  NH1 ARG A  87     4576   4836   4604   -320    335    -36       N  
ATOM    662  NH2 ARG A  87     -65.963  27.080  82.240  1.00 37.70           N  
ANISOU  662  NH2 ARG A  87     4606   4992   4726   -298    299    -31       N  
ATOM    663  N   ILE A  88     -61.409  23.255  78.203  1.00 22.51           N  
ANISOU  663  N   ILE A  88     2782   3003   2768   -390    206    -83       N  
ATOM    664  CA  ILE A  88     -60.405  24.243  77.795  1.00 21.92           C  
ANISOU  664  CA  ILE A  88     2716   2927   2687   -359    182    -76       C  
ATOM    665  C   ILE A  88     -60.930  25.632  78.135  1.00 21.91           C  
ANISOU  665  C   ILE A  88     2691   2944   2689   -328    179    -60       C  
ATOM    666  O   ILE A  88     -62.007  26.062  77.652  1.00 25.14           O  
ANISOU  666  O   ILE A  88     3058   3389   3104   -332    175    -56       O  
ATOM    667  CB  ILE A  88     -60.083  24.151  76.262  1.00 20.57           C  
ANISOU  667  CB  ILE A  88     2529   2776   2510   -373    158    -86       C  
ATOM    668  CG1 ILE A  88     -59.568  22.744  75.893  1.00 22.25           C  
ANISOU  668  CG1 ILE A  88     2765   2968   2721   -404    164   -105       C  
ATOM    669  CG2 ILE A  88     -59.130  25.317  75.831  1.00 21.03           C  
ANISOU  669  CG2 ILE A  88     2592   2836   2563   -341    134    -75       C  
ATOM    670  CD1 ILE A  88     -59.437  22.517  74.393  1.00 20.90           C  
ANISOU  670  CD1 ILE A  88     2578   2821   2542   -424    145   -120       C  
ATOM    671  N   ILE A  89     -60.190  26.334  78.984  1.00 21.55           N  
ANISOU  671  N   ILE A  89     2674   2875   2641   -297    180    -51       N  
ATOM    672  CA  ILE A  89     -60.567  27.697  79.364  1.00 21.45           C  
ANISOU  672  CA  ILE A  89     2646   2872   2631   -266    179    -38       C  
ATOM    673  C   ILE A  89     -59.574  28.643  78.691  1.00 22.07           C  
ANISOU  673  C   ILE A  89     2730   2947   2707   -244    153    -33       C  
ATOM    674  O   ILE A  89     -58.404  28.725  79.097  1.00 22.23           O  
ANISOU  674  O   ILE A  89     2786   2940   2722   -232    147    -33       O  
ATOM    675  CB  ILE A  89     -60.543  27.920  80.897  1.00 21.00           C  
ANISOU  675  CB  ILE A  89     2617   2790   2572   -248    202    -34       C  
ATOM    676  CG1 ILE A  89     -61.585  27.022  81.565  1.00 21.31           C  
ANISOU  676  CG1 ILE A  89     2650   2834   2614   -271    232    -37       C  
ATOM    677  CG2 ILE A  89     -60.852  29.395  81.256  1.00 23.09           C  
ANISOU  677  CG2 ILE A  89     2870   3062   2842   -214    202    -24       C  
ATOM    678  CD1 ILE A  89     -61.610  27.158  83.084  1.00 24.27           C  
ANISOU  678  CD1 ILE A  89     3054   3187   2981   -257    257    -33       C  
ATOM    679  N   SER A  90     -60.036  29.325  77.648  1.00 22.30           N  
ANISOU  679  N   SER A  90     2725   3008   2740   -240    136    -26       N  
ATOM    680  CA ASER A  90     -59.138  30.286  77.022  0.50 22.26           C  
ANISOU  680  CA ASER A  90     2725   2999   2733   -219    113    -18       C  
ATOM    681  CA BSER A  90     -59.226  30.301  76.914  0.50 21.94           C  
ANISOU  681  CA BSER A  90     2681   2962   2692   -220    112    -17       C  
ATOM    682  C   SER A  90     -59.396  31.649  77.603  1.00 21.84           C  
ANISOU  682  C   SER A  90     2668   2942   2688   -185    116     -4       C  
ATOM    683  O   SER A  90     -60.488  31.953  78.058  1.00 22.67           O  
ANISOU  683  O   SER A  90     2751   3060   2802   -177    131      0       O  
ATOM    684  CB ASER A  90     -59.254  30.261  75.509  0.50 22.44           C  
ANISOU  684  CB ASER A  90     2722   3054   2751   -233     91    -16       C  
ATOM    685  CB BSER A  90     -59.746  30.368  75.473  0.50 21.99           C  
ANISOU  685  CB BSER A  90     2651   3008   2697   -233     93    -14       C  
ATOM    686  OG ASER A  90     -58.693  29.043  75.050  0.50 23.40           O  
ANISOU  686  OG ASER A  90     2858   3169   2864   -262     90    -33       O  
ATOM    687  OG BSER A  90     -59.013  31.263  74.663  0.50 20.42           O  
ANISOU  687  OG BSER A  90     2453   2812   2495   -217     71     -3       O  
ATOM    688  N   HIS A  91     -58.340  32.451  77.669  1.00 20.64           N  
ANISOU  688  N   HIS A  91     2539   2768   2534   -165    105      0       N  
ATOM    689  CA  HIS A  91     -58.477  33.728  78.333  1.00 20.45           C  
ANISOU  689  CA  HIS A  91     2518   2733   2519   -134    111     10       C  
ATOM    690  C   HIS A  91     -59.540  34.581  77.655  1.00 20.76           C  
ANISOU  690  C   HIS A  91     2516   2800   2570   -119    106     25       C  
ATOM    691  O   HIS A  91     -59.563  34.695  76.424  1.00 21.14           O  
ANISOU  691  O   HIS A  91     2543   2873   2618   -125     86     33       O  
ATOM    692  CB  HIS A  91     -57.151  34.498  78.390  1.00 20.27           C  
ANISOU  692  CB  HIS A  91     2524   2683   2495   -118     97     12       C  
ATOM    693  CG  HIS A  91     -57.217  35.646  79.343  1.00 17.49           C  
ANISOU  693  CG  HIS A  91     2185   2310   2150    -90    107     15       C  
ATOM    694  ND1 HIS A  91     -56.813  35.553  80.663  1.00 20.42           N  
ANISOU  694  ND1 HIS A  91     2589   2655   2514    -85    121      4       N  
ATOM    695  CD2 HIS A  91     -57.735  36.879  79.197  1.00 16.48           C  
ANISOU  695  CD2 HIS A  91     2041   2186   2036    -65    108     27       C  
ATOM    696  CE1 HIS A  91     -57.049  36.710  81.264  1.00 16.23           C  
ANISOU  696  CE1 HIS A  91     2064   2111   1991    -60    130      7       C  
ATOM    697  NE2 HIS A  91     -57.621  37.522  80.401  1.00 22.39           N  
ANISOU  697  NE2 HIS A  91     2814   2907   2786    -47    124     20       N  
ATOM    698  N   PRO A  92     -60.473  35.151  78.439  1.00 21.88           N  
ANISOU  698  N   PRO A  92     2646   2943   2724   -100    126     29       N  
ATOM    699  CA  PRO A  92     -61.539  35.897  77.783  1.00 22.42           C  
ANISOU  699  CA  PRO A  92     2671   3041   2808    -85    122     45       C  
ATOM    700  C   PRO A  92     -61.110  37.120  76.961  1.00 21.85           C  
ANISOU  700  C   PRO A  92     2594   2967   2741    -61    101     63       C  
ATOM    701  O   PRO A  92     -61.862  37.545  76.083  1.00 23.14           O  
ANISOU  701  O   PRO A  92     2720   3160   2913    -54     89     80       O  
ATOM    702  CB  PRO A  92     -62.444  36.347  78.941  1.00 22.37           C  
ANISOU  702  CB  PRO A  92     2659   3028   2814    -64    151     44       C  
ATOM    703  CG  PRO A  92     -61.615  36.286  80.135  1.00 23.13           C  
ANISOU  703  CG  PRO A  92     2802   3086   2900    -61    166     30       C  
ATOM    704  CD  PRO A  92     -60.679  35.097  79.891  1.00 22.54           C  
ANISOU  704  CD  PRO A  92     2752   3005   2808    -92    153     19       C  
ATOM    705  N   PHE A  93     -59.909  37.666  77.202  1.00 21.58           N  
ANISOU  705  N   PHE A  93     2597   2900   2704    -52     95     61       N  
ATOM    706  CA  PHE A  93     -59.474  38.810  76.415  1.00 20.89           C  
ANISOU  706  CA  PHE A  93     2506   2807   2622    -32     77     79       C  
ATOM    707  C   PHE A  93     -58.566  38.432  75.244  1.00 20.27           C  
ANISOU  707  C   PHE A  93     2433   2739   2530    -52     53     82       C  
ATOM    708  O   PHE A  93     -58.063  39.314  74.541  1.00 19.90           O  
ANISOU  708  O   PHE A  93     2387   2687   2486    -40     38     98       O  
ATOM    709  CB  PHE A  93     -58.759  39.875  77.266  1.00 20.80           C  
ANISOU  709  CB  PHE A  93     2529   2755   2620     -8     85     77       C  
ATOM    710  CG  PHE A  93     -59.523  40.301  78.470  1.00 23.27           C  
ANISOU  710  CG  PHE A  93     2844   3053   2944     12    112     70       C  
ATOM    711  CD1 PHE A  93     -60.919  40.197  78.527  1.00 23.03           C  
ANISOU  711  CD1 PHE A  93     2776   3048   2924     20    126     76       C  
ATOM    712  CD2 PHE A  93     -58.839  40.824  79.556  1.00 23.53           C  
ANISOU  712  CD2 PHE A  93     2915   3047   2976     23    124     57       C  
ATOM    713  CE1 PHE A  93     -61.615  40.599  79.665  1.00 25.71           C  
ANISOU  713  CE1 PHE A  93     3118   3375   3274     40    156     69       C  
ATOM    714  CE2 PHE A  93     -59.521  41.244  80.702  1.00 26.35           C  
ANISOU  714  CE2 PHE A  93     3279   3391   3341     42    152     48       C  
ATOM    715  CZ  PHE A  93     -60.919  41.090  80.755  1.00 25.50           C  
ANISOU  715  CZ  PHE A  93     3134   3309   3244     51    169     54       C  
ATOM    716  N   PHE A  94     -58.341  37.126  75.050  1.00 19.23           N  
ANISOU  716  N   PHE A  94     2305   2619   2384    -83     50     67       N  
ATOM    717  CA  PHE A  94     -57.495  36.654  73.945  1.00 19.32           C  
ANISOU  717  CA  PHE A  94     2320   2640   2380   -104     31     66       C  
ATOM    718  C   PHE A  94     -57.939  37.289  72.646  1.00 19.76           C  
ANISOU  718  C   PHE A  94     2346   2727   2434    -98     12     88       C  
ATOM    719  O   PHE A  94     -59.144  37.285  72.310  1.00 20.19           O  
ANISOU  719  O   PHE A  94     2366   2814   2493    -97     10     97       O  
ATOM    720  CB  PHE A  94     -57.525  35.127  73.825  1.00 19.02           C  
ANISOU  720  CB  PHE A  94     2283   2614   2329   -137     35     46       C  
ATOM    721  CG  PHE A  94     -56.783  34.623  72.617  1.00 17.42           C  
ANISOU  721  CG  PHE A  94     2082   2425   2110   -158     18     43       C  
ATOM    722  CD1 PHE A  94     -55.414  34.809  72.503  1.00 18.85           C  
ANISOU  722  CD1 PHE A  94     2291   2582   2288   -156     12     41       C  
ATOM    723  CD2 PHE A  94     -57.464  34.014  71.569  1.00 19.61           C  
ANISOU  723  CD2 PHE A  94     2333   2741   2377   -180      8     42       C  
ATOM    724  CE1 PHE A  94     -54.710  34.374  71.340  1.00 21.78           C  
ANISOU  724  CE1 PHE A  94     2664   2968   2645   -174      0     38       C  
ATOM    725  CE2 PHE A  94     -56.791  33.567  70.428  1.00 23.33           C  
ANISOU  725  CE2 PHE A  94     2808   3226   2831   -200     -6     37       C  
ATOM    726  CZ  PHE A  94     -55.400  33.734  70.325  1.00 20.28           C  
ANISOU  726  CZ  PHE A  94     2451   2815   2442   -196     -8     35       C  
ATOM    727  N   ASN A  95     -56.978  37.884  71.937  1.00 18.99           N  
ANISOU  727  N   ASN A  95     2262   2622   2332    -94     -2     99       N  
ATOM    728  CA  ASN A  95     -57.270  38.437  70.627  1.00 20.37           C  
ANISOU  728  CA  ASN A  95     2413   2827   2500    -91    -21    122       C  
ATOM    729  C   ASN A  95     -56.638  37.563  69.563  1.00 20.54           C  
ANISOU  729  C   ASN A  95     2438   2869   2498   -122    -33    113       C  
ATOM    730  O   ASN A  95     -55.437  37.322  69.574  1.00 19.00           O  
ANISOU  730  O   ASN A  95     2271   2653   2298   -131    -31    102       O  
ATOM    731  CB  ASN A  95     -56.760  39.877  70.551  1.00 19.65           C  
ANISOU  731  CB  ASN A  95     2333   2712   2421    -63    -25    145       C  
ATOM    732  CG  ASN A  95     -57.125  40.544  69.246  1.00 21.49           C  
ANISOU  732  CG  ASN A  95     2542   2975   2647    -56    -44    175       C  
ATOM    733  OD1 ASN A  95     -56.552  40.228  68.199  1.00 22.40           O  
ANISOU  733  OD1 ASN A  95     2660   3109   2742    -75    -58    177       O  
ATOM    734  ND2 ASN A  95     -58.084  41.474  69.295  1.00 23.65           N  
ANISOU  734  ND2 ASN A  95     2794   3255   2939    -27    -45    198       N  
ATOM    735  N   ASP A  96     -57.472  37.124  68.616  1.00 21.60           N  
ANISOU  735  N   ASP A  96     2542   3046   2618   -137    -46    118       N  
ATOM    736  CA  ASP A  96     -57.103  36.200  67.549  1.00 22.65           C  
ANISOU  736  CA  ASP A  96     2676   3205   2725   -169    -57    105       C  
ATOM    737  C   ASP A  96     -56.080  36.798  66.563  1.00 21.54           C  
ANISOU  737  C   ASP A  96     2549   3064   2571   -167    -68    120       C  
ATOM    738  O   ASP A  96     -55.253  36.068  66.018  1.00 21.71           O  
ANISOU  738  O   ASP A  96     2586   3088   2575   -190    -68    103       O  
ATOM    739  CB  ASP A  96     -58.374  35.740  66.804  1.00 25.02           C  
ANISOU  739  CB  ASP A  96     2938   3556   3014   -185    -70    108       C  
ATOM    740  CG  ASP A  96     -58.092  34.681  65.764  1.00 28.60           C  
ANISOU  740  CG  ASP A  96     3393   4036   3439   -222    -79     89       C  
ATOM    741  OD1 ASP A  96     -58.069  33.478  66.123  1.00 34.26           O  
ANISOU  741  OD1 ASP A  96     4118   4745   4153   -248    -67     60       O  
ATOM    742  OD2 ASP A  96     -57.907  35.053  64.572  1.00 31.53           O  
ANISOU  742  OD2 ASP A  96     3758   4434   3789   -226    -97    104       O  
ATOM    743  N   PHE A  97     -56.106  38.115  66.375  1.00 20.61           N  
ANISOU  743  N   PHE A  97     2427   2942   2463   -140    -76    150       N  
ATOM    744  CA  PHE A  97     -55.207  38.735  65.430  1.00 20.26           C  
ANISOU  744  CA  PHE A  97     2395   2898   2405   -140    -85    167       C  
ATOM    745  C   PHE A  97     -53.845  39.022  66.048  1.00 18.98           C  
ANISOU  745  C   PHE A  97     2266   2690   2255   -135    -72    159       C  
ATOM    746  O   PHE A  97     -52.822  38.721  65.454  1.00 18.66           O  
ANISOU  746  O   PHE A  97     2241   2649   2201   -151    -72    152       O  
ATOM    747  CB  PHE A  97     -55.823  40.048  64.903  1.00 20.42           C  
ANISOU  747  CB  PHE A  97     2397   2931   2431   -113    -98    207       C  
ATOM    748  CG  PHE A  97     -55.002  40.719  63.856  1.00 21.47           C  
ANISOU  748  CG  PHE A  97     2541   3067   2548   -113   -108    230       C  
ATOM    749  CD1 PHE A  97     -55.369  40.595  62.514  1.00 24.15           C  
ANISOU  749  CD1 PHE A  97     2864   3455   2858   -126   -127    246       C  
ATOM    750  CD2 PHE A  97     -53.878  41.511  64.188  1.00 21.99           C  
ANISOU  750  CD2 PHE A  97     2635   3091   2630   -102    -97    236       C  
ATOM    751  CE1 PHE A  97     -54.621  41.225  61.516  1.00 25.25           C  
ANISOU  751  CE1 PHE A  97     3015   3598   2980   -127   -133    269       C  
ATOM    752  CE2 PHE A  97     -53.110  42.130  63.191  1.00 24.76           C  
ANISOU  752  CE2 PHE A  97     2997   3446   2967   -105   -103    259       C  
ATOM    753  CZ  PHE A  97     -53.489  41.988  61.850  1.00 25.84           C  
ANISOU  753  CZ  PHE A  97     3117   3629   3071   -117   -120    276       C  
ATOM    754  N   THR A  98     -53.818  39.564  67.272  1.00 18.71           N  
ANISOU  754  N   THR A  98     2243   2619   2247   -113    -60    157       N  
ATOM    755  CA  THR A  98     -52.579  40.065  67.852  1.00 17.95           C  
ANISOU  755  CA  THR A  98     2176   2481   2163   -107    -52    153       C  
ATOM    756  C   THR A  98     -51.954  39.023  68.756  1.00 17.64           C  
ANISOU  756  C   THR A  98     2155   2422   2125   -121    -40    121       C  
ATOM    757  O   THR A  98     -50.779  39.140  69.088  1.00 17.53           O  
ANISOU  757  O   THR A  98     2163   2381   2117   -123    -36    113       O  
ATOM    758  CB  THR A  98     -52.834  41.318  68.716  1.00 19.33           C  
ANISOU  758  CB  THR A  98     2356   2624   2364    -76    -46    167       C  
ATOM    759  OG1 THR A  98     -53.759  40.995  69.776  1.00 19.34           O  
ANISOU  759  OG1 THR A  98     2351   2621   2376    -67    -36    154       O  
ATOM    760  CG2 THR A  98     -53.408  42.481  67.866  1.00 19.50           C  
ANISOU  760  CG2 THR A  98     2361   2659   2388    -57    -56    204       C  
ATOM    761  N   PHE A  99     -52.744  38.014  69.145  1.00 16.89           N  
ANISOU  761  N   PHE A  99     2051   2341   2027   -131    -35    104       N  
ATOM    762  CA  PHE A  99     -52.388  37.038  70.195  1.00 16.60           C  
ANISOU  762  CA  PHE A  99     2031   2282   1994   -140    -23     77       C  
ATOM    763  C   PHE A  99     -52.174  37.727  71.575  1.00 15.20           C  
ANISOU  763  C   PHE A  99     1872   2067   1835   -119    -13     75       C  
ATOM    764  O   PHE A  99     -51.497  37.188  72.456  1.00 16.61           O  
ANISOU  764  O   PHE A  99     2072   2222   2016   -123     -6     58       O  
ATOM    765  CB  PHE A  99     -51.190  36.132  69.838  1.00 17.26           C  
ANISOU  765  CB  PHE A  99     2131   2359   2066   -161    -22     59       C  
ATOM    766  CG  PHE A  99     -51.470  35.040  68.809  1.00 15.76           C  
ANISOU  766  CG  PHE A  99     1929   2202   1857   -187    -24     48       C  
ATOM    767  CD1 PHE A  99     -52.666  34.993  68.086  1.00 18.83           C  
ANISOU  767  CD1 PHE A  99     2292   2628   2234   -194    -32     56       C  
ATOM    768  CD2 PHE A  99     -50.492  34.059  68.569  1.00 16.97           C  
ANISOU  768  CD2 PHE A  99     2097   2347   2002   -204    -19     28       C  
ATOM    769  CE1 PHE A  99     -52.880  33.988  67.134  1.00 16.25           C  
ANISOU  769  CE1 PHE A  99     1956   2330   1887   -221    -36     42       C  
ATOM    770  CE2 PHE A  99     -50.705  33.050  67.604  1.00 16.38           C  
ANISOU  770  CE2 PHE A  99     2016   2300   1910   -229    -19     13       C  
ATOM    771  CZ  PHE A  99     -51.896  33.020  66.889  1.00 15.49           C  
ANISOU  771  CZ  PHE A  99     1879   2224   1784   -239    -28     19       C  
ATOM    772  N   ASP A 100     -52.720  38.928  71.755  1.00 15.37           N  
ANISOU  772  N   ASP A 100     1888   2083   1870    -96    -14     94       N  
ATOM    773  CA  ASP A 100     -52.767  39.457  73.128  1.00 16.33           C  
ANISOU  773  CA  ASP A 100     2026   2173   2007    -78     -2     88       C  
ATOM    774  C   ASP A 100     -53.534  38.470  74.032  1.00 16.50           C  
ANISOU  774  C   ASP A 100     2045   2198   2025    -84     12     70       C  
ATOM    775  O   ASP A 100     -54.474  37.820  73.615  1.00 17.76           O  
ANISOU  775  O   ASP A 100     2181   2387   2179    -94     12     70       O  
ATOM    776  CB  ASP A 100     -53.404  40.844  73.164  1.00 16.35           C  
ANISOU  776  CB  ASP A 100     2020   2167   2025    -51      0    109       C  
ATOM    777  CG  ASP A 100     -52.994  41.683  74.374  1.00 18.87           C  
ANISOU  777  CG  ASP A 100     2365   2446   2360    -33     10    101       C  
ATOM    778  OD1 ASP A 100     -52.097  41.284  75.136  1.00 16.34           O  
ANISOU  778  OD1 ASP A 100     2069   2104   2035    -43     13     83       O  
ATOM    779  OD2 ASP A 100     -53.587  42.757  74.534  1.00 17.33           O  
ANISOU  779  OD2 ASP A 100     2165   2240   2180    -10     16    115       O  
ATOM    780  N   TYR A 101     -53.095  38.363  75.289  1.00 15.95           N  
ANISOU  780  N   TYR A 101     2001   2100   1959    -80     22     55       N  
ATOM    781  CA  TYR A 101     -53.705  37.461  76.284  1.00 16.53           C  
ANISOU  781  CA  TYR A 101     2079   2173   2028    -86     37     40       C  
ATOM    782  C   TYR A 101     -53.690  36.012  75.816  1.00 15.20           C  
ANISOU  782  C   TYR A 101     1904   2022   1847   -112     36     29       C  
ATOM    783  O   TYR A 101     -54.675  35.289  75.984  1.00 15.41           O  
ANISOU  783  O   TYR A 101     1918   2065   1872   -122     46     24       O  
ATOM    784  CB  TYR A 101     -55.116  37.922  76.702  1.00 17.44           C  
ANISOU  784  CB  TYR A 101     2175   2298   2153    -70     51     47       C  
ATOM    785  CG  TYR A 101     -55.148  39.277  77.352  1.00 17.42           C  
ANISOU  785  CG  TYR A 101     2182   2271   2164    -42     58     53       C  
ATOM    786  CD1 TYR A 101     -55.047  39.403  78.733  1.00 17.85           C  
ANISOU  786  CD1 TYR A 101     2263   2300   2219    -34     73     39       C  
ATOM    787  CD2 TYR A 101     -55.274  40.436  76.584  1.00 18.54           C  
ANISOU  787  CD2 TYR A 101     2311   2415   2319    -25     49     73       C  
ATOM    788  CE1 TYR A 101     -55.074  40.640  79.332  1.00 19.00           C  
ANISOU  788  CE1 TYR A 101     2421   2422   2377    -11     81     40       C  
ATOM    789  CE2 TYR A 101     -55.298  41.667  77.155  1.00 17.95           C  
ANISOU  789  CE2 TYR A 101     2247   2313   2258      0     57     77       C  
ATOM    790  CZ  TYR A 101     -55.196  41.764  78.552  1.00 18.75           C  
ANISOU  790  CZ  TYR A 101     2375   2388   2359      6     74     59       C  
ATOM    791  OH  TYR A 101     -55.202  43.053  79.081  1.00 22.95           O  
ANISOU  791  OH  TYR A 101     2921   2891   2907     30     83     60       O  
ATOM    792  N   ASP A 102     -52.543  35.578  75.282  1.00 16.25           N  
ANISOU  792  N   ASP A 102     2050   2150   1974   -125     26     24       N  
ATOM    793  CA  ASP A 102     -52.387  34.214  74.742  1.00 15.82           C  
ANISOU  793  CA  ASP A 102     1994   2108   1910   -150     26     12       C  
ATOM    794  C   ASP A 102     -52.089  33.178  75.840  1.00 15.62           C  
ANISOU  794  C   ASP A 102     1991   2062   1882   -157     38     -4       C  
ATOM    795  O   ASP A 102     -50.938  32.743  76.063  1.00 14.97           O  
ANISOU  795  O   ASP A 102     1929   1960   1799   -160     34    -11       O  
ATOM    796  CB  ASP A 102     -51.341  34.182  73.621  1.00 16.12           C  
ANISOU  796  CB  ASP A 102     2032   2151   1942   -159     13     13       C  
ATOM    797  CG  ASP A 102     -51.373  32.891  72.801  1.00 15.33           C  
ANISOU  797  CG  ASP A 102     1925   2069   1830   -184     14      0       C  
ATOM    798  OD1 ASP A 102     -52.360  32.091  72.884  1.00 16.08           O  
ANISOU  798  OD1 ASP A 102     2010   2177   1922   -197     22     -8       O  
ATOM    799  OD2 ASP A 102     -50.411  32.740  72.021  1.00 16.30           O  
ANISOU  799  OD2 ASP A 102     2053   2192   1948   -191      9     -3       O  
ATOM    800  N   ILE A 103     -53.168  32.758  76.517  1.00 16.22           N  
ANISOU  800  N   ILE A 103     2062   2142   1958   -159     52     -7       N  
ATOM    801  CA  ILE A 103     -53.029  31.782  77.607  1.00 16.91           C  
ANISOU  801  CA  ILE A 103     2172   2210   2042   -166     65    -18       C  
ATOM    802  C   ILE A 103     -54.334  30.996  77.712  1.00 16.24           C  
ANISOU  802  C   ILE A 103     2072   2143   1957   -181     81    -22       C  
ATOM    803  O   ILE A 103     -55.443  31.526  77.462  1.00 16.94           O  
ANISOU  803  O   ILE A 103     2133   2253   2050   -178     84    -15       O  
ATOM    804  CB  ILE A 103     -52.641  32.480  78.951  1.00 16.72           C  
ANISOU  804  CB  ILE A 103     2173   2161   2019   -146     69    -16       C  
ATOM    805  CG1 ILE A 103     -52.352  31.414  80.022  1.00 18.39           C  
ANISOU  805  CG1 ILE A 103     2411   2353   2223   -153     80    -24       C  
ATOM    806  CG2 ILE A 103     -53.708  33.520  79.343  1.00 17.89           C  
ANISOU  806  CG2 ILE A 103     2308   2316   2173   -129     79     -9       C  
ATOM    807  CD1 ILE A 103     -51.768  31.965  81.319  1.00 19.38           C  
ANISOU  807  CD1 ILE A 103     2566   2455   2343   -136     80    -24       C  
ATOM    808  N   ALA A 104     -54.187  29.706  77.989  1.00 14.67           N  
ANISOU  808  N   ALA A 104     1887   1933   1754   -200     90    -32       N  
ATOM    809  CA  ALA A 104     -55.349  28.876  78.216  1.00 17.73           C  
ANISOU  809  CA  ALA A 104     2263   2332   2142   -218    108    -37       C  
ATOM    810  C   ALA A 104     -55.060  27.912  79.328  1.00 16.74           C  
ANISOU  810  C   ALA A 104     2169   2180   2013   -224    124    -42       C  
ATOM    811  O   ALA A 104     -53.905  27.567  79.548  1.00 17.16           O  
ANISOU  811  O   ALA A 104     2247   2210   2063   -219    117    -44       O  
ATOM    812  CB  ALA A 104     -55.718  28.115  76.959  1.00 18.67           C  
ANISOU  812  CB  ALA A 104     2360   2473   2259   -244    103    -45       C  
ATOM    813  N   LEU A 105     -56.123  27.453  79.992  1.00 17.45           N  
ANISOU  813  N   LEU A 105     2253   2273   2103   -234    145    -42       N  
ATOM    814  CA  LEU A 105     -55.987  26.440  81.034  1.00 17.93           C  
ANISOU  814  CA  LEU A 105     2344   2309   2159   -242    162    -44       C  
ATOM    815  C   LEU A 105     -56.736  25.175  80.600  1.00 17.81           C  
ANISOU  815  C   LEU A 105     2318   2301   2148   -275    177    -53       C  
ATOM    816  O   LEU A 105     -57.893  25.238  80.163  1.00 19.99           O  
ANISOU  816  O   LEU A 105     2562   2604   2430   -289    183    -55       O  
ATOM    817  CB  LEU A 105     -56.523  26.977  82.367  1.00 18.75           C  
ANISOU  817  CB  LEU A 105     2459   2408   2258   -227    180    -37       C  
ATOM    818  CG  LEU A 105     -55.989  28.341  82.799  1.00 18.10           C  
ANISOU  818  CG  LEU A 105     2384   2320   2171   -197    168    -32       C  
ATOM    819  CD1 LEU A 105     -56.923  28.918  83.895  1.00 19.61           C  
ANISOU  819  CD1 LEU A 105     2577   2515   2360   -185    190    -28       C  
ATOM    820  CD2 LEU A 105     -54.552  28.201  83.293  1.00 22.89           C  
ANISOU  820  CD2 LEU A 105     3028   2900   2771   -187    154    -31       C  
ATOM    821  N   LEU A 106     -56.043  24.051  80.704  1.00 18.12           N  
ANISOU  821  N   LEU A 106     2383   2314   2186   -287    181    -58       N  
ATOM    822  CA  LEU A 106     -56.550  22.751  80.249  1.00 19.21           C  
ANISOU  822  CA  LEU A 106     2518   2451   2331   -320    194    -69       C  
ATOM    823  C   LEU A 106     -56.824  21.865  81.453  1.00 18.67           C  
ANISOU  823  C   LEU A 106     2477   2357   2261   -328    220    -63       C  
ATOM    824  O   LEU A 106     -55.927  21.629  82.270  1.00 19.98           O  
ANISOU  824  O   LEU A 106     2677   2493   2420   -313    220    -55       O  
ATOM    825  CB  LEU A 106     -55.533  22.092  79.321  1.00 17.95           C  
ANISOU  825  CB  LEU A 106     2369   2278   2174   -327    182    -80       C  
ATOM    826  CG  LEU A 106     -55.342  22.625  77.891  1.00 22.64           C  
ANISOU  826  CG  LEU A 106     2937   2900   2767   -330    161    -89       C  
ATOM    827  CD1 LEU A 106     -55.285  24.102  77.715  1.00 24.92           C  
ANISOU  827  CD1 LEU A 106     3208   3210   3052   -305    143    -78       C  
ATOM    828  CD2 LEU A 106     -54.101  22.024  77.283  1.00 21.45           C  
ANISOU  828  CD2 LEU A 106     2805   2728   2617   -330    153    -98       C  
ATOM    829  N   GLU A 107     -58.070  21.418  81.588  1.00 20.88           N  
ANISOU  829  N   GLU A 107     2739   2650   2545   -353    241    -66       N  
ATOM    830  CA  GLU A 107     -58.445  20.533  82.714  1.00 21.09           C  
ANISOU  830  CA  GLU A 107     2791   2652   2570   -365    269    -59       C  
ATOM    831  C   GLU A 107     -58.395  19.076  82.259  1.00 21.23           C  
ANISOU  831  C   GLU A 107     2820   2649   2596   -397    280    -70       C  
ATOM    832  O   GLU A 107     -59.030  18.698  81.266  1.00 21.17           O  
ANISOU  832  O   GLU A 107     2786   2660   2598   -426    280    -85       O  
ATOM    833  CB  GLU A 107     -59.826  20.861  83.253  1.00 21.58           C  
ANISOU  833  CB  GLU A 107     2828   2737   2632   -374    291    -55       C  
ATOM    834  CG  GLU A 107     -60.151  20.141  84.546  1.00 23.76           C  
ANISOU  834  CG  GLU A 107     3134   2991   2903   -382    322    -44       C  
ATOM    835  CD  GLU A 107     -61.519  20.571  85.097  1.00 25.61           C  
ANISOU  835  CD  GLU A 107     3340   3250   3139   -388    347    -40       C  
ATOM    836  OE1 GLU A 107     -62.356  21.145  84.352  1.00 27.69           O  
ANISOU  836  OE1 GLU A 107     3558   3549   3412   -394    341    -48       O  
ATOM    837  OE2 GLU A 107     -61.764  20.308  86.286  1.00 28.10           O  
ANISOU  837  OE2 GLU A 107     3680   3551   3444   -388    373    -29       O  
ATOM    838  N   LEU A 108     -57.609  18.284  82.969  1.00 20.82           N  
ANISOU  838  N   LEU A 108     2810   2558   2543   -391    288    -61       N  
ATOM    839  CA  LEU A 108     -57.526  16.835  82.714  1.00 21.15           C  
ANISOU  839  CA  LEU A 108     2871   2570   2596   -419    303    -69       C  
ATOM    840  C   LEU A 108     -58.771  16.143  83.194  1.00 23.17           C  
ANISOU  840  C   LEU A 108     3122   2826   2857   -452    335    -68       C  
ATOM    841  O   LEU A 108     -59.282  16.470  84.263  1.00 23.48           O  
ANISOU  841  O   LEU A 108     3166   2869   2887   -444    351    -53       O  
ATOM    842  CB  LEU A 108     -56.293  16.229  83.395  1.00 21.06           C  
ANISOU  842  CB  LEU A 108     2905   2516   2582   -399    302    -56       C  
ATOM    843  CG  LEU A 108     -54.972  16.957  83.069  1.00 22.01           C  
ANISOU  843  CG  LEU A 108     3028   2635   2697   -365    272    -55       C  
ATOM    844  CD1 LEU A 108     -53.859  16.392  83.945  1.00 22.20           C  
ANISOU  844  CD1 LEU A 108     3095   2620   2719   -342    271    -38       C  
ATOM    845  CD2 LEU A 108     -54.624  16.895  81.563  1.00 21.60           C  
ANISOU  845  CD2 LEU A 108     2956   2595   2656   -375    257    -77       C  
ATOM    846  N   GLU A 109     -59.249  15.173  82.413  1.00 23.81           N  
ANISOU  846  N   GLU A 109     3194   2903   2952   -490    345    -86       N  
ATOM    847  CA  GLU A 109     -60.378  14.342  82.852  1.00 25.33           C  
ANISOU  847  CA  GLU A 109     3382   3089   3151   -527    378    -86       C  
ATOM    848  C   GLU A 109     -60.076  13.571  84.129  1.00 24.59           C  
ANISOU  848  C   GLU A 109     3336   2953   3055   -522    402    -65       C  
ATOM    849  O   GLU A 109     -60.946  13.448  85.006  1.00 24.81           O  
ANISOU  849  O   GLU A 109     3364   2982   3079   -535    429    -53       O  
ATOM    850  CB  GLU A 109     -60.817  13.421  81.729  1.00 25.98           C  
ANISOU  850  CB  GLU A 109     3450   3173   3249   -570    382   -112       C  
ATOM    851  CG  GLU A 109     -62.051  12.605  82.099  1.00 30.59           C  
ANISOU  851  CG  GLU A 109     4026   3754   3844   -614    415   -114       C  
ATOM    852  CD  GLU A 109     -62.417  11.607  81.027  1.00 35.30           C  
ANISOU  852  CD  GLU A 109     4612   4346   4455   -661    419   -143       C  
ATOM    853  OE1 GLU A 109     -62.676  10.418  81.364  1.00 37.84           O  
ANISOU  853  OE1 GLU A 109     4957   4630   4789   -692    447   -145       O  
ATOM    854  OE2 GLU A 109     -62.431  12.025  79.851  1.00 33.92           O  
ANISOU  854  OE2 GLU A 109     4407   4203   4278   -666    394   -163       O  
ATOM    855  N   LYS A 110     -58.855  13.037  84.214  1.00 23.71           N  
ANISOU  855  N   LYS A 110     3262   2802   2944   -504    394    -59       N  
ATOM    856  CA  LYS A 110     -58.378  12.298  85.375  1.00 24.27           C  
ANISOU  856  CA  LYS A 110     3382   2830   3011   -493    412    -35       C  
ATOM    857  C   LYS A 110     -57.019  12.830  85.813  1.00 23.44           C  
ANISOU  857  C   LYS A 110     3300   2712   2893   -447    387    -19       C  
ATOM    858  O   LYS A 110     -56.197  13.206  84.987  1.00 23.35           O  
ANISOU  858  O   LYS A 110     3280   2707   2886   -430    360    -31       O  
ATOM    859  CB  LYS A 110     -58.268  10.805  85.068  1.00 24.82           C  
ANISOU  859  CB  LYS A 110     3476   2855   3101   -522    432    -42       C  
ATOM    860  CG  LYS A 110     -59.562  10.182  84.581  1.00 27.32           C  
ANISOU  860  CG  LYS A 110     3768   3180   3431   -574    456    -60       C  
ATOM    861  CD  LYS A 110     -59.382   8.696  84.378  1.00 28.33           C  
ANISOU  861  CD  LYS A 110     3928   3258   3579   -601    478    -67       C  
ATOM    862  CE  LYS A 110     -60.635   8.114  83.714  1.00 31.24           C  
ANISOU  862  CE  LYS A 110     4269   3639   3963   -658    498    -92       C  
ATOM    863  NZ  LYS A 110     -60.596   6.620  83.538  1.00 34.93           N  
ANISOU  863  NZ  LYS A 110     4768   4052   4452   -691    524   -101       N  
ATOM    864  N   PRO A 111     -56.754  12.846  87.111  1.00 23.83           N  
ANISOU  864  N   PRO A 111     3382   2746   2926   -426    394      8       N  
ATOM    865  CA  PRO A 111     -55.538  13.510  87.519  1.00 24.13           C  
ANISOU  865  CA  PRO A 111     3437   2781   2951   -384    366     20       C  
ATOM    866  C   PRO A 111     -54.235  12.839  87.139  1.00 24.73           C  
ANISOU  866  C   PRO A 111     3534   2822   3038   -367    350     22       C  
ATOM    867  O   PRO A 111     -54.123  11.605  87.048  1.00 25.21           O  
ANISOU  867  O   PRO A 111     3618   2845   3115   -382    367     24       O  
ATOM    868  CB  PRO A 111     -55.659  13.580  89.043  1.00 24.10           C  
ANISOU  868  CB  PRO A 111     3465   2769   2923   -371    379     49       C  
ATOM    869  CG  PRO A 111     -56.630  12.510  89.402  1.00 24.74           C  
ANISOU  869  CG  PRO A 111     3558   2831   3011   -406    418     55       C  
ATOM    870  CD  PRO A 111     -57.588  12.438  88.246  1.00 23.59           C  
ANISOU  870  CD  PRO A 111     3371   2707   2886   -442    426     27       C  
ATOM    871  N   ALA A 112     -53.230  13.668  86.894  1.00 24.46           N  
ANISOU  871  N   ALA A 112     3494   2801   3000   -336    318     20       N  
ATOM    872  CA  ALA A 112     -51.850  13.214  86.829  1.00 24.41           C  
ANISOU  872  CA  ALA A 112     3509   2766   3001   -310    301     28       C  
ATOM    873  C   ALA A 112     -51.424  12.489  88.106  1.00 25.91           C  
ANISOU  873  C   ALA A 112     3742   2921   3182   -295    309     60       C  
ATOM    874  O   ALA A 112     -51.868  12.829  89.227  1.00 26.41           O  
ANISOU  874  O   ALA A 112     3819   2992   3221   -292    316     79       O  
ATOM    875  CB  ALA A 112     -50.944  14.410  86.586  1.00 23.96           C  
ANISOU  875  CB  ALA A 112     3434   2733   2936   -280    267     25       C  
ATOM    876  N   GLU A 113     -50.586  11.470  87.953  1.00 26.82           N  
ANISOU  876  N   GLU A 113     3880   2997   3315   -285    310     67       N  
ATOM    877  CA  GLU A 113     -49.951  10.873  89.129  1.00 28.17           C  
ANISOU  877  CA  GLU A 113     4090   3136   3476   -263    310    102       C  
ATOM    878  C   GLU A 113     -48.511  11.363  89.142  1.00 27.29           C  
ANISOU  878  C   GLU A 113     3977   3027   3364   -223    273    109       C  
ATOM    879  O   GLU A 113     -47.770  11.081  88.203  1.00 28.18           O  
ANISOU  879  O   GLU A 113     4078   3129   3501   -215    265     95       O  
ATOM    880  CB  GLU A 113     -49.964   9.346  89.044  1.00 29.07           C  
ANISOU  880  CB  GLU A 113     4232   3199   3614   -276    336    110       C  
ATOM    881  CG  GLU A 113     -51.355   8.748  88.970  1.00 33.83           C  
ANISOU  881  CG  GLU A 113     4836   3796   4223   -320    374    101       C  
ATOM    882  CD  GLU A 113     -51.325   7.251  89.210  1.00 38.99           C  
ANISOU  882  CD  GLU A 113     5526   4392   4895   -331    402    116       C  
ATOM    883  OE1 GLU A 113     -50.439   6.573  88.643  1.00 42.06           O  
ANISOU  883  OE1 GLU A 113     5924   4748   5309   -317    397    112       O  
ATOM    884  OE2 GLU A 113     -52.167   6.760  89.977  1.00 43.45           O  
ANISOU  884  OE2 GLU A 113     6112   4944   5452   -353    430    134       O  
ATOM    885  N   TYR A 114     -48.099  12.068  90.195  1.00 26.93           N  
ANISOU  885  N   TYR A 114     3943   2997   3291   -199    253    131       N  
ATOM    886  CA  TYR A 114     -46.730  12.624  90.257  1.00 26.25           C  
ANISOU  886  CA  TYR A 114     3852   2918   3203   -163    215    137       C  
ATOM    887  C   TYR A 114     -45.710  11.496  90.369  1.00 27.06           C  
ANISOU  887  C   TYR A 114     3977   2980   3325   -141    212    157       C  
ATOM    888  O   TYR A 114     -46.015  10.458  90.999  1.00 29.01           O  
ANISOU  888  O   TYR A 114     4257   3193   3573   -146    233    180       O  
ATOM    889  CB  TYR A 114     -46.575  13.572  91.439  1.00 25.72           C  
ANISOU  889  CB  TYR A 114     3797   2876   3100   -147    195    154       C  
ATOM    890  CG  TYR A 114     -47.317  14.878  91.314  1.00 23.69           C  
ANISOU  890  CG  TYR A 114     3515   2660   2827   -159    193    133       C  
ATOM    891  CD1 TYR A 114     -47.904  15.272  90.105  1.00 24.50           C  
ANISOU  891  CD1 TYR A 114     3582   2779   2947   -178    201    103       C  
ATOM    892  CD2 TYR A 114     -47.395  15.749  92.407  1.00 24.94           C  
ANISOU  892  CD2 TYR A 114     3686   2839   2950   -149    181    144       C  
ATOM    893  CE1 TYR A 114     -48.584  16.489  89.999  1.00 25.54           C  
ANISOU  893  CE1 TYR A 114     3691   2947   3066   -186    199     88       C  
ATOM    894  CE2 TYR A 114     -48.056  16.987  92.312  1.00 24.25           C  
ANISOU  894  CE2 TYR A 114     3577   2786   2850   -157    181    125       C  
ATOM    895  CZ  TYR A 114     -48.654  17.334  91.104  1.00 24.88           C  
ANISOU  895  CZ  TYR A 114     3621   2881   2952   -175    190     98       C  
ATOM    896  OH  TYR A 114     -49.318  18.537  91.006  1.00 24.64           O  
ANISOU  896  OH  TYR A 114     3570   2882   2912   -179    190     82       O  
ATOM    897  N   SER A 115     -44.535  11.687  89.763  1.00 26.59           N  
ANISOU  897  N   SER A 115     3900   2921   3283   -117    187    151       N  
ATOM    898  CA  SER A 115     -43.449  10.664  89.689  1.00 28.07           C  
ANISOU  898  CA  SER A 115     4100   3070   3496    -91    182    167       C  
ATOM    899  C   SER A 115     -42.131  11.345  89.323  1.00 28.33           C  
ANISOU  899  C   SER A 115     4107   3120   3537    -61    146    162       C  
ATOM    900  O   SER A 115     -42.088  12.566  89.234  1.00 28.00           O  
ANISOU  900  O   SER A 115     4042   3117   3479    -62    126    149       O  
ATOM    901  CB  SER A 115     -43.764   9.668  88.579  1.00 28.80           C  
ANISOU  901  CB  SER A 115     4189   3131   3622   -110    213    145       C  
ATOM    902  OG  SER A 115     -43.654  10.312  87.307  1.00 29.55           O  
ANISOU  902  OG  SER A 115     4246   3251   3729   -119    207    109       O  
ATOM    903  N   SER A 116     -41.085  10.556  89.063  1.00 29.01           N  
ANISOU  903  N   SER A 116     4195   3177   3651    -35    142    172       N  
ATOM    904  CA  SER A 116     -39.795  11.042  88.530  1.00 29.87           C  
ANISOU  904  CA  SER A 116     4274   3299   3776     -8    113    165       C  
ATOM    905  C   SER A 116     -39.988  11.805  87.212  1.00 28.99           C  
ANISOU  905  C   SER A 116     4126   3215   3674    -28    117    125       C  
ATOM    906  O   SER A 116     -39.208  12.704  86.881  1.00 30.44           O  
ANISOU  906  O   SER A 116     4281   3426   3858    -15     91    116       O  
ATOM    907  CB  SER A 116     -38.831   9.852  88.297  1.00 30.28           C  
ANISOU  907  CB  SER A 116     4333   3309   3864     20    119    178       C  
ATOM    908  OG  SER A 116     -39.310   8.972  87.288  1.00 34.36           O  
ANISOU  908  OG  SER A 116     4852   3795   4407      0    156    154       O  
ATOM    909  N   MET A 117     -41.042  11.478  86.480  1.00 27.56           N  
ANISOU  909  N   MET A 117     3945   3028   3498    -60    147    101       N  
ATOM    910  CA  MET A 117     -41.219  12.038  85.142  1.00 26.39           C  
ANISOU  910  CA  MET A 117     3764   2903   3358    -79    152     65       C  
ATOM    911  C   MET A 117     -42.348  13.057  85.017  1.00 25.49           C  
ANISOU  911  C   MET A 117     3638   2828   3221   -108    153     50       C  
ATOM    912  O   MET A 117     -42.485  13.690  83.978  1.00 25.75           O  
ANISOU  912  O   MET A 117     3643   2885   3256   -121    152     24       O  
ATOM    913  CB  MET A 117     -41.422  10.920  84.117  1.00 27.54           C  
ANISOU  913  CB  MET A 117     3915   3018   3532    -94    184     44       C  
ATOM    914  CG  MET A 117     -40.208  10.044  83.898  1.00 27.43           C  
ANISOU  914  CG  MET A 117     3905   2969   3548    -64    185     50       C  
ATOM    915  SD  MET A 117     -38.916  10.913  82.981  1.00 30.33           S  
ANISOU  915  SD  MET A 117     4231   3365   3928    -42    161     34       S  
ATOM    916  CE  MET A 117     -39.470  10.850  81.273  1.00 30.67           C  
ANISOU  916  CE  MET A 117     4255   3417   3980    -76    188    -13       C  
ATOM    917  N   VAL A 118     -43.184  13.163  86.047  1.00 24.48           N  
ANISOU  917  N   VAL A 118     3530   2703   3070   -117    158     66       N  
ATOM    918  CA  VAL A 118     -44.412  13.950  85.998  1.00 23.19           C  
ANISOU  918  CA  VAL A 118     3356   2570   2886   -144    165     54       C  
ATOM    919  C   VAL A 118     -44.477  14.782  87.278  1.00 23.64           C  
ANISOU  919  C   VAL A 118     3424   2645   2913   -132    148     74       C  
ATOM    920  O   VAL A 118     -44.728  14.263  88.364  1.00 23.45           O  
ANISOU  920  O   VAL A 118     3431   2605   2876   -129    156     98       O  
ATOM    921  CB  VAL A 118     -45.679  13.031  85.788  1.00 22.65           C  
ANISOU  921  CB  VAL A 118     3299   2484   2823   -178    201     45       C  
ATOM    922  CG1 VAL A 118     -46.959  13.812  85.865  1.00 23.22           C  
ANISOU  922  CG1 VAL A 118     3358   2589   2876   -203    209     36       C  
ATOM    923  CG2 VAL A 118     -45.613  12.309  84.417  1.00 24.61           C  
ANISOU  923  CG2 VAL A 118     3535   2718   3098   -193    217     18       C  
ATOM    924  N   ARG A 119     -44.200  16.080  87.157  1.00 22.23           N  
ANISOU  924  N   ARG A 119     3223   2499   2723   -125    125     66       N  
ATOM    925  CA  ARG A 119     -44.199  16.954  88.329  1.00 22.22           C  
ANISOU  925  CA  ARG A 119     3234   2516   2694   -114    107     81       C  
ATOM    926  C   ARG A 119     -44.635  18.326  87.884  1.00 21.17           C  
ANISOU  926  C   ARG A 119     3074   2418   2552   -122     99     61       C  
ATOM    927  O   ARG A 119     -44.321  18.726  86.767  1.00 21.17           O  
ANISOU  927  O   ARG A 119     3047   2429   2568   -125     93     43       O  
ATOM    928  CB  ARG A 119     -42.795  17.100  88.920  1.00 23.10           C  
ANISOU  928  CB  ARG A 119     3352   2624   2803    -83     75     98       C  
ATOM    929  CG  ARG A 119     -42.160  15.865  89.528  1.00 27.15           C  
ANISOU  929  CG  ARG A 119     3891   3103   3323    -65     75    124       C  
ATOM    930  CD  ARG A 119     -40.882  16.296  90.214  1.00 36.69           C  
ANISOU  930  CD  ARG A 119     5100   4319   4522    -36     38    141       C  
ATOM    931  NE  ARG A 119     -40.084  15.183  90.707  1.00 43.67           N  
ANISOU  931  NE  ARG A 119     6002   5173   5416    -13     32    169       N  
ATOM    932  CZ  ARG A 119     -38.831  15.290  91.155  1.00 44.93           C  
ANISOU  932  CZ  ARG A 119     6158   5336   5577     16     -2    185       C  
ATOM    933  NH1 ARG A 119     -38.211  16.471  91.178  1.00 45.85           N  
ANISOU  933  NH1 ARG A 119     6252   5483   5684     21    -32    176       N  
ATOM    934  NH2 ARG A 119     -38.198  14.202  91.581  1.00 45.74           N  
ANISOU  934  NH2 ARG A 119     6278   5409   5691     38     -5    213       N  
ATOM    935  N   PRO A 120     -45.306  19.065  88.749  1.00 19.92           N  
ANISOU  935  N   PRO A 120     2925   2276   2368   -126    101     66       N  
ATOM    936  CA  PRO A 120     -45.750  20.426  88.415  1.00 19.47           C  
ANISOU  936  CA  PRO A 120     2845   2249   2304   -131     94     49       C  
ATOM    937  C   PRO A 120     -44.645  21.462  88.486  1.00 19.10           C  
ANISOU  937  C   PRO A 120     2789   2215   2254   -112     61     47       C  
ATOM    938  O   PRO A 120     -43.664  21.301  89.230  1.00 20.75           O  
ANISOU  938  O   PRO A 120     3013   2414   2455    -94     41     62       O  
ATOM    939  CB  PRO A 120     -46.771  20.718  89.508  1.00 20.20           C  
ANISOU  939  CB  PRO A 120     2956   2349   2370   -138    110     56       C  
ATOM    940  CG  PRO A 120     -46.233  19.984  90.713  1.00 18.93           C  
ANISOU  940  CG  PRO A 120     2832   2168   2192   -125    105     80       C  
ATOM    941  CD  PRO A 120     -45.601  18.711  90.162  1.00 19.91           C  
ANISOU  941  CD  PRO A 120     2958   2265   2340   -122    107     88       C  
ATOM    942  N   ILE A 121     -44.841  22.558  87.754  1.00 17.44           N  
ANISOU  942  N   ILE A 121     2552   2026   2049   -117     56     31       N  
ATOM    943  CA  ILE A 121     -43.968  23.695  87.833  1.00 18.39           C  
ANISOU  943  CA  ILE A 121     2663   2158   2165   -104     28     27       C  
ATOM    944  C   ILE A 121     -44.684  24.784  88.647  1.00 18.55           C  
ANISOU  944  C   ILE A 121     2692   2192   2162   -105     30     24       C  
ATOM    945  O   ILE A 121     -45.879  24.958  88.504  1.00 20.12           O  
ANISOU  945  O   ILE A 121     2886   2399   2358   -117     53     17       O  
ATOM    946  CB  ILE A 121     -43.595  24.209  86.393  1.00 17.56           C  
ANISOU  946  CB  ILE A 121     2524   2064   2084   -108     22     12       C  
ATOM    947  CG1 ILE A 121     -42.600  25.365  86.473  1.00 16.21           C  
ANISOU  947  CG1 ILE A 121     2343   1903   1912    -96     -6      9       C  
ATOM    948  CG2 ILE A 121     -44.840  24.604  85.547  1.00 18.38           C  
ANISOU  948  CG2 ILE A 121     2609   2184   2191   -125     42     -1       C  
ATOM    949  CD1 ILE A 121     -41.904  25.620  85.166  1.00 14.86           C  
ANISOU  949  CD1 ILE A 121     2144   1738   1764    -97    -14      0       C  
ATOM    950  N   SER A 122     -43.915  25.508  89.462  1.00 20.73           N  
ANISOU  950  N   SER A 122     2980   2472   2424    -93      6     27       N  
ATOM    951  CA  SER A 122     -44.441  26.594  90.297  1.00 19.96           C  
ANISOU  951  CA  SER A 122     2895   2386   2304    -93      7     20       C  
ATOM    952  C   SER A 122     -44.837  27.819  89.482  1.00 19.80           C  
ANISOU  952  C   SER A 122     2850   2379   2296    -97      9      4       C  
ATOM    953  O   SER A 122     -44.133  28.191  88.541  1.00 19.10           O  
ANISOU  953  O   SER A 122     2738   2293   2227    -96     -6     -2       O  
ATOM    954  CB  SER A 122     -43.388  27.025  91.315  1.00 21.61           C  
ANISOU  954  CB  SER A 122     3124   2595   2494    -81    -22     25       C  
ATOM    955  OG  SER A 122     -43.132  25.946  92.218  1.00 24.14           O  
ANISOU  955  OG  SER A 122     3470   2904   2797    -75    -24     44       O  
ATOM    956  N   LEU A 123     -45.966  28.413  89.834  1.00 19.07           N  
ANISOU  956  N   LEU A 123     2760   2293   2192   -101     29     -2       N  
ATOM    957  CA  LEU A 123     -46.409  29.652  89.205  1.00 18.87           C  
ANISOU  957  CA  LEU A 123     2713   2278   2177   -101     32    -15       C  
ATOM    958  C   LEU A 123     -45.814  30.850  89.929  1.00 19.36           C  
ANISOU  958  C   LEU A 123     2789   2339   2226    -93     14    -23       C  
ATOM    959  O   LEU A 123     -45.764  30.869  91.170  1.00 20.68           O  
ANISOU  959  O   LEU A 123     2987   2504   2368    -90     13    -22       O  
ATOM    960  CB  LEU A 123     -47.940  29.756  89.197  1.00 19.02           C  
ANISOU  960  CB  LEU A 123     2726   2306   2195   -107     64    -18       C  
ATOM    961  CG  LEU A 123     -48.690  28.707  88.380  1.00 19.45           C  
ANISOU  961  CG  LEU A 123     2762   2363   2263   -120     82    -14       C  
ATOM    962  CD1 LEU A 123     -50.153  28.796  88.757  1.00 21.68           C  
ANISOU  962  CD1 LEU A 123     3042   2655   2539   -126    113    -16       C  
ATOM    963  CD2 LEU A 123     -48.466  28.880  86.877  1.00 21.89           C  
ANISOU  963  CD2 LEU A 123     3040   2682   2598   -124     73    -19       C  
ATOM    964  N   PRO A 124     -45.367  31.869  89.178  1.00 18.32           N  
ANISOU  964  N   PRO A 124     2638   2210   2112    -91      0    -31       N  
ATOM    965  CA  PRO A 124     -44.843  33.088  89.807  1.00 19.11           C  
ANISOU  965  CA  PRO A 124     2751   2307   2204    -87    -15    -42       C  
ATOM    966  C   PRO A 124     -45.957  34.007  90.282  1.00 20.01           C  
ANISOU  966  C   PRO A 124     2873   2421   2308    -83      7    -52       C  
ATOM    967  O   PRO A 124     -46.964  34.173  89.599  1.00 20.89           O  
ANISOU  967  O   PRO A 124     2965   2538   2433    -83     28    -51       O  
ATOM    968  CB  PRO A 124     -44.032  33.738  88.679  1.00 18.11           C  
ANISOU  968  CB  PRO A 124     2599   2181   2103    -88    -33    -44       C  
ATOM    969  CG  PRO A 124     -44.851  33.425  87.461  1.00 17.50           C  
ANISOU  969  CG  PRO A 124     2494   2111   2044    -92    -15    -40       C  
ATOM    970  CD  PRO A 124     -45.329  31.969  87.703  1.00 18.05           C  
ANISOU  970  CD  PRO A 124     2571   2181   2105    -95      0    -31       C  
ATOM    971  N   ASP A 125     -45.758  34.618  91.442  1.00 21.43           N  
ANISOU  971  N   ASP A 125     3081   2596   2465    -80      2    -61       N  
ATOM    972  CA  ASP A 125     -46.652  35.691  91.889  1.00 21.55           C  
ANISOU  972  CA  ASP A 125     3106   2609   2475    -75     23    -75       C  
ATOM    973  C   ASP A 125     -46.633  36.831  90.887  1.00 20.80           C  
ANISOU  973  C   ASP A 125     2986   2509   2408    -72     20    -81       C  
ATOM    974  O   ASP A 125     -45.682  36.971  90.112  1.00 19.61           O  
ANISOU  974  O   ASP A 125     2821   2357   2275    -76     -3    -78       O  
ATOM    975  CB  ASP A 125     -46.170  36.278  93.221  1.00 23.27           C  
ANISOU  975  CB  ASP A 125     3359   2820   2662    -75     13    -89       C  
ATOM    976  CG  ASP A 125     -46.413  35.375  94.400  1.00 28.49           C  
ANISOU  976  CG  ASP A 125     4050   3486   3288    -76     21    -83       C  
ATOM    977  OD1 ASP A 125     -47.019  34.295  94.257  1.00 32.58           O  
ANISOU  977  OD1 ASP A 125     4563   4009   3806    -78     38    -68       O  
ATOM    978  OD2 ASP A 125     -45.961  35.760  95.496  1.00 34.79           O  
ANISOU  978  OD2 ASP A 125     4880   4282   4057    -77     10    -93       O  
ATOM    979  N   ALA A 126     -47.647  37.689  90.966  1.00 21.94           N  
ANISOU  979  N   ALA A 126     3130   2650   2556    -64     44    -89       N  
ATOM    980  CA  ALA A 126     -47.729  38.874  90.102  1.00 21.11           C  
ANISOU  980  CA  ALA A 126     3006   2538   2479    -58     44    -93       C  
ATOM    981  C   ALA A 126     -46.530  39.814  90.221  1.00 20.22           C  
ANISOU  981  C   ALA A 126     2904   2409   2369    -62     18   -103       C  
ATOM    982  O   ALA A 126     -46.102  40.396  89.234  1.00 20.68           O  
ANISOU  982  O   ALA A 126     2943   2463   2452    -64      7    -99       O  
ATOM    983  CB  ALA A 126     -49.003  39.602  90.382  1.00 22.36           C  
ANISOU  983  CB  ALA A 126     3164   2692   2639    -45     75    -99       C  
ATOM    984  N   SER A 127     -45.978  39.895  91.436  1.00 21.12           N  
ANISOU  984  N   SER A 127     3051   2518   2456    -67      8   -117       N  
ATOM    985  CA  SER A 127     -44.783  40.701  91.716  1.00 21.40           C  
ANISOU  985  CA  SER A 127     3099   2541   2491    -75    -19   -130       C  
ATOM    986  C   SER A 127     -43.437  40.092  91.255  1.00 21.74           C  
ANISOU  986  C   SER A 127     3127   2591   2541    -86    -53   -120       C  
ATOM    987  O   SER A 127     -42.395  40.711  91.438  1.00 22.15           O  
ANISOU  987  O   SER A 127     3185   2636   2595    -95    -77   -129       O  
ATOM    988  CB  SER A 127     -44.703  40.969  93.226  1.00 22.63           C  
ANISOU  988  CB  SER A 127     3295   2693   2612    -78    -20   -149       C  
ATOM    989  OG  SER A 127     -44.411  39.795  93.933  1.00 25.29           O  
ANISOU  989  OG  SER A 127     3645   3044   2920    -81    -30   -140       O  
ATOM    990  N   HIS A 128     -43.437  38.881  90.703  1.00 20.99           N  
ANISOU  990  N   HIS A 128     3014   2509   2450    -85    -54   -102       N  
ATOM    991  CA  HIS A 128     -42.203  38.165  90.430  1.00 21.23           C  
ANISOU  991  CA  HIS A 128     3034   2546   2484    -92    -82    -93       C  
ATOM    992  C   HIS A 128     -41.520  38.824  89.222  1.00 21.28           C  
ANISOU  992  C   HIS A 128     3013   2550   2524    -97    -93    -91       C  
ATOM    993  O   HIS A 128     -42.148  39.056  88.194  1.00 21.30           O  
ANISOU  993  O   HIS A 128     2995   2552   2545    -94    -77    -84       O  
ATOM    994  CB  HIS A 128     -42.520  36.689  90.130  1.00 20.53           C  
ANISOU  994  CB  HIS A 128     2937   2470   2395    -89    -74    -76       C  
ATOM    995  CG  HIS A 128     -41.333  35.769  90.208  1.00 21.68           C  
ANISOU  995  CG  HIS A 128     3079   2620   2539    -91   -100    -66       C  
ATOM    996  ND1 HIS A 128     -41.283  34.685  91.067  1.00 24.33           N  
ANISOU  996  ND1 HIS A 128     3434   2959   2852    -88   -103    -57       N  
ATOM    997  CD2 HIS A 128     -40.179  35.742  89.501  1.00 22.61           C  
ANISOU  997  CD2 HIS A 128     3175   2740   2677    -95   -122    -63       C  
ATOM    998  CE1 HIS A 128     -40.136  34.051  90.902  1.00 24.88           C  
ANISOU  998  CE1 HIS A 128     3493   3032   2929    -87   -127    -48       C  
ATOM    999  NE2 HIS A 128     -39.451  34.662  89.951  1.00 23.69           N  
ANISOU  999  NE2 HIS A 128     3316   2880   2805    -92   -138    -52       N  
ATOM   1000  N   VAL A 129     -40.248  39.163  89.386  1.00 20.64           N  
ANISOU 1000  N   VAL A 129     2931   2466   2446   -106   -121    -96       N  
ATOM   1001  CA  VAL A 129     -39.461  39.810  88.332  1.00 21.68           C  
ANISOU 1001  CA  VAL A 129     3038   2594   2606   -114   -132    -94       C  
ATOM   1002  C   VAL A 129     -38.541  38.809  87.654  1.00 21.16           C  
ANISOU 1002  C   VAL A 129     2947   2541   2553   -116   -147    -81       C  
ATOM   1003  O   VAL A 129     -37.777  38.096  88.303  1.00 21.32           O  
ANISOU 1003  O   VAL A 129     2972   2567   2561   -117   -166    -79       O  
ATOM   1004  CB  VAL A 129     -38.647  40.982  88.919  1.00 22.57           C  
ANISOU 1004  CB  VAL A 129     3163   2694   2719   -126   -151   -111       C  
ATOM   1005  CG1 VAL A 129     -37.713  41.615  87.878  1.00 23.19           C  
ANISOU 1005  CG1 VAL A 129     3215   2769   2828   -138   -162   -108       C  
ATOM   1006  CG2 VAL A 129     -39.592  42.038  89.512  1.00 23.12           C  
ANISOU 1006  CG2 VAL A 129     3258   2747   2780   -123   -132   -127       C  
ATOM   1007  N   PHE A 130     -38.629  38.762  86.329  1.00 20.58           N  
ANISOU 1007  N   PHE A 130     2847   2470   2501   -117   -136    -71       N  
ATOM   1008  CA  PHE A 130     -37.646  38.071  85.508  1.00 19.79           C  
ANISOU 1008  CA  PHE A 130     2722   2380   2418   -120   -147    -62       C  
ATOM   1009  C   PHE A 130     -36.891  39.164  84.724  1.00 20.09           C  
ANISOU 1009  C   PHE A 130     2742   2413   2479   -132   -154    -64       C  
ATOM   1010  O   PHE A 130     -37.367  39.650  83.692  1.00 20.50           O  
ANISOU 1010  O   PHE A 130     2782   2464   2545   -133   -138    -58       O  
ATOM   1011  CB  PHE A 130     -38.327  37.051  84.579  1.00 20.46           C  
ANISOU 1011  CB  PHE A 130     2793   2475   2508   -114   -127    -51       C  
ATOM   1012  CG  PHE A 130     -39.204  36.045  85.287  1.00 19.54           C  
ANISOU 1012  CG  PHE A 130     2694   2361   2371   -106   -116    -48       C  
ATOM   1013  CD1 PHE A 130     -38.667  34.891  85.871  1.00 19.70           C  
ANISOU 1013  CD1 PHE A 130     2721   2383   2382   -101   -126    -43       C  
ATOM   1014  CD2 PHE A 130     -40.589  36.216  85.303  1.00 19.22           C  
ANISOU 1014  CD2 PHE A 130     2662   2320   2323   -102    -93    -49       C  
ATOM   1015  CE1 PHE A 130     -39.501  33.945  86.506  1.00 20.07           C  
ANISOU 1015  CE1 PHE A 130     2786   2429   2411    -96   -113    -39       C  
ATOM   1016  CE2 PHE A 130     -41.428  35.284  85.945  1.00 22.34           C  
ANISOU 1016  CE2 PHE A 130     3072   2717   2700    -97    -79    -46       C  
ATOM   1017  CZ  PHE A 130     -40.880  34.152  86.520  1.00 19.98           C  
ANISOU 1017  CZ  PHE A 130     2781   2417   2391    -95    -88    -41       C  
ATOM   1018  N   PRO A 131     -35.736  39.585  85.231  1.00 19.63           N  
ANISOU 1018  N   PRO A 131     2682   2352   2425   -141   -178    -71       N  
ATOM   1019  CA  PRO A 131     -35.088  40.811  84.716  1.00 20.11           C  
ANISOU 1019  CA  PRO A 131     2731   2403   2506   -156   -183    -75       C  
ATOM   1020  C   PRO A 131     -34.518  40.641  83.317  1.00 18.90           C  
ANISOU 1020  C   PRO A 131     2547   2259   2377   -160   -178    -63       C  
ATOM   1021  O   PRO A 131     -34.132  39.546  82.943  1.00 17.59           O  
ANISOU 1021  O   PRO A 131     2364   2106   2213   -155   -179    -56       O  
ATOM   1022  CB  PRO A 131     -33.952  41.084  85.696  1.00 20.90           C  
ANISOU 1022  CB  PRO A 131     2837   2503   2603   -167   -213    -87       C  
ATOM   1023  CG  PRO A 131     -33.752  39.805  86.459  1.00 21.71           C  
ANISOU 1023  CG  PRO A 131     2944   2619   2686   -156   -227    -83       C  
ATOM   1024  CD  PRO A 131     -34.981  38.937  86.319  1.00 20.50           C  
ANISOU 1024  CD  PRO A 131     2801   2468   2520   -140   -202    -75       C  
ATOM   1025  N   ALA A 132     -34.453  41.737  82.571  1.00 19.35           N  
ANISOU 1025  N   ALA A 132     2596   2305   2450   -171   -170    -61       N  
ATOM   1026  CA  ALA A 132     -33.696  41.754  81.300  1.00 18.98           C  
ANISOU 1026  CA  ALA A 132     2519   2266   2425   -179   -166    -50       C  
ATOM   1027  C   ALA A 132     -32.315  41.157  81.476  1.00 20.19           C  
ANISOU 1027  C   ALA A 132     2652   2432   2588   -186   -186    -53       C  
ATOM   1028  O   ALA A 132     -31.623  41.440  82.455  1.00 19.58           O  
ANISOU 1028  O   ALA A 132     2581   2351   2509   -193   -208    -63       O  
ATOM   1029  CB  ALA A 132     -33.581  43.193  80.779  1.00 19.23           C  
ANISOU 1029  CB  ALA A 132     2551   2282   2474   -193   -160    -48       C  
ATOM   1030  N   GLY A 133     -31.907  40.293  80.561  1.00 18.92           N  
ANISOU 1030  N   GLY A 133     2466   2285   2435   -182   -178    -43       N  
ATOM   1031  CA  GLY A 133     -30.612  39.658  80.674  1.00 18.99           C  
ANISOU 1031  CA  GLY A 133     2453   2306   2457   -184   -194    -44       C  
ATOM   1032  C   GLY A 133     -30.641  38.256  81.270  1.00 18.51           C  
ANISOU 1032  C   GLY A 133     2395   2254   2384   -166   -201    -43       C  
ATOM   1033  O   GLY A 133     -29.690  37.493  81.052  1.00 19.81           O  
ANISOU 1033  O   GLY A 133     2536   2429   2561   -162   -207    -40       O  
ATOM   1034  N   LYS A 134     -31.690  37.919  82.022  1.00 18.08           N  
ANISOU 1034  N   LYS A 134     2369   2194   2307   -155   -198    -45       N  
ATOM   1035  CA  LYS A 134     -31.713  36.608  82.715  1.00 18.94           C  
ANISOU 1035  CA  LYS A 134     2485   2307   2403   -139   -205    -42       C  
ATOM   1036  C   LYS A 134     -31.797  35.465  81.733  1.00 18.81           C  
ANISOU 1036  C   LYS A 134     2454   2298   2395   -130   -186    -34       C  
ATOM   1037  O   LYS A 134     -32.625  35.478  80.813  1.00 17.48           O  
ANISOU 1037  O   LYS A 134     2286   2131   2226   -131   -162    -33       O  
ATOM   1038  CB  LYS A 134     -32.859  36.506  83.713  1.00 18.42           C  
ANISOU 1038  CB  LYS A 134     2454   2234   2310   -132   -202    -45       C  
ATOM   1039  CG  LYS A 134     -32.844  35.173  84.496  1.00 20.89           C  
ANISOU 1039  CG  LYS A 134     2778   2551   2610   -117   -209    -39       C  
ATOM   1040  CD  LYS A 134     -33.935  35.137  85.513  1.00 21.77           C  
ANISOU 1040  CD  LYS A 134     2923   2655   2692   -112   -205    -42       C  
ATOM   1041  CE  LYS A 134     -33.897  33.790  86.301  1.00 25.13           C  
ANISOU 1041  CE  LYS A 134     3362   3082   3104    -97   -211    -32       C  
ATOM   1042  NZ  LYS A 134     -32.571  33.513  86.904  1.00 29.17           N  
ANISOU 1042  NZ  LYS A 134     3864   3601   3620    -93   -242    -28       N  
ATOM   1043  N   ALA A 135     -30.930  34.468  81.946  1.00 18.52           N  
ANISOU 1043  N   ALA A 135     2404   2266   2366   -119   -196    -30       N  
ATOM   1044  CA  ALA A 135     -30.941  33.225  81.148  1.00 19.22           C  
ANISOU 1044  CA  ALA A 135     2481   2357   2464   -108   -177    -26       C  
ATOM   1045  C   ALA A 135     -32.066  32.333  81.666  1.00 19.48           C  
ANISOU 1045  C   ALA A 135     2543   2384   2477    -97   -167    -23       C  
ATOM   1046  O   ALA A 135     -32.166  32.030  82.866  1.00 20.99           O  
ANISOU 1046  O   ALA A 135     2753   2569   2652    -89   -182    -20       O  
ATOM   1047  CB  ALA A 135     -29.602  32.506  81.201  1.00 20.53           C  
ANISOU 1047  CB  ALA A 135     2622   2528   2649    -97   -190    -21       C  
ATOM   1048  N   ILE A 136     -32.931  31.980  80.747  1.00 16.74           N  
ANISOU 1048  N   ILE A 136     2197   2036   2127   -100   -141    -25       N  
ATOM   1049  CA AILE A 136     -34.029  31.058  81.040  0.50 15.88           C  
ANISOU 1049  CA AILE A 136     2111   1922   2003    -93   -126    -23       C  
ATOM   1050  CA BILE A 136     -34.136  31.170  80.963  0.50 17.77           C  
ANISOU 1050  CA BILE A 136     2350   2161   2242    -95   -125    -24       C  
ATOM   1051  C   ILE A 136     -34.174  30.050  79.899  1.00 16.24           C  
ANISOU 1051  C   ILE A 136     2145   1968   2058    -93   -103    -26       C  
ATOM   1052  O   ILE A 136     -33.404  30.056  78.922  1.00 17.28           O  
ANISOU 1052  O   ILE A 136     2253   2107   2207    -95    -97    -28       O  
ATOM   1053  CB AILE A 136     -35.347  31.812  81.378  0.50 15.24           C  
ANISOU 1053  CB AILE A 136     2050   1840   1903   -101   -119    -26       C  
ATOM   1054  CB BILE A 136     -35.411  32.087  80.888  0.50 18.05           C  
ANISOU 1054  CB BILE A 136     2398   2198   2261   -105   -114    -27       C  
ATOM   1055  CG1AILE A 136     -35.796  32.689  80.203  0.50 12.28           C  
ANISOU 1055  CG1AILE A 136     1661   1473   1532   -112   -106    -29       C  
ATOM   1056  CG1BILE A 136     -35.533  32.960  82.138  0.50 19.82           C  
ANISOU 1056  CG1BILE A 136     2642   2418   2473   -105   -132    -28       C  
ATOM   1057  CG2AILE A 136     -35.177  32.647  82.677  0.50 15.15           C  
ANISOU 1057  CG2AILE A 136     2054   1823   1878   -100   -141    -27       C  
ATOM   1058  CG2BILE A 136     -36.720  31.289  80.703  0.50 20.97           C  
ANISOU 1058  CG2BILE A 136     2782   2567   2619   -105    -93    -27       C  
ATOM   1059  CD1AILE A 136     -37.080  33.442  80.463  0.50 11.45           C  
ANISOU 1059  CD1AILE A 136     1572   1367   1413   -116    -98    -29       C  
ATOM   1060  CD1BILE A 136     -36.828  33.734  82.172  0.50 22.89           C  
ANISOU 1060  CD1BILE A 136     3044   2804   2848   -110   -119    -31       C  
ATOM   1061  N   TRP A 137     -35.082  29.095  80.061  1.00 17.23           N  
ANISOU 1061  N   TRP A 137     2288   2086   2173    -90    -88    -26       N  
ATOM   1062  CA  TRP A 137     -35.169  27.958  79.151  1.00 17.72           C  
ANISOU 1062  CA  TRP A 137     2345   2146   2244    -89    -66    -30       C  
ATOM   1063  C   TRP A 137     -36.489  27.812  78.425  1.00 17.07           C  
ANISOU 1063  C   TRP A 137     2268   2068   2149   -103    -45    -37       C  
ATOM   1064  O   TRP A 137     -37.546  27.906  79.004  1.00 16.39           O  
ANISOU 1064  O   TRP A 137     2199   1981   2048   -106    -42    -35       O  
ATOM   1065  CB  TRP A 137     -34.934  26.667  79.936  1.00 19.01           C  
ANISOU 1065  CB  TRP A 137     2522   2292   2411    -74    -67    -24       C  
ATOM   1066  CG  TRP A 137     -33.587  26.652  80.525  1.00 20.17           C  
ANISOU 1066  CG  TRP A 137     2658   2436   2571    -59    -89    -16       C  
ATOM   1067  CD1 TRP A 137     -33.189  27.193  81.729  1.00 24.39           C  
ANISOU 1067  CD1 TRP A 137     3199   2970   3096    -53   -117     -8       C  
ATOM   1068  CD2 TRP A 137     -32.429  26.122  79.915  1.00 24.26           C  
ANISOU 1068  CD2 TRP A 137     3152   2952   3112    -49    -87    -17       C  
ATOM   1069  NE1 TRP A 137     -31.841  27.012  81.895  1.00 24.84           N  
ANISOU 1069  NE1 TRP A 137     3237   3028   3171    -40   -134     -2       N  
ATOM   1070  CE2 TRP A 137     -31.341  26.377  80.785  1.00 26.01           C  
ANISOU 1070  CE2 TRP A 137     3365   3176   3343    -36   -116     -7       C  
ATOM   1071  CE3 TRP A 137     -32.194  25.460  78.699  1.00 23.16           C  
ANISOU 1071  CE3 TRP A 137     2998   2811   2989    -49    -63    -27       C  
ATOM   1072  CZ2 TRP A 137     -30.040  25.957  80.494  1.00 26.36           C  
ANISOU 1072  CZ2 TRP A 137     3382   3221   3413    -21   -121     -5       C  
ATOM   1073  CZ3 TRP A 137     -30.903  25.052  78.402  1.00 24.74           C  
ANISOU 1073  CZ3 TRP A 137     3174   3010   3215    -35    -65    -26       C  
ATOM   1074  CH2 TRP A 137     -29.836  25.294  79.306  1.00 27.15           C  
ANISOU 1074  CH2 TRP A 137     3468   3318   3531    -20    -94    -14       C  
ATOM   1075  N   VAL A 138     -36.421  27.538  77.134  1.00 16.32           N  
ANISOU 1075  N   VAL A 138     2159   1982   2061   -111    -28    -46       N  
ATOM   1076  CA  VAL A 138     -37.600  27.067  76.414  1.00 16.53           C  
ANISOU 1076  CA  VAL A 138     2190   2014   2076   -124     -8    -54       C  
ATOM   1077  C   VAL A 138     -37.410  25.593  76.061  1.00 16.25           C  
ANISOU 1077  C   VAL A 138     2159   1965   2049   -122      9    -63       C  
ATOM   1078  O   VAL A 138     -36.296  25.153  75.753  1.00 16.45           O  
ANISOU 1078  O   VAL A 138     2174   1985   2092   -112     11    -65       O  
ATOM   1079  CB  VAL A 138     -37.847  27.906  75.112  1.00 16.86           C  
ANISOU 1079  CB  VAL A 138     2215   2078   2113   -138     -2    -58       C  
ATOM   1080  CG1 VAL A 138     -36.631  27.831  74.117  1.00 16.20           C  
ANISOU 1080  CG1 VAL A 138     2111   2000   2043   -138      3    -63       C  
ATOM   1081  CG2 VAL A 138     -39.162  27.528  74.446  1.00 17.83           C  
ANISOU 1081  CG2 VAL A 138     2341   2212   2221   -154     13    -65       C  
ATOM   1082  N   THR A 139     -38.496  24.832  76.150  1.00 16.67           N  
ANISOU 1082  N   THR A 139     2227   2012   2093   -131     22    -67       N  
ATOM   1083  CA  THR A 139     -38.474  23.412  75.823  1.00 17.23           C  
ANISOU 1083  CA  THR A 139     2307   2066   2172   -132     42    -78       C  
ATOM   1084  C   THR A 139     -39.613  23.046  74.883  1.00 17.51           C  
ANISOU 1084  C   THR A 139     2343   2114   2196   -155     60    -92       C  
ATOM   1085  O   THR A 139     -40.678  23.659  74.894  1.00 17.22           O  
ANISOU 1085  O   THR A 139     2305   2093   2144   -168     57    -90       O  
ATOM   1086  CB  THR A 139     -38.559  22.524  77.082  1.00 17.35           C  
ANISOU 1086  CB  THR A 139     2346   2056   2192   -120     41    -68       C  
ATOM   1087  OG1 THR A 139     -39.644  22.963  77.904  1.00 17.38           O  
ANISOU 1087  OG1 THR A 139     2362   2063   2177   -127     36    -60       O  
ATOM   1088  CG2 THR A 139     -37.272  22.584  77.883  1.00 18.71           C  
ANISOU 1088  CG2 THR A 139     2515   2216   2377    -96     22    -54       C  
ATOM   1089  N   GLY A 140     -39.394  22.030  74.062  1.00 17.28           N  
ANISOU 1089  N   GLY A 140     2314   2076   2174   -162     79   -109       N  
ATOM   1090  CA  GLY A 140     -40.469  21.610  73.180  1.00 17.76           C  
ANISOU 1090  CA  GLY A 140     2377   2149   2223   -187     95   -125       C  
ATOM   1091  C   GLY A 140     -39.963  20.632  72.152  1.00 17.55           C  
ANISOU 1091  C   GLY A 140     2351   2114   2204   -193    116   -147       C  
ATOM   1092  O   GLY A 140     -38.741  20.382  72.046  1.00 17.46           O  
ANISOU 1092  O   GLY A 140     2335   2090   2210   -176    119   -148       O  
ATOM   1093  N   TRP A 141     -40.920  20.120  71.378  1.00 18.28           N  
ANISOU 1093  N   TRP A 141     2446   2215   2283   -219    130   -165       N  
ATOM   1094  CA  TRP A 141     -40.647  19.201  70.308  1.00 18.28           C  
ANISOU 1094  CA  TRP A 141     2450   2211   2287   -231    152   -191       C  
ATOM   1095  C   TRP A 141     -40.786  19.878  68.974  1.00 18.38           C  
ANISOU 1095  C   TRP A 141     2446   2261   2278   -249    152   -202       C  
ATOM   1096  O   TRP A 141     -40.864  19.198  67.944  1.00 19.76           O  
ANISOU 1096  O   TRP A 141     2624   2439   2445   -267    170   -227       O  
ATOM   1097  CB  TRP A 141     -41.650  18.058  70.410  1.00 18.74           C  
ANISOU 1097  CB  TRP A 141     2526   2251   2343   -252    168   -206       C  
ATOM   1098  CG  TRP A 141     -41.384  17.121  71.516  1.00 19.06           C  
ANISOU 1098  CG  TRP A 141     2588   2249   2405   -236    176   -198       C  
ATOM   1099  CD1 TRP A 141     -40.529  16.026  71.500  1.00 19.89           C  
ANISOU 1099  CD1 TRP A 141     2706   2318   2532   -222    194   -207       C  
ATOM   1100  CD2 TRP A 141     -42.006  17.114  72.807  1.00 18.76           C  
ANISOU 1100  CD2 TRP A 141     2561   2198   2368   -231    167   -177       C  
ATOM   1101  NE1 TRP A 141     -40.564  15.374  72.715  1.00 18.88           N  
ANISOU 1101  NE1 TRP A 141     2598   2156   2420   -208    195   -191       N  
ATOM   1102  CE2 TRP A 141     -41.492  15.988  73.513  1.00 17.64           C  
ANISOU 1102  CE2 TRP A 141     2441   2013   2247   -216    180   -173       C  
ATOM   1103  CE3 TRP A 141     -42.971  17.916  73.418  1.00 19.93           C  
ANISOU 1103  CE3 TRP A 141     2705   2367   2501   -238    153   -162       C  
ATOM   1104  CZ2 TRP A 141     -41.871  15.687  74.831  1.00 18.26           C  
ANISOU 1104  CZ2 TRP A 141     2538   2069   2329   -208    176   -152       C  
ATOM   1105  CZ3 TRP A 141     -43.345  17.624  74.750  1.00 20.89           C  
ANISOU 1105  CZ3 TRP A 141     2844   2466   2626   -230    151   -144       C  
ATOM   1106  CH2 TRP A 141     -42.815  16.493  75.422  1.00 19.41           C  
ANISOU 1106  CH2 TRP A 141     2679   2237   2457   -217    163   -139       C  
ATOM   1107  N   GLY A 142     -40.776  21.215  68.959  1.00 16.37           N  
ANISOU 1107  N   GLY A 142     2174   2032   2013   -244    132   -184       N  
ATOM   1108  CA  GLY A 142     -40.916  21.952  67.710  1.00 18.51           C  
ANISOU 1108  CA  GLY A 142     2430   2339   2262   -259    130   -189       C  
ATOM   1109  C   GLY A 142     -39.725  21.850  66.770  1.00 17.96           C  
ANISOU 1109  C   GLY A 142     2354   2272   2196   -255    144   -201       C  
ATOM   1110  O   GLY A 142     -38.725  21.144  67.027  1.00 17.48           O  
ANISOU 1110  O   GLY A 142     2299   2186   2159   -239    157   -207       O  
ATOM   1111  N   HIS A 143     -39.847  22.569  65.655  1.00 18.78           N  
ANISOU 1111  N   HIS A 143     2447   2412   2278   -269    142   -202       N  
ATOM   1112  CA  HIS A 143     -38.808  22.530  64.639  1.00 18.54           C  
ANISOU 1112  CA  HIS A 143     2410   2390   2245   -269    159   -214       C  
ATOM   1113  C   HIS A 143     -37.463  22.906  65.210  1.00 19.40           C  
ANISOU 1113  C   HIS A 143     2509   2482   2381   -242    157   -200       C  
ATOM   1114  O   HIS A 143     -37.347  23.888  65.963  1.00 17.53           O  
ANISOU 1114  O   HIS A 143     2264   2245   2151   -230    136   -175       O  
ATOM   1115  CB  HIS A 143     -39.147  23.442  63.470  1.00 19.18           C  
ANISOU 1115  CB  HIS A 143     2480   2512   2295   -287    154   -209       C  
ATOM   1116  CG  HIS A 143     -40.368  23.026  62.719  1.00 19.66           C  
ANISOU 1116  CG  HIS A 143     2547   2597   2327   -316    155   -226       C  
ATOM   1117  ND1 HIS A 143     -40.711  23.602  61.513  1.00 20.79           N  
ANISOU 1117  ND1 HIS A 143     2683   2780   2436   -335    152   -226       N  
ATOM   1118  CD2 HIS A 143     -41.327  22.106  62.989  1.00 20.10           C  
ANISOU 1118  CD2 HIS A 143     2614   2642   2380   -330    158   -242       C  
ATOM   1119  CE1 HIS A 143     -41.841  23.059  61.081  1.00 24.22           C  
ANISOU 1119  CE1 HIS A 143     3122   3230   2848   -360    150   -242       C  
ATOM   1120  NE2 HIS A 143     -42.242  22.161  61.966  1.00 24.20           N  
ANISOU 1120  NE2 HIS A 143     3131   3198   2866   -359    154   -253       N  
ATOM   1121  N   THR A 144     -36.452  22.141  64.787  1.00 18.22           N  
ANISOU 1121  N   THR A 144     2359   2318   2246   -234    180   -217       N  
ATOM   1122  CA  THR A 144     -35.077  22.302  65.269  1.00 19.95           C  
ANISOU 1122  CA  THR A 144     2565   2520   2494   -208    181   -207       C  
ATOM   1123  C   THR A 144     -34.201  23.165  64.381  1.00 20.03           C  
ANISOU 1123  C   THR A 144     2556   2556   2500   -210    187   -202       C  
ATOM   1124  O   THR A 144     -33.068  23.503  64.760  1.00 18.97           O  
ANISOU 1124  O   THR A 144     2405   2413   2389   -191    185   -191       O  
ATOM   1125  CB  THR A 144     -34.383  20.944  65.470  1.00 19.79           C  
ANISOU 1125  CB  THR A 144     2553   2467   2500   -193    203   -225       C  
ATOM   1126  OG1 THR A 144     -34.312  20.237  64.213  1.00 23.23           O  
ANISOU 1126  OG1 THR A 144     2994   2909   2923   -208    233   -255       O  
ATOM   1127  CG2 THR A 144     -35.132  20.104  66.491  1.00 21.42           C  
ANISOU 1127  CG2 THR A 144     2779   2644   2715   -189    197   -224       C  
ATOM   1128  N   GLN A 145     -34.711  23.480  63.192  1.00 20.40           N  
ANISOU 1128  N   GLN A 145     2604   2633   2515   -234    195   -211       N  
ATOM   1129  CA  GLN A 145     -34.049  24.438  62.252  1.00 21.60           C  
ANISOU 1129  CA  GLN A 145     2740   2813   2655   -240    201   -202       C  
ATOM   1130  C   GLN A 145     -35.169  25.171  61.565  1.00 19.24           C  
ANISOU 1130  C   GLN A 145     2446   2547   2318   -263    189   -194       C  
ATOM   1131  O   GLN A 145     -36.216  24.572  61.302  1.00 20.58           O  
ANISOU 1131  O   GLN A 145     2630   2723   2468   -279    189   -209       O  
ATOM   1132  CB  GLN A 145     -33.229  23.729  61.157  1.00 22.41           C  
ANISOU 1132  CB  GLN A 145     2840   2920   2754   -244    236   -228       C  
ATOM   1133  CG  GLN A 145     -32.146  22.842  61.661  1.00 29.17           C  
ANISOU 1133  CG  GLN A 145     3691   3745   3648   -220    253   -240       C  
ATOM   1134  CD  GLN A 145     -30.842  23.559  61.850  1.00 35.42           C  
ANISOU 1134  CD  GLN A 145     4455   4537   4464   -203    253   -223       C  
ATOM   1135  OE1 GLN A 145     -30.103  23.804  60.876  1.00 40.29           O  
ANISOU 1135  OE1 GLN A 145     5061   5174   5076   -209    275   -229       O  
ATOM   1136  NE2 GLN A 145     -30.529  23.897  63.105  1.00 37.87           N  
ANISOU 1136  NE2 GLN A 145     4757   4829   4802   -183    228   -201       N  
ATOM   1137  N   TYR A 146     -34.996  26.469  61.337  1.00 19.29           N  
ANISOU 1137  N   TYR A 146     2440   2573   2317   -265    177   -169       N  
ATOM   1138  CA  TYR A 146     -35.987  27.178  60.575  1.00 17.75           C  
ANISOU 1138  CA  TYR A 146     2248   2410   2086   -284    166   -159       C  
ATOM   1139  C   TYR A 146     -35.988  26.637  59.140  1.00 18.67           C  
ANISOU 1139  C   TYR A 146     2371   2553   2171   -305    190   -181       C  
ATOM   1140  O   TYR A 146     -34.949  26.600  58.504  1.00 20.78           O  
ANISOU 1140  O   TYR A 146     2632   2825   2440   -304    212   -188       O  
ATOM   1141  CB  TYR A 146     -35.776  28.702  60.571  1.00 17.99           C  
ANISOU 1141  CB  TYR A 146     2267   2453   2116   -281    150   -125       C  
ATOM   1142  CG  TYR A 146     -36.876  29.349  59.802  1.00 19.16           C  
ANISOU 1142  CG  TYR A 146     2418   2633   2227   -298    139   -112       C  
ATOM   1143  CD1 TYR A 146     -36.760  29.586  58.427  1.00 19.63           C  
ANISOU 1143  CD1 TYR A 146     2478   2725   2255   -315    152   -112       C  
ATOM   1144  CD2 TYR A 146     -38.095  29.640  60.417  1.00 18.21           C  
ANISOU 1144  CD2 TYR A 146     2303   2514   2104   -297    115   -100       C  
ATOM   1145  CE1 TYR A 146     -37.804  30.161  57.699  1.00 17.59           C  
ANISOU 1145  CE1 TYR A 146     2223   2500   1962   -330    138    -97       C  
ATOM   1146  CE2 TYR A 146     -39.146  30.210  59.704  1.00 18.32           C  
ANISOU 1146  CE2 TYR A 146     2316   2558   2086   -310    102    -86       C  
ATOM   1147  CZ  TYR A 146     -39.006  30.442  58.314  1.00 18.39           C  
ANISOU 1147  CZ  TYR A 146     2324   2601   2061   -327    112    -84       C  
ATOM   1148  OH  TYR A 146     -40.041  30.981  57.592  1.00 20.74           O  
ANISOU 1148  OH  TYR A 146     2622   2933   2327   -338     97    -68       O  
ATOM   1149  N   GLY A 147     -37.157  26.156  58.701  1.00 18.71           N  
ANISOU 1149  N   GLY A 147     2387   2574   2147   -324    185   -194       N  
ATOM   1150  CA  GLY A 147     -37.308  25.489  57.373  1.00 20.13           C  
ANISOU 1150  CA  GLY A 147     2576   2780   2291   -348    206   -222       C  
ATOM   1151  C   GLY A 147     -37.195  23.980  57.474  1.00 21.32           C  
ANISOU 1151  C   GLY A 147     2741   2905   2454   -350    229   -261       C  
ATOM   1152  O   GLY A 147     -37.211  23.271  56.460  1.00 21.77           O  
ANISOU 1152  O   GLY A 147     2809   2977   2486   -369    250   -290       O  
ATOM   1153  N   GLY A 148     -37.042  23.502  58.704  1.00 19.99           N  
ANISOU 1153  N   GLY A 148     2574   2699   2324   -330    224   -260       N  
ATOM   1154  CA  GLY A 148     -36.732  22.124  59.034  1.00 19.89           C  
ANISOU 1154  CA  GLY A 148     2573   2651   2333   -324    246   -290       C  
ATOM   1155  C   GLY A 148     -37.940  21.352  59.517  1.00 21.28           C  
ANISOU 1155  C   GLY A 148     2764   2816   2507   -337    237   -302       C  
ATOM   1156  O   GLY A 148     -39.052  21.540  59.022  1.00 21.33           O  
ANISOU 1156  O   GLY A 148     2773   2850   2481   -361    224   -304       O  
ATOM   1157  N   THR A 150     -37.704  20.484  60.494  1.00 22.17           N  
ANISOU 1157  N   THR A 150     2885   2886   2654   -320    243   -309       N  
ATOM   1158  CA ATHR A 150     -38.715  19.585  61.040  0.50 22.57           C  
ANISOU 1158  CA ATHR A 150     2951   2917   2707   -332    241   -322       C  
ATOM   1159  CA BTHR A 150     -38.768  19.652  61.050  0.50 22.31           C  
ANISOU 1159  CA BTHR A 150     2918   2886   2674   -332    239   -320       C  
ATOM   1160  C   THR A 150     -38.641  19.528  62.564  1.00 22.42           C  
ANISOU 1160  C   THR A 150     2933   2863   2723   -306    227   -300       C  
ATOM   1161  O   THR A 150     -37.646  19.967  63.165  1.00 21.99           O  
ANISOU 1161  O   THR A 150     2867   2794   2692   -279    223   -281       O  
ATOM   1162  CB ATHR A 150     -38.561  18.139  60.466  0.50 23.14           C  
ANISOU 1162  CB ATHR A 150     3043   2967   2782   -344    274   -364       C  
ATOM   1163  CB BTHR A 150     -38.855  18.238  60.359  0.50 23.14           C  
ANISOU 1163  CB BTHR A 150     3043   2976   2774   -351    269   -363       C  
ATOM   1164  OG1ATHR A 150     -37.214  17.693  60.633  0.50 25.61           O  
ANISOU 1164  OG1ATHR A 150     3355   3250   3126   -316    296   -369       O  
ATOM   1165  OG1BTHR A 150     -40.124  17.633  60.638  0.50 23.57           O  
ANISOU 1165  OG1BTHR A 150     3110   3026   2821   -374    262   -374       O  
ATOM   1166  CG2ATHR A 150     -38.896  18.110  59.000  0.50 23.63           C  
ANISOU 1166  CG2ATHR A 150     3109   3067   2802   -375    285   -389       C  
ATOM   1167  CG2BTHR A 150     -37.770  17.315  60.850  0.50 23.14           C  
ANISOU 1167  CG2BTHR A 150     3051   2929   2812   -325    294   -375       C  
ATOM   1168  N   GLY A 151     -39.678  18.958  63.157  1.00 22.73           N  
ANISOU 1168  N   GLY A 151     2984   2889   2763   -318    221   -304       N  
ATOM   1169  CA  GLY A 151     -39.732  18.760  64.617  1.00 21.87           C  
ANISOU 1169  CA  GLY A 151     2881   2746   2682   -297    211   -285       C  
ATOM   1170  C   GLY A 151     -38.823  17.674  65.142  1.00 22.03           C  
ANISOU 1170  C   GLY A 151     2914   2721   2735   -276    231   -294       C  
ATOM   1171  O   GLY A 151     -38.225  16.909  64.377  1.00 22.36           O  
ANISOU 1171  O   GLY A 151     2962   2752   2781   -277    257   -320       O  
ATOM   1172  N   ALA A 152     -38.713  17.615  66.468  1.00 21.53           N  
ANISOU 1172  N   ALA A 152     2855   2631   2695   -254    219   -272       N  
ATOM   1173  CA  ALA A 152     -37.836  16.706  67.178  1.00 23.22           C  
ANISOU 1173  CA  ALA A 152     3079   2802   2942   -227    232   -271       C  
ATOM   1174  C   ALA A 152     -38.599  15.538  67.771  1.00 23.02           C  
ANISOU 1174  C   ALA A 152     3078   2742   2925   -236    243   -279       C  
ATOM   1175  O   ALA A 152     -39.724  15.693  68.272  1.00 24.28           O  
ANISOU 1175  O   ALA A 152     3244   2908   3073   -252    231   -271       O  
ATOM   1176  CB  ALA A 152     -37.085  17.458  68.308  1.00 23.49           C  
ANISOU 1176  CB  ALA A 152     3101   2830   2993   -196    209   -237       C  
ATOM   1177  N   LEU A 153     -37.974  14.358  67.751  1.00 23.78           N  
ANISOU 1177  N   LEU A 153     3190   2799   3046   -224    268   -294       N  
ATOM   1178  CA  LEU A 153     -38.546  13.239  68.494  1.00 23.14           C  
ANISOU 1178  CA  LEU A 153     3135   2678   2981   -227    279   -296       C  
ATOM   1179  C   LEU A 153     -38.223  13.408  69.963  1.00 22.34           C  
ANISOU 1179  C   LEU A 153     3036   2556   2897   -197    260   -260       C  
ATOM   1180  O   LEU A 153     -39.076  13.197  70.821  1.00 22.53           O  
ANISOU 1180  O   LEU A 153     3074   2568   2918   -205    253   -247       O  
ATOM   1181  CB  LEU A 153     -37.955  11.899  68.038  1.00 23.48           C  
ANISOU 1181  CB  LEU A 153     3196   2679   3047   -221    313   -323       C  
ATOM   1182  CG  LEU A 153     -38.319  11.423  66.620  1.00 25.27           C  
ANISOU 1182  CG  LEU A 153     3428   2916   3255   -254    339   -366       C  
ATOM   1183  CD1 LEU A 153     -37.612  10.098  66.296  1.00 27.08           C  
ANISOU 1183  CD1 LEU A 153     3678   3098   3514   -242    376   -392       C  
ATOM   1184  CD2 LEU A 153     -39.840  11.312  66.429  1.00 29.22           C  
ANISOU 1184  CD2 LEU A 153     3939   3433   3730   -298    334   -379       C  
ATOM   1185  N   ILE A 154     -36.976  13.767  70.256  1.00 21.34           N  
ANISOU 1185  N   ILE A 154     2894   2426   2788   -163    251   -243       N  
ATOM   1186  CA  ILE A 154     -36.567  13.923  71.670  1.00 20.61           C  
ANISOU 1186  CA  ILE A 154     2803   2317   2710   -133    230   -209       C  
ATOM   1187  C   ILE A 154     -36.742  15.381  72.082  1.00 19.36           C  
ANISOU 1187  C   ILE A 154     2627   2197   2533   -134    198   -187       C  
ATOM   1188  O   ILE A 154     -36.323  16.296  71.373  1.00 20.01           O  
ANISOU 1188  O   ILE A 154     2687   2311   2606   -137    191   -191       O  
ATOM   1189  CB  ILE A 154     -35.120  13.419  71.960  1.00 22.54           C  
ANISOU 1189  CB  ILE A 154     3041   2534   2988    -94    235   -199       C  
ATOM   1190  CG1 ILE A 154     -35.098  11.875  71.805  1.00 23.94           C  
ANISOU 1190  CG1 ILE A 154     3244   2663   3189    -90    268   -217       C  
ATOM   1191  CG2 ILE A 154     -34.676  13.826  73.372  1.00 23.57           C  
ANISOU 1191  CG2 ILE A 154     3169   2658   3127    -66    205   -162       C  
ATOM   1192  CD1 ILE A 154     -33.802  11.167  72.167  1.00 28.91           C  
ANISOU 1192  CD1 ILE A 154     3870   3257   3856    -48    276   -206       C  
ATOM   1193  N   LEU A 155     -37.367  15.562  73.253  1.00 18.12           N  
ANISOU 1193  N   LEU A 155     2482   2034   2369   -133    181   -165       N  
ATOM   1194  CA  LEU A 155     -37.606  16.901  73.780  1.00 17.74           C  
ANISOU 1194  CA  LEU A 155     2421   2017   2303   -133    152   -146       C  
ATOM   1195  C   LEU A 155     -36.299  17.718  73.722  1.00 17.54           C  
ANISOU 1195  C   LEU A 155     2371   2006   2288   -110    136   -136       C  
ATOM   1196  O   LEU A 155     -35.222  17.265  74.151  1.00 19.29           O  
ANISOU 1196  O   LEU A 155     2590   2207   2533    -83    134   -126       O  
ATOM   1197  CB  LEU A 155     -38.076  16.812  75.242  1.00 15.85           C  
ANISOU 1197  CB  LEU A 155     2200   1762   2061   -124    139   -121       C  
ATOM   1198  CG  LEU A 155     -38.489  18.153  75.882  1.00 16.99           C  
ANISOU 1198  CG  LEU A 155     2335   1934   2185   -126    113   -104       C  
ATOM   1199  CD1 LEU A 155     -39.673  18.767  75.153  1.00 18.29           C  
ANISOU 1199  CD1 LEU A 155     2492   2128   2328   -156    116   -117       C  
ATOM   1200  CD2 LEU A 155     -38.793  18.056  77.376  1.00 17.18           C  
ANISOU 1200  CD2 LEU A 155     2379   1943   2205   -115    100    -81       C  
ATOM   1201  N   GLN A 156     -36.402  18.958  73.266  1.00 17.23           N  
ANISOU 1201  N   GLN A 156     2312   2000   2232   -121    123   -135       N  
ATOM   1202  CA  GLN A 156     -35.245  19.841  73.134  1.00 18.13           C  
ANISOU 1202  CA  GLN A 156     2402   2130   2355   -106    109   -126       C  
ATOM   1203  C   GLN A 156     -35.320  20.952  74.185  1.00 16.93           C  
ANISOU 1203  C   GLN A 156     2248   1990   2195    -99     79   -103       C  
ATOM   1204  O   GLN A 156     -36.435  21.382  74.582  1.00 15.94           O  
ANISOU 1204  O   GLN A 156     2134   1873   2050   -113     72    -99       O  
ATOM   1205  CB  GLN A 156     -35.276  20.570  71.803  1.00 19.21           C  
ANISOU 1205  CB  GLN A 156     2522   2298   2479   -124    116   -140       C  
ATOM   1206  CG  GLN A 156     -35.054  19.659  70.595  1.00 19.39           C  
ANISOU 1206  CG  GLN A 156     2545   2317   2507   -132    147   -167       C  
ATOM   1207  CD  GLN A 156     -33.718  18.946  70.612  1.00 18.01           C  
ANISOU 1207  CD  GLN A 156     2362   2119   2362   -106    159   -169       C  
ATOM   1208  OE1 GLN A 156     -32.670  19.548  70.385  1.00 20.84           O  
ANISOU 1208  OE1 GLN A 156     2696   2490   2731    -94    154   -164       O  
ATOM   1209  NE2 GLN A 156     -33.753  17.625  70.862  1.00 19.04           N  
ANISOU 1209  NE2 GLN A 156     2512   2216   2508    -97    176   -178       N  
ATOM   1210  N   LYS A 157     -34.135  21.415  74.600  1.00 17.70           N  
ANISOU 1210  N   LYS A 157     2330   2089   2308    -80     62    -91       N  
ATOM   1211  CA  LYS A 157     -34.064  22.592  75.457  1.00 16.68           C  
ANISOU 1211  CA  LYS A 157     2196   1973   2170    -77     33    -74       C  
ATOM   1212  C   LYS A 157     -33.171  23.651  74.857  1.00 16.85           C  
ANISOU 1212  C   LYS A 157     2189   2015   2198    -78     25    -74       C  
ATOM   1213  O   LYS A 157     -32.170  23.319  74.222  1.00 17.29           O  
ANISOU 1213  O   LYS A 157     2226   2070   2272    -70     35    -80       O  
ATOM   1214  CB  LYS A 157     -33.556  22.192  76.835  1.00 17.00           C  
ANISOU 1214  CB  LYS A 157     2246   1994   2220    -54     15    -56       C  
ATOM   1215  CG  LYS A 157     -32.146  21.532  76.802  1.00 16.33           C  
ANISOU 1215  CG  LYS A 157     2144   1896   2163    -30     15    -53       C  
ATOM   1216  CD  LYS A 157     -31.702  21.150  78.192  1.00 19.90           C  
ANISOU 1216  CD  LYS A 157     2607   2333   2621     -7     -7    -32       C  
ATOM   1217  CE  LYS A 157     -30.407  20.323  78.094  1.00 23.71           C  
ANISOU 1217  CE  LYS A 157     3072   2801   3136     20     -4    -28       C  
ATOM   1218  NZ  LYS A 157     -29.893  19.955  79.464  1.00 27.42           N  
ANISOU 1218  NZ  LYS A 157     3549   3258   3610     45    -30     -3       N  
ATOM   1219  N   GLY A 158     -33.530  24.911  75.052  1.00 16.13           N  
ANISOU 1219  N   GLY A 158     2095   1941   2093    -89      9    -67       N  
ATOM   1220  CA  GLY A 158     -32.714  25.987  74.587  1.00 18.09           C  
ANISOU 1220  CA  GLY A 158     2319   2207   2347    -92      0    -65       C  
ATOM   1221  C   GLY A 158     -32.610  27.071  75.627  1.00 16.87           C  
ANISOU 1221  C   GLY A 158     2166   2055   2188    -91    -28    -51       C  
ATOM   1222  O   GLY A 158     -33.593  27.380  76.304  1.00 16.76           O  
ANISOU 1222  O   GLY A 158     2172   2039   2157    -95    -35    -47       O  
ATOM   1223  N   GLU A 159     -31.407  27.612  75.764  1.00 17.16           N  
ANISOU 1223  N   GLU A 159     2182   2097   2242    -85    -42    -47       N  
ATOM   1224  CA  GLU A 159     -31.158  28.709  76.712  1.00 18.65           C  
ANISOU 1224  CA  GLU A 159     2370   2288   2428    -86    -70    -37       C  
ATOM   1225  C   GLU A 159     -31.268  30.065  76.017  1.00 17.75           C  
ANISOU 1225  C   GLU A 159     2245   2188   2309   -105    -69    -38       C  
ATOM   1226  O   GLU A 159     -30.602  30.311  74.990  1.00 17.25           O  
ANISOU 1226  O   GLU A 159     2161   2136   2258   -112    -57    -41       O  
ATOM   1227  CB  GLU A 159     -29.787  28.546  77.347  1.00 19.90           C  
ANISOU 1227  CB  GLU A 159     2510   2445   2607    -72    -89    -31       C  
ATOM   1228  CG  GLU A 159     -29.575  29.479  78.544  1.00 24.40           C  
ANISOU 1228  CG  GLU A 159     3085   3016   3171    -74   -121    -24       C  
ATOM   1229  CD  GLU A 159     -28.304  29.205  79.303  1.00 31.48           C  
ANISOU 1229  CD  GLU A 159     3964   3912   4084    -59   -145    -17       C  
ATOM   1230  OE1 GLU A 159     -27.364  28.610  78.724  1.00 36.48           O  
ANISOU 1230  OE1 GLU A 159     4571   4549   4742    -48   -137    -17       O  
ATOM   1231  OE2 GLU A 159     -28.253  29.579  80.495  1.00 32.66           O  
ANISOU 1231  OE2 GLU A 159     4125   4061   4222    -57   -173    -11       O  
ATOM   1232  N   ILE A 160     -32.144  30.923  76.536  1.00 16.63           N  
ANISOU 1232  N   ILE A 160     2121   2046   2150   -112    -78    -34       N  
ATOM   1233  CA  ILE A 160     -32.439  32.205  75.885  1.00 17.13           C  
ANISOU 1233  CA  ILE A 160     2180   2119   2210   -128    -75    -33       C  
ATOM   1234  C   ILE A 160     -32.499  33.259  76.962  1.00 17.72           C  
ANISOU 1234  C   ILE A 160     2266   2187   2281   -130    -97    -29       C  
ATOM   1235  O   ILE A 160     -32.686  32.942  78.142  1.00 19.32           O  
ANISOU 1235  O   ILE A 160     2485   2381   2476   -121   -111    -29       O  
ATOM   1236  CB  ILE A 160     -33.763  32.137  75.065  1.00 16.32           C  
ANISOU 1236  CB  ILE A 160     2088   2023   2089   -136    -56    -34       C  
ATOM   1237  CG1 ILE A 160     -34.857  31.482  75.883  1.00 15.11           C  
ANISOU 1237  CG1 ILE A 160     1958   1862   1922   -130    -56    -36       C  
ATOM   1238  CG2 ILE A 160     -33.595  31.365  73.715  1.00 17.51           C  
ANISOU 1238  CG2 ILE A 160     2226   2185   2243   -141    -33    -41       C  
ATOM   1239  CD1 ILE A 160     -36.189  31.491  75.184  1.00 15.83           C  
ANISOU 1239  CD1 ILE A 160     2056   1962   1996   -139    -41    -37       C  
ATOM   1240  N   ARG A 161     -32.303  34.521  76.576  1.00 17.19           N  
ANISOU 1240  N   ARG A 161     2190   2123   2218   -143   -100    -26       N  
ATOM   1241  CA  ARG A 161     -32.293  35.628  77.577  1.00 16.69           C  
ANISOU 1241  CA  ARG A 161     2138   2049   2152   -147   -120    -25       C  
ATOM   1242  C   ARG A 161     -33.452  36.598  77.492  1.00 15.48           C  
ANISOU 1242  C   ARG A 161     2002   1892   1987   -153   -113    -23       C  
ATOM   1243  O   ARG A 161     -33.893  36.974  76.403  1.00 15.25           O  
ANISOU 1243  O   ARG A 161     1967   1869   1957   -159    -97    -17       O  
ATOM   1244  CB  ARG A 161     -30.963  36.394  77.542  1.00 17.13           C  
ANISOU 1244  CB  ARG A 161     2173   2106   2228   -158   -133    -25       C  
ATOM   1245  CG  ARG A 161     -29.788  35.543  78.094  1.00 19.00           C  
ANISOU 1245  CG  ARG A 161     2394   2347   2478   -148   -149    -27       C  
ATOM   1246  CD  ARG A 161     -28.448  36.267  78.112  1.00 23.87           C  
ANISOU 1246  CD  ARG A 161     2985   2968   3117   -160   -164    -28       C  
ATOM   1247  NE  ARG A 161     -27.369  35.347  78.507  1.00 23.55           N  
ANISOU 1247  NE  ARG A 161     2924   2934   3091   -148   -177    -28       N  
ATOM   1248  CZ  ARG A 161     -27.029  35.042  79.758  1.00 25.62           C  
ANISOU 1248  CZ  ARG A 161     3192   3194   3349   -139   -205    -28       C  
ATOM   1249  NH1 ARG A 161     -27.644  35.588  80.799  1.00 27.22           N  
ANISOU 1249  NH1 ARG A 161     3423   3389   3532   -143   -221    -31       N  
ATOM   1250  NH2 ARG A 161     -26.020  34.190  79.965  1.00 27.00           N  
ANISOU 1250  NH2 ARG A 161     3343   3376   3539   -125   -216    -24       N  
ATOM   1251  N   VAL A 162     -33.988  36.968  78.652  1.00 14.07           N  
ANISOU 1251  N   VAL A 162     1847   1703   1798   -148   -124    -26       N  
ATOM   1252  CA  VAL A 162     -35.086  37.925  78.689  1.00 13.79           C  
ANISOU 1252  CA  VAL A 162     1826   1659   1753   -150   -117    -25       C  
ATOM   1253  C   VAL A 162     -34.620  39.228  78.051  1.00 13.94           C  
ANISOU 1253  C   VAL A 162     1835   1674   1787   -163   -117    -20       C  
ATOM   1254  O   VAL A 162     -33.496  39.639  78.260  1.00 15.17           O  
ANISOU 1254  O   VAL A 162     1981   1826   1956   -172   -130    -23       O  
ATOM   1255  CB  VAL A 162     -35.511  38.173  80.153  1.00 12.92           C  
ANISOU 1255  CB  VAL A 162     1742   1538   1630   -144   -129    -32       C  
ATOM   1256  CG1 VAL A 162     -36.611  39.205  80.181  1.00 15.56           C  
ANISOU 1256  CG1 VAL A 162     2091   1863   1959   -144   -118    -31       C  
ATOM   1257  CG2 VAL A 162     -36.027  36.871  80.770  1.00 15.60           C  
ANISOU 1257  CG2 VAL A 162     2092   1880   1953   -133   -126    -34       C  
ATOM   1258  N   ILE A 163     -35.461  39.826  77.211  1.00 14.27           N  
ANISOU 1258  N   ILE A 163     1878   1718   1827   -164   -102    -11       N  
ATOM   1259  CA  ILE A 163     -35.123  41.126  76.614  1.00 13.68           C  
ANISOU 1259  CA  ILE A 163     1798   1635   1766   -175   -100     -3       C  
ATOM   1260  C   ILE A 163     -35.943  42.253  77.214  1.00 14.30           C  
ANISOU 1260  C   ILE A 163     1897   1693   1842   -171    -99     -3       C  
ATOM   1261  O   ILE A 163     -37.106  42.096  77.569  1.00 15.39           O  
ANISOU 1261  O   ILE A 163     2049   1831   1968   -159    -93     -3       O  
ATOM   1262  CB  ILE A 163     -35.236  41.012  75.060  1.00 13.19           C  
ANISOU 1262  CB  ILE A 163     1719   1590   1705   -180    -83     11       C  
ATOM   1263  CG1 ILE A 163     -34.160  40.004  74.576  1.00 14.63           C  
ANISOU 1263  CG1 ILE A 163     1880   1787   1892   -184    -82      7       C  
ATOM   1264  CG2 ILE A 163     -35.227  42.414  74.364  1.00 14.08           C  
ANISOU 1264  CG2 ILE A 163     1831   1692   1828   -189    -77     26       C  
ATOM   1265  CD1 ILE A 163     -34.317  39.548  73.146  1.00 17.48           C  
ANISOU 1265  CD1 ILE A 163     2227   2167   2246   -188    -64     15       C  
ATOM   1266  N   ASN A 164     -35.303  43.399  77.402  1.00 15.16           N  
ANISOU 1266  N   ASN A 164     2009   1784   1966   -183   -106     -4       N  
ATOM   1267  CA  ASN A 164     -36.025  44.576  77.823  1.00 15.57           C  
ANISOU 1267  CA  ASN A 164     2081   1813   2021   -179   -102     -4       C  
ATOM   1268  C   ASN A 164     -37.286  44.863  77.009  1.00 16.07           C  
ANISOU 1268  C   ASN A 164     2145   1879   2079   -167    -84     13       C  
ATOM   1269  O   ASN A 164     -37.268  44.768  75.765  1.00 14.67           O  
ANISOU 1269  O   ASN A 164     1952   1718   1905   -170    -76     30       O  
ATOM   1270  CB  ASN A 164     -35.030  45.723  77.713  1.00 15.15           C  
ANISOU 1270  CB  ASN A 164     2026   1741   1988   -198   -107     -4       C  
ATOM   1271  CG  ASN A 164     -35.651  47.094  77.950  1.00 18.18           C  
ANISOU 1271  CG  ASN A 164     2431   2096   2381   -196   -100     -2       C  
ATOM   1272  OD1 ASN A 164     -36.216  47.674  77.063  1.00 18.61           O  
ANISOU 1272  OD1 ASN A 164     2484   2146   2442   -191    -86     16       O  
ATOM   1273  ND2 ASN A 164     -35.501  47.612  79.163  1.00 21.85           N  
ANISOU 1273  ND2 ASN A 164     2916   2539   2845   -200   -110    -22       N  
ATOM   1274  N   GLN A 165     -38.377  45.224  77.681  1.00 16.00           N  
ANISOU 1274  N   GLN A 165     2156   1860   2065   -152    -79      9       N  
ATOM   1275  CA  GLN A 165     -39.669  45.410  77.004  1.00 16.96           C  
ANISOU 1275  CA  GLN A 165     2274   1988   2183   -137    -64     26       C  
ATOM   1276  C   GLN A 165     -39.661  46.504  75.937  1.00 16.86           C  
ANISOU 1276  C   GLN A 165     2255   1965   2184   -140    -56     48       C  
ATOM   1277  O   GLN A 165     -40.278  46.309  74.872  1.00 17.13           O  
ANISOU 1277  O   GLN A 165     2276   2020   2214   -134    -49     67       O  
ATOM   1278  CB  GLN A 165     -40.794  45.655  78.021  1.00 16.09           C  
ANISOU 1278  CB  GLN A 165     2182   1864   2066   -120    -57     16       C  
ATOM   1279  CG  GLN A 165     -42.199  45.576  77.408  1.00 15.92           C  
ANISOU 1279  CG  GLN A 165     2152   1858   2040   -103    -43     32       C  
ATOM   1280  CD  GLN A 165     -42.644  44.168  77.124  1.00 13.09           C  
ANISOU 1280  CD  GLN A 165     1780   1530   1664   -102    -43     32       C  
ATOM   1281  OE1 GLN A 165     -41.836  43.210  77.205  1.00 18.28           O  
ANISOU 1281  OE1 GLN A 165     2434   2199   2315   -114    -51     23       O  
ATOM   1282  NE2 GLN A 165     -43.888  44.023  76.667  1.00 16.54           N  
ANISOU 1282  NE2 GLN A 165     2206   1982   2096    -90    -33     44       N  
ATOM   1283  N   THR A 166     -39.023  47.645  76.205  1.00 16.53           N  
ANISOU 1283  N   THR A 166     2225   1896   2161   -149    -59     46       N  
ATOM   1284  CA  THR A 166     -38.918  48.690  75.202  1.00 17.23           C  
ANISOU 1284  CA  THR A 166     2310   1971   2264   -153    -51     69       C  
ATOM   1285  C   THR A 166     -38.161  48.207  74.003  1.00 15.70           C  
ANISOU 1285  C   THR A 166     2095   1802   2068   -168    -51     83       C  
ATOM   1286  O   THR A 166     -38.575  48.474  72.872  1.00 15.67           O  
ANISOU 1286  O   THR A 166     2082   1808   2062   -164    -42    108       O  
ATOM   1287  CB  THR A 166     -38.301  49.947  75.806  1.00 15.88           C  
ANISOU 1287  CB  THR A 166     2158   1762   2115   -164    -52     61       C  
ATOM   1288  OG1 THR A 166     -39.119  50.322  76.899  1.00 21.96           O  
ANISOU 1288  OG1 THR A 166     2949   2511   2884   -148    -49     45       O  
ATOM   1289  CG2 THR A 166     -38.292  51.096  74.787  1.00 19.82           C  
ANISOU 1289  CG2 THR A 166     2656   2242   2631   -166    -41     88       C  
ATOM   1290  N   THR A 167     -37.040  47.504  74.211  1.00 16.09           N  
ANISOU 1290  N   THR A 167     2134   1862   2117   -183    -60     68       N  
ATOM   1291  CA  THR A 167     -36.321  46.858  73.087  1.00 16.28           C  
ANISOU 1291  CA  THR A 167     2136   1912   2137   -196    -56     78       C  
ATOM   1292  C   THR A 167     -37.227  45.906  72.314  1.00 16.27           C  
ANISOU 1292  C   THR A 167     2125   1942   2114   -184    -49     87       C  
ATOM   1293  O   THR A 167     -37.290  45.971  71.057  1.00 15.56           O  
ANISOU 1293  O   THR A 167     2025   1870   2019   -188    -40    107       O  
ATOM   1294  CB  THR A 167     -35.065  46.159  73.627  1.00 15.58           C  
ANISOU 1294  CB  THR A 167     2037   1830   2054   -209    -68     58       C  
ATOM   1295  OG1 THR A 167     -34.237  47.192  74.201  1.00 15.81           O  
ANISOU 1295  OG1 THR A 167     2073   1832   2103   -224    -75     52       O  
ATOM   1296  CG2 THR A 167     -34.306  45.391  72.531  1.00 16.53           C  
ANISOU 1296  CG2 THR A 167     2133   1976   2171   -219    -61     65       C  
ATOM   1297  N   CYS A 168     -37.995  45.093  73.024  1.00 15.29           N  
ANISOU 1297  N   CYS A 168     2006   1825   1978   -170    -53     74       N  
ATOM   1298  CA  CYS A 168     -38.866  44.078  72.406  1.00 17.75           C  
ANISOU 1298  CA  CYS A 168     2308   2166   2270   -163    -48     78       C  
ATOM   1299  C   CYS A 168     -39.906  44.782  71.521  1.00 15.29           C  
ANISOU 1299  C   CYS A 168     1995   1861   1954   -154    -40    102       C  
ATOM   1300  O   CYS A 168     -40.083  44.432  70.324  1.00 17.07           O  
ANISOU 1300  O   CYS A 168     2207   2112   2165   -158    -35    116       O  
ATOM   1301  CB  CYS A 168     -39.554  43.295  73.505  1.00 18.00           C  
ANISOU 1301  CB  CYS A 168     2348   2197   2292   -151    -51     60       C  
ATOM   1302  SG  CYS A 168     -40.739  42.100  72.971  1.00 21.43           S  
ANISOU 1302  SG  CYS A 168     2774   2663   2705   -144    -45     61       S  
ATOM   1303  N   GLU A 169     -40.489  45.863  72.045  1.00 15.48           N  
ANISOU 1303  N   GLU A 169     2032   1860   1989   -142    -39    109       N  
ATOM   1304  CA  GLU A 169     -41.511  46.646  71.336  1.00 15.80           C  
ANISOU 1304  CA  GLU A 169     2071   1902   2029   -128    -34    135       C  
ATOM   1305  C   GLU A 169     -40.989  47.174  70.022  1.00 16.79           C  
ANISOU 1305  C   GLU A 169     2188   2035   2155   -139    -30    161       C  
ATOM   1306  O   GLU A 169     -41.729  47.212  69.031  1.00 17.83           O  
ANISOU 1306  O   GLU A 169     2311   2190   2274   -133    -28    183       O  
ATOM   1307  CB  GLU A 169     -41.985  47.829  72.185  1.00 15.68           C  
ANISOU 1307  CB  GLU A 169     2074   1852   2033   -113    -31    136       C  
ATOM   1308  CG  GLU A 169     -42.788  47.416  73.413  1.00 16.47           C  
ANISOU 1308  CG  GLU A 169     2183   1947   2130    -99    -30    115       C  
ATOM   1309  CD  GLU A 169     -43.029  48.580  74.344  1.00 20.47           C  
ANISOU 1309  CD  GLU A 169     2709   2414   2654    -87    -25    110       C  
ATOM   1310  OE1 GLU A 169     -42.476  49.695  74.098  1.00 23.10           O  
ANISOU 1310  OE1 GLU A 169     3051   2720   3005    -92    -23    121       O  
ATOM   1311  OE2 GLU A 169     -43.739  48.385  75.342  1.00 25.05           O  
ANISOU 1311  OE2 GLU A 169     3298   2989   3231    -74    -22     94       O  
ATOM   1312  N   ASN A 170     -39.722  47.583  70.006  1.00 15.62           N  
ANISOU 1312  N   ASN A 170     2043   1871   2020   -157    -29    158       N  
ATOM   1313  CA  ASN A 170     -39.146  48.175  68.793  1.00 17.52           C  
ANISOU 1313  CA  ASN A 170     2279   2117   2262   -170    -23    183       C  
ATOM   1314  C   ASN A 170     -38.440  47.219  67.843  1.00 16.31           C  
ANISOU 1314  C   ASN A 170     2108   1997   2092   -186    -19    181       C  
ATOM   1315  O   ASN A 170     -38.142  47.580  66.701  1.00 16.37           O  
ANISOU 1315  O   ASN A 170     2111   2017   2093   -196    -11    204       O  
ATOM   1316  CB  ASN A 170     -38.235  49.334  69.186  1.00 17.23           C  
ANISOU 1316  CB  ASN A 170     2254   2042   2252   -181    -20    184       C  
ATOM   1317  CG  ASN A 170     -39.014  50.492  69.751  1.00 18.81           C  
ANISOU 1317  CG  ASN A 170     2472   2207   2469   -164    -19    193       C  
ATOM   1318  OD1 ASN A 170     -39.620  51.247  69.012  1.00 20.24           O  
ANISOU 1318  OD1 ASN A 170     2656   2384   2652   -154    -13    224       O  
ATOM   1319  ND2 ASN A 170     -39.056  50.604  71.083  1.00 19.08           N  
ANISOU 1319  ND2 ASN A 170     2519   2216   2513   -159    -24    167       N  
ATOM   1320  N   LEU A 171     -38.211  45.994  68.297  1.00 15.92           N  
ANISOU 1320  N   LEU A 171     2053   1963   2035   -189    -23    155       N  
ATOM   1321  CA  LEU A 171     -37.778  44.933  67.408  1.00 15.63           C  
ANISOU 1321  CA  LEU A 171     2001   1959   1980   -200    -17    150       C  
ATOM   1322  C   LEU A 171     -38.974  44.419  66.578  1.00 15.62           C  
ANISOU 1322  C   LEU A 171     1995   1988   1951   -192    -16    161       C  
ATOM   1323  O   LEU A 171     -38.791  44.041  65.415  1.00 15.57           O  
ANISOU 1323  O   LEU A 171     1980   2010   1926   -202     -9    169       O  
ATOM   1324  CB  LEU A 171     -37.213  43.750  68.213  1.00 15.58           C  
ANISOU 1324  CB  LEU A 171     1990   1954   1975   -202    -21    120       C  
ATOM   1325  CG  LEU A 171     -35.886  43.977  68.945  1.00 15.86           C  
ANISOU 1325  CG  LEU A 171     2024   1970   2034   -212    -25    106       C  
ATOM   1326  CD1 LEU A 171     -35.611  42.716  69.821  1.00 16.21           C  
ANISOU 1326  CD1 LEU A 171     2064   2017   2076   -207    -32     80       C  
ATOM   1327  CD2 LEU A 171     -34.741  44.195  67.960  1.00 14.84           C  
ANISOU 1327  CD2 LEU A 171     1880   1848   1909   -231    -14    116       C  
ATOM   1328  N   LEU A 172     -40.169  44.462  67.162  1.00 16.06           N  
ANISOU 1328  N   LEU A 172     2056   2041   2006   -175    -23    161       N  
ATOM   1329  CA  LEU A 172     -41.393  44.003  66.525  1.00 17.51           C  
ANISOU 1329  CA  LEU A 172     2232   2254   2166   -167    -25    170       C  
ATOM   1330  C   LEU A 172     -42.454  45.108  66.584  1.00 18.54           C  
ANISOU 1330  C   LEU A 172     2366   2375   2304   -148    -29    195       C  
ATOM   1331  O   LEU A 172     -43.434  45.008  67.329  1.00 17.80           O  
ANISOU 1331  O   LEU A 172     2273   2277   2213   -133    -33    189       O  
ATOM   1332  CB  LEU A 172     -41.879  42.707  67.206  1.00 17.96           C  
ANISOU 1332  CB  LEU A 172     2286   2322   2215   -165    -27    143       C  
ATOM   1333  CG  LEU A 172     -40.918  41.527  67.019  1.00 20.00           C  
ANISOU 1333  CG  LEU A 172     2540   2592   2467   -180    -22    120       C  
ATOM   1334  CD1 LEU A 172     -41.214  40.411  68.012  1.00 22.18           C  
ANISOU 1334  CD1 LEU A 172     2819   2865   2744   -176    -24     94       C  
ATOM   1335  CD2 LEU A 172     -40.935  40.979  65.590  1.00 22.61           C  
ANISOU 1335  CD2 LEU A 172     2861   2957   2772   -193    -16    126       C  
ATOM   1336  N   PRO A 173     -42.265  46.186  65.786  1.00 19.50           N  
ANISOU 1336  N   PRO A 173     2490   2490   2428   -149    -26    225       N  
ATOM   1337  CA  PRO A 173     -43.047  47.392  66.001  1.00 20.47           C  
ANISOU 1337  CA  PRO A 173     2620   2592   2567   -128    -28    249       C  
ATOM   1338  C   PRO A 173     -44.540  47.175  65.837  1.00 21.06           C  
ANISOU 1338  C   PRO A 173     2683   2689   2628   -110    -35    260       C  
ATOM   1339  O   PRO A 173     -44.968  46.445  64.908  1.00 22.16           O  
ANISOU 1339  O   PRO A 173     2808   2870   2741   -116    -40    265       O  
ATOM   1340  CB  PRO A 173     -42.551  48.370  64.928  1.00 21.92           C  
ANISOU 1340  CB  PRO A 173     2807   2772   2750   -135    -23    283       C  
ATOM   1341  CG  PRO A 173     -41.361  47.833  64.401  1.00 21.27           C  
ANISOU 1341  CG  PRO A 173     2722   2702   2659   -160    -17    273       C  
ATOM   1342  CD  PRO A 173     -41.265  46.349  64.715  1.00 20.40           C  
ANISOU 1342  CD  PRO A 173     2603   2615   2535   -168    -19    238       C  
ATOM   1343  N   GLN A 174     -45.308  47.792  66.749  1.00 22.45           N  
ANISOU 1343  N   GLN A 174     2865   2841   2825    -87    -35    260       N  
ATOM   1344  CA  GLN A 174     -46.762  47.745  66.725  1.00 24.53           C  
ANISOU 1344  CA  GLN A 174     3114   3123   3083    -66    -40    271       C  
ATOM   1345  C   GLN A 174     -47.347  46.341  66.911  1.00 23.76           C  
ANISOU 1345  C   GLN A 174     3002   3059   2966    -73    -44    247       C  
ATOM   1346  O   GLN A 174     -48.514  46.092  66.554  1.00 25.47           O  
ANISOU 1346  O   GLN A 174     3201   3305   3172    -63    -50    257       O  
ATOM   1347  CB  GLN A 174     -47.304  48.436  65.460  1.00 25.82           C  
ANISOU 1347  CB  GLN A 174     3267   3306   3236    -57    -46    314       C  
ATOM   1348  CG  GLN A 174     -47.044  49.949  65.486  1.00 29.17           C  
ANISOU 1348  CG  GLN A 174     3707   3689   3686    -43    -40    341       C  
ATOM   1349  CD  GLN A 174     -47.190  50.604  64.128  1.00 34.84           C  
ANISOU 1349  CD  GLN A 174     4421   4425   4393    -40    -45    386       C  
ATOM   1350  OE1 GLN A 174     -46.941  49.986  63.095  1.00 40.79           O  
ANISOU 1350  OE1 GLN A 174     5166   5217   5116    -58    -50    392       O  
ATOM   1351  NE2 GLN A 174     -47.581  51.873  64.124  1.00 37.70           N  
ANISOU 1351  NE2 GLN A 174     4791   4757   4777    -16    -42    417       N  
ATOM   1352  N   GLN A 175     -46.570  45.443  67.515  1.00 21.57           N  
ANISOU 1352  N   GLN A 175     2732   2777   2687    -89    -40    215       N  
ATOM   1353  CA  GLN A 175     -47.023  44.054  67.727  1.00 21.44           C  
ANISOU 1353  CA  GLN A 175     2706   2787   2655    -98    -42    191       C  
ATOM   1354  C   GLN A 175     -46.951  43.556  69.174  1.00 21.09           C  
ANISOU 1354  C   GLN A 175     2672   2719   2621    -95    -37    161       C  
ATOM   1355  O   GLN A 175     -47.520  42.477  69.513  1.00 22.64           O  
ANISOU 1355  O   GLN A 175     2862   2932   2807    -99    -36    143       O  
ATOM   1356  CB  GLN A 175     -46.227  43.108  66.870  1.00 21.67           C  
ANISOU 1356  CB  GLN A 175     2731   2839   2662   -122    -42    181       C  
ATOM   1357  CG  GLN A 175     -46.506  43.303  65.373  1.00 23.35           C  
ANISOU 1357  CG  GLN A 175     2932   3086   2853   -128    -48    207       C  
ATOM   1358  CD  GLN A 175     -45.751  42.325  64.534  1.00 27.24           C  
ANISOU 1358  CD  GLN A 175     3423   3603   3324   -153    -44    193       C  
ATOM   1359  OE1 GLN A 175     -46.041  41.133  64.549  1.00 33.69           O  
ANISOU 1359  OE1 GLN A 175     4235   4440   4128   -164    -44    170       O  
ATOM   1360  NE2 GLN A 175     -44.756  42.808  63.812  1.00 29.85           N  
ANISOU 1360  NE2 GLN A 175     3759   3931   3651   -163    -40    205       N  
ATOM   1361  N   ILE A 176     -46.230  44.288  70.005  1.00 18.81           N  
ANISOU 1361  N   ILE A 176     2402   2394   2352    -91    -33    156       N  
ATOM   1362  CA  ILE A 176     -45.993  43.853  71.377  1.00 17.51           C  
ANISOU 1362  CA  ILE A 176     2251   2208   2194    -90    -30    128       C  
ATOM   1363  C   ILE A 176     -46.856  44.596  72.382  1.00 16.93           C  
ANISOU 1363  C   ILE A 176     2186   2113   2135    -68    -24    128       C  
ATOM   1364  O   ILE A 176     -46.909  45.834  72.397  1.00 17.46           O  
ANISOU 1364  O   ILE A 176     2260   2157   2218    -56    -22    143       O  
ATOM   1365  CB  ILE A 176     -44.507  44.077  71.732  1.00 16.89           C  
ANISOU 1365  CB  ILE A 176     2187   2106   2126   -103    -32    117       C  
ATOM   1366  CG1 ILE A 176     -43.580  43.288  70.778  1.00 15.22           C  
ANISOU 1366  CG1 ILE A 176     1966   1915   1902   -123    -34    115       C  
ATOM   1367  CG2 ILE A 176     -44.302  43.797  73.211  1.00 17.28           C  
ANISOU 1367  CG2 ILE A 176     2252   2132   2180   -100    -32     92       C  
ATOM   1368  CD1 ILE A 176     -43.771  41.792  70.826  1.00 16.37           C  
ANISOU 1368  CD1 ILE A 176     2106   2084   2032   -130    -34     97       C  
ATOM   1369  N   THR A 177     -47.554  43.837  73.222  1.00 16.11           N  
ANISOU 1369  N   THR A 177     2082   2015   2026    -64    -20    111       N  
ATOM   1370  CA  THR A 177     -48.350  44.362  74.337  1.00 15.89           C  
ANISOU 1370  CA  THR A 177     2063   1967   2008    -45    -10    104       C  
ATOM   1371  C   THR A 177     -47.695  44.091  75.690  1.00 15.83           C  
ANISOU 1371  C   THR A 177     2078   1935   2000    -50     -8     78       C  
ATOM   1372  O   THR A 177     -46.739  43.303  75.767  1.00 15.87           O  
ANISOU 1372  O   THR A 177     2089   1944   1997    -67    -15     65       O  
ATOM   1373  CB  THR A 177     -49.787  43.751  74.384  1.00 16.44           C  
ANISOU 1373  CB  THR A 177     2113   2063   2071    -35     -4    106       C  
ATOM   1374  OG1 THR A 177     -49.651  42.399  74.837  1.00 18.05           O  
ANISOU 1374  OG1 THR A 177     2319   2279   2260    -51     -3     85       O  
ATOM   1375  CG2 THR A 177     -50.414  43.752  72.977  1.00 17.25           C  
ANISOU 1375  CG2 THR A 177     2188   2198   2167    -35    -11    130       C  
ATOM   1376  N   PRO A 178     -48.241  44.690  76.762  1.00 15.57           N  
ANISOU 1376  N   PRO A 178     2060   1881   1976    -34      2     69       N  
ATOM   1377  CA  PRO A 178     -47.681  44.374  78.073  1.00 16.49           C  
ANISOU 1377  CA  PRO A 178     2200   1979   2086    -40      3     44       C  
ATOM   1378  C   PRO A 178     -47.837  42.926  78.527  1.00 17.10           C  
ANISOU 1378  C   PRO A 178     2275   2076   2144    -49      4     30       C  
ATOM   1379  O   PRO A 178     -47.168  42.525  79.501  1.00 18.28           O  
ANISOU 1379  O   PRO A 178     2445   2215   2287    -56      0     13       O  
ATOM   1380  CB  PRO A 178     -48.464  45.289  79.005  1.00 18.33           C  
ANISOU 1380  CB  PRO A 178     2446   2189   2328    -19     18     38       C  
ATOM   1381  CG  PRO A 178     -48.665  46.492  78.202  1.00 17.75           C  
ANISOU 1381  CG  PRO A 178     2365   2104   2274     -7     20     59       C  
ATOM   1382  CD  PRO A 178     -49.031  45.939  76.825  1.00 16.61           C  
ANISOU 1382  CD  PRO A 178     2192   1995   2124    -11     13     82       C  
ATOM   1383  N   ARG A 179     -48.712  42.168  77.863  1.00 16.28           N  
ANISOU 1383  N   ARG A 179     2149   2001   2034    -50      8     39       N  
ATOM   1384  CA  ARG A 179     -48.863  40.755  78.185  1.00 14.91           C  
ANISOU 1384  CA  ARG A 179     1975   1844   1846    -61     10     27       C  
ATOM   1385  C   ARG A 179     -47.746  39.884  77.634  1.00 15.75           C  
ANISOU 1385  C   ARG A 179     2081   1958   1946    -80     -2     24       C  
ATOM   1386  O   ARG A 179     -47.607  38.714  78.039  1.00 17.05           O  
ANISOU 1386  O   ARG A 179     2251   2128   2100    -89     -1     12       O  
ATOM   1387  CB  ARG A 179     -50.228  40.208  77.735  1.00 14.33           C  
ANISOU 1387  CB  ARG A 179     1878   1799   1769    -59     20     34       C  
ATOM   1388  CG  ARG A 179     -51.400  40.481  78.661  1.00 15.05           C  
ANISOU 1388  CG  ARG A 179     1970   1886   1863    -43     37     31       C  
ATOM   1389  CD  ARG A 179     -51.678  41.980  78.901  1.00 16.69           C  
ANISOU 1389  CD  ARG A 179     2182   2073   2087    -21     43     38       C  
ATOM   1390  NE  ARG A 179     -52.040  42.676  77.676  1.00 15.26           N  
ANISOU 1390  NE  ARG A 179     1977   1904   1917    -13     36     61       N  
ATOM   1391  CZ  ARG A 179     -52.290  43.994  77.628  1.00 17.59           C  
ANISOU 1391  CZ  ARG A 179     2273   2180   2229      8     41     73       C  
ATOM   1392  NH1 ARG A 179     -52.159  44.742  78.719  1.00 17.09           N  
ANISOU 1392  NH1 ARG A 179     2234   2084   2173     21     52     60       N  
ATOM   1393  NH2 ARG A 179     -52.657  44.552  76.506  1.00 18.64           N  
ANISOU 1393  NH2 ARG A 179     2384   2326   2371     17     34     98       N  
ATOM   1394  N   MET A 180     -46.941  40.438  76.737  1.00 14.76           N  
ANISOU 1394  N   MET A 180     1950   1831   1827    -85    -12     33       N  
ATOM   1395  CA  MET A 180     -45.873  39.730  76.036  1.00 13.57           C  
ANISOU 1395  CA  MET A 180     1795   1689   1673   -101    -20     31       C  
ATOM   1396  C   MET A 180     -44.490  40.024  76.528  1.00 15.02           C  
ANISOU 1396  C   MET A 180     1993   1852   1863   -106    -30     23       C  
ATOM   1397  O   MET A 180     -44.220  41.116  77.027  1.00 15.71           O  
ANISOU 1397  O   MET A 180     2092   1918   1960   -100    -32     24       O  
ATOM   1398  CB  MET A 180     -45.919  40.006  74.537  1.00 14.09           C  
ANISOU 1398  CB  MET A 180     1841   1774   1738   -106    -23     48       C  
ATOM   1399  CG  MET A 180     -47.315  39.783  73.972  1.00 13.85           C  
ANISOU 1399  CG  MET A 180     1792   1769   1700   -102    -18     57       C  
ATOM   1400  SD  MET A 180     -47.459  40.420  72.243  1.00 17.36           S  
ANISOU 1400  SD  MET A 180     2217   2238   2142   -105    -24     83       S  
ATOM   1401  CE  MET A 180     -49.220  40.320  71.941  1.00 15.96           C  
ANISOU 1401  CE  MET A 180     2017   2089   1958    -96    -21     93       C  
ATOM   1402  N   MET A 181     -43.594  39.084  76.297  1.00 13.88           N  
ANISOU 1402  N   MET A 181     1845   1713   1714   -117    -35     16       N  
ATOM   1403  CA  MET A 181     -42.162  39.291  76.514  1.00 15.27           C  
ANISOU 1403  CA  MET A 181     2027   1876   1899   -124    -46     11       C  
ATOM   1404  C   MET A 181     -41.385  38.682  75.347  1.00 16.05           C  
ANISOU 1404  C   MET A 181     2109   1990   1998   -136    -46     14       C  
ATOM   1405  O   MET A 181     -41.722  37.587  74.884  1.00 16.16           O  
ANISOU 1405  O   MET A 181     2116   2021   2004   -140    -40     10       O  
ATOM   1406  CB  MET A 181     -41.698  38.692  77.866  1.00 14.16           C  
ANISOU 1406  CB  MET A 181     1903   1722   1754   -122    -52     -4       C  
ATOM   1407  CG  MET A 181     -41.741  37.166  77.969  1.00 17.48           C  
ANISOU 1407  CG  MET A 181     2323   2154   2166   -124    -49    -10       C  
ATOM   1408  SD  MET A 181     -41.419  36.665  79.667  1.00 24.21           S  
ANISOU 1408  SD  MET A 181     3200   2991   3010   -119    -57    -22       S  
ATOM   1409  CE  MET A 181     -40.031  37.649  79.967  1.00 16.56           C  
ANISOU 1409  CE  MET A 181     2232   2008   2052   -122    -76    -24       C  
ATOM   1410  N   CYS A 182     -40.308  39.346  74.915  1.00 15.84           N  
ANISOU 1410  N   CYS A 182     2077   1957   1983   -143    -52     19       N  
ATOM   1411  CA  CYS A 182     -39.312  38.794  73.964  1.00 16.03           C  
ANISOU 1411  CA  CYS A 182     2087   1995   2011   -154    -50     19       C  
ATOM   1412  C   CYS A 182     -38.217  38.100  74.744  1.00 15.41           C  
ANISOU 1412  C   CYS A 182     2010   1907   1939   -155    -59      5       C  
ATOM   1413  O   CYS A 182     -37.726  38.629  75.737  1.00 13.91           O  
ANISOU 1413  O   CYS A 182     1829   1700   1755   -153    -70      1       O  
ATOM   1414  CB  CYS A 182     -38.633  39.951  73.224  1.00 16.48           C  
ANISOU 1414  CB  CYS A 182     2135   2047   2078   -162    -51     31       C  
ATOM   1415  SG  CYS A 182     -39.612  40.720  71.921  1.00 21.67           S  
ANISOU 1415  SG  CYS A 182     2786   2719   2727   -161    -42     54       S  
ATOM   1416  N   VAL A 183     -37.811  36.914  74.324  1.00 13.82           N  
ANISOU 1416  N   VAL A 183     1800   1716   1734   -157    -54     -1       N  
ATOM   1417  CA  VAL A 183     -36.803  36.173  75.011  1.00 15.27           C  
ANISOU 1417  CA  VAL A 183     1983   1893   1926   -154    -62    -11       C  
ATOM   1418  C   VAL A 183     -36.011  35.488  73.912  1.00 14.12           C  
ANISOU 1418  C   VAL A 183     1820   1760   1786   -161    -52    -13       C  
ATOM   1419  O   VAL A 183     -36.588  34.813  73.050  1.00 15.18           O  
ANISOU 1419  O   VAL A 183     1950   1908   1910   -164    -38    -14       O  
ATOM   1420  CB  VAL A 183     -37.407  35.076  75.915  1.00 14.58           C  
ANISOU 1420  CB  VAL A 183     1910   1801   1829   -145    -61    -18       C  
ATOM   1421  CG1 VAL A 183     -36.363  34.612  76.904  1.00 15.03           C  
ANISOU 1421  CG1 VAL A 183     1971   1847   1894   -139    -76    -23       C  
ATOM   1422  CG2 VAL A 183     -38.616  35.590  76.686  1.00 14.60           C  
ANISOU 1422  CG2 VAL A 183     1930   1797   1820   -140    -62    -17       C  
ATOM   1423  N   GLY A 184     -34.705  35.649  73.950  1.00 13.33           N  
ANISOU 1423  N   GLY A 184     1707   1656   1702   -163    -58    -14       N  
ATOM   1424  CA  GLY A 184     -33.815  35.200  72.859  1.00 13.52           C  
ANISOU 1424  CA  GLY A 184     1711   1693   1734   -169    -45    -15       C  
ATOM   1425  C   GLY A 184     -32.557  36.035  72.792  1.00 14.53           C  
ANISOU 1425  C   GLY A 184     1822   1818   1881   -176    -52    -11       C  
ATOM   1426  O   GLY A 184     -31.977  36.372  73.840  1.00 15.08           O  
ANISOU 1426  O   GLY A 184     1892   1876   1962   -174    -71    -13       O  
ATOM   1427  N   PHE A 184A    -32.089  36.236  71.556  1.00 14.58           N  
ANISOU 1427  N   PHE A 184A    1812   1838   1890   -187    -36     -7       N  
ATOM   1428  CA  PHE A 184A    -30.876  37.025  71.287  1.00 16.74           C  
ANISOU 1428  CA  PHE A 184A    2067   2112   2183   -198    -38     -2       C  
ATOM   1429  C   PHE A 184A    -31.043  37.906  70.103  1.00 17.60           C  
ANISOU 1429  C   PHE A 184A    2172   2230   2286   -212    -23     11       C  
ATOM   1430  O   PHE A 184A    -31.694  37.528  69.119  1.00 17.18           O  
ANISOU 1430  O   PHE A 184A    2122   2193   2214   -214     -7     14       O  
ATOM   1431  CB  PHE A 184A    -29.716  36.070  71.029  1.00 16.57           C  
ANISOU 1431  CB  PHE A 184A    2022   2097   2177   -194    -30    -11       C  
ATOM   1432  CG  PHE A 184A    -29.472  35.143  72.176  1.00 17.23           C  
ANISOU 1432  CG  PHE A 184A    2109   2172   2268   -177    -45    -20       C  
ATOM   1433  CD1 PHE A 184A    -28.753  35.568  73.284  1.00 18.39           C  
ANISOU 1433  CD1 PHE A 184A    2250   2308   2429   -176    -69    -20       C  
ATOM   1434  CD2 PHE A 184A    -29.998  33.850  72.166  1.00 17.83           C  
ANISOU 1434  CD2 PHE A 184A    2194   2247   2334   -165    -36    -28       C  
ATOM   1435  CE1 PHE A 184A    -28.551  34.741  74.369  1.00 20.03           C  
ANISOU 1435  CE1 PHE A 184A    2462   2509   2640   -160    -86    -25       C  
ATOM   1436  CE2 PHE A 184A    -29.807  32.996  73.272  1.00 18.81           C  
ANISOU 1436  CE2 PHE A 184A    2323   2359   2463   -148    -50    -33       C  
ATOM   1437  CZ  PHE A 184A    -29.055  33.448  74.385  1.00 18.09           C  
ANISOU 1437  CZ  PHE A 184A    2227   2261   2386   -145    -76    -30       C  
ATOM   1438  N   LEU A 185     -30.490  39.111  70.189  1.00 16.89           N  
ANISOU 1438  N   LEU A 185     2077   2131   2210   -224    -29     21       N  
ATOM   1439  CA  LEU A 185     -30.466  39.955  68.978  1.00 17.43           C  
ANISOU 1439  CA  LEU A 185     2141   2209   2274   -238    -12     37       C  
ATOM   1440  C   LEU A 185     -29.785  39.285  67.779  1.00 18.29           C  
ANISOU 1440  C   LEU A 185     2231   2339   2380   -245     11     35       C  
ATOM   1441  O   LEU A 185     -30.181  39.502  66.635  1.00 17.92           O  
ANISOU 1441  O   LEU A 185     2186   2307   2315   -253     27     46       O  
ATOM   1442  CB  LEU A 185     -29.840  41.333  69.265  1.00 18.44           C  
ANISOU 1442  CB  LEU A 185     2265   2318   2421   -253    -20     47       C  
ATOM   1443  CG  LEU A 185     -30.521  42.199  70.318  1.00 20.53           C  
ANISOU 1443  CG  LEU A 185     2553   2560   2689   -249    -38     48       C  
ATOM   1444  CD1 LEU A 185     -29.750  43.506  70.481  1.00 18.66           C  
ANISOU 1444  CD1 LEU A 185     2312   2305   2474   -267    -43     55       C  
ATOM   1445  CD2 LEU A 185     -31.939  42.533  69.998  1.00 22.13           C  
ANISOU 1445  CD2 LEU A 185     2775   2761   2871   -240    -34     60       C  
ATOM   1446  N   SER A 186     -28.780  38.460  68.061  1.00 19.13           N  
ANISOU 1446  N   SER A 186     2319   2448   2503   -240     12     21       N  
ATOM   1447  CA  SER A 186     -28.069  37.670  67.045  1.00 20.56           C  
ANISOU 1447  CA  SER A 186     2480   2648   2684   -243     36     15       C  
ATOM   1448  C   SER A 186     -28.846  36.448  66.565  1.00 19.75           C  
ANISOU 1448  C   SER A 186     2389   2556   2559   -233     49      3       C  
ATOM   1449  O   SER A 186     -28.397  35.776  65.630  1.00 22.23           O  
ANISOU 1449  O   SER A 186     2692   2886   2869   -235     72     -5       O  
ATOM   1450  CB  SER A 186     -26.695  37.200  67.552  1.00 21.50           C  
ANISOU 1450  CB  SER A 186     2572   2764   2832   -238     33      4       C  
ATOM   1451  OG  SER A 186     -26.816  36.464  68.755  1.00 25.60           O  
ANISOU 1451  OG  SER A 186     3098   3272   3359   -220     12     -6       O  
ATOM   1452  N   GLY A 186A    -30.008  36.175  67.154  1.00 17.78           N  
ANISOU 1452  N   GLY A 186A    2161   2300   2295   -223     35      1       N  
ATOM   1453  CA  GLY A 186A    -30.726  34.970  66.796  1.00 19.71           C  
ANISOU 1453  CA  GLY A 186A    2416   2553   2521   -216     46    -13       C  
ATOM   1454  C   GLY A 186A    -29.997  33.734  67.278  1.00 19.94           C  
ANISOU 1454  C   GLY A 186A    2436   2574   2567   -203     49    -30       C  
ATOM   1455  O   GLY A 186A    -29.411  33.736  68.380  1.00 22.78           O  
ANISOU 1455  O   GLY A 186A    2789   2918   2948   -193     32    -31       O  
ATOM   1456  N   GLY A 187     -30.131  32.643  66.526  1.00 19.60           N  
ANISOU 1456  N   GLY A 187     2393   2540   2512   -201     70    -45       N  
ATOM   1457  CA  GLY A 187     -29.401  31.423  66.794  1.00 20.25           C  
ANISOU 1457  CA  GLY A 187     2468   2614   2614   -187     79    -61       C  
ATOM   1458  C   GLY A 187     -30.135  30.411  67.640  1.00 20.11           C  
ANISOU 1458  C   GLY A 187     2468   2580   2593   -173     70    -70       C  
ATOM   1459  O   GLY A 187     -30.099  29.196  67.362  1.00 20.64           O  
ANISOU 1459  O   GLY A 187     2539   2643   2662   -166     88    -86       O  
ATOM   1460  N   VAL A 188     -30.814  30.883  68.685  1.00 18.76           N  
ANISOU 1460  N   VAL A 188     2311   2398   2419   -170     46    -60       N  
ATOM   1461  CA  VAL A 188     -31.553  30.013  69.629  1.00 17.90           C  
ANISOU 1461  CA  VAL A 188     2221   2272   2306   -158     37    -66       C  
ATOM   1462  C   VAL A 188     -32.954  30.616  69.776  1.00 17.23           C  
ANISOU 1462  C   VAL A 188     2156   2192   2199   -167     28    -58       C  
ATOM   1463  O   VAL A 188     -33.110  31.826  69.996  1.00 17.01           O  
ANISOU 1463  O   VAL A 188     2127   2167   2169   -172     15    -45       O  
ATOM   1464  CB  VAL A 188     -30.891  29.915  71.028  1.00 18.64           C  
ANISOU 1464  CB  VAL A 188     2314   2349   2422   -141     15    -60       C  
ATOM   1465  CG1 VAL A 188     -31.606  28.904  71.877  1.00 18.54           C  
ANISOU 1465  CG1 VAL A 188     2321   2319   2403   -130     11    -64       C  
ATOM   1466  CG2 VAL A 188     -29.407  29.561  70.902  1.00 20.57           C  
ANISOU 1466  CG2 VAL A 188     2531   2592   2692   -131     20    -63       C  
ATOM   1467  N   ASP A 189     -33.979  29.796  69.610  1.00 17.15           N  
ANISOU 1467  N   ASP A 189     2160   2182   2173   -169     37    -68       N  
ATOM   1468  CA  ASP A 189     -35.349  30.340  69.620  1.00 16.99           C  
ANISOU 1468  CA  ASP A 189     2153   2171   2133   -178     30    -61       C  
ATOM   1469  C   ASP A 189     -36.349  29.203  69.722  1.00 16.63           C  
ANISOU 1469  C   ASP A 189     2122   2122   2075   -180     38    -73       C  
ATOM   1470  O   ASP A 189     -36.029  28.025  69.447  1.00 18.18           O  
ANISOU 1470  O   ASP A 189     2321   2312   2277   -179     53    -88       O  
ATOM   1471  CB  ASP A 189     -35.607  31.091  68.301  1.00 16.50           C  
ANISOU 1471  CB  ASP A 189     2082   2133   2053   -194     38    -55       C  
ATOM   1472  CG  ASP A 189     -36.662  32.214  68.403  1.00 16.75           C  
ANISOU 1472  CG  ASP A 189     2120   2173   2072   -198     25    -39       C  
ATOM   1473  OD1 ASP A 189     -37.253  32.435  69.486  1.00 17.20           O  
ANISOU 1473  OD1 ASP A 189     2187   2217   2132   -189     12    -34       O  
ATOM   1474  OD2 ASP A 189     -36.897  32.899  67.364  1.00 17.63           O  
ANISOU 1474  OD2 ASP A 189     2226   2304   2169   -208     30    -29       O  
ATOM   1475  N   SER A 190     -37.570  29.538  70.112  1.00 16.92           N  
ANISOU 1475  N   SER A 190     2168   2161   2098   -184     30    -67       N  
ATOM   1476  CA  SER A 190     -38.650  28.565  69.976  1.00 16.50           C  
ANISOU 1476  CA  SER A 190     2126   2110   2033   -192     39    -78       C  
ATOM   1477  C   SER A 190     -38.964  28.467  68.489  1.00 16.60           C  
ANISOU 1477  C   SER A 190     2131   2149   2027   -209     52    -87       C  
ATOM   1478  O   SER A 190     -38.520  29.294  67.680  1.00 17.66           O  
ANISOU 1478  O   SER A 190     2255   2299   2156   -214     52    -79       O  
ATOM   1479  CB  SER A 190     -39.913  29.016  70.741  1.00 15.36           C  
ANISOU 1479  CB  SER A 190     1990   1967   1880   -192     29    -69       C  
ATOM   1480  OG  SER A 190     -40.240  30.327  70.322  1.00 17.12           O  
ANISOU 1480  OG  SER A 190     2204   2207   2095   -194     20    -55       O  
ATOM   1481  N   CYS A 191     -39.717  27.429  68.111  1.00 15.94           N  
ANISOU 1481  N   CYS A 191     2055   2069   1933   -222     64   -103       N  
ATOM   1482  CA  CYS A 191     -40.137  27.372  66.715  1.00 16.26           C  
ANISOU 1482  CA  CYS A 191     2089   2138   1950   -241     73   -112       C  
ATOM   1483  C   CYS A 191     -41.464  26.613  66.583  1.00 15.51           C  
ANISOU 1483  C   CYS A 191     2001   2052   1840   -258     76   -124       C  
ATOM   1484  O   CYS A 191     -42.139  26.345  67.564  1.00 16.16           O  
ANISOU 1484  O   CYS A 191     2090   2119   1929   -254     71   -121       O  
ATOM   1485  CB  CYS A 191     -39.005  26.874  65.824  1.00 15.77           C  
ANISOU 1485  CB  CYS A 191     2024   2077   1890   -244     91   -126       C  
ATOM   1486  SG  CYS A 191     -39.191  27.264  64.026  1.00 20.24           S  
ANISOU 1486  SG  CYS A 191     2583   2685   2424   -266    100   -130       S  
ATOM   1487  N   GLN A 192     -41.913  26.406  65.358  1.00 16.37           N  
ANISOU 1487  N   GLN A 192     2106   2187   1925   -278     82   -135       N  
ATOM   1488  CA  GLN A 192     -43.217  25.819  65.134  1.00 17.12           C  
ANISOU 1488  CA  GLN A 192     2204   2297   2005   -298     82   -147       C  
ATOM   1489  C   GLN A 192     -43.368  24.475  65.829  1.00 16.71           C  
ANISOU 1489  C   GLN A 192     2166   2215   1967   -301     95   -166       C  
ATOM   1490  O   GLN A 192     -42.521  23.582  65.693  1.00 17.49           O  
ANISOU 1490  O   GLN A 192     2276   2294   2077   -299    112   -184       O  
ATOM   1491  CB  GLN A 192     -43.438  25.641  63.617  1.00 17.10           C  
ANISOU 1491  CB  GLN A 192     2197   2329   1973   -322     88   -161       C  
ATOM   1492  CG  GLN A 192     -44.844  25.162  63.303  1.00 20.07           C  
ANISOU 1492  CG  GLN A 192     2570   2726   2329   -345     83   -172       C  
ATOM   1493  CD  GLN A 192     -45.858  26.273  63.419  1.00 22.04           C  
ANISOU 1493  CD  GLN A 192     2803   3001   2570   -342     61   -145       C  
ATOM   1494  OE1 GLN A 192     -45.527  27.456  63.290  1.00 25.32           O  
ANISOU 1494  OE1 GLN A 192     3211   3426   2984   -328     50   -120       O  
ATOM   1495  NE2 GLN A 192     -47.112  25.913  63.687  1.00 24.42           N  
ANISOU 1495  NE2 GLN A 192     3100   3313   2868   -355     54   -149       N  
ATOM   1496  N   GLY A 193     -44.426  24.359  66.632  1.00 18.19           N  
ANISOU 1496  N   GLY A 193     2355   2399   2157   -304     88   -161       N  
ATOM   1497  CA  GLY A 193     -44.660  23.132  67.396  1.00 17.33           C  
ANISOU 1497  CA  GLY A 193     2262   2260   2062   -307    101   -175       C  
ATOM   1498  C   GLY A 193     -44.286  23.287  68.868  1.00 17.30           C  
ANISOU 1498  C   GLY A 193     2268   2225   2080   -282     96   -158       C  
ATOM   1499  O   GLY A 193     -44.580  22.421  69.682  1.00 18.29           O  
ANISOU 1499  O   GLY A 193     2407   2326   2216   -283    104   -162       O  
ATOM   1500  N   ASP A 194     -43.629  24.407  69.191  1.00 16.04           N  
ANISOU 1500  N   ASP A 194     2101   2068   1925   -262     82   -138       N  
ATOM   1501  CA  ASP A 194     -43.289  24.743  70.592  1.00 16.22           C  
ANISOU 1501  CA  ASP A 194     2132   2067   1964   -240     73   -122       C  
ATOM   1502  C   ASP A 194     -44.407  25.543  71.253  1.00 15.19           C  
ANISOU 1502  C   ASP A 194     1997   1947   1827   -239     62   -107       C  
ATOM   1503  O   ASP A 194     -44.442  25.603  72.486  1.00 14.51           O  
ANISOU 1503  O   ASP A 194     1921   1842   1748   -225     58    -97       O  
ATOM   1504  CB  ASP A 194     -41.979  25.527  70.682  1.00 15.46           C  
ANISOU 1504  CB  ASP A 194     2030   1966   1879   -221     64   -111       C  
ATOM   1505  CG  ASP A 194     -40.762  24.687  70.308  1.00 16.17           C  
ANISOU 1505  CG  ASP A 194     2123   2040   1982   -215     77   -124       C  
ATOM   1506  OD1 ASP A 194     -40.727  23.472  70.649  1.00 16.56           O  
ANISOU 1506  OD1 ASP A 194     2186   2066   2040   -215     89   -135       O  
ATOM   1507  OD2 ASP A 194     -39.822  25.223  69.690  1.00 15.96           O  
ANISOU 1507  OD2 ASP A 194     2084   2022   1957   -211     76   -122       O  
ATOM   1508  N   SER A 195     -45.339  26.083  70.483  1.00 15.81           N  
ANISOU 1508  N   SER A 195     2061   2057   1891   -252     58   -105       N  
ATOM   1509  CA  SER A 195     -46.447  26.912  71.007  1.00 17.08           C  
ANISOU 1509  CA  SER A 195     2214   2230   2047   -249     49    -90       C  
ATOM   1510  C   SER A 195     -47.103  26.257  72.200  1.00 15.16           C  
ANISOU 1510  C   SER A 195     1983   1968   1810   -248     56    -91       C  
ATOM   1511  O   SER A 195     -47.325  25.031  72.187  1.00 14.82           O  
ANISOU 1511  O   SER A 195     1949   1914   1768   -263     69   -106       O  
ATOM   1512  CB  SER A 195     -47.613  27.002  69.997  1.00 18.85           C  
ANISOU 1512  CB  SER A 195     2419   2489   2254   -269     46    -93       C  
ATOM   1513  OG  SER A 195     -47.293  27.520  68.736  1.00 25.06           O  
ANISOU 1513  OG  SER A 195     3194   3300   3027   -275     40    -91       O  
ATOM   1514  N   GLY A 196     -47.428  27.027  73.212  1.00 15.23           N  
ANISOU 1514  N   GLY A 196     1994   1971   1822   -233     50    -77       N  
ATOM   1515  CA  GLY A 196     -48.125  26.523  74.408  1.00 15.85           C  
ANISOU 1515  CA  GLY A 196     2085   2035   1904   -232     59    -75       C  
ATOM   1516  C   GLY A 196     -47.227  25.986  75.511  1.00 15.25           C  
ANISOU 1516  C   GLY A 196     2033   1925   1836   -219     62    -74       C  
ATOM   1517  O   GLY A 196     -47.646  25.880  76.687  1.00 14.91           O  
ANISOU 1517  O   GLY A 196     2003   1868   1793   -213     66    -68       O  
ATOM   1518  N   GLY A 197     -46.001  25.638  75.159  1.00 15.85           N  
ANISOU 1518  N   GLY A 197     2114   1989   1919   -213     59    -79       N  
ATOM   1519  CA  GLY A 197     -45.056  25.110  76.127  1.00 16.33           C  
ANISOU 1519  CA  GLY A 197     2195   2020   1989   -198     58    -75       C  
ATOM   1520  C   GLY A 197     -44.490  26.136  77.085  1.00 15.84           C  
ANISOU 1520  C   GLY A 197     2138   1952   1927   -178     42    -61       C  
ATOM   1521  O   GLY A 197     -44.696  27.355  76.916  1.00 16.38           O  
ANISOU 1521  O   GLY A 197     2195   2036   1992   -175     33    -55       O  
ATOM   1522  N   PRO A 198     -43.784  25.656  78.103  1.00 16.05           N  
ANISOU 1522  N   PRO A 198     2184   1956   1959   -165     39    -56       N  
ATOM   1523  CA  PRO A 198     -43.351  26.547  79.176  1.00 17.33           C  
ANISOU 1523  CA  PRO A 198     2354   2113   2117   -149     23    -45       C  
ATOM   1524  C   PRO A 198     -42.003  27.182  78.902  1.00 16.25           C  
ANISOU 1524  C   PRO A 198     2208   1976   1991   -139      6    -43       C  
ATOM   1525  O   PRO A 198     -41.094  26.556  78.330  1.00 15.66           O  
ANISOU 1525  O   PRO A 198     2127   1896   1927   -137      7    -47       O  
ATOM   1526  CB  PRO A 198     -43.246  25.606  80.378  1.00 18.01           C  
ANISOU 1526  CB  PRO A 198     2466   2177   2202   -142     26    -39       C  
ATOM   1527  CG  PRO A 198     -42.836  24.294  79.773  1.00 18.78           C  
ANISOU 1527  CG  PRO A 198     2563   2261   2310   -146     37    -45       C  
ATOM   1528  CD  PRO A 198     -43.577  24.232  78.457  1.00 17.89           C  
ANISOU 1528  CD  PRO A 198     2433   2166   2197   -166     50    -59       C  
ATOM   1529  N   LEU A 199     -41.893  28.452  79.327  1.00 15.98           N  
ANISOU 1529  N   LEU A 199     2172   1947   1952   -133     -8    -38       N  
ATOM   1530  CA  LEU A 199     -40.595  29.054  79.591  1.00 16.42           C  
ANISOU 1530  CA  LEU A 199     2224   1998   2016   -123    -27    -34       C  
ATOM   1531  C   LEU A 199     -40.260  28.760  81.035  1.00 16.91           C  
ANISOU 1531  C   LEU A 199     2308   2046   2072   -111    -37    -28       C  
ATOM   1532  O   LEU A 199     -40.991  29.184  81.920  1.00 18.13           O  
ANISOU 1532  O   LEU A 199     2477   2198   2212   -110    -37    -26       O  
ATOM   1533  CB  LEU A 199     -40.665  30.574  79.465  1.00 18.25           C  
ANISOU 1533  CB  LEU A 199     2448   2239   2247   -124    -36    -32       C  
ATOM   1534  CG  LEU A 199     -40.296  31.383  78.261  1.00 22.66           C  
ANISOU 1534  CG  LEU A 199     2985   2810   2814   -130    -37    -32       C  
ATOM   1535  CD1 LEU A 199     -40.474  32.844  78.737  1.00 19.63           C  
ANISOU 1535  CD1 LEU A 199     2605   2425   2428   -127    -47    -28       C  
ATOM   1536  CD2 LEU A 199     -38.921  31.103  77.711  1.00 23.84           C  
ANISOU 1536  CD2 LEU A 199     3122   2959   2978   -129    -43    -34       C  
ATOM   1537  N   SER A 200     -39.177  28.046  81.265  1.00 16.04           N  
ANISOU 1537  N   SER A 200     2198   1925   1971   -102    -46    -25       N  
ATOM   1538  CA  SER A 200     -38.770  27.704  82.640  1.00 17.02           C  
ANISOU 1538  CA  SER A 200     2343   2037   2086    -90    -60    -17       C  
ATOM   1539  C   SER A 200     -37.587  28.520  83.153  1.00 17.47           C  
ANISOU 1539  C   SER A 200     2395   2097   2147    -83    -87    -14       C  
ATOM   1540  O   SER A 200     -36.591  28.652  82.478  1.00 17.89           O  
ANISOU 1540  O   SER A 200     2427   2154   2218    -81    -95    -16       O  
ATOM   1541  CB  SER A 200     -38.434  26.226  82.751  1.00 16.94           C  
ANISOU 1541  CB  SER A 200     2341   2012   2084    -82    -53    -11       C  
ATOM   1542  OG  SER A 200     -39.469  25.390  82.241  1.00 19.79           O  
ANISOU 1542  OG  SER A 200     2707   2368   2444    -93    -27    -16       O  
ATOM   1543  N   SER A 201     -37.699  29.028  84.377  1.00 18.89           N  
ANISOU 1543  N   SER A 201     2593   2274   2309    -80   -101    -11       N  
ATOM   1544  CA  SER A 201     -36.681  29.926  84.885  1.00 18.96           C  
ANISOU 1544  CA  SER A 201     2597   2287   2318    -77   -128    -11       C  
ATOM   1545  C   SER A 201     -36.173  29.381  86.196  1.00 19.97           C  
ANISOU 1545  C   SER A 201     2745   2410   2432    -66   -147     -2       C  
ATOM   1546  O   SER A 201     -36.983  29.054  87.063  1.00 19.12           O  
ANISOU 1546  O   SER A 201     2664   2297   2302    -64   -140      3       O  
ATOM   1547  CB  SER A 201     -37.286  31.311  85.108  1.00 19.63           C  
ANISOU 1547  CB  SER A 201     2689   2376   2393    -86   -128    -20       C  
ATOM   1548  OG  SER A 201     -36.399  32.164  85.787  1.00 21.94           O  
ANISOU 1548  OG  SER A 201     2983   2671   2683    -87   -154    -23       O  
ATOM   1549  N   VAL A 202     -34.854  29.297  86.312  1.00 21.05           N  
ANISOU 1549  N   VAL A 202     2867   2550   2582    -59   -171      3       N  
ATOM   1550  CA  VAL A 202     -34.214  28.853  87.561  1.00 22.37           C  
ANISOU 1550  CA  VAL A 202     3049   2715   2735    -47   -196     15       C  
ATOM   1551  C   VAL A 202     -33.745  30.074  88.366  1.00 23.84           C  
ANISOU 1551  C   VAL A 202     3239   2911   2906    -54   -224      7       C  
ATOM   1552  O   VAL A 202     -32.902  30.858  87.915  1.00 24.29           O  
ANISOU 1552  O   VAL A 202     3272   2975   2980    -61   -238      0       O  
ATOM   1553  CB  VAL A 202     -32.988  27.962  87.283  1.00 23.09           C  
ANISOU 1553  CB  VAL A 202     3119   2805   2850    -31   -209     26       C  
ATOM   1554  CG1 VAL A 202     -32.489  27.315  88.570  1.00 23.37           C  
ANISOU 1554  CG1 VAL A 202     3172   2838   2869    -16   -233     43       C  
ATOM   1555  CG2 VAL A 202     -33.333  26.875  86.286  1.00 23.40           C  
ANISOU 1555  CG2 VAL A 202     3151   2833   2908    -26   -179     28       C  
ATOM   1556  N   GLU A 203     -34.241  30.174  89.591  1.00 24.29           N  
ANISOU 1556  N   GLU A 203     3329   2968   2931    -54   -230      9       N  
ATOM   1557  CA  GLU A 203     -33.884  31.275  90.474  1.00 25.92           C  
ANISOU 1557  CA  GLU A 203     3546   3183   3119    -63   -256     -1       C  
ATOM   1558  C   GLU A 203     -32.526  30.992  91.060  1.00 26.69           C  
ANISOU 1558  C   GLU A 203     3633   3290   3219    -55   -293      9       C  
ATOM   1559  O   GLU A 203     -32.062  29.852  91.005  1.00 26.52           O  
ANISOU 1559  O   GLU A 203     3604   3267   3207    -39   -297     27       O  
ATOM   1560  CB  GLU A 203     -34.888  31.404  91.624  1.00 27.39           C  
ANISOU 1560  CB  GLU A 203     3773   3368   3268    -65   -248     -3       C  
ATOM   1561  CG  GLU A 203     -36.265  31.919  91.265  1.00 27.15           C  
ANISOU 1561  CG  GLU A 203     3753   3331   3233    -72   -213    -14       C  
ATOM   1562  CD  GLU A 203     -36.242  33.388  90.845  1.00 31.03           C  
ANISOU 1562  CD  GLU A 203     4233   3822   3734    -85   -215    -34       C  
ATOM   1563  OE1 GLU A 203     -35.874  34.241  91.688  1.00 31.00           O  
ANISOU 1563  OE1 GLU A 203     4244   3822   3714    -92   -234    -45       O  
ATOM   1564  OE2 GLU A 203     -36.603  33.673  89.681  1.00 31.69           O  
ANISOU 1564  OE2 GLU A 203     4296   3903   3842    -89   -196    -37       O  
ATOM   1565  N   ALA A 204     -31.897  32.012  91.644  1.00 28.36           N  
ANISOU 1565  N   ALA A 204     3844   3512   3420    -67   -322     -3       N  
ATOM   1566  CA  ALA A 204     -30.572  31.838  92.244  1.00 29.56           C  
ANISOU 1566  CA  ALA A 204     3982   3678   3573    -62   -363      6       C  
ATOM   1567  C   ALA A 204     -30.532  30.666  93.246  1.00 29.73           C  
ANISOU 1567  C   ALA A 204     4026   3701   3570    -43   -376     29       C  
ATOM   1568  O   ALA A 204     -29.557  29.919  93.287  1.00 30.75           O  
ANISOU 1568  O   ALA A 204     4135   3836   3713    -27   -398     46       O  
ATOM   1569  CB  ALA A 204     -30.059  33.164  92.881  1.00 29.84           C  
ANISOU 1569  CB  ALA A 204     4020   3723   3594    -82   -391    -14       C  
ATOM   1570  N   ASP A 204A    -31.615  30.464  93.991  1.00 30.09           N  
ANISOU 1570  N   ASP A 204A    4112   3740   3581    -42   -359     31       N  
ATOM   1571  CA  ASP A 204A    -31.683  29.366  94.975  1.00 31.34           C  
ANISOU 1571  CA  ASP A 204A    4297   3899   3713    -26   -368     55       C  
ATOM   1572  C   ASP A 204A    -32.024  28.002  94.382  1.00 30.87           C  
ANISOU 1572  C   ASP A 204A    4234   3822   3673     -8   -341     75       C  
ATOM   1573  O   ASP A 204A    -32.130  27.021  95.113  1.00 31.09           O  
ANISOU 1573  O   ASP A 204A    4285   3846   3682      6   -344     98       O  
ATOM   1574  CB  ASP A 204A    -32.645  29.703  96.131  1.00 31.93           C  
ANISOU 1574  CB  ASP A 204A    4418   3976   3739    -34   -360     49       C  
ATOM   1575  CG  ASP A 204A    -34.118  29.832  95.689  1.00 32.23           C  
ANISOU 1575  CG  ASP A 204A    4472   3999   3776    -41   -313     39       C  
ATOM   1576  OD1 ASP A 204A    -34.463  29.687  94.492  1.00 32.53           O  
ANISOU 1576  OD1 ASP A 204A    4487   4027   3848    -41   -287     35       O  
ATOM   1577  OD2 ASP A 204A    -34.968  30.071  96.576  1.00 35.87           O  
ANISOU 1577  OD2 ASP A 204A    4969   4460   4199    -47   -301     34       O  
ATOM   1578  N   GLY A 205     -32.195  27.940  93.064  1.00 29.77           N  
ANISOU 1578  N   GLY A 205     4068   3673   3570    -10   -315     67       N  
ATOM   1579  CA  GLY A 205     -32.522  26.698  92.377  1.00 29.77           C  
ANISOU 1579  CA  GLY A 205     4064   3656   3591      3   -288     81       C  
ATOM   1580  C   GLY A 205     -33.997  26.375  92.190  1.00 29.02           C  
ANISOU 1580  C   GLY A 205     3993   3547   3485     -5   -247     77       C  
ATOM   1581  O   GLY A 205     -34.308  25.432  91.465  1.00 29.34           O  
ANISOU 1581  O   GLY A 205     4029   3573   3547      1   -222     83       O  
ATOM   1582  N   ARG A 206     -34.904  27.134  92.825  1.00 28.64           N  
ANISOU 1582  N   ARG A 206     3971   3504   3408    -18   -239     66       N  
ATOM   1583  CA  ARG A 206     -36.336  26.924  92.594  1.00 27.67           C  
ANISOU 1583  CA  ARG A 206     3865   3372   3278    -27   -199     61       C  
ATOM   1584  C   ARG A 206     -36.659  27.278  91.134  1.00 25.72           C  
ANISOU 1584  C   ARG A 206     3587   3122   3062    -36   -178     45       C  
ATOM   1585  O   ARG A 206     -36.071  28.219  90.582  1.00 25.04           O  
ANISOU 1585  O   ARG A 206     3478   3045   2992    -42   -191     32       O  
ATOM   1586  CB  ARG A 206     -37.204  27.733  93.556  1.00 29.14           C  
ANISOU 1586  CB  ARG A 206     4080   3564   3426    -37   -193     51       C  
ATOM   1587  CG  ARG A 206     -37.407  27.113  94.946  1.00 32.22           C  
ANISOU 1587  CG  ARG A 206     4510   3955   3778    -31   -198     70       C  
ATOM   1588  CD  ARG A 206     -38.332  27.989  95.803  1.00 36.66           C  
ANISOU 1588  CD  ARG A 206     5101   4525   4305    -42   -186     55       C  
ATOM   1589  NE  ARG A 206     -37.869  29.381  95.790  1.00 39.48           N  
ANISOU 1589  NE  ARG A 206     5448   4893   4661    -51   -206     32       N  
ATOM   1590  CZ  ARG A 206     -38.614  30.453  96.061  1.00 41.50           C  
ANISOU 1590  CZ  ARG A 206     5715   5150   4901    -62   -191     11       C  
ATOM   1591  NH1 ARG A 206     -39.895  30.335  96.404  1.00 41.31           N  
ANISOU 1591  NH1 ARG A 206     5713   5123   4859    -65   -156      9       N  
ATOM   1592  NH2 ARG A 206     -38.065  31.661  95.993  1.00 42.82           N  
ANISOU 1592  NH2 ARG A 206     5873   5324   5073    -70   -211    -10       N  
ATOM   1593  N   ILE A 207     -37.578  26.522  90.538  1.00 23.58           N  
ANISOU 1593  N   ILE A 207     3318   2840   2800    -39   -145     47       N  
ATOM   1594  CA  ILE A 207     -37.977  26.706  89.125  1.00 23.26           C  
ANISOU 1594  CA  ILE A 207     3252   2801   2787    -48   -124     33       C  
ATOM   1595  C   ILE A 207     -39.398  27.267  89.076  1.00 21.73           C  
ANISOU 1595  C   ILE A 207     3067   2611   2580    -62    -99     22       C  
ATOM   1596  O   ILE A 207     -40.316  26.740  89.727  1.00 22.59           O  
ANISOU 1596  O   ILE A 207     3199   2714   2671    -64    -80     29       O  
ATOM   1597  CB  ILE A 207     -37.881  25.388  88.328  1.00 23.57           C  
ANISOU 1597  CB  ILE A 207     3281   2826   2849    -43   -108     40       C  
ATOM   1598  CG1 ILE A 207     -36.425  24.916  88.260  1.00 25.42           C  
ANISOU 1598  CG1 ILE A 207     3500   3056   3101    -27   -132     50       C  
ATOM   1599  CG2 ILE A 207     -38.369  25.589  86.884  1.00 23.11           C  
ANISOU 1599  CG2 ILE A 207     3199   2772   2812    -56    -86     25       C  
ATOM   1600  CD1 ILE A 207     -36.279  23.446  87.981  1.00 27.68           C  
ANISOU 1600  CD1 ILE A 207     3790   3323   3404    -16   -117     62       C  
ATOM   1601  N   PHE A 208     -39.557  28.384  88.351  1.00 19.98           N  
ANISOU 1601  N   PHE A 208     2826   2398   2368    -70    -97      7       N  
ATOM   1602  CA  PHE A 208     -40.857  28.984  88.128  1.00 17.47           C  
ANISOU 1602  CA  PHE A 208     2509   2085   2044    -80    -74     -2       C  
ATOM   1603  C   PHE A 208     -41.147  28.985  86.642  1.00 15.64           C  
ANISOU 1603  C   PHE A 208     2249   1858   1837    -87    -60     -8       C  
ATOM   1604  O   PHE A 208     -40.227  29.061  85.846  1.00 17.88           O  
ANISOU 1604  O   PHE A 208     2512   2143   2139    -86    -72    -10       O  
ATOM   1605  CB  PHE A 208     -40.900  30.442  88.653  1.00 17.39           C  
ANISOU 1605  CB  PHE A 208     2505   2081   2022    -81    -84    -13       C  
ATOM   1606  CG  PHE A 208     -40.922  30.512  90.151  1.00 19.26           C  
ANISOU 1606  CG  PHE A 208     2774   2317   2228    -78    -92    -10       C  
ATOM   1607  CD1 PHE A 208     -39.748  30.369  90.871  1.00 21.04           C  
ANISOU 1607  CD1 PHE A 208     3008   2541   2443    -72   -123     -4       C  
ATOM   1608  CD2 PHE A 208     -42.130  30.636  90.827  1.00 21.85           C  
ANISOU 1608  CD2 PHE A 208     3123   2645   2535    -80    -69    -13       C  
ATOM   1609  CE1 PHE A 208     -39.769  30.398  92.280  1.00 21.73           C  
ANISOU 1609  CE1 PHE A 208     3128   2631   2497    -69   -132     -1       C  
ATOM   1610  CE2 PHE A 208     -42.160  30.618  92.241  1.00 23.68           C  
ANISOU 1610  CE2 PHE A 208     3387   2876   2732    -77    -74    -11       C  
ATOM   1611  CZ  PHE A 208     -40.958  30.496  92.934  1.00 21.23           C  
ANISOU 1611  CZ  PHE A 208     3088   2567   2410    -72   -107     -5       C  
ATOM   1612  N   GLN A 209     -42.420  28.974  86.287  1.00 14.90           N  
ANISOU 1612  N   GLN A 209     2153   1769   1741    -95    -36    -12       N  
ATOM   1613  CA  GLN A 209     -42.750  29.187  84.872  1.00 14.27           C  
ANISOU 1613  CA  GLN A 209     2045   1697   1679   -103    -26    -18       C  
ATOM   1614  C   GLN A 209     -42.869  30.683  84.595  1.00 15.27           C  
ANISOU 1614  C   GLN A 209     2160   1832   1807   -104    -32    -25       C  
ATOM   1615  O   GLN A 209     -43.700  31.358  85.191  1.00 16.41           O  
ANISOU 1615  O   GLN A 209     2315   1979   1941   -103    -24    -27       O  
ATOM   1616  CB  GLN A 209     -44.042  28.477  84.497  1.00 13.87           C  
ANISOU 1616  CB  GLN A 209     1993   1651   1628   -114      0    -19       C  
ATOM   1617  CG  GLN A 209     -44.295  28.631  82.988  1.00 13.75           C  
ANISOU 1617  CG  GLN A 209     1949   1649   1628   -123      6    -26       C  
ATOM   1618  CD  GLN A 209     -45.443  27.776  82.496  1.00 17.43           C  
ANISOU 1618  CD  GLN A 209     2409   2120   2094   -137     29    -28       C  
ATOM   1619  OE1 GLN A 209     -45.887  26.880  83.185  1.00 19.87           O  
ANISOU 1619  OE1 GLN A 209     2734   2419   2395   -140     41    -25       O  
ATOM   1620  NE2 GLN A 209     -45.893  28.030  81.261  1.00 15.25           N  
ANISOU 1620  NE2 GLN A 209     2109   1860   1825   -147     34    -34       N  
ATOM   1621  N   ALA A 210     -42.068  31.156  83.642  1.00 15.49           N  
ANISOU 1621  N   ALA A 210     2169   1866   1853   -105    -43    -27       N  
ATOM   1622  CA  ALA A 210     -42.014  32.607  83.410  1.00 14.78           C  
ANISOU 1622  CA  ALA A 210     2070   1778   1766   -105    -50    -31       C  
ATOM   1623  C   ALA A 210     -42.996  33.022  82.354  1.00 16.39           C  
ANISOU 1623  C   ALA A 210     2256   1994   1977   -110    -35    -30       C  
ATOM   1624  O   ALA A 210     -43.492  34.158  82.346  1.00 16.17           O  
ANISOU 1624  O   ALA A 210     2227   1967   1950   -108    -32    -31       O  
ATOM   1625  CB  ALA A 210     -40.585  33.034  83.037  1.00 16.25           C  
ANISOU 1625  CB  ALA A 210     2245   1963   1966   -106    -71    -31       C  
ATOM   1626  N   GLY A 211     -43.330  32.089  81.478  1.00 14.70           N  
ANISOU 1626  N   GLY A 211     2030   1789   1767   -117    -24    -29       N  
ATOM   1627  CA  GLY A 211     -44.062  32.432  80.275  1.00 15.28           C  
ANISOU 1627  CA  GLY A 211     2082   1877   1845   -124    -14    -28       C  
ATOM   1628  C   GLY A 211     -44.539  31.215  79.523  1.00 14.39           C  
ANISOU 1628  C   GLY A 211     1961   1774   1734   -135     -1    -31       C  
ATOM   1629  O   GLY A 211     -44.244  30.056  79.924  1.00 14.51           O  
ANISOU 1629  O   GLY A 211     1987   1779   1747   -136      2    -33       O  
ATOM   1630  N   VAL A 212     -45.259  31.489  78.430  1.00 14.33           N  
ANISOU 1630  N   VAL A 212     1934   1785   1727   -143      5    -30       N  
ATOM   1631  CA  VAL A 212     -45.831  30.462  77.538  1.00 14.59           C  
ANISOU 1631  CA  VAL A 212     1955   1830   1757   -157     16    -35       C  
ATOM   1632  C   VAL A 212     -45.452  30.809  76.103  1.00 14.73           C  
ANISOU 1632  C   VAL A 212     1954   1865   1778   -164     12    -35       C  
ATOM   1633  O   VAL A 212     -45.469  31.987  75.721  1.00 13.94           O  
ANISOU 1633  O   VAL A 212     1845   1773   1680   -159      4    -26       O  
ATOM   1634  CB  VAL A 212     -47.332  30.468  77.625  1.00 14.60           C  
ANISOU 1634  CB  VAL A 212     1949   1844   1752   -163     28    -34       C  
ATOM   1635  CG1 VAL A 212     -47.947  29.387  76.693  1.00 13.97           C  
ANISOU 1635  CG1 VAL A 212     1858   1780   1671   -182     38    -42       C  
ATOM   1636  CG2 VAL A 212     -47.830  30.310  79.088  1.00 16.86           C  
ANISOU 1636  CG2 VAL A 212     2256   2117   2034   -155     36    -33       C  
ATOM   1637  N   VAL A 213     -44.983  29.828  75.356  1.00 15.23           N  
ANISOU 1637  N   VAL A 213     2015   1930   1843   -174     17    -44       N  
ATOM   1638  CA  VAL A 213     -44.496  30.089  73.984  1.00 15.44           C  
ANISOU 1638  CA  VAL A 213     2025   1973   1868   -182     14    -45       C  
ATOM   1639  C   VAL A 213     -45.680  30.556  73.189  1.00 15.47           C  
ANISOU 1639  C   VAL A 213     2013   2003   1862   -191     15    -40       C  
ATOM   1640  O   VAL A 213     -46.687  29.875  73.123  1.00 15.81           O  
ANISOU 1640  O   VAL A 213     2053   2056   1899   -202     23    -46       O  
ATOM   1641  CB  VAL A 213     -43.992  28.799  73.343  1.00 15.98           C  
ANISOU 1641  CB  VAL A 213     2094   2039   1937   -193     24    -59       C  
ATOM   1642  CG1 VAL A 213     -43.599  29.044  71.916  1.00 16.85           C  
ANISOU 1642  CG1 VAL A 213     2190   2169   2043   -202     25    -62       C  
ATOM   1643  CG2 VAL A 213     -42.793  28.269  74.096  1.00 16.55           C  
ANISOU 1643  CG2 VAL A 213     2180   2086   2022   -181     23    -62       C  
ATOM   1644  N   SER A 214     -45.598  31.734  72.574  1.00 14.27           N  
ANISOU 1644  N   SER A 214     1850   1863   1709   -186      7    -28       N  
ATOM   1645  CA  SER A 214     -46.758  32.292  71.888  1.00 14.72           C  
ANISOU 1645  CA  SER A 214     1890   1946   1757   -190      5    -18       C  
ATOM   1646  C   SER A 214     -46.546  32.440  70.341  1.00 14.89           C  
ANISOU 1646  C   SER A 214     1897   1993   1767   -202      2    -15       C  
ATOM   1647  O   SER A 214     -47.298  31.881  69.562  1.00 17.77           O  
ANISOU 1647  O   SER A 214     2252   2382   2119   -217      4    -21       O  
ATOM   1648  CB  SER A 214     -47.139  33.673  72.495  1.00 15.30           C  
ANISOU 1648  CB  SER A 214     1963   2013   1838   -172     -1     -2       C  
ATOM   1649  OG  SER A 214     -48.298  34.230  71.897  1.00 16.56           O  
ANISOU 1649  OG  SER A 214     2104   2197   1992   -172     -4     10       O  
ATOM   1650  N   TRP A 215     -45.601  33.259  69.900  1.00 12.90           N  
ANISOU 1650  N   TRP A 215     1645   1738   1519   -197     -3     -5       N  
ATOM   1651  CA  TRP A 215     -45.461  33.441  68.433  1.00 13.30           C  
ANISOU 1651  CA  TRP A 215     1685   1816   1555   -209     -4      0       C  
ATOM   1652  C   TRP A 215     -44.067  34.046  68.152  1.00 15.14           C  
ANISOU 1652  C   TRP A 215     1921   2037   1795   -205     -5      6       C  
ATOM   1653  O   TRP A 215     -43.285  34.288  69.075  1.00 15.87           O  
ANISOU 1653  O   TRP A 215     2022   2102   1904   -195     -6      5       O  
ATOM   1654  CB  TRP A 215     -46.565  34.373  67.892  1.00 13.49           C  
ANISOU 1654  CB  TRP A 215     1694   1863   1569   -205    -13     21       C  
ATOM   1655  CG  TRP A 215     -46.573  35.778  68.437  1.00 14.87           C  
ANISOU 1655  CG  TRP A 215     1870   2022   1758   -185    -20     42       C  
ATOM   1656  CD1 TRP A 215     -47.167  36.199  69.601  1.00 14.08           C  
ANISOU 1656  CD1 TRP A 215     1774   1905   1672   -170    -20     45       C  
ATOM   1657  CD2 TRP A 215     -45.916  36.935  67.875  1.00 15.35           C  
ANISOU 1657  CD2 TRP A 215     1930   2080   1821   -180    -24     61       C  
ATOM   1658  NE1 TRP A 215     -46.971  37.557  69.759  1.00 16.49           N  
ANISOU 1658  NE1 TRP A 215     2082   2196   1988   -155    -25     63       N  
ATOM   1659  CE2 TRP A 215     -46.218  38.029  68.716  1.00 15.55           C  
ANISOU 1659  CE2 TRP A 215     1960   2085   1864   -161    -28     75       C  
ATOM   1660  CE3 TRP A 215     -45.164  37.164  66.702  1.00 16.63           C  
ANISOU 1660  CE3 TRP A 215     2090   2256   1974   -190    -24     70       C  
ATOM   1661  CZ2 TRP A 215     -45.739  39.322  68.467  1.00 16.73           C  
ANISOU 1661  CZ2 TRP A 215     2113   2223   2023   -153    -32     95       C  
ATOM   1662  CZ3 TRP A 215     -44.687  38.459  66.458  1.00 17.85           C  
ANISOU 1662  CZ3 TRP A 215     2246   2401   2136   -182    -27     92       C  
ATOM   1663  CH2 TRP A 215     -44.985  39.516  67.336  1.00 19.12           C  
ANISOU 1663  CH2 TRP A 215     2412   2537   2317   -164    -31    105       C  
ATOM   1664  N   GLY A 216     -43.756  34.255  66.886  1.00 15.42           N  
ANISOU 1664  N   GLY A 216     1949   2094   1817   -215     -3     12       N  
ATOM   1665  CA  GLY A 216     -42.511  34.877  66.517  1.00 17.06           C  
ANISOU 1665  CA  GLY A 216     2157   2294   2032   -214     -1     19       C  
ATOM   1666  C   GLY A 216     -42.493  35.098  65.026  1.00 17.49           C  
ANISOU 1666  C   GLY A 216     2203   2378   2064   -228      3     28       C  
ATOM   1667  O   GLY A 216     -43.201  34.423  64.273  1.00 19.09           O  
ANISOU 1667  O   GLY A 216     2402   2607   2245   -240      4     20       O  
ATOM   1668  N   ASP A 217     -41.686  36.080  64.616  1.00 17.19           N  
ANISOU 1668  N   ASP A 217     2164   2337   2031   -226      3     46       N  
ATOM   1669  CA  ASP A 217     -41.462  36.314  63.194  1.00 16.95           C  
ANISOU 1669  CA  ASP A 217     2128   2334   1978   -239      9     56       C  
ATOM   1670  C   ASP A 217     -40.306  35.394  62.762  1.00 17.30           C  
ANISOU 1670  C   ASP A 217     2174   2379   2021   -250     26     34       C  
ATOM   1671  O   ASP A 217     -39.123  35.693  62.949  1.00 18.78           O  
ANISOU 1671  O   ASP A 217     2360   2549   2226   -248     33     34       O  
ATOM   1672  CB  ASP A 217     -41.129  37.772  62.953  1.00 16.89           C  
ANISOU 1672  CB  ASP A 217     2121   2321   1977   -233      5     86       C  
ATOM   1673  CG  ASP A 217     -41.009  38.103  61.447  1.00 17.31           C  
ANISOU 1673  CG  ASP A 217     2171   2405   2003   -247     11    103       C  
ATOM   1674  OD1 ASP A 217     -40.901  37.220  60.612  1.00 24.45           O  
ANISOU 1674  OD1 ASP A 217     3073   3333   2883   -262     20     87       O  
ATOM   1675  OD2 ASP A 217     -41.002  39.312  61.129  1.00 18.28           O  
ANISOU 1675  OD2 ASP A 217     2294   2526   2127   -242      6    133       O  
ATOM   1676  N   GLY A 219     -40.672  34.258  62.185  1.00 17.68           N  
ANISOU 1676  N   GLY A 219     2222   2446   2049   -263     34     12       N  
ATOM   1677  CA  GLY A 219     -39.725  33.173  61.883  1.00 18.13           C  
ANISOU 1677  CA  GLY A 219     2281   2499   2107   -271     53    -14       C  
ATOM   1678  C   GLY A 219     -39.191  32.570  63.157  1.00 17.27           C  
ANISOU 1678  C   GLY A 219     2176   2357   2029   -258     54    -29       C  
ATOM   1679  O   GLY A 219     -39.806  32.729  64.212  1.00 19.39           O  
ANISOU 1679  O   GLY A 219     2448   2609   2310   -247     41    -24       O  
ATOM   1680  N   CYS A 220     -38.023  31.944  63.080  1.00 18.46           N  
ANISOU 1680  N   CYS A 220     2325   2497   2193   -257     70    -45       N  
ATOM   1681  CA  CYS A 220     -37.367  31.370  64.249  1.00 18.73           C  
ANISOU 1681  CA  CYS A 220     2360   2499   2255   -243     70    -56       C  
ATOM   1682  C   CYS A 220     -35.890  31.616  64.121  1.00 18.30           C  
ANISOU 1682  C   CYS A 220     2296   2438   2220   -238     79    -55       C  
ATOM   1683  O   CYS A 220     -35.307  31.363  63.037  1.00 18.94           O  
ANISOU 1683  O   CYS A 220     2371   2534   2290   -248     99    -63       O  
ATOM   1684  CB  CYS A 220     -37.580  29.855  64.260  1.00 19.76           C  
ANISOU 1684  CB  CYS A 220     2500   2625   2384   -246     82    -83       C  
ATOM   1685  SG  CYS A 220     -39.270  29.324  64.076  1.00 20.65           S  
ANISOU 1685  SG  CYS A 220     2621   2753   2472   -259     77    -91       S  
ATOM   1686  N   ALA A 221     -35.294  32.063  65.221  1.00 16.43           N  
ANISOU 1686  N   ALA A 221     2055   2178   2010   -225     67    -47       N  
ATOM   1687  CA  ALA A 221     -33.836  32.175  65.350  1.00 17.11           C  
ANISOU 1687  CA  ALA A 221     2127   2253   2119   -220     73    -47       C  
ATOM   1688  C   ALA A 221     -33.185  33.196  64.417  1.00 17.34           C  
ANISOU 1688  C   ALA A 221     2144   2298   2145   -231     81    -33       C  
ATOM   1689  O   ALA A 221     -31.969  33.213  64.234  1.00 17.50           O  
ANISOU 1689  O   ALA A 221     2149   2317   2183   -231     92    -35       O  
ATOM   1690  CB  ALA A 221     -33.163  30.783  65.277  1.00 16.38           C  
ANISOU 1690  CB  ALA A 221     2031   2154   2037   -213     91    -71       C  
ATOM   1691  N   GLN A 221A    -33.997  34.093  63.844  1.00 17.79           N  
ANISOU 1691  N   GLN A 221A    2207   2370   2181   -241     76    -15       N  
ATOM   1692  CA  GLN A 221A    -33.442  35.123  62.953  1.00 18.58           C  
ANISOU 1692  CA  GLN A 221A    2299   2484   2277   -252     85      3       C  
ATOM   1693  C   GLN A 221A    -32.973  36.351  63.706  1.00 18.37           C  
ANISOU 1693  C   GLN A 221A    2269   2438   2274   -249     70     22       C  
ATOM   1694  O   GLN A 221A    -33.455  36.655  64.787  1.00 16.82           O  
ANISOU 1694  O   GLN A 221A    2080   2223   2089   -239     51     25       O  
ATOM   1695  CB  GLN A 221A    -34.431  35.494  61.841  1.00 19.68           C  
ANISOU 1695  CB  GLN A 221A    2446   2650   2380   -264     87     16       C  
ATOM   1696  CG  GLN A 221A    -34.882  34.230  61.087  1.00 26.37           C  
ANISOU 1696  CG  GLN A 221A    3299   3517   3202   -271    101     -7       C  
ATOM   1697  CD  GLN A 221A    -36.296  34.290  60.520  1.00 31.67           C  
ANISOU 1697  CD  GLN A 221A    3980   4212   3840   -278     91      0       C  
ATOM   1698  OE1 GLN A 221A    -36.912  35.363  60.419  1.00 34.77           O  
ANISOU 1698  OE1 GLN A 221A    4375   4611   4225   -278     77     26       O  
ATOM   1699  NE2 GLN A 221A    -36.822  33.116  60.141  1.00 34.26           N  
ANISOU 1699  NE2 GLN A 221A    4315   4553   4150   -286     99    -24       N  
ATOM   1700  N   ARG A 222     -31.998  37.027  63.118  1.00 17.55           N  
ANISOU 1700  N   ARG A 222     2153   2339   2178   -260     82     32       N  
ATOM   1701  CA  ARG A 222     -31.412  38.211  63.756  1.00 17.67           C  
ANISOU 1701  CA  ARG A 222     2162   2334   2218   -261     71     48       C  
ATOM   1702  C   ARG A 222     -32.523  39.207  64.062  1.00 16.39           C  
ANISOU 1702  C   ARG A 222     2017   2163   2048   -258     54     67       C  
ATOM   1703  O   ARG A 222     -33.388  39.452  63.215  1.00 16.14           O  
ANISOU 1703  O   ARG A 222     1993   2148   1990   -262     57     81       O  
ATOM   1704  CB  ARG A 222     -30.436  38.832  62.771  1.00 18.50           C  
ANISOU 1704  CB  ARG A 222     2254   2450   2326   -278     90     60       C  
ATOM   1705  CG  ARG A 222     -29.493  39.858  63.370  1.00 22.63           C  
ANISOU 1705  CG  ARG A 222     2765   2952   2880   -285     84     71       C  
ATOM   1706  CD  ARG A 222     -28.731  40.547  62.268  1.00 26.56           C  
ANISOU 1706  CD  ARG A 222     3253   3463   3377   -304    106     87       C  
ATOM   1707  NE  ARG A 222     -27.688  41.435  62.795  1.00 29.40           N  
ANISOU 1707  NE  ARG A 222     3597   3803   3769   -314    102     94       N  
ATOM   1708  CZ  ARG A 222     -27.034  42.334  62.058  1.00 28.52           C  
ANISOU 1708  CZ  ARG A 222     3479   3695   3664   -334    119    113       C  
ATOM   1709  NH1 ARG A 222     -26.093  43.086  62.610  1.00 33.72           N  
ANISOU 1709  NH1 ARG A 222     4122   4336   4355   -346    114    116       N  
ATOM   1710  NH2 ARG A 222     -27.317  42.477  60.766  1.00 28.71           N  
ANISOU 1710  NH2 ARG A 222     3509   3740   3658   -343    140    129       N  
ATOM   1711  N   ASN A 223     -32.507  39.765  65.281  1.00 15.46           N  
ANISOU 1711  N   ASN A 223     1903   2019   1951   -251     35     68       N  
ATOM   1712  CA  ASN A 223     -33.415  40.849  65.665  1.00 15.50           C  
ANISOU 1712  CA  ASN A 223     1923   2010   1955   -247     22     86       C  
ATOM   1713  C   ASN A 223     -34.858  40.408  65.783  1.00 15.18           C  
ANISOU 1713  C   ASN A 223     1896   1978   1894   -235     15     84       C  
ATOM   1714  O   ASN A 223     -35.767  41.232  65.897  1.00 16.02           O  
ANISOU 1714  O   ASN A 223     2013   2078   1997   -229      7    101       O  
ATOM   1715  CB  ASN A 223     -33.269  42.057  64.731  1.00 17.15           C  
ANISOU 1715  CB  ASN A 223     2133   2221   2162   -259     31    113       C  
ATOM   1716  CG  ASN A 223     -31.904  42.703  64.844  1.00 18.35           C  
ANISOU 1716  CG  ASN A 223     2273   2359   2340   -273     36    115       C  
ATOM   1717  OD1 ASN A 223     -31.250  42.625  65.884  1.00 15.94           O  
ANISOU 1717  OD1 ASN A 223     1963   2037   2059   -271     25    100       O  
ATOM   1718  ND2 ASN A 223     -31.450  43.295  63.764  1.00 19.91           N  
ANISOU 1718  ND2 ASN A 223     2466   2567   2534   -288     53    134       N  
ATOM   1719  N   LYS A 224     -35.063  39.087  65.744  1.00 15.08           N  
ANISOU 1719  N   LYS A 224     1881   1978   1870   -231     19     65       N  
ATOM   1720  CA  LYS A 224     -36.425  38.536  65.802  1.00 15.61           C  
ANISOU 1720  CA  LYS A 224     1957   2056   1918   -224     14     61       C  
ATOM   1721  C   LYS A 224     -36.542  37.450  66.862  1.00 15.33           C  
ANISOU 1721  C   LYS A 224     1926   2009   1889   -214      8     38       C  
ATOM   1722  O   LYS A 224     -36.693  36.260  66.545  1.00 15.53           O  
ANISOU 1722  O   LYS A 224     1950   2046   1904   -216     17     22       O  
ATOM   1723  CB  LYS A 224     -36.846  38.069  64.414  1.00 16.05           C  
ANISOU 1723  CB  LYS A 224     2010   2144   1945   -234     26     63       C  
ATOM   1724  CG  LYS A 224     -36.907  39.221  63.418  1.00 19.06           C  
ANISOU 1724  CG  LYS A 224     2390   2537   2315   -242     29     92       C  
ATOM   1725  CD  LYS A 224     -37.153  38.704  62.017  1.00 22.90           C  
ANISOU 1725  CD  LYS A 224     2874   3058   2769   -254     41     92       C  
ATOM   1726  CE  LYS A 224     -37.132  39.823  60.999  1.00 29.36           C  
ANISOU 1726  CE  LYS A 224     3693   3889   3573   -262     45    124       C  
ATOM   1727  NZ  LYS A 224     -37.304  39.256  59.636  1.00 35.43           N  
ANISOU 1727  NZ  LYS A 224     4460   4696   4305   -276     57    122       N  
ATOM   1728  N   PRO A 225     -36.411  37.834  68.152  1.00 15.57           N  
ANISOU 1728  N   PRO A 225     1963   2015   1939   -205     -5     36       N  
ATOM   1729  CA  PRO A 225     -36.597  36.868  69.228  1.00 15.48           C  
ANISOU 1729  CA  PRO A 225     1958   1992   1931   -195    -11     19       C  
ATOM   1730  C   PRO A 225     -38.052  36.448  69.370  1.00 14.94           C  
ANISOU 1730  C   PRO A 225     1899   1931   1845   -190    -12     18       C  
ATOM   1731  O   PRO A 225     -38.950  37.220  69.070  1.00 18.88           O  
ANISOU 1731  O   PRO A 225     2400   2437   2336   -189    -15     32       O  
ATOM   1732  CB  PRO A 225     -36.100  37.601  70.472  1.00 15.09           C  
ANISOU 1732  CB  PRO A 225     1915   1918   1901   -189    -26     20       C  
ATOM   1733  CG  PRO A 225     -36.350  39.089  70.168  1.00 14.10           C  
ANISOU 1733  CG  PRO A 225     1792   1787   1777   -192    -28     39       C  
ATOM   1734  CD  PRO A 225     -36.238  39.213  68.631  1.00 14.41           C  
ANISOU 1734  CD  PRO A 225     1820   1848   1805   -204    -15     51       C  
ATOM   1735  N   GLY A 226     -38.249  35.211  69.815  1.00 15.85           N  
ANISOU 1735  N   GLY A 226     2020   2045   1959   -187     -9      1       N  
ATOM   1736  CA  GLY A 226     -39.578  34.666  70.040  1.00 15.65           C  
ANISOU 1736  CA  GLY A 226     2001   2026   1919   -185     -9     -3       C  
ATOM   1737  C   GLY A 226     -40.329  35.437  71.093  1.00 16.21           C  
ANISOU 1737  C   GLY A 226     2081   2083   1993   -174    -19      5       C  
ATOM   1738  O   GLY A 226     -39.719  36.063  71.982  1.00 15.63           O  
ANISOU 1738  O   GLY A 226     2014   1990   1934   -167    -28      7       O  
ATOM   1739  N   VAL A 227     -41.654  35.431  70.952  1.00 15.11           N  
ANISOU 1739  N   VAL A 227     1943   1957   1843   -174    -17      9       N  
ATOM   1740  CA  VAL A 227     -42.552  36.130  71.853  1.00 15.34           C  
ANISOU 1740  CA  VAL A 227     1979   1976   1875   -162    -22     16       C  
ATOM   1741  C   VAL A 227     -43.337  35.187  72.742  1.00 15.31           C  
ANISOU 1741  C   VAL A 227     1984   1968   1867   -160    -19      4       C  
ATOM   1742  O   VAL A 227     -43.799  34.126  72.284  1.00 16.43           O  
ANISOU 1742  O   VAL A 227     2121   2124   1999   -169    -11     -4       O  
ATOM   1743  CB  VAL A 227     -43.497  37.120  71.095  1.00 15.81           C  
ANISOU 1743  CB  VAL A 227     2029   2051   1928   -160    -24     35       C  
ATOM   1744  CG1 VAL A 227     -44.291  38.004  72.083  1.00 15.17           C  
ANISOU 1744  CG1 VAL A 227     1955   1954   1855   -144    -26     42       C  
ATOM   1745  CG2 VAL A 227     -42.690  38.033  70.181  1.00 15.20           C  
ANISOU 1745  CG2 VAL A 227     1946   1976   1855   -164    -25     49       C  
ATOM   1746  N   TYR A 228     -43.373  35.511  74.048  1.00 14.86           N  
ANISOU 1746  N   TYR A 228     1940   1891   1816   -149    -22      2       N  
ATOM   1747  CA  TYR A 228     -43.969  34.658  75.047  1.00 15.72           C  
ANISOU 1747  CA  TYR A 228     2060   1993   1920   -146    -18     -7       C  
ATOM   1748  C   TYR A 228     -44.977  35.419  75.899  1.00 13.85           C  
ANISOU 1748  C   TYR A 228     1830   1750   1683   -135    -16     -2       C  
ATOM   1749  O   TYR A 228     -44.803  36.610  76.124  1.00 13.60           O  
ANISOU 1749  O   TYR A 228     1801   1708   1658   -126    -21      5       O  
ATOM   1750  CB  TYR A 228     -42.860  34.208  75.970  1.00 14.73           C  
ANISOU 1750  CB  TYR A 228     1949   1848   1801   -142    -24    -15       C  
ATOM   1751  CG  TYR A 228     -41.810  33.413  75.247  1.00 14.80           C  
ANISOU 1751  CG  TYR A 228     1950   1859   1814   -149    -23    -21       C  
ATOM   1752  CD1 TYR A 228     -41.817  32.009  75.318  1.00 16.58           C  
ANISOU 1752  CD1 TYR A 228     2180   2082   2036   -153    -15    -30       C  
ATOM   1753  CD2 TYR A 228     -40.827  34.039  74.468  1.00 15.47           C  
ANISOU 1753  CD2 TYR A 228     2024   1948   1907   -153    -28    -16       C  
ATOM   1754  CE1 TYR A 228     -40.851  31.256  74.681  1.00 18.52           C  
ANISOU 1754  CE1 TYR A 228     2419   2329   2288   -157    -12    -37       C  
ATOM   1755  CE2 TYR A 228     -39.855  33.253  73.779  1.00 14.83           C  
ANISOU 1755  CE2 TYR A 228     1934   1871   1831   -158    -24    -23       C  
ATOM   1756  CZ  TYR A 228     -39.889  31.877  73.905  1.00 17.00           C  
ANISOU 1756  CZ  TYR A 228     2214   2142   2104   -159    -16    -34       C  
ATOM   1757  OH  TYR A 228     -38.958  31.093  73.278  1.00 17.74           O  
ANISOU 1757  OH  TYR A 228     2300   2236   2204   -162     -9    -42       O  
ATOM   1758  N   THR A 229     -46.058  34.757  76.330  1.00 14.66           N  
ANISOU 1758  N   THR A 229     1934   1859   1778   -135     -6     -6       N  
ATOM   1759  CA  THR A 229     -47.013  35.333  77.251  1.00 14.58           C  
ANISOU 1759  CA  THR A 229     1930   1842   1767   -124      0     -4       C  
ATOM   1760  C   THR A 229     -46.387  35.373  78.629  1.00 15.09           C  
ANISOU 1760  C   THR A 229     2019   1884   1831   -117     -3    -12       C  
ATOM   1761  O   THR A 229     -45.848  34.369  79.086  1.00 16.25           O  
ANISOU 1761  O   THR A 229     2176   2023   1973   -122     -4    -18       O  
ATOM   1762  CB  THR A 229     -48.289  34.485  77.295  1.00 15.56           C  
ANISOU 1762  CB  THR A 229     2046   1982   1885   -130     14     -7       C  
ATOM   1763  OG1 THR A 229     -48.791  34.413  75.951  1.00 16.36           O  
ANISOU 1763  OG1 THR A 229     2124   2109   1985   -139     12     -1       O  
ATOM   1764  CG2 THR A 229     -49.330  35.114  78.176  1.00 15.39           C  
ANISOU 1764  CG2 THR A 229     2027   1957   1864   -117     23     -4       C  
ATOM   1765  N   ARG A 230     -46.390  36.543  79.253  1.00 14.16           N  
ANISOU 1765  N   ARG A 230     1910   1752   1717   -106     -5    -10       N  
ATOM   1766  CA  ARG A 230     -45.891  36.692  80.643  1.00 15.93           C  
ANISOU 1766  CA  ARG A 230     2160   1957   1936   -100     -9    -19       C  
ATOM   1767  C   ARG A 230     -46.829  36.059  81.646  1.00 17.88           C  
ANISOU 1767  C   ARG A 230     2419   2203   2170    -97      6    -24       C  
ATOM   1768  O   ARG A 230     -48.006  36.418  81.697  1.00 20.12           O  
ANISOU 1768  O   ARG A 230     2696   2494   2454    -91     20    -21       O  
ATOM   1769  CB  ARG A 230     -45.768  38.195  80.943  1.00 15.33           C  
ANISOU 1769  CB  ARG A 230     2091   1865   1868    -91    -13    -18       C  
ATOM   1770  CG  ARG A 230     -44.587  38.880  80.308  1.00 18.15           C  
ANISOU 1770  CG  ARG A 230     2443   2216   2237    -96    -28    -15       C  
ATOM   1771  CD  ARG A 230     -44.688  40.390  80.537  1.00 16.74           C  
ANISOU 1771  CD  ARG A 230     2272   2019   2068    -88    -27    -14       C  
ATOM   1772  NE  ARG A 230     -43.575  41.076  79.902  1.00 16.33           N  
ANISOU 1772  NE  ARG A 230     2215   1960   2029    -96    -39    -10       N  
ATOM   1773  CZ  ARG A 230     -42.348  41.215  80.417  1.00 16.31           C  
ANISOU 1773  CZ  ARG A 230     2223   1945   2030   -104    -54    -19       C  
ATOM   1774  NH1 ARG A 230     -42.034  40.691  81.603  1.00 18.02           N  
ANISOU 1774  NH1 ARG A 230     2457   2156   2233   -104    -61    -32       N  
ATOM   1775  NH2 ARG A 230     -41.385  41.860  79.735  1.00 17.86           N  
ANISOU 1775  NH2 ARG A 230     2410   2135   2240   -113    -63    -14       N  
ATOM   1776  N   LEU A 231     -46.320  35.110  82.446  1.00 17.73           N  
ANISOU 1776  N   LEU A 231     2419   2178   2142   -101      3    -29       N  
ATOM   1777  CA  LEU A 231     -47.206  34.446  83.403  1.00 18.26           C  
ANISOU 1777  CA  LEU A 231     2499   2244   2194   -100     19    -31       C  
ATOM   1778  C   LEU A 231     -47.569  35.227  84.687  1.00 18.18           C  
ANISOU 1778  C   LEU A 231     2511   2223   2173    -90     26    -37       C  
ATOM   1779  O   LEU A 231     -48.698  35.068  85.186  1.00 16.87           O  
ANISOU 1779  O   LEU A 231     2347   2062   1999    -87     46    -38       O  
ATOM   1780  CB  LEU A 231     -46.624  33.078  83.784  1.00 19.35           C  
ANISOU 1780  CB  LEU A 231     2650   2378   2325   -107     16    -31       C  
ATOM   1781  CG  LEU A 231     -47.594  31.969  84.174  1.00 24.13           C  
ANISOU 1781  CG  LEU A 231     3260   2987   2921   -113     36    -30       C  
ATOM   1782  CD1 LEU A 231     -48.854  31.886  83.291  1.00 25.27           C  
ANISOU 1782  CD1 LEU A 231     3379   3149   3072   -120     52    -29       C  
ATOM   1783  CD2 LEU A 231     -46.846  30.651  84.192  1.00 23.52           C  
ANISOU 1783  CD2 LEU A 231     3192   2902   2842   -119     31    -28       C  
ATOM   1784  N   PRO A 232     -46.653  36.086  85.204  1.00 17.30           N  
ANISOU 1784  N   PRO A 232     2414   2098   2060    -85     10    -43       N  
ATOM   1785  CA  PRO A 232     -47.013  36.681  86.500  1.00 17.44           C  
ANISOU 1785  CA  PRO A 232     2459   2106   2063    -77     18    -52       C  
ATOM   1786  C   PRO A 232     -48.326  37.452  86.494  1.00 17.83           C  
ANISOU 1786  C   PRO A 232     2500   2157   2117    -68     42    -54       C  
ATOM   1787  O   PRO A 232     -49.039  37.456  87.503  1.00 19.85           O  
ANISOU 1787  O   PRO A 232     2773   2410   2358    -62     60    -60       O  
ATOM   1788  CB  PRO A 232     -45.857  37.643  86.762  1.00 17.05           C  
ANISOU 1788  CB  PRO A 232     2421   2042   2016    -77     -3    -60       C  
ATOM   1789  CG  PRO A 232     -44.681  36.941  86.198  1.00 17.04           C  
ANISOU 1789  CG  PRO A 232     2409   2044   2020    -86    -25    -54       C  
ATOM   1790  CD  PRO A 232     -45.222  36.321  84.886  1.00 17.32           C  
ANISOU 1790  CD  PRO A 232     2417   2094   2070    -89    -15    -44       C  
ATOM   1791  N   LEU A 233     -48.651  38.072  85.358  1.00 19.74           N  
ANISOU 1791  N   LEU A 233     2717   2405   2380    -64     42    -47       N  
ATOM   1792  CA  LEU A 233     -49.850  38.891  85.232  1.00 20.35           C  
ANISOU 1792  CA  LEU A 233     2781   2484   2466    -51     62    -45       C  
ATOM   1793  C   LEU A 233     -51.109  38.074  85.405  1.00 20.54           C  
ANISOU 1793  C   LEU A 233     2794   2525   2485    -51     85    -42       C  
ATOM   1794  O   LEU A 233     -52.156  38.619  85.751  1.00 21.67           O  
ANISOU 1794  O   LEU A 233     2932   2669   2632    -39    106    -43       O  
ATOM   1795  CB  LEU A 233     -49.900  39.476  83.815  1.00 21.15           C  
ANISOU 1795  CB  LEU A 233     2854   2593   2590    -48     54    -32       C  
ATOM   1796  CG  LEU A 233     -48.887  40.571  83.569  1.00 24.59           C  
ANISOU 1796  CG  LEU A 233     3298   3010   3037    -47     38    -33       C  
ATOM   1797  CD1 LEU A 233     -48.672  40.855  82.054  1.00 27.80           C  
ANISOU 1797  CD1 LEU A 233     3677   3426   3459    -49     28    -17       C  
ATOM   1798  CD2 LEU A 233     -49.409  41.803  84.283  1.00 28.14           C  
ANISOU 1798  CD2 LEU A 233     3761   3439   3491    -30     52    -40       C  
ATOM   1799  N   PHE A 234     -51.000  36.763  85.178  1.00 18.60           N  
ANISOU 1799  N   PHE A 234     2544   2292   2233    -66     82    -38       N  
ATOM   1800  CA  PHE A 234     -52.171  35.877  85.148  1.00 18.48           C  
ANISOU 1800  CA  PHE A 234     2514   2293   2215    -72    102    -34       C  
ATOM   1801  C   PHE A 234     -52.355  35.024  86.392  1.00 18.52           C  
ANISOU 1801  C   PHE A 234     2545   2293   2199    -77    117    -40       C  
ATOM   1802  O   PHE A 234     -53.279  34.189  86.440  1.00 18.25           O  
ANISOU 1802  O   PHE A 234     2500   2271   2163    -86    136    -37       O  
ATOM   1803  CB  PHE A 234     -52.112  34.943  83.926  1.00 19.14           C  
ANISOU 1803  CB  PHE A 234     2574   2393   2306    -87     94    -27       C  
ATOM   1804  CG  PHE A 234     -52.233  35.683  82.640  1.00 18.62           C  
ANISOU 1804  CG  PHE A 234     2479   2339   2256    -83     83    -19       C  
ATOM   1805  CD1 PHE A 234     -53.479  36.138  82.209  1.00 21.43           C  
ANISOU 1805  CD1 PHE A 234     2808   2712   2622    -76     96    -13       C  
ATOM   1806  CD2 PHE A 234     -51.070  36.006  81.914  1.00 19.33           C  
ANISOU 1806  CD2 PHE A 234     2570   2423   2352    -85     62    -17       C  
ATOM   1807  CE1 PHE A 234     -53.599  36.892  81.023  1.00 22.43           C  
ANISOU 1807  CE1 PHE A 234     2909   2850   2762    -70     84     -1       C  
ATOM   1808  CE2 PHE A 234     -51.156  36.775  80.737  1.00 20.86           C  
ANISOU 1808  CE2 PHE A 234     2741   2627   2558    -81     53     -7       C  
ATOM   1809  CZ  PHE A 234     -52.410  37.212  80.294  1.00 22.02           C  
ANISOU 1809  CZ  PHE A 234     2863   2791   2713    -73     63      2       C  
ATOM   1810  N   ARG A 235     -51.506  35.266  87.392  1.00 18.74           N  
ANISOU 1810  N   ARG A 235     2606   2304   2212    -73    109    -47       N  
ATOM   1811  CA  ARG A 235     -51.567  34.565  88.657  1.00 20.14           C  
ANISOU 1811  CA  ARG A 235     2812   2476   2364    -77    120    -49       C  
ATOM   1812  C   ARG A 235     -52.967  34.507  89.266  1.00 19.67           C  
ANISOU 1812  C   ARG A 235     2750   2424   2298    -74    154    -51       C  
ATOM   1813  O   ARG A 235     -53.435  33.427  89.614  1.00 20.89           O  
ANISOU 1813  O   ARG A 235     2909   2585   2443    -86    170    -46       O  
ATOM   1814  CB  ARG A 235     -50.575  35.147  89.657  1.00 21.22           C  
ANISOU 1814  CB  ARG A 235     2983   2597   2483    -71    105    -58       C  
ATOM   1815  CG  ARG A 235     -50.517  34.298  90.978  1.00 22.08           C  
ANISOU 1815  CG  ARG A 235     3126   2702   2561    -76    113    -58       C  
ATOM   1816  CD  ARG A 235     -49.883  32.908  90.709  1.00 21.15           C  
ANISOU 1816  CD  ARG A 235     3010   2586   2442    -87    100    -45       C  
ATOM   1817  NE  ARG A 235     -49.964  31.914  91.807  1.00 22.96           N  
ANISOU 1817  NE  ARG A 235     3268   2812   2645    -92    110    -38       N  
ATOM   1818  CZ  ARG A 235     -50.992  31.092  91.986  1.00 24.58           C  
ANISOU 1818  CZ  ARG A 235     3471   3022   2846   -100    138    -32       C  
ATOM   1819  NH1 ARG A 235     -52.042  31.182  91.183  1.00 24.76           N  
ANISOU 1819  NH1 ARG A 235     3462   3055   2889   -104    157    -33       N  
ATOM   1820  NH2 ARG A 235     -50.979  30.188  92.971  1.00 26.00           N  
ANISOU 1820  NH2 ARG A 235     3681   3197   3002   -105    147    -22       N  
ATOM   1821  N   ASP A 236     -53.643  35.641  89.373  1.00 20.55           N  
ANISOU 1821  N   ASP A 236     2854   2536   2418    -60    168    -57       N  
ATOM   1822  CA  ASP A 236     -54.960  35.660  90.028  1.00 20.97           C  
ANISOU 1822  CA  ASP A 236     2903   2597   2466    -55    204    -60       C  
ATOM   1823  C   ASP A 236     -56.004  34.994  89.143  1.00 20.81           C  
ANISOU 1823  C   ASP A 236     2844   2599   2465    -64    217    -50       C  
ATOM   1824  O   ASP A 236     -56.892  34.298  89.634  1.00 21.63           O  
ANISOU 1824  O   ASP A 236     2945   2713   2562    -72    243    -48       O  
ATOM   1825  CB  ASP A 236     -55.397  37.105  90.361  1.00 23.78           C  
ANISOU 1825  CB  ASP A 236     3261   2946   2830    -34    218    -71       C  
ATOM   1826  CG  ASP A 236     -54.608  37.719  91.498  1.00 26.27           C  
ANISOU 1826  CG  ASP A 236     3619   3240   3121    -28    213    -86       C  
ATOM   1827  OD1 ASP A 236     -53.981  37.001  92.282  1.00 31.79           O  
ANISOU 1827  OD1 ASP A 236     4348   3936   3794    -39    205    -87       O  
ATOM   1828  OD2 ASP A 236     -54.620  38.973  91.607  1.00 32.66           O  
ANISOU 1828  OD2 ASP A 236     4433   4036   3939    -13    216    -97       O  
ATOM   1829  N   TRP A 237     -55.889  35.191  87.830  1.00 19.78           N  
ANISOU 1829  N   TRP A 237     2682   2477   2355    -64    198    -43       N  
ATOM   1830  CA  TRP A 237     -56.822  34.597  86.909  1.00 18.57           C  
ANISOU 1830  CA  TRP A 237     2490   2347   2217    -75    205    -35       C  
ATOM   1831  C   TRP A 237     -56.696  33.085  86.955  1.00 18.23           C  
ANISOU 1831  C   TRP A 237     2455   2308   2165    -99    207    -33       C  
ATOM   1832  O   TRP A 237     -57.704  32.359  86.914  1.00 19.06           O  
ANISOU 1832  O   TRP A 237     2541   2427   2273   -113    227    -30       O  
ATOM   1833  CB  TRP A 237     -56.509  35.101  85.498  1.00 18.54           C  
ANISOU 1833  CB  TRP A 237     2459   2352   2233    -72    181    -28       C  
ATOM   1834  CG  TRP A 237     -57.379  34.505  84.470  1.00 19.93           C  
ANISOU 1834  CG  TRP A 237     2596   2555   2421    -85    182    -21       C  
ATOM   1835  CD1 TRP A 237     -58.694  34.799  84.268  1.00 22.10           C  
ANISOU 1835  CD1 TRP A 237     2837   2851   2710    -79    200    -16       C  
ATOM   1836  CD2 TRP A 237     -57.037  33.494  83.513  1.00 18.71           C  
ANISOU 1836  CD2 TRP A 237     2430   2410   2267   -108    167    -18       C  
ATOM   1837  NE1 TRP A 237     -59.201  34.057  83.228  1.00 23.17           N  
ANISOU 1837  NE1 TRP A 237     2940   3012   2853    -98    193    -11       N  
ATOM   1838  CE2 TRP A 237     -58.224  33.215  82.769  1.00 20.93           C  
ANISOU 1838  CE2 TRP A 237     2671   2721   2559   -117    175    -14       C  
ATOM   1839  CE3 TRP A 237     -55.860  32.776  83.216  1.00 19.34           C  
ANISOU 1839  CE3 TRP A 237     2530   2479   2340   -121    149    -21       C  
ATOM   1840  CZ2 TRP A 237     -58.260  32.306  81.710  1.00 21.13           C  
ANISOU 1840  CZ2 TRP A 237     2678   2764   2587   -141    163    -14       C  
ATOM   1841  CZ3 TRP A 237     -55.918  31.826  82.139  1.00 20.47           C  
ANISOU 1841  CZ3 TRP A 237     2654   2638   2487   -142    141    -21       C  
ATOM   1842  CH2 TRP A 237     -57.115  31.620  81.415  1.00 19.57           C  
ANISOU 1842  CH2 TRP A 237     2503   2552   2381   -153    148    -18       C  
ATOM   1843  N   ILE A 238     -55.458  32.612  87.046  1.00 16.72           N  
ANISOU 1843  N   ILE A 238     2290   2100   1962   -105    186    -33       N  
ATOM   1844  CA  ILE A 238     -55.274  31.155  87.157  1.00 16.86           C  
ANISOU 1844  CA  ILE A 238     2319   2115   1973   -126    189    -30       C  
ATOM   1845  C   ILE A 238     -55.902  30.648  88.466  1.00 17.99           C  
ANISOU 1845  C   ILE A 238     2484   2254   2097   -130    218    -29       C  
ATOM   1846  O   ILE A 238     -56.604  29.642  88.462  1.00 19.69           O  
ANISOU 1846  O   ILE A 238     2692   2475   2313   -148    236    -26       O  
ATOM   1847  CB  ILE A 238     -53.806  30.752  87.052  1.00 16.41           C  
ANISOU 1847  CB  ILE A 238     2285   2042   1910   -128    163    -29       C  
ATOM   1848  CG1 ILE A 238     -53.304  31.043  85.616  1.00 17.30           C  
ANISOU 1848  CG1 ILE A 238     2371   2162   2041   -129    140    -29       C  
ATOM   1849  CG2 ILE A 238     -53.588  29.252  87.402  1.00 17.45           C  
ANISOU 1849  CG2 ILE A 238     2435   2164   2033   -144    169    -24       C  
ATOM   1850  CD1 ILE A 238     -51.793  31.057  85.497  1.00 20.88           C  
ANISOU 1850  CD1 ILE A 238     2841   2599   2491   -125    113    -29       C  
ATOM   1851  N   LYS A 239     -55.596  31.306  89.567  1.00 19.96           N  
ANISOU 1851  N   LYS A 239     2763   2492   2328   -115    222    -34       N  
ATOM   1852  CA  LYS A 239     -56.190  30.938  90.864  1.00 21.00           C  
ANISOU 1852  CA  LYS A 239     2920   2621   2439   -118    251    -33       C  
ATOM   1853  C   LYS A 239     -57.729  30.936  90.808  1.00 22.12           C  
ANISOU 1853  C   LYS A 239     3032   2781   2591   -122    285    -33       C  
ATOM   1854  O   LYS A 239     -58.380  29.973  91.263  1.00 22.33           O  
ANISOU 1854  O   LYS A 239     3063   2812   2611   -139    310    -28       O  
ATOM   1855  CB  LYS A 239     -55.667  31.864  91.959  1.00 21.45           C  
ANISOU 1855  CB  LYS A 239     3011   2666   2472   -101    248    -41       C  
ATOM   1856  CG  LYS A 239     -56.251  31.598  93.372  1.00 25.66           C  
ANISOU 1856  CG  LYS A 239     3575   3199   2978   -103    280    -42       C  
ATOM   1857  CD  LYS A 239     -55.804  30.248  93.900  1.00 30.13           C  
ANISOU 1857  CD  LYS A 239     4168   3756   3523   -118    278    -29       C  
ATOM   1858  CE  LYS A 239     -56.163  30.040  95.367  1.00 34.50           C  
ANISOU 1858  CE  LYS A 239     4759   4308   4042   -119    306    -28       C  
ATOM   1859  NZ  LYS A 239     -55.453  28.826  95.816  1.00 39.24           N  
ANISOU 1859  NZ  LYS A 239     5389   4896   4623   -131    295    -11       N  
ATOM   1860  N   GLU A 240     -58.304  31.980  90.212  1.00 23.01           N  
ANISOU 1860  N   GLU A 240     3113   2907   2724   -108    287    -38       N  
ATOM   1861  CA  GLU A 240     -59.762  32.118  90.106  1.00 25.04           C  
ANISOU 1861  CA  GLU A 240     3335   3184   2996   -108    317    -38       C  
ATOM   1862  C   GLU A 240     -60.421  30.985  89.334  1.00 25.15           C  
ANISOU 1862  C   GLU A 240     3318   3215   3023   -134    322    -31       C  
ATOM   1863  O   GLU A 240     -61.506  30.532  89.692  1.00 25.78           O  
ANISOU 1863  O   GLU A 240     3382   3308   3106   -145    353    -29       O  
ATOM   1864  CB  GLU A 240     -60.115  33.463  89.498  1.00 26.41           C  
ANISOU 1864  CB  GLU A 240     3479   3365   3190    -85    312    -40       C  
ATOM   1865  CG  GLU A 240     -59.920  34.603  90.464  1.00 31.37           C  
ANISOU 1865  CG  GLU A 240     4135   3977   3808    -61    322    -51       C  
ATOM   1866  CD  GLU A 240     -59.799  35.954  89.792  1.00 37.27           C  
ANISOU 1866  CD  GLU A 240     4865   4720   4576    -37    307    -53       C  
ATOM   1867  OE1 GLU A 240     -59.840  36.044  88.533  1.00 40.97           O  
ANISOU 1867  OE1 GLU A 240     5299   5201   5066    -38    287    -43       O  
ATOM   1868  OE2 GLU A 240     -59.651  36.947  90.533  1.00 40.74           O  
ANISOU 1868  OE2 GLU A 240     5327   5143   5009    -18    317    -63       O  
ATOM   1869  N   ASN A 241     -59.741  30.483  88.305  1.00 23.71           N  
ANISOU 1869  N   ASN A 241     3128   3032   2849   -146    293    -28       N  
ATOM   1870  CA  ASN A 241     -60.349  29.489  87.425  1.00 23.64           C  
ANISOU 1870  CA  ASN A 241     3089   3040   2854   -172    295    -25       C  
ATOM   1871  C   ASN A 241     -59.986  28.062  87.731  1.00 22.93           C  
ANISOU 1871  C   ASN A 241     3024   2935   2754   -197    301    -23       C  
ATOM   1872  O   ASN A 241     -60.653  27.139  87.240  1.00 23.98           O  
ANISOU 1872  O   ASN A 241     3136   3078   2896   -223    311    -23       O  
ATOM   1873  CB  ASN A 241     -60.022  29.812  85.958  1.00 24.04           C  
ANISOU 1873  CB  ASN A 241     3110   3102   2921   -171    264    -25       C  
ATOM   1874  CG  ASN A 241     -60.774  31.038  85.465  1.00 24.02           C  
ANISOU 1874  CG  ASN A 241     3070   3120   2935   -151    264    -23       C  
ATOM   1875  OD1 ASN A 241     -61.838  30.917  84.876  1.00 30.12           O  
ANISOU 1875  OD1 ASN A 241     3802   3919   3722   -160    271    -20       O  
ATOM   1876  ND2 ASN A 241     -60.263  32.232  85.776  1.00 24.44           N  
ANISOU 1876  ND2 ASN A 241     3138   3160   2986   -124    256    -23       N  
ATOM   1877  N   THR A 242     -58.968  27.863  88.559  1.00 20.77           N  
ANISOU 1877  N   THR A 242     2796   2637   2460   -190    294    -21       N  
ATOM   1878  CA  THR A 242     -58.497  26.499  88.791  1.00 20.26           C  
ANISOU 1878  CA  THR A 242     2757   2554   2388   -210    296    -15       C  
ATOM   1879  C   THR A 242     -58.346  26.135  90.263  1.00 21.77           C  
ANISOU 1879  C   THR A 242     2991   2727   2552   -207    315     -8       C  
ATOM   1880  O   THR A 242     -58.216  24.959  90.587  1.00 23.72           O  
ANISOU 1880  O   THR A 242     3259   2960   2793   -224    324      0       O  
ATOM   1881  CB  THR A 242     -57.119  26.235  88.153  1.00 19.98           C  
ANISOU 1881  CB  THR A 242     2735   2502   2353   -207    262    -15       C  
ATOM   1882  OG1 THR A 242     -56.103  26.978  88.844  1.00 19.10           O  
ANISOU 1882  OG1 THR A 242     2653   2378   2227   -184    245    -14       O  
ATOM   1883  CG2 THR A 242     -57.131  26.601  86.692  1.00 19.31           C  
ANISOU 1883  CG2 THR A 242     2614   2435   2290   -209    242    -22       C  
ATOM   1884  N   GLY A 243     -58.267  27.146  91.113  1.00 23.17           N  
ANISOU 1884  N   GLY A 243     3185   2905   2714   -186    319    -11       N  
ATOM   1885  CA  GLY A 243     -57.924  26.943  92.519  1.00 24.56           C  
ANISOU 1885  CA  GLY A 243     3406   3066   2858   -181    330     -4       C  
ATOM   1886  C   GLY A 243     -56.430  26.820  92.777  1.00 23.78           C  
ANISOU 1886  C   GLY A 243     3342   2947   2744   -171    297      0       C  
ATOM   1887  O   GLY A 243     -55.994  26.759  93.918  1.00 25.35           O  
ANISOU 1887  O   GLY A 243     3581   3137   2915   -165    299      6       O  
ATOM   1888  N   VAL A 244     -55.617  26.774  91.718  1.00 22.99           N  
ANISOU 1888  N   VAL A 244     3228   2844   2664   -170    266     -2       N  
ATOM   1889  CA  VAL A 244     -54.175  26.564  91.871  1.00 22.96           C  
ANISOU 1889  CA  VAL A 244     3252   2823   2651   -161    235      3       C  
ATOM   1890  C   VAL A 244     -53.433  27.876  92.219  1.00 23.64           C  
ANISOU 1890  C   VAL A 244     3348   2910   2726   -140    213     -5       C  
ATOM   1891  O   VAL A 244     -53.575  28.868  91.486  1.00 24.10           O  
ANISOU 1891  O   VAL A 244     3379   2978   2801   -132    205    -16       O  
ATOM   1892  CB  VAL A 244     -53.597  25.945  90.568  1.00 22.86           C  
ANISOU 1892  CB  VAL A 244     3218   2806   2663   -169    215      3       C  
ATOM   1893  CG1 VAL A 244     -52.104  25.759  90.659  1.00 23.25           C  
ANISOU 1893  CG1 VAL A 244     3289   2839   2707   -158    184      9       C  
ATOM   1894  CG2 VAL A 244     -54.316  24.596  90.252  1.00 21.85           C  
ANISOU 1894  CG2 VAL A 244     3083   2673   2545   -194    238      9       C  
TER    1895      VAL A 244                                                      
ATOM   1896  N   GLU B   1     -68.482  29.701  55.551  1.00 32.14           N  
ANISOU 1896  N   GLU B   1     4001   4481   3729   -277    115    -96       N  
ATOM   1897  CA  GLU B   1     -67.372  29.357  54.632  1.00 31.33           C  
ANISOU 1897  CA  GLU B   1     3931   4323   3649   -249     98    -57       C  
ATOM   1898  C   GLU B   1     -66.933  30.571  53.829  1.00 30.31           C  
ANISOU 1898  C   GLU B   1     3792   4168   3554   -196     92    -68       C  
ATOM   1899  O   GLU B   1     -67.749  31.305  53.282  1.00 29.32           O  
ANISOU 1899  O   GLU B   1     3643   4054   3443   -172     94    -99       O  
ATOM   1900  CB  GLU B   1     -67.828  28.239  53.702  1.00 32.35           C  
ANISOU 1900  CB  GLU B   1     4073   4441   3779   -258     94    -40       C  
ATOM   1901  CG  GLU B   1     -66.776  27.272  53.297  1.00 35.67           C  
ANISOU 1901  CG  GLU B   1     4532   4818   4204   -257     79      5       C  
ATOM   1902  CD  GLU B   1     -67.393  25.938  52.931  1.00 36.87           C  
ANISOU 1902  CD  GLU B   1     4697   4970   4342   -287     78     19       C  
ATOM   1903  OE1 GLU B   1     -67.498  25.060  53.819  1.00 41.54           O  
ANISOU 1903  OE1 GLU B   1     5306   5575   4903   -333     79     33       O  
ATOM   1904  OE2 GLU B   1     -67.821  25.792  51.771  1.00 36.52           O  
ANISOU 1904  OE2 GLU B   1     4647   4914   4315   -266     76     15       O  
ATOM   1905  N   VAL B   2     -65.622  30.779  53.800  1.00 29.71           N  
ANISOU 1905  N   VAL B   2     3739   4058   3491   -179     82    -42       N  
ATOM   1906  CA  VAL B   2     -64.976  31.873  53.101  1.00 28.32           C  
ANISOU 1906  CA  VAL B   2     3563   3853   3344   -136     76    -47       C  
ATOM   1907  C   VAL B   2     -65.106  31.749  51.568  1.00 25.79           C  
ANISOU 1907  C   VAL B   2     3249   3504   3047   -107     67    -39       C  
ATOM   1908  O   VAL B   2     -64.852  30.695  51.016  1.00 26.55           O  
ANISOU 1908  O   VAL B   2     3363   3582   3141   -115     62    -12       O  
ATOM   1909  CB  VAL B   2     -63.458  31.854  53.472  1.00 29.02           C  
ANISOU 1909  CB  VAL B   2     3675   3915   3435   -134     68    -19       C  
ATOM   1910  CG1 VAL B   2     -62.655  32.816  52.600  1.00 28.56           C  
ANISOU 1910  CG1 VAL B   2     3623   3822   3405    -94     62    -18       C  
ATOM   1911  CG2 VAL B   2     -63.277  32.190  54.960  1.00 28.08           C  
ANISOU 1911  CG2 VAL B   2     3549   3824   3296   -158     76    -29       C  
ATOM   1912  N   GLN B   3     -65.507  32.822  50.891  1.00 23.57           N  
ANISOU 1912  N   GLN B   3     2955   3217   2785    -73     65    -62       N  
ATOM   1913  CA  GLN B   3     -65.325  32.896  49.442  1.00 22.34           C  
ANISOU 1913  CA  GLN B   3     2811   3027   2651    -43     55    -51       C  
ATOM   1914  C   GLN B   3     -64.812  34.258  49.006  1.00 21.49           C  
ANISOU 1914  C   GLN B   3     2707   2894   2563     -8     48    -60       C  
ATOM   1915  O   GLN B   3     -65.390  35.261  49.356  1.00 20.34           O  
ANISOU 1915  O   GLN B   3     2543   2763   2421      5     49    -91       O  
ATOM   1916  CB  GLN B   3     -66.605  32.583  48.670  1.00 22.97           C  
ANISOU 1916  CB  GLN B   3     2876   3121   2732    -37     54    -67       C  
ATOM   1917  CG  GLN B   3     -66.329  32.439  47.171  1.00 23.37           C  
ANISOU 1917  CG  GLN B   3     2943   3136   2801    -12     44    -50       C  
ATOM   1918  CD  GLN B   3     -67.420  31.766  46.429  1.00 25.96           C  
ANISOU 1918  CD  GLN B   3     3260   3476   3127    -13     43    -58       C  
ATOM   1919  OE1 GLN B   3     -68.289  31.128  47.012  1.00 26.11           O  
ANISOU 1919  OE1 GLN B   3     3264   3529   3129    -40     52    -71       O  
ATOM   1920  NE2 GLN B   3     -67.368  31.858  45.101  1.00 26.61           N  
ANISOU 1920  NE2 GLN B   3     3353   3532   3227     13     33    -50       N  
ATOM   1921  N   LEU B   4     -63.765  34.284  48.171  1.00 20.01           N  
ANISOU 1921  N   LEU B   4     2543   2670   2389      6     41    -36       N  
ATOM   1922  CA  LEU B   4     -63.320  35.541  47.583  1.00 20.64           C  
ANISOU 1922  CA  LEU B   4     2632   2724   2487     35     35    -43       C  
ATOM   1923  C   LEU B   4     -63.883  35.691  46.181  1.00 20.71           C  
ANISOU 1923  C   LEU B   4     2647   2715   2509     59     25    -44       C  
ATOM   1924  O   LEU B   4     -63.807  34.750  45.368  1.00 21.16           O  
ANISOU 1924  O   LEU B   4     2712   2761   2566     55     23    -24       O  
ATOM   1925  CB  LEU B   4     -61.776  35.588  47.519  1.00 20.44           C  
ANISOU 1925  CB  LEU B   4     2628   2672   2466     33     34    -18       C  
ATOM   1926  CG  LEU B   4     -60.958  35.427  48.795  1.00 23.54           C  
ANISOU 1926  CG  LEU B   4     3020   3076   2846     11     41    -12       C  
ATOM   1927  CD1 LEU B   4     -59.450  35.636  48.534  1.00 22.60           C  
ANISOU 1927  CD1 LEU B   4     2920   2931   2735     15     38      6       C  
ATOM   1928  CD2 LEU B   4     -61.409  36.299  49.947  1.00 26.52           C  
ANISOU 1928  CD2 LEU B   4     3380   3479   3218      8     46    -39       C  
ATOM   1929  N   VAL B   5     -64.512  36.842  45.938  1.00 20.74           N  
ANISOU 1929  N   VAL B   5     2644   2715   2523     84     17    -70       N  
ATOM   1930  CA  VAL B   5     -65.128  37.118  44.642  1.00 22.07           C  
ANISOU 1930  CA  VAL B   5     2818   2865   2702    110      4    -74       C  
ATOM   1931  C   VAL B   5     -64.466  38.306  43.977  1.00 21.75           C  
ANISOU 1931  C   VAL B   5     2803   2788   2675    133     -7    -71       C  
ATOM   1932  O   VAL B   5     -64.477  39.421  44.510  1.00 22.45           O  
ANISOU 1932  O   VAL B   5     2890   2873   2768    145    -12    -91       O  
ATOM   1933  CB  VAL B   5     -66.639  37.393  44.784  1.00 22.97           C  
ANISOU 1933  CB  VAL B   5     2905   3007   2816    124     -1   -111       C  
ATOM   1934  CG1 VAL B   5     -67.223  37.759  43.442  1.00 23.21           C  
ANISOU 1934  CG1 VAL B   5     2944   3016   2857    154    -19   -116       C  
ATOM   1935  CG2 VAL B   5     -67.358  36.188  45.343  1.00 24.57           C  
ANISOU 1935  CG2 VAL B   5     3085   3249   3003     96     11   -115       C  
ATOM   1936  N   GLN B   6     -63.938  38.084  42.770  1.00 20.68           N  
ANISOU 1936  N   GLN B   6     2690   2623   2543    138    -13    -47       N  
ATOM   1937  CA  GLN B   6     -63.166  39.114  42.093  1.00 21.20           C  
ANISOU 1937  CA  GLN B   6     2785   2652   2617    151    -22    -40       C  
ATOM   1938  C   GLN B   6     -64.007  39.869  41.097  1.00 21.61           C  
ANISOU 1938  C   GLN B   6     2847   2685   2677    180    -42    -52       C  
ATOM   1939  O   GLN B   6     -65.088  39.400  40.688  1.00 22.51           O  
ANISOU 1939  O   GLN B   6     2947   2815   2792    190    -48    -63       O  
ATOM   1940  CB  GLN B   6     -61.962  38.508  41.389  1.00 20.58           C  
ANISOU 1940  CB  GLN B   6     2727   2555   2537    135    -16     -8       C  
ATOM   1941  CG  GLN B   6     -61.029  37.804  42.374  1.00 21.36           C  
ANISOU 1941  CG  GLN B   6     2818   2669   2628    110     -1      3       C  
ATOM   1942  CD  GLN B   6     -59.760  37.267  41.738  1.00 18.17           C  
ANISOU 1942  CD  GLN B   6     2431   2248   2224     97      4     27       C  
ATOM   1943  OE1 GLN B   6     -59.301  36.142  42.042  1.00 17.27           O  
ANISOU 1943  OE1 GLN B   6     2310   2146   2105     81     10     40       O  
ATOM   1944  NE2 GLN B   6     -59.191  38.049  40.823  1.00 20.25           N  
ANISOU 1944  NE2 GLN B   6     2718   2485   2492    104     -1     32       N  
ATOM   1945  N   SER B   7     -63.512  41.046  40.713  1.00 21.84           N  
ANISOU 1945  N   SER B   7     2904   2682   2711    192    -53    -51       N  
ATOM   1946  CA  SER B   7     -64.176  41.867  39.731  1.00 23.04           C  
ANISOU 1946  CA  SER B   7     3075   2808   2870    220    -76    -60       C  
ATOM   1947  C   SER B   7     -64.133  41.224  38.334  1.00 22.85           C  
ANISOU 1947  C   SER B   7     3068   2770   2843    220    -81    -38       C  
ATOM   1948  O   SER B   7     -63.352  40.294  38.071  1.00 22.15           O  
ANISOU 1948  O   SER B   7     2981   2685   2748    196    -66    -14       O  
ATOM   1949  CB  SER B   7     -63.555  43.260  39.724  1.00 22.04           C  
ANISOU 1949  CB  SER B   7     2979   2647   2747    228    -88    -62       C  
ATOM   1950  OG  SER B   7     -62.145  43.197  39.580  1.00 22.36           O  
ANISOU 1950  OG  SER B   7     3042   2672   2783    202    -73    -36       O  
ATOM   1951  N   GLY B   8     -65.026  41.675  37.457  1.00 23.10           N  
ANISOU 1951  N   GLY B   8     3110   2788   2879    246   -104    -47       N  
ATOM   1952  CA  GLY B   8     -65.066  41.180  36.089  1.00 24.15           C  
ANISOU 1952  CA  GLY B   8     3261   2907   3008    247   -110    -28       C  
ATOM   1953  C   GLY B   8     -63.835  41.400  35.231  1.00 24.34           C  
ANISOU 1953  C   GLY B   8     3324   2900   3026    230   -108      1       C  
ATOM   1954  O   GLY B   8     -63.001  42.279  35.475  1.00 24.75           O  
ANISOU 1954  O   GLY B   8     3398   2929   3076    222   -107      6       O  
ATOM   1955  N   ALA B   9     -63.743  40.584  34.180  1.00 24.57           N  
ANISOU 1955  N   ALA B   9     3358   2928   3050    222   -105     19       N  
ATOM   1956  CA  ALA B   9     -62.694  40.692  33.179  1.00 24.24           C  
ANISOU 1956  CA  ALA B   9     3350   2861   2999    204   -103     44       C  
ATOM   1957  C   ALA B   9     -62.608  42.101  32.585  1.00 24.53           C  
ANISOU 1957  C   ALA B   9     3430   2858   3032    214   -125     45       C  
ATOM   1958  O   ALA B   9     -63.628  42.828  32.519  1.00 25.79           O  
ANISOU 1958  O   ALA B   9     3594   3006   3197    245   -150     28       O  
ATOM   1959  CB  ALA B   9     -62.944  39.687  32.069  1.00 23.86           C  
ANISOU 1959  CB  ALA B   9     3299   2820   2946    200   -102     56       C  
ATOM   1960  N   GLU B  10     -61.395  42.481  32.176  1.00 24.92           N  
ANISOU 1960  N   GLU B  10     3509   2887   3072    189   -117     63       N  
ATOM   1961  CA  GLU B  10     -61.165  43.774  31.545  1.00 26.22           C  
ANISOU 1961  CA  GLU B  10     3722   3012   3229    191   -136     69       C  
ATOM   1962  C   GLU B  10     -60.396  43.609  30.274  1.00 25.25           C  
ANISOU 1962  C   GLU B  10     3630   2874   3090    165   -132     93       C  
ATOM   1963  O   GLU B  10     -59.635  42.645  30.109  1.00 25.14           O  
ANISOU 1963  O   GLU B  10     3600   2881   3072    140   -109    102       O  
ATOM   1964  CB  GLU B  10     -60.366  44.721  32.440  1.00 26.84           C  
ANISOU 1964  CB  GLU B  10     3814   3077   3309    179   -130     64       C  
ATOM   1965  CG  GLU B  10     -60.731  44.662  33.933  1.00 31.49           C  
ANISOU 1965  CG  GLU B  10     4363   3690   3911    191   -122     42       C  
ATOM   1966  CD  GLU B  10     -61.100  46.017  34.486  1.00 35.47           C  
ANISOU 1966  CD  GLU B  10     4886   4171   4422    212   -143     24       C  
ATOM   1967  OE1 GLU B  10     -60.965  47.012  33.749  1.00 38.49           O  
ANISOU 1967  OE1 GLU B  10     5314   4513   4798    214   -163     32       O  
ATOM   1968  OE2 GLU B  10     -61.526  46.097  35.660  1.00 36.16           O  
ANISOU 1968  OE2 GLU B  10     4942   4278   4520    224   -139      2       O  
ATOM   1969  N   VAL B  11     -60.613  44.568  29.379  1.00 26.19           N  
ANISOU 1969  N   VAL B  11     3795   2956   3199    171   -157    100       N  
ATOM   1970  CA  VAL B  11     -59.792  44.745  28.216  1.00 25.92           C  
ANISOU 1970  CA  VAL B  11     3801   2904   3146    141   -155    121       C  
ATOM   1971  C   VAL B  11     -59.119  46.092  28.366  1.00 25.83           C  
ANISOU 1971  C   VAL B  11     3834   2857   3125    125   -162    125       C  
ATOM   1972  O   VAL B  11     -59.798  47.105  28.595  1.00 27.00           O  
ANISOU 1972  O   VAL B  11     4004   2976   3278    152   -190    116       O  
ATOM   1973  CB  VAL B  11     -60.616  44.681  26.905  1.00 27.06           C  
ANISOU 1973  CB  VAL B  11     3967   3033   3280    156   -179    130       C  
ATOM   1974  CG1 VAL B  11     -59.749  45.072  25.715  1.00 27.72           C  
ANISOU 1974  CG1 VAL B  11     4100   3094   3339    120   -179    152       C  
ATOM   1975  CG2 VAL B  11     -61.146  43.269  26.704  1.00 25.45           C  
ANISOU 1975  CG2 VAL B  11     3720   2866   3084    164   -168    127       C  
ATOM   1976  N   LYS B  12     -57.806  46.091  28.237  1.00 24.22           N  
ANISOU 1976  N   LYS B  12     3641   2655   2907     84   -139    135       N  
ATOM   1977  CA  LYS B  12     -57.007  47.295  28.443  1.00 25.79           C  
ANISOU 1977  CA  LYS B  12     3879   2824   3095     61   -140    138       C  
ATOM   1978  C   LYS B  12     -56.054  47.507  27.314  1.00 26.92           C  
ANISOU 1978  C   LYS B  12     4063   2953   3211     17   -132    157       C  
ATOM   1979  O   LYS B  12     -55.357  46.597  26.880  1.00 27.37           O  
ANISOU 1979  O   LYS B  12     4100   3039   3260    -10   -108    161       O  
ATOM   1980  CB  LYS B  12     -56.282  47.265  29.791  1.00 25.22           C  
ANISOU 1980  CB  LYS B  12     3776   2773   3034     51   -116    125       C  
ATOM   1981  CG  LYS B  12     -57.220  47.368  30.994  1.00 25.55           C  
ANISOU 1981  CG  LYS B  12     3785   2822   3099     91   -126    104       C  
ATOM   1982  CD  LYS B  12     -57.769  48.800  31.093  1.00 28.91           C  
ANISOU 1982  CD  LYS B  12     4253   3205   3527    111   -158     98       C  
ATOM   1983  CE  LYS B  12     -58.950  48.903  32.040  1.00 30.68           C  
ANISOU 1983  CE  LYS B  12     4446   3438   3773    156   -174     73       C  
ATOM   1984  NZ  LYS B  12     -59.336  50.348  32.082  1.00 33.36           N  
ANISOU 1984  NZ  LYS B  12     4828   3732   4114    175   -206     65       N  
ATOM   1985  N   LYS B  13     -56.072  48.724  26.801  1.00 28.44           N  
ANISOU 1985  N   LYS B  13     4315   3103   3389      8   -155    166       N  
ATOM   1986  CA  LYS B  13     -55.141  49.122  25.778  1.00 29.50           C  
ANISOU 1986  CA  LYS B  13     4496   3221   3493    -40   -148    183       C  
ATOM   1987  C   LYS B  13     -53.733  49.091  26.378  1.00 29.93           C  
ANISOU 1987  C   LYS B  13     4535   3297   3542    -83   -112    177       C  
ATOM   1988  O   LYS B  13     -53.531  49.500  27.539  1.00 29.38           O  
ANISOU 1988  O   LYS B  13     4450   3227   3486    -75   -107    163       O  
ATOM   1989  CB  LYS B  13     -55.508  50.539  25.333  1.00 30.53           C  
ANISOU 1989  CB  LYS B  13     4696   3294   3609    -38   -185    194       C  
ATOM   1990  CG  LYS B  13     -54.866  50.980  24.055  1.00 32.46           C  
ANISOU 1990  CG  LYS B  13     5000   3516   3819    -86   -187    215       C  
ATOM   1991  CD  LYS B  13     -55.127  52.461  23.821  1.00 33.61           C  
ANISOU 1991  CD  LYS B  13     5219   3600   3950    -86   -224    226       C  
ATOM   1992  CE  LYS B  13     -54.667  52.860  22.453  1.00 38.85           C  
ANISOU 1992  CE  LYS B  13     5946   4239   4574   -133   -231    250       C  
ATOM   1993  NZ  LYS B  13     -54.764  54.334  22.294  1.00 40.74           N  
ANISOU 1993  NZ  LYS B  13     6264   4416   4799   -140   -266    261       N  
ATOM   1994  N   PRO B  14     -52.752  48.578  25.620  1.00 30.49           N  
ANISOU 1994  N   PRO B  14     4605   3388   3591   -127    -88    182       N  
ATOM   1995  CA  PRO B  14     -51.379  48.640  26.119  1.00 31.19           C  
ANISOU 1995  CA  PRO B  14     4681   3497   3672   -169    -55    172       C  
ATOM   1996  C   PRO B  14     -51.015  50.060  26.582  1.00 31.36           C  
ANISOU 1996  C   PRO B  14     4748   3482   3685   -186    -64    173       C  
ATOM   1997  O   PRO B  14     -51.361  51.053  25.926  1.00 33.14           O  
ANISOU 1997  O   PRO B  14     5035   3663   3894   -193    -90    187       O  
ATOM   1998  CB  PRO B  14     -50.537  48.213  24.912  1.00 30.71           C  
ANISOU 1998  CB  PRO B  14     4632   3454   3582   -217    -37    179       C  
ATOM   1999  CG  PRO B  14     -51.485  47.433  24.033  1.00 31.33           C  
ANISOU 1999  CG  PRO B  14     4704   3537   3664   -191    -52    189       C  
ATOM   2000  CD  PRO B  14     -52.822  48.080  24.235  1.00 31.40           C  
ANISOU 2000  CD  PRO B  14     4737   3508   3686   -144    -90    196       C  
ATOM   2001  N   GLY B  15     -50.344  50.143  27.725  1.00 31.26           N  
ANISOU 2001  N   GLY B  15     4706   3487   3684   -192    -44    156       N  
ATOM   2002  CA  GLY B  15     -50.017  51.399  28.386  1.00 30.16           C  
ANISOU 2002  CA  GLY B  15     4600   3318   3543   -203    -49    152       C  
ATOM   2003  C   GLY B  15     -50.987  51.869  29.472  1.00 29.80           C  
ANISOU 2003  C   GLY B  15     4545   3254   3525   -152    -72    142       C  
ATOM   2004  O   GLY B  15     -50.635  52.729  30.283  1.00 29.02           O  
ANISOU 2004  O   GLY B  15     4457   3139   3429   -159    -71    133       O  
ATOM   2005  N   SER B  16     -52.207  51.331  29.484  1.00 29.13           N  
ANISOU 2005  N   SER B  16     4437   3171   3458   -104    -92    142       N  
ATOM   2006  CA  SER B  16     -53.210  51.735  30.468  1.00 28.18           C  
ANISOU 2006  CA  SER B  16     4304   3039   3364    -55   -114    129       C  
ATOM   2007  C   SER B  16     -52.943  51.110  31.845  1.00 27.53           C  
ANISOU 2007  C   SER B  16     4160   2998   3302    -44    -89    110       C  
ATOM   2008  O   SER B  16     -51.905  50.471  32.055  1.00 26.12           O  
ANISOU 2008  O   SER B  16     3953   2852   3118    -74    -58    107       O  
ATOM   2009  CB  SER B  16     -54.639  51.443  29.986  1.00 28.13           C  
ANISOU 2009  CB  SER B  16     4296   3023   3369     -8   -144    132       C  
ATOM   2010  OG  SER B  16     -54.883  50.049  29.828  1.00 30.66           O  
ANISOU 2010  OG  SER B  16     4567   3386   3696      2   -129    132       O  
ATOM   2011  N   SER B  17     -53.857  51.358  32.765  1.00 27.88           N  
ANISOU 2011  N   SER B  17     4185   3039   3369     -3   -106     94       N  
ATOM   2012  CA  SER B  17     -53.831  50.751  34.082  1.00 28.36           C  
ANISOU 2012  CA  SER B  17     4189   3138   3447     12    -87     77       C  
ATOM   2013  C   SER B  17     -55.102  49.950  34.289  1.00 27.79           C  
ANISOU 2013  C   SER B  17     4080   3086   3393     54    -99     69       C  
ATOM   2014  O   SER B  17     -56.175  50.302  33.766  1.00 29.72           O  
ANISOU 2014  O   SER B  17     4343   3307   3641     84   -128     69       O  
ATOM   2015  CB  SER B  17     -53.735  51.797  35.183  1.00 28.83           C  
ANISOU 2015  CB  SER B  17     4254   3183   3516     18    -92     60       C  
ATOM   2016  OG  SER B  17     -52.488  52.480  35.148  1.00 32.03           O  
ANISOU 2016  OG  SER B  17     4688   3575   3906    -25    -77     63       O  
ATOM   2017  N   VAL B  18     -54.982  48.876  35.073  1.00 25.94           N  
ANISOU 2017  N   VAL B  18     3793   2896   3169     57    -77     62       N  
ATOM   2018  CA  VAL B  18     -56.126  48.119  35.516  1.00 24.83           C  
ANISOU 2018  CA  VAL B  18     3612   2778   3042     92    -84     52       C  
ATOM   2019  C   VAL B  18     -56.104  48.027  37.042  1.00 22.85           C  
ANISOU 2019  C   VAL B  18     3322   2554   2804     99    -71     33       C  
ATOM   2020  O   VAL B  18     -55.015  47.948  37.647  1.00 24.28           O  
ANISOU 2020  O   VAL B  18     3495   2750   2982     73    -50     33       O  
ATOM   2021  CB  VAL B  18     -56.148  46.717  34.841  1.00 23.91           C  
ANISOU 2021  CB  VAL B  18     3473   2689   2923     86    -72     65       C  
ATOM   2022  CG1 VAL B  18     -55.007  45.818  35.308  1.00 23.86           C  
ANISOU 2022  CG1 VAL B  18     3437   2715   2914     58    -42     67       C  
ATOM   2023  CG2 VAL B  18     -57.495  46.040  35.022  1.00 26.10           C  
ANISOU 2023  CG2 VAL B  18     3719   2984   3213    120    -83     55       C  
ATOM   2024  N   LYS B  19     -57.284  48.074  37.665  1.00 23.23           N  
ANISOU 2024  N   LYS B  19     3349   2611   2866    132    -86     15       N  
ATOM   2025  CA  LYS B  19     -57.403  47.862  39.113  1.00 22.47           C  
ANISOU 2025  CA  LYS B  19     3211   2546   2779    138    -73     -4       C  
ATOM   2026  C   LYS B  19     -58.421  46.751  39.358  1.00 23.20           C  
ANISOU 2026  C   LYS B  19     3264   2673   2879    156    -72    -11       C  
ATOM   2027  O   LYS B  19     -59.615  46.916  39.084  1.00 24.96           O  
ANISOU 2027  O   LYS B  19     3484   2891   3108    185    -93    -23       O  
ATOM   2028  CB  LYS B  19     -57.807  49.153  39.838  1.00 23.03           C  
ANISOU 2028  CB  LYS B  19     3293   2598   2859    157    -90    -27       C  
ATOM   2029  CG  LYS B  19     -57.635  49.042  41.356  1.00 23.06           C  
ANISOU 2029  CG  LYS B  19     3259   2633   2868    154    -73    -46       C  
ATOM   2030  CD  LYS B  19     -57.867  50.402  42.040  1.00 25.05           C  
ANISOU 2030  CD  LYS B  19     3524   2866   3130    169    -88    -70       C  
ATOM   2031  CE  LYS B  19     -57.756  50.258  43.565  1.00 26.82           C  
ANISOU 2031  CE  LYS B  19     3708   3126   3358    165    -71    -90       C  
ATOM   2032  NZ  LYS B  19     -57.945  51.590  44.236  1.00 30.02           N  
ANISOU 2032  NZ  LYS B  19     4124   3512   3772    179    -85   -116       N  
ATOM   2033  N   VAL B  20     -57.930  45.605  39.816  1.00 20.13           N  
ANISOU 2033  N   VAL B  20     2845   2316   2486    139    -50     -3       N  
ATOM   2034  CA  VAL B  20     -58.744  44.425  40.008  1.00 19.95           C  
ANISOU 2034  CA  VAL B  20     2788   2326   2466    147    -46     -6       C  
ATOM   2035  C   VAL B  20     -59.123  44.396  41.508  1.00 19.10           C  
ANISOU 2035  C   VAL B  20     2646   2247   2362    151    -39    -27       C  
ATOM   2036  O   VAL B  20     -58.276  44.696  42.368  1.00 20.26           O  
ANISOU 2036  O   VAL B  20     2790   2400   2507    136    -27    -30       O  
ATOM   2037  CB  VAL B  20     -57.922  43.182  39.635  1.00 19.50           C  
ANISOU 2037  CB  VAL B  20     2724   2285   2403    124    -29     15       C  
ATOM   2038  CG1 VAL B  20     -58.667  41.897  39.963  1.00 23.05           C  
ANISOU 2038  CG1 VAL B  20     3140   2766   2854    128    -24     14       C  
ATOM   2039  CG2 VAL B  20     -57.559  43.232  38.122  1.00 22.77           C  
ANISOU 2039  CG2 VAL B  20     3168   2672   2810    118    -35     34       C  
ATOM   2040  N   SER B  21     -60.359  44.016  41.807  1.00 19.44           N  
ANISOU 2040  N   SER B  21     2664   2313   2410    169    -46    -43       N  
ATOM   2041  CA  SER B  21     -60.801  43.913  43.196  1.00 20.15           C  
ANISOU 2041  CA  SER B  21     2721   2436   2501    169    -38    -65       C  
ATOM   2042  C   SER B  21     -61.115  42.479  43.585  1.00 20.10           C  
ANISOU 2042  C   SER B  21     2684   2466   2487    155    -24    -59       C  
ATOM   2043  O   SER B  21     -61.352  41.621  42.757  1.00 20.04           O  
ANISOU 2043  O   SER B  21     2677   2458   2477    154    -25    -44       O  
ATOM   2044  CB  SER B  21     -62.005  44.837  43.411  1.00 21.60           C  
ANISOU 2044  CB  SER B  21     2896   2618   2693    199    -57    -98       C  
ATOM   2045  OG  SER B  21     -63.144  44.401  42.698  1.00 25.43           O  
ANISOU 2045  OG  SER B  21     3372   3109   3180    218    -69   -104       O  
ATOM   2046  N   CYS B  22     -61.137  42.259  44.897  1.00 20.74           N  
ANISOU 2046  N   CYS B  22     2740   2577   2564    143    -12    -71       N  
ATOM   2047  CA  CYS B  22     -61.264  40.946  45.473  1.00 21.08           C  
ANISOU 2047  CA  CYS B  22     2760   2652   2596    124      1    -63       C  
ATOM   2048  C   CYS B  22     -62.046  41.120  46.758  1.00 22.26           C  
ANISOU 2048  C   CYS B  22     2880   2836   2741    122      5    -92       C  
ATOM   2049  O   CYS B  22     -61.485  41.633  47.718  1.00 21.72           O  
ANISOU 2049  O   CYS B  22     2809   2774   2671    113     12    -99       O  
ATOM   2050  CB  CYS B  22     -59.853  40.474  45.803  1.00 21.19           C  
ANISOU 2050  CB  CYS B  22     2783   2664   2605    100     13    -40       C  
ATOM   2051  SG  CYS B  22     -59.726  38.900  46.712  1.00 24.82           S  
ANISOU 2051  SG  CYS B  22     3222   3157   3050     74     25    -27       S  
ATOM   2052  N   LYS B  23     -63.326  40.734  46.747  1.00 21.76           N  
ANISOU 2052  N   LYS B  23     2795   2796   2676    129      2   -110       N  
ATOM   2053  CA  LYS B  23     -64.215  40.854  47.934  1.00 23.45           C  
ANISOU 2053  CA  LYS B  23     2977   3051   2884    124      7   -142       C  
ATOM   2054  C   LYS B  23     -64.363  39.558  48.728  1.00 23.14           C  
ANISOU 2054  C   LYS B  23     2919   3048   2826     91     23   -134       C  
ATOM   2055  O   LYS B  23     -64.668  38.502  48.192  1.00 22.81           O  
ANISOU 2055  O   LYS B  23     2877   3010   2778     82     25   -118       O  
ATOM   2056  CB  LYS B  23     -65.595  41.430  47.556  1.00 25.01           C  
ANISOU 2056  CB  LYS B  23     3157   3255   3089    153     -7   -178       C  
ATOM   2057  CG  LYS B  23     -66.496  41.670  48.801  1.00 28.52           C  
ANISOU 2057  CG  LYS B  23     3565   3745   3527    148     -1   -219       C  
ATOM   2058  CD  LYS B  23     -67.235  42.997  48.745  1.00 32.50           C  
ANISOU 2058  CD  LYS B  23     4061   4243   4046    184    -20   -260       C  
ATOM   2059  CE  LYS B  23     -68.213  43.131  49.925  1.00 36.29           C  
ANISOU 2059  CE  LYS B  23     4496   4773   4517    178    -13   -306       C  
ATOM   2060  NZ  LYS B  23     -68.772  44.521  49.920  1.00 40.14           N  
ANISOU 2060  NZ  LYS B  23     4978   5250   5023    217    -34   -349       N  
ATOM   2061  N   ALA B  24     -64.118  39.663  50.026  1.00 23.19           N  
ANISOU 2061  N   ALA B  24     2912   3078   2821     72     34   -144       N  
ATOM   2062  CA  ALA B  24     -64.318  38.549  50.929  1.00 24.41           C  
ANISOU 2062  CA  ALA B  24     3052   3268   2955     38     47   -138       C  
ATOM   2063  C   ALA B  24     -65.809  38.545  51.247  1.00 25.49           C  
ANISOU 2063  C   ALA B  24     3156   3444   3085     38     49   -175       C  
ATOM   2064  O   ALA B  24     -66.355  39.535  51.749  1.00 25.95           O  
ANISOU 2064  O   ALA B  24     3195   3517   3147     52     47   -212       O  
ATOM   2065  CB  ALA B  24     -63.508  38.758  52.185  1.00 24.42           C  
ANISOU 2065  CB  ALA B  24     3052   3282   2946     19     56   -136       C  
ATOM   2066  N   SER B  25     -66.459  37.442  50.900  1.00 26.27           N  
ANISOU 2066  N   SER B  25     3250   3559   3174     23     52   -167       N  
ATOM   2067  CA  SER B  25     -67.909  37.329  50.928  1.00 29.18           C  
ANISOU 2067  CA  SER B  25     3588   3963   3537     23     54   -202       C  
ATOM   2068  C   SER B  25     -68.484  37.448  52.326  1.00 30.20           C  
ANISOU 2068  C   SER B  25     3687   4141   3646     -2     67   -235       C  
ATOM   2069  O   SER B  25     -69.633  37.912  52.486  1.00 31.91           O  
ANISOU 2069  O   SER B  25     3872   4390   3864      7     66   -279       O  
ATOM   2070  CB  SER B  25     -68.310  35.983  50.316  1.00 29.78           C  
ANISOU 2070  CB  SER B  25     3668   4044   3603      4     57   -182       C  
ATOM   2071  OG  SER B  25     -67.830  34.929  51.134  1.00 32.45           O  
ANISOU 2071  OG  SER B  25     4014   4395   3919    -37     69   -157       O  
ATOM   2072  N   GLY B  26     -67.711  37.061  53.344  1.00 30.30           N  
ANISOU 2072  N   GLY B  26     3707   4162   3642    -34     78   -216       N  
ATOM   2073  CA  GLY B  26     -68.176  37.118  54.743  1.00 30.64           C  
ANISOU 2073  CA  GLY B  26     3725   4255   3663    -65     92   -244       C  
ATOM   2074  C   GLY B  26     -68.117  38.485  55.425  1.00 30.30           C  
ANISOU 2074  C   GLY B  26     3665   4220   3628    -46     91   -279       C  
ATOM   2075  O   GLY B  26     -68.476  38.629  56.607  1.00 31.49           O  
ANISOU 2075  O   GLY B  26     3791   4413   3761    -70    103   -306       O  
ATOM   2076  N   GLY B  27     -67.620  39.495  54.714  1.00 29.06           N  
ANISOU 2076  N   GLY B  27     3521   4021   3498     -5     76   -279       N  
ATOM   2077  CA  GLY B  27     -67.579  40.862  55.240  1.00 28.49           C  
ANISOU 2077  CA  GLY B  27     3437   3951   3439     17     72   -313       C  
ATOM   2078  C   GLY B  27     -66.348  41.226  56.062  1.00 27.20           C  
ANISOU 2078  C   GLY B  27     3289   3776   3271      5     78   -296       C  
ATOM   2079  O   GLY B  27     -66.244  42.344  56.565  1.00 27.94           O  
ANISOU 2079  O   GLY B  27     3373   3870   3374     21     75   -324       O  
ATOM   2080  N   THR B  28     -65.384  40.308  56.174  1.00 26.02           N  
ANISOU 2080  N   THR B  28     3163   3615   3109    -21     84   -252       N  
ATOM   2081  CA  THR B  28     -64.191  40.565  56.984  1.00 25.06           C  
ANISOU 2081  CA  THR B  28     3054   3486   2982    -33     88   -236       C  
ATOM   2082  C   THR B  28     -62.998  39.738  56.529  1.00 24.10           C  
ANISOU 2082  C   THR B  28     2965   3332   2859    -42     86   -186       C  
ATOM   2083  O   THR B  28     -63.163  38.610  56.082  1.00 24.70           O  
ANISOU 2083  O   THR B  28     3051   3407   2928    -56     85   -163       O  
ATOM   2084  CB  THR B  28     -64.408  40.347  58.519  1.00 24.61           C  
ANISOU 2084  CB  THR B  28     2975   3479   2898    -70    103   -253       C  
ATOM   2085  OG1 THR B  28     -63.196  40.663  59.181  1.00 25.44           O  
ANISOU 2085  OG1 THR B  28     3095   3572   3000    -77    105   -238       O  
ATOM   2086  CG2 THR B  28     -64.778  38.909  58.881  1.00 25.31           C  
ANISOU 2086  CG2 THR B  28     3065   3595   2958   -111    112   -234       C  
ATOM   2087  N   PHE B  29     -61.802  40.314  56.617  1.00 23.23           N  
ANISOU 2087  N   PHE B  29     2873   3196   2759    -34     83   -173       N  
ATOM   2088  CA  PHE B  29     -60.563  39.563  56.365  1.00 22.51           C  
ANISOU 2088  CA  PHE B  29     2807   3080   2665    -44     81   -132       C  
ATOM   2089  C   PHE B  29     -60.019  38.892  57.608  1.00 22.82           C  
ANISOU 2089  C   PHE B  29     2846   3144   2680    -77     87   -120       C  
ATOM   2090  O   PHE B  29     -59.072  38.096  57.550  1.00 21.56           O  
ANISOU 2090  O   PHE B  29     2707   2970   2515    -86     83    -89       O  
ATOM   2091  CB  PHE B  29     -59.493  40.493  55.775  1.00 22.53           C  
ANISOU 2091  CB  PHE B  29     2829   3045   2688    -21     76   -126       C  
ATOM   2092  CG  PHE B  29     -59.804  40.953  54.372  1.00 22.89           C  
ANISOU 2092  CG  PHE B  29     2886   3058   2755      8     66   -127       C  
ATOM   2093  CD1 PHE B  29     -59.815  40.043  53.320  1.00 25.51           C  
ANISOU 2093  CD1 PHE B  29     3231   3372   3089     10     61   -101       C  
ATOM   2094  CD2 PHE B  29     -60.084  42.301  54.114  1.00 22.45           C  
ANISOU 2094  CD2 PHE B  29     2828   2986   2715     33     60   -153       C  
ATOM   2095  CE1 PHE B  29     -60.104  40.454  52.018  1.00 24.60           C  
ANISOU 2095  CE1 PHE B  29     3128   3228   2992     35     52   -101       C  
ATOM   2096  CE2 PHE B  29     -60.353  42.731  52.800  1.00 24.68           C  
ANISOU 2096  CE2 PHE B  29     3126   3235   3014     59     48   -151       C  
ATOM   2097  CZ  PHE B  29     -60.376  41.819  51.759  1.00 22.48           C  
ANISOU 2097  CZ  PHE B  29     2861   2943   2737     59     45   -125       C  
ATOM   2098  N   SER B  30     -60.611  39.210  58.749  1.00 23.18           N  
ANISOU 2098  N   SER B  30     2870   3228   2710    -94     96   -147       N  
ATOM   2099  CA  SER B  30     -60.207  38.542  59.978  1.00 23.46           C  
ANISOU 2099  CA  SER B  30     2907   3290   2718   -129    101   -135       C  
ATOM   2100  C   SER B  30     -58.669  38.550  60.186  1.00 23.19           C  
ANISOU 2100  C   SER B  30     2894   3233   2686   -127     96   -111       C  
ATOM   2101  O   SER B  30     -58.012  39.575  59.942  1.00 24.02           O  
ANISOU 2101  O   SER B  30     2999   3316   2810   -105     95   -120       O  
ATOM   2102  CB  SER B  30     -60.726  37.111  59.971  1.00 23.48           C  
ANISOU 2102  CB  SER B  30     2917   3306   2699   -156    101   -114       C  
ATOM   2103  OG  SER B  30     -60.736  36.619  61.295  1.00 27.38           O  
ANISOU 2103  OG  SER B  30     3408   3834   3161   -195    106   -113       O  
ATOM   2104  N   SER B  31     -58.088  37.425  60.612  1.00 23.03           N  
ANISOU 2104  N   SER B  31     2889   3214   2646   -150     90    -81       N  
ATOM   2105  CA  SER B  31     -56.655  37.393  60.874  1.00 22.28           C  
ANISOU 2105  CA  SER B  31     2811   3101   2553   -147     83    -63       C  
ATOM   2106  C   SER B  31     -55.873  36.800  59.724  1.00 21.23           C  
ANISOU 2106  C   SER B  31     2699   2930   2436   -130     71    -35       C  
ATOM   2107  O   SER B  31     -54.915  36.089  59.953  1.00 21.55           O  
ANISOU 2107  O   SER B  31     2756   2962   2471   -136     60    -13       O  
ATOM   2108  CB  SER B  31     -56.318  36.670  62.182  1.00 23.41           C  
ANISOU 2108  CB  SER B  31     2960   3270   2666   -180     80    -50       C  
ATOM   2109  OG  SER B  31     -57.115  37.218  63.237  1.00 26.50           O  
ANISOU 2109  OG  SER B  31     3329   3701   3039   -199     93    -79       O  
ATOM   2110  N   TYR B  32     -56.285  37.112  58.493  1.00 18.93           N  
ANISOU 2110  N   TYR B  32     2408   2617   2167   -107     71    -39       N  
ATOM   2111  CA  TYR B  32     -55.689  36.524  57.273  1.00 19.15           C  
ANISOU 2111  CA  TYR B  32     2454   2611   2210    -92     62    -16       C  
ATOM   2112  C   TYR B  32     -55.156  37.586  56.321  1.00 18.46           C  
ANISOU 2112  C   TYR B  32     2370   2497   2148    -65     63    -25       C  
ATOM   2113  O   TYR B  32     -55.605  38.744  56.370  1.00 18.82           O  
ANISOU 2113  O   TYR B  32     2405   2545   2201    -55     70    -49       O  
ATOM   2114  CB  TYR B  32     -56.746  35.647  56.595  1.00 19.63           C  
ANISOU 2114  CB  TYR B  32     2517   2673   2269    -95     60     -7       C  
ATOM   2115  CG  TYR B  32     -57.325  34.667  57.575  1.00 19.88           C  
ANISOU 2115  CG  TYR B  32     2549   2733   2273   -127     59      0       C  
ATOM   2116  CD1 TYR B  32     -56.728  33.440  57.806  1.00 21.73           C  
ANISOU 2116  CD1 TYR B  32     2803   2960   2494   -143     47     28       C  
ATOM   2117  CD2 TYR B  32     -58.411  35.033  58.378  1.00 23.48           C  
ANISOU 2117  CD2 TYR B  32     2985   3225   2714   -144     71    -24       C  
ATOM   2118  CE1 TYR B  32     -57.249  32.560  58.748  1.00 25.26           C  
ANISOU 2118  CE1 TYR B  32     3256   3431   2913   -176     45     37       C  
ATOM   2119  CE2 TYR B  32     -58.916  34.187  59.341  1.00 27.98           C  
ANISOU 2119  CE2 TYR B  32     3555   3823   3254   -180     72    -19       C  
ATOM   2120  CZ  TYR B  32     -58.343  32.951  59.520  1.00 25.77           C  
ANISOU 2120  CZ  TYR B  32     3300   3532   2959   -198     59     14       C  
ATOM   2121  OH  TYR B  32     -58.878  32.120  60.474  1.00 33.03           O  
ANISOU 2121  OH  TYR B  32     4226   4478   3846   -237     60     21       O  
ATOM   2122  N   ALA B  33     -54.219  37.193  55.433  1.00 18.11           N  
ANISOU 2122  N   ALA B  33     2341   2426   2115    -55     56     -7       N  
ATOM   2123  CA  ALA B  33     -53.653  38.113  54.488  1.00 18.22           C  
ANISOU 2123  CA  ALA B  33     2362   2415   2148    -37     58    -13       C  
ATOM   2124  C   ALA B  33     -54.211  37.821  53.135  1.00 18.04           C  
ANISOU 2124  C   ALA B  33     2346   2371   2136    -24     54     -5       C  
ATOM   2125  O   ALA B  33     -54.874  36.809  52.937  1.00 18.02           O  
ANISOU 2125  O   ALA B  33     2343   2374   2128    -29     50      7       O  
ATOM   2126  CB  ALA B  33     -52.105  38.068  54.460  1.00 18.34           C  
ANISOU 2126  CB  ALA B  33     2384   2418   2165    -37     55     -5       C  
ATOM   2127  N   ILE B  34     -53.985  38.753  52.226  1.00 17.27           N  
ANISOU 2127  N   ILE B  34     2257   2252   2054     -9     56    -11       N  
ATOM   2128  CA  ILE B  34     -54.368  38.579  50.832  1.00 17.99           C  
ANISOU 2128  CA  ILE B  34     2358   2321   2155      4     52     -3       C  
ATOM   2129  C   ILE B  34     -53.110  38.588  50.002  1.00 19.07           C  
ANISOU 2129  C   ILE B  34     2509   2436   2299      5     51      7       C  
ATOM   2130  O   ILE B  34     -52.203  39.410  50.222  1.00 19.97           O  
ANISOU 2130  O   ILE B  34     2627   2546   2416      2     56     -1       O  
ATOM   2131  CB  ILE B  34     -55.350  39.669  50.357  1.00 18.66           C  
ANISOU 2131  CB  ILE B  34     2444   2397   2250     20     52    -21       C  
ATOM   2132  CG1 ILE B  34     -56.702  39.581  51.080  1.00 19.16           C  
ANISOU 2132  CG1 ILE B  34     2487   2486   2306     19     52    -36       C  
ATOM   2133  CG2 ILE B  34     -55.537  39.558  48.835  1.00 20.03           C  
ANISOU 2133  CG2 ILE B  34     2632   2545   2433     32     46    -10       C  
ATOM   2134  CD1 ILE B  34     -57.485  38.358  50.817  1.00 22.16           C  
ANISOU 2134  CD1 ILE B  34     2862   2878   2679     13     50    -25       C  
ATOM   2135  N   SER B  35     -53.027  37.636  49.069  1.00 18.81           N  
ANISOU 2135  N   SER B  35     2482   2394   2269      7     46     23       N  
ATOM   2136  CA  SER B  35     -51.888  37.496  48.198  1.00 17.77           C  
ANISOU 2136  CA  SER B  35     2361   2247   2144      7     45     30       C  
ATOM   2137  C   SER B  35     -52.392  37.589  46.748  1.00 17.90           C  
ANISOU 2137  C   SER B  35     2389   2244   2168     17     43     35       C  
ATOM   2138  O   SER B  35     -53.507  37.139  46.448  1.00 17.49           O  
ANISOU 2138  O   SER B  35     2335   2194   2117     23     39     39       O  
ATOM   2139  CB  SER B  35     -51.299  36.121  48.470  1.00 18.62           C  
ANISOU 2139  CB  SER B  35     2464   2363   2246      1     38     42       C  
ATOM   2140  OG  SER B  35     -50.087  35.914  47.812  1.00 22.81           O  
ANISOU 2140  OG  SER B  35     2999   2885   2781      1     36     43       O  
ATOM   2141  N   TRP B  36     -51.595  38.169  45.854  1.00 15.97           N  
ANISOU 2141  N   TRP B  36     2158   1983   1928     15     47     33       N  
ATOM   2142  CA  TRP B  36     -51.999  38.243  44.425  1.00 15.40           C  
ANISOU 2142  CA  TRP B  36     2099   1891   1860     22     44     40       C  
ATOM   2143  C   TRP B  36     -51.015  37.443  43.594  1.00 16.19           C  
ANISOU 2143  C   TRP B  36     2201   1989   1961     15     44     47       C  
ATOM   2144  O   TRP B  36     -49.819  37.526  43.785  1.00 15.36           O  
ANISOU 2144  O   TRP B  36     2094   1887   1854      5     49     41       O  
ATOM   2145  CB  TRP B  36     -52.028  39.714  43.950  1.00 16.84           C  
ANISOU 2145  CB  TRP B  36     2300   2053   2044     24     46     31       C  
ATOM   2146  CG  TRP B  36     -53.165  40.474  44.503  1.00 18.72           C  
ANISOU 2146  CG  TRP B  36     2537   2291   2285     36     42     21       C  
ATOM   2147  CD1 TRP B  36     -53.191  41.195  45.679  1.00 21.29           C  
ANISOU 2147  CD1 TRP B  36     2854   2625   2609     35     45      7       C  
ATOM   2148  CD2 TRP B  36     -54.481  40.600  43.931  1.00 18.53           C  
ANISOU 2148  CD2 TRP B  36     2516   2258   2265     53     32     20       C  
ATOM   2149  NE1 TRP B  36     -54.435  41.775  45.846  1.00 19.81           N  
ANISOU 2149  NE1 TRP B  36     2666   2436   2426     51     38     -5       N  
ATOM   2150  CE2 TRP B  36     -55.237  41.446  44.787  1.00 20.47           C  
ANISOU 2150  CE2 TRP B  36     2755   2509   2513     63     29      2       C  
ATOM   2151  CE3 TRP B  36     -55.081  40.114  42.753  1.00 19.26           C  
ANISOU 2151  CE3 TRP B  36     2617   2341   2359     61     25     30       C  
ATOM   2152  CZ2 TRP B  36     -56.568  41.786  44.523  1.00 20.51           C  
ANISOU 2152  CZ2 TRP B  36     2760   2511   2523     82     18     -8       C  
ATOM   2153  CZ3 TRP B  36     -56.405  40.472  42.475  1.00 21.83           C  
ANISOU 2153  CZ3 TRP B  36     2943   2663   2689     80     15     22       C  
ATOM   2154  CH2 TRP B  36     -57.126  41.313  43.352  1.00 20.05           C  
ANISOU 2154  CH2 TRP B  36     2709   2442   2466     91     11      2       C  
ATOM   2155  N   VAL B  37     -51.573  36.613  42.713  1.00 16.57           N  
ANISOU 2155  N   VAL B  37     2251   2033   2012     21     39     57       N  
ATOM   2156  CA  VAL B  37     -50.825  35.697  41.848  1.00 15.81           C  
ANISOU 2156  CA  VAL B  37     2153   1936   1917     17     37     62       C  
ATOM   2157  C   VAL B  37     -51.437  35.730  40.453  1.00 16.90           C  
ANISOU 2157  C   VAL B  37     2305   2060   2058     22     36     68       C  
ATOM   2158  O   VAL B  37     -52.678  35.728  40.314  1.00 18.97           O  
ANISOU 2158  O   VAL B  37     2568   2318   2320     32     31     73       O  
ATOM   2159  CB  VAL B  37     -50.893  34.228  42.402  1.00 16.14           C  
ANISOU 2159  CB  VAL B  37     2182   1991   1960     20     28     69       C  
ATOM   2160  CG1 VAL B  37     -50.143  33.281  41.504  1.00 18.17           C  
ANISOU 2160  CG1 VAL B  37     2437   2246   2221     19     24     71       C  
ATOM   2161  CG2 VAL B  37     -50.332  34.201  43.820  1.00 17.16           C  
ANISOU 2161  CG2 VAL B  37     2301   2133   2084     15     27     65       C  
ATOM   2162  N   ARG B  38     -50.600  35.750  39.418  1.00 16.63           N  
ANISOU 2162  N   ARG B  38     2277   2019   2021     13     39     67       N  
ATOM   2163  CA  ARG B  38     -51.154  35.690  38.051  1.00 17.98           C  
ANISOU 2163  CA  ARG B  38     2461   2179   2193     16     37     74       C  
ATOM   2164  C   ARG B  38     -50.736  34.420  37.306  1.00 18.59           C  
ANISOU 2164  C   ARG B  38     2529   2263   2273     14     35     76       C  
ATOM   2165  O   ARG B  38     -49.730  33.796  37.636  1.00 19.06           O  
ANISOU 2165  O   ARG B  38     2574   2333   2334      9     35     69       O  
ATOM   2166  CB  ARG B  38     -50.846  36.960  37.240  1.00 18.95           C  
ANISOU 2166  CB  ARG B  38     2608   2285   2308      5     42     71       C  
ATOM   2167  CG  ARG B  38     -49.421  37.038  36.719  1.00 20.19           C  
ANISOU 2167  CG  ARG B  38     2766   2446   2459    -16     52     62       C  
ATOM   2168  CD  ARG B  38     -49.301  38.239  35.788  1.00 19.68           C  
ANISOU 2168  CD  ARG B  38     2731   2363   2383    -31     56     63       C  
ATOM   2169  NE  ARG B  38     -47.972  38.249  35.202  1.00 23.18           N  
ANISOU 2169  NE  ARG B  38     3175   2816   2818    -56     68     53       N  
ATOM   2170  CZ  ARG B  38     -47.467  39.289  34.549  1.00 23.04           C  
ANISOU 2170  CZ  ARG B  38     3182   2786   2787    -79     76     50       C  
ATOM   2171  NH1 ARG B  38     -48.212  40.394  34.376  1.00 22.09           N  
ANISOU 2171  NH1 ARG B  38     3092   2639   2661    -77     69     60       N  
ATOM   2172  NH2 ARG B  38     -46.236  39.218  34.071  1.00 27.05           N  
ANISOU 2172  NH2 ARG B  38     3685   3308   3285   -105     89     36       N  
ATOM   2173  N   GLN B  39     -51.527  34.062  36.309  1.00 20.03           N  
ANISOU 2173  N   GLN B  39     2716   2438   2455     21     30     83       N  
ATOM   2174  CA  GLN B  39     -51.188  32.959  35.422  1.00 22.08           C  
ANISOU 2174  CA  GLN B  39     2969   2702   2718     19     28     84       C  
ATOM   2175  C   GLN B  39     -51.282  33.563  34.014  1.00 23.55           C  
ANISOU 2175  C   GLN B  39     3174   2878   2898     12     32     86       C  
ATOM   2176  O   GLN B  39     -52.379  33.782  33.523  1.00 22.10           O  
ANISOU 2176  O   GLN B  39     3001   2685   2713     21     26     94       O  
ATOM   2177  CB  GLN B  39     -52.145  31.790  35.652  1.00 22.28           C  
ANISOU 2177  CB  GLN B  39     2983   2731   2750     32     19     92       C  
ATOM   2178  CG  GLN B  39     -52.037  30.629  34.643  1.00 24.46           C  
ANISOU 2178  CG  GLN B  39     3254   3009   3030     33     14     93       C  
ATOM   2179  CD  GLN B  39     -50.677  29.985  34.589  1.00 25.92           C  
ANISOU 2179  CD  GLN B  39     3427   3203   3218     27     14     81       C  
ATOM   2180  OE1 GLN B  39     -49.808  30.405  33.824  1.00 26.45           O  
ANISOU 2180  OE1 GLN B  39     3496   3273   3281     16     22     71       O  
ATOM   2181  NE2 GLN B  39     -50.482  28.954  35.402  1.00 24.29           N  
ANISOU 2181  NE2 GLN B  39     3210   3002   3019     34      4     81       N  
ATOM   2182  N   ALA B  41     -50.117  33.851  33.427  1.00 25.15           N  
ANISOU 2182  N   ALA B  41     3380   3084   3094     -6     41     76       N  
ATOM   2183  CA  ALA B  41     -50.056  34.392  32.066  1.00 27.89           C  
ANISOU 2183  CA  ALA B  41     3746   3423   3429    -20     45     78       C  
ATOM   2184  C   ALA B  41     -49.848  33.309  30.992  1.00 29.08           C  
ANISOU 2184  C   ALA B  41     3885   3582   3580    -22     44     74       C  
ATOM   2185  O   ALA B  41     -49.660  33.621  29.818  1.00 31.18           O  
ANISOU 2185  O   ALA B  41     4166   3846   3836    -37     49     73       O  
ATOM   2186  CB  ALA B  41     -49.009  35.527  31.978  1.00 27.58           C  
ANISOU 2186  CB  ALA B  41     3722   3381   3378    -44     56     68       C  
ATOM   2187  N   GLY B  42     -49.949  32.034  31.383  1.00 29.54           N  
ANISOU 2187  N   GLY B  42     3922   3651   3651     -8     38     72       N  
ATOM   2188  CA  GLY B  42     -49.736  30.903  30.473  1.00 31.25           C  
ANISOU 2188  CA  GLY B  42     4126   3877   3872     -8     35     66       C  
ATOM   2189  C   GLY B  42     -48.403  30.179  30.628  1.00 31.46           C  
ANISOU 2189  C   GLY B  42     4130   3920   3903    -13     37     46       C  
ATOM   2190  O   GLY B  42     -48.226  29.061  30.119  1.00 33.25           O  
ANISOU 2190  O   GLY B  42     4342   4154   4137     -8     31     38       O  
ATOM   2191  N   GLN B  43     -47.452  30.812  31.302  1.00 31.70           N  
ANISOU 2191  N   GLN B  43     4157   3957   3930    -23     44     34       N  
ATOM   2192  CA  GLN B  43     -46.119  30.238  31.504  1.00 31.21           C  
ANISOU 2192  CA  GLN B  43     4073   3914   3873    -27     44      9       C  
ATOM   2193  C   GLN B  43     -45.938  29.613  32.884  1.00 30.07           C  
ANISOU 2193  C   GLN B  43     3914   3772   3741     -9     31      8       C  
ATOM   2194  O   GLN B  43     -44.905  28.995  33.159  1.00 31.07           O  
ANISOU 2194  O   GLN B  43     4020   3911   3873     -6     26    -13       O  
ATOM   2195  CB  GLN B  43     -45.047  31.317  31.311  1.00 32.46           C  
ANISOU 2195  CB  GLN B  43     4234   4083   4017    -53     61     -8       C  
ATOM   2196  CG  GLN B  43     -44.638  31.510  29.845  1.00 37.20           C  
ANISOU 2196  CG  GLN B  43     4838   4692   4603    -77     72    -19       C  
ATOM   2197  CD  GLN B  43     -43.192  31.996  29.686  1.00 42.90           C  
ANISOU 2197  CD  GLN B  43     5549   5436   5313   -104     87    -48       C  
ATOM   2198  OE1 GLN B  43     -42.845  32.641  28.686  1.00 45.49           O  
ANISOU 2198  OE1 GLN B  43     5889   5770   5623   -134    102    -55       O  
ATOM   2199  NE2 GLN B  43     -42.339  31.680  30.669  1.00 44.24           N  
ANISOU 2199  NE2 GLN B  43     5696   5621   5493    -96     83    -68       N  
ATOM   2200  N   GLY B  44     -46.937  29.768  33.743  1.00 26.74           N  
ANISOU 2200  N   GLY B  44     3502   3336   3320      2     25     29       N  
ATOM   2201  CA  GLY B  44     -46.807  29.361  35.146  1.00 23.88           C  
ANISOU 2201  CA  GLY B  44     3133   2976   2966     14     15     31       C  
ATOM   2202  C   GLY B  44     -47.211  30.449  36.131  1.00 22.56           C  
ANISOU 2202  C   GLY B  44     2976   2804   2792     10     21     40       C  
ATOM   2203  O   GLY B  44     -47.320  31.645  35.793  1.00 21.06           O  
ANISOU 2203  O   GLY B  44     2799   2609   2593     -2     33     42       O  
ATOM   2204  N   LEU B  45     -47.407  30.053  37.379  1.00 20.00           N  
ANISOU 2204  N   LEU B  45     2647   2480   2471     20     11     46       N  
ATOM   2205  CA  LEU B  45     -47.821  30.996  38.419  1.00 21.18           C  
ANISOU 2205  CA  LEU B  45     2804   2628   2615     17     16     53       C  
ATOM   2206  C   LEU B  45     -46.735  32.002  38.795  1.00 19.57           C  
ANISOU 2206  C   LEU B  45     2598   2432   2407      6     26     38       C  
ATOM   2207  O   LEU B  45     -45.548  31.669  38.882  1.00 20.29           O  
ANISOU 2207  O   LEU B  45     2676   2535   2499      3     24     20       O  
ATOM   2208  CB  LEU B  45     -48.258  30.210  39.660  1.00 19.28           C  
ANISOU 2208  CB  LEU B  45     2560   2390   2377     26      3     63       C  
ATOM   2209  CG  LEU B  45     -49.432  29.257  39.511  1.00 21.93           C  
ANISOU 2209  CG  LEU B  45     2898   2718   2714     33     -7     79       C  
ATOM   2210  CD1 LEU B  45     -49.700  28.557  40.871  1.00 22.07           C  
ANISOU 2210  CD1 LEU B  45     2916   2740   2730     35    -19     87       C  
ATOM   2211  CD2 LEU B  45     -50.684  29.960  39.026  1.00 21.30           C  
ANISOU 2211  CD2 LEU B  45     2828   2633   2632     33      2     87       C  
ATOM   2212  N   GLU B  46     -47.148  33.260  39.013  1.00 19.61           N  
ANISOU 2212  N   GLU B  46     2616   2430   2405     -1     37     41       N  
ATOM   2213  CA  GLU B  46     -46.237  34.332  39.348  1.00 20.62           C  
ANISOU 2213  CA  GLU B  46     2745   2563   2527    -15     48     28       C  
ATOM   2214  C   GLU B  46     -46.785  35.097  40.556  1.00 19.43           C  
ANISOU 2214  C   GLU B  46     2599   2410   2374    -12     49     33       C  
ATOM   2215  O   GLU B  46     -47.909  35.621  40.517  1.00 19.32           O  
ANISOU 2215  O   GLU B  46     2597   2384   2360     -7     49     44       O  
ATOM   2216  CB  GLU B  46     -46.136  35.320  38.193  1.00 20.96           C  
ANISOU 2216  CB  GLU B  46     2806   2596   2562    -31     60     25       C  
ATOM   2217  CG  GLU B  46     -45.414  34.845  36.981  1.00 25.39           C  
ANISOU 2217  CG  GLU B  46     3362   3164   3120    -42     64     15       C  
ATOM   2218  CD  GLU B  46     -45.194  36.008  36.026  1.00 31.78           C  
ANISOU 2218  CD  GLU B  46     4193   3964   3916    -65     77     12       C  
ATOM   2219  OE1 GLU B  46     -44.201  36.753  36.213  1.00 33.88           O  
ANISOU 2219  OE1 GLU B  46     4460   4239   4175    -85     89     -3       O  
ATOM   2220  OE2 GLU B  46     -46.019  36.174  35.105  1.00 35.46           O  
ANISOU 2220  OE2 GLU B  46     4678   4415   4379    -65     76     26       O  
ATOM   2221  N   TRP B  47     -46.004  35.191  41.625  1.00 19.42           N  
ANISOU 2221  N   TRP B  47     2586   2421   2371    -14     49     22       N  
ATOM   2222  CA  TRP B  47     -46.422  35.957  42.764  1.00 20.27           C  
ANISOU 2222  CA  TRP B  47     2696   2529   2476    -14     51     24       C  
ATOM   2223  C   TRP B  47     -46.224  37.438  42.509  1.00 20.11           C  
ANISOU 2223  C   TRP B  47     2691   2499   2451    -27     64     16       C  
ATOM   2224  O   TRP B  47     -45.173  37.877  42.012  1.00 22.14           O  
ANISOU 2224  O   TRP B  47     2949   2759   2704    -43     73      3       O  
ATOM   2225  CB  TRP B  47     -45.645  35.527  43.994  1.00 19.92           C  
ANISOU 2225  CB  TRP B  47     2636   2501   2431    -12     45     16       C  
ATOM   2226  CG  TRP B  47     -46.171  36.073  45.303  1.00 20.58           C  
ANISOU 2226  CG  TRP B  47     2719   2589   2511    -11     45     18       C  
ATOM   2227  CD1 TRP B  47     -47.331  35.731  45.917  1.00 24.39           C  
ANISOU 2227  CD1 TRP B  47     3202   3072   2992     -4     39     31       C  
ATOM   2228  CD2 TRP B  47     -45.543  37.058  46.142  1.00 20.33           C  
ANISOU 2228  CD2 TRP B  47     2685   2565   2475    -20     54      5       C  
ATOM   2229  NE1 TRP B  47     -47.465  36.421  47.108  1.00 23.07           N  
ANISOU 2229  NE1 TRP B  47     3032   2914   2820     -7     43     25       N  
ATOM   2230  CE2 TRP B  47     -46.373  37.231  47.273  1.00 20.75           C  
ANISOU 2230  CE2 TRP B  47     2736   2623   2525    -16     51     10       C  
ATOM   2231  CE3 TRP B  47     -44.341  37.775  46.066  1.00 23.24           C  
ANISOU 2231  CE3 TRP B  47     3051   2940   2841    -33     64    -14       C  
ATOM   2232  CZ2 TRP B  47     -46.042  38.109  48.317  1.00 19.62           C  
ANISOU 2232  CZ2 TRP B  47     2588   2489   2376    -22     57     -2       C  
ATOM   2233  CZ3 TRP B  47     -44.015  38.652  47.092  1.00 20.49           C  
ANISOU 2233  CZ3 TRP B  47     2699   2598   2488    -39     70    -24       C  
ATOM   2234  CH2 TRP B  47     -44.859  38.819  48.200  1.00 19.94           C  
ANISOU 2234  CH2 TRP B  47     2628   2533   2417    -33     66    -18       C  
ATOM   2235  N   MET B  48     -47.251  38.229  42.822  1.00 19.18           N  
ANISOU 2235  N   MET B  48     2585   2370   2334    -22     64     23       N  
ATOM   2236  CA  MET B  48     -47.181  39.661  42.626  1.00 21.04           C  
ANISOU 2236  CA  MET B  48     2839   2591   2565    -32     72     16       C  
ATOM   2237  C   MET B  48     -46.914  40.440  43.891  1.00 20.80           C  
ANISOU 2237  C   MET B  48     2803   2567   2532    -35     76      6       C  
ATOM   2238  O   MET B  48     -46.187  41.455  43.875  1.00 22.74           O  
ANISOU 2238  O   MET B  48     3060   2808   2774    -51     86     -5       O  
ATOM   2239  CB  MET B  48     -48.459  40.140  41.953  1.00 21.79           C  
ANISOU 2239  CB  MET B  48     2953   2665   2661    -21     66     27       C  
ATOM   2240  CG  MET B  48     -48.677  39.445  40.617  1.00 23.50           C  
ANISOU 2240  CG  MET B  48     3176   2875   2878    -20     63     37       C  
ATOM   2241  SD  MET B  48     -50.129  40.037  39.718  1.00 26.60           S  
ANISOU 2241  SD  MET B  48     3593   3243   3272     -7     53     48       S  
ATOM   2242  CE  MET B  48     -49.547  41.696  39.313  1.00 29.21           C  
ANISOU 2242  CE  MET B  48     3956   3549   3594    -25     58     42       C  
ATOM   2243  N   GLY B  49     -47.554  40.032  44.967  1.00 20.02           N  
ANISOU 2243  N   GLY B  49     2690   2479   2436    -23     70      8       N  
ATOM   2244  CA  GLY B  49     -47.379  40.628  46.260  1.00 18.85           C  
ANISOU 2244  CA  GLY B  49     2534   2341   2285    -25     74     -2       C  
ATOM   2245  C   GLY B  49     -48.573  40.320  47.141  1.00 18.99           C  
ANISOU 2245  C   GLY B  49     2543   2369   2305    -13     67      2       C  
ATOM   2246  O   GLY B  49     -49.392  39.442  46.813  1.00 18.03           O  
ANISOU 2246  O   GLY B  49     2418   2248   2184     -4     60     14       O  
ATOM   2247  N   GLY B  50     -48.673  41.027  48.269  1.00 19.02           N  
ANISOU 2247  N   GLY B  50     2541   2381   2306    -14     70     -9       N  
ATOM   2248  CA  GLY B  50     -49.803  40.840  49.154  1.00 19.57           C  
ANISOU 2248  CA  GLY B  50     2599   2463   2374     -6     66     -9       C  
ATOM   2249  C   GLY B  50     -49.834  41.871  50.261  1.00 18.86           C  
ANISOU 2249  C   GLY B  50     2503   2381   2281     -9     71    -26       C  
ATOM   2250  O   GLY B  50     -48.989  42.781  50.294  1.00 19.99           O  
ANISOU 2250  O   GLY B  50     2653   2516   2424    -17     77    -37       O  
ATOM   2251  N   ILE B  51     -50.813  41.742  51.145  1.00 20.31           N  
ANISOU 2251  N   ILE B  51     2674   2581   2461     -5     69    -31       N  
ATOM   2252  CA  ILE B  51     -50.974  42.682  52.254  1.00 20.90           C  
ANISOU 2252  CA  ILE B  51     2740   2667   2533     -7     73    -50       C  
ATOM   2253  C   ILE B  51     -51.850  42.068  53.312  1.00 20.63           C  
ANISOU 2253  C   ILE B  51     2687   2661   2489     -9     72    -53       C  
ATOM   2254  O   ILE B  51     -52.718  41.238  53.020  1.00 19.79           O  
ANISOU 2254  O   ILE B  51     2577   2560   2381     -6     67    -44       O  
ATOM   2255  CB  ILE B  51     -51.593  44.026  51.755  1.00 22.23           C  
ANISOU 2255  CB  ILE B  51     2922   2813   2712      5     72    -65       C  
ATOM   2256  CG1 ILE B  51     -51.505  45.129  52.814  1.00 23.51           C  
ANISOU 2256  CG1 ILE B  51     3077   2982   2874      3     77    -88       C  
ATOM   2257  CG2 ILE B  51     -53.038  43.821  51.314  1.00 22.44           C  
ANISOU 2257  CG2 ILE B  51     2946   2838   2743     21     64    -66       C  
ATOM   2258  CD1 ILE B  51     -51.887  46.518  52.264  1.00 23.89           C  
ANISOU 2258  CD1 ILE B  51     3144   3000   2933     15     72   -102       C  
ATOM   2259  N   ILE B  52     -51.610  42.452  54.571  1.00 21.94           N  
ANISOU 2259  N   ILE B  52     2841   2848   2648    -18     77    -66       N  
ATOM   2260  CA  ILE B  52     -52.562  42.137  55.616  1.00 23.37           C  
ANISOU 2260  CA  ILE B  52     3004   3058   2817    -24     78    -75       C  
ATOM   2261  C   ILE B  52     -53.549  43.296  55.683  1.00 25.06           C  
ANISOU 2261  C   ILE B  52     3212   3269   3039    -12     79   -100       C  
ATOM   2262  O   ILE B  52     -53.139  44.422  55.972  1.00 26.14           O  
ANISOU 2262  O   ILE B  52     3352   3399   3182     -9     83   -117       O  
ATOM   2263  CB  ILE B  52     -51.868  41.955  56.955  1.00 22.91           C  
ANISOU 2263  CB  ILE B  52     2936   3025   2745    -40     81    -78       C  
ATOM   2264  CG1 ILE B  52     -50.942  40.725  56.914  1.00 22.68           C  
ANISOU 2264  CG1 ILE B  52     2912   2996   2707    -49     74    -54       C  
ATOM   2265  CG2 ILE B  52     -52.917  41.840  58.055  1.00 23.56           C  
ANISOU 2265  CG2 ILE B  52     2999   3139   2812    -50     84    -90       C  
ATOM   2266  CD1 ILE B  52     -50.065  40.604  58.155  1.00 24.92           C  
ANISOU 2266  CD1 ILE B  52     3189   3301   2977    -62     73    -57       C  
ATOM   2267  N   PRO B  52A    -54.829  43.053  55.335  1.00 27.09           N  
ANISOU 2267  N   PRO B  52A    3462   3531   3298     -3     75   -105       N  
ATOM   2268  CA  PRO B  52A    -55.773  44.194  55.212  1.00 29.09           C  
ANISOU 2268  CA  PRO B  52A    3712   3779   3563     15     72   -133       C  
ATOM   2269  C   PRO B  52A    -56.011  45.008  56.489  1.00 32.03           C  
ANISOU 2269  C   PRO B  52A    4064   4175   3930     11     78   -163       C  
ATOM   2270  O   PRO B  52A    -56.058  46.247  56.431  1.00 32.36           O  
ANISOU 2270  O   PRO B  52A    4111   4200   3985     26     74   -184       O  
ATOM   2271  CB  PRO B  52A    -57.066  43.533  54.750  1.00 28.78           C  
ANISOU 2271  CB  PRO B  52A    3663   3750   3523     22     67   -133       C  
ATOM   2272  CG  PRO B  52A    -56.595  42.298  54.012  1.00 28.14           C  
ANISOU 2272  CG  PRO B  52A    3595   3660   3438     14     66   -100       C  
ATOM   2273  CD  PRO B  52A    -55.408  41.807  54.800  1.00 26.88           C  
ANISOU 2273  CD  PRO B  52A    3437   3511   3267     -6     71    -86       C  
ATOM   2274  N   ILE B  53     -56.146  44.330  57.623  1.00 34.84           N  
ANISOU 2274  N   ILE B  53     4401   4569   4268     -9     85   -164       N  
ATOM   2275  CA  ILE B  53     -56.331  45.018  58.916  1.00 38.36           C  
ANISOU 2275  CA  ILE B  53     4826   5042   4705    -17     92   -194       C  
ATOM   2276  C   ILE B  53     -55.048  45.748  59.414  1.00 39.98           C  
ANISOU 2276  C   ILE B  53     5039   5238   4912    -22     96   -195       C  
ATOM   2277  O   ILE B  53     -55.150  46.745  60.136  1.00 41.59           O  
ANISOU 2277  O   ILE B  53     5232   5452   5120    -19     99   -224       O  
ATOM   2278  CB  ILE B  53     -56.942  44.041  59.978  1.00 38.69           C  
ANISOU 2278  CB  ILE B  53     4846   5130   4722    -42     98   -195       C  
ATOM   2279  CG1 ILE B  53     -58.407  43.734  59.628  1.00 38.52           C  
ANISOU 2279  CG1 ILE B  53     4810   5124   4700    -36     96   -209       C  
ATOM   2280  CG2 ILE B  53     -56.836  44.595  61.411  1.00 38.82           C  
ANISOU 2280  CG2 ILE B  53     4844   5180   4726    -57    107   -220       C  
ATOM   2281  CD1 ILE B  53     -59.033  42.567  60.379  1.00 37.98           C  
ANISOU 2281  CD1 ILE B  53     4728   5097   4606    -66    103   -204       C  
ATOM   2282  N   PHE B  54     -53.870  45.278  58.995  1.00 41.26           N  
ANISOU 2282  N   PHE B  54     5220   5383   5075    -28     95   -168       N  
ATOM   2283  CA  PHE B  54     -52.535  45.756  59.460  1.00 42.50           C  
ANISOU 2283  CA  PHE B  54     5382   5536   5231    -37    100   -168       C  
ATOM   2284  C   PHE B  54     -51.671  46.237  58.280  1.00 42.27           C  
ANISOU 2284  C   PHE B  54     5377   5466   5216    -28     98   -157       C  
ATOM   2285  O   PHE B  54     -50.490  45.874  58.137  1.00 42.22           O  
ANISOU 2285  O   PHE B  54     5379   5455   5207    -37    100   -143       O  
ATOM   2286  CB  PHE B  54     -51.854  44.609  60.255  1.00 43.18           C  
ANISOU 2286  CB  PHE B  54     5463   5648   5297    -58    101   -149       C  
ATOM   2287  CG  PHE B  54     -50.389  44.834  60.596  1.00 45.40           C  
ANISOU 2287  CG  PHE B  54     5748   5925   5576    -65    104   -146       C  
ATOM   2288  CD1 PHE B  54     -49.467  43.798  60.410  1.00 46.46           C  
ANISOU 2288  CD1 PHE B  54     5891   6058   5704    -71     98   -122       C  
ATOM   2289  CD2 PHE B  54     -49.938  46.048  61.130  1.00 48.22           C  
ANISOU 2289  CD2 PHE B  54     6101   6282   5937    -66    111   -170       C  
ATOM   2290  CE1 PHE B  54     -48.108  43.969  60.718  1.00 48.52           C  
ANISOU 2290  CE1 PHE B  54     6153   6320   5963    -77     99   -124       C  
ATOM   2291  CE2 PHE B  54     -48.576  46.235  61.441  1.00 49.76           C  
ANISOU 2291  CE2 PHE B  54     6299   6477   6130    -74    113   -170       C  
ATOM   2292  CZ  PHE B  54     -47.657  45.187  61.235  1.00 49.43           C  
ANISOU 2292  CZ  PHE B  54     6262   6436   6081    -80    108   -147       C  
ATOM   2293  N   GLY B  55     -52.281  47.001  57.391  1.00 41.77           N  
ANISOU 2293  N   GLY B  55     5327   5376   5169    -10     92   -166       N  
ATOM   2294  CA  GLY B  55     -51.779  47.097  56.014  1.00 40.67           C  
ANISOU 2294  CA  GLY B  55     5213   5200   5040     -4     88   -149       C  
ATOM   2295  C   GLY B  55     -50.524  47.824  55.568  1.00 39.51           C  
ANISOU 2295  C   GLY B  55     5086   5028   4898    -12     92   -147       C  
ATOM   2296  O   GLY B  55     -50.586  49.020  55.260  1.00 41.41           O  
ANISOU 2296  O   GLY B  55     5343   5243   5147     -5     90   -161       O  
ATOM   2297  N   THR B  56     -49.491  47.112  55.478  1.00 38.53           N  
ANISOU 2297  N   THR B  56     4963   4911   4767    -25     97   -132       N  
ATOM   2298  CA  THR B  56     -48.348  47.516  54.604  1.00 36.47           C  
ANISOU 2298  CA  THR B  56     4723   4626   4509    -34    101   -126       C  
ATOM   2299  C   THR B  56     -48.039  46.494  53.489  1.00 33.90           C  
ANISOU 2299  C   THR B  56     4405   4292   4183    -35     98   -103       C  
ATOM   2300  O   THR B  56     -47.633  45.362  53.766  1.00 32.42           O  
ANISOU 2300  O   THR B  56     4204   4126   3989    -39     97    -92       O  
ATOM   2301  CB  THR B  56     -47.017  47.835  55.357  1.00 36.64           C  
ANISOU 2301  CB  THR B  56     4737   4661   4524    -52    111   -136       C  
ATOM   2302  OG1 THR B  56     -47.270  48.642  56.518  1.00 40.52           O  
ANISOU 2302  OG1 THR B  56     5217   5165   5014    -52    114   -158       O  
ATOM   2303  CG2 THR B  56     -46.059  48.589  54.434  1.00 37.54           C  
ANISOU 2303  CG2 THR B  56     4873   4748   4640    -64    116   -138       C  
ATOM   2304  N   ALA B  57     -48.176  46.915  52.233  1.00 31.84           N  
ANISOU 2304  N   ALA B  57     4168   4001   3929    -32     95    -97       N  
ATOM   2305  CA  ALA B  57     -47.996  45.982  51.111  1.00 30.33           C  
ANISOU 2305  CA  ALA B  57     3983   3802   3737    -32     92    -77       C  
ATOM   2306  C   ALA B  57     -46.576  45.447  50.930  1.00 29.02           C  
ANISOU 2306  C   ALA B  57     3814   3647   3566    -48     99    -74       C  
ATOM   2307  O   ALA B  57     -45.586  46.168  51.104  1.00 28.85           O  
ANISOU 2307  O   ALA B  57     3796   3624   3541    -63    108    -86       O  
ATOM   2308  CB  ALA B  57     -48.486  46.603  49.813  1.00 30.12           C  
ANISOU 2308  CB  ALA B  57     3985   3742   3717    -26     87    -72       C  
ATOM   2309  N   ASN B  58     -46.501  44.167  50.577  1.00 27.40           N  
ANISOU 2309  N   ASN B  58     3600   3452   3359    -45     95    -60       N  
ATOM   2310  CA  ASN B  58     -45.285  43.505  50.141  1.00 26.74           C  
ANISOU 2310  CA  ASN B  58     3511   3377   3272    -55     97    -58       C  
ATOM   2311  C   ASN B  58     -45.359  43.211  48.634  1.00 27.11           C  
ANISOU 2311  C   ASN B  58     3574   3405   3322    -56     96    -47       C  
ATOM   2312  O   ASN B  58     -46.423  42.834  48.138  1.00 26.59           O  
ANISOU 2312  O   ASN B  58     3514   3329   3260    -43     89    -34       O  
ATOM   2313  CB  ASN B  58     -45.085  42.224  50.981  1.00 26.87           C  
ANISOU 2313  CB  ASN B  58     3506   3419   3285    -50     89    -53       C  
ATOM   2314  CG  ASN B  58     -45.203  42.493  52.502  1.00 26.84           C  
ANISOU 2314  CG  ASN B  58     3488   3434   3274    -51     89    -62       C  
ATOM   2315  OD1 ASN B  58     -46.137  42.034  53.169  1.00 23.06           O  
ANISOU 2315  OD1 ASN B  58     3004   2966   2794    -44     83    -55       O  
ATOM   2316  ND2 ASN B  58     -44.264  43.271  53.034  1.00 29.42           N  
ANISOU 2316  ND2 ASN B  58     3811   3768   3598    -62     98    -79       N  
ATOM   2317  N   TYR B  59     -44.252  43.420  47.909  1.00 26.09           N  
ANISOU 2317  N   TYR B  59     3450   3273   3189    -72    104    -54       N  
ATOM   2318  CA  TYR B  59     -44.244  43.268  46.439  1.00 26.53           C  
ANISOU 2318  CA  TYR B  59     3522   3313   3245    -77    105    -46       C  
ATOM   2319  C   TYR B  59     -43.190  42.320  45.922  1.00 27.54           C  
ANISOU 2319  C   TYR B  59     3637   3458   3371    -85    107    -50       C  
ATOM   2320  O   TYR B  59     -42.126  42.200  46.520  1.00 28.38           O  
ANISOU 2320  O   TYR B  59     3725   3584   3474    -93    111    -66       O  
ATOM   2321  CB  TYR B  59     -44.048  44.623  45.742  1.00 25.17           C  
ANISOU 2321  CB  TYR B  59     3378   3116   3068    -95    113    -51       C  
ATOM   2322  CG  TYR B  59     -45.128  45.601  46.052  1.00 24.79           C  
ANISOU 2322  CG  TYR B  59     3348   3046   3024    -84    107    -48       C  
ATOM   2323  CD1 TYR B  59     -46.406  45.427  45.541  1.00 22.87           C  
ANISOU 2323  CD1 TYR B  59     3115   2787   2786    -65     95    -35       C  
ATOM   2324  CD2 TYR B  59     -44.895  46.683  46.907  1.00 25.74           C  
ANISOU 2324  CD2 TYR B  59     3473   3164   3144    -91    112    -63       C  
ATOM   2325  CE1 TYR B  59     -47.411  46.322  45.829  1.00 23.25           C  
ANISOU 2325  CE1 TYR B  59     3177   2817   2840    -51     87    -37       C  
ATOM   2326  CE2 TYR B  59     -45.906  47.603  47.216  1.00 24.06           C  
ANISOU 2326  CE2 TYR B  59     3275   2930   2936    -78    104    -65       C  
ATOM   2327  CZ  TYR B  59     -47.169  47.417  46.656  1.00 21.99           C  
ANISOU 2327  CZ  TYR B  59     3022   2653   2681    -57     91    -53       C  
ATOM   2328  OH  TYR B  59     -48.201  48.290  46.925  1.00 24.79           O  
ANISOU 2328  OH  TYR B  59     3388   2988   3042    -40     80    -59       O  
ATOM   2329  N   ALA B  60     -43.478  41.647  44.809  1.00 28.66           N  
ANISOU 2329  N   ALA B  60     3783   3592   3514    -81    103    -39       N  
ATOM   2330  CA  ALA B  60     -42.452  40.906  44.092  1.00 29.99           C  
ANISOU 2330  CA  ALA B  60     3940   3774   3681    -91    106    -49       C  
ATOM   2331  C   ALA B  60     -41.577  41.897  43.333  1.00 31.47           C  
ANISOU 2331  C   ALA B  60     4142   3958   3858   -120    121    -63       C  
ATOM   2332  O   ALA B  60     -42.064  42.885  42.765  1.00 31.00           O  
ANISOU 2332  O   ALA B  60     4111   3874   3794   -130    126    -55       O  
ATOM   2333  CB  ALA B  60     -43.060  39.895  43.124  1.00 29.75           C  
ANISOU 2333  CB  ALA B  60     3912   3739   3655    -79     97    -34       C  
ATOM   2334  N   GLN B  61     -40.283  41.597  43.333  1.00 33.10           N  
ANISOU 2334  N   GLN B  61     4329   4188   4060   -133    128    -84       N  
ATOM   2335  CA  GLN B  61     -39.248  42.394  42.671  1.00 35.09           C  
ANISOU 2335  CA  GLN B  61     4588   4445   4299   -167    146   -104       C  
ATOM   2336  C   GLN B  61     -39.546  42.667  41.194  1.00 35.32           C  
ANISOU 2336  C   GLN B  61     4644   4456   4320   -185    151    -94       C  
ATOM   2337  O   GLN B  61     -39.374  43.795  40.708  1.00 35.82           O  
ANISOU 2337  O   GLN B  61     4735   4505   4371   -213    163    -95       O  
ATOM   2338  CB  GLN B  61     -37.911  41.666  42.809  1.00 35.69           C  
ANISOU 2338  CB  GLN B  61     4631   4556   4374   -173    149   -132       C  
ATOM   2339  CG  GLN B  61     -36.696  42.573  42.700  1.00 40.52           C  
ANISOU 2339  CG  GLN B  61     5240   5182   4972   -209    168   -160       C  
ATOM   2340  CD  GLN B  61     -36.714  43.662  43.757  1.00 45.06           C  
ANISOU 2340  CD  GLN B  61     5825   5750   5545   -215    173   -162       C  
ATOM   2341  OE1 GLN B  61     -37.071  44.807  43.478  1.00 46.94           O  
ANISOU 2341  OE1 GLN B  61     6096   5965   5776   -234    182   -153       O  
ATOM   2342  NE2 GLN B  61     -36.353  43.303  44.985  1.00 47.03           N  
ANISOU 2342  NE2 GLN B  61     6049   6020   5801   -198    166   -173       N  
ATOM   2343  N   LYS B  62     -40.009  41.634  40.496  1.00 35.67           N  
ANISOU 2343  N   LYS B  62     4682   4500   4370   -169    142    -83       N  
ATOM   2344  CA  LYS B  62     -40.370  41.732  39.082  1.00 37.09           C  
ANISOU 2344  CA  LYS B  62     4886   4665   4543   -182    145    -72       C  
ATOM   2345  C   LYS B  62     -41.382  42.852  38.810  1.00 38.12           C  
ANISOU 2345  C   LYS B  62     5056   4760   4668   -185    142    -51       C  
ATOM   2346  O   LYS B  62     -41.345  43.471  37.741  1.00 38.94           O  
ANISOU 2346  O   LYS B  62     5189   4848   4758   -210    149    -47       O  
ATOM   2347  CB  LYS B  62     -40.923  40.393  38.585  1.00 37.52           C  
ANISOU 2347  CB  LYS B  62     4926   4724   4607   -158    132    -62       C  
ATOM   2348  CG  LYS B  62     -41.316  40.403  37.113  1.00 37.21           C  
ANISOU 2348  CG  LYS B  62     4908   4672   4560   -170    134    -51       C  
ATOM   2349  CD  LYS B  62     -41.742  39.050  36.623  1.00 36.45           C  
ANISOU 2349  CD  LYS B  62     4795   4582   4473   -148    123    -45       C  
ATOM   2350  CE  LYS B  62     -42.142  39.152  35.162  1.00 38.32           C  
ANISOU 2350  CE  LYS B  62     5054   4806   4700   -162    126    -34       C  
ATOM   2351  NZ  LYS B  62     -42.767  37.890  34.699  1.00 37.48           N  
ANISOU 2351  NZ  LYS B  62     4934   4702   4604   -139    114    -25       N  
ATOM   2352  N   PHE B  63     -42.266  43.089  39.782  1.00 38.83           N  
ANISOU 2352  N   PHE B  63     5148   4836   4768   -161    132    -40       N  
ATOM   2353  CA  PHE B  63     -43.398  44.013  39.657  1.00 39.63           C  
ANISOU 2353  CA  PHE B  63     5282   4904   4871   -153    124    -23       C  
ATOM   2354  C   PHE B  63     -43.274  45.270  40.507  1.00 40.90           C  
ANISOU 2354  C   PHE B  63     5458   5053   5030   -161    127    -30       C  
ATOM   2355  O   PHE B  63     -44.145  46.150  40.443  1.00 42.02           O  
ANISOU 2355  O   PHE B  63     5628   5165   5172   -154    118    -20       O  
ATOM   2356  CB  PHE B  63     -44.692  43.320  40.061  1.00 39.14           C  
ANISOU 2356  CB  PHE B  63     5210   4838   4823   -116    108     -8       C  
ATOM   2357  CG  PHE B  63     -45.084  42.201  39.165  1.00 37.42           C  
ANISOU 2357  CG  PHE B  63     4985   4625   4608   -106    102      3       C  
ATOM   2358  CD1 PHE B  63     -45.570  42.447  37.885  1.00 37.46           C  
ANISOU 2358  CD1 PHE B  63     5017   4609   4606   -112     98     15       C  
ATOM   2359  CD2 PHE B  63     -44.964  40.891  39.602  1.00 35.97           C  
ANISOU 2359  CD2 PHE B  63     4769   4464   4433    -91     98      1       C  
ATOM   2360  CE1 PHE B  63     -45.935  41.395  37.056  1.00 37.28           C  
ANISOU 2360  CE1 PHE B  63     4986   4593   4586   -103     93     23       C  
ATOM   2361  CE2 PHE B  63     -45.322  39.837  38.782  1.00 34.88           C  
ANISOU 2361  CE2 PHE B  63     4625   4329   4299    -81     91     10       C  
ATOM   2362  CZ  PHE B  63     -45.811  40.087  37.510  1.00 37.23           C  
ANISOU 2362  CZ  PHE B  63     4946   4609   4590    -87     90     20       C  
ATOM   2363  N   GLN B  64     -42.224  45.344  41.324  1.00 41.52           N  
ANISOU 2363  N   GLN B  64     5515   5155   5106   -174    138    -50       N  
ATOM   2364  CA  GLN B  64     -41.860  46.577  42.013  1.00 41.73           C  
ANISOU 2364  CA  GLN B  64     5556   5172   5129   -189    145    -61       C  
ATOM   2365  C   GLN B  64     -41.978  47.772  41.059  1.00 40.89           C  
ANISOU 2365  C   GLN B  64     5496   5032   5009   -214    147    -54       C  
ATOM   2366  O   GLN B  64     -41.470  47.749  39.931  1.00 41.80           O  
ANISOU 2366  O   GLN B  64     5626   5145   5110   -241    154    -53       O  
ATOM   2367  CB  GLN B  64     -40.425  46.496  42.555  1.00 42.18           C  
ANISOU 2367  CB  GLN B  64     5587   5261   5179   -211    161    -86       C  
ATOM   2368  CG  GLN B  64     -40.277  45.755  43.878  1.00 44.65           C  
ANISOU 2368  CG  GLN B  64     5862   5601   5503   -188    156    -95       C  
ATOM   2369  CD  GLN B  64     -40.715  46.563  45.085  1.00 45.30           C  
ANISOU 2369  CD  GLN B  64     5947   5675   5590   -178    153    -97       C  
ATOM   2370  OE1 GLN B  64     -40.831  46.024  46.189  1.00 47.92           O  
ANISOU 2370  OE1 GLN B  64     6253   6026   5929   -159    147    -99       O  
ATOM   2371  NE2 GLN B  64     -40.953  47.859  44.890  1.00 46.66           N  
ANISOU 2371  NE2 GLN B  64     6153   5820   5758   -193    156    -96       N  
ATOM   2372  N   GLY B  65     -42.659  48.809  41.520  1.00 40.06           N  
ANISOU 2372  N   GLY B  65     5415   4897   4907   -206    138    -50       N  
ATOM   2373  CA  GLY B  65     -42.958  49.945  40.661  1.00 38.42           C  
ANISOU 2373  CA  GLY B  65     5258   4650   4689   -223    132    -41       C  
ATOM   2374  C   GLY B  65     -44.382  49.806  40.172  1.00 36.63           C  
ANISOU 2374  C   GLY B  65     5048   4398   4472   -191    110    -21       C  
ATOM   2375  O   GLY B  65     -45.287  50.453  40.720  1.00 37.95           O  
ANISOU 2375  O   GLY B  65     5227   4544   4650   -167     95    -20       O  
ATOM   2376  N   ARG B  66     -44.596  48.938  39.178  1.00 34.08           N  
ANISOU 2376  N   ARG B  66     4723   4081   4146   -188    108     -9       N  
ATOM   2377  CA  ARG B  66     -45.876  48.930  38.447  1.00 31.41           C  
ANISOU 2377  CA  ARG B  66     4407   3715   3812   -164     87     10       C  
ATOM   2378  C   ARG B  66     -47.108  48.398  39.183  1.00 29.47           C  
ANISOU 2378  C   ARG B  66     4136   3475   3586   -119     72     12       C  
ATOM   2379  O   ARG B  66     -48.214  48.635  38.740  1.00 28.62           O  
ANISOU 2379  O   ARG B  66     4048   3343   3483    -97     54     22       O  
ATOM   2380  CB  ARG B  66     -45.751  48.203  37.122  1.00 31.92           C  
ANISOU 2380  CB  ARG B  66     4478   3785   3866   -176     90     21       C  
ATOM   2381  CG  ARG B  66     -44.717  48.784  36.216  1.00 30.86           C  
ANISOU 2381  CG  ARG B  66     4373   3643   3708   -224    103     19       C  
ATOM   2382  CD  ARG B  66     -44.914  48.254  34.825  1.00 30.08           C  
ANISOU 2382  CD  ARG B  66     4289   3541   3597   -232    100     33       C  
ATOM   2383  NE  ARG B  66     -44.731  46.801  34.744  1.00 26.24           N  
ANISOU 2383  NE  ARG B  66     3757   3093   3120   -220    108     28       N  
ATOM   2384  CZ  ARG B  66     -45.624  45.947  34.247  1.00 23.48           C  
ANISOU 2384  CZ  ARG B  66     3399   2744   2779   -194     96     41       C  
ATOM   2385  NH1 ARG B  66     -46.782  46.370  33.743  1.00 25.14           N  
ANISOU 2385  NH1 ARG B  66     3640   2923   2990   -175     75     58       N  
ATOM   2386  NH2 ARG B  66     -45.339  44.657  34.191  1.00 25.31           N  
ANISOU 2386  NH2 ARG B  66     3592   3008   3018   -186    103     35       N  
ATOM   2387  N   VAL B  67     -46.917  47.729  40.315  1.00 27.34           N  
ANISOU 2387  N   VAL B  67     3825   3236   3326   -107     80      2       N  
ATOM   2388  CA  VAL B  67     -48.059  47.177  41.080  1.00 26.10           C  
ANISOU 2388  CA  VAL B  67     3643   3089   3184    -71     68      3       C  
ATOM   2389  C   VAL B  67     -48.306  47.952  42.352  1.00 25.36           C  
ANISOU 2389  C   VAL B  67     3542   2994   3098    -60     66    -11       C  
ATOM   2390  O   VAL B  67     -47.379  48.222  43.083  1.00 24.17           O  
ANISOU 2390  O   VAL B  67     3382   2857   2945    -77     79    -23       O  
ATOM   2391  CB  VAL B  67     -47.786  45.701  41.490  1.00 26.08           C  
ANISOU 2391  CB  VAL B  67     3600   3124   3187    -65     76      3       C  
ATOM   2392  CG1 VAL B  67     -48.887  45.156  42.436  1.00 25.01           C  
ANISOU 2392  CG1 VAL B  67     3439   3002   3063    -35     67      3       C  
ATOM   2393  CG2 VAL B  67     -47.693  44.830  40.272  1.00 28.30           C  
ANISOU 2393  CG2 VAL B  67     3882   3407   3463    -70     76     15       C  
ATOM   2394  N   THR B  68     -49.568  48.228  42.639  1.00 24.28           N  
ANISOU 2394  N   THR B  68     3407   2846   2971    -32     50    -13       N  
ATOM   2395  CA  THR B  68     -49.968  48.757  43.940  1.00 24.37           C  
ANISOU 2395  CA  THR B  68     3404   2865   2992    -18     47    -30       C  
ATOM   2396  C   THR B  68     -51.047  47.860  44.546  1.00 23.02           C  
ANISOU 2396  C   THR B  68     3199   2719   2829      9     41    -32       C  
ATOM   2397  O   THR B  68     -52.058  47.584  43.900  1.00 23.37           O  
ANISOU 2397  O   THR B  68     3248   2755   2878     28     28    -25       O  
ATOM   2398  CB  THR B  68     -50.543  50.189  43.813  1.00 25.18           C  
ANISOU 2398  CB  THR B  68     3541   2930   3099     -8     31    -38       C  
ATOM   2399  OG1 THR B  68     -49.561  51.019  43.196  1.00 28.43           O  
ANISOU 2399  OG1 THR B  68     3988   3316   3498    -37     36    -35       O  
ATOM   2400  CG2 THR B  68     -50.888  50.751  45.189  1.00 26.29           C  
ANISOU 2400  CG2 THR B  68     3662   3080   3248      6     30    -60       C  
ATOM   2401  N   ILE B  69     -50.842  47.430  45.792  1.00 22.00           N  
ANISOU 2401  N   ILE B  69     3038   2620   2701      8     51    -41       N  
ATOM   2402  CA  ILE B  69     -51.795  46.526  46.450  1.00 21.70           C  
ANISOU 2402  CA  ILE B  69     2969   2609   2667     25     48    -43       C  
ATOM   2403  C   ILE B  69     -52.351  47.244  47.688  1.00 22.15           C  
ANISOU 2403  C   ILE B  69     3011   2675   2728     36     45    -65       C  
ATOM   2404  O   ILE B  69     -51.574  47.771  48.509  1.00 23.10           O  
ANISOU 2404  O   ILE B  69     3128   2802   2846     23     54    -76       O  
ATOM   2405  CB  ILE B  69     -51.109  45.160  46.813  1.00 20.76           C  
ANISOU 2405  CB  ILE B  69     2825   2520   2542     13     58    -33       C  
ATOM   2406  CG1 ILE B  69     -50.789  44.359  45.542  1.00 20.98           C  
ANISOU 2406  CG1 ILE B  69     2863   2541   2568      8     58    -15       C  
ATOM   2407  CG2 ILE B  69     -51.990  44.307  47.774  1.00 21.59           C  
ANISOU 2407  CG2 ILE B  69     2901   2655   2647     23     56    -35       C  
ATOM   2408  CD1 ILE B  69     -49.870  43.186  45.762  1.00 20.27           C  
ANISOU 2408  CD1 ILE B  69     2754   2474   2473     -4     66     -8       C  
ATOM   2409  N   THR B  70     -53.676  47.294  47.788  1.00 21.69           N  
ANISOU 2409  N   THR B  70     2945   2620   2677     58     33    -75       N  
ATOM   2410  CA  THR B  70     -54.371  47.949  48.890  1.00 22.13           C  
ANISOU 2410  CA  THR B  70     2984   2688   2737     71     30   -100       C  
ATOM   2411  C   THR B  70     -55.471  47.040  49.395  1.00 22.71           C  
ANISOU 2411  C   THR B  70     3026   2793   2809     81     29   -106       C  
ATOM   2412  O   THR B  70     -55.782  46.026  48.756  1.00 22.97           O  
ANISOU 2412  O   THR B  70     3056   2833   2840     81     28    -90       O  
ATOM   2413  CB  THR B  70     -54.948  49.340  48.484  1.00 22.66           C  
ANISOU 2413  CB  THR B  70     3076   2719   2814     90     12   -117       C  
ATOM   2414  OG1 THR B  70     -55.817  49.191  47.343  1.00 23.09           O  
ANISOU 2414  OG1 THR B  70     3146   2755   2874    109     -4   -109       O  
ATOM   2415  CG2 THR B  70     -53.806  50.314  48.145  1.00 22.82           C  
ANISOU 2415  CG2 THR B  70     3130   2707   2832     73     15   -112       C  
ATOM   2416  N   ALA B  71     -56.032  47.345  50.563  1.00 23.27           N  
ANISOU 2416  N   ALA B  71     3072   2888   2880     85     30   -131       N  
ATOM   2417  CA  ALA B  71     -57.171  46.589  51.047  1.00 24.38           C  
ANISOU 2417  CA  ALA B  71     3184   3063   3018     91     30   -141       C  
ATOM   2418  C   ALA B  71     -57.926  47.357  52.105  1.00 25.53           C  
ANISOU 2418  C   ALA B  71     3307   3227   3165    101     28   -176       C  
ATOM   2419  O   ALA B  71     -57.305  48.010  52.940  1.00 27.91           O  
ANISOU 2419  O   ALA B  71     3608   3532   3466     93     34   -188       O  
ATOM   2420  CB  ALA B  71     -56.718  45.236  51.628  1.00 24.32           C  
ANISOU 2420  CB  ALA B  71     3159   3086   2995     68     44   -122       C  
ATOM   2421  N   ASP B  72     -59.246  47.250  52.052  1.00 25.48           N  
ANISOU 2421  N   ASP B  72     3284   3235   3162    118     19   -196       N  
ATOM   2422  CA  ASP B  72     -60.141  47.904  53.008  1.00 26.09           C  
ANISOU 2422  CA  ASP B  72     3334   3337   3242    130     16   -237       C  
ATOM   2423  C   ASP B  72     -60.923  46.846  53.789  1.00 25.75           C  
ANISOU 2423  C   ASP B  72     3254   3345   3184    115     28   -245       C  
ATOM   2424  O   ASP B  72     -61.862  46.237  53.260  1.00 25.07           O  
ANISOU 2424  O   ASP B  72     3159   3269   3097    122     23   -247       O  
ATOM   2425  CB  ASP B  72     -61.112  48.796  52.244  1.00 27.58           C  
ANISOU 2425  CB  ASP B  72     3531   3500   3447    165     -7   -260       C  
ATOM   2426  CG  ASP B  72     -61.945  49.671  53.172  1.00 31.75           C  
ANISOU 2426  CG  ASP B  72     4033   4049   3982    182    -14   -309       C  
ATOM   2427  OD1 ASP B  72     -63.185  49.567  53.139  1.00 38.07           O  
ANISOU 2427  OD1 ASP B  72     4809   4870   4786    200    -23   -336       O  
ATOM   2428  OD2 ASP B  72     -61.356  50.457  53.944  1.00 38.23           O  
ANISOU 2428  OD2 ASP B  72     4854   4866   4804    177    -10   -321       O  
ATOM   2429  N   GLU B  73     -60.567  46.668  55.062  1.00 26.01           N  
ANISOU 2429  N   GLU B  73     3269   3411   3204     91     43   -252       N  
ATOM   2430  CA  GLU B  73     -61.320  45.745  55.921  1.00 25.84           C  
ANISOU 2430  CA  GLU B  73     3215   3439   3164     71     54   -262       C  
ATOM   2431  C   GLU B  73     -62.814  46.098  55.997  1.00 26.21           C  
ANISOU 2431  C   GLU B  73     3234   3509   3215     90     46   -304       C  
ATOM   2432  O   GLU B  73     -63.657  45.219  56.026  1.00 26.12           O  
ANISOU 2432  O   GLU B  73     3203   3529   3192     79     51   -308       O  
ATOM   2433  CB  GLU B  73     -60.650  45.636  57.300  1.00 26.15           C  
ANISOU 2433  CB  GLU B  73     3242   3507   3186     43     69   -264       C  
ATOM   2434  CG  GLU B  73     -61.512  45.118  58.434  1.00 25.03           C  
ANISOU 2434  CG  GLU B  73     3067   3421   3024     21     80   -287       C  
ATOM   2435  CD  GLU B  73     -61.890  43.643  58.314  1.00 27.46           C  
ANISOU 2435  CD  GLU B  73     3371   3750   3313     -3     86   -262       C  
ATOM   2436  OE1 GLU B  73     -61.303  42.914  57.451  1.00 26.78           O  
ANISOU 2436  OE1 GLU B  73     3310   3635   3229     -3     82   -224       O  
ATOM   2437  OE2 GLU B  73     -62.794  43.240  59.103  1.00 26.07           O  
ANISOU 2437  OE2 GLU B  73     3168   3619   3119    -23     94   -284       O  
ATOM   2438  N   SER B  74     -63.156  47.381  56.017  1.00 25.67           N  
ANISOU 2438  N   SER B  74     3162   3427   3163    117     34   -339       N  
ATOM   2439  CA  SER B  74     -64.557  47.749  56.228  1.00 26.51           C  
ANISOU 2439  CA  SER B  74     3236   3562   3274    136     25   -387       C  
ATOM   2440  C   SER B  74     -65.483  47.234  55.113  1.00 26.47           C  
ANISOU 2440  C   SER B  74     3231   3551   3275    154     13   -385       C  
ATOM   2441  O   SER B  74     -66.623  46.819  55.385  1.00 27.71           O  
ANISOU 2441  O   SER B  74     3355   3750   3425    152     16   -414       O  
ATOM   2442  CB  SER B  74     -64.674  49.264  56.384  1.00 26.23           C  
ANISOU 2442  CB  SER B  74     3202   3505   3258    168      9   -425       C  
ATOM   2443  OG  SER B  74     -64.054  49.897  55.276  1.00 28.18           O  
ANISOU 2443  OG  SER B  74     3492   3692   3523    190     -9   -402       O  
ATOM   2444  N   THR B  75     -64.995  47.239  53.865  1.00 26.79           N  
ANISOU 2444  N   THR B  75     3308   3543   3327    169      1   -352       N  
ATOM   2445  CA  THR B  75     -65.780  46.743  52.723  1.00 27.51           C  
ANISOU 2445  CA  THR B  75     3404   3626   3423    186    -11   -346       C  
ATOM   2446  C   THR B  75     -65.295  45.332  52.367  1.00 27.11           C  
ANISOU 2446  C   THR B  75     3363   3580   3358    156      4   -301       C  
ATOM   2447  O   THR B  75     -65.740  44.756  51.364  1.00 27.58           O  
ANISOU 2447  O   THR B  75     3430   3630   3420    165     -3   -287       O  
ATOM   2448  CB  THR B  75     -65.623  47.640  51.473  1.00 28.74           C  
ANISOU 2448  CB  THR B  75     3597   3724   3600    221    -37   -338       C  
ATOM   2449  OG1 THR B  75     -64.248  47.688  51.103  1.00 28.99           O  
ANISOU 2449  OG1 THR B  75     3666   3719   3631    207    -31   -297       O  
ATOM   2450  CG2 THR B  75     -66.086  49.060  51.754  1.00 28.36           C  
ANISOU 2450  CG2 THR B  75     3544   3663   3568    254    -57   -383       C  
ATOM   2451  N   SER B  76     -64.418  44.805  53.227  1.00 25.72           N  
ANISOU 2451  N   SER B  76     3186   3419   3166    123     23   -280       N  
ATOM   2452  CA ASER B  76     -63.679  43.562  52.997  0.50 25.42           C  
ANISOU 2452  CA ASER B  76     3163   3379   3116     96     34   -236       C  
ATOM   2453  CA BSER B  76     -63.736  43.525  52.998  0.50 24.73           C  
ANISOU 2453  CA BSER B  76     3075   3294   3029     96     34   -237       C  
ATOM   2454  C   SER B  76     -63.329  43.336  51.537  1.00 24.27           C  
ANISOU 2454  C   SER B  76     3049   3192   2982    110     24   -206       C  
ATOM   2455  O   SER B  76     -63.570  42.254  50.960  1.00 24.00           O  
ANISOU 2455  O   SER B  76     3015   3162   2941    101     26   -186       O  
ATOM   2456  CB ASER B  76     -64.369  42.353  53.610  0.50 25.64           C  
ANISOU 2456  CB ASER B  76     3167   3453   3123     67     47   -237       C  
ATOM   2457  CB BSER B  76     -64.532  42.304  53.515  0.50 24.71           C  
ANISOU 2457  CB BSER B  76     3047   3337   3006     69     47   -239       C  
ATOM   2458  OG ASER B  76     -64.026  42.296  54.986  0.50 28.01           O  
ANISOU 2458  OG ASER B  76     3453   3784   3406     40     61   -245       O  
ATOM   2459  OG BSER B  76     -65.817  42.146  52.925  0.50 23.16           O  
ANISOU 2459  OG BSER B  76     2834   3154   2813     84     39   -262       O  
ATOM   2460  N   THR B  77     -62.688  44.355  50.973  1.00 22.70           N  
ANISOU 2460  N   THR B  77     2875   2952   2797    129     13   -202       N  
ATOM   2461  CA  THR B  77     -62.236  44.288  49.574  1.00 21.20           C  
ANISOU 2461  CA  THR B  77     2718   2722   2616    140      3   -174       C  
ATOM   2462  C   THR B  77     -60.767  44.595  49.456  1.00 21.47           C  
ANISOU 2462  C   THR B  77     2780   2728   2651    128      8   -149       C  
ATOM   2463  O   THR B  77     -60.277  45.558  50.041  1.00 20.25           O  
ANISOU 2463  O   THR B  77     2630   2565   2500    129      9   -162       O  
ATOM   2464  CB  THR B  77     -63.067  45.220  48.677  1.00 21.44           C  
ANISOU 2464  CB  THR B  77     2758   2726   2661    176    -20   -193       C  
ATOM   2465  OG1 THR B  77     -64.461  44.951  48.861  1.00 25.05           O  
ANISOU 2465  OG1 THR B  77     3184   3215   3118    188    -25   -223       O  
ATOM   2466  CG2 THR B  77     -62.754  44.989  47.183  1.00 19.14           C  
ANISOU 2466  CG2 THR B  77     2500   2398   2375    183    -30   -163       C  
ATOM   2467  N   ALA B  78     -60.050  43.785  48.676  1.00 20.16           N  
ANISOU 2467  N   ALA B  78     2630   2548   2481    116     12   -116       N  
ATOM   2468  CA  ALA B  78     -58.646  44.049  48.400  1.00 19.41           C  
ANISOU 2468  CA  ALA B  78     2560   2428   2387    105     17    -95       C  
ATOM   2469  C   ALA B  78     -58.467  44.382  46.943  1.00 19.38           C  
ANISOU 2469  C   ALA B  78     2588   2386   2390    116      6    -81       C  
ATOM   2470  O   ALA B  78     -59.283  44.016  46.114  1.00 20.16           O  
ANISOU 2470  O   ALA B  78     2687   2480   2491    129     -3    -78       O  
ATOM   2471  CB  ALA B  78     -57.801  42.802  48.736  1.00 19.86           C  
ANISOU 2471  CB  ALA B  78     2611   2503   2433     79     31    -71       C  
ATOM   2472  N   TYR B  79     -57.376  45.076  46.645  1.00 18.32           N  
ANISOU 2472  N   TYR B  79     2478   2225   2257    108      8    -72       N  
ATOM   2473  CA  TYR B  79     -57.167  45.580  45.294  1.00 18.25           C  
ANISOU 2473  CA  TYR B  79     2504   2179   2251    114     -3    -60       C  
ATOM   2474  C   TYR B  79     -55.753  45.409  44.834  1.00 17.44           C  
ANISOU 2474  C   TYR B  79     2419   2064   2142     91      8    -39       C  
ATOM   2475  O   TYR B  79     -54.833  45.464  45.612  1.00 19.57           O  
ANISOU 2475  O   TYR B  79     2683   2346   2409     74     20    -41       O  
ATOM   2476  CB  TYR B  79     -57.504  47.078  45.215  1.00 19.32           C  
ANISOU 2476  CB  TYR B  79     2661   2285   2395    132    -20    -78       C  
ATOM   2477  CG  TYR B  79     -58.924  47.464  45.621  1.00 19.46           C  
ANISOU 2477  CG  TYR B  79     2661   2312   2422    161    -35   -107       C  
ATOM   2478  CD1 TYR B  79     -59.959  47.530  44.680  1.00 21.66           C  
ANISOU 2478  CD1 TYR B  79     2947   2576   2705    186    -55   -110       C  
ATOM   2479  CD2 TYR B  79     -59.229  47.709  46.950  1.00 19.41           C  
ANISOU 2479  CD2 TYR B  79     2625   2332   2416    162    -29   -132       C  
ATOM   2480  CE1 TYR B  79     -61.239  47.850  45.055  1.00 22.96           C  
ANISOU 2480  CE1 TYR B  79     3091   2753   2878    213    -70   -142       C  
ATOM   2481  CE2 TYR B  79     -60.528  48.050  47.347  1.00 23.84           C  
ANISOU 2481  CE2 TYR B  79     3166   2908   2985    187    -42   -165       C  
ATOM   2482  CZ  TYR B  79     -61.512  48.119  46.395  1.00 22.88           C  
ANISOU 2482  CZ  TYR B  79     3051   2772   2870    213    -62   -170       C  
ATOM   2483  OH  TYR B  79     -62.788  48.450  46.789  1.00 26.04           O  
ANISOU 2483  OH  TYR B  79     3426   3190   3278    240    -76   -207       O  
ATOM   2484  N   MET B  80     -55.609  45.229  43.526  1.00 16.79           N  
ANISOU 2484  N   MET B  80     2359   1960   2058     89      3    -22       N  
ATOM   2485  CA  MET B  80     -54.323  45.181  42.877  1.00 18.10           C  
ANISOU 2485  CA  MET B  80     2545   2115   2218     66     12     -6       C  
ATOM   2486  C   MET B  80     -54.431  46.046  41.640  1.00 19.67           C  
ANISOU 2486  C   MET B  80     2783   2275   2414     69     -1      0       C  
ATOM   2487  O   MET B  80     -55.265  45.780  40.741  1.00 19.72           O  
ANISOU 2487  O   MET B  80     2798   2273   2423     84    -14      7       O  
ATOM   2488  CB  MET B  80     -53.995  43.742  42.495  1.00 18.41           C  
ANISOU 2488  CB  MET B  80     2568   2174   2253     57     21      9       C  
ATOM   2489  CG  MET B  80     -52.602  43.566  41.998  1.00 19.86           C  
ANISOU 2489  CG  MET B  80     2763   2355   2430     32     33     19       C  
ATOM   2490  SD  MET B  80     -52.292  44.127  40.299  1.00 24.56           S  
ANISOU 2490  SD  MET B  80     3397   2916   3017     22     28     31       S  
ATOM   2491  CE  MET B  80     -53.447  43.169  39.332  1.00 23.52           C  
ANISOU 2491  CE  MET B  80     3261   2786   2889     41     16     42       C  
ATOM   2492  N   GLU B  81     -53.622  47.109  41.612  1.00 20.18           N  
ANISOU 2492  N   GLU B  81     2874   2317   2475     54      1     -3       N  
ATOM   2493  CA  GLU B  81     -53.516  47.967  40.440  1.00 21.57           C  
ANISOU 2493  CA  GLU B  81     3096   2455   2645     49    -11      6       C  
ATOM   2494  C   GLU B  81     -52.195  47.721  39.705  1.00 21.07           C  
ANISOU 2494  C   GLU B  81     3047   2392   2569     14      5     20       C  
ATOM   2495  O   GLU B  81     -51.142  47.768  40.312  1.00 21.83           O  
ANISOU 2495  O   GLU B  81     3133   2501   2660     -8     22     14       O  
ATOM   2496  CB  GLU B  81     -53.628  49.445  40.852  1.00 23.20           C  
ANISOU 2496  CB  GLU B  81     3328   2632   2855     54    -23     -8       C  
ATOM   2497  CG  GLU B  81     -53.633  50.394  39.638  1.00 26.87           C  
ANISOU 2497  CG  GLU B  81     3848   3051   3312     49    -41      3       C  
ATOM   2498  CD  GLU B  81     -54.224  51.756  39.910  1.00 34.36           C  
ANISOU 2498  CD  GLU B  81     4823   3963   4267     69    -65    -12       C  
ATOM   2499  OE1 GLU B  81     -54.406  52.147  41.082  1.00 35.07           O  
ANISOU 2499  OE1 GLU B  81     4892   4064   4367     81    -64    -33       O  
ATOM   2500  OE2 GLU B  81     -54.515  52.439  38.909  1.00 37.03           O  
ANISOU 2500  OE2 GLU B  81     5208   4263   4601     72    -87     -2       O  
ATOM   2501  N   LEU B  82     -52.263  47.466  38.403  1.00 21.03           N  
ANISOU 2501  N   LEU B  82     3063   2372   2555      8      0     35       N  
ATOM   2502  CA  LEU B  82     -51.085  47.196  37.575  1.00 21.29           C  
ANISOU 2502  CA  LEU B  82     3108   2407   2573    -27     15     45       C  
ATOM   2503  C   LEU B  82     -51.089  48.219  36.459  1.00 24.10           C  
ANISOU 2503  C   LEU B  82     3517   2724   2916    -40      3     55       C  
ATOM   2504  O   LEU B  82     -52.044  48.302  35.687  1.00 23.91           O  
ANISOU 2504  O   LEU B  82     3513   2680   2893    -21    -17     64       O  
ATOM   2505  CB  LEU B  82     -51.119  45.768  36.965  1.00 21.02           C  
ANISOU 2505  CB  LEU B  82     3049   2398   2538    -25     22     55       C  
ATOM   2506  CG  LEU B  82     -49.949  45.324  36.056  1.00 21.03           C  
ANISOU 2506  CG  LEU B  82     3056   2408   2525    -59     38     60       C  
ATOM   2507  CD1 LEU B  82     -48.675  45.408  36.858  1.00 21.77           C  
ANISOU 2507  CD1 LEU B  82     3134   2522   2617    -82     57     47       C  
ATOM   2508  CD2 LEU B  82     -50.120  43.880  35.513  1.00 20.85           C  
ANISOU 2508  CD2 LEU B  82     3007   2409   2506    -52     40     67       C  
ATOM   2509  N   SER B  82A    -50.017  48.984  36.388  1.00 25.14           N  
ANISOU 2509  N   SER B  82A    3673   2845   3035    -74     14     53       N  
ATOM   2510  CA  SER B  82A    -50.005  50.145  35.509  1.00 27.45           C  
ANISOU 2510  CA  SER B  82A    4023   3095   3313    -91      0     62       C  
ATOM   2511  C   SER B  82A    -49.063  49.871  34.354  1.00 27.73           C  
ANISOU 2511  C   SER B  82A    4076   3135   3326   -132     15     72       C  
ATOM   2512  O   SER B  82A    -48.289  48.908  34.388  1.00 27.82           O  
ANISOU 2512  O   SER B  82A    4052   3182   3335   -147     37     67       O  
ATOM   2513  CB  SER B  82A    -49.591  51.388  36.315  1.00 28.20           C  
ANISOU 2513  CB  SER B  82A    4138   3169   3408   -101     -1     50       C  
ATOM   2514  OG  SER B  82A    -48.260  51.270  36.791  1.00 31.48           O  
ANISOU 2514  OG  SER B  82A    4536   3611   3816   -136     27     40       O  
ATOM   2515  N   SER B  82B    -49.122  50.730  33.330  1.00 28.42           N  
ANISOU 2515  N   SER B  82B    4219   3185   3396   -151      1     85       N  
ATOM   2516  CA  SER B  82B    -48.230  50.637  32.177  1.00 28.02           C  
ANISOU 2516  CA  SER B  82B    4191   3136   3318   -197     15     94       C  
ATOM   2517  C   SER B  82B    -48.327  49.237  31.548  1.00 27.48           C  
ANISOU 2517  C   SER B  82B    4088   3102   3252   -190     24     98       C  
ATOM   2518  O   SER B  82B    -47.326  48.553  31.346  1.00 26.19           O  
ANISOU 2518  O   SER B  82B    3900   2972   3080   -218     48     90       O  
ATOM   2519  CB  SER B  82B    -46.798  51.025  32.595  1.00 28.72           C  
ANISOU 2519  CB  SER B  82B    4277   3240   3394   -242     42     80       C  
ATOM   2520  OG  SER B  82B    -46.749  52.345  33.153  1.00 29.90           O  
ANISOU 2520  OG  SER B  82B    4463   3356   3542   -249     33     76       O  
ATOM   2521  N   LEU B  82C    -49.562  48.828  31.254  1.00 26.91           N  
ANISOU 2521  N   LEU B  82C    4013   3020   3191   -151      3    107       N  
ATOM   2522  CA  LEU B  82C    -49.853  47.451  30.839  1.00 27.23           C  
ANISOU 2522  CA  LEU B  82C    4015   3091   3238   -137      8    110       C  
ATOM   2523  C   LEU B  82C    -49.189  47.092  29.531  1.00 28.80           C  
ANISOU 2523  C   LEU B  82C    4229   3298   3414   -174     19    118       C  
ATOM   2524  O   LEU B  82C    -49.215  47.878  28.569  1.00 29.25           O  
ANISOU 2524  O   LEU B  82C    4338   3326   3450   -196      9    130       O  
ATOM   2525  CB  LEU B  82C    -51.354  47.202  30.761  1.00 26.90           C  
ANISOU 2525  CB  LEU B  82C    3970   3037   3212    -90    -18    117       C  
ATOM   2526  CG  LEU B  82C    -51.994  47.134  32.158  1.00 25.86           C  
ANISOU 2526  CG  LEU B  82C    3804   2915   3105    -54    -22    103       C  
ATOM   2527  CD1 LEU B  82C    -53.498  47.348  32.113  1.00 24.56           C  
ANISOU 2527  CD1 LEU B  82C    3646   2732   2952    -11    -51    104       C  
ATOM   2528  CD2 LEU B  82C    -51.645  45.833  32.886  1.00 26.60           C  
ANISOU 2528  CD2 LEU B  82C    3842   3053   3211    -49     -2     94       C  
ATOM   2529  N   ARG B  83     -48.611  45.888  29.516  1.00 28.91           N  
ANISOU 2529  N   ARG B  83     4199   3353   3433   -180     39    109       N  
ATOM   2530  CA  ARG B  83     -47.921  45.306  28.377  1.00 28.99           C  
ANISOU 2530  CA  ARG B  83     4210   3382   3424   -212     53    109       C  
ATOM   2531  C   ARG B  83     -48.734  44.136  27.799  1.00 29.63           C  
ANISOU 2531  C   ARG B  83     4268   3476   3515   -185     45    115       C  
ATOM   2532  O   ARG B  83     -49.573  43.544  28.483  1.00 28.81           O  
ANISOU 2532  O   ARG B  83     4135   3377   3434   -145     35    115       O  
ATOM   2533  CB  ARG B  83     -46.546  44.781  28.815  1.00 28.76           C  
ANISOU 2533  CB  ARG B  83     4143   3391   3393   -239     81     87       C  
ATOM   2534  CG  ARG B  83     -45.739  45.690  29.722  1.00 27.18           C  
ANISOU 2534  CG  ARG B  83     3949   3187   3189   -259     92     75       C  
ATOM   2535  CD  ARG B  83     -44.559  44.959  30.328  1.00 24.68           C  
ANISOU 2535  CD  ARG B  83     3586   2915   2879   -272    115     50       C  
ATOM   2536  NE  ARG B  83     -43.760  45.850  31.160  1.00 24.47           N  
ANISOU 2536  NE  ARG B  83     3563   2886   2847   -293    126     37       N  
ATOM   2537  CZ  ARG B  83     -42.690  45.482  31.863  1.00 26.00           C  
ANISOU 2537  CZ  ARG B  83     3721   3115   3045   -304    144     13       C  
ATOM   2538  NH1 ARG B  83     -42.254  44.214  31.834  1.00 26.09           N  
ANISOU 2538  NH1 ARG B  83     3687   3163   3065   -295    151     -1       N  
ATOM   2539  NH2 ARG B  83     -42.055  46.398  32.595  1.00 28.32           N  
ANISOU 2539  NH2 ARG B  83     4023   3405   3334   -324    153      2       N  
ATOM   2540  N   SER B  84     -48.489  43.787  26.535  1.00 29.50           N  
ANISOU 2540  N   SER B  84     4263   3466   3480   -209     49    120       N  
ATOM   2541  CA  SER B  84     -49.137  42.608  25.956  1.00 30.83           C  
ANISOU 2541  CA  SER B  84     4406   3650   3657   -186     44    124       C  
ATOM   2542  C   SER B  84     -48.931  41.351  26.813  1.00 29.65           C  
ANISOU 2542  C   SER B  84     4198   3534   3532   -165     55    109       C  
ATOM   2543  O   SER B  84     -49.874  40.564  26.999  1.00 30.20           O  
ANISOU 2543  O   SER B  84     4247   3608   3619   -129     44    114       O  
ATOM   2544  CB  SER B  84     -48.643  42.355  24.519  1.00 31.24           C  
ANISOU 2544  CB  SER B  84     4474   3712   3685   -222     53    126       C  
ATOM   2545  OG  SER B  84     -48.943  43.466  23.682  1.00 35.76           O  
ANISOU 2545  OG  SER B  84     5104   4250   4232   -242     39    143       O  
ATOM   2546  N   GLU B  85     -47.722  41.219  27.376  1.00 29.46           N  
ANISOU 2546  N   GLU B  85     4152   3534   3508   -186     75     91       N  
ATOM   2547  CA  GLU B  85     -47.320  40.061  28.169  1.00 28.43           C  
ANISOU 2547  CA  GLU B  85     3971   3434   3396   -169     83     75       C  
ATOM   2548  C   GLU B  85     -48.032  40.035  29.522  1.00 26.70           C  
ANISOU 2548  C   GLU B  85     3737   3209   3200   -133     72     79       C  
ATOM   2549  O   GLU B  85     -47.961  39.027  30.230  1.00 27.44           O  
ANISOU 2549  O   GLU B  85     3793   3323   3310   -115     74     71       O  
ATOM   2550  CB  GLU B  85     -45.805  40.042  28.399  1.00 29.61           C  
ANISOU 2550  CB  GLU B  85     4103   3611   3539   -201    104     52       C  
ATOM   2551  CG  GLU B  85     -45.295  41.216  29.259  1.00 32.30           C  
ANISOU 2551  CG  GLU B  85     4458   3939   3873   -216    110     47       C  
ATOM   2552  CD  GLU B  85     -43.807  41.178  29.521  1.00 35.23           C  
ANISOU 2552  CD  GLU B  85     4807   4340   4236   -247    130     21       C  
ATOM   2553  OE1 GLU B  85     -43.056  40.660  28.653  1.00 38.09           O  
ANISOU 2553  OE1 GLU B  85     5158   4728   4588   -272    142      6       O  
ATOM   2554  OE2 GLU B  85     -43.384  41.656  30.594  1.00 34.81           O  
ANISOU 2554  OE2 GLU B  85     4748   4290   4190   -246    135     12       O  
ATOM   2555  N   ASP B  86     -48.711  41.128  29.864  1.00 24.53           N  
ANISOU 2555  N   ASP B  86     3491   2905   2923   -125     61     89       N  
ATOM   2556  CA  ASP B  86     -49.507  41.173  31.108  1.00 22.02           C  
ANISOU 2556  CA  ASP B  86     3159   2583   2625    -91     51     90       C  
ATOM   2557  C   ASP B  86     -50.887  40.560  30.906  1.00 21.67           C  
ANISOU 2557  C   ASP B  86     3107   2534   2592    -58     34    100       C  
ATOM   2558  O   ASP B  86     -51.702  40.530  31.834  1.00 21.57           O  
ANISOU 2558  O   ASP B  86     3081   2520   2593    -31     26     99       O  
ATOM   2559  CB  ASP B  86     -49.679  42.611  31.585  1.00 22.95           C  
ANISOU 2559  CB  ASP B  86     3308   2673   2738    -93     44     91       C  
ATOM   2560  CG  ASP B  86     -48.399  43.217  32.062  1.00 20.67           C  
ANISOU 2560  CG  ASP B  86     3022   2391   2441   -124     61     79       C  
ATOM   2561  OD1 ASP B  86     -47.550  42.479  32.571  1.00 24.38           O  
ANISOU 2561  OD1 ASP B  86     3458   2890   2916   -131     75     66       O  
ATOM   2562  OD2 ASP B  86     -48.224  44.458  31.952  1.00 21.84           O  
ANISOU 2562  OD2 ASP B  86     3207   2514   2577   -141     58     81       O  
ATOM   2563  N   THR B  87     -51.207  40.162  29.682  1.00 20.71           N  
ANISOU 2563  N   THR B  87     2997   2410   2463    -61     30    108       N  
ATOM   2564  CA  THR B  87     -52.408  39.376  29.449  1.00 21.16           C  
ANISOU 2564  CA  THR B  87     3040   2468   2531    -32     17    115       C  
ATOM   2565  C   THR B  87     -52.375  38.079  30.262  1.00 20.75           C  
ANISOU 2565  C   THR B  87     2945   2444   2496    -19     23    108       C  
ATOM   2566  O   THR B  87     -51.504  37.225  30.059  1.00 21.13           O  
ANISOU 2566  O   THR B  87     2974   2512   2544    -32     34    101       O  
ATOM   2567  CB  THR B  87     -52.586  39.087  27.938  1.00 21.09           C  
ANISOU 2567  CB  THR B  87     3048   2456   2509    -42     13    123       C  
ATOM   2568  OG1 THR B  87     -52.866  40.327  27.281  1.00 22.58           O  
ANISOU 2568  OG1 THR B  87     3282   2614   2682    -49      1    133       O  
ATOM   2569  CG2 THR B  87     -53.750  38.176  27.683  1.00 21.09           C  
ANISOU 2569  CG2 THR B  87     3031   2462   2520    -14      2    128       C  
ATOM   2570  N   ALA B  88     -53.275  37.983  31.243  1.00 20.13           N  
ANISOU 2570  N   ALA B  88     2853   2366   2430      7     15    107       N  
ATOM   2571  CA  ALA B  88     -53.184  36.927  32.247  1.00 20.07           C  
ANISOU 2571  CA  ALA B  88     2810   2380   2434     15     20    102       C  
ATOM   2572  C   ALA B  88     -54.470  36.871  33.032  1.00 19.54           C  
ANISOU 2572  C   ALA B  88     2733   2314   2377     40     10    102       C  
ATOM   2573  O   ALA B  88     -55.299  37.815  33.007  1.00 19.90           O  
ANISOU 2573  O   ALA B  88     2796   2345   2423     52     -1    102       O  
ATOM   2574  CB  ALA B  88     -52.007  37.217  33.212  1.00 19.62           C  
ANISOU 2574  CB  ALA B  88     2744   2332   2377      1     32     92       C  
ATOM   2575  N   VAL B  89     -54.627  35.770  33.764  1.00 18.75           N  
ANISOU 2575  N   VAL B  89     2606   2233   2286     46     12    101       N  
ATOM   2576  CA  VAL B  89     -55.664  35.663  34.753  1.00 17.66           C  
ANISOU 2576  CA  VAL B  89     2453   2102   2153     62      6     97       C  
ATOM   2577  C   VAL B  89     -55.011  36.035  36.077  1.00 16.74           C  
ANISOU 2577  C   VAL B  89     2329   1994   2039     55     13     91       C  
ATOM   2578  O   VAL B  89     -53.986  35.447  36.436  1.00 17.30           O  
ANISOU 2578  O   VAL B  89     2389   2074   2109     44     20     90       O  
ATOM   2579  CB  VAL B  89     -56.243  34.233  34.799  1.00 17.02           C  
ANISOU 2579  CB  VAL B  89     2351   2037   2077     67      4    101       C  
ATOM   2580  CG1 VAL B  89     -57.222  34.149  35.956  1.00 19.83           C  
ANISOU 2580  CG1 VAL B  89     2692   2406   2437     76      2     95       C  
ATOM   2581  CG2 VAL B  89     -56.972  33.947  33.501  1.00 20.02           C  
ANISOU 2581  CG2 VAL B  89     2739   2411   2457     74     -2    106       C  
ATOM   2582  N   TYR B  90     -55.557  37.097  36.703  1.00 16.46           N  
ANISOU 2582  N   TYR B  90     2299   1951   2003     64      9     83       N  
ATOM   2583  CA  TYR B  90     -55.114  37.573  38.027  1.00 16.06           C  
ANISOU 2583  CA  TYR B  90     2240   1908   1953     60     15     75       C  
ATOM   2584  C   TYR B  90     -55.986  37.004  39.117  1.00 16.19           C  
ANISOU 2584  C   TYR B  90     2235   1945   1973     68     13     70       C  
ATOM   2585  O   TYR B  90     -57.225  37.111  39.053  1.00 17.05           O  
ANISOU 2585  O   TYR B  90     2339   2056   2084     82      6     65       O  
ATOM   2586  CB  TYR B  90     -55.147  39.121  38.064  1.00 15.96           C  
ANISOU 2586  CB  TYR B  90     2249   1875   1939     63     11     68       C  
ATOM   2587  CG  TYR B  90     -54.121  39.667  37.110  1.00 17.73           C  
ANISOU 2587  CG  TYR B  90     2498   2082   2156     46     15     73       C  
ATOM   2588  CD1 TYR B  90     -54.378  39.687  35.729  1.00 18.68           C  
ANISOU 2588  CD1 TYR B  90     2638   2188   2272     46      9     82       C  
ATOM   2589  CD2 TYR B  90     -52.859  40.067  37.554  1.00 16.42           C  
ANISOU 2589  CD2 TYR B  90     2335   1918   1986     27     27     68       C  
ATOM   2590  CE1 TYR B  90     -53.386  40.103  34.821  1.00 17.49           C  
ANISOU 2590  CE1 TYR B  90     2511   2025   2111     24     15     86       C  
ATOM   2591  CE2 TYR B  90     -51.866  40.502  36.647  1.00 17.09           C  
ANISOU 2591  CE2 TYR B  90     2441   1992   2062      6     33     70       C  
ATOM   2592  CZ  TYR B  90     -52.173  40.534  35.274  1.00 17.27           C  
ANISOU 2592  CZ  TYR B  90     2484   1999   2077      3     27     80       C  
ATOM   2593  OH  TYR B  90     -51.179  40.936  34.411  1.00 19.25           O  
ANISOU 2593  OH  TYR B  90     2755   2242   2315    -23     35     81       O  
ATOM   2594  N   TYR B  91     -55.329  36.340  40.075  1.00 17.21           N  
ANISOU 2594  N   TYR B  91     2349   2090   2101     57     20     71       N  
ATOM   2595  CA  TYR B  91     -56.011  35.752  41.240  1.00 15.65           C  
ANISOU 2595  CA  TYR B  91     2132   1913   1901     58     19     68       C  
ATOM   2596  C   TYR B  91     -55.646  36.461  42.505  1.00 15.93           C  
ANISOU 2596  C   TYR B  91     2162   1957   1934     53     24     58       C  
ATOM   2597  O   TYR B  91     -54.496  36.835  42.688  1.00 16.28           O  
ANISOU 2597  O   TYR B  91     2212   1997   1978     44     29     57       O  
ATOM   2598  CB  TYR B  91     -55.574  34.296  41.470  1.00 15.97           C  
ANISOU 2598  CB  TYR B  91     2163   1965   1940     48     19     78       C  
ATOM   2599  CG  TYR B  91     -55.948  33.343  40.354  1.00 16.91           C  
ANISOU 2599  CG  TYR B  91     2283   2079   2062     51     14     88       C  
ATOM   2600  CD1 TYR B  91     -57.217  32.791  40.287  1.00 18.55           C  
ANISOU 2600  CD1 TYR B  91     2484   2296   2269     56     11     88       C  
ATOM   2601  CD2 TYR B  91     -55.012  32.999  39.394  1.00 17.79           C  
ANISOU 2601  CD2 TYR B  91     2403   2181   2177     48     14     93       C  
ATOM   2602  CE1 TYR B  91     -57.565  31.919  39.261  1.00 18.65           C  
ANISOU 2602  CE1 TYR B  91     2498   2305   2285     58      7     96       C  
ATOM   2603  CE2 TYR B  91     -55.353  32.123  38.336  1.00 17.53           C  
ANISOU 2603  CE2 TYR B  91     2370   2143   2146     51     10    100       C  
ATOM   2604  CZ  TYR B  91     -56.621  31.604  38.288  1.00 19.57           C  
ANISOU 2604  CZ  TYR B  91     2623   2409   2405     57      6    102       C  
ATOM   2605  OH  TYR B  91     -56.964  30.703  37.270  1.00 22.76           O  
ANISOU 2605  OH  TYR B  91     3027   2810   2811     59      2    108       O  
ATOM   2606  N   CYS B  92     -56.643  36.595  43.364  1.00 16.72           N  
ANISOU 2606  N   CYS B  92     2249   2072   2032     57     23     48       N  
ATOM   2607  CA  CYS B  92     -56.335  36.935  44.743  1.00 16.82           C  
ANISOU 2607  CA  CYS B  92     2251   2099   2039     49     29     39       C  
ATOM   2608  C   CYS B  92     -56.569  35.639  45.531  1.00 17.08           C  
ANISOU 2608  C   CYS B  92     2271   2155   2064     36     29     46       C  
ATOM   2609  O   CYS B  92     -57.402  34.789  45.151  1.00 17.60           O  
ANISOU 2609  O   CYS B  92     2332   2226   2128     36     26     52       O  
ATOM   2610  CB  CYS B  92     -57.242  38.080  45.208  1.00 17.80           C  
ANISOU 2610  CB  CYS B  92     2371   2227   2166     60     27     18       C  
ATOM   2611  SG  CYS B  92     -58.993  37.601  45.323  1.00 23.48           S  
ANISOU 2611  SG  CYS B  92     3072   2968   2882     67     23      7       S  
ATOM   2612  N   ALA B  93     -55.865  35.501  46.657  1.00 15.29           N  
ANISOU 2612  N   ALA B  93     2039   1940   1830     24     32     47       N  
ATOM   2613  CA  ALA B  93     -56.060  34.331  47.531  1.00 16.08           C  
ANISOU 2613  CA  ALA B  93     2132   2059   1919      9     30     55       C  
ATOM   2614  C   ALA B  93     -55.880  34.774  48.979  1.00 16.73           C  
ANISOU 2614  C   ALA B  93     2206   2161   1991     -2     34     45       C  
ATOM   2615  O   ALA B  93     -55.061  35.644  49.258  1.00 17.22           O  
ANISOU 2615  O   ALA B  93     2269   2217   2056      0     38     38       O  
ATOM   2616  CB  ALA B  93     -55.083  33.281  47.217  1.00 16.35           C  
ANISOU 2616  CB  ALA B  93     2175   2084   1954      4     23     72       C  
ATOM   2617  N   ARG B  94     -56.661  34.193  49.871  1.00 16.12           N  
ANISOU 2617  N   ARG B  94     2120   2106   1900    -17     35     44       N  
ATOM   2618  CA  ARG B  94     -56.541  34.454  51.281  1.00 15.43           C  
ANISOU 2618  CA  ARG B  94     2024   2040   1799    -31     39     36       C  
ATOM   2619  C   ARG B  94     -55.579  33.438  51.828  1.00 15.74           C  
ANISOU 2619  C   ARG B  94     2073   2078   1828    -44     30     55       C  
ATOM   2620  O   ARG B  94     -55.645  32.238  51.532  1.00 15.21           O  
ANISOU 2620  O   ARG B  94     2016   2006   1758    -51     22     72       O  
ATOM   2621  CB  ARG B  94     -57.899  34.362  51.965  1.00 15.61           C  
ANISOU 2621  CB  ARG B  94     2032   2091   1808    -44     45     23       C  
ATOM   2622  CG  ARG B  94     -57.850  34.997  53.373  1.00 20.00           C  
ANISOU 2622  CG  ARG B  94     2576   2672   2352    -57     51      7       C  
ATOM   2623  CD  ARG B  94     -59.151  34.896  54.117  1.00 20.72           C  
ANISOU 2623  CD  ARG B  94     2650   2797   2427    -74     59    -10       C  
ATOM   2624  NE  ARG B  94     -59.331  33.535  54.604  1.00 22.86           N  
ANISOU 2624  NE  ARG B  94     2928   3080   2676   -102     55      9       N  
ATOM   2625  CZ  ARG B  94     -60.178  33.219  55.573  1.00 27.54           C  
ANISOU 2625  CZ  ARG B  94     3511   3708   3247   -130     62     -1       C  
ATOM   2626  NH1 ARG B  94     -60.913  34.174  56.137  1.00 29.70           N  
ANISOU 2626  NH1 ARG B  94     3760   4008   3517   -130     73    -33       N  
ATOM   2627  NH2 ARG B  94     -60.298  31.954  55.957  1.00 29.76           N  
ANISOU 2627  NH2 ARG B  94     3805   3996   3507   -159     58     20       N  
ATOM   2628  N   THR B  95     -54.703  33.923  52.690  1.00 16.15           N  
ANISOU 2628  N   THR B  95     2123   2135   1876    -48     31     51       N  
ATOM   2629  CA  THR B  95     -53.650  33.057  53.289  1.00 16.04           C  
ANISOU 2629  CA  THR B  95     2120   2121   1854    -57     19     66       C  
ATOM   2630  C   THR B  95     -54.150  32.396  54.559  1.00 17.79           C  
ANISOU 2630  C   THR B  95     2343   2366   2052    -81     16     71       C  
ATOM   2631  O   THR B  95     -55.239  32.690  55.037  1.00 18.14           O  
ANISOU 2631  O   THR B  95     2376   2431   2086    -94     26     61       O  
ATOM   2632  CB  THR B  95     -52.385  33.885  53.633  1.00 17.62           C  
ANISOU 2632  CB  THR B  95     2317   2318   2059    -50     21     56       C  
ATOM   2633  OG1 THR B  95     -52.664  34.760  54.753  1.00 17.61           O  
ANISOU 2633  OG1 THR B  95     2304   2338   2047    -60     31     40       O  
ATOM   2634  CG2 THR B  95     -51.936  34.707  52.437  1.00 17.38           C  
ANISOU 2634  CG2 THR B  95     2288   2267   2048    -33     27     48       C  
ATOM   2635  N   PHE B  96     -53.363  31.467  55.073  1.00 17.10           N  
ANISOU 2635  N   PHE B  96     2268   2274   1954    -89      1     88       N  
ATOM   2636  CA  PHE B  96     -53.507  31.078  56.485  1.00 18.15           C  
ANISOU 2636  CA  PHE B  96     2405   2428   2061   -115     -4     93       C  
ATOM   2637  C   PHE B  96     -53.426  32.231  57.467  1.00 17.88           C  
ANISOU 2637  C   PHE B  96     2356   2417   2020   -120      9     73       C  
ATOM   2638  O   PHE B  96     -52.980  33.324  57.145  1.00 16.44           O  
ANISOU 2638  O   PHE B  96     2162   2229   1854   -103     18     57       O  
ATOM   2639  CB  PHE B  96     -52.442  30.052  56.862  1.00 17.66           C  
ANISOU 2639  CB  PHE B  96     2364   2354   1993   -116    -28    112       C  
ATOM   2640  CG  PHE B  96     -52.685  28.653  56.347  1.00 20.23           C  
ANISOU 2640  CG  PHE B  96     2709   2662   2316   -120    -45    133       C  
ATOM   2641  CD1 PHE B  96     -53.626  28.375  55.364  1.00 22.19           C  
ANISOU 2641  CD1 PHE B  96     2955   2903   2573   -119    -38    135       C  
ATOM   2642  CD2 PHE B  96     -51.879  27.620  56.821  1.00 20.40           C  
ANISOU 2642  CD2 PHE B  96     2751   2670   2328   -123    -71    150       C  
ATOM   2643  CE1 PHE B  96     -53.834  27.043  54.895  1.00 21.51           C  
ANISOU 2643  CE1 PHE B  96     2889   2800   2484   -124    -54    155       C  
ATOM   2644  CE2 PHE B  96     -52.056  26.286  56.355  1.00 21.56           C  
ANISOU 2644  CE2 PHE B  96     2921   2797   2474   -126    -91    170       C  
ATOM   2645  CZ  PHE B  96     -53.029  26.014  55.380  1.00 23.21           C  
ANISOU 2645  CZ  PHE B  96     3128   3001   2691   -127    -81    172       C  
ATOM   2646  N   HIS B  97     -53.833  31.960  58.710  1.00 18.82           N  
ANISOU 2646  N   HIS B  97     2476   2561   2113   -147      9     74       N  
ATOM   2647  CA  HIS B  97     -53.688  32.876  59.810  1.00 19.21           C  
ANISOU 2647  CA  HIS B  97     2513   2635   2152   -156     18     57       C  
ATOM   2648  C   HIS B  97     -52.298  33.492  59.860  1.00 18.79           C  
ANISOU 2648  C   HIS B  97     2458   2570   2112   -137     14     52       C  
ATOM   2649  O   HIS B  97     -51.308  32.763  59.801  1.00 19.36           O  
ANISOU 2649  O   HIS B  97     2544   2626   2184   -131     -4     67       O  
ATOM   2650  CB  HIS B  97     -53.960  32.114  61.098  1.00 18.99           C  
ANISOU 2650  CB  HIS B  97     2496   2630   2091   -190     11     68       C  
ATOM   2651  CG  HIS B  97     -54.208  32.998  62.268  1.00 20.01           C  
ANISOU 2651  CG  HIS B  97     2607   2793   2204   -206     25     47       C  
ATOM   2652  ND1 HIS B  97     -53.235  33.806  62.804  1.00 21.50           N  
ANISOU 2652  ND1 HIS B  97     2788   2984   2397   -196     26     36       N  
ATOM   2653  CD2 HIS B  97     -55.341  33.250  62.976  1.00 20.47           C  
ANISOU 2653  CD2 HIS B  97     2651   2885   2242   -231     40     30       C  
ATOM   2654  CE1 HIS B  97     -53.742  34.510  63.804  1.00 20.47           C  
ANISOU 2654  CE1 HIS B  97     2641   2886   2250   -214     40     15       C  
ATOM   2655  NE2 HIS B  97     -55.016  34.171  63.946  1.00 21.49           N  
ANISOU 2655  NE2 HIS B  97     2765   3037   2364   -236     49     11       N  
ATOM   2656  N   ILE B  98     -52.222  34.802  60.052  1.00 18.51           N  
ANISOU 2656  N   ILE B  98     2404   2543   2084   -129     29     28       N  
ATOM   2657  CA  ILE B  98     -50.947  35.495  59.921  1.00 19.70           C  
ANISOU 2657  CA  ILE B  98     2554   2683   2250   -113     28     20       C  
ATOM   2658  C   ILE B  98     -49.970  35.297  61.092  1.00 20.42           C  
ANISOU 2658  C   ILE B  98     2647   2787   2324   -123     18     22       C  
ATOM   2659  O   ILE B  98     -48.800  35.690  61.020  1.00 20.40           O  
ANISOU 2659  O   ILE B  98     2642   2776   2331   -110     15     16       O  
ATOM   2660  CB  ILE B  98     -51.201  36.996  59.683  1.00 19.20           C  
ANISOU 2660  CB  ILE B  98     2473   2619   2201   -102     46     -6       C  
ATOM   2661  CG1 ILE B  98     -52.095  37.541  60.802  1.00 23.17           C  
ANISOU 2661  CG1 ILE B  98     2961   3154   2688   -119     57    -24       C  
ATOM   2662  CG2 ILE B  98     -51.841  37.183  58.299  1.00 19.42           C  
ANISOU 2662  CG2 ILE B  98     2503   2626   2249    -85     51     -7       C  
ATOM   2663  CD1 ILE B  98     -51.947  39.002  61.072  1.00 27.65           C  
ANISOU 2663  CD1 ILE B  98     3515   3726   3266   -110     70    -52       C  
ATOM   2664  N   ARG B  99     -50.466  34.740  62.195  1.00 20.37           N  
ANISOU 2664  N   ARG B  99     2645   2802   2291   -147     13     30       N  
ATOM   2665  CA  ARG B  99     -49.641  34.577  63.393  1.00 21.08           C  
ANISOU 2665  CA  ARG B  99     2740   2908   2362   -158      2     32       C  
ATOM   2666  C   ARG B  99     -49.481  33.142  63.881  1.00 21.19           C  
ANISOU 2666  C   ARG B  99     2779   2918   2354   -173    -23     60       C  
ATOM   2667  O   ARG B  99     -48.599  32.870  64.709  1.00 20.48           O  
ANISOU 2667  O   ARG B  99     2698   2833   2251   -176    -40     65       O  
ATOM   2668  CB  ARG B  99     -50.138  35.484  64.530  1.00 22.35           C  
ANISOU 2668  CB  ARG B  99     2884   3102   2507   -177     19     12       C  
ATOM   2669  CG  ARG B  99     -49.002  35.873  65.466  1.00 21.62           C  
ANISOU 2669  CG  ARG B  99     2788   3020   2406   -177     13      4       C  
ATOM   2670  CD  ARG B  99     -49.431  36.885  66.494  1.00 24.09           C  
ANISOU 2670  CD  ARG B  99     3081   3365   2706   -193     30    -20       C  
ATOM   2671  NE  ARG B  99     -50.044  38.022  65.840  1.00 22.05           N  
ANISOU 2671  NE  ARG B  99     2804   3103   2470   -180     51    -44       N  
ATOM   2672  CZ  ARG B  99     -49.370  39.091  65.419  1.00 25.33           C  
ANISOU 2672  CZ  ARG B  99     3210   3505   2908   -160     60    -62       C  
ATOM   2673  NH1 ARG B  99     -48.057  39.169  65.601  1.00 26.80           N  
ANISOU 2673  NH1 ARG B  99     3400   3687   3098   -153     51    -62       N  
ATOM   2674  NH2 ARG B  99     -49.999  40.082  64.799  1.00 25.14           N  
ANISOU 2674  NH2 ARG B  99     3175   3475   2904   -148     75    -82       N  
ATOM   2675  N   ARG B 100     -50.315  32.233  63.379  1.00 19.37           N  
ANISOU 2675  N   ARG B 100     2563   2679   2120   -182    -28     77       N  
ATOM   2676  CA  ARG B 100     -50.284  30.830  63.806  1.00 20.45           C  
ANISOU 2676  CA  ARG B 100     2729   2808   2234   -199    -54    105       C  
ATOM   2677  C   ARG B 100     -49.039  30.071  63.362  1.00 20.69           C  
ANISOU 2677  C   ARG B 100     2775   2809   2277   -174    -83    118       C  
ATOM   2678  O   ARG B 100     -48.656  29.081  63.997  1.00 21.46           O  
ANISOU 2678  O   ARG B 100     2899   2900   2355   -184   -110    138       O  
ATOM   2679  CB  ARG B 100     -51.551  30.116  63.342  1.00 20.52           C  
ANISOU 2679  CB  ARG B 100     2747   2815   2236   -216    -49    117       C  
ATOM   2680  CG  ARG B 100     -51.650  28.653  63.802  1.00 22.27           C  
ANISOU 2680  CG  ARG B 100     3003   3027   2431   -239    -75    147       C  
ATOM   2681  CD  ARG B 100     -51.622  28.589  65.337  1.00 24.97           C  
ANISOU 2681  CD  ARG B 100     3356   3396   2736   -272    -81    152       C  
ATOM   2682  NE  ARG B 100     -51.709  27.244  65.899  1.00 30.34           N  
ANISOU 2682  NE  ARG B 100     4076   4066   3387   -299   -108    182       N  
ATOM   2683  CZ  ARG B 100     -50.662  26.470  66.157  1.00 30.23           C  
ANISOU 2683  CZ  ARG B 100     4090   4028   3369   -288   -144    201       C  
ATOM   2684  NH1 ARG B 100     -49.426  26.897  65.892  1.00 31.42           N  
ANISOU 2684  NH1 ARG B 100     4229   4165   3544   -250   -154    190       N  
ATOM   2685  NH2 ARG B 100     -50.838  25.278  66.692  1.00 31.95           N  
ANISOU 2685  NH2 ARG B 100     4348   4234   3557   -315   -170    229       N  
ATOM   2686  N   TYR B 100A    -48.434  30.475  62.245  1.00 20.77           N  
ANISOU 2686  N   TYR B 100A    2773   2801   2319   -144    -78    107       N  
ATOM   2687  CA  TYR B 100A    -47.303  29.717  61.685  1.00 20.61           C  
ANISOU 2687  CA  TYR B 100A    2763   2754   2312   -120   -105    115       C  
ATOM   2688  C   TYR B 100A    -46.052  30.568  61.718  1.00 20.52           C  
ANISOU 2688  C   TYR B 100A    2734   2748   2315    -99   -103     92       C  
ATOM   2689  O   TYR B 100A    -46.019  31.687  61.188  1.00 21.20           O  
ANISOU 2689  O   TYR B 100A    2798   2838   2418    -91    -78     73       O  
ATOM   2690  CB  TYR B 100A    -47.622  29.250  60.245  1.00 21.11           C  
ANISOU 2690  CB  TYR B 100A    2829   2794   2398   -104   -104    120       C  
ATOM   2691  CG  TYR B 100A    -48.852  28.387  60.248  1.00 20.20           C  
ANISOU 2691  CG  TYR B 100A    2731   2675   2267   -127   -106    140       C  
ATOM   2692  CD1 TYR B 100A    -48.767  27.010  60.443  1.00 21.53           C  
ANISOU 2692  CD1 TYR B 100A    2930   2827   2423   -133   -136    164       C  
ATOM   2693  CD2 TYR B 100A    -50.130  28.970  60.129  1.00 22.22           C  
ANISOU 2693  CD2 TYR B 100A    2976   2948   2520   -143    -79    134       C  
ATOM   2694  CE1 TYR B 100A    -49.933  26.227  60.506  1.00 23.34           C  
ANISOU 2694  CE1 TYR B 100A    3178   3056   2635   -160   -137    182       C  
ATOM   2695  CE2 TYR B 100A    -51.307  28.191  60.191  1.00 21.94           C  
ANISOU 2695  CE2 TYR B 100A    2954   2916   2468   -167    -78    149       C  
ATOM   2696  CZ  TYR B 100A    -51.173  26.814  60.359  1.00 22.57           C  
ANISOU 2696  CZ  TYR B 100A    3064   2977   2533   -177   -106    174       C  
ATOM   2697  OH  TYR B 100A    -52.303  26.042  60.453  1.00 26.71           O  
ANISOU 2697  OH  TYR B 100A    3605   3505   3039   -206   -106    188       O  
ATOM   2698  N   ARG B 100B    -45.016  30.031  62.344  1.00 21.45           N  
ANISOU 2698  N   ARG B 100B    2861   2863   2425    -92   -130     95       N  
ATOM   2699  CA  ARG B 100B    -43.747  30.753  62.405  1.00 20.94           C  
ANISOU 2699  CA  ARG B 100B    2778   2806   2372    -74   -130     72       C  
ATOM   2700  C   ARG B 100B    -43.171  31.016  61.020  1.00 21.39           C  
ANISOU 2700  C   ARG B 100B    2820   2848   2460    -50   -122     56       C  
ATOM   2701  O   ARG B 100B    -42.428  31.989  60.827  1.00 21.73           O  
ANISOU 2701  O   ARG B 100B    2843   2900   2515    -42   -107     32       O  
ATOM   2702  CB  ARG B 100B    -42.727  30.013  63.264  1.00 21.51           C  
ANISOU 2702  CB  ARG B 100B    2863   2879   2432    -66   -165     76       C  
ATOM   2703  CG  ARG B 100B    -43.148  29.791  64.724  1.00 21.57           C  
ANISOU 2703  CG  ARG B 100B    2888   2903   2406    -93   -175     90       C  
ATOM   2704  CD  ARG B 100B    -43.212  31.100  65.506  1.00 23.47           C  
ANISOU 2704  CD  ARG B 100B    3106   3174   2638   -107   -148     71       C  
ATOM   2705  NE  ARG B 100B    -41.903  31.590  65.952  1.00 22.25           N  
ANISOU 2705  NE  ARG B 100B    2936   3030   2487    -91   -156     50       N  
ATOM   2706  CZ  ARG B 100B    -41.324  31.293  67.127  1.00 23.41           C  
ANISOU 2706  CZ  ARG B 100B    3094   3190   2612    -96   -180     53       C  
ATOM   2707  NH1 ARG B 100B    -41.915  30.492  68.018  1.00 26.00           N  
ANISOU 2707  NH1 ARG B 100B    3450   3520   2909   -119   -199     79       N  
ATOM   2708  NH2 ARG B 100B    -40.150  31.820  67.429  1.00 22.88           N  
ANISOU 2708  NH2 ARG B 100B    3008   3135   2551    -81   -184     30       N  
ATOM   2709  N   SER B 100C    -43.536  30.191  60.044  1.00 21.50           N  
ANISOU 2709  N   SER B 100C    2845   2840   2484    -42   -130     69       N  
ATOM   2710  CA  SER B 100C    -43.077  30.423  58.665  1.00 21.86           C  
ANISOU 2710  CA  SER B 100C    2876   2873   2556    -23   -121     55       C  
ATOM   2711  C   SER B 100C    -43.799  31.553  57.925  1.00 22.19           C  
ANISOU 2711  C   SER B 100C    2905   2917   2609    -30    -85     46       C  
ATOM   2712  O   SER B 100C    -43.425  31.890  56.789  1.00 24.82           O  
ANISOU 2712  O   SER B 100C    3229   3241   2961    -18    -75     34       O  
ATOM   2713  CB  SER B 100C    -43.099  29.142  57.833  1.00 22.80           C  
ANISOU 2713  CB  SER B 100C    3011   2969   2685    -10   -143     68       C  
ATOM   2714  OG  SER B 100C    -44.365  28.561  57.839  1.00 22.02           O  
ANISOU 2714  OG  SER B 100C    2929   2861   2575    -26   -143     92       O  
ATOM   2715  N   GLY B 100D    -44.851  32.087  58.513  1.00 20.97           N  
ANISOU 2715  N   GLY B 100D    2752   2775   2442    -48    -68     51       N  
ATOM   2716  CA  GLY B 100D    -45.526  33.225  57.881  1.00 20.39           C  
ANISOU 2716  CA  GLY B 100D    2667   2701   2379    -50    -39     41       C  
ATOM   2717  C   GLY B 100D    -46.784  32.741  57.187  1.00 19.83           C  
ANISOU 2717  C   GLY B 100D    2604   2619   2309    -54    -35     56       C  
ATOM   2718  O   GLY B 100D    -47.460  31.855  57.717  1.00 19.92           O  
ANISOU 2718  O   GLY B 100D    2630   2634   2306    -66    -47     73       O  
ATOM   2719  N   TYR B 100E    -47.105  33.293  55.996  1.00 18.23           N  
ANISOU 2719  N   TYR B 100E    2398   2405   2125    -45    -20     50       N  
ATOM   2720  CA  TYR B 100E    -48.451  33.118  55.409  1.00 18.02           C  
ANISOU 2720  CA  TYR B 100E    2375   2373   2099    -49    -12     59       C  
ATOM   2721  C   TYR B 100E    -48.530  33.199  53.877  1.00 17.50           C  
ANISOU 2721  C   TYR B 100E    2310   2286   2052    -36     -7     58       C  
ATOM   2722  O   TYR B 100E    -49.434  32.600  53.323  1.00 16.48           O  
ANISOU 2722  O   TYR B 100E    2187   2151   1925    -36     -8     70       O  
ATOM   2723  CB  TYR B 100E    -49.467  34.103  56.047  1.00 17.95           C  
ANISOU 2723  CB  TYR B 100E    2358   2381   2083    -61      6     48       C  
ATOM   2724  CG  TYR B 100E    -48.887  35.470  56.285  1.00 18.61           C  
ANISOU 2724  CG  TYR B 100E    2429   2469   2172    -57     19     27       C  
ATOM   2725  CD1 TYR B 100E    -48.315  35.804  57.519  1.00 19.79           C  
ANISOU 2725  CD1 TYR B 100E    2573   2637   2309    -66     19     19       C  
ATOM   2726  CD2 TYR B 100E    -48.894  36.433  55.277  1.00 20.02           C  
ANISOU 2726  CD2 TYR B 100E    2607   2634   2368    -46     32     16       C  
ATOM   2727  CE1 TYR B 100E    -47.750  37.069  57.735  1.00 20.45           C  
ANISOU 2727  CE1 TYR B 100E    2646   2724   2398    -64     31     -2       C  
ATOM   2728  CE2 TYR B 100E    -48.331  37.684  55.474  1.00 21.68           C  
ANISOU 2728  CE2 TYR B 100E    2810   2844   2582    -45     43     -3       C  
ATOM   2729  CZ  TYR B 100E    -47.767  37.987  56.711  1.00 20.87           C  
ANISOU 2729  CZ  TYR B 100E    2699   2760   2469    -54     44    -12       C  
ATOM   2730  OH  TYR B 100E    -47.223  39.239  56.909  1.00 24.63           O  
ANISOU 2730  OH  TYR B 100E    3170   3238   2951    -54     55    -32       O  
ATOM   2731  N   TYR B 100F    -47.644  33.948  53.217  1.00 16.59           N  
ANISOU 2731  N   TYR B 100F    2190   2165   1951    -26      1     44       N  
ATOM   2732  CA  TYR B 100F    -47.800  34.106  51.755  1.00 16.80           C  
ANISOU 2732  CA  TYR B 100F    2219   2174   1992    -18      8     44       C  
ATOM   2733  C   TYR B 100F    -47.601  32.799  51.003  1.00 17.08           C  
ANISOU 2733  C   TYR B 100F    2261   2198   2033    -10     -8     56       C  
ATOM   2734  O   TYR B 100F    -47.996  32.704  49.810  1.00 18.83           O  
ANISOU 2734  O   TYR B 100F    2485   2406   2263     -5     -4     59       O  
ATOM   2735  CB  TYR B 100F    -46.875  35.198  51.226  1.00 15.46           C  
ANISOU 2735  CB  TYR B 100F    2045   2000   1830    -16     20     26       C  
ATOM   2736  CG  TYR B 100F    -47.312  36.618  51.611  1.00 16.41           C  
ANISOU 2736  CG  TYR B 100F    2164   2123   1950    -21     36     15       C  
ATOM   2737  CD1 TYR B 100F    -48.653  37.041  51.526  1.00 17.37           C  
ANISOU 2737  CD1 TYR B 100F    2287   2241   2070    -20     42     17       C  
ATOM   2738  CD2 TYR B 100F    -46.363  37.525  52.058  1.00 18.00           C  
ANISOU 2738  CD2 TYR B 100F    2359   2330   2150    -26     44     -2       C  
ATOM   2739  CE1 TYR B 100F    -49.030  38.337  51.879  1.00 16.41           C  
ANISOU 2739  CE1 TYR B 100F    2165   2120   1950    -21     53      3       C  
ATOM   2740  CE2 TYR B 100F    -46.724  38.850  52.391  1.00 18.19           C  
ANISOU 2740  CE2 TYR B 100F    2384   2354   2174    -30     57    -14       C  
ATOM   2741  CZ  TYR B 100F    -48.050  39.242  52.302  1.00 18.36           C  
ANISOU 2741  CZ  TYR B 100F    2409   2370   2197    -26     60    -12       C  
ATOM   2742  OH  TYR B 100F    -48.365  40.541  52.645  1.00 21.50           O  
ANISOU 2742  OH  TYR B 100F    2807   2765   2596    -27     69    -27       O  
ATOM   2743  N   ASP B 100G    -46.943  31.828  51.640  1.00 17.75           N  
ANISOU 2743  N   ASP B 100G    2348   2286   2112     -9    -27     61       N  
ATOM   2744  CA  ASP B 100G    -46.798  30.492  51.057  1.00 17.92           C  
ANISOU 2744  CA  ASP B 100G    2376   2294   2137     -1    -46     72       C  
ATOM   2745  C   ASP B 100G    -47.930  29.534  51.405  1.00 17.47           C  
ANISOU 2745  C   ASP B 100G    2332   2234   2070     -9    -56     93       C  
ATOM   2746  O   ASP B 100G    -47.829  28.323  51.184  1.00 19.20           O  
ANISOU 2746  O   ASP B 100G    2562   2442   2290     -5    -76    104       O  
ATOM   2747  CB  ASP B 100G    -45.453  29.870  51.395  1.00 18.28           C  
ANISOU 2747  CB  ASP B 100G    2419   2341   2185      9    -67     64       C  
ATOM   2748  CG  ASP B 100G    -45.152  29.855  52.864  1.00 18.87           C  
ANISOU 2748  CG  ASP B 100G    2496   2429   2244      3    -78     65       C  
ATOM   2749  OD1 ASP B 100G    -45.935  30.333  53.723  1.00 20.08           O  
ANISOU 2749  OD1 ASP B 100G    2653   2593   2385    -12    -68     72       O  
ATOM   2750  OD2 ASP B 100G    -44.059  29.342  53.166  1.00 22.12           O  
ANISOU 2750  OD2 ASP B 100G    2906   2840   2657     13    -98     57       O  
ATOM   2751  N   LYS B 100H    -49.022  30.059  51.940  1.00 17.02           N  
ANISOU 2751  N   LYS B 100H    2276   2189   2003    -23    -43     96       N  
ATOM   2752  CA  LYS B 100H    -50.106  29.215  52.430  1.00 14.93           C  
ANISOU 2752  CA  LYS B 100H    2022   1927   1725    -38    -49    113       C  
ATOM   2753  C   LYS B 100H    -51.425  29.836  51.912  1.00 16.41           C  
ANISOU 2753  C   LYS B 100H    2202   2119   1913    -42    -29    109       C  
ATOM   2754  O   LYS B 100H    -52.257  30.321  52.638  1.00 17.29           O  
ANISOU 2754  O   LYS B 100H    2308   2248   2012    -55    -18    105       O  
ATOM   2755  CB  LYS B 100H    -50.060  29.112  53.975  1.00 15.22           C  
ANISOU 2755  CB  LYS B 100H    2064   1980   1739    -54    -56    117       C  
ATOM   2756  CG  LYS B 100H    -48.705  28.545  54.472  1.00 18.60           C  
ANISOU 2756  CG  LYS B 100H    2498   2402   2166    -46    -80    119       C  
ATOM   2757  CD  LYS B 100H    -48.611  28.469  55.991  1.00 18.32           C  
ANISOU 2757  CD  LYS B 100H    2471   2383   2107    -63    -89    124       C  
ATOM   2758  CE  LYS B 100H    -47.204  28.177  56.422  1.00 22.07           C  
ANISOU 2758  CE  LYS B 100H    2948   2854   2584    -49   -111    120       C  
ATOM   2759  NZ  LYS B 100H    -46.475  29.454  56.339  1.00 22.05           N  
ANISOU 2759  NZ  LYS B 100H    2924   2862   2592    -40    -93     96       N  
ATOM   2760  N   MET B 100I    -51.584  29.817  50.600  1.00 17.89           N  
ANISOU 2760  N   MET B 100I    2388   2292   2116    -30    -25    108       N  
ATOM   2761  CA  MET B 100I    -52.744  30.398  50.001  1.00 18.05           C  
ANISOU 2761  CA  MET B 100I    2403   2315   2140    -29    -10    103       C  
ATOM   2762  C   MET B 100I    -53.832  29.332  49.846  1.00 19.78           C  
ANISOU 2762  C   MET B 100I    2629   2536   2352    -39    -16    116       C  
ATOM   2763  O   MET B 100I    -53.718  28.395  49.031  1.00 17.65           O  
ANISOU 2763  O   MET B 100I    2366   2250   2088    -34    -26    126       O  
ATOM   2764  CB  MET B 100I    -52.343  31.003  48.651  1.00 17.83           C  
ANISOU 2764  CB  MET B 100I    2372   2271   2130    -12     -4     96       C  
ATOM   2765  CG  MET B 100I    -51.609  32.342  48.774  1.00 17.77           C  
ANISOU 2765  CG  MET B 100I    2360   2265   2127     -8      7     80       C  
ATOM   2766  SD  MET B 100I    -50.987  32.824  47.169  1.00 20.11           S  
ANISOU 2766  SD  MET B 100I    2660   2543   2440      5     12     75       S  
ATOM   2767  CE  MET B 100I    -49.734  31.580  46.856  1.00 22.76           C  
ANISOU 2767  CE  MET B 100I    2996   2873   2779      8     -3     79       C  
ATOM   2768  N   ASP B 101     -54.870  29.429  50.670  1.00 20.60           N  
ANISOU 2768  N   ASP B 101     2728   2659   2440    -56     -9    114       N  
ATOM   2769  CA  ASP B 101     -55.843  28.338  50.652  1.00 22.32           C  
ANISOU 2769  CA  ASP B 101     2954   2881   2648    -72    -13    126       C  
ATOM   2770  C   ASP B 101     -57.210  28.659  50.051  1.00 22.12           C  
ANISOU 2770  C   ASP B 101     2915   2865   2623    -72      0    115       C  
ATOM   2771  O   ASP B 101     -57.856  27.755  49.539  1.00 23.61           O  
ANISOU 2771  O   ASP B 101     3110   3050   2810    -79     -4    124       O  
ATOM   2772  CB  ASP B 101     -55.925  27.521  51.973  1.00 23.73           C  
ANISOU 2772  CB  ASP B 101     3143   3071   2801   -100    -23    138       C  
ATOM   2773  CG  ASP B 101     -56.472  28.321  53.113  1.00 25.08           C  
ANISOU 2773  CG  ASP B 101     3302   3271   2955   -116     -9    124       C  
ATOM   2774  OD1 ASP B 101     -56.442  29.566  53.001  1.00 26.39           O  
ANISOU 2774  OD1 ASP B 101     3452   3444   3133   -102      4    105       O  
ATOM   2775  OD2 ASP B 101     -56.913  27.720  54.131  1.00 29.27           O  
ANISOU 2775  OD2 ASP B 101     3842   3819   3462   -145    -12    131       O  
ATOM   2776  N   HIS B 102     -57.663  29.906  50.126  1.00 20.38           N  
ANISOU 2776  N   HIS B 102     2679   2657   2407    -65     13     95       N  
ATOM   2777  CA  HIS B 102     -58.945  30.296  49.520  1.00 21.12           C  
ANISOU 2777  CA  HIS B 102     2760   2760   2504    -59     22     81       C  
ATOM   2778  C   HIS B 102     -58.685  31.232  48.371  1.00 18.74           C  
ANISOU 2778  C   HIS B 102     2457   2439   2224    -31     24     73       C  
ATOM   2779  O   HIS B 102     -58.199  32.339  48.550  1.00 19.49           O  
ANISOU 2779  O   HIS B 102     2549   2531   2325    -21     28     62       O  
ATOM   2780  CB  HIS B 102     -59.881  30.975  50.513  1.00 21.16           C  
ANISOU 2780  CB  HIS B 102     2748   2797   2497    -71     33     59       C  
ATOM   2781  CG  HIS B 102     -60.339  30.072  51.613  1.00 25.06           C  
ANISOU 2781  CG  HIS B 102     3243   3313   2964   -105     34     65       C  
ATOM   2782  ND1 HIS B 102     -61.249  29.053  51.411  1.00 27.50           N  
ANISOU 2782  ND1 HIS B 102     3554   3631   3262   -124     33     71       N  
ATOM   2783  CD2 HIS B 102     -60.018  30.040  52.927  1.00 28.27           C  
ANISOU 2783  CD2 HIS B 102     3651   3737   3353   -127     35     66       C  
ATOM   2784  CE1 HIS B 102     -61.465  28.431  52.557  1.00 29.79           C  
ANISOU 2784  CE1 HIS B 102     3850   3942   3527   -158     34     77       C  
ATOM   2785  NE2 HIS B 102     -60.749  29.023  53.495  1.00 29.08           N  
ANISOU 2785  NE2 HIS B 102     3760   3858   3432   -160     35     74       N  
ATOM   2786  N   TRP B 103     -59.029  30.777  47.170  1.00 17.59           N  
ANISOU 2786  N   TRP B 103     2315   2280   2087    -22     20     79       N  
ATOM   2787  CA  TRP B 103     -58.748  31.510  45.957  1.00 18.42           C  
ANISOU 2787  CA  TRP B 103     2424   2365   2209      1     20     75       C  
ATOM   2788  C   TRP B 103     -59.988  32.139  45.365  1.00 17.50           C  
ANISOU 2788  C   TRP B 103     2298   2254   2097     14     22     59       C  
ATOM   2789  O   TRP B 103     -61.060  31.558  45.353  1.00 18.56           O  
ANISOU 2789  O   TRP B 103     2424   2404   2225      7     23     55       O  
ATOM   2790  CB  TRP B 103     -58.114  30.573  44.940  1.00 17.45           C  
ANISOU 2790  CB  TRP B 103     2314   2223   2095      5     12     92       C  
ATOM   2791  CG  TRP B 103     -56.712  30.139  45.331  1.00 16.99           C  
ANISOU 2791  CG  TRP B 103     2263   2155   2036      0      6    103       C  
ATOM   2792  CD1 TRP B 103     -56.364  29.288  46.362  1.00 17.41           C  
ANISOU 2792  CD1 TRP B 103     2321   2216   2079    -15     -1    112       C  
ATOM   2793  CD2 TRP B 103     -55.481  30.538  44.710  1.00 16.43           C  
ANISOU 2793  CD2 TRP B 103     2199   2069   1976     11      5    102       C  
ATOM   2794  NE1 TRP B 103     -55.004  29.135  46.397  1.00 16.44           N  
ANISOU 2794  NE1 TRP B 103     2204   2082   1960    -10     -8    116       N  
ATOM   2795  CE2 TRP B 103     -54.424  29.880  45.404  1.00 16.40           C  
ANISOU 2795  CE2 TRP B 103     2198   2064   1968      4     -3    109       C  
ATOM   2796  CE3 TRP B 103     -55.166  31.354  43.606  1.00 16.72           C  
ANISOU 2796  CE3 TRP B 103     2239   2092   2023     23      9     97       C  
ATOM   2797  CZ2 TRP B 103     -53.099  30.028  45.050  1.00 15.22           C  
ANISOU 2797  CZ2 TRP B 103     2051   1905   1827     11     -6    106       C  
ATOM   2798  CZ3 TRP B 103     -53.840  31.538  43.264  1.00 17.58           C  
ANISOU 2798  CZ3 TRP B 103     2352   2191   2136     25      9     95       C  
ATOM   2799  CH2 TRP B 103     -52.804  30.849  43.971  1.00 19.38           C  
ANISOU 2799  CH2 TRP B 103     2579   2423   2363     19      2     98       C  
ATOM   2800  N   GLY B 104     -59.839  33.361  44.887  1.00 17.42           N  
ANISOU 2800  N   GLY B 104     2291   2231   2097     32     22     48       N  
ATOM   2801  CA  GLY B 104     -60.846  33.936  44.010  1.00 17.85           C  
ANISOU 2801  CA  GLY B 104     2342   2281   2158     50     19     36       C  
ATOM   2802  C   GLY B 104     -60.939  33.213  42.690  1.00 18.11           C  
ANISOU 2802  C   GLY B 104     2384   2301   2198     56     14     49       C  
ATOM   2803  O   GLY B 104     -60.108  32.335  42.390  1.00 17.90           O  
ANISOU 2803  O   GLY B 104     2367   2265   2171     47     13     67       O  
ATOM   2804  N   GLN B 105     -61.954  33.574  41.907  1.00 18.55           N  
ANISOU 2804  N   GLN B 105     2436   2355   2257     72      9     37       N  
ATOM   2805  CA  GLN B 105     -62.215  32.897  40.622  1.00 20.27           C  
ANISOU 2805  CA  GLN B 105     2660   2563   2479     78      4     48       C  
ATOM   2806  C   GLN B 105     -61.308  33.342  39.481  1.00 20.57           C  
ANISOU 2806  C   GLN B 105     2719   2572   2525     88     -1     59       C  
ATOM   2807  O   GLN B 105     -61.336  32.749  38.403  1.00 20.97           O  
ANISOU 2807  O   GLN B 105     2776   2614   2578     90     -4     69       O  
ATOM   2808  CB  GLN B 105     -63.699  32.993  40.199  1.00 20.19           C  
ANISOU 2808  CB  GLN B 105     2636   2565   2469     91     -1     30       C  
ATOM   2809  CG  GLN B 105     -64.092  34.319  39.500  1.00 21.57           C  
ANISOU 2809  CG  GLN B 105     2819   2724   2652    118    -13     16       C  
ATOM   2810  CD  GLN B 105     -64.309  35.529  40.437  1.00 23.14           C  
ANISOU 2810  CD  GLN B 105     3011   2929   2852    128    -14     -6       C  
ATOM   2811  OE1 GLN B 105     -63.839  35.560  41.591  1.00 20.88           O  
ANISOU 2811  OE1 GLN B 105     2718   2655   2561    113     -5     -8       O  
ATOM   2812  NE2 GLN B 105     -65.056  36.514  39.949  1.00 24.54           N  
ANISOU 2812  NE2 GLN B 105     3190   3097   3036    153    -28    -25       N  
ATOM   2813  N   GLY B 106     -60.501  34.380  39.720  1.00 19.01           N  
ANISOU 2813  N   GLY B 106     2533   2362   2330     91      0     57       N  
ATOM   2814  CA  GLY B 106     -59.597  34.898  38.706  1.00 18.85           C  
ANISOU 2814  CA  GLY B 106     2534   2316   2312     94     -2     66       C  
ATOM   2815  C   GLY B 106     -60.270  36.039  37.969  1.00 18.86           C  
ANISOU 2815  C   GLY B 106     2548   2301   2317    113    -12     57       C  
ATOM   2816  O   GLY B 106     -61.517  36.084  37.879  1.00 20.30           O  
ANISOU 2816  O   GLY B 106     2720   2492   2500    127    -20     45       O  
ATOM   2817  N   THR B 107     -59.437  36.972  37.517  1.00 18.82           N  
ANISOU 2817  N   THR B 107     2566   2274   2312    112    -14     61       N  
ATOM   2818  CA  THR B 107     -59.877  38.079  36.661  1.00 18.89           C  
ANISOU 2818  CA  THR B 107     2597   2258   2321    128    -27     57       C  
ATOM   2819  C   THR B 107     -59.001  38.077  35.429  1.00 17.71           C  
ANISOU 2819  C   THR B 107     2473   2090   2167    117    -27     73       C  
ATOM   2820  O   THR B 107     -57.785  38.343  35.510  1.00 18.09           O  
ANISOU 2820  O   THR B 107     2531   2132   2212     99    -17     79       O  
ATOM   2821  CB  THR B 107     -59.782  39.484  37.373  1.00 19.10           C  
ANISOU 2821  CB  THR B 107     2635   2273   2350    135    -32     44       C  
ATOM   2822  OG1 THR B 107     -60.640  39.506  38.524  1.00 20.37           O  
ANISOU 2822  OG1 THR B 107     2769   2456   2514    145    -32     25       O  
ATOM   2823  CG2 THR B 107     -60.258  40.611  36.433  1.00 21.67           C  
ANISOU 2823  CG2 THR B 107     2990   2569   2676    153    -52     41       C  
ATOM   2824  N   LEU B 108     -59.641  37.843  34.270  1.00 17.30           N  
ANISOU 2824  N   LEU B 108     2429   2031   2113    126    -37     78       N  
ATOM   2825  CA  LEU B 108     -58.948  37.929  33.000  1.00 18.67           C  
ANISOU 2825  CA  LEU B 108     2627   2187   2280    115    -37     91       C  
ATOM   2826  C   LEU B 108     -58.704  39.390  32.618  1.00 17.95           C  
ANISOU 2826  C   LEU B 108     2572   2066   2183    116    -47     92       C  
ATOM   2827  O   LEU B 108     -59.672  40.159  32.549  1.00 20.28           O  
ANISOU 2827  O   LEU B 108     2878   2348   2481    138    -66     84       O  
ATOM   2828  CB  LEU B 108     -59.712  37.206  31.881  1.00 19.14           C  
ANISOU 2828  CB  LEU B 108     2685   2249   2338    123    -45     96       C  
ATOM   2829  CG  LEU B 108     -59.042  37.318  30.513  1.00 20.71           C  
ANISOU 2829  CG  LEU B 108     2911   2432   2527    110    -46    109       C  
ATOM   2830  CD1 LEU B 108     -57.610  36.733  30.494  1.00 23.67           C  
ANISOU 2830  CD1 LEU B 108     3281   2815   2898     82    -27    115       C  
ATOM   2831  CD2 LEU B 108     -59.922  36.667  29.440  1.00 22.39           C  
ANISOU 2831  CD2 LEU B 108     3122   2648   2738    121    -55    113       C  
ATOM   2832  N   VAL B 109     -57.435  39.748  32.440  1.00 17.81           N  
ANISOU 2832  N   VAL B 109     2571   2039   2157     91    -37     99       N  
ATOM   2833  CA  VAL B 109     -57.105  41.072  31.887  1.00 19.33           C  
ANISOU 2833  CA  VAL B 109     2804   2201   2340     85    -46    102       C  
ATOM   2834  C   VAL B 109     -56.484  40.820  30.539  1.00 19.75           C  
ANISOU 2834  C   VAL B 109     2878   2247   2379     63    -42    115       C  
ATOM   2835  O   VAL B 109     -55.412  40.227  30.451  1.00 18.63           O  
ANISOU 2835  O   VAL B 109     2726   2120   2233     39    -24    117       O  
ATOM   2836  CB  VAL B 109     -56.154  41.864  32.750  1.00 19.62           C  
ANISOU 2836  CB  VAL B 109     2847   2231   2375     69    -36     97       C  
ATOM   2837  CG1 VAL B 109     -55.938  43.221  32.114  1.00 20.29           C  
ANISOU 2837  CG1 VAL B 109     2980   2282   2449     61    -48    102       C  
ATOM   2838  CG2 VAL B 109     -56.741  42.056  34.139  1.00 20.70           C  
ANISOU 2838  CG2 VAL B 109     2961   2380   2524     88    -38     82       C  
ATOM   2839  N   THR B 110     -57.175  41.223  29.466  1.00 20.31           N  
ANISOU 2839  N   THR B 110     2977   2298   2443     73    -61    123       N  
ATOM   2840  CA  THR B 110     -56.598  41.124  28.146  1.00 20.89           C  
ANISOU 2840  CA  THR B 110     3074   2364   2499     49    -58    135       C  
ATOM   2841  C   THR B 110     -56.007  42.451  27.731  1.00 21.81           C  
ANISOU 2841  C   THR B 110     3238   2449   2599     28    -64    142       C  
ATOM   2842  O   THR B 110     -56.716  43.461  27.663  1.00 22.44           O  
ANISOU 2842  O   THR B 110     3348   2499   2678     46    -88    143       O  
ATOM   2843  CB  THR B 110     -57.655  40.682  27.151  1.00 20.69           C  
ANISOU 2843  CB  THR B 110     3053   2337   2473     68    -74    141       C  
ATOM   2844  OG1 THR B 110     -58.256  39.438  27.553  1.00 21.94           O  
ANISOU 2844  OG1 THR B 110     3167   2523   2645     84    -68    134       O  
ATOM   2845  CG2 THR B 110     -57.037  40.508  25.794  1.00 21.03           C  
ANISOU 2845  CG2 THR B 110     3118   2375   2496     40    -70    153       C  
ATOM   2846  N   VAL B 111     -54.715  42.451  27.445  1.00 22.18           N  
ANISOU 2846  N   VAL B 111     3293   2503   2632    -10    -44    144       N  
ATOM   2847  CA  VAL B 111     -54.037  43.684  27.068  1.00 23.97           C  
ANISOU 2847  CA  VAL B 111     3567   2701   2840    -38    -47    150       C  
ATOM   2848  C   VAL B 111     -53.895  43.707  25.546  1.00 24.97           C  
ANISOU 2848  C   VAL B 111     3727   2818   2943    -61    -51    164       C  
ATOM   2849  O   VAL B 111     -53.014  43.092  24.986  1.00 25.66           O  
ANISOU 2849  O   VAL B 111     3804   2928   3019    -92    -31    163       O  
ATOM   2850  CB  VAL B 111     -52.684  43.887  27.749  1.00 23.87           C  
ANISOU 2850  CB  VAL B 111     3546   2702   2823    -69    -22    141       C  
ATOM   2851  CG1 VAL B 111     -52.163  45.266  27.404  1.00 25.36           C  
ANISOU 2851  CG1 VAL B 111     3787   2858   2991    -98    -27    147       C  
ATOM   2852  CG2 VAL B 111     -52.805  43.764  29.295  1.00 23.87           C  
ANISOU 2852  CG2 VAL B 111     3509   2715   2845    -47    -17    128       C  
ATOM   2853  N   SER B 112     -54.791  44.447  24.906  1.00 25.54           N  
ANISOU 2853  N   SER B 112     3840   2858   3008    -46    -79    175       N  
ATOM   2854  CA  SER B 112     -54.870  44.495  23.442  1.00 26.65           C  
ANISOU 2854  CA  SER B 112     4015   2985   3124    -64    -89    190       C  
ATOM   2855  C   SER B 112     -55.584  45.778  23.020  1.00 28.18           C  
ANISOU 2855  C   SER B 112     4267   3131   3307    -52   -124    201       C  
ATOM   2856  O   SER B 112     -56.431  46.282  23.735  1.00 28.95           O  
ANISOU 2856  O   SER B 112     4366   3212   3423    -14   -145    195       O  
ATOM   2857  CB  SER B 112     -55.637  43.270  22.925  1.00 27.34           C  
ANISOU 2857  CB  SER B 112     4070   3098   3222    -41    -91    189       C  
ATOM   2858  OG  SER B 112     -55.777  43.343  21.507  1.00 28.59           O  
ANISOU 2858  OG  SER B 112     4263   3245   3356    -57   -102    203       O  
ATOM   2859  N   SER B 113     -55.261  46.267  21.833  1.00 29.72           N  
ANISOU 2859  N   SER B 113     4513   3307   3473    -84   -132    217       N  
ATOM   2860  CA  SER B 113     -55.950  47.445  21.293  1.00 31.42           C  
ANISOU 2860  CA  SER B 113     4792   3472   3675    -73   -170    231       C  
ATOM   2861  C   SER B 113     -57.157  47.026  20.441  1.00 31.27           C  
ANISOU 2861  C   SER B 113     4775   3448   3657    -39   -198    238       C  
ATOM   2862  O   SER B 113     -57.878  47.901  19.908  1.00 32.05           O  
ANISOU 2862  O   SER B 113     4925   3506   3746    -22   -236    248       O  
ATOM   2863  CB  SER B 113     -54.973  48.292  20.473  1.00 32.20           C  
ANISOU 2863  CB  SER B 113     4951   3547   3736   -130   -167    247       C  
ATOM   2864  OG  SER B 113     -54.438  47.510  19.426  1.00 35.61           O  
ANISOU 2864  OG  SER B 113     5376   4006   4146   -166   -147    253       O  
ATOM   2865  N   ALA B 114     -57.384  45.712  20.320  1.00 29.59           N  
ANISOU 2865  N   ALA B 114     4510   3277   3457    -28   -180    230       N  
ATOM   2866  CA  ALA B 114     -58.504  45.167  19.542  1.00 29.69           C  
ANISOU 2866  CA  ALA B 114     4517   3293   3472      3   -202    233       C  
ATOM   2867  C   ALA B 114     -59.848  45.588  20.100  1.00 30.16           C  
ANISOU 2867  C   ALA B 114     4573   3334   3553     60   -236    223       C  
ATOM   2868  O   ALA B 114     -59.997  45.784  21.310  1.00 29.13           O  
ANISOU 2868  O   ALA B 114     4417   3206   3446     82   -233    208       O  
ATOM   2869  CB  ALA B 114     -58.432  43.623  19.468  1.00 29.31           C  
ANISOU 2869  CB  ALA B 114     4408   3293   3434      3   -174    224       C  
ATOM   2870  N   SER B 115     -60.833  45.690  19.216  1.00 31.14           N  
ANISOU 2870  N   SER B 115     4719   3441   3670     85   -269    229       N  
ATOM   2871  CA ASER B 115     -62.198  46.037  19.608  0.50 32.13           C  
ANISOU 2871  CA ASER B 115     4839   3553   3817    143   -304    214       C  
ATOM   2872  CA BSER B 115     -62.204  46.040  19.593  0.50 31.49           C  
ANISOU 2872  CA BSER B 115     4758   3472   3736    143   -305    214       C  
ATOM   2873  C   SER B 115     -63.031  44.808  19.980  1.00 31.63           C  
ANISOU 2873  C   SER B 115     4708   3532   3777    174   -293    195       C  
ATOM   2874  O   SER B 115     -62.875  43.730  19.386  1.00 30.78           O  
ANISOU 2874  O   SER B 115     4576   3455   3665    158   -273    200       O  
ATOM   2875  CB ASER B 115     -62.895  46.829  18.495  0.50 33.17           C  
ANISOU 2875  CB ASER B 115     5030   3644   3929    158   -350    227       C  
ATOM   2876  CB BSER B 115     -62.904  46.783  18.447  0.50 32.39           C  
ANISOU 2876  CB BSER B 115     4931   3547   3830    157   -350    227       C  
ATOM   2877  OG ASER B 115     -62.668  46.248  17.222  0.50 35.17           O  
ANISOU 2877  OG ASER B 115     5297   3908   4159    130   -344    244       O  
ATOM   2878  OG BSER B 115     -62.272  48.021  18.156  0.50 30.92           O  
ANISOU 2878  OG BSER B 115     4813   3314   3621    131   -366    245       O  
ATOM   2879  N   THR B 116     -63.908  44.965  20.974  1.00 32.13           N  
ANISOU 2879  N   THR B 116     4742   3600   3865    216   -306    173       N  
ATOM   2880  CA  THR B 116     -64.838  43.896  21.364  1.00 32.03           C  
ANISOU 2880  CA  THR B 116     4669   3627   3873    245   -299    153       C  
ATOM   2881  C   THR B 116     -65.698  43.525  20.159  1.00 32.52           C  
ANISOU 2881  C   THR B 116     4740   3690   3927    262   -322    156       C  
ATOM   2882  O   THR B 116     -66.207  44.403  19.439  1.00 33.30           O  
ANISOU 2882  O   THR B 116     4885   3754   4014    281   -361    161       O  
ATOM   2883  CB  THR B 116     -65.710  44.310  22.567  1.00 32.14           C  
ANISOU 2883  CB  THR B 116     4656   3644   3912    286   -313    124       C  
ATOM   2884  OG1 THR B 116     -64.865  44.401  23.717  1.00 34.69           O  
ANISOU 2884  OG1 THR B 116     4963   3976   4243    266   -286    121       O  
ATOM   2885  CG2 THR B 116     -66.843  43.293  22.853  1.00 31.66           C  
ANISOU 2885  CG2 THR B 116     4538   3623   3868    316   -311    101       C  
ATOM   2886  N   LYS B 117     -65.826  42.222  19.918  1.00 31.11           N  
ANISOU 2886  N   LYS B 117     4518   3549   3751    256   -299    154       N  
ATOM   2887  CA  LYS B 117     -66.542  41.728  18.753  1.00 31.25           C  
ANISOU 2887  CA  LYS B 117     4539   3573   3760    267   -315    157       C  
ATOM   2888  C   LYS B 117     -67.107  40.348  19.052  1.00 29.96           C  
ANISOU 2888  C   LYS B 117     4314   3456   3614    276   -294    141       C  
ATOM   2889  O   LYS B 117     -66.386  39.464  19.509  1.00 29.32           O  
ANISOU 2889  O   LYS B 117     4201   3400   3538    250   -258    143       O  
ATOM   2890  CB  LYS B 117     -65.603  41.674  17.544  1.00 30.77           C  
ANISOU 2890  CB  LYS B 117     4518   3502   3671    225   -307    184       C  
ATOM   2891  CG  LYS B 117     -66.234  41.114  16.288  1.00 32.58           C  
ANISOU 2891  CG  LYS B 117     4751   3740   3888    231   -321    189       C  
ATOM   2892  CD  LYS B 117     -65.238  41.029  15.151  1.00 35.13           C  
ANISOU 2892  CD  LYS B 117     5109   4058   4182    185   -308    213       C  
ATOM   2893  CE  LYS B 117     -65.845  40.354  13.915  1.00 36.21           C  
ANISOU 2893  CE  LYS B 117     5244   4207   4306    189   -319    216       C  
ATOM   2894  NZ  LYS B 117     -66.552  39.041  14.194  1.00 35.72           N  
ANISOU 2894  NZ  LYS B 117     5118   4187   4266    210   -303    197       N  
ATOM   2895  N   GLY B 118     -68.400  40.174  18.822  1.00 30.04           N  
ANISOU 2895  N   GLY B 118     4307   3476   3632    314   -318    123       N  
ATOM   2896  CA  GLY B 118     -69.000  38.857  18.973  1.00 28.63           C  
ANISOU 2896  CA  GLY B 118     4074   3340   3465    319   -299    108       C  
ATOM   2897  C   GLY B 118     -68.576  37.893  17.865  1.00 27.87           C  
ANISOU 2897  C   GLY B 118     3977   3257   3355    292   -283    125       C  
ATOM   2898  O   GLY B 118     -68.104  38.312  16.798  1.00 29.12           O  
ANISOU 2898  O   GLY B 118     4178   3393   3491    275   -293    145       O  
ATOM   2899  N   PRO B 119     -68.729  36.585  18.123  1.00 26.72           N  
ANISOU 2899  N   PRO B 119     3784   3148   3221    284   -257    116       N  
ATOM   2900  CA  PRO B 119     -68.294  35.617  17.137  1.00 26.40           C  
ANISOU 2900  CA  PRO B 119     3739   3121   3169    259   -241    128       C  
ATOM   2901  C   PRO B 119     -69.343  35.393  16.075  1.00 24.51           C  
ANISOU 2901  C   PRO B 119     3502   2888   2923    280   -264    122       C  
ATOM   2902  O   PRO B 119     -70.552  35.571  16.316  1.00 26.27           O  
ANISOU 2902  O   PRO B 119     3709   3118   3156    316   -286    102       O  
ATOM   2903  CB  PRO B 119     -68.144  34.312  17.946  1.00 25.16           C  
ANISOU 2903  CB  PRO B 119     3533   2999   3030    246   -209    119       C  
ATOM   2904  CG  PRO B 119     -69.051  34.474  19.131  1.00 23.86           C  
ANISOU 2904  CG  PRO B 119     3340   2845   2882    273   -214     97       C  
ATOM   2905  CD  PRO B 119     -69.076  35.965  19.418  1.00 26.73           C  
ANISOU 2905  CD  PRO B 119     3736   3176   3242    291   -239     96       C  
ATOM   2906  N   SER B 120     -68.866  34.979  14.911  1.00 24.08           N  
ANISOU 2906  N   SER B 120     3463   2834   2851    257   -259    138       N  
ATOM   2907  CA  SER B 120     -69.719  34.323  13.957  1.00 23.85           C  
ANISOU 2907  CA  SER B 120     3422   2821   2817    270   -270    131       C  
ATOM   2908  C   SER B 120     -69.704  32.847  14.287  1.00 21.68           C  
ANISOU 2908  C   SER B 120     3097   2583   2558    257   -239    121       C  
ATOM   2909  O   SER B 120     -68.649  32.296  14.540  1.00 24.70           O  
ANISOU 2909  O   SER B 120     3471   2971   2941    226   -210    130       O  
ATOM   2910  CB  SER B 120     -69.224  34.516  12.530  1.00 23.24           C  
ANISOU 2910  CB  SER B 120     3386   2732   2714    248   -278    152       C  
ATOM   2911  OG  SER B 120     -69.374  35.863  12.128  1.00 28.33           O  
ANISOU 2911  OG  SER B 120     4082   3340   3342    261   -312    162       O  
ATOM   2912  N   VAL B 121     -70.868  32.239  14.259  1.00 21.57           N  
ANISOU 2912  N   VAL B 121     3051   2591   2553    280   -246    102       N  
ATOM   2913  CA  VAL B 121     -71.007  30.801  14.530  1.00 21.16           C  
ANISOU 2913  CA  VAL B 121     2954   2572   2514    268   -220     92       C  
ATOM   2914  C   VAL B 121     -71.471  30.027  13.299  1.00 20.63           C  
ANISOU 2914  C   VAL B 121     2880   2520   2438    267   -224     89       C  
ATOM   2915  O   VAL B 121     -72.568  30.255  12.765  1.00 22.05           O  
ANISOU 2915  O   VAL B 121     3059   2704   2614    294   -248     77       O  
ATOM   2916  CB  VAL B 121     -71.997  30.573  15.673  1.00 20.91           C  
ANISOU 2916  CB  VAL B 121     2885   2559   2501    289   -219     67       C  
ATOM   2917  CG1 VAL B 121     -72.160  29.069  15.987  1.00 22.46           C  
ANISOU 2917  CG1 VAL B 121     3039   2786   2708    273   -193     58       C  
ATOM   2918  CG2 VAL B 121     -71.535  31.293  16.922  1.00 22.91           C  
ANISOU 2918  CG2 VAL B 121     3142   2800   2762    289   -214     68       C  
ATOM   2919  N   PHE B 122     -70.653  29.045  12.906  1.00 19.78           N  
ANISOU 2919  N   PHE B 122     2763   2423   2329    236   -199     98       N  
ATOM   2920  CA  PHE B 122     -70.915  28.310  11.665  1.00 19.72           C  
ANISOU 2920  CA  PHE B 122     2752   2430   2312    231   -200     97       C  
ATOM   2921  C   PHE B 122     -71.044  26.821  11.975  1.00 20.93           C  
ANISOU 2921  C   PHE B 122     2862   2610   2481    219   -176     85       C  
ATOM   2922  O   PHE B 122     -70.273  26.290  12.763  1.00 19.77           O  
ANISOU 2922  O   PHE B 122     2701   2464   2345    201   -154     88       O  
ATOM   2923  CB  PHE B 122     -69.814  28.522  10.640  1.00 20.64           C  
ANISOU 2923  CB  PHE B 122     2900   2534   2408    203   -196    116       C  
ATOM   2924  CG  PHE B 122     -69.587  29.974  10.271  1.00 20.13           C  
ANISOU 2924  CG  PHE B 122     2886   2440   2325    207   -219    132       C  
ATOM   2925  CD1 PHE B 122     -70.622  30.752   9.724  1.00 21.65           C  
ANISOU 2925  CD1 PHE B 122     3100   2621   2507    237   -254    129       C  
ATOM   2926  CD2 PHE B 122     -68.362  30.557  10.490  1.00 21.93           C  
ANISOU 2926  CD2 PHE B 122     3139   2650   2544    181   -208    147       C  
ATOM   2927  CE1 PHE B 122     -70.392  32.124   9.407  1.00 18.36           C  
ANISOU 2927  CE1 PHE B 122     2734   2170   2070    240   -279    145       C  
ATOM   2928  CE2 PHE B 122     -68.138  31.899  10.172  1.00 22.66           C  
ANISOU 2928  CE2 PHE B 122     3281   2712   2616    181   -229    162       C  
ATOM   2929  CZ  PHE B 122     -69.162  32.663   9.608  1.00 21.80           C  
ANISOU 2929  CZ  PHE B 122     3198   2588   2497    210   -266    162       C  
ATOM   2930  N   PRO B 123     -72.025  26.149  11.356  1.00 20.98           N  
ANISOU 2930  N   PRO B 123     2848   2636   2488    230   -183     71       N  
ATOM   2931  CA  PRO B 123     -72.122  24.726  11.641  1.00 21.31           C  
ANISOU 2931  CA  PRO B 123     2853   2699   2543    216   -161     60       C  
ATOM   2932  C   PRO B 123     -71.031  23.882  10.969  1.00 22.22           C  
ANISOU 2932  C   PRO B 123     2970   2816   2656    187   -143     70       C  
ATOM   2933  O   PRO B 123     -70.558  24.185   9.849  1.00 22.26           O  
ANISOU 2933  O   PRO B 123     2997   2816   2644    178   -148     79       O  
ATOM   2934  CB  PRO B 123     -73.521  24.385  11.114  1.00 23.06           C  
ANISOU 2934  CB  PRO B 123     3055   2942   2764    236   -175     41       C  
ATOM   2935  CG  PRO B 123     -73.625  25.288   9.867  1.00 22.96           C  
ANISOU 2935  CG  PRO B 123     3076   2917   2731    249   -200     50       C  
ATOM   2936  CD  PRO B 123     -72.892  26.548  10.229  1.00 22.85           C  
ANISOU 2936  CD  PRO B 123     3098   2875   2710    250   -209     67       C  
ATOM   2937  N   LEU B 124     -70.607  22.824  11.655  1.00 21.54           N  
ANISOU 2937  N   LEU B 124     2861   2738   2586    171   -122     66       N  
ATOM   2938  CA  LEU B 124     -69.727  21.826  11.037  1.00 20.20           C  
ANISOU 2938  CA  LEU B 124     2684   2573   2417    148   -106     67       C  
ATOM   2939  C   LEU B 124     -70.564  20.558  10.910  1.00 20.17           C  
ANISOU 2939  C   LEU B 124     2651   2589   2425    149   -102     52       C  
ATOM   2940  O   LEU B 124     -70.705  19.837  11.871  1.00 18.71           O  
ANISOU 2940  O   LEU B 124     2447   2407   2254    144    -92     46       O  
ATOM   2941  CB  LEU B 124     -68.447  21.611  11.883  1.00 19.69           C  
ANISOU 2941  CB  LEU B 124     2621   2498   2364    131    -90     74       C  
ATOM   2942  CG  LEU B 124     -67.607  22.868  12.149  1.00 21.58           C  
ANISOU 2942  CG  LEU B 124     2887   2719   2593    128    -92     88       C  
ATOM   2943  CD1 LEU B 124     -66.549  22.603  13.210  1.00 23.02           C  
ANISOU 2943  CD1 LEU B 124     3064   2894   2788    115    -77     91       C  
ATOM   2944  CD2 LEU B 124     -66.911  23.305  10.857  1.00 24.24           C  
ANISOU 2944  CD2 LEU B 124     3248   3054   2910    113    -94     95       C  
ATOM   2945  N   ALA B 125     -71.158  20.354   9.732  1.00 19.85           N  
ANISOU 2945  N   ALA B 125     2608   2560   2373    153   -110     45       N  
ATOM   2946  CA  ALA B 125     -72.223  19.353   9.516  1.00 20.19           C  
ANISOU 2946  CA  ALA B 125     2625   2624   2423    157   -110     28       C  
ATOM   2947  C   ALA B 125     -71.649  17.966   9.558  1.00 19.90           C  
ANISOU 2947  C   ALA B 125     2571   2591   2400    136    -92     23       C  
ATOM   2948  O   ALA B 125     -70.514  17.753   9.103  1.00 20.21           O  
ANISOU 2948  O   ALA B 125     2618   2623   2438    121    -85     29       O  
ATOM   2949  CB  ALA B 125     -72.911  19.578   8.153  1.00 20.95           C  
ANISOU 2949  CB  ALA B 125     2725   2731   2502    168   -125     22       C  
ATOM   2950  N   PRO B 126     -72.430  17.011  10.093  1.00 18.88           N  
ANISOU 2950  N   PRO B 126     2419   2473   2283    133    -87     10       N  
ATOM   2951  CA  PRO B 126     -71.952  15.636  10.035  1.00 20.15           C  
ANISOU 2951  CA  PRO B 126     2566   2633   2456    115    -75      5       C  
ATOM   2952  C   PRO B 126     -71.867  15.168   8.585  1.00 21.65           C  
ANISOU 2952  C   PRO B 126     2753   2834   2639    111    -76     -2       C  
ATOM   2953  O   PRO B 126     -72.794  15.437   7.810  1.00 24.79           O  
ANISOU 2953  O   PRO B 126     3147   3247   3025    122    -85    -10       O  
ATOM   2954  CB  PRO B 126     -73.046  14.862  10.781  1.00 20.01           C  
ANISOU 2954  CB  PRO B 126     2528   2627   2447    111    -71     -7       C  
ATOM   2955  CG  PRO B 126     -74.286  15.719  10.651  1.00 19.24           C  
ANISOU 2955  CG  PRO B 126     2426   2547   2339    131    -83    -16       C  
ATOM   2956  CD  PRO B 126     -73.790  17.128  10.662  1.00 19.56           C  
ANISOU 2956  CD  PRO B 126     2489   2574   2370    146    -93     -3       C  
ATOM   2957  N   SER B 127     -70.792  14.439   8.270  1.00 23.12           N  
ANISOU 2957  N   SER B 127     2939   3014   2832     96    -67     -3       N  
ATOM   2958  CA  SER B 127     -70.490  13.988   6.900  1.00 24.15           C  
ANISOU 2958  CA  SER B 127     3065   3154   2955     89    -67    -12       C  
ATOM   2959  C   SER B 127     -71.624  13.138   6.307  1.00 25.27           C  
ANISOU 2959  C   SER B 127     3188   3314   3099     90    -69    -27       C  
ATOM   2960  O   SER B 127     -72.201  12.294   6.988  1.00 25.32           O  
ANISOU 2960  O   SER B 127     3180   3321   3118     86    -65    -35       O  
ATOM   2961  CB  SER B 127     -69.153  13.211   6.855  1.00 24.15           C  
ANISOU 2961  CB  SER B 127     3062   3147   2968     73    -57    -16       C  
ATOM   2962  OG  SER B 127     -68.846  12.741   5.545  1.00 27.53           O  
ANISOU 2962  OG  SER B 127     3484   3588   3390     65    -55    -29       O  
ATOM   2963  N   SER B 128     -71.883  13.332   5.011  1.00 25.83           N  
ANISOU 2963  N   SER B 128     3259   3400   3154     93    -74    -33       N  
ATOM   2964  CA  SER B 128     -72.844  12.482   4.296  1.00 27.20           C  
ANISOU 2964  CA  SER B 128     3414   3593   3329     93    -75    -50       C  
ATOM   2965  C   SER B 128     -72.322  11.054   4.252  1.00 27.66           C  
ANISOU 2965  C   SER B 128     3457   3648   3405     76    -65    -63       C  
ATOM   2966  O   SER B 128     -73.090  10.095   4.045  1.00 28.33           O  
ANISOU 2966  O   SER B 128     3524   3744   3496     72    -63    -78       O  
ATOM   2967  CB  SER B 128     -73.072  12.996   2.863  1.00 27.65           C  
ANISOU 2967  CB  SER B 128     3477   3665   3362     97    -84    -52       C  
ATOM   2968  OG  SER B 128     -71.872  12.937   2.119  1.00 30.35           O  
ANISOU 2968  OG  SER B 128     3827   4006   3698     82    -78    -51       O  
ATOM   2969  N   LYS B 129     -71.020  10.908   4.468  1.00 27.07           N  
ANISOU 2969  N   LYS B 129     3389   3559   3338     67    -59    -58       N  
ATOM   2970  CA  LYS B 129     -70.387   9.603   4.448  1.00 27.81           C  
ANISOU 2970  CA  LYS B 129     3470   3646   3450     55    -53    -72       C  
ATOM   2971  C   LYS B 129     -70.241   8.964   5.837  1.00 27.37           C  
ANISOU 2971  C   LYS B 129     3414   3569   3415     52    -51    -68       C  
ATOM   2972  O   LYS B 129     -69.569   7.935   5.978  1.00 27.89           O  
ANISOU 2972  O   LYS B 129     3476   3623   3499     44    -50    -78       O  
ATOM   2973  CB  LYS B 129     -69.023   9.713   3.775  1.00 27.97           C  
ANISOU 2973  CB  LYS B 129     3493   3666   3467     48    -49    -77       C  
ATOM   2974  CG  LYS B 129     -69.109  10.217   2.342  1.00 30.61           C  
ANISOU 2974  CG  LYS B 129     3829   4023   3778     45    -50    -81       C  
ATOM   2975  CD  LYS B 129     -67.769  10.123   1.660  1.00 34.26           C  
ANISOU 2975  CD  LYS B 129     4290   4490   4237     31    -43    -92       C  
ATOM   2976  CE  LYS B 129     -67.713  11.003   0.425  1.00 36.43           C  
ANISOU 2976  CE  LYS B 129     4576   4785   4481     24    -44    -89       C  
ATOM   2977  NZ  LYS B 129     -68.787  10.712  -0.568  1.00 40.61           N  
ANISOU 2977  NZ  LYS B 129     5097   5333   4999     27    -49    -97       N  
ATOM   2978  N   SER B 130     -70.865   9.560   6.852  1.00 26.91           N  
ANISOU 2978  N   SER B 130     3364   3507   3355     57    -53    -55       N  
ATOM   2979  CA ASER B 130     -70.872   8.982   8.200  0.50 26.88           C  
ANISOU 2979  CA ASER B 130     3363   3485   3366     51    -52    -50       C  
ATOM   2980  CA BSER B 130     -70.818   9.006   8.196  0.50 26.32           C  
ANISOU 2980  CA BSER B 130     3292   3413   3295     51    -52    -50       C  
ATOM   2981  C   SER B 130     -71.162   7.510   8.126  1.00 27.14           C  
ANISOU 2981  C   SER B 130     3386   3514   3414     38    -51    -64       C  
ATOM   2982  O   SER B 130     -72.134   7.115   7.476  1.00 27.57           O  
ANISOU 2982  O   SER B 130     3427   3585   3462     36    -50    -76       O  
ATOM   2983  CB ASER B 130     -71.974   9.600   9.052  0.50 26.90           C  
ANISOU 2983  CB ASER B 130     3366   3494   3361     55    -52    -43       C  
ATOM   2984  CB BSER B 130     -71.762   9.774   9.136  0.50 26.27           C  
ANISOU 2984  CB BSER B 130     3289   3411   3281     56    -52    -40       C  
ATOM   2985  OG ASER B 130     -71.865   9.155  10.389  0.30 27.12           O  
ANISOU 2985  OG ASER B 130     3400   3506   3400     45    -50    -36       O  
ATOM   2986  OG BSER B 130     -71.408  11.155   9.237  0.70 23.18           O  
ANISOU 2986  OG BSER B 130     2910   3019   2879     69    -54    -28       O  
ATOM   2987  N   THR B 131     -70.340   6.703   8.795  1.00 27.51           N  
ANISOU 2987  N   THR B 131     3439   3537   3477     31    -54    -64       N  
ATOM   2988  CA  THR B 131     -70.464   5.250   8.749  1.00 27.42           C  
ANISOU 2988  CA  THR B 131     3423   3514   3481     19    -57    -76       C  
ATOM   2989  C   THR B 131     -71.771   4.791   9.358  1.00 27.77           C  
ANISOU 2989  C   THR B 131     3466   3563   3522      5    -55    -76       C  
ATOM   2990  O   THR B 131     -72.092   5.165  10.483  1.00 26.87           O  
ANISOU 2990  O   THR B 131     3361   3444   3403      1    -53    -63       O  
ATOM   2991  CB  THR B 131     -69.270   4.584   9.435  1.00 28.31           C  
ANISOU 2991  CB  THR B 131     3548   3598   3612     17    -65    -75       C  
ATOM   2992  OG1 THR B 131     -68.074   5.007   8.759  1.00 30.11           O  
ANISOU 2992  OG1 THR B 131     3771   3828   3842     28    -66    -82       O  
ATOM   2993  CG2 THR B 131     -69.367   3.055   9.362  1.00 27.85           C  
ANISOU 2993  CG2 THR B 131     3489   3522   3570      6    -73    -89       C  
ATOM   2994  N   SER B 132     -72.514   4.000   8.588  1.00 27.56           N  
ANISOU 2994  N   SER B 132     3427   3548   3495     -2    -53    -92       N  
ATOM   2995  CA ASER B 132     -73.759   3.412   9.074  0.50 28.05           C  
ANISOU 2995  CA ASER B 132     3487   3618   3554    -20    -50    -97       C  
ATOM   2996  CA BSER B 132     -73.763   3.386   9.045  0.50 27.94           C  
ANISOU 2996  CA BSER B 132     3472   3603   3540    -20    -50    -97       C  
ATOM   2997  C   SER B 132     -73.502   2.456  10.235  1.00 27.80           C  
ANISOU 2997  C   SER B 132     3473   3554   3533    -40    -54    -89       C  
ATOM   2998  O   SER B 132     -72.709   1.509  10.127  1.00 28.32           O  
ANISOU 2998  O   SER B 132     3548   3595   3616    -42    -64    -93       O  
ATOM   2999  CB ASER B 132     -74.507   2.719   7.938  0.50 28.13           C  
ANISOU 2999  CB ASER B 132     3480   3646   3562    -26    -47   -117       C  
ATOM   3000  CB BSER B 132     -74.415   2.618   7.889  0.50 28.01           C  
ANISOU 3000  CB BSER B 132     3466   3629   3549    -26    -48   -118       C  
ATOM   3001  OG ASER B 132     -75.051   3.687   7.059  0.50 29.41           O  
ANISOU 3001  OG ASER B 132     3627   3839   3709    -10    -44   -123       O  
ATOM   3002  OG BSER B 132     -75.777   2.326   8.152  0.50 28.73           O  
ANISOU 3002  OG BSER B 132     3547   3737   3630    -42    -42   -126       O  
ATOM   3003  N   GLY B 133     -74.172   2.721  11.350  1.00 27.00           N  
ANISOU 3003  N   GLY B 133     3379   3456   3423    -53    -50    -79       N  
ATOM   3004  CA  GLY B 133     -73.978   1.937  12.570  1.00 26.72           C  
ANISOU 3004  CA  GLY B 133     3366   3392   3394    -74    -55    -68       C  
ATOM   3005  C   GLY B 133     -72.715   2.338  13.322  1.00 25.90           C  
ANISOU 3005  C   GLY B 133     3280   3263   3298    -62    -64    -51       C  
ATOM   3006  O   GLY B 133     -72.340   1.708  14.318  1.00 27.36           O  
ANISOU 3006  O   GLY B 133     3487   3420   3489    -76    -72    -40       O  
ATOM   3007  N   GLY B 134     -72.053   3.386  12.838  1.00 24.67           N  
ANISOU 3007  N   GLY B 134     3116   3117   3142    -37    -62    -48       N  
ATOM   3008  CA  GLY B 134     -70.829   3.887  13.436  1.00 22.67           C  
ANISOU 3008  CA  GLY B 134     2875   2844   2895    -25    -69    -35       C  
ATOM   3009  C   GLY B 134     -71.012   5.218  14.141  1.00 22.33           C  
ANISOU 3009  C   GLY B 134     2833   2814   2839    -18    -61    -22       C  
ATOM   3010  O   GLY B 134     -72.088   5.519  14.686  1.00 21.50           O  
ANISOU 3010  O   GLY B 134     2724   2725   2721    -29    -54    -20       O  
ATOM   3011  N   THR B 135     -69.939   5.995  14.133  1.00 22.33           N  
ANISOU 3011  N   THR B 135     2835   2807   2841     -1    -64    -15       N  
ATOM   3012  CA  THR B 135     -69.851   7.236  14.894  1.00 23.00           C  
ANISOU 3012  CA  THR B 135     2925   2898   2917      7    -59     -2       C  
ATOM   3013  C   THR B 135     -69.611   8.377  13.949  1.00 21.89           C  
ANISOU 3013  C   THR B 135     2775   2774   2768     25    -55     -4       C  
ATOM   3014  O   THR B 135     -68.737   8.313  13.061  1.00 22.29           O  
ANISOU 3014  O   THR B 135     2823   2822   2824     33    -58    -11       O  
ATOM   3015  CB  THR B 135     -68.675   7.186  15.876  1.00 22.97           C  
ANISOU 3015  CB  THR B 135     2937   2869   2922      8    -67     10       C  
ATOM   3016  OG1 THR B 135     -68.874   6.115  16.790  1.00 24.96           O  
ANISOU 3016  OG1 THR B 135     3203   3102   3180    -11    -74     15       O  
ATOM   3017  CG2 THR B 135     -68.517   8.512  16.653  1.00 24.25           C  
ANISOU 3017  CG2 THR B 135     3103   3036   3075     15    -62     23       C  
ATOM   3018  N   ALA B 136     -70.417   9.415  14.142  1.00 20.80           N  
ANISOU 3018  N   ALA B 136     2633   2653   2616     31    -50      0       N  
ATOM   3019  CA  ALA B 136     -70.371  10.662  13.394  1.00 20.02           C  
ANISOU 3019  CA  ALA B 136     2532   2568   2505     48    -50      1       C  
ATOM   3020  C   ALA B 136     -69.766  11.761  14.256  1.00 20.04           C  
ANISOU 3020  C   ALA B 136     2547   2562   2505     55    -49     15       C  
ATOM   3021  O   ALA B 136     -69.835  11.703  15.483  1.00 20.57           O  
ANISOU 3021  O   ALA B 136     2620   2622   2576     48    -48     23       O  
ATOM   3022  CB  ALA B 136     -71.751  11.072  12.922  1.00 19.40           C  
ANISOU 3022  CB  ALA B 136     2442   2514   2415     53    -49     -8       C  
ATOM   3023  N   ALA B 137     -69.150  12.757  13.622  1.00 18.20           N  
ANISOU 3023  N   ALA B 137     2320   2331   2265     66    -50     19       N  
ATOM   3024  CA  ALA B 137     -68.717  13.959  14.325  1.00 17.94           C  
ANISOU 3024  CA  ALA B 137     2299   2292   2227     74    -50     32       C  
ATOM   3025  C   ALA B 137     -69.399  15.144  13.705  1.00 15.79           C  
ANISOU 3025  C   ALA B 137     2030   2032   1939     88    -54     32       C  
ATOM   3026  O   ALA B 137     -69.606  15.195  12.474  1.00 17.07           O  
ANISOU 3026  O   ALA B 137     2189   2203   2093     92    -57     26       O  
ATOM   3027  CB  ALA B 137     -67.211  14.134  14.211  1.00 16.91           C  
ANISOU 3027  CB  ALA B 137     2177   2148   2100     72    -49     36       C  
ATOM   3028  N   LEU B 138     -69.730  16.120  14.541  1.00 16.83           N  
ANISOU 3028  N   LEU B 138     2167   2162   2066     96    -56     38       N  
ATOM   3029  CA  LEU B 138     -70.344  17.369  14.102  1.00 17.58           C  
ANISOU 3029  CA  LEU B 138     2269   2264   2147    113    -65     39       C  
ATOM   3030  C   LEU B 138     -69.873  18.430  15.057  1.00 17.76           C  
ANISOU 3030  C   LEU B 138     2305   2274   2169    118    -66     49       C  
ATOM   3031  O   LEU B 138     -69.255  18.139  16.085  1.00 17.66           O  
ANISOU 3031  O   LEU B 138     2293   2252   2165    109    -59     55       O  
ATOM   3032  CB  LEU B 138     -71.890  17.271  14.043  1.00 18.13           C  
ANISOU 3032  CB  LEU B 138     2322   2353   2213    122    -70     24       C  
ATOM   3033  CG  LEU B 138     -72.608  16.855  15.324  1.00 20.32           C  
ANISOU 3033  CG  LEU B 138     2586   2639   2497    115    -64     17       C  
ATOM   3034  CD1 LEU B 138     -73.208  18.075  15.991  1.00 24.34           C  
ANISOU 3034  CD1 LEU B 138     3095   3152   2999    132    -71     14       C  
ATOM   3035  CD2 LEU B 138     -73.711  15.852  15.025  1.00 27.45           C  
ANISOU 3035  CD2 LEU B 138     3469   3562   3401    107    -62      0       C  
ATOM   3036  N   GLY B 139     -70.111  19.671  14.710  1.00 17.35           N  
ANISOU 3036  N   GLY B 139     2266   2220   2105    134    -76     52       N  
ATOM   3037  CA  GLY B 139     -69.571  20.724  15.541  1.00 18.38           C  
ANISOU 3037  CA  GLY B 139     2412   2337   2235    138    -77     62       C  
ATOM   3038  C   GLY B 139     -70.026  22.110  15.159  1.00 18.44           C  
ANISOU 3038  C   GLY B 139     2436   2340   2229    157    -92     64       C  
ATOM   3039  O   GLY B 139     -70.883  22.279  14.287  1.00 19.07           O  
ANISOU 3039  O   GLY B 139     2516   2429   2302    170   -104     57       O  
ATOM   3040  N   CYS B 140     -69.401  23.099  15.791  1.00 18.52           N  
ANISOU 3040  N   CYS B 140     2463   2334   2238    159    -93     74       N  
ATOM   3041  CA  CYS B 140     -69.587  24.526  15.442  1.00 20.02           C  
ANISOU 3041  CA  CYS B 140     2678   2512   2415    176   -110     78       C  
ATOM   3042  C   CYS B 140     -68.261  25.234  15.458  1.00 19.91           C  
ANISOU 3042  C   CYS B 140     2689   2479   2395    163   -106     94       C  
ATOM   3043  O   CYS B 140     -67.457  25.043  16.373  1.00 19.02           O  
ANISOU 3043  O   CYS B 140     2573   2362   2292    151    -92     98       O  
ATOM   3044  CB  CYS B 140     -70.501  25.251  16.438  1.00 22.18           C  
ANISOU 3044  CB  CYS B 140     2945   2788   2693    197   -120     68       C  
ATOM   3045  SG  CYS B 140     -72.223  24.820  16.271  1.00 26.30           S  
ANISOU 3045  SG  CYS B 140     3439   3336   3218    216   -131     44       S  
ATOM   3046  N   LEU B 141     -68.059  26.082  14.442  1.00 18.84           N  
ANISOU 3046  N   LEU B 141     2582   2332   2243    164   -118    102       N  
ATOM   3047  CA  LEU B 141     -66.897  26.902  14.321  1.00 18.34           C  
ANISOU 3047  CA  LEU B 141     2548   2252   2169    149   -115    116       C  
ATOM   3048  C   LEU B 141     -67.281  28.272  14.867  1.00 18.68           C  
ANISOU 3048  C   LEU B 141     2614   2277   2209    167   -132    120       C  
ATOM   3049  O   LEU B 141     -68.240  28.910  14.415  1.00 21.18           O  
ANISOU 3049  O   LEU B 141     2942   2587   2517    189   -154    117       O  
ATOM   3050  CB  LEU B 141     -66.476  26.971  12.845  1.00 18.50           C  
ANISOU 3050  CB  LEU B 141     2588   2271   2170    134   -118    123       C  
ATOM   3051  CG  LEU B 141     -65.449  28.050  12.508  1.00 21.35           C  
ANISOU 3051  CG  LEU B 141     2986   2613   2512    115   -118    137       C  
ATOM   3052  CD1 LEU B 141     -64.138  27.836  13.272  1.00 22.55           C  
ANISOU 3052  CD1 LEU B 141     3130   2766   2672     93    -96    137       C  
ATOM   3053  CD2 LEU B 141     -65.238  28.025  10.974  1.00 21.06           C  
ANISOU 3053  CD2 LEU B 141     2970   2581   2453     99   -122    142       C  
ATOM   3054  N   VAL B 142     -66.542  28.689  15.880  1.00 19.01           N  
ANISOU 3054  N   VAL B 142     2658   2308   2256    160   -122    124       N  
ATOM   3055  CA  VAL B 142     -66.859  29.936  16.601  1.00 19.54           C  
ANISOU 3055  CA  VAL B 142     2743   2358   2323    177   -137    124       C  
ATOM   3056  C   VAL B 142     -65.742  30.905  16.280  1.00 20.45           C  
ANISOU 3056  C   VAL B 142     2895   2451   2423    158   -137    140       C  
ATOM   3057  O   VAL B 142     -64.655  30.890  16.892  1.00 20.88           O  
ANISOU 3057  O   VAL B 142     2949   2503   2481    138   -119    144       O  
ATOM   3058  CB  VAL B 142     -67.017  29.678  18.141  1.00 18.41           C  
ANISOU 3058  CB  VAL B 142     2572   2223   2199    183   -126    115       C  
ATOM   3059  CG1 VAL B 142     -67.399  30.983  18.902  1.00 21.36           C  
ANISOU 3059  CG1 VAL B 142     2961   2581   2573    203   -142    111       C  
ATOM   3060  CG2 VAL B 142     -68.075  28.567  18.380  1.00 19.83           C  
ANISOU 3060  CG2 VAL B 142     2716   2429   2391    193   -123     99       C  
ATOM   3061  N   LYS B 143     -66.007  31.751  15.269  1.00 21.78           N  
ANISOU 3061  N   LYS B 143     3100   2603   2574    163   -158    148       N  
ATOM   3062  CA  LYS B 143     -64.945  32.488  14.603  1.00 22.62           C  
ANISOU 3062  CA  LYS B 143     3245   2692   2659    136   -156    164       C  
ATOM   3063  C   LYS B 143     -64.937  34.009  14.823  1.00 22.51           C  
ANISOU 3063  C   LYS B 143     3273   2645   2633    143   -177    173       C  
ATOM   3064  O   LYS B 143     -65.992  34.637  14.852  1.00 23.45           O  
ANISOU 3064  O   LYS B 143     3403   2751   2755    175   -204    168       O  
ATOM   3065  CB  LYS B 143     -65.034  32.184  13.097  1.00 23.20           C  
ANISOU 3065  CB  LYS B 143     3333   2771   2712    124   -162    169       C  
ATOM   3066  CG  LYS B 143     -63.782  32.522  12.327  1.00 25.15           C  
ANISOU 3066  CG  LYS B 143     3609   3011   2935     85   -151    182       C  
ATOM   3067  CD  LYS B 143     -63.912  32.088  10.853  1.00 29.95           C  
ANISOU 3067  CD  LYS B 143     4227   3630   3523     71   -155    185       C  
ATOM   3068  CE  LYS B 143     -63.034  32.908   9.925  1.00 32.96           C  
ANISOU 3068  CE  LYS B 143     4654   3998   3871     35   -156    200       C  
ATOM   3069  NZ  LYS B 143     -61.664  33.105  10.440  1.00 34.26           N  
ANISOU 3069  NZ  LYS B 143     4821   4164   4033      2   -131    200       N  
ATOM   3070  N   ASP B 144     -63.736  34.562  14.982  1.00 23.05           N  
ANISOU 3070  N   ASP B 144     3364   2702   2693    114   -164    182       N  
ATOM   3071  CA  ASP B 144     -63.495  36.020  14.914  1.00 24.67           C  
ANISOU 3071  CA  ASP B 144     3620   2873   2881    110   -182    195       C  
ATOM   3072  C   ASP B 144     -64.185  36.796  16.033  1.00 24.60           C  
ANISOU 3072  C   ASP B 144     3611   2848   2889    143   -199    187       C  
ATOM   3073  O   ASP B 144     -65.020  37.705  15.790  1.00 24.79           O  
ANISOU 3073  O   ASP B 144     3664   2847   2908    169   -233    188       O  
ATOM   3074  CB  ASP B 144     -63.862  36.575  13.520  1.00 25.31           C  
ANISOU 3074  CB  ASP B 144     3746   2936   2936    107   -208    208       C  
ATOM   3075  CG  ASP B 144     -62.964  36.059  12.421  1.00 27.88           C  
ANISOU 3075  CG  ASP B 144     4079   3276   3239     65   -189    216       C  
ATOM   3076  OD1 ASP B 144     -61.840  35.580  12.679  1.00 28.56           O  
ANISOU 3076  OD1 ASP B 144     4146   3379   3325     34   -158    213       O  
ATOM   3077  OD2 ASP B 144     -63.370  36.160  11.243  1.00 31.53           O  
ANISOU 3077  OD2 ASP B 144     4567   3733   3680     62   -206    224       O  
ATOM   3078  N   TYR B 145     -63.840  36.449  17.274  1.00 23.83           N  
ANISOU 3078  N   TYR B 145     3480   2764   2812    143   -179    177       N  
ATOM   3079  CA  TYR B 145     -64.376  37.134  18.436  1.00 24.02           C  
ANISOU 3079  CA  TYR B 145     3499   2777   2851    170   -191    167       C  
ATOM   3080  C   TYR B 145     -63.248  37.722  19.270  1.00 23.99           C  
ANISOU 3080  C   TYR B 145     3506   2762   2847    148   -175    171       C  
ATOM   3081  O   TYR B 145     -62.105  37.328  19.145  1.00 22.66           O  
ANISOU 3081  O   TYR B 145     3335   2603   2672    114   -150    177       O  
ATOM   3082  CB  TYR B 145     -65.300  36.224  19.297  1.00 23.84           C  
ANISOU 3082  CB  TYR B 145     3424   2782   2852    196   -185    147       C  
ATOM   3083  CG  TYR B 145     -64.580  35.068  19.941  1.00 23.09           C  
ANISOU 3083  CG  TYR B 145     3291   2714   2768    174   -152    145       C  
ATOM   3084  CD1 TYR B 145     -64.385  33.866  19.250  1.00 24.25           C  
ANISOU 3084  CD1 TYR B 145     3419   2881   2913    160   -138    146       C  
ATOM   3085  CD2 TYR B 145     -64.086  35.172  21.233  1.00 23.71           C  
ANISOU 3085  CD2 TYR B 145     3354   2795   2858    170   -138    140       C  
ATOM   3086  CE1 TYR B 145     -63.688  32.807  19.838  1.00 24.80           C  
ANISOU 3086  CE1 TYR B 145     3458   2971   2994    142   -112    143       C  
ATOM   3087  CE2 TYR B 145     -63.409  34.110  21.832  1.00 25.68           C  
ANISOU 3087  CE2 TYR B 145     3574   3067   3117    152   -112    138       C  
ATOM   3088  CZ  TYR B 145     -63.222  32.941  21.139  1.00 25.17           C  
ANISOU 3088  CZ  TYR B 145     3493   3020   3052    140   -101    140       C  
ATOM   3089  OH  TYR B 145     -62.535  31.901  21.753  1.00 22.59           O  
ANISOU 3089  OH  TYR B 145     3138   2710   2735    125    -80    137       O  
ATOM   3090  N   PHE B 146     -63.593  38.709  20.114  1.00 24.08           N  
ANISOU 3090  N   PHE B 146     3528   2754   2866    168   -190    165       N  
ATOM   3091  CA  PHE B 146     -62.649  39.330  21.034  1.00 25.29           C  
ANISOU 3091  CA  PHE B 146     3690   2898   3022    151   -176    166       C  
ATOM   3092  C   PHE B 146     -63.451  40.031  22.141  1.00 25.35           C  
ANISOU 3092  C   PHE B 146     3689   2896   3046    185   -193    150       C  
ATOM   3093  O   PHE B 146     -64.484  40.629  21.857  1.00 26.09           O  
ANISOU 3093  O   PHE B 146     3798   2974   3141    216   -224    144       O  
ATOM   3094  CB  PHE B 146     -61.727  40.313  20.308  1.00 26.48           C  
ANISOU 3094  CB  PHE B 146     3894   3019   3148    121   -181    183       C  
ATOM   3095  CG  PHE B 146     -60.831  41.047  21.229  1.00 26.56           C  
ANISOU 3095  CG  PHE B 146     3914   3018   3160    104   -169    183       C  
ATOM   3096  CD1 PHE B 146     -59.545  40.590  21.457  1.00 25.24           C  
ANISOU 3096  CD1 PHE B 146     3733   2868   2988     67   -137    185       C  
ATOM   3097  CD2 PHE B 146     -61.291  42.194  21.903  1.00 27.77           C  
ANISOU 3097  CD2 PHE B 146     4088   3143   3320    127   -191    177       C  
ATOM   3098  CE1 PHE B 146     -58.695  41.260  22.346  1.00 30.74           C  
ANISOU 3098  CE1 PHE B 146     4437   3557   3687     51   -125    182       C  
ATOM   3099  CE2 PHE B 146     -60.459  42.866  22.794  1.00 29.09           C  
ANISOU 3099  CE2 PHE B 146     4263   3301   3489    111   -179    176       C  
ATOM   3100  CZ  PHE B 146     -59.154  42.408  23.008  1.00 29.30           C  
ANISOU 3100  CZ  PHE B 146     4276   3346   3510     72   -146    179       C  
ATOM   3101  N   PRO B 147     -63.014  39.906  23.417  1.00 24.89           N  
ANISOU 3101  N   PRO B 147     3604   2852   3002    180   -173    141       N  
ATOM   3102  CA  PRO B 147     -61.887  39.096  23.860  1.00 24.56           C  
ANISOU 3102  CA  PRO B 147     3538   2831   2961    149   -140    145       C  
ATOM   3103  C   PRO B 147     -62.358  37.670  24.162  1.00 23.86           C  
ANISOU 3103  C   PRO B 147     3401   2777   2886    157   -126    136       C  
ATOM   3104  O   PRO B 147     -63.521  37.342  23.938  1.00 22.80           O  
ANISOU 3104  O   PRO B 147     3254   2652   2759    181   -140    128       O  
ATOM   3105  CB  PRO B 147     -61.454  39.812  25.159  1.00 24.74           C  
ANISOU 3105  CB  PRO B 147     3559   2847   2993    149   -134    137       C  
ATOM   3106  CG  PRO B 147     -62.738  40.285  25.725  1.00 25.21           C  
ANISOU 3106  CG  PRO B 147     3610   2904   3065    187   -157    121       C  
ATOM   3107  CD  PRO B 147     -63.597  40.683  24.526  1.00 25.61           C  
ANISOU 3107  CD  PRO B 147     3688   2934   3106    207   -186    125       C  
ATOM   3108  N   GLU B 148     -61.465  36.871  24.751  1.00 24.50           N  
ANISOU 3108  N   GLU B 148     3458   2878   2973    135   -101    137       N  
ATOM   3109  CA  GLU B 148     -61.855  35.642  25.426  1.00 23.63           C  
ANISOU 3109  CA  GLU B 148     3305   2796   2876    141    -89    128       C  
ATOM   3110  C   GLU B 148     -62.649  36.044  26.674  1.00 23.52           C  
ANISOU 3110  C   GLU B 148     3275   2787   2875    163    -95    113       C  
ATOM   3111  O   GLU B 148     -62.536  37.197  27.124  1.00 22.94           O  
ANISOU 3111  O   GLU B 148     3220   2695   2800    169   -104    110       O  
ATOM   3112  CB  GLU B 148     -60.598  34.878  25.854  1.00 23.87           C  
ANISOU 3112  CB  GLU B 148     3321   2841   2910    115    -65    131       C  
ATOM   3113  CG  GLU B 148     -59.902  34.140  24.743  1.00 25.70           C  
ANISOU 3113  CG  GLU B 148     3554   3078   3133     95    -56    138       C  
ATOM   3114  CD  GLU B 148     -60.393  32.706  24.664  1.00 27.02           C  
ANISOU 3114  CD  GLU B 148     3690   3267   3310    101    -52    134       C  
ATOM   3115  OE1 GLU B 148     -61.548  32.504  24.231  1.00 27.86           O  
ANISOU 3115  OE1 GLU B 148     3792   3375   3417    118    -64    132       O  
ATOM   3116  OE2 GLU B 148     -59.626  31.785  25.035  1.00 28.97           O  
ANISOU 3116  OE2 GLU B 148     3918   3527   3563     88    -37    132       O  
ATOM   3117  N   PRO B 149     -63.474  35.147  27.217  1.00 23.19           N  
ANISOU 3117  N   PRO B 149     3200   2770   2843    173    -92    103       N  
ATOM   3118  CA  PRO B 149     -63.767  33.773  26.765  1.00 23.81           C  
ANISOU 3118  CA  PRO B 149     3256   2868   2924    168    -84    104       C  
ATOM   3119  C   PRO B 149     -65.093  33.663  26.025  1.00 24.83           C  
ANISOU 3119  C   PRO B 149     3379   3002   3051    190   -101     95       C  
ATOM   3120  O   PRO B 149     -65.873  34.604  25.995  1.00 24.85           O  
ANISOU 3120  O   PRO B 149     3392   2995   3054    213   -120     85       O  
ATOM   3121  CB  PRO B 149     -63.890  33.035  28.082  1.00 23.47           C  
ANISOU 3121  CB  PRO B 149     3181   2847   2890    163    -71     96       C  
ATOM   3122  CG  PRO B 149     -64.627  34.031  28.954  1.00 22.57           C  
ANISOU 3122  CG  PRO B 149     3065   2733   2779    182    -81     81       C  
ATOM   3123  CD  PRO B 149     -63.969  35.370  28.589  1.00 23.39           C  
ANISOU 3123  CD  PRO B 149     3203   2806   2877    184    -90     87       C  
ATOM   3124  N   VAL B 150     -65.349  32.489  25.455  1.00 25.57           N  
ANISOU 3124  N   VAL B 150     3457   3112   3146    184    -94     97       N  
ATOM   3125  CA  VAL B 150     -66.642  32.171  24.922  1.00 26.15           C  
ANISOU 3125  CA  VAL B 150     3518   3197   3220    203   -107     85       C  
ATOM   3126  C   VAL B 150     -67.024  30.887  25.657  1.00 26.53           C  
ANISOU 3126  C   VAL B 150     3532   3273   3276    193    -92     78       C  
ATOM   3127  O   VAL B 150     -66.133  30.148  26.093  1.00 26.68           O  
ANISOU 3127  O   VAL B 150     3544   3294   3297    172    -75     87       O  
ATOM   3128  CB  VAL B 150     -66.525  32.036  23.362  1.00 26.74           C  
ANISOU 3128  CB  VAL B 150     3613   3262   3285    200   -115     96       C  
ATOM   3129  CG1 VAL B 150     -66.294  30.624  22.898  1.00 27.06           C  
ANISOU 3129  CG1 VAL B 150     3635   3319   3328    184   -100    101       C  
ATOM   3130  CG2 VAL B 150     -67.677  32.748  22.635  1.00 29.48           C  
ANISOU 3130  CG2 VAL B 150     3971   3603   3628    229   -141     87       C  
ATOM   3131  N   THR B 151     -68.314  30.659  25.869  1.00 26.53           N  
ANISOU 3131  N   THR B 151     3509   3292   3279    207    -98     59       N  
ATOM   3132  CA  THR B 151     -68.754  29.352  26.372  1.00 27.05           C  
ANISOU 3132  CA  THR B 151     3546   3383   3348    193    -85     53       C  
ATOM   3133  C   THR B 151     -69.609  28.676  25.328  1.00 25.67           C  
ANISOU 3133  C   THR B 151     3361   3220   3171    200    -91     47       C  
ATOM   3134  O   THR B 151     -70.455  29.314  24.692  1.00 25.82           O  
ANISOU 3134  O   THR B 151     3384   3239   3188    223   -108     35       O  
ATOM   3135  CB  THR B 151     -69.543  29.430  27.703  1.00 27.14           C  
ANISOU 3135  CB  THR B 151     3533   3416   3361    195    -81     33       C  
ATOM   3136  OG1 THR B 151     -70.765  30.141  27.492  1.00 29.39           O  
ANISOU 3136  OG1 THR B 151     3810   3712   3647    222    -98      9       O  
ATOM   3137  CG2 THR B 151     -68.709  30.126  28.759  1.00 29.52           C  
ANISOU 3137  CG2 THR B 151     3843   3708   3665    189    -75     38       C  
ATOM   3138  N   VAL B 152     -69.357  27.382  25.165  1.00 24.42           N  
ANISOU 3138  N   VAL B 152     3193   3070   3014    180    -78     54       N  
ATOM   3139  CA  VAL B 152     -70.161  26.556  24.308  1.00 23.06           C  
ANISOU 3139  CA  VAL B 152     3009   2912   2841    181    -80     47       C  
ATOM   3140  C   VAL B 152     -70.793  25.409  25.083  1.00 22.24           C  
ANISOU 3140  C   VAL B 152     2879   2832   2738    164    -68     37       C  
ATOM   3141  O   VAL B 152     -70.118  24.696  25.840  1.00 23.11           O  
ANISOU 3141  O   VAL B 152     2989   2941   2851    142    -56     48       O  
ATOM   3142  CB  VAL B 152     -69.335  25.942  23.144  1.00 23.73           C  
ANISOU 3142  CB  VAL B 152     3108   2985   2925    171    -78     64       C  
ATOM   3143  CG1 VAL B 152     -70.283  25.265  22.126  1.00 24.30           C  
ANISOU 3143  CG1 VAL B 152     3168   3071   2995    176    -83     54       C  
ATOM   3144  CG2 VAL B 152     -68.486  27.016  22.469  1.00 24.47           C  
ANISOU 3144  CG2 VAL B 152     3231   3055   3013    178    -86     76       C  
ATOM   3145  N   SER B 153     -72.093  25.240  24.886  1.00 20.09           N  
ANISOU 3145  N   SER B 153     2586   2582   2464    173    -73     16       N  
ATOM   3146  CA  SER B 153     -72.791  24.026  25.295  1.00 19.79           C  
ANISOU 3146  CA  SER B 153     2527   2569   2425    152    -62      6       C  
ATOM   3147  C   SER B 153     -73.465  23.443  24.094  1.00 20.08           C  
ANISOU 3147  C   SER B 153     2556   2615   2460    158    -67     -1       C  
ATOM   3148  O   SER B 153     -73.502  24.061  23.025  1.00 19.76           O  
ANISOU 3148  O   SER B 153     2525   2563   2418    179    -81      0       O  
ATOM   3149  CB  SER B 153     -73.820  24.291  26.433  1.00 20.71           C  
ANISOU 3149  CB  SER B 153     2619   2713   2537    151    -59    -20       C  
ATOM   3150  OG  SER B 153     -74.904  25.081  25.959  1.00 24.28           O  
ANISOU 3150  OG  SER B 153     3058   3180   2988    179    -74    -45       O  
ATOM   3151  N   TRP B 154     -73.935  22.219  24.265  1.00 19.10           N  
ANISOU 3151  N   TRP B 154     2415   2507   2334    135    -56     -7       N  
ATOM   3152  CA  TRP B 154     -74.723  21.511  23.267  1.00 19.84           C  
ANISOU 3152  CA  TRP B 154     2497   2614   2426    136    -59    -18       C  
ATOM   3153  C   TRP B 154     -76.114  21.125  23.810  1.00 21.38           C  
ANISOU 3153  C   TRP B 154     2662   2846   2614    127    -54    -47       C  
ATOM   3154  O   TRP B 154     -76.260  20.572  24.902  1.00 21.38           O  
ANISOU 3154  O   TRP B 154     2653   2859   2610    100    -40    -50       O  
ATOM   3155  CB  TRP B 154     -73.957  20.278  22.810  1.00 19.60           C  
ANISOU 3155  CB  TRP B 154     2477   2571   2400    115    -51      1       C  
ATOM   3156  CG  TRP B 154     -72.800  20.672  21.947  1.00 17.42           C  
ANISOU 3156  CG  TRP B 154     2224   2267   2127    126    -57     21       C  
ATOM   3157  CD1 TRP B 154     -71.531  21.004  22.342  1.00 15.47           C  
ANISOU 3157  CD1 TRP B 154     1996   1998   1885    122    -54     40       C  
ATOM   3158  CD2 TRP B 154     -72.837  20.829  20.524  1.00 16.69           C  
ANISOU 3158  CD2 TRP B 154     2137   2170   2033    141    -66     21       C  
ATOM   3159  NE1 TRP B 154     -70.758  21.326  21.230  1.00 17.41           N  
ANISOU 3159  NE1 TRP B 154     2258   2227   2130    131    -60     51       N  
ATOM   3160  CE2 TRP B 154     -71.547  21.244  20.110  1.00 15.93           C  
ANISOU 3160  CE2 TRP B 154     2064   2050   1938    142    -68     41       C  
ATOM   3161  CE3 TRP B 154     -73.837  20.650  19.560  1.00 15.86           C  
ANISOU 3161  CE3 TRP B 154     2021   2082   1925    151    -74      6       C  
ATOM   3162  CZ2 TRP B 154     -71.231  21.471  18.755  1.00 16.01           C  
ANISOU 3162  CZ2 TRP B 154     2087   2052   1944    151    -75     46       C  
ATOM   3163  CZ3 TRP B 154     -73.522  20.867  18.216  1.00 17.28           C  
ANISOU 3163  CZ3 TRP B 154     2214   2252   2101    163    -83     13       C  
ATOM   3164  CH2 TRP B 154     -72.227  21.280  17.830  1.00 18.82           C  
ANISOU 3164  CH2 TRP B 154     2433   2423   2295    161    -83     33       C  
ATOM   3165  N   ASN B 155     -77.134  21.377  23.016  1.00 20.62           N  
ANISOU 3165  N   ASN B 155     2550   2768   2516    147    -64    -69       N  
ATOM   3166  CA  ASN B 155     -78.495  21.064  23.452  1.00 20.27           C  
ANISOU 3166  CA  ASN B 155     2473   2764   2465    139    -59   -103       C  
ATOM   3167  C   ASN B 155     -78.798  21.600  24.861  1.00 21.00           C  
ANISOU 3167  C   ASN B 155     2552   2873   2553    132    -53   -119       C  
ATOM   3168  O   ASN B 155     -79.393  20.922  25.698  1.00 22.10           O  
ANISOU 3168  O   ASN B 155     2673   3041   2685    102    -38   -134       O  
ATOM   3169  CB  ASN B 155     -78.744  19.552  23.328  1.00 20.98           C  
ANISOU 3169  CB  ASN B 155     2555   2865   2551    104    -44   -102       C  
ATOM   3170  CG  ASN B 155     -78.791  19.085  21.871  1.00 24.02           C  
ANISOU 3170  CG  ASN B 155     2944   3243   2939    115    -52    -98       C  
ATOM   3171  OD1 ASN B 155     -78.703  19.907  20.953  1.00 28.11           O  
ANISOU 3171  OD1 ASN B 155     3470   3750   3459    147    -69    -96       O  
ATOM   3172  ND2 ASN B 155     -78.966  17.775  21.655  1.00 23.43           N  
ANISOU 3172  ND2 ASN B 155     2865   3175   2863     86    -40    -96       N  
ATOM   3173  N   SER B 156     -78.455  22.865  25.049  1.00 22.17           N  
ANISOU 3173  N   SER B 156     2711   3008   2706    160    -66   -118       N  
ATOM   3174  CA  SER B 156     -78.675  23.587  26.300  1.00 23.20           C  
ANISOU 3174  CA  SER B 156     2829   3152   2834    160    -63   -135       C  
ATOM   3175  C   SER B 156     -78.018  22.928  27.507  1.00 22.33           C  
ANISOU 3175  C   SER B 156     2726   3040   2720    121    -42   -117       C  
ATOM   3176  O   SER B 156     -78.500  23.075  28.651  1.00 22.58           O  
ANISOU 3176  O   SER B 156     2738   3097   2743    107    -33   -137       O  
ATOM   3177  CB  SER B 156     -80.177  23.825  26.527  1.00 24.76           C  
ANISOU 3177  CB  SER B 156     2988   3395   3027    170    -66   -183       C  
ATOM   3178  OG  SER B 156     -80.762  24.456  25.401  1.00 29.25           O  
ANISOU 3178  OG  SER B 156     3552   3961   3598    210    -90   -199       O  
ATOM   3179  N   GLY B 157     -76.914  22.215  27.269  1.00 21.50           N  
ANISOU 3179  N   GLY B 157     2646   2906   2619    105    -36    -82       N  
ATOM   3180  CA  GLY B 157     -76.195  21.539  28.364  1.00 20.75           C  
ANISOU 3180  CA  GLY B 157     2562   2803   2519     70    -21    -63       C  
ATOM   3181  C   GLY B 157     -76.622  20.105  28.611  1.00 21.91           C  
ANISOU 3181  C   GLY B 157     2702   2965   2657     31     -8    -63       C  
ATOM   3182  O   GLY B 157     -76.024  19.445  29.461  1.00 21.41           O  
ANISOU 3182  O   GLY B 157     2653   2893   2589      1      1    -45       O  
ATOM   3183  N   ALA B 158     -77.639  19.617  27.892  1.00 21.16           N  
ANISOU 3183  N   ALA B 158     2588   2892   2559     30     -8    -83       N  
ATOM   3184  CA  ALA B 158     -78.091  18.244  28.028  1.00 22.39           C  
ANISOU 3184  CA  ALA B 158     2741   3062   2706     -9      4    -85       C  
ATOM   3185  C   ALA B 158     -77.124  17.242  27.408  1.00 21.69           C  
ANISOU 3185  C   ALA B 158     2678   2938   2625    -19      3    -53       C  
ATOM   3186  O   ALA B 158     -77.107  16.079  27.803  1.00 21.93           O  
ANISOU 3186  O   ALA B 158     2718   2967   2649    -55     11    -44       O  
ATOM   3187  CB  ALA B 158     -79.496  18.065  27.434  1.00 23.21           C  
ANISOU 3187  CB  ALA B 158     2813   3203   2803     -7      5   -120       C  
ATOM   3188  N   LEU B 159     -76.322  17.700  26.438  1.00 20.46           N  
ANISOU 3188  N   LEU B 159     2537   2755   2482     11     -9    -37       N  
ATOM   3189  CA  LEU B 159     -75.411  16.803  25.721  1.00 21.36           C  
ANISOU 3189  CA  LEU B 159     2671   2840   2605      6    -11    -13       C  
ATOM   3190  C   LEU B 159     -74.015  17.156  26.173  1.00 21.16           C  
ANISOU 3190  C   LEU B 159     2669   2783   2586     11    -15     12       C  
ATOM   3191  O   LEU B 159     -73.520  18.249  25.890  1.00 19.99           O  
ANISOU 3191  O   LEU B 159     2527   2626   2444     38    -22     16       O  
ATOM   3192  CB  LEU B 159     -75.551  17.064  24.220  1.00 22.12           C  
ANISOU 3192  CB  LEU B 159     2763   2933   2707     34    -21    -18       C  
ATOM   3193  CG  LEU B 159     -75.305  15.964  23.188  1.00 26.49           C  
ANISOU 3193  CG  LEU B 159     3323   3474   3266     26    -22    -10       C  
ATOM   3194  CD1 LEU B 159     -74.734  16.598  21.929  1.00 21.63           C  
ANISOU 3194  CD1 LEU B 159     2716   2844   2658     56    -33     -4       C  
ATOM   3195  CD2 LEU B 159     -74.529  14.691  23.630  1.00 23.58           C  
ANISOU 3195  CD2 LEU B 159     2973   3084   2902     -3    -18      9       C  
ATOM   3196  N   THR B 160     -73.394  16.246  26.921  1.00 21.77           N  
ANISOU 3196  N   THR B 160     2762   2846   2663    -16    -11     29       N  
ATOM   3197  CA  THR B 160     -72.073  16.501  27.462  1.00 22.07           C  
ANISOU 3197  CA  THR B 160     2821   2858   2708    -12    -15     50       C  
ATOM   3198  C   THR B 160     -71.078  15.418  27.049  1.00 20.55           C  
ANISOU 3198  C   THR B 160     2647   2637   2525    -19    -21     68       C  
ATOM   3199  O   THR B 160     -69.897  15.720  26.812  1.00 20.57           O  
ANISOU 3199  O   THR B 160     2662   2617   2537     -4    -27     80       O  
ATOM   3200  CB  THR B 160     -72.104  16.598  29.010  1.00 22.55           C  
ANISOU 3200  CB  THR B 160     2884   2925   2757    -34     -9     52       C  
ATOM   3201  OG1 THR B 160     -72.797  15.461  29.497  1.00 26.02           O  
ANISOU 3201  OG1 THR B 160     3324   3376   3186    -69     -3     49       O  
ATOM   3202  CG2 THR B 160     -72.837  17.892  29.490  1.00 22.34           C  
ANISOU 3202  CG2 THR B 160     2838   2925   2724    -20     -5     33       C  
ATOM   3203  N   SER B 161     -71.539  14.166  26.942  1.00 21.35           N  
ANISOU 3203  N   SER B 161     2750   2738   2623    -42    -20     67       N  
ATOM   3204  CA ASER B 161     -70.647  13.091  26.549  0.50 20.75           C  
ANISOU 3204  CA ASER B 161     2692   2634   2558    -47    -29     80       C  
ATOM   3205  CA BSER B 161     -70.670  13.069  26.530  0.50 20.68           C  
ANISOU 3205  CA BSER B 161     2683   2626   2550    -48    -29     80       C  
ATOM   3206  C   SER B 161     -70.130  13.285  25.122  1.00 19.76           C  
ANISOU 3206  C   SER B 161     2562   2500   2445    -21    -34     77       C  
ATOM   3207  O   SER B 161     -70.890  13.601  24.204  1.00 21.12           O  
ANISOU 3207  O   SER B 161     2720   2690   2616    -10    -31     64       O  
ATOM   3208  CB ASER B 161     -71.335  11.732  26.690  0.50 21.59           C  
ANISOU 3208  CB ASER B 161     2804   2742   2659    -79    -28     78       C  
ATOM   3209  CB BSER B 161     -71.418  11.733  26.569  0.50 21.45           C  
ANISOU 3209  CB BSER B 161     2784   2726   2641    -78    -28     76       C  
ATOM   3210  OG ASER B 161     -71.826  11.553  28.011  0.50 22.83           O  
ANISOU 3210  OG ASER B 161     2966   2908   2799   -109    -23     80       O  
ATOM   3211  OG BSER B 161     -70.568  10.653  26.211  0.50 22.19           O  
ANISOU 3211  OG BSER B 161     2896   2789   2747    -81    -40     87       O  
ATOM   3212  N   GLY B 162     -68.821  13.090  24.952  1.00 19.41           N  
ANISOU 3212  N   GLY B 162     2532   2431   2413    -12    -42     88       N  
ATOM   3213  CA  GLY B 162     -68.177  13.202  23.638  1.00 17.69           C  
ANISOU 3213  CA  GLY B 162     2310   2206   2204      8    -46     85       C  
ATOM   3214  C   GLY B 162     -67.883  14.618  23.167  1.00 18.09           C  
ANISOU 3214  C   GLY B 162     2356   2263   2253     30    -43     83       C  
ATOM   3215  O   GLY B 162     -67.428  14.800  22.008  1.00 17.61           O  
ANISOU 3215  O   GLY B 162     2294   2201   2197     43    -45     80       O  
ATOM   3216  N   VAL B 163     -68.218  15.621  23.961  1.00 19.22           N  
ANISOU 3216  N   VAL B 163     2498   2416   2389     33    -39     84       N  
ATOM   3217  CA  VAL B 163     -67.956  17.018  23.553  1.00 18.76           C  
ANISOU 3217  CA  VAL B 163     2439   2360   2327     54    -38     84       C  
ATOM   3218  C   VAL B 163     -66.486  17.402  23.778  1.00 19.02           C  
ANISOU 3218  C   VAL B 163     2485   2375   2366     58    -40     94       C  
ATOM   3219  O   VAL B 163     -65.927  17.117  24.836  1.00 20.19           O  
ANISOU 3219  O   VAL B 163     2639   2514   2517     49    -41    101       O  
ATOM   3220  CB  VAL B 163     -68.896  18.040  24.298  1.00 19.13           C  
ANISOU 3220  CB  VAL B 163     2479   2424   2365     59    -35     77       C  
ATOM   3221  CG1 VAL B 163     -68.526  19.473  23.946  1.00 18.79           C  
ANISOU 3221  CG1 VAL B 163     2442   2377   2320     80    -38     78       C  
ATOM   3222  CG2 VAL B 163     -70.362  17.770  24.025  1.00 19.47           C  
ANISOU 3222  CG2 VAL B 163     2505   2490   2401     56    -34     61       C  
ATOM   3223  N   HIS B 164     -65.872  18.030  22.780  1.00 18.30           N  
ANISOU 3223  N   HIS B 164     2397   2280   2275     70    -41     94       N  
ATOM   3224  CA  HIS B 164     -64.586  18.703  22.949  1.00 17.90           C  
ANISOU 3224  CA  HIS B 164     2356   2218   2226     73    -40     99       C  
ATOM   3225  C   HIS B 164     -64.705  20.124  22.446  1.00 17.72           C  
ANISOU 3225  C   HIS B 164     2341   2198   2195     85    -40    100       C  
ATOM   3226  O   HIS B 164     -64.925  20.381  21.246  1.00 17.83           O  
ANISOU 3226  O   HIS B 164     2356   2215   2203     91    -42     96       O  
ATOM   3227  CB  HIS B 164     -63.455  18.025  22.186  1.00 18.52           C  
ANISOU 3227  CB  HIS B 164     2436   2288   2313     71    -42     96       C  
ATOM   3228  CG  HIS B 164     -63.183  16.622  22.635  1.00 18.19           C  
ANISOU 3228  CG  HIS B 164     2392   2238   2282     62    -48     95       C  
ATOM   3229  ND1 HIS B 164     -62.713  16.318  23.899  1.00 18.83           N  
ANISOU 3229  ND1 HIS B 164     2479   2309   2367     56    -52    102       N  
ATOM   3230  CD2 HIS B 164     -63.326  15.441  21.991  1.00 20.55           C  
ANISOU 3230  CD2 HIS B 164     2686   2535   2588     58    -52     89       C  
ATOM   3231  CE1 HIS B 164     -62.549  15.007  23.997  1.00 20.67           C  
ANISOU 3231  CE1 HIS B 164     2713   2531   2609     50    -60    100       C  
ATOM   3232  NE2 HIS B 164     -62.952  14.450  22.867  1.00 21.36           N  
ANISOU 3232  NE2 HIS B 164     2793   2623   2699     51    -60     92       N  
ATOM   3233  N   THR B 165     -64.460  21.051  23.334  1.00 18.51           N  
ANISOU 3233  N   THR B 165     2447   2295   2292     88    -38    104       N  
ATOM   3234  CA  THR B 165     -64.386  22.449  22.965  1.00 18.07           C  
ANISOU 3234  CA  THR B 165     2403   2235   2228     98    -40    105       C  
ATOM   3235  C   THR B 165     -62.928  22.863  23.045  1.00 17.80           C  
ANISOU 3235  C   THR B 165     2379   2190   2194     92    -36    110       C  
ATOM   3236  O   THR B 165     -62.338  22.884  24.117  1.00 20.05           O  
ANISOU 3236  O   THR B 165     2663   2471   2483     87    -33    113       O  
ATOM   3237  CB  THR B 165     -65.252  23.334  23.879  1.00 18.49           C  
ANISOU 3237  CB  THR B 165     2454   2293   2277    107    -42    103       C  
ATOM   3238  OG1 THR B 165     -66.638  22.977  23.722  1.00 18.82           O  
ANISOU 3238  OG1 THR B 165     2483   2350   2317    113    -46     93       O  
ATOM   3239  CG2 THR B 165     -64.990  24.824  23.606  1.00 19.26           C  
ANISOU 3239  CG2 THR B 165     2569   2381   2367    118    -47    105       C  
ATOM   3240  N   PHE B 166     -62.346  23.158  21.907  1.00 16.89           N  
ANISOU 3240  N   PHE B 166     2272   2072   2073     89    -36    110       N  
ATOM   3241  CA  PHE B 166     -60.919  23.399  21.812  1.00 17.90           C  
ANISOU 3241  CA  PHE B 166     2407   2195   2200     79    -30    110       C  
ATOM   3242  C   PHE B 166     -60.496  24.740  22.359  1.00 18.95           C  
ANISOU 3242  C   PHE B 166     2555   2320   2326     79    -28    115       C  
ATOM   3243  O   PHE B 166     -61.239  25.723  22.232  1.00 20.00           O  
ANISOU 3243  O   PHE B 166     2700   2448   2451     88    -34    119       O  
ATOM   3244  CB  PHE B 166     -60.484  23.254  20.363  1.00 16.13           C  
ANISOU 3244  CB  PHE B 166     2186   1975   1969     72    -28    105       C  
ATOM   3245  CG  PHE B 166     -60.541  21.837  19.866  1.00 16.34           C  
ANISOU 3245  CG  PHE B 166     2196   2008   2004     70    -29     97       C  
ATOM   3246  CD1 PHE B 166     -59.490  20.985  20.127  1.00 17.70           C  
ANISOU 3246  CD1 PHE B 166     2357   2180   2187     63    -27     89       C  
ATOM   3247  CD2 PHE B 166     -61.642  21.368  19.164  1.00 16.83           C  
ANISOU 3247  CD2 PHE B 166     2252   2076   2065     76    -33     96       C  
ATOM   3248  CE1 PHE B 166     -59.538  19.655  19.702  1.00 17.84           C  
ANISOU 3248  CE1 PHE B 166     2361   2201   2215     63    -30     79       C  
ATOM   3249  CE2 PHE B 166     -61.680  20.038  18.717  1.00 17.45           C  
ANISOU 3249  CE2 PHE B 166     2317   2161   2154     73    -34     87       C  
ATOM   3250  CZ  PHE B 166     -60.643  19.205  19.001  1.00 20.44           C  
ANISOU 3250  CZ  PHE B 166     2687   2535   2543     67    -33     80       C  
ATOM   3251  N   PRO B 167     -59.286  24.798  22.938  1.00 19.68           N  
ANISOU 3251  N   PRO B 167     2647   2410   2422     69    -22    113       N  
ATOM   3252  CA  PRO B 167     -58.717  26.089  23.346  1.00 20.34           C  
ANISOU 3252  CA  PRO B 167     2746   2485   2497     65    -19    117       C  
ATOM   3253  C   PRO B 167     -58.711  26.989  22.128  1.00 20.44           C  
ANISOU 3253  C   PRO B 167     2779   2494   2494     60    -20    120       C  
ATOM   3254  O   PRO B 167     -58.471  26.526  21.007  1.00 20.22           O  
ANISOU 3254  O   PRO B 167     2750   2471   2460     52    -18    116       O  
ATOM   3255  CB  PRO B 167     -57.303  25.726  23.785  1.00 20.07           C  
ANISOU 3255  CB  PRO B 167     2704   2454   2468     54    -12    109       C  
ATOM   3256  CG  PRO B 167     -57.397  24.238  24.165  1.00 20.92           C  
ANISOU 3256  CG  PRO B 167     2791   2566   2590     58    -16    105       C  
ATOM   3257  CD  PRO B 167     -58.411  23.654  23.263  1.00 20.42           C  
ANISOU 3257  CD  PRO B 167     2725   2506   2526     64    -20    106       C  
ATOM   3258  N   ALA B 168     -59.002  28.268  22.333  1.00 21.27           N  
ANISOU 3258  N   ALA B 168     2904   2587   2590     64    -24    126       N  
ATOM   3259  CA  ALA B 168     -59.050  29.174  21.201  1.00 22.39           C  
ANISOU 3259  CA  ALA B 168     3073   2720   2715     58    -29    131       C  
ATOM   3260  C   ALA B 168     -57.641  29.514  20.723  1.00 22.71           C  
ANISOU 3260  C   ALA B 168     3124   2762   2744     31    -18    129       C  
ATOM   3261  O   ALA B 168     -56.677  29.444  21.483  1.00 22.91           O  
ANISOU 3261  O   ALA B 168     3139   2790   2774     22     -8    123       O  
ATOM   3262  CB  ALA B 168     -59.809  30.456  21.568  1.00 22.78           C  
ANISOU 3262  CB  ALA B 168     3144   2753   2759     72    -42    138       C  
ATOM   3263  N   VAL B 169     -57.530  29.854  19.444  1.00 23.45           N  
ANISOU 3263  N   VAL B 169     3237   2853   2819     18    -19    132       N  
ATOM   3264  CA  VAL B 169     -56.258  30.294  18.867  1.00 25.17           C  
ANISOU 3264  CA  VAL B 169     3468   3076   3021    -13     -7    128       C  
ATOM   3265  C   VAL B 169     -56.358  31.785  18.557  1.00 26.18           C  
ANISOU 3265  C   VAL B 169     3638   3182   3128    -22    -15    141       C  
ATOM   3266  O   VAL B 169     -57.362  32.247  18.032  1.00 26.23           O  
ANISOU 3266  O   VAL B 169     3665   3174   3127     -9    -31    151       O  
ATOM   3267  CB  VAL B 169     -55.902  29.485  17.593  1.00 25.53           C  
ANISOU 3267  CB  VAL B 169     3505   3139   3058    -29      0    119       C  
ATOM   3268  CG1 VAL B 169     -54.596  29.976  16.977  1.00 28.28           C  
ANISOU 3268  CG1 VAL B 169     3865   3496   3385    -66     14    111       C  
ATOM   3269  CG2 VAL B 169     -55.810  28.008  17.937  1.00 26.86           C  
ANISOU 3269  CG2 VAL B 169     3635   3324   3248    -18      4    105       C  
ATOM   3270  N   LEU B 170     -55.326  32.532  18.929  1.00 28.24           N  
ANISOU 3270  N   LEU B 170     3911   3439   3380    -44     -5    139       N  
ATOM   3271  CA  LEU B 170     -55.306  33.968  18.669  1.00 30.32           C  
ANISOU 3271  CA  LEU B 170     4218   3679   3623    -57    -12    151       C  
ATOM   3272  C   LEU B 170     -54.814  34.152  17.231  1.00 31.69           C  
ANISOU 3272  C   LEU B 170     4415   3857   3768    -91     -8    153       C  
ATOM   3273  O   LEU B 170     -53.789  33.602  16.835  1.00 32.20           O  
ANISOU 3273  O   LEU B 170     4464   3946   3827   -117     11    139       O  
ATOM   3274  CB  LEU B 170     -54.425  34.692  19.700  1.00 31.14           C  
ANISOU 3274  CB  LEU B 170     4327   3778   3729    -69     -2    147       C  
ATOM   3275  CG  LEU B 170     -54.265  36.227  19.722  1.00 33.63           C  
ANISOU 3275  CG  LEU B 170     4688   4066   4026    -84     -9    158       C  
ATOM   3276  CD1 LEU B 170     -53.130  36.684  18.817  1.00 36.48           C  
ANISOU 3276  CD1 LEU B 170     5071   4431   4357   -131      5    156       C  
ATOM   3277  CD2 LEU B 170     -55.580  36.959  19.413  1.00 34.21           C  
ANISOU 3277  CD2 LEU B 170     4793   4111   4096    -59    -37    174       C  
ATOM   3278  N   GLU B 171     -55.578  34.889  16.436  1.00 32.87           N  
ANISOU 3278  N   GLU B 171     4603   3985   3900    -88    -26    169       N  
ATOM   3279  CA  GLU B 171     -55.251  35.054  15.017  1.00 34.07           C  
ANISOU 3279  CA  GLU B 171     4782   4142   4023   -121    -25    173       C  
ATOM   3280  C   GLU B 171     -54.459  36.342  14.819  1.00 34.40           C  
ANISOU 3280  C   GLU B 171     4868   4165   4035   -158    -22    182       C  
ATOM   3281  O   GLU B 171     -54.480  37.231  15.669  1.00 34.56           O  
ANISOU 3281  O   GLU B 171     4908   4164   4061   -151    -29    188       O  
ATOM   3282  CB  GLU B 171     -56.525  35.047  14.172  1.00 34.63           C  
ANISOU 3282  CB  GLU B 171     4871   4201   4087    -99    -49    186       C  
ATOM   3283  CG  GLU B 171     -57.305  33.723  14.360  1.00 37.17           C  
ANISOU 3283  CG  GLU B 171     5146   4541   4435    -66    -49    176       C  
ATOM   3284  CD  GLU B 171     -58.690  33.723  13.759  1.00 39.93           C  
ANISOU 3284  CD  GLU B 171     5507   4880   4784    -37    -74    185       C  
ATOM   3285  OE1 GLU B 171     -59.563  34.485  14.253  1.00 41.58           O  
ANISOU 3285  OE1 GLU B 171     5734   5067   4999     -9    -95    193       O  
ATOM   3286  OE2 GLU B 171     -58.917  32.930  12.817  1.00 41.92           O  
ANISOU 3286  OE2 GLU B 171     5747   5150   5031    -41    -72    181       O  
ATOM   3287  N   SER B 172     -53.785  36.452  13.682  1.00 35.05           N  
ANISOU 3287  N   SER B 172     4971   4259   4087   -201    -12    181       N  
ATOM   3288  CA  SER B 172     -52.979  37.643  13.402  1.00 35.35           C  
ANISOU 3288  CA  SER B 172     5055   4283   4094   -245     -8    189       C  
ATOM   3289  C   SER B 172     -53.823  38.920  13.394  1.00 35.16           C  
ANISOU 3289  C   SER B 172     5089   4212   4059   -231    -38    214       C  
ATOM   3290  O   SER B 172     -53.298  40.007  13.651  1.00 36.35           O  
ANISOU 3290  O   SER B 172     5277   4341   4194   -256    -39    221       O  
ATOM   3291  CB  SER B 172     -52.244  37.491  12.085  1.00 35.84           C  
ANISOU 3291  CB  SER B 172     5130   4367   4121   -295      7    183       C  
ATOM   3292  OG  SER B 172     -53.143  37.628  11.005  1.00 37.44           O  
ANISOU 3292  OG  SER B 172     5366   4556   4306   -291    -15    202       O  
ATOM   3293  N   SER B 173     -55.124  38.786  13.121  1.00 33.70           N  
ANISOU 3293  N   SER B 173     4910   4012   3883   -191    -65    225       N  
ATOM   3294  CA  SER B 173     -56.083  39.890  13.223  1.00 33.24           C  
ANISOU 3294  CA  SER B 173     4898   3909   3822   -166   -100    243       C  
ATOM   3295  C   SER B 173     -56.244  40.437  14.648  1.00 32.42           C  
ANISOU 3295  C   SER B 173     4787   3788   3744   -137   -105    239       C  
ATOM   3296  O   SER B 173     -56.685  41.573  14.842  1.00 32.72           O  
ANISOU 3296  O   SER B 173     4868   3787   3775   -126   -130    251       O  
ATOM   3297  CB  SER B 173     -57.457  39.438  12.712  1.00 33.36           C  
ANISOU 3297  CB  SER B 173     4908   3921   3846   -124   -126    248       C  
ATOM   3298  OG  SER B 173     -57.986  38.383  13.524  1.00 33.10           O  
ANISOU 3298  OG  SER B 173     4815   3910   3849    -85   -118    232       O  
ATOM   3299  N   GLY B 174     -55.894  39.615  15.633  1.00 30.87           N  
ANISOU 3299  N   GLY B 174     4536   3619   3575   -126    -83    222       N  
ATOM   3300  CA  GLY B 174     -56.087  39.952  17.043  1.00 29.35           C  
ANISOU 3300  CA  GLY B 174     4328   3416   3408    -98    -85    216       C  
ATOM   3301  C   GLY B 174     -57.422  39.433  17.560  1.00 28.46           C  
ANISOU 3301  C   GLY B 174     4186   3304   3323    -44   -103    211       C  
ATOM   3302  O   GLY B 174     -57.830  39.729  18.685  1.00 28.75           O  
ANISOU 3302  O   GLY B 174     4210   3333   3381    -17   -109    206       O  
ATOM   3303  N   LEU B 175     -58.114  38.662  16.719  1.00 28.39           N  
ANISOU 3303  N   LEU B 175     4165   3308   3313    -32   -110    212       N  
ATOM   3304  CA  LEU B 175     -59.372  38.019  17.099  1.00 27.02           C  
ANISOU 3304  CA  LEU B 175     3959   3142   3164     14   -123    205       C  
ATOM   3305  C   LEU B 175     -59.089  36.550  17.353  1.00 25.97           C  
ANISOU 3305  C   LEU B 175     3773   3047   3049     12    -99    192       C  
ATOM   3306  O   LEU B 175     -58.117  36.013  16.853  1.00 26.75           O  
ANISOU 3306  O   LEU B 175     3863   3163   3138    -20    -78    189       O  
ATOM   3307  CB  LEU B 175     -60.410  38.154  15.989  1.00 27.77           C  
ANISOU 3307  CB  LEU B 175     4079   3225   3247     31   -151    213       C  
ATOM   3308  CG  LEU B 175     -60.723  39.589  15.520  1.00 28.16           C  
ANISOU 3308  CG  LEU B 175     4191   3233   3276     33   -182    228       C  
ATOM   3309  CD1 LEU B 175     -61.630  39.603  14.308  1.00 27.21           C  
ANISOU 3309  CD1 LEU B 175     4094   3104   3141     46   -209    236       C  
ATOM   3310  CD2 LEU B 175     -61.331  40.454  16.612  1.00 31.60           C  
ANISOU 3310  CD2 LEU B 175     4633   3646   3730     67   -202    222       C  
ATOM   3311  N   TYR B 176     -59.959  35.931  18.123  1.00 24.30           N  
ANISOU 3311  N   TYR B 176     3526   2846   2862     45   -102    183       N  
ATOM   3312  CA  TYR B 176     -59.833  34.508  18.455  1.00 22.51           C  
ANISOU 3312  CA  TYR B 176     3251   2649   2652     47    -83    172       C  
ATOM   3313  C   TYR B 176     -60.798  33.683  17.635  1.00 22.43           C  
ANISOU 3313  C   TYR B 176     3228   2651   2644     63    -93    170       C  
ATOM   3314  O   TYR B 176     -61.848  34.140  17.155  1.00 22.28           O  
ANISOU 3314  O   TYR B 176     3225   2619   2620     84   -116    173       O  
ATOM   3315  CB  TYR B 176     -60.167  34.267  19.935  1.00 22.74           C  
ANISOU 3315  CB  TYR B 176     3250   2684   2706     69    -80    162       C  
ATOM   3316  CG  TYR B 176     -59.257  34.968  20.913  1.00 23.32           C  
ANISOU 3316  CG  TYR B 176     3330   2749   2780     56    -70    162       C  
ATOM   3317  CD1 TYR B 176     -58.111  34.345  21.387  1.00 25.75           C  
ANISOU 3317  CD1 TYR B 176     3616   3074   3093     35    -47    156       C  
ATOM   3318  CD2 TYR B 176     -59.535  36.269  21.336  1.00 25.09           C  
ANISOU 3318  CD2 TYR B 176     3583   2949   3002     66    -85    165       C  
ATOM   3319  CE1 TYR B 176     -57.264  34.972  22.289  1.00 25.97           C  
ANISOU 3319  CE1 TYR B 176     3648   3097   3123     24    -38    153       C  
ATOM   3320  CE2 TYR B 176     -58.685  36.940  22.239  1.00 25.90           C  
ANISOU 3320  CE2 TYR B 176     3692   3044   3105     53    -75    164       C  
ATOM   3321  CZ  TYR B 176     -57.548  36.281  22.699  1.00 26.87           C  
ANISOU 3321  CZ  TYR B 176     3790   3186   3232     31    -51    158       C  
ATOM   3322  OH  TYR B 176     -56.707  36.906  23.583  1.00 28.30           O  
ANISOU 3322  OH  TYR B 176     3976   3363   3414     18    -41    155       O  
ATOM   3323  N   SER B 177     -60.440  32.412  17.519  1.00 21.50           N  
ANISOU 3323  N   SER B 177     3077   2558   2535     54    -75    162       N  
ATOM   3324  CA ASER B 177     -61.310  31.436  16.924  0.50 21.02           C  
ANISOU 3324  CA ASER B 177     2995   2511   2480     68    -80    157       C  
ATOM   3325  CA BSER B 177     -61.344  31.432  16.953  0.50 20.82           C  
ANISOU 3325  CA BSER B 177     2969   2486   2454     69    -81    157       C  
ATOM   3326  C   SER B 177     -61.173  30.087  17.636  1.00 20.15           C  
ANISOU 3326  C   SER B 177     2843   2423   2392     70    -65    146       C  
ATOM   3327  O   SER B 177     -60.081  29.753  18.081  1.00 20.95           O  
ANISOU 3327  O   SER B 177     2933   2531   2497     53    -49    142       O  
ATOM   3328  CB ASER B 177     -60.940  31.292  15.456  0.50 21.22           C  
ANISOU 3328  CB ASER B 177     3036   2541   2483     46    -79    161       C  
ATOM   3329  CB BSER B 177     -61.119  31.286  15.447  0.50 20.94           C  
ANISOU 3329  CB BSER B 177     3001   2506   2449     50    -82    162       C  
ATOM   3330  OG ASER B 177     -61.790  30.367  14.840  0.50 21.82           O  
ANISOU 3330  OG ASER B 177     3093   2631   2564     60    -84    156       O  
ATOM   3331  OG BSER B 177     -61.484  32.477  14.777  0.50 20.83           O  
ANISOU 3331  OG BSER B 177     3030   2469   2415     51   -102    174       O  
ATOM   3332  N   LEU B 178     -62.279  29.334  17.711  1.00 19.23           N  
ANISOU 3332  N   LEU B 178     2704   2316   2286     91    -72    140       N  
ATOM   3333  CA  LEU B 178     -62.213  27.944  18.215  1.00 18.83           C  
ANISOU 3333  CA  LEU B 178     2618   2283   2253     90    -59    131       C  
ATOM   3334  C   LEU B 178     -63.295  27.136  17.538  1.00 18.14           C  
ANISOU 3334  C   LEU B 178     2516   2207   2168    103    -67    126       C  
ATOM   3335  O   LEU B 178     -64.197  27.696  16.942  1.00 19.23           O  
ANISOU 3335  O   LEU B 178     2668   2342   2298    117    -82    128       O  
ATOM   3336  CB  LEU B 178     -62.370  27.912  19.746  1.00 18.74           C  
ANISOU 3336  CB  LEU B 178     2592   2272   2257    100    -56    128       C  
ATOM   3337  CG  LEU B 178     -63.693  28.288  20.422  1.00 17.57           C  
ANISOU 3337  CG  LEU B 178     2438   2123   2114    124    -68    124       C  
ATOM   3338  CD1 LEU B 178     -64.829  27.296  20.257  1.00 19.64           C  
ANISOU 3338  CD1 LEU B 178     2676   2402   2383    135    -72    116       C  
ATOM   3339  CD2 LEU B 178     -63.434  28.450  21.927  1.00 20.57           C  
ANISOU 3339  CD2 LEU B 178     2808   2503   2505    124    -62    122       C  
ATOM   3340  N   SER B 179     -63.182  25.801  17.629  1.00 18.68           N  
ANISOU 3340  N   SER B 179     2559   2291   2249     97    -57    119       N  
ATOM   3341  CA ASER B 179     -64.284  24.902  17.271  0.50 18.72           C  
ANISOU 3341  CA ASER B 179     2545   2307   2259    108    -62    112       C  
ATOM   3342  CA BSER B 179     -64.293  24.909  17.279  0.50 18.73           C  
ANISOU 3342  CA BSER B 179     2546   2309   2261    108    -62    112       C  
ATOM   3343  C   SER B 179     -64.709  24.104  18.501  1.00 18.16           C  
ANISOU 3343  C   SER B 179     2452   2244   2206    113    -57    106       C  
ATOM   3344  O   SER B 179     -63.921  23.877  19.403  1.00 17.42           O  
ANISOU 3344  O   SER B 179     2353   2146   2120    104    -49    108       O  
ATOM   3345  CB ASER B 179     -63.917  23.955  16.136  0.50 19.06           C  
ANISOU 3345  CB ASER B 179     2581   2361   2301     96    -57    107       C  
ATOM   3346  CB BSER B 179     -63.959  23.971  16.127  0.50 18.95           C  
ANISOU 3346  CB BSER B 179     2568   2347   2287     96    -57    107       C  
ATOM   3347  OG ASER B 179     -63.517  24.645  14.959  0.50 21.02           O  
ANISOU 3347  OG ASER B 179     2850   2605   2529     87    -60    112       O  
ATOM   3348  OG BSER B 179     -64.184  24.566  14.857  0.50 21.09           O  
ANISOU 3348  OG BSER B 179     2856   2616   2539     96    -65    111       O  
ATOM   3349  N   SER B 180     -65.985  23.716  18.530  1.00 17.17           N  
ANISOU 3349  N   SER B 180     2312   2128   2083    125    -63     99       N  
ATOM   3350  CA  SER B 180     -66.498  22.765  19.493  1.00 17.35           C  
ANISOU 3350  CA  SER B 180     2314   2161   2118    122    -58     93       C  
ATOM   3351  C   SER B 180     -67.104  21.626  18.688  1.00 17.11           C  
ANISOU 3351  C   SER B 180     2269   2143   2090    119    -58     86       C  
ATOM   3352  O   SER B 180     -67.858  21.836  17.726  1.00 17.39           O  
ANISOU 3352  O   SER B 180     2305   2185   2117    129    -66     81       O  
ATOM   3353  CB  SER B 180     -67.581  23.418  20.390  1.00 17.74           C  
ANISOU 3353  CB  SER B 180     2357   2216   2166    136    -64     87       C  
ATOM   3354  OG  SER B 180     -68.112  22.460  21.299  1.00 18.64           O  
ANISOU 3354  OG  SER B 180     2452   2342   2287    128    -57     80       O  
ATOM   3355  N   VAL B 181     -66.741  20.406  19.058  1.00 16.83           N  
ANISOU 3355  N   VAL B 181     2222   2108   2064    106    -51     84       N  
ATOM   3356  CA  VAL B 181     -67.166  19.217  18.319  1.00 17.74           C  
ANISOU 3356  CA  VAL B 181     2326   2232   2183    101    -51     77       C  
ATOM   3357  C   VAL B 181     -67.786  18.231  19.251  1.00 16.74           C  
ANISOU 3357  C   VAL B 181     2186   2111   2064     92    -48     73       C  
ATOM   3358  O   VAL B 181     -67.547  18.266  20.468  1.00 16.49           O  
ANISOU 3358  O   VAL B 181     2155   2073   2035     86    -45     78       O  
ATOM   3359  CB  VAL B 181     -66.003  18.522  17.548  1.00 18.03           C  
ANISOU 3359  CB  VAL B 181     2364   2263   2225     91    -47     76       C  
ATOM   3360  CG1 VAL B 181     -65.332  19.513  16.586  1.00 17.79           C  
ANISOU 3360  CG1 VAL B 181     2347   2229   2182     93    -48     80       C  
ATOM   3361  CG2 VAL B 181     -65.029  17.936  18.539  1.00 17.92           C  
ANISOU 3361  CG2 VAL B 181     2350   2238   2223     82    -44     79       C  
ATOM   3362  N   VAL B 182     -68.621  17.364  18.708  1.00 17.46           N  
ANISOU 3362  N   VAL B 182     2266   2213   2157     88    -48     64       N  
ATOM   3363  CA  VAL B 182     -69.159  16.241  19.481  1.00 18.26           C  
ANISOU 3363  CA  VAL B 182     2357   2318   2263     73    -45     60       C  
ATOM   3364  C   VAL B 182     -69.255  15.031  18.584  1.00 18.02           C  
ANISOU 3364  C   VAL B 182     2320   2288   2237     65    -45     53       C  
ATOM   3365  O   VAL B 182     -69.492  15.170  17.360  1.00 17.40           O  
ANISOU 3365  O   VAL B 182     2238   2219   2156     74    -48     47       O  
ATOM   3366  CB  VAL B 182     -70.520  16.612  20.156  1.00 18.60           C  
ANISOU 3366  CB  VAL B 182     2388   2380   2298     74    -43     51       C  
ATOM   3367  CG1 VAL B 182     -71.562  16.993  19.137  1.00 19.76           C  
ANISOU 3367  CG1 VAL B 182     2525   2545   2438     88    -48     37       C  
ATOM   3368  CG2 VAL B 182     -71.032  15.468  21.028  1.00 20.17           C  
ANISOU 3368  CG2 VAL B 182     2582   2584   2499     51    -38     48       C  
ATOM   3369  N   THR B 183     -68.942  13.860  19.126  1.00 17.55           N  
ANISOU 3369  N   THR B 183     2263   2218   2187     50    -45     55       N  
ATOM   3370  CA  THR B 183     -69.179  12.605  18.429  1.00 17.34           C  
ANISOU 3370  CA  THR B 183     2230   2191   2166     40    -47     47       C  
ATOM   3371  C   THR B 183     -70.443  11.996  18.966  1.00 16.94           C  
ANISOU 3371  C   THR B 183     2173   2154   2111     25    -43     41       C  
ATOM   3372  O   THR B 183     -70.691  12.039  20.172  1.00 18.06           O  
ANISOU 3372  O   THR B 183     2318   2294   2248     13    -41     46       O  
ATOM   3373  CB  THR B 183     -68.008  11.602  18.548  1.00 15.94           C  
ANISOU 3373  CB  THR B 183     2062   1991   2003     34    -53     50       C  
ATOM   3374  OG1 THR B 183     -67.669  11.450  19.932  1.00 20.36           O  
ANISOU 3374  OG1 THR B 183     2634   2537   2565     24    -55     61       O  
ATOM   3375  CG2 THR B 183     -66.807  12.122  17.770  1.00 19.66           C  
ANISOU 3375  CG2 THR B 183     2535   2457   2478     47    -54     49       C  
ATOM   3376  N   VAL B 184     -71.265  11.489  18.043  1.00 17.48           N  
ANISOU 3376  N   VAL B 184     2229   2236   2178     23    -42     28       N  
ATOM   3377  CA  VAL B 184     -72.564  10.901  18.309  1.00 17.86           C  
ANISOU 3377  CA  VAL B 184     2266   2301   2218      6    -38     17       C  
ATOM   3378  C   VAL B 184     -72.789   9.638  17.442  1.00 18.59           C  
ANISOU 3378  C   VAL B 184     2354   2392   2317     -5    -39      8       C  
ATOM   3379  O   VAL B 184     -72.100   9.428  16.435  1.00 19.79           O  
ANISOU 3379  O   VAL B 184     2507   2535   2476      6    -43      7       O  
ATOM   3380  CB  VAL B 184     -73.722  11.902  18.058  1.00 17.61           C  
ANISOU 3380  CB  VAL B 184     2217   2299   2175     20    -35      4       C  
ATOM   3381  CG1 VAL B 184     -73.462  13.173  18.816  1.00 19.52           C  
ANISOU 3381  CG1 VAL B 184     2463   2540   2412     33    -36     11       C  
ATOM   3382  CG2 VAL B 184     -73.883  12.168  16.571  1.00 19.31           C  
ANISOU 3382  CG2 VAL B 184     2424   2523   2389     39    -40     -5       C  
ATOM   3383  N   PRO B 185     -73.779   8.823  17.781  1.00 18.69           N  
ANISOU 3383  N   PRO B 185     2362   2416   2325    -27    -34     -1       N  
ATOM   3384  CA  PRO B 185     -73.999   7.686  16.904  1.00 19.10           C  
ANISOU 3384  CA  PRO B 185     2410   2465   2382    -37    -36    -11       C  
ATOM   3385  C   PRO B 185     -74.542   8.160  15.545  1.00 18.83           C  
ANISOU 3385  C   PRO B 185     2357   2455   2345    -18    -35    -26       C  
ATOM   3386  O   PRO B 185     -75.429   9.013  15.511  1.00 18.44           O  
ANISOU 3386  O   PRO B 185     2292   2430   2283     -8    -32    -35       O  
ATOM   3387  CB  PRO B 185     -75.092   6.893  17.632  1.00 19.28           C  
ANISOU 3387  CB  PRO B 185     2430   2498   2395    -69    -29    -19       C  
ATOM   3388  CG  PRO B 185     -74.937   7.305  19.088  1.00 19.02           C  
ANISOU 3388  CG  PRO B 185     2410   2461   2357    -81    -27     -6       C  
ATOM   3389  CD  PRO B 185     -74.660   8.797  18.967  1.00 19.92           C  
ANISOU 3389  CD  PRO B 185     2515   2584   2468    -49    -27     -4       C  
ATOM   3390  N   SER B 186     -74.038   7.613  14.448  1.00 19.63           N  
ANISOU 3390  N   SER B 186     2457   2548   2455    -12    -39    -30       N  
ATOM   3391  CA ASER B 186     -74.574   7.923  13.127  0.50 20.79           C  
ANISOU 3391  CA ASER B 186     2587   2716   2595      3    -40    -44       C  
ATOM   3392  CA BSER B 186     -74.583   7.932  13.129  0.50 19.48           C  
ANISOU 3392  CA BSER B 186     2421   2551   2429      3    -39    -44       C  
ATOM   3393  C   SER B 186     -76.079   7.655  13.089  1.00 21.00           C  
ANISOU 3393  C   SER B 186     2596   2771   2612     -8    -34    -62       C  
ATOM   3394  O   SER B 186     -76.831   8.340  12.385  1.00 20.41           O  
ANISOU 3394  O   SER B 186     2506   2722   2528      8    -35    -74       O  
ATOM   3395  CB ASER B 186     -73.862   7.083  12.079  0.50 21.34           C  
ANISOU 3395  CB ASER B 186     2657   2774   2675      3    -43    -49       C  
ATOM   3396  CB BSER B 186     -73.887   7.117  12.056  0.50 19.83           C  
ANISOU 3396  CB BSER B 186     2466   2584   2483      4    -43    -49       C  
ATOM   3397  OG ASER B 186     -74.317   7.389  10.775  0.50 23.73           O  
ANISOU 3397  OG ASER B 186     2946   3099   2970     16    -44    -61       O  
ATOM   3398  OG BSER B 186     -72.518   7.453  11.975  0.50 14.02           O  
ANISOU 3398  OG BSER B 186     1743   1830   1756     15    -48    -38       O  
ATOM   3399  N   SER B 187     -76.503   6.653  13.852  1.00 21.23           N  
ANISOU 3399  N   SER B 187     2627   2796   2642    -36    -29    -64       N  
ATOM   3400  CA  SER B 187     -77.921   6.270  13.910  1.00 22.10           C  
ANISOU 3400  CA  SER B 187     2720   2935   2741    -54    -21    -85       C  
ATOM   3401  C   SER B 187     -78.866   7.307  14.534  1.00 23.07           C  
ANISOU 3401  C   SER B 187     2827   3087   2850    -48    -17    -94       C  
ATOM   3402  O   SER B 187     -80.087   7.209  14.391  1.00 24.12           O  
ANISOU 3402  O   SER B 187     2938   3252   2973    -56    -12   -117       O  
ATOM   3403  CB  SER B 187     -78.049   4.907  14.594  1.00 21.71           C  
ANISOU 3403  CB  SER B 187     2683   2871   2695    -92    -17    -83       C  
ATOM   3404  OG  SER B 187     -77.613   4.960  15.936  1.00 23.14           O  
ANISOU 3404  OG  SER B 187     2883   3034   2874   -106    -17    -66       O  
ATOM   3405  N   SER B 188     -78.295   8.317  15.183  1.00 22.33           N  
ANISOU 3405  N   SER B 188     2743   2985   2757    -32    -20    -80       N  
ATOM   3406  CA  SER B 188     -79.085   9.382  15.814  1.00 23.23           C  
ANISOU 3406  CA  SER B 188     2843   3125   2860    -23    -18    -91       C  
ATOM   3407  C   SER B 188     -79.333  10.580  14.906  1.00 21.92           C  
ANISOU 3407  C   SER B 188     2665   2973   2689     15    -29    -99       C  
ATOM   3408  O   SER B 188     -80.184  11.439  15.220  1.00 22.72           O  
ANISOU 3408  O   SER B 188     2752   3099   2783     28    -31   -116       O  
ATOM   3409  CB  SER B 188     -78.388   9.885  17.083  1.00 22.54           C  
ANISOU 3409  CB  SER B 188     2772   3019   2772    -27    -17    -73       C  
ATOM   3410  OG  SER B 188     -77.248  10.658  16.770  1.00 24.24           O  
ANISOU 3410  OG  SER B 188     3003   3212   2996     -1    -26    -54       O  
ATOM   3411  N   LEU B 189     -78.615  10.635  13.775  1.00 21.46           N  
ANISOU 3411  N   LEU B 189     2617   2900   2637     32    -37    -90       N  
ATOM   3412  CA  LEU B 189     -78.636  11.835  12.929  1.00 22.21           C  
ANISOU 3412  CA  LEU B 189     2711   3001   2727     66    -49    -91       C  
ATOM   3413  C   LEU B 189     -79.992  12.114  12.299  1.00 22.34           C  
ANISOU 3413  C   LEU B 189     2703   3051   2733     80    -56   -118       C  
ATOM   3414  O   LEU B 189     -80.318  13.274  12.049  1.00 24.58           O  
ANISOU 3414  O   LEU B 189     2986   3344   3010    108    -69   -123       O  
ATOM   3415  CB  LEU B 189     -77.594  11.737  11.816  1.00 20.86           C  
ANISOU 3415  CB  LEU B 189     2556   2811   2561     74    -54    -77       C  
ATOM   3416  CG  LEU B 189     -76.139  11.697  12.305  1.00 21.17           C  
ANISOU 3416  CG  LEU B 189     2616   2818   2608     68    -51    -53       C  
ATOM   3417  CD1 LEU B 189     -75.185  11.573  11.110  1.00 21.91           C  
ANISOU 3417  CD1 LEU B 189     2719   2900   2704     73    -55    -47       C  
ATOM   3418  CD2 LEU B 189     -75.784  12.916  13.164  1.00 20.40           C  
ANISOU 3418  CD2 LEU B 189     2530   2711   2508     80    -55    -41       C  
ATOM   3419  N   GLY B 190     -80.766  11.066  12.030  1.00 22.97           N  
ANISOU 3419  N   GLY B 190     2766   3151   2812     61    -48   -136       N  
ATOM   3420  CA  GLY B 190     -82.057  11.238  11.368  1.00 24.49           C  
ANISOU 3420  CA  GLY B 190     2932   3379   2995     73    -54   -166       C  
ATOM   3421  C   GLY B 190     -83.164  11.754  12.262  1.00 25.17           C  
ANISOU 3421  C   GLY B 190     2996   3495   3074     76    -53   -190       C  
ATOM   3422  O   GLY B 190     -84.209  12.216  11.739  1.00 26.85           O  
ANISOU 3422  O   GLY B 190     3186   3737   3278     96    -64   -218       O  
ATOM   3423  N   THR B 191     -82.980  11.681  13.589  1.00 24.38           N  
ANISOU 3423  N   THR B 191     2901   3389   2975     55    -42   -184       N  
ATOM   3424  CA  THR B 191     -84.063  12.043  14.525  1.00 25.48           C  
ANISOU 3424  CA  THR B 191     3014   3561   3105     50    -37   -212       C  
ATOM   3425  C   THR B 191     -83.661  13.082  15.566  1.00 25.11           C  
ANISOU 3425  C   THR B 191     2977   3504   3059     62    -40   -202       C  
ATOM   3426  O   THR B 191     -84.493  13.905  15.992  1.00 25.73           O  
ANISOU 3426  O   THR B 191     3035   3610   3131     78    -46   -228       O  
ATOM   3427  CB  THR B 191     -84.598  10.816  15.295  1.00 25.68           C  
ANISOU 3427  CB  THR B 191     3029   3602   3125      1    -16   -224       C  
ATOM   3428  OG1 THR B 191     -83.501  10.112  15.896  1.00 25.21           O  
ANISOU 3428  OG1 THR B 191     3001   3507   3073    -25     -8   -191       O  
ATOM   3429  CG2 THR B 191     -85.362   9.875  14.404  1.00 26.39           C  
ANISOU 3429  CG2 THR B 191     3102   3714   3212    -12    -12   -245       C  
ATOM   3430  N   GLN B 192     -82.407  13.039  16.013  1.00 23.89           N  
ANISOU 3430  N   GLN B 192     2853   3313   2912     54    -37   -168       N  
ATOM   3431  CA  GLN B 192     -81.947  13.949  17.044  1.00 23.40           C  
ANISOU 3431  CA  GLN B 192     2800   3240   2851     61    -38   -158       C  
ATOM   3432  C   GLN B 192     -81.570  15.293  16.446  1.00 23.71           C  
ANISOU 3432  C   GLN B 192     2851   3266   2893    105    -58   -150       C  
ATOM   3433  O   GLN B 192     -80.942  15.347  15.364  1.00 24.58           O  
ANISOU 3433  O   GLN B 192     2978   3357   3006    119    -67   -134       O  
ATOM   3434  CB  GLN B 192     -80.740  13.370  17.787  1.00 23.41           C  
ANISOU 3434  CB  GLN B 192     2828   3207   2858     36    -28   -126       C  
ATOM   3435  CG  GLN B 192     -80.237  14.196  19.003  1.00 23.25           C  
ANISOU 3435  CG  GLN B 192     2818   3176   2838     39    -27   -115       C  
ATOM   3436  CD  GLN B 192     -81.304  14.556  20.029  1.00 27.64           C  
ANISOU 3436  CD  GLN B 192     3350   3767   3383     29    -21   -142       C  
ATOM   3437  OE1 GLN B 192     -81.827  13.693  20.736  1.00 33.27           O  
ANISOU 3437  OE1 GLN B 192     4055   4498   4089     -8     -6   -152       O  
ATOM   3438  NE2 GLN B 192     -81.595  15.841  20.145  1.00 28.20           N  
ANISOU 3438  NE2 GLN B 192     3413   3849   3454     62    -32   -155       N  
ATOM   3439  N   THR B 193     -81.970  16.368  17.124  1.00 23.19           N  
ANISOU 3439  N   THR B 193     2777   3211   2823    123    -65   -164       N  
ATOM   3440  CA ATHR B 193     -81.481  17.686  16.757  0.50 23.06           C  
ANISOU 3440  CA ATHR B 193     2778   3174   2809    161    -85   -152       C  
ATOM   3441  CA BTHR B 193     -81.532  17.725  16.818  0.50 22.12           C  
ANISOU 3441  CA BTHR B 193     2658   3057   2690    161    -85   -154       C  
ATOM   3442  C   THR B 193     -80.312  18.110  17.661  1.00 21.76           C  
ANISOU 3442  C   THR B 193     2638   2980   2650    154    -79   -125       C  
ATOM   3443  O   THR B 193     -80.311  17.911  18.889  1.00 22.44           O  
ANISOU 3443  O   THR B 193     2718   3072   2735    132    -66   -126       O  
ATOM   3444  CB ATHR B 193     -82.615  18.739  16.669  0.50 23.52           C  
ANISOU 3444  CB ATHR B 193     2815   3258   2862    195   -104   -186       C  
ATOM   3445  CB BTHR B 193     -82.676  18.723  17.113  0.50 22.25           C  
ANISOU 3445  CB BTHR B 193     2650   3101   2701    189   -100   -189       C  
ATOM   3446  OG1ATHR B 193     -83.504  18.577  17.774  0.50 26.05           O  
ANISOU 3446  OG1ATHR B 193     3106   3612   3179    180    -93   -216       O  
ATOM   3447  OG1BTHR B 193     -83.741  18.498  16.189  0.50 19.44           O  
ANISOU 3447  OG1BTHR B 193     2272   2774   2341    203   -109   -217       O  
ATOM   3448  CG2ATHR B 193     -83.400  18.562  15.372  0.50 24.19           C  
ANISOU 3448  CG2ATHR B 193     2888   3361   2943    213   -118   -204       C  
ATOM   3449  CG2BTHR B 193     -82.205  20.167  17.002  0.50 23.23           C  
ANISOU 3449  CG2BTHR B 193     2797   3202   2828    226   -121   -178       C  
ATOM   3450  N   TYR B 194     -79.290  18.679  17.027  1.00 20.62           N  
ANISOU 3450  N   TYR B 194     2522   2805   2509    170    -89    -99       N  
ATOM   3451  CA  TYR B 194     -78.076  19.097  17.693  1.00 20.16           C  
ANISOU 3451  CA  TYR B 194     2487   2717   2455    164    -85    -73       C  
ATOM   3452  C   TYR B 194     -77.907  20.587  17.552  1.00 20.54           C  
ANISOU 3452  C   TYR B 194     2552   2753   2502    197   -104    -70       C  
ATOM   3453  O   TYR B 194     -77.871  21.109  16.446  1.00 21.88           O  
ANISOU 3453  O   TYR B 194     2733   2912   2666    217   -120    -66       O  
ATOM   3454  CB  TYR B 194     -76.839  18.360  17.103  1.00 17.84           C  
ANISOU 3454  CB  TYR B 194     2214   2397   2166    148    -78    -46       C  
ATOM   3455  CG  TYR B 194     -76.879  16.867  17.403  1.00 18.86           C  
ANISOU 3455  CG  TYR B 194     2334   2533   2300    116    -62    -47       C  
ATOM   3456  CD1 TYR B 194     -76.557  16.392  18.688  1.00 20.15           C  
ANISOU 3456  CD1 TYR B 194     2499   2691   2466     92    -49    -40       C  
ATOM   3457  CD2 TYR B 194     -77.272  15.949  16.436  1.00 15.59           C  
ANISOU 3457  CD2 TYR B 194     1911   2128   1885    109    -61    -55       C  
ATOM   3458  CE1 TYR B 194     -76.591  15.015  19.004  1.00 21.70           C  
ANISOU 3458  CE1 TYR B 194     2693   2888   2664     60    -38    -38       C  
ATOM   3459  CE2 TYR B 194     -77.328  14.566  16.745  1.00 16.07           C  
ANISOU 3459  CE2 TYR B 194     1966   2191   1950     78    -48    -55       C  
ATOM   3460  CZ  TYR B 194     -76.966  14.119  18.041  1.00 20.76           C  
ANISOU 3460  CZ  TYR B 194     2567   2776   2546     54    -37    -46       C  
ATOM   3461  OH  TYR B 194     -77.006  12.782  18.379  1.00 20.76           O  
ANISOU 3461  OH  TYR B 194     2567   2773   2548     22    -28    -45       O  
ATOM   3462  N   ILE B 195     -77.782  21.271  18.667  1.00 20.23           N  
ANISOU 3462  N   ILE B 195     2514   2710   2464    199   -102    -71       N  
ATOM   3463  CA  ILE B 195     -77.726  22.722  18.635  1.00 21.26           C  
ANISOU 3463  CA  ILE B 195     2658   2827   2593    230   -122    -72       C  
ATOM   3464  C   ILE B 195     -76.584  23.123  19.485  1.00 21.14           C  
ANISOU 3464  C   ILE B 195     2663   2788   2582    220   -113    -50       C  
ATOM   3465  O   ILE B 195     -76.516  22.723  20.650  1.00 21.24           O  
ANISOU 3465  O   ILE B 195     2664   2808   2596    200    -98    -52       O  
ATOM   3466  CB  ILE B 195     -79.017  23.327  19.214  1.00 22.03           C  
ANISOU 3466  CB  ILE B 195     2729   2953   2689    250   -132   -108       C  
ATOM   3467  CG1 ILE B 195     -80.208  22.904  18.336  1.00 25.02           C  
ANISOU 3467  CG1 ILE B 195     3084   3359   3063    262   -141   -134       C  
ATOM   3468  CG2 ILE B 195     -78.853  24.854  19.324  1.00 24.02           C  
ANISOU 3468  CG2 ILE B 195     3000   3185   2942    283   -154   -108       C  
ATOM   3469  CD1 ILE B 195     -81.567  23.152  18.971  1.00 28.18           C  
ANISOU 3469  CD1 ILE B 195     3448   3798   3462    274   -146   -178       C  
ATOM   3470  N   CYS B 196     -75.672  23.905  18.943  1.00 21.04           N  
ANISOU 3470  N   CYS B 196     2681   2747   2568    231   -123    -29       N  
ATOM   3471  CA  CYS B 196     -74.624  24.447  19.786  1.00 21.71           C  
ANISOU 3471  CA  CYS B 196     2784   2811   2656    223   -117    -11       C  
ATOM   3472  C   CYS B 196     -75.053  25.821  20.309  1.00 20.88           C  
ANISOU 3472  C   CYS B 196     2682   2701   2550    250   -133    -24       C  
ATOM   3473  O   CYS B 196     -75.572  26.648  19.554  1.00 22.24           O  
ANISOU 3473  O   CYS B 196     2864   2868   2718    277   -157    -32       O  
ATOM   3474  CB  CYS B 196     -73.296  24.471  19.048  1.00 22.84           C  
ANISOU 3474  CB  CYS B 196     2954   2926   2796    213   -114     17       C  
ATOM   3475  SG  CYS B 196     -73.188  25.733  17.826  1.00 25.34           S  
ANISOU 3475  SG  CYS B 196     3304   3223   3104    238   -139     24       S  
ATOM   3476  N   ASN B 197     -74.876  26.019  21.618  1.00 21.25           N  
ANISOU 3476  N   ASN B 197     2722   2752   2602    241   -123    -27       N  
ATOM   3477  CA  ASN B 197     -75.231  27.259  22.289  1.00 21.76           C  
ANISOU 3477  CA  ASN B 197     2786   2814   2667    264   -137    -42       C  
ATOM   3478  C   ASN B 197     -73.975  28.027  22.596  1.00 21.59           C  
ANISOU 3478  C   ASN B 197     2795   2761   2646    260   -136    -18       C  
ATOM   3479  O   ASN B 197     -73.149  27.583  23.375  1.00 20.59           O  
ANISOU 3479  O   ASN B 197     2669   2631   2522    236   -117     -4       O  
ATOM   3480  CB  ASN B 197     -76.008  26.971  23.595  1.00 21.76           C  
ANISOU 3480  CB  ASN B 197     2754   2846   2669    255   -125    -68       C  
ATOM   3481  CG  ASN B 197     -76.924  25.763  23.473  1.00 23.92           C  
ANISOU 3481  CG  ASN B 197     2997   3152   2940    239   -114    -85       C  
ATOM   3482  OD1 ASN B 197     -76.670  24.689  24.056  1.00 22.91           O  
ANISOU 3482  OD1 ASN B 197     2861   3034   2811    206    -93    -77       O  
ATOM   3483  ND2 ASN B 197     -77.960  25.898  22.665  1.00 23.84           N  
ANISOU 3483  ND2 ASN B 197     2974   3158   2928    262   -130   -108       N  
ATOM   3484  N   VAL B 198     -73.811  29.198  21.978  1.00 21.91           N  
ANISOU 3484  N   VAL B 198     2863   2777   2684    284   -158    -13       N  
ATOM   3485  CA  VAL B 198     -72.576  29.938  22.123  1.00 23.06           C  
ANISOU 3485  CA  VAL B 198     3040   2892   2828    277   -156     10       C  
ATOM   3486  C   VAL B 198     -72.886  31.232  22.848  1.00 24.25           C  
ANISOU 3486  C   VAL B 198     3198   3034   2982    300   -172     -4       C  
ATOM   3487  O   VAL B 198     -73.803  31.950  22.452  1.00 24.58           O  
ANISOU 3487  O   VAL B 198     3241   3075   3023    331   -198    -22       O  
ATOM   3488  CB  VAL B 198     -71.915  30.216  20.746  1.00 22.94           C  
ANISOU 3488  CB  VAL B 198     3060   2852   2803    276   -166     32       C  
ATOM   3489  CG1 VAL B 198     -70.624  31.010  20.906  1.00 23.16           C  
ANISOU 3489  CG1 VAL B 198     3121   2852   2828    264   -163     54       C  
ATOM   3490  CG2 VAL B 198     -71.667  28.908  20.010  1.00 23.13           C  
ANISOU 3490  CG2 VAL B 198     3074   2888   2825    255   -151     41       C  
ATOM   3491  N   ASN B 199     -72.165  31.475  23.950  1.00 24.89           N  
ANISOU 3491  N   ASN B 199     3279   3110   3067    286   -158      2       N  
ATOM   3492  CA AASN B 199     -72.307  32.707  24.734  0.50 25.81           C  
ANISOU 3492  CA AASN B 199     3403   3217   3188    306   -171    -11       C  
ATOM   3493  CA BASN B 199     -72.313  32.711  24.710  0.50 25.84           C  
ANISOU 3493  CA BASN B 199     3407   3221   3192    306   -172    -11       C  
ATOM   3494  C   ASN B 199     -71.001  33.474  24.682  1.00 26.19           C  
ANISOU 3494  C   ASN B 199     3488   3230   3232    295   -171     14       C  
ATOM   3495  O   ASN B 199     -69.937  32.934  25.019  1.00 25.99           O  
ANISOU 3495  O   ASN B 199     3466   3203   3207    267   -148     33       O  
ATOM   3496  CB AASN B 199     -72.604  32.435  26.225  0.50 26.33           C  
ANISOU 3496  CB AASN B 199     3436   3309   3260    296   -155    -29       C  
ATOM   3497  CB BASN B 199     -72.751  32.406  26.159  0.50 26.37           C  
ANISOU 3497  CB BASN B 199     3439   3317   3265    298   -156    -32       C  
ATOM   3498  CG AASN B 199     -73.933  31.738  26.477  0.50 27.30           C  
ANISOU 3498  CG AASN B 199     3518   3471   3383    301   -153    -60       C  
ATOM   3499  CG BASN B 199     -73.113  33.652  26.953  0.50 27.81           C  
ANISOU 3499  CG BASN B 199     3620   3494   3451    322   -172    -54       C  
ATOM   3500  OD1AASN B 199     -74.180  31.278  27.598  0.50 30.83           O  
ANISOU 3500  OD1AASN B 199     3939   3944   3831    285   -136    -73       O  
ATOM   3501  OD1BASN B 199     -73.093  34.762  26.434  0.50 30.50           O  
ANISOU 3501  OD1BASN B 199     3989   3807   3792    347   -196    -53       O  
ATOM   3502  ND2AASN B 199     -74.799  31.675  25.469  0.50 31.02           N  
ANISOU 3502  ND2AASN B 199     3986   3948   3853    321   -170    -72       N  
ATOM   3503  ND2BASN B 199     -73.451  33.462  28.226  0.50 30.47           N  
ANISOU 3503  ND2BASN B 199     3928   3858   3792    313   -158    -73       N  
ATOM   3504  N   HIS B 200     -71.067  34.728  24.257  1.00 26.98           N  
ANISOU 3504  N   HIS B 200     3619   3304   3330    318   -196     14       N  
ATOM   3505  CA  HIS B 200     -69.907  35.605  24.316  1.00 27.23           C  
ANISOU 3505  CA  HIS B 200     3687   3302   3356    307   -196     34       C  
ATOM   3506  C   HIS B 200     -70.273  36.808  25.184  1.00 28.92           C  
ANISOU 3506  C   HIS B 200     3905   3506   3577    330   -213     16       C  
ATOM   3507  O   HIS B 200     -70.718  37.848  24.689  1.00 29.15           O  
ANISOU 3507  O   HIS B 200     3961   3512   3605    358   -244      9       O  
ATOM   3508  CB  HIS B 200     -69.451  36.027  22.914  1.00 26.37           C  
ANISOU 3508  CB  HIS B 200     3621   3165   3234    304   -211     56       C  
ATOM   3509  CG  HIS B 200     -68.243  36.908  22.915  1.00 26.35           C  
ANISOU 3509  CG  HIS B 200     3658   3131   3224    287   -210     76       C  
ATOM   3510  ND1 HIS B 200     -67.001  36.499  23.357  1.00 25.94           N  
ANISOU 3510  ND1 HIS B 200     3603   3082   3171    254   -181     91       N  
ATOM   3511  CD2 HIS B 200     -68.104  38.203  22.558  1.00 21.83           C  
ANISOU 3511  CD2 HIS B 200     3127   2523   2643    298   -234     82       C  
ATOM   3512  CE1 HIS B 200     -66.143  37.495  23.224  1.00 24.15           C  
ANISOU 3512  CE1 HIS B 200     3415   2826   2935    243   -186    105       C  
ATOM   3513  NE2 HIS B 200     -66.791  38.543  22.754  1.00 27.14           N  
ANISOU 3513  NE2 HIS B 200     3823   3179   3309    268   -218    101       N  
ATOM   3514  N   LYS B 201     -70.079  36.655  26.488  1.00 29.71           N  
ANISOU 3514  N   LYS B 201     3980   3623   3685    320   -194      6       N  
ATOM   3515  CA  LYS B 201     -70.546  37.676  27.439  1.00 31.87           C  
ANISOU 3515  CA  LYS B 201     4249   3894   3967    343   -208    -18       C  
ATOM   3516  C   LYS B 201     -70.012  39.101  27.227  1.00 32.44           C  
ANISOU 3516  C   LYS B 201     4366   3924   4037    354   -229     -9       C  
ATOM   3517  O   LYS B 201     -70.791  40.059  27.316  1.00 33.49           O  
ANISOU 3517  O   LYS B 201     4505   4046   4175    388   -258    -32       O  
ATOM   3518  CB  LYS B 201     -70.386  37.189  28.882  1.00 32.13           C  
ANISOU 3518  CB  LYS B 201     4248   3955   4006    325   -181    -28       C  
ATOM   3519  CG  LYS B 201     -71.345  36.045  29.213  1.00 35.07           C  
ANISOU 3519  CG  LYS B 201     4576   4370   4379    321   -169    -47       C  
ATOM   3520  CD  LYS B 201     -72.810  36.489  29.120  1.00 40.39           C  
ANISOU 3520  CD  LYS B 201     5229   5060   5058    356   -193    -85       C  
ATOM   3521  CE  LYS B 201     -73.385  36.929  30.456  1.00 41.99           C  
ANISOU 3521  CE  LYS B 201     5401   5286   5266    365   -191   -119       C  
ATOM   3522  NZ  LYS B 201     -73.877  35.749  31.233  1.00 45.65           N  
ANISOU 3522  NZ  LYS B 201     5822   5796   5727    340   -165   -132       N  
ATOM   3523  N   PRO B 202     -68.711  39.260  26.901  1.00 32.66           N  
ANISOU 3523  N   PRO B 202     4427   3927   4056    327   -218     21       N  
ATOM   3524  CA  PRO B 202     -68.207  40.621  26.686  1.00 32.91           C  
ANISOU 3524  CA  PRO B 202     4505   3918   4083    333   -238     29       C  
ATOM   3525  C   PRO B 202     -68.912  41.425  25.599  1.00 33.59           C  
ANISOU 3525  C   PRO B 202     4625   3974   4163    362   -277     27       C  
ATOM   3526  O   PRO B 202     -68.875  42.646  25.632  1.00 33.51           O  
ANISOU 3526  O   PRO B 202     4650   3930   4152    378   -302     25       O  
ATOM   3527  CB  PRO B 202     -66.759  40.398  26.262  1.00 32.34           C  
ANISOU 3527  CB  PRO B 202     4457   3831   3998    293   -216     61       C  
ATOM   3528  CG  PRO B 202     -66.404  39.068  26.779  1.00 32.15           C  
ANISOU 3528  CG  PRO B 202     4395   3843   3979    270   -183     64       C  
ATOM   3529  CD  PRO B 202     -67.642  38.260  26.719  1.00 32.39           C  
ANISOU 3529  CD  PRO B 202     4390   3902   4016    289   -187     45       C  
ATOM   3530  N   SER B 203     -69.521  40.752  24.629  1.00 34.11           N  
ANISOU 3530  N   SER B 203     4685   4051   4224    370   -285     29       N  
ATOM   3531  CA  SER B 203     -70.227  41.438  23.546  1.00 34.70           C  
ANISOU 3531  CA  SER B 203     4793   4099   4291    398   -325     27       C  
ATOM   3532  C   SER B 203     -71.726  41.246  23.684  1.00 36.01           C  
ANISOU 3532  C   SER B 203     4923   4291   4469    439   -345     -8       C  
ATOM   3533  O   SER B 203     -72.507  41.793  22.893  1.00 37.27           O  
ANISOU 3533  O   SER B 203     5102   4432   4625    471   -383    -17       O  
ATOM   3534  CB  SER B 203     -69.778  40.900  22.188  1.00 35.06           C  
ANISOU 3534  CB  SER B 203     4863   4138   4319    376   -321     56       C  
ATOM   3535  OG  SER B 203     -70.404  39.649  21.952  1.00 31.77           O  
ANISOU 3535  OG  SER B 203     4404   3759   3906    377   -307     46       O  
ATOM   3536  N   ASN B 204     -72.124  40.457  24.682  1.00 36.19           N  
ANISOU 3536  N   ASN B 204     4891   4355   4503    435   -320    -30       N  
ATOM   3537  CA  ASN B 204     -73.510  40.082  24.866  1.00 37.46           C  
ANISOU 3537  CA  ASN B 204     5009   4551   4674    465   -331    -67       C  
ATOM   3538  C   ASN B 204     -74.038  39.422  23.589  1.00 37.55           C  
ANISOU 3538  C   ASN B 204     5021   4568   4676    471   -342    -61       C  
ATOM   3539  O   ASN B 204     -75.100  39.787  23.076  1.00 38.40           O  
ANISOU 3539  O   ASN B 204     5128   4676   4786    508   -375    -85       O  
ATOM   3540  CB  ASN B 204     -74.333  41.322  25.260  1.00 38.30           C  
ANISOU 3540  CB  ASN B 204     5120   4643   4790    510   -369   -101       C  
ATOM   3541  CG  ASN B 204     -75.632  40.970  25.928  1.00 40.39           C  
ANISOU 3541  CG  ASN B 204     5327   4953   5066    535   -372   -148       C  
ATOM   3542  OD1 ASN B 204     -76.706  41.390  25.480  1.00 44.56           O  
ANISOU 3542  OD1 ASN B 204     5851   5483   5599    576   -407   -178       O  
ATOM   3543  ND2 ASN B 204     -75.554  40.197  27.006  1.00 42.30           N  
ANISOU 3543  ND2 ASN B 204     5527   5234   5312    509   -335   -158       N  
ATOM   3544  N   THR B 205     -73.255  38.479  23.054  1.00 36.91           N  
ANISOU 3544  N   THR B 205     4945   4492   4586    434   -315    -31       N  
ATOM   3545  CA  THR B 205     -73.628  37.738  21.843  1.00 36.40           C  
ANISOU 3545  CA  THR B 205     4881   4437   4513    434   -319    -23       C  
ATOM   3546  C   THR B 205     -74.075  36.348  22.300  1.00 35.69           C  
ANISOU 3546  C   THR B 205     4738   4394   4429    418   -289    -37       C  
ATOM   3547  O   THR B 205     -73.326  35.630  22.945  1.00 35.65           O  
ANISOU 3547  O   THR B 205     4719   4402   4426    385   -256    -25       O  
ATOM   3548  CB  THR B 205     -72.462  37.636  20.817  1.00 36.17           C  
ANISOU 3548  CB  THR B 205     4895   4381   4467    403   -311     17       C  
ATOM   3549  OG1 THR B 205     -72.047  38.947  20.413  1.00 38.40           O  
ANISOU 3549  OG1 THR B 205     5231   4619   4741    412   -339     31       O  
ATOM   3550  CG2 THR B 205     -72.885  36.863  19.543  1.00 36.26           C  
ANISOU 3550  CG2 THR B 205     4905   4404   4469    402   -316     23       C  
ATOM   3551  N   LYS B 206     -75.321  36.013  22.003  1.00 35.23           N  
ANISOU 3551  N   LYS B 206     4651   4361   4373    442   -303    -65       N  
ATOM   3552  CA  LYS B 206     -75.854  34.675  22.232  1.00 34.28           C  
ANISOU 3552  CA  LYS B 206     4484   4284   4256    426   -278    -79       C  
ATOM   3553  C   LYS B 206     -76.298  34.088  20.920  1.00 33.44           C  
ANISOU 3553  C   LYS B 206     4380   4182   4141    430   -288    -74       C  
ATOM   3554  O   LYS B 206     -77.088  34.700  20.180  1.00 34.53           O  
ANISOU 3554  O   LYS B 206     4530   4314   4277    465   -322    -89       O  
ATOM   3555  CB  LYS B 206     -77.039  34.716  23.195  1.00 34.54           C  
ANISOU 3555  CB  LYS B 206     4473   4353   4299    446   -282   -123       C  
ATOM   3556  CG  LYS B 206     -76.707  34.230  24.586  1.00 37.01           C  
ANISOU 3556  CG  LYS B 206     4757   4688   4616    417   -249   -128       C  
ATOM   3557  CD  LYS B 206     -75.913  35.265  25.388  1.00 39.71           C  
ANISOU 3557  CD  LYS B 206     5122   5004   4962    419   -251   -119       C  
ATOM   3558  CE  LYS B 206     -76.731  35.845  26.531  1.00 39.56           C  
ANISOU 3558  CE  LYS B 206     5071   5007   4952    438   -257   -161       C  
ATOM   3559  NZ  LYS B 206     -77.140  34.789  27.493  1.00 43.22           N  
ANISOU 3559  NZ  LYS B 206     5489   5518   5414    411   -226   -178       N  
ATOM   3560  N   VAL B 207     -75.782  32.904  20.611  1.00 30.63           N  
ANISOU 3560  N   VAL B 207     4018   3840   3783    397   -260    -55       N  
ATOM   3561  CA  VAL B 207     -76.150  32.243  19.379  1.00 29.59           C  
ANISOU 3561  CA  VAL B 207     3885   3715   3643    398   -266    -51       C  
ATOM   3562  C   VAL B 207     -76.440  30.777  19.657  1.00 28.94           C  
ANISOU 3562  C   VAL B 207     3762   3669   3564    372   -236    -59       C  
ATOM   3563  O   VAL B 207     -75.650  30.099  20.310  1.00 29.07           O  
ANISOU 3563  O   VAL B 207     3773   3689   3584    341   -207    -44       O  
ATOM   3564  CB  VAL B 207     -75.022  32.338  18.316  1.00 29.09           C  
ANISOU 3564  CB  VAL B 207     3866   3620   3567    379   -266    -13       C  
ATOM   3565  CG1 VAL B 207     -75.469  31.713  16.995  1.00 30.22           C  
ANISOU 3565  CG1 VAL B 207     4010   3773   3701    382   -274    -11       C  
ATOM   3566  CG2 VAL B 207     -74.591  33.793  18.076  1.00 30.24           C  
ANISOU 3566  CG2 VAL B 207     4059   3724   3705    396   -293      0       C  
ATOM   3567  N   ASP B 208     -77.579  30.320  19.157  1.00 27.84           N  
ANISOU 3567  N   ASP B 208     3598   3557   3424    387   -246    -83       N  
ATOM   3568  CA  ASP B 208     -77.945  28.909  19.115  1.00 28.18           C  
ANISOU 3568  CA  ASP B 208     3608   3632   3468    363   -222    -90       C  
ATOM   3569  C   ASP B 208     -77.910  28.512  17.649  1.00 27.96           C  
ANISOU 3569  C   ASP B 208     3596   3598   3431    364   -231    -77       C  
ATOM   3570  O   ASP B 208     -78.606  29.107  16.815  1.00 30.74           O  
ANISOU 3570  O   ASP B 208     3957   3947   3778    395   -261    -89       O  
ATOM   3571  CB  ASP B 208     -79.335  28.694  19.704  1.00 29.10           C  
ANISOU 3571  CB  ASP B 208     3680   3789   3588    377   -225   -134       C  
ATOM   3572  CG  ASP B 208     -79.414  29.112  21.159  1.00 31.20           C  
ANISOU 3572  CG  ASP B 208     3929   4066   3860    374   -215   -150       C  
ATOM   3573  OD1 ASP B 208     -78.565  28.665  21.949  1.00 32.92           O  
ANISOU 3573  OD1 ASP B 208     4150   4279   4080    343   -190   -131       O  
ATOM   3574  OD2 ASP B 208     -80.311  29.918  21.506  1.00 34.95           O  
ANISOU 3574  OD2 ASP B 208     4388   4553   4338    405   -236   -185       O  
ATOM   3575  N   LYS B 209     -77.069  27.541  17.315  1.00 26.34           N  
ANISOU 3575  N   LYS B 209     3396   3389   3224    332   -208    -53       N  
ATOM   3576  CA  LYS B 209     -76.952  27.156  15.905  1.00 24.45           C  
ANISOU 3576  CA  LYS B 209     3171   3144   2976    330   -215    -40       C  
ATOM   3577  C   LYS B 209     -77.283  25.697  15.748  1.00 25.20           C  
ANISOU 3577  C   LYS B 209     3235   3266   3073    308   -193    -48       C  
ATOM   3578  O   LYS B 209     -76.639  24.858  16.363  1.00 24.34           O  
ANISOU 3578  O   LYS B 209     3119   3160   2970    278   -168    -38       O  
ATOM   3579  CB  LYS B 209     -75.558  27.475  15.345  1.00 24.32           C  
ANISOU 3579  CB  LYS B 209     3195   3095   2952    313   -211     -5       C  
ATOM   3580  CG  LYS B 209     -75.319  27.012  13.881  1.00 25.48           C  
ANISOU 3580  CG  LYS B 209     3356   3239   3087    305   -214      7       C  
ATOM   3581  CD  LYS B 209     -76.102  27.804  12.833  1.00 30.55           C  
ANISOU 3581  CD  LYS B 209     4017   3876   3717    336   -249      1       C  
ATOM   3582  CE  LYS B 209     -75.757  29.296  12.931  1.00 33.38           C  
ANISOU 3582  CE  LYS B 209     4415   4200   4068    353   -273     12       C  
ATOM   3583  NZ  LYS B 209     -76.370  30.116  11.819  1.00 36.07           N  
ANISOU 3583  NZ  LYS B 209     4784   4527   4394    381   -312     11       N  
ATOM   3584  N   LYS B 210     -78.286  25.404  14.919  1.00 24.46           N  
ANISOU 3584  N   LYS B 210     3127   3193   2975    322   -206    -67       N  
ATOM   3585  CA  LYS B 210     -78.655  24.019  14.607  1.00 25.24           C  
ANISOU 3585  CA  LYS B 210     3198   3316   3075    301   -188    -76       C  
ATOM   3586  C   LYS B 210     -77.636  23.491  13.612  1.00 24.75           C  
ANISOU 3586  C   LYS B 210     3158   3237   3008    282   -180    -48       C  
ATOM   3587  O   LYS B 210     -77.299  24.175  12.617  1.00 24.72           O  
ANISOU 3587  O   LYS B 210     3184   3215   2994    294   -198    -34       O  
ATOM   3588  CB  LYS B 210     -80.085  23.913  14.066  1.00 26.04           C  
ANISOU 3588  CB  LYS B 210     3273   3447   3173    324   -204   -109       C  
ATOM   3589  CG  LYS B 210     -80.561  22.481  13.850  1.00 30.55           C  
ANISOU 3589  CG  LYS B 210     3814   4047   3745    299   -185   -121       C  
ATOM   3590  CD  LYS B 210     -82.093  22.421  13.812  1.00 35.01           C  
ANISOU 3590  CD  LYS B 210     4344   4651   4309    318   -196   -163       C  
ATOM   3591  CE  LYS B 210     -82.700  23.368  12.774  1.00 38.93           C  
ANISOU 3591  CE  LYS B 210     4850   5144   4797    360   -232   -174       C  
ATOM   3592  NZ  LYS B 210     -82.842  22.769  11.408  1.00 42.90           N  
ANISOU 3592  NZ  LYS B 210     5356   5652   5292    359   -238   -170       N  
ATOM   3593  N   VAL B 211     -77.115  22.305  13.916  1.00 23.63           N  
ANISOU 3593  N   VAL B 211     3006   3100   2874    251   -154    -41       N  
ATOM   3594  CA  VAL B 211     -76.110  21.618  13.106  1.00 23.64           C  
ANISOU 3594  CA  VAL B 211     3021   3089   2873    230   -143    -20       C  
ATOM   3595  C   VAL B 211     -76.786  20.365  12.531  1.00 25.46           C  
ANISOU 3595  C   VAL B 211     3226   3343   3104    219   -136    -35       C  
ATOM   3596  O   VAL B 211     -77.109  19.424  13.245  1.00 25.25           O  
ANISOU 3596  O   VAL B 211     3178   3331   3087    201   -120    -45       O  
ATOM   3597  CB  VAL B 211     -74.866  21.257  13.943  1.00 23.14           C  
ANISOU 3597  CB  VAL B 211     2966   3009   2818    205   -123     -1       C  
ATOM   3598  CG1 VAL B 211     -73.786  20.597  13.070  1.00 22.37           C  
ANISOU 3598  CG1 VAL B 211     2880   2900   2719    186   -114     14       C  
ATOM   3599  CG2 VAL B 211     -74.298  22.483  14.650  1.00 21.40           C  
ANISOU 3599  CG2 VAL B 211     2766   2768   2596    215   -130     10       C  
ATOM   3600  N   GLU B 212     -76.960  20.379  11.218  1.00 27.95           N  
ANISOU 3600  N   GLU B 212     3549   3662   3411    228   -147    -35       N  
ATOM   3601  CA  GLU B 212     -77.899  19.532  10.517  1.00 30.79           C  
ANISOU 3601  CA  GLU B 212     3884   4046   3768    227   -148    -55       C  
ATOM   3602  C   GLU B 212     -77.147  18.781   9.442  1.00 30.75           C  
ANISOU 3602  C   GLU B 212     3888   4036   3760    210   -140    -43       C  
ATOM   3603  O   GLU B 212     -76.211  19.327   8.873  1.00 30.15           O  
ANISOU 3603  O   GLU B 212     3839   3940   3676    209   -145    -24       O  
ATOM   3604  CB  GLU B 212     -78.877  20.459   9.802  1.00 32.32           C  
ANISOU 3604  CB  GLU B 212     4080   4249   3950    261   -176    -69       C  
ATOM   3605  CG  GLU B 212     -80.209  19.854   9.461  1.00 37.11           C  
ANISOU 3605  CG  GLU B 212     4655   4890   4557    268   -180   -100       C  
ATOM   3606  CD  GLU B 212     -81.295  20.879   9.581  1.00 40.94           C  
ANISOU 3606  CD  GLU B 212     5132   5386   5037    305   -206   -123       C  
ATOM   3607  OE1 GLU B 212     -81.107  22.009   9.073  1.00 43.90           O  
ANISOU 3607  OE1 GLU B 212     5536   5741   5402    329   -232   -112       O  
ATOM   3608  OE2 GLU B 212     -82.327  20.551  10.208  1.00 46.49           O  
ANISOU 3608  OE2 GLU B 212     5801   6119   5745    307   -202   -153       O  
ATOM   3609  N   PRO B 213     -77.576  17.541   9.130  1.00 31.88           N  
ANISOU 3609  N   PRO B 213     4008   4197   3908    195   -129    -56       N  
ATOM   3610  CA  PRO B 213     -76.987  16.848   7.995  1.00 33.16           C  
ANISOU 3610  CA  PRO B 213     4175   4357   4067    182   -124    -50       C  
ATOM   3611  C   PRO B 213     -77.209  17.578   6.678  1.00 34.67           C  
ANISOU 3611  C   PRO B 213     4382   4552   4241    199   -144    -49       C  
ATOM   3612  O   PRO B 213     -76.249  17.789   5.929  1.00 35.67           O  
ANISOU 3612  O   PRO B 213     4530   4665   4358    191   -144    -33       O  
ATOM   3613  CB  PRO B 213     -77.737  15.517   7.978  1.00 32.64           C  
ANISOU 3613  CB  PRO B 213     4080   4314   4009    167   -112    -70       C  
ATOM   3614  CG  PRO B 213     -78.163  15.319   9.382  1.00 31.84           C  
ANISOU 3614  CG  PRO B 213     3965   4216   3918    160   -103    -77       C  
ATOM   3615  CD  PRO B 213     -78.499  16.670   9.883  1.00 31.95           C  
ANISOU 3615  CD  PRO B 213     3987   4228   3926    184   -118    -78       C  
ATOM   3616  N   LYS B 214     -78.453  17.981   6.412  1.00 37.01           N  
ANISOU 3616  N   LYS B 214     4666   4866   4530    223   -162    -67       N  
ATOM   3617  CA  LYS B 214     -78.902  18.288   5.026  1.00 39.16           C  
ANISOU 3617  CA  LYS B 214     4946   5147   4785    238   -182    -71       C  
ATOM   3618  C   LYS B 214     -78.051  17.613   3.935  1.00 39.19           C  
ANISOU 3618  C   LYS B 214     4959   5149   4782    216   -172    -61       C  
ATOM   3619  O   LYS B 214     -78.177  16.407   3.691  1.00 40.31           O  
ANISOU 3619  O   LYS B 214     5077   5306   4931    199   -156    -73       O  
ATOM   3620  CB  LYS B 214     -79.052  19.802   4.768  1.00 39.89           C  
ANISOU 3620  CB  LYS B 214     5068   5225   4862    267   -211    -63       C  
ATOM   3621  CG  LYS B 214     -79.570  20.143   3.349  1.00 42.21           C  
ANISOU 3621  CG  LYS B 214     5375   5528   5136    283   -236    -66       C  
ATOM   3622  CD  LYS B 214     -78.439  20.559   2.403  1.00 44.08           C  
ANISOU 3622  CD  LYS B 214     5650   5743   5354    268   -239    -39       C  
ATOM   3623  CE  LYS B 214     -78.665  20.133   0.943  1.00 44.71           C  
ANISOU 3623  CE  LYS B 214     5732   5840   5418    263   -247    -43       C  
ATOM   3624  NZ  LYS B 214     -78.581  18.644   0.728  1.00 45.13           N  
ANISOU 3624  NZ  LYS B 214     5751   5914   5482    239   -220    -56       N  
TER    3625      LYS B 214                                                      
ATOM   3626  N   VAL C   3     -35.459  31.645  41.658  1.00 36.86           N  
ANISOU 3626  N   VAL C   3     4781   4580   4645   -242    -93      9       N  
ATOM   3627  CA  VAL C   3     -35.262  30.624  40.566  1.00 35.56           C  
ANISOU 3627  CA  VAL C   3     4598   4446   4467   -238    -80     16       C  
ATOM   3628  C   VAL C   3     -35.380  29.143  41.003  1.00 34.15           C  
ANISOU 3628  C   VAL C   3     4403   4287   4284   -208    -69      1       C  
ATOM   3629  O   VAL C   3     -34.360  28.468  41.211  1.00 35.26           O  
ANISOU 3629  O   VAL C   3     4524   4459   4413   -208    -63     -7       O  
ATOM   3630  CB  VAL C   3     -33.984  30.882  39.694  1.00 36.12           C  
ANISOU 3630  CB  VAL C   3     4653   4549   4522   -271    -78     28       C  
ATOM   3631  CG1 VAL C   3     -34.360  31.159  38.248  1.00 35.23           C  
ANISOU 3631  CG1 VAL C   3     4546   4436   4404   -284    -78     48       C  
ATOM   3632  CG2 VAL C   3     -33.127  32.020  40.249  1.00 37.90           C  
ANISOU 3632  CG2 VAL C   3     4884   4769   4748   -303    -88     31       C  
ATOM   3633  N   LEU C   4     -36.631  28.664  41.136  1.00 31.59           N  
ANISOU 3633  N   LEU C   4     4090   3945   3968   -182    -68     -3       N  
ATOM   3634  CA  LEU C   4     -36.944  27.251  41.455  1.00 26.37           C  
ANISOU 3634  CA  LEU C   4     3419   3296   3303   -155    -61    -13       C  
ATOM   3635  C   LEU C   4     -37.170  26.423  40.204  1.00 24.02           C  
ANISOU 3635  C   LEU C   4     3115   3013   2997   -148    -55     -6       C  
ATOM   3636  O   LEU C   4     -38.086  26.683  39.425  1.00 24.77           O  
ANISOU 3636  O   LEU C   4     3221   3094   3097   -147    -56      4       O  
ATOM   3637  CB  LEU C   4     -38.156  27.084  42.388  1.00 25.51           C  
ANISOU 3637  CB  LEU C   4     3322   3166   3205   -134    -64    -21       C  
ATOM   3638  CG  LEU C   4     -38.303  27.993  43.596  1.00 23.56           C  
ANISOU 3638  CG  LEU C   4     3084   2900   2968   -136    -72    -30       C  
ATOM   3639  CD1 LEU C   4     -39.490  27.585  44.486  1.00 23.52           C  
ANISOU 3639  CD1 LEU C   4     3085   2884   2968   -112    -73    -39       C  
ATOM   3640  CD2 LEU C   4     -37.007  28.064  44.389  1.00 26.10           C  
ANISOU 3640  CD2 LEU C   4     3394   3237   3285   -146    -72    -38       C  
ATOM   3641  N   THR C   5     -36.361  25.390  40.043  1.00 21.52           N  
ANISOU 3641  N   THR C   5     2781   2727   2669   -141    -50    -13       N  
ATOM   3642  CA ATHR C   5     -36.496  24.598  38.818  0.50 21.01           C  
ANISOU 3642  CA ATHR C   5     2709   2678   2595   -133    -46     -8       C  
ATOM   3643  CA BTHR C   5     -36.376  24.551  38.839  0.50 20.17           C  
ANISOU 3643  CA BTHR C   5     2601   2574   2487   -133    -46     -9       C  
ATOM   3644  C   THR C   5     -37.242  23.291  39.014  1.00 20.22           C  
ANISOU 3644  C   THR C   5     2612   2574   2496   -105    -46    -16       C  
ATOM   3645  O   THR C   5     -37.004  22.525  39.940  1.00 19.68           O  
ANISOU 3645  O   THR C   5     2541   2510   2428    -91    -48    -28       O  
ATOM   3646  CB ATHR C   5     -35.173  24.424  38.036  0.50 22.14           C  
ANISOU 3646  CB ATHR C   5     2831   2861   2721   -144    -43     -8       C  
ATOM   3647  CB BTHR C   5     -34.916  24.152  38.475  0.50 20.56           C  
ANISOU 3647  CB BTHR C   5     2627   2664   2519   -139    -43    -15       C  
ATOM   3648  OG1ATHR C   5     -34.211  23.765  38.850  0.50 24.12           O  
ANISOU 3648  OG1ATHR C   5     3067   3132   2964   -135    -43    -24       O  
ATOM   3649  OG1BTHR C   5     -34.111  25.342  38.350  0.50 20.24           O  
ANISOU 3649  OG1BTHR C   5     2582   2632   2475   -170    -43     -6       O  
ATOM   3650  CG2ATHR C   5     -34.618  25.776  37.626  0.50 21.58           C  
ANISOU 3650  CG2ATHR C   5     2759   2792   2647   -178    -44      5       C  
ATOM   3651  CG2BTHR C   5     -34.864  23.333  37.179  0.50 19.43           C  
ANISOU 3651  CG2BTHR C   5     2473   2545   2364   -129    -40    -14       C  
ATOM   3652  N   GLN C   6     -38.199  23.085  38.119  1.00 18.00           N  
ANISOU 3652  N   GLN C   6     2338   2284   2217    -99    -45     -8       N  
ATOM   3653  CA  GLN C   6     -39.014  21.876  38.098  1.00 16.98           C  
ANISOU 3653  CA  GLN C   6     2214   2150   2089    -76    -47    -13       C  
ATOM   3654  C   GLN C   6     -38.908  21.268  36.723  1.00 17.29           C  
ANISOU 3654  C   GLN C   6     2246   2207   2118    -71    -45    -10       C  
ATOM   3655  O   GLN C   6     -38.802  21.978  35.742  1.00 18.18           O  
ANISOU 3655  O   GLN C   6     2355   2325   2227    -85    -42      1       O  
ATOM   3656  CB  GLN C   6     -40.489  22.189  38.339  1.00 16.90           C  
ANISOU 3656  CB  GLN C   6     2219   2111   2090    -72    -48     -7       C  
ATOM   3657  CG  GLN C   6     -40.853  22.657  39.743  1.00 18.69           C  
ANISOU 3657  CG  GLN C   6     2454   2322   2326    -71    -51    -12       C  
ATOM   3658  CD  GLN C   6     -42.339  22.936  39.800  1.00 15.76           C  
ANISOU 3658  CD  GLN C   6     2095   1930   1961    -65    -53     -8       C  
ATOM   3659  OE1 GLN C   6     -42.777  24.064  40.029  1.00 15.12           O  
ANISOU 3659  OE1 GLN C   6     2023   1834   1888    -71    -55     -6       O  
ATOM   3660  NE2 GLN C   6     -43.117  21.898  39.606  1.00 15.66           N  
ANISOU 3660  NE2 GLN C   6     2085   1919   1947    -52    -53     -7       N  
ATOM   3661  N   PRO C   7     -38.990  19.933  36.648  1.00 17.82           N  
ANISOU 3661  N   PRO C   7     2310   2280   2180    -50    -50    -18       N  
ATOM   3662  CA  PRO C   7     -39.071  19.311  35.334  1.00 17.98           C  
ANISOU 3662  CA  PRO C   7     2325   2314   2191    -42    -50    -17       C  
ATOM   3663  C   PRO C   7     -40.367  19.769  34.657  1.00 17.53           C  
ANISOU 3663  C   PRO C   7     2281   2238   2143    -46    -47     -4       C  
ATOM   3664  O   PRO C   7     -41.433  19.852  35.272  1.00 17.61           O  
ANISOU 3664  O   PRO C   7     2305   2224   2163    -43    -49     -1       O  
ATOM   3665  CB  PRO C   7     -39.105  17.797  35.656  1.00 17.75           C  
ANISOU 3665  CB  PRO C   7     2298   2286   2160    -18    -59    -30       C  
ATOM   3666  CG  PRO C   7     -39.569  17.713  37.083  1.00 17.93           C  
ANISOU 3666  CG  PRO C   7     2333   2288   2193    -17    -63    -32       C  
ATOM   3667  CD  PRO C   7     -39.054  18.974  37.754  1.00 19.08           C  
ANISOU 3667  CD  PRO C   7     2475   2433   2342    -35    -56    -29       C  
ATOM   3668  N   PRO C   8     -40.289  20.067  33.364  1.00 17.64           N  
ANISOU 3668  N   PRO C   8     2288   2265   2150    -52    -43      4       N  
ATOM   3669  CA  PRO C   8     -41.532  20.485  32.729  1.00 17.89           C  
ANISOU 3669  CA  PRO C   8     2332   2278   2188    -54    -42     16       C  
ATOM   3670  C   PRO C   8     -42.613  19.398  32.585  1.00 17.56           C  
ANISOU 3670  C   PRO C   8     2299   2225   2149    -35    -46     12       C  
ATOM   3671  O   PRO C   8     -43.823  19.707  32.540  1.00 16.95           O  
ANISOU 3671  O   PRO C   8     2234   2128   2080    -35    -45     20       O  
ATOM   3672  CB  PRO C   8     -41.070  20.963  31.343  1.00 19.15           C  
ANISOU 3672  CB  PRO C   8     2481   2458   2336    -66    -37     25       C  
ATOM   3673  CG  PRO C   8     -39.754  20.434  31.169  1.00 20.30           C  
ANISOU 3673  CG  PRO C   8     2608   2638   2468    -64    -37     14       C  
ATOM   3674  CD  PRO C   8     -39.110  20.245  32.492  1.00 18.61           C  
ANISOU 3674  CD  PRO C   8     2392   2422   2257    -61    -40      3       C  
ATOM   3675  N   SER C   9     -42.180  18.141  32.522  1.00 17.63           N  
ANISOU 3675  N   SER C   9     2302   2246   2151    -19    -52      0       N  
ATOM   3676  CA  SER C   9     -43.090  17.055  32.308  1.00 17.18           C  
ANISOU 3676  CA  SER C   9     2254   2178   2094     -4    -59     -2       C  
ATOM   3677  C   SER C   9     -42.705  15.920  33.199  1.00 17.25           C  
ANISOU 3677  C   SER C   9     2266   2187   2103      9    -69    -15       C  
ATOM   3678  O   SER C   9     -41.514  15.598  33.326  1.00 18.68           O  
ANISOU 3678  O   SER C   9     2436   2385   2275     15    -72    -26       O  
ATOM   3679  CB  SER C   9     -43.006  16.590  30.846  1.00 17.59           C  
ANISOU 3679  CB  SER C   9     2298   2249   2137      4    -59     -3       C  
ATOM   3680  OG  SER C   9     -43.745  15.404  30.623  1.00 18.60           O  
ANISOU 3680  OG  SER C   9     2435   2367   2265     20    -69     -8       O  
ATOM   3681  N   VAL C  11     -43.715  15.260  33.858  1.00 16.44           N  
ANISOU 3681  N   VAL C  11     2178   2063   2006     14    -76    -13       N  
ATOM   3682  CA  VAL C  11     -43.529  13.965  34.543  1.00 16.22           C  
ANISOU 3682  CA  VAL C  11     2157   2030   1976     27    -91    -22       C  
ATOM   3683  C   VAL C  11     -44.715  13.110  34.107  1.00 15.77           C  
ANISOU 3683  C   VAL C  11     2113   1958   1920     32    -99    -18       C  
ATOM   3684  O   VAL C  11     -45.775  13.634  33.853  1.00 16.25           O  
ANISOU 3684  O   VAL C  11     2177   2011   1986     23    -92     -8       O  
ATOM   3685  CB  VAL C  11     -43.466  14.129  36.122  1.00 16.59           C  
ANISOU 3685  CB  VAL C  11     2209   2067   2029     20    -92    -22       C  
ATOM   3686  CG1 VAL C  11     -43.518  12.805  36.860  1.00 19.64           C  
ANISOU 3686  CG1 VAL C  11     2607   2443   2413     30   -109    -28       C  
ATOM   3687  CG2 VAL C  11     -42.191  14.828  36.503  1.00 18.99           C  
ANISOU 3687  CG2 VAL C  11     2500   2385   2329     16    -86    -29       C  
ATOM   3688  N   SER C  12     -44.543  11.776  33.982  1.00 15.48           N  
ANISOU 3688  N   SER C  12     2084   1918   1879     46   -116    -27       N  
ATOM   3689  CA  SER C  12     -45.576  10.858  33.593  1.00 16.27           C  
ANISOU 3689  CA  SER C  12     2198   2004   1979     50   -127    -23       C  
ATOM   3690  C   SER C  12     -45.579   9.657  34.479  1.00 15.14           C  
ANISOU 3690  C   SER C  12     2071   1847   1836     54   -148    -26       C  
ATOM   3691  O   SER C  12     -44.530   9.178  34.911  1.00 18.05           O  
ANISOU 3691  O   SER C  12     2439   2218   2200     66   -158    -38       O  
ATOM   3692  CB  SER C  12     -45.375  10.342  32.143  1.00 16.38           C  
ANISOU 3692  CB  SER C  12     2208   2029   1988     65   -133    -31       C  
ATOM   3693  OG  SER C  12     -45.233  11.388  31.200  1.00 19.87           O  
ANISOU 3693  OG  SER C  12     2634   2488   2427     60   -116    -27       O  
ATOM   3694  N   GLY C  13     -46.778   9.134  34.685  1.00 15.24           N  
ANISOU 3694  N   GLY C  13     2097   1842   1850     45   -155    -16       N  
ATOM   3695  CA  GLY C  13     -46.953   7.833  35.354  1.00 14.40           C  
ANISOU 3695  CA  GLY C  13     2011   1719   1742     47   -179    -16       C  
ATOM   3696  C   GLY C  13     -48.300   7.276  35.008  1.00 13.57           C  
ANISOU 3696  C   GLY C  13     1918   1601   1637     36   -186     -5       C  
ATOM   3697  O   GLY C  13     -49.237   8.014  34.621  1.00 14.29           O  
ANISOU 3697  O   GLY C  13     2002   1698   1730     25   -171      4       O  
ATOM   3698  N   ALA C  14     -48.436   5.970  35.156  1.00 13.98           N  
ANISOU 3698  N   ALA C  14     1990   1636   1686     39   -212     -6       N  
ATOM   3699  CA  ALA C  14     -49.699   5.283  34.894  1.00 15.23           C  
ANISOU 3699  CA  ALA C  14     2163   1781   1843     25   -224      6       C  
ATOM   3700  C   ALA C  14     -50.579   5.283  36.131  1.00 15.10           C  
ANISOU 3700  C   ALA C  14     2153   1761   1825      0   -224     23       C  
ATOM   3701  O   ALA C  14     -50.075   5.453  37.240  1.00 15.66           O  
ANISOU 3701  O   ALA C  14     2223   1833   1895     -4   -223     24       O  
ATOM   3702  CB  ALA C  14     -49.398   3.846  34.504  1.00 16.46           C  
ANISOU 3702  CB  ALA C  14     2340   1917   1995     39   -256     -3       C  
ATOM   3703  N   PRO C  15     -51.891   5.042  35.961  1.00 14.37           N  
ANISOU 3703  N   PRO C  15     2065   1666   1729    -19   -226     36       N  
ATOM   3704  CA  PRO C  15     -52.726   5.025  37.150  1.00 17.07           C  
ANISOU 3704  CA  PRO C  15     2409   2010   2065    -45   -227     52       C  
ATOM   3705  C   PRO C  15     -52.217   3.962  38.156  1.00 16.09           C  
ANISOU 3705  C   PRO C  15     2306   1870   1937    -50   -253     55       C  
ATOM   3706  O   PRO C  15     -51.842   2.836  37.769  1.00 17.14           O  
ANISOU 3706  O   PRO C  15     2459   1982   2070    -41   -279     51       O  
ATOM   3707  CB  PRO C  15     -54.096   4.707  36.595  1.00 17.47           C  
ANISOU 3707  CB  PRO C  15     2464   2063   2112    -61   -230     63       C  
ATOM   3708  CG  PRO C  15     -54.069   5.266  35.154  1.00 16.09           C  
ANISOU 3708  CG  PRO C  15     2278   1894   1943    -43   -216     53       C  
ATOM   3709  CD  PRO C  15     -52.640   4.994  34.692  1.00 14.81           C  
ANISOU 3709  CD  PRO C  15     2119   1723   1785    -17   -224     36       C  
ATOM   3710  N   GLY C  16     -52.163   4.318  39.449  1.00 15.65           N  
ANISOU 3710  N   GLY C  16     2245   1822   1878    -63   -247     62       N  
ATOM   3711  CA  GLY C  16     -51.613   3.397  40.450  1.00 17.60           C  
ANISOU 3711  CA  GLY C  16     2511   2054   2121    -67   -271     66       C  
ATOM   3712  C   GLY C  16     -50.145   3.592  40.767  1.00 17.61           C  
ANISOU 3712  C   GLY C  16     2510   2055   2128    -44   -271     50       C  
ATOM   3713  O   GLY C  16     -49.666   3.236  41.852  1.00 18.79           O  
ANISOU 3713  O   GLY C  16     2667   2198   2273    -48   -282     54       O  
ATOM   3714  N   GLN C  17     -49.405   4.168  39.843  1.00 17.02           N  
ANISOU 3714  N   GLN C  17     2422   1986   2059    -20   -258     34       N  
ATOM   3715  CA  GLN C  17     -47.989   4.431  40.000  1.00 15.41           C  
ANISOU 3715  CA  GLN C  17     2211   1786   1858      2   -255     17       C  
ATOM   3716  C   GLN C  17     -47.697   5.503  41.046  1.00 16.63           C  
ANISOU 3716  C   GLN C  17     2348   1957   2013     -5   -234     19       C  
ATOM   3717  O   GLN C  17     -48.546   6.356  41.282  1.00 16.00           O  
ANISOU 3717  O   GLN C  17     2256   1890   1934    -21   -215     28       O  
ATOM   3718  CB  GLN C  17     -47.420   4.841  38.627  1.00 18.12           C  
ANISOU 3718  CB  GLN C  17     2542   2139   2206     25   -245      1       C  
ATOM   3719  CG  GLN C  17     -45.922   4.681  38.541  1.00 19.50           C  
ANISOU 3719  CG  GLN C  17     2713   2318   2379     51   -252    -18       C  
ATOM   3720  CD  GLN C  17     -45.350   4.699  37.115  1.00 15.62           C  
ANISOU 3720  CD  GLN C  17     2212   1836   1887     74   -250    -34       C  
ATOM   3721  OE1 GLN C  17     -46.039   4.780  36.061  1.00 17.95           O  
ANISOU 3721  OE1 GLN C  17     2505   2133   2184     73   -244    -32       O  
ATOM   3722  NE2 GLN C  17     -44.065   4.623  37.080  1.00 17.44           N  
ANISOU 3722  NE2 GLN C  17     2434   2077   2114     95   -254    -52       N  
ATOM   3723  N   ARG C  18     -46.503   5.478  41.631  1.00 16.96           N  
ANISOU 3723  N   ARG C  18     2388   2000   2055      8   -238      8       N  
ATOM   3724  CA  ARG C  18     -46.008   6.626  42.429  1.00 17.82           C  
ANISOU 3724  CA  ARG C  18     2478   2127   2166      5   -217      5       C  
ATOM   3725  C   ARG C  18     -45.077   7.462  41.576  1.00 17.59           C  
ANISOU 3725  C   ARG C  18     2431   2111   2141     23   -201    -10       C  
ATOM   3726  O   ARG C  18     -44.136   6.955  40.978  1.00 18.18           O  
ANISOU 3726  O   ARG C  18     2507   2186   2214     43   -211    -24       O  
ATOM   3727  CB  ARG C  18     -45.249   6.154  43.671  1.00 19.91           C  
ANISOU 3727  CB  ARG C  18     2751   2388   2427      7   -231      3       C  
ATOM   3728  CG  ARG C  18     -44.665   7.304  44.552  1.00 22.60           C  
ANISOU 3728  CG  ARG C  18     3072   2746   2769      5   -210     -2       C  
ATOM   3729  CD  ARG C  18     -43.912   6.696  45.743  1.00 24.72           C  
ANISOU 3729  CD  ARG C  18     3349   3010   3032      8   -226     -3       C  
ATOM   3730  NE  ARG C  18     -43.208   7.702  46.564  1.00 25.88           N  
ANISOU 3730  NE  ARG C  18     3479   3175   3181      8   -210    -11       N  
ATOM   3731  CZ  ARG C  18     -41.945   8.079  46.360  1.00 28.99           C  
ANISOU 3731  CZ  ARG C  18     3860   3577   3576     25   -204    -27       C  
ATOM   3732  NH1 ARG C  18     -41.228   7.561  45.364  1.00 29.00           N  
ANISOU 3732  NH1 ARG C  18     3864   3577   3577     46   -214    -40       N  
ATOM   3733  NH2 ARG C  18     -41.391   8.981  47.157  1.00 31.79           N  
ANISOU 3733  NH2 ARG C  18     4201   3947   3932     23   -190    -32       N  
ATOM   3734  N   VAL C  19     -45.342   8.770  41.502  1.00 16.90           N  
ANISOU 3734  N   VAL C  19     2325   2037   2058     14   -176     -8       N  
ATOM   3735  CA  VAL C  19     -44.452   9.673  40.804  1.00 18.19           C  
ANISOU 3735  CA  VAL C  19     2473   2215   2225     25   -161    -19       C  
ATOM   3736  C   VAL C  19     -43.993  10.744  41.768  1.00 17.87           C  
ANISOU 3736  C   VAL C  19     2419   2184   2186     17   -146    -21       C  
ATOM   3737  O   VAL C  19     -44.676  11.030  42.761  1.00 17.37           O  
ANISOU 3737  O   VAL C  19     2358   2120   2124      4   -143    -13       O  
ATOM   3738  CB  VAL C  19     -45.092  10.334  39.551  1.00 18.17           C  
ANISOU 3738  CB  VAL C  19     2462   2217   2225     22   -147    -16       C  
ATOM   3739  CG1 VAL C  19     -45.377   9.282  38.483  1.00 20.79           C  
ANISOU 3739  CG1 VAL C  19     2805   2541   2554     33   -161    -18       C  
ATOM   3740  CG2 VAL C  19     -46.380  11.119  39.928  1.00 19.22           C  
ANISOU 3740  CG2 VAL C  19     2594   2349   2362      5   -134     -3       C  
ATOM   3741  N   THR C  20     -42.829  11.301  41.487  1.00 18.14           N  
ANISOU 3741  N   THR C  20     2440   2231   2220     26   -139    -32       N  
ATOM   3742  CA ATHR C  20     -42.318  12.401  42.270  0.50 18.99           C  
ANISOU 3742  CA ATHR C  20     2535   2348   2331     18   -126    -35       C  
ATOM   3743  CA BTHR C  20     -42.304  12.410  42.269  0.50 17.85           C  
ANISOU 3743  CA BTHR C  20     2391   2204   2186     18   -125    -35       C  
ATOM   3744  C   THR C  20     -42.014  13.568  41.339  1.00 18.18           C  
ANISOU 3744  C   THR C  20     2419   2257   2232     15   -109    -36       C  
ATOM   3745  O   THR C  20     -41.630  13.372  40.158  1.00 17.56           O  
ANISOU 3745  O   THR C  20     2336   2186   2150     23   -110    -40       O  
ATOM   3746  CB ATHR C  20     -41.110  11.965  43.146  0.50 19.16           C  
ANISOU 3746  CB ATHR C  20     2555   2376   2348     27   -135    -45       C  
ATOM   3747  CB BTHR C  20     -41.015  12.037  43.009  0.50 17.79           C  
ANISOU 3747  CB BTHR C  20     2380   2205   2174     28   -133    -46       C  
ATOM   3748  OG1ATHR C  20     -40.602  13.093  43.858  0.50 22.64           O  
ANISOU 3748  OG1ATHR C  20     2983   2827   2791     19   -121    -48       O  
ATOM   3749  OG1BTHR C  20     -40.002  11.695  42.053  0.50 16.89           O  
ANISOU 3749  OG1BTHR C  20     2260   2104   2055     44   -138    -59       O  
ATOM   3750  CG2ATHR C  20     -39.995  11.363  42.316  0.50 19.95           C  
ANISOU 3750  CG2ATHR C  20     2651   2487   2442     46   -143    -59       C  
ATOM   3751  CG2BTHR C  20     -41.254  10.901  44.028  0.50 16.06           C  
ANISOU 3751  CG2BTHR C  20     2178   1974   1952     30   -152    -43       C  
ATOM   3752  N   ILE C  21     -42.227  14.769  41.856  1.00 16.19           N  
ANISOU 3752  N   ILE C  21     2161   2005   1984      2    -97    -33       N  
ATOM   3753  CA  ILE C  21     -41.982  16.021  41.161  1.00 17.60           C  
ANISOU 3753  CA  ILE C  21     2330   2190   2167     -5    -84    -31       C  
ATOM   3754  C   ILE C  21     -40.993  16.844  41.971  1.00 17.27           C  
ANISOU 3754  C   ILE C  21     2279   2156   2126    -11    -79    -38       C  
ATOM   3755  O   ILE C  21     -41.262  17.177  43.130  1.00 17.50           O  
ANISOU 3755  O   ILE C  21     2311   2180   2159    -16    -79    -38       O  
ATOM   3756  CB  ILE C  21     -43.277  16.772  40.932  1.00 17.30           C  
ANISOU 3756  CB  ILE C  21     2297   2141   2136    -13    -77    -22       C  
ATOM   3757  CG1 ILE C  21     -44.219  15.967  40.018  1.00 17.57           C  
ANISOU 3757  CG1 ILE C  21     2338   2169   2167     -8    -81    -15       C  
ATOM   3758  CG2 ILE C  21     -42.991  18.144  40.324  1.00 16.98           C  
ANISOU 3758  CG2 ILE C  21     2251   2103   2099    -23    -67    -19       C  
ATOM   3759  CD1 ILE C  21     -45.614  16.513  39.904  1.00 19.20           C  
ANISOU 3759  CD1 ILE C  21     2550   2368   2378    -14    -76     -7       C  
ATOM   3760  N   SER C  22     -39.830  17.101  41.386  1.00 17.78           N  
ANISOU 3760  N   SER C  22     2332   2237   2186    -12    -76    -44       N  
ATOM   3761  CA ASER C  22     -38.740  17.775  42.092  0.50 17.39           C  
ANISOU 3761  CA ASER C  22     2273   2199   2136    -19    -73    -51       C  
ATOM   3762  CA BSER C  22     -38.757  17.773  42.098  0.50 18.84           C  
ANISOU 3762  CA BSER C  22     2456   2382   2319    -19    -73    -51       C  
ATOM   3763  C   SER C  22     -38.795  19.266  41.892  1.00 18.47           C  
ANISOU 3763  C   SER C  22     2406   2332   2278    -36    -63    -44       C  
ATOM   3764  O   SER C  22     -39.212  19.740  40.837  1.00 19.43           O  
ANISOU 3764  O   SER C  22     2530   2451   2402    -42    -59    -36       O  
ATOM   3765  CB ASER C  22     -37.370  17.284  41.614  0.50 18.09           C  
ANISOU 3765  CB ASER C  22     2348   2313   2214    -11    -76    -61       C  
ATOM   3766  CB BSER C  22     -37.398  17.260  41.644  0.50 19.79           C  
ANISOU 3766  CB BSER C  22     2564   2527   2429    -11    -76    -61       C  
ATOM   3767  OG ASER C  22     -37.227  17.472  40.220  0.50 13.76           O  
ANISOU 3767  OG ASER C  22     1793   1777   1660    -13    -71    -58       O  
ATOM   3768  OG BSER C  22     -36.497  17.308  42.723  0.50 23.92           O  
ANISOU 3768  OG BSER C  22     3081   3059   2949    -10    -78    -71       O  
ATOM   3769  N   CYS C  23     -38.347  19.985  42.916  1.00 18.34           N  
ANISOU 3769  N   CYS C  23     2388   2315   2266    -45    -62    -49       N  
ATOM   3770  CA  CYS C  23     -38.235  21.412  42.886  1.00 20.62           C  
ANISOU 3770  CA  CYS C  23     2676   2598   2560    -62    -57    -44       C  
ATOM   3771  C   CYS C  23     -36.797  21.715  43.357  1.00 20.95           C  
ANISOU 3771  C   CYS C  23     2706   2659   2597    -70    -57    -53       C  
ATOM   3772  O   CYS C  23     -36.464  21.453  44.497  1.00 21.02           O  
ANISOU 3772  O   CYS C  23     2713   2670   2606    -65    -60    -61       O  
ATOM   3773  CB  CYS C  23     -39.277  21.965  43.846  1.00 21.91           C  
ANISOU 3773  CB  CYS C  23     2850   2741   2733    -62    -59    -44       C  
ATOM   3774  SG  CYS C  23     -39.339  23.736  44.127  1.00 24.97           S  
ANISOU 3774  SG  CYS C  23     3244   3114   3130    -78    -59    -42       S  
ATOM   3775  N   SER C  24     -35.939  22.215  42.468  1.00 21.72           N  
ANISOU 3775  N   SER C  24     2792   2773   2687    -84    -53    -50       N  
ATOM   3776  CA  SER C  24     -34.537  22.489  42.801  1.00 22.40           C  
ANISOU 3776  CA  SER C  24     2863   2882   2765    -94    -53    -57       C  
ATOM   3777  C   SER C  24     -34.277  23.989  42.968  1.00 22.61           C  
ANISOU 3777  C   SER C  24     2892   2900   2797   -120    -52    -51       C  
ATOM   3778  O   SER C  24     -34.508  24.761  42.046  1.00 22.51           O  
ANISOU 3778  O   SER C  24     2884   2882   2786   -136    -51    -38       O  
ATOM   3779  CB  SER C  24     -33.577  21.923  41.731  1.00 23.13           C  
ANISOU 3779  CB  SER C  24     2937   3008   2841    -92    -51    -60       C  
ATOM   3780  OG  SER C  24     -33.784  20.528  41.490  1.00 28.77           O  
ANISOU 3780  OG  SER C  24     3652   3728   3550    -67    -55    -67       O  
ATOM   3781  N   GLY C  25     -33.785  24.367  44.140  1.00 21.70           N  
ANISOU 3781  N   GLY C  25     2776   2785   2686   -124    -54    -59       N  
ATOM   3782  CA  GLY C  25     -33.542  25.762  44.463  1.00 22.87           C  
ANISOU 3782  CA  GLY C  25     2930   2921   2840   -148    -57    -55       C  
ATOM   3783  C   GLY C  25     -32.132  26.074  44.915  1.00 22.63           C  
ANISOU 3783  C   GLY C  25     2883   2915   2801   -163    -57    -63       C  
ATOM   3784  O   GLY C  25     -31.164  25.418  44.504  1.00 25.02           O  
ANISOU 3784  O   GLY C  25     3167   3251   3089   -162    -54    -67       O  
ATOM   3785  N   SER C  26     -32.002  27.122  45.719  1.00 23.03           N  
ANISOU 3785  N   SER C  26     2941   2950   2860   -178    -62    -64       N  
ATOM   3786  CA  SER C  26     -30.675  27.516  46.187  1.00 22.82           C  
ANISOU 3786  CA  SER C  26     2900   2946   2825   -196    -63    -71       C  
ATOM   3787  C   SER C  26     -30.794  27.846  47.657  1.00 21.86           C  
ANISOU 3787  C   SER C  26     2785   2808   2713   -190    -68    -83       C  
ATOM   3788  O   SER C  26     -31.896  27.749  48.247  1.00 20.33           O  
ANISOU 3788  O   SER C  26     2605   2589   2530   -172    -71    -86       O  
ATOM   3789  CB  SER C  26     -30.145  28.712  45.392  1.00 24.16           C  
ANISOU 3789  CB  SER C  26     3071   3118   2992   -232    -66    -57       C  
ATOM   3790  OG  SER C  26     -30.959  29.821  45.653  1.00 27.42           O  
ANISOU 3790  OG  SER C  26     3508   3491   3421   -241    -76    -51       O  
ATOM   3791  N   SER C  27     -29.680  28.251  48.252  1.00 20.98           N  
ANISOU 3791  N   SER C  27     2662   2714   2596   -205    -70    -90       N  
ATOM   3792  CA  SER C  27     -29.659  28.544  49.685  1.00 21.73           C  
ANISOU 3792  CA  SER C  27     2761   2798   2698   -199    -75   -103       C  
ATOM   3793  C   SER C  27     -30.628  29.665  50.089  1.00 22.69           C  
ANISOU 3793  C   SER C  27     2905   2880   2837   -204    -84   -101       C  
ATOM   3794  O   SER C  27     -31.244  29.598  51.138  1.00 23.29           O  
ANISOU 3794  O   SER C  27     2988   2942   2920   -186    -87   -112       O  
ATOM   3795  CB  SER C  27     -28.237  28.883  50.141  1.00 21.93           C  
ANISOU 3795  CB  SER C  27     2770   2850   2715   -218    -76   -111       C  
ATOM   3796  OG  SER C  27     -27.445  27.684  50.119  1.00 26.54           O  
ANISOU 3796  OG  SER C  27     3331   3470   3282   -203    -69   -119       O  
ATOM   3797  N   SER C  27A    -30.778  30.689  49.262  1.00 23.03           N  
ANISOU 3797  N   SER C  27A    2961   2906   2885   -227    -90    -88       N  
ATOM   3798  CA  SER C  27A    -31.642  31.821  49.657  1.00 23.30           C  
ANISOU 3798  CA  SER C  27A    3019   2900   2934   -229   -103    -89       C  
ATOM   3799  C   SER C  27A    -33.142  31.497  49.609  1.00 23.27           C  
ANISOU 3799  C   SER C  27A    3028   2874   2938   -201   -103    -89       C  
ATOM   3800  O   SER C  27A    -33.970  32.258  50.170  1.00 23.41           O  
ANISOU 3800  O   SER C  27A    3063   2865   2968   -193   -114    -96       O  
ATOM   3801  CB  SER C  27A    -31.374  33.027  48.772  1.00 24.10           C  
ANISOU 3801  CB  SER C  27A    3134   2986   3038   -262   -114    -73       C  
ATOM   3802  OG  SER C  27A    -31.555  32.653  47.432  1.00 25.64           O  
ANISOU 3802  OG  SER C  27A    3326   3190   3226   -267   -107    -57       O  
ATOM   3803  N   ASN C  27B    -33.499  30.433  48.909  1.00 20.42           N  
ANISOU 3803  N   ASN C  27B    2660   2528   2571   -188    -92    -83       N  
ATOM   3804  CA  ASN C  27B    -34.913  30.022  48.902  1.00 19.57           C  
ANISOU 3804  CA  ASN C  27B    2563   2405   2470   -163    -91    -83       C  
ATOM   3805  C   ASN C  27B    -35.098  28.737  49.675  1.00 18.70           C  
ANISOU 3805  C   ASN C  27B    2441   2311   2354   -139    -84    -92       C  
ATOM   3806  O   ASN C  27B    -35.194  28.807  50.898  1.00 17.04           O  
ANISOU 3806  O   ASN C  27B    2230   2100   2146   -130    -87   -105       O  
ATOM   3807  CB  ASN C  27B    -35.548  30.064  47.498  1.00 19.04           C  
ANISOU 3807  CB  ASN C  27B    2503   2327   2402   -167    -90    -67       C  
ATOM   3808  CG  ASN C  27B    -34.694  29.449  46.439  1.00 20.21           C  
ANISOU 3808  CG  ASN C  27B    2637   2502   2539   -178    -81    -57       C  
ATOM   3809  OD1 ASN C  27B    -34.458  28.252  46.430  1.00 20.56           O  
ANISOU 3809  OD1 ASN C  27B    2667   2568   2574   -164    -73    -61       O  
ATOM   3810  ND2 ASN C  27B    -34.254  30.270  45.507  1.00 25.48           N  
ANISOU 3810  ND2 ASN C  27B    3309   3167   3205   -204    -85    -44       N  
ATOM   3811  N   ILE C  28     -35.086  27.583  49.019  1.00 19.55           N  
ANISOU 3811  N   ILE C  28     2540   2436   2454   -131    -76    -87       N  
ATOM   3812  CA  ILE C  28     -35.373  26.318  49.689  1.00 19.64           C  
ANISOU 3812  CA  ILE C  28     2545   2458   2459   -109    -72    -93       C  
ATOM   3813  C   ILE C  28     -34.425  26.007  50.829  1.00 19.87           C  
ANISOU 3813  C   ILE C  28     2563   2505   2484   -107    -73   -106       C  
ATOM   3814  O   ILE C  28     -34.823  25.479  51.869  1.00 20.15           O  
ANISOU 3814  O   ILE C  28     2597   2541   2517    -92    -74   -113       O  
ATOM   3815  CB  ILE C  28     -35.400  25.162  48.686  1.00 20.12           C  
ANISOU 3815  CB  ILE C  28     2601   2531   2512   -101    -67    -86       C  
ATOM   3816  CG1 ILE C  28     -36.553  25.409  47.697  1.00 20.87           C  
ANISOU 3816  CG1 ILE C  28     2708   2609   2613   -100    -66    -74       C  
ATOM   3817  CG2 ILE C  28     -35.496  23.810  49.406  1.00 19.20           C  
ANISOU 3817  CG2 ILE C  28     2479   2426   2389    -82    -67    -92       C  
ATOM   3818  CD1 ILE C  28     -36.684  24.332  46.586  1.00 23.82           C  
ANISOU 3818  CD1 ILE C  28     3078   2992   2979    -92    -62    -67       C  
ATOM   3819  N   GLY C  29     -33.156  26.339  50.621  1.00 19.78           N  
ANISOU 3819  N   GLY C  29     2541   2509   2467   -123    -72   -107       N  
ATOM   3820  CA  GLY C  29     -32.156  26.107  51.653  1.00 19.47           C  
ANISOU 3820  CA  GLY C  29     2489   2488   2422   -121    -73   -120       C  
ATOM   3821  C   GLY C  29     -32.452  26.795  52.975  1.00 20.66           C  
ANISOU 3821  C   GLY C  29     2645   2626   2580   -120    -78   -130       C  
ATOM   3822  O   GLY C  29     -32.027  26.311  54.003  1.00 22.93           O  
ANISOU 3822  O   GLY C  29     2924   2926   2862   -111    -78   -141       O  
ATOM   3823  N   SER C  30     -33.162  27.925  52.930  1.00 20.28           N  
ANISOU 3823  N   SER C  30     2611   2553   2542   -127    -84   -128       N  
ATOM   3824  CA  SER C  30     -33.448  28.755  54.109  1.00 21.01           C  
ANISOU 3824  CA  SER C  30     2709   2632   2641   -125    -91   -141       C  
ATOM   3825  C   SER C  30     -34.918  28.802  54.519  1.00 20.06           C  
ANISOU 3825  C   SER C  30     2600   2497   2527   -106    -94   -143       C  
ATOM   3826  O   SER C  30     -35.265  29.507  55.480  1.00 20.92           O  
ANISOU 3826  O   SER C  30     2712   2596   2639   -101   -102   -156       O  
ATOM   3827  CB  SER C  30     -32.995  30.193  53.865  1.00 21.75           C  
ANISOU 3827  CB  SER C  30     2812   2710   2743   -148   -100   -140       C  
ATOM   3828  OG  SER C  30     -31.589  30.192  53.622  1.00 24.43           O  
ANISOU 3828  OG  SER C  30     3138   3070   3075   -168    -98   -139       O  
ATOM   3829  N   ASN C  31     -35.789  28.080  53.817  1.00 19.60           N  
ANISOU 3829  N   ASN C  31     2545   2437   2467    -96    -89   -133       N  
ATOM   3830  CA  ASN C  31     -37.229  28.313  53.923  1.00 17.93           C  
ANISOU 3830  CA  ASN C  31     2343   2211   2259    -82    -93   -134       C  
ATOM   3831  C   ASN C  31     -38.004  27.035  53.764  1.00 18.19           C  
ANISOU 3831  C   ASN C  31     2372   2254   2284    -69    -86   -127       C  
ATOM   3832  O   ASN C  31     -37.455  25.996  53.409  1.00 19.10           O  
ANISOU 3832  O   ASN C  31     2481   2383   2393    -69    -81   -121       O  
ATOM   3833  CB  ASN C  31     -37.672  29.331  52.870  1.00 18.10           C  
ANISOU 3833  CB  ASN C  31     2380   2209   2290    -91    -98   -127       C  
ATOM   3834  CG  ASN C  31     -37.163  30.707  53.172  1.00 18.71           C  
ANISOU 3834  CG  ASN C  31     2465   2270   2375   -104   -110   -134       C  
ATOM   3835  OD1 ASN C  31     -37.705  31.371  54.074  1.00 19.77           O  
ANISOU 3835  OD1 ASN C  31     2605   2394   2513    -93   -119   -149       O  
ATOM   3836  ND2 ASN C  31     -36.087  31.137  52.480  1.00 18.26           N  
ANISOU 3836  ND2 ASN C  31     2409   2211   2319   -128   -111   -126       N  
ATOM   3837  N   TYR C  32     -39.289  27.135  54.057  1.00 17.91           N  
ANISOU 3837  N   TYR C  32     2341   2214   2249    -56    -89   -129       N  
ATOM   3838  CA  TYR C  32     -40.258  26.048  53.843  1.00 16.97           C  
ANISOU 3838  CA  TYR C  32     2221   2104   2124    -46    -84   -121       C  
ATOM   3839  C   TYR C  32     -40.759  26.052  52.409  1.00 16.92           C  
ANISOU 3839  C   TYR C  32     2222   2084   2120    -49    -82   -108       C  
ATOM   3840  O   TYR C  32     -40.733  27.097  51.753  1.00 18.97           O  
ANISOU 3840  O   TYR C  32     2491   2328   2389    -55    -85   -108       O  
ATOM   3841  CB  TYR C  32     -41.439  26.209  54.784  1.00 17.92           C  
ANISOU 3841  CB  TYR C  32     2340   2230   2240    -33    -87   -130       C  
ATOM   3842  CG  TYR C  32     -41.029  26.069  56.217  1.00 17.52           C  
ANISOU 3842  CG  TYR C  32     2279   2195   2182    -29    -89   -141       C  
ATOM   3843  CD1 TYR C  32     -40.650  27.188  56.948  1.00 19.36           C  
ANISOU 3843  CD1 TYR C  32     2511   2423   2420    -29    -96   -157       C  
ATOM   3844  CD2 TYR C  32     -40.959  24.799  56.816  1.00 17.55           C  
ANISOU 3844  CD2 TYR C  32     2276   2219   2175    -28    -86   -136       C  
ATOM   3845  CE1 TYR C  32     -40.258  27.050  58.290  1.00 18.72           C  
ANISOU 3845  CE1 TYR C  32     2421   2360   2333    -25    -97   -168       C  
ATOM   3846  CE2 TYR C  32     -40.556  24.656  58.147  1.00 19.30           C  
ANISOU 3846  CE2 TYR C  32     2488   2456   2390    -25    -88   -145       C  
ATOM   3847  CZ  TYR C  32     -40.177  25.795  58.840  1.00 18.38           C  
ANISOU 3847  CZ  TYR C  32     2369   2337   2278    -24    -93   -162       C  
ATOM   3848  OH  TYR C  32     -39.772  25.654  60.155  1.00 18.77           O  
ANISOU 3848  OH  TYR C  32     2409   2404   2320    -21    -94   -172       O  
ATOM   3849  N   VAL C  33     -41.266  24.896  51.970  1.00 16.48           N  
ANISOU 3849  N   VAL C  33     2166   2037   2059    -44    -78    -99       N  
ATOM   3850  CA  VAL C  33     -41.752  24.772  50.605  1.00 15.79           C  
ANISOU 3850  CA  VAL C  33     2085   1940   1974    -46    -75    -87       C  
ATOM   3851  C   VAL C  33     -43.218  24.387  50.657  1.00 15.93           C  
ANISOU 3851  C   VAL C  33     2105   1960   1987    -36    -75    -84       C  
ATOM   3852  O   VAL C  33     -43.652  23.526  51.454  1.00 15.74           O  
ANISOU 3852  O   VAL C  33     2075   1950   1954    -31    -75    -84       O  
ATOM   3853  CB  VAL C  33     -41.004  23.628  49.822  1.00 14.71           C  
ANISOU 3853  CB  VAL C  33     1945   1811   1832    -49    -71    -78       C  
ATOM   3854  CG1 VAL C  33     -41.609  23.444  48.427  1.00 15.25           C  
ANISOU 3854  CG1 VAL C  33     2019   1872   1902    -49    -69    -66       C  
ATOM   3855  CG2 VAL C  33     -39.581  24.039  49.672  1.00 16.67           C  
ANISOU 3855  CG2 VAL C  33     2188   2062   2082    -59    -70    -81       C  
ATOM   3856  N   SER C  34     -43.983  25.024  49.781  1.00 15.83           N  
ANISOU 3856  N   SER C  34     2100   1936   1980    -34    -76    -80       N  
ATOM   3857  CA  SER C  34     -45.362  24.647  49.535  1.00 14.43           C  
ANISOU 3857  CA  SER C  34     1923   1762   1797    -25    -75    -76       C  
ATOM   3858  C   SER C  34     -45.563  24.125  48.119  1.00 13.89           C  
ANISOU 3858  C   SER C  34     1861   1688   1731    -29    -72    -63       C  
ATOM   3859  O   SER C  34     -44.752  24.368  47.262  1.00 14.14           O  
ANISOU 3859  O   SER C  34     1895   1711   1767    -36    -70    -58       O  
ATOM   3860  CB  SER C  34     -46.299  25.875  49.700  1.00 15.03           C  
ANISOU 3860  CB  SER C  34     2004   1831   1877    -16    -81    -86       C  
ATOM   3861  OG  SER C  34     -46.288  26.281  51.081  1.00 17.83           O  
ANISOU 3861  OG  SER C  34     2351   2194   2228    -10    -86   -101       O  
ATOM   3862  N   TRP C  35     -46.685  23.439  47.915  1.00 13.64           N  
ANISOU 3862  N   TRP C  35     1828   1663   1692    -23    -71    -57       N  
ATOM   3863  CA  TRP C  35     -47.040  22.902  46.573  1.00 13.41           C  
ANISOU 3863  CA  TRP C  35     1803   1629   1663    -25    -68    -45       C  
ATOM   3864  C   TRP C  35     -48.493  23.176  46.266  1.00 12.51           C  
ANISOU 3864  C   TRP C  35     1690   1516   1546    -17    -69    -45       C  
ATOM   3865  O   TRP C  35     -49.391  23.096  47.142  1.00 14.56           O  
ANISOU 3865  O   TRP C  35     1944   1790   1798    -12    -71    -50       O  
ATOM   3866  CB  TRP C  35     -46.864  21.373  46.552  1.00 13.36           C  
ANISOU 3866  CB  TRP C  35     1795   1632   1649    -27    -68    -38       C  
ATOM   3867  CG  TRP C  35     -45.430  20.928  46.650  1.00 13.60           C  
ANISOU 3867  CG  TRP C  35     1823   1663   1680    -31    -68    -39       C  
ATOM   3868  CD1 TRP C  35     -44.718  20.667  47.804  1.00 11.95           C  
ANISOU 3868  CD1 TRP C  35     1610   1462   1468    -32    -70    -45       C  
ATOM   3869  CD2 TRP C  35     -44.539  20.752  45.571  1.00 11.49           C  
ANISOU 3869  CD2 TRP C  35     1557   1392   1415    -34    -66    -35       C  
ATOM   3870  NE1 TRP C  35     -43.429  20.306  47.477  1.00 15.42           N  
ANISOU 3870  NE1 TRP C  35     2048   1903   1909    -34    -71    -46       N  
ATOM   3871  CE2 TRP C  35     -43.295  20.326  46.100  1.00 13.46           C  
ANISOU 3871  CE2 TRP C  35     1802   1649   1663    -35    -68    -40       C  
ATOM   3872  CE3 TRP C  35     -44.690  20.869  44.185  1.00 13.84           C  
ANISOU 3872  CE3 TRP C  35     1858   1685   1716    -35    -64    -28       C  
ATOM   3873  CZ2 TRP C  35     -42.170  20.081  45.288  1.00 15.16           C  
ANISOU 3873  CZ2 TRP C  35     2014   1870   1878    -36    -67    -41       C  
ATOM   3874  CZ3 TRP C  35     -43.595  20.563  43.367  1.00 16.41           C  
ANISOU 3874  CZ3 TRP C  35     2180   2015   2040    -37    -62    -27       C  
ATOM   3875  CH2 TRP C  35     -42.342  20.174  43.921  1.00 15.49           C  
ANISOU 3875  CH2 TRP C  35     2056   1908   1920    -37    -64    -34       C  
ATOM   3876  N   TYR C  36     -48.755  23.419  44.976  1.00 14.83           N  
ANISOU 3876  N   TYR C  36     1991   1800   1844    -17    -67    -37       N  
ATOM   3877  CA  TYR C  36     -50.066  23.741  44.491  1.00 15.95           C  
ANISOU 3877  CA  TYR C  36     2135   1942   1984     -9    -69    -37       C  
ATOM   3878  C   TYR C  36     -50.370  22.941  43.260  1.00 15.94           C  
ANISOU 3878  C   TYR C  36     2136   1940   1981    -12    -65    -24       C  
ATOM   3879  O   TYR C  36     -49.458  22.623  42.477  1.00 16.73           O  
ANISOU 3879  O   TYR C  36     2239   2034   2085    -18    -63    -18       O  
ATOM   3880  CB  TYR C  36     -50.136  25.224  44.073  1.00 15.75           C  
ANISOU 3880  CB  TYR C  36     2118   1899   1967     -4    -74    -42       C  
ATOM   3881  CG  TYR C  36     -49.995  26.186  45.246  1.00 16.47           C  
ANISOU 3881  CG  TYR C  36     2210   1988   2061      2    -80    -57       C  
ATOM   3882  CD1 TYR C  36     -51.122  26.661  45.921  1.00 16.90           C  
ANISOU 3882  CD1 TYR C  36     2260   2052   2110     17    -86    -69       C  
ATOM   3883  CD2 TYR C  36     -48.739  26.595  45.673  1.00 16.12           C  
ANISOU 3883  CD2 TYR C  36     2167   1935   2023     -7    -82    -60       C  
ATOM   3884  CE1 TYR C  36     -50.963  27.530  47.030  1.00 16.62           C  
ANISOU 3884  CE1 TYR C  36     2224   2016   2076     25    -93    -86       C  
ATOM   3885  CE2 TYR C  36     -48.557  27.456  46.798  1.00 16.35           C  
ANISOU 3885  CE2 TYR C  36     2196   1962   2055     -2    -89    -75       C  
ATOM   3886  CZ  TYR C  36     -49.691  27.907  47.450  1.00 15.89           C  
ANISOU 3886  CZ  TYR C  36     2135   1911   1991     15    -95    -88       C  
ATOM   3887  OH  TYR C  36     -49.605  28.751  48.555  1.00 17.35           O  
ANISOU 3887  OH  TYR C  36     2319   2096   2177     24   -104   -106       O  
ATOM   3888  N   GLN C  37     -51.633  22.591  43.129  1.00 16.40           N  
ANISOU 3888  N   GLN C  37     2191   2007   2031     -6    -65    -23       N  
ATOM   3889  CA  GLN C  37     -52.117  21.971  41.898  1.00 17.42           C  
ANISOU 3889  CA  GLN C  37     2323   2135   2159     -8    -63    -12       C  
ATOM   3890  C   GLN C  37     -52.942  22.960  41.125  1.00 17.61           C  
ANISOU 3890  C   GLN C  37     2351   2152   2186      1    -64    -13       C  
ATOM   3891  O   GLN C  37     -53.715  23.687  41.724  1.00 18.57           O  
ANISOU 3891  O   GLN C  37     2471   2279   2305     11    -68    -23       O  
ATOM   3892  CB  GLN C  37     -52.987  20.751  42.266  1.00 18.06           C  
ANISOU 3892  CB  GLN C  37     2399   2234   2228    -11    -64     -8       C  
ATOM   3893  CG  GLN C  37     -53.700  20.038  41.087  1.00 17.91           C  
ANISOU 3893  CG  GLN C  37     2383   2216   2207    -12    -63      2       C  
ATOM   3894  CD  GLN C  37     -54.704  19.046  41.579  1.00 20.06           C  
ANISOU 3894  CD  GLN C  37     2649   2506   2465    -18    -66      6       C  
ATOM   3895  OE1 GLN C  37     -55.686  19.401  42.261  1.00 21.69           O  
ANISOU 3895  OE1 GLN C  37     2847   2729   2663    -15    -66      1       O  
ATOM   3896  NE2 GLN C  37     -54.461  17.762  41.282  1.00 19.86           N  
ANISOU 3896  NE2 GLN C  37     2630   2479   2438    -27    -70     15       N  
ATOM   3897  N   GLN C  38     -52.795  23.003  39.799  1.00 17.98           N  
ANISOU 3897  N   GLN C  38     2405   2189   2237      0    -62     -5       N  
ATOM   3898  CA  GLN C  38     -53.783  23.717  39.000  1.00 18.59           C  
ANISOU 3898  CA  GLN C  38     2487   2263   2315      9    -64     -4       C  
ATOM   3899  C   GLN C  38     -54.363  22.830  37.914  1.00 20.16           C  
ANISOU 3899  C   GLN C  38     2685   2467   2509      8    -61      6       C  
ATOM   3900  O   GLN C  38     -53.653  22.447  36.991  1.00 18.62           O  
ANISOU 3900  O   GLN C  38     2492   2266   2316      1    -58     14       O  
ATOM   3901  CB  GLN C  38     -53.226  25.033  38.431  1.00 18.28           C  
ANISOU 3901  CB  GLN C  38     2458   2202   2285      9    -68     -3       C  
ATOM   3902  CG  GLN C  38     -54.314  25.906  37.844  1.00 19.50           C  
ANISOU 3902  CG  GLN C  38     2620   2350   2440     22    -74     -5       C  
ATOM   3903  CD  GLN C  38     -53.842  27.206  37.242  1.00 20.17           C  
ANISOU 3903  CD  GLN C  38     2720   2411   2534     20    -82     -2       C  
ATOM   3904  OE1 GLN C  38     -52.680  27.340  36.807  1.00 25.13           O  
ANISOU 3904  OE1 GLN C  38     3352   3029   3167      5    -80      7       O  
ATOM   3905  NE2 GLN C  38     -54.755  28.180  37.200  1.00 22.47           N  
ANISOU 3905  NE2 GLN C  38     3019   2694   2826     36    -92     -9       N  
ATOM   3906  N   LYS C  39     -55.633  22.459  38.116  1.00 22.62           N  
ANISOU 3906  N   LYS C  39     2990   2794   2812     13    -61      3       N  
ATOM   3907  CA ALYS C  39     -56.381  21.699  37.121  0.50 23.65           C  
ANISOU 3907  CA ALYS C  39     3119   2930   2936     13    -59     11       C  
ATOM   3908  CA BLYS C  39     -56.422  21.714  37.129  0.50 23.93           C  
ANISOU 3908  CA BLYS C  39     3155   2966   2972     13    -59     11       C  
ATOM   3909  C   LYS C  39     -56.743  22.647  35.976  1.00 25.14           C  
ANISOU 3909  C   LYS C  39     3315   3108   3129     21    -60     13       C  
ATOM   3910  O   LYS C  39     -56.808  23.871  36.163  1.00 25.37           O  
ANISOU 3910  O   LYS C  39     3350   3128   3163     30    -65      7       O  
ATOM   3911  CB ALYS C  39     -57.637  21.069  37.737  0.50 23.81           C  
ANISOU 3911  CB ALYS C  39     3130   2974   2944     13    -60      9       C  
ATOM   3912  CB BLYS C  39     -57.738  21.224  37.736  0.50 24.30           C  
ANISOU 3912  CB BLYS C  39     3192   3036   3006     15    -61      7       C  
ATOM   3913  CG ALYS C  39     -57.362  19.980  38.765  0.50 23.03           C  
ANISOU 3913  CG ALYS C  39     3027   2886   2839      1    -62     11       C  
ATOM   3914  CG BLYS C  39     -57.590  20.160  38.785  0.50 24.79           C  
ANISOU 3914  CG BLYS C  39     3248   3111   3060      3    -62      9       C  
ATOM   3915  CD ALYS C  39     -58.653  19.597  39.481  0.50 22.99           C  
ANISOU 3915  CD ALYS C  39     3009   2907   2817     -2    -63      8       C  
ATOM   3916  CD BLYS C  39     -56.924  18.939  38.226  0.50 26.20           C  
ANISOU 3916  CD BLYS C  39     3432   3281   3240     -8    -62     19       C  
ATOM   3917  CE ALYS C  39     -58.463  18.421  40.427  0.50 25.94           C  
ANISOU 3917  CE ALYS C  39     3381   3293   3183    -18    -67     14       C  
ATOM   3918  CE BLYS C  39     -56.757  17.920  39.309  0.50 28.40           C  
ANISOU 3918  CE BLYS C  39     3709   3570   3512    -20    -67     22       C  
ATOM   3919  NZ ALYS C  39     -58.031  18.847  41.789  0.50 27.30           N  
ANISOU 3919  NZ ALYS C  39     3547   3472   3353    -18    -67      6       N  
ATOM   3920  NZ BLYS C  39     -55.495  17.199  39.052  0.50 29.65           N  
ANISOU 3920  NZ BLYS C  39     3875   3713   3678    -24    -69     26       N  
ATOM   3921  N   PRO C  40     -56.961  22.089  34.758  1.00 26.18           N  
ANISOU 3921  N   PRO C  40     3448   3240   3260     20    -58     22       N  
ATOM   3922  CA  PRO C  40     -57.302  23.008  33.675  1.00 27.70           C  
ANISOU 3922  CA  PRO C  40     3648   3422   3455     27    -59     26       C  
ATOM   3923  C   PRO C  40     -58.599  23.760  33.967  1.00 28.93           C  
ANISOU 3923  C   PRO C  40     3802   3584   3606     43    -64     16       C  
ATOM   3924  O   PRO C  40     -59.568  23.158  34.454  1.00 29.41           O  
ANISOU 3924  O   PRO C  40     3852   3665   3656     45    -63     12       O  
ATOM   3925  CB  PRO C  40     -57.450  22.080  32.457  1.00 28.23           C  
ANISOU 3925  CB  PRO C  40     3714   3494   3519     24    -55     35       C  
ATOM   3926  CG  PRO C  40     -56.589  20.864  32.805  1.00 27.55           C  
ANISOU 3926  CG  PRO C  40     3623   3411   3432     13    -54     37       C  
ATOM   3927  CD  PRO C  40     -56.832  20.690  34.288  1.00 26.65           C  
ANISOU 3927  CD  PRO C  40     3505   3306   3316     11    -56     29       C  
ATOM   3928  N   GLY C  41     -58.579  25.075  33.732  1.00 28.81           N  
ANISOU 3928  N   GLY C  41     3797   3553   3597     52    -71     14       N  
ATOM   3929  CA  GLY C  41     -59.743  25.943  33.914  1.00 29.37           C  
ANISOU 3929  CA  GLY C  41     3869   3628   3664     72    -79      2       C  
ATOM   3930  C   GLY C  41     -60.177  26.182  35.352  1.00 29.87           C  
ANISOU 3930  C   GLY C  41     3924   3706   3721     81    -83    -14       C  
ATOM   3931  O   GLY C  41     -61.333  26.532  35.605  1.00 32.03           O  
ANISOU 3931  O   GLY C  41     4191   3994   3985     98    -88    -26       O  
ATOM   3932  N   THR C  42     -59.252  25.993  36.293  1.00 29.04           N  
ANISOU 3932  N   THR C  42     3817   3598   3620     71    -81    -16       N  
ATOM   3933  CA  THR C  42     -59.551  26.040  37.733  1.00 27.90           C  
ANISOU 3933  CA  THR C  42     3661   3471   3468     77    -83    -31       C  
ATOM   3934  C   THR C  42     -58.507  26.926  38.433  1.00 26.03           C  
ANISOU 3934  C   THR C  42     3434   3213   3242     76    -89    -37       C  
ATOM   3935  O   THR C  42     -57.364  26.989  37.980  1.00 23.88           O  
ANISOU 3935  O   THR C  42     3172   2921   2981     63    -87    -26       O  
ATOM   3936  CB  THR C  42     -59.530  24.598  38.311  1.00 28.32           C  
ANISOU 3936  CB  THR C  42     3701   3547   3513     61    -74    -25       C  
ATOM   3937  OG1 THR C  42     -60.371  23.751  37.504  1.00 32.03           O  
ANISOU 3937  OG1 THR C  42     4165   4031   3974     57    -70    -17       O  
ATOM   3938  CG2 THR C  42     -60.029  24.553  39.727  1.00 30.81           C  
ANISOU 3938  CG2 THR C  42     4002   3887   3816     65    -76    -38       C  
ATOM   3939  N   ALA C  43     -58.894  27.597  39.537  1.00 23.98           N  
ANISOU 3939  N   ALA C  43     3170   2962   2978     91    -97    -55       N  
ATOM   3940  CA  ALA C  43     -57.926  28.339  40.354  1.00 22.92           C  
ANISOU 3940  CA  ALA C  43     3043   2811   2853     90   -103    -63       C  
ATOM   3941  C   ALA C  43     -56.988  27.296  41.014  1.00 21.39           C  
ANISOU 3941  C   ALA C  43     2841   2627   2660     69    -93    -55       C  
ATOM   3942  O   ALA C  43     -57.404  26.156  41.224  1.00 21.35           O  
ANISOU 3942  O   ALA C  43     2822   2645   2644     62    -85    -50       O  
ATOM   3943  CB  ALA C  43     -58.643  29.178  41.430  1.00 22.92           C  
ANISOU 3943  CB  ALA C  43     3039   2823   2847    113   -115    -86       C  
ATOM   3944  N   PRO C  44     -55.731  27.661  41.296  1.00 20.49           N  
ANISOU 3944  N   PRO C  44     2735   2493   2556     59    -94    -53       N  
ATOM   3945  CA  PRO C  44     -54.816  26.732  42.008  1.00 19.00           C  
ANISOU 3945  CA  PRO C  44     2538   2314   2367     43    -86    -49       C  
ATOM   3946  C   PRO C  44     -55.335  26.311  43.399  1.00 18.66           C  
ANISOU 3946  C   PRO C  44     2480   2299   2312     48    -85    -61       C  
ATOM   3947  O   PRO C  44     -56.180  26.982  44.034  1.00 18.43           O  
ANISOU 3947  O   PRO C  44     2445   2281   2276     66    -92    -77       O  
ATOM   3948  CB  PRO C  44     -53.518  27.539  42.124  1.00 19.01           C  
ANISOU 3948  CB  PRO C  44     2551   2292   2381     35    -91    -49       C  
ATOM   3949  CG  PRO C  44     -53.589  28.495  40.951  1.00 22.66           C  
ANISOU 3949  CG  PRO C  44     3029   2730   2851     38    -98    -43       C  
ATOM   3950  CD  PRO C  44     -55.039  28.897  40.883  1.00 20.81           C  
ANISOU 3950  CD  PRO C  44     2794   2503   2610     59   -104    -53       C  
ATOM   3951  N   LYS C  45     -54.853  25.152  43.815  1.00 16.79           N  
ANISOU 3951  N   LYS C  45     2235   2074   2071     34    -78    -53       N  
ATOM   3952  CA ALYS C  45     -55.245  24.582  45.110  0.50 17.48           C  
ANISOU 3952  CA ALYS C  45     2307   2188   2144     33    -77    -60       C  
ATOM   3953  CA BLYS C  45     -55.248  24.556  45.090  0.50 17.12           C  
ANISOU 3953  CA BLYS C  45     2263   2143   2100     33    -77    -59       C  
ATOM   3954  C   LYS C  45     -54.016  24.219  45.905  1.00 16.49           C  
ANISOU 3954  C   LYS C  45     2182   2059   2023     22    -76    -58       C  
ATOM   3955  O   LYS C  45     -53.109  23.569  45.393  1.00 16.60           O  
ANISOU 3955  O   LYS C  45     2202   2062   2044     10    -72    -47       O  
ATOM   3956  CB ALYS C  45     -56.110  23.324  44.929  0.50 17.06           C  
ANISOU 3956  CB ALYS C  45     2246   2158   2078     25    -73    -49       C  
ATOM   3957  CB BLYS C  45     -56.024  23.264  44.820  0.50 16.28           C  
ANISOU 3957  CB BLYS C  45     2148   2056   1980     24    -72    -47       C  
ATOM   3958  CG ALYS C  45     -56.816  22.909  46.218  0.50 19.75           C  
ANISOU 3958  CG ALYS C  45     2570   2533   2402     24    -73    -55       C  
ATOM   3959  CG BLYS C  45     -56.340  22.501  46.066  0.50 17.41           C  
ANISOU 3959  CG BLYS C  45     2278   2229   2109     16    -72    -49       C  
ATOM   3960  CD ALYS C  45     -57.927  21.899  45.981  0.50 22.58           C  
ANISOU 3960  CD ALYS C  45     2919   2916   2743     14    -71    -45       C  
ATOM   3961  CD BLYS C  45     -57.091  21.249  45.777  0.50 18.26           C  
ANISOU 3961  CD BLYS C  45     2380   2354   2204      3    -70    -35       C  
ATOM   3962  CE ALYS C  45     -57.382  20.498  45.850  0.50 25.55           C  
ANISOU 3962  CE ALYS C  45     3301   3288   3120     -7    -70    -27       C  
ATOM   3963  CE BLYS C  45     -57.567  20.623  47.066  0.50 18.67           C  
ANISOU 3963  CE BLYS C  45     2418   2439   2238     -7    -71    -35       C  
ATOM   3964  NZ ALYS C  45     -58.401  19.503  46.278  0.50 25.21           N  
ANISOU 3964  NZ ALYS C  45     3246   3275   3056    -21    -71    -19       N  
ATOM   3965  NZ BLYS C  45     -58.740  21.315  47.607  0.50 22.01           N  
ANISOU 3965  NZ BLYS C  45     2824   2892   2645      6    -73    -50       N  
ATOM   3966  N   LEU C  46     -53.994  24.604  47.191  1.00 15.93           N  
ANISOU 3966  N   LEU C  46     2104   2002   1948     27    -79    -72       N  
ATOM   3967  CA  LEU C  46     -52.843  24.315  48.050  1.00 16.36           C  
ANISOU 3967  CA  LEU C  46     2157   2054   2005     18    -78    -72       C  
ATOM   3968  C   LEU C  46     -52.881  22.822  48.414  1.00 14.38           C  
ANISOU 3968  C   LEU C  46     1899   1822   1743      4    -74    -60       C  
ATOM   3969  O   LEU C  46     -53.891  22.372  48.941  1.00 18.15           O  
ANISOU 3969  O   LEU C  46     2366   2326   2206      4    -74    -60       O  
ATOM   3970  CB  LEU C  46     -52.921  25.162  49.333  1.00 15.36           C  
ANISOU 3970  CB  LEU C  46     2023   1939   1875     29    -83    -91       C  
ATOM   3971  CG  LEU C  46     -51.829  24.945  50.384  1.00 18.78           C  
ANISOU 3971  CG  LEU C  46     2453   2374   2309     22    -83    -94       C  
ATOM   3972  CD1 LEU C  46     -50.438  25.391  49.897  1.00 17.42           C  
ANISOU 3972  CD1 LEU C  46     2293   2173   2153     14    -83    -91       C  
ATOM   3973  CD2 LEU C  46     -52.212  25.684  51.674  1.00 18.55           C  
ANISOU 3973  CD2 LEU C  46     2413   2364   2272     35    -89   -114       C  
ATOM   3974  N   LEU C  47     -51.774  22.088  48.205  1.00 13.36           N  
ANISOU 3974  N   LEU C  47     1776   1680   1619     -7    -72    -50       N  
ATOM   3975  CA  LEU C  47     -51.681  20.632  48.471  1.00 14.25           C  
ANISOU 3975  CA  LEU C  47     1888   1803   1724    -20    -73    -38       C  
ATOM   3976  C   LEU C  47     -50.834  20.445  49.738  1.00 14.19           C  
ANISOU 3976  C   LEU C  47     1876   1802   1714    -23    -75    -43       C  
ATOM   3977  O   LEU C  47     -51.168  19.644  50.607  1.00 15.62           O  
ANISOU 3977  O   LEU C  47     2051   2002   1881    -31    -77    -38       O  
ATOM   3978  CB  LEU C  47     -50.996  19.941  47.292  1.00 15.30           C  
ANISOU 3978  CB  LEU C  47     2031   1917   1864    -25    -72    -27       C  
ATOM   3979  CG  LEU C  47     -51.686  19.997  45.941  1.00 16.48           C  
ANISOU 3979  CG  LEU C  47     2186   2059   2017    -22    -70    -21       C  
ATOM   3980  CD1 LEU C  47     -50.779  19.288  44.925  1.00 17.60           C  
ANISOU 3980  CD1 LEU C  47     2336   2186   2166    -26    -70    -12       C  
ATOM   3981  CD2 LEU C  47     -53.086  19.320  46.011  1.00 17.87           C  
ANISOU 3981  CD2 LEU C  47     2357   2254   2180    -26    -71    -14       C  
ATOM   3982  N   ILE C  48     -49.744  21.202  49.850  1.00 13.83           N  
ANISOU 3982  N   ILE C  48     1833   1742   1679    -20    -74    -51       N  
ATOM   3983  CA  ILE C  48     -48.733  20.994  50.916  1.00 13.98           C  
ANISOU 3983  CA  ILE C  48     1849   1765   1696    -23    -76    -56       C  
ATOM   3984  C   ILE C  48     -48.133  22.341  51.345  1.00 15.24           C  
ANISOU 3984  C   ILE C  48     2007   1918   1865    -16    -76    -71       C  
ATOM   3985  O   ILE C  48     -47.871  23.167  50.485  1.00 15.21           O  
ANISOU 3985  O   ILE C  48     2011   1896   1873    -14    -75    -73       O  
ATOM   3986  CB  ILE C  48     -47.556  20.094  50.361  1.00 14.58           C  
ANISOU 3986  CB  ILE C  48     1932   1829   1778    -29    -76    -47       C  
ATOM   3987  CG1 ILE C  48     -48.060  18.704  49.985  1.00 16.13           C  
ANISOU 3987  CG1 ILE C  48     2134   2029   1966    -36    -80    -33       C  
ATOM   3988  CG2 ILE C  48     -46.344  20.098  51.359  1.00 15.51           C  
ANISOU 3988  CG2 ILE C  48     2047   1949   1896    -30    -78    -54       C  
ATOM   3989  CD1 ILE C  48     -48.434  17.717  51.151  1.00 16.70           C  
ANISOU 3989  CD1 ILE C  48     2203   2118   2023    -44    -87    -27       C  
ATOM   3990  N   TYR C  49     -47.931  22.538  52.671  1.00 14.47           N  
ANISOU 3990  N   TYR C  49     1902   1834   1762    -14    -78    -81       N  
ATOM   3991  CA  TYR C  49     -47.250  23.736  53.164  1.00 14.87           C  
ANISOU 3991  CA  TYR C  49     1952   1876   1821     -9    -80    -96       C  
ATOM   3992  C   TYR C  49     -46.254  23.292  54.250  1.00 13.60           C  
ANISOU 3992  C   TYR C  49     1786   1725   1657    -14    -81    -99       C  
ATOM   3993  O   TYR C  49     -46.304  22.096  54.665  1.00 14.46           O  
ANISOU 3993  O   TYR C  49     1892   1848   1756    -20    -81    -90       O  
ATOM   3994  CB  TYR C  49     -48.275  24.779  53.681  1.00 15.26           C  
ANISOU 3994  CB  TYR C  49     1996   1935   1867      5    -85   -111       C  
ATOM   3995  CG  TYR C  49     -48.966  24.316  54.936  1.00 15.73           C  
ANISOU 3995  CG  TYR C  49     2041   2026   1909      7    -85   -116       C  
ATOM   3996  CD1 TYR C  49     -48.429  24.620  56.183  1.00 16.88           C  
ANISOU 3996  CD1 TYR C  49     2179   2184   2052     10    -88   -129       C  
ATOM   3997  CD2 TYR C  49     -50.134  23.568  54.879  1.00 15.45           C  
ANISOU 3997  CD2 TYR C  49     1998   2012   1859      5    -84   -108       C  
ATOM   3998  CE1 TYR C  49     -49.023  24.199  57.335  1.00 19.37           C  
ANISOU 3998  CE1 TYR C  49     2479   2532   2349     11    -89   -133       C  
ATOM   3999  CE2 TYR C  49     -50.726  23.094  56.048  1.00 18.61           C  
ANISOU 3999  CE2 TYR C  49     2384   2447   2241      4    -85   -110       C  
ATOM   4000  CZ  TYR C  49     -50.153  23.400  57.261  1.00 18.21           C  
ANISOU 4000  CZ  TYR C  49     2325   2408   2186      6    -87   -122       C  
ATOM   4001  OH  TYR C  49     -50.744  22.966  58.435  1.00 19.83           O  
ANISOU 4001  OH  TYR C  49     2514   2651   2371      4    -88   -124       O  
ATOM   4002  N   ASP C  50     -45.293  24.157  54.590  1.00 15.09           N  
ANISOU 4002  N   ASP C  50     1975   1904   1854    -13    -83   -110       N  
ATOM   4003  CA  ASP C  50     -44.278  23.806  55.612  1.00 13.90           C  
ANISOU 4003  CA  ASP C  50     1818   1763   1700    -17    -83   -115       C  
ATOM   4004  C   ASP C  50     -43.647  22.444  55.306  1.00 15.28           C  
ANISOU 4004  C   ASP C  50     1995   1939   1871    -25    -82   -101       C  
ATOM   4005  O   ASP C  50     -43.432  21.625  56.200  1.00 16.65           O  
ANISOU 4005  O   ASP C  50     2165   2128   2035    -26    -84    -99       O  
ATOM   4006  CB  ASP C  50     -44.866  23.871  57.059  1.00 16.34           C  
ANISOU 4006  CB  ASP C  50     2116   2096   1997    -11    -86   -125       C  
ATOM   4007  CG  ASP C  50     -44.950  25.305  57.575  1.00 17.46           C  
ANISOU 4007  CG  ASP C  50     2255   2234   2143     -1    -91   -145       C  
ATOM   4008  OD1 ASP C  50     -44.525  26.222  56.857  1.00 19.42           O  
ANISOU 4008  OD1 ASP C  50     2514   2459   2406     -1    -94   -149       O  
ATOM   4009  OD2 ASP C  50     -45.399  25.501  58.742  1.00 20.01           O  
ANISOU 4009  OD2 ASP C  50     2568   2579   2457      7    -94   -158       O  
ATOM   4010  N   ASN C  51     -43.308  22.257  54.019  1.00 13.84           N  
ANISOU 4010  N   ASN C  51     1821   1743   1696    -28    -79    -92       N  
ATOM   4011  CA  ASN C  51     -42.570  21.071  53.484  1.00 14.31           C  
ANISOU 4011  CA  ASN C  51     1883   1800   1753    -31    -80    -82       C  
ATOM   4012  C   ASN C  51     -43.418  19.816  53.311  1.00 15.08           C  
ANISOU 4012  C   ASN C  51     1985   1903   1842    -32    -83    -70       C  
ATOM   4013  O   ASN C  51     -43.347  19.169  52.282  1.00 15.26           O  
ANISOU 4013  O   ASN C  51     2014   1918   1866    -32    -84    -61       O  
ATOM   4014  CB  ASN C  51     -41.338  20.697  54.328  1.00 14.56           C  
ANISOU 4014  CB  ASN C  51     1910   1840   1781    -32    -82    -88       C  
ATOM   4015  CG  ASN C  51     -40.355  21.827  54.491  1.00 15.37           C  
ANISOU 4015  CG  ASN C  51     2008   1940   1892    -35    -80   -100       C  
ATOM   4016  OD1 ASN C  51     -40.269  22.726  53.650  1.00 17.33           O  
ANISOU 4016  OD1 ASN C  51     2259   2176   2149    -39    -78   -101       O  
ATOM   4017  ND2 ASN C  51     -39.550  21.755  55.588  1.00 16.14           N  
ANISOU 4017  ND2 ASN C  51     2099   2048   1986    -34    -83   -109       N  
ATOM   4018  N   ASN C  52     -44.193  19.462  54.328  1.00 15.82           N  
ANISOU 4018  N   ASN C  52     2075   2011   1924    -33    -86    -68       N  
ATOM   4019  CA  ASN C  52     -44.875  18.195  54.377  1.00 16.18           C  
ANISOU 4019  CA  ASN C  52     2125   2064   1960    -38    -92    -54       C  
ATOM   4020  C   ASN C  52     -46.259  18.206  55.034  1.00 15.22           C  
ANISOU 4020  C   ASN C  52     1997   1961   1826    -43    -92    -51       C  
ATOM   4021  O   ASN C  52     -46.812  17.131  55.287  1.00 16.61           O  
ANISOU 4021  O   ASN C  52     2176   2145   1990    -52    -98    -38       O  
ATOM   4022  CB  ASN C  52     -43.987  17.165  55.066  1.00 17.06           C  
ANISOU 4022  CB  ASN C  52     2240   2178   2065    -40   -100    -51       C  
ATOM   4023  CG  ASN C  52     -43.733  17.484  56.539  1.00 20.78           C  
ANISOU 4023  CG  ASN C  52     2701   2665   2529    -41   -101    -59       C  
ATOM   4024  OD1 ASN C  52     -44.308  18.403  57.083  1.00 19.20           O  
ANISOU 4024  OD1 ASN C  52     2491   2476   2327    -39    -96    -67       O  
ATOM   4025  ND2 ASN C  52     -42.854  16.706  57.177  1.00 26.06           N  
ANISOU 4025  ND2 ASN C  52     3374   3336   3193    -41   -108    -58       N  
ATOM   4026  N   GLN C  53     -46.834  19.374  55.284  1.00 14.92           N  
ANISOU 4026  N   GLN C  53     1950   1930   1789    -36    -87    -63       N  
ATOM   4027  CA  GLN C  53     -48.140  19.431  55.950  1.00 16.82           C  
ANISOU 4027  CA  GLN C  53     2180   2196   2014    -38    -87    -63       C  
ATOM   4028  C   GLN C  53     -49.266  19.467  54.941  1.00 18.50           C  
ANISOU 4028  C   GLN C  53     2395   2408   2228    -38    -85    -57       C  
ATOM   4029  O   GLN C  53     -49.207  20.249  54.000  1.00 19.31           O  
ANISOU 4029  O   GLN C  53     2502   2492   2342    -29    -82    -62       O  
ATOM   4030  CB  GLN C  53     -48.192  20.664  56.865  1.00 17.08           C  
ANISOU 4030  CB  GLN C  53     2201   2241   2047    -27    -86    -82       C  
ATOM   4031  CG  GLN C  53     -47.100  20.691  57.891  1.00 18.60           C  
ANISOU 4031  CG  GLN C  53     2390   2437   2239    -28    -88    -90       C  
ATOM   4032  CD  GLN C  53     -47.301  19.640  58.947  1.00 20.27           C  
ANISOU 4032  CD  GLN C  53     2596   2673   2433    -38    -92    -80       C  
ATOM   4033  OE1 GLN C  53     -46.617  18.606  58.959  1.00 21.21           O  
ANISOU 4033  OE1 GLN C  53     2723   2783   2550    -46    -97    -67       O  
ATOM   4034  NE2 GLN C  53     -48.268  19.874  59.803  1.00 20.66           N  
ANISOU 4034  NE2 GLN C  53     2631   2753   2466    -37    -92    -85       N  
ATOM   4035  N   ARG C  54     -50.300  18.651  55.137  1.00 18.75           N  
ANISOU 4035  N   ARG C  54     2422   2458   2242    -48    -88    -45       N  
ATOM   4036  CA  ARG C  54     -51.391  18.574  54.167  1.00 19.85           C  
ANISOU 4036  CA  ARG C  54     2563   2599   2380    -49    -86    -39       C  
ATOM   4037  C   ARG C  54     -52.634  19.208  54.763  1.00 20.85           C  
ANISOU 4037  C   ARG C  54     2672   2758   2492    -44    -84    -48       C  
ATOM   4038  O   ARG C  54     -53.091  18.769  55.841  1.00 22.59           O  
ANISOU 4038  O   ARG C  54     2881   3009   2693    -53    -87    -45       O  
ATOM   4039  CB  ARG C  54     -51.614  17.092  53.828  1.00 21.08           C  
ANISOU 4039  CB  ARG C  54     2728   2753   2528    -66    -92    -18       C  
ATOM   4040  CG  ARG C  54     -52.401  16.785  52.583  1.00 25.01           C  
ANISOU 4040  CG  ARG C  54     3232   3243   3028    -68    -92     -9       C  
ATOM   4041  CD  ARG C  54     -52.355  15.269  52.206  1.00 30.75           C  
ANISOU 4041  CD  ARG C  54     3973   3959   3750    -84   -102     11       C  
ATOM   4042  NE  ARG C  54     -52.330  14.411  53.378  1.00 36.47           N  
ANISOU 4042  NE  ARG C  54     4696   4700   4459   -100   -111     21       N  
ATOM   4043  CZ  ARG C  54     -51.375  13.525  53.671  1.00 36.98           C  
ANISOU 4043  CZ  ARG C  54     4775   4749   4526   -105   -121     28       C  
ATOM   4044  NH1 ARG C  54     -50.328  13.322  52.867  1.00 36.38           N  
ANISOU 4044  NH1 ARG C  54     4713   4644   4466    -94   -124     25       N  
ATOM   4045  NH2 ARG C  54     -51.480  12.820  54.781  1.00 38.80           N  
ANISOU 4045  NH2 ARG C  54     5006   4996   4742   -121   -131     38       N  
ATOM   4046  N   PRO C  55     -53.145  20.293  54.137  1.00 21.71           N  
ANISOU 4046  N   PRO C  55     2780   2863   2608    -28    -81    -61       N  
ATOM   4047  CA  PRO C  55     -54.407  20.880  54.610  1.00 23.16           C  
ANISOU 4047  CA  PRO C  55     2945   3079   2775    -19    -81    -73       C  
ATOM   4048  C   PRO C  55     -55.563  19.883  54.478  1.00 25.13           C  
ANISOU 4048  C   PRO C  55     3188   3356   3006    -35    -81    -57       C  
ATOM   4049  O   PRO C  55     -55.493  18.914  53.726  1.00 25.00           O  
ANISOU 4049  O   PRO C  55     3182   3323   2992    -49    -82    -39       O  
ATOM   4050  CB  PRO C  55     -54.614  22.105  53.706  1.00 24.19           C  
ANISOU 4050  CB  PRO C  55     3081   3189   2920      1    -80    -87       C  
ATOM   4051  CG  PRO C  55     -53.402  22.238  52.869  1.00 21.86           C  
ANISOU 4051  CG  PRO C  55     2805   2853   2648      0    -79    -82       C  
ATOM   4052  CD  PRO C  55     -52.696  20.906  52.875  1.00 20.06           C  
ANISOU 4052  CD  PRO C  55     2584   2620   2419    -19    -79    -63       C  
ATOM   4053  N   SER C  56     -56.625  20.101  55.246  1.00 26.79           N  
ANISOU 4053  N   SER C  56     3377   3609   3194    -32    -82    -65       N  
ATOM   4054  CA  SER C  56     -57.782  19.227  55.133  1.00 28.19           C  
ANISOU 4054  CA  SER C  56     3545   3817   3351    -50    -83    -51       C  
ATOM   4055  C   SER C  56     -58.390  19.382  53.738  1.00 28.26           C  
ANISOU 4055  C   SER C  56     3561   3810   3368    -43    -80    -48       C  
ATOM   4056  O   SER C  56     -58.337  20.463  53.127  1.00 28.47           O  
ANISOU 4056  O   SER C  56     3591   3817   3408    -20    -79    -64       O  
ATOM   4057  CB  SER C  56     -58.798  19.549  56.215  1.00 29.39           C  
ANISOU 4057  CB  SER C  56     3668   4024   3474    -47    -83    -62       C  
ATOM   4058  OG  SER C  56     -58.992  20.953  56.244  1.00 33.59           O  
ANISOU 4058  OG  SER C  56     4192   4558   4011    -16    -82    -90       O  
ATOM   4059  N   GLY C  57     -58.930  18.282  53.227  1.00 28.13           N  
ANISOU 4059  N   GLY C  57     3547   3798   3342    -65    -82    -28       N  
ATOM   4060  CA  GLY C  57     -59.575  18.281  51.926  1.00 28.01           C  
ANISOU 4060  CA  GLY C  57     3538   3772   3333    -61    -80    -24       C  
ATOM   4061  C   GLY C  57     -58.615  18.089  50.776  1.00 27.51           C  
ANISOU 4061  C   GLY C  57     3499   3657   3295    -59    -80    -16       C  
ATOM   4062  O   GLY C  57     -58.991  18.228  49.592  1.00 29.36           O  
ANISOU 4062  O   GLY C  57     3741   3878   3538    -53    -78    -15       O  
ATOM   4063  N   VAL C  58     -57.363  17.788  51.113  1.00 25.80           N  
ANISOU 4063  N   VAL C  58     3295   3418   3091    -63    -82    -13       N  
ATOM   4064  CA  VAL C  58     -56.379  17.428  50.111  1.00 23.42           C  
ANISOU 4064  CA  VAL C  58     3013   3075   2809    -63    -83     -5       C  
ATOM   4065  C   VAL C  58     -56.225  15.919  50.193  1.00 22.85           C  
ANISOU 4065  C   VAL C  58     2952   3000   2730    -86    -91     15       C  
ATOM   4066  O   VAL C  58     -56.000  15.387  51.286  1.00 22.05           O  
ANISOU 4066  O   VAL C  58     2847   2912   2618    -98    -96     21       O  
ATOM   4067  CB  VAL C  58     -55.025  18.110  50.422  1.00 22.59           C  
ANISOU 4067  CB  VAL C  58     2915   2947   2720    -51    -81    -16       C  
ATOM   4068  CG1 VAL C  58     -53.896  17.585  49.497  1.00 23.59           C  
ANISOU 4068  CG1 VAL C  58     3060   3040   2865    -53    -82     -8       C  
ATOM   4069  CG2 VAL C  58     -55.167  19.622  50.250  1.00 23.05           C  
ANISOU 4069  CG2 VAL C  58     2968   3003   2787    -30    -76    -35       C  
ATOM   4070  N   PRO C  59     -56.332  15.222  49.043  1.00 21.51           N  
ANISOU 4070  N   PRO C  59     2794   2811   2566    -91    -94     26       N  
ATOM   4071  CA  PRO C  59     -56.166  13.774  49.038  1.00 22.04           C  
ANISOU 4071  CA  PRO C  59     2876   2870   2629   -111   -106     44       C  
ATOM   4072  C   PRO C  59     -54.877  13.280  49.695  1.00 22.07           C  
ANISOU 4072  C   PRO C  59     2890   2857   2638   -112   -113     46       C  
ATOM   4073  O   PRO C  59     -53.819  13.877  49.497  1.00 21.53           O  
ANISOU 4073  O   PRO C  59     2825   2770   2585    -96   -108     35       O  
ATOM   4074  CB  PRO C  59     -56.185  13.446  47.537  1.00 22.08           C  
ANISOU 4074  CB  PRO C  59     2894   2851   2646   -106   -107     49       C  
ATOM   4075  CG  PRO C  59     -57.066  14.450  46.988  1.00 22.74           C  
ANISOU 4075  CG  PRO C  59     2965   2947   2729    -95    -97     39       C  
ATOM   4076  CD  PRO C  59     -56.674  15.709  47.698  1.00 21.83           C  
ANISOU 4076  CD  PRO C  59     2838   2838   2617    -79    -89     23       C  
ATOM   4077  N   ASP C  60     -55.009  12.212  50.493  1.00 22.87           N  
ANISOU 4077  N   ASP C  60     2997   2968   2726   -133   -126     61       N  
ATOM   4078  CA  ASP C  60     -53.925  11.491  51.149  1.00 22.85           C  
ANISOU 4078  CA  ASP C  60     3007   2949   2725   -137   -137     65       C  
ATOM   4079  C   ASP C  60     -52.772  11.053  50.233  1.00 20.72           C  
ANISOU 4079  C   ASP C  60     2756   2643   2472   -124   -143     63       C  
ATOM   4080  O   ASP C  60     -51.651  10.862  50.693  1.00 21.41           O  
ANISOU 4080  O   ASP C  60     2850   2718   2565   -117   -148     58       O  
ATOM   4081  CB  ASP C  60     -54.484  10.234  51.851  1.00 24.58           C  
ANISOU 4081  CB  ASP C  60     3235   3180   2925   -165   -154     87       C  
ATOM   4082  CG  ASP C  60     -55.297  10.567  53.078  1.00 29.28           C  
ANISOU 4082  CG  ASP C  60     3809   3818   3499   -180   -150     89       C  
ATOM   4083  OD1 ASP C  60     -55.305  11.750  53.476  1.00 32.78           O  
ANISOU 4083  OD1 ASP C  60     4233   4278   3943   -164   -135     72       O  
ATOM   4084  OD2 ASP C  60     -55.932   9.640  53.640  1.00 34.29           O  
ANISOU 4084  OD2 ASP C  60     4447   4469   4115   -208   -162    108       O  
ATOM   4085  N   ARG C  61     -53.049  10.873  48.948  1.00 20.85           N  
ANISOU 4085  N   ARG C  61     2781   2645   2498   -119   -143     64       N  
ATOM   4086  CA  ARG C  61     -52.001  10.457  48.035  1.00 19.76           C  
ANISOU 4086  CA  ARG C  61     2657   2478   2373   -105   -149     59       C  
ATOM   4087  C   ARG C  61     -50.932  11.511  47.762  1.00 18.54           C  
ANISOU 4087  C   ARG C  61     2495   2316   2232    -84   -136     42       C  
ATOM   4088  O   ARG C  61     -49.910  11.205  47.143  1.00 19.05           O  
ANISOU 4088  O   ARG C  61     2568   2364   2306    -72   -141     37       O  
ATOM   4089  CB  ARG C  61     -52.580  10.010  46.702  1.00 20.21           C  
ANISOU 4089  CB  ARG C  61     2722   2523   2433   -105   -153     64       C  
ATOM   4090  CG  ARG C  61     -53.370  11.004  45.929  1.00 23.39           C  
ANISOU 4090  CG  ARG C  61     3112   2936   2839    -99   -136     59       C  
ATOM   4091  CD  ARG C  61     -53.742  10.344  44.613  1.00 24.44           C  
ANISOU 4091  CD  ARG C  61     3256   3055   2975    -99   -143     64       C  
ATOM   4092  NE  ARG C  61     -54.618  11.162  43.771  1.00 24.69           N  
ANISOU 4092  NE  ARG C  61     3276   3096   3009    -94   -129     61       N  
ATOM   4093  CZ  ARG C  61     -55.910  11.393  44.009  1.00 23.33           C  
ANISOU 4093  CZ  ARG C  61     3093   2946   2824   -105   -125     66       C  
ATOM   4094  NH1 ARG C  61     -56.499  10.937  45.109  1.00 25.56           N  
ANISOU 4094  NH1 ARG C  61     3372   3248   3092   -124   -132     75       N  
ATOM   4095  NH2 ARG C  61     -56.611  12.119  43.164  1.00 25.57           N  
ANISOU 4095  NH2 ARG C  61     3369   3236   3111    -97   -115     62       N  
ATOM   4096  N   PHE C  62     -51.189  12.759  48.167  1.00 17.67           N  
ANISOU 4096  N   PHE C  62     2369   2222   2124    -80   -121     33       N  
ATOM   4097  CA  PHE C  62     -50.168  13.784  48.052  1.00 16.88           C  
ANISOU 4097  CA  PHE C  62     2262   2115   2035    -65   -111     19       C  
ATOM   4098  C   PHE C  62     -49.347  13.901  49.334  1.00 16.85           C  
ANISOU 4098  C   PHE C  62     2255   2117   2029    -65   -113     14       C  
ATOM   4099  O   PHE C  62     -49.873  13.913  50.453  1.00 17.90           O  
ANISOU 4099  O   PHE C  62     2381   2269   2151    -74   -114     16       O  
ATOM   4100  CB  PHE C  62     -50.825  15.126  47.748  1.00 17.32           C  
ANISOU 4100  CB  PHE C  62     2307   2179   2095    -58    -98     11       C  
ATOM   4101  CG  PHE C  62     -51.563  15.144  46.454  1.00 15.57           C  
ANISOU 4101  CG  PHE C  62     2088   1952   1877    -56    -95     16       C  
ATOM   4102  CD1 PHE C  62     -50.884  15.254  45.268  1.00 18.65           C  
ANISOU 4102  CD1 PHE C  62     2484   2325   2278    -48    -93     13       C  
ATOM   4103  CD2 PHE C  62     -52.948  15.114  46.439  1.00 21.08           C  
ANISOU 4103  CD2 PHE C  62     2780   2664   2564    -63    -94     21       C  
ATOM   4104  CE1 PHE C  62     -51.582  15.286  44.049  1.00 16.93           C  
ANISOU 4104  CE1 PHE C  62     2268   2103   2062    -45    -90     17       C  
ATOM   4105  CE2 PHE C  62     -53.639  15.125  45.227  1.00 20.53           C  
ANISOU 4105  CE2 PHE C  62     2713   2591   2497    -61    -92     24       C  
ATOM   4106  CZ  PHE C  62     -52.951  15.230  44.049  1.00 18.76           C  
ANISOU 4106  CZ  PHE C  62     2497   2348   2286    -51    -90     23       C  
ATOM   4107  N   SER C  63     -48.038  13.959  49.144  1.00 16.71           N  
ANISOU 4107  N   SER C  63     2241   2088   2021    -55   -114      6       N  
ATOM   4108  CA  SER C  63     -47.120  14.152  50.257  1.00 16.39           C  
ANISOU 4108  CA  SER C  63     2196   2053   1980    -53   -114     -2       C  
ATOM   4109  C   SER C  63     -45.931  14.976  49.804  1.00 16.66           C  
ANISOU 4109  C   SER C  63     2226   2080   2025    -41   -107    -14       C  
ATOM   4110  O   SER C  63     -45.616  15.077  48.594  1.00 16.55           O  
ANISOU 4110  O   SER C  63     2214   2055   2018    -35   -104    -16       O  
ATOM   4111  CB  SER C  63     -46.679  12.802  50.852  1.00 17.88           C  
ANISOU 4111  CB  SER C  63     2397   2237   2160    -57   -131      6       C  
ATOM   4112  OG  SER C  63     -45.919  12.020  49.921  1.00 19.24           O  
ANISOU 4112  OG  SER C  63     2580   2392   2337    -48   -141      5       O  
ATOM   4113  N   GLY C  64     -45.246  15.571  50.764  1.00 15.73           N  
ANISOU 4113  N   GLY C  64     2100   1969   1908    -40   -104    -23       N  
ATOM   4114  CA  GLY C  64     -44.096  16.432  50.442  1.00 16.96           C  
ANISOU 4114  CA  GLY C  64     2250   2120   2073    -33    -97    -35       C  
ATOM   4115  C   GLY C  64     -42.895  16.124  51.299  1.00 16.66           C  
ANISOU 4115  C   GLY C  64     2210   2087   2032    -30   -102    -42       C  
ATOM   4116  O   GLY C  64     -43.042  15.692  52.439  1.00 17.68           O  
ANISOU 4116  O   GLY C  64     2340   2225   2154    -33   -108    -40       O  
ATOM   4117  N   SER C  65     -41.704  16.381  50.762  1.00 17.29           N  
ANISOU 4117  N   SER C  65     2286   2165   2117    -24   -100    -50       N  
ATOM   4118  CA  SER C  65     -40.483  16.351  51.559  1.00 17.78           C  
ANISOU 4118  CA  SER C  65     2344   2235   2178    -20   -102    -60       C  
ATOM   4119  C   SER C  65     -39.528  17.438  51.090  1.00 18.73           C  
ANISOU 4119  C   SER C  65     2453   2357   2304    -21    -93    -69       C  
ATOM   4120  O   SER C  65     -39.665  18.012  49.993  1.00 17.90           O  
ANISOU 4120  O   SER C  65     2348   2248   2205    -24    -87    -67       O  
ATOM   4121  CB  SER C  65     -39.857  14.962  51.491  1.00 18.08           C  
ANISOU 4121  CB  SER C  65     2389   2271   2208    -12   -116    -59       C  
ATOM   4122  OG  SER C  65     -39.404  14.726  50.180  1.00 20.40           O  
ANISOU 4122  OG  SER C  65     2684   2562   2505     -5   -116    -61       O  
ATOM   4123  N   LYS C  66     -38.561  17.729  51.935  1.00 19.67           N  
ANISOU 4123  N   LYS C  66     2566   2486   2422    -21    -93    -79       N  
ATOM   4124  CA  LYS C  66     -37.507  18.661  51.613  1.00 20.53           C  
ANISOU 4124  CA  LYS C  66     2664   2601   2535    -25    -87    -88       C  
ATOM   4125  C   LYS C  66     -36.191  18.140  52.160  1.00 22.71           C  
ANISOU 4125  C   LYS C  66     2934   2891   2805    -19    -92    -97       C  
ATOM   4126  O   LYS C  66     -36.143  17.535  53.259  1.00 22.66           O  
ANISOU 4126  O   LYS C  66     2929   2888   2793    -13    -99    -99       O  
ATOM   4127  CB  LYS C  66     -37.828  20.029  52.217  1.00 21.27           C  
ANISOU 4127  CB  LYS C  66     2755   2691   2635    -34    -81    -92       C  
ATOM   4128  CG  LYS C  66     -36.711  21.035  52.085  1.00 23.64           C  
ANISOU 4128  CG  LYS C  66     3047   2996   2940    -42    -77   -100       C  
ATOM   4129  CD  LYS C  66     -36.865  22.173  53.057  1.00 24.60           C  
ANISOU 4129  CD  LYS C  66     3167   3114   3067    -48    -76   -107       C  
ATOM   4130  CE  LYS C  66     -35.558  22.886  53.226  1.00 23.77           C  
ANISOU 4130  CE  LYS C  66     3052   3016   2962    -58    -76   -116       C  
ATOM   4131  NZ  LYS C  66     -35.646  23.965  54.215  1.00 19.71           N  
ANISOU 4131  NZ  LYS C  66     2538   2497   2453    -62    -77   -125       N  
ATOM   4132  N   SER C  67     -35.124  18.384  51.408  1.00 22.23           N  
ANISOU 4132  N   SER C  67     2864   2841   2742    -19    -89   -103       N  
ATOM   4133  CA  SER C  67     -33.788  18.082  51.870  1.00 24.99           C  
ANISOU 4133  CA  SER C  67     3204   3209   3085    -13    -93   -115       C  
ATOM   4134  C   SER C  67     -32.801  19.069  51.242  1.00 23.35           C  
ANISOU 4134  C   SER C  67     2981   3015   2877    -25    -85   -121       C  
ATOM   4135  O   SER C  67     -32.657  19.142  50.011  1.00 22.97           O  
ANISOU 4135  O   SER C  67     2930   2971   2827    -28    -82   -117       O  
ATOM   4136  CB  SER C  67     -33.441  16.648  51.516  1.00 25.51           C  
ANISOU 4136  CB  SER C  67     3273   3279   3141      5   -105   -117       C  
ATOM   4137  OG  SER C  67     -32.042  16.395  51.620  1.00 31.19           O  
ANISOU 4137  OG  SER C  67     3980   4020   3851     14   -109   -131       O  
ATOM   4138  N   GLY C  68     -32.152  19.846  52.090  1.00 23.12           N  
ANISOU 4138  N   GLY C  68     2943   2993   2848    -34    -83   -128       N  
ATOM   4139  CA  GLY C  68     -31.131  20.793  51.616  1.00 22.51           C  
ANISOU 4139  CA  GLY C  68     2852   2931   2769    -49    -77   -133       C  
ATOM   4140  C   GLY C  68     -31.729  21.898  50.771  1.00 20.98           C  
ANISOU 4140  C   GLY C  68     2665   2723   2585    -67    -71   -122       C  
ATOM   4141  O   GLY C  68     -32.578  22.654  51.259  1.00 21.83           O  
ANISOU 4141  O   GLY C  68     2782   2810   2702    -74    -71   -119       O  
ATOM   4142  N   THR C  69     -31.352  21.961  49.484  1.00 21.46           N  
ANISOU 4142  N   THR C  69     2719   2795   2640    -74    -68   -117       N  
ATOM   4143  CA  THR C  69     -31.902  23.002  48.617  1.00 21.17           C  
ANISOU 4143  CA  THR C  69     2689   2743   2611    -92    -64   -105       C  
ATOM   4144  C   THR C  69     -32.896  22.453  47.599  1.00 20.62           C  
ANISOU 4144  C   THR C  69     2629   2663   2544    -83    -63    -95       C  
ATOM   4145  O   THR C  69     -33.257  23.133  46.630  1.00 22.02           O  
ANISOU 4145  O   THR C  69     2810   2832   2724    -96    -60    -85       O  
ATOM   4146  CB  THR C  69     -30.809  23.806  47.862  1.00 20.86           C  
ANISOU 4146  CB  THR C  69     2636   2725   2565   -115    -60   -103       C  
ATOM   4147  OG1 THR C  69     -29.934  22.884  47.209  1.00 22.33           O  
ANISOU 4147  OG1 THR C  69     2806   2943   2735   -106    -59   -109       O  
ATOM   4148  CG2 THR C  69     -29.976  24.660  48.799  1.00 20.29           C  
ANISOU 4148  CG2 THR C  69     2558   2659   2494   -131    -62   -111       C  
ATOM   4149  N   SER C  70     -33.346  21.230  47.852  1.00 19.86           N  
ANISOU 4149  N   SER C  70     2537   2564   2445    -62    -67    -98       N  
ATOM   4150  CA  SER C  70     -34.356  20.572  47.014  1.00 20.39           C  
ANISOU 4150  CA  SER C  70     2614   2620   2513    -53    -68    -89       C  
ATOM   4151  C   SER C  70     -35.571  20.140  47.828  1.00 18.76           C  
ANISOU 4151  C   SER C  70     2421   2393   2313    -43    -71    -86       C  
ATOM   4152  O   SER C  70     -35.500  19.951  49.045  1.00 19.02           O  
ANISOU 4152  O   SER C  70     2455   2426   2346    -39    -75    -92       O  
ATOM   4153  CB  SER C  70     -33.762  19.357  46.305  1.00 21.56           C  
ANISOU 4153  CB  SER C  70     2756   2786   2650    -37    -72    -94       C  
ATOM   4154  OG  SER C  70     -32.864  19.784  45.288  1.00 26.93           O  
ANISOU 4154  OG  SER C  70     3421   3489   3323    -46    -67    -95       O  
ATOM   4155  N   ALA C  71     -36.683  19.996  47.120  1.00 17.42           N  
ANISOU 4155  N   ALA C  71     2261   2209   2147    -41    -71    -76       N  
ATOM   4156  CA  ALA C  71     -37.965  19.538  47.669  1.00 17.35           C  
ANISOU 4156  CA  ALA C  71     2264   2186   2142    -35    -74    -71       C  
ATOM   4157  C   ALA C  71     -38.676  18.675  46.655  1.00 17.63           C  
ANISOU 4157  C   ALA C  71     2307   2217   2176    -28    -76    -63       C  
ATOM   4158  O   ALA C  71     -38.431  18.743  45.409  1.00 18.86           O  
ANISOU 4158  O   ALA C  71     2460   2377   2330    -29    -73    -61       O  
ATOM   4159  CB  ALA C  71     -38.839  20.734  48.049  1.00 17.67           C  
ANISOU 4159  CB  ALA C  71     2309   2213   2191    -44    -70    -69       C  
ATOM   4160  N   VAL C  72     -39.571  17.835  47.151  1.00 17.51           N  
ANISOU 4160  N   VAL C  72     2301   2194   2159    -22    -82    -59       N  
ATOM   4161  CA  VAL C  72     -40.270  16.895  46.309  1.00 17.72           C  
ANISOU 4161  CA  VAL C  72     2336   2215   2183    -15    -87    -52       C  
ATOM   4162  C   VAL C  72     -41.726  16.721  46.708  1.00 16.10           C  
ANISOU 4162  C   VAL C  72     2140   2000   1979    -19    -89    -43       C  
ATOM   4163  O   VAL C  72     -42.044  16.637  47.895  1.00 18.12           O  
ANISOU 4163  O   VAL C  72     2396   2257   2232    -21    -92    -43       O  
ATOM   4164  CB  VAL C  72     -39.549  15.541  46.358  1.00 18.97           C  
ANISOU 4164  CB  VAL C  72     2497   2378   2334     -3   -100    -57       C  
ATOM   4165  CG1 VAL C  72     -40.297  14.511  45.579  1.00 23.06           C  
ANISOU 4165  CG1 VAL C  72     3026   2887   2849      4   -108    -50       C  
ATOM   4166  CG2 VAL C  72     -38.198  15.677  45.740  1.00 21.27           C  
ANISOU 4166  CG2 VAL C  72     2776   2685   2621      3    -98    -67       C  
ATOM   4167  N   LEU C  73     -42.610  16.682  45.711  1.00 14.79           N  
ANISOU 4167  N   LEU C  73     1978   1827   1815    -19    -87    -35       N  
ATOM   4168  CA  LEU C  73     -44.010  16.316  45.870  1.00 13.34           C  
ANISOU 4168  CA  LEU C  73     1802   1639   1629    -22    -89    -27       C  
ATOM   4169  C   LEU C  73     -44.144  14.867  45.340  1.00 15.02           C  
ANISOU 4169  C   LEU C  73     2024   1847   1837    -17   -101    -22       C  
ATOM   4170  O   LEU C  73     -43.762  14.587  44.171  1.00 15.29           O  
ANISOU 4170  O   LEU C  73     2060   1880   1872    -11   -102    -23       O  
ATOM   4171  CB  LEU C  73     -44.931  17.279  45.056  1.00 14.05           C  
ANISOU 4171  CB  LEU C  73     1890   1723   1724    -26    -80    -22       C  
ATOM   4172  CG  LEU C  73     -46.413  16.953  45.048  1.00 15.22           C  
ANISOU 4172  CG  LEU C  73     2043   1871   1869    -28    -82    -14       C  
ATOM   4173  CD1 LEU C  73     -46.954  17.267  46.458  1.00 15.03           C  
ANISOU 4173  CD1 LEU C  73     2015   1856   1841    -32    -82    -17       C  
ATOM   4174  CD2 LEU C  73     -47.160  17.727  43.993  1.00 17.99           C  
ANISOU 4174  CD2 LEU C  73     2394   2217   2224    -27    -75    -11       C  
ATOM   4175  N   ALA C  74     -44.728  13.987  46.141  1.00 15.42           N  
ANISOU 4175  N   ALA C  74     2082   1895   1881    -21   -111    -15       N  
ATOM   4176  CA  ALA C  74     -44.952  12.608  45.709  1.00 16.81           C  
ANISOU 4176  CA  ALA C  74     2271   2063   2052    -18   -126     -9       C  
ATOM   4177  C   ALA C  74     -46.446  12.444  45.569  1.00 16.89           C  
ANISOU 4177  C   ALA C  74     2286   2072   2059    -29   -127      2       C  
ATOM   4178  O   ALA C  74     -47.248  12.862  46.449  1.00 16.79           O  
ANISOU 4178  O   ALA C  74     2269   2068   2043    -39   -122      7       O  
ATOM   4179  CB  ALA C  74     -44.419  11.594  46.766  1.00 17.81           C  
ANISOU 4179  CB  ALA C  74     2408   2188   2172    -17   -143     -9       C  
ATOM   4180  N   ILE C  75     -46.832  11.825  44.458  1.00 16.56           N  
ANISOU 4180  N   ILE C  75     2252   2021   2017    -26   -132      7       N  
ATOM   4181  CA  ILE C  75     -48.203  11.444  44.257  1.00 16.60           C  
ANISOU 4181  CA  ILE C  75     2263   2026   2019    -37   -135     18       C  
ATOM   4182  C   ILE C  75     -48.236   9.939  44.248  1.00 17.64           C  
ANISOU 4182  C   ILE C  75     2412   2145   2144    -40   -157     25       C  
ATOM   4183  O   ILE C  75     -47.772   9.325  43.306  1.00 17.88           O  
ANISOU 4183  O   ILE C  75     2450   2166   2177    -28   -166     20       O  
ATOM   4184  CB  ILE C  75     -48.792  11.969  42.924  1.00 15.86           C  
ANISOU 4184  CB  ILE C  75     2165   1931   1929    -34   -125     19       C  
ATOM   4185  CG1 ILE C  75     -48.581  13.494  42.767  1.00 18.46           C  
ANISOU 4185  CG1 ILE C  75     2481   2268   2266    -30   -107     12       C  
ATOM   4186  CG2 ILE C  75     -50.274  11.623  42.892  1.00 18.75           C  
ANISOU 4186  CG2 ILE C  75     2534   2301   2289    -47   -128     30       C  
ATOM   4187  CD1 ILE C  75     -48.891  14.047  41.347  1.00 19.65           C  
ANISOU 4187  CD1 ILE C  75     2628   2416   2421    -25    -99     12       C  
ATOM   4188  N   THR C  76     -48.747   9.368  45.313  1.00 17.73           N  
ANISOU 4188  N   THR C  76     2430   2159   2147    -54   -167     35       N  
ATOM   4189  CA  THR C  76     -48.657   7.914  45.453  1.00 20.36           C  
ANISOU 4189  CA  THR C  76     2785   2478   2475    -58   -192     42       C  
ATOM   4190  C   THR C  76     -49.992   7.256  45.119  1.00 21.10           C  
ANISOU 4190  C   THR C  76     2887   2568   2561    -76   -201     57       C  
ATOM   4191  O   THR C  76     -50.966   7.386  45.883  1.00 24.64           O  
ANISOU 4191  O   THR C  76     3331   3032   3001    -96   -198     69       O  
ATOM   4192  CB  THR C  76     -48.151   7.558  46.910  1.00 19.18           C  
ANISOU 4192  CB  THR C  76     2639   2329   2318    -64   -203     45       C  
ATOM   4193  OG1 THR C  76     -46.912   8.256  47.151  1.00 23.27           O  
ANISOU 4193  OG1 THR C  76     3146   2852   2842    -48   -193     30       O  
ATOM   4194  CG2 THR C  76     -47.927   6.035  47.065  1.00 22.16           C  
ANISOU 4194  CG2 THR C  76     3043   2687   2690    -67   -233     53       C  
ATOM   4195  N   GLY C  77     -50.047   6.495  44.013  1.00 20.59           N  
ANISOU 4195  N   GLY C  77     2836   2488   2500    -69   -214     57       N  
ATOM   4196  CA  GLY C  77     -51.297   5.905  43.545  1.00 19.73           C  
ANISOU 4196  CA  GLY C  77     2735   2376   2385    -86   -222     70       C  
ATOM   4197  C   GLY C  77     -52.029   6.865  42.626  1.00 19.14           C  
ANISOU 4197  C   GLY C  77     2644   2315   2315    -84   -200     67       C  
ATOM   4198  O   GLY C  77     -53.225   7.044  42.750  1.00 18.91           O  
ANISOU 4198  O   GLY C  77     2608   2298   2278   -101   -195     78       O  
ATOM   4199  N   LEU C  78     -51.314   7.476  41.694  1.00 18.17           N  
ANISOU 4199  N   LEU C  78     2513   2189   2201    -62   -189     54       N  
ATOM   4200  CA  LEU C  78     -51.930   8.563  40.900  1.00 19.24           C  
ANISOU 4200  CA  LEU C  78     2632   2336   2340    -59   -167     51       C  
ATOM   4201  C   LEU C  78     -53.135   8.082  40.077  1.00 18.25           C  
ANISOU 4201  C   LEU C  78     2512   2210   2211    -69   -172     60       C  
ATOM   4202  O   LEU C  78     -53.236   6.913  39.672  1.00 18.28           O  
ANISOU 4202  O   LEU C  78     2534   2200   2213    -72   -192     64       O  
ATOM   4203  CB  LEU C  78     -50.907   9.221  39.985  1.00 19.34           C  
ANISOU 4203  CB  LEU C  78     2638   2348   2363    -38   -157     37       C  
ATOM   4204  CG  LEU C  78     -50.425   8.441  38.791  1.00 19.35           C  
ANISOU 4204  CG  LEU C  78     2649   2337   2366    -24   -169     31       C  
ATOM   4205  CD1 LEU C  78     -51.250   8.863  37.575  1.00 21.38           C  
ANISOU 4205  CD1 LEU C  78     2900   2599   2625    -23   -158     33       C  
ATOM   4206  CD2 LEU C  78     -48.932   8.648  38.524  1.00 17.55           C  
ANISOU 4206  CD2 LEU C  78     2415   2110   2142     -5   -167     16       C  
ATOM   4207  N   GLN C  79     -54.065   8.990  39.821  1.00 17.89           N  
ANISOU 4207  N   GLN C  79     2453   2180   2165    -73   -155     62       N  
ATOM   4208  CA  GLN C  79     -55.224   8.643  39.038  1.00 19.37           C  
ANISOU 4208  CA  GLN C  79     2642   2371   2347    -81   -158     69       C  
ATOM   4209  C   GLN C  79     -55.341   9.583  37.844  1.00 17.36           C  
ANISOU 4209  C   GLN C  79     2376   2119   2099    -66   -142     62       C  
ATOM   4210  O   GLN C  79     -54.644  10.628  37.766  1.00 15.69           O  
ANISOU 4210  O   GLN C  79     2156   1910   1896    -53   -128     53       O  
ATOM   4211  CB  GLN C  79     -56.483   8.693  39.921  1.00 20.93           C  
ANISOU 4211  CB  GLN C  79     2832   2589   2532   -103   -156     80       C  
ATOM   4212  CG  GLN C  79     -56.307   7.861  41.230  1.00 24.98           C  
ANISOU 4212  CG  GLN C  79     3354   3101   3035   -121   -172     90       C  
ATOM   4213  CD  GLN C  79     -56.372   6.367  40.948  1.00 29.21           C  
ANISOU 4213  CD  GLN C  79     3913   3617   3568   -133   -198    100       C  
ATOM   4214  OE1 GLN C  79     -57.337   5.895  40.329  1.00 35.91           O  
ANISOU 4214  OE1 GLN C  79     4766   4468   4411   -145   -204    108       O  
ATOM   4215  NE2 GLN C  79     -55.348   5.608  41.373  1.00 26.28           N  
ANISOU 4215  NE2 GLN C  79     3559   3226   3200   -129   -215     99       N  
ATOM   4216  N   SER C  80     -56.219   9.201  36.921  1.00 18.36           N  
ANISOU 4216  N   SER C  80     2506   2246   2223    -70   -145     66       N  
ATOM   4217  CA  SER C  80     -56.400   9.935  35.683  1.00 19.69           C  
ANISOU 4217  CA  SER C  80     2667   2417   2397    -56   -132     61       C  
ATOM   4218  C   SER C  80     -56.814  11.374  35.953  1.00 19.61           C  
ANISOU 4218  C   SER C  80     2640   2422   2388    -53   -113     58       C  
ATOM   4219  O   SER C  80     -56.415  12.279  35.211  1.00 20.66           O  
ANISOU 4219  O   SER C  80     2768   2554   2528    -39   -102     52       O  
ATOM   4220  CB  SER C  80     -57.396   9.228  34.750  1.00 20.54           C  
ANISOU 4220  CB  SER C  80     2779   2524   2500    -62   -140     66       C  
ATOM   4221  OG  SER C  80     -58.697   9.165  35.296  1.00 20.18           O  
ANISOU 4221  OG  SER C  80     2729   2495   2443    -81   -140     76       O  
ATOM   4222  N   GLU C  81     -57.568  11.596  37.034  1.00 19.38           N  
ANISOU 4222  N   GLU C  81     2605   2409   2351    -65   -111     62       N  
ATOM   4223  CA  GLU C  81     -57.980  12.965  37.350  1.00 19.67           C  
ANISOU 4223  CA  GLU C  81     2627   2459   2387    -58    -97     56       C  
ATOM   4224  C   GLU C  81     -56.855  13.834  37.945  1.00 19.46           C  
ANISOU 4224  C   GLU C  81     2598   2426   2369    -48    -90     48       C  
ATOM   4225  O   GLU C  81     -57.068  15.044  38.163  1.00 21.12           O  
ANISOU 4225  O   GLU C  81     2800   2643   2581    -40    -81     42       O  
ATOM   4226  CB  GLU C  81     -59.193  12.971  38.294  1.00 20.62           C  
ANISOU 4226  CB  GLU C  81     2737   2604   2492    -71    -97     60       C  
ATOM   4227  CG  GLU C  81     -58.924  12.338  39.611  1.00 24.53           C  
ANISOU 4227  CG  GLU C  81     3235   3106   2981    -86   -105     65       C  
ATOM   4228  CD  GLU C  81     -59.437  10.899  39.658  1.00 30.39           C  
ANISOU 4228  CD  GLU C  81     3986   3847   3712   -108   -121     79       C  
ATOM   4229  OE1 GLU C  81     -59.303  10.130  38.663  1.00 27.55           O  
ANISOU 4229  OE1 GLU C  81     3639   3470   3357   -107   -130     82       O  
ATOM   4230  OE2 GLU C  81     -60.007  10.542  40.707  1.00 35.02           O  
ANISOU 4230  OE2 GLU C  81     4568   4453   4285   -126   -126     86       O  
ATOM   4231  N   ASP C  82     -55.682  13.260  38.214  1.00 18.32           N  
ANISOU 4231  N   ASP C  82     2462   2270   2230    -48    -97     47       N  
ATOM   4232  CA  ASP C  82     -54.540  14.068  38.693  1.00 17.65           C  
ANISOU 4232  CA  ASP C  82     2374   2179   2153    -40    -91     39       C  
ATOM   4233  C   ASP C  82     -53.788  14.771  37.551  1.00 16.91           C  
ANISOU 4233  C   ASP C  82     2279   2076   2068    -28    -83     34       C  
ATOM   4234  O   ASP C  82     -52.793  15.473  37.787  1.00 17.64           O  
ANISOU 4234  O   ASP C  82     2370   2166   2168    -23    -79     29       O  
ATOM   4235  CB  ASP C  82     -53.574  13.186  39.503  1.00 17.50           C  
ANISOU 4235  CB  ASP C  82     2363   2155   2134    -44   -101     39       C  
ATOM   4236  CG  ASP C  82     -54.197  12.628  40.734  1.00 18.33           C  
ANISOU 4236  CG  ASP C  82     2467   2269   2227    -58   -108     45       C  
ATOM   4237  OD1 ASP C  82     -55.033  13.361  41.332  1.00 21.91           O  
ANISOU 4237  OD1 ASP C  82     2909   2739   2675    -62   -101     44       O  
ATOM   4238  OD2 ASP C  82     -53.848  11.466  41.117  1.00 19.40           O  
ANISOU 4238  OD2 ASP C  82     2615   2398   2360    -66   -123     50       O  
ATOM   4239  N   GLU C  83     -54.202  14.546  36.297  1.00 16.51           N  
ANISOU 4239  N   GLU C  83     2232   2024   2018    -24    -83     37       N  
ATOM   4240  CA  GLU C  83     -53.644  15.287  35.185  1.00 17.96           C  
ANISOU 4240  CA  GLU C  83     2412   2203   2208    -15    -76     35       C  
ATOM   4241  C   GLU C  83     -53.840  16.791  35.492  1.00 16.53           C  
ANISOU 4241  C   GLU C  83     2226   2023   2031    -13    -67     33       C  
ATOM   4242  O   GLU C  83     -54.962  17.248  35.647  1.00 19.79           O  
ANISOU 4242  O   GLU C  83     2636   2442   2441    -12    -64     33       O  
ATOM   4243  CB  GLU C  83     -54.348  14.867  33.880  1.00 17.61           C  
ANISOU 4243  CB  GLU C  83     2371   2160   2162    -12    -77     39       C  
ATOM   4244  CG  GLU C  83     -54.234  13.371  33.582  1.00 22.62           C  
ANISOU 4244  CG  GLU C  83     3013   2789   2792    -13    -90     40       C  
ATOM   4245  CD  GLU C  83     -55.375  12.791  32.726  1.00 26.60           C  
ANISOU 4245  CD  GLU C  83     3520   3296   3292    -15    -94     45       C  
ATOM   4246  OE1 GLU C  83     -55.468  11.533  32.555  1.00 22.19           O  
ANISOU 4246  OE1 GLU C  83     2970   2732   2729    -18   -108     46       O  
ATOM   4247  OE2 GLU C  83     -56.208  13.595  32.255  1.00 28.88           O  
ANISOU 4247  OE2 GLU C  83     3802   3591   3579    -14    -85     47       O  
ATOM   4248  N   ALA C  84     -52.731  17.518  35.609  1.00 15.51           N  
ANISOU 4248  N   ALA C  84     2096   1889   1908    -12    -63     29       N  
ATOM   4249  CA  ALA C  84     -52.747  18.884  36.116  1.00 14.50           C  
ANISOU 4249  CA  ALA C  84     1966   1758   1785    -11    -58     26       C  
ATOM   4250  C   ALA C  84     -51.333  19.443  36.055  1.00 15.05           C  
ANISOU 4250  C   ALA C  84     2036   1823   1860    -13    -56     24       C  
ATOM   4251  O   ALA C  84     -50.344  18.705  35.812  1.00 16.11           O  
ANISOU 4251  O   ALA C  84     2168   1960   1993    -14    -58     23       O  
ATOM   4252  CB  ALA C  84     -53.212  18.897  37.561  1.00 15.33           C  
ANISOU 4252  CB  ALA C  84     2068   1869   1886    -13    -60     21       C  
ATOM   4253  N   ASP C  85     -51.202  20.745  36.341  1.00 15.52           N  
ANISOU 4253  N   ASP C  85     2096   1876   1924    -14    -54     22       N  
ATOM   4254  CA  ASP C  85     -49.910  21.360  36.547  1.00 16.30           C  
ANISOU 4254  CA  ASP C  85     2195   1972   2028    -20    -53     20       C  
ATOM   4255  C   ASP C  85     -49.690  21.431  38.060  1.00 15.40           C  
ANISOU 4255  C   ASP C  85     2078   1858   1915    -21    -55     11       C  
ATOM   4256  O   ASP C  85     -50.650  21.626  38.827  1.00 17.10           O  
ANISOU 4256  O   ASP C  85     2294   2075   2129    -16    -57      7       O  
ATOM   4257  CB  ASP C  85     -49.878  22.733  35.905  1.00 16.76           C  
ANISOU 4257  CB  ASP C  85     2258   2019   2091    -23    -53     24       C  
ATOM   4258  CG  ASP C  85     -50.051  22.652  34.401  1.00 19.56           C  
ANISOU 4258  CG  ASP C  85     2614   2375   2443    -24    -51     33       C  
ATOM   4259  OD1 ASP C  85     -49.170  22.091  33.765  1.00 23.70           O  
ANISOU 4259  OD1 ASP C  85     3132   2908   2963    -28    -48     36       O  
ATOM   4260  OD2 ASP C  85     -51.100  23.109  33.890  1.00 26.86           O  
ANISOU 4260  OD2 ASP C  85     3544   3293   3368    -18    -52     37       O  
ATOM   4261  N   TYR C  86     -48.436  21.263  38.465  1.00 15.30           N  
ANISOU 4261  N   TYR C  86     2062   1848   1903    -26    -55      8       N  
ATOM   4262  CA  TYR C  86     -48.035  21.265  39.880  1.00 14.71           C  
ANISOU 4262  CA  TYR C  86     1984   1776   1828    -27    -57      0       C  
ATOM   4263  C   TYR C  86     -46.922  22.255  40.047  1.00 15.49           C  
ANISOU 4263  C   TYR C  86     2083   1871   1933    -34    -57     -3       C  
ATOM   4264  O   TYR C  86     -45.967  22.271  39.285  1.00 15.99           O  
ANISOU 4264  O   TYR C  86     2143   1937   1995    -41    -55      1       O  
ATOM   4265  CB  TYR C  86     -47.564  19.863  40.304  1.00 14.56           C  
ANISOU 4265  CB  TYR C  86     1962   1766   1803    -26    -60     -1       C  
ATOM   4266  CG  TYR C  86     -48.710  18.891  40.299  1.00 12.86           C  
ANISOU 4266  CG  TYR C  86     1750   1554   1583    -23    -64      3       C  
ATOM   4267  CD1 TYR C  86     -49.093  18.245  39.108  1.00 14.19           C  
ANISOU 4267  CD1 TYR C  86     1922   1722   1749    -20    -64      9       C  
ATOM   4268  CD2 TYR C  86     -49.525  18.735  41.405  1.00 14.60           C  
ANISOU 4268  CD2 TYR C  86     1970   1780   1800    -23    -66      1       C  
ATOM   4269  CE1 TYR C  86     -50.174  17.354  39.079  1.00 14.96           C  
ANISOU 4269  CE1 TYR C  86     2022   1821   1841    -20    -69     13       C  
ATOM   4270  CE2 TYR C  86     -50.625  17.840  41.391  1.00 13.74           C  
ANISOU 4270  CE2 TYR C  86     1862   1676   1683    -25    -70      7       C  
ATOM   4271  CZ  TYR C  86     -50.955  17.191  40.206  1.00 14.39           C  
ANISOU 4271  CZ  TYR C  86     1949   1755   1764    -24    -71     13       C  
ATOM   4272  OH  TYR C  86     -52.060  16.377  40.230  1.00 14.24           O  
ANISOU 4272  OH  TYR C  86     1931   1741   1737    -28    -76     19       O  
ATOM   4273  N   TYR C  87     -47.040  23.101  41.069  1.00 15.72           N  
ANISOU 4273  N   TYR C  87     2113   1894   1965    -34    -59    -10       N  
ATOM   4274  CA  TYR C  87     -46.061  24.170  41.297  1.00 13.87           C  
ANISOU 4274  CA  TYR C  87     1880   1653   1736    -43    -61    -13       C  
ATOM   4275  C   TYR C  87     -45.529  24.140  42.715  1.00 15.51           C  
ANISOU 4275  C   TYR C  87     2083   1865   1944    -43    -63    -23       C  
ATOM   4276  O   TYR C  87     -46.339  24.035  43.663  1.00 16.02           O  
ANISOU 4276  O   TYR C  87     2147   1933   2007    -35    -65    -30       O  
ATOM   4277  CB  TYR C  87     -46.705  25.551  41.114  1.00 15.16           C  
ANISOU 4277  CB  TYR C  87     2054   1799   1906    -43    -66    -13       C  
ATOM   4278  CG  TYR C  87     -47.163  25.776  39.709  1.00 14.47           C  
ANISOU 4278  CG  TYR C  87     1973   1706   1820    -44    -66     -2       C  
ATOM   4279  CD1 TYR C  87     -48.469  25.452  39.335  1.00 14.84           C  
ANISOU 4279  CD1 TYR C  87     2021   1753   1863    -32    -65      0       C  
ATOM   4280  CD2 TYR C  87     -46.312  26.359  38.787  1.00 16.05           C  
ANISOU 4280  CD2 TYR C  87     2177   1902   2021    -58    -66      8       C  
ATOM   4281  CE1 TYR C  87     -48.913  25.676  38.030  1.00 16.82           C  
ANISOU 4281  CE1 TYR C  87     2278   1998   2114    -32    -65     10       C  
ATOM   4282  CE2 TYR C  87     -46.740  26.563  37.483  1.00 16.50           C  
ANISOU 4282  CE2 TYR C  87     2238   1954   2077    -60    -66     19       C  
ATOM   4283  CZ  TYR C  87     -48.050  26.233  37.135  1.00 18.87           C  
ANISOU 4283  CZ  TYR C  87     2541   2253   2376    -46    -65     19       C  
ATOM   4284  OH  TYR C  87     -48.502  26.435  35.843  1.00 18.28           O  
ANISOU 4284  OH  TYR C  87     2471   2174   2299    -47    -65     30       O  
ATOM   4285  N   CYS C  88     -44.219  24.287  42.857  1.00 14.46           N  
ANISOU 4285  N   CYS C  88     1945   1736   1811    -53    -62    -25       N  
ATOM   4286  CA  CYS C  88     -43.679  24.514  44.198  1.00 14.75           C  
ANISOU 4286  CA  CYS C  88     1979   1777   1849    -54    -64    -35       C  
ATOM   4287  C   CYS C  88     -43.588  26.018  44.401  1.00 15.69           C  
ANISOU 4287  C   CYS C  88     2106   1880   1977    -60    -70    -39       C  
ATOM   4288  O   CYS C  88     -43.664  26.759  43.436  1.00 17.15           O  
ANISOU 4288  O   CYS C  88     2298   2053   2164    -67    -72    -31       O  
ATOM   4289  CB  CYS C  88     -42.352  23.851  44.361  1.00 16.64           C  
ANISOU 4289  CB  CYS C  88     2209   2030   2084    -59    -62    -38       C  
ATOM   4290  SG  CYS C  88     -41.068  24.358  43.175  1.00 20.93           S  
ANISOU 4290  SG  CYS C  88     2747   2578   2625    -75    -59    -31       S  
ATOM   4291  N   GLN C  89     -43.523  26.412  45.670  1.00 15.18           N  
ANISOU 4291  N   GLN C  89     2039   1814   1913    -57    -74    -51       N  
ATOM   4292  CA  GLN C  89     -43.440  27.819  46.068  1.00 16.06           C  
ANISOU 4292  CA  GLN C  89     2160   1909   2032    -61    -83    -58       C  
ATOM   4293  C   GLN C  89     -42.537  27.922  47.309  1.00 17.48           C  
ANISOU 4293  C   GLN C  89     2333   2097   2212    -64    -85    -69       C  
ATOM   4294  O   GLN C  89     -42.646  27.083  48.197  1.00 17.19           O  
ANISOU 4294  O   GLN C  89     2286   2075   2169    -55    -81    -75       O  
ATOM   4295  CB  GLN C  89     -44.839  28.351  46.398  1.00 16.05           C  
ANISOU 4295  CB  GLN C  89     2166   1899   2033    -44    -90    -65       C  
ATOM   4296  CG  GLN C  89     -44.848  29.902  46.606  1.00 15.77           C  
ANISOU 4296  CG  GLN C  89     2145   1841   2007    -45   -104    -73       C  
ATOM   4297  CD  GLN C  89     -46.052  30.418  47.411  1.00 15.89           C  
ANISOU 4297  CD  GLN C  89     2163   1854   2021    -23   -113    -89       C  
ATOM   4298  OE1 GLN C  89     -46.801  29.653  47.979  1.00 18.47           O  
ANISOU 4298  OE1 GLN C  89     2478   2200   2339    -10   -107    -94       O  
ATOM   4299  NE2 GLN C  89     -46.226  31.744  47.444  1.00 18.68           N  
ANISOU 4299  NE2 GLN C  89     2531   2184   2382    -19   -129    -97       N  
ATOM   4300  N   SER C  90     -41.693  28.970  47.343  1.00 17.18           N  
ANISOU 4300  N   SER C  90     2300   2047   2180    -78    -91    -71       N  
ATOM   4301  CA  SER C  90     -40.885  29.218  48.522  1.00 17.91           C  
ANISOU 4301  CA  SER C  90     2388   2145   2273    -82    -94    -83       C  
ATOM   4302  C   SER C  90     -40.617  30.706  48.691  1.00 19.21           C  
ANISOU 4302  C   SER C  90     2565   2287   2446    -92   -108    -88       C  
ATOM   4303  O   SER C  90     -40.570  31.433  47.730  1.00 20.21           O  
ANISOU 4303  O   SER C  90     2704   2398   2577   -104   -114    -77       O  
ATOM   4304  CB  SER C  90     -39.534  28.495  48.364  1.00 18.18           C  
ANISOU 4304  CB  SER C  90     2409   2199   2300    -95    -86    -78       C  
ATOM   4305  OG  SER C  90     -38.775  28.586  49.562  1.00 22.58           O  
ANISOU 4305  OG  SER C  90     2958   2764   2856    -96    -88    -90       O  
ATOM   4306  N   ARG C  91     -40.422  31.128  49.929  1.00 19.64           N  
ANISOU 4306  N   ARG C  91     2618   2341   2502    -87   -114   -103       N  
ATOM   4307  CA  ARG C  91     -39.803  32.443  50.143  1.00 20.47           C  
ANISOU 4307  CA  ARG C  91     2736   2427   2616   -101   -128   -108       C  
ATOM   4308  C   ARG C  91     -38.386  32.468  49.527  1.00 21.04           C  
ANISOU 4308  C   ARG C  91     2803   2506   2685   -130   -124    -96       C  
ATOM   4309  O   ARG C  91     -37.685  31.453  49.507  1.00 20.64           O  
ANISOU 4309  O   ARG C  91     2736   2482   2627   -133   -111    -93       O  
ATOM   4310  CB  ARG C  91     -39.739  32.750  51.623  1.00 20.09           C  
ANISOU 4310  CB  ARG C  91     2684   2382   2569    -90   -135   -128       C  
ATOM   4311  CG  ARG C  91     -39.306  34.209  51.873  1.00 23.55           C  
ANISOU 4311  CG  ARG C  91     3138   2793   3016   -102   -154   -136       C  
ATOM   4312  CD  ARG C  91     -40.242  34.859  52.868  1.00 33.38           C  
ANISOU 4312  CD  ARG C  91     4391   4028   4265    -77   -168   -157       C  
ATOM   4313  NE  ARG C  91     -39.958  34.591  54.277  1.00 37.90           N  
ANISOU 4313  NE  ARG C  91     4948   4619   4832    -67   -165   -175       N  
ATOM   4314  CZ  ARG C  91     -38.838  34.048  54.755  1.00 38.59           C  
ANISOU 4314  CZ  ARG C  91     5022   4726   4915    -80   -156   -174       C  
ATOM   4315  NH1 ARG C  91     -37.854  33.690  53.940  1.00 41.12           N  
ANISOU 4315  NH1 ARG C  91     5339   5052   5234   -104   -147   -157       N  
ATOM   4316  NH2 ARG C  91     -38.705  33.860  56.060  1.00 37.65           N  
ANISOU 4316  NH2 ARG C  91     4891   4623   4791    -69   -155   -191       N  
ATOM   4317  N   ASP C  92     -37.983  33.626  49.004  1.00 23.84           N  
ANISOU 4317  N   ASP C  92     3173   2839   3046   -151   -137    -89       N  
ATOM   4318  CA  ASP C  92     -36.610  33.876  48.531  1.00 26.63           C  
ANISOU 4318  CA  ASP C  92     3521   3201   3395   -183   -136    -78       C  
ATOM   4319  C   ASP C  92     -36.249  35.260  49.055  1.00 28.90           C  
ANISOU 4319  C   ASP C  92     3826   3463   3692   -199   -156    -84       C  
ATOM   4320  O   ASP C  92     -36.703  36.267  48.520  1.00 29.74           O  
ANISOU 4320  O   ASP C  92     3955   3539   3806   -206   -173    -77       O  
ATOM   4321  CB  ASP C  92     -36.514  33.870  47.001  1.00 26.85           C  
ANISOU 4321  CB  ASP C  92     3552   3230   3420   -201   -133    -56       C  
ATOM   4322  CG  ASP C  92     -35.079  33.998  46.494  1.00 29.05           C  
ANISOU 4322  CG  ASP C  92     3819   3528   3689   -235   -130    -45       C  
ATOM   4323  OD1 ASP C  92     -34.430  32.977  46.315  1.00 28.36           O  
ANISOU 4323  OD1 ASP C  92     3710   3474   3590   -234   -115    -44       O  
ATOM   4324  OD2 ASP C  92     -34.597  35.118  46.214  1.00 33.97           O  
ANISOU 4324  OD2 ASP C  92     4456   4135   4315   -263   -144    -36       O  
ATOM   4325  N   ILE C  93     -35.450  35.302  50.119  1.00 30.42           N  
ANISOU 4325  N   ILE C  93     4008   3666   3882   -203   -157    -97       N  
ATOM   4326  CA  ILE C  93     -35.161  36.549  50.867  1.00 31.85           C  
ANISOU 4326  CA  ILE C  93     4206   3823   4073   -213   -178   -108       C  
ATOM   4327  C   ILE C  93     -36.419  37.254  51.409  1.00 31.80           C  
ANISOU 4327  C   ILE C  93     4219   3786   4077   -186   -195   -123       C  
ATOM   4328  O   ILE C  93     -36.865  36.957  52.528  1.00 31.94           O  
ANISOU 4328  O   ILE C  93     4229   3813   4094   -160   -193   -143       O  
ATOM   4329  CB  ILE C  93     -34.282  37.587  50.081  1.00 32.58           C  
ANISOU 4329  CB  ILE C  93     4313   3901   4167   -254   -192    -91       C  
ATOM   4330  CG1 ILE C  93     -33.097  36.923  49.384  1.00 34.97           C  
ANISOU 4330  CG1 ILE C  93     4593   4239   4456   -281   -175    -75       C  
ATOM   4331  CG2 ILE C  93     -33.828  38.735  51.027  1.00 32.50           C  
ANISOU 4331  CG2 ILE C  93     4317   3868   4165   -266   -214   -104       C  
ATOM   4332  CD1 ILE C  93     -32.150  36.263  50.341  1.00 37.07           C  
ANISOU 4332  CD1 ILE C  93     4834   4538   4713   -279   -163    -88       C  
ATOM   4333  N   SER C  94     -36.963  38.191  50.621  1.00 32.48           N  
ANISOU 4333  N   SER C  94     4331   3839   4171   -192   -212   -114       N  
ATOM   4334  CA  SER C  94     -38.107  39.040  51.043  1.00 32.66           C  
ANISOU 4334  CA  SER C  94     4376   3831   4203   -165   -233   -130       C  
ATOM   4335  C   SER C  94     -39.298  39.001  50.084  1.00 31.71           C  
ANISOU 4335  C   SER C  94     4266   3697   4084   -149   -235   -122       C  
ATOM   4336  O   SER C  94     -40.208  39.843  50.170  1.00 33.04           O  
ANISOU 4336  O   SER C  94     4457   3837   4260   -130   -256   -133       O  
ATOM   4337  CB  SER C  94     -37.666  40.493  51.211  1.00 34.16           C  
ANISOU 4337  CB  SER C  94     4594   3983   4404   -184   -263   -134       C  
ATOM   4338  OG  SER C  94     -36.643  40.591  52.186  1.00 37.04           O  
ANISOU 4338  OG  SER C  94     4948   4359   4767   -197   -264   -144       O  
ATOM   4339  N   GLN C  95     -39.266  38.070  49.142  1.00 28.30           N  
ANISOU 4339  N   GLN C  95     3821   3286   3645   -156   -214   -103       N  
ATOM   4340  CA  GLN C  95     -40.390  37.864  48.229  1.00 25.82           C  
ANISOU 4340  CA  GLN C  95     3514   2965   3330   -140   -212    -95       C  
ATOM   4341  C   GLN C  95     -40.674  36.377  48.166  1.00 23.71           C  
ANISOU 4341  C   GLN C  95     3221   2735   3054   -126   -185    -93       C  
ATOM   4342  O   GLN C  95     -39.945  35.591  48.747  1.00 25.44           O  
ANISOU 4342  O   GLN C  95     3419   2980   3266   -131   -171    -96       O  
ATOM   4343  CB  GLN C  95     -40.098  38.414  46.834  1.00 26.60           C  
ANISOU 4343  CB  GLN C  95     3630   3046   3431   -169   -220    -70       C  
ATOM   4344  CG  GLN C  95     -38.843  37.808  46.210  1.00 25.81           C  
ANISOU 4344  CG  GLN C  95     3511   2973   3321   -202   -202    -51       C  
ATOM   4345  CD  GLN C  95     -38.592  38.264  44.780  1.00 30.60           C  
ANISOU 4345  CD  GLN C  95     4132   3570   3926   -231   -208    -24       C  
ATOM   4346  OE1 GLN C  95     -37.482  38.093  44.248  1.00 34.61           O  
ANISOU 4346  OE1 GLN C  95     4627   4097   4425   -263   -200     -9       O  
ATOM   4347  NE2 GLN C  95     -39.603  38.830  44.146  1.00 30.48           N  
ANISOU 4347  NE2 GLN C  95     4139   3526   3917   -220   -222    -19       N  
ATOM   4348  N   TYR C  96     -41.766  36.021  47.501  1.00 20.61           N  
ANISOU 4348  N   TYR C  96     2830   2341   2659   -109   -181    -88       N  
ATOM   4349  CA  TYR C  96     -42.129  34.625  47.333  1.00 18.79           C  
ANISOU 4349  CA  TYR C  96     2579   2142   2420    -97   -159    -85       C  
ATOM   4350  C   TYR C  96     -42.028  34.311  45.863  1.00 18.91           C  
ANISOU 4350  C   TYR C  96     2595   2158   2431   -112   -151    -62       C  
ATOM   4351  O   TYR C  96     -42.274  35.166  45.025  1.00 20.97           O  
ANISOU 4351  O   TYR C  96     2875   2395   2698   -121   -164    -52       O  
ATOM   4352  CB  TYR C  96     -43.544  34.407  47.889  1.00 16.91           C  
ANISOU 4352  CB  TYR C  96     2338   1907   2180    -64   -160   -100       C  
ATOM   4353  CG  TYR C  96     -43.497  34.260  49.407  1.00 17.80           C  
ANISOU 4353  CG  TYR C  96     2439   2034   2289    -50   -160   -121       C  
ATOM   4354  CD1 TYR C  96     -43.450  32.977  49.983  1.00 18.85           C  
ANISOU 4354  CD1 TYR C  96     2551   2199   2413    -44   -143   -123       C  
ATOM   4355  CD2 TYR C  96     -43.383  35.365  50.234  1.00 20.81           C  
ANISOU 4355  CD2 TYR C  96     2832   2397   2677    -45   -179   -138       C  
ATOM   4356  CE1 TYR C  96     -43.340  32.817  51.388  1.00 20.93           C  
ANISOU 4356  CE1 TYR C  96     2802   2479   2673    -34   -143   -140       C  
ATOM   4357  CE2 TYR C  96     -43.287  35.210  51.627  1.00 20.58           C  
ANISOU 4357  CE2 TYR C  96     2791   2385   2645    -32   -179   -158       C  
ATOM   4358  CZ  TYR C  96     -43.269  33.926  52.186  1.00 20.78           C  
ANISOU 4358  CZ  TYR C  96     2792   2444   2659    -27   -159   -158       C  
ATOM   4359  OH  TYR C  96     -43.169  33.743  53.552  1.00 23.20           O  
ANISOU 4359  OH  TYR C  96     3085   2769   2960    -17   -159   -175       O  
ATOM   4360  N   VAL C  97     -41.613  33.080  45.580  1.00 18.73           N  
ANISOU 4360  N   VAL C  97     2553   2164   2401   -116   -132    -55       N  
ATOM   4361  CA  VAL C  97     -41.363  32.651  44.190  1.00 19.09           C  
ANISOU 4361  CA  VAL C  97     2595   2218   2441   -130   -123    -35       C  
ATOM   4362  C   VAL C  97     -41.959  31.262  43.950  1.00 18.63           C  
ANISOU 4362  C   VAL C  97     2522   2182   2376   -112   -108    -35       C  
ATOM   4363  O   VAL C  97     -42.068  30.454  44.861  1.00 18.67           O  
ANISOU 4363  O   VAL C  97     2515   2202   2377    -98   -101    -46       O  
ATOM   4364  CB  VAL C  97     -39.862  32.633  43.865  1.00 19.73           C  
ANISOU 4364  CB  VAL C  97     2667   2314   2517   -159   -119    -26       C  
ATOM   4365  CG1 VAL C  97     -39.271  34.014  44.033  1.00 20.33           C  
ANISOU 4365  CG1 VAL C  97     2759   2367   2599   -181   -136    -24       C  
ATOM   4366  CG2 VAL C  97     -39.095  31.689  44.743  1.00 21.68           C  
ANISOU 4366  CG2 VAL C  97     2892   2587   2756   -155   -108    -36       C  
ATOM   4367  N   PHE C  98     -42.381  31.038  42.714  1.00 17.73           N  
ANISOU 4367  N   PHE C  98     2411   2067   2258   -114   -104    -21       N  
ATOM   4368  CA  PHE C  98     -42.921  29.755  42.269  1.00 18.02           C  
ANISOU 4368  CA  PHE C  98     2436   2122   2289   -100    -91    -18       C  
ATOM   4369  C   PHE C  98     -41.929  29.041  41.378  1.00 18.23           C  
ANISOU 4369  C   PHE C  98     2450   2169   2307   -115    -82     -7       C  
ATOM   4370  O   PHE C  98     -41.188  29.674  40.657  1.00 20.44           O  
ANISOU 4370  O   PHE C  98     2733   2448   2586   -136    -84      4       O  
ATOM   4371  CB  PHE C  98     -44.200  29.969  41.454  1.00 16.87           C  
ANISOU 4371  CB  PHE C  98     2301   1963   2145    -89    -95    -12       C  
ATOM   4372  CG  PHE C  98     -45.386  30.321  42.279  1.00 18.34           C  
ANISOU 4372  CG  PHE C  98     2494   2139   2335    -67   -102    -26       C  
ATOM   4373  CD1 PHE C  98     -46.092  29.356  42.987  1.00 18.59           C  
ANISOU 4373  CD1 PHE C  98     2515   2188   2362    -50    -95    -35       C  
ATOM   4374  CD2 PHE C  98     -45.783  31.637  42.357  1.00 19.77           C  
ANISOU 4374  CD2 PHE C  98     2694   2295   2524    -65   -118    -30       C  
ATOM   4375  CE1 PHE C  98     -47.186  29.680  43.770  1.00 19.62           C  
ANISOU 4375  CE1 PHE C  98     2647   2316   2492    -30   -101    -49       C  
ATOM   4376  CE2 PHE C  98     -46.921  31.986  43.121  1.00 21.93           C  
ANISOU 4376  CE2 PHE C  98     2972   2563   2799    -40   -126    -46       C  
ATOM   4377  CZ  PHE C  98     -47.614  31.006  43.839  1.00 22.78           C  
ANISOU 4377  CZ  PHE C  98     3063   2693   2899    -24   -117    -56       C  
ATOM   4378  N   GLY C  99     -41.954  27.703  41.370  1.00 17.74           N  
ANISOU 4378  N   GLY C  99     2374   2127   2238   -103    -72    -10       N  
ATOM   4379  CA  GLY C  99     -41.237  26.964  40.344  1.00 16.97           C  
ANISOU 4379  CA  GLY C  99     2266   2050   2131   -110    -64     -1       C  
ATOM   4380  C   GLY C  99     -41.957  27.151  39.043  1.00 16.41           C  
ANISOU 4380  C   GLY C  99     2202   1973   2060   -111    -64     11       C  
ATOM   4381  O   GLY C  99     -43.094  27.641  38.986  1.00 17.68           O  
ANISOU 4381  O   GLY C  99     2376   2114   2227   -102    -69     12       O  
ATOM   4382  N   GLY C 100     -41.288  26.750  37.975  1.00 16.62           N  
ANISOU 4382  N   GLY C 100     2219   2018   2078   -120    -59     19       N  
ATOM   4383  CA  GLY C 100     -41.832  26.919  36.623  1.00 17.17           C  
ANISOU 4383  CA  GLY C 100     2294   2085   2145   -123    -58     33       C  
ATOM   4384  C   GLY C 100     -43.037  26.041  36.308  1.00 17.58           C  
ANISOU 4384  C   GLY C 100     2347   2134   2197   -102    -55     31       C  
ATOM   4385  O   GLY C 100     -43.689  26.247  35.279  1.00 19.25           O  
ANISOU 4385  O   GLY C 100     2565   2341   2408   -101    -55     41       O  
ATOM   4386  N   GLY C 101     -43.280  25.007  37.133  1.00 17.54           N  
ANISOU 4386  N   GLY C 101     2337   2135   2191    -86    -53     20       N  
ATOM   4387  CA  GLY C 101     -44.422  24.108  36.983  1.00 16.34           C  
ANISOU 4387  CA  GLY C 101     2188   1982   2039    -68    -51     18       C  
ATOM   4388  C   GLY C 101     -44.084  22.805  36.287  1.00 14.80           C  
ANISOU 4388  C   GLY C 101     1982   1805   1835    -61    -48     18       C  
ATOM   4389  O   GLY C 101     -43.226  22.750  35.382  1.00 16.26           O  
ANISOU 4389  O   GLY C 101     2158   2005   2013    -69    -45     21       O  
ATOM   4390  N   THR C 102     -44.776  21.770  36.696  1.00 15.44           N  
ANISOU 4390  N   THR C 102     2064   1885   1916    -48    -49     13       N  
ATOM   4391  CA  THR C 102     -44.607  20.450  36.086  1.00 15.28           C  
ANISOU 4391  CA  THR C 102     2039   1879   1889    -38    -50     11       C  
ATOM   4392  C   THR C 102     -45.971  19.945  35.645  1.00 14.79           C  
ANISOU 4392  C   THR C 102     1985   1809   1827    -30    -51     15       C  
ATOM   4393  O   THR C 102     -46.886  19.842  36.447  1.00 16.45           O  
ANISOU 4393  O   THR C 102     2200   2009   2040    -26    -54     14       O  
ATOM   4394  CB  THR C 102     -43.912  19.436  37.081  1.00 14.58           C  
ANISOU 4394  CB  THR C 102     1946   1797   1796    -31    -55      0       C  
ATOM   4395  OG1 THR C 102     -42.572  19.853  37.361  1.00 14.33           O  
ANISOU 4395  OG1 THR C 102     1905   1777   1761    -39    -53     -5       O  
ATOM   4396  CG2 THR C 102     -43.926  18.003  36.515  1.00 16.61           C  
ANISOU 4396  CG2 THR C 102     2203   2062   2047    -18    -60     -3       C  
ATOM   4397  N   LYS C 103     -46.141  19.627  34.367  1.00 14.74           N  
ANISOU 4397  N   LYS C 103     1976   1808   1816    -27    -50     20       N  
ATOM   4398  CA  LYS C 103     -47.389  18.979  33.935  1.00 15.92           C  
ANISOU 4398  CA  LYS C 103     2132   1952   1965    -19    -52     23       C  
ATOM   4399  C   LYS C 103     -47.309  17.459  34.116  1.00 14.56           C  
ANISOU 4399  C   LYS C 103     1960   1785   1789     -9    -60     16       C  
ATOM   4400  O   LYS C 103     -46.344  16.833  33.632  1.00 16.57           O  
ANISOU 4400  O   LYS C 103     2209   2051   2037     -4    -63     11       O  
ATOM   4401  CB  LYS C 103     -47.674  19.249  32.429  1.00 16.92           C  
ANISOU 4401  CB  LYS C 103     2258   2083   2089    -19    -49     30       C  
ATOM   4402  CG  LYS C 103     -49.064  18.776  32.036  1.00 20.32           C  
ANISOU 4402  CG  LYS C 103     2694   2507   2519    -12    -51     33       C  
ATOM   4403  CD  LYS C 103     -49.390  19.075  30.580  1.00 28.43           C  
ANISOU 4403  CD  LYS C 103     3720   3539   3544    -11    -48     41       C  
ATOM   4404  CE  LYS C 103     -48.851  18.021  29.647  1.00 33.86           C  
ANISOU 4404  CE  LYS C 103     4401   4241   4224     -4    -50     37       C  
ATOM   4405  NZ  LYS C 103     -48.866  18.396  28.191  1.00 37.86           N  
ANISOU 4405  NZ  LYS C 103     4904   4758   4725     -5    -46     44       N  
ATOM   4406  N   LEU C 104     -48.307  16.889  34.787  1.00 15.31           N  
ANISOU 4406  N   LEU C 104     2062   1871   1884     -8    -65     17       N  
ATOM   4407  CA  LEU C 104     -48.377  15.444  34.938  1.00 14.70           C  
ANISOU 4407  CA  LEU C 104     1990   1794   1803     -1    -75     14       C  
ATOM   4408  C   LEU C 104     -49.179  14.878  33.768  1.00 15.24           C  
ANISOU 4408  C   LEU C 104     2062   1862   1868      3    -78     18       C  
ATOM   4409  O   LEU C 104     -50.338  15.251  33.592  1.00 15.82           O  
ANISOU 4409  O   LEU C 104     2137   1931   1943     -1    -74     24       O  
ATOM   4410  CB  LEU C 104     -49.055  15.048  36.259  1.00 15.01           C  
ANISOU 4410  CB  LEU C 104     2034   1826   1841     -6    -81     15       C  
ATOM   4411  CG  LEU C 104     -49.333  13.533  36.350  1.00 15.60           C  
ANISOU 4411  CG  LEU C 104     2119   1897   1911     -4    -95     15       C  
ATOM   4412  CD1 LEU C 104     -48.068  12.614  36.386  1.00 18.57           C  
ANISOU 4412  CD1 LEU C 104     2498   2273   2285      6   -107      6       C  
ATOM   4413  CD2 LEU C 104     -50.232  13.230  37.579  1.00 17.68           C  
ANISOU 4413  CD2 LEU C 104     2387   2158   2172    -14   -100     21       C  
ATOM   4414  N   THR C 105     -48.523  14.001  32.997  1.00 16.31           N  
ANISOU 4414  N   THR C 105     2196   2002   1999     13    -85     12       N  
ATOM   4415  CA  THR C 105     -49.196  13.201  31.973  1.00 15.79           C  
ANISOU 4415  CA  THR C 105     2135   1935   1930     19    -92     13       C  
ATOM   4416  C   THR C 105     -49.493  11.824  32.559  1.00 14.47           C  
ANISOU 4416  C   THR C 105     1980   1757   1760     21   -109     11       C  
ATOM   4417  O   THR C 105     -48.590  11.146  33.099  1.00 15.97           O  
ANISOU 4417  O   THR C 105     2174   1946   1949     28   -120      3       O  
ATOM   4418  CB  THR C 105     -48.301  13.046  30.749  1.00 16.49           C  
ANISOU 4418  CB  THR C 105     2215   2037   2013     30    -92      6       C  
ATOM   4419  OG1 THR C 105     -48.159  14.343  30.121  1.00 18.32           O  
ANISOU 4419  OG1 THR C 105     2437   2278   2245     23    -77     12       O  
ATOM   4420  CG2 THR C 105     -48.956  12.061  29.752  1.00 18.36           C  
ANISOU 4420  CG2 THR C 105     2458   2273   2246     39   -102      4       C  
ATOM   4421  N   VAL C 106     -50.747  11.403  32.420  1.00 14.01           N  
ANISOU 4421  N   VAL C 106     1929   1692   1701     15   -113     18       N  
ATOM   4422  CA  VAL C 106     -51.133  10.067  32.857  1.00 14.93           C  
ANISOU 4422  CA  VAL C 106     2060   1797   1814     13   -132     19       C  
ATOM   4423  C   VAL C 106     -50.951   9.075  31.730  1.00 14.19           C  
ANISOU 4423  C   VAL C 106     1973   1700   1718     26   -146     12       C  
ATOM   4424  O   VAL C 106     -51.434   9.282  30.618  1.00 15.76           O  
ANISOU 4424  O   VAL C 106     2168   1905   1917     30   -140     13       O  
ATOM   4425  CB  VAL C 106     -52.560  10.040  33.424  1.00 16.33           C  
ANISOU 4425  CB  VAL C 106     2243   1972   1991     -3   -132     30       C  
ATOM   4426  CG1 VAL C 106     -52.994   8.604  33.646  1.00 15.46           C  
ANISOU 4426  CG1 VAL C 106     2148   1849   1876     -9   -154     34       C  
ATOM   4427  CG2 VAL C 106     -52.592  10.801  34.765  1.00 18.10           C  
ANISOU 4427  CG2 VAL C 106     2461   2200   2216    -13   -123     34       C  
ATOM   4428  N   LEU C 106A    -50.147   8.045  31.993  1.00 13.93           N  
ANISOU 4428  N   LEU C 106A    1949   1660   1682     36   -164      2       N  
ATOM   4429  CA  LEU C 106A    -49.843   7.018  30.979  1.00 14.20           C  
ANISOU 4429  CA  LEU C 106A    1992   1691   1714     54   -182     -9       C  
ATOM   4430  C   LEU C 106A    -51.033   6.075  30.679  1.00 13.89           C  
ANISOU 4430  C   LEU C 106A    1968   1636   1672     46   -198     -2       C  
ATOM   4431  O   LEU C 106A    -51.788   5.719  31.561  1.00 14.62           O  
ANISOU 4431  O   LEU C 106A    2072   1717   1765     28   -205     10       O  
ATOM   4432  CB  LEU C 106A    -48.621   6.211  31.426  1.00 14.85           C  
ANISOU 4432  CB  LEU C 106A    2081   1769   1793     70   -200    -23       C  
ATOM   4433  CG  LEU C 106A    -47.283   6.938  31.607  1.00 16.28           C  
ANISOU 4433  CG  LEU C 106A    2245   1969   1973     80   -189    -33       C  
ATOM   4434  CD1 LEU C 106A    -46.273   5.920  32.201  1.00 16.12           C  
ANISOU 4434  CD1 LEU C 106A    2234   1941   1948     96   -212    -47       C  
ATOM   4435  CD2 LEU C 106A    -46.739   7.562  30.304  1.00 15.06           C  
ANISOU 4435  CD2 LEU C 106A    2071   1838   1814     92   -175    -41       C  
ATOM   4436  N   ARG C 108     -51.212   5.768  29.391  1.00 15.92           N  
ANISOU 4436  N   ARG C 108     2224   1896   1927     57   -202     -8       N  
ATOM   4437  CA  ARG C 108     -52.373   5.109  28.795  1.00 19.00           C  
ANISOU 4437  CA  ARG C 108     2625   2276   2316     50   -212     -2       C  
ATOM   4438  C   ARG C 108     -51.751   4.250  27.693  1.00 17.37           C  
ANISOU 4438  C   ARG C 108     2424   2070   2107     75   -230    -20       C  
ATOM   4439  O   ARG C 108     -50.704   4.596  27.192  1.00 16.76           O  
ANISOU 4439  O   ARG C 108     2332   2008   2026     94   -223    -33       O  
ATOM   4440  CB  ARG C 108     -53.093   6.242  27.998  1.00 21.03           C  
ANISOU 4440  CB  ARG C 108     2866   2552   2575     45   -187      5       C  
ATOM   4441  CG  ARG C 108     -54.476   6.459  28.215  1.00 25.51           C  
ANISOU 4441  CG  ARG C 108     3435   3117   3142     25   -181     20       C  
ATOM   4442  CD  ARG C 108     -55.019   6.795  26.909  1.00 19.87           C  
ANISOU 4442  CD  ARG C 108     2711   2413   2425     31   -172     19       C  
ATOM   4443  NE  ARG C 108     -55.223   5.548  26.179  1.00 16.57           N  
ANISOU 4443  NE  ARG C 108     2307   1984   2004     38   -194     12       N  
ATOM   4444  CZ  ARG C 108     -56.378   4.917  26.072  1.00 16.85           C  
ANISOU 4444  CZ  ARG C 108     2352   2012   2038     24   -205     20       C  
ATOM   4445  NH1 ARG C 108     -57.483   5.427  26.633  1.00 18.72           N  
ANISOU 4445  NH1 ARG C 108     2585   2254   2273      3   -194     34       N  
ATOM   4446  NH2 ARG C 108     -56.404   3.756  25.390  1.00 18.91           N  
ANISOU 4446  NH2 ARG C 108     2628   2261   2297     33   -229     12       N  
ATOM   4447  N   THR C 109     -52.420   3.188  27.249  1.00 17.15           N  
ANISOU 4447  N   THR C 109     2413   2025   2077     74   -252    -20       N  
ATOM   4448  CA  THR C 109     -51.969   2.536  26.012  1.00 17.88           C  
ANISOU 4448  CA  THR C 109     2506   2121   2165    100   -267    -39       C  
ATOM   4449  C   THR C 109     -52.254   3.399  24.771  1.00 17.15           C  
ANISOU 4449  C   THR C 109     2392   2053   2070    105   -244    -39       C  
ATOM   4450  O   THR C 109     -53.156   4.280  24.757  1.00 16.14           O  
ANISOU 4450  O   THR C 109     2256   1932   1945     86   -222    -23       O  
ATOM   4451  CB  THR C 109     -52.676   1.186  25.777  1.00 18.77           C  
ANISOU 4451  CB  THR C 109     2645   2208   2278     98   -299    -40       C  
ATOM   4452  OG1 THR C 109     -54.102   1.403  25.799  1.00 21.71           O  
ANISOU 4452  OG1 THR C 109     3020   2579   2652     71   -290    -21       O  
ATOM   4453  CG2 THR C 109     -52.261   0.139  26.809  1.00 21.28           C  
ANISOU 4453  CG2 THR C 109     2989   2500   2597     97   -329    -42       C  
ATOM   4454  N   VAL C 110     -51.461   3.168  23.733  1.00 16.72           N  
ANISOU 4454  N   VAL C 110     2330   2014   2011    131   -249    -58       N  
ATOM   4455  CA  VAL C 110     -51.706   3.828  22.463  1.00 17.93           C  
ANISOU 4455  CA  VAL C 110     2464   2189   2159    136   -231    -58       C  
ATOM   4456  C   VAL C 110     -53.154   3.663  21.983  1.00 16.83           C  
ANISOU 4456  C   VAL C 110     2332   2041   2022    122   -231    -47       C  
ATOM   4457  O   VAL C 110     -53.742   2.568  22.084  1.00 17.69           O  
ANISOU 4457  O   VAL C 110     2463   2128   2132    119   -256    -48       O  
ATOM   4458  CB  VAL C 110     -50.691   3.393  21.396  1.00 17.90           C  
ANISOU 4458  CB  VAL C 110     2450   2206   2145    167   -241    -82       C  
ATOM   4459  CG1 VAL C 110     -51.115   3.859  19.979  1.00 18.65           C  
ANISOU 4459  CG1 VAL C 110     2528   2324   2234    172   -227    -82       C  
ATOM   4460  CG2 VAL C 110     -49.316   3.927  21.762  1.00 20.77           C  
ANISOU 4460  CG2 VAL C 110     2796   2590   2504    177   -231    -91       C  
ATOM   4461  N   ALA C 111     -53.698   4.766  21.473  1.00 15.94           N  
ANISOU 4461  N   ALA C 111     2203   1944   1908    112   -206    -35       N  
ATOM   4462  CA  ALA C 111     -55.071   4.826  20.951  1.00 16.07           C  
ANISOU 4462  CA  ALA C 111     2222   1959   1926     99   -202    -24       C  
ATOM   4463  C   ALA C 111     -55.035   5.676  19.689  1.00 15.63           C  
ANISOU 4463  C   ALA C 111     2146   1928   1864    109   -183    -25       C  
ATOM   4464  O   ALA C 111     -54.596   6.822  19.726  1.00 15.99           O  
ANISOU 4464  O   ALA C 111     2176   1989   1910    106   -161    -19       O  
ATOM   4465  CB  ALA C 111     -56.022   5.421  21.971  1.00 16.40           C  
ANISOU 4465  CB  ALA C 111     2267   1993   1973     73   -190     -5       C  
ATOM   4466  N   ALA C 112     -55.446   5.098  18.565  1.00 16.60           N  
ANISOU 4466  N   ALA C 112     2269   2055   1982    119   -192    -33       N  
ATOM   4467  CA  ALA C 112     -55.453   5.814  17.305  1.00 17.12           C  
ANISOU 4467  CA  ALA C 112     2317   2147   2041    128   -176    -33       C  
ATOM   4468  C   ALA C 112     -56.612   6.840  17.249  1.00 17.25           C  
ANISOU 4468  C   ALA C 112     2328   2165   2061    109   -155    -14       C  
ATOM   4469  O   ALA C 112     -57.722   6.585  17.749  1.00 17.83           O  
ANISOU 4469  O   ALA C 112     2412   2224   2138     94   -160     -5       O  
ATOM   4470  CB  ALA C 112     -55.578   4.830  16.175  1.00 18.11           C  
ANISOU 4470  CB  ALA C 112     2445   2276   2160    146   -194    -49       C  
ATOM   4471  N   PRO C 113     -56.354   8.005  16.643  1.00 16.77           N  
ANISOU 4471  N   PRO C 113     2251   2126   1997    110   -135     -7       N  
ATOM   4472  CA  PRO C 113     -57.459   8.963  16.519  1.00 18.38           C  
ANISOU 4472  CA  PRO C 113     2451   2330   2202     97   -119      9       C  
ATOM   4473  C   PRO C 113     -58.478   8.504  15.497  1.00 18.14           C  
ANISOU 4473  C   PRO C 113     2422   2304   2167    101   -124      8       C  
ATOM   4474  O   PRO C 113     -58.101   7.834  14.513  1.00 19.46           O  
ANISOU 4474  O   PRO C 113     2585   2482   2328    117   -134     -5       O  
ATOM   4475  CB  PRO C 113     -56.774  10.220  15.950  1.00 16.93           C  
ANISOU 4475  CB  PRO C 113     2251   2166   2013     99   -101     16       C  
ATOM   4476  CG  PRO C 113     -55.541   9.749  15.274  1.00 19.37           C  
ANISOU 4476  CG  PRO C 113     2551   2494   2314    114   -107      2       C  
ATOM   4477  CD  PRO C 113     -55.110   8.468  15.983  1.00 17.01           C  
ANISOU 4477  CD  PRO C 113     2264   2180   2018    122   -127    -14       C  
ATOM   4478  N   SER C 114     -59.749   8.839  15.725  1.00 17.96           N  
ANISOU 4478  N   SER C 114     2402   2275   2146     88   -119     19       N  
ATOM   4479  CA ASER C 114     -60.704   8.857  14.631  0.50 18.89           C  
ANISOU 4479  CA ASER C 114     2516   2404   2259     92   -117     21       C  
ATOM   4480  CA BSER C 114     -60.719   8.864  14.639  0.50 18.52           C  
ANISOU 4480  CA BSER C 114     2469   2357   2212     91   -117     21       C  
ATOM   4481  C   SER C 114     -60.575  10.216  13.977  1.00 17.94           C  
ANISOU 4481  C   SER C 114     2382   2299   2136     94    -98     30       C  
ATOM   4482  O   SER C 114     -60.383  11.210  14.641  1.00 18.75           O  
ANISOU 4482  O   SER C 114     2484   2399   2242     87    -86     39       O  
ATOM   4483  CB ASER C 114     -62.126   8.595  15.117  0.50 18.91           C  
ANISOU 4483  CB ASER C 114     2525   2397   2263     77   -120     27       C  
ATOM   4484  CB BSER C 114     -62.155   8.622  15.125  0.50 18.48           C  
ANISOU 4484  CB BSER C 114     2470   2343   2208     77   -120     28       C  
ATOM   4485  OG ASER C 114     -62.201   7.342  15.778  0.50 22.32           O  
ANISOU 4485  OG ASER C 114     2971   2812   2697     70   -140     21       O  
ATOM   4486  OG BSER C 114     -62.549   9.535  16.142  0.50 19.35           O  
ANISOU 4486  OG BSER C 114     2580   2451   2323     65   -108     39       O  
ATOM   4487  N   VAL C 115     -60.620  10.223  12.641  1.00 16.31           N  
ANISOU 4487  N   VAL C 115     2166   2109   1920    105    -96     27       N  
ATOM   4488  CA  VAL C 115     -60.370  11.427  11.841  1.00 17.30           C  
ANISOU 4488  CA  VAL C 115     2281   2252   2040    108    -81     37       C  
ATOM   4489  C   VAL C 115     -61.603  11.873  11.036  1.00 17.08           C  
ANISOU 4489  C   VAL C 115     2251   2230   2008    108    -75     45       C  
ATOM   4490  O   VAL C 115     -62.299  11.060  10.425  1.00 18.39           O  
ANISOU 4490  O   VAL C 115     2416   2399   2170    113    -83     38       O  
ATOM   4491  CB  VAL C 115     -59.174  11.200  10.886  1.00 16.81           C  
ANISOU 4491  CB  VAL C 115     2206   2211   1968    120    -82     28       C  
ATOM   4492  CG1 VAL C 115     -58.810  12.504  10.168  1.00 18.83           C  
ANISOU 4492  CG1 VAL C 115     2452   2486   2218    116    -67     42       C  
ATOM   4493  CG2 VAL C 115     -57.975  10.671  11.715  1.00 18.52           C  
ANISOU 4493  CG2 VAL C 115     2426   2424   2188    122    -89     18       C  
ATOM   4494  N   PHE C 116     -61.846  13.176  11.066  1.00 17.04           N  
ANISOU 4494  N   PHE C 116     2243   2226   2004    103    -63     59       N  
ATOM   4495  CA  PHE C 116     -62.997  13.742  10.374  1.00 17.01           C  
ANISOU 4495  CA  PHE C 116     2239   2228   1996    105    -58     66       C  
ATOM   4496  C   PHE C 116     -62.584  15.027   9.737  1.00 17.26           C  
ANISOU 4496  C   PHE C 116     2267   2269   2024    105    -49     80       C  
ATOM   4497  O   PHE C 116     -61.850  15.809  10.314  1.00 18.80           O  
ANISOU 4497  O   PHE C 116     2464   2457   2223     98    -44     87       O  
ATOM   4498  CB  PHE C 116     -64.150  14.048  11.331  1.00 17.23           C  
ANISOU 4498  CB  PHE C 116     2273   2243   2029     99    -58     70       C  
ATOM   4499  CG  PHE C 116     -64.558  12.889  12.185  1.00 17.66           C  
ANISOU 4499  CG  PHE C 116     2333   2289   2088     92    -68     61       C  
ATOM   4500  CD1 PHE C 116     -65.630  12.074  11.798  1.00 17.99           C  
ANISOU 4500  CD1 PHE C 116     2375   2335   2125     92    -75     56       C  
ATOM   4501  CD2 PHE C 116     -63.883  12.593  13.385  1.00 15.77           C  
ANISOU 4501  CD2 PHE C 116     2100   2037   1857     84    -71     58       C  
ATOM   4502  CE1 PHE C 116     -66.029  10.977  12.589  1.00 18.86           C  
ANISOU 4502  CE1 PHE C 116     2492   2436   2237     82    -87     50       C  
ATOM   4503  CE2 PHE C 116     -64.274  11.491  14.167  1.00 15.60           C  
ANISOU 4503  CE2 PHE C 116     2085   2005   1836     76    -83     52       C  
ATOM   4504  CZ  PHE C 116     -65.358  10.708  13.778  1.00 18.42           C  
ANISOU 4504  CZ  PHE C 116     2443   2367   2189     73    -91     49       C  
ATOM   4505  N   ILE C 117     -63.032  15.221   8.505  1.00 17.56           N  
ANISOU 4505  N   ILE C 117     2299   2322   2053    112    -47     83       N  
ATOM   4506  CA  ILE C 117     -62.796  16.494   7.805  1.00 17.76           C  
ANISOU 4506  CA  ILE C 117     2322   2354   2071    110    -39     99       C  
ATOM   4507  C   ILE C 117     -64.122  17.224   7.597  1.00 16.75           C  
ANISOU 4507  C   ILE C 117     2199   2220   1943    114    -38    107       C  
ATOM   4508  O   ILE C 117     -65.144  16.583   7.314  1.00 17.92           O  
ANISOU 4508  O   ILE C 117     2346   2374   2090    121    -41     99       O  
ATOM   4509  CB  ILE C 117     -62.054  16.260   6.442  1.00 17.75           C  
ANISOU 4509  CB  ILE C 117     2308   2381   2057    114    -38     99       C  
ATOM   4510  CG1 ILE C 117     -61.640  17.622   5.819  1.00 16.28           C  
ANISOU 4510  CG1 ILE C 117     2121   2202   1863    106    -32    120       C  
ATOM   4511  CG2 ILE C 117     -62.887  15.351   5.478  1.00 18.60           C  
ANISOU 4511  CG2 ILE C 117     2409   2502   2157    127    -43     89       C  
ATOM   4512  CD1 ILE C 117     -60.439  17.455   4.793  1.00 19.60           C  
ANISOU 4512  CD1 ILE C 117     2525   2655   2267    104    -30    121       C  
ATOM   4513  N   PHE C 118     -64.111  18.550   7.740  1.00 16.57           N  
ANISOU 4513  N   PHE C 118     2184   2188   1922    110    -36    121       N  
ATOM   4514  CA  PHE C 118     -65.321  19.357   7.569  1.00 17.92           C  
ANISOU 4514  CA  PHE C 118     2362   2353   2092    117    -37    127       C  
ATOM   4515  C   PHE C 118     -65.055  20.464   6.542  1.00 18.29           C  
ANISOU 4515  C   PHE C 118     2413   2405   2132    115    -37    145       C  
ATOM   4516  O   PHE C 118     -64.188  21.313   6.756  1.00 18.51           O  
ANISOU 4516  O   PHE C 118     2447   2424   2161    104    -37    157       O  
ATOM   4517  CB  PHE C 118     -65.663  20.035   8.888  1.00 17.85           C  
ANISOU 4517  CB  PHE C 118     2364   2323   2094    115    -40    127       C  
ATOM   4518  CG  PHE C 118     -66.071  19.078   9.970  1.00 18.52           C  
ANISOU 4518  CG  PHE C 118     2447   2404   2185    114    -41    113       C  
ATOM   4519  CD1 PHE C 118     -67.380  18.590  10.015  1.00 18.66           C  
ANISOU 4519  CD1 PHE C 118     2460   2429   2199    121    -43    104       C  
ATOM   4520  CD2 PHE C 118     -65.183  18.741  10.976  1.00 18.71           C  
ANISOU 4520  CD2 PHE C 118     2472   2419   2217    105    -40    109       C  
ATOM   4521  CE1 PHE C 118     -67.780  17.706  11.014  1.00 21.90           C  
ANISOU 4521  CE1 PHE C 118     2869   2839   2613    116    -45     93       C  
ATOM   4522  CE2 PHE C 118     -65.585  17.878  12.020  1.00 21.01           C  
ANISOU 4522  CE2 PHE C 118     2763   2707   2513    102    -43     97       C  
ATOM   4523  CZ  PHE C 118     -66.888  17.368  12.028  1.00 20.65           C  
ANISOU 4523  CZ  PHE C 118     2714   2670   2463    106    -45     91       C  
ATOM   4524  N   PRO C 119     -65.795  20.476   5.426  1.00 18.88           N  
ANISOU 4524  N   PRO C 119     2483   2493   2197    125    -37    148       N  
ATOM   4525  CA  PRO C 119     -65.675  21.629   4.535  1.00 19.79           C  
ANISOU 4525  CA  PRO C 119     2605   2610   2304    122    -39    167       C  
ATOM   4526  C   PRO C 119     -66.198  22.928   5.167  1.00 19.85           C  
ANISOU 4526  C   PRO C 119     2631   2592   2318    125    -46    176       C  
ATOM   4527  O   PRO C 119     -66.936  22.883   6.160  1.00 20.19           O  
ANISOU 4527  O   PRO C 119     2678   2622   2370    133    -49    164       O  
ATOM   4528  CB  PRO C 119     -66.584  21.240   3.352  1.00 18.95           C  
ANISOU 4528  CB  PRO C 119     2491   2524   2187    135    -39    164       C  
ATOM   4529  CG  PRO C 119     -66.815  19.782   3.481  1.00 22.51           C  
ANISOU 4529  CG  PRO C 119     2928   2985   2638    140    -37    145       C  
ATOM   4530  CD  PRO C 119     -66.834  19.546   4.960  1.00 19.46           C  
ANISOU 4530  CD  PRO C 119     2549   2581   2266    136    -38    135       C  
ATOM   4531  N   PRO C 120     -65.816  24.100   4.612  1.00 20.04           N  
ANISOU 4531  N   PRO C 120     2667   2609   2338    117    -52    196       N  
ATOM   4532  CA  PRO C 120     -66.465  25.324   5.036  1.00 20.25           C  
ANISOU 4532  CA  PRO C 120     2714   2610   2370    125    -63    202       C  
ATOM   4533  C   PRO C 120     -67.971  25.215   4.822  1.00 21.36           C  
ANISOU 4533  C   PRO C 120     2854   2755   2508    147    -66    191       C  
ATOM   4534  O   PRO C 120     -68.428  24.704   3.791  1.00 22.17           O  
ANISOU 4534  O   PRO C 120     2946   2879   2601    154    -63    191       O  
ATOM   4535  CB  PRO C 120     -65.877  26.401   4.098  1.00 21.34           C  
ANISOU 4535  CB  PRO C 120     2863   2744   2499    112    -70    228       C  
ATOM   4536  CG  PRO C 120     -64.732  25.783   3.406  1.00 21.54           C  
ANISOU 4536  CG  PRO C 120     2872   2796   2515     94    -60    235       C  
ATOM   4537  CD  PRO C 120     -64.877  24.299   3.480  1.00 18.95           C  
ANISOU 4537  CD  PRO C 120     2523   2489   2187    103    -50    213       C  
ATOM   4538  N   SER C 121     -68.722  25.719   5.790  1.00 22.68           N  
ANISOU 4538  N   SER C 121     3031   2904   2683    160    -73    182       N  
ATOM   4539  CA  SER C 121     -70.174  25.807   5.699  1.00 23.11           C  
ANISOU 4539  CA  SER C 121     3085   2964   2733    183    -78    171       C  
ATOM   4540  C   SER C 121     -70.623  26.787   4.622  1.00 24.27           C  
ANISOU 4540  C   SER C 121     3244   3107   2871    193    -89    185       C  
ATOM   4541  O   SER C 121     -69.928  27.753   4.318  1.00 23.28           O  
ANISOU 4541  O   SER C 121     3136   2964   2746    183    -98    204       O  
ATOM   4542  CB  SER C 121     -70.758  26.254   7.051  1.00 24.02           C  
ANISOU 4542  CB  SER C 121     3206   3063   2856    195    -85    157       C  
ATOM   4543  OG  SER C 121     -70.324  27.570   7.355  1.00 24.28           O  
ANISOU 4543  OG  SER C 121     3263   3068   2896    194    -98    168       O  
ATOM   4544  N   ASP C 122     -71.806  26.547   4.083  1.00 25.73           N  
ANISOU 4544  N   ASP C 122     3422   3308   3048    212    -90    176       N  
ATOM   4545  CA  ASP C 122     -72.419  27.496   3.170  1.00 28.70           C  
ANISOU 4545  CA  ASP C 122     3810   3679   3415    226   -102    187       C  
ATOM   4546  C   ASP C 122     -72.552  28.875   3.825  1.00 29.07           C  
ANISOU 4546  C   ASP C 122     3883   3693   3468    237   -121    190       C  
ATOM   4547  O   ASP C 122     -72.353  29.908   3.179  1.00 29.70           O  
ANISOU 4547  O   ASP C 122     3983   3756   3545    236   -135    209       O  
ATOM   4548  CB  ASP C 122     -73.798  26.993   2.740  1.00 30.31           C  
ANISOU 4548  CB  ASP C 122     4000   3907   3609    248   -100    171       C  
ATOM   4549  CG  ASP C 122     -73.810  26.539   1.312  1.00 34.56           C  
ANISOU 4549  CG  ASP C 122     4528   4466   4135    245    -95    181       C  
ATOM   4550  OD1 ASP C 122     -73.499  25.353   1.049  1.00 38.73           O  
ANISOU 4550  OD1 ASP C 122     5037   5015   4661    234    -81    175       O  
ATOM   4551  OD2 ASP C 122     -74.112  27.389   0.446  1.00 40.89           O  
ANISOU 4551  OD2 ASP C 122     5343   5265   4930    255   -105    194       O  
ATOM   4552  N   GLU C 123     -72.864  28.872   5.125  1.00 28.65           N  
ANISOU 4552  N   GLU C 123     3829   3632   3423    245   -122    172       N  
ATOM   4553  CA  GLU C 123     -73.015  30.114   5.891  1.00 28.62           C  
ANISOU 4553  CA  GLU C 123     3849   3599   3426    259   -142    170       C  
ATOM   4554  C   GLU C 123     -71.705  30.870   5.960  1.00 27.61           C  
ANISOU 4554  C   GLU C 123     3742   3441   3306    236   -149    191       C  
ATOM   4555  O   GLU C 123     -71.676  32.084   5.793  1.00 28.71           O  
ANISOU 4555  O   GLU C 123     3909   3554   3447    241   -169    203       O  
ATOM   4556  CB  GLU C 123     -73.460  29.852   7.344  1.00 28.89           C  
ANISOU 4556  CB  GLU C 123     3875   3635   3466    270   -140    146       C  
ATOM   4557  CG  GLU C 123     -74.337  28.639   7.609  1.00 34.68           C  
ANISOU 4557  CG  GLU C 123     4580   4404   4193    276   -125    126       C  
ATOM   4558  CD  GLU C 123     -75.798  28.867   7.316  1.00 41.48           C  
ANISOU 4558  CD  GLU C 123     5435   5283   5042    306   -133    111       C  
ATOM   4559  OE1 GLU C 123     -76.630  28.643   8.229  1.00 45.10           O  
ANISOU 4559  OE1 GLU C 123     5881   5759   5498    320   -133     89       O  
ATOM   4560  OE2 GLU C 123     -76.109  29.254   6.170  1.00 43.73           O  
ANISOU 4560  OE2 GLU C 123     5728   5569   5320    315   -140    121       O  
ATOM   4561  N   GLN C 124     -70.605  30.163   6.242  1.00 25.66           N  
ANISOU 4561  N   GLN C 124     3484   3201   3065    209   -134    196       N  
ATOM   4562  CA  GLN C 124     -69.308  30.848   6.277  1.00 24.84           C  
ANISOU 4562  CA  GLN C 124     3397   3074   2966    184   -140    217       C  
ATOM   4563  C   GLN C 124     -68.964  31.381   4.891  1.00 25.10           C  
ANISOU 4563  C   GLN C 124     3440   3107   2989    172   -146    244       C  
ATOM   4564  O   GLN C 124     -68.538  32.528   4.736  1.00 24.81           O  
ANISOU 4564  O   GLN C 124     3429   3044   2953    162   -164    263       O  
ATOM   4565  CB  GLN C 124     -68.193  29.943   6.795  1.00 24.24           C  
ANISOU 4565  CB  GLN C 124     3305   3010   2896    160   -122    216       C  
ATOM   4566  CG  GLN C 124     -66.920  30.694   6.922  1.00 22.02           C  
ANISOU 4566  CG  GLN C 124     3039   2709   2620    134   -129    236       C  
ATOM   4567  CD  GLN C 124     -65.742  29.828   7.307  1.00 19.25           C  
ANISOU 4567  CD  GLN C 124     2671   2372   2271    111   -112    235       C  
ATOM   4568  OE1 GLN C 124     -65.770  28.602   7.211  1.00 20.81           O  
ANISOU 4568  OE1 GLN C 124     2845   2596   2466    112    -96    223       O  
ATOM   4569  NE2 GLN C 124     -64.678  30.478   7.725  1.00 19.59           N  
ANISOU 4569  NE2 GLN C 124     2726   2398   2320     90   -118    248       N  
ATOM   4570  N   LEU C 125     -69.179  30.553   3.886  1.00 26.19           N  
ANISOU 4570  N   LEU C 125     3559   3277   3116    172   -133    245       N  
ATOM   4571  CA  LEU C 125     -68.866  30.975   2.530  1.00 27.64           C  
ANISOU 4571  CA  LEU C 125     3748   3466   3286    160   -138    270       C  
ATOM   4572  C   LEU C 125     -69.632  32.233   2.176  1.00 29.15           C  
ANISOU 4572  C   LEU C 125     3968   3633   3476    177   -162    280       C  
ATOM   4573  O   LEU C 125     -69.055  33.147   1.589  1.00 30.47           O  
ANISOU 4573  O   LEU C 125     4156   3783   3638    159   -176    306       O  
ATOM   4574  CB  LEU C 125     -69.171  29.851   1.575  1.00 25.89           C  
ANISOU 4574  CB  LEU C 125     3500   3283   3054    163   -121    265       C  
ATOM   4575  CG  LEU C 125     -68.019  28.957   1.099  1.00 28.16           C  
ANISOU 4575  CG  LEU C 125     3766   3598   3335    139   -104    271       C  
ATOM   4576  CD1 LEU C 125     -66.549  29.237   1.536  1.00 26.32           C  
ANISOU 4576  CD1 LEU C 125     3537   3357   3105    109   -103    285       C  
ATOM   4577  CD2 LEU C 125     -68.353  27.504   1.159  1.00 26.33           C  
ANISOU 4577  CD2 LEU C 125     3508   3394   3103    148    -87    248       C  
ATOM   4578  N   LYS C 126     -70.901  32.312   2.586  1.00 31.77           N  
ANISOU 4578  N   LYS C 126     4302   3961   3810    210   -169    258       N  
ATOM   4579  CA  LYS C 126     -71.696  33.480   2.209  1.00 34.31           C  
ANISOU 4579  CA  LYS C 126     4650   4259   4128    231   -194    264       C  
ATOM   4580  C   LYS C 126     -71.187  34.703   2.941  1.00 34.96           C  
ANISOU 4580  C   LYS C 126     4766   4298   4221    225   -217    273       C  
ATOM   4581  O   LYS C 126     -71.157  35.805   2.377  1.00 36.63           O  
ANISOU 4581  O   LYS C 126     5007   4483   4428    224   -241    293       O  
ATOM   4582  CB  LYS C 126     -73.212  33.239   2.325  1.00 35.13           C  
ANISOU 4582  CB  LYS C 126     4744   4377   4227    270   -196    238       C  
ATOM   4583  CG  LYS C 126     -73.825  33.174   3.713  1.00 37.75           C  
ANISOU 4583  CG  LYS C 126     5072   4705   4568    291   -198    208       C  
ATOM   4584  CD  LYS C 126     -75.148  32.421   3.683  1.00 41.47           C  
ANISOU 4584  CD  LYS C 126     5519   5209   5030    318   -189    183       C  
ATOM   4585  CE  LYS C 126     -76.090  32.978   2.613  1.00 44.73           C  
ANISOU 4585  CE  LYS C 126     5941   5625   5430    342   -204    187       C  
ATOM   4586  NZ  LYS C 126     -76.803  31.893   1.892  1.00 46.06           N  
ANISOU 4586  NZ  LYS C 126     6080   5834   5587    347   -186    178       N  
ATOM   4587  N   SER C 127     -70.687  34.467   4.157  1.00 34.85           N  
ANISOU 4587  N   SER C 127     4747   4277   4219    218   -211    260       N  
ATOM   4588  CA ASER C 127     -70.169  35.524   5.026  0.50 35.30           C  
ANISOU 4588  CA ASER C 127     4832   4293   4287    213   -231    265       C  
ATOM   4589  CA BSER C 127     -70.178  35.536   5.017  0.50 34.69           C  
ANISOU 4589  CA BSER C 127     4755   4215   4209    213   -232    265       C  
ATOM   4590  C   SER C 127     -68.852  36.105   4.523  1.00 35.07           C  
ANISOU 4590  C   SER C 127     4821   4248   4258    173   -238    299       C  
ATOM   4591  O   SER C 127     -68.456  37.196   4.936  1.00 36.12           O  
ANISOU 4591  O   SER C 127     4985   4343   4398    166   -262    309       O  
ATOM   4592  CB ASER C 127     -70.014  35.002   6.462  0.50 34.92           C  
ANISOU 4592  CB ASER C 127     4770   4247   4251    216   -220    240       C  
ATOM   4593  CB BSER C 127     -70.031  35.036   6.456  0.50 34.19           C  
ANISOU 4593  CB BSER C 127     4678   4154   4158    217   -221    240       C  
ATOM   4594  OG ASER C 127     -71.260  34.577   6.986  0.50 36.03           O  
ANISOU 4594  OG ASER C 127     4896   4404   4390    251   -217    210       O  
ATOM   4595  OG BSER C 127     -68.780  34.401   6.622  0.50 31.46           O  
ANISOU 4595  OG BSER C 127     4319   3819   3816    182   -202    251       O  
ATOM   4596  N   GLY C 128     -68.166  35.374   3.636  1.00 34.30           N  
ANISOU 4596  N   GLY C 128     4702   4180   4149    147   -218    315       N  
ATOM   4597  CA  GLY C 128     -66.940  35.867   3.006  1.00 33.30           C  
ANISOU 4597  CA  GLY C 128     4586   4049   4017    107   -223    348       C  
ATOM   4598  C   GLY C 128     -65.587  35.208   3.246  1.00 33.10           C  
ANISOU 4598  C   GLY C 128     4540   4045   3992     72   -202    355       C  
ATOM   4599  O   GLY C 128     -64.576  35.697   2.753  1.00 33.32           O  
ANISOU 4599  O   GLY C 128     4576   4071   4012     38   -207    383       O  
ATOM   4600  N   THR C 129     -65.555  34.094   3.982  1.00 31.29           N  
ANISOU 4600  N   THR C 129     4283   3836   3768     81   -180    330       N  
ATOM   4601  CA  THR C 129     -64.294  33.405   4.341  1.00 30.00           C  
ANISOU 4601  CA  THR C 129     4100   3692   3606     53   -162    332       C  
ATOM   4602  C   THR C 129     -64.419  31.880   4.213  1.00 27.19           C  
ANISOU 4602  C   THR C 129     3708   3376   3247     62   -136    312       C  
ATOM   4603  O   THR C 129     -65.516  31.367   4.051  1.00 27.39           O  
ANISOU 4603  O   THR C 129     3725   3411   3271     89   -132    295       O  
ATOM   4604  CB  THR C 129     -63.898  33.722   5.805  1.00 30.31           C  
ANISOU 4604  CB  THR C 129     4150   3704   3663     51   -167    320       C  
ATOM   4605  OG1 THR C 129     -62.701  33.013   6.142  1.00 36.08           O  
ANISOU 4605  OG1 THR C 129     4860   4456   4393     26   -149    320       O  
ATOM   4606  CG2 THR C 129     -65.019  33.332   6.765  1.00 28.23           C  
ANISOU 4606  CG2 THR C 129     3882   3434   3409     87   -165    288       C  
ATOM   4607  N   ALA C 130     -63.293  31.163   4.280  1.00 25.98           N  
ANISOU 4607  N   ALA C 130     3534   3246   3090     40   -120    313       N  
ATOM   4608  CA  ALA C 130     -63.338  29.701   4.234  1.00 23.80           C  
ANISOU 4608  CA  ALA C 130     3227   3003   2812     50    -99    292       C  
ATOM   4609  C   ALA C 130     -62.379  29.016   5.208  1.00 22.90           C  
ANISOU 4609  C   ALA C 130     3100   2896   2706     38    -88    280       C  
ATOM   4610  O   ALA C 130     -61.170  29.174   5.138  1.00 24.19           O  
ANISOU 4610  O   ALA C 130     3260   3068   2865     13    -85    294       O  
ATOM   4611  CB  ALA C 130     -63.095  29.201   2.767  1.00 23.89           C  
ANISOU 4611  CB  ALA C 130     3220   3052   2804     42    -90    304       C  
ATOM   4612  N   SER C 131     -62.947  28.212   6.100  1.00 20.87           N  
ANISOU 4612  N   SER C 131     2835   2637   2460     57    -81    255       N  
ATOM   4613  CA  SER C 131     -62.143  27.459   7.025  1.00 19.99           C  
ANISOU 4613  CA  SER C 131     2710   2530   2355     49    -71    243       C  
ATOM   4614  C   SER C 131     -62.418  25.996   6.813  1.00 18.56           C  
ANISOU 4614  C   SER C 131     2506   2376   2170     61    -58    224       C  
ATOM   4615  O   SER C 131     -63.584  25.596   6.755  1.00 20.04           O  
ANISOU 4615  O   SER C 131     2691   2564   2358     81    -58    212       O  
ATOM   4616  CB  SER C 131     -62.579  27.799   8.441  1.00 19.62           C  
ANISOU 4616  CB  SER C 131     2677   2455   2324     59    -77    229       C  
ATOM   4617  OG  SER C 131     -62.358  29.175   8.730  1.00 20.31           O  
ANISOU 4617  OG  SER C 131     2788   2512   2415     51    -93    244       O  
ATOM   4618  N   VAL C 132     -61.356  25.216   6.734  1.00 17.63           N  
ANISOU 4618  N   VAL C 132     2371   2279   2047     50    -49    221       N  
ATOM   4619  CA  VAL C 132     -61.487  23.773   6.569  1.00 17.87           C  
ANISOU 4619  CA  VAL C 132     2382   2333   2075     61    -40    202       C  
ATOM   4620  C   VAL C 132     -60.964  23.138   7.869  1.00 17.31           C  
ANISOU 4620  C   VAL C 132     2308   2253   2015     59    -37    186       C  
ATOM   4621  O   VAL C 132     -59.856  23.446   8.287  1.00 18.77           O  
ANISOU 4621  O   VAL C 132     2493   2437   2202     44    -37    192       O  
ATOM   4622  CB  VAL C 132     -60.691  23.219   5.348  1.00 18.18           C  
ANISOU 4622  CB  VAL C 132     2402   2408   2097     55    -34    206       C  
ATOM   4623  CG1 VAL C 132     -61.144  21.794   5.048  1.00 18.57           C  
ANISOU 4623  CG1 VAL C 132     2435   2475   2144     72    -30    185       C  
ATOM   4624  CG2 VAL C 132     -60.897  24.095   4.099  1.00 20.40           C  
ANISOU 4624  CG2 VAL C 132     2687   2698   2365     49    -38    227       C  
ATOM   4625  N   VAL C 133     -61.738  22.227   8.470  1.00 17.18           N  
ANISOU 4625  N   VAL C 133     2288   2233   2006     73    -36    168       N  
ATOM   4626  CA  VAL C 133     -61.395  21.747   9.833  1.00 17.18           C  
ANISOU 4626  CA  VAL C 133     2289   2220   2017     71    -36    155       C  
ATOM   4627  C   VAL C 133     -61.146  20.262   9.749  1.00 17.16           C  
ANISOU 4627  C   VAL C 133     2272   2235   2012     76    -33    139       C  
ATOM   4628  O   VAL C 133     -61.950  19.520   9.200  1.00 18.35           O  
ANISOU 4628  O   VAL C 133     2418   2396   2160     87    -33    131       O  
ATOM   4629  CB  VAL C 133     -62.489  22.051  10.833  1.00 17.10           C  
ANISOU 4629  CB  VAL C 133     2290   2190   2017     80    -40    149       C  
ATOM   4630  CG1 VAL C 133     -62.105  21.571  12.245  1.00 18.67           C  
ANISOU 4630  CG1 VAL C 133     2489   2379   2227     76    -39    137       C  
ATOM   4631  CG2 VAL C 133     -62.749  23.560  10.885  1.00 17.94           C  
ANISOU 4631  CG2 VAL C 133     2413   2277   2127     79    -46    162       C  
ATOM   4632  N   CYS C 134     -60.028  19.813  10.309  1.00 18.42           N  
ANISOU 4632  N   CYS C 134     2427   2398   2174     69    -31    134       N  
ATOM   4633  CA  CYS C 134     -59.717  18.390  10.456  1.00 17.68           C  
ANISOU 4633  CA  CYS C 134     2324   2314   2080     75    -33    117       C  
ATOM   4634  C   CYS C 134     -59.687  18.096  11.964  1.00 17.92           C  
ANISOU 4634  C   CYS C 134     2361   2324   2122     73    -35    108       C  
ATOM   4635  O   CYS C 134     -59.005  18.792  12.754  1.00 19.57           O  
ANISOU 4635  O   CYS C 134     2575   2524   2338     63    -33    113       O  
ATOM   4636  CB  CYS C 134     -58.366  18.046   9.828  1.00 18.85           C  
ANISOU 4636  CB  CYS C 134     2459   2487   2217     72    -31    115       C  
ATOM   4637  SG  CYS C 134     -57.967  16.286   9.738  1.00 22.81           S  
ANISOU 4637  SG  CYS C 134     2949   3002   2715     86    -37     91       S  
ATOM   4638  N   LEU C 135     -60.421  17.055  12.341  1.00 15.48           N  
ANISOU 4638  N   LEU C 135     2053   2011   1817     80    -39     96       N  
ATOM   4639  CA  LEU C 135     -60.551  16.702  13.751  1.00 16.26           C  
ANISOU 4639  CA  LEU C 135     2158   2093   1925     76    -43     89       C  
ATOM   4640  C   LEU C 135     -59.907  15.328  13.945  1.00 16.55           C  
ANISOU 4640  C   LEU C 135     2193   2135   1962     78    -49     75       C  
ATOM   4641  O   LEU C 135     -60.222  14.384  13.203  1.00 17.17           O  
ANISOU 4641  O   LEU C 135     2267   2221   2034     86    -55     67       O  
ATOM   4642  CB  LEU C 135     -62.014  16.572  14.150  1.00 16.01           C  
ANISOU 4642  CB  LEU C 135     2132   2055   1896     79    -45     87       C  
ATOM   4643  CG  LEU C 135     -62.312  15.889  15.490  1.00 15.90           C  
ANISOU 4643  CG  LEU C 135     2123   2031   1889     73    -50     79       C  
ATOM   4644  CD1 LEU C 135     -61.745  16.644  16.720  1.00 18.05           C  
ANISOU 4644  CD1 LEU C 135     2400   2291   2169     66    -47     82       C  
ATOM   4645  CD2 LEU C 135     -63.818  15.595  15.730  1.00 18.67           C  
ANISOU 4645  CD2 LEU C 135     2473   2383   2237     74    -52     77       C  
ATOM   4646  N   LEU C 136     -59.018  15.228  14.948  1.00 17.21           N  
ANISOU 4646  N   LEU C 136     2279   2211   2051     73    -51     72       N  
ATOM   4647  CA  LEU C 136     -58.467  13.935  15.392  1.00 16.21           C  
ANISOU 4647  CA  LEU C 136     2152   2082   1925     76    -60     58       C  
ATOM   4648  C   LEU C 136     -59.029  13.713  16.787  1.00 15.58           C  
ANISOU 4648  C   LEU C 136     2082   1983   1854     69    -64     58       C  
ATOM   4649  O   LEU C 136     -58.721  14.476  17.687  1.00 17.37           O  
ANISOU 4649  O   LEU C 136     2311   2202   2086     62    -59     62       O  
ATOM   4650  CB  LEU C 136     -56.944  14.007  15.494  1.00 15.92           C  
ANISOU 4650  CB  LEU C 136     2109   2054   1886     76    -59     55       C  
ATOM   4651  CG  LEU C 136     -56.118  14.024  14.204  1.00 18.24           C  
ANISOU 4651  CG  LEU C 136     2389   2373   2167     83    -57     53       C  
ATOM   4652  CD1 LEU C 136     -56.419  15.233  13.303  1.00 21.40           C  
ANISOU 4652  CD1 LEU C 136     2785   2784   2562     78    -47     69       C  
ATOM   4653  CD2 LEU C 136     -54.635  13.960  14.589  1.00 20.34           C  
ANISOU 4653  CD2 LEU C 136     2647   2650   2430     83    -57     46       C  
ATOM   4654  N   ASN C 137     -59.860  12.679  16.955  1.00 15.97           N  
ANISOU 4654  N   ASN C 137     2137   2027   1903     69    -74     52       N  
ATOM   4655  CA  ASN C 137     -60.569  12.509  18.205  1.00 16.80           C  
ANISOU 4655  CA  ASN C 137     2249   2120   2013     58    -77     54       C  
ATOM   4656  C   ASN C 137     -60.033  11.390  19.068  1.00 16.78           C  
ANISOU 4656  C   ASN C 137     2254   2107   2013     55    -90     46       C  
ATOM   4657  O   ASN C 137     -59.886  10.261  18.596  1.00 16.99           O  
ANISOU 4657  O   ASN C 137     2286   2133   2038     60   -103     38       O  
ATOM   4658  CB  ASN C 137     -62.037  12.223  17.860  1.00 17.56           C  
ANISOU 4658  CB  ASN C 137     2346   2221   2106     56    -79     56       C  
ATOM   4659  CG  ASN C 137     -62.954  12.316  19.062  1.00 22.06           C  
ANISOU 4659  CG  ASN C 137     2918   2786   2676     44    -80     59       C  
ATOM   4660  OD1 ASN C 137     -63.133  13.383  19.635  1.00 27.34           O  
ANISOU 4660  OD1 ASN C 137     3584   3456   3347     43    -71     63       O  
ATOM   4661  ND2 ASN C 137     -63.563  11.207  19.411  1.00 25.97           N  
ANISOU 4661  ND2 ASN C 137     3419   3280   3169     35    -91     57       N  
ATOM   4662  N   ASN C 138     -59.806  11.718  20.345  1.00 15.60           N  
ANISOU 4662  N   ASN C 138     2109   1950   1870     46    -88     49       N  
ATOM   4663  CA  ASN C 138     -59.536  10.712  21.394  1.00 16.95           C  
ANISOU 4663  CA  ASN C 138     2289   2109   2043     39   -101     45       C  
ATOM   4664  C   ASN C 138     -58.346   9.772  21.153  1.00 16.33           C  
ANISOU 4664  C   ASN C 138     2215   2026   1965     49   -113     34       C  
ATOM   4665  O   ASN C 138     -58.506   8.535  21.065  1.00 18.03           O  
ANISOU 4665  O   ASN C 138     2440   2233   2178     50   -131     28       O  
ATOM   4666  CB  ASN C 138     -60.793   9.884  21.672  1.00 16.52           C  
ANISOU 4666  CB  ASN C 138     2240   2051   1985     27   -111     47       C  
ATOM   4667  CG  ASN C 138     -61.913  10.701  22.295  1.00 17.80           C  
ANISOU 4667  CG  ASN C 138     2397   2221   2144     17   -101     56       C  
ATOM   4668  OD1 ASN C 138     -61.780  11.897  22.562  1.00 18.48           O  
ANISOU 4668  OD1 ASN C 138     2477   2311   2233     21    -88     58       O  
ATOM   4669  ND2 ASN C 138     -63.045  10.068  22.480  1.00 24.87           N  
ANISOU 4669  ND2 ASN C 138     3295   3121   3035      6   -108     59       N  
ATOM   4670  N   PHE C 139     -57.162  10.342  21.082  1.00 16.83           N  
ANISOU 4670  N   PHE C 139     2271   2095   2028     56   -106     31       N  
ATOM   4671  CA  PHE C 139     -55.958   9.573  20.765  1.00 16.18           C  
ANISOU 4671  CA  PHE C 139     2188   2015   1943     69   -117     18       C  
ATOM   4672  C   PHE C 139     -54.881   9.661  21.823  1.00 16.86           C  
ANISOU 4672  C   PHE C 139     2275   2097   2033     68   -118     14       C  
ATOM   4673  O   PHE C 139     -54.931  10.515  22.742  1.00 15.70           O  
ANISOU 4673  O   PHE C 139     2127   1946   1891     57   -107     23       O  
ATOM   4674  CB  PHE C 139     -55.385   9.989  19.410  1.00 16.19           C  
ANISOU 4674  CB  PHE C 139     2176   2037   1937     82   -109     14       C  
ATOM   4675  CG  PHE C 139     -54.952  11.417  19.352  1.00 16.91           C  
ANISOU 4675  CG  PHE C 139     2256   2140   2029     76    -91     24       C  
ATOM   4676  CD1 PHE C 139     -55.869  12.403  19.008  1.00 15.75           C  
ANISOU 4676  CD1 PHE C 139     2108   1994   1884     68    -79     36       C  
ATOM   4677  CD2 PHE C 139     -53.632  11.791  19.595  1.00 16.41           C  
ANISOU 4677  CD2 PHE C 139     2185   2086   1964     77    -87     20       C  
ATOM   4678  CE1 PHE C 139     -55.492  13.744  18.936  1.00 14.87           C  
ANISOU 4678  CE1 PHE C 139     1990   1889   1772     62    -66     46       C  
ATOM   4679  CE2 PHE C 139     -53.240  13.128  19.532  1.00 17.33           C  
ANISOU 4679  CE2 PHE C 139     2294   2212   2080     68    -72     31       C  
ATOM   4680  CZ  PHE C 139     -54.174  14.108  19.176  1.00 17.42           C  
ANISOU 4680  CZ  PHE C 139     2305   2219   2093     60    -63     45       C  
ATOM   4681  N   TYR C 140     -53.926   8.736  21.747  1.00 15.56           N  
ANISOU 4681  N   TYR C 140     2114   1933   1866     81   -132      0       N  
ATOM   4682  CA  TYR C 140     -52.799   8.747  22.669  1.00 16.71           C  
ANISOU 4682  CA  TYR C 140     2259   2078   2013     83   -135     -5       C  
ATOM   4683  C   TYR C 140     -51.626   8.049  22.000  1.00 16.46           C  
ANISOU 4683  C   TYR C 140     2221   2059   1973    105   -146    -23       C  
ATOM   4684  O   TYR C 140     -51.801   6.989  21.454  1.00 16.33           O  
ANISOU 4684  O   TYR C 140     2213   2038   1953    117   -164    -34       O  
ATOM   4685  CB  TYR C 140     -53.159   8.060  24.005  1.00 15.66           C  
ANISOU 4685  CB  TYR C 140     2143   1922   1885     73   -148     -3       C  
ATOM   4686  CG  TYR C 140     -52.053   8.221  25.011  1.00 16.87           C  
ANISOU 4686  CG  TYR C 140     2295   2075   2041     74   -148     -7       C  
ATOM   4687  CD1 TYR C 140     -50.928   7.352  25.006  1.00 15.63           C  
ANISOU 4687  CD1 TYR C 140     2140   1919   1879     92   -164    -23       C  
ATOM   4688  CD2 TYR C 140     -52.076   9.302  25.922  1.00 18.06           C  
ANISOU 4688  CD2 TYR C 140     2441   2226   2197     60   -132      4       C  
ATOM   4689  CE1 TYR C 140     -49.849   7.564  25.926  1.00 14.29           C  
ANISOU 4689  CE1 TYR C 140     1967   1751   1710     94   -163    -28       C  
ATOM   4690  CE2 TYR C 140     -51.059   9.498  26.817  1.00 14.76           C  
ANISOU 4690  CE2 TYR C 140     2020   1808   1780     60   -131     -1       C  
ATOM   4691  CZ  TYR C 140     -49.944   8.651  26.816  1.00 17.54           C  
ANISOU 4691  CZ  TYR C 140     2374   2164   2128     76   -146    -16       C  
ATOM   4692  OH  TYR C 140     -48.892   8.835  27.695  1.00 20.05           O  
ANISOU 4692  OH  TYR C 140     2688   2484   2446     78   -145    -21       O  
ATOM   4693  N   PRO C 141     -50.415   8.604  22.078  1.00 17.49           N  
ANISOU 4693  N   PRO C 141     2338   2207   2099    109   -138    -29       N  
ATOM   4694  CA  PRO C 141     -50.007   9.806  22.785  1.00 18.56           C  
ANISOU 4694  CA  PRO C 141     2466   2347   2239     95   -120    -18       C  
ATOM   4695  C   PRO C 141     -50.351  11.085  22.025  1.00 18.04           C  
ANISOU 4695  C   PRO C 141     2388   2294   2171     84   -101     -4       C  
ATOM   4696  O   PRO C 141     -50.903  11.030  20.928  1.00 17.25           O  
ANISOU 4696  O   PRO C 141     2285   2203   2067     89    -99     -3       O  
ATOM   4697  CB  PRO C 141     -48.485   9.639  22.855  1.00 20.05           C  
ANISOU 4697  CB  PRO C 141     2643   2555   2420    107   -124    -33       C  
ATOM   4698  CG  PRO C 141     -48.118   8.903  21.718  1.00 20.89           C  
ANISOU 4698  CG  PRO C 141     2743   2680   2515    128   -134    -48       C  
ATOM   4699  CD  PRO C 141     -49.253   7.882  21.526  1.00 18.30           C  
ANISOU 4699  CD  PRO C 141     2434   2329   2192    132   -151    -49       C  
ATOM   4700  N   ARG C 142     -49.971  12.216  22.598  1.00 19.29           N  
ANISOU 4700  N   ARG C 142     2541   2454   2332     71    -87      5       N  
ATOM   4701  CA  ARG C 142     -50.346  13.530  22.109  1.00 20.30           C  
ANISOU 4701  CA  ARG C 142     2664   2588   2461     58    -72     20       C  
ATOM   4702  C   ARG C 142     -49.764  13.812  20.716  1.00 20.44           C  
ANISOU 4702  C   ARG C 142     2665   2633   2466     62    -67     20       C  
ATOM   4703  O   ARG C 142     -50.346  14.563  19.947  1.00 20.67           O  
ANISOU 4703  O   ARG C 142     2693   2666   2494     56    -59     32       O  
ATOM   4704  CB  ARG C 142     -49.876  14.578  23.124  1.00 22.62           C  
ANISOU 4704  CB  ARG C 142     2957   2876   2761     44    -63     27       C  
ATOM   4705  CG  ARG C 142     -50.385  15.970  22.901  1.00 25.30           C  
ANISOU 4705  CG  ARG C 142     3298   3211   3105     30    -52     43       C  
ATOM   4706  CD  ARG C 142     -49.893  16.891  24.043  1.00 32.38           C  
ANISOU 4706  CD  ARG C 142     4197   4098   4008     18    -48     48       C  
ATOM   4707  NE  ARG C 142     -48.985  17.916  23.536  1.00 39.24           N  
ANISOU 4707  NE  ARG C 142     5057   4982   4871      6    -41     55       N  
ATOM   4708  CZ  ARG C 142     -49.353  19.158  23.248  1.00 41.07           C  
ANISOU 4708  CZ  ARG C 142     5293   5206   5105     -6    -36     70       C  
ATOM   4709  NH1 ARG C 142     -48.466  20.028  22.783  1.00 43.84           N  
ANISOU 4709  NH1 ARG C 142     5637   5570   5449    -20    -32     78       N  
ATOM   4710  NH2 ARG C 142     -50.602  19.543  23.436  1.00 40.55           N  
ANISOU 4710  NH2 ARG C 142     5239   5120   5047     -4    -36     75       N  
ATOM   4711  N   GLU C 143     -48.611  13.214  20.415  1.00 20.12           N  
ANISOU 4711  N   GLU C 143     2614   2616   2415     74    -72      6       N  
ATOM   4712  CA  GLU C 143     -47.854  13.600  19.227  1.00 21.12           C  
ANISOU 4712  CA  GLU C 143     2721   2777   2527     75    -66      5       C  
ATOM   4713  C   GLU C 143     -48.476  13.054  17.973  1.00 20.56           C  
ANISOU 4713  C   GLU C 143     2648   2717   2449     87    -70      2       C  
ATOM   4714  O   GLU C 143     -48.715  11.854  17.853  1.00 21.92           O  
ANISOU 4714  O   GLU C 143     2825   2883   2620    106    -84    -14       O  
ATOM   4715  CB  GLU C 143     -46.392  13.194  19.347  1.00 22.72           C  
ANISOU 4715  CB  GLU C 143     2908   3007   2717     84    -71    -10       C  
ATOM   4716  CG  GLU C 143     -45.712  13.838  20.574  1.00 26.64           C  
ANISOU 4716  CG  GLU C 143     3406   3497   3221     70    -66     -6       C  
ATOM   4717  CD  GLU C 143     -46.069  13.185  21.901  1.00 30.31           C  
ANISOU 4717  CD  GLU C 143     3889   3929   3700     75    -75    -12       C  
ATOM   4718  OE1 GLU C 143     -46.131  13.909  22.930  1.00 31.44           O  
ANISOU 4718  OE1 GLU C 143     4039   4055   3852     60    -69     -2       O  
ATOM   4719  OE2 GLU C 143     -46.273  11.945  21.906  1.00 30.00           O  
ANISOU 4719  OE2 GLU C 143     3858   3882   3660     94    -90    -26       O  
ATOM   4720  N   ALA C 144     -48.782  13.958  17.056  1.00 19.58           N  
ANISOU 4720  N   ALA C 144     2516   2605   2318     77    -59     16       N  
ATOM   4721  CA  ALA C 144     -49.347  13.580  15.792  1.00 19.77           C  
ANISOU 4721  CA  ALA C 144     2535   2642   2334     87    -61     14       C  
ATOM   4722  C   ALA C 144     -48.893  14.580  14.750  1.00 20.10           C  
ANISOU 4722  C   ALA C 144     2561   2715   2362     75    -49     28       C  
ATOM   4723  O   ALA C 144     -48.610  15.735  15.086  1.00 21.30           O  
ANISOU 4723  O   ALA C 144     2713   2864   2516     54    -40     44       O  
ATOM   4724  CB  ALA C 144     -50.868  13.604  15.881  1.00 19.84           C  
ANISOU 4724  CB  ALA C 144     2562   2621   2356     85    -61     23       C  
ATOM   4725  N   LYS C 145     -48.878  14.159  13.503  1.00 21.77           N  
ANISOU 4725  N   LYS C 145     2759   2954   2559     87    -51     21       N  
ATOM   4726  CA  LYS C 145     -48.641  15.096  12.401  1.00 21.98           C  
ANISOU 4726  CA  LYS C 145     2771   3010   2570     73    -41     37       C  
ATOM   4727  C   LYS C 145     -49.884  15.146  11.495  1.00 21.91           C  
ANISOU 4727  C   LYS C 145     2768   2993   2562     77    -40     45       C  
ATOM   4728  O   LYS C 145     -50.441  14.127  11.110  1.00 21.26           O  
ANISOU 4728  O   LYS C 145     2689   2908   2480     97    -49     30       O  
ATOM   4729  CB  LYS C 145     -47.345  14.770  11.632  1.00 23.56           C  
ANISOU 4729  CB  LYS C 145     2943   3263   2746     80    -41     24       C  
ATOM   4730  CG  LYS C 145     -47.127  15.551  10.311  1.00 27.81           C  
ANISOU 4730  CG  LYS C 145     3463   3840   3264     67    -32     40       C  
ATOM   4731  CD  LYS C 145     -45.862  15.104   9.583  1.00 34.46           C  
ANISOU 4731  CD  LYS C 145     4275   4741   4079     76    -34     23       C  
ATOM   4732  CE  LYS C 145     -46.078  13.769   8.885  1.00 35.14           C  
ANISOU 4732  CE  LYS C 145     4353   4841   4157    111    -46     -4       C  
ATOM   4733  NZ  LYS C 145     -44.942  12.840   9.152  1.00 32.19           N  
ANISOU 4733  NZ  LYS C 145     3963   4496   3771    134    -56    -33       N  
ATOM   4734  N   VAL C 146     -50.352  16.358  11.245  1.00 21.85           N  
ANISOU 4734  N   VAL C 146     2767   2977   2557     57    -31     69       N  
ATOM   4735  CA  VAL C 146     -51.484  16.583  10.343  1.00 23.39           C  
ANISOU 4735  CA  VAL C 146     2968   3168   2751     59    -30     79       C  
ATOM   4736  C   VAL C 146     -51.004  17.438   9.174  1.00 23.61           C  
ANISOU 4736  C   VAL C 146     2981   3230   2761     45    -23     95       C  
ATOM   4737  O   VAL C 146     -50.558  18.569   9.365  1.00 25.32           O  
ANISOU 4737  O   VAL C 146     3199   3446   2976     21    -17    115       O  
ATOM   4738  CB  VAL C 146     -52.689  17.265  11.072  1.00 23.86           C  
ANISOU 4738  CB  VAL C 146     3051   3185   2831     51    -28     92       C  
ATOM   4739  CG1 VAL C 146     -53.898  17.272  10.190  1.00 25.99           C  
ANISOU 4739  CG1 VAL C 146     3325   3451   3100     58    -28     97       C  
ATOM   4740  CG2 VAL C 146     -52.999  16.534  12.350  1.00 25.65           C  
ANISOU 4740  CG2 VAL C 146     3290   3383   3074     59    -34     79       C  
ATOM   4741  N   GLN C 147     -51.083  16.872   7.977  1.00 23.60           N  
ANISOU 4741  N   GLN C 147     2965   3259   2744     58    -24     88       N  
ATOM   4742  CA  GLN C 147     -50.628  17.525   6.767  1.00 24.22           C  
ANISOU 4742  CA  GLN C 147     3026   3377   2800     45    -18    103       C  
ATOM   4743  C   GLN C 147     -51.844  17.815   5.890  1.00 23.45           C  
ANISOU 4743  C   GLN C 147     2937   3270   2703     48    -17    114       C  
ATOM   4744  O   GLN C 147     -52.653  16.906   5.595  1.00 23.11           O  
ANISOU 4744  O   GLN C 147     2897   3220   2665     70    -22     99       O  
ATOM   4745  CB  GLN C 147     -49.598  16.600   6.085  1.00 25.62           C  
ANISOU 4745  CB  GLN C 147     3175   3605   2955     61    -21     81       C  
ATOM   4746  CG  GLN C 147     -49.073  16.988   4.728  1.00 29.75           C  
ANISOU 4746  CG  GLN C 147     3674   4181   3450     52    -15     90       C  
ATOM   4747  CD  GLN C 147     -48.341  18.293   4.750  1.00 34.66           C  
ANISOU 4747  CD  GLN C 147     4290   4816   4061     17     -8    118       C  
ATOM   4748  OE1 GLN C 147     -48.730  19.246   4.062  1.00 38.36           O  
ANISOU 4748  OE1 GLN C 147     4764   5287   4524     -3     -4    144       O  
ATOM   4749  NE2 GLN C 147     -47.290  18.367   5.563  1.00 38.75           N  
ANISOU 4749  NE2 GLN C 147     4802   5343   4578      8     -7    113       N  
ATOM   4750  N   TRP C 148     -51.992  19.086   5.517  1.00 22.84           N  
ANISOU 4750  N   TRP C 148     2865   3190   2622     25    -12    142       N  
ATOM   4751  CA  TRP C 148     -53.017  19.510   4.553  1.00 22.04           C  
ANISOU 4751  CA  TRP C 148     2770   3086   2517     26    -12    156       C  
ATOM   4752  C   TRP C 148     -52.544  19.377   3.102  1.00 22.40           C  
ANISOU 4752  C   TRP C 148     2791   3183   2535     25     -9    159       C  
ATOM   4753  O   TRP C 148     -51.413  19.756   2.776  1.00 24.11           O  
ANISOU 4753  O   TRP C 148     2990   3436   2733      8     -6    167       O  
ATOM   4754  CB  TRP C 148     -53.448  20.953   4.813  1.00 21.88           C  
ANISOU 4754  CB  TRP C 148     2771   3035   2505      3    -12    184       C  
ATOM   4755  CG  TRP C 148     -54.339  21.088   6.037  1.00 19.86           C  
ANISOU 4755  CG  TRP C 148     2541   2730   2276     10    -16    180       C  
ATOM   4756  CD1 TRP C 148     -53.960  21.459   7.301  1.00 21.38           C  
ANISOU 4756  CD1 TRP C 148     2744   2897   2483      0    -17    180       C  
ATOM   4757  CD2 TRP C 148     -55.753  20.856   6.099  1.00 20.09           C  
ANISOU 4757  CD2 TRP C 148     2583   2732   2317     27    -18    175       C  
ATOM   4758  NE1 TRP C 148     -55.051  21.474   8.139  1.00 19.42           N  
ANISOU 4758  NE1 TRP C 148     2516   2610   2254     11    -20    175       N  
ATOM   4759  CE2 TRP C 148     -56.163  21.112   7.430  1.00 19.98           C  
ANISOU 4759  CE2 TRP C 148     2587   2680   2324     27    -21    172       C  
ATOM   4760  CE3 TRP C 148     -56.709  20.425   5.172  1.00 22.62           C  
ANISOU 4760  CE3 TRP C 148     2901   3061   2633     42    -19    171       C  
ATOM   4761  CZ2 TRP C 148     -57.483  20.973   7.846  1.00 19.92           C  
ANISOU 4761  CZ2 TRP C 148     2593   2646   2329     41    -24    166       C  
ATOM   4762  CZ3 TRP C 148     -58.040  20.291   5.598  1.00 21.07           C  
ANISOU 4762  CZ3 TRP C 148     2720   2836   2451     56    -22    165       C  
ATOM   4763  CH2 TRP C 148     -58.399  20.545   6.919  1.00 21.39           C  
ANISOU 4763  CH2 TRP C 148     2776   2843   2510     54    -25    162       C  
ATOM   4764  N   LYS C 149     -53.400  18.827   2.249  1.00 22.01           N  
ANISOU 4764  N   LYS C 149     2740   3141   2483     44    -11    151       N  
ATOM   4765  CA  LYS C 149     -53.132  18.785   0.809  1.00 22.70           C  
ANISOU 4765  CA  LYS C 149     2804   3276   2543     44     -8    155       C  
ATOM   4766  C   LYS C 149     -54.324  19.331   0.038  1.00 23.56           C  
ANISOU 4766  C   LYS C 149     2926   3373   2654     44     -9    172       C  
ATOM   4767  O   LYS C 149     -55.476  18.960   0.289  1.00 23.62           O  
ANISOU 4767  O   LYS C 149     2950   3349   2678     60    -12    163       O  
ATOM   4768  CB  LYS C 149     -52.846  17.348   0.346  1.00 23.50           C  
ANISOU 4768  CB  LYS C 149     2886   3410   2635     73    -12    122       C  
ATOM   4769  CG  LYS C 149     -51.697  16.640   1.059  1.00 25.06           C  
ANISOU 4769  CG  LYS C 149     3070   3622   2830     81    -15    100       C  
ATOM   4770  CD  LYS C 149     -51.769  15.143   0.793  1.00 32.21           C  
ANISOU 4770  CD  LYS C 149     3967   4540   3733    116    -25     65       C  
ATOM   4771  CE  LYS C 149     -50.445  14.426   1.099  1.00 35.79           C  
ANISOU 4771  CE  LYS C 149     4400   5025   4174    128    -30     41       C  
ATOM   4772  NZ  LYS C 149     -50.063  14.413   2.549  1.00 39.95           N  
ANISOU 4772  NZ  LYS C 149     4941   5517   4720    122    -32     38       N  
ATOM   4773  N   VAL C 150     -54.028  20.184  -0.930  1.00 22.78           N  
ANISOU 4773  N   VAL C 150     2819   3303   2534     24     -6    196       N  
ATOM   4774  CA  VAL C 150     -55.049  20.880  -1.674  1.00 23.72           C  
ANISOU 4774  CA  VAL C 150     2950   3410   2652     21     -7    216       C  
ATOM   4775  C   VAL C 150     -54.680  20.585  -3.128  1.00 24.65           C  
ANISOU 4775  C   VAL C 150     3041   3586   2740     23     -4    216       C  
ATOM   4776  O   VAL C 150     -53.574  20.955  -3.562  1.00 25.32           O  
ANISOU 4776  O   VAL C 150     3106   3712   2801      3     -1    228       O  
ATOM   4777  CB  VAL C 150     -55.007  22.396  -1.397  1.00 22.87           C  
ANISOU 4777  CB  VAL C 150     2863   3277   2548    -10     -9    250       C  
ATOM   4778  CG1 VAL C 150     -56.061  23.102  -2.213  1.00 24.34           C  
ANISOU 4778  CG1 VAL C 150     3064   3451   2731    -11    -13    270       C  
ATOM   4779  CG2 VAL C 150     -55.305  22.678   0.081  1.00 24.64           C  
ANISOU 4779  CG2 VAL C 150     3114   3449   2801    -10    -13    246       C  
ATOM   4780  N   ASP C 151     -55.557  19.867  -3.826  1.00 25.96           N  
ANISOU 4780  N   ASP C 151     3203   3757   2904     48     -5    201       N  
ATOM   4781  CA  ASP C 151     -55.259  19.343  -5.177  1.00 26.99           C  
ANISOU 4781  CA  ASP C 151     3305   3945   3007     57     -3    194       C  
ATOM   4782  C   ASP C 151     -53.971  18.507  -5.152  1.00 27.08           C  
ANISOU 4782  C   ASP C 151     3287   4000   3002     65     -3    170       C  
ATOM   4783  O   ASP C 151     -53.148  18.577  -6.081  1.00 26.76           O  
ANISOU 4783  O   ASP C 151     3219   4018   2931     57      1    174       O  
ATOM   4784  CB  ASP C 151     -55.126  20.489  -6.202  1.00 28.13           C  
ANISOU 4784  CB  ASP C 151     3444   4115   3128     31     -1    228       C  
ATOM   4785  CG  ASP C 151     -56.476  21.137  -6.565  1.00 29.23           C  
ANISOU 4785  CG  ASP C 151     3608   4221   3278     32     -4    246       C  
ATOM   4786  OD1 ASP C 151     -57.523  20.517  -6.289  1.00 29.23           O  
ANISOU 4786  OD1 ASP C 151     3620   4191   3297     57     -7    228       O  
ATOM   4787  OD2 ASP C 151     -56.460  22.262  -7.143  1.00 32.13           O  
ANISOU 4787  OD2 ASP C 151     3982   4594   3633      7     -6    279       O  
ATOM   4788  N   ASN C 152     -53.790  17.752  -4.068  1.00 27.59           N  
ANISOU 4788  N   ASN C 152     3358   4038   3085     79     -6    147       N  
ATOM   4789  CA  ASN C 152     -52.602  16.932  -3.822  1.00 28.61           C  
ANISOU 4789  CA  ASN C 152     3465   4201   3203     90     -8    121       C  
ATOM   4790  C   ASN C 152     -51.313  17.750  -3.632  1.00 28.60           C  
ANISOU 4790  C   ASN C 152     3450   4231   3186     60     -2    139       C  
ATOM   4791  O   ASN C 152     -50.215  17.194  -3.717  1.00 30.29           O  
ANISOU 4791  O   ASN C 152     3637   4489   3381     68     -3    120       O  
ATOM   4792  CB  ASN C 152     -52.433  15.858  -4.923  1.00 30.01           C  
ANISOU 4792  CB  ASN C 152     3616   4429   3359    119    -12     94       C  
ATOM   4793  CG  ASN C 152     -51.827  14.578  -4.396  1.00 31.20           C  
ANISOU 4793  CG  ASN C 152     3757   4586   3512    147    -22     55       C  
ATOM   4794  OD1 ASN C 152     -51.220  13.813  -5.149  1.00 35.25           O  
ANISOU 4794  OD1 ASN C 152     4243   5149   4003    169    -27     31       O  
ATOM   4795  ND2 ASN C 152     -51.961  14.347  -3.088  1.00 32.07           N  
ANISOU 4795  ND2 ASN C 152     3890   4646   3650    149    -26     49       N  
ATOM   4796  N   ALA C 153     -51.445  19.058  -3.383  1.00 27.79           N  
ANISOU 4796  N   ALA C 153     3365   4105   3089     27      2    174       N  
ATOM   4797  CA  ALA C 153     -50.280  19.918  -3.090  1.00 26.75           C  
ANISOU 4797  CA  ALA C 153     3224   3995   2944     -6      6    195       C  
ATOM   4798  C   ALA C 153     -50.175  20.154  -1.581  1.00 27.08           C  
ANISOU 4798  C   ALA C 153     3289   3985   3014    -13      4    194       C  
ATOM   4799  O   ALA C 153     -51.124  20.655  -0.964  0.50 24.35           O  
ANISOU 4799  O   ALA C 153     2975   3583   2694    -16      1    206       O  
ATOM   4800  CB  ALA C 153     -50.375  21.232  -3.806  1.00 27.04           C  
ANISOU 4800  CB  ALA C 153     3267   4040   2967    -42      8    235       C  
ATOM   4801  N   LEU C 154     -49.038  19.765  -1.007  1.00 28.00           N  
ANISOU 4801  N   LEU C 154     3390   4125   3124    -14      5    179       N  
ATOM   4802  CA  LEU C 154     -48.780  19.957   0.424  1.00 28.96           C  
ANISOU 4802  CA  LEU C 154     3529   4205   3268    -21      3    177       C  
ATOM   4803  C   LEU C 154     -48.817  21.441   0.789  1.00 29.25           C  
ANISOU 4803  C   LEU C 154     3588   4214   3313    -60      4    214       C  
ATOM   4804  O   LEU C 154     -48.171  22.272   0.139  1.00 30.20           O  
ANISOU 4804  O   LEU C 154     3696   4368   3410    -91      6    239       O  
ATOM   4805  CB  LEU C 154     -47.435  19.315   0.834  1.00 29.59           C  
ANISOU 4805  CB  LEU C 154     3584   4325   3336    -15      4    155       C  
ATOM   4806  CG  LEU C 154     -47.260  17.804   0.584  1.00 33.07           C  
ANISOU 4806  CG  LEU C 154     4005   4791   3769     26     -1    114       C  
ATOM   4807  CD1 LEU C 154     -45.786  17.406   0.693  1.00 36.24           C  
ANISOU 4807  CD1 LEU C 154     4375   5246   4147     28     -1     96       C  
ATOM   4808  CD2 LEU C 154     -48.077  16.971   1.537  1.00 36.84           C  
ANISOU 4808  CD2 LEU C 154     4508   5211   4278     53     -9     93       C  
ATOM   4809  N   GLN C 155     -49.588  21.766   1.819  1.00 29.11           N  
ANISOU 4809  N   GLN C 155     3602   4134   3326    -58      1    217       N  
ATOM   4810  CA  GLN C 155     -49.733  23.130   2.314  1.00 29.55           C  
ANISOU 4810  CA  GLN C 155     3682   4152   3391    -88     -3    248       C  
ATOM   4811  C   GLN C 155     -48.779  23.363   3.478  1.00 30.85           C  
ANISOU 4811  C   GLN C 155     3848   4308   3563   -104     -2    246       C  
ATOM   4812  O   GLN C 155     -48.379  22.407   4.166  1.00 31.76           O  
ANISOU 4812  O   GLN C 155     3954   4428   3685    -84     -1    218       O  
ATOM   4813  CB  GLN C 155     -51.174  23.379   2.799  1.00 29.25           C  
ANISOU 4813  CB  GLN C 155     3678   4054   3382    -74     -8    250       C  
ATOM   4814  CG  GLN C 155     -52.232  23.111   1.780  1.00 28.71           C  
ANISOU 4814  CG  GLN C 155     3610   3989   3309    -56     -8    249       C  
ATOM   4815  CD  GLN C 155     -52.111  24.031   0.585  1.00 28.90           C  
ANISOU 4815  CD  GLN C 155     3630   4039   3311    -81     -9    280       C  
ATOM   4816  OE1 GLN C 155     -52.327  25.241   0.683  1.00 27.74           O  
ANISOU 4816  OE1 GLN C 155     3507   3865   3170   -104    -16    307       O  
ATOM   4817  NE2 GLN C 155     -51.785  23.451  -0.563  1.00 28.67           N  
ANISOU 4817  NE2 GLN C 155     3574   4063   3257    -75     -5    274       N  
ATOM   4818  N   SER C 156     -48.443  24.635   3.689  1.00 31.57           N  
ANISOU 4818  N   SER C 156     3955   4387   3655   -139     -6    275       N  
ATOM   4819  CA  SER C 156     -47.572  25.070   4.766  1.00 32.82           C  
ANISOU 4819  CA  SER C 156     4116   4533   3819   -159     -7    277       C  
ATOM   4820  C   SER C 156     -47.923  26.531   5.048  1.00 32.20           C  
ANISOU 4820  C   SER C 156     4070   4411   3752   -189    -17    309       C  
ATOM   4821  O   SER C 156     -48.204  27.273   4.127  1.00 33.18           O  
ANISOU 4821  O   SER C 156     4201   4541   3865   -207    -21    335       O  
ATOM   4822  CB  SER C 156     -46.097  24.931   4.332  1.00 33.90           C  
ANISOU 4822  CB  SER C 156     4218   4736   3926   -179     -2    278       C  
ATOM   4823  OG  SER C 156     -45.332  25.993   4.867  1.00 38.04           O  
ANISOU 4823  OG  SER C 156     4751   5254   4449   -218     -5    301       O  
ATOM   4824  N   GLY C 157     -47.951  26.931   6.318  1.00 31.46           N  
ANISOU 4824  N   GLY C 157     3998   4274   3682   -192    -21    307       N  
ATOM   4825  CA  GLY C 157     -48.141  28.351   6.668  1.00 30.91           C  
ANISOU 4825  CA  GLY C 157     3960   4162   3622   -220    -34    335       C  
ATOM   4826  C   GLY C 157     -49.578  28.845   6.783  1.00 29.97           C  
ANISOU 4826  C   GLY C 157     3874   3989   3524   -203    -43    339       C  
ATOM   4827  O   GLY C 157     -49.824  29.966   7.221  1.00 31.30           O  
ANISOU 4827  O   GLY C 157     4071   4116   3704   -219    -57    357       O  
ATOM   4828  N   ASN C 158     -50.548  28.019   6.402  1.00 28.47           N  
ANISOU 4828  N   ASN C 158     3679   3798   3338   -169    -38    322       N  
ATOM   4829  CA  ASN C 158     -51.953  28.471   6.384  1.00 26.90           C  
ANISOU 4829  CA  ASN C 158     3509   3556   3156   -152    -47    326       C  
ATOM   4830  C   ASN C 158     -52.892  27.638   7.270  1.00 26.10           C  
ANISOU 4830  C   ASN C 158     3412   3428   3076   -115    -44    297       C  
ATOM   4831  O   ASN C 158     -54.111  27.654   7.078  1.00 26.54           O  
ANISOU 4831  O   ASN C 158     3480   3462   3140    -95    -48    294       O  
ATOM   4832  CB  ASN C 158     -52.521  28.582   4.941  1.00 26.79           C  
ANISOU 4832  CB  ASN C 158     3491   3562   3125   -151    -48    341       C  
ATOM   4833  CG  ASN C 158     -52.311  27.308   4.087  1.00 28.37           C  
ANISOU 4833  CG  ASN C 158     3657   3814   3308   -134    -35    324       C  
ATOM   4834  OD1 ASN C 158     -52.598  27.309   2.874  1.00 28.91           O  
ANISOU 4834  OD1 ASN C 158     3718   3908   3360   -134    -34    334       O  
ATOM   4835  ND2 ASN C 158     -51.802  26.253   4.684  1.00 27.70           N  
ANISOU 4835  ND2 ASN C 158     3554   3745   3226   -119    -26    297       N  
ATOM   4836  N   SER C 159     -52.328  26.898   8.222  1.00 24.86           N  
ANISOU 4836  N   SER C 159     3243   3275   2926   -108    -37    276       N  
ATOM   4837  CA  SER C 159     -53.189  26.174   9.162  1.00 23.80           C  
ANISOU 4837  CA  SER C 159     3116   3115   2812    -79    -36    252       C  
ATOM   4838  C   SER C 159     -52.805  26.428  10.617  1.00 23.88           C  
ANISOU 4838  C   SER C 159     3137   3099   2839    -84    -38    244       C  
ATOM   4839  O   SER C 159     -51.680  26.820  10.883  1.00 24.33           O  
ANISOU 4839  O   SER C 159     3189   3165   2890   -107    -39    252       O  
ATOM   4840  CB  SER C 159     -53.170  24.671   8.863  1.00 24.23           C  
ANISOU 4840  CB  SER C 159     3147   3199   2860    -57    -26    228       C  
ATOM   4841  OG  SER C 159     -51.852  24.182   8.855  1.00 26.10           O  
ANISOU 4841  OG  SER C 159     3361   3471   3085    -67    -21    222       O  
ATOM   4842  N   GLN C 160     -53.734  26.231  11.556  1.00 23.67           N  
ANISOU 4842  N   GLN C 160     3123   3041   2831    -63    -41    229       N  
ATOM   4843  CA  GLN C 160     -53.396  26.344  13.000  1.00 23.63           C  
ANISOU 4843  CA  GLN C 160     3125   3013   2840    -65    -43    220       C  
ATOM   4844  C   GLN C 160     -53.990  25.142  13.726  1.00 23.37           C  
ANISOU 4844  C   GLN C 160     3086   2977   2816    -40    -38    195       C  
ATOM   4845  O   GLN C 160     -55.092  24.704  13.390  1.00 22.83           O  
ANISOU 4845  O   GLN C 160     3019   2905   2750    -21    -37    188       O  
ATOM   4846  CB  GLN C 160     -53.945  27.628  13.608  1.00 24.72           C  
ANISOU 4846  CB  GLN C 160     3291   3111   2990    -70    -55    229       C  
ATOM   4847  CG  GLN C 160     -53.306  28.912  13.072  1.00 29.67           C  
ANISOU 4847  CG  GLN C 160     3930   3733   3610    -99    -65    256       C  
ATOM   4848  CD  GLN C 160     -53.780  30.168  13.798  1.00 33.95           C  
ANISOU 4848  CD  GLN C 160     4503   4230   4166   -101    -82    263       C  
ATOM   4849  OE1 GLN C 160     -54.946  30.571  13.690  1.00 38.05           O  
ANISOU 4849  OE1 GLN C 160     5039   4727   4692    -83    -91    262       O  
ATOM   4850  NE2 GLN C 160     -52.863  30.807  14.543  1.00 36.19           N  
ANISOU 4850  NE2 GLN C 160     4794   4503   4455   -122    -88    269       N  
ATOM   4851  N   GLU C 161     -53.259  24.624  14.708  1.00 22.67           N  
ANISOU 4851  N   GLU C 161     2990   2891   2733    -41    -34    182       N  
ATOM   4852  CA  GLU C 161     -53.728  23.507  15.510  1.00 21.12           C  
ANISOU 4852  CA  GLU C 161     2790   2690   2545    -22    -32    161       C  
ATOM   4853  C   GLU C 161     -54.108  23.934  16.914  1.00 20.83           C  
ANISOU 4853  C   GLU C 161     2768   2623   2524    -19    -36    155       C  
ATOM   4854  O   GLU C 161     -53.536  24.893  17.474  1.00 21.59           O  
ANISOU 4854  O   GLU C 161     2873   2706   2625    -34    -40    163       O  
ATOM   4855  CB  GLU C 161     -52.666  22.433  15.612  1.00 21.87           C  
ANISOU 4855  CB  GLU C 161     2866   2810   2633    -21    -27    148       C  
ATOM   4856  CG  GLU C 161     -52.394  21.800  14.286  1.00 23.22           C  
ANISOU 4856  CG  GLU C 161     3021   3015   2788    -16    -24    147       C  
ATOM   4857  CD  GLU C 161     -51.473  20.581  14.372  1.00 26.96           C  
ANISOU 4857  CD  GLU C 161     3476   3513   3254     -8    -22    129       C  
ATOM   4858  OE1 GLU C 161     -50.946  20.291  15.478  1.00 29.40           O  
ANISOU 4858  OE1 GLU C 161     3786   3814   3571     -8    -23    119       O  
ATOM   4859  OE2 GLU C 161     -51.269  19.941  13.320  1.00 29.31           O  
ANISOU 4859  OE2 GLU C 161     3759   3840   3538      0    -21    124       O  
ATOM   4860  N   SER C 162     -55.093  23.227  17.460  1.00 18.26           N  
ANISOU 4860  N   SER C 162     2443   2288   2205     -2    -36    141       N  
ATOM   4861  CA  SER C 162     -55.436  23.354  18.866  1.00 18.01           C  
ANISOU 4861  CA  SER C 162     2420   2236   2186      2    -39    132       C  
ATOM   4862  C   SER C 162     -55.591  21.944  19.436  1.00 18.38           C  
ANISOU 4862  C   SER C 162     2459   2292   2234     12    -36    116       C  
ATOM   4863  O   SER C 162     -56.136  21.091  18.797  1.00 19.39           O  
ANISOU 4863  O   SER C 162     2580   2429   2356     22    -35    111       O  
ATOM   4864  CB  SER C 162     -56.725  24.124  19.058  1.00 18.36           C  
ANISOU 4864  CB  SER C 162     2478   2261   2235     12    -45    133       C  
ATOM   4865  OG  SER C 162     -56.983  24.283  20.444  1.00 19.58           O  
ANISOU 4865  OG  SER C 162     2638   2401   2399     16    -48    123       O  
ATOM   4866  N   VAL C 163     -55.177  21.734  20.689  1.00 18.52           N  
ANISOU 4866  N   VAL C 163     2477   2301   2258     10    -37    107       N  
ATOM   4867  CA AVAL C 163     -55.196  20.400  21.283  0.50 17.85           C  
ANISOU 4867  CA AVAL C 163     2386   2222   2174     17    -37     94       C  
ATOM   4868  CA BVAL C 163     -55.207  20.406  21.264  0.50 18.41           C  
ANISOU 4868  CA BVAL C 163     2457   2293   2245     17    -37     94       C  
ATOM   4869  C   VAL C 163     -55.837  20.531  22.643  1.00 17.71           C  
ANISOU 4869  C   VAL C 163     2376   2190   2165     19    -40     88       C  
ATOM   4870  O   VAL C 163     -55.550  21.493  23.373  1.00 18.99           O  
ANISOU 4870  O   VAL C 163     2544   2340   2333     14    -41     90       O  
ATOM   4871  CB AVAL C 163     -53.773  19.872  21.498  0.50 17.50           C  
ANISOU 4871  CB AVAL C 163     2333   2189   2127     11    -36     89       C  
ATOM   4872  CB BVAL C 163     -53.771  19.827  21.321  0.50 18.57           C  
ANISOU 4872  CB BVAL C 163     2468   2327   2262     12    -36     90       C  
ATOM   4873  CG1AVAL C 163     -53.803  18.415  21.935  0.50 18.16           C  
ANISOU 4873  CG1AVAL C 163     2413   2276   2210     20    -40     76       C  
ATOM   4874  CG1BVAL C 163     -52.825  20.729  22.099  0.50 19.88           C  
ANISOU 4874  CG1BVAL C 163     2635   2486   2431     -1    -35     93       C  
ATOM   4875  CG2AVAL C 163     -52.971  19.979  20.221  0.50 16.70           C  
ANISOU 4875  CG2AVAL C 163     2222   2108   2015      7    -33     95       C  
ATOM   4876  CG2BVAL C 163     -53.755  18.394  21.848  0.50 19.00           C  
ANISOU 4876  CG2BVAL C 163     2520   2384   2316     20    -40     76       C  
ATOM   4877  N   THR C 164     -56.715  19.595  22.974  1.00 16.86           N  
ANISOU 4877  N   THR C 164     2267   2084   2057     26    -42     81       N  
ATOM   4878  CA  THR C 164     -57.347  19.619  24.301  1.00 16.18           C  
ANISOU 4878  CA  THR C 164     2183   1990   1974     27    -44     75       C  
ATOM   4879  C   THR C 164     -56.383  19.213  25.384  1.00 15.71           C  
ANISOU 4879  C   THR C 164     2123   1928   1919     21    -45     69       C  
ATOM   4880  O   THR C 164     -55.356  18.560  25.124  1.00 17.35           O  
ANISOU 4880  O   THR C 164     2327   2141   2125     18    -46     67       O  
ATOM   4881  CB  THR C 164     -58.544  18.708  24.371  1.00 16.60           C  
ANISOU 4881  CB  THR C 164     2235   2050   2024     31    -47     70       C  
ATOM   4882  OG1 THR C 164     -58.101  17.364  24.108  1.00 17.28           O  
ANISOU 4882  OG1 THR C 164     2318   2141   2106     30    -50     67       O  
ATOM   4883  CG2 THR C 164     -59.646  19.136  23.345  1.00 19.88           C  
ANISOU 4883  CG2 THR C 164     2651   2470   2435     39    -46     75       C  
ATOM   4884  N   GLU C 165     -56.734  19.557  26.619  1.00 16.64           N  
ANISOU 4884  N   GLU C 165     2243   2039   2040     20    -47     65       N  
ATOM   4885  CA  GLU C 165     -56.051  19.045  27.784  1.00 18.51           C  
ANISOU 4885  CA  GLU C 165     2479   2275   2280     14    -48     59       C  
ATOM   4886  C   GLU C 165     -56.285  17.541  27.831  1.00 16.73           C  
ANISOU 4886  C   GLU C 165     2252   2056   2050     14    -53     56       C  
ATOM   4887  O   GLU C 165     -57.301  17.045  27.341  1.00 18.15           O  
ANISOU 4887  O   GLU C 165     2431   2240   2224     17    -55     57       O  
ATOM   4888  CB  GLU C 165     -56.735  19.670  29.010  1.00 19.59           C  
ANISOU 4888  CB  GLU C 165     2617   2408   2418     15    -49     55       C  
ATOM   4889  CG  GLU C 165     -58.215  19.298  29.048  1.00 26.70           C  
ANISOU 4889  CG  GLU C 165     3515   3317   3312     20    -51     54       C  
ATOM   4890  CD  GLU C 165     -59.038  19.927  30.154  1.00 35.58           C  
ANISOU 4890  CD  GLU C 165     4638   4446   4435     23    -52     47       C  
ATOM   4891  OE1 GLU C 165     -59.984  20.663  29.805  1.00 39.44           O  
ANISOU 4891  OE1 GLU C 165     5126   4938   4921     33    -53     46       O  
ATOM   4892  OE2 GLU C 165     -58.782  19.643  31.353  1.00 37.22           O  
ANISOU 4892  OE2 GLU C 165     4843   4656   4642     18    -54     43       O  
ATOM   4893  N   GLN C 166     -55.340  16.796  28.394  1.00 16.28           N  
ANISOU 4893  N   GLN C 166     2195   1997   1993     11    -57     52       N  
ATOM   4894  CA  GLN C 166     -55.563  15.363  28.548  1.00 15.23           C  
ANISOU 4894  CA  GLN C 166     2065   1866   1857     10    -66     49       C  
ATOM   4895  C   GLN C 166     -56.900  15.095  29.272  1.00 16.65           C  
ANISOU 4895  C   GLN C 166     2246   2047   2032      5    -69     51       C  
ATOM   4896  O   GLN C 166     -57.199  15.662  30.337  1.00 15.94           O  
ANISOU 4896  O   GLN C 166     2154   1959   1943      1    -66     50       O  
ATOM   4897  CB  GLN C 166     -54.389  14.739  29.294  1.00 15.70           C  
ANISOU 4897  CB  GLN C 166     2126   1921   1917      9    -72     43       C  
ATOM   4898  CG  GLN C 166     -54.444  13.230  29.225  1.00 15.54           C  
ANISOU 4898  CG  GLN C 166     2112   1899   1893     10    -85     40       C  
ATOM   4899  CD  GLN C 166     -53.229  12.517  29.814  1.00 16.62           C  
ANISOU 4899  CD  GLN C 166     2252   2032   2030     13    -94     33       C  
ATOM   4900  OE1 GLN C 166     -52.899  11.361  29.413  1.00 17.55           O  
ANISOU 4900  OE1 GLN C 166     2376   2147   2146     20   -107     27       O  
ATOM   4901  NE2 GLN C 166     -52.595  13.138  30.788  1.00 16.70           N  
ANISOU 4901  NE2 GLN C 166     2260   2042   2044     10    -89     31       N  
ATOM   4902  N   ASP C 167     -57.694  14.173  28.732  1.00 15.43           N  
ANISOU 4902  N   ASP C 167     2094   1896   1873      3    -75     53       N  
ATOM   4903  CA  ASP C 167     -59.006  13.891  29.301  1.00 16.80           C  
ANISOU 4903  CA  ASP C 167     2266   2077   2039     -5    -78     56       C  
ATOM   4904  C   ASP C 167     -58.854  13.293  30.702  1.00 16.89           C  
ANISOU 4904  C   ASP C 167     2280   2087   2049    -17    -85     56       C  
ATOM   4905  O   ASP C 167     -58.081  12.347  30.898  1.00 15.64           O  
ANISOU 4905  O   ASP C 167     2130   1920   1892    -19    -95     55       O  
ATOM   4906  CB  ASP C 167     -59.802  12.926  28.429  1.00 17.57           C  
ANISOU 4906  CB  ASP C 167     2366   2178   2131     -8    -85     58       C  
ATOM   4907  CG  ASP C 167     -61.235  12.785  28.911  1.00 18.98           C  
ANISOU 4907  CG  ASP C 167     2540   2370   2300    -18    -86     62       C  
ATOM   4908  OD1 ASP C 167     -62.003  13.732  28.687  1.00 24.58           O  
ANISOU 4908  OD1 ASP C 167     3242   3090   3008    -12    -78     61       O  
ATOM   4909  OD2 ASP C 167     -61.576  11.793  29.611  1.00 22.40           O  
ANISOU 4909  OD2 ASP C 167     2978   2805   2728    -33    -97     66       O  
ATOM   4910  N   SER C 168     -59.628  13.822  31.652  1.00 17.40           N  
ANISOU 4910  N   SER C 168     2338   2164   2109    -22    -81     57       N  
ATOM   4911  CA  SER C 168     -59.499  13.406  33.050  1.00 18.07           C  
ANISOU 4911  CA  SER C 168     2424   2252   2190    -34    -86     57       C  
ATOM   4912  C   SER C 168     -59.967  11.991  33.369  1.00 18.76           C  
ANISOU 4912  C   SER C 168     2518   2341   2269    -51   -100     65       C  
ATOM   4913  O   SER C 168     -59.673  11.504  34.485  1.00 20.35           O  
ANISOU 4913  O   SER C 168     2723   2542   2467    -62   -107     67       O  
ATOM   4914  CB  SER C 168     -60.188  14.419  33.962  1.00 19.33           C  
ANISOU 4914  CB  SER C 168     2573   2427   2345    -33    -79     54       C  
ATOM   4915  OG  SER C 168     -61.585  14.385  33.781  1.00 22.42           O  
ANISOU 4915  OG  SER C 168     2957   2838   2725    -37    -78     56       O  
ATOM   4916  N   LYS C 169     -60.739  11.374  32.470  1.00 19.31           N  
ANISOU 4916  N   LYS C 169     2591   2413   2335    -54   -105     68       N  
ATOM   4917  CA  LYS C 169     -61.274  10.034  32.677  1.00 20.80           C  
ANISOU 4917  CA  LYS C 169     2788   2601   2515    -73   -121     77       C  
ATOM   4918  C   LYS C 169     -60.557   9.020  31.796  1.00 20.05           C  
ANISOU 4918  C   LYS C 169     2709   2485   2426    -68   -135     75       C  
ATOM   4919  O   LYS C 169     -60.185   7.929  32.267  1.00 20.79           O  
ANISOU 4919  O   LYS C 169     2817   2565   2518    -78   -153     79       O  
ATOM   4920  CB  LYS C 169     -62.779   9.989  32.408  1.00 22.70           C  
ANISOU 4920  CB  LYS C 169     3020   2863   2743    -84   -120     82       C  
ATOM   4921  CG  LYS C 169     -63.554  11.056  33.145  1.00 26.83           C  
ANISOU 4921  CG  LYS C 169     3525   3412   3258    -84   -107     79       C  
ATOM   4922  CD  LYS C 169     -65.063  10.905  32.940  1.00 32.90           C  
ANISOU 4922  CD  LYS C 169     4283   4207   4011    -96   -107     83       C  
ATOM   4923  CE  LYS C 169     -65.830  11.744  33.953  1.00 34.88           C  
ANISOU 4923  CE  LYS C 169     4515   4489   4249    -97    -99     80       C  
ATOM   4924  NZ  LYS C 169     -65.224  11.645  35.313  1.00 36.29           N  
ANISOU 4924  NZ  LYS C 169     4695   4669   4427   -106   -102     81       N  
ATOM   4925  N   ASP C 170     -60.391   9.328  30.504  1.00 18.77           N  
ANISOU 4925  N   ASP C 170     2544   2318   2268    -52   -129     69       N  
ATOM   4926  CA  ASP C 170     -59.794   8.298  29.628  1.00 18.49           C  
ANISOU 4926  CA  ASP C 170     2522   2266   2236    -45   -144     65       C  
ATOM   4927  C   ASP C 170     -58.346   8.568  29.167  1.00 16.03           C  
ANISOU 4927  C   ASP C 170     2211   1946   1934    -24   -141     55       C  
ATOM   4928  O   ASP C 170     -57.752   7.775  28.439  1.00 16.19           O  
ANISOU 4928  O   ASP C 170     2240   1957   1956    -14   -154     48       O  
ATOM   4929  CB  ASP C 170     -60.707   8.005  28.420  1.00 20.41           C  
ANISOU 4929  CB  ASP C 170     2764   2514   2476    -44   -146     66       C  
ATOM   4930  CG  ASP C 170     -60.751   9.128  27.392  1.00 23.93           C  
ANISOU 4930  CG  ASP C 170     3197   2970   2925    -27   -128     62       C  
ATOM   4931  OD1 ASP C 170     -59.821   9.940  27.286  1.00 22.46           O  
ANISOU 4931  OD1 ASP C 170     3006   2783   2745    -14   -118     57       O  
ATOM   4932  OD2 ASP C 170     -61.733   9.168  26.600  1.00 32.44           O  
ANISOU 4932  OD2 ASP C 170     4270   4057   3998    -28   -126     64       O  
ATOM   4933  N   SER C 171     -57.801   9.708  29.595  1.00 15.34           N  
ANISOU 4933  N   SER C 171     2114   1865   1851    -19   -126     53       N  
ATOM   4934  CA  SER C 171     -56.421  10.083  29.388  1.00 14.63           C  
ANISOU 4934  CA  SER C 171     2021   1771   1767     -4   -121     45       C  
ATOM   4935  C   SER C 171     -56.005  10.258  27.912  1.00 15.03           C  
ANISOU 4935  C   SER C 171     2067   1826   1818     11   -117     39       C  
ATOM   4936  O   SER C 171     -54.830  10.218  27.597  1.00 15.54           O  
ANISOU 4936  O   SER C 171     2129   1891   1883     22   -118     32       O  
ATOM   4937  CB  SER C 171     -55.479   9.089  30.079  1.00 15.06           C  
ANISOU 4937  CB  SER C 171     2087   1814   1822     -3   -138     40       C  
ATOM   4938  OG  SER C 171     -55.802   9.059  31.494  1.00 16.16           O  
ANISOU 4938  OG  SER C 171     2229   1952   1959    -19   -140     47       O  
ATOM   4939  N   THR C 172     -56.968  10.525  27.051  1.00 16.69           N  
ANISOU 4939  N   THR C 172     2273   2042   2026     11   -112     43       N  
ATOM   4940  CA  THR C 172     -56.636  10.793  25.663  1.00 15.47           C  
ANISOU 4940  CA  THR C 172     2113   1895   1871     24   -107     40       C  
ATOM   4941  C   THR C 172     -56.616  12.301  25.359  1.00 16.22           C  
ANISOU 4941  C   THR C 172     2197   1999   1968     25    -89     44       C  
ATOM   4942  O   THR C 172     -56.965  13.127  26.210  1.00 18.95           O  
ANISOU 4942  O   THR C 172     2541   2343   2316     18    -81     49       O  
ATOM   4943  CB  THR C 172     -57.653  10.136  24.699  1.00 16.51           C  
ANISOU 4943  CB  THR C 172     2247   2028   1998     24   -113     41       C  
ATOM   4944  OG1 THR C 172     -58.962  10.680  24.950  1.00 20.09           O  
ANISOU 4944  OG1 THR C 172     2697   2487   2449     14   -106     49       O  
ATOM   4945  CG2 THR C 172     -57.674   8.614  24.892  1.00 16.31           C  
ANISOU 4945  CG2 THR C 172     2235   1991   1970     22   -136     36       C  
ATOM   4946  N   TYR C 173     -56.272  12.628  24.118  1.00 15.55           N  
ANISOU 4946  N   TYR C 173     2106   1922   1881     34    -84     43       N  
ATOM   4947  CA  TYR C 173     -56.255  14.020  23.636  1.00 15.34           C  
ANISOU 4947  CA  TYR C 173     2073   1902   1855     34    -70     50       C  
ATOM   4948  C   TYR C 173     -57.140  14.097  22.402  1.00 15.56           C  
ANISOU 4948  C   TYR C 173     2098   1937   1878     39    -68     53       C  
ATOM   4949  O   TYR C 173     -57.388  13.088  21.724  1.00 16.08           O  
ANISOU 4949  O   TYR C 173     2165   2005   1940     44    -76     49       O  
ATOM   4950  CB  TYR C 173     -54.856  14.422  23.211  1.00 16.34           C  
ANISOU 4950  CB  TYR C 173     2192   2036   1980     38    -66     48       C  
ATOM   4951  CG  TYR C 173     -53.867  14.295  24.311  1.00 16.46           C  
ANISOU 4951  CG  TYR C 173     2208   2047   1999     35    -68     43       C  
ATOM   4952  CD1 TYR C 173     -53.571  15.389  25.142  1.00 17.06           C  
ANISOU 4952  CD1 TYR C 173     2284   2119   2080     27    -61     47       C  
ATOM   4953  CD2 TYR C 173     -53.181  13.106  24.510  1.00 16.35           C  
ANISOU 4953  CD2 TYR C 173     2197   2034   1983     41    -80     32       C  
ATOM   4954  CE1 TYR C 173     -52.615  15.266  26.172  1.00 18.48           C  
ANISOU 4954  CE1 TYR C 173     2464   2296   2263     24    -63     42       C  
ATOM   4955  CE2 TYR C 173     -52.268  12.962  25.541  1.00 18.46           C  
ANISOU 4955  CE2 TYR C 173     2464   2297   2252     40    -83     27       C  
ATOM   4956  CZ  TYR C 173     -51.975  14.032  26.350  1.00 20.11           C  
ANISOU 4956  CZ  TYR C 173     2671   2503   2465     31    -74     32       C  
ATOM   4957  OH  TYR C 173     -51.024  13.833  27.335  1.00 20.58           O  
ANISOU 4957  OH  TYR C 173     2730   2561   2526     30    -77     26       O  
ATOM   4958  N   SER C 174     -57.608  15.301  22.105  1.00 14.56           N  
ANISOU 4958  N   SER C 174     1969   1812   1752     38    -58     61       N  
ATOM   4959  CA  SER C 174     -58.200  15.530  20.768  1.00 15.18           C  
ANISOU 4959  CA  SER C 174     2043   1898   1825     44    -55     65       C  
ATOM   4960  C   SER C 174     -57.540  16.758  20.154  1.00 15.18           C  
ANISOU 4960  C   SER C 174     2041   1902   1825     43    -47     73       C  
ATOM   4961  O   SER C 174     -56.990  17.570  20.862  1.00 15.64           O  
ANISOU 4961  O   SER C 174     2100   1953   1887     37    -45     76       O  
ATOM   4962  CB  SER C 174     -59.700  15.691  20.876  1.00 14.34           C  
ANISOU 4962  CB  SER C 174     1940   1791   1718     44    -55     68       C  
ATOM   4963  OG  SER C 174     -60.263  14.435  21.267  1.00 15.41           O  
ANISOU 4963  OG  SER C 174     2077   1926   1851     41    -64     63       O  
ATOM   4964  N   LEU C 175     -57.549  16.871  18.820  1.00 16.11           N  
ANISOU 4964  N   LEU C 175     2153   2031   1935     48    -45     77       N  
ATOM   4965  CA  LEU C 175     -56.789  17.932  18.143  1.00 16.79           C  
ANISOU 4965  CA  LEU C 175     2237   2125   2019     43    -40     87       C  
ATOM   4966  C   LEU C 175     -57.613  18.391  16.952  1.00 15.99           C  
ANISOU 4966  C   LEU C 175     2134   2029   1911     47    -38     95       C  
ATOM   4967  O   LEU C 175     -58.311  17.600  16.318  1.00 16.14           O  
ANISOU 4967  O   LEU C 175     2151   2055   1926     56    -40     90       O  
ATOM   4968  CB  LEU C 175     -55.405  17.390  17.716  1.00 17.79           C  
ANISOU 4968  CB  LEU C 175     2353   2268   2139     43    -40     82       C  
ATOM   4969  CG  LEU C 175     -54.409  18.268  16.932  1.00 19.11           C  
ANISOU 4969  CG  LEU C 175     2512   2451   2297     34    -34     92       C  
ATOM   4970  CD1 LEU C 175     -52.949  17.749  17.030  1.00 21.74           C  
ANISOU 4970  CD1 LEU C 175     2833   2802   2624     33    -35     83       C  
ATOM   4971  CD2 LEU C 175     -54.806  18.309  15.453  1.00 18.94           C  
ANISOU 4971  CD2 LEU C 175     2485   2447   2266     38    -33     98       C  
ATOM   4972  N   SER C 176     -57.596  19.702  16.761  1.00 15.88           N  
ANISOU 4972  N   SER C 176     2126   2009   1899     41    -35    107       N  
ATOM   4973  CA  SER C 176     -58.172  20.295  15.561  1.00 17.11           C  
ANISOU 4973  CA  SER C 176     2283   2171   2048     44    -34    118       C  
ATOM   4974  C   SER C 176     -57.068  20.950  14.773  1.00 16.95           C  
ANISOU 4974  C   SER C 176     2257   2162   2019     33    -32    130       C  
ATOM   4975  O   SER C 176     -56.132  21.560  15.329  1.00 18.84           O  
ANISOU 4975  O   SER C 176     2499   2397   2261     20    -32    135       O  
ATOM   4976  CB  SER C 176     -59.240  21.317  15.903  1.00 17.18           C  
ANISOU 4976  CB  SER C 176     2304   2163   2063     48    -37    123       C  
ATOM   4977  OG  SER C 176     -58.697  22.542  16.427  1.00 18.64           O  
ANISOU 4977  OG  SER C 176     2498   2331   2252     38    -40    132       O  
ATOM   4978  N   SER C 177     -57.169  20.822  13.453  1.00 17.68           N  
ANISOU 4978  N   SER C 177     2343   2274   2101     35    -30    135       N  
ATOM   4979  CA  SER C 177     -56.294  21.558  12.552  1.00 18.97           C  
ANISOU 4979  CA  SER C 177     2501   2453   2253     22    -28    150       C  
ATOM   4980  C   SER C 177     -57.210  22.322  11.625  1.00 18.71           C  
ANISOU 4980  C   SER C 177     2477   2417   2217     24    -31    164       C  
ATOM   4981  O   SER C 177     -58.138  21.731  11.056  1.00 19.56           O  
ANISOU 4981  O   SER C 177     2581   2530   2322     38    -30    157       O  
ATOM   4982  CB  SER C 177     -55.370  20.664  11.741  1.00 20.19           C  
ANISOU 4982  CB  SER C 177     2637   2641   2394     23    -25    144       C  
ATOM   4983  OG  SER C 177     -54.537  21.502  10.921  1.00 20.21           O  
ANISOU 4983  OG  SER C 177     2633   2663   2384      6    -23    161       O  
ATOM   4984  N   THR C 178     -56.996  23.627  11.544  1.00 18.41           N  
ANISOU 4984  N   THR C 178     2451   2367   2179     10    -34    182       N  
ATOM   4985  CA  THR C 178     -57.861  24.440  10.709  1.00 19.42           C  
ANISOU 4985  CA  THR C 178     2589   2488   2303     13    -39    195       C  
ATOM   4986  C   THR C 178     -57.042  25.078   9.617  1.00 18.46           C  
ANISOU 4986  C   THR C 178     2464   2385   2167     -7    -40    216       C  
ATOM   4987  O   THR C 178     -56.073  25.767   9.893  1.00 19.61           O  
ANISOU 4987  O   THR C 178     2613   2528   2311    -27    -42    228       O  
ATOM   4988  CB  THR C 178     -58.575  25.483  11.551  1.00 18.91           C  
ANISOU 4988  CB  THR C 178     2546   2388   2251     16    -49    199       C  
ATOM   4989  OG1 THR C 178     -59.336  24.822  12.584  1.00 20.25           O  
ANISOU 4989  OG1 THR C 178     2715   2548   2431     32    -47    179       O  
ATOM   4990  CG2 THR C 178     -59.503  26.374  10.726  1.00 20.67           C  
ANISOU 4990  CG2 THR C 178     2783   2601   2470     22    -57    212       C  
ATOM   4991  N   LEU C 179     -57.453  24.808   8.381  1.00 18.33           N  
ANISOU 4991  N   LEU C 179     2439   2389   2138      0    -38    220       N  
ATOM   4992  CA  LEU C 179     -56.884  25.421   7.181  1.00 20.51           C  
ANISOU 4992  CA  LEU C 179     2710   2686   2396    -18    -39    242       C  
ATOM   4993  C   LEU C 179     -57.697  26.669   6.849  1.00 20.77           C  
ANISOU 4993  C   LEU C 179     2767   2693   2431    -21    -50    261       C  
ATOM   4994  O   LEU C 179     -58.928  26.593   6.642  1.00 20.91           O  
ANISOU 4994  O   LEU C 179     2792   2700   2454      0    -53    255       O  
ATOM   4995  CB  LEU C 179     -56.941  24.403   6.051  1.00 19.59           C  
ANISOU 4995  CB  LEU C 179     2571   2607   2264     -7    -31    234       C  
ATOM   4996  CG  LEU C 179     -56.427  24.884   4.711  1.00 20.62           C  
ANISOU 4996  CG  LEU C 179     2692   2768   2373    -23    -31    255       C  
ATOM   4997  CD1 LEU C 179     -54.924  24.905   4.695  1.00 21.91           C  
ANISOU 4997  CD1 LEU C 179     2840   2961   2524    -46    -27    260       C  
ATOM   4998  CD2 LEU C 179     -56.920  23.969   3.585  1.00 20.55           C  
ANISOU 4998  CD2 LEU C 179     2666   2789   2351     -5    -26    245       C  
ATOM   4999  N   THR C 180     -57.038  27.830   6.820  1.00 23.18           N  
ANISOU 4999  N   THR C 180     3086   2988   2734    -46    -58    284       N  
ATOM   5000  CA  THR C 180     -57.765  29.080   6.505  1.00 26.61           C  
ANISOU 5000  CA  THR C 180     3547   3392   3170    -48    -74    303       C  
ATOM   5001  C   THR C 180     -57.310  29.679   5.178  1.00 27.30           C  
ANISOU 5001  C   THR C 180     3633   3501   3237    -71    -78    331       C  
ATOM   5002  O   THR C 180     -56.127  29.911   4.977  1.00 28.01           O  
ANISOU 5002  O   THR C 180     3716   3611   3316   -100    -76    345       O  
ATOM   5003  CB  THR C 180     -57.679  30.120   7.618  1.00 27.55           C  
ANISOU 5003  CB  THR C 180     3692   3471   3305    -56    -87    307       C  
ATOM   5004  OG1 THR C 180     -58.171  29.534   8.820  1.00 30.14           O  
ANISOU 5004  OG1 THR C 180     4019   3784   3649    -34    -83    281       O  
ATOM   5005  CG2 THR C 180     -58.571  31.328   7.292  1.00 29.14           C  
ANISOU 5005  CG2 THR C 180     3924   3640   3510    -51   -107    322       C  
ATOM   5006  N   LEU C 181     -58.280  29.875   4.290  1.00 27.51           N  
ANISOU 5006  N   LEU C 181     3667   3526   3259    -58    -83    337       N  
ATOM   5007  CA  LEU C 181     -58.078  30.440   2.948  1.00 28.16           C  
ANISOU 5007  CA  LEU C 181     3750   3628   3320    -76    -88    364       C  
ATOM   5008  C   LEU C 181     -59.115  31.514   2.737  1.00 27.24           C  
ANISOU 5008  C   LEU C 181     3666   3475   3210    -68   -107    378       C  
ATOM   5009  O   LEU C 181     -60.176  31.501   3.367  1.00 27.07           O  
ANISOU 5009  O   LEU C 181     3656   3425   3204    -39   -112    360       O  
ATOM   5010  CB  LEU C 181     -58.310  29.378   1.863  1.00 27.78           C  
ANISOU 5010  CB  LEU C 181     3674   3624   3257    -63    -74    355       C  
ATOM   5011  CG  LEU C 181     -57.534  28.076   1.744  1.00 30.50           C  
ANISOU 5011  CG  LEU C 181     3984   4012   3592    -60    -57    337       C  
ATOM   5012  CD1 LEU C 181     -56.061  28.289   2.056  1.00 32.23           C  
ANISOU 5012  CD1 LEU C 181     4194   4249   3804    -91    -54    346       C  
ATOM   5013  CD2 LEU C 181     -58.132  27.038   2.656  1.00 33.95           C  
ANISOU 5013  CD2 LEU C 181     4415   4436   4047    -31    -50    304       C  
ATOM   5014  N   SER C 182     -58.852  32.435   1.809  1.00 27.65           N  
ANISOU 5014  N   SER C 182     3731   3528   3247    -92   -119    409       N  
ATOM   5015  CA  SER C 182     -59.920  33.320   1.360  1.00 27.69           C  
ANISOU 5015  CA  SER C 182     3764   3502   3254    -79   -138    421       C  
ATOM   5016  C   SER C 182     -60.965  32.498   0.599  1.00 26.40           C  
ANISOU 5016  C   SER C 182     3585   3361   3085    -48   -128    406       C  
ATOM   5017  O   SER C 182     -60.646  31.438   0.058  1.00 25.56           O  
ANISOU 5017  O   SER C 182     3446   3298   2967    -47   -110    396       O  
ATOM   5018  CB  SER C 182     -59.368  34.409   0.438  1.00 28.07           C  
ANISOU 5018  CB  SER C 182     3829   3550   3285   -114   -155    461       C  
ATOM   5019  OG  SER C 182     -58.826  33.822  -0.735  1.00 30.60           O  
ANISOU 5019  OG  SER C 182     4121   3925   3582   -130   -140    472       O  
ATOM   5020  N   LYS C 183     -62.209  32.964   0.587  1.00 26.32           N  
ANISOU 5020  N   LYS C 183     3596   3323   3083    -21   -142    401       N  
ATOM   5021  CA  LYS C 183     -63.246  32.327  -0.222  1.00 26.05           C  
ANISOU 5021  CA  LYS C 183     3548   3309   3041      6   -135    390       C  
ATOM   5022  C   LYS C 183     -62.770  32.195  -1.679  1.00 25.57           C  
ANISOU 5022  C   LYS C 183     3471   3288   2956    -13   -129    412       C  
ATOM   5023  O   LYS C 183     -62.856  31.124  -2.279  1.00 22.94           O  
ANISOU 5023  O   LYS C 183     3109   2993   2614     -3   -112    398       O  
ATOM   5024  CB  LYS C 183     -64.558  33.115  -0.124  1.00 27.25           C  
ANISOU 5024  CB  LYS C 183     3727   3425   3201     33   -154    387       C  
ATOM   5025  CG  LYS C 183     -65.648  32.681  -1.068  1.00 29.18           C  
ANISOU 5025  CG  LYS C 183     3962   3689   3436     59   -151    379       C  
ATOM   5026  CD  LYS C 183     -66.945  33.451  -0.745  1.00 31.76           C  
ANISOU 5026  CD  LYS C 183     4316   3981   3772     90   -171    371       C  
ATOM   5027  CE  LYS C 183     -68.116  32.977  -1.574  1.00 33.81           C  
ANISOU 5027  CE  LYS C 183     4563   4261   4022    118   -167    360       C  
ATOM   5028  NZ  LYS C 183     -67.946  33.429  -2.980  1.00 38.01           N  
ANISOU 5028  NZ  LYS C 183     5100   4807   4535    104   -173    389       N  
ATOM   5029  N   ALA C 184     -62.211  33.270  -2.218  1.00 26.00           N  
ANISOU 5029  N   ALA C 184     3544   3334   2999    -43   -145    445       N  
ATOM   5030  CA  ALA C 184     -61.707  33.216  -3.599  1.00 26.56           C  
ANISOU 5030  CA  ALA C 184     3600   3447   3044    -65   -140    469       C  
ATOM   5031  C   ALA C 184     -60.665  32.103  -3.812  1.00 26.97           C  
ANISOU 5031  C   ALA C 184     3611   3552   3083    -78   -116    459       C  
ATOM   5032  O   ALA C 184     -60.720  31.368  -4.816  1.00 25.97           O  
ANISOU 5032  O   ALA C 184     3459   3470   2940    -72   -104    456       O  
ATOM   5033  CB  ALA C 184     -61.151  34.583  -4.009  1.00 27.14           C  
ANISOU 5033  CB  ALA C 184     3702   3502   3107   -102   -162    510       C  
ATOM   5034  N   ASP C 185     -59.723  31.960  -2.877  1.00 26.49           N  
ANISOU 5034  N   ASP C 185     3545   3489   3031    -94   -111    453       N  
ATOM   5035  CA  ASP C 185     -58.713  30.902  -3.029  1.00 26.38           C  
ANISOU 5035  CA  ASP C 185     3494   3526   3005   -103    -91    441       C  
ATOM   5036  C   ASP C 185     -59.313  29.513  -2.878  1.00 24.93           C  
ANISOU 5036  C   ASP C 185     3286   3357   2828    -66    -75    404       C  
ATOM   5037  O   ASP C 185     -58.950  28.595  -3.595  1.00 25.31           O  
ANISOU 5037  O   ASP C 185     3304   3452   2860    -62    -62    394       O  
ATOM   5038  CB  ASP C 185     -57.552  31.083  -2.046  1.00 26.80           C  
ANISOU 5038  CB  ASP C 185     3546   3573   3064   -127    -89    442       C  
ATOM   5039  CG  ASP C 185     -56.587  32.201  -2.449  1.00 31.44           C  
ANISOU 5039  CG  ASP C 185     4145   4167   3635   -174   -101    481       C  
ATOM   5040  OD1 ASP C 185     -56.520  32.539  -3.662  1.00 36.55           O  
ANISOU 5040  OD1 ASP C 185     4787   4841   4258   -191   -105    505       O  
ATOM   5041  OD2 ASP C 185     -55.875  32.729  -1.554  1.00 35.23           O  
ANISOU 5041  OD2 ASP C 185     4637   4626   4124   -195   -107    487       O  
ATOM   5042  N   TYR C 186     -60.235  29.364  -1.922  1.00 22.49           N  
ANISOU 5042  N   TYR C 186     2992   3010   2543    -39    -77    383       N  
ATOM   5043  CA  TYR C 186     -60.939  28.099  -1.744  1.00 22.15           C  
ANISOU 5043  CA  TYR C 186     2932   2977   2508     -7    -65    350       C  
ATOM   5044  C   TYR C 186     -61.625  27.617  -3.047  1.00 22.03           C  
ANISOU 5044  C   TYR C 186     2902   2992   2477      8    -62    349       C  
ATOM   5045  O   TYR C 186     -61.600  26.421  -3.404  1.00 21.33           O  
ANISOU 5045  O   TYR C 186     2787   2935   2382     22    -50    328       O  
ATOM   5046  CB  TYR C 186     -61.946  28.261  -0.590  1.00 21.99           C  
ANISOU 5046  CB  TYR C 186     2932   2912   2512     15    -72    334       C  
ATOM   5047  CG  TYR C 186     -62.801  27.049  -0.372  1.00 20.34           C  
ANISOU 5047  CG  TYR C 186     2708   2711   2310     45    -62    303       C  
ATOM   5048  CD1 TYR C 186     -62.250  25.881   0.142  1.00 19.91           C  
ANISOU 5048  CD1 TYR C 186     2634   2673   2259     47    -51    282       C  
ATOM   5049  CD2 TYR C 186     -64.153  27.067  -0.661  1.00 18.36           C  
ANISOU 5049  CD2 TYR C 186     2464   2450   2061     69    -67    296       C  
ATOM   5050  CE1 TYR C 186     -63.039  24.742   0.329  1.00 18.89           C  
ANISOU 5050  CE1 TYR C 186     2493   2549   2136     71    -45    256       C  
ATOM   5051  CE2 TYR C 186     -64.958  25.926  -0.469  1.00 18.44           C  
ANISOU 5051  CE2 TYR C 186     2460   2469   2077     92    -59    269       C  
ATOM   5052  CZ  TYR C 186     -64.382  24.770   0.052  1.00 18.38           C  
ANISOU 5052  CZ  TYR C 186     2435   2476   2074     91    -48    250       C  
ATOM   5053  OH  TYR C 186     -65.116  23.606   0.259  1.00 21.30           O  
ANISOU 5053  OH  TYR C 186     2793   2853   2449    110    -43    225       O  
ATOM   5054  N   GLU C 187     -62.216  28.567  -3.760  1.00 21.84           N  
ANISOU 5054  N   GLU C 187     2896   2956   2446      6    -74    371       N  
ATOM   5055  CA  GLU C 187     -62.908  28.309  -5.008  1.00 23.68           C  
ANISOU 5055  CA  GLU C 187     3119   3215   2663     19    -72    373       C  
ATOM   5056  C   GLU C 187     -61.994  27.893  -6.163  1.00 24.54           C  
ANISOU 5056  C   GLU C 187     3200   3378   2745      2    -63    383       C  
ATOM   5057  O   GLU C 187     -62.496  27.390  -7.175  1.00 26.01           O  
ANISOU 5057  O   GLU C 187     3372   3594   2919     16    -59    378       O  
ATOM   5058  CB  GLU C 187     -63.730  29.553  -5.392  1.00 23.84           C  
ANISOU 5058  CB  GLU C 187     3170   3205   2682     20    -91    396       C  
ATOM   5059  CG  GLU C 187     -64.842  29.828  -4.385  1.00 25.81           C  
ANISOU 5059  CG  GLU C 187     3442   3409   2955     46   -100    379       C  
ATOM   5060  CD  GLU C 187     -65.539  31.167  -4.586  1.00 28.77           C  
ANISOU 5060  CD  GLU C 187     3851   3748   3331     49   -122    400       C  
ATOM   5061  OE1 GLU C 187     -64.959  32.097  -5.194  1.00 30.42           O  
ANISOU 5061  OE1 GLU C 187     4075   3955   3528     23   -134    432       O  
ATOM   5062  OE2 GLU C 187     -66.687  31.285  -4.120  1.00 29.63           O  
ANISOU 5062  OE2 GLU C 187     3973   3833   3453     78   -129    383       O  
ATOM   5063  N   LYS C 188     -60.680  28.066  -6.004  1.00 24.37           N  
ANISOU 5063  N   LYS C 188     3170   3375   2715    -28    -60    395       N  
ATOM   5064  CA  LYS C 188     -59.718  27.700  -7.086  1.00 24.94           C  
ANISOU 5064  CA  LYS C 188     3211   3507   2758    -45    -51    404       C  
ATOM   5065  C   LYS C 188     -59.286  26.229  -7.092  1.00 25.10           C  
ANISOU 5065  C   LYS C 188     3197   3566   2774    -27    -36    370       C  
ATOM   5066  O   LYS C 188     -58.525  25.792  -7.979  1.00 25.70           O  
ANISOU 5066  O   LYS C 188     3245   3697   2825    -35    -29    371       O  
ATOM   5067  CB  LYS C 188     -58.472  28.579  -7.009  1.00 25.68           C  
ANISOU 5067  CB  LYS C 188     3308   3610   2840    -87    -56    433       C  
ATOM   5068  CG  LYS C 188     -58.690  30.074  -7.156  1.00 26.86           C  
ANISOU 5068  CG  LYS C 188     3492   3724   2988   -112    -75    471       C  
ATOM   5069  CD  LYS C 188     -57.378  30.764  -6.826  1.00 32.94           C  
ANISOU 5069  CD  LYS C 188     4264   4502   3749   -155    -79    494       C  
ATOM   5070  CE  LYS C 188     -57.395  32.289  -7.034  1.00 34.27           C  
ANISOU 5070  CE  LYS C 188     4469   4638   3914   -187   -101    536       C  
ATOM   5071  NZ  LYS C 188     -58.076  33.035  -5.913  1.00 34.56           N  
ANISOU 5071  NZ  LYS C 188     4546   4603   3981   -176   -118    534       N  
ATOM   5072  N   HIS C 189     -59.721  25.475  -6.087  1.00 23.82           N  
ANISOU 5072  N   HIS C 189     3038   3376   2635     -3    -33    341       N  
ATOM   5073  CA  HIS C 189     -59.279  24.067  -5.944  1.00 24.39           C  
ANISOU 5073  CA  HIS C 189     3083   3477   2706     14    -23    309       C  
ATOM   5074  C   HIS C 189     -60.417  23.077  -5.823  1.00 24.32           C  
ANISOU 5074  C   HIS C 189     3074   3455   2711     48    -21    280       C  
ATOM   5075  O   HIS C 189     -61.539  23.443  -5.434  1.00 25.68           O  
ANISOU 5075  O   HIS C 189     3268   3589   2900     59    -27    281       O  
ATOM   5076  CB  HIS C 189     -58.339  23.947  -4.746  1.00 23.75           C  
ANISOU 5076  CB  HIS C 189     3002   3384   2637      3    -20    300       C  
ATOM   5077  CG  HIS C 189     -57.211  24.920  -4.774  1.00 25.08           C  
ANISOU 5077  CG  HIS C 189     3171   3566   2792    -33    -22    328       C  
ATOM   5078  ND1 HIS C 189     -57.236  26.114  -4.086  1.00 29.01           N  
ANISOU 5078  ND1 HIS C 189     3698   4022   3302    -53    -31    351       N  
ATOM   5079  CD2 HIS C 189     -56.038  24.895  -5.450  1.00 24.79           C  
ANISOU 5079  CD2 HIS C 189     3109   3582   2729    -53    -18    337       C  
ATOM   5080  CE1 HIS C 189     -56.112  26.772  -4.317  1.00 27.77           C  
ANISOU 5080  CE1 HIS C 189     3535   3889   3128    -88    -33    375       C  
ATOM   5081  NE2 HIS C 189     -55.364  26.045  -5.130  1.00 29.21           N  
ANISOU 5081  NE2 HIS C 189     3682   4130   3285    -89    -23    367       N  
ATOM   5082  N   LYS C 190     -60.133  21.809  -6.111  1.00 23.95           N  
ANISOU 5082  N   LYS C 190     3003   3440   2658     65    -16    253       N  
ATOM   5083  CA  LYS C 190     -61.151  20.775  -6.081  1.00 25.33           C  
ANISOU 5083  CA  LYS C 190     3176   3604   2843     94    -17    227       C  
ATOM   5084  C   LYS C 190     -61.040  19.890  -4.839  1.00 24.44           C  
ANISOU 5084  C   LYS C 190     3067   3469   2751    104    -17    201       C  
ATOM   5085  O   LYS C 190     -62.012  19.749  -4.095  1.00 24.35           O  
ANISOU 5085  O   LYS C 190     3072   3421   2759    115    -20    193       O  
ATOM   5086  CB  LYS C 190     -61.041  19.898  -7.329  1.00 25.79           C  
ANISOU 5086  CB  LYS C 190     3208   3711   2880    108    -14    212       C  
ATOM   5087  CG  LYS C 190     -62.123  18.826  -7.430  1.00 29.41           C  
ANISOU 5087  CG  LYS C 190     3666   4161   3348    136    -17    186       C  
ATOM   5088  CD  LYS C 190     -61.666  17.665  -8.313  1.00 35.00           C  
ANISOU 5088  CD  LYS C 190     4346   4913   4038    153    -17    162       C  
ATOM   5089  CE  LYS C 190     -62.670  16.518  -8.281  1.00 37.31           C  
ANISOU 5089  CE  LYS C 190     4642   5193   4343    178    -23    134       C  
ATOM   5090  NZ  LYS C 190     -62.098  15.271  -8.898  1.00 42.62           N  
ANISOU 5090  NZ  LYS C 190     5291   5901   5001    197    -27    106       N  
ATOM   5091  N   VAL C 191     -59.866  19.296  -4.654  1.00 24.20           N  
ANISOU 5091  N   VAL C 191     3019   3461   2713    102    -14    189       N  
ATOM   5092  CA  VAL C 191     -59.678  18.302  -3.604  1.00 23.69           C  
ANISOU 5092  CA  VAL C 191     2957   3380   2666    113    -17    163       C  
ATOM   5093  C   VAL C 191     -59.004  18.846  -2.345  1.00 22.87           C  
ANISOU 5093  C   VAL C 191     2864   3250   2575     96    -16    171       C  
ATOM   5094  O   VAL C 191     -57.893  19.394  -2.379  1.00 23.67           O  
ANISOU 5094  O   VAL C 191     2958   3371   2665     78    -13    183       O  
ATOM   5095  CB  VAL C 191     -58.867  17.088  -4.107  1.00 24.22           C  
ANISOU 5095  CB  VAL C 191     2998   3486   2717    129    -18    137       C  
ATOM   5096  CG1 VAL C 191     -58.805  16.000  -3.033  1.00 24.50           C  
ANISOU 5096  CG1 VAL C 191     3040   3498   2771    142    -24    110       C  
ATOM   5097  CG2 VAL C 191     -59.477  16.533  -5.407  1.00 25.60           C  
ANISOU 5097  CG2 VAL C 191     3160   3690   2878    146    -20    128       C  
ATOM   5098  N   TYR C 192     -59.687  18.641  -1.226  1.00 21.60           N  
ANISOU 5098  N   TYR C 192     2722   3048   2437    103    -19    162       N  
ATOM   5099  CA  TYR C 192     -59.207  19.075   0.076  1.00 21.47           C  
ANISOU 5099  CA  TYR C 192     2718   3003   2435     90    -19    166       C  
ATOM   5100  C   TYR C 192     -59.003  17.851   0.954  1.00 20.31           C  
ANISOU 5100  C   TYR C 192     2570   2848   2301    103    -22    139       C  
ATOM   5101  O   TYR C 192     -59.896  17.030   1.094  1.00 21.84           O  
ANISOU 5101  O   TYR C 192     2767   3028   2502    118    -26    123       O  
ATOM   5102  CB  TYR C 192     -60.205  20.038   0.713  1.00 20.72           C  
ANISOU 5102  CB  TYR C 192     2648   2868   2357     85    -21    180       C  
ATOM   5103  CG  TYR C 192     -60.157  21.395   0.045  1.00 19.64           C  
ANISOU 5103  CG  TYR C 192     2518   2734   2210     69    -22    209       C  
ATOM   5104  CD1 TYR C 192     -60.881  21.644  -1.136  1.00 20.47           C  
ANISOU 5104  CD1 TYR C 192     2622   2854   2303     74    -23    219       C  
ATOM   5105  CD2 TYR C 192     -59.313  22.387   0.517  1.00 18.34           C  
ANISOU 5105  CD2 TYR C 192     2362   2560   2046     45    -23    228       C  
ATOM   5106  CE1 TYR C 192     -60.799  22.888  -1.762  1.00 19.80           C  
ANISOU 5106  CE1 TYR C 192     2545   2769   2207     58    -26    247       C  
ATOM   5107  CE2 TYR C 192     -59.225  23.612  -0.080  1.00 19.23           C  
ANISOU 5107  CE2 TYR C 192     2485   2674   2150     27    -27    256       C  
ATOM   5108  CZ  TYR C 192     -59.944  23.847  -1.262  1.00 18.62           C  
ANISOU 5108  CZ  TYR C 192     2406   2608   2059     33    -29    267       C  
ATOM   5109  OH  TYR C 192     -59.777  25.095  -1.831  1.00 20.88           O  
ANISOU 5109  OH  TYR C 192     2705   2893   2336     12    -35    297       O  
ATOM   5110  N   ALA C 193     -57.796  17.714   1.486  1.00 20.49           N  
ANISOU 5110  N   ALA C 193     2584   2879   2321     95    -21    135       N  
ATOM   5111  CA  ALA C 193     -57.444  16.482   2.214  1.00 20.14           C  
ANISOU 5111  CA  ALA C 193     2537   2831   2285    109    -26    108       C  
ATOM   5112  C   ALA C 193     -56.591  16.772   3.431  1.00 20.84           C  
ANISOU 5112  C   ALA C 193     2632   2904   2383     97    -25    110       C  
ATOM   5113  O   ALA C 193     -55.747  17.660   3.402  1.00 21.68           O  
ANISOU 5113  O   ALA C 193     2733   3023   2481     79    -20    126       O  
ATOM   5114  CB  ALA C 193     -56.744  15.495   1.282  1.00 21.45           C  
ANISOU 5114  CB  ALA C 193     2680   3038   2431    125    -30     89       C  
ATOM   5115  N   CYS C 194     -56.900  16.070   4.520  1.00 20.44           N  
ANISOU 5115  N   CYS C 194     2592   2825   2349    104    -31     95       N  
ATOM   5116  CA ACYS C 194     -56.013  16.085   5.676  0.50 20.29           C  
ANISOU 5116  CA ACYS C 194     2577   2795   2339     97    -31     92       C  
ATOM   5117  CA BCYS C 194     -56.145  16.078   5.741  0.50 20.99           C  
ANISOU 5117  CA BCYS C 194     2667   2879   2429     97    -31     92       C  
ATOM   5118  C   CYS C 194     -55.504  14.684   5.902  1.00 20.88           C  
ANISOU 5118  C   CYS C 194     2645   2878   2413    115    -40     65       C  
ATOM   5119  O   CYS C 194     -56.249  13.706   5.920  1.00 21.55           O  
ANISOU 5119  O   CYS C 194     2736   2950   2504    129    -49     50       O  
ATOM   5120  CB ACYS C 194     -56.594  16.705   6.964  0.50 20.08           C  
ANISOU 5120  CB ACYS C 194     2571   2728   2332     86    -30    101       C  
ATOM   5121  CB BCYS C 194     -57.133  16.320   6.870  0.50 21.06           C  
ANISOU 5121  CB BCYS C 194     2697   2847   2459     94    -33     96       C  
ATOM   5122  SG ACYS C 194     -58.001  15.871   7.706  0.50 18.66           S  
ANISOU 5122  SG ACYS C 194     2406   2515   2168     98    -37     89       S  
ATOM   5123  SG BCYS C 194     -56.429  16.240   8.448  0.50 24.07           S  
ANISOU 5123  SG BCYS C 194     3086   3206   2853     86    -34     90       S  
ATOM   5124  N   GLU C 195     -54.182  14.614   6.003  1.00 20.68           N  
ANISOU 5124  N   GLU C 195     2605   2875   2377    113    -39     59       N  
ATOM   5125  CA  GLU C 195     -53.449  13.343   6.195  1.00 19.89           C  
ANISOU 5125  CA  GLU C 195     2497   2787   2273    132    -50     32       C  
ATOM   5126  C   GLU C 195     -52.867  13.288   7.600  1.00 19.80           C  
ANISOU 5126  C   GLU C 195     2495   2754   2275    126    -53     28       C  
ATOM   5127  O   GLU C 195     -52.118  14.187   7.996  1.00 21.11           O  
ANISOU 5127  O   GLU C 195     2656   2926   2438    109    -44     41       O  
ATOM   5128  CB  GLU C 195     -52.282  13.226   5.217  1.00 21.10           C  
ANISOU 5128  CB  GLU C 195     2623   2992   2401    139    -49     23       C  
ATOM   5129  CG  GLU C 195     -51.457  11.942   5.406  1.00 23.96           C  
ANISOU 5129  CG  GLU C 195     2976   3369   2758    164    -63     -8       C  
ATOM   5130  CD  GLU C 195     -50.118  12.020   4.726  1.00 30.70           C  
ANISOU 5130  CD  GLU C 195     3801   4279   3586    167    -61    -17       C  
ATOM   5131  OE1 GLU C 195     -49.284  12.871   5.141  1.00 34.34           O  
ANISOU 5131  OE1 GLU C 195     4254   4753   4042    147    -51     -3       O  
ATOM   5132  OE2 GLU C 195     -49.925  11.236   3.768  1.00 31.99           O  
ANISOU 5132  OE2 GLU C 195     3948   4474   3732    190    -69    -37       O  
ATOM   5133  N   VAL C 196     -53.178  12.206   8.309  1.00 19.45           N  
ANISOU 5133  N   VAL C 196     2464   2685   2243    140    -65     10       N  
ATOM   5134  CA  VAL C 196     -52.791  12.074   9.706  1.00 18.20           C  
ANISOU 5134  CA  VAL C 196     2316   2502   2097    135    -69      7       C  
ATOM   5135  C   VAL C 196     -51.803  10.929   9.922  1.00 18.59           C  
ANISOU 5135  C   VAL C 196     2359   2563   2140    155    -83    -19       C  
ATOM   5136  O   VAL C 196     -52.084   9.779   9.548  1.00 19.76           O  
ANISOU 5136  O   VAL C 196     2512   2710   2288    175    -99    -38       O  
ATOM   5137  CB  VAL C 196     -54.045  11.831  10.570  1.00 17.74           C  
ANISOU 5137  CB  VAL C 196     2281   2402   2058    131    -73     11       C  
ATOM   5138  CG1 VAL C 196     -53.673  11.576  12.033  1.00 17.70           C  
ANISOU 5138  CG1 VAL C 196     2287   2372   2065    126    -78      7       C  
ATOM   5139  CG2 VAL C 196     -54.991  13.038  10.510  1.00 19.13           C  
ANISOU 5139  CG2 VAL C 196     2463   2566   2240    114    -61     35       C  
ATOM   5140  N   THR C 197     -50.684  11.268  10.569  1.00 19.25           N  
ANISOU 5140  N   THR C 197     2435   2656   2221    149    -80    -19       N  
ATOM   5141  CA  THR C 197     -49.675  10.290  10.968  1.00 18.49           C  
ANISOU 5141  CA  THR C 197     2335   2571   2121    168    -94    -44       C  
ATOM   5142  C   THR C 197     -49.676  10.225  12.496  1.00 17.69           C  
ANISOU 5142  C   THR C 197     2252   2433   2038    160    -97    -41       C  
ATOM   5143  O   THR C 197     -49.619  11.234  13.164  1.00 18.75           O  
ANISOU 5143  O   THR C 197     2388   2557   2178    138    -84    -23       O  
ATOM   5144  CB  THR C 197     -48.280  10.632  10.422  1.00 18.68           C  
ANISOU 5144  CB  THR C 197     2331   2645   2123    171    -88    -50       C  
ATOM   5145  OG1 THR C 197     -48.348  10.795   8.983  1.00 23.39           O  
ANISOU 5145  OG1 THR C 197     2909   3278   2701    175    -83    -49       O  
ATOM   5146  CG2 THR C 197     -47.350   9.471  10.684  1.00 20.69           C  
ANISOU 5146  CG2 THR C 197     2580   2912   2370    198   -106    -81       C  
ATOM   5147  N   HIS C 198     -49.767   9.009  13.023  1.00 17.18           N  
ANISOU 5147  N   HIS C 198     2202   2348   1980    177   -117    -60       N  
ATOM   5148  CA  HIS C 198     -49.843   8.823  14.488  1.00 16.64           C  
ANISOU 5148  CA  HIS C 198     2152   2244   1927    168   -122    -57       C  
ATOM   5149  C   HIS C 198     -49.452   7.369  14.787  1.00 17.96           C  
ANISOU 5149  C   HIS C 198     2329   2401   2093    193   -148    -83       C  
ATOM   5150  O   HIS C 198     -49.704   6.508  13.982  1.00 20.61           O  
ANISOU 5150  O   HIS C 198     2667   2741   2423    211   -163    -97       O  
ATOM   5151  CB  HIS C 198     -51.266   9.154  15.003  1.00 15.82           C  
ANISOU 5151  CB  HIS C 198     2067   2105   1839    150   -117    -38       C  
ATOM   5152  CG  HIS C 198     -51.432   8.884  16.462  1.00 15.27           C  
ANISOU 5152  CG  HIS C 198     2016   2003   1784    142   -124    -36       C  
ATOM   5153  ND1 HIS C 198     -51.207   9.821  17.441  1.00 20.69           N  
ANISOU 5153  ND1 HIS C 198     2702   2682   2477    124   -111    -23       N  
ATOM   5154  CD2 HIS C 198     -51.738   7.728  17.091  1.00 12.77           C  
ANISOU 5154  CD2 HIS C 198     1717   1662   1473    148   -144    -46       C  
ATOM   5155  CE1 HIS C 198     -51.394   9.262  18.626  1.00 12.99           C  
ANISOU 5155  CE1 HIS C 198     1743   1681   1512    121   -121    -25       C  
ATOM   5156  NE2 HIS C 198     -51.677   7.977  18.442  1.00 18.08           N  
ANISOU 5156  NE2 HIS C 198     2399   2314   2155    135   -142    -38       N  
ATOM   5157  N   GLN C 199     -48.879   7.118  15.971  1.00 18.51           N  
ANISOU 5157  N   GLN C 199     2408   2455   2170    192   -155    -87       N  
ATOM   5158  CA  GLN C 199     -48.387   5.782  16.331  1.00 20.45           C  
ANISOU 5158  CA  GLN C 199     2665   2690   2414    216   -183   -111       C  
ATOM   5159  C   GLN C 199     -49.471   4.708  16.323  1.00 20.46           C  
ANISOU 5159  C   GLN C 199     2691   2656   2424    221   -204   -114       C  
ATOM   5160  O   GLN C 199     -49.182   3.522  16.100  1.00 21.91           O  
ANISOU 5160  O   GLN C 199     2885   2835   2605    245   -231   -137       O  
ATOM   5161  CB  GLN C 199     -47.766   5.814  17.716  1.00 20.01           C  
ANISOU 5161  CB  GLN C 199     2618   2619   2367    210   -185   -110       C  
ATOM   5162  CG  GLN C 199     -47.116   4.488  18.086  1.00 22.09           C  
ANISOU 5162  CG  GLN C 199     2893   2872   2627    237   -215   -135       C  
ATOM   5163  CD  GLN C 199     -46.409   4.497  19.430  1.00 24.69           C  
ANISOU 5163  CD  GLN C 199     3229   3190   2963    233   -219   -136       C  
ATOM   5164  OE1 GLN C 199     -45.316   3.897  19.602  1.00 22.74           O  
ANISOU 5164  OE1 GLN C 199     2978   2955   2706    257   -235   -158       O  
ATOM   5165  NE2 GLN C 199     -47.020   5.133  20.391  1.00 27.27           N  
ANISOU 5165  NE2 GLN C 199     3565   3493   3302    205   -206   -113       N  
ATOM   5166  N   GLY C 200     -50.712   5.087  16.587  1.00 19.91           N  
ANISOU 5166  N   GLY C 200     2633   2564   2366    197   -195    -93       N  
ATOM   5167  CA  GLY C 200     -51.820   4.129  16.573  1.00 20.31           C  
ANISOU 5167  CA  GLY C 200     2707   2585   2424    196   -214    -94       C  
ATOM   5168  C   GLY C 200     -52.264   3.721  15.168  1.00 21.19           C  
ANISOU 5168  C   GLY C 200     2814   2711   2528    211   -220   -104       C  
ATOM   5169  O   GLY C 200     -53.075   2.800  14.983  1.00 21.16           O  
ANISOU 5169  O   GLY C 200     2827   2685   2527    213   -240   -108       O  
ATOM   5170  N   LEU C 201     -51.713   4.390  14.167  1.00 22.85           N  
ANISOU 5170  N   LEU C 201     2998   2958   2725    220   -205   -107       N  
ATOM   5171  CA  LEU C 201     -52.086   4.146  12.776  1.00 24.54           C  
ANISOU 5171  CA  LEU C 201     3203   3192   2929    233   -207   -116       C  
ATOM   5172  C   LEU C 201     -50.930   3.483  12.028  1.00 26.41           C  
ANISOU 5172  C   LEU C 201     3426   3459   3150    267   -222   -145       C  
ATOM   5173  O   LEU C 201     -49.854   4.061  11.912  1.00 27.75           O  
ANISOU 5173  O   LEU C 201     3573   3662   3308    272   -210   -149       O  
ATOM   5174  CB  LEU C 201     -52.456   5.471  12.086  1.00 23.37           C  
ANISOU 5174  CB  LEU C 201     3035   3067   2776    217   -178    -95       C  
ATOM   5175  CG  LEU C 201     -53.639   6.270  12.667  1.00 22.93           C  
ANISOU 5175  CG  LEU C 201     2991   2989   2735    189   -162    -69       C  
ATOM   5176  CD1 LEU C 201     -53.742   7.657  12.000  1.00 21.98           C  
ANISOU 5176  CD1 LEU C 201     2851   2892   2608    176   -136    -50       C  
ATOM   5177  CD2 LEU C 201     -54.937   5.509  12.536  1.00 24.48           C  
ANISOU 5177  CD2 LEU C 201     3204   3159   2937    186   -175    -68       C  
ATOM   5178  N   SER C 202     -51.157   2.265  11.542  1.00 28.75           N  
ANISOU 5178  N   SER C 202     3734   3744   3444    289   -250   -166       N  
ATOM   5179  CA  SER C 202     -50.107   1.494  10.876  1.00 30.24           C  
ANISOU 5179  CA  SER C 202     3912   3960   3617    326   -270   -199       C  
ATOM   5180  C   SER C 202     -49.636   2.153   9.590  1.00 30.94           C  
ANISOU 5180  C   SER C 202     3966   4103   3685    336   -252   -204       C  
ATOM   5181  O   SER C 202     -48.502   1.915   9.141  1.00 31.97           O  
ANISOU 5181  O   SER C 202     4077   4272   3798    362   -259   -228       O  
ATOM   5182  CB  SER C 202     -50.571   0.064  10.588  1.00 30.85           C  
ANISOU 5182  CB  SER C 202     4014   4010   3697    347   -307   -221       C  
ATOM   5183  OG  SER C 202     -51.580   0.068   9.595  1.00 33.26           O  
ANISOU 5183  OG  SER C 202     4318   4318   4002    343   -304   -216       O  
ATOM   5184  N   SER C 203     -50.509   2.963   8.984  1.00 30.47           N  
ANISOU 5184  N   SER C 203     3899   4050   3627    315   -230   -182       N  
ATOM   5185  CA  SER C 203     -50.106   3.844   7.886  1.00 30.58           C  
ANISOU 5185  CA  SER C 203     3882   4116   3623    315   -208   -177       C  
ATOM   5186  C   SER C 203     -50.982   5.117   7.951  1.00 28.82           C  
ANISOU 5186  C   SER C 203     3658   3885   3408    280   -180   -142       C  
ATOM   5187  O   SER C 203     -52.065   5.062   8.536  1.00 27.87           O  
ANISOU 5187  O   SER C 203     3560   3723   3305    263   -181   -127       O  
ATOM   5188  CB  SER C 203     -50.199   3.113   6.537  1.00 31.09           C  
ANISOU 5188  CB  SER C 203     3935   4206   3671    343   -223   -201       C  
ATOM   5189  OG  SER C 203     -51.461   3.246   5.909  1.00 34.96           O  
ANISOU 5189  OG  SER C 203     4433   4684   4168    332   -217   -187       O  
ATOM   5190  N   PRO C 204     -50.512   6.250   7.369  1.00 27.90           N  
ANISOU 5190  N   PRO C 204     3517   3807   3278    268   -156   -127       N  
ATOM   5191  CA  PRO C 204     -51.278   7.497   7.526  1.00 26.97           C  
ANISOU 5191  CA  PRO C 204     3401   3676   3169    236   -133    -94       C  
ATOM   5192  C   PRO C 204     -52.692   7.416   6.953  1.00 26.20           C  
ANISOU 5192  C   PRO C 204     3316   3561   3079    232   -133    -85       C  
ATOM   5193  O   PRO C 204     -52.913   6.814   5.879  1.00 26.92           O  
ANISOU 5193  O   PRO C 204     3399   3669   3158    250   -142   -100       O  
ATOM   5194  CB  PRO C 204     -50.445   8.539   6.779  1.00 27.23           C  
ANISOU 5194  CB  PRO C 204     3406   3758   3182    227   -114    -84       C  
ATOM   5195  CG  PRO C 204     -49.035   7.956   6.747  1.00 28.60           C  
ANISOU 5195  CG  PRO C 204     3562   3967   3340    248   -124   -110       C  
ATOM   5196  CD  PRO C 204     -49.237   6.473   6.647  1.00 28.94           C  
ANISOU 5196  CD  PRO C 204     3617   3995   3385    280   -151   -140       C  
ATOM   5197  N   VAL C 205     -53.622   8.074   7.642  1.00 24.30           N  
ANISOU 5197  N   VAL C 205     3091   3288   2854    209   -122    -62       N  
ATOM   5198  CA  VAL C 205     -55.029   8.094   7.292  1.00 24.16           C  
ANISOU 5198  CA  VAL C 205     3084   3251   2843    202   -121    -52       C  
ATOM   5199  C   VAL C 205     -55.325   9.429   6.652  1.00 23.70           C  
ANISOU 5199  C   VAL C 205     3014   3211   2779    186    -99    -29       C  
ATOM   5200  O   VAL C 205     -54.927  10.469   7.185  1.00 23.83           O  
ANISOU 5200  O   VAL C 205     3029   3228   2799    169    -86    -12       O  
ATOM   5201  CB  VAL C 205     -55.909   7.917   8.558  1.00 23.86           C  
ANISOU 5201  CB  VAL C 205     3071   3169   2826    187   -125    -43       C  
ATOM   5202  CG1 VAL C 205     -57.378   8.327   8.308  1.00 25.93           C  
ANISOU 5202  CG1 VAL C 205     3340   3418   3093    175   -118    -27       C  
ATOM   5203  CG2 VAL C 205     -55.804   6.477   9.067  1.00 24.41           C  
ANISOU 5203  CG2 VAL C 205     3156   3218   2901    201   -151    -64       C  
ATOM   5204  N   THR C 206     -55.995   9.400   5.498  1.00 22.84           N  
ANISOU 5204  N   THR C 206     2899   3117   2662    193    -98    -28       N  
ATOM   5205  CA  THR C 206     -56.382  10.638   4.802  1.00 23.54           C  
ANISOU 5205  CA  THR C 206     2979   3220   2743    179    -80     -5       C  
ATOM   5206  C   THR C 206     -57.894  10.741   4.774  1.00 22.79           C  
ANISOU 5206  C   THR C 206     2898   3101   2659    173    -79      5       C  
ATOM   5207  O   THR C 206     -58.590   9.768   4.485  1.00 23.89           O  
ANISOU 5207  O   THR C 206     3043   3232   2800    185    -92     -9       O  
ATOM   5208  CB  THR C 206     -55.855  10.675   3.356  1.00 23.61           C  
ANISOU 5208  CB  THR C 206     2964   3275   2730    190    -78    -10       C  
ATOM   5209  OG1 THR C 206     -54.431  10.630   3.382  1.00 26.59           O  
ANISOU 5209  OG1 THR C 206     3325   3683   3095    194    -78    -20       O  
ATOM   5210  CG2 THR C 206     -56.284  11.959   2.647  1.00 25.62           C  
ANISOU 5210  CG2 THR C 206     3213   3543   2978    173    -62     16       C  
ATOM   5211  N   LYS C 207     -58.412  11.921   5.110  1.00 20.98           N  
ANISOU 5211  N   LYS C 207     2675   2860   2436    156    -66     28       N  
ATOM   5212  CA  LYS C 207     -59.810  12.231   4.918  1.00 21.73           C  
ANISOU 5212  CA  LYS C 207     2780   2941   2537    152    -64     38       C  
ATOM   5213  C   LYS C 207     -59.853  13.376   3.949  1.00 21.88           C  
ANISOU 5213  C   LYS C 207     2789   2981   2545    146    -52     56       C  
ATOM   5214  O   LYS C 207     -59.058  14.322   4.025  1.00 22.10           O  
ANISOU 5214  O   LYS C 207     2813   3017   2569    135    -44     70       O  
ATOM   5215  CB  LYS C 207     -60.548  12.554   6.217  1.00 21.58           C  
ANISOU 5215  CB  LYS C 207     2778   2888   2535    140    -62     46       C  
ATOM   5216  CG  LYS C 207     -60.588  11.375   7.229  1.00 23.23           C  
ANISOU 5216  CG  LYS C 207     2997   3076   2754    142    -76     30       C  
ATOM   5217  CD  LYS C 207     -61.427  10.170   6.772  1.00 24.87           C  
ANISOU 5217  CD  LYS C 207     3209   3280   2961    151    -90     16       C  
ATOM   5218  CE  LYS C 207     -61.355   9.051   7.804  1.00 28.50           C  
ANISOU 5218  CE  LYS C 207     3682   3716   3429    149   -106      4       C  
ATOM   5219  NZ  LYS C 207     -61.951   7.786   7.292  1.00 28.59           N  
ANISOU 5219  NZ  LYS C 207     3700   3725   3439    158   -124    -11       N  
ATOM   5220  N   SER C 208     -60.749  13.256   2.992  1.00 21.82           N  
ANISOU 5220  N   SER C 208     2778   2981   2530    154    -53     56       N  
ATOM   5221  CA  SER C 208     -60.807  14.244   1.936  1.00 23.69           C  
ANISOU 5221  CA  SER C 208     3007   3240   2755    150    -44     73       C  
ATOM   5222  C   SER C 208     -62.221  14.489   1.493  1.00 22.97           C  
ANISOU 5222  C   SER C 208     2921   3140   2665    153    -43     80       C  
ATOM   5223  O   SER C 208     -63.118  13.696   1.788  1.00 23.25           O  
ANISOU 5223  O   SER C 208     2965   3162   2709    160    -50     68       O  
ATOM   5224  CB  SER C 208     -59.993  13.755   0.734  1.00 24.36           C  
ANISOU 5224  CB  SER C 208     3071   3366   2820    161    -45     63       C  
ATOM   5225  OG  SER C 208     -60.624  12.644   0.132  1.00 26.64           O  
ANISOU 5225  OG  SER C 208     3357   3660   3106    179    -55     44       O  
ATOM   5226  N   PHE C 209     -62.415  15.580   0.751  1.00 22.87           N  
ANISOU 5226  N   PHE C 209     2907   3139   2644    148    -36     99       N  
ATOM   5227  CA  PHE C 209     -63.668  15.816   0.049  1.00 22.97           C  
ANISOU 5227  CA  PHE C 209     2922   3152   2653    154    -36    104       C  
ATOM   5228  C   PHE C 209     -63.356  16.592  -1.226  1.00 23.70           C  
ANISOU 5228  C   PHE C 209     3005   3273   2728    152    -31    120       C  
ATOM   5229  O   PHE C 209     -62.285  17.217  -1.347  1.00 22.51           O  
ANISOU 5229  O   PHE C 209     2849   3135   2570    139    -27    133       O  
ATOM   5230  CB  PHE C 209     -64.684  16.600   0.901  1.00 21.51           C  
ANISOU 5230  CB  PHE C 209     2755   2937   2482    149    -35    114       C  
ATOM   5231  CG  PHE C 209     -64.237  17.992   1.272  1.00 20.36           C  
ANISOU 5231  CG  PHE C 209     2619   2780   2339    136    -31    136       C  
ATOM   5232  CD1 PHE C 209     -64.508  19.057   0.431  1.00 20.47           C  
ANISOU 5232  CD1 PHE C 209     2635   2800   2343    133    -29    155       C  
ATOM   5233  CD2 PHE C 209     -63.573  18.237   2.486  1.00 20.10           C  
ANISOU 5233  CD2 PHE C 209     2594   2727   2317    125    -30    137       C  
ATOM   5234  CE1 PHE C 209     -64.098  20.374   0.750  1.00 18.55           C  
ANISOU 5234  CE1 PHE C 209     2405   2542   2102    119    -30    176       C  
ATOM   5235  CE2 PHE C 209     -63.160  19.513   2.834  1.00 18.94           C  
ANISOU 5235  CE2 PHE C 209     2456   2567   2172    112    -29    156       C  
ATOM   5236  CZ  PHE C 209     -63.420  20.619   1.971  1.00 18.29           C  
ANISOU 5236  CZ  PHE C 209     2379   2488   2081    109    -30    176       C  
ATOM   5237  N   ASN C 210     -64.287  16.530  -2.180  1.00 23.97           N  
ANISOU 5237  N   ASN C 210     3035   3318   2754    162    -32    120       N  
ATOM   5238  CA  ASN C 210     -64.219  17.362  -3.366  1.00 25.68           C  
ANISOU 5238  CA  ASN C 210     3246   3559   2954    158    -28    139       C  
ATOM   5239  C   ASN C 210     -65.143  18.529  -3.177  1.00 26.82           C  
ANISOU 5239  C   ASN C 210     3407   3679   3104    154    -28    158       C  
ATOM   5240  O   ASN C 210     -66.311  18.325  -2.888  1.00 27.28           O  
ANISOU 5240  O   ASN C 210     3472   3721   3171    164    -31    150       O  
ATOM   5241  CB  ASN C 210     -64.666  16.601  -4.606  1.00 27.14           C  
ANISOU 5241  CB  ASN C 210     3415   3772   3124    174    -30    127       C  
ATOM   5242  CG  ASN C 210     -63.807  15.408  -4.903  1.00 29.76           C  
ANISOU 5242  CG  ASN C 210     3730   4129   3448    183    -33    104       C  
ATOM   5243  OD1 ASN C 210     -64.328  14.335  -5.228  1.00 34.24           O  
ANISOU 5243  OD1 ASN C 210     4292   4700   4015    199    -40     83       O  
ATOM   5244  ND2 ASN C 210     -62.494  15.566  -4.786  1.00 31.93           N  
ANISOU 5244  ND2 ASN C 210     3996   4421   3716    175    -30    107       N  
ATOM   5245  N   ARG C 211     -64.626  19.738  -3.327  1.00 28.20           N  
ANISOU 5245  N   ARG C 211     3588   3852   3273    139    -26    182       N  
ATOM   5246  CA  ARG C 211     -65.448  20.951  -3.212  1.00 30.12           C  
ANISOU 5246  CA  ARG C 211     3851   4072   3522    137    -30    201       C  
ATOM   5247  C   ARG C 211     -66.688  20.875  -4.108  1.00 32.05           C  
ANISOU 5247  C   ARG C 211     4094   4325   3760    153    -32    199       C  
ATOM   5248  O   ARG C 211     -66.582  20.548  -5.284  1.00 33.53           O  
ANISOU 5248  O   ARG C 211     4266   4543   3930    157    -30    199       O  
ATOM   5249  CB  ARG C 211     -64.611  22.222  -3.504  1.00 28.84           C  
ANISOU 5249  CB  ARG C 211     3696   3910   3350    116    -32    229       C  
ATOM   5250  CG  ARG C 211     -65.356  23.569  -3.376  1.00 29.11           C  
ANISOU 5250  CG  ARG C 211     3755   3915   3390    114    -41    249       C  
ATOM   5251  CD  ARG C 211     -64.466  24.757  -3.676  1.00 25.69           C  
ANISOU 5251  CD  ARG C 211     3332   3481   2948     90    -45    279       C  
ATOM   5252  NE  ARG C 211     -63.947  24.705  -5.044  1.00 30.11           N  
ANISOU 5252  NE  ARG C 211     3875   4081   3484     81    -42    292       N  
ATOM   5253  CZ  ARG C 211     -64.608  25.154  -6.092  1.00 29.27           C  
ANISOU 5253  CZ  ARG C 211     3771   3983   3365     86    -47    305       C  
ATOM   5254  NH1 ARG C 211     -64.054  25.034  -7.297  1.00 32.55           N  
ANISOU 5254  NH1 ARG C 211     4169   4441   3758     76    -43    316       N  
ATOM   5255  NH2 ARG C 211     -65.813  25.721  -5.921  1.00 30.93           N  
ANISOU 5255  NH2 ARG C 211     4003   4164   3585    101    -56    307       N  
ATOM   5256  N   GLY C 212     -67.863  21.134  -3.525  1.00 34.36           N  
ANISOU 5256  N   GLY C 212     4400   4593   4063    164    -37    194       N  
ATOM   5257  CA  GLY C 212     -69.108  21.247  -4.303  1.00 35.84           C  
ANISOU 5257  CA  GLY C 212     4587   4787   4243    180    -40    194       C  
ATOM   5258  C   GLY C 212     -69.885  19.955  -4.459  1.00 36.57           C  
ANISOU 5258  C   GLY C 212     4666   4893   4336    194    -38    169       C  
ATOM   5259  O   GLY C 212     -70.911  19.754  -3.793  1.00 37.59           O  
ANISOU 5259  O   GLY C 212     4800   5008   4473    202    -40    158       O  
TER    5260      GLY C 212                                                      
HETATM 5261  C1  EDO A   1     -37.732  42.623  81.328  1.00 22.26           C  
HETATM 5262  O1  EDO A   1     -38.432  42.459  80.081  1.00 21.78           O  
HETATM 5263  C2  EDO A   1     -38.685  42.421  82.492  1.00 21.56           C  
HETATM 5264  O2  EDO A   1     -39.221  41.093  82.431  1.00 20.09           O  
HETATM 5265  C1  EDO A   2     -34.343  21.719  84.919  1.00 35.22           C  
HETATM 5266  O1  EDO A   2     -34.651  20.653  85.829  1.00 33.97           O  
HETATM 5267  C2  EDO A   2     -33.469  22.746  85.617  1.00 37.26           C  
HETATM 5268  O2  EDO A   2     -32.230  22.120  85.962  1.00 38.46           O  
HETATM 5269  C1  EDO A   3     -38.466  15.897  80.103  1.00 23.15           C  
HETATM 5270  O1  EDO A   3     -38.510  15.693  81.518  1.00 22.75           O  
HETATM 5271  C2  EDO A   3     -38.719  14.575  79.391  1.00 23.55           C  
HETATM 5272  O2  EDO A   3     -37.623  13.692  79.656  1.00 23.77           O  
HETATM 5273  C1  EDO A   4     -45.081  19.449  62.432  1.00 30.67           C  
HETATM 5274  O1  EDO A   4     -43.693  19.219  62.115  1.00 33.46           O  
HETATM 5275  C2  EDO A   4     -45.416  20.936  62.350  1.00 30.15           C  
HETATM 5276  O2  EDO A   4     -44.971  21.461  61.090  1.00 25.69           O  
HETATM 5277  C1  EDO A   6     -55.258  38.872  83.555  1.00 30.81           C  
HETATM 5278  O1  EDO A   6     -56.539  38.209  83.612  1.00 25.54           O  
HETATM 5279  C2  EDO A   6     -55.430  40.361  83.292  1.00 31.16           C  
HETATM 5280  O2  EDO A   6     -56.708  40.536  82.675  1.00 33.37           O  
HETATM 5281  C1  EDO A   7     -54.470  24.891  65.699  1.00 29.71           C  
HETATM 5282  O1  EDO A   7     -53.687  24.550  66.870  1.00 24.76           O  
HETATM 5283  C2  EDO A   7     -54.668  26.402  65.501  1.00 30.26           C  
HETATM 5284  O2  EDO A   7     -55.539  26.954  66.494  1.00 33.77           O  
HETATM 5285 NA    NA A 245     -23.888  29.290  76.788  1.00 40.84          NA  
HETATM 5286 NA    NA A 246     -43.577  20.015  65.785  1.00 39.73          NA  
HETATM 5287 CL    CL A 247     -26.298  39.142  80.678  1.00 65.53          CL  
HETATM 5288  C1  EDO B 215     -44.503  36.722  56.401  1.00 23.77           C  
HETATM 5289  O1  EDO B 215     -43.360  35.858  56.562  1.00 27.92           O  
HETATM 5290  C2  EDO B 215     -45.182  36.490  55.041  1.00 23.45           C  
HETATM 5291  O2  EDO B 215     -45.266  35.091  54.712  1.00 17.47           O  
HETATM 5292  C1  EDO B 216     -61.443  48.920  41.361  1.00 40.91           C  
HETATM 5293  O1  EDO B 216     -61.943  49.431  40.122  1.00 41.35           O  
HETATM 5294  C2  EDO B 216     -61.605  47.402  41.420  1.00 39.41           C  
HETATM 5295  O2  EDO B 216     -62.338  46.899  40.295  1.00 41.99           O  
HETATM 5296  C1  EDO B 217     -74.707  19.355  35.404  1.00 43.14           C  
HETATM 5297  O1  EDO B 217     -74.864  20.687  34.897  1.00 42.85           O  
HETATM 5298  C2  EDO B 217     -74.795  18.307  34.291  1.00 43.58           C  
HETATM 5299  O2  EDO B 217     -74.736  18.922  33.003  1.00 43.25           O  
HETATM 5300 NA    NA B 218     -75.045   6.393   4.499  1.00 48.95          NA  
HETATM 5301 NA    NA B 219     -82.140  26.810  16.948  1.00 53.27          NA  
HETATM 5302  C1  EDO C  10     -45.005   8.239  17.689  1.00 32.63           C  
HETATM 5303  O1  EDO C  10     -45.066   9.566  18.222  1.00 37.88           O  
HETATM 5304  C2  EDO C  10     -44.931   7.363  18.903  1.00 32.77           C  
HETATM 5305  O2  EDO C  10     -46.001   7.880  19.688  1.00 28.46           O  
HETATM 5306 NA    NA C 213     -52.055  20.806  10.890  1.00 32.49          NA  
HETATM 5307  O   HOH A   8     -33.580  34.595  69.610  1.00 15.50           O  
HETATM 5308  O   HOH A   9     -40.809   8.835  75.865  1.00 18.52           O  
HETATM 5309  O   HOH A  12     -59.485  41.864  71.894  1.00 27.23           O  
HETATM 5310  O   HOH A  13     -45.345  46.622  76.424  1.00 16.70           O  
HETATM 5311  O   HOH A  14     -39.575  41.714  76.444  1.00 15.42           O  
HETATM 5312  O   HOH A  15     -39.015  34.382  66.624  1.00 17.53           O  
HETATM 5313  O   HOH A 149     -26.761  33.405  65.234  1.00 43.12           O  
HETATM 5314  O   HOH A 218     -24.734  23.428  77.061  1.00 27.55           O  
HETATM 5315  O   HOH A 248     -39.156  53.027  67.123  1.00 21.19           O  
HETATM 5316  O   HOH A 249     -36.449  43.116  64.134  1.00 22.96           O  
HETATM 5317  O   HOH A 250     -39.762  37.101  66.564  1.00 18.95           O  
HETATM 5318  O   HOH A 251     -48.492  50.305  81.173  1.00 40.00           O  
HETATM 5319  O   HOH A 252     -34.462  50.060  74.404  1.00 18.11           O  
HETATM 5320  O   HOH A 253     -37.976  46.174  80.526  1.00 23.12           O  
HETATM 5321  O   HOH A 254     -29.436  32.716  88.612  1.00 53.51           O  
HETATM 5322  O   HOH A 255     -28.795  39.604  72.522  1.00 18.16           O  
HETATM 5323  O   HOH A 256     -39.183  25.102  79.600  1.00 18.00           O  
HETATM 5324  O   HOH A 257     -33.013  29.838  84.274  1.00 19.01           O  
HETATM 5325  O   HOH A 258     -31.189  40.329  76.830  1.00 15.37           O  
HETATM 5326  O   HOH A 259     -28.899  29.129  82.849  1.00 37.51           O  
HETATM 5327  O   HOH A 260     -32.297  46.271  75.771  1.00 15.11           O  
HETATM 5328  O   HOH A 261     -28.834  34.609  83.943  1.00 24.67           O  
HETATM 5329  O   HOH A 262     -55.935  43.292  73.284  1.00 20.73           O  
HETATM 5330  O   HOH A 263     -30.373  38.730  74.652  1.00 16.97           O  
HETATM 5331  O   HOH A 264     -38.267  49.783  65.142  1.00 13.17           O  
HETATM 5332  O   HOH A 265     -41.428  24.506  90.028  1.00 23.10           O  
HETATM 5333  O   HOH A 266     -37.537  21.105  69.447  1.00 17.68           O  
HETATM 5334  O   HOH A 267     -55.059  43.061  70.843  1.00 25.06           O  
HETATM 5335  O   HOH A 268     -27.134  39.021  70.403  1.00 32.53           O  
HETATM 5336  O   HOH A 269     -29.305  26.568  73.811  1.00 25.10           O  
HETATM 5337  O   HOH A 270     -44.646  46.670  69.485  1.00 18.22           O  
HETATM 5338  O   HOH A 271     -59.075  42.549  66.728  1.00 30.29           O  
HETATM 5339  O   HOH A 272     -28.676  43.304  66.043  1.00 18.56           O  
HETATM 5340  O   HOH A 273     -33.328  32.764  94.472  1.00 30.54           O  
HETATM 5341  O   HOH A 274     -35.914  35.945  88.172  1.00 21.43           O  
HETATM 5342  O   HOH A 275     -30.545  18.417  69.245  1.00 28.17           O  
HETATM 5343  O   HOH A 276     -35.002  20.566  61.405  1.00 21.85           O  
HETATM 5344  O   HOH A 277     -31.971  11.266  83.237  1.00 38.16           O  
HETATM 5345  O   HOH A 278     -51.325  44.308  81.421  1.00 21.81           O  
HETATM 5346  O   HOH A 279     -34.018  25.386  56.190  1.00 22.25           O  
HETATM 5347  O   HOH A 280     -45.276  47.708  78.907  1.00 27.21           O  
HETATM 5348  O   HOH A 281     -32.976  34.636  91.457  1.00 33.98           O  
HETATM 5349  O   HOH A 282     -38.643  48.743  79.460  1.00 22.97           O  
HETATM 5350  O   HOH A 283     -33.817  39.179  60.553  1.00 29.34           O  
HETATM 5351  O   HOH A 284     -32.464  27.820  61.632  1.00 22.94           O  
HETATM 5352  O   HOH A 285     -41.937  43.288  91.956  1.00 28.70           O  
HETATM 5353  O   HOH A 286     -38.815  38.679  91.902  1.00 22.67           O  
HETATM 5354  O   HOH A 287     -30.931  36.145  60.538  1.00 28.82           O  
HETATM 5355  O   HOH A 288     -38.685  49.267  62.452  1.00 22.70           O  
HETATM 5356  O   HOH A 289     -27.012  40.963  65.610  1.00 31.36           O  
HETATM 5357  O   HOH A 290     -32.037  13.867  69.399  1.00 30.37           O  
HETATM 5358  O   HOH A 291     -56.150  45.178  77.707  1.00 32.22           O  
HETATM 5359  O   HOH A 292     -59.951  14.879  75.354  1.00 20.69           O  
HETATM 5360  O   HOH A 293     -47.006  26.144  79.327  1.00 19.83           O  
HETATM 5361  O   HOH A 294     -42.060  32.141  71.177  1.00 17.46           O  
HETATM 5362  O   HOH A 295     -26.800  43.696  67.906  1.00 19.55           O  
HETATM 5363  O   HOH A 296     -30.748  28.122  84.381  1.00 26.39           O  
HETATM 5364  O   HOH A 297     -59.148  39.372  66.240  1.00 34.59           O  
HETATM 5365  O   HOH A 298     -60.276  38.071  68.389  1.00 31.53           O  
HETATM 5366  O   HOH A 299     -30.570  32.633  85.142  1.00 26.37           O  
HETATM 5367  O   HOH A 300     -28.645  17.393  70.919  1.00 25.65           O  
HETATM 5368  O   HOH A 301     -58.172  41.924  74.120  1.00 24.50           O  
HETATM 5369  O   HOH A 302     -36.720  37.083  91.510  1.00 33.88           O  
HETATM 5370  O   HOH A 303     -38.286  45.900  61.810  1.00 28.36           O  
HETATM 5371  O   HOH A 304     -26.046  41.177  68.794  1.00 30.80           O  
HETATM 5372  O   HOH A 305     -27.992  29.635  74.441  1.00 31.04           O  
HETATM 5373  O   HOH A 306     -32.921  30.755  61.653  1.00 28.96           O  
HETATM 5374  O   HOH A 307     -44.892  45.977  80.789  1.00 34.44           O  
HETATM 5375  O   HOH A 308     -42.124  38.303  94.041  1.00 39.79           O  
HETATM 5376  O   HOH A 309     -41.781  51.685  72.471  1.00 27.35           O  
HETATM 5377  O   HOH A 310     -29.979  29.800  88.937  1.00 37.94           O  
HETATM 5378  O   HOH A 311     -47.013  47.644  74.559  1.00 29.48           O  
HETATM 5379  O   HOH A 312     -29.055  41.344  59.121  1.00 29.93           O  
HETATM 5380  O   HOH A 313     -31.059  11.448  79.659  1.00 36.69           O  
HETATM 5381  O   HOH A 314     -26.737  27.299  70.109  1.00 27.70           O  
HETATM 5382  O   HOH A 315     -28.102  42.149  79.749  1.00 30.79           O  
HETATM 5383  O   HOH A 316     -41.005   9.083  78.492  1.00 25.09           O  
HETATM 5384  O   HOH A 317     -32.381  43.446  77.054  0.50 14.25           O  
HETATM 5385  O   HOH A 318     -41.784  44.774  89.661  1.00 33.46           O  
HETATM 5386  O   HOH A 319     -35.977  43.071  61.579  1.00 19.41           O  
HETATM 5387  O   HOH A 320     -36.237  45.205  59.822  1.00 19.51           O  
HETATM 5388  O   HOH A 321     -46.673  49.939  78.999  1.00 24.91           O  
HETATM 5389  O   HOH A 322     -26.802  46.037  69.610  1.00 19.27           O  
HETATM 5390  O   HOH A 323     -43.577  46.761  90.327  1.00 26.95           O  
HETATM 5391  O   HOH A 324     -25.572  25.940  78.974  1.00 32.39           O  
HETATM 5392  O   HOH A 325     -33.207  42.974  61.234  1.00 20.35           O  
HETATM 5393  O   HOH A 326     -43.127  47.612  92.825  1.00 40.03           O  
HETATM 5394  O   HOH A 327     -49.378  41.245  68.000  1.00 20.77           O  
HETATM 5395  O   HOH A 328     -53.111  47.210  76.228  1.00 38.45           O  
HETATM 5396  O   HOH A 329     -40.053  33.970  94.798  1.00 42.16           O  
HETATM 5397  O   HOH A 330     -40.673  40.278  85.145  1.00 35.94           O  
HETATM 5398  O   HOH A 331     -40.932   2.321  74.633  1.00 39.97           O  
HETATM 5399  O   HOH A 332     -35.630  13.884  66.038  1.00 33.35           O  
HETATM 5400  O   HOH A 333     -29.055  28.111  65.277  1.00 30.93           O  
HETATM 5401  O   HOH A 334     -40.483  26.371  92.991  1.00 42.71           O  
HETATM 5402  O   HOH A 335     -40.831  19.975  57.808  1.00 32.57           O  
HETATM 5403  O   HOH A 336     -37.555  14.458  87.313  1.00 32.87           O  
HETATM 5404  O   HOH A 337     -34.978  50.446  76.825  1.00 33.45           O  
HETATM 5405  O   HOH A 338     -41.354   7.749  89.672  1.00 32.79           O  
HETATM 5406  O   HOH A 339     -25.548  33.702  76.720  1.00 36.46           O  
HETATM 5407  O   HOH A 340     -23.914  32.437  78.819  1.00 39.78           O  
HETATM 5408  O   HOH A 341     -30.754  43.198  84.529  1.00 32.07           O  
HETATM 5409  O   HOH A 342     -35.294  17.685  63.911  1.00 31.53           O  
HETATM 5410  O   HOH A 343     -34.626  13.231  68.605  1.00 26.40           O  
HETATM 5411  O   HOH A 344     -26.925  20.162  78.016  1.00 40.33           O  
HETATM 5412  O   HOH A 345     -43.436  44.568  63.055  1.00 37.10           O  
HETATM 5413  O   HOH A 346     -26.421  33.508  82.724  1.00 40.16           O  
HETATM 5414  O   HOH A 347     -39.830  15.163  62.608  1.00 40.51           O  
HETATM 5415  O   HOH A 348     -39.502  43.173  62.767  1.00 40.85           O  
HETATM 5416  O   HOH A 349     -60.692  27.820  72.641  1.00 29.06           O  
HETATM 5417  O   HOH A 350     -58.248  29.059  73.232  1.00 29.23           O  
HETATM 5418  O   HOH A 351     -32.596  23.830  90.015  1.00 36.04           O  
HETATM 5419  O   HOH A 352     -31.229  22.944  66.719  1.00 28.02           O  
HETATM 5420  O   HOH A 353     -45.630  43.747  81.306  1.00 38.10           O  
HETATM 5421  O   HOH A 354     -30.163  39.368  84.834  1.00 44.76           O  
HETATM 5422  O   HOH A 355     -41.424   7.636  86.171  1.00 42.86           O  
HETATM 5423  O   HOH A 356     -26.876  30.987  82.178  1.00 44.44           O  
HETATM 5424  O   HOH A 357     -31.015  37.545  86.566  1.00 45.17           O  
HETATM 5425  O   HOH A 358     -35.696  52.995  77.034  1.00 44.23           O  
HETATM 5426  O   HOH A 359     -25.352  36.514  75.397  1.00 30.95           O  
HETATM 5427  O   HOH A 360     -30.347  42.037  87.194  1.00 38.59           O  
HETATM 5428  O   HOH A 361     -49.682  22.811  63.084  1.00 34.90           O  
HETATM 5429  O   HOH A 362     -47.649  23.079  64.537  1.00 29.24           O  
HETATM 5430  O   HOH A 363     -48.137  24.144  66.837  1.00 35.31           O  
HETATM 5431  O   HOH A 364     -46.248  26.123  67.241  1.00 34.12           O  
HETATM 5432  O   HOH A 365     -27.257  38.340  75.706  1.00 39.70           O  
HETATM 5433  O   HOH A 366     -28.694  40.114  77.781  1.00 20.79           O  
HETATM 5434  O   HOH A 367     -24.770  36.112  72.880  1.00 37.69           O  
HETATM 5435  O   HOH A 368     -22.217  35.805  72.975  1.00 39.01           O  
HETATM 5436  O   HOH A 369     -21.736  33.428  74.526  1.00 27.39           O  
HETATM 5437  O   HOH A 370     -33.341  22.909  57.275  1.00 42.26           O  
HETATM 5438  O   HOH A 371     -24.592  24.589  74.343  1.00 31.01           O  
HETATM 5439  O   HOH A 372     -45.128  15.887  82.075  1.00 19.13           O  
HETATM 5440  O   HOH A 373     -42.140  15.654  79.657  1.00 22.78           O  
HETATM 5441  O   HOH A 374     -44.796  15.116  78.322  1.00 18.72           O  
HETATM 5442  O   HOH A 375     -26.108  33.282  71.801  1.00 42.36           O  
HETATM 5443  O   HOH A 376     -47.581  31.021  66.859  1.00 26.87           O  
HETATM 5444  O   HOH A 377     -43.239  23.362  74.101  1.00 15.06           O  
HETATM 5445  O   HOH A 378     -43.492  21.287  72.183  1.00 15.14           O  
HETATM 5446  O   HOH A 379     -44.814  37.888  62.475  1.00 35.57           O  
HETATM 5447  O   HOH A 380     -43.770  40.267  62.438  1.00 38.46           O  
HETATM 5448  O   HOH A 381     -43.330  34.377  92.786  1.00 23.48           O  
HETATM 5449  O   HOH A 382     -42.652  17.757  59.984  1.00 38.58           O  
HETATM 5450  O   HOH A 383     -57.252  28.647  98.493  1.00 43.89           O  
HETATM 5451  O   HOH A 384     -40.783  14.370  81.965  1.00 23.06           O  
HETATM 5452  O   HOH A 385     -39.964  30.272  55.034  1.00 16.17           O  
HETATM 5453  O   HOH A 386     -32.645  22.238  69.253  1.00 19.71           O  
HETATM 5454  O   HOH A 387     -34.209  34.888  67.019  1.00 17.53           O  
HETATM 5455  O   HOH A 388     -36.854  34.686  64.237  1.00 14.91           O  
HETATM 5456  O   HOH A 389     -35.838  44.073  84.221  1.00 26.64           O  
HETATM 5457  O   HOH A 390     -36.878  32.397  72.010  1.00 16.43           O  
HETATM 5458  O   HOH A 391     -52.252  47.535  78.368  1.00 35.01           O  
HETATM 5459  O   HOH A 405     -62.388  18.176  64.720  1.00 32.22           O  
HETATM 5460  O   HOH A 406     -31.472  22.442  82.704  1.00 46.21           O  
HETATM 5461  O   HOH A 408     -32.487  27.847  58.407  1.00 35.92           O  
HETATM 5462  O   HOH A 409     -35.222   5.351  80.687  1.00 39.59           O  
HETATM 5463  O   HOH A 411     -28.086  22.443  80.932  1.00 36.69           O  
HETATM 5464  O   HOH A 414     -29.059  27.385  93.208  1.00 36.56           O  
HETATM 5465  O   HOH A 416     -50.513  43.960  69.574  1.00 41.76           O  
HETATM 5466  O   HOH A 417     -53.381  42.760  82.526  1.00 40.96           O  
HETATM 5467  O   HOH A 419     -29.523  26.362  90.890  1.00 44.87           O  
HETATM 5468  O   HOH A 420     -53.032  45.065  70.776  1.00 36.31           O  
HETATM 5469  O   HOH A 422     -50.704  47.118  73.826  1.00 34.98           O  
HETATM 5470  O   HOH A 425     -44.122  40.960  87.745  1.00 25.54           O  
HETATM 5471  O   HOH A 426     -42.702  43.319  87.521  1.00 23.40           O  
HETATM 5472  O   HOH A 427     -44.106  44.614  85.072  1.00 25.27           O  
HETATM 5473  O   HOH A 428     -47.236  46.311  82.888  1.00 32.98           O  
HETATM 5474  O   HOH A 429     -48.981  48.302  82.712  1.00 29.99           O  
HETATM 5475  O   HOH A 430     -45.259  46.516  86.736  1.00 20.59           O  
HETATM 5476  O   HOH A 431     -46.204  39.858  84.199  1.00 24.88           O  
HETATM 5477  O   HOH A 432     -48.809  42.138  93.073  1.00 26.02           O  
HETATM 5478  O   HOH A 433     -47.887  39.487  93.763  1.00 19.50           O  
HETATM 5479  O   HOH A 434     -49.654  37.331  92.951  1.00 27.03           O  
HETATM 5480  O   HOH A 435     -48.571  33.142  87.488  1.00 17.80           O  
HETATM 5481  O   HOH A 436     -47.847  27.003  91.798  1.00 27.41           O  
HETATM 5482  O   HOH A 437     -47.837  24.783  90.263  1.00 22.94           O  
HETATM 5483  O   HOH A 438     -45.986  23.448  92.473  1.00 31.33           O  
HETATM 5484  O   HOH A 439     -50.153  22.576  92.313  1.00 24.11           O  
HETATM 5485  O   HOH A 440     -49.287  20.201  93.068  1.00 23.37           O  
HETATM 5486  O   HOH A 441     -47.865  10.231  93.134  1.00 34.97           O  
HETATM 5487  O   HOH A 442     -45.708   7.774  90.939  1.00 31.78           O  
HETATM 5488  O   HOH A 443     -44.998   8.785  85.404  1.00 23.27           O  
HETATM 5489  O   HOH A 444     -38.215   7.622  76.667  1.00 37.41           O  
HETATM 5490  O   HOH A 445     -51.428   6.452  80.997  1.00 44.07           O  
HETATM 5491  O   HOH A 446     -51.546   7.009  83.804  1.00 32.56           O  
HETATM 5492  O   HOH A 447     -58.649  15.832  86.981  1.00 30.34           O  
HETATM 5493  O   HOH A 448     -60.382  18.616  87.781  1.00 28.49           O  
HETATM 5494  O   HOH A 449     -30.930  29.226  99.040  1.00 23.64           O  
HETATM 5495  O   HOH A 450     -33.531  29.754  99.424  1.00 31.57           O  
HETATM 5496  O   HOH A 451     -48.623  37.032  72.634  1.00 18.90           O  
HETATM 5497  O   HOH A 452     -50.029  37.155  75.221  1.00 17.18           O  
HETATM 5498  O   HOH A 453     -52.362  38.286  89.055  1.00 27.69           O  
HETATM 5499  O   HOH A 454     -47.423  32.070  93.017  1.00 21.49           O  
HETATM 5500  O   HOH A 455     -45.401  29.270  93.358  1.00 25.09           O  
HETATM 5501  O   HOH A 456     -45.239  26.659  93.999  1.00 34.29           O  
HETATM 5502  O   HOH A 457     -51.983  26.050  94.843  1.00 35.06           O  
HETATM 5503  O   HOH A 458     -52.024  23.737  94.054  1.00 30.39           O  
HETATM 5504  O   HOH A 459     -51.480  19.229  94.631  1.00 35.08           O  
HETATM 5505  O   HOH A 460     -49.642  12.508  92.720  1.00 27.37           O  
HETATM 5506  O   HOH A 462     -46.035  13.142  67.585  1.00 32.71           O  
HETATM 5507  O   HOH A 463     -51.005  10.665  68.976  1.00 38.18           O  
HETATM 5508  O   HOH A 464     -50.003   6.773  71.657  1.00 41.09           O  
HETATM 5509  O   HOH A 465     -56.147  13.203  70.276  1.00 37.45           O  
HETATM 5510  O   HOH A 466     -39.352  22.843  90.722  1.00 36.06           O  
HETATM 5511  O   HOH A 467     -61.729  34.759  86.231  1.00 35.89           O  
HETATM 5512  O   HOH A 468     -59.453  38.305  84.109  1.00 32.23           O  
HETATM 5513  O   HOH A 469     -61.797  33.044  82.609  1.00 30.53           O  
HETATM 5514  O   HOH A 470     -56.653  39.199  87.366  1.00 35.29           O  
HETATM 5515  O   HOH A 471     -54.517  37.620  86.800  1.00 21.46           O  
HETATM 5516  O   HOH A 473     -57.155  21.489  59.847  1.00 32.87           O  
HETATM 5517  O   HOH A 476     -41.963  15.478  66.914  1.00 42.82           O  
HETATM 5518  O   HOH A 477     -43.529   3.346  73.463  1.00 30.55           O  
HETATM 5519  O   HOH A 478     -62.566  28.479  67.968  1.00 31.90           O  
HETATM 5520  O   HOH A 482     -33.560  19.560  59.504  1.00 36.97           O  
HETATM 5521  O   HOH A 483     -58.502  10.278  80.518  0.50 21.17           O  
HETATM 5522  O   HOH A 484     -40.906  42.889  85.336  1.00 35.11           O  
HETATM 5523  O   HOH A 485     -33.362  36.286  88.929  1.00 34.07           O  
HETATM 5524  O   HOH A 487     -39.098  45.662  89.056  1.00 34.47           O  
HETATM 5525  O   HOH A 488     -35.389  17.666  87.525  1.00 45.93           O  
HETATM 5526  O   HOH A 617     -26.480  29.754  68.317  1.00 39.40           O  
HETATM 5527  O   HOH A 622     -56.229  44.494  68.557  1.00 38.64           O  
HETATM 5528  O   HOH A 623     -46.277  28.722  66.089  1.00 29.66           O  
HETATM 5529  O   HOH A 625     -52.161  23.618  63.445  1.00 44.74           O  
HETATM 5530  O   HOH A 627     -31.936  16.230  67.557  1.00 40.93           O  
HETATM 5531  O   HOH A 628     -47.519  16.255  64.561  1.00 34.54           O  
HETATM 5532  O   HOH A 637     -59.628  43.094  75.915  1.00 36.12           O  
HETATM 5533  O   HOH A 639     -66.009  18.251  67.407  1.00 38.48           O  
HETATM 5534  O   HOH A 647     -29.263  38.558  59.184  1.00 36.98           O  
HETATM 5535  O   HOH A 648     -43.824  22.974  91.529  1.00 38.80           O  
HETATM 5536  O   HOH A 649     -30.768  24.204  84.300  1.00 41.81           O  
HETATM 5537  O   HOH A 651     -42.807  36.842  82.608  1.00 22.82           O  
HETATM 5538  O   HOH A 652     -43.339  39.204  83.702  1.00 19.44           O  
HETATM 5539  O   HOH A 654     -42.943  50.499  68.421  1.00 47.68           O  
HETATM 5540  O   HOH A 659     -58.693  11.582  73.237  1.00 42.87           O  
HETATM 5541  O   HOH A 660     -49.196   6.131  76.752  1.00 43.70           O  
HETATM 5542  O   HOH A 661     -44.336   5.980  89.937  1.00 47.28           O  
HETATM 5543  O   HOH A 662     -54.648   6.922  80.616  1.00 37.31           O  
HETATM 5544  O   HOH A 663     -63.938   9.445  83.382  1.00 38.34           O  
HETATM 5545  O   HOH A 664     -51.489  13.724  92.121  1.00 42.13           O  
HETATM 5546  O   HOH A 665     -48.048  16.581  95.761  1.00 43.04           O  
HETATM 5547  O   HOH A 666     -55.982  31.297  66.364  1.00 38.11           O  
HETATM 5548  O   HOH A 667     -37.312  31.732  88.114  1.00 29.54           O  
HETATM 5549  O   HOH A 675     -42.079  50.430  76.875  1.00 38.37           O  
HETATM 5550  O   HOH B 220     -45.215  42.581  26.268  1.00 36.32           O  
HETATM 5551  O   HOH B 221     -49.238  43.673  55.352  1.00 22.33           O  
HETATM 5552  O   HOH B 222     -42.291  45.275  48.576  1.00 30.29           O  
HETATM 5553  O   HOH B 223     -54.455  49.476  51.996  1.00 23.31           O  
HETATM 5554  O   HOH B 224     -57.568  51.232  47.086  1.00 26.82           O  
HETATM 5555  O   HOH B 225     -64.228  52.028  53.352  1.00 23.85           O  
HETATM 5556  O   HOH B 226     -54.547  48.924  44.855  1.00 20.39           O  
HETATM 5557  O   HOH B 227     -72.677  -1.095  14.539  1.00 30.37           O  
HETATM 5558  O   HOH B 228     -46.329  39.795  59.369  1.00 30.59           O  
HETATM 5559  O   HOH B 229     -46.584  34.336  61.368  1.00 21.21           O  
HETATM 5560  O   HOH B 230     -48.754  32.501  60.326  1.00 17.99           O  
HETATM 5561  O   HOH B 231     -45.914  33.412  64.764  1.00 23.21           O  
HETATM 5562  O   HOH B 232     -47.562  51.836  40.052  1.00 43.93           O  
HETATM 5563  O   HOH B 233     -50.276  42.911  65.999  1.00 28.63           O  
HETATM 5564  O   HOH B 234     -58.915  47.301  23.186  1.00 24.60           O  
HETATM 5565  O   HOH B 235     -50.581  53.359  33.225  1.00 27.44           O  
HETATM 5566  O   HOH B 236     -58.181  47.917  56.131  1.00 29.16           O  
HETATM 5567  O   HOH B 237     -42.602  31.193  54.375  1.00 22.75           O  
HETATM 5568  O   HOH B 238     -50.397  49.890  49.594  1.00 33.48           O  
HETATM 5569  O   HOH B 239     -49.966  50.637  40.127  1.00 27.72           O  
HETATM 5570  O   HOH B 240     -66.924  43.585  38.104  1.00 29.39           O  
HETATM 5571  O   HOH B 241     -47.789  50.415  48.334  1.00 32.77           O  
HETATM 5572  O   HOH B 242     -57.922  50.935  27.778  1.00 28.77           O  
HETATM 5573  O   HOH B 243     -43.573  42.495  34.858  1.00 33.99           O  
HETATM 5574  O   HOH B 244     -65.197  41.899  43.747  1.00 32.00           O  
HETATM 5575  O   HOH B 245     -66.707  45.066  57.571  1.00 28.67           O  
HETATM 5576  O   HOH B 246     -41.421  33.560  58.664  1.00 37.42           O  
HETATM 5577  O   HOH B 247     -61.569  43.921  37.162  1.00 29.86           O  
HETATM 5578  O   HOH B 248     -63.837  50.091  18.902  1.00 30.68           O  
HETATM 5579  O   HOH B 249     -65.156  44.505  59.409  1.00 33.25           O  
HETATM 5580  O   HOH B 250     -56.935  54.310  30.476  1.00 34.57           O  
HETATM 5581  O   HOH B 251     -64.349  49.602  16.042  1.00 28.01           O  
HETATM 5582  O   HOH B 252     -62.627  43.638  16.887  1.00 29.55           O  
HETATM 5583  O   HOH B 253     -45.682  48.891  50.399  1.00 43.99           O  
HETATM 5584  O   HOH B 254     -64.246  51.441  13.983  1.00 27.88           O  
HETATM 5585  O   HOH B 255     -56.750  53.340  27.524  1.00 39.16           O  
HETATM 5586  O   HOH B 256     -69.095  43.472  57.730  1.00 25.07           O  
HETATM 5587  O   HOH B 257     -57.509  55.405  26.133  1.00 29.17           O  
HETATM 5588  O   HOH B 258     -66.416  47.877  16.305  1.00 34.38           O  
HETATM 5589  O   HOH B 259     -63.484  49.239  49.064  1.00 32.40           O  
HETATM 5590  O   HOH B 260     -43.125  46.394  37.855  1.00 42.08           O  
HETATM 5591  O   HOH B 261     -53.350  40.056  24.179  1.00 30.36           O  
HETATM 5592  O   HOH B 262     -56.712  40.882  57.896  1.00 26.16           O  
HETATM 5593  O   HOH B 263     -61.562  49.562  34.071  1.00 38.74           O  
HETATM 5594  O   HOH B 264     -54.240  51.389  43.922  1.00 32.02           O  
HETATM 5595  O   HOH B 265     -55.915  53.545  32.614  1.00 38.95           O  
HETATM 5596  O   HOH B 266     -42.663  44.560  35.137  1.00 29.72           O  
HETATM 5597  O   HOH B 267     -60.037  45.084  16.371  1.00 34.89           O  
HETATM 5598  O   HOH B 268     -71.569  44.592  22.347  1.00 41.28           O  
HETATM 5599  O   HOH B 269     -51.489  43.464  22.688  1.00 33.18           O  
HETATM 5600  O   HOH B 270     -72.120  42.379  27.870  1.00 38.47           O  
HETATM 5601  O   HOH B 271     -50.716  54.406  27.338  1.00 35.05           O  
HETATM 5602  O   HOH B 272     -61.929  48.243  27.537  1.00 39.70           O  
HETATM 5603  O   HOH B 273     -39.651  39.188  41.474  1.00 39.89           O  
HETATM 5604  O   HOH B 274     -56.710  50.322  54.671  1.00 35.30           O  
HETATM 5605  O   HOH B 275     -51.965  53.906  37.707  1.00 39.11           O  
HETATM 5606  O   HOH B 276     -53.072  44.914  20.515  1.00 33.34           O  
HETATM 5607  O   HOH B 277     -60.941  51.558  43.886  1.00 39.00           O  
HETATM 5608  O   HOH B 278     -45.134  41.508  32.614  1.00 33.74           O  
HETATM 5609  O   HOH B 279     -62.972  46.244  29.934  1.00 40.52           O  
HETATM 5610  O   HOH B 280     -56.347  48.305  17.106  1.00 36.19           O  
HETATM 5611  O   HOH B 281     -59.632  48.939  35.985  1.00 36.74           O  
HETATM 5612  O   HOH B 282     -66.065  45.139  16.866  1.00 38.41           O  
HETATM 5613  O   HOH B 283     -55.698  55.121  34.475  1.00 38.69           O  
HETATM 5614  O   HOH B 284     -73.624  46.270  21.410  1.00 38.12           O  
HETATM 5615  O   HOH B 285     -64.561  43.620  26.467  1.00 34.31           O  
HETATM 5616  O   HOH B 286     -73.913  45.255  18.428  1.00 44.22           O  
HETATM 5617  O   HOH B 287     -60.307  47.198  15.222  1.00 34.86           O  
HETATM 5618  O   HOH B 288     -47.153  44.716  57.131  1.00 33.53           O  
HETATM 5619  O   HOH B 289     -43.343  49.843  48.355  1.00 41.05           O  
HETATM 5620  O   HOH B 290     -62.997  47.605  14.863  1.00 36.17           O  
HETATM 5621  O   HOH B 291     -46.908  45.867  25.098  1.00 32.77           O  
HETATM 5622  O   HOH B 292     -61.415  49.775  56.379  1.00 26.51           O  
HETATM 5623  O   HOH B 293     -44.662  48.564  31.542  1.00 22.46           O  
HETATM 5624  O   HOH B 294     -42.818  35.834  59.228  1.00 36.68           O  
HETATM 5625  O   HOH B 295     -63.093  39.998  61.898  1.00 32.55           O  
HETATM 5626  O   HOH B 296     -59.306  38.889  63.479  1.00 32.63           O  
HETATM 5627  O   HOH B 299     -65.324  37.256  56.063  1.00 30.43           O  
HETATM 5628  O   HOH B 300     -65.017  35.269  53.035  1.00 20.73           O  
HETATM 5629  O   HOH B 301     -56.017  40.801  20.573  1.00 21.91           O  
HETATM 5630  O   HOH B 302     -55.684  39.428  22.868  1.00 23.22           O  
HETATM 5631  O   HOH B 303     -58.645  37.490  25.684  1.00 20.75           O  
HETATM 5632  O   HOH B 304     -60.517  40.245  28.950  1.00 22.54           O  
HETATM 5633  O   HOH B 305     -63.163  39.093  28.930  1.00 23.42           O  
HETATM 5634  O   HOH B 306     -64.550  41.432  28.832  1.00 30.70           O  
HETATM 5635  O   HOH B 307     -65.357  37.676  30.702  1.00 27.01           O  
HETATM 5636  O   HOH B 308     -65.885  36.378  37.147  1.00 38.22           O  
HETATM 5637  O   HOH B 309     -62.395  37.242  34.311  1.00 24.47           O  
HETATM 5638  O   HOH B 310     -63.512  37.723  36.859  1.00 21.01           O  
HETATM 5639  O   HOH B 311     -66.140  38.885  33.536  1.00 30.05           O  
HETATM 5640  O   HOH B 312     -59.577  32.768  29.448  1.00 40.04           O  
HETATM 5641  O   HOH B 313     -62.356  30.099  28.419  1.00 37.98           O  
HETATM 5642  O   HOH B 314     -62.057  26.735  24.795  1.00 29.98           O  
HETATM 5643  O   HOH B 315     -66.879  26.009  26.733  1.00 30.59           O  
HETATM 5644  O   HOH B 316     -68.222  22.845  25.900  1.00 25.93           O  
HETATM 5645  O   HOH B 317     -73.111  20.807  26.643  1.00 21.29           O  
HETATM 5646  O   HOH B 318     -74.179  20.610  31.127  1.00 32.01           O  
HETATM 5647  O   HOH B 319     -72.885  28.623  26.299  1.00 34.16           O  
HETATM 5648  O   HOH B 320     -68.924  17.996  28.080  1.00 28.22           O  
HETATM 5649  O   HOH B 321     -70.868  13.502  30.332  1.00 36.86           O  
HETATM 5650  O   HOH B 322     -65.462  14.428  25.633  1.00 30.40           O  
HETATM 5651  O   HOH B 323     -66.145  18.399  27.196  1.00 25.97           O  
HETATM 5652  O   HOH B 325     -62.401  18.160  26.032  1.00 30.06           O  
HETATM 5653  O   HOH B 326     -64.390  20.536  26.191  1.00 29.50           O  
HETATM 5654  O   HOH B 327     -65.833  12.810  21.085  1.00 19.09           O  
HETATM 5655  O   HOH B 337     -59.136  26.528  18.487  1.00 24.22           O  
HETATM 5656  O   HOH B 338     -58.087  26.839  16.000  1.00 26.66           O  
HETATM 5657  O   HOH B 339     -61.054  25.529  14.567  1.00 20.41           O  
HETATM 5658  O   HOH B 340     -75.228  11.547  25.308  1.00 27.46           O  
HETATM 5659  O   HOH B 341     -74.312  13.617  27.283  1.00 23.87           O  
HETATM 5660  O   HOH B 342     -74.484  12.537  29.314  1.00 35.96           O  
HETATM 5661  O   HOH B 343     -72.178  12.054  22.434  1.00 22.57           O  
HETATM 5662  O   HOH B 344     -74.583  10.907  22.232  1.00 27.35           O  
HETATM 5663  O   HOH B 345     -76.658  11.823  20.905  1.00 25.34           O  
HETATM 5664  O   HOH B 346     -78.991  16.141  24.300  1.00 31.46           O  
HETATM 5665  O   HOH B 347     -82.544  14.633  23.640  1.00 30.65           O  
HETATM 5666  O   HOH B 348     -80.489  23.968  22.639  1.00 23.28           O  
HETATM 5667  O   HOH B 351     -58.375  29.551  60.682  1.00 34.43           O  
HETATM 5668  O   HOH B 352     -56.892  29.137  56.672  1.00 30.55           O  
HETATM 5669  O   HOH B 353     -55.201  29.447  59.113  1.00 19.00           O  
HETATM 5670  O   HOH B 354     -62.508  32.208  58.057  1.00 41.28           O  
HETATM 5671  O   HOH B 355     -55.749  28.991  61.769  1.00 38.51           O  
HETATM 5672  O   HOH B 356     -53.284  24.184  58.785  1.00 36.17           O  
HETATM 5673  O   HOH B 358     -52.100  23.389  61.302  1.00 30.25           O  
HETATM 5674  O   HOH B 365     -44.148  28.736  67.989  1.00 26.59           O  
HETATM 5675  O   HOH B 391     -49.087  26.744  32.167  1.00 44.91           O  
HETATM 5676  O   HOH B 392     -44.798  26.508  30.811  1.00 36.12           O  
HETATM 5677  O   HOH B 399     -42.400  32.395  38.646  1.00 38.45           O  
HETATM 5678  O   HOH B 401     -43.089  30.470  35.161  1.00 39.13           O  
HETATM 5679  O   HOH B 402     -44.383  37.444  31.735  1.00 47.52           O  
HETATM 5680  O   HOH B 403     -49.713  36.418  28.308  1.00 30.03           O  
HETATM 5681  O   HOH B 404     -43.404  33.692  41.111  1.00 27.98           O  
HETATM 5682  O   HOH B 407     -56.735  51.835  37.573  1.00 44.86           O  
HETATM 5683  O   HOH B 410     -64.948  44.047  44.694  1.00 43.52           O  
HETATM 5684  O   HOH B 413     -64.108  45.029  15.198  1.00 36.16           O  
HETATM 5685  O   HOH B 415     -65.361  44.097  12.957  1.00 47.37           O  
HETATM 5686  O   HOH B 486     -75.991   0.814   5.263  1.00 42.10           O  
HETATM 5687  O   HOH B 489     -54.846  26.985  61.421  1.00 40.46           O  
HETATM 5688  O   HOH B 490     -65.206  33.172  43.612  1.00 23.12           O  
HETATM 5689  O   HOH B 491     -67.100  33.743  41.452  1.00 41.63           O  
HETATM 5690  O   HOH B 492     -61.478  29.837  42.978  1.00 27.70           O  
HETATM 5691  O   HOH B 493     -63.749  30.858  43.463  1.00 33.42           O  
HETATM 5692  O   HOH B 494     -61.033  27.830  44.506  1.00 30.39           O  
HETATM 5693  O   HOH B 496     -61.623  30.005  38.151  1.00 33.06           O  
HETATM 5694  O   HOH B 497     -55.292  30.442  35.065  1.00 21.89           O  
HETATM 5695  O   HOH B 498     -47.525  32.921  33.506  1.00 24.61           O  
HETATM 5696  O   HOH B 501     -68.276  34.830  27.681  1.00 26.62           O  
HETATM 5697  O   HOH B 502     -70.113  33.083  28.336  1.00 40.61           O  
HETATM 5698  O   HOH B 503     -62.692  30.715  25.803  1.00 27.23           O  
HETATM 5699  O   HOH B 504     -60.355  29.118  24.813  1.00 29.03           O  
HETATM 5700  O   HOH B 505     -52.825  31.225  20.023  1.00 38.70           O  
HETATM 5701  O   HOH B 506     -54.040  33.867  12.139  1.00 38.03           O  
HETATM 5702  O   HOH B 507     -43.678  32.974  34.425  1.00 39.18           O  
HETATM 5703  O   HOH B 515     -56.500  25.660  48.216  1.00 19.00           O  
HETATM 5704  O   HOH B 517     -59.526  25.811  51.401  1.00 41.68           O  
HETATM 5705  O   HOH B 518     -62.194  36.303  54.686  1.00 35.70           O  
HETATM 5706  O   HOH B 538     -83.407  15.449  12.571  1.00 37.62           O  
HETATM 5707  O   HOH B 557     -65.964  12.845   4.685  1.00 37.70           O  
HETATM 5708  O   HOH B 561     -76.249  21.260   7.082  1.00 38.33           O  
HETATM 5709  O   HOH B 562     -79.827  27.536  13.545  1.00 25.82           O  
HETATM 5710  O   HOH B 563     -75.688  22.921  31.730  1.00 34.29           O  
HETATM 5711  O   HOH B 564     -82.002  19.881  26.042  1.00 31.63           O  
HETATM 5712  O   HOH B 565     -81.656  21.666  22.160  1.00 32.04           O  
HETATM 5713  O   HOH B 566     -81.834  19.753  20.575  1.00 33.37           O  
HETATM 5714  O   HOH B 567     -70.112  25.580  28.827  1.00 42.49           O  
HETATM 5715  O   HOH B 568     -79.442  32.221  17.850  1.00 33.65           O  
HETATM 5716  O   HOH B 569     -73.421  33.625  13.886  1.00 34.09           O  
HETATM 5717  O   HOH B 570     -74.314  30.430  10.187  1.00 44.79           O  
HETATM 5718  O   HOH B 576     -68.541  14.454  10.170  1.00 23.57           O  
HETATM 5719  O   HOH B 577     -68.998  11.773  10.624  1.00 21.58           O  
HETATM 5720  O   HOH B 578     -67.221  10.201   9.207  1.00 22.41           O  
HETATM 5721  O   HOH B 580     -79.435   8.444  11.194  1.00 33.75           O  
HETATM 5722  O   HOH B 581     -79.449  18.677  14.232  1.00 26.71           O  
HETATM 5723  O   HOH B 582     -82.134   8.809  13.698  1.00 26.87           O  
HETATM 5724  O   HOH B 583     -84.439   5.183  14.892  1.00 40.73           O  
HETATM 5725  O   HOH B 584     -83.448   7.692  11.687  1.00 28.48           O  
HETATM 5726  O   HOH B 585     -81.005   6.324  10.786  1.00 39.44           O  
HETATM 5727  O   HOH B 586     -81.957   4.759  14.500  1.00 42.31           O  
HETATM 5728  O   HOH B 588     -76.688  16.654  12.834  1.00 27.21           O  
HETATM 5729  O   HOH B 589     -68.213   7.873  10.383  1.00 23.39           O  
HETATM 5730  O   HOH B 590     -67.519   4.909  12.743  1.00 32.78           O  
HETATM 5731  O   HOH B 591     -65.644   6.554  11.493  1.00 44.80           O  
HETATM 5732  O   HOH B 593     -69.454  18.727   6.945  1.00 22.71           O  
HETATM 5733  O   HOH B 594     -71.202  22.475   7.669  1.00 21.96           O  
HETATM 5734  O   HOH B 596     -59.596  36.810  11.600  1.00 35.34           O  
HETATM 5735  O   HOH B 604     -60.279  28.165  46.744  1.00 21.28           O  
HETATM 5736  O   HOH B 610     -43.136  38.901  53.634  1.00 35.81           O  
HETATM 5737  O   HOH B 611     -63.521  47.516  22.416  1.00 35.60           O  
HETATM 5738  O   HOH B 612     -62.374  52.486  19.922  1.00 24.94           O  
HETATM 5739  O   HOH B 614     -59.379  29.925  36.807  1.00 41.49           O  
HETATM 5740  O   HOH B 615     -63.558  35.769  32.147  1.00 32.67           O  
HETATM 5741  O   HOH B 616     -63.279  33.094  35.955  1.00 39.43           O  
HETATM 5742  O   HOH B 618     -62.169  52.980  51.478  1.00 33.43           O  
HETATM 5743  O   HOH B 619     -61.269  29.165  56.256  1.00 36.96           O  
HETATM 5744  O   HOH B 620     -57.524  31.353  54.850  1.00 21.18           O  
HETATM 5745  O   HOH B 621     -58.000  51.852  35.631  1.00 36.33           O  
HETATM 5746  O   HOH B 626     -47.531  38.099  61.277  1.00 32.82           O  
HETATM 5747  O   HOH B 629     -56.557  33.020  10.250  1.00 39.55           O  
HETATM 5748  O   HOH B 631     -60.564  27.750  14.831  1.00 39.65           O  
HETATM 5749  O   HOH B 638     -39.863  46.221  34.811  1.00 41.44           O  
HETATM 5750  O   HOH B 640     -61.786  33.880  31.451  1.00 35.81           O  
HETATM 5751  O   HOH B 641     -54.432  27.002  21.811  1.00 35.32           O  
HETATM 5752  O   HOH B 643     -69.563  39.872  14.785  1.00 41.98           O  
HETATM 5753  O   HOH B 646     -63.254  26.242  44.741  1.00 40.68           O  
HETATM 5754  O   HOH B 650     -61.202  34.045  34.979  1.00 46.13           O  
HETATM 5755  O   HOH B 653     -46.600  48.252  26.467  1.00 42.49           O  
HETATM 5756  O   HOH B 657     -53.346  40.764  19.333  1.00 33.74           O  
HETATM 5757  O   HOH B 672     -81.906  25.938  21.467  1.00 39.38           O  
HETATM 5758  O   HOH C   2     -39.414  15.009  39.156  1.00 22.93           O  
HETATM 5759  O   HOH C 214     -36.251  14.258  53.969  1.00 51.31           O  
HETATM 5760  O   HOH C 215     -39.584  17.110  31.804  1.00 20.20           O  
HETATM 5761  O   HOH C 216     -40.781  23.730  34.652  1.00 20.75           O  
HETATM 5762  O   HOH C 217     -41.264  29.590  52.189  1.00 17.34           O  
HETATM 5763  O   HOH C 218     -39.087  25.305  36.528  1.00 21.89           O  
HETATM 5764  O   HOH C 219     -39.140  16.634  54.757  1.00 25.24           O  
HETATM 5765  O   HOH C 220     -36.674  15.652  49.680  1.00 31.49           O  
HETATM 5766  O   HOH C 221     -27.063  27.977  47.054  1.00 27.63           O  
HETATM 5767  O   HOH C 222     -39.557  15.228  29.711  1.00 25.49           O  
HETATM 5768  O   HOH C 223     -35.250  37.504  46.051  1.00 30.31           O  
HETATM 5769  O   HOH C 224     -36.366  39.604  48.122  1.00 33.02           O  
HETATM 5770  O   HOH C 225     -35.916  19.894  39.720  1.00 23.30           O  
HETATM 5771  O   HOH C 226     -35.442  32.890  56.010  1.00 35.46           O  
HETATM 5772  O   HOH C 227     -38.373  14.195  36.523  1.00 31.42           O  
HETATM 5773  O   HOH C 228     -37.035  26.818  35.392  1.00 37.75           O  
HETATM 5774  O   HOH C 229     -31.006  21.990  44.550  1.00 32.06           O  
HETATM 5775  O   HOH C 230     -56.089  -0.332  24.287  1.00 28.25           O  
HETATM 5776  O   HOH C 231     -58.051  -0.865  26.264  1.00 35.80           O  
HETATM 5777  O   HOH C 232     -37.211  11.844  45.078  1.00 40.24           O  
HETATM 5778  O   HOH C 233     -32.431  22.997  53.812  1.00 30.27           O  
HETATM 5779  O   HOH C 234     -43.176  12.088  50.114  1.00 29.59           O  
HETATM 5780  O   HOH C 235     -44.063  27.332  60.578  1.00 20.05           O  
HETATM 5781  O   HOH C 236     -44.475  26.430  53.130  1.00 20.28           O  
HETATM 5782  O   HOH C 237     -40.626   9.812  36.867  1.00 39.71           O  
HETATM 5783  O   HOH C 238     -38.928  34.115  58.500  1.00 40.96           O  
HETATM 5784  O   HOH C 239     -30.849  24.271  41.877  1.00 33.83           O  
HETATM 5785  O   HOH C 240     -38.321  13.769  41.152  1.00 27.41           O  
HETATM 5786  O   HOH C 241     -27.668  24.474  46.056  1.00 39.40           O  
HETATM 5787  O   HOH C 242     -26.200  25.321  48.009  1.00 35.93           O  
HETATM 5788  O   HOH C 243     -41.696  13.605  48.653  1.00 32.49           O  
HETATM 5789  O   HOH C 244     -32.306  19.513  54.741  1.00 38.41           O  
HETATM 5790  O   HOH C 245     -41.390  27.472  61.612  1.00 19.94           O  
HETATM 5791  O   HOH C 246     -33.684  17.088  48.462  1.00 35.86           O  
HETATM 5792  O   HOH C 247     -39.396  18.584  56.514  1.00 35.36           O  
HETATM 5793  O   HOH C 248     -35.331  15.999  39.119  1.00 41.92           O  
HETATM 5794  O   HOH C 249     -38.669  33.179  40.276  1.00 38.76           O  
HETATM 5795  O   HOH C 250     -35.203  33.873  53.018  1.00 31.79           O  
HETATM 5796  O   HOH C 251     -32.950  33.759  52.178  1.00 39.06           O  
HETATM 5797  O   HOH C 252     -29.684  19.838  48.464  1.00 31.16           O  
HETATM 5798  O   HOH C 253     -30.077  33.217  52.296  1.00 35.39           O  
HETATM 5799  O   HOH C 254     -41.324  10.083  39.309  1.00 23.89           O  
HETATM 5800  O   HOH C 256     -24.556  29.564  48.834  1.00 30.04           O  
HETATM 5801  O   HOH C 258     -23.452  31.675  47.675  1.00 25.96           O  
HETATM 5802  O   HOH C 260     -49.268  18.566  12.665  1.00 28.55           O  
HETATM 5803  O   HOH C 261     -49.620  16.861  18.369  1.00 34.31           O  
HETATM 5804  O   HOH C 262     -46.222  16.293  16.744  1.00 28.17           O  
HETATM 5805  O   HOH C 263     -47.941   9.329  17.630  1.00 18.50           O  
HETATM 5806  O   HOH C 264     -44.925  10.391  20.683  1.00 25.34           O  
HETATM 5807  O   HOH C 265     -44.278   8.601  22.385  1.00 28.94           O  
HETATM 5808  O   HOH C 266     -40.222   6.205  17.708  1.00 25.93           O  
HETATM 5809  O   HOH C 267     -49.319   6.793  11.020  1.00 22.01           O  
HETATM 5810  O   HOH C 268     -46.386  10.430   7.339  1.00 28.30           O  
HETATM 5811  O   HOH C 269     -49.305  13.137   8.025  1.00 22.39           O  
HETATM 5812  O   HOH C 270     -50.348  21.280   6.235  1.00 28.46           O  
HETATM 5813  O   HOH C 271     -48.332  21.038   8.133  1.00 49.07           O  
HETATM 5814  O   HOH C 272     -50.689  24.363   6.388  1.00 27.82           O  
HETATM 5815  O   HOH C 273     -49.277  26.985   9.242  1.00 27.19           O  
HETATM 5816  O   HOH C 274     -55.957  28.658  10.057  1.00 27.66           O  
HETATM 5817  O   HOH C 275     -62.474  35.354   2.057  1.00 31.12           O  
HETATM 5818  O   HOH C 276     -62.223  36.056  -1.128  1.00 30.26           O  
HETATM 5819  O   HOH C 277     -57.961  35.979  -2.106  1.00 36.72           O  
HETATM 5820  O   HOH C 278     -55.988  32.373   0.976  1.00 29.84           O  
HETATM 5821  O   HOH C 280     -59.022  26.086 -10.728  1.00 33.63           O  
HETATM 5822  O   HOH C 281     -57.822  22.728 -11.702  1.00 27.51           O  
HETATM 5823  O   HOH C 282     -58.350  22.737  -9.060  1.00 30.53           O  
HETATM 5824  O   HOH C 283     -53.222  21.056 -10.397  1.00 20.29           O  
HETATM 5825  O   HOH C 284     -54.441  23.063  -9.024  1.00 30.07           O  
HETATM 5826  O   HOH C 285     -52.053  22.909  -7.388  1.00 31.97           O  
HETATM 5827  O   HOH C 286     -51.444  20.452  -7.441  1.00 31.73           O  
HETATM 5828  O   HOH C 287     -52.956  23.194  -4.861  1.00 33.19           O  
HETATM 5829  O   HOH C 288     -53.646  16.994  -8.529  1.00 29.15           O  
HETATM 5830  O   HOH C 289     -55.991  14.563  -5.248  1.00 35.78           O  
HETATM 5831  O   HOH C 290     -55.286  14.549  -2.128  1.00 36.06           O  
HETATM 5832  O   HOH C 291     -55.559  17.167  -2.022  1.00 22.38           O  
HETATM 5833  O   HOH C 324     -61.646  15.758  27.061  1.00 25.68           O  
HETATM 5834  O   HOH C 328     -65.183   8.462  16.640  1.00 35.33           O  
HETATM 5835  O   HOH C 329     -62.255   7.987  18.589  1.00 25.16           O  
HETATM 5836  O   HOH C 330     -59.866   6.871  19.245  1.00 26.18           O  
HETATM 5837  O   HOH C 331     -59.835   6.055  22.255  1.00 37.21           O  
HETATM 5838  O   HOH C 332     -56.945  29.143  12.527  1.00 35.19           O  
HETATM 5839  O   HOH C 333     -53.840  30.114   9.485  1.00 30.64           O  
HETATM 5840  O   HOH C 334     -47.583  24.667   8.233  1.00 33.50           O  
HETATM 5841  O   HOH C 335     -57.550  24.364  14.774  1.00 17.09           O  
HETATM 5842  O   HOH C 336     -60.441  24.540  17.113  1.00 20.10           O  
HETATM 5843  O   HOH C 357     -53.444  22.314  57.900  1.00 30.62           O  
HETATM 5844  O   HOH C 359     -49.001  22.412  60.300  1.00 21.41           O  
HETATM 5845  O   HOH C 360     -46.523  23.626  60.368  1.00 21.72           O  
HETATM 5846  O   HOH C 366     -50.304  16.753  57.345  1.00 28.13           O  
HETATM 5847  O   HOH C 367     -55.108  16.676  55.896  1.00 30.93           O  
HETATM 5848  O   HOH C 368     -46.495  15.084  53.467  1.00 14.72           O  
HETATM 5849  O   HOH C 369     -44.774   8.023  48.744  1.00 35.77           O  
HETATM 5850  O   HOH C 370     -47.503  10.530  48.441  1.00 16.20           O  
HETATM 5851  O   HOH C 371     -49.187   9.792  50.439  1.00 27.62           O  
HETATM 5852  O   HOH C 372     -48.245   3.958  44.168  1.00 24.25           O  
HETATM 5853  O   HOH C 373     -42.907  12.912  31.297  1.00 21.09           O  
HETATM 5854  O   HOH C 374     -45.168  10.334  28.672  1.00 30.94           O  
HETATM 5855  O   HOH C 375     -48.921  12.287  25.520  1.00 30.97           O  
HETATM 5856  O   HOH C 376     -46.781  13.908  25.534  1.00 29.23           O  
HETATM 5857  O   HOH C 377     -42.597  15.026  28.025  1.00 34.74           O  
HETATM 5858  O   HOH C 378     -46.320  16.071  30.989  1.00 16.50           O  
HETATM 5859  O   HOH C 379     -46.137  17.956  28.947  1.00 27.15           O  
HETATM 5860  O   HOH C 380     -50.340  15.727  28.920  1.00 21.11           O  
HETATM 5861  O   HOH C 381     -51.819  15.748  31.247  1.00 17.58           O  
HETATM 5862  O   HOH C 382     -52.939  18.078  29.304  1.00 31.24           O  
HETATM 5863  O   HOH C 383     -53.120  19.960  32.567  1.00 32.74           O  
HETATM 5864  O   HOH C 384     -53.586  22.619  34.415  1.00 32.75           O  
HETATM 5865  O   HOH C 385     -51.160  25.701  35.123  1.00 33.19           O  
HETATM 5866  O   HOH C 386     -50.742  21.227  31.010  1.00 35.06           O  
HETATM 5867  O   HOH C 387     -44.897  22.193  31.988  1.00 23.14           O  
HETATM 5868  O   HOH C 388     -46.578  23.248  34.183  1.00 25.35           O  
HETATM 5869  O   HOH C 389     -43.813  24.383  32.833  1.00 28.73           O  
HETATM 5870  O   HOH C 390     -46.651  25.905  33.813  1.00 29.16           O  
HETATM 5871  O   HOH C 393     -41.994  27.412  32.666  1.00 29.95           O  
HETATM 5872  O   HOH C 394     -41.056  25.072  32.429  1.00 34.55           O  
HETATM 5873  O   HOH C 395     -36.717  23.238  34.053  1.00 34.35           O  
HETATM 5874  O   HOH C 396     -44.201  26.603  33.167  1.00 23.07           O  
HETATM 5875  O   HOH C 397     -40.749  29.441  33.848  1.00 36.59           O  
HETATM 5876  O   HOH C 398     -39.238  29.703  37.620  1.00 34.41           O  
HETATM 5877  O   HOH C 400     -44.267  29.587  37.468  1.00 19.19           O  
HETATM 5878  O   HOH C 412     -62.682  30.242  -8.903  1.00 46.22           O  
HETATM 5879  O   HOH C 418     -63.193  32.461  -7.407  1.00 29.31           O  
HETATM 5880  O   HOH C 421     -60.610  32.730  -7.333  1.00 38.44           O  
HETATM 5881  O   HOH C 423     -63.526  35.526  -7.182  1.00 42.38           O  
HETATM 5882  O   HOH C 424     -65.794  34.672  -4.983  1.00 32.81           O  
HETATM 5883  O   HOH C 461     -47.144  16.152  60.791  1.00 34.31           O  
HETATM 5884  O   HOH C 472     -58.836  16.236  54.617  1.00 49.03           O  
HETATM 5885  O   HOH C 474     -41.471  14.858  54.864  1.00 30.89           O  
HETATM 5886  O   HOH C 475     -44.744  13.274  54.489  1.00 44.72           O  
HETATM 5887  O   HOH C 479     -43.266  20.575  58.871  1.00 38.56           O  
HETATM 5888  O   HOH C 480     -41.944  19.792  49.881  1.00 14.47           O  
HETATM 5889  O   HOH C 481     -35.896  19.799  55.843  1.00 42.01           O  
HETATM 5890  O   HOH C 495     -61.493  28.403  40.066  1.00 36.47           O  
HETATM 5891  O   HOH C 499     -59.188  21.021  26.824  1.00 29.25           O  
HETATM 5892  O   HOH C 500     -62.352  28.129  33.798  1.00 47.18           O  
HETATM 5893  O   HOH C 508     -41.126  32.789  40.779  1.00 29.68           O  
HETATM 5894  O   HOH C 509     -42.704  35.360  42.363  1.00 38.09           O  
HETATM 5895  O   HOH C 510     -41.423  24.471  29.846  1.00 32.36           O  
HETATM 5896  O   HOH C 511     -35.912  16.472  47.486  1.00 37.34           O  
HETATM 5897  O   HOH C 512     -56.847  17.476  44.492  1.00 32.02           O  
HETATM 5898  O   HOH C 513     -56.317  15.554  42.010  1.00 22.71           O  
HETATM 5899  O   HOH C 514     -56.395  23.173  49.690  1.00 17.73           O  
HETATM 5900  O   HOH C 516     -58.320  21.514  50.125  1.00 34.46           O  
HETATM 5901  O   HOH C 519     -57.382   6.666  37.213  1.00 23.02           O  
HETATM 5902  O   HOH C 520     -59.827   7.578  36.934  1.00 27.60           O  
HETATM 5903  O   HOH C 521     -61.488  10.526  37.231  1.00 44.94           O  
HETATM 5904  O   HOH C 522     -57.742   5.278  34.246  1.00 32.01           O  
HETATM 5905  O   HOH C 523     -60.166   6.942  34.684  1.00 29.37           O  
HETATM 5906  O   HOH C 524     -50.890  23.350  10.993  1.00 33.72           O  
HETATM 5907  O   HOH C 525     -50.678  25.710  15.447  1.00 33.92           O  
HETATM 5908  O   HOH C 526     -52.142  27.354  17.373  1.00 36.76           O  
HETATM 5909  O   HOH C 527     -53.282  23.966  21.500  1.00 27.60           O  
HETATM 5910  O   HOH C 528     -52.737  19.013  25.661  1.00 28.34           O  
HETATM 5911  O   HOH C 529     -54.432   2.172  29.205  1.00 20.25           O  
HETATM 5912  O   HOH C 530     -56.855   2.703  28.954  1.00 36.61           O  
HETATM 5913  O   HOH C 531     -59.979   4.023  26.758  1.00 31.23           O  
HETATM 5914  O   HOH C 532     -56.212   6.278  32.284  1.00 31.30           O  
HETATM 5915  O   HOH C 533     -57.366   4.284  36.043  1.00 41.72           O  
HETATM 5916  O   HOH C 534     -55.294   0.658  16.154  1.00 39.08           O  
HETATM 5917  O   HOH C 535     -56.167   2.420  18.435  1.00 36.00           O  
HETATM 5918  O   HOH C 536     -48.993   1.265  24.444  0.50 25.00           O  
HETATM 5919  O   HOH C 537     -42.248   7.671  17.712  1.00 36.32           O  
HETATM 5920  O   HOH C 539     -42.374  14.360   9.213  1.00 29.02           O  
HETATM 5921  O   HOH C 540     -61.646  23.624  -8.946  1.00 34.11           O  
HETATM 5922  O   HOH C 541     -67.201  26.807  -3.166  1.00 32.16           O  
HETATM 5923  O   HOH C 542     -68.801  25.095  -2.451  1.00 37.09           O  
HETATM 5924  O   HOH C 543     -67.869  20.872  -0.336  1.00 33.10           O  
HETATM 5925  O   HOH C 544     -69.669  17.182  -3.002  1.00 42.93           O  
HETATM 5926  O   HOH C 545     -68.245  16.271  -1.161  1.00 49.62           O  
HETATM 5927  O   HOH C 546     -66.528  14.652  -1.715  1.00 33.84           O  
HETATM 5928  O   HOH C 547     -65.875  13.295   1.363  1.00 35.70           O  
HETATM 5929  O   HOH C 548     -71.819  16.065  -2.725  1.00 37.88           O  
HETATM 5930  O   HOH C 549     -62.563  10.691   3.292  1.00 29.96           O  
HETATM 5931  O   HOH C 550     -57.852  12.573  -1.694  1.00 38.40           O  
HETATM 5932  O   HOH C 551     -53.415   8.250   3.578  1.00 28.84           O  
HETATM 5933  O   HOH C 552     -56.603   6.942   4.267  1.00 29.20           O  
HETATM 5934  O   HOH C 553     -54.150   3.419   8.078  1.00 40.94           O  
HETATM 5935  O   HOH C 554     -59.916   7.167   5.196  1.00 30.17           O  
HETATM 5936  O   HOH C 555     -60.769   7.574  11.300  1.00 26.00           O  
HETATM 5937  O   HOH C 556     -64.639   8.391   6.841  1.00 39.54           O  
HETATM 5938  O   HOH C 558     -66.504  14.611   8.675  1.00 25.36           O  
HETATM 5939  O   HOH C 559     -67.627  27.009   8.133  1.00 23.82           O  
HETATM 5940  O   HOH C 560     -65.570  24.412   8.328  1.00 21.46           O  
HETATM 5941  O   HOH C 571     -73.849  33.407   6.855  1.00 39.12           O  
HETATM 5942  O   HOH C 572     -73.474  36.142   5.568  1.00 53.09           O  
HETATM 5943  O   HOH C 573     -56.237  16.845  -7.194  1.00 37.39           O  
HETATM 5944  O   HOH C 574     -59.314  10.029   1.494  1.00 40.67           O  
HETATM 5945  O   HOH C 575     -64.724  12.998   7.405  1.00 19.74           O  
HETATM 5946  O   HOH C 579     -64.409  10.598   8.837  1.00 18.08           O  
HETATM 5947  O   HOH C 587     -48.904  26.197   1.017  1.00 37.97           O  
HETATM 5948  O   HOH C 592     -70.601  22.418   3.244  1.00 33.34           O  
HETATM 5949  O   HOH C 595     -46.644   6.711  12.989  1.00 36.69           O  
HETATM 5950  O   HOH C 597     -59.112  15.632  25.849  1.00 20.28           O  
HETATM 5951  O   HOH C 598     -59.505  13.455  24.192  1.00 18.89           O  
HETATM 5952  O   HOH C 599     -61.951  11.836  25.881  1.00 31.47           O  
HETATM 5953  O   HOH C 600     -58.946  17.467  31.822  1.00 40.12           O  
HETATM 5954  O   HOH C 601     -61.011  16.315  31.020  1.00 25.73           O  
HETATM 5955  O   HOH C 602     -56.269  17.429  32.272  1.00 35.31           O  
HETATM 5956  O   HOH C 603     -57.454  16.945  34.575  1.00 36.31           O  
HETATM 5957  O   HOH C 605     -58.031  26.430  46.039  1.00 24.83           O  
HETATM 5958  O   HOH C 606     -59.448  25.301  43.060  1.00 33.21           O  
HETATM 5959  O   HOH C 607     -57.451  21.571  42.259  1.00 25.29           O  
HETATM 5960  O   HOH C 608     -57.013  23.459  40.411  1.00 19.62           O  
HETATM 5961  O   HOH C 609     -42.130  41.525  49.403  1.00 31.01           O  
HETATM 5962  O   HOH C 613     -46.614  16.544  22.385  1.00 37.66           O  
HETATM 5963  O   HOH C 624     -35.655  39.453  42.078  1.00 42.23           O  
HETATM 5964  O   HOH C 630     -60.488  30.009  10.192  1.00 39.20           O  
HETATM 5965  O   HOH C 632     -53.175  12.060   1.418  1.00 38.01           O  
HETATM 5966  O   HOH C 633     -69.466  19.052   0.292  1.00 37.10           O  
HETATM 5967  O   HOH C 634     -67.748  23.515  -0.305  1.00 38.90           O  
HETATM 5968  O   HOH C 635     -74.060  26.310   6.467  1.00 39.02           O  
HETATM 5969  O   HOH C 636     -76.570  28.557   4.055  1.00 36.28           O  
HETATM 5970  O   HOH C 642     -54.581  22.307  25.818  1.00 44.05           O  
HETATM 5971  O   HOH C 644     -66.881  35.170   7.831  1.00 31.41           O  
HETATM 5972  O   HOH C 645     -37.960  14.514  43.586  1.00 41.69           O  
HETATM 5973  O   HOH C 655     -26.545  21.107  45.788  1.00 46.82           O  
HETATM 5974  O   HOH C 656     -39.823  37.200  53.546  1.00 41.97           O  
HETATM 5975  O   HOH C 658     -58.188  16.522  -9.132  1.00 39.99           O  
HETATM 5976  O   HOH C 668     -62.227  13.647  -2.182  1.00 39.38           O  
HETATM 5977  O   HOH C 669     -64.779  12.647  -1.615  1.00 34.35           O  
HETATM 5978  O   HOH C 670     -53.865   1.692  11.191  1.00 42.55           O  
HETATM 5979  O   HOH C 671     -60.536   4.761  14.999  1.00 46.58           O  
HETATM 5980  O   HOH C 673     -37.099  31.936  39.522  1.00 31.83           O  
HETATM 5981  O   HOH C 674     -35.587  34.046  41.374  1.00 41.70           O  
HETATM 5982  O   HOH C 676     -45.770  15.601  27.284  1.00 54.02           O  
CONECT  208  322                                                                
CONECT  209  322                                                                
CONECT  322  208  209                                                           
CONECT 1302 1415                                                                
CONECT 1415 1302                                                                
CONECT 1486 1685                                                                
CONECT 1685 1486                                                                
CONECT 2051 2611                                                                
CONECT 2611 2051                                                                
CONECT 3045 3475                                                                
CONECT 3475 3045                                                                
CONECT 3774 4290                                                                
CONECT 4290 3774                                                                
CONECT 4637 5122 5123                                                           
CONECT 4737 5306                                                                
CONECT 4859 5306                                                                
CONECT 4983 5306                                                                
CONECT 5122 4637                                                                
CONECT 5123 4637                                                                
CONECT 5261 5262 5263                                                           
CONECT 5262 5261                                                                
CONECT 5263 5261 5264                                                           
CONECT 5264 5263                                                                
CONECT 5265 5266 5267                                                           
CONECT 5266 5265                                                                
CONECT 5267 5265 5268                                                           
CONECT 5268 5267                                                                
CONECT 5269 5270 5271                                                           
CONECT 5270 5269                                                                
CONECT 5271 5269 5272                                                           
CONECT 5272 5271                                                                
CONECT 5273 5274 5275                                                           
CONECT 5274 5273                                                                
CONECT 5275 5273 5276                                                           
CONECT 5276 5275                                                                
CONECT 5277 5278 5279                                                           
CONECT 5278 5277                                                                
CONECT 5279 5277 5280                                                           
CONECT 5280 5279                                                                
CONECT 5281 5282 5283                                                           
CONECT 5282 5281                                                                
CONECT 5283 5281 5284                                                           
CONECT 5284 5283                                                                
CONECT 5288 5289 5290                                                           
CONECT 5289 5288                                                                
CONECT 5290 5288 5291                                                           
CONECT 5291 5290                                                                
CONECT 5292 5293 5294                                                           
CONECT 5293 5292                                                                
CONECT 5294 5292 5295                                                           
CONECT 5295 5294                                                                
CONECT 5296 5297 5298                                                           
CONECT 5297 5296                                                                
CONECT 5298 5296 5299                                                           
CONECT 5299 5298                                                                
CONECT 5302 5303 5304                                                           
CONECT 5303 5302                                                                
CONECT 5304 5302 5305                                                           
CONECT 5305 5304                                                                
CONECT 5306 4737 4859 4983 5906                                                 
CONECT 5906 5306                                                                
MASTER      423    0   16   14   60    0   22    6 5879    3   61   54          
END

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Related entries of code: 3nps

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
2xzc	RCSB PDB PDBbind	216aa, >2XZC_2\|Chain... *
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	3nps
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	membrane-type serine protease 1 (MT-SP1), Wild-type matriptase
Ligand Name	Fab Inhibitor S4
EC.Number	E.C.3.4.21.109
Resolution	1.5(Å)
Affinity (Kd/Ki/IC50)	Ki=70.4pM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2012) J.Mol.Biol. Vol. 415: pp. 699-715

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): Q9Y5Y6
Entrez Gene ID	NCBI Entrez Gene ID: 6768
ASD	Information of known allosteric effects of PDB entries

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