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Browse entries in the PDBbind-CN Database

HEADER    RNA BINDING PROTEIN/RNA                 27-MAR-12   4ED5              
TITLE     CRYSTAL STRUCTURE OF THE TWO N-TERMINAL RRM DOMAINS OF HUR COMPLEXED  
TITLE    2 WITH RNA                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELAV-LIKE PROTEIN 1;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RRM1/RRM2 DOMAINS, UNP RESIDUES 18-186;                    
COMPND   5 SYNONYM: HU-ANTIGEN R, HUR;                                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-R(*A*UP*UP*UP*UP*UP*AP*UP*UP*UP*U)-3';                  
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 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: ELAVL1, HUR;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    RRM, RNA BINDING, NUCLEUS, RNA BINDING PROTEIN-RNA COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.WANG,F.ZENG,Q.LIU,L.NIU,M.TENG,X.LI                                 
REVDAT   2   10-APR-13 4ED5    1       JRNL                                     
REVDAT   1   23-MAY-12 4ED5    0                                                
JRNL        AUTH   H.WANG,F.ZENG,Q.LIU,H.LIU,Z.LIU,L.NIU,M.TENG,X.LI            
JRNL        TITL   THE STRUCTURE OF THE ARE-BINDING DOMAINS OF HU ANTIGEN R     
JRNL        TITL 2 (HUR) UNDERGOES CONFORMATIONAL CHANGES DURING RNA BINDING.   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69   373 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   23519412                                                     
JRNL        DOI    10.1107/S0907444912047828                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 26384                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1393                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1942                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2526                                    
REMARK   3   NUCLEIC ACID ATOMS       : 349                                     
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 252                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.15000                                             
REMARK   3    B22 (A**2) : 2.11000                                              
REMARK   3    B33 (A**2) : -1.35000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.52000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.318        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.884                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3035 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4151 ; 1.217 ; 2.121       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   343 ; 5.385 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;32.968 ;22.762       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   435 ;13.109 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;19.675 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   486 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2106 ; 0.005 ; 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):  1689 ; 0.416 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2705 ; 0.800 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1346 ; 1.507 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1446 ; 2.517 ; 4.500       
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  : 4                                          
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    18        A   185                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8556  -1.1936  -4.5015              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1441 T22:   0.0994                                     
REMARK   3      T33:   0.1499 T12:  -0.0011                                     
REMARK   3      T13:  -0.0129 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5405 L22:   0.1219                                     
REMARK   3      L33:   1.5511 L12:  -0.1034                                     
REMARK   3      L13:  -0.3070 L23:  -0.0270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0142 S12:   0.0176 S13:  -0.0037                       
REMARK   3      S21:   0.0312 S22:   0.0128 S23:  -0.0014                       
REMARK   3      S31:   0.0103 S32:   0.0527 S33:  -0.0270                       
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    18        B   186                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.4542   0.4721 -20.9817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1063 T22:   0.1695                                     
REMARK   3      T33:   0.1495 T12:   0.0356                                     
REMARK   3      T13:   0.0125 T23:   0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0883 L22:   0.1743                                     
REMARK   3      L33:   4.2709 L12:  -0.0283                                     
REMARK   3      L13:   0.3244 L23:   0.0954                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0358 S12:   0.2869 S13:   0.0389                       
REMARK   3      S21:   0.0214 S22:  -0.0231 S23:  -0.0103                       
REMARK   3      S31:  -0.0301 S32:  -0.3691 S33:  -0.0127                       
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     2        C    11                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.8444  -6.3734 -21.9508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2357 T22:   0.0902                                     
REMARK   3      T33:   0.0454 T12:  -0.0625                                     
REMARK   3      T13:   0.0588 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.6682 L22:   1.9439                                     
REMARK   3      L33:   7.6362 L12:  -1.9251                                     
REMARK   3      L13:  -1.4653 L23:   3.7514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1741 S12:   0.3790 S13:  -0.5320                       
REMARK   3      S21:   0.6175 S22:  -0.2868 S23:   0.2536                       
REMARK   3      S31:   1.2644 S32:  -0.5808 S33:   0.4608                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D    11                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3048  -8.0399  -4.4849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1592 T22:   0.0643                                     
REMARK   3      T33:   0.1059 T12:   0.0145                                     
REMARK   3      T13:   0.0289 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.8439 L22:   1.3730                                     
REMARK   3      L33:   7.0924 L12:  -0.1202                                     
REMARK   3      L13:  -9.1544 L23:   0.9660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6021 S12:  -0.2398 S13:  -0.8435                       
REMARK   3      S21:  -0.1607 S22:   0.0920 S23:  -0.1848                       
REMARK   3      S31:   0.3488 S32:   0.1920 S33:   0.5100                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4ED5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071467.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97930                            
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27777                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 5000, 0.1M HEPES, PH7.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 287K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       68.38500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.37500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       68.38500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.37500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9670 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   186                                                      
REMARK 465     LEU A   187                                                      
REMARK 465     GLU A   188                                                      
REMARK 465     HIS A   189                                                      
REMARK 465     HIS A   190                                                      
REMARK 465     HIS A   191                                                      
REMARK 465     HIS A   192                                                      
REMARK 465     HIS A   193                                                      
REMARK 465     HIS A   194                                                      
REMARK 465     LEU B   187                                                      
REMARK 465     GLU B   188                                                      
REMARK 465     HIS B   189                                                      
REMARK 465     HIS B   190                                                      
REMARK 465     HIS B   191                                                      
REMARK 465     HIS B   192                                                      
REMARK 465     HIS B   193                                                      
REMARK 465     HIS B   194                                                      
REMARK 465       A C     1                                                      
REMARK 465       A D     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  34    OD2                                                 
REMARK 470     ARG A  37    CZ   NH1  NH2                                       
REMARK 470     LYS A  50    CE   NZ                                             
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     LYS A  72    CG   CD   CE   NZ                                   
REMARK 470     ARG A  85    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  88    OG                                                  
REMARK 470     LYS A 120    CE   NZ                                             
REMARK 470     ILE A 152    CD1                                                 
REMARK 470     GLN B  29    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  30    CG   OD1  ND2                                       
REMARK 470     THR B  32    OG1  CG2                                            
REMARK 470     ASP B  34    CB   CG   OD1  OD2                                  
REMARK 470     GLU B  35    OE2                                                 
REMARK 470     ARG B  37    NH1  NH2                                            
REMARK 470     GLU B  45    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B  55    CG   CD   CE   NZ                                   
REMARK 470     VAL B  69    CG1  CG2                                            
REMARK 470     THR B  70    OG1  CG2                                            
REMARK 470     LYS B  72    CB   CG   CD   CE   NZ                              
REMARK 470     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  76    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR B  80    CG2                                                 
REMARK 470     SER B  88    OG                                                  
REMARK 470     ILE B  91    CD1                                                 
REMARK 470     THR B 116    OG1  CG2                                            
REMARK 470     GLN B 119    OE1  NE2                                            
REMARK 470     LYS B 120    CG   CD   CE   NZ                                   
REMARK 470     ASN B 134    OD1  ND2                                            
REMARK 470     ARG B 136    NE   CZ   NH1  NH2                                  
REMARK 470     VAL B 139    CG1                                                 
REMARK 470     ASP B 140    CG   OD1  OD2                                       
REMARK 470     THR B 142    CG2                                                 
REMARK 470     THR B 143    CG2                                                 
REMARK 470     GLU B 162    OE2                                                 
REMARK 470     GLU B 177    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 186    C    O    OD1                                       
REMARK 470       U C   2    P    OP1  OP2  O5'  C5'  C4'  O4'                   
REMARK 470       U C   2    C3'  C2'  O2'  C1'  N1   C2   O2                    
REMARK 470       U C   2    N3   C4   O4   C5   C6                              
REMARK 470       U C  11    O2'  N1   C2   O2   N3   C4   O4                    
REMARK 470       U C  11    C5   C6                                             
REMARK 470       U D   2    P    OP1  OP2  O5'  C5'  C4'  O4'                   
REMARK 470       U D   2    C3'  O3'  C2'  O2'  C1'  N1   C2                    
REMARK 470       U D   2    O2   N3   C5   C6                                   
REMARK 470       U D  11    O2'  N1   C2   O2   N3   C4   O4                    
REMARK 470       U D  11    C5   C6                                             
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   O4     U D     2     P      U D     3              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500      U D   2   C4      U D   2   O4      0.215                       
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    GLN A  87     -122.15     54.74                                   
REMARK 500    ASP B 105       56.97   -107.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M2M A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 102                 
DBREF  4ED5 A   18   186  UNP    Q15717   ELAV1_HUMAN     18    186             
DBREF  4ED5 B   18   186  UNP    Q15717   ELAV1_HUMAN     18    186             
DBREF  4ED5 C    1    11  PDB    4ED5     4ED5             1     11             
DBREF  4ED5 D    1    11  PDB    4ED5     4ED5             1     11             
SEQADV 4ED5 LEU A  187  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 GLU A  188  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS A  189  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS A  190  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS A  191  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS A  192  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS A  193  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS A  194  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 LEU B  187  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 GLU B  188  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS B  189  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS B  190  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS B  191  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS B  192  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS B  193  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4ED5 HIS B  194  UNP  Q15717              EXPRESSION TAG                 
SEQRES   1 A  177  GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO GLN ASN          
SEQRES   2 A  177  MET THR GLN ASP GLU LEU ARG SER LEU PHE SER SER ILE          
SEQRES   3 A  177  GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP LYS VAL          
SEQRES   4 A  177  ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN TYR VAL          
SEQRES   5 A  177  THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR LEU ASN          
SEQRES   6 A  177  GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL SER TYR          
SEQRES   7 A  177  ALA ARG PRO SER SER GLU VAL ILE LYS ASP ALA ASN LEU          
SEQRES   8 A  177  TYR ILE SER GLY LEU PRO ARG THR MET THR GLN LYS ASP          
SEQRES   9 A  177  VAL GLU ASP MET PHE SER ARG PHE GLY ARG ILE ILE ASN          
SEQRES  10 A  177  SER ARG VAL LEU VAL ASP GLN THR THR GLY LEU SER ARG          
SEQRES  11 A  177  GLY VAL ALA PHE ILE ARG PHE ASP LYS ARG SER GLU ALA          
SEQRES  12 A  177  GLU GLU ALA ILE THR SER PHE ASN GLY HIS LYS PRO PRO          
SEQRES  13 A  177  GLY SER SER GLU PRO ILE THR VAL LYS PHE ALA ALA ASN          
SEQRES  14 A  177  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  177  GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO GLN ASN          
SEQRES   2 B  177  MET THR GLN ASP GLU LEU ARG SER LEU PHE SER SER ILE          
SEQRES   3 B  177  GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP LYS VAL          
SEQRES   4 B  177  ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN TYR VAL          
SEQRES   5 B  177  THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR LEU ASN          
SEQRES   6 B  177  GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL SER TYR          
SEQRES   7 B  177  ALA ARG PRO SER SER GLU VAL ILE LYS ASP ALA ASN LEU          
SEQRES   8 B  177  TYR ILE SER GLY LEU PRO ARG THR MET THR GLN LYS ASP          
SEQRES   9 B  177  VAL GLU ASP MET PHE SER ARG PHE GLY ARG ILE ILE ASN          
SEQRES  10 B  177  SER ARG VAL LEU VAL ASP GLN THR THR GLY LEU SER ARG          
SEQRES  11 B  177  GLY VAL ALA PHE ILE ARG PHE ASP LYS ARG SER GLU ALA          
SEQRES  12 B  177  GLU GLU ALA ILE THR SER PHE ASN GLY HIS LYS PRO PRO          
SEQRES  13 B  177  GLY SER SER GLU PRO ILE THR VAL LYS PHE ALA ALA ASN          
SEQRES  14 B  177  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C   11    A   U   U   U   U   U   A   U   U   U   U                  
SEQRES   1 D   11    A   U   U   U   U   U   A   U   U   U   U                  
HET    GOL  A 201       6                                                       
HET    GOL  A 202       6                                                       
HET    GOL  A 203       6                                                       
HET    GOL  A 204       6                                                       
HET    GOL  A 205       6                                                       
HET    M2M  A 206       9                                                       
HET    EDO  A 207       4                                                       
HET    EDO  A 208       4                                                       
HET    GOL  D 101       6                                                       
HET    GOL  D 102       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     M2M 1-METHOXY-2-(2-METHOXYETHOXY)ETHANE                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  GOL    7(C3 H8 O3)                                                  
FORMUL  10  M2M    C6 H14 O3                                                    
FORMUL  11  EDO    2(C2 H6 O2)                                                  
FORMUL  15  HOH   *252(H2 O)                                                    
HELIX    1   1 THR A   32  SER A   42  1                                  11    
HELIX    2   2 THR A   70  ASN A   82  1                                  13    
HELIX    3   3 SER A  100  LYS A  104  5                                   5    
HELIX    4   4 THR A  118  SER A  127  1                                  10    
HELIX    5   5 ARG A  128  GLY A  130  5                                   3    
HELIX    6   6 LYS A  156  ASN A  168  1                                  13    
HELIX    7   7 THR B   32  SER B   42  1                                  11    
HELIX    8   8 THR B   70  ASN B   82  1                                  13    
HELIX    9   9 THR B  118  SER B  127  1                                  10    
HELIX   10  10 ARG B  128  GLY B  130  5                                   3    
HELIX   11  11 LYS B  156  ASN B  168  1                                  13    
SHEET    1   A 4 VAL A  46  ARG A  53  0                                        
SHEET    2   A 4 SER A  60  TYR A  68 -1  O  ASN A  67   N  SER A  48           
SHEET    3   A 4 ASN A  21  ASN A  25 -1  N  VAL A  24   O  GLY A  64           
SHEET    4   A 4 LYS A  92  TYR A  95 -1  O  SER A  94   N  ILE A  23           
SHEET    1   B 2 ARG A  85  LEU A  86  0                                        
SHEET    2   B 2 LYS A  89  THR A  90 -1  O  LYS A  89   N  LEU A  86           
SHEET    1   C 4 ILE A 132  VAL A 139  0                                        
SHEET    2   C 4 SER A 146  PHE A 154 -1  O  ARG A 147   N  LEU A 138           
SHEET    3   C 4 ASN A 107  SER A 111 -1  N  ILE A 110   O  ALA A 150           
SHEET    4   C 4 THR A 180  PHE A 183 -1  O  LYS A 182   N  TYR A 109           
SHEET    1   D 4 VAL B  46  ARG B  53  0                                        
SHEET    2   D 4 SER B  60  TYR B  68 -1  O  LEU B  61   N  ILE B  52           
SHEET    3   D 4 ASN B  21  ASN B  25 -1  N  VAL B  24   O  GLY B  64           
SHEET    4   D 4 LYS B  92  TYR B  95 -1  O  SER B  94   N  ILE B  23           
SHEET    1   E 2 ARG B  85  LEU B  86  0                                        
SHEET    2   E 2 LYS B  89  THR B  90 -1  O  LYS B  89   N  LEU B  86           
SHEET    1   F 4 ILE B 132  VAL B 139  0                                        
SHEET    2   F 4 SER B 146  PHE B 154 -1  O  ARG B 153   N  ILE B 133           
SHEET    3   F 4 ASN B 107  SER B 111 -1  N  LEU B 108   O  ILE B 152           
SHEET    4   F 4 THR B 180  PHE B 183 -1  O  LYS B 182   N  TYR B 109           
SITE     1 AC1 10 GLY A  18  THR A  20  VAL A  69  THR A  70                    
SITE     2 AC1 10 ALA A  71  GLY A 174  SER A 175  SER A 176                    
SITE     3 AC1 10 HOH A 344  HOH A 404                                          
SITE     1 AC2  6 THR A 118  GLN A 119  VAL A 137  VAL A 139                    
SITE     2 AC2  6 HOH A 355  HOH A 427                                          
SITE     1 AC3  4 SER A 146  ARG A 147  HOH A 380  HOH A 438                    
SITE     1 AC4  3 ASN A  21  GLU A  47  ASN A  67                               
SITE     1 AC5  4 SER A 111  GLU A 177  THR A 180  HOH A 433                    
SITE     1 AC6  8 ILE A  78  ASN A  82  ILE A  91  LYS A  92                    
SITE     2 AC6  8 VAL A  93  SER A  94  HOH A 374    U D   5                    
SITE     1 AC7  5 MET A 117  ASP A 121  HOH A 361  HOH A 424                    
SITE     2 AC7  5 HIS B  59                                                     
SITE     1 AC8  4 TYR A  95  HOH A 327  HOH A 374  HOH A 382                    
SITE     1 AC9  6 VAL A 139  ARG A 147    U D   3    U D   4                    
SITE     2 AC9  6   U D   5  HOH D 216                                          
SITE     1 BC1  9 TYR A  26  ASN A 134  ARG A 136  PHE A 151                    
SITE     2 BC1  9   U D   4    A D   7  HOH D 209  HOH D 210                    
SITE     3 BC1  9 HOH D 211                                                     
CRYST1  136.770   62.750   53.290  90.00 111.89  90.00 C 1 2 1       8          
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      0.007312  0.000000  0.002938        0.00000                         
SCALE2      0.000000  0.015936  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020223        0.00000                         
ATOM      1  N   GLY A  18     -23.762  11.874  13.324  1.00 16.71           N  
ANISOU    1  N   GLY A  18     2805   1575   1968    294    164   -119       N  
ATOM      2  CA  GLY A  18     -22.621  11.407  12.474  1.00 16.33           C  
ANISOU    2  CA  GLY A  18     2730   1517   1958    219    138   -125       C  
ATOM      3  C   GLY A  18     -22.741   9.937  12.084  1.00 15.69           C  
ANISOU    3  C   GLY A  18     2553   1502   1906    208    103    -90       C  
ATOM      4  O   GLY A  18     -23.452   9.180  12.731  1.00 15.58           O  
ANISOU    4  O   GLY A  18     2493   1544   1883    234     95    -70       O  
ATOM      5  N   ARG A  19     -22.034   9.536  11.031  1.00 15.35           N  
ANISOU    5  N   ARG A  19     2486   1452   1895    167     86    -84       N  
ATOM      6  CA  ARG A  19     -22.129   8.166  10.513  1.00 14.85           C  
ANISOU    6  CA  ARG A  19     2345   1438   1858    156     58    -54       C  
ATOM      7  C   ARG A  19     -21.394   7.160  11.411  1.00 14.66           C  
ANISOU    7  C   ARG A  19     2283   1454   1835    119     29    -64       C  
ATOM      8  O   ARG A  19     -20.305   7.479  11.957  1.00 14.82           O  
ANISOU    8  O   ARG A  19     2322   1465   1844     78     22    -99       O  
ATOM      9  CB  ARG A  19     -21.602   8.098   9.078  1.00 14.61           C  
ANISOU    9  CB  ARG A  19     2306   1387   1857    132     51    -46       C  
ATOM     10  CG  ARG A  19     -22.534   8.764   8.042  1.00 15.23           C  
ANISOU   10  CG  ARG A  19     2405   1449   1935    182     77    -21       C  
ATOM     11  CD  ARG A  19     -21.851   8.896   6.685  1.00 17.14           C  
ANISOU   11  CD  ARG A  19     2649   1664   2200    155     73    -18       C  
ATOM     12  NE  ARG A  19     -20.694   9.787   6.755  1.00 17.66           N  
ANISOU   12  NE  ARG A  19     2772   1675   2263    107     83    -53       N  
ATOM     13  CZ  ARG A  19     -19.825   9.970   5.767  1.00 18.08           C  
ANISOU   13  CZ  ARG A  19     2831   1706   2333     67     80    -57       C  
ATOM     14  NH1 ARG A  19     -19.975   9.327   4.616  1.00 17.37           N  
ANISOU   14  NH1 ARG A  19     2695   1640   2264     76     67    -31       N  
ATOM     15  NH2 ARG A  19     -18.806  10.796   5.940  1.00 18.05           N  
ANISOU   15  NH2 ARG A  19     2878   1659   2320     13     90    -91       N  
ATOM     16  N   THR A  20     -21.994   5.971  11.562  1.00 14.42           N  
ANISOU   16  N   THR A  20     2201   1468   1811    131     16    -33       N  
ATOM     17  CA  THR A  20     -21.456   4.897  12.434  1.00 14.32           C  
ANISOU   17  CA  THR A  20     2156   1491   1793    110     -6    -32       C  
ATOM     18  C   THR A  20     -21.151   3.570  11.724  1.00 13.97           C  
ANISOU   18  C   THR A  20     2072   1461   1776     91    -27     -9       C  
ATOM     19  O   THR A  20     -20.407   2.730  12.256  1.00 13.93           O  
ANISOU   19  O   THR A  20     2051   1476   1768     76    -45     -9       O  
ATOM     20  CB  THR A  20     -22.404   4.582  13.617  1.00 14.50           C  
ANISOU   20  CB  THR A  20     2168   1551   1790    141      2    -16       C  
ATOM     21  OG1 THR A  20     -23.669   4.108  13.133  1.00 14.43           O  
ANISOU   21  OG1 THR A  20     2131   1565   1787    164     11     20       O  
ATOM     22  CG2 THR A  20     -22.613   5.798  14.507  1.00 14.90           C  
ANISOU   22  CG2 THR A  20     2263   1591   1808    164     22    -43       C  
ATOM     23  N   ASN A  21     -21.716   3.385  10.532  1.00 13.80           N  
ANISOU   23  N   ASN A  21     2036   1430   1775     95    -24     10       N  
ATOM     24  CA  ASN A  21     -21.692   2.103   9.827  1.00 13.55           C  
ANISOU   24  CA  ASN A  21     1974   1409   1766     78    -38     31       C  
ATOM     25  C   ASN A  21     -20.588   2.043   8.763  1.00 13.36           C  
ANISOU   25  C   ASN A  21     1949   1363   1763     55    -52     18       C  
ATOM     26  O   ASN A  21     -20.508   2.916   7.882  1.00 13.34           O  
ANISOU   26  O   ASN A  21     1960   1340   1769     54    -44      8       O  
ATOM     27  CB  ASN A  21     -23.063   1.850   9.201  1.00 13.56           C  
ANISOU   27  CB  ASN A  21     1953   1429   1769     90    -26     57       C  
ATOM     28  CG  ASN A  21     -23.260   0.412   8.756  1.00 13.44           C  
ANISOU   28  CG  ASN A  21     1914   1426   1768     64    -37     76       C  
ATOM     29  OD1 ASN A  21     -22.741  -0.525   9.359  1.00 13.45           O  
ANISOU   29  OD1 ASN A  21     1918   1423   1768     51    -46     81       O  
ATOM     30  ND2 ASN A  21     -24.028   0.237   7.687  1.00 13.42           N  
ANISOU   30  ND2 ASN A  21     1890   1437   1772     58    -33     88       N  
ATOM     31  N   LEU A  22     -19.739   1.021   8.865  1.00 13.27           N  
ANISOU   31  N   LEU A  22     1926   1360   1757     42    -69     19       N  
ATOM     32  CA  LEU A  22     -18.585   0.864   7.969  1.00 13.15           C  
ANISOU   32  CA  LEU A  22     1905   1337   1755     25    -83      7       C  
ATOM     33  C   LEU A  22     -18.730  -0.377   7.103  1.00 13.00           C  
ANISOU   33  C   LEU A  22     1872   1313   1754     24    -90     26       C  
ATOM     34  O   LEU A  22     -19.258  -1.389   7.554  1.00 13.06           O  
ANISOU   34  O   LEU A  22     1880   1324   1758     28    -89     45       O  
ATOM     35  CB  LEU A  22     -17.270   0.786   8.776  1.00 13.30           C  
ANISOU   35  CB  LEU A  22     1920   1379   1754     19    -97    -11       C  
ATOM     36  CG  LEU A  22     -17.026   1.919   9.783  1.00 13.55           C  
ANISOU   36  CG  LEU A  22     1968   1420   1761     10    -91    -37       C  
ATOM     37  CD1 LEU A  22     -15.811   1.664  10.661  1.00 13.77           C  
ANISOU   37  CD1 LEU A  22     1980   1492   1760      3   -107    -53       C  
ATOM     38  CD2 LEU A  22     -16.862   3.243   9.064  1.00 13.61           C  
ANISOU   38  CD2 LEU A  22     1997   1398   1774    -13    -79    -60       C  
ATOM     39  N   ILE A  23     -18.303  -0.274   5.852  1.00 12.87           N  
ANISOU   39  N   ILE A  23     1849   1286   1753     15    -95     19       N  
ATOM     40  CA  ILE A  23     -18.117  -1.463   5.020  1.00 12.79           C  
ANISOU   40  CA  ILE A  23     1833   1270   1756     13   -103     28       C  
ATOM     41  C   ILE A  23     -16.630  -1.795   5.006  1.00 12.84           C  
ANISOU   41  C   ILE A  23     1834   1288   1755     19   -118     17       C  
ATOM     42  O   ILE A  23     -15.793  -0.916   4.920  1.00 12.86           O  
ANISOU   42  O   ILE A  23     1830   1306   1752     10   -122     -2       O  
ATOM     43  CB  ILE A  23     -18.690  -1.295   3.587  1.00 12.66           C  
ANISOU   43  CB  ILE A  23     1807   1246   1756      3    -99     30       C  
ATOM     44  CG1 ILE A  23     -18.639  -2.622   2.810  1.00 12.65           C  
ANISOU   44  CG1 ILE A  23     1807   1237   1764     -3   -105     35       C  
ATOM     45  CG2 ILE A  23     -18.013  -0.109   2.802  1.00 12.60           C  
ANISOU   45  CG2 ILE A  23     1797   1236   1753     -1    -98     14       C  
ATOM     46  CD1 ILE A  23     -19.429  -2.599   1.542  1.00 12.60           C  
ANISOU   46  CD1 ILE A  23     1787   1233   1767    -16   -101     36       C  
ATOM     47  N   VAL A  24     -16.309  -3.073   5.120  1.00 12.93           N  
ANISOU   47  N   VAL A  24     1854   1298   1762     36   -123     28       N  
ATOM     48  CA  VAL A  24     -14.926  -3.507   5.217  1.00 13.08           C  
ANISOU   48  CA  VAL A  24     1865   1341   1764     58   -135     23       C  
ATOM     49  C   VAL A  24     -14.683  -4.506   4.088  1.00 13.08           C  
ANISOU   49  C   VAL A  24     1874   1322   1774     70   -137     27       C  
ATOM     50  O   VAL A  24     -15.288  -5.578   4.075  1.00 13.18           O  
ANISOU   50  O   VAL A  24     1915   1302   1791     76   -129     42       O  
ATOM     51  CB  VAL A  24     -14.644  -4.167   6.595  1.00 13.34           C  
ANISOU   51  CB  VAL A  24     1908   1390   1770     86   -136     37       C  
ATOM     52  CG1 VAL A  24     -13.130  -4.441   6.768  1.00 13.58           C  
ANISOU   52  CG1 VAL A  24     1920   1469   1772    118   -150     31       C  
ATOM     53  CG2 VAL A  24     -15.162  -3.282   7.745  1.00 13.36           C  
ANISOU   53  CG2 VAL A  24     1907   1407   1762     73   -132     32       C  
ATOM     54  N   ASN A  25     -13.830  -4.137   3.137  1.00 13.03           N  
ANISOU   54  N   ASN A  25     1847   1335   1769     69   -145     12       N  
ATOM     55  CA  ASN A  25     -13.605  -4.935   1.928  1.00 13.04           C  
ANISOU   55  CA  ASN A  25     1855   1321   1778     81   -146     12       C  
ATOM     56  C   ASN A  25     -12.217  -5.559   1.987  1.00 13.31           C  
ANISOU   56  C   ASN A  25     1882   1390   1786    125   -155     11       C  
ATOM     57  O   ASN A  25     -11.372  -5.093   2.753  1.00 13.45           O  
ANISOU   57  O   ASN A  25     1874   1458   1780    134   -163      7       O  
ATOM     58  CB  ASN A  25     -13.729  -4.041   0.686  1.00 12.82           C  
ANISOU   58  CB  ASN A  25     1807   1297   1768     53   -147     -2       C  
ATOM     59  CG  ASN A  25     -15.153  -3.560   0.453  1.00 12.82           C  
ANISOU   59  CG  ASN A  25     1812   1271   1786     25   -136      3       C  
ATOM     60  OD1 ASN A  25     -16.004  -4.311  -0.059  1.00 15.28           O  
ANISOU   60  OD1 ASN A  25     2138   1561   2108     17   -131      8       O  
ATOM     61  ND2 ASN A  25     -15.425  -2.312   0.814  1.00 12.57           N  
ANISOU   61  ND2 ASN A  25     1772   1247   1756      9   -131      0       N  
ATOM     62  N   TYR A  26     -11.995  -6.598   1.178  1.00 13.45           N  
ANISOU   62  N   TYR A  26     1921   1387   1802    153   -153     14       N  
ATOM     63  CA  TYR A  26     -10.706  -7.305   1.067  1.00 13.79           C  
ANISOU   63  CA  TYR A  26     1959   1465   1814    211   -158     16       C  
ATOM     64  C   TYR A  26     -10.356  -8.057   2.354  1.00 14.14           C  
ANISOU   64  C   TYR A  26     2026   1519   1829    261   -155     36       C  
ATOM     65  O   TYR A  26      -9.215  -8.050   2.806  1.00 14.43           O  
ANISOU   65  O   TYR A  26     2032   1622   1829    303   -163     39       O  
ATOM     66  CB  TYR A  26      -9.570  -6.368   0.618  1.00 13.79           C  
ANISOU   66  CB  TYR A  26     1901   1539   1799    205   -171      0       C  
ATOM     67  CG  TYR A  26     -10.002  -5.512  -0.545  1.00 14.76           C  
ANISOU   67  CG  TYR A  26     2009   1650   1951    155   -170    -15       C  
ATOM     68  CD1 TYR A  26     -10.344  -6.103  -1.764  1.00 16.68           C  
ANISOU   68  CD1 TYR A  26     2270   1859   2208    160   -166    -18       C  
ATOM     69  CD2 TYR A  26     -10.154  -4.134  -0.409  1.00 14.96           C  
ANISOU   69  CD2 TYR A  26     2009   1691   1986    104   -171    -25       C  
ATOM     70  CE1 TYR A  26     -10.785  -5.342  -2.827  1.00 18.29           C  
ANISOU   70  CE1 TYR A  26     2458   2057   2433    121   -164    -27       C  
ATOM     71  CE2 TYR A  26     -10.588  -3.347  -1.484  1.00 16.86           C  
ANISOU   71  CE2 TYR A  26     2242   1915   2248     67   -166    -32       C  
ATOM     72  CZ  TYR A  26     -10.894  -3.972  -2.688  1.00 18.74           C  
ANISOU   72  CZ  TYR A  26     2490   2132   2499     78   -164    -31       C  
ATOM     73  OH  TYR A  26     -11.335  -3.232  -3.760  1.00 22.28           O  
ANISOU   73  OH  TYR A  26     2930   2573   2964     49   -159    -35       O  
ATOM     74  N   LEU A  27     -11.361  -8.701   2.937  1.00 14.18           N  
ANISOU   74  N   LEU A  27     2080   1463   1845    254   -141     53       N  
ATOM     75  CA  LEU A  27     -11.138  -9.565   4.097  1.00 14.58           C  
ANISOU   75  CA  LEU A  27     2165   1510   1866    306   -133     79       C  
ATOM     76  C   LEU A  27     -10.490 -10.869   3.639  1.00 15.05           C  
ANISOU   76  C   LEU A  27     2272   1543   1902    375   -122     91       C  
ATOM     77  O   LEU A  27     -10.731 -11.326   2.516  1.00 15.03           O  
ANISOU   77  O   LEU A  27     2299   1496   1916    365   -115     79       O  
ATOM     78  CB  LEU A  27     -12.447  -9.858   4.840  1.00 14.54           C  
ANISOU   78  CB  LEU A  27     2201   1447   1877    271   -118     95       C  
ATOM     79  CG  LEU A  27     -13.179  -8.662   5.449  1.00 14.58           C  
ANISOU   79  CG  LEU A  27     2167   1474   1897    217   -124     87       C  
ATOM     80  CD1 LEU A  27     -14.436  -9.099   6.168  1.00 14.24           C  
ANISOU   80  CD1 LEU A  27     2163   1386   1864    190   -107    106       C  
ATOM     81  CD2 LEU A  27     -12.253  -7.885   6.400  1.00 14.26           C  
ANISOU   81  CD2 LEU A  27     2081   1509   1827    238   -138     82       C  
ATOM     82  N   PRO A  28      -9.630 -11.458   4.487  1.00 15.52           N  
ANISOU   82  N   PRO A  28     2342   1638   1918    452   -119    113       N  
ATOM     83  CA  PRO A  28      -9.152 -12.786   4.121  1.00 16.12           C  
ANISOU   83  CA  PRO A  28     2482   1674   1968    529   -101    130       C  
ATOM     84  C   PRO A  28     -10.304 -13.760   3.946  1.00 17.43           C  
ANISOU   84  C   PRO A  28     2742   1722   2158    500    -75    139       C  
ATOM     85  O   PRO A  28     -11.321 -13.659   4.649  1.00 16.86           O  
ANISOU   85  O   PRO A  28     2687   1615   2104    446    -67    149       O  
ATOM     86  CB  PRO A  28      -8.266 -13.181   5.304  1.00 16.60           C  
ANISOU   86  CB  PRO A  28     2539   1793   1974    617   -100    160       C  
ATOM     87  CG  PRO A  28      -7.693 -11.859   5.775  1.00 16.32           C  
ANISOU   87  CG  PRO A  28     2403   1870   1928    588   -127    143       C  
ATOM     88  CD  PRO A  28      -8.877 -10.885   5.616  1.00 15.66           C  
ANISOU   88  CD  PRO A  28     2305   1746   1899    479   -133    121       C  
ATOM     89  N   GLN A  29     -10.131 -14.693   3.008  1.00 19.10           N  
ANISOU   89  N   GLN A  29     3014   1877   2364    531    -59    134       N  
ATOM     90  CA  GLN A  29     -11.129 -15.707   2.700  1.00 21.03           C  
ANISOU   90  CA  GLN A  29     3357   2007   2625    495    -31    136       C  
ATOM     91  C   GLN A  29     -11.635 -16.478   3.898  1.00 21.62           C  
ANISOU   91  C   GLN A  29     3504   2025   2686    506     -6    172       C  
ATOM     92  O   GLN A  29     -12.809 -16.817   3.956  1.00 21.56           O  
ANISOU   92  O   GLN A  29     3544   1946   2700    430     12    172       O  
ATOM     93  CB  GLN A  29     -10.591 -16.700   1.667  1.00 21.84           C  
ANISOU   93  CB  GLN A  29     3527   2061   2710    550    -15    125       C  
ATOM     94  CG  GLN A  29     -10.865 -16.291   0.243  1.00 24.97           C  
ANISOU   94  CG  GLN A  29     3893   2459   3137    491    -27     85       C  
ATOM     95  CD  GLN A  29     -12.348 -16.324  -0.114  1.00 28.52           C  
ANISOU   95  CD  GLN A  29     4369   2843   3623    378    -19     67       C  
ATOM     96  OE1 GLN A  29     -12.779 -15.599  -1.000  1.00 29.91           O  
ANISOU   96  OE1 GLN A  29     4491   3048   3826    316    -35     39       O  
ATOM     97  NE2 GLN A  29     -13.130 -17.168   0.576  1.00 30.45           N  
ANISOU   97  NE2 GLN A  29     4696   3008   3865    351      9     85       N  
ATOM     98  N   ASN A  30     -10.747 -16.750   4.849  1.00 22.74           N  
ANISOU   98  N   ASN A  30     3650   2207   2785    600     -2    204       N  
ATOM     99  CA  ASN A  30     -11.097 -17.570   6.004  1.00 23.59           C  
ANISOU   99  CA  ASN A  30     3834   2261   2870    627     26    246       C  
ATOM    100  C   ASN A  30     -11.394 -16.785   7.275  1.00 22.88           C  
ANISOU  100  C   ASN A  30     3682   2233   2778    603     12    263       C  
ATOM    101  O   ASN A  30     -11.537 -17.370   8.342  1.00 22.79           O  
ANISOU  101  O   ASN A  30     3721   2198   2741    637     32    301       O  
ATOM    102  CB  ASN A  30      -9.996 -18.609   6.266  1.00 24.98           C  
ANISOU  102  CB  ASN A  30     4075   2427   2988    763     47    279       C  
ATOM    103  CG  ASN A  30      -8.672 -17.981   6.712  1.00 26.59           C  
ANISOU  103  CG  ASN A  30     4184   2770   3150    852     19    287       C  
ATOM    104  OD1 ASN A  30      -7.688 -18.690   6.907  1.00 31.20           O  
ANISOU  104  OD1 ASN A  30     4800   3376   3679    974     32    314       O  
ATOM    105  ND2 ASN A  30      -8.645 -16.667   6.881  1.00 26.83           N  
ANISOU  105  ND2 ASN A  30     4100   2895   3199    793    -16    263       N  
ATOM    106  N   MET A  31     -11.482 -15.461   7.168  1.00 22.10           N  
ANISOU  106  N   MET A  31     3481   2212   2705    546    -21    234       N  
ATOM    107  CA  MET A  31     -11.848 -14.648   8.321  1.00 21.58           C  
ANISOU  107  CA  MET A  31     3362   2201   2639    516    -33    243       C  
ATOM    108  C   MET A  31     -13.300 -14.903   8.700  1.00 21.06           C  
ANISOU  108  C   MET A  31     3341   2062   2598    438    -12    253       C  
ATOM    109  O   MET A  31     -14.172 -14.924   7.841  1.00 21.47           O  
ANISOU  109  O   MET A  31     3408   2063   2685    364     -7    232       O  
ATOM    110  CB  MET A  31     -11.650 -13.157   8.034  1.00 21.88           C  
ANISOU  110  CB  MET A  31     3294   2322   2695    469    -66    206       C  
ATOM    111  CG  MET A  31     -11.633 -12.316   9.293  1.00 23.20           C  
ANISOU  111  CG  MET A  31     3407   2560   2846    463    -79    211       C  
ATOM    112  SD  MET A  31     -11.244 -10.584   8.996  1.00 27.22           S  
ANISOU  112  SD  MET A  31     3814   3159   3370    411   -112    167       S  
ATOM    113  CE  MET A  31     -10.773 -10.121  10.655  1.00 25.55           C  
ANISOU  113  CE  MET A  31     3562   3033   3111    441   -122    179       C  
ATOM    114  N   THR A  32     -13.558 -15.074   9.988  1.00 20.43           N  
ANISOU  114  N   THR A  32     3276   1990   2497    453     -1    286       N  
ATOM    115  CA  THR A  32     -14.914 -15.307  10.461  1.00 19.86           C  
ANISOU  115  CA  THR A  32     3241   1865   2442    379     19    300       C  
ATOM    116  C   THR A  32     -15.539 -14.025  10.957  1.00 18.78           C  
ANISOU  116  C   THR A  32     3020   1793   2323    322     -2    283       C  
ATOM    117  O   THR A  32     -14.842 -13.021  11.159  1.00 18.08           O  
ANISOU  117  O   THR A  32     2858   1785   2227    345    -29    265       O  
ATOM    118  CB  THR A  32     -14.943 -16.345  11.591  1.00 20.36           C  
ANISOU  118  CB  THR A  32     3381   1887   2467    428     50    351       C  
ATOM    119  OG1 THR A  32     -14.331 -15.790  12.764  1.00 21.09           O  
ANISOU  119  OG1 THR A  32     3418   2068   2525    485     35    368       O  
ATOM    120  CG2 THR A  32     -14.188 -17.613  11.173  1.00 21.89           C  
ANISOU  120  CG2 THR A  32     3670   2013   2634    506     76    372       C  
ATOM    121  N   GLN A  33     -16.857 -14.062  11.133  1.00 18.37           N  
ANISOU  121  N   GLN A  33     2981   1708   2289    246     13    288       N  
ATOM    122  CA  GLN A  33     -17.602 -12.937  11.682  1.00 17.63           C  
ANISOU  122  CA  GLN A  33     2820   1671   2206    200      0    277       C  
ATOM    123  C   GLN A  33     -17.102 -12.598  13.084  1.00 17.90           C  
ANISOU  123  C   GLN A  33     2831   1765   2206    253     -6    297       C  
ATOM    124  O   GLN A  33     -16.950 -11.425  13.409  1.00 16.74           O  
ANISOU  124  O   GLN A  33     2617   1685   2060    249    -28    275       O  
ATOM    125  CB  GLN A  33     -19.103 -13.238  11.704  1.00 18.02           C  
ANISOU  125  CB  GLN A  33     2892   1685   2270    117     22    286       C  
ATOM    126  CG  GLN A  33     -19.976 -12.088  12.185  1.00 17.66           C  
ANISOU  126  CG  GLN A  33     2777   1701   2232     77     12    275       C  
ATOM    127  CD  GLN A  33     -21.434 -12.298  11.829  1.00 21.42           C  
ANISOU  127  CD  GLN A  33     3257   2161   2721     -7     29    276       C  
ATOM    128  OE1 GLN A  33     -21.808 -12.298  10.650  1.00 19.56           O  
ANISOU  128  OE1 GLN A  33     3014   1911   2508    -51     26    252       O  
ATOM    129  NE2 GLN A  33     -22.271 -12.494  12.853  1.00 21.95           N  
ANISOU  129  NE2 GLN A  33     3329   2241   2769    -32     48    304       N  
ATOM    130  N   ASP A  34     -16.829 -13.626  13.899  1.00 18.31           N  
ANISOU  130  N   ASP A  34     2943   1791   2224    303     16    339       N  
ATOM    131  CA  ASP A  34     -16.313 -13.423  15.253  0.50 18.60           C  
ANISOU  131  CA  ASP A  34     2958   1890   2218    361     11    362       C  
ATOM    132  C   ASP A  34     -14.969 -12.705  15.237  1.00 17.80           C  
ANISOU  132  C   ASP A  34     2794   1872   2096    419    -20    338       C  
ATOM    133  O   ASP A  34     -14.719 -11.839  16.068  1.00 18.08           O  
ANISOU  133  O   ASP A  34     2773   1985   2111    427    -37    327       O  
ATOM    134  CB  ASP A  34     -16.182 -14.753  15.999  1.00 20.27           C  
ANISOU  134  CB  ASP A  34     3254   2055   2393    416     44    416       C  
ATOM    135  CG  ASP A  34     -17.523 -15.415  16.264  1.00 22.59           C  
ANISOU  135  CG  ASP A  34     3607   2279   2698    347     78    443       C  
ATOM    136  OD1 ASP A  34     -18.528 -14.681  16.440  1.00 25.45           O  
ANISOU  136  OD1 ASP A  34     3922   2668   3079    276     72    428       O  
ATOM    137  N   GLU A  35     -14.108 -13.069  14.291  1.00 17.80           N  
ANISOU  137  N   GLU A  35     2806   1860   2099    456    -25    328       N  
ATOM    138  CA  GLU A  35     -12.800 -12.431  14.123  1.00 17.13           C  
ANISOU  138  CA  GLU A  35     2656   1861   1991    502    -54    304       C  
ATOM    139  C   GLU A  35     -12.908 -10.961  13.663  1.00 16.66           C  
ANISOU  139  C   GLU A  35     2521   1848   1962    435    -81    253       C  
ATOM    140  O   GLU A  35     -12.179 -10.081  14.165  1.00 16.40           O  
ANISOU  140  O   GLU A  35     2425   1903   1903    444   -103    232       O  
ATOM    141  CB  GLU A  35     -11.936 -13.240  13.166  1.00 17.65           C  
ANISOU  141  CB  GLU A  35     2756   1903   2049    560    -49    308       C  
ATOM    142  CG  GLU A  35     -11.473 -14.611  13.723  1.00 20.01           C  
ANISOU  142  CG  GLU A  35     3132   2171   2300    657    -22    360       C  
ATOM    143  CD  GLU A  35     -10.799 -15.484  12.673  1.00 22.56           C  
ANISOU  143  CD  GLU A  35     3505   2448   2617    714    -11    363       C  
ATOM    144  OE1 GLU A  35     -10.195 -16.514  13.033  1.00 24.21           O  
ANISOU  144  OE1 GLU A  35     3775   2643   2780    813     11    403       O  
ATOM    145  OE2 GLU A  35     -10.864 -15.141  11.477  1.00 25.76           O  
ANISOU  145  OE2 GLU A  35     3892   2834   3060    667    -22    326       O  
ATOM    146  N   LEU A  36     -13.836 -10.705  12.746  1.00 15.85           N  
ANISOU  146  N   LEU A  36     2427   1688   1908    366    -77    235       N  
ATOM    147  CA  LEU A  36     -14.137  -9.347  12.300  1.00 15.32           C  
ANISOU  147  CA  LEU A  36     2303   1647   1869    305    -94    194       C  
ATOM    148  C   LEU A  36     -14.584  -8.494  13.478  1.00 15.26           C  
ANISOU  148  C   LEU A  36     2267   1684   1848    286    -98    190       C  
ATOM    149  O   LEU A  36     -14.036  -7.412  13.694  1.00 15.13           O  
ANISOU  149  O   LEU A  36     2202   1727   1821    276   -116    159       O  
ATOM    150  CB  LEU A  36     -15.209  -9.347  11.198  1.00 14.98           C  
ANISOU  150  CB  LEU A  36     2279   1540   1874    244    -85    183       C  
ATOM    151  CG  LEU A  36     -15.621  -7.967  10.638  1.00 14.83           C  
ANISOU  151  CG  LEU A  36     2212   1542   1883    191    -98    148       C  
ATOM    152  CD1 LEU A  36     -14.463  -7.358   9.855  1.00 14.35           C  
ANISOU  152  CD1 LEU A  36     2114   1517   1822    202   -117    120       C  
ATOM    153  CD2 LEU A  36     -16.876  -8.089   9.757  1.00 14.29           C  
ANISOU  153  CD2 LEU A  36     2158   1423   1849    138    -86    146       C  
ATOM    154  N   ARG A  37     -15.564  -8.985  14.242  1.00 15.42           N  
ANISOU  154  N   ARG A  37     2320   1675   1866    277    -79    219       N  
ATOM    155  CA  ARG A  37     -16.048  -8.271  15.436  0.50 15.44           C  
ANISOU  155  CA  ARG A  37     2298   1720   1849    266    -79    217       C  
ATOM    156  C   ARG A  37     -14.926  -7.969  16.438  1.00 16.23           C  
ANISOU  156  C   ARG A  37     2366   1900   1900    315    -94    213       C  
ATOM    157  O   ARG A  37     -14.811  -6.834  16.919  1.00 16.67           O  
ANISOU  157  O   ARG A  37     2382   2007   1945    294   -108    181       O  
ATOM    158  CB  ARG A  37     -17.175  -9.043  16.120  1.00 15.69           C  
ANISOU  158  CB  ARG A  37     2369   1714   1876    255    -53    256       C  
ATOM    159  CG  ARG A  37     -17.809  -8.312  17.330  1.00 17.82           C  
ANISOU  159  CG  ARG A  37     2614   2030   2126    245    -51    256       C  
ATOM    160  CD  ARG A  37     -18.703  -9.240  18.129  1.00 20.35           C  
ANISOU  160  CD  ARG A  37     2974   2326   2431    243    -24    302       C  
ATOM    161  NE  ARG A  37     -20.048  -9.289  17.563  1.00 22.65           N  
ANISOU  161  NE  ARG A  37     3273   2579   2753    180     -8    305       N  
ATOM    162  N   SER A  38     -14.090  -8.968  16.725  1.00 16.62           N  
ANISOU  162  N   SER A  38     2436   1963   1916    380    -91    243       N  
ATOM    163  CA  SER A  38     -13.017  -8.826  17.718  1.00 17.96           C  
ANISOU  163  CA  SER A  38     2570   2226   2027    434   -105    244       C  
ATOM    164  C   SER A  38     -11.970  -7.832  17.302  1.00 17.27           C  
ANISOU  164  C   SER A  38     2420   2210   1930    420   -133    197       C  
ATOM    165  O   SER A  38     -11.556  -6.995  18.116  1.00 17.69           O  
ANISOU  165  O   SER A  38     2429   2343   1949    411   -148    171       O  
ATOM    166  CB  SER A  38     -12.333 -10.169  18.022  1.00 17.94           C  
ANISOU  166  CB  SER A  38     2606   2226   1985    522    -93    292       C  
ATOM    167  OG  SER A  38     -13.243 -11.013  18.682  1.00 21.67           O  
ANISOU  167  OG  SER A  38     3138   2640   2454    530    -65    338       O  
ATOM    168  N   LEU A  39     -11.540  -7.928  16.045  1.00 16.89           N  
ANISOU  168  N   LEU A  39     2372   2138   1908    414   -138    184       N  
ATOM    169  CA  LEU A  39     -10.598  -6.968  15.476  1.00 16.96           C  
ANISOU  169  CA  LEU A  39     2323   2209   1912    388   -161    139       C  
ATOM    170  C   LEU A  39     -11.091  -5.529  15.626  1.00 16.38           C  
ANISOU  170  C   LEU A  39     2226   2141   1858    311   -167     96       C  
ATOM    171  O   LEU A  39     -10.342  -4.658  16.057  1.00 17.59           O  
ANISOU  171  O   LEU A  39     2334   2371   1978    290   -183     62       O  
ATOM    172  CB  LEU A  39     -10.332  -7.272  13.996  1.00 16.48           C  
ANISOU  172  CB  LEU A  39     2272   2104   1884    384   -161    134       C  
ATOM    173  CG  LEU A  39      -9.630  -6.170  13.181  1.00 17.16           C  
ANISOU  173  CG  LEU A  39     2307   2235   1979    336   -179     88       C  
ATOM    174  CD1 LEU A  39      -8.225  -5.852  13.750  1.00 18.96           C  
ANISOU  174  CD1 LEU A  39     2472   2589   2144    360   -198     72       C  
ATOM    175  CD2 LEU A  39      -9.553  -6.524  11.697  1.00 15.47           C  
ANISOU  175  CD2 LEU A  39     2107   1971   1801    333   -176     87       C  
ATOM    176  N   PHE A  40     -12.332  -5.275  15.227  1.00 15.40           N  
ANISOU  176  N   PHE A  40     2134   1937   1782    269   -154     96       N  
ATOM    177  CA  PHE A  40     -12.890  -3.921  15.286  1.00 15.15           C  
ANISOU  177  CA  PHE A  40     2091   1898   1767    209   -154     59       C  
ATOM    178  C   PHE A  40     -13.277  -3.445  16.704  1.00 15.37           C  
ANISOU  178  C   PHE A  40     2116   1961   1763    208   -151     53       C  
ATOM    179  O   PHE A  40     -13.383  -2.255  16.938  1.00 15.34           O  
ANISOU  179  O   PHE A  40     2104   1969   1756    167   -153     16       O  
ATOM    180  CB  PHE A  40     -14.057  -3.775  14.310  1.00 14.71           C  
ANISOU  180  CB  PHE A  40     2063   1760   1766    175   -140     62       C  
ATOM    181  CG  PHE A  40     -13.615  -3.515  12.897  1.00 14.47           C  
ANISOU  181  CG  PHE A  40     2023   1709   1764    153   -147     44       C  
ATOM    182  CD1 PHE A  40     -13.101  -4.552  12.114  1.00 14.50           C  
ANISOU  182  CD1 PHE A  40     2034   1701   1773    184   -149     63       C  
ATOM    183  CD2 PHE A  40     -13.688  -2.233  12.355  1.00 14.27           C  
ANISOU  183  CD2 PHE A  40     1989   1676   1756    107   -148      9       C  
ATOM    184  CE1 PHE A  40     -12.668  -4.317  10.808  1.00 14.37           C  
ANISOU  184  CE1 PHE A  40     2006   1674   1780    166   -155     46       C  
ATOM    185  CE2 PHE A  40     -13.269  -1.982  11.036  1.00 14.27           C  
ANISOU  185  CE2 PHE A  40     1981   1661   1779     87   -152     -4       C  
ATOM    186  CZ  PHE A  40     -12.757  -3.035  10.260  1.00 14.07           C  
ANISOU  186  CZ  PHE A  40     1954   1633   1760    116   -157     14       C  
ATOM    187  N  ASER A  41     -13.468  -4.384  17.629  0.50 15.65           N  
ANISOU  187  N  ASER A  41     2165   2010   1772    254   -144     92       N  
ATOM    188  N  BSER A  41     -13.470  -4.384  17.629  0.50 15.65           N  
ANISOU  188  N  BSER A  41     2165   2010   1772    254   -144     92       N  
ATOM    189  CA ASER A  41     -13.801  -4.037  19.014  0.50 15.91           C  
ANISOU  189  CA ASER A  41     2193   2084   1768    260   -141     90       C  
ATOM    190  CA BSER A  41     -13.795  -4.037  19.017  0.50 15.91           C  
ANISOU  190  CA BSER A  41     2193   2085   1768    260   -141     90       C  
ATOM    191  C  ASER A  41     -12.644  -3.359  19.757  0.50 16.30           C  
ANISOU  191  C  ASER A  41     2198   2231   1763    260   -161     54       C  
ATOM    192  C  BSER A  41     -12.646  -3.340  19.745  0.50 16.29           C  
ANISOU  192  C  BSER A  41     2198   2230   1763    259   -161     53       C  
ATOM    193  O  ASER A  41     -12.857  -2.733  20.797  0.50 16.51           O  
ANISOU  193  O  ASER A  41     2218   2296   1759    249   -161     35       O  
ATOM    194  O  BSER A  41     -12.866  -2.685  20.765  0.50 16.49           O  
ANISOU  194  O  BSER A  41     2216   2293   1758    246   -161     33       O  
ATOM    195  CB ASER A  41     -14.288  -5.263  19.787  0.50 16.17           C  
ANISOU  195  CB ASER A  41     2255   2107   1784    310   -126    146       C  
ATOM    196  CB BSER A  41     -14.242  -5.267  19.805  0.50 16.19           C  
ANISOU  196  CB BSER A  41     2255   2112   1784    311   -126    146       C  
ATOM    197  OG ASER A  41     -13.251  -6.218  19.928  0.50 16.56           O  
ANISOU  197  OG ASER A  41     2299   2195   1797    370   -131    173       O  
ATOM    198  OG BSER A  41     -15.425  -5.815  19.260  0.50 15.93           O  
ANISOU  198  OG BSER A  41     2262   1997   1795    294   -106    174       O  
ATOM    199  N   SER A  42     -11.428  -3.484  19.224  1.00 16.45           N  
ANISOU  199  N   SER A  42     2186   2299   1765    269   -177     43       N  
ATOM    200  CA  SER A  42     -10.257  -2.783  19.786  1.00 17.70           C  
ANISOU  200  CA  SER A  42     2292   2565   1867    253   -198      2       C  
ATOM    201  C   SER A  42     -10.409  -1.251  19.746  1.00 17.62           C  
ANISOU  201  C   SER A  42     2281   2547   1866    170   -199    -59       C  
ATOM    202  O   SER A  42      -9.828  -0.545  20.586  1.00 17.99           O  
ANISOU  202  O   SER A  42     2300   2674   1862    143   -210    -98       O  
ATOM    203  CB  SER A  42      -8.975  -3.178  19.046  1.00 18.61           C  
ANISOU  203  CB  SER A  42     2368   2740   1963    274   -213      1       C  
ATOM    204  OG  SER A  42      -8.907  -2.526  17.775  1.00 18.98           O  
ANISOU  204  OG  SER A  42     2417   2740   2056    217   -214    -28       O  
ATOM    205  N   ILE A  43     -11.181  -0.744  18.776  1.00 16.78           N  
ANISOU  205  N   ILE A  43     2210   2347   1819    132   -186    -68       N  
ATOM    206  CA  ILE A  43     -11.358   0.717  18.602  1.00 16.89           C  
ANISOU  206  CA  ILE A  43     2239   2335   1844     61   -181   -121       C  
ATOM    207  C   ILE A  43     -12.374   1.275  19.605  1.00 16.83           C  
ANISOU  207  C   ILE A  43     2263   2304   1827     58   -166   -130       C  
ATOM    208  O   ILE A  43     -12.142   2.297  20.256  1.00 16.83           O  
ANISOU  208  O   ILE A  43     2267   2331   1794     18   -166   -178       O  
ATOM    209  CB  ILE A  43     -11.809   1.081  17.159  1.00 16.39           C  
ANISOU  209  CB  ILE A  43     2202   2184   1841     32   -170   -122       C  
ATOM    210  CG1 ILE A  43     -10.820   0.539  16.116  1.00 17.10           C  
ANISOU  210  CG1 ILE A  43     2262   2298   1938     36   -183   -114       C  
ATOM    211  CG2 ILE A  43     -12.004   2.595  16.999  1.00 17.14           C  
ANISOU  211  CG2 ILE A  43     2327   2242   1942    -33   -158   -171       C  
ATOM    212  CD1 ILE A  43      -9.385   1.128  16.198  1.00 20.08           C  
ANISOU  212  CD1 ILE A  43     2593   2768   2269     -7   -200   -156       C  
ATOM    213  N   GLY A  44     -13.502   0.589  19.732  1.00 16.08           N  
ANISOU  213  N   GLY A  44     2192   2160   1758    100   -152    -86       N  
ATOM    214  CA  GLY A  44     -14.554   1.022  20.642  1.00 16.16           C  
ANISOU  214  CA  GLY A  44     2227   2154   1758    106   -137    -88       C  
ATOM    215  C   GLY A  44     -15.691   0.035  20.599  1.00 15.90           C  
ANISOU  215  C   GLY A  44     2209   2079   1752    146   -122    -31       C  
ATOM    216  O   GLY A  44     -15.570  -1.043  20.004  1.00 15.73           O  
ANISOU  216  O   GLY A  44     2184   2042   1752    168   -125      7       O  
ATOM    217  N   GLU A  45     -16.796   0.411  21.224  1.00 15.93           N  
ANISOU  217  N   GLU A  45     2233   2068   1753    153   -105    -28       N  
ATOM    218  CA  GLU A  45     -17.939  -0.463  21.350  1.00 15.81           C  
ANISOU  218  CA  GLU A  45     2227   2028   1753    180    -89     23       C  
ATOM    219  C   GLU A  45     -18.662  -0.646  20.017  1.00 15.40           C  
ANISOU  219  C   GLU A  45     2186   1910   1754    165    -79     40       C  
ATOM    220  O   GLU A  45     -19.212   0.302  19.444  1.00 15.25           O  
ANISOU  220  O   GLU A  45     2179   1859   1755    148    -70     18       O  
ATOM    221  CB  GLU A  45     -18.902   0.053  22.420  1.00 16.04           C  
ANISOU  221  CB  GLU A  45     2265   2074   1754    193    -73     20       C  
ATOM    222  CG  GLU A  45     -20.028  -0.932  22.725  1.00 16.49           C  
ANISOU  222  CG  GLU A  45     2324   2125   1816    215    -55     76       C  
ATOM    223  CD  GLU A  45     -21.002  -0.424  23.782  1.00 18.10           C  
ANISOU  223  CD  GLU A  45     2531   2359   1988    232    -38     76       C  
ATOM    224  OE1 GLU A  45     -21.106   0.797  23.996  1.00 17.17           O  
ANISOU  224  OE1 GLU A  45     2425   2243   1857    229    -35     31       O  
ATOM    225  OE2 GLU A  45     -21.662  -1.268  24.407  1.00 21.09           O  
ANISOU  225  OE2 GLU A  45     2905   2756   2352    249    -26    121       O  
ATOM    226  N   VAL A  46     -18.663  -1.888  19.561  1.00 15.30           N  
ANISOU  226  N   VAL A  46     2173   1880   1759    176    -80     81       N  
ATOM    227  CA  VAL A  46     -19.273  -2.271  18.299  1.00 14.98           C  
ANISOU  227  CA  VAL A  46     2141   1786   1764    158    -72     97       C  
ATOM    228  C   VAL A  46     -20.747  -2.621  18.530  1.00 15.02           C  
ANISOU  228  C   VAL A  46     2151   1781   1773    155    -51    129       C  
ATOM    229  O   VAL A  46     -21.073  -3.448  19.395  1.00 15.28           O  
ANISOU  229  O   VAL A  46     2190   1831   1784    169    -41    163       O  
ATOM    230  CB  VAL A  46     -18.503  -3.487  17.686  1.00 14.95           C  
ANISOU  230  CB  VAL A  46     2143   1766   1772    168    -81    121       C  
ATOM    231  CG1 VAL A  46     -19.280  -4.133  16.551  1.00 14.73           C  
ANISOU  231  CG1 VAL A  46     2129   1685   1784    147    -70    142       C  
ATOM    232  CG2 VAL A  46     -17.104  -3.055  17.215  1.00 14.92           C  
ANISOU  232  CG2 VAL A  46     2122   1782   1764    167   -102     88       C  
ATOM    233  N   GLU A  47     -21.632  -1.966  17.779  1.00 14.83           N  
ANISOU  233  N   GLU A  47     2124   1738   1771    139    -41    120       N  
ATOM    234  CA  GLU A  47     -23.060  -2.264  17.834  0.50 14.91           C  
ANISOU  234  CA  GLU A  47     2128   1756   1782    132    -22    149       C  
ATOM    235  C   GLU A  47     -23.357  -3.602  17.152  1.00 14.89           C  
ANISOU  235  C   GLU A  47     2132   1727   1801    105    -17    182       C  
ATOM    236  O   GLU A  47     -24.113  -4.409  17.682  1.00 15.76           O  
ANISOU  236  O   GLU A  47     2243   1848   1896     94     -1    216       O  
ATOM    237  CB  GLU A  47     -23.867  -1.120  17.206  1.00 15.06           C  
ANISOU  237  CB  GLU A  47     2139   1775   1810    133    -13    129       C  
ATOM    238  CG  GLU A  47     -25.402  -1.261  17.315  1.00 15.82           C  
ANISOU  238  CG  GLU A  47     2214   1903   1894    132      8    157       C  
ATOM    239  CD  GLU A  47     -26.024  -2.101  16.195  1.00 17.93           C  
ANISOU  239  CD  GLU A  47     2467   2161   2186     96     12    179       C  
ATOM    240  OE1 GLU A  47     -27.016  -2.806  16.469  1.00 22.13           O  
ANISOU  240  OE1 GLU A  47     2981   2723   2703     75     27    209       O  
ATOM    241  OE2 GLU A  47     -25.552  -2.059  15.041  1.00 14.67           O  
ANISOU  241  OE2 GLU A  47     2058   1714   1803     83      1    165       O  
ATOM    242  N   SER A  48     -22.771  -3.838  15.980  1.00 14.65           N  
ANISOU  242  N   SER A  48     2107   1659   1800     91    -28    172       N  
ATOM    243  CA  SER A  48     -22.919  -5.116  15.266  1.00 14.94           C  
ANISOU  243  CA  SER A  48     2160   1662   1854     65    -23    196       C  
ATOM    244  C   SER A  48     -21.850  -5.237  14.196  1.00 14.83           C  
ANISOU  244  C   SER A  48     2155   1614   1865     67    -39    177       C  
ATOM    245  O   SER A  48     -21.349  -4.218  13.699  1.00 14.43           O  
ANISOU  245  O   SER A  48     2090   1569   1825     73    -52    147       O  
ATOM    246  CB  SER A  48     -24.300  -5.234  14.605  1.00 15.09           C  
ANISOU  246  CB  SER A  48     2162   1687   1883     26     -8    207       C  
ATOM    247  OG  SER A  48     -24.390  -4.378  13.489  1.00 16.74           O  
ANISOU  247  OG  SER A  48     2352   1894   2113     23    -16    181       O  
ATOM    248  N   ALA A  49     -21.513  -6.479  13.854  1.00 14.59           N  
ANISOU  248  N   ALA A  49     2154   1548   1840     62    -36    197       N  
ATOM    249  CA  ALA A  49     -20.613  -6.799  12.752  1.00 14.55           C  
ANISOU  249  CA  ALA A  49     2161   1512   1856     66    -48    183       C  
ATOM    250  C   ALA A  49     -21.212  -7.974  12.004  1.00 15.29           C  
ANISOU  250  C   ALA A  49     2286   1560   1963     31    -34    200       C  
ATOM    251  O   ALA A  49     -21.774  -8.897  12.613  1.00 14.96           O  
ANISOU  251  O   ALA A  49     2276   1502   1908     17    -14    230       O  
ATOM    252  CB  ALA A  49     -19.231  -7.176  13.254  1.00 14.58           C  
ANISOU  252  CB  ALA A  49     2178   1522   1840    113    -59    186       C  
ATOM    253  N   LYS A  50     -21.094  -7.930  10.684  1.00 15.05           N  
ANISOU  253  N   LYS A  50     2251   1509   1957     14    -41    181       N  
ATOM    254  CA  LYS A  50     -21.641  -8.983   9.855  1.00 15.75           C  
ANISOU  254  CA  LYS A  50     2370   1556   2056    -27    -28    188       C  
ATOM    255  C   LYS A  50     -20.653  -9.264   8.749  1.00 15.74           C  
ANISOU  255  C   LYS A  50     2385   1526   2071    -10    -39    169       C  
ATOM    256  O   LYS A  50     -20.157  -8.348   8.106  1.00 14.66           O  
ANISOU  256  O   LYS A  50     2213   1411   1947      3    -57    145       O  
ATOM    257  CB  LYS A  50     -23.026  -8.600   9.313  1.00 16.14           C  
ANISOU  257  CB  LYS A  50     2387   1633   2114    -82    -21    182       C  
ATOM    258  CG  LYS A  50     -23.638  -9.632   8.359  1.00 17.03           C  
ANISOU  258  CG  LYS A  50     2526   1713   2233   -140     -8    181       C  
ATOM    259  CD  LYS A  50     -25.050  -9.246   7.989  1.00 21.15           C  
ANISOU  259  CD  LYS A  50     3001   2287   2749   -192     -2    178       C  
ATOM    260  N   LEU A  51     -20.325 -10.539   8.587  1.00 16.37           N  
ANISOU  260  N   LEU A  51     2523   1552   2145     -5    -27    182       N  
ATOM    261  CA  LEU A  51     -19.518 -10.998   7.482  1.00 16.95           C  
ANISOU  261  CA  LEU A  51     2619   1594   2229     12    -33    166       C  
ATOM    262  C   LEU A  51     -20.462 -11.489   6.409  1.00 17.46           C  
ANISOU  262  C   LEU A  51     2698   1629   2307    -54    -23    153       C  
ATOM    263  O   LEU A  51     -21.321 -12.341   6.679  1.00 18.43           O  
ANISOU  263  O   LEU A  51     2862   1720   2422   -101      0    168       O  
ATOM    264  CB  LEU A  51     -18.637 -12.166   7.931  1.00 17.51           C  
ANISOU  264  CB  LEU A  51     2757   1619   2278     64    -21    188       C  
ATOM    265  CG  LEU A  51     -17.844 -12.842   6.813  1.00 18.40           C  
ANISOU  265  CG  LEU A  51     2905   1691   2393     90    -21    174       C  
ATOM    266  CD1 LEU A  51     -16.658 -11.968   6.462  1.00 17.86           C  
ANISOU  266  CD1 LEU A  51     2782   1679   2326    140    -48    155       C  
ATOM    267  CD2 LEU A  51     -17.401 -14.260   7.216  1.00 19.06           C  
ANISOU  267  CD2 LEU A  51     3081   1709   2452    134      4    202       C  
ATOM    268  N   ILE A  52     -20.323 -10.970   5.192  1.00 16.94           N  
ANISOU  268  N   ILE A  52     2600   1578   2258    -63    -37    125       N  
ATOM    269  CA  ILE A  52     -21.219 -11.401   4.122  1.00 17.06           C  
ANISOU  269  CA  ILE A  52     2622   1580   2281   -127    -30    109       C  
ATOM    270  C   ILE A  52     -20.729 -12.684   3.460  1.00 18.08           C  
ANISOU  270  C   ILE A  52     2824   1640   2407   -127    -17    102       C  
ATOM    271  O   ILE A  52     -19.559 -12.801   3.084  1.00 17.57           O  
ANISOU  271  O   ILE A  52     2775   1560   2342    -69    -26     95       O  
ATOM    272  CB  ILE A  52     -21.484 -10.292   3.046  1.00 16.66           C  
ANISOU  272  CB  ILE A  52     2504   1581   2245   -140    -48     85       C  
ATOM    273  CG1 ILE A  52     -21.978  -8.994   3.708  1.00 14.58           C  
ANISOU  273  CG1 ILE A  52     2182   1376   1981   -131    -54     93       C  
ATOM    274  CG2 ILE A  52     -22.491 -10.811   2.004  1.00 17.00           C  
ANISOU  274  CG2 ILE A  52     2547   1624   2286   -209    -40     68       C  
ATOM    275  CD1 ILE A  52     -23.201  -9.160   4.639  1.00 14.62           C  
ANISOU  275  CD1 ILE A  52     2182   1402   1971   -168    -38    113       C  
ATOM    276  N   ARG A  53     -21.647 -13.640   3.338  1.00 18.89           N  
ANISOU  276  N   ARG A  53     2973   1704   2501   -195      5    102       N  
ATOM    277  CA  ARG A  53     -21.364 -14.933   2.760  1.00 20.52           C  
ANISOU  277  CA  ARG A  53     3268   1831   2699   -207     24     93       C  
ATOM    278  C   ARG A  53     -22.346 -15.228   1.622  1.00 20.83           C  
ANISOU  278  C   ARG A  53     3303   1874   2739   -298     29     61       C  
ATOM    279  O   ARG A  53     -23.457 -14.693   1.607  1.00 20.37           O  
ANISOU  279  O   ARG A  53     3184   1877   2679   -359     26     58       O  
ATOM    280  CB  ARG A  53     -21.453 -16.024   3.843  1.00 21.40           C  
ANISOU  280  CB  ARG A  53     3466   1875   2791   -209     55    125       C  
ATOM    281  CG  ARG A  53     -20.816 -15.641   5.192  1.00 23.49           C  
ANISOU  281  CG  ARG A  53     3717   2160   3047   -133     51    160       C  
ATOM    282  CD  ARG A  53     -20.434 -16.880   6.012  1.00 28.35           C  
ANISOU  282  CD  ARG A  53     4437   2695   3637    -99     83    194       C  
ATOM    283  NE  ARG A  53     -20.685 -16.808   7.461  1.00 29.85           N  
ANISOU  283  NE  ARG A  53     4626   2903   3811    -85     93    233       N  
ATOM    284  CZ  ARG A  53     -20.865 -15.713   8.208  1.00 27.88           C  
ANISOU  284  CZ  ARG A  53     4292   2734   3565    -74     73    241       C  
ATOM    285  NH1 ARG A  53     -20.819 -14.503   7.690  0.60 27.64           N  
ANISOU  285  NH1 ARG A  53     4174   2773   3555    -73     42    213       N  
ATOM    286  NH2 ARG A  53     -21.092 -15.848   9.510  1.00 27.10           N  
ANISOU  286  NH2 ARG A  53     4206   2643   3446    -62     87    277       N  
ATOM    287  N   ASP A  54     -21.933 -16.076   0.681  1.00 21.38           N  
ANISOU  287  N   ASP A  54     3434   1884   2804   -302     38     37       N  
ATOM    288  CA  ASP A  54     -22.791 -16.494  -0.424  1.00 22.90           C  
ANISOU  288  CA  ASP A  54     3633   2078   2991   -393     44      1       C  
ATOM    289  C   ASP A  54     -24.028 -17.233   0.085  1.00 23.82           C  
ANISOU  289  C   ASP A  54     3786   2176   3089   -497     72      7       C  
ATOM    290  O   ASP A  54     -23.916 -18.125   0.914  1.00 24.30           O  
ANISOU  290  O   ASP A  54     3933   2160   3138   -499    100     30       O  
ATOM    291  CB  ASP A  54     -22.022 -17.401  -1.390  1.00 23.46           C  
ANISOU  291  CB  ASP A  54     3784   2074   3056   -372     53    -26       C  
ATOM    292  CG  ASP A  54     -22.927 -18.018  -2.456  1.00 25.75           C  
ANISOU  292  CG  ASP A  54     4096   2355   3331   -478     64    -68       C  
ATOM    293  OD1 ASP A  54     -23.509 -17.266  -3.261  1.00 27.76           O  
ANISOU  293  OD1 ASP A  54     4263   2696   3589   -516     43    -90       O  
ATOM    294  OD2 ASP A  54     -23.056 -19.259  -2.495  1.00 28.54           O  
ANISOU  294  OD2 ASP A  54     4559   2618   3667   -523     96    -79       O  
ATOM    295  N   LYS A  55     -25.200 -16.860  -0.425  1.00 24.57           N  
ANISOU  295  N   LYS A  55     3813   2349   3176   -584     66    -12       N  
ATOM    296  CA  LYS A  55     -26.473 -17.452   0.015  1.00 25.93           C  
ANISOU  296  CA  LYS A  55     3998   2530   3323   -696     91     -8       C  
ATOM    297  C   LYS A  55     -26.626 -18.921  -0.361  1.00 26.93           C  
ANISOU  297  C   LYS A  55     4244   2558   3431   -778    125    -32       C  
ATOM    298  O   LYS A  55     -27.235 -19.706   0.379  1.00 28.00           O  
ANISOU  298  O   LYS A  55     4439   2652   3548   -850    157    -16       O  
ATOM    299  CB  LYS A  55     -27.658 -16.649  -0.541  1.00 26.17           C  
ANISOU  299  CB  LYS A  55     3914   2690   3342   -761     74    -25       C  
ATOM    300  N   VAL A  56     -26.068 -19.288  -1.510  1.00 27.00           N  
ANISOU  300  N   VAL A  56     4291   2526   3441   -768    120    -69       N  
ATOM    301  CA  VAL A  56     -26.278 -20.613  -2.096  1.00 27.58           C  
ANISOU  301  CA  VAL A  56     4478   2509   3493   -854    152   -104       C  
ATOM    302  C   VAL A  56     -25.360 -21.701  -1.523  1.00 27.58           C  
ANISOU  302  C   VAL A  56     4628   2360   3490   -797    186    -84       C  
ATOM    303  O   VAL A  56     -25.822 -22.811  -1.243  1.00 28.55           O  
ANISOU  303  O   VAL A  56     4860   2397   3591   -881    227    -87       O  
ATOM    304  CB  VAL A  56     -26.172 -20.555  -3.664  1.00 27.87           C  
ANISOU  304  CB  VAL A  56     4492   2572   3524   -872    134   -159       C  
ATOM    305  CG1 VAL A  56     -25.827 -21.914  -4.273  1.00 28.67           C  
ANISOU  305  CG1 VAL A  56     4739   2548   3608   -910    167   -195       C  
ATOM    306  CG2 VAL A  56     -27.474 -20.035  -4.265  1.00 29.01           C  
ANISOU  306  CG2 VAL A  56     4527   2846   3649   -979    119   -185       C  
ATOM    307  N   ALA A  57     -24.077 -21.378  -1.359  1.00 26.32           N  
ANISOU  307  N   ALA A  57     4474   2177   3348   -657    172    -63       N  
ATOM    308  CA  ALA A  57     -23.046 -22.366  -1.023  1.00 26.20           C  
ANISOU  308  CA  ALA A  57     4595   2035   3324   -576    201    -46       C  
ATOM    309  C   ALA A  57     -22.334 -22.090   0.305  1.00 25.12           C  
ANISOU  309  C   ALA A  57     4457   1895   3194   -468    201     12       C  
ATOM    310  O   ALA A  57     -21.630 -22.950   0.825  1.00 25.49           O  
ANISOU  310  O   ALA A  57     4617   1845   3225   -400    231     38       O  
ATOM    311  CB  ALA A  57     -22.027 -22.471  -2.158  1.00 26.16           C  
ANISOU  311  CB  ALA A  57     4613   2005   3321   -500    189    -79       C  
ATOM    312  N   GLY A  58     -22.488 -20.879   0.828  1.00 23.84           N  
ANISOU  312  N   GLY A  58     4168   1841   3049   -444    168     32       N  
ATOM    313  CA  GLY A  58     -22.073 -20.585   2.190  1.00 23.06           C  
ANISOU  313  CA  GLY A  58     4058   1753   2950   -369    168     83       C  
ATOM    314  C   GLY A  58     -20.712 -19.953   2.427  1.00 22.13           C  
ANISOU  314  C   GLY A  58     3902   1667   2840   -230    142    100       C  
ATOM    315  O   GLY A  58     -20.424 -19.573   3.544  1.00 21.79           O  
ANISOU  315  O   GLY A  58     3833   1654   2794   -175    138    138       O  
ATOM    316  N   HIS A  59     -19.888 -19.821   1.395  1.00 22.19           N  
ANISOU  316  N   HIS A  59     3899   1679   2853   -177    125     72       N  
ATOM    317  CA  HIS A  59     -18.546 -19.224   1.548  1.00 22.30           C  
ANISOU  317  CA  HIS A  59     3868   1737   2868    -52    101     86       C  
ATOM    318  C   HIS A  59     -18.547 -17.698   1.741  1.00 20.79           C  
ANISOU  318  C   HIS A  59     3541   1661   2698    -45     62     86       C  
ATOM    319  O   HIS A  59     -19.381 -16.979   1.161  1.00 19.54           O  
ANISOU  319  O   HIS A  59     3311   1555   2558   -117     46     63       O  
ATOM    320  CB  HIS A  59     -17.635 -19.599   0.361  1.00 23.14           C  
ANISOU  320  CB  HIS A  59     4008   1817   2968      3     98     56       C  
ATOM    321  CG  HIS A  59     -18.161 -19.167  -0.978  1.00 24.87           C  
ANISOU  321  CG  HIS A  59     4174   2071   3203    -69     80      9       C  
ATOM    322  ND1 HIS A  59     -19.055 -19.923  -1.708  1.00 26.45           N  
ANISOU  322  ND1 HIS A  59     4434   2218   3398   -166    101    -23       N  
ATOM    323  CD2 HIS A  59     -17.916 -18.056  -1.718  1.00 26.67           C  
ANISOU  323  CD2 HIS A  59     4297   2388   3449    -59     45    -10       C  
ATOM    324  CE1 HIS A  59     -19.335 -19.299  -2.839  1.00 27.88           C  
ANISOU  324  CE1 HIS A  59     4542   2460   3591   -206     77    -60       C  
ATOM    325  NE2 HIS A  59     -18.655 -18.165  -2.872  1.00 26.76           N  
ANISOU  325  NE2 HIS A  59     4302   2400   3464   -140     44    -50       N  
ATOM    326  N   SER A  60     -17.595 -17.207   2.538  1.00 19.82           N  
ANISOU  326  N   SER A  60     3384   1579   2569     45     48    112       N  
ATOM    327  CA  SER A  60     -17.418 -15.763   2.716  1.00 18.96           C  
ANISOU  327  CA  SER A  60     3161   1569   2476     57     14    108       C  
ATOM    328  C   SER A  60     -17.294 -15.074   1.366  1.00 18.20           C  
ANISOU  328  C   SER A  60     3005   1512   2397     39     -9     72       C  
ATOM    329  O   SER A  60     -16.678 -15.625   0.449  1.00 17.83           O  
ANISOU  329  O   SER A  60     2994   1435   2344     68     -6     54       O  
ATOM    330  CB  SER A  60     -16.164 -15.455   3.538  1.00 18.92           C  
ANISOU  330  CB  SER A  60     3134   1603   2452    156      2    131       C  
ATOM    331  OG  SER A  60     -15.890 -14.062   3.464  1.00 20.01           O  
ANISOU  331  OG  SER A  60     3171   1828   2605    157    -29    118       O  
ATOM    332  N   LEU A  61     -17.873 -13.879   1.242  1.00 16.54           N  
ANISOU  332  N   LEU A  61     2710   1368   2207     -2    -28     62       N  
ATOM    333  CA  LEU A  61     -17.637 -13.059   0.057  1.00 16.47           C  
ANISOU  333  CA  LEU A  61     2641   1405   2212     -6    -50     35       C  
ATOM    334  C   LEU A  61     -16.533 -12.023   0.298  1.00 15.72           C  
ANISOU  334  C   LEU A  61     2487   1370   2118     55    -71     39       C  
ATOM    335  O   LEU A  61     -16.315 -11.145  -0.520  1.00 15.85           O  
ANISOU  335  O   LEU A  61     2448   1429   2145     51    -88     22       O  
ATOM    336  CB  LEU A  61     -18.938 -12.401  -0.433  1.00 16.13           C  
ANISOU  336  CB  LEU A  61     2547   1398   2183    -83    -54     21       C  
ATOM    337  CG  LEU A  61     -20.052 -13.351  -0.908  1.00 17.86           C  
ANISOU  337  CG  LEU A  61     2810   1580   2396   -161    -35      8       C  
ATOM    338  CD1 LEU A  61     -21.174 -12.543  -1.507  1.00 19.07           C  
ANISOU  338  CD1 LEU A  61     2892   1799   2554   -221    -45     -5       C  
ATOM    339  CD2 LEU A  61     -19.569 -14.387  -1.935  1.00 19.91           C  
ANISOU  339  CD2 LEU A  61     3135   1784   2647   -158    -26    -17       C  
ATOM    340  N   GLY A  62     -15.836 -12.139   1.426  1.00 15.81           N  
ANISOU  340  N   GLY A  62     2508   1386   2112    108    -70     62       N  
ATOM    341  CA  GLY A  62     -14.616 -11.363   1.688  1.00 14.49           C  
ANISOU  341  CA  GLY A  62     2291   1280   1934    164    -89     63       C  
ATOM    342  C   GLY A  62     -14.857  -9.894   1.998  1.00 14.02           C  
ANISOU  342  C   GLY A  62     2160   1277   1888    134   -105     57       C  
ATOM    343  O   GLY A  62     -13.991  -9.050   1.762  1.00 13.82           O  
ANISOU  343  O   GLY A  62     2089   1303   1860    151   -120     46       O  
ATOM    344  N   TYR A  63     -16.059  -9.592   2.473  1.00 13.90           N  
ANISOU  344  N   TYR A  63     2142   1254   1886     85    -98     63       N  
ATOM    345  CA  TYR A  63     -16.405  -8.246   2.903  1.00 13.56           C  
ANISOU  345  CA  TYR A  63     2047   1253   1850     65   -107     59       C  
ATOM    346  C   TYR A  63     -17.434  -8.309   4.018  1.00 13.64           C  
ANISOU  346  C   TYR A  63     2069   1257   1858     42    -95     78       C  
ATOM    347  O   TYR A  63     -18.109  -9.323   4.205  1.00 13.93           O  
ANISOU  347  O   TYR A  63     2147   1256   1891     23    -79     91       O  
ATOM    348  CB  TYR A  63     -16.860  -7.353   1.732  1.00 13.25           C  
ANISOU  348  CB  TYR A  63     1972   1232   1831     31   -113     41       C  
ATOM    349  CG  TYR A  63     -18.277  -7.559   1.236  1.00 13.27           C  
ANISOU  349  CG  TYR A  63     1977   1222   1844    -17   -103     41       C  
ATOM    350  CD1 TYR A  63     -18.595  -8.611   0.367  1.00 13.50           C  
ANISOU  350  CD1 TYR A  63     2037   1220   1873    -39    -96     33       C  
ATOM    351  CD2 TYR A  63     -19.283  -6.686   1.604  1.00 13.14           C  
ANISOU  351  CD2 TYR A  63     1931   1232   1829    -39    -99     46       C  
ATOM    352  CE1 TYR A  63     -19.880  -8.779  -0.101  1.00 13.60           C  
ANISOU  352  CE1 TYR A  63     2043   1238   1888    -92    -88     29       C  
ATOM    353  CE2 TYR A  63     -20.578  -6.856   1.153  1.00 13.24           C  
ANISOU  353  CE2 TYR A  63     1934   1254   1842    -81    -91     47       C  
ATOM    354  CZ  TYR A  63     -20.866  -7.898   0.304  1.00 13.47           C  
ANISOU  354  CZ  TYR A  63     1986   1262   1871   -112    -86     38       C  
ATOM    355  OH  TYR A  63     -22.149  -8.036  -0.147  1.00 15.86           O  
ANISOU  355  OH  TYR A  63     2270   1589   2166   -162    -79     35       O  
ATOM    356  N   GLY A  64     -17.536  -7.233   4.783  1.00 13.46           N  
ANISOU  356  N   GLY A  64     2012   1270   1832     43   -100     78       N  
ATOM    357  CA  GLY A  64     -18.468  -7.237   5.913  1.00 13.57           C  
ANISOU  357  CA  GLY A  64     2032   1287   1837     29    -89     95       C  
ATOM    358  C   GLY A  64     -18.849  -5.835   6.310  1.00 13.34           C  
ANISOU  358  C   GLY A  64     1966   1294   1809     22    -93     87       C  
ATOM    359  O   GLY A  64     -18.383  -4.888   5.705  1.00 13.13           O  
ANISOU  359  O   GLY A  64     1916   1283   1791     24   -102     68       O  
ATOM    360  N   PHE A  65     -19.697  -5.718   7.327  1.00 13.45           N  
ANISOU  360  N   PHE A  65     1979   1320   1812     14    -83    101       N  
ATOM    361  CA  PHE A  65     -20.093  -4.423   7.865  1.00 13.34           C  
ANISOU  361  CA  PHE A  65     1940   1335   1792     17    -82     93       C  
ATOM    362  C   PHE A  65     -19.847  -4.374   9.355  1.00 13.51           C  
ANISOU  362  C   PHE A  65     1968   1375   1790     38    -80    101       C  
ATOM    363  O   PHE A  65     -20.109  -5.343  10.073  1.00 13.75           O  
ANISOU  363  O   PHE A  65     2018   1398   1807     41    -72    125       O  
ATOM    364  CB  PHE A  65     -21.572  -4.137   7.600  1.00 13.35           C  
ANISOU  364  CB  PHE A  65     1926   1352   1796     -6    -69    101       C  
ATOM    365  CG  PHE A  65     -21.924  -4.071   6.142  1.00 13.23           C  
ANISOU  365  CG  PHE A  65     1897   1334   1798    -25    -70     92       C  
ATOM    366  CD1 PHE A  65     -21.902  -2.847   5.460  1.00 13.05           C  
ANISOU  366  CD1 PHE A  65     1856   1323   1781    -13    -72     79       C  
ATOM    367  CD2 PHE A  65     -22.249  -5.234   5.439  1.00 13.36           C  
ANISOU  367  CD2 PHE A  65     1924   1334   1820    -56    -67     97       C  
ATOM    368  CE1 PHE A  65     -22.224  -2.785   4.096  1.00 12.98           C  
ANISOU  368  CE1 PHE A  65     1831   1319   1782    -26    -73     74       C  
ATOM    369  CE2 PHE A  65     -22.586  -5.181   4.082  1.00 13.30           C  
ANISOU  369  CE2 PHE A  65     1899   1332   1821    -75    -70     86       C  
ATOM    370  CZ  PHE A  65     -22.563  -3.966   3.406  1.00 13.09           C  
ANISOU  370  CZ  PHE A  65     1846   1327   1800    -57    -74     76       C  
ATOM    371  N   VAL A  66     -19.343  -3.239   9.810  1.00 13.45           N  
ANISOU  371  N   VAL A  66     1949   1389   1773     50    -87     82       N  
ATOM    372  CA  VAL A  66     -19.132  -3.007  11.234  1.00 13.65           C  
ANISOU  372  CA  VAL A  66     1975   1440   1770     68    -86     83       C  
ATOM    373  C   VAL A  66     -19.828  -1.720  11.612  1.00 13.64           C  
ANISOU  373  C   VAL A  66     1968   1451   1762     65    -77     68       C  
ATOM    374  O   VAL A  66     -19.509  -0.636  11.098  1.00 13.54           O  
ANISOU  374  O   VAL A  66     1955   1433   1756     58    -79     43       O  
ATOM    375  CB  VAL A  66     -17.631  -2.939  11.609  1.00 13.75           C  
ANISOU  375  CB  VAL A  66     1982   1477   1764     85   -102     67       C  
ATOM    376  CG1 VAL A  66     -17.479  -2.590  13.091  1.00 14.00           C  
ANISOU  376  CG1 VAL A  66     2011   1547   1761    100   -103     63       C  
ATOM    377  CG2 VAL A  66     -16.938  -4.291  11.285  1.00 13.86           C  
ANISOU  377  CG2 VAL A  66     2007   1481   1777    106   -108     86       C  
ATOM    378  N   ASN A  67     -20.795  -1.843  12.505  1.00 13.80           N  
ANISOU  378  N   ASN A  67     1989   1488   1766     72    -64     86       N  
ATOM    379  CA  ASN A  67     -21.510  -0.671  12.950  1.00 13.88           C  
ANISOU  379  CA  ASN A  67     1998   1511   1763     81    -52     74       C  
ATOM    380  C   ASN A  67     -21.139  -0.370  14.395  1.00 14.12           C  
ANISOU  380  C   ASN A  67     2036   1568   1761     98    -53     64       C  
ATOM    381  O   ASN A  67     -21.281  -1.217  15.278  1.00 14.29           O  
ANISOU  381  O   ASN A  67     2055   1609   1765    106    -52     87       O  
ATOM    382  CB  ASN A  67     -23.010  -0.844  12.764  1.00 13.94           C  
ANISOU  382  CB  ASN A  67     1993   1533   1771     80    -36     97       C  
ATOM    383  CG  ASN A  67     -23.777   0.397  13.136  1.00 14.48           C  
ANISOU  383  CG  ASN A  67     2062   1618   1820    106    -20     87       C  
ATOM    384  OD1 ASN A  67     -23.529   1.476  12.595  1.00 14.37           O  
ANISOU  384  OD1 ASN A  67     2064   1585   1813    116    -17     65       O  
ATOM    385  ND2 ASN A  67     -24.688   0.265  14.093  1.00 15.25           N  
ANISOU  385  ND2 ASN A  67     2150   1752   1891    120     -7    105       N  
ATOM    386  N   TYR A  68     -20.609   0.826  14.611  1.00 14.19           N  
ANISOU  386  N   TYR A  68     2056   1576   1759     98    -54     29       N  
ATOM    387  CA  TYR A  68     -20.231   1.254  15.952  1.00 14.48           C  
ANISOU  387  CA  TYR A  68     2100   1642   1759    108    -55     11       C  
ATOM    388  C   TYR A  68     -21.395   1.903  16.651  1.00 14.68           C  
ANISOU  388  C   TYR A  68     2136   1677   1764    130    -35     13       C  
ATOM    389  O   TYR A  68     -22.292   2.467  16.003  1.00 14.63           O  
ANISOU  389  O   TYR A  68     2136   1653   1769    140    -19     17       O  
ATOM    390  CB  TYR A  68     -19.060   2.233  15.899  1.00 14.58           C  
ANISOU  390  CB  TYR A  68     2126   1653   1763     86    -64    -34       C  
ATOM    391  CG  TYR A  68     -17.751   1.542  15.670  1.00 14.55           C  
ANISOU  391  CG  TYR A  68     2100   1670   1758     72    -87    -37       C  
ATOM    392  CD1 TYR A  68     -17.227   1.411  14.387  1.00 14.31           C  
ANISOU  392  CD1 TYR A  68     2063   1618   1757     55    -94    -38       C  
ATOM    393  CD2 TYR A  68     -17.043   0.978  16.741  1.00 14.81           C  
ANISOU  393  CD2 TYR A  68     2115   1755   1755     85    -99    -35       C  
ATOM    394  CE1 TYR A  68     -16.010   0.752  14.171  1.00 14.34           C  
ANISOU  394  CE1 TYR A  68     2044   1651   1755     53   -113    -39       C  
ATOM    395  CE2 TYR A  68     -15.846   0.320  16.536  1.00 14.86           C  
ANISOU  395  CE2 TYR A  68     2098   1794   1753     87   -118    -33       C  
ATOM    396  CZ  TYR A  68     -15.327   0.211  15.246  1.00 14.63           C  
ANISOU  396  CZ  TYR A  68     2063   1743   1753     71   -125    -36       C  
ATOM    397  OH  TYR A  68     -14.125  -0.442  15.044  1.00 14.75           O  
ANISOU  397  OH  TYR A  68     2051   1799   1753     81   -142    -33       O  
ATOM    398  N   VAL A  69     -21.362   1.850  17.976  1.00 14.96           N  
ANISOU  398  N   VAL A  69     2171   1748   1764    145    -34     10       N  
ATOM    399  CA  VAL A  69     -22.297   2.618  18.787  1.00 15.23           C  
ANISOU  399  CA  VAL A  69     2219   1798   1770    171    -14      4       C  
ATOM    400  C   VAL A  69     -22.127   4.117  18.514  1.00 15.37           C  
ANISOU  400  C   VAL A  69     2276   1781   1784    170     -4    -40       C  
ATOM    401  O   VAL A  69     -23.131   4.826  18.356  1.00 15.50           O  
ANISOU  401  O   VAL A  69     2309   1785   1794    200     19    -38       O  
ATOM    402  CB  VAL A  69     -22.135   2.319  20.299  1.00 15.55           C  
ANISOU  402  CB  VAL A  69     2253   1886   1768    185    -17      5       C  
ATOM    403  CG1 VAL A  69     -22.923   3.327  21.152  1.00 15.90           C  
ANISOU  403  CG1 VAL A  69     2317   1945   1777    215      4    -14       C  
ATOM    404  CG2 VAL A  69     -22.561   0.872  20.606  1.00 15.52           C  
ANISOU  404  CG2 VAL A  69     2223   1908   1765    191    -18     57       C  
ATOM    405  N   THR A  70     -20.880   4.596  18.441  1.00 15.43           N  
ANISOU  405  N   THR A  70     2299   1775   1789    137    -16    -79       N  
ATOM    406  CA  THR A  70     -20.635   6.038  18.299  1.00 15.70           C  
ANISOU  406  CA  THR A  70     2384   1768   1812    124     -2   -125       C  
ATOM    407  C   THR A  70     -19.967   6.437  16.986  1.00 15.51           C  
ANISOU  407  C   THR A  70     2374   1700   1821     90     -5   -138       C  
ATOM    408  O   THR A  70     -19.236   5.653  16.397  1.00 15.23           O  
ANISOU  408  O   THR A  70     2305   1677   1807     66    -26   -126       O  
ATOM    409  CB  THR A  70     -19.801   6.652  19.477  1.00 16.15           C  
ANISOU  409  CB  THR A  70     2463   1849   1826    100     -6   -174       C  
ATOM    410  OG1 THR A  70     -18.408   6.389  19.281  1.00 16.13           O  
ANISOU  410  OG1 THR A  70     2437   1869   1823     51    -30   -195       O  
ATOM    411  CG2 THR A  70     -20.255   6.121  20.841  1.00 16.35           C  
ANISOU  411  CG2 THR A  70     2466   1932   1814    133     -7   -160       C  
ATOM    412  N   ALA A  71     -20.209   7.673  16.549  1.00 15.74           N  
ANISOU  412  N   ALA A  71     2458   1674   1848     91     19   -161       N  
ATOM    413  CA  ALA A  71     -19.633   8.158  15.294  1.00 15.64           C  
ANISOU  413  CA  ALA A  71     2465   1614   1862     59     22   -171       C  
ATOM    414  C   ALA A  71     -18.133   8.446  15.400  1.00 15.83           C  
ANISOU  414  C   ALA A  71     2494   1646   1875    -10      7   -214       C  
ATOM    415  O   ALA A  71     -17.405   8.263  14.430  1.00 15.63           O  
ANISOU  415  O   ALA A  71     2452   1615   1873    -44     -5   -212       O  
ATOM    416  CB  ALA A  71     -20.373   9.383  14.796  1.00 15.91           C  
ANISOU  416  CB  ALA A  71     2567   1585   1895     88     57   -176       C  
ATOM    417  N   LYS A  72     -17.678   8.919  16.561  1.00 16.28           N  
ANISOU  417  N   LYS A  72     2570   1723   1891    -34      7   -254       N  
ATOM    418  CA  LYS A  72     -16.240   9.128  16.754  1.00 16.56           C  
ANISOU  418  CA  LYS A  72     2596   1789   1905   -107    -10   -297       C  
ATOM    419  C   LYS A  72     -15.456   7.812  16.640  1.00 16.22           C  
ANISOU  419  C   LYS A  72     2473   1820   1871   -111    -45   -273       C  
ATOM    420  O   LYS A  72     -14.344   7.797  16.126  1.00 16.28           O  
ANISOU  420  O   LYS A  72     2457   1852   1877   -160    -59   -290       O  
ATOM    421  CB  LYS A  72     -15.946   9.812  18.093  1.00 17.17           C  
ANISOU  421  CB  LYS A  72     2704   1889   1930   -133     -4   -348       C  
ATOM    422  N   ASP A  73     -16.043   6.711  17.106  1.00 15.94           N  
ANISOU  422  N   ASP A  73     2398   1820   1839    -57    -56   -232       N  
ATOM    423  CA  ASP A  73     -15.380   5.412  17.024  1.00 15.71           C  
ANISOU  423  CA  ASP A  73     2307   1849   1813    -48    -83   -203       C  
ATOM    424  C   ASP A  73     -15.303   4.911  15.592  1.00 15.28           C  
ANISOU  424  C   ASP A  73     2237   1765   1804    -47    -88   -176       C  
ATOM    425  O   ASP A  73     -14.268   4.414  15.179  1.00 15.26           O  
ANISOU  425  O   ASP A  73     2199   1798   1799    -64   -107   -177       O  
ATOM    426  CB  ASP A  73     -16.024   4.379  17.955  1.00 15.64           C  
ANISOU  426  CB  ASP A  73     2273   1876   1792      5    -88   -166       C  
ATOM    427  CG  ASP A  73     -15.678   4.626  19.410  1.00 16.85           C  
ANISOU  427  CG  ASP A  73     2423   2087   1891      2    -93   -193       C  
ATOM    428  OD1 ASP A  73     -14.660   5.307  19.673  1.00 19.23           O  
ANISOU  428  OD1 ASP A  73     2724   2421   2161    -46   -101   -241       O  
ATOM    429  OD2 ASP A  73     -16.412   4.141  20.285  1.00 16.14           O  
ANISOU  429  OD2 ASP A  73     2329   2017   1787     43    -88   -168       O  
ATOM    430  N   ALA A  74     -16.378   5.091  14.828  1.00 15.01           N  
ANISOU  430  N   ALA A  74     2228   1672   1803    -25    -70   -153       N  
ATOM    431  CA  ALA A  74     -16.377   4.733  13.418  1.00 14.65           C  
ANISOU  431  CA  ALA A  74     2171   1598   1797    -26    -72   -131       C  
ATOM    432  C   ALA A  74     -15.270   5.501  12.715  1.00 14.80           C  
ANISOU  432  C   ALA A  74     2199   1609   1816    -78    -74   -164       C  
ATOM    433  O   ALA A  74     -14.488   4.921  11.965  1.00 14.65           O  
ANISOU  433  O   ALA A  74     2146   1611   1808    -90    -90   -157       O  
ATOM    434  CB  ALA A  74     -17.729   5.027  12.779  1.00 14.47           C  
ANISOU  434  CB  ALA A  74     2172   1526   1798      4    -51   -108       C  
ATOM    435  N   GLU A  75     -15.183   6.800  12.987  1.00 15.21           N  
ANISOU  435  N   GLU A  75     2298   1631   1849   -111    -56   -202       N  
ATOM    436  CA  GLU A  75     -14.184   7.646  12.333  1.00 15.49           C  
ANISOU  436  CA  GLU A  75     2351   1652   1880   -174    -52   -235       C  
ATOM    437  C   GLU A  75     -12.771   7.174  12.700  1.00 15.64           C  
ANISOU  437  C   GLU A  75     2316   1755   1870   -215    -79   -256       C  
ATOM    438  O   GLU A  75     -11.923   7.030  11.812  1.00 15.59           O  
ANISOU  438  O   GLU A  75     2283   1769   1873   -245    -89   -256       O  
ATOM    439  CB  GLU A  75     -14.416   9.122  12.685  1.00 16.61           C  
ANISOU  439  CB  GLU A  75     2571   1736   2002   -204    -21   -273       C  
ATOM    440  CG  GLU A  75     -13.381  10.072  12.105  1.00 20.53           C  
ANISOU  440  CG  GLU A  75     3098   2213   2489   -285    -11   -310       C  
ATOM    441  CD  GLU A  75     -13.580  11.500  12.556  1.00 26.79           C  
ANISOU  441  CD  GLU A  75     3984   2938   3258   -319     24   -351       C  
ATOM    442  OE1 GLU A  75     -13.840  11.730  13.763  1.00 29.96           O  
ANISOU  442  OE1 GLU A  75     4406   3350   3627   -312     28   -376       O  
ATOM    443  OE2 GLU A  75     -13.474  12.397  11.693  1.00 29.63           O  
ANISOU  443  OE2 GLU A  75     4402   3230   3626   -351     51   -358       O  
ATOM    444  N   ARG A  76     -12.536   6.895  13.990  1.00 15.89           N  
ANISOU  444  N   ARG A  76     2327   1845   1865   -210    -91   -270       N  
ATOM    445  CA  ARG A  76     -11.239   6.376  14.449  1.00 16.31           C  
ANISOU  445  CA  ARG A  76     2320   1998   1880   -235   -118   -286       C  
ATOM    446  C   ARG A  76     -10.885   5.021  13.819  1.00 15.79           C  
ANISOU  446  C   ARG A  76     2197   1971   1831   -189   -139   -243       C  
ATOM    447  O   ARG A  76      -9.715   4.753  13.543  1.00 15.99           O  
ANISOU  447  O   ARG A  76     2175   2066   1834   -211   -156   -252       O  
ATOM    448  CB  ARG A  76     -11.168   6.298  15.983  1.00 17.65           C  
ANISOU  448  CB  ARG A  76     2479   2228   2001   -226   -126   -305       C  
ATOM    449  CG  ARG A  76      -9.730   6.085  16.516  1.00 21.60           C  
ANISOU  449  CG  ARG A  76     2917   2846   2446   -263   -151   -332       C  
ATOM    450  CD  ARG A  76      -9.517   6.657  17.919  1.00 27.92           C  
ANISOU  450  CD  ARG A  76     3722   3699   3188   -293   -153   -377       C  
ATOM    451  NE  ARG A  76     -10.500   6.129  18.861  1.00 31.81           N  
ANISOU  451  NE  ARG A  76     4225   4181   3679   -223   -150   -349       N  
ATOM    452  CZ  ARG A  76     -10.350   5.001  19.550  1.00 33.66           C  
ANISOU  452  CZ  ARG A  76     4410   4489   3890   -164   -168   -315       C  
ATOM    453  NH1 ARG A  76      -9.246   4.271  19.429  1.00 35.21           N  
ANISOU  453  NH1 ARG A  76     4542   4778   4060   -155   -192   -304       N  
ATOM    454  NH2 ARG A  76     -11.308   4.608  20.368  1.00 35.13           N  
ANISOU  454  NH2 ARG A  76     4612   4658   4075   -109   -161   -288       N  
ATOM    455  N   ALA A  77     -11.893   4.174  13.612  1.00 15.33           N  
ANISOU  455  N   ALA A  77     2146   1873   1808   -127   -136   -198       N  
ATOM    456  CA  ALA A  77     -11.702   2.868  12.987  1.00 15.03           C  
ANISOU  456  CA  ALA A  77     2073   1852   1788    -82   -150   -158       C  
ATOM    457  C   ALA A  77     -11.241   2.988  11.540  1.00 14.85           C  
ANISOU  457  C   ALA A  77     2043   1809   1792   -105   -150   -158       C  
ATOM    458  O   ALA A  77     -10.413   2.193  11.096  1.00 14.86           O  
ANISOU  458  O   ALA A  77     2005   1857   1786    -88   -166   -146       O  
ATOM    459  CB  ALA A  77     -12.984   2.051  13.055  1.00 14.68           C  
ANISOU  459  CB  ALA A  77     2047   1759   1771    -29   -141   -115       C  
ATOM    460  N   ILE A  78     -11.812   3.936  10.802  1.00 14.73           N  
ANISOU  460  N   ILE A  78     2067   1726   1804   -134   -131   -167       N  
ATOM    461  CA  ILE A  78     -11.358   4.217   9.441  1.00 15.06           C  
ANISOU  461  CA  ILE A  78     2105   1751   1867   -161   -129   -169       C  
ATOM    462  C   ILE A  78      -9.882   4.643   9.455  1.00 15.94           C  
ANISOU  462  C   ILE A  78     2183   1932   1942   -217   -139   -203       C  
ATOM    463  O   ILE A  78      -9.062   4.085   8.728  1.00 16.35           O  
ANISOU  463  O   ILE A  78     2193   2029   1992   -213   -153   -194       O  
ATOM    464  CB  ILE A  78     -12.202   5.310   8.753  1.00 14.54           C  
ANISOU  464  CB  ILE A  78     2095   1603   1828   -179   -102   -172       C  
ATOM    465  CG1 ILE A  78     -13.643   4.830   8.534  1.00 14.67           C  
ANISOU  465  CG1 ILE A  78     2128   1572   1876   -123    -93   -136       C  
ATOM    466  CG2 ILE A  78     -11.549   5.740   7.407  1.00 15.64           C  
ANISOU  466  CG2 ILE A  78     2231   1732   1981   -216    -98   -177       C  
ATOM    467  CD1 ILE A  78     -14.558   5.926   8.012  1.00 14.18           C  
ANISOU  467  CD1 ILE A  78     2117   1441   1828   -123    -65   -136       C  
ATOM    468  N   ASN A  79      -9.547   5.611  10.302  1.00 16.79           N  
ANISOU  468  N   ASN A  79     2309   2056   2016   -270   -133   -243       N  
ATOM    469  CA  ASN A  79      -8.181   6.134  10.344  1.00 17.83           C  
ANISOU  469  CA  ASN A  79     2407   2262   2106   -342   -141   -281       C  
ATOM    470  C   ASN A  79      -7.146   5.098  10.804  1.00 17.80           C  
ANISOU  470  C   ASN A  79     2323   2377   2061   -314   -171   -275       C  
ATOM    471  O   ASN A  79      -6.027   5.072  10.282  1.00 18.09           O  
ANISOU  471  O   ASN A  79     2311   2488   2073   -346   -181   -285       O  
ATOM    472  CB  ASN A  79      -8.111   7.420  11.172  1.00 18.88           C  
ANISOU  472  CB  ASN A  79     2586   2380   2208   -414   -125   -330       C  
ATOM    473  CG  ASN A  79      -8.925   8.578  10.540  1.00 20.86           C  
ANISOU  473  CG  ASN A  79     2924   2512   2491   -441    -90   -337       C  
ATOM    474  OD1 ASN A  79      -9.579   9.345  11.245  1.00 25.52           O  
ANISOU  474  OD1 ASN A  79     3576   3047   3074   -449    -70   -357       O  
ATOM    475  ND2 ASN A  79      -8.876   8.696   9.220  1.00 22.95           N  
ANISOU  475  ND2 ASN A  79     3195   2738   2786   -448    -80   -318       N  
ATOM    476  N   THR A  80      -7.533   4.240  11.745  1.00 16.94           N  
ANISOU  476  N   THR A  80     2203   2292   1941   -249   -181   -253       N  
ATOM    477  CA  THR A  80      -6.639   3.205  12.293  1.00 17.73           C  
ANISOU  477  CA  THR A  80     2237   2504   1998   -203   -206   -240       C  
ATOM    478  C   THR A  80      -6.543   1.945  11.423  1.00 16.51           C  
ANISOU  478  C   THR A  80     2060   2349   1865   -130   -213   -195       C  
ATOM    479  O   THR A  80      -5.461   1.393  11.238  1.00 17.01           O  
ANISOU  479  O   THR A  80     2067   2505   1892   -109   -229   -190       O  
ATOM    480  CB  THR A  80      -7.097   2.780  13.716  1.00 16.98           C  
ANISOU  480  CB  THR A  80     2145   2430   1876   -159   -210   -232       C  
ATOM    481  OG1 THR A  80      -7.235   3.946  14.528  1.00 20.09           O  
ANISOU  481  OG1 THR A  80     2566   2820   2247   -224   -201   -277       O  
ATOM    482  CG2 THR A  80      -6.105   1.840  14.380  1.00 18.64           C  
ANISOU  482  CG2 THR A  80     2290   2765   2028   -108   -232   -218       C  
ATOM    483  N   LEU A  81      -7.677   1.485  10.910  1.00 15.54           N  
ANISOU  483  N   LEU A  81     1981   2126   1795    -90   -202   -162       N  
ATOM    484  CA  LEU A  81      -7.755   0.137  10.334  1.00 15.29           C  
ANISOU  484  CA  LEU A  81     1944   2084   1782    -17   -206   -120       C  
ATOM    485  C   LEU A  81      -7.818   0.083   8.809  1.00 15.03           C  
ANISOU  485  C   LEU A  81     1919   2004   1788    -24   -201   -112       C  
ATOM    486  O   LEU A  81      -7.524  -0.953   8.226  1.00 14.92           O  
ANISOU  486  O   LEU A  81     1893   1999   1777     29   -206    -88       O  
ATOM    487  CB  LEU A  81      -8.919  -0.652  10.943  1.00 15.04           C  
ANISOU  487  CB  LEU A  81     1952   1992   1770     35   -198    -86       C  
ATOM    488  CG  LEU A  81      -8.888  -0.817  12.467  1.00 15.37           C  
ANISOU  488  CG  LEU A  81     1986   2085   1770     58   -203    -85       C  
ATOM    489  CD1 LEU A  81     -10.105  -1.563  12.939  1.00 15.14           C  
ANISOU  489  CD1 LEU A  81     1998   1990   1763    100   -190    -49       C  
ATOM    490  CD2 LEU A  81      -7.597  -1.529  12.914  1.00 16.83           C  
ANISOU  490  CD2 LEU A  81     2119   2380   1896    103   -220    -78       C  
ATOM    491  N   ASN A  82      -8.203   1.179   8.165  1.00 14.83           N  
ANISOU  491  N   ASN A  82     1917   1925   1791    -83   -188   -132       N  
ATOM    492  CA  ASN A  82      -8.096   1.247   6.702  1.00 15.29           C  
ANISOU  492  CA  ASN A  82     1975   1956   1878    -94   -184   -127       C  
ATOM    493  C   ASN A  82      -6.657   0.931   6.275  1.00 15.75           C  
ANISOU  493  C   ASN A  82     1975   2109   1900    -93   -198   -134       C  
ATOM    494  O   ASN A  82      -5.704   1.487   6.822  1.00 16.21           O  
ANISOU  494  O   ASN A  82     1997   2249   1914   -134   -206   -161       O  
ATOM    495  CB  ASN A  82      -8.506   2.623   6.175  1.00 14.54           C  
ANISOU  495  CB  ASN A  82     1915   1804   1805   -160   -165   -147       C  
ATOM    496  CG  ASN A  82      -8.598   2.660   4.664  1.00 15.57           C  
ANISOU  496  CG  ASN A  82     2050   1899   1967   -163   -158   -135       C  
ATOM    497  OD1 ASN A  82      -9.119   1.741   4.042  1.00 13.96           O  
ANISOU  497  OD1 ASN A  82     1849   1668   1788   -114   -161   -109       O  
ATOM    498  ND2 ASN A  82      -8.126   3.747   4.068  1.00 15.79           N  
ANISOU  498  ND2 ASN A  82     2083   1925   1991   -225   -147   -155       N  
ATOM    499  N   GLY A  83      -6.503   0.025   5.324  1.00 15.96           N  
ANISOU  499  N   GLY A  83     1991   2132   1939    -45   -202   -111       N  
ATOM    500  CA  GLY A  83      -5.167  -0.392   4.912  1.00 17.04           C  
ANISOU  500  CA  GLY A  83     2071   2367   2036    -27   -215   -113       C  
ATOM    501  C   GLY A  83      -4.471  -1.432   5.783  1.00 17.22           C  
ANISOU  501  C   GLY A  83     2060   2473   2010     46   -228    -99       C  
ATOM    502  O   GLY A  83      -3.345  -1.814   5.486  1.00 17.94           O  
ANISOU  502  O   GLY A  83     2099   2659   2060     74   -238    -98       O  
ATOM    503  N   LEU A  84      -5.123  -1.918   6.839  1.00 17.10           N  
ANISOU  503  N   LEU A  84     2074   2428   1995     83   -227    -83       N  
ATOM    504  CA  LEU A  84      -4.499  -2.927   7.703  1.00 17.67           C  
ANISOU  504  CA  LEU A  84     2122   2574   2016    162   -237    -63       C  
ATOM    505  C   LEU A  84      -4.198  -4.230   6.943  1.00 17.70           C  
ANISOU  505  C   LEU A  84     2135   2573   2018    250   -235    -32       C  
ATOM    506  O   LEU A  84      -5.062  -4.754   6.246  1.00 16.08           O  
ANISOU  506  O   LEU A  84     1984   2265   1860    265   -223    -16       O  
ATOM    507  CB  LEU A  84      -5.372  -3.230   8.927  1.00 17.95           C  
ANISOU  507  CB  LEU A  84     2197   2567   2055    185   -232    -47       C  
ATOM    508  CG  LEU A  84      -4.952  -4.411   9.805  1.00 18.37           C  
ANISOU  508  CG  LEU A  84     2245   2673   2061    279   -235    -14       C  
ATOM    509  CD1 LEU A  84      -3.648  -4.073  10.534  1.00 21.51           C  
ANISOU  509  CD1 LEU A  84     2566   3223   2383    282   -253    -32       C  
ATOM    510  CD2 LEU A  84      -6.059  -4.774  10.792  1.00 18.17           C  
ANISOU  510  CD2 LEU A  84     2273   2578   2052    297   -225      7       C  
ATOM    511  N   ARG A  85      -2.981  -4.755   7.092  1.00 18.50           N  
ANISOU  511  N   ARG A  85     2185   2788   2058    310   -245    -24       N  
ATOM    512  CA  ARG A  85      -2.641  -6.030   6.452  1.00 19.26           C  
ANISOU  512  CA  ARG A  85     2298   2878   2142    408   -239      6       C  
ATOM    513  C   ARG A  85      -3.138  -7.210   7.272  1.00 19.90           C  
ANISOU  513  C   ARG A  85     2437   2908   2214    494   -228     44       C  
ATOM    514  O   ARG A  85      -2.840  -7.332   8.468  1.00 20.67           O  
ANISOU  514  O   ARG A  85     2517   3071   2267    527   -233     55       O  
ATOM    515  CB  ARG A  85      -1.132  -6.158   6.191  1.00 20.42           C  
ANISOU  515  CB  ARG A  85     2365   3173   2219    452   -251      3       C  
ATOM    516  N   LEU A  86      -3.918  -8.068   6.625  1.00 19.65           N  
ANISOU  516  N   LEU A  86     2481   2761   2225    525   -211     64       N  
ATOM    517  CA  LEU A  86      -4.410  -9.298   7.238  1.00 19.98           C  
ANISOU  517  CA  LEU A  86     2595   2737   2261    602   -194    102       C  
ATOM    518  C   LEU A  86      -4.093 -10.445   6.284  1.00 20.19           C  
ANISOU  518  C   LEU A  86     2666   2725   2281    682   -180    120       C  
ATOM    519  O   LEU A  86      -4.641 -10.504   5.178  1.00 18.71           O  
ANISOU  519  O   LEU A  86     2512   2457   2140    646   -173    107       O  
ATOM    520  CB  LEU A  86      -5.921  -9.202   7.506  1.00 19.38           C  
ANISOU  520  CB  LEU A  86     2581   2539   2243    540   -182    105       C  
ATOM    521  CG  LEU A  86      -6.430  -8.154   8.503  1.00 19.60           C  
ANISOU  521  CG  LEU A  86     2582   2586   2279    471   -190     90       C  
ATOM    522  CD1 LEU A  86      -7.949  -8.059   8.472  1.00 18.65           C  
ANISOU  522  CD1 LEU A  86     2517   2351   2216    414   -176     92       C  
ATOM    523  CD2 LEU A  86      -5.949  -8.450   9.922  1.00 18.99           C  
ANISOU  523  CD2 LEU A  86     2489   2583   2144    526   -193    110       C  
ATOM    524  N   GLN A  87      -3.181 -11.332   6.698  1.00 21.43           N  
ANISOU  524  N   GLN A  87     2823   2946   2374    795   -175    149       N  
ATOM    525  CA  GLN A  87      -2.669 -12.389   5.831  1.00 22.33           C  
ANISOU  525  CA  GLN A  87     2978   3039   2466    887   -160    164       C  
ATOM    526  C   GLN A  87      -2.113 -11.755   4.537  1.00 22.03           C  
ANISOU  526  C   GLN A  87     2880   3051   2439    848   -174    131       C  
ATOM    527  O   GLN A  87      -1.256 -10.892   4.620  1.00 22.20           O  
ANISOU  527  O   GLN A  87     2806   3201   2429    822   -194    113       O  
ATOM    528  CB  GLN A  87      -3.745 -13.469   5.591  1.00 22.88           C  
ANISOU  528  CB  GLN A  87     3172   2944   2576    903   -131    184       C  
ATOM    529  CG  GLN A  87      -4.096 -14.262   6.867  1.00 24.47           C  
ANISOU  529  CG  GLN A  87     3438   3106   2752    960   -112    226       C  
ATOM    530  CD  GLN A  87      -5.406 -15.023   6.761  1.00 26.65           C  
ANISOU  530  CD  GLN A  87     3829   3219   3078    925    -84    238       C  
ATOM    531  OE1 GLN A  87      -6.323 -14.781   7.534  1.00 27.47           O  
ANISOU  531  OE1 GLN A  87     3949   3280   3207    864    -81    244       O  
ATOM    532  NE2 GLN A  87      -5.506 -15.935   5.792  1.00 25.81           N  
ANISOU  532  NE2 GLN A  87     3801   3024   2980    957    -62    238       N  
ATOM    533  N   SER A  88      -2.608 -12.129   3.358  1.00 22.05           N  
ANISOU  533  N   SER A  88     2936   2958   2484    834   -162    121       N  
ATOM    534  CA  SER A  88      -2.109 -11.522   2.114  1.00 21.82           C  
ANISOU  534  CA  SER A  88     2851   2977   2463    798   -174     92       C  
ATOM    535  C   SER A  88      -2.965 -10.352   1.608  1.00 21.21           C  
ANISOU  535  C   SER A  88     2755   2854   2452    666   -183     62       C  
ATOM    536  O   SER A  88      -2.739  -9.817   0.508  1.00 20.85           O  
ANISOU  536  O   SER A  88     2673   2828   2420    626   -189     40       O  
ATOM    537  CB  SER A  88      -1.932 -12.586   1.024  1.00 22.71           C  
ANISOU  537  CB  SER A  88     3023   3037   2569    874   -156     97       C  
ATOM    538  N   LYS A  89      -3.928  -9.944   2.430  1.00 20.53           N  
ANISOU  538  N   LYS A  89     2690   2710   2398    605   -183     63       N  
ATOM    539  CA  LYS A  89      -4.879  -8.895   2.062  1.00 19.93           C  
ANISOU  539  CA  LYS A  89     2610   2582   2381    495   -187     40       C  
ATOM    540  C   LYS A  89      -4.528  -7.559   2.702  1.00 19.57           C  
ANISOU  540  C   LYS A  89     2494   2617   2326    428   -203     22       C  
ATOM    541  O   LYS A  89      -3.849  -7.498   3.747  1.00 19.83           O  
ANISOU  541  O   LYS A  89     2490   2732   2311    455   -211     27       O  
ATOM    542  CB  LYS A  89      -6.304  -9.309   2.455  1.00 19.51           C  
ANISOU  542  CB  LYS A  89     2631   2410   2370    468   -173     51       C  
ATOM    543  CG  LYS A  89      -6.725 -10.689   1.936  1.00 21.51           C  
ANISOU  543  CG  LYS A  89     2968   2574   2631    520   -153     66       C  
ATOM    544  CD  LYS A  89      -7.695 -10.670   0.740  1.00 23.72           C  
ANISOU  544  CD  LYS A  89     3279   2772   2960    460   -146     48       C  
ATOM    545  CE  LYS A  89      -7.104 -10.092  -0.526  1.00 23.78           C  
ANISOU  545  CE  LYS A  89     3238   2827   2971    445   -157     25       C  
ATOM    546  NZ  LYS A  89      -7.663 -10.802  -1.720  1.00 26.55           N  
ANISOU  546  NZ  LYS A  89     3640   3104   3342    442   -145     15       N  
ATOM    547  N   THR A  90      -4.997  -6.489   2.066  1.00 18.55           N  
ANISOU  547  N   THR A  90     2351   2463   2236    341   -205     -1       N  
ATOM    548  CA  THR A  90      -4.904  -5.143   2.621  1.00 18.07           C  
ANISOU  548  CA  THR A  90     2248   2444   2174    264   -213    -22       C  
ATOM    549  C   THR A  90      -6.335  -4.638   2.707  1.00 16.33           C  
ANISOU  549  C   THR A  90     2076   2122   2008    207   -203    -24       C  
ATOM    550  O   THR A  90      -6.949  -4.338   1.678  1.00 15.08           O  
ANISOU  550  O   THR A  90     1934   1908   1888    174   -197    -30       O  
ATOM    551  CB  THR A  90      -4.037  -4.249   1.720  1.00 18.73           C  
ANISOU  551  CB  THR A  90     2274   2597   2245    216   -219    -44       C  
ATOM    552  OG1 THR A  90      -2.758  -4.875   1.554  1.00 21.36           O  
ANISOU  552  OG1 THR A  90     2559   3033   2523    280   -227    -38       O  
ATOM    553  CG2 THR A  90      -3.829  -2.881   2.366  1.00 20.09           C  
ANISOU  553  CG2 THR A  90     2413   2811   2407    130   -223    -69       C  
ATOM    554  N   ILE A  91      -6.891  -4.583   3.918  1.00 15.11           N  
ANISOU  554  N   ILE A  91     1940   1950   1852    203   -202    -18       N  
ATOM    555  CA  ILE A  91      -8.323  -4.296   4.033  1.00 14.18           C  
ANISOU  555  CA  ILE A  91     1867   1741   1778    166   -191    -15       C  
ATOM    556  C   ILE A  91      -8.636  -2.845   3.674  1.00 13.93           C  
ANISOU  556  C   ILE A  91     1825   1699   1770     91   -188    -38       C  
ATOM    557  O   ILE A  91      -7.784  -1.978   3.778  1.00 14.14           O  
ANISOU  557  O   ILE A  91     1815   1785   1773     56   -194    -59       O  
ATOM    558  CB  ILE A  91      -8.931  -4.661   5.415  1.00 14.25           C  
ANISOU  558  CB  ILE A  91     1902   1733   1780    184   -187      1       C  
ATOM    559  CG1 ILE A  91      -8.373  -3.779   6.530  1.00 14.48           C  
ANISOU  559  CG1 ILE A  91     1896   1832   1775    160   -196    -16       C  
ATOM    560  CG2 ILE A  91      -8.773  -6.162   5.716  1.00 14.55           C  
ANISOU  560  CG2 ILE A  91     1970   1759   1797    261   -182     30       C  
ATOM    561  CD1 ILE A  91      -9.123  -3.943   7.872  1.00 14.52           C  
ANISOU  561  CD1 ILE A  91     1926   1817   1773    170   -190     -3       C  
ATOM    562  N   LYS A  92      -9.862  -2.610   3.231  1.00 13.58           N  
ANISOU  562  N   LYS A  92     1813   1580   1765     68   -177    -34       N  
ATOM    563  CA  LYS A  92     -10.365  -1.268   3.053  1.00 13.41           C  
ANISOU  563  CA  LYS A  92     1798   1536   1762     13   -168    -48       C  
ATOM    564  C   LYS A  92     -11.483  -1.077   4.063  1.00 13.31           C  
ANISOU  564  C   LYS A  92     1815   1485   1758     10   -160    -42       C  
ATOM    565  O   LYS A  92     -12.343  -1.957   4.229  1.00 13.20           O  
ANISOU  565  O   LYS A  92     1822   1436   1757     36   -156    -22       O  
ATOM    566  CB  LYS A  92     -10.911  -1.043   1.644  1.00 13.16           C  
ANISOU  566  CB  LYS A  92     1775   1463   1760     -1   -160    -45       C  
ATOM    567  CG  LYS A  92     -11.400   0.401   1.441  1.00 13.08           C  
ANISOU  567  CG  LYS A  92     1780   1427   1764    -46   -146    -56       C  
ATOM    568  CD  LYS A  92     -11.985   0.654   0.061  1.00 12.89           C  
ANISOU  568  CD  LYS A  92     1763   1370   1763    -51   -137    -48       C  
ATOM    569  CE  LYS A  92     -12.542   2.080  -0.027  1.00 12.91           C  
ANISOU  569  CE  LYS A  92     1792   1340   1774    -82   -118    -51       C  
ATOM    570  NZ  LYS A  92     -12.837   2.449  -1.426  1.00 15.35           N  
ANISOU  570  NZ  LYS A  92     2103   1632   2097    -84   -109    -42       N  
ATOM    571  N   VAL A  93     -11.436   0.052   4.757  1.00 13.43           N  
ANISOU  571  N   VAL A  93     1832   1509   1762    -25   -155    -60       N  
ATOM    572  CA  VAL A  93     -12.463   0.434   5.707  1.00 13.39           C  
ANISOU  572  CA  VAL A  93     1854   1473   1760    -27   -145    -57       C  
ATOM    573  C   VAL A  93     -12.955   1.811   5.308  1.00 13.36           C  
ANISOU  573  C   VAL A  93     1874   1432   1769    -63   -128    -71       C  
ATOM    574  O   VAL A  93     -12.157   2.750   5.251  1.00 13.59           O  
ANISOU  574  O   VAL A  93     1901   1477   1784   -103   -126    -95       O  
ATOM    575  CB  VAL A  93     -11.905   0.513   7.135  1.00 13.69           C  
ANISOU  575  CB  VAL A  93     1882   1558   1763    -27   -152    -69       C  
ATOM    576  CG1 VAL A  93     -13.013   0.923   8.113  1.00 13.67           C  
ANISOU  576  CG1 VAL A  93     1909   1525   1762    -25   -140    -67       C  
ATOM    577  CG2 VAL A  93     -11.290  -0.820   7.529  1.00 13.83           C  
ANISOU  577  CG2 VAL A  93     1879   1618   1759     21   -166    -51       C  
ATOM    578  N   SER A  94     -14.253   1.922   5.038  1.00 13.16           N  
ANISOU  578  N   SER A  94     1872   1362   1766    -49   -115    -55       N  
ATOM    579  CA  SER A  94     -14.858   3.166   4.590  1.00 13.19           C  
ANISOU  579  CA  SER A  94     1905   1327   1778    -64    -95    -60       C  
ATOM    580  C   SER A  94     -16.304   3.244   5.085  1.00 13.13           C  
ANISOU  580  C   SER A  94     1917   1297   1775    -36    -81    -44       C  
ATOM    581  O   SER A  94     -16.868   2.241   5.487  1.00 13.02           O  
ANISOU  581  O   SER A  94     1889   1295   1763    -15    -88    -26       O  
ATOM    582  CB  SER A  94     -14.789   3.289   3.044  1.00 13.05           C  
ANISOU  582  CB  SER A  94     1882   1297   1780    -69    -91    -52       C  
ATOM    583  OG  SER A  94     -15.466   2.217   2.397  1.00 12.80           O  
ANISOU  583  OG  SER A  94     1834   1266   1766    -42    -98    -30       O  
ATOM    584  N   TYR A  95     -16.888   4.437   5.091  1.00 13.28           N  
ANISOU  584  N   TYR A  95     1971   1286   1791    -35    -59    -48       N  
ATOM    585  CA  TYR A  95     -18.294   4.577   5.456  1.00 13.30           C  
ANISOU  585  CA  TYR A  95     1986   1278   1790      1    -44    -30       C  
ATOM    586  C   TYR A  95     -19.180   3.829   4.476  1.00 13.08           C  
ANISOU  586  C   TYR A  95     1931   1261   1779     22    -46     -3       C  
ATOM    587  O   TYR A  95     -19.022   3.975   3.275  1.00 13.00           O  
ANISOU  587  O   TYR A  95     1916   1244   1780     18    -45      1       O  
ATOM    588  CB  TYR A  95     -18.716   6.056   5.537  1.00 13.61           C  
ANISOU  588  CB  TYR A  95     2075   1278   1815     12    -15    -39       C  
ATOM    589  CG  TYR A  95     -18.136   6.785   6.731  1.00 13.92           C  
ANISOU  589  CG  TYR A  95     2150   1308   1833    -10     -9    -70       C  
ATOM    590  CD1 TYR A  95     -18.449   6.402   8.040  1.00 13.98           C  
ANISOU  590  CD1 TYR A  95     2150   1340   1823      3    -15    -74       C  
ATOM    591  CD2 TYR A  95     -17.262   7.859   6.553  1.00 14.23           C  
ANISOU  591  CD2 TYR A  95     2231   1314   1863    -51      3    -98       C  
ATOM    592  CE1 TYR A  95     -17.890   7.087   9.158  1.00 14.33           C  
ANISOU  592  CE1 TYR A  95     2225   1381   1841    -21    -10   -108       C  
ATOM    593  CE2 TYR A  95     -16.718   8.550   7.655  1.00 14.92           C  
ANISOU  593  CE2 TYR A  95     2353   1394   1923    -84     10   -134       C  
ATOM    594  CZ  TYR A  95     -17.023   8.156   8.942  1.00 14.66           C  
ANISOU  594  CZ  TYR A  95     2308   1390   1872    -67      1   -140       C  
ATOM    595  OH  TYR A  95     -16.465   8.857  10.001  1.00 15.09           O  
ANISOU  595  OH  TYR A  95     2396   1444   1896   -102      7   -180       O  
ATOM    596  N   ALA A  96     -20.102   3.022   4.993  1.00 13.04           N  
ANISOU  596  N   ALA A  96     1907   1278   1770     38    -48     14       N  
ATOM    597  CA  ALA A  96     -21.088   2.356   4.139  1.00 12.95           C  
ANISOU  597  CA  ALA A  96     1868   1285   1766     47    -48     36       C  
ATOM    598  C   ALA A  96     -22.121   3.389   3.690  1.00 13.12           C  
ANISOU  598  C   ALA A  96     1897   1312   1776     80    -26     48       C  
ATOM    599  O   ALA A  96     -22.579   4.215   4.498  1.00 13.34           O  
ANISOU  599  O   ALA A  96     1949   1335   1786    106     -9     48       O  
ATOM    600  CB  ALA A  96     -21.775   1.226   4.889  1.00 12.97           C  
ANISOU  600  CB  ALA A  96     1852   1312   1763     43    -52     50       C  
ATOM    601  N   ARG A  97     -22.474   3.359   2.409  1.00 13.08           N  
ANISOU  601  N   ARG A  97     1874   1319   1777     86    -25     59       N  
ATOM    602  CA  ARG A  97     -23.602   4.158   1.918  1.00 13.32           C  
ANISOU  602  CA  ARG A  97     1901   1371   1787    129     -4     79       C  
ATOM    603  C   ARG A  97     -24.906   3.471   2.356  1.00 13.45           C  
ANISOU  603  C   ARG A  97     1878   1446   1785    138     -3     96       C  
ATOM    604  O   ARG A  97     -24.893   2.269   2.661  1.00 13.32           O  
ANISOU  604  O   ARG A  97     1840   1445   1778    100    -18     94       O  
ATOM    605  CB  ARG A  97     -23.530   4.299   0.398  1.00 13.28           C  
ANISOU  605  CB  ARG A  97     1884   1373   1789    133     -4     86       C  
ATOM    606  CG  ARG A  97     -22.286   5.038  -0.097  1.00 13.34           C  
ANISOU  606  CG  ARG A  97     1929   1329   1810    119     -1     73       C  
ATOM    607  CD  ARG A  97     -21.942   4.687  -1.539  1.00 13.10           C  
ANISOU  607  CD  ARG A  97     1875   1311   1791    107    -11     76       C  
ATOM    608  NE  ARG A  97     -21.403   3.331  -1.674  1.00 13.56           N  
ANISOU  608  NE  ARG A  97     1903   1383   1867     67    -37     63       N  
ATOM    609  CZ  ARG A  97     -21.665   2.530  -2.712  1.00 12.76           C  
ANISOU  609  CZ  ARG A  97     1768   1313   1768     58    -48     66       C  
ATOM    610  NH1 ARG A  97     -22.472   2.954  -3.679  1.00 12.92           N  
ANISOU  610  NH1 ARG A  97     1770   1366   1773     84    -38     83       N  
ATOM    611  NH2 ARG A  97     -21.117   1.325  -2.789  1.00 12.60           N  
ANISOU  611  NH2 ARG A  97     1736   1292   1761     26    -67     53       N  
ATOM    612  N   PRO A  98     -26.032   4.226   2.420  1.00 13.97           N  
ANISOU  612  N   PRO A  98     1938   1549   1822    190     19    114       N  
ATOM    613  CA  PRO A  98     -27.290   3.581   2.798  1.00 13.97           C  
ANISOU  613  CA  PRO A  98     1890   1622   1798    193     20    131       C  
ATOM    614  C   PRO A  98     -27.593   2.396   1.903  1.00 14.01           C  
ANISOU  614  C   PRO A  98     1845   1669   1808    146      3    134       C  
ATOM    615  O   PRO A  98     -27.449   2.476   0.662  1.00 13.85           O  
ANISOU  615  O   PRO A  98     1814   1655   1793    146     -1    134       O  
ATOM    616  CB  PRO A  98     -28.327   4.690   2.615  1.00 15.30           C  
ANISOU  616  CB  PRO A  98     2054   1831   1927    268     46    153       C  
ATOM    617  CG  PRO A  98     -27.555   5.961   2.918  1.00 14.88           C  
ANISOU  617  CG  PRO A  98     2075   1699   1878    303     63    141       C  
ATOM    618  CD  PRO A  98     -26.179   5.692   2.304  1.00 14.12           C  
ANISOU  618  CD  PRO A  98     2000   1543   1822    249     45    121       C  
ATOM    619  N   SER A  99     -27.976   1.287   2.534  1.00 13.93           N  
ANISOU  619  N   SER A  99     1812   1685   1796    102     -4    134       N  
ATOM    620  CA  SER A  99     -28.301   0.082   1.801  1.00 13.97           C  
ANISOU  620  CA  SER A  99     1782   1722   1803     45    -16    132       C  
ATOM    621  C   SER A  99     -29.531   0.309   0.920  1.00 14.33           C  
ANISOU  621  C   SER A  99     1771   1861   1813     60     -9    146       C  
ATOM    622  O   SER A  99     -30.541   0.835   1.372  1.00 14.67           O  
ANISOU  622  O   SER A  99     1785   1970   1820     98      6    164       O  
ATOM    623  CB  SER A  99     -28.540  -1.089   2.757  1.00 14.06           C  
ANISOU  623  CB  SER A  99     1793   1737   1814     -7    -19    133       C  
ATOM    624  OG  SER A  99     -28.589  -2.294   2.021  1.00 14.12           O  
ANISOU  624  OG  SER A  99     1790   1748   1829    -71    -28    124       O  
ATOM    625  N   SER A 100     -29.427  -0.090  -0.342  1.00 14.59           N  
ANISOU  625  N   SER A 100     1785   1909   1851     34    -19    137       N  
ATOM    626  CA  SER A 100     -30.483   0.151  -1.309  1.00 15.02           C  
ANISOU  626  CA  SER A 100     1780   2061   1866     50    -14    149       C  
ATOM    627  C   SER A 100     -30.235  -0.657  -2.556  1.00 15.10           C  
ANISOU  627  C   SER A 100     1775   2078   1885     -2    -30    131       C  
ATOM    628  O   SER A 100     -29.091  -0.961  -2.894  1.00 14.84           O  
ANISOU  628  O   SER A 100     1783   1965   1889    -21    -41    113       O  
ATOM    629  CB  SER A 100     -30.495   1.627  -1.706  1.00 15.48           C  
ANISOU  629  CB  SER A 100     1849   2122   1910    141      1    167       C  
ATOM    630  OG  SER A 100     -31.362   1.833  -2.799  1.00 15.71           O  
ANISOU  630  OG  SER A 100     1822   2247   1900    166      4    181       O  
ATOM    631  N   GLU A 101     -31.311  -0.965  -3.269  1.00 15.08           N  
ANISOU  631  N   GLU A 101     1708   2181   1842    -23    -30    134       N  
ATOM    632  CA  GLU A 101     -31.183  -1.651  -4.536  1.00 15.15           C  
ANISOU  632  CA  GLU A 101     1698   2209   1850    -71    -44    113       C  
ATOM    633  C   GLU A 101     -30.418  -0.787  -5.566  1.00 14.89           C  
ANISOU  633  C   GLU A 101     1682   2145   1830    -13    -46    116       C  
ATOM    634  O   GLU A 101     -29.721  -1.313  -6.447  1.00 14.95           O  
ANISOU  634  O   GLU A 101     1704   2119   1858    -46    -59     95       O  
ATOM    635  CB  GLU A 101     -32.573  -2.064  -5.021  1.00 15.77           C  
ANISOU  635  CB  GLU A 101     1696   2425   1872   -109    -43    114       C  
ATOM    636  CG  GLU A 101     -32.598  -2.710  -6.352  1.00 17.24           C  
ANISOU  636  CG  GLU A 101     1856   2650   2047   -160    -56     89       C  
ATOM    637  CD  GLU A 101     -33.921  -3.389  -6.641  1.00 19.79           C  
ANISOU  637  CD  GLU A 101     2101   3107   2312   -229    -56     80       C  
ATOM    638  OE1 GLU A 101     -34.981  -2.941  -6.130  1.00 18.84           O  
ANISOU  638  OE1 GLU A 101     1923   3091   2146   -201    -45    105       O  
ATOM    639  OE2 GLU A 101     -33.886  -4.373  -7.407  1.00 20.80           O  
ANISOU  639  OE2 GLU A 101     2226   3242   2435   -312    -66     47       O  
ATOM    640  N   VAL A 102     -30.506   0.534  -5.428  1.00 14.91           N  
ANISOU  640  N   VAL A 102     1692   2151   1821     74    -31    143       N  
ATOM    641  CA  VAL A 102     -29.935   1.437  -6.428  1.00 14.81           C  
ANISOU  641  CA  VAL A 102     1697   2117   1812    129    -27    153       C  
ATOM    642  C   VAL A 102     -28.403   1.341  -6.550  1.00 14.29           C  
ANISOU  642  C   VAL A 102     1694   1937   1800    108    -36    134       C  
ATOM    643  O   VAL A 102     -27.854   1.622  -7.617  1.00 14.22           O  
ANISOU  643  O   VAL A 102     1690   1917   1795    121    -39    133       O  
ATOM    644  CB  VAL A 102     -30.416   2.918  -6.271  1.00 15.08           C  
ANISOU  644  CB  VAL A 102     1740   2173   1817    231     -1    189       C  
ATOM    645  CG1 VAL A 102     -31.924   2.977  -6.012  1.00 15.65           C  
ANISOU  645  CG1 VAL A 102     1745   2371   1831    261      9    209       C  
ATOM    646  CG2 VAL A 102     -29.661   3.648  -5.159  1.00 17.74           C  
ANISOU  646  CG2 VAL A 102     2151   2405   2185    259     12    191       C  
ATOM    647  N   ILE A 103     -27.727   0.913  -5.486  1.00 13.99           N  
ANISOU  647  N   ILE A 103     1697   1825   1795     76    -41    120       N  
ATOM    648  CA  ILE A 103     -26.255   0.924  -5.482  1.00 13.59           C  
ANISOU  648  CA  ILE A 103     1697   1680   1784     65    -49    104       C  
ATOM    649  C   ILE A 103     -25.649  -0.385  -5.974  1.00 13.44           C  
ANISOU  649  C   ILE A 103     1679   1641   1785      4    -68     77       C  
ATOM    650  O   ILE A 103     -24.435  -0.477  -6.198  1.00 13.17           O  
ANISOU  650  O   ILE A 103     1677   1550   1777     -1    -76     65       O  
ATOM    651  CB  ILE A 103     -25.642   1.337  -4.107  1.00 13.39           C  
ANISOU  651  CB  ILE A 103     1720   1588   1780     75    -43    104       C  
ATOM    652  CG1 ILE A 103     -26.011   0.333  -2.991  1.00 13.41           C  
ANISOU  652  CG1 ILE A 103     1718   1593   1784     35    -49     97       C  
ATOM    653  CG2 ILE A 103     -26.085   2.724  -3.710  1.00 13.59           C  
ANISOU  653  CG2 ILE A 103     1762   1616   1786    138    -20    126       C  
ATOM    654  CD1 ILE A 103     -25.289   0.627  -1.621  1.00 13.23           C  
ANISOU  654  CD1 ILE A 103     1739   1509   1779     43    -46     93       C  
ATOM    655  N   LYS A 104     -26.495  -1.401  -6.139  1.00 13.69           N  
ANISOU  655  N   LYS A 104     1678   1723   1799    -42    -74     67       N  
ATOM    656  CA  LYS A 104     -26.027  -2.726  -6.539  1.00 13.67           C  
ANISOU  656  CA  LYS A 104     1691   1693   1810   -101    -87     40       C  
ATOM    657  C   LYS A 104     -25.721  -2.801  -8.037  1.00 13.70           C  
ANISOU  657  C   LYS A 104     1679   1719   1808   -102    -96     26       C  
ATOM    658  O   LYS A 104     -26.224  -1.998  -8.807  1.00 13.85           O  
ANISOU  658  O   LYS A 104     1661   1797   1803    -68    -91     41       O  
ATOM    659  CB  LYS A 104     -27.071  -3.783  -6.165  1.00 14.04           C  
ANISOU  659  CB  LYS A 104     1719   1780   1836   -163    -86     31       C  
ATOM    660  CG  LYS A 104     -27.248  -3.931  -4.662  1.00 15.10           C  
ANISOU  660  CG  LYS A 104     1875   1886   1977   -169    -78     43       C  
ATOM    661  CD  LYS A 104     -28.366  -4.920  -4.323  1.00 17.44           C  
ANISOU  661  CD  LYS A 104     2150   2230   2248   -238    -72     38       C  
ATOM    662  CE  LYS A 104     -27.905  -6.379  -4.447  1.00 20.56           C  
ANISOU  662  CE  LYS A 104     2593   2562   2655   -306    -75     12       C  
ATOM    663  NZ  LYS A 104     -28.870  -7.270  -3.710  1.00 20.98           N  
ANISOU  663  NZ  LYS A 104     2645   2639   2687   -377    -63     13       N  
ATOM    664  N   ASP A 105     -24.893  -3.779  -8.427  1.00 13.63           N  
ANISOU  664  N   ASP A 105     1700   1662   1815   -135   -106      0       N  
ATOM    665  CA  ASP A 105     -24.554  -4.033  -9.835  1.00 13.70           C  
ANISOU  665  CA  ASP A 105     1698   1690   1817   -141   -114    -18       C  
ATOM    666  C   ASP A 105     -24.169  -2.765 -10.607  1.00 13.55           C  
ANISOU  666  C   ASP A 105     1661   1691   1795    -83   -111      2       C  
ATOM    667  O   ASP A 105     -24.742  -2.457 -11.662  1.00 13.77           O  
ANISOU  667  O   ASP A 105     1649   1788   1796    -73   -111      5       O  
ATOM    668  CB  ASP A 105     -25.705  -4.756 -10.513  1.00 15.03           C  
ANISOU  668  CB  ASP A 105     1829   1932   1951   -193   -116    -36       C  
ATOM    669  CG  ASP A 105     -26.160  -5.973  -9.726  1.00 18.30           C  
ANISOU  669  CG  ASP A 105     2268   2322   2363   -261   -113    -53       C  
ATOM    670  OD1 ASP A 105     -25.331  -6.896  -9.532  1.00 22.66           O  
ANISOU  670  OD1 ASP A 105     2878   2794   2936   -282   -115    -73       O  
ATOM    671  OD2 ASP A 105     -27.328  -5.991  -9.274  1.00 21.20           O  
ANISOU  671  OD2 ASP A 105     2600   2750   2705   -290   -107    -45       O  
ATOM    672  N   ALA A 106     -23.214  -2.022 -10.050  1.00 13.23           N  
ANISOU  672  N   ALA A 106     1652   1595   1781    -48   -107     15       N  
ATOM    673  CA  ALA A 106     -22.790  -0.751 -10.641  1.00 13.16           C  
ANISOU  673  CA  ALA A 106     1640   1590   1769     -1    -98     36       C  
ATOM    674  C   ALA A 106     -21.315  -0.814 -11.008  1.00 12.94           C  
ANISOU  674  C   ALA A 106     1638   1514   1763     -1   -104     24       C  
ATOM    675  O   ALA A 106     -20.655   0.223 -11.188  1.00 12.86           O  
ANISOU  675  O   ALA A 106     1641   1487   1758     26    -94     40       O  
ATOM    676  CB  ALA A 106     -23.071   0.414  -9.682  1.00 13.14           C  
ANISOU  676  CB  ALA A 106     1653   1571   1767     36    -81     63       C  
ATOM    677  N   ASN A 107     -20.824  -2.046 -11.158  1.00 12.92           N  
ANISOU  677  N   ASN A 107     1646   1494   1768    -31   -117     -3       N  
ATOM    678  CA  ASN A 107     -19.405  -2.312 -11.354  1.00 12.77           C  
ANISOU  678  CA  ASN A 107     1648   1439   1764    -26   -124    -16       C  
ATOM    679  C   ASN A 107     -19.108  -2.637 -12.812  1.00 12.89           C  
ANISOU  679  C   ASN A 107     1646   1485   1766    -25   -130    -29       C  
ATOM    680  O   ASN A 107     -19.738  -3.521 -13.394  1.00 13.10           O  
ANISOU  680  O   ASN A 107     1664   1536   1778    -48   -135    -49       O  
ATOM    681  CB  ASN A 107     -18.971  -3.485 -10.460  1.00 12.75           C  
ANISOU  681  CB  ASN A 107     1678   1393   1774    -44   -131    -34       C  
ATOM    682  CG  ASN A 107     -17.460  -3.652 -10.398  1.00 13.54           C  
ANISOU  682  CG  ASN A 107     1795   1466   1883    -26   -136    -41       C  
ATOM    683  OD1 ASN A 107     -16.720  -2.682 -10.440  1.00 14.97           O  
ANISOU  683  OD1 ASN A 107     1968   1652   2068    -10   -133    -30       O  
ATOM    684  ND2 ASN A 107     -17.006  -4.893 -10.288  1.00 13.36           N  
ANISOU  684  ND2 ASN A 107     1799   1417   1859    -27   -142    -60       N  
ATOM    685  N   LEU A 108     -18.162  -1.909 -13.402  1.00 12.81           N  
ANISOU  685  N   LEU A 108     1633   1478   1758     -3   -127    -20       N  
ATOM    686  CA  LEU A 108     -17.819  -2.107 -14.805  1.00 12.94           C  
ANISOU  686  CA  LEU A 108     1630   1529   1758      4   -131    -30       C  
ATOM    687  C   LEU A 108     -16.470  -2.782 -14.985  1.00 12.92           C  
ANISOU  687  C   LEU A 108     1641   1507   1760      9   -138    -49       C  
ATOM    688  O   LEU A 108     -15.511  -2.493 -14.254  1.00 12.79           O  
ANISOU  688  O   LEU A 108     1638   1466   1757     16   -137    -43       O  
ATOM    689  CB  LEU A 108     -17.798  -0.777 -15.575  1.00 12.99           C  
ANISOU  689  CB  LEU A 108     1618   1565   1753     29   -118      0       C  
ATOM    690  CG  LEU A 108     -19.055   0.097 -15.671  1.00 13.13           C  
ANISOU  690  CG  LEU A 108     1620   1615   1754     47   -105     27       C  
ATOM    691  CD1 LEU A 108     -18.714   1.455 -16.270  1.00 13.23           C  
ANISOU  691  CD1 LEU A 108     1636   1632   1758     78    -86     61       C  
ATOM    692  CD2 LEU A 108     -20.169  -0.574 -16.471  1.00 13.38           C  
ANISOU  692  CD2 LEU A 108     1616   1711   1758     39   -113     15       C  
ATOM    693  N   TYR A 109     -16.431  -3.647 -15.997  1.00 13.11           N  
ANISOU  693  N   TYR A 109     1660   1552   1768      7   -146    -74       N  
ATOM    694  CA  TYR A 109     -15.218  -4.158 -16.578  1.00 13.19           C  
ANISOU  694  CA  TYR A 109     1675   1564   1771     26   -150    -90       C  
ATOM    695  C   TYR A 109     -14.881  -3.382 -17.879  1.00 13.26           C  
ANISOU  695  C   TYR A 109     1650   1624   1763     41   -146    -78       C  
ATOM    696  O   TYR A 109     -15.739  -3.224 -18.774  1.00 13.40           O  
ANISOU  696  O   TYR A 109     1646   1681   1763     37   -145    -77       O  
ATOM    697  CB  TYR A 109     -15.386  -5.653 -16.863  1.00 13.73           C  
ANISOU  697  CB  TYR A 109     1772   1615   1829     17   -157   -127       C  
ATOM    698  CG  TYR A 109     -14.242  -6.257 -17.627  1.00 14.64           C  
ANISOU  698  CG  TYR A 109     1895   1739   1929     47   -159   -146       C  
ATOM    699  CD1 TYR A 109     -13.182  -6.879 -16.954  1.00 15.84           C  
ANISOU  699  CD1 TYR A 109     2076   1859   2084     77   -160   -152       C  
ATOM    700  CD2 TYR A 109     -14.208  -6.201 -19.013  1.00 16.16           C  
ANISOU  700  CD2 TYR A 109     2063   1980   2099     54   -161   -157       C  
ATOM    701  CE1 TYR A 109     -12.130  -7.438 -17.642  1.00 15.81           C  
ANISOU  701  CE1 TYR A 109     2076   1871   2059    116   -160   -168       C  
ATOM    702  CE2 TYR A 109     -13.160  -6.752 -19.721  1.00 17.78           C  
ANISOU  702  CE2 TYR A 109     2273   2197   2285     87   -162   -175       C  
ATOM    703  CZ  TYR A 109     -12.122  -7.375 -19.026  1.00 17.30           C  
ANISOU  703  CZ  TYR A 109     2242   2106   2227    120   -161   -180       C  
ATOM    704  OH  TYR A 109     -11.087  -7.924 -19.728  1.00 16.33           O  
ANISOU  704  OH  TYR A 109     2122   2004   2079    163   -161   -196       O  
ATOM    705  N   ILE A 110     -13.638  -2.896 -17.975  1.00 13.23           N  
ANISOU  705  N   ILE A 110     1639   1628   1759     57   -143    -67       N  
ATOM    706  CA  ILE A 110     -13.191  -2.118 -19.144  1.00 13.34           C  
ANISOU  706  CA  ILE A 110     1624   1688   1756     68   -135    -51       C  
ATOM    707  C   ILE A 110     -11.943  -2.751 -19.758  1.00 13.50           C  
ANISOU  707  C   ILE A 110     1636   1735   1760     88   -141    -69       C  
ATOM    708  O   ILE A 110     -11.019  -3.113 -19.042  1.00 13.49           O  
ANISOU  708  O   ILE A 110     1643   1721   1764     97   -144    -76       O  
ATOM    709  CB  ILE A 110     -12.915  -0.635 -18.772  1.00 13.26           C  
ANISOU  709  CB  ILE A 110     1613   1672   1755     60   -119    -14       C  
ATOM    710  CG1 ILE A 110     -14.168   0.025 -18.164  1.00 13.17           C  
ANISOU  710  CG1 ILE A 110     1615   1636   1754     54   -111      6       C  
ATOM    711  CG2 ILE A 110     -12.436   0.179 -19.999  1.00 13.46           C  
ANISOU  711  CG2 ILE A 110     1615   1740   1759     67   -106      8       C  
ATOM    712  CD1 ILE A 110     -13.820   1.086 -17.110  1.00 15.48           C  
ANISOU  712  CD1 ILE A 110     1930   1889   2063     40    -97     27       C  
ATOM    713  N   SER A 111     -11.908  -2.888 -21.079  1.00 13.70           N  
ANISOU  713  N   SER A 111     1640   1805   1761    102   -141    -76       N  
ATOM    714  CA  SER A 111     -10.674  -3.314 -21.743  1.00 13.91           C  
ANISOU  714  CA  SER A 111     1652   1867   1765    127   -143    -88       C  
ATOM    715  C   SER A 111     -10.384  -2.511 -23.012  1.00 14.07           C  
ANISOU  715  C   SER A 111     1637   1947   1763    133   -133    -68       C  
ATOM    716  O   SER A 111     -11.262  -1.853 -23.557  1.00 14.08           O  
ANISOU  716  O   SER A 111     1628   1961   1759    126   -127    -49       O  
ATOM    717  CB  SER A 111     -10.701  -4.821 -22.050  1.00 14.12           C  
ANISOU  717  CB  SER A 111     1703   1884   1778    149   -153   -132       C  
ATOM    718  OG  SER A 111     -11.765  -5.132 -22.909  1.00 14.25           O  
ANISOU  718  OG  SER A 111     1719   1914   1780    136   -156   -149       O  
ATOM    719  N   GLY A 112      -9.133  -2.567 -23.454  1.00 14.26           N  
ANISOU  719  N   GLY A 112     1639   2012   1767    151   -131    -69       N  
ATOM    720  CA  GLY A 112      -8.718  -1.907 -24.690  1.00 14.48           C  
ANISOU  720  CA  GLY A 112     1633   2102   1768    157   -120    -49       C  
ATOM    721  C   GLY A 112      -8.109  -0.544 -24.412  1.00 14.50           C  
ANISOU  721  C   GLY A 112     1622   2110   1775    127   -102     -8       C  
ATOM    722  O   GLY A 112      -7.752   0.169 -25.345  1.00 14.72           O  
ANISOU  722  O   GLY A 112     1628   2183   1782    124    -88     16       O  
ATOM    723  N   LEU A 113      -7.990  -0.189 -23.128  1.00 14.31           N  
ANISOU  723  N   LEU A 113     1618   2043   1778    101   -101     -2       N  
ATOM    724  CA  LEU A 113      -7.404   1.094 -22.735  1.00 14.41           C  
ANISOU  724  CA  LEU A 113     1629   2052   1793     60    -82     30       C  
ATOM    725  C   LEU A 113      -5.930   1.119 -23.083  1.00 14.73           C  
ANISOU  725  C   LEU A 113     1630   2160   1805     53    -78     29       C  
ATOM    726  O   LEU A 113      -5.251   0.106 -22.927  1.00 14.79           O  
ANISOU  726  O   LEU A 113     1619   2201   1800     84    -94      2       O  
ATOM    727  CB  LEU A 113      -7.568   1.355 -21.235  1.00 14.19           C  
ANISOU  727  CB  LEU A 113     1631   1968   1795     33    -83     28       C  
ATOM    728  CG  LEU A 113      -8.988   1.552 -20.699  1.00 13.93           C  
ANISOU  728  CG  LEU A 113     1634   1872   1787     34    -82     34       C  
ATOM    729  CD1 LEU A 113      -9.005   1.363 -19.201  1.00 13.73           C  
ANISOU  729  CD1 LEU A 113     1630   1802   1785     19    -90     22       C  
ATOM    730  CD2 LEU A 113      -9.529   2.936 -21.078  1.00 14.06           C  
ANISOU  730  CD2 LEU A 113     1670   1868   1802     19    -56     73       C  
ATOM    731  N   PRO A 114      -5.434   2.267 -23.569  1.00 15.00           N  
ANISOU  731  N   PRO A 114     1655   2220   1826     16    -55     61       N  
ATOM    732  CA  PRO A 114      -3.999   2.358 -23.817  1.00 15.38           C  
ANISOU  732  CA  PRO A 114     1658   2345   1842     -3    -50     62       C  
ATOM    733  C   PRO A 114      -3.245   2.120 -22.518  1.00 15.39           C  
ANISOU  733  C   PRO A 114     1649   2352   1846    -23    -60     43       C  
ATOM    734  O   PRO A 114      -3.663   2.608 -21.453  1.00 15.21           O  
ANISOU  734  O   PRO A 114     1660   2268   1850    -56    -58     45       O  
ATOM    735  CB  PRO A 114      -3.814   3.808 -24.274  1.00 15.70           C  
ANISOU  735  CB  PRO A 114     1708   2383   1873    -60    -17    102       C  
ATOM    736  CG  PRO A 114      -5.178   4.203 -24.826  1.00 15.52           C  
ANISOU  736  CG  PRO A 114     1727   2305   1866    -36     -7    124       C  
ATOM    737  CD  PRO A 114      -6.127   3.534 -23.874  1.00 15.07           C  
ANISOU  737  CD  PRO A 114     1696   2189   1842    -11    -29     99       C  
ATOM    738  N   ARG A 115      -2.143   1.383 -22.610  1.00 15.65           N  
ANISOU  738  N   ARG A 115     1633   2465   1847      4    -72     26       N  
ATOM    739  CA  ARG A 115      -1.349   1.037 -21.428  1.00 15.75           C  
ANISOU  739  CA  ARG A 115     1626   2506   1851     -1    -83      9       C  
ATOM    740  C   ARG A 115      -0.754   2.241 -20.694  1.00 16.00           C  
ANISOU  740  C   ARG A 115     1650   2550   1879    -89    -68     23       C  
ATOM    741  O   ARG A 115      -0.326   2.113 -19.541  1.00 16.04           O  
ANISOU  741  O   ARG A 115     1646   2568   1882   -103    -78      9       O  
ATOM    742  CB  ARG A 115      -0.232   0.051 -21.792  1.00 16.11           C  
ANISOU  742  CB  ARG A 115     1616   2652   1851     57    -95     -7       C  
ATOM    743  CG  ARG A 115       0.894   0.653 -22.616  1.00 16.99           C  
ANISOU  743  CG  ARG A 115     1667   2871   1918     25    -80      9       C  
ATOM    744  CD  ARG A 115       1.878  -0.425 -23.021  1.00 19.70           C  
ANISOU  744  CD  ARG A 115     1957   3316   2212    103    -91     -8       C  
ATOM    745  NE  ARG A 115       3.054   0.120 -23.688  1.00 21.17           N  
ANISOU  745  NE  ARG A 115     2072   3624   2347     70    -77      7       N  
ATOM    746  CZ  ARG A 115       3.837  -0.570 -24.515  1.00 21.25           C  
ANISOU  746  CZ  ARG A 115     2032   3734   2307    135    -79      1       C  
ATOM    747  NH1 ARG A 115       4.888   0.016 -25.068  1.00 21.43           N  
ANISOU  747  NH1 ARG A 115     1986   3875   2282     95    -65     18       N  
ATOM    748  NH2 ARG A 115       3.562  -1.837 -24.807  1.00 18.66           N  
ANISOU  748  NH2 ARG A 115     1726   3387   1975    237    -93    -22       N  
ATOM    749  N   THR A 116      -0.738   3.401 -21.357  1.00 16.22           N  
ANISOU  749  N   THR A 116     1687   2575   1903   -149    -42     49       N  
ATOM    750  CA  THR A 116      -0.222   4.632 -20.737  1.00 16.58           C  
ANISOU  750  CA  THR A 116     1739   2618   1941   -246    -20     60       C  
ATOM    751  C   THR A 116      -1.231   5.280 -19.777  1.00 16.27           C  
ANISOU  751  C   THR A 116     1773   2464   1944   -276    -13     63       C  
ATOM    752  O   THR A 116      -0.885   6.200 -19.026  1.00 16.63           O  
ANISOU  752  O   THR A 116     1839   2494   1987   -355      3     62       O  
ATOM    753  CB  THR A 116       0.213   5.673 -21.811  1.00 17.06           C  
ANISOU  753  CB  THR A 116     1796   2709   1978   -305     12     91       C  
ATOM    754  OG1 THR A 116      -0.885   5.926 -22.703  1.00 16.81           O  
ANISOU  754  OG1 THR A 116     1812   2608   1969   -270     25    116       O  
ATOM    755  CG2 THR A 116       1.417   5.154 -22.599  1.00 17.49           C  
ANISOU  755  CG2 THR A 116     1768   2897   1982   -289      7     88       C  
ATOM    756  N   MET A 117      -2.482   4.834 -19.807  1.00 15.76           N  
ANISOU  756  N   MET A 117     1749   2324   1914   -217    -22     63       N  
ATOM    757  CA  MET A 117      -3.464   5.402 -18.890  1.00 15.50           C  
ANISOU  757  CA  MET A 117     1781   2193   1917   -235    -15     66       C  
ATOM    758  C   MET A 117      -3.234   4.893 -17.466  1.00 15.36           C  
ANISOU  758  C   MET A 117     1756   2174   1906   -238    -36     38       C  
ATOM    759  O   MET A 117      -3.219   3.681 -17.227  1.00 15.12           O  
ANISOU  759  O   MET A 117     1700   2169   1877   -179    -62     19       O  
ATOM    760  CB  MET A 117      -4.898   5.106 -19.351  1.00 15.08           C  
ANISOU  760  CB  MET A 117     1764   2077   1891   -175    -18     77       C  
ATOM    761  CG  MET A 117      -5.314   5.883 -20.594  1.00 15.28           C  
ANISOU  761  CG  MET A 117     1808   2091   1907   -173      8    111       C  
ATOM    762  SD  MET A 117      -7.072   5.802 -20.940  1.00 18.63           S  
ANISOU  762  SD  MET A 117     2273   2453   2354   -111      8    127       S  
ATOM    763  CE  MET A 117      -7.770   6.891 -19.692  1.00 17.97           C  
ANISOU  763  CE  MET A 117     2260   2273   2294   -143     29    138       C  
ATOM    764  N   THR A 118      -3.048   5.825 -16.529  1.00 15.57           N  
ANISOU  764  N   THR A 118     1811   2170   1934   -307    -21     35       N  
ATOM    765  CA  THR A 118      -2.956   5.487 -15.106  1.00 15.45           C  
ANISOU  765  CA  THR A 118     1796   2150   1926   -312    -39     11       C  
ATOM    766  C   THR A 118      -4.354   5.311 -14.510  1.00 14.96           C  
ANISOU  766  C   THR A 118     1788   1991   1903   -271    -43     12       C  
ATOM    767  O   THR A 118      -5.362   5.642 -15.137  1.00 14.78           O  
ANISOU  767  O   THR A 118     1805   1911   1899   -249    -30     32       O  
ATOM    768  CB  THR A 118      -2.233   6.584 -14.294  1.00 15.94           C  
ANISOU  768  CB  THR A 118     1869   2219   1969   -410    -21      2       C  
ATOM    769  OG1 THR A 118      -2.975   7.806 -14.403  1.00 16.94           O  
ANISOU  769  OG1 THR A 118     2073   2249   2114   -451     12     20       O  
ATOM    770  CG2 THR A 118      -0.790   6.804 -14.796  1.00 16.55           C  
ANISOU  770  CG2 THR A 118     1881   2408   1999   -466    -15     -2       C  
ATOM    771  N   GLN A 119      -4.402   4.802 -13.283  1.00 14.79           N  
ANISOU  771  N   GLN A 119     1767   1965   1889   -260    -62     -8       N  
ATOM    772  CA  GLN A 119      -5.645   4.733 -12.527  1.00 14.41           C  
ANISOU  772  CA  GLN A 119     1768   1835   1873   -234    -64     -7       C  
ATOM    773  C   GLN A 119      -6.344   6.089 -12.496  1.00 14.53           C  
ANISOU  773  C   GLN A 119     1846   1773   1900   -273    -33      9       C  
ATOM    774  O   GLN A 119      -7.544   6.170 -12.744  1.00 14.27           O  
ANISOU  774  O   GLN A 119     1850   1684   1889   -235    -26     25       O  
ATOM    775  CB  GLN A 119      -5.397   4.235 -11.101  1.00 14.78           C  
ANISOU  775  CB  GLN A 119     1806   1893   1917   -233    -82    -29       C  
ATOM    776  CG  GLN A 119      -6.698   4.018 -10.296  1.00 16.43           C  
ANISOU  776  CG  GLN A 119     2060   2026   2157   -201    -86    -28       C  
ATOM    777  CD  GLN A 119      -6.442   3.480  -8.900  1.00 20.18           C  
ANISOU  777  CD  GLN A 119     2526   2515   2626   -195   -103    -46       C  
ATOM    778  OE1 GLN A 119      -5.364   3.674  -8.338  1.00 22.35           O  
ANISOU  778  OE1 GLN A 119     2770   2848   2873   -231   -107    -61       O  
ATOM    779  NE2 GLN A 119      -7.437   2.812  -8.330  1.00 19.55           N  
ANISOU  779  NE2 GLN A 119     2469   2391   2569   -153   -112    -45       N  
ATOM    780  N   LYS A 120      -5.593   7.148 -12.180  1.00 14.99           N  
ANISOU  780  N   LYS A 120     1921   1834   1941   -350    -12      5       N  
ATOM    781  CA  LYS A 120      -6.166   8.487 -12.128  1.00 15.24           C  
ANISOU  781  CA  LYS A 120     2029   1783   1979   -387     24     20       C  
ATOM    782  C   LYS A 120      -6.718   8.928 -13.501  1.00 15.29           C  
ANISOU  782  C   LYS A 120     2059   1762   1988   -360     47     56       C  
ATOM    783  O   LYS A 120      -7.783   9.551 -13.566  1.00 15.27           O  
ANISOU  783  O   LYS A 120     2117   1685   1998   -332     68     78       O  
ATOM    784  CB  LYS A 120      -5.129   9.499 -11.609  1.00 15.86           C  
ANISOU  784  CB  LYS A 120     2125   1871   2032   -489     45      4       C  
ATOM    785  CG  LYS A 120      -5.647  10.928 -11.492  1.00 17.31           C  
ANISOU  785  CG  LYS A 120     2406   1953   2218   -532     89     17       C  
ATOM    786  CD  LYS A 120      -4.516  11.941 -11.700  1.00 19.33           C  
ANISOU  786  CD  LYS A 120     2679   2224   2441   -642    118     11       C  
ATOM    787  N   ASP A 121      -5.988   8.615 -14.575  1.00 15.41           N  
ANISOU  787  N   ASP A 121     2025   1844   1986   -362     43     64       N  
ATOM    788  CA  ASP A 121      -6.427   8.916 -15.938  1.00 15.48           C  
ANISOU  788  CA  ASP A 121     2046   1843   1992   -331     61     98       C  
ATOM    789  C   ASP A 121      -7.760   8.224 -16.257  1.00 14.99           C  
ANISOU  789  C   ASP A 121     1985   1759   1950   -244     46    108       C  
ATOM    790  O   ASP A 121      -8.638   8.818 -16.867  1.00 15.06           O  
ANISOU  790  O   ASP A 121     2034   1728   1961   -213     68    139       O  
ATOM    791  CB  ASP A 121      -5.397   8.434 -16.965  1.00 15.64           C  
ANISOU  791  CB  ASP A 121     2000   1956   1988   -339     53     99       C  
ATOM    792  CG  ASP A 121      -4.131   9.258 -16.978  1.00 18.07           C  
ANISOU  792  CG  ASP A 121     2301   2299   2265   -432     75     97       C  
ATOM    793  OD1 ASP A 121      -4.192  10.493 -16.779  1.00 19.69           O  
ANISOU  793  OD1 ASP A 121     2575   2438   2467   -493    111    110       O  
ATOM    794  OD2 ASP A 121      -3.059   8.665 -17.243  1.00 21.05           O  
ANISOU  794  OD2 ASP A 121     2607   2774   2618   -446     57     83       O  
ATOM    795  N   VAL A 122      -7.899   6.967 -15.838  1.00 14.57           N  
ANISOU  795  N   VAL A 122     1889   1738   1909   -206     11     83       N  
ATOM    796  CA  VAL A 122      -9.135   6.202 -16.069  1.00 14.17           C  
ANISOU  796  CA  VAL A 122     1836   1675   1874   -138     -5     86       C  
ATOM    797  C   VAL A 122     -10.265   6.819 -15.263  1.00 14.10           C  
ANISOU  797  C   VAL A 122     1880   1596   1881   -126      9     97       C  
ATOM    798  O   VAL A 122     -11.393   7.001 -15.768  1.00 14.06           O  
ANISOU  798  O   VAL A 122     1891   1573   1876    -82     18    119       O  
ATOM    799  CB  VAL A 122      -8.937   4.675 -15.747  1.00 13.85           C  
ANISOU  799  CB  VAL A 122     1750   1675   1839   -109    -41     56       C  
ATOM    800  CG1 VAL A 122     -10.242   3.896 -15.917  1.00 13.54           C  
ANISOU  800  CG1 VAL A 122     1713   1619   1813    -58    -55     54       C  
ATOM    801  CG2 VAL A 122      -7.863   4.098 -16.642  1.00 14.01           C  
ANISOU  801  CG2 VAL A 122     1720   1765   1836   -106    -51     48       C  
ATOM    802  N   GLU A 123      -9.965   7.178 -14.016  1.00 14.15           N  
ANISOU  802  N   GLU A 123     1912   1571   1894   -164     11     81       N  
ATOM    803  CA  GLU A 123     -10.969   7.804 -13.166  1.00 14.81           C  
ANISOU  803  CA  GLU A 123     2050   1589   1988   -151     27     89       C  
ATOM    804  C   GLU A 123     -11.400   9.158 -13.745  1.00 14.79           C  
ANISOU  804  C   GLU A 123     2109   1535   1974   -148     68    123       C  
ATOM    805  O   GLU A 123     -12.602   9.442 -13.798  1.00 14.53           O  
ANISOU  805  O   GLU A 123     2105   1473   1943    -94     80    144       O  
ATOM    806  CB  GLU A 123     -10.491   7.916 -11.710  1.00 15.07           C  
ANISOU  806  CB  GLU A 123     2098   1603   2025   -193     21     61       C  
ATOM    807  CG  GLU A 123     -10.590   6.586 -10.954  1.00 16.81           C  
ANISOU  807  CG  GLU A 123     2276   1855   2258   -168    -15     38       C  
ATOM    808  CD  GLU A 123     -10.421   6.716  -9.434  1.00 21.47           C  
ANISOU  808  CD  GLU A 123     2883   2424   2849   -194    -19     16       C  
ATOM    809  OE1 GLU A 123     -10.460   7.845  -8.898  1.00 23.42           O  
ANISOU  809  OE1 GLU A 123     3182   2624   3091   -228      6     16       O  
ATOM    810  OE2 GLU A 123     -10.249   5.674  -8.765  1.00 23.44           O  
ANISOU  810  OE2 GLU A 123     3099   2703   3102   -180    -46     -1       O  
ATOM    811  N   ASP A 124     -10.424   9.953 -14.204  1.00 15.08           N  
ANISOU  811  N   ASP A 124     2165   1568   1996   -202     92    130       N  
ATOM    812  CA  ASP A 124     -10.680  11.225 -14.905  1.00 16.53           C  
ANISOU  812  CA  ASP A 124     2417   1700   2164   -202    137    168       C  
ATOM    813  C   ASP A 124     -11.634  11.026 -16.078  1.00 16.84           C  
ANISOU  813  C   ASP A 124     2440   1761   2196   -123    139    202       C  
ATOM    814  O   ASP A 124     -12.471  11.876 -16.349  1.00 17.33           O  
ANISOU  814  O   ASP A 124     2560   1777   2247    -80    171    237       O  
ATOM    815  CB  ASP A 124      -9.379  11.853 -15.445  1.00 17.10           C  
ANISOU  815  CB  ASP A 124     2495   1784   2216   -280    158    171       C  
ATOM    816  CG  ASP A 124      -8.524  12.494 -14.355  1.00 18.59           C  
ANISOU  816  CG  ASP A 124     2722   1942   2401   -371    171    142       C  
ATOM    817  OD1 ASP A 124      -9.019  12.699 -13.232  1.00 18.66           O  
ANISOU  817  OD1 ASP A 124     2770   1900   2419   -368    172    125       O  
ATOM    818  OD2 ASP A 124      -7.339  12.795 -14.632  1.00 21.93           O  
ANISOU  818  OD2 ASP A 124     3130   2399   2805   -449    180    134       O  
ATOM    819  N   MET A 125     -11.490   9.905 -16.773  1.00 16.71           N  
ANISOU  819  N   MET A 125     2348   1820   2182   -102    106    192       N  
ATOM    820  CA  MET A 125     -12.290   9.626 -17.957  1.00 17.44           C  
ANISOU  820  CA  MET A 125     2414   1951   2261    -38    104    218       C  
ATOM    821  C   MET A 125     -13.737   9.247 -17.619  1.00 17.04           C  
ANISOU  821  C   MET A 125     2359   1899   2215     26     93    221       C  
ATOM    822  O   MET A 125     -14.655   9.577 -18.368  1.00 17.70           O  
ANISOU  822  O   MET A 125     2449   1997   2280     84    107    253       O  
ATOM    823  CB  MET A 125     -11.632   8.515 -18.784  1.00 17.48           C  
ANISOU  823  CB  MET A 125     2344   2035   2262    -41     73    199       C  
ATOM    824  CG  MET A 125     -12.383   8.163 -20.048  1.00 19.17           C  
ANISOU  824  CG  MET A 125     2527   2299   2458     17     69    218       C  
ATOM    825  SD  MET A 125     -11.459   6.955 -20.993  1.00 22.93           S  
ANISOU  825  SD  MET A 125     2928   2859   2924      9     38    191       S  
ATOM    826  CE  MET A 125     -12.638   6.593 -22.284  1.00 23.96           C  
ANISOU  826  CE  MET A 125     3029   3043   3031     76     33    208       C  
ATOM    827  N   PHE A 126     -13.939   8.587 -16.483  1.00 16.48           N  
ANISOU  827  N   PHE A 126     2277   1820   2166     17     69    190       N  
ATOM    828  CA  PHE A 126     -15.261   8.058 -16.130  1.00 16.42           C  
ANISOU  828  CA  PHE A 126     2253   1825   2160     67     55    189       C  
ATOM    829  C   PHE A 126     -16.012   8.921 -15.090  1.00 16.76           C  
ANISOU  829  C   PHE A 126     2354   1809   2204     86     78    202       C  
ATOM    830  O   PHE A 126     -17.222   8.772 -14.908  1.00 17.01           O  
ANISOU  830  O   PHE A 126     2377   1858   2228    136     76    212       O  
ATOM    831  CB  PHE A 126     -15.166   6.570 -15.714  1.00 15.33           C  
ANISOU  831  CB  PHE A 126     2062   1725   2040     52     14    149       C  
ATOM    832  CG  PHE A 126     -14.981   5.637 -16.891  1.00 15.43           C  
ANISOU  832  CG  PHE A 126     2021   1800   2043     60     -6    140       C  
ATOM    833  CD1 PHE A 126     -16.068   5.010 -17.480  1.00 13.83           C  
ANISOU  833  CD1 PHE A 126     1786   1642   1827     96    -18    140       C  
ATOM    834  CD2 PHE A 126     -13.723   5.458 -17.462  1.00 14.93           C  
ANISOU  834  CD2 PHE A 126     1940   1756   1976     32    -11    130       C  
ATOM    835  CE1 PHE A 126     -15.899   4.175 -18.593  1.00 15.30           C  
ANISOU  835  CE1 PHE A 126     1929   1884   1999    100    -35    126       C  
ATOM    836  CE2 PHE A 126     -13.536   4.634 -18.578  1.00 14.77           C  
ANISOU  836  CE2 PHE A 126     1876   1793   1942     46    -27    120       C  
ATOM    837  CZ  PHE A 126     -14.625   3.993 -19.147  1.00 15.41           C  
ANISOU  837  CZ  PHE A 126     1932   1910   2012     78    -39    116       C  
ATOM    838  N   SER A 127     -15.304   9.844 -14.446  1.00 17.24           N  
ANISOU  838  N   SER A 127     2475   1807   2270     46    103    201       N  
ATOM    839  CA  SER A 127     -15.894  10.659 -13.382  1.00 17.65           C  
ANISOU  839  CA  SER A 127     2590   1795   2320     61    126    206       C  
ATOM    840  C   SER A 127     -17.110  11.510 -13.798  1.00 17.93           C  
ANISOU  840  C   SER A 127     2668   1814   2330    142    160    250       C  
ATOM    841  O   SER A 127     -17.958  11.812 -12.958  1.00 17.74           O  
ANISOU  841  O   SER A 127     2673   1765   2301    180    170    253       O  
ATOM    842  CB  SER A 127     -14.831  11.540 -12.717  1.00 17.88           C  
ANISOU  842  CB  SER A 127     2683   1759   2353     -8    149    192       C  
ATOM    843  OG  SER A 127     -14.351  12.505 -13.611  1.00 20.62           O  
ANISOU  843  OG  SER A 127     3077   2076   2683    -23    185    219       O  
ATOM    844  N   ARG A 128     -17.198  11.877 -15.075  1.00 18.19           N  
ANISOU  844  N   ARG A 128     2701   1869   2342    174    177    284       N  
ATOM    845  CA  ARG A 128     -18.327  12.678 -15.576  1.00 19.23           C  
ANISOU  845  CA  ARG A 128     2869   1998   2439    265    210    332       C  
ATOM    846  C   ARG A 128     -19.683  11.991 -15.392  1.00 18.75           C  
ANISOU  846  C   ARG A 128     2749   2008   2366    330    188    334       C  
ATOM    847  O   ARG A 128     -20.717  12.661 -15.342  1.00 19.16           O  
ANISOU  847  O   ARG A 128     2831   2059   2388    410    215    368       O  
ATOM    848  CB  ARG A 128     -18.140  13.061 -17.057  1.00 20.56           C  
ANISOU  848  CB  ARG A 128     3036   2192   2582    290    229    371       C  
ATOM    849  CG  ARG A 128     -18.154  11.901 -18.065  1.00 22.45           C  
ANISOU  849  CG  ARG A 128     3176   2535   2820    290    190    360       C  
ATOM    850  CD  ARG A 128     -18.007  12.404 -19.532  1.00 26.84           C  
ANISOU  850  CD  ARG A 128     3735   3119   3344    323    213    402       C  
ATOM    851  NE  ARG A 128     -19.270  12.437 -20.267  1.00 28.94           N  
ANISOU  851  NE  ARG A 128     3970   3456   3569    417    217    438       N  
ATOM    852  CZ  ARG A 128     -19.466  11.901 -21.476  1.00 31.30           C  
ANISOU  852  CZ  ARG A 128     4202   3847   3845    442    201    447       C  
ATOM    853  NH1 ARG A 128     -18.480  11.280 -22.125  1.00 30.10           N  
ANISOU  853  NH1 ARG A 128     4011   3721   3706    384    179    423       N  
ATOM    854  NH2 ARG A 128     -20.661  11.997 -22.050  1.00 33.18           N  
ANISOU  854  NH2 ARG A 128     4408   4159   4037    528    206    479       N  
ATOM    855  N   PHE A 129     -19.671  10.665 -15.284  1.00 17.66           N  
ANISOU  855  N   PHE A 129     2530   1932   2248    296    142    298       N  
ATOM    856  CA  PHE A 129     -20.905   9.892 -15.194  1.00 17.63           C  
ANISOU  856  CA  PHE A 129     2463   2005   2230    337    120    296       C  
ATOM    857  C   PHE A 129     -21.446   9.784 -13.783  1.00 17.51           C  
ANISOU  857  C   PHE A 129     2460   1966   2226    338    116    279       C  
ATOM    858  O   PHE A 129     -22.619   9.474 -13.585  1.00 17.75           O  
ANISOU  858  O   PHE A 129     2453   2056   2236    381    110    287       O  
ATOM    859  CB  PHE A 129     -20.740   8.518 -15.871  1.00 16.85           C  
ANISOU  859  CB  PHE A 129     2282   1981   2140    300     79    266       C  
ATOM    860  CG  PHE A 129     -20.361   8.624 -17.315  1.00 17.38           C  
ANISOU  860  CG  PHE A 129     2331   2086   2188    311     83    284       C  
ATOM    861  CD1 PHE A 129     -21.285   9.086 -18.260  1.00 17.91           C  
ANISOU  861  CD1 PHE A 129     2381   2213   2210    383     99    324       C  
ATOM    862  CD2 PHE A 129     -19.075   8.320 -17.730  1.00 17.17           C  
ANISOU  862  CD2 PHE A 129     2301   2040   2181    255     72    265       C  
ATOM    863  CE1 PHE A 129     -20.934   9.211 -19.610  1.00 16.63           C  
ANISOU  863  CE1 PHE A 129     2202   2090   2027    396    104    343       C  
ATOM    864  CE2 PHE A 129     -18.717   8.442 -19.074  1.00 20.47           C  
ANISOU  864  CE2 PHE A 129     2701   2497   2578    266     78    282       C  
ATOM    865  CZ  PHE A 129     -19.649   8.896 -20.017  1.00 18.13           C  
ANISOU  865  CZ  PHE A 129     2392   2257   2241    336     94    322       C  
ATOM    866  N   GLY A 130     -20.614  10.092 -12.795  1.00 17.35           N  
ANISOU  866  N   GLY A 130     2492   1868   2233    289    122    258       N  
ATOM    867  CA  GLY A 130     -21.085  10.086 -11.414  1.00 16.53           C  
ANISOU  867  CA  GLY A 130     2406   1739   2136    292    121    243       C  
ATOM    868  C   GLY A 130     -19.990   9.727 -10.439  1.00 15.73           C  
ANISOU  868  C   GLY A 130     2318   1591   2069    215    104    203       C  
ATOM    869  O   GLY A 130     -18.831   9.593 -10.817  1.00 15.70           O  
ANISOU  869  O   GLY A 130     2312   1572   2079    161     96    188       O  
ATOM    870  N   ARG A 131     -20.368   9.584  -9.178  1.00 15.20           N  
ANISOU  870  N   ARG A 131     2260   1509   2007    214     99    187       N  
ATOM    871  CA  ARG A 131     -19.426   9.254  -8.113  1.00 15.79           C  
ANISOU  871  CA  ARG A 131     2345   1549   2107    149     84    151       C  
ATOM    872  C   ARG A 131     -18.813   7.871  -8.317  1.00 14.72           C  
ANISOU  872  C   ARG A 131     2142   1458   1991    105     44    126       C  
ATOM    873  O   ARG A 131     -19.526   6.893  -8.546  1.00 14.23           O  
ANISOU  873  O   ARG A 131     2028   1449   1929    120     23    126       O  
ATOM    874  CB  ARG A 131     -20.127   9.340  -6.752  1.00 16.01           C  
ANISOU  874  CB  ARG A 131     2391   1563   2131    168     87    143       C  
ATOM    875  CG  ARG A 131     -19.249   8.949  -5.576  1.00 19.11           C  
ANISOU  875  CG  ARG A 131     2787   1931   2542    109     70    107       C  
ATOM    876  CD  ARG A 131     -20.009   9.014  -4.265  1.00 20.24           C  
ANISOU  876  CD  ARG A 131     2946   2067   2678    132     74    101       C  
ATOM    877  NE  ARG A 131     -19.181   8.445  -3.215  1.00 25.80           N  
ANISOU  877  NE  ARG A 131     3640   2765   3396     79     52     68       N  
ATOM    878  CZ  ARG A 131     -19.575   8.217  -1.969  1.00 24.65           C  
ANISOU  878  CZ  ARG A 131     3496   2621   3247     84     47     57       C  
ATOM    879  NH1 ARG A 131     -20.809   8.525  -1.580  1.00 23.08           N  
ANISOU  879  NH1 ARG A 131     3308   2431   3032    139     63     75       N  
ATOM    880  NH2 ARG A 131     -18.710   7.683  -1.115  1.00 25.55           N  
ANISOU  880  NH2 ARG A 131     3599   2739   3371     38     27     30       N  
ATOM    881  N   ILE A 132     -17.486   7.809  -8.256  1.00 13.77           N  
ANISOU  881  N   ILE A 132     2028   1320   1885     49     36    105       N  
ATOM    882  CA  ILE A 132     -16.758   6.564  -8.376  1.00 13.55           C  
ANISOU  882  CA  ILE A 132     1947   1330   1870     17      2     82       C  
ATOM    883  C   ILE A 132     -16.445   6.013  -6.975  1.00 13.41           C  
ANISOU  883  C   ILE A 132     1928   1304   1863     -7    -14     57       C  
ATOM    884  O   ILE A 132     -15.826   6.709  -6.162  1.00 14.23           O  
ANISOU  884  O   ILE A 132     2066   1376   1964    -36     -4     44       O  
ATOM    885  CB  ILE A 132     -15.465   6.762  -9.194  1.00 14.20           C  
ANISOU  885  CB  ILE A 132     2025   1417   1952    -20      3     77       C  
ATOM    886  CG1 ILE A 132     -15.818   7.092 -10.665  1.00 13.48           C  
ANISOU  886  CG1 ILE A 132     1927   1345   1849      9     16    104       C  
ATOM    887  CG2 ILE A 132     -14.557   5.548  -9.066  1.00 13.08           C  
ANISOU  887  CG2 ILE A 132     1838   1313   1820    -45    -28     51       C  
ATOM    888  CD1 ILE A 132     -14.635   7.478 -11.537  1.00 14.39           C  
ANISOU  888  CD1 ILE A 132     2043   1466   1959    -25     24    106       C  
ATOM    889  N   ILE A 133     -16.904   4.792  -6.697  1.00 12.83           N  
ANISOU  889  N   ILE A 133     1818   1259   1796      2    -37     49       N  
ATOM    890  CA  ILE A 133     -16.687   4.129  -5.390  1.00 12.70           C  
ANISOU  890  CA  ILE A 133     1799   1239   1786    -12    -52     31       C  
ATOM    891  C   ILE A 133     -15.265   3.558  -5.273  1.00 12.64           C  
ANISOU  891  C   ILE A 133     1775   1247   1782    -42    -70     11       C  
ATOM    892  O   ILE A 133     -14.583   3.764  -4.278  1.00 12.72           O  
ANISOU  892  O   ILE A 133     1795   1251   1787    -64    -72     -4       O  
ATOM    893  CB  ILE A 133     -17.739   3.005  -5.112  1.00 12.55           C  
ANISOU  893  CB  ILE A 133     1756   1241   1770      5    -65     34       C  
ATOM    894  CG1 ILE A 133     -19.172   3.563  -5.120  1.00 12.68           C  
ANISOU  894  CG1 ILE A 133     1777   1265   1775     37    -48     55       C  
ATOM    895  CG2 ILE A 133     -17.473   2.301  -3.770  1.00 13.99           C  
ANISOU  895  CG2 ILE A 133     1942   1418   1957     -7    -78     21       C  
ATOM    896  CD1 ILE A 133     -19.385   4.801  -4.209  1.00 12.88           C  
ANISOU  896  CD1 ILE A 133     1846   1257   1792     52    -26     61       C  
ATOM    897  N   ASN A 134     -14.841   2.833  -6.299  1.00 12.57           N  
ANISOU  897  N   ASN A 134     1737   1264   1774    -40    -82      9       N  
ATOM    898  CA  ASN A 134     -13.498   2.271  -6.357  1.00 13.21           C  
ANISOU  898  CA  ASN A 134     1797   1372   1850    -55    -97     -7       C  
ATOM    899  C   ASN A 134     -13.146   1.906  -7.799  1.00 12.59           C  
ANISOU  899  C   ASN A 134     1695   1320   1769    -47   -101     -5       C  
ATOM    900  O   ASN A 134     -14.026   1.778  -8.658  1.00 12.54           O  
ANISOU  900  O   ASN A 134     1684   1313   1765    -30    -98      6       O  
ATOM    901  CB  ASN A 134     -13.383   1.025  -5.475  1.00 13.51           C  
ANISOU  901  CB  ASN A 134     1827   1417   1889    -42   -115    -17       C  
ATOM    902  CG  ASN A 134     -14.261  -0.096  -5.957  1.00 15.79           C  
ANISOU  902  CG  ASN A 134     2113   1703   2186    -21   -122    -13       C  
ATOM    903  OD1 ASN A 134     -13.787  -1.035  -6.589  1.00 22.35           O  
ANISOU  903  OD1 ASN A 134     2932   2547   3012     -9   -132    -21       O  
ATOM    904  ND2 ASN A 134     -15.559   0.015  -5.711  1.00 16.25           N  
ANISOU  904  ND2 ASN A 134     2180   1745   2249    -17   -115     -3       N  
ATOM    905  N   SER A 135     -11.856   1.713  -8.042  1.00 12.71           N  
ANISOU  905  N   SER A 135     1688   1368   1773    -58   -109    -15       N  
ATOM    906  CA  SER A 135     -11.358   1.443  -9.376  1.00 13.30           C  
ANISOU  906  CA  SER A 135     1738   1474   1840    -50   -112    -14       C  
ATOM    907  C   SER A 135     -10.018   0.745  -9.311  1.00 13.33           C  
ANISOU  907  C   SER A 135     1713   1524   1826    -45   -126    -29       C  
ATOM    908  O   SER A 135      -9.319   0.811  -8.311  1.00 14.10           O  
ANISOU  908  O   SER A 135     1806   1639   1914    -58   -131    -37       O  
ATOM    909  CB  SER A 135     -11.204   2.749 -10.159  1.00 12.94           C  
ANISOU  909  CB  SER A 135     1700   1426   1789    -75    -91      0       C  
ATOM    910  OG  SER A 135     -10.157   3.528  -9.588  1.00 14.65           O  
ANISOU  910  OG  SER A 135     1919   1653   1994   -117    -84     -7       O  
ATOM    911  N   ARG A 136      -9.653   0.096 -10.408  1.00 14.65           N  
ANISOU  911  N   ARG A 136     1860   1722   1986    -23   -132    -32       N  
ATOM    912  CA  ARG A 136      -8.428  -0.677 -10.464  1.00 15.11           C  
ANISOU  912  CA  ARG A 136     1888   1831   2020     -1   -144    -43       C  
ATOM    913  C   ARG A 136      -7.987  -0.803 -11.916  1.00 15.13           C  
ANISOU  913  C   ARG A 136     1867   1872   2009     11   -142    -43       C  
ATOM    914  O   ARG A 136      -8.805  -1.095 -12.785  1.00 15.68           O  
ANISOU  914  O   ARG A 136     1948   1921   2088     25   -140    -41       O  
ATOM    915  CB  ARG A 136      -8.676  -2.054  -9.837  1.00 15.56           C  
ANISOU  915  CB  ARG A 136     1964   1870   2079     42   -156    -52       C  
ATOM    916  CG  ARG A 136      -7.509  -3.031  -9.912  1.00 18.86           C  
ANISOU  916  CG  ARG A 136     2362   2336   2467     87   -165    -61       C  
ATOM    917  CD  ARG A 136      -6.295  -2.529  -9.177  1.00 24.98           C  
ANISOU  917  CD  ARG A 136     3101   3176   3216     76   -169    -62       C  
ATOM    918  NE  ARG A 136      -6.303  -2.932  -7.773  1.00 29.28           N  
ANISOU  918  NE  ARG A 136     3659   3710   3756     92   -175    -61       N  
ATOM    919  CZ  ARG A 136      -5.220  -3.315  -7.097  1.00 32.38           C  
ANISOU  919  CZ  ARG A 136     4022   4168   4113    122   -183    -64       C  
ATOM    920  NH1 ARG A 136      -5.323  -3.664  -5.826  1.00 32.88           N  
ANISOU  920  NH1 ARG A 136     4101   4222   4171    139   -187    -61       N  
ATOM    921  NH2 ARG A 136      -4.034  -3.373  -7.691  1.00 34.62           N  
ANISOU  921  NH2 ARG A 136     4258   4535   4360    140   -186    -67       N  
ATOM    922  N   VAL A 137      -6.704  -0.563 -12.171  1.00 14.70           N  
ANISOU  922  N   VAL A 137     1776   1883   1928      4   -142    -45       N  
ATOM    923  CA  VAL A 137      -6.107  -0.877 -13.462  1.00 14.49           C  
ANISOU  923  CA  VAL A 137     1720   1906   1881     25   -142    -47       C  
ATOM    924  C   VAL A 137      -5.174  -2.070 -13.264  1.00 13.99           C  
ANISOU  924  C   VAL A 137     1635   1890   1789     81   -155    -60       C  
ATOM    925  O   VAL A 137      -4.248  -2.022 -12.449  1.00 14.22           O  
ANISOU  925  O   VAL A 137     1639   1969   1796     80   -160    -62       O  
ATOM    926  CB  VAL A 137      -5.350   0.326 -14.064  1.00 15.24           C  
ANISOU  926  CB  VAL A 137     1785   2047   1960    -24   -128    -35       C  
ATOM    927  CG1 VAL A 137      -4.685  -0.071 -15.387  1.00 15.15           C  
ANISOU  927  CG1 VAL A 137     1737   2096   1921      4   -128    -35       C  
ATOM    928  CG2 VAL A 137      -6.305   1.470 -14.294  1.00 14.88           C  
ANISOU  928  CG2 VAL A 137     1773   1942   1937    -64   -110    -18       C  
ATOM    929  N   LEU A 138      -5.462  -3.152 -13.979  1.00 13.99           N  
ANISOU  929  N   LEU A 138     1653   1877   1787    131   -160    -69       N  
ATOM    930  CA  LEU A 138      -4.683  -4.380 -13.857  1.00 14.30           C  
ANISOU  930  CA  LEU A 138     1689   1947   1796    200   -167    -81       C  
ATOM    931  C   LEU A 138      -3.328  -4.276 -14.572  1.00 14.72           C  
ANISOU  931  C   LEU A 138     1686   2102   1807    221   -166    -80       C  
ATOM    932  O   LEU A 138      -3.241  -3.778 -15.691  1.00 14.73           O  
ANISOU  932  O   LEU A 138     1665   2130   1803    201   -160    -77       O  
ATOM    933  CB  LEU A 138      -5.468  -5.566 -14.400  1.00 14.27           C  
ANISOU  933  CB  LEU A 138     1736   1885   1801    240   -167    -95       C  
ATOM    934  CG  LEU A 138      -6.909  -5.812 -13.913  1.00 13.96           C  
ANISOU  934  CG  LEU A 138     1749   1756   1798    215   -166    -98       C  
ATOM    935  CD1 LEU A 138      -7.345  -7.204 -14.401  1.00 14.15           C  
ANISOU  935  CD1 LEU A 138     1825   1735   1816    255   -164   -119       C  
ATOM    936  CD2 LEU A 138      -7.012  -5.714 -12.404  1.00 13.85           C  
ANISOU  936  CD2 LEU A 138     1750   1718   1796    205   -168    -89       C  
ATOM    937  N   VAL A 139      -2.290  -4.770 -13.900  1.00 15.29           N  
ANISOU  937  N   VAL A 139     1731   2235   1842    265   -172    -81       N  
ATOM    938  CA  VAL A 139      -0.917  -4.712 -14.379  1.00 16.14           C  
ANISOU  938  CA  VAL A 139     1773   2459   1899    290   -172    -80       C  
ATOM    939  C   VAL A 139      -0.412  -6.125 -14.642  1.00 16.24           C  
ANISOU  939  C   VAL A 139     1801   2494   1876    397   -173    -88       C  
ATOM    940  O   VAL A 139      -0.743  -7.062 -13.910  1.00 15.97           O  
ANISOU  940  O   VAL A 139     1818   2403   1845    449   -175    -91       O  
ATOM    941  CB  VAL A 139      -0.021  -4.049 -13.319  1.00 17.08           C  
ANISOU  941  CB  VAL A 139     1840   2657   1991    256   -176    -74       C  
ATOM    942  CG1 VAL A 139       1.447  -4.135 -13.697  1.00 18.64           C  
ANISOU  942  CG1 VAL A 139     1960   2997   2125    288   -177    -73       C  
ATOM    943  CG2 VAL A 139      -0.448  -2.610 -13.118  1.00 18.81           C  
ANISOU  943  CG2 VAL A 139     2057   2849   2242    149   -170    -69       C  
ATOM    944  N   ASP A 140       0.400  -6.256 -15.684  1.00 16.31           N  
ANISOU  944  N   ASP A 140     1768   2583   1846    431   -170    -91       N  
ATOM    945  CA  ASP A 140       1.098  -7.492 -16.018  1.00 16.87           C  
ANISOU  945  CA  ASP A 140     1845   2694   1870    542   -168    -98       C  
ATOM    946  C   ASP A 140       2.337  -7.531 -15.134  1.00 17.34           C  
ANISOU  946  C   ASP A 140     1844   2870   1876    583   -172    -87       C  
ATOM    947  O   ASP A 140       3.242  -6.714 -15.295  1.00 17.61           O  
ANISOU  947  O   ASP A 140     1794   3021   1877    544   -174    -80       O  
ATOM    948  CB  ASP A 140       1.493  -7.444 -17.504  1.00 17.40           C  
ANISOU  948  CB  ASP A 140     1881   2817   1913    557   -162   -104       C  
ATOM    949  CG  ASP A 140       2.192  -8.696 -17.987  1.00 20.44           C  
ANISOU  949  CG  ASP A 140     2279   3241   2245    678   -156   -115       C  
ATOM    950  OD1 ASP A 140       2.768  -9.454 -17.171  1.00 23.53           O  
ANISOU  950  OD1 ASP A 140     2679   3658   2602    759   -156   -110       O  
ATOM    951  OD2 ASP A 140       2.173  -8.918 -19.223  1.00 25.02           O  
ANISOU  951  OD2 ASP A 140     2864   3830   2814    698   -150   -127       O  
ATOM    952  N   GLN A 141       2.373  -8.487 -14.210  1.00 18.04           N  
ANISOU  952  N   GLN A 141     1974   2930   1950    660   -173    -84       N  
ATOM    953  CA  GLN A 141       3.489  -8.632 -13.266  1.00 19.60           C  
ANISOU  953  CA  GLN A 141     2115   3243   2090    714   -178    -71       C  
ATOM    954  C   GLN A 141       4.817  -9.036 -13.906  1.00 20.57           C  
ANISOU  954  C   GLN A 141     2171   3511   2135    802   -175    -68       C  
ATOM    955  O   GLN A 141       5.865  -8.917 -13.256  1.00 21.19           O  
ANISOU  955  O   GLN A 141     2174   3723   2155    831   -180    -57       O  
ATOM    956  CB  GLN A 141       3.126  -9.590 -12.111  1.00 20.20           C  
ANISOU  956  CB  GLN A 141     2261   3247   2168    784   -176    -64       C  
ATOM    957  CG  GLN A 141       1.993  -9.044 -11.227  1.00 21.10           C  
ANISOU  957  CG  GLN A 141     2417   3253   2345    692   -182    -64       C  
ATOM    958  CD  GLN A 141       1.594  -9.953 -10.056  1.00 23.14           C  
ANISOU  958  CD  GLN A 141     2745   3440   2606    753   -178    -53       C  
ATOM    959  OE1 GLN A 141       0.501  -9.801  -9.498  1.00 25.47           O  
ANISOU  959  OE1 GLN A 141     3093   3629   2953    695   -178    -54       O  
ATOM    960  NE2 GLN A 141       2.466 -10.881  -9.680  1.00 21.38           N  
ANISOU  960  NE2 GLN A 141     2522   3279   2321    872   -173    -40       N  
ATOM    961  N   THR A 142       4.792  -9.487 -15.164  1.00 21.03           N  
ANISOU  961  N   THR A 142     2249   3553   2186    843   -165    -78       N  
ATOM    962  CA  THR A 142       6.047  -9.844 -15.850  1.00 22.88           C  
ANISOU  962  CA  THR A 142     2417   3932   2343    932   -160    -75       C  
ATOM    963  C   THR A 142       6.757  -8.623 -16.398  1.00 22.51           C  
ANISOU  963  C   THR A 142     2260   4018   2276    841   -165    -71       C  
ATOM    964  O   THR A 142       7.979  -8.601 -16.487  1.00 23.58           O  
ANISOU  964  O   THR A 142     2305   4317   2338    885   -165    -62       O  
ATOM    965  CB  THR A 142       5.864 -10.809 -17.041  1.00 22.98           C  
ANISOU  965  CB  THR A 142     2492   3892   2346   1017   -147    -91       C  
ATOM    966  OG1 THR A 142       5.074 -10.169 -18.054  1.00 25.58           O  
ANISOU  966  OG1 THR A 142     2834   4158   2728    922   -147   -104       O  
ATOM    967  CG2 THR A 142       5.232 -12.118 -16.612  1.00 23.99           C  
ANISOU  967  CG2 THR A 142     2743   3886   2486   1108   -136    -98       C  
ATOM    968  N   THR A 143       5.983  -7.606 -16.758  1.00 22.02           N  
ANISOU  968  N   THR A 143     2205   3886   2274    715   -166    -75       N  
ATOM    969  CA  THR A 143       6.514  -6.438 -17.438  1.00 22.24           C  
ANISOU  969  CA  THR A 143     2150   4011   2289    620   -164    -69       C  
ATOM    970  C   THR A 143       6.295  -5.136 -16.665  1.00 21.78           C  
ANISOU  970  C   THR A 143     2068   3943   2263    483   -168    -64       C  
ATOM    971  O   THR A 143       6.880  -4.105 -17.009  1.00 22.38           O  
ANISOU  971  O   THR A 143     2075   4108   2319    394   -163    -58       O  
ATOM    972  CB  THR A 143       5.864  -6.290 -18.820  1.00 22.03           C  
ANISOU  972  CB  THR A 143     2158   3918   2295    596   -155    -75       C  
ATOM    973  OG1 THR A 143       4.448  -6.154 -18.657  1.00 22.56           O  
ANISOU  973  OG1 THR A 143     2312   3821   2439    545   -156    -82       O  
ATOM    974  CG2 THR A 143       6.167  -7.515 -19.708  1.00 23.53           C  
ANISOU  974  CG2 THR A 143     2370   4127   2445    726   -148    -86       C  
ATOM    975  N   GLY A 144       5.434  -5.169 -15.647  1.00 20.59           N  
ANISOU  975  N   GLY A 144     1981   3682   2161    462   -174    -67       N  
ATOM    976  CA  GLY A 144       5.096  -3.968 -14.879  1.00 20.30           C  
ANISOU  976  CA  GLY A 144     1940   3616   2158    338   -175    -65       C  
ATOM    977  C   GLY A 144       4.126  -3.007 -15.566  1.00 20.17           C  
ANISOU  977  C   GLY A 144     1965   3496   2202    242   -165    -64       C  
ATOM    978  O   GLY A 144       3.718  -1.982 -14.968  1.00 20.61           O  
ANISOU  978  O   GLY A 144     2035   3507   2289    144   -162    -62       O  
ATOM    979  N   LEU A 145       3.732  -3.342 -16.793  1.00 19.35           N  
ANISOU  979  N   LEU A 145     1886   3354   2110    276   -159    -63       N  
ATOM    980  CA  LEU A 145       2.873  -2.468 -17.610  1.00 19.13           C  
ANISOU  980  CA  LEU A 145     1891   3248   2129    200   -147    -57       C  
ATOM    981  C   LEU A 145       1.386  -2.782 -17.443  1.00 18.20           C  
ANISOU  981  C   LEU A 145     1862   2980   2074    209   -150    -62       C  
ATOM    982  O   LEU A 145       1.003  -3.941 -17.260  1.00 17.72           O  
ANISOU  982  O   LEU A 145     1843   2871   2018    287   -157    -73       O  
ATOM    983  CB  LEU A 145       3.236  -2.582 -19.098  1.00 19.64           C  
ANISOU  983  CB  LEU A 145     1927   3368   2167    226   -138    -53       C  
ATOM    984  CG  LEU A 145       4.673  -2.413 -19.618  1.00 21.61           C  
ANISOU  984  CG  LEU A 145     2084   3780   2347    231   -133    -47       C  
ATOM    985  CD1 LEU A 145       4.860  -3.208 -20.930  1.00 22.25           C  
ANISOU  985  CD1 LEU A 145     2158   3897   2401    315   -130    -51       C  
ATOM    986  CD2 LEU A 145       5.039  -0.949 -19.820  1.00 22.66           C  
ANISOU  986  CD2 LEU A 145     2177   3958   2475    106   -118    -31       C  
ATOM    987  N   SER A 146       0.562  -1.738 -17.531  1.00 17.50           N  
ANISOU  987  N   SER A 146     1802   2820   2026    128   -140    -52       N  
ATOM    988  CA  SER A 146      -0.890  -1.873 -17.556  1.00 16.91           C  
ANISOU  988  CA  SER A 146     1799   2623   2005    129   -141    -54       C  
ATOM    989  C   SER A 146      -1.315  -2.815 -18.667  1.00 16.64           C  
ANISOU  989  C   SER A 146     1785   2570   1968    193   -143    -64       C  
ATOM    990  O   SER A 146      -0.742  -2.805 -19.763  1.00 15.97           O  
ANISOU  990  O   SER A 146     1665   2550   1853    208   -137    -62       O  
ATOM    991  CB  SER A 146      -1.570  -0.509 -17.744  1.00 16.74           C  
ANISOU  991  CB  SER A 146     1797   2550   2014     45   -125    -36       C  
ATOM    992  OG  SER A 146      -2.940  -0.677 -18.092  1.00 17.03           O  
ANISOU  992  OG  SER A 146     1887   2496   2088     58   -125    -35       O  
ATOM    993  N   ARG A 147      -2.316  -3.640 -18.355  1.00 15.90           N  
ANISOU  993  N   ARG A 147     1750   2390   1903    225   -150    -77       N  
ATOM    994  CA  ARG A 147      -2.929  -4.536 -19.326  1.00 16.07           C  
ANISOU  994  CA  ARG A 147     1804   2378   1925    271   -151    -94       C  
ATOM    995  C   ARG A 147      -4.013  -3.823 -20.133  1.00 14.95           C  
ANISOU  995  C   ARG A 147     1675   2195   1809    224   -144    -85       C  
ATOM    996  O   ARG A 147      -4.602  -4.402 -21.031  1.00 14.87           O  
ANISOU  996  O   ARG A 147     1685   2167   1797    247   -145   -100       O  
ATOM    997  CB  ARG A 147      -3.498  -5.783 -18.616  1.00 16.25           C  
ANISOU  997  CB  ARG A 147     1888   2328   1960    317   -157   -113       C  
ATOM    998  CG  ARG A 147      -2.416  -6.630 -17.912  1.00 18.47           C  
ANISOU  998  CG  ARG A 147     2162   2650   2205    386   -160   -117       C  
ATOM    999  CD  ARG A 147      -2.993  -7.840 -17.183  1.00 22.45           C  
ANISOU  999  CD  ARG A 147     2740   3069   2720    431   -161   -131       C  
ATOM   1000  NE  ARG A 147      -3.967  -8.527 -18.019  1.00 27.17           N  
ANISOU 1000  NE  ARG A 147     3394   3598   3331    434   -157   -153       N  
ATOM   1001  CZ  ARG A 147      -4.859  -9.414 -17.584  1.00 30.66           C  
ANISOU 1001  CZ  ARG A 147     3910   3949   3792    438   -155   -168       C  
ATOM   1002  NH1 ARG A 147      -4.917  -9.749 -16.291  1.00 30.02           N  
ANISOU 1002  NH1 ARG A 147     3859   3827   3720    449   -155   -158       N  
ATOM   1003  NH2 ARG A 147      -5.705  -9.960 -18.456  1.00 30.37           N  
ANISOU 1003  NH2 ARG A 147     3915   3865   3761    426   -151   -193       N  
ATOM   1004  N   GLY A 148      -4.251  -2.553 -19.820  1.00 14.68           N  
ANISOU 1004  N   GLY A 148     1632   2150   1795    160   -136    -62       N  
ATOM   1005  CA  GLY A 148      -5.327  -1.788 -20.447  1.00 14.46           C  
ANISOU 1005  CA  GLY A 148     1620   2084   1788    126   -127    -47       C  
ATOM   1006  C   GLY A 148      -6.698  -2.265 -20.015  1.00 14.14           C  
ANISOU 1006  C   GLY A 148     1627   1967   1779    129   -134    -58       C  
ATOM   1007  O   GLY A 148      -7.693  -1.959 -20.658  1.00 14.03           O  
ANISOU 1007  O   GLY A 148     1623   1934   1773    119   -129    -51       O  
ATOM   1008  N   VAL A 149      -6.736  -3.032 -18.928  1.00 14.06           N  
ANISOU 1008  N   VAL A 149     1641   1920   1779    145   -143    -73       N  
ATOM   1009  CA  VAL A 149      -7.986  -3.570 -18.384  1.00 13.82           C  
ANISOU 1009  CA  VAL A 149     1655   1821   1775    141   -148    -83       C  
ATOM   1010  C   VAL A 149      -8.196  -2.905 -17.028  1.00 13.61           C  
ANISOU 1010  C   VAL A 149     1640   1759   1772    110   -147    -68       C  
ATOM   1011  O   VAL A 149      -7.256  -2.792 -16.229  1.00 13.70           O  
ANISOU 1011  O   VAL A 149     1639   1792   1776    111   -148    -66       O  
ATOM   1012  CB  VAL A 149      -7.924  -5.083 -18.173  1.00 13.98           C  
ANISOU 1012  CB  VAL A 149     1709   1816   1786    185   -157   -111       C  
ATOM   1013  CG1 VAL A 149      -9.169  -5.550 -17.448  1.00 15.05           C  
ANISOU 1013  CG1 VAL A 149     1890   1882   1948    166   -159   -119       C  
ATOM   1014  CG2 VAL A 149      -7.785  -5.831 -19.514  1.00 14.84           C  
ANISOU 1014  CG2 VAL A 149     1818   1952   1869    218   -157   -133       C  
ATOM   1015  N   ALA A 150      -9.413  -2.448 -16.777  1.00 13.38           N  
ANISOU 1015  N   ALA A 150     1631   1686   1766     84   -143    -59       N  
ATOM   1016  CA  ALA A 150      -9.687  -1.731 -15.544  1.00 13.21           C  
ANISOU 1016  CA  ALA A 150     1624   1630   1764     57   -138    -46       C  
ATOM   1017  C   ALA A 150     -11.056  -2.057 -15.027  1.00 13.16           C  
ANISOU 1017  C   ALA A 150     1647   1575   1778     52   -140    -48       C  
ATOM   1018  O   ALA A 150     -11.913  -2.542 -15.779  1.00 13.54           O  
ANISOU 1018  O   ALA A 150     1698   1622   1823     57   -142    -56       O  
ATOM   1019  CB  ALA A 150      -9.523  -0.230 -15.741  1.00 13.24           C  
ANISOU 1019  CB  ALA A 150     1618   1645   1769     23   -122    -21       C  
ATOM   1020  N   PHE A 151     -11.240  -1.823 -13.726  1.00 12.89           N  
ANISOU 1020  N   PHE A 151     1631   1510   1759     38   -140    -43       N  
ATOM   1021  CA  PHE A 151     -12.557  -1.870 -13.108  1.00 12.74           C  
ANISOU 1021  CA  PHE A 151     1634   1452   1756     28   -138    -39       C  
ATOM   1022  C   PHE A 151     -12.901  -0.490 -12.579  1.00 12.67           C  
ANISOU 1022  C   PHE A 151     1629   1429   1755      9   -125    -17       C  
ATOM   1023  O   PHE A 151     -12.026   0.241 -12.100  1.00 12.73           O  
ANISOU 1023  O   PHE A 151     1636   1439   1761     -6   -119    -13       O  
ATOM   1024  CB  PHE A 151     -12.610  -2.895 -11.969  1.00 12.72           C  
ANISOU 1024  CB  PHE A 151     1656   1419   1760     36   -146    -51       C  
ATOM   1025  CG  PHE A 151     -12.530  -4.304 -12.436  1.00 12.89           C  
ANISOU 1025  CG  PHE A 151     1692   1434   1771     56   -153    -72       C  
ATOM   1026  CD1 PHE A 151     -13.691  -4.996 -12.791  1.00 13.40           C  
ANISOU 1026  CD1 PHE A 151     1775   1479   1838     42   -153    -84       C  
ATOM   1027  CD2 PHE A 151     -11.295  -4.931 -12.576  1.00 13.08           C  
ANISOU 1027  CD2 PHE A 151     1715   1476   1778     89   -158    -83       C  
ATOM   1028  CE1 PHE A 151     -13.622  -6.313 -13.227  1.00 14.18           C  
ANISOU 1028  CE1 PHE A 151     1902   1561   1925     53   -155   -108       C  
ATOM   1029  CE2 PHE A 151     -11.214  -6.244 -13.019  1.00 13.91           C  
ANISOU 1029  CE2 PHE A 151     1849   1565   1871    116   -160   -103       C  
ATOM   1030  CZ  PHE A 151     -12.376  -6.933 -13.358  1.00 13.99           C  
ANISOU 1030  CZ  PHE A 151     1889   1542   1886     95   -157   -118       C  
ATOM   1031  N   ILE A 152     -14.181  -0.150 -12.684  1.00 12.62           N  
ANISOU 1031  N   ILE A 152     1630   1412   1754      9   -117     -6       N  
ATOM   1032  CA  ILE A 152     -14.718   1.110 -12.188  1.00 12.86           C  
ANISOU 1032  CA  ILE A 152     1676   1422   1787      4   -100     16       C  
ATOM   1033  C   ILE A 152     -16.109   0.828 -11.644  1.00 12.57           C  
ANISOU 1033  C   ILE A 152     1645   1376   1755     11   -101     20       C  
ATOM   1034  O   ILE A 152     -16.989   0.392 -12.384  1.00 12.63           O  
ANISOU 1034  O   ILE A 152     1636   1412   1753     18   -104     19       O  
ATOM   1035  CB  ILE A 152     -14.811   2.172 -13.306  1.00 13.42           C  
ANISOU 1035  CB  ILE A 152     1744   1509   1847     12    -83     39       C  
ATOM   1036  CG1 ILE A 152     -13.407   2.657 -13.708  1.00 15.92           C  
ANISOU 1036  CG1 ILE A 152     2056   1835   2157     -7    -77     39       C  
ATOM   1037  CG2 ILE A 152     -15.681   3.370 -12.864  1.00 13.74           C  
ANISOU 1037  CG2 ILE A 152     1813   1522   1886     23    -60     65       C  
ATOM   1038  N  AARG A 153     -16.296   1.069 -10.349  0.50 12.51           N  
ANISOU 1038  N  AARG A 153     1657   1339   1756      5    -97     22       N  
ATOM   1039  N  BARG A 153     -16.294   1.057 -10.346  0.50 12.50           N  
ANISOU 1039  N  BARG A 153     1657   1338   1756      5    -98     21       N  
ATOM   1040  CA AARG A 153     -17.618   0.955  -9.735  0.50 12.53           C  
ANISOU 1040  CA AARG A 153     1662   1339   1757     12    -94     29       C  
ATOM   1041  CA BARG A 153     -17.622   0.956  -9.738  0.50 12.51           C  
ANISOU 1041  CA BARG A 153     1660   1337   1755     12    -94     29       C  
ATOM   1042  C  AARG A 153     -18.191   2.333  -9.447  0.50 12.62           C  
ANISOU 1042  C  AARG A 153     1693   1340   1763     30    -72     52       C  
ATOM   1043  C  BARG A 153     -18.185   2.338  -9.461  0.50 12.62           C  
ANISOU 1043  C  BARG A 153     1693   1340   1763     30    -72     52       C  
ATOM   1044  O  AARG A 153     -17.528   3.180  -8.832  0.50 12.90           O  
ANISOU 1044  O  AARG A 153     1756   1341   1803     23    -61     54       O  
ATOM   1045  O  BARG A 153     -17.512   3.194  -8.868  0.50 12.84           O  
ANISOU 1045  O  BARG A 153     1749   1334   1795     23    -61     54       O  
ATOM   1046  CB AARG A 153     -17.573   0.128  -8.446  0.50 12.58           C  
ANISOU 1046  CB AARG A 153     1681   1324   1774     -1   -104     16       C  
ATOM   1047  CB BARG A 153     -17.600   0.131  -8.444  0.50 12.47           C  
ANISOU 1047  CB BARG A 153     1667   1310   1760     -1   -104     16       C  
ATOM   1048  CG AARG A 153     -18.924   0.104  -7.731  0.50 13.02           C  
ANISOU 1048  CG AARG A 153     1738   1384   1826      2    -98     25       C  
ATOM   1049  CG BARG A 153     -18.937   0.211  -7.695  0.50 12.60           C  
ANISOU 1049  CG BARG A 153     1685   1329   1772      3    -97     27       C  
ATOM   1050  CD AARG A 153     -18.855  -0.586  -6.392  0.50 12.49           C  
ANISOU 1050  CD AARG A 153     1686   1292   1766    -10   -104     18       C  
ATOM   1051  CD BARG A 153     -18.991  -0.686  -6.481  0.50 12.41           C  
ANISOU 1051  CD BARG A 153     1673   1286   1755    -11   -105     17       C  
ATOM   1052  NE AARG A 153     -18.675  -2.025  -6.537  0.50 12.68           N  
ANISOU 1052  NE AARG A 153     1713   1313   1793    -26   -117      2       N  
ATOM   1053  NE BARG A 153     -19.112  -2.093  -6.846  0.50 12.47           N  
ANISOU 1053  NE BARG A 153     1678   1297   1762    -29   -116      3       N  
ATOM   1054  CZ AARG A 153     -19.645  -2.867  -6.882  0.50 12.56           C  
ANISOU 1054  CZ AARG A 153     1690   1313   1770    -44   -118     -3       C  
ATOM   1055  CZ BARG A 153     -18.118  -2.973  -6.753  0.50 12.46           C  
ANISOU 1055  CZ BARG A 153     1694   1273   1766    -30   -125    -12       C  
ATOM   1056  NH1BARG A 153     -16.931  -2.595  -6.297  0.50 12.38           N  
ANISOU 1056  NH1BARG A 153     1691   1253   1760    -17   -128    -13       N  
ATOM   1057  NH2AARG A 153     -19.393  -4.163  -6.976  0.50 12.67           N  
ANISOU 1057  NH2AARG A 153     1723   1307   1785    -61   -124    -20       N  
ATOM   1058  NH2BARG A 153     -18.320  -4.234  -7.105  0.50 12.61           N  
ANISOU 1058  NH2BARG A 153     1724   1284   1781    -44   -129    -26       N  
ATOM   1059  N   PHE A 154     -19.418   2.557  -9.902  1.00 12.77           N  
ANISOU 1059  N   PHE A 154     1696   1389   1765     55    -64     69       N  
ATOM   1060  CA  PHE A 154     -20.105   3.813  -9.685  1.00 12.98           C  
ANISOU 1060  CA  PHE A 154     1744   1408   1778     89    -39     95       C  
ATOM   1061  C   PHE A 154     -21.019   3.677  -8.472  1.00 12.99           C  
ANISOU 1061  C   PHE A 154     1748   1409   1777     97    -38     97       C  
ATOM   1062  O   PHE A 154     -21.362   2.567  -8.053  1.00 12.88           O  
ANISOU 1062  O   PHE A 154     1711   1413   1768     74    -55     82       O  
ATOM   1063  CB  PHE A 154     -20.932   4.207 -10.920  1.00 13.23           C  
ANISOU 1063  CB  PHE A 154     1752   1490   1783    127    -29    119       C  
ATOM   1064  CG  PHE A 154     -20.122   4.820 -12.034  1.00 13.32           C  
ANISOU 1064  CG  PHE A 154     1775   1495   1792    133    -19    130       C  
ATOM   1065  CD1 PHE A 154     -19.753   6.169 -11.989  1.00 14.24           C  
ANISOU 1065  CD1 PHE A 154     1942   1565   1903    151     10    153       C  
ATOM   1066  CD2 PHE A 154     -19.753   4.070 -13.134  1.00 13.26           C  
ANISOU 1066  CD2 PHE A 154     1732   1525   1781    118    -36    118       C  
ATOM   1067  CE1 PHE A 154     -19.007   6.748 -13.031  1.00 13.99           C  
ANISOU 1067  CE1 PHE A 154     1923   1527   1866    150     23    166       C  
ATOM   1068  CE2 PHE A 154     -19.022   4.639 -14.177  1.00 13.47           C  
ANISOU 1068  CE2 PHE A 154     1764   1552   1800    124    -25    131       C  
ATOM   1069  CZ  PHE A 154     -18.645   5.981 -14.125  1.00 13.61           C  
ANISOU 1069  CZ  PHE A 154     1830   1525   1814    138      4    157       C  
ATOM   1070  N   ASP A 155     -21.409   4.820  -7.920  1.00 13.19           N  
ANISOU 1070  N   ASP A 155     1807   1412   1792    130    -14    115       N  
ATOM   1071  CA  ASP A 155     -22.339   4.864  -6.792  1.00 13.27           C  
ANISOU 1071  CA  ASP A 155     1821   1429   1793    148     -8    120       C  
ATOM   1072  C   ASP A 155     -23.668   4.180  -7.149  1.00 13.41           C  
ANISOU 1072  C   ASP A 155     1783   1524   1788    162    -15    129       C  
ATOM   1073  O   ASP A 155     -24.220   3.397  -6.355  1.00 13.36           O  
ANISOU 1073  O   ASP A 155     1757   1539   1782    141    -25    120       O  
ATOM   1074  CB  ASP A 155     -22.558   6.322  -6.383  1.00 13.58           C  
ANISOU 1074  CB  ASP A 155     1913   1430   1817    193     24    139       C  
ATOM   1075  CG  ASP A 155     -23.514   6.489  -5.202  1.00 13.73           C  
ANISOU 1075  CG  ASP A 155     1937   1459   1821    222     34    145       C  
ATOM   1076  OD1 ASP A 155     -23.612   5.593  -4.329  1.00 13.53           O  
ANISOU 1076  OD1 ASP A 155     1890   1445   1806    191     16    128       O  
ATOM   1077  OD2 ASP A 155     -24.146   7.565  -5.138  1.00 14.11           O  
ANISOU 1077  OD2 ASP A 155     2018   1500   1844    281     63    168       O  
ATOM   1078  N   LYS A 156     -24.144   4.436  -8.361  1.00 13.62           N  
ANISOU 1078  N   LYS A 156     1784   1599   1792    191    -10    146       N  
ATOM   1079  CA  LYS A 156     -25.459   3.974  -8.804  1.00 13.88           C  
ANISOU 1079  CA  LYS A 156     1758   1726   1792    205    -14    155       C  
ATOM   1080  C   LYS A 156     -25.350   3.270 -10.132  1.00 13.89           C  
ANISOU 1080  C   LYS A 156     1719   1772   1786    180    -30    145       C  
ATOM   1081  O   LYS A 156     -24.544   3.663 -10.971  1.00 13.82           O  
ANISOU 1081  O   LYS A 156     1728   1738   1785    188    -27    148       O  
ATOM   1082  CB  LYS A 156     -26.411   5.161  -8.947  1.00 14.37           C  
ANISOU 1082  CB  LYS A 156     1822   1827   1813    286     14    193       C  
ATOM   1083  CG  LYS A 156     -26.641   5.938  -7.649  1.00 17.23           C  
ANISOU 1083  CG  LYS A 156     2228   2145   2173    321     35    203       C  
ATOM   1084  CD  LYS A 156     -27.680   7.046  -7.823  1.00 20.95           C  
ANISOU 1084  CD  LYS A 156     2704   2661   2597    416     66    242       C  
ATOM   1085  CE  LYS A 156     -27.158   8.191  -8.704  1.00 25.25           C  
ANISOU 1085  CE  LYS A 156     3301   3158   3133    465     92    267       C  
ATOM   1086  NZ  LYS A 156     -27.730   9.507  -8.254  1.00 27.88           N  
ANISOU 1086  NZ  LYS A 156     3692   3468   3433    557    132    299       N  
ATOM   1087  N   ARG A 157     -26.179   2.249 -10.357  1.00 14.03           N  
ANISOU 1087  N   ARG A 157     1684   1861   1785    147    -45    131       N  
ATOM   1088  CA  ARG A 157     -26.101   1.504 -11.627  1.00 14.09           C  
ANISOU 1088  CA  ARG A 157     1657   1915   1783    116    -61    113       C  
ATOM   1089  C   ARG A 157     -26.422   2.378 -12.849  1.00 14.40           C  
ANISOU 1089  C   ARG A 157     1672   2013   1787    174    -49    140       C  
ATOM   1090  O   ARG A 157     -25.831   2.179 -13.901  1.00 14.36           O  
ANISOU 1090  O   ARG A 157     1661   2011   1783    164    -57    131       O  
ATOM   1091  CB  ARG A 157     -26.956   0.224 -11.585  1.00 14.30           C  
ANISOU 1091  CB  ARG A 157     1639   2003   1791     55    -77     87       C  
ATOM   1092  CG  ARG A 157     -27.063  -0.548 -12.920  1.00 14.51           C  
ANISOU 1092  CG  ARG A 157     1628   2087   1797     19    -91     64       C  
ATOM   1093  CD  ARG A 157     -27.949  -1.788 -12.760  1.00 14.82           C  
ANISOU 1093  CD  ARG A 157     1634   2182   1816    -56   -102     34       C  
ATOM   1094  NE  ARG A 157     -28.232  -2.477 -14.021  1.00 15.16           N  
ANISOU 1094  NE  ARG A 157     1639   2292   1827    -95   -114      7       N  
ATOM   1095  CZ  ARG A 157     -27.478  -3.441 -14.553  1.00 15.07           C  
ANISOU 1095  CZ  ARG A 157     1658   2233   1834   -144   -126    -30       C  
ATOM   1096  NH1 ARG A 157     -26.344  -3.832 -13.971  1.00 14.66           N  
ANISOU 1096  NH1 ARG A 157     1671   2069   1830   -152   -127    -41       N  
ATOM   1097  NH2 ARG A 157     -27.853  -4.016 -15.679  1.00 15.46           N  
ANISOU 1097  NH2 ARG A 157     1672   2352   1849   -181   -135    -58       N  
ATOM   1098  N   SER A 158     -27.342   3.343 -12.710  1.00 14.76           N  
ANISOU 1098  N   SER A 158     1705   2107   1796    242    -29    176       N  
ATOM   1099  CA  SER A 158     -27.676   4.260 -13.819  1.00 15.14           C  
ANISOU 1099  CA  SER A 158     1738   2212   1805    313    -12    211       C  
ATOM   1100  C   SER A 158     -26.456   5.009 -14.365  1.00 14.96           C  
ANISOU 1100  C   SER A 158     1772   2104   1807    332      0    222       C  
ATOM   1101  O   SER A 158     -26.381   5.285 -15.566  1.00 15.17           O  
ANISOU 1101  O   SER A 158     1783   2171   1810    359      4    237       O  
ATOM   1102  CB  SER A 158     -28.738   5.293 -13.414  1.00 15.62           C  
ANISOU 1102  CB  SER A 158     1793   2319   1821    401     14    253       C  
ATOM   1103  OG  SER A 158     -28.232   6.136 -12.385  1.00 15.46           O  
ANISOU 1103  OG  SER A 158     1850   2195   1829    428     36    265       O  
ATOM   1104  N   GLU A 159     -25.531   5.352 -13.469  1.00 14.63           N  
ANISOU 1104  N   GLU A 159     1796   1956   1807    314      7    216       N  
ATOM   1105  CA  GLU A 159     -24.263   5.999 -13.829  1.00 14.48           C  
ANISOU 1105  CA  GLU A 159     1833   1857   1814    311     19    221       C  
ATOM   1106  C   GLU A 159     -23.354   5.112 -14.693  1.00 14.22           C  
ANISOU 1106  C   GLU A 159     1777   1828   1799    257     -5    192       C  
ATOM   1107  O   GLU A 159     -22.772   5.573 -15.689  1.00 14.32           O  
ANISOU 1107  O   GLU A 159     1799   1838   1805    271      4    207       O  
ATOM   1108  CB  GLU A 159     -23.539   6.448 -12.559  1.00 14.27           C  
ANISOU 1108  CB  GLU A 159     1869   1731   1821    291     29    212       C  
ATOM   1109  CG  GLU A 159     -24.346   7.496 -11.772  1.00 14.61           C  
ANISOU 1109  CG  GLU A 159     1950   1759   1842    353     59    241       C  
ATOM   1110  CD  GLU A 159     -23.849   7.718 -10.353  1.00 16.69           C  
ANISOU 1110  CD  GLU A 159     2265   1942   2134    326     63    223       C  
ATOM   1111  OE1 GLU A 159     -23.082   6.889  -9.803  1.00 15.94           O  
ANISOU 1111  OE1 GLU A 159     2164   1821   2073    261     39    189       O  
ATOM   1112  OE2 GLU A 159     -24.243   8.738  -9.772  1.00 20.10           O  
ANISOU 1112  OE2 GLU A 159     2748   2340   2550    376     93    243       O  
ATOM   1113  N   ALA A 160     -23.213   3.856 -14.279  1.00 13.93           N  
ANISOU 1113  N   ALA A 160     1718   1794   1783    199    -32    154       N  
ATOM   1114  CA  ALA A 160     -22.484   2.848 -15.046  1.00 13.76           C  
ANISOU 1114  CA  ALA A 160     1676   1780   1772    155    -54    123       C  
ATOM   1115  C   ALA A 160     -23.111   2.605 -16.418  1.00 14.07           C  
ANISOU 1115  C   ALA A 160     1664   1908   1773    169    -60    126       C  
ATOM   1116  O   ALA A 160     -22.399   2.463 -17.399  1.00 14.05           O  
ANISOU 1116  O   ALA A 160     1658   1912   1770    164    -65    119       O  
ATOM   1117  CB  ALA A 160     -22.410   1.528 -14.253  1.00 13.53           C  
ANISOU 1117  CB  ALA A 160     1644   1732   1766     99    -76     85       C  
ATOM   1118  N   GLU A 161     -24.442   2.554 -16.479  1.00 14.40           N  
ANISOU 1118  N   GLU A 161     1663   2030   1777    188    -59    135       N  
ATOM   1119  CA  GLU A 161     -25.164   2.416 -17.755  1.00 14.80           C  
ANISOU 1119  CA  GLU A 161     1656   2186   1780    205    -64    139       C  
ATOM   1120  C   GLU A 161     -24.879   3.559 -18.718  1.00 15.01           C  
ANISOU 1120  C   GLU A 161     1693   2224   1786    271    -43    180       C  
ATOM   1121  O   GLU A 161     -24.709   3.330 -19.921  1.00 15.16           O  
ANISOU 1121  O   GLU A 161     1684   2295   1783    272    -51    175       O  
ATOM   1122  CB  GLU A 161     -26.677   2.280 -17.523  1.00 15.21           C  
ANISOU 1122  CB  GLU A 161     1653   2337   1788    216    -65    146       C  
ATOM   1123  CG  GLU A 161     -27.042   1.040 -16.714  1.00 15.60           C  
ANISOU 1123  CG  GLU A 161     1690   2386   1852    138    -83    105       C  
ATOM   1124  CD  GLU A 161     -28.536   0.898 -16.423  1.00 19.86           C  
ANISOU 1124  CD  GLU A 161     2168   3034   2344    138    -83    112       C  
ATOM   1125  OE1 GLU A 161     -29.005  -0.265 -16.423  1.00 20.16           O  
ANISOU 1125  OE1 GLU A 161     2175   3114   2370     61   -100     73       O  
ATOM   1126  OE2 GLU A 161     -29.232   1.923 -16.196  1.00 19.19           O  
ANISOU 1126  OE2 GLU A 161     2069   2994   2229    212    -64    154       O  
ATOM   1127  N   GLU A 162     -24.834   4.788 -18.184  1.00 15.08           N  
ANISOU 1127  N   GLU A 162     1749   2182   1798    326    -15    221       N  
ATOM   1128  CA  GLU A 162     -24.508   5.960 -18.990  1.00 15.53           C  
ANISOU 1128  CA  GLU A 162     1836   2229   1837    387     13    265       C  
ATOM   1129  C   GLU A 162     -23.087   5.850 -19.564  1.00 15.08           C  
ANISOU 1129  C   GLU A 162     1806   2114   1810    348      9    251       C  
ATOM   1130  O   GLU A 162     -22.845   6.212 -20.721  1.00 15.74           O  
ANISOU 1130  O   GLU A 162     1881   2230   1869    375     18    271       O  
ATOM   1131  CB  GLU A 162     -24.685   7.266 -18.180  1.00 15.98           C  
ANISOU 1131  CB  GLU A 162     1958   2221   1892    446     49    305       C  
ATOM   1132  CG  GLU A 162     -26.150   7.585 -17.745  1.00 18.06           C  
ANISOU 1132  CG  GLU A 162     2193   2557   2112    511     60    330       C  
ATOM   1133  CD  GLU A 162     -27.033   8.174 -18.840  1.00 22.73           C  
ANISOU 1133  CD  GLU A 162     2748   3252   2637    599     77    375       C  
ATOM   1134  OE1 GLU A 162     -28.191   8.553 -18.533  1.00 24.18           O  
ANISOU 1134  OE1 GLU A 162     2908   3504   2776    667     90    402       O  
ATOM   1135  OE2 GLU A 162     -26.593   8.263 -20.003  1.00 24.71           O  
ANISOU 1135  OE2 GLU A 162     2990   3524   2874    607     78    386       O  
ATOM   1136  N   ALA A 163     -22.163   5.330 -18.763  1.00 14.63           N  
ANISOU 1136  N   ALA A 163     1777   1983   1800    287     -4    217       N  
ATOM   1137  CA  ALA A 163     -20.772   5.132 -19.205  1.00 14.41           C  
ANISOU 1137  CA  ALA A 163     1765   1913   1797    249    -10    201       C  
ATOM   1138  C   ALA A 163     -20.687   4.141 -20.352  1.00 14.43           C  
ANISOU 1138  C   ALA A 163     1716   1985   1782    231    -34    175       C  
ATOM   1139  O   ALA A 163     -19.988   4.385 -21.336  1.00 14.53           O  
ANISOU 1139  O   ALA A 163     1728   2009   1786    238    -28    184       O  
ATOM   1140  CB  ALA A 163     -19.889   4.660 -18.030  1.00 14.00           C  
ANISOU 1140  CB  ALA A 163     1743   1786   1790    195    -22    169       C  
ATOM   1141  N   ILE A 164     -21.405   3.027 -20.219  1.00 14.40           N  
ANISOU 1141  N   ILE A 164     1673   2025   1771    204    -58    140       N  
ATOM   1142  CA  ILE A 164     -21.438   1.983 -21.261  1.00 15.10           C  
ANISOU 1142  CA  ILE A 164     1720   2179   1841    180    -79    107       C  
ATOM   1143  C   ILE A 164     -21.889   2.598 -22.574  1.00 16.70           C  
ANISOU 1143  C   ILE A 164     1887   2464   1995    228    -69    137       C  
ATOM   1144  O   ILE A 164     -21.164   2.562 -23.565  1.00 17.09           O  
ANISOU 1144  O   ILE A 164     1930   2527   2035    231    -70    134       O  
ATOM   1145  CB  ILE A 164     -22.356   0.802 -20.848  1.00 14.79           C  
ANISOU 1145  CB  ILE A 164     1651   2174   1793    136   -100     67       C  
ATOM   1146  CG1 ILE A 164     -21.731   0.043 -19.673  1.00 14.18           C  
ANISOU 1146  CG1 ILE A 164     1614   2011   1762     91   -110     38       C  
ATOM   1147  CG2 ILE A 164     -22.636  -0.176 -22.039  1.00 15.59           C  
ANISOU 1147  CG2 ILE A 164     1710   2353   1860    110   -118     31       C  
ATOM   1148  CD1 ILE A 164     -22.700  -0.942 -18.990  1.00 14.28           C  
ANISOU 1148  CD1 ILE A 164     1613   2041   1770     46   -122      9       C  
ATOM   1149  N   THR A 165     -23.075   3.205 -22.572  1.00 17.91           N  
ANISOU 1149  N   THR A 165     2017   2677   2112    274    -57    168       N  
ATOM   1150  CA  THR A 165     -23.613   3.762 -23.803  1.00 19.38           C  
ANISOU 1150  CA  THR A 165     2165   2956   2243    330    -47    201       C  
ATOM   1151  C   THR A 165     -22.687   4.824 -24.425  1.00 19.21           C  
ANISOU 1151  C   THR A 165     2185   2891   2224    371    -21    243       C  
ATOM   1152  O   THR A 165     -22.553   4.890 -25.652  1.00 19.43           O  
ANISOU 1152  O   THR A 165     2185   2980   2217    393    -20    254       O  
ATOM   1153  CB  THR A 165     -25.067   4.245 -23.607  1.00 19.85           C  
ANISOU 1153  CB  THR A 165     2188   3099   2256    384    -37    231       C  
ATOM   1154  OG1 THR A 165     -25.883   3.097 -23.340  1.00 22.76           O  
ANISOU 1154  OG1 THR A 165     2504   3532   2612    328    -64    186       O  
ATOM   1155  CG2 THR A 165     -25.604   4.909 -24.850  1.00 20.74           C  
ANISOU 1155  CG2 THR A 165     2263   3314   2305    457    -23    273       C  
ATOM   1156  N   SER A 166     -22.031   5.630 -23.590  1.00 19.13           N  
ANISOU 1156  N   SER A 166     2242   2778   2251    375      2    266       N  
ATOM   1157  CA  SER A 166     -21.105   6.651 -24.099  1.00 19.95           C  
ANISOU 1157  CA  SER A 166     2393   2831   2356    397     31    304       C  
ATOM   1158  C   SER A 166     -19.811   6.094 -24.662  1.00 19.48           C  
ANISOU 1158  C   SER A 166     2329   2755   2317    346     17    276       C  
ATOM   1159  O   SER A 166     -19.337   6.580 -25.686  1.00 20.33           O  
ANISOU 1159  O   SER A 166     2438   2884   2403    367     32    303       O  
ATOM   1160  CB  SER A 166     -20.776   7.689 -23.031  1.00 19.94           C  
ANISOU 1160  CB  SER A 166     2470   2724   2383    403     61    331       C  
ATOM   1161  OG  SER A 166     -21.957   8.318 -22.565  1.00 23.55           O  
ANISOU 1161  OG  SER A 166     2937   3197   2815    465     79    363       O  
ATOM   1162  N   PHE A 167     -19.249   5.078 -24.006  1.00 19.10           N  
ANISOU 1162  N   PHE A 167     2277   2674   2307    286     -9    225       N  
ATOM   1163  CA  PHE A 167     -17.878   4.633 -24.291  1.00 18.88           C  
ANISOU 1163  CA  PHE A 167     2253   2621   2299    244    -18    200       C  
ATOM   1164  C   PHE A 167     -17.690   3.285 -24.990  1.00 18.13           C  
ANISOU 1164  C   PHE A 167     2112   2580   2195    221    -49    152       C  
ATOM   1165  O   PHE A 167     -16.702   3.102 -25.688  1.00 18.30           O  
ANISOU 1165  O   PHE A 167     2128   2613   2213    212    -51    144       O  
ATOM   1166  CB  PHE A 167     -17.035   4.644 -23.005  1.00 18.69           C  
ANISOU 1166  CB  PHE A 167     2270   2511   2322    202    -19    185       C  
ATOM   1167  CG  PHE A 167     -16.624   6.024 -22.557  1.00 21.44           C  
ANISOU 1167  CG  PHE A 167     2675   2794   2678    206     16    225       C  
ATOM   1168  CD1 PHE A 167     -16.385   7.027 -23.479  1.00 25.03           C  
ANISOU 1168  CD1 PHE A 167     3147   3255   3107    232     46    269       C  
ATOM   1169  CD2 PHE A 167     -16.441   6.303 -21.212  1.00 24.02           C  
ANISOU 1169  CD2 PHE A 167     3041   3049   3035    180     21    218       C  
ATOM   1170  CE1 PHE A 167     -15.990   8.296 -23.069  1.00 26.47           C  
ANISOU 1170  CE1 PHE A 167     3396   3367   3295    227     83    305       C  
ATOM   1171  CE2 PHE A 167     -16.048   7.566 -20.797  1.00 25.05           C  
ANISOU 1171  CE2 PHE A 167     3233   3115   3170    175     55    249       C  
ATOM   1172  CZ  PHE A 167     -15.826   8.562 -21.734  1.00 24.85           C  
ANISOU 1172  CZ  PHE A 167     3234   3090   3120    196     87    292       C  
ATOM   1173  N   ASN A 168     -18.605   2.343 -24.791  1.00 17.64           N  
ANISOU 1173  N   ASN A 168     2024   2553   2127    208    -71    118       N  
ATOM   1174  CA  ASN A 168     -18.432   0.994 -25.338  1.00 17.90           C  
ANISOU 1174  CA  ASN A 168     2031   2619   2151    178    -97     64       C  
ATOM   1175  C   ASN A 168     -18.344   1.037 -26.858  1.00 18.25           C  
ANISOU 1175  C   ASN A 168     2040   2743   2152    202    -96     68       C  
ATOM   1176  O   ASN A 168     -19.206   1.640 -27.511  1.00 18.05           O  
ANISOU 1176  O   ASN A 168     1985   2785   2087    238    -87     99       O  
ATOM   1177  CB  ASN A 168     -19.582   0.074 -24.907  1.00 18.13           C  
ANISOU 1177  CB  ASN A 168     2042   2674   2172    150   -115     29       C  
ATOM   1178  CG  ASN A 168     -19.409  -1.348 -25.410  1.00 18.67           C  
ANISOU 1178  CG  ASN A 168     2103   2760   2231    111   -137    -31       C  
ATOM   1179  OD1 ASN A 168     -18.394  -2.009 -25.138  1.00 16.14           O  
ANISOU 1179  OD1 ASN A 168     1814   2383   1936     94   -143    -58       O  
ATOM   1180  ND2 ASN A 168     -20.404  -1.830 -26.142  1.00 17.45           N  
ANISOU 1180  ND2 ASN A 168     1907   2688   2033     98   -147    -53       N  
ATOM   1181  N   GLY A 169     -17.288   0.425 -27.399  1.00 17.69           N  
ANISOU 1181  N   GLY A 169     1969   2668   2082    189   -105     41       N  
ATOM   1182  CA  GLY A 169     -17.069   0.353 -28.850  1.00 18.36           C  
ANISOU 1182  CA  GLY A 169     2021   2829   2125    210   -106     39       C  
ATOM   1183  C   GLY A 169     -16.414   1.607 -29.405  1.00 18.71           C  
ANISOU 1183  C   GLY A 169     2070   2878   2160    245    -79     96       C  
ATOM   1184  O   GLY A 169     -16.211   1.725 -30.608  1.00 18.78           O  
ANISOU 1184  O   GLY A 169     2053   2952   2132    268    -75    106       O  
ATOM   1185  N   HIS A 170     -16.093   2.552 -28.523  1.00 18.82           N  
ANISOU 1185  N   HIS A 170     2123   2823   2206    244    -59    134       N  
ATOM   1186  CA  HIS A 170     -15.543   3.840 -28.936  1.00 19.35           C  
ANISOU 1186  CA  HIS A 170     2209   2879   2263    265    -27    191       C  
ATOM   1187  C   HIS A 170     -14.060   3.959 -28.645  1.00 19.18           C  
ANISOU 1187  C   HIS A 170     2209   2812   2268    231    -20    188       C  
ATOM   1188  O   HIS A 170     -13.552   3.353 -27.705  1.00 18.79           O  
ANISOU 1188  O   HIS A 170     2172   2718   2252    198    -34    154       O  
ATOM   1189  CB  HIS A 170     -16.304   4.993 -28.282  1.00 19.87           C  
ANISOU 1189  CB  HIS A 170     2312   2904   2334    291     -1    240       C  
ATOM   1190  CG  HIS A 170     -17.689   5.177 -28.822  1.00 22.99           C  
ANISOU 1190  CG  HIS A 170     2678   3370   2686    342      1    260       C  
ATOM   1191  ND1 HIS A 170     -18.800   5.273 -28.014  1.00 26.08           N  
ANISOU 1191  ND1 HIS A 170     3073   3757   3081    357     -1    264       N  
ATOM   1192  CD2 HIS A 170     -18.145   5.261 -30.095  1.00 26.93           C  
ANISOU 1192  CD2 HIS A 170     3136   3962   3133    384      3    278       C  
ATOM   1193  CE1 HIS A 170     -19.880   5.417 -28.760  1.00 26.75           C  
ANISOU 1193  CE1 HIS A 170     3117   3932   3114    407      1    284       C  
ATOM   1194  NE2 HIS A 170     -19.511   5.415 -30.028  1.00 28.70           N  
ANISOU 1194  NE2 HIS A 170     3338   4241   3327    425      3    293       N  
ATOM   1195  N   LYS A 171     -13.370   4.744 -29.463  1.00 19.52           N  
ANISOU 1195  N   LYS A 171     2253   2874   2289    239      4    225       N  
ATOM   1196  CA  LYS A 171     -11.949   4.996 -29.275  1.00 19.96           C  
ANISOU 1196  CA  LYS A 171     2322   2904   2359    201     15    228       C  
ATOM   1197  C   LYS A 171     -11.783   6.228 -28.399  1.00 20.55           C  
ANISOU 1197  C   LYS A 171     2452   2900   2454    176     46    267       C  
ATOM   1198  O   LYS A 171     -12.378   7.266 -28.690  1.00 20.79           O  
ANISOU 1198  O   LYS A 171     2515   2914   2469    203     76    316       O  
ATOM   1199  CB  LYS A 171     -11.274   5.275 -30.622  1.00 20.07           C  
ANISOU 1199  CB  LYS A 171     2310   2983   2334    213     30    251       C  
ATOM   1200  CG  LYS A 171     -11.339   4.152 -31.658  1.00 21.16           C  
ANISOU 1200  CG  LYS A 171     2395   3204   2441    240      3    213       C  
ATOM   1201  CD  LYS A 171     -10.630   4.596 -32.946  1.00 22.65           C  
ANISOU 1201  CD  LYS A 171     2560   3456   2589    253     22    244       C  
ATOM   1202  CE  LYS A 171     -11.147   3.872 -34.177  1.00 25.81           C  
ANISOU 1202  CE  LYS A 171     2915   3945   2945    295      5    222       C  
ATOM   1203  NZ  LYS A 171     -11.351   2.415 -33.947  1.00 26.51           N  
ANISOU 1203  NZ  LYS A 171     2986   4044   3042    290    -32    150       N  
ATOM   1204  N   PRO A 172     -10.954   6.137 -27.343  1.00 20.95           N  
ANISOU 1204  N   PRO A 172     2519   2904   2537    127     42    245       N  
ATOM   1205  CA  PRO A 172     -10.568   7.350 -26.609  1.00 21.21           C  
ANISOU 1205  CA  PRO A 172     2608   2866   2584     89     74    276       C  
ATOM   1206  C   PRO A 172      -9.723   8.276 -27.487  1.00 22.13           C  
ANISOU 1206  C   PRO A 172     2736   2999   2673     67    109    317       C  
ATOM   1207  O   PRO A 172      -9.037   7.789 -28.389  1.00 22.43           O  
ANISOU 1207  O   PRO A 172     2726   3107   2688     68    100    309       O  
ATOM   1208  CB  PRO A 172      -9.723   6.807 -25.443  1.00 20.74           C  
ANISOU 1208  CB  PRO A 172     2543   2783   2553     39     55    235       C  
ATOM   1209  CG  PRO A 172     -10.018   5.307 -25.384  1.00 20.73           C  
ANISOU 1209  CG  PRO A 172     2498   2820   2560     67     14    187       C  
ATOM   1210  CD  PRO A 172     -10.261   4.941 -26.824  1.00 20.95           C  
ANISOU 1210  CD  PRO A 172     2489   2917   2554    107     10    192       C  
ATOM   1211  N   PRO A 173      -9.757   9.611 -27.234  1.00 22.93           N  
ANISOU 1211  N   PRO A 173     2906   3033   2773     46    152    361       N  
ATOM   1212  CA  PRO A 173      -8.889  10.505 -28.002  1.00 22.83           C  
ANISOU 1212  CA  PRO A 173     2913   3027   2733     11    189    400       C  
ATOM   1213  C   PRO A 173      -7.425  10.115 -27.852  1.00 22.22           C  
ANISOU 1213  C   PRO A 173     2793   2992   2656    -60    178    369       C  
ATOM   1214  O   PRO A 173      -6.981   9.773 -26.759  1.00 22.14           O  
ANISOU 1214  O   PRO A 173     2778   2963   2671   -102    160    332       O  
ATOM   1215  CB  PRO A 173      -9.153  11.892 -27.385  1.00 23.71           C  
ANISOU 1215  CB  PRO A 173     3124   3036   2851    -12    236    439       C  
ATOM   1216  CG  PRO A 173      -9.720  11.621 -26.039  1.00 23.59           C  
ANISOU 1216  CG  PRO A 173     3127   2966   2870    -12    217    406       C  
ATOM   1217  CD  PRO A 173     -10.531  10.350 -26.219  1.00 23.68           C  
ANISOU 1217  CD  PRO A 173     3070   3040   2888     51    170    375       C  
ATOM   1218  N   GLY A 174      -6.688  10.142 -28.955  1.00 21.45           N  
ANISOU 1218  N   GLY A 174     2661   2964   2526    -68    188    386       N  
ATOM   1219  CA  GLY A 174      -5.297   9.738 -28.937  1.00 20.69           C  
ANISOU 1219  CA  GLY A 174     2511   2931   2419   -125    178    361       C  
ATOM   1220  C   GLY A 174      -5.037   8.240 -29.039  1.00 19.40           C  
ANISOU 1220  C   GLY A 174     2270   2846   2257    -86    129    309       C  
ATOM   1221  O   GLY A 174      -3.891   7.805 -28.948  1.00 19.60           O  
ANISOU 1221  O   GLY A 174     2246   2932   2269   -118    118    286       O  
ATOM   1222  N   SER A 175      -6.088   7.450 -29.232  1.00 18.18           N  
ANISOU 1222  N   SER A 175     2105   2691   2111    -16    103    291       N  
ATOM   1223  CA  SER A 175      -5.941   6.003 -29.366  1.00 17.34           C  
ANISOU 1223  CA  SER A 175     1943   2643   2003     22     62    241       C  
ATOM   1224  C   SER A 175      -6.742   5.482 -30.553  1.00 17.12           C  
ANISOU 1224  C   SER A 175     1893   2662   1952     86     52    241       C  
ATOM   1225  O   SER A 175      -7.897   5.880 -30.763  1.00 17.85           O  
ANISOU 1225  O   SER A 175     2012   2726   2045    116     60    264       O  
ATOM   1226  CB  SER A 175      -6.386   5.297 -28.081  1.00 16.76           C  
ANISOU 1226  CB  SER A 175     1883   2517   1967     25     35    201       C  
ATOM   1227  OG  SER A 175      -6.486   3.903 -28.279  1.00 15.82           O  
ANISOU 1227  OG  SER A 175     1730   2437   1845     69      1    156       O  
ATOM   1228  N   SER A 176      -6.127   4.591 -31.326  1.00 16.69           N  
ANISOU 1228  N   SER A 176     1786   2684   1869    110     35    214       N  
ATOM   1229  CA  SER A 176      -6.804   3.932 -32.444  1.00 16.69           C  
ANISOU 1229  CA  SER A 176     1762   2738   1843    167     21    201       C  
ATOM   1230  C   SER A 176      -7.591   2.699 -31.998  1.00 16.32           C  
ANISOU 1230  C   SER A 176     1716   2670   1813    194    -14    147       C  
ATOM   1231  O   SER A 176      -8.207   2.014 -32.823  1.00 16.38           O  
ANISOU 1231  O   SER A 176     1706   2721   1798    231    -29    124       O  
ATOM   1232  CB  SER A 176      -5.786   3.512 -33.499  1.00 17.04           C  
ANISOU 1232  CB  SER A 176     1756   2873   1845    182     20    193       C  
ATOM   1233  OG  SER A 176      -5.003   2.430 -33.020  1.00 16.91           O  
ANISOU 1233  OG  SER A 176     1718   2876   1833    188     -3    144       O  
ATOM   1234  N   GLU A 177      -7.557   2.405 -30.700  1.00 15.98           N  
ANISOU 1234  N   GLU A 177     1697   2567   1809    171    -26    125       N  
ATOM   1235  CA  GLU A 177      -8.141   1.166 -30.183  1.00 16.43           C  
ANISOU 1235  CA  GLU A 177     1761   2599   1882    189    -55     73       C  
ATOM   1236  C   GLU A 177      -9.509   1.354 -29.512  1.00 16.69           C  
ANISOU 1236  C   GLU A 177     1825   2574   1941    185    -59     77       C  
ATOM   1237  O   GLU A 177      -9.612   2.025 -28.480  1.00 16.47           O  
ANISOU 1237  O   GLU A 177     1826   2487   1943    159    -49     97       O  
ATOM   1238  CB  GLU A 177      -7.154   0.494 -29.228  1.00 16.15           C  
ANISOU 1238  CB  GLU A 177     1727   2546   1864    179    -67     43       C  
ATOM   1239  CG  GLU A 177      -7.628  -0.847 -28.666  1.00 18.45           C  
ANISOU 1239  CG  GLU A 177     2039   2803   2169    199    -93     -8       C  
ATOM   1240  CD  GLU A 177      -6.543  -1.575 -27.898  1.00 20.35           C  
ANISOU 1240  CD  GLU A 177     2278   3040   2413    208   -101    -33       C  
ATOM   1241  OE1 GLU A 177      -5.395  -1.097 -27.877  1.00 23.70           O  
ANISOU 1241  OE1 GLU A 177     2674   3506   2823    199    -91    -15       O  
ATOM   1242  OE2 GLU A 177      -6.835  -2.634 -27.314  1.00 20.45           O  
ANISOU 1242  OE2 GLU A 177     2319   3013   2438    225   -117    -69       O  
ATOM   1243  N   PRO A 178     -10.570   0.762 -30.102  1.00 17.31           N  
ANISOU 1243  N   PRO A 178     1896   2678   2005    208    -73     56       N  
ATOM   1244  CA  PRO A 178     -11.913   0.820 -29.509  1.00 17.62           C  
ANISOU 1244  CA  PRO A 178     1953   2683   2060    204    -78     57       C  
ATOM   1245  C   PRO A 178     -11.927   0.122 -28.159  1.00 17.32           C  
ANISOU 1245  C   PRO A 178     1943   2579   2061    181    -93     25       C  
ATOM   1246  O   PRO A 178     -11.271  -0.903 -27.999  1.00 17.39           O  
ANISOU 1246  O   PRO A 178     1954   2583   2072    181   -107    -15       O  
ATOM   1247  CB  PRO A 178     -12.777   0.032 -30.505  1.00 18.14           C  
ANISOU 1247  CB  PRO A 178     1993   2811   2091    223    -94     26       C  
ATOM   1248  CG  PRO A 178     -11.783  -0.825 -31.286  1.00 18.66           C  
ANISOU 1248  CG  PRO A 178     2042   2915   2133    234   -103    -10       C  
ATOM   1249  CD  PRO A 178     -10.559   0.027 -31.383  1.00 17.92           C  
ANISOU 1249  CD  PRO A 178     1942   2827   2040    235    -83     30       C  
ATOM   1250  N   ILE A 179     -12.645   0.671 -27.187  1.00 16.71           N  
ANISOU 1250  N   ILE A 179     1889   2452   2009    168    -87     44       N  
ATOM   1251  CA  ILE A 179     -12.691   0.020 -25.880  1.00 15.92           C  
ANISOU 1251  CA  ILE A 179     1814   2291   1943    147   -100     16       C  
ATOM   1252  C   ILE A 179     -13.995  -0.737 -25.626  1.00 15.72           C  
ANISOU 1252  C   ILE A 179     1792   2262   1918    141   -115    -11       C  
ATOM   1253  O   ILE A 179     -15.033  -0.417 -26.196  1.00 16.14           O  
ANISOU 1253  O   ILE A 179     1826   2356   1948    151   -113      2       O  
ATOM   1254  CB  ILE A 179     -12.402   1.008 -24.720  1.00 15.99           C  
ANISOU 1254  CB  ILE A 179     1851   2243   1982    127    -85     47       C  
ATOM   1255  CG1 ILE A 179     -13.410   2.163 -24.692  1.00 15.93           C  
ANISOU 1255  CG1 ILE A 179     1856   2224   1971    137    -65     90       C  
ATOM   1256  CG2 ILE A 179     -10.965   1.539 -24.810  1.00 15.16           C  
ANISOU 1256  CG2 ILE A 179     1741   2145   1874    114    -73     62       C  
ATOM   1257  CD1 ILE A 179     -13.261   3.064 -23.457  1.00 15.67           C  
ANISOU 1257  CD1 ILE A 179     1862   2124   1966    116    -49    112       C  
ATOM   1258  N   THR A 180     -13.918  -1.764 -24.782  1.00 14.82           N  
ANISOU 1258  N   THR A 180     1701   2105   1824    124   -129    -48       N  
ATOM   1259  CA  THR A 180     -15.093  -2.475 -24.314  1.00 14.47           C  
ANISOU 1259  CA  THR A 180     1667   2047   1783    103   -140    -73       C  
ATOM   1260  C   THR A 180     -15.437  -1.968 -22.913  1.00 14.06           C  
ANISOU 1260  C   THR A 180     1638   1940   1765     90   -135    -51       C  
ATOM   1261  O   THR A 180     -14.565  -1.913 -22.055  1.00 13.78           O  
ANISOU 1261  O   THR A 180     1625   1859   1754     87   -133    -49       O  
ATOM   1262  CB  THR A 180     -14.820  -3.985 -24.294  1.00 15.14           C  
ANISOU 1262  CB  THR A 180     1776   2109   1865     92   -154   -126       C  
ATOM   1263  OG1 THR A 180     -14.548  -4.400 -25.631  1.00 16.15           O  
ANISOU 1263  OG1 THR A 180     1886   2291   1958    107   -158   -148       O  
ATOM   1264  CG2 THR A 180     -16.006  -4.763 -23.768  1.00 15.49           C  
ANISOU 1264  CG2 THR A 180     1838   2135   1912     56   -162   -153       C  
ATOM   1265  N   VAL A 181     -16.686  -1.531 -22.724  1.00 14.02           N  
ANISOU 1265  N   VAL A 181     1622   1950   1754     86   -131    -35       N  
ATOM   1266  CA  VAL A 181     -17.202  -1.147 -21.401  1.00 13.81           C  
ANISOU 1266  CA  VAL A 181     1616   1878   1753     76   -126    -19       C  
ATOM   1267  C   VAL A 181     -18.481  -1.958 -21.162  1.00 14.29           C  
ANISOU 1267  C   VAL A 181     1668   1959   1803     51   -137    -43       C  
ATOM   1268  O   VAL A 181     -19.437  -1.859 -21.935  1.00 14.30           O  
ANISOU 1268  O   VAL A 181     1634   2029   1771     55   -138    -41       O  
ATOM   1269  CB  VAL A 181     -17.464   0.385 -21.292  1.00 13.84           C  
ANISOU 1269  CB  VAL A 181     1620   1883   1756    103   -105     32       C  
ATOM   1270  CG1 VAL A 181     -17.884   0.785 -19.872  1.00 13.64           C  
ANISOU 1270  CG1 VAL A 181     1621   1805   1754     96    -98     45       C  
ATOM   1271  CG2 VAL A 181     -16.204   1.178 -21.713  1.00 13.82           C  
ANISOU 1271  CG2 VAL A 181     1628   1868   1757    114    -91     55       C  
ATOM   1272  N   LYS A 182     -18.476  -2.778 -20.116  1.00 14.15           N  
ANISOU 1272  N   LYS A 182     1679   1889   1808     23   -144    -67       N  
ATOM   1273  CA  LYS A 182     -19.618  -3.652 -19.799  1.00 15.04           C  
ANISOU 1273  CA  LYS A 182     1790   2014   1911    -16   -151    -92       C  
ATOM   1274  C   LYS A 182     -19.690  -3.903 -18.302  1.00 15.09           C  
ANISOU 1274  C   LYS A 182     1830   1957   1947    -34   -150    -91       C  
ATOM   1275  O   LYS A 182     -18.711  -3.664 -17.584  1.00 14.22           O  
ANISOU 1275  O   LYS A 182     1747   1792   1864    -17   -147    -80       O  
ATOM   1276  CB  LYS A 182     -19.512  -4.995 -20.543  1.00 15.33           C  
ANISOU 1276  CB  LYS A 182     1839   2058   1930    -46   -162   -142       C  
ATOM   1277  CG  LYS A 182     -18.255  -5.815 -20.214  1.00 17.01           C  
ANISOU 1277  CG  LYS A 182     2101   2199   2163    -40   -164   -165       C  
ATOM   1278  CD  LYS A 182     -18.215  -7.096 -21.039  1.00 20.45           C  
ANISOU 1278  CD  LYS A 182     2560   2637   2574    -62   -170   -215       C  
ATOM   1279  CE  LYS A 182     -16.789  -7.590 -21.209  1.00 21.75           C  
ANISOU 1279  CE  LYS A 182     2758   2760   2744    -25   -169   -228       C  
ATOM   1280  NZ  LYS A 182     -16.749  -8.979 -21.765  1.00 24.70           N  
ANISOU 1280  NZ  LYS A 182     3178   3112   3097    -43   -169   -281       N  
ATOM   1281  N   PHE A 183     -20.837  -4.392 -17.828  1.00 15.50           N  
ANISOU 1281  N   PHE A 183     1876   2023   1989    -70   -151   -101       N  
ATOM   1282  CA  PHE A 183     -20.923  -4.808 -16.435  1.00 16.00           C  
ANISOU 1282  CA  PHE A 183     1974   2028   2078    -91   -149   -102       C  
ATOM   1283  C   PHE A 183     -19.954  -5.966 -16.158  1.00 17.18           C  
ANISOU 1283  C   PHE A 183     2176   2107   2243   -102   -153   -132       C  
ATOM   1284  O   PHE A 183     -19.855  -6.912 -16.950  1.00 17.06           O  
ANISOU 1284  O   PHE A 183     2177   2095   2212   -122   -157   -166       O  
ATOM   1285  CB  PHE A 183     -22.371  -5.114 -16.032  1.00 16.32           C  
ANISOU 1285  CB  PHE A 183     1993   2109   2100   -132   -148   -106       C  
ATOM   1286  CG  PHE A 183     -23.251  -3.880 -16.002  1.00 14.75           C  
ANISOU 1286  CG  PHE A 183     1747   1975   1884   -100   -140    -68       C  
ATOM   1287  CD1 PHE A 183     -23.052  -2.900 -15.036  1.00 14.74           C  
ANISOU 1287  CD1 PHE A 183     1759   1938   1904    -62   -130    -33       C  
ATOM   1288  CD2 PHE A 183     -24.244  -3.697 -16.947  1.00 14.50           C  
ANISOU 1288  CD2 PHE A 183     1660   2041   1809   -103   -142    -67       C  
ATOM   1289  CE1 PHE A 183     -23.830  -1.765 -14.999  1.00 15.77           C  
ANISOU 1289  CE1 PHE A 183     1859   2118   2015    -22   -119      2       C  
ATOM   1290  CE2 PHE A 183     -25.040  -2.567 -16.929  1.00 16.88           C  
ANISOU 1290  CE2 PHE A 183     1920   2405   2087    -57   -132    -28       C  
ATOM   1291  CZ  PHE A 183     -24.825  -1.582 -15.952  1.00 15.53           C  
ANISOU 1291  CZ  PHE A 183     1774   2186   1941    -13   -119      8       C  
ATOM   1292  N   ALA A 184     -19.207  -5.847 -15.063  1.00 17.48           N  
ANISOU 1292  N   ALA A 184     2244   2088   2308    -84   -150   -118       N  
ATOM   1293  CA  ALA A 184     -18.208  -6.846 -14.683  1.00 19.20           C  
ANISOU 1293  CA  ALA A 184     2513   2246   2537    -76   -151   -137       C  
ATOM   1294  C   ALA A 184     -18.866  -8.173 -14.296  1.00 20.62           C  
ANISOU 1294  C   ALA A 184     2737   2388   2710   -121   -148   -164       C  
ATOM   1295  O   ALA A 184     -20.022  -8.182 -13.867  1.00 20.98           O  
ANISOU 1295  O   ALA A 184     2770   2450   2751   -162   -145   -160       O  
ATOM   1296  CB  ALA A 184     -17.371  -6.322 -13.532  1.00 18.20           C  
ANISOU 1296  CB  ALA A 184     2398   2085   2433    -47   -149   -113       C  
ATOM   1297  N   ALA A 185     -18.138  -9.275 -14.500  1.00 22.41           N  
ANISOU 1297  N   ALA A 185     3016   2568   2932   -112   -146   -190       N  
ATOM   1298  CA  ALA A 185     -18.435 -10.603 -13.912  1.00 24.06           C  
ANISOU 1298  CA  ALA A 185     3293   2711   3136   -145   -135   -211       C  
ATOM   1299  C   ALA A 185     -17.914 -11.749 -14.763  1.00 25.28           C  
ANISOU 1299  C   ALA A 185     3503   2830   3271   -140   -130   -249       C  
ATOM   1300  O   ALA A 185     -17.228 -12.644 -14.261  1.00 26.91           O  
ANISOU 1300  O   ALA A 185     3779   2967   3478   -112   -119   -255       O  
ATOM   1301  CB  ALA A 185     -19.922 -10.791 -13.622  1.00 24.70           C  
ANISOU 1301  CB  ALA A 185     3365   2810   3209   -219   -131   -216       C  
TER    1302      ALA A 185                                                      
ATOM   1303  N   GLY B  18     -37.403  15.208 -38.439  1.00 42.28           N  
ANISOU 1303  N   GLY B  18     5335   6474   4257   -168    158   2962       N  
ATOM   1304  CA  GLY B  18     -38.426  14.676 -37.491  1.00 40.56           C  
ANISOU 1304  CA  GLY B  18     5133   6113   4166     58    151   2767       C  
ATOM   1305  C   GLY B  18     -38.275  13.180 -37.263  1.00 38.32           C  
ANISOU 1305  C   GLY B  18     4591   6065   3905     77    173   2507       C  
ATOM   1306  O   GLY B  18     -37.691  12.475 -38.093  1.00 38.19           O  
ANISOU 1306  O   GLY B  18     4357   6370   3783      2    192   2471       O  
ATOM   1307  N   ARG B  19     -38.811  12.696 -36.141  1.00 36.32           N  
ANISOU 1307  N   ARG B  19     4370   5650   3779    184    168   2328       N  
ATOM   1308  CA  ARG B  19     -38.698  11.291 -35.771  1.00 34.17           C  
ANISOU 1308  CA  ARG B  19     3906   5533   3544    201    183   2088       C  
ATOM   1309  C   ARG B  19     -39.479  10.400 -36.728  1.00 33.43           C  
ANISOU 1309  C   ARG B  19     3610   5740   3351    333    191   2014       C  
ATOM   1310  O   ARG B  19     -40.663  10.636 -36.977  1.00 33.73           O  
ANISOU 1310  O   ARG B  19     3668   5786   3362    498    181   2056       O  
ATOM   1311  CB  ARG B  19     -39.177  11.069 -34.332  1.00 32.90           C  
ANISOU 1311  CB  ARG B  19     3847   5122   3531    276    174   1942       C  
ATOM   1312  CG  ARG B  19     -38.288  11.703 -33.270  1.00 34.27           C  
ANISOU 1312  CG  ARG B  19     4188   5033   3801    127    167   1957       C  
ATOM   1313  CD  ARG B  19     -38.910  11.597 -31.880  1.00 35.11           C  
ANISOU 1313  CD  ARG B  19     4399   4903   4037    226    156   1828       C  
ATOM   1314  NE  ARG B  19     -40.091  12.451 -31.745  1.00 38.37           N  
ANISOU 1314  NE  ARG B  19     4970   5146   4463    404    139   1909       N  
ATOM   1315  CZ  ARG B  19     -40.820  12.575 -30.636  1.00 38.84           C  
ANISOU 1315  CZ  ARG B  19     5131   5017   4609    526    128   1822       C  
ATOM   1316  NH1 ARG B  19     -40.503  11.895 -29.547  1.00 37.71           N  
ANISOU 1316  NH1 ARG B  19     4954   4822   4552    472    133   1661       N  
ATOM   1317  NH2 ARG B  19     -41.874  13.383 -30.618  1.00 40.30           N  
ANISOU 1317  NH2 ARG B  19     5447   5084   4779    718    111   1899       N  
ATOM   1318  N   THR B  20     -38.806   9.388 -37.275  1.00 32.32           N  
ANISOU 1318  N   THR B  20     3272   5862   3145    266    206   1898       N  
ATOM   1319  CA  THR B  20     -39.459   8.405 -38.141  1.00 31.43           C  
ANISOU 1319  CA  THR B  20     2969   6034   2938    368    211   1786       C  
ATOM   1320  C   THR B  20     -39.692   7.065 -37.437  1.00 29.07           C  
ANISOU 1320  C   THR B  20     2604   5724   2718    410    210   1530       C  
ATOM   1321  O   THR B  20     -40.483   6.254 -37.919  1.00 28.89           O  
ANISOU 1321  O   THR B  20     2468   5869   2640    491    207   1417       O  
ATOM   1322  CB  THR B  20     -38.614   8.093 -39.389  1.00 32.43           C  
ANISOU 1322  CB  THR B  20     2918   6493   2910    286    225   1811       C  
ATOM   1323  OG1 THR B  20     -37.282   7.770 -38.982  1.00 31.72           O  
ANISOU 1323  OG1 THR B  20     2798   6410   2846    153    235   1742       O  
ATOM   1324  CG2 THR B  20     -38.592   9.266 -40.378  1.00 35.54           C  
ANISOU 1324  CG2 THR B  20     3344   6976   3183    251    226   2076       C  
ATOM   1325  N   ASN B  21     -38.988   6.838 -36.323  1.00 27.35           N  
ANISOU 1325  N   ASN B  21     2460   5314   2617    342    209   1445       N  
ATOM   1326  CA  ASN B  21     -38.869   5.507 -35.701  1.00 24.99           C  
ANISOU 1326  CA  ASN B  21     2107   5009   2379    358    206   1217       C  
ATOM   1327  C   ASN B  21     -39.871   5.268 -34.576  1.00 23.24           C  
ANISOU 1327  C   ASN B  21     1983   4574   2274    428    195   1134       C  
ATOM   1328  O   ASN B  21     -39.957   6.054 -33.630  1.00 22.78           O  
ANISOU 1328  O   ASN B  21     2065   4282   2307    423    191   1204       O  
ATOM   1329  CB  ASN B  21     -37.430   5.280 -35.207  1.00 25.01           C  
ANISOU 1329  CB  ASN B  21     2102   4988   2412    257    211   1171       C  
ATOM   1330  CG  ASN B  21     -37.117   3.809 -34.936  1.00 24.23           C  
ANISOU 1330  CG  ASN B  21     1929   4948   2330    298    205    947       C  
ATOM   1331  OD1 ASN B  21     -37.701   2.905 -35.541  1.00 25.63           O  
ANISOU 1331  OD1 ASN B  21     2027   5256   2454    368    201    828       O  
ATOM   1332  ND2 ASN B  21     -36.183   3.570 -34.029  1.00 22.58           N  
ANISOU 1332  ND2 ASN B  21     1754   4639   2185    256    203    889       N  
ATOM   1333  N   LEU B  22     -40.630   4.181 -34.693  1.00 22.23           N  
ANISOU 1333  N   LEU B  22     1780   4538   2129    482    190    982       N  
ATOM   1334  CA  LEU B  22     -41.710   3.866 -33.749  1.00 21.01           C  
ANISOU 1334  CA  LEU B  22     1687   4246   2052    531    180    905       C  
ATOM   1335  C   LEU B  22     -41.465   2.563 -33.016  1.00 19.69           C  
ANISOU 1335  C   LEU B  22     1526   4006   1950    495    172    717       C  
ATOM   1336  O   LEU B  22     -40.931   1.623 -33.600  1.00 20.35           O  
ANISOU 1336  O   LEU B  22     1536   4211   1984    475    169    604       O  
ATOM   1337  CB  LEU B  22     -43.045   3.720 -34.494  1.00 21.47           C  
ANISOU 1337  CB  LEU B  22     1655   4490   2012    604    176    900       C  
ATOM   1338  CG  LEU B  22     -43.547   4.880 -35.349  1.00 22.68           C  
ANISOU 1338  CG  LEU B  22     1790   4755   2072    682    179   1086       C  
ATOM   1339  CD1 LEU B  22     -44.821   4.470 -36.045  1.00 22.38           C  
ANISOU 1339  CD1 LEU B  22     1627   4956   1921    751    173   1041       C  
ATOM   1340  CD2 LEU B  22     -43.781   6.090 -34.465  1.00 22.32           C  
ANISOU 1340  CD2 LEU B  22     1904   4471   2107    742    176   1218       C  
ATOM   1341  N   ILE B  23     -41.870   2.503 -31.749  1.00 18.10           N  
ANISOU 1341  N   ILE B  23     1419   3607   1850    496    166    682       N  
ATOM   1342  CA  ILE B  23     -41.954   1.223 -31.050  1.00 17.13           C  
ANISOU 1342  CA  ILE B  23     1317   3413   1777    464    154    519       C  
ATOM   1343  C   ILE B  23     -43.427   0.814 -30.969  1.00 17.22           C  
ANISOU 1343  C   ILE B  23     1302   3485   1758    473    148    467       C  
ATOM   1344  O   ILE B  23     -44.289   1.630 -30.650  1.00 17.36           O  
ANISOU 1344  O   ILE B  23     1330   3493   1773    523    152    553       O  
ATOM   1345  CB  ILE B  23     -41.245   1.220 -29.646  1.00 16.21           C  
ANISOU 1345  CB  ILE B  23     1310   3069   1779    437    150    503       C  
ATOM   1346  CG1 ILE B  23     -41.244  -0.191 -29.036  1.00 15.75           C  
ANISOU 1346  CG1 ILE B  23     1286   2939   1759    410    134    348       C  
ATOM   1347  CG2 ILE B  23     -41.853   2.248 -28.701  1.00 15.94           C  
ANISOU 1347  CG2 ILE B  23     1358   2893   1806    462    154    596       C  
ATOM   1348  CD1 ILE B  23     -40.310  -0.357 -27.822  1.00 15.08           C  
ANISOU 1348  CD1 ILE B  23     1287   2676   1765    397    128    328       C  
ATOM   1349  N   VAL B  24     -43.695  -0.448 -31.284  1.00 17.41           N  
ANISOU 1349  N   VAL B  24     1292   3580   1744    424    135    323       N  
ATOM   1350  CA  VAL B  24     -45.054  -1.000 -31.262  1.00 18.15           C  
ANISOU 1350  CA  VAL B  24     1345   3765   1786    384    127    257       C  
ATOM   1351  C   VAL B  24     -45.169  -2.107 -30.202  1.00 17.84           C  
ANISOU 1351  C   VAL B  24     1402   3561   1817    297    111    140       C  
ATOM   1352  O   VAL B  24     -44.532  -3.140 -30.330  1.00 18.32           O  
ANISOU 1352  O   VAL B  24     1513   3557   1890    257     95     26       O  
ATOM   1353  CB  VAL B  24     -45.441  -1.529 -32.673  1.00 18.87           C  
ANISOU 1353  CB  VAL B  24     1319   4106   1744    365    121    187       C  
ATOM   1354  CG1 VAL B  24     -46.899  -1.808 -32.758  1.00 19.53           C  
ANISOU 1354  CG1 VAL B  24     1330   4346   1746    317    115    150       C  
ATOM   1355  CG2 VAL B  24     -45.064  -0.516 -33.736  1.00 20.59           C  
ANISOU 1355  CG2 VAL B  24     1453   4479   1890    448    136    314       C  
ATOM   1356  N   ASN B  25     -45.973  -1.888 -29.156  1.00 17.83           N  
ANISOU 1356  N   ASN B  25     1430   3496   1851    278    113    172       N  
ATOM   1357  CA  ASN B  25     -46.077  -2.845 -28.038  1.00 17.23           C  
ANISOU 1357  CA  ASN B  25     1452   3260   1837    184     98     92       C  
ATOM   1358  C   ASN B  25     -47.447  -3.562 -27.991  1.00 18.71           C  
ANISOU 1358  C   ASN B  25     1592   3573   1943     65     88     26       C  
ATOM   1359  O   ASN B  25     -48.405  -3.098 -28.599  1.00 19.58           O  
ANISOU 1359  O   ASN B  25     1579   3909   1953     82     96     58       O  
ATOM   1360  CB  ASN B  25     -45.829  -2.134 -26.692  1.00 16.30           C  
ANISOU 1360  CB  ASN B  25     1404   2975   1814    227    107    171       C  
ATOM   1361  CG  ASN B  25     -44.439  -1.520 -26.578  1.00 15.18           C  
ANISOU 1361  CG  ASN B  25     1315   2706   1747    299    113    225       C  
ATOM   1362  OD1 ASN B  25     -44.277  -0.312 -26.736  1.00 16.39           O  
ANISOU 1362  OD1 ASN B  25     1449   2876   1903    373    128    329       O  
ATOM   1363  ND2 ASN B  25     -43.437  -2.342 -26.290  1.00 14.93           N  
ANISOU 1363  ND2 ASN B  25     1356   2552   1764    277    100    157       N  
ATOM   1364  N   TYR B  26     -47.530  -4.672 -27.243  1.00 19.52           N  
ANISOU 1364  N   TYR B  26     1797   3542   2079    -60     70    -56       N  
ATOM   1365  CA  TYR B  26     -48.759  -5.489 -27.104  1.00 20.92           C  
ANISOU 1365  CA  TYR B  26     1950   3825   2173   -229     57   -121       C  
ATOM   1366  C   TYR B  26     -49.270  -6.122 -28.408  1.00 22.29           C  
ANISOU 1366  C   TYR B  26     2052   4188   2230   -317     44   -220       C  
ATOM   1367  O   TYR B  26     -50.480  -6.180 -28.666  1.00 23.04           O  
ANISOU 1367  O   TYR B  26     2031   4515   2209   -414     44   -234       O  
ATOM   1368  CB  TYR B  26     -49.887  -4.707 -26.394  1.00 21.46           C  
ANISOU 1368  CB  TYR B  26     1914   4047   2194   -221     75    -36       C  
ATOM   1369  CG  TYR B  26     -49.399  -3.906 -25.215  1.00 21.24           C  
ANISOU 1369  CG  TYR B  26     1945   3859   2268   -112     89     53       C  
ATOM   1370  CD1 TYR B  26     -49.017  -4.529 -24.036  1.00 21.83           C  
ANISOU 1370  CD1 TYR B  26     2145   3727   2421   -188     78     38       C  
ATOM   1371  CD2 TYR B  26     -49.304  -2.524 -25.292  1.00 22.06           C  
ANISOU 1371  CD2 TYR B  26     1992   4008   2383     64    109    152       C  
ATOM   1372  CE1 TYR B  26     -48.560  -3.781 -22.951  1.00 23.11           C  
ANISOU 1372  CE1 TYR B  26     2352   3765   2665    -92     90    109       C  
ATOM   1373  CE2 TYR B  26     -48.846  -1.776 -24.236  1.00 22.65           C  
ANISOU 1373  CE2 TYR B  26     2133   3928   2544    152    118    216       C  
ATOM   1374  CZ  TYR B  26     -48.477  -2.403 -23.066  1.00 22.79           C  
ANISOU 1374  CZ  TYR B  26     2252   3772   2633     72    110    189       C  
ATOM   1375  OH  TYR B  26     -48.026  -1.638 -22.013  1.00 23.84           O  
ANISOU 1375  OH  TYR B  26     2442   3775   2841    155    118    242       O  
ATOM   1376  N   LEU B  27     -48.343  -6.628 -29.218  1.00 22.62           N  
ANISOU 1376  N   LEU B  27     2153   4154   2287   -283     30   -301       N  
ATOM   1377  CA  LEU B  27     -48.716  -7.332 -30.443  1.00 23.82           C  
ANISOU 1377  CA  LEU B  27     2257   4467   2326   -367     14   -422       C  
ATOM   1378  C   LEU B  27     -49.251  -8.723 -30.095  1.00 24.95           C  
ANISOU 1378  C   LEU B  27     2529   4503   2446   -589    -20   -549       C  
ATOM   1379  O   LEU B  27     -48.853  -9.293 -29.087  1.00 24.45           O  
ANISOU 1379  O   LEU B  27     2635   4178   2476   -631    -34   -554       O  
ATOM   1380  CB  LEU B  27     -47.508  -7.433 -31.384  1.00 23.59           C  
ANISOU 1380  CB  LEU B  27     2250   4403   2309   -245     10   -477       C  
ATOM   1381  CG  LEU B  27     -46.946  -6.084 -31.838  1.00 21.90           C  
ANISOU 1381  CG  LEU B  27     1916   4303   2100    -66     40   -342       C  
ATOM   1382  CD1 LEU B  27     -45.555  -6.253 -32.449  1.00 20.48           C  
ANISOU 1382  CD1 LEU B  27     1773   4066   1943     41     37   -388       C  
ATOM   1383  CD2 LEU B  27     -47.907  -5.366 -32.793  1.00 21.92           C  
ANISOU 1383  CD2 LEU B  27     1732   4625   1971    -51     54   -286       C  
ATOM   1384  N   PRO B  28     -50.174  -9.262 -30.910  1.00 27.05           N  
ANISOU 1384  N   PRO B  28     2723   4975   2580   -743    -34   -647       N  
ATOM   1385  CA  PRO B  28     -50.585 -10.655 -30.641  1.00 28.83           C  
ANISOU 1385  CA  PRO B  28     3113   5059   2782   -985    -72   -777       C  
ATOM   1386  C   PRO B  28     -49.388 -11.610 -30.726  1.00 29.30           C  
ANISOU 1386  C   PRO B  28     3408   4796   2929   -933   -104   -891       C  
ATOM   1387  O   PRO B  28     -48.528 -11.445 -31.587  1.00 28.76           O  
ANISOU 1387  O   PRO B  28     3316   4751   2862   -766   -102   -939       O  
ATOM   1388  CB  PRO B  28     -51.608 -10.960 -31.744  1.00 30.51           C  
ANISOU 1388  CB  PRO B  28     3189   5581   2822  -1142    -83   -878       C  
ATOM   1389  CG  PRO B  28     -51.619  -9.754 -32.668  1.00 29.68           C  
ANISOU 1389  CG  PRO B  28     2849   5776   2652   -944    -51   -798       C  
ATOM   1390  CD  PRO B  28     -51.004  -8.609 -31.940  1.00 27.62           C  
ANISOU 1390  CD  PRO B  28     2567   5419   2509   -726    -19   -627       C  
ATOM   1391  N   GLN B  29     -49.341 -12.585 -29.823  1.00 30.55           N  
ANISOU 1391  N   GLN B  29     3791   4671   3147  -1065   -134   -927       N  
ATOM   1392  CA  GLN B  29     -48.223 -13.531 -29.708  1.00 31.69           C  
ANISOU 1392  CA  GLN B  29     4189   4477   3373   -986   -170  -1023       C  
ATOM   1393  C   GLN B  29     -47.835 -14.224 -31.017  1.00 33.50           C  
ANISOU 1393  C   GLN B  29     4474   4720   3534   -952   -198  -1211       C  
ATOM   1394  O   GLN B  29     -46.670 -14.570 -31.216  1.00 33.48           O  
ANISOU 1394  O   GLN B  29     4592   4544   3584   -762   -215  -1279       O  
ATOM   1395  CB  GLN B  29     -48.545 -14.597 -28.650  1.00 33.14           C  
ANISOU 1395  CB  GLN B  29     4621   4375   3595  -1188   -207  -1034       C  
ATOM   1396  N   ASN B  30     -48.811 -14.420 -31.902  1.00 35.42           N  
ANISOU 1396  N   ASN B  30     4615   5197   3645  -1128   -205  -1301       N  
ATOM   1397  CA  ASN B  30     -48.602 -15.160 -33.144  1.00 37.55           C  
ANISOU 1397  CA  ASN B  30     4940   5498   3828  -1133   -236  -1504       C  
ATOM   1398  C   ASN B  30     -48.276 -14.280 -34.359  1.00 37.32           C  
ANISOU 1398  C   ASN B  30     4661   5795   3724   -945   -204  -1505       C  
ATOM   1399  O   ASN B  30     -48.001 -14.800 -35.451  1.00 38.76           O  
ANISOU 1399  O   ASN B  30     4860   6044   3823   -914   -226  -1675       O  
ATOM   1400  CB  ASN B  30     -49.816 -16.056 -33.437  1.00 40.10           C  
ANISOU 1400  CB  ASN B  30     5326   5875   4033  -1469   -270  -1631       C  
ATOM   1401  N   MET B  31     -48.300 -12.958 -34.177  1.00 35.82           N  
ANISOU 1401  N   MET B  31     4251   5803   3555   -820   -156  -1317       N  
ATOM   1402  CA  MET B  31     -48.006 -12.024 -35.279  1.00 35.66           C  
ANISOU 1402  CA  MET B  31     4001   6088   3460   -652   -126  -1278       C  
ATOM   1403  C   MET B  31     -46.556 -12.141 -35.758  1.00 35.30           C  
ANISOU 1403  C   MET B  31     4014   5948   3452   -427   -129  -1340       C  
ATOM   1404  O   MET B  31     -45.614 -12.116 -34.954  1.00 34.27           O  
ANISOU 1404  O   MET B  31     3999   5580   3441   -300   -128  -1286       O  
ATOM   1405  CB  MET B  31     -48.321 -10.562 -34.905  1.00 34.09           C  
ANISOU 1405  CB  MET B  31     3601   6069   3281   -562    -79  -1051       C  
ATOM   1406  CG  MET B  31     -48.268  -9.597 -36.103  1.00 35.25           C  
ANISOU 1406  CG  MET B  31     3517   6551   3325   -430    -52   -990       C  
ATOM   1407  SD  MET B  31     -49.065  -7.986 -35.852  1.00 36.68           S  
ANISOU 1407  SD  MET B  31     3483   6971   3482   -356     -9   -747       S  
ATOM   1408  CE  MET B  31     -47.678  -6.934 -35.555  1.00 33.85           C  
ANISOU 1408  CE  MET B  31     3146   6469   3247   -126     19   -590       C  
ATOM   1409  N   THR B  32     -46.410 -12.279 -37.074  1.00 35.81           N  
ANISOU 1409  N   THR B  32     3981   6232   3394   -380   -135  -1459       N  
ATOM   1410  CA  THR B  32     -45.117 -12.337 -37.741  1.00 35.78           C  
ANISOU 1410  CA  THR B  32     3975   6242   3377   -164   -135  -1529       C  
ATOM   1411  C   THR B  32     -44.622 -10.932 -38.074  1.00 34.13           C  
ANISOU 1411  C   THR B  32     3540   6272   3158     -8    -86  -1336       C  
ATOM   1412  O   THR B  32     -45.404  -9.976 -38.094  1.00 32.98           O  
ANISOU 1412  O   THR B  32     3236   6312   2985    -59    -58  -1180       O  
ATOM   1413  CB  THR B  32     -45.219 -13.141 -39.059  1.00 37.37           C  
ANISOU 1413  CB  THR B  32     4167   6604   3429   -191   -164  -1759       C  
ATOM   1414  N   GLN B  33     -43.322 -10.827 -38.349  1.00 33.89           N  
ANISOU 1414  N   GLN B  33     3501   6242   3135    181    -80  -1347       N  
ATOM   1415  CA  GLN B  33     -42.693  -9.593 -38.813  1.00 32.86           C  
ANISOU 1415  CA  GLN B  33     3170   6343   2971    308    -39  -1179       C  
ATOM   1416  C   GLN B  33     -43.300  -9.135 -40.145  1.00 33.97           C  
ANISOU 1416  C   GLN B  33     3102   6857   2949    279    -25  -1171       C  
ATOM   1417  O   GLN B  33     -43.542  -7.941 -40.340  1.00 33.03           O  
ANISOU 1417  O   GLN B  33     2827   6917   2805    296      8   -972       O  
ATOM   1418  CB  GLN B  33     -41.180  -9.813 -38.943  1.00 33.31           C  
ANISOU 1418  CB  GLN B  33     3253   6371   3032    492    -41  -1236       C  
ATOM   1419  CG  GLN B  33     -40.356  -8.640 -39.454  1.00 31.64           C  
ANISOU 1419  CG  GLN B  33     2845   6408   2769    597     -1  -1071       C  
ATOM   1420  CD  GLN B  33     -38.865  -8.855 -39.215  1.00 32.36           C  
ANISOU 1420  CD  GLN B  33     2967   6452   2878    759     -4  -1109       C  
ATOM   1421  OE1 GLN B  33     -38.420  -8.990 -38.072  1.00 29.58           O  
ANISOU 1421  OE1 GLN B  33     2743   5846   2649    788    -11  -1076       O  
ATOM   1422  NE2 GLN B  33     -38.087  -8.880 -40.295  1.00 32.43           N  
ANISOU 1422  NE2 GLN B  33     2838   6738   2745    868      3  -1177       N  
ATOM   1423  N   ASP B  34     -43.546 -10.088 -41.048  1.00 35.96           N  
ANISOU 1423  N   ASP B  34     3364   7216   3084    241    -53  -1389       N  
ATOM   1424  CA  ASP B  34     -44.221  -9.815 -42.318  0.50 37.09           C  
ANISOU 1424  CA  ASP B  34     3310   7731   3052    197    -46  -1410       C  
ATOM   1425  C   ASP B  34     -45.569  -9.133 -42.073  1.00 36.88           C  
ANISOU 1425  C   ASP B  34     3186   7813   3013     66    -32  -1262       C  
ATOM   1426  O   ASP B  34     -45.862  -8.092 -42.669  1.00 36.65           O  
ANISOU 1426  O   ASP B  34     2963   8062   2900    111     -4  -1099       O  
ATOM   1427  N   GLU B  35     -46.372  -9.729 -41.191  1.00 36.78           N  
ANISOU 1427  N   GLU B  35     3311   7590   3072    -88    -53  -1316       N  
ATOM   1428  CA  GLU B  35     -47.653  -9.155 -40.758  1.00 36.52           C  
ANISOU 1428  CA  GLU B  35     3191   7658   3027   -205    -42  -1185       C  
ATOM   1429  C   GLU B  35     -47.510  -7.752 -40.143  1.00 34.41           C  
ANISOU 1429  C   GLU B  35     2849   7381   2844    -83     -3   -915       C  
ATOM   1430  O   GLU B  35     -48.306  -6.853 -40.435  1.00 34.14           O  
ANISOU 1430  O   GLU B  35     2652   7587   2731    -68     15   -773       O  
ATOM   1431  CB  GLU B  35     -48.319 -10.082 -39.742  1.00 37.14           C  
ANISOU 1431  CB  GLU B  35     3451   7480   3180   -394    -70  -1280       C  
ATOM   1432  CG  GLU B  35     -48.941 -11.339 -40.327  1.00 40.49           C  
ANISOU 1432  CG  GLU B  35     3943   7949   3494   -589   -112  -1525       C  
ATOM   1433  CD  GLU B  35     -49.460 -12.263 -39.244  1.00 43.40           C  
ANISOU 1433  CD  GLU B  35     4528   8019   3943   -795   -142  -1596       C  
ATOM   1434  OE1 GLU B  35     -50.218 -11.788 -38.363  1.00 44.32           O  
ANISOU 1434  OE1 GLU B  35     4601   8139   4099   -878   -126  -1452       O  
ATOM   1435  N   LEU B  36     -46.500  -7.575 -39.290  1.00 32.89           N  
ANISOU 1435  N   LEU B  36     2783   6912   2802      8      6   -850       N  
ATOM   1436  CA  LEU B  36     -46.200  -6.263 -38.698  1.00 31.11           C  
ANISOU 1436  CA  LEU B  36     2519   6641   2661    114     38   -613       C  
ATOM   1437  C   LEU B  36     -45.965  -5.195 -39.766  1.00 31.31           C  
ANISOU 1437  C   LEU B  36     2366   6949   2580    224     63   -473       C  
ATOM   1438  O   LEU B  36     -46.581  -4.126 -39.722  1.00 30.74           O  
ANISOU 1438  O   LEU B  36     2209   6983   2487    263     81   -292       O  
ATOM   1439  CB  LEU B  36     -44.987  -6.343 -37.757  1.00 29.52           C  
ANISOU 1439  CB  LEU B  36     2469   6135   2612    185     40   -595       C  
ATOM   1440  CG  LEU B  36     -44.433  -5.036 -37.153  1.00 28.07           C  
ANISOU 1440  CG  LEU B  36     2269   5879   2516    279     70   -375       C  
ATOM   1441  CD1 LEU B  36     -45.488  -4.233 -36.393  1.00 28.14           C  
ANISOU 1441  CD1 LEU B  36     2266   5860   2565    250     82   -233       C  
ATOM   1442  CD2 LEU B  36     -43.229  -5.313 -36.243  1.00 26.20           C  
ANISOU 1442  CD2 LEU B  36     2170   5377   2407    328     66   -393       C  
ATOM   1443  N   ARG B  37     -45.053  -5.490 -40.697  1.00 32.29           N  
ANISOU 1443  N   ARG B  37     2445   7192   2630    284     62   -553       N  
ATOM   1444  CA  ARG B  37     -44.699  -4.592 -41.798  0.50 33.38           C  
ANISOU 1444  CA  ARG B  37     2417   7618   2649    372     84   -424       C  
ATOM   1445  C   ARG B  37     -45.904  -4.280 -42.680  1.00 34.53           C  
ANISOU 1445  C   ARG B  37     2401   8081   2638    343     83   -388       C  
ATOM   1446  O   ARG B  37     -46.145  -3.112 -43.014  1.00 34.82           O  
ANISOU 1446  O   ARG B  37     2338   8269   2623    412    103   -175       O  
ATOM   1447  CB  ARG B  37     -43.573  -5.197 -42.645  1.00 34.52           C  
ANISOU 1447  CB  ARG B  37     2527   7873   2714    430     79   -562       C  
ATOM   1448  CG  ARG B  37     -43.015  -4.256 -43.710  1.00 36.57           C  
ANISOU 1448  CG  ARG B  37     2615   8432   2847    507    104   -410       C  
ATOM   1449  CD  ARG B  37     -42.144  -4.985 -44.729  1.00 39.96           C  
ANISOU 1449  CD  ARG B  37     2967   9068   3147    561     98   -583       C  
ATOM   1450  NE  ARG B  37     -40.795  -5.237 -44.232  1.00 42.65           N  
ANISOU 1450  NE  ARG B  37     3386   9256   3564    633    100   -625       N  
ATOM   1451  CZ  ARG B  37     -40.407  -6.367 -43.647  1.00 43.76           C  
ANISOU 1451  CZ  ARG B  37     3676   9169   3781    658     74   -833       C  
ATOM   1452  N   SER B  38     -46.667  -5.321 -43.032  1.00 35.36           N  
ANISOU 1452  N   SER B  38     2491   8282   2660    237     58   -592       N  
ATOM   1453  CA  SER B  38     -47.876  -5.168 -43.849  1.00 36.69           C  
ANISOU 1453  CA  SER B  38     2491   8791   2659    190     53   -587       C  
ATOM   1454  C   SER B  38     -48.892  -4.210 -43.211  1.00 35.80           C  
ANISOU 1454  C   SER B  38     2335   8698   2570    210     65   -389       C  
ATOM   1455  O   SER B  38     -49.458  -3.353 -43.892  1.00 36.21           O  
ANISOU 1455  O   SER B  38     2230   9032   2495    288     75   -243       O  
ATOM   1456  CB  SER B  38     -48.534  -6.531 -44.123  1.00 38.20           C  
ANISOU 1456  CB  SER B  38     2706   9036   2772     26     18   -859       C  
ATOM   1457  OG  SER B  38     -47.689  -7.388 -44.869  1.00 39.00           O  
ANISOU 1457  OG  SER B  38     2841   9158   2821     39      3  -1058       O  
ATOM   1458  N   LEU B  39     -49.106  -4.356 -41.905  1.00 34.50           N  
ANISOU 1458  N   LEU B  39     2312   8243   2555    158     62   -385       N  
ATOM   1459  CA  LEU B  39     -50.057  -3.511 -41.174  1.00 33.73           C  
ANISOU 1459  CA  LEU B  39     2182   8153   2478    194     72   -223       C  
ATOM   1460  C   LEU B  39     -49.684  -2.023 -41.214  1.00 33.02           C  
ANISOU 1460  C   LEU B  39     2070   8061   2414    377     97     36       C  
ATOM   1461  O   LEU B  39     -50.539  -1.154 -41.439  1.00 33.15           O  
ANISOU 1461  O   LEU B  39     1980   8275   2339    470    102    181       O  
ATOM   1462  CB  LEU B  39     -50.193  -4.001 -39.723  1.00 32.67           C  
ANISOU 1462  CB  LEU B  39     2213   7700   2501    101     66   -276       C  
ATOM   1463  CG  LEU B  39     -51.068  -3.214 -38.743  1.00 31.61           C  
ANISOU 1463  CG  LEU B  39     2067   7538   2404    145     76   -133       C  
ATOM   1464  CD1 LEU B  39     -52.513  -3.085 -39.238  1.00 33.68           C  
ANISOU 1464  CD1 LEU B  39     2137   8179   2481    120     70   -127       C  
ATOM   1465  CD2 LEU B  39     -51.028  -3.879 -37.382  1.00 29.06           C  
ANISOU 1465  CD2 LEU B  39     1907   6909   2226     32     68   -208       C  
ATOM   1466  N   PHE B  40     -48.403  -1.741 -40.993  1.00 32.21           N  
ANISOU 1466  N   PHE B  40     2076   7737   2426    427    109     91       N  
ATOM   1467  CA  PHE B  40     -47.922  -0.366 -40.917  1.00 32.02           C  
ANISOU 1467  CA  PHE B  40     2076   7646   2443    558    129    332       C  
ATOM   1468  C   PHE B  40     -47.687   0.234 -42.304  1.00 33.43           C  
ANISOU 1468  C   PHE B  40     2119   8118   2465    631    137    444       C  
ATOM   1469  O   PHE B  40     -47.718   1.459 -42.471  1.00 33.64           O  
ANISOU 1469  O   PHE B  40     2144   8166   2469    739    147    670       O  
ATOM   1470  CB  PHE B  40     -46.708  -0.271 -39.966  1.00 30.64           C  
ANISOU 1470  CB  PHE B  40     2069   7126   2448    551    137    352       C  
ATOM   1471  CG  PHE B  40     -47.110  -0.242 -38.506  1.00 29.47           C  
ANISOU 1471  CG  PHE B  40     2047   6705   2443    532    135    353       C  
ATOM   1472  CD1 PHE B  40     -47.520  -1.410 -37.857  1.00 28.77           C  
ANISOU 1472  CD1 PHE B  40     2008   6523   2399    420    119    169       C  
ATOM   1473  CD2 PHE B  40     -47.140   0.957 -37.803  1.00 27.79           C  
ANISOU 1473  CD2 PHE B  40     1911   6341   2308    621    145    536       C  
ATOM   1474  CE1 PHE B  40     -47.940  -1.383 -36.530  1.00 26.66           C  
ANISOU 1474  CE1 PHE B  40     1840   6046   2243    396    117    179       C  
ATOM   1475  CE2 PHE B  40     -47.550   0.992 -36.462  1.00 27.17           C  
ANISOU 1475  CE2 PHE B  40     1934   6045   2343    612    143    526       C  
ATOM   1476  CZ  PHE B  40     -47.952  -0.177 -35.831  1.00 26.11           C  
ANISOU 1476  CZ  PHE B  40     1823   5853   2244    499    131    353       C  
ATOM   1477  N   SER B  41     -47.505  -0.649 -43.293  1.00 34.91           N  
ANISOU 1477  N   SER B  41     2203   8528   2535    572    128    284       N  
ATOM   1478  CA  SER B  41     -47.455  -0.286 -44.720  1.00 36.90           C  
ANISOU 1478  CA  SER B  41     2288   9134   2597    624    133    355       C  
ATOM   1479  C   SER B  41     -48.733   0.383 -45.197  1.00 38.32           C  
ANISOU 1479  C   SER B  41     2340   9584   2637    700    129    483       C  
ATOM   1480  O   SER B  41     -48.720   1.114 -46.183  1.00 39.40           O  
ANISOU 1480  O   SER B  41     2368   9968   2635    784    135    639       O  
ATOM   1481  CB  SER B  41     -47.202  -1.523 -45.588  1.00 37.64           C  
ANISOU 1481  CB  SER B  41     2296   9422   2581    544    120    105       C  
ATOM   1482  OG  SER B  41     -45.909  -2.047 -45.359  1.00 37.93           O  
ANISOU 1482  OG  SER B  41     2429   9273   2710    526    124      4       O  
ATOM   1483  N   SER B  42     -49.834   0.136 -44.489  1.00 38.80           N  
ANISOU 1483  N   SER B  42     2406   9616   2720    673    117    423       N  
ATOM   1484  CA  SER B  42     -51.134   0.680 -44.882  1.00 40.38           C  
ANISOU 1484  CA  SER B  42     2461  10116   2765    759    110    522       C  
ATOM   1485  C   SER B  42     -51.279   2.181 -44.584  1.00 40.80           C  
ANISOU 1485  C   SER B  42     2574  10081   2847    951    119    809       C  
ATOM   1486  O   SER B  42     -52.177   2.829 -45.112  1.00 42.53           O  
ANISOU 1486  O   SER B  42     2675  10571   2916   1081    112    936       O  
ATOM   1487  CB  SER B  42     -52.279  -0.130 -44.258  1.00 40.55           C  
ANISOU 1487  CB  SER B  42     2444  10194   2771    650     94    354       C  
ATOM   1488  OG  SER B  42     -52.329   0.024 -42.854  1.00 38.60           O  
ANISOU 1488  OG  SER B  42     2352   9615   2701    648     98    378       O  
ATOM   1489  N   ILE B  43     -50.387   2.724 -43.757  1.00 39.60           N  
ANISOU 1489  N   ILE B  43     2612   9556   2878    973    131    906       N  
ATOM   1490  CA  ILE B  43     -50.356   4.160 -43.467  1.00 40.01           C  
ANISOU 1490  CA  ILE B  43     2772   9459   2970   1139    136   1169       C  
ATOM   1491  C   ILE B  43     -49.466   4.867 -44.488  1.00 41.18           C  
ANISOU 1491  C   ILE B  43     2916   9682   3047   1173    144   1347       C  
ATOM   1492  O   ILE B  43     -49.753   5.996 -44.905  1.00 42.47           O  
ANISOU 1492  O   ILE B  43     3098   9907   3133   1322    140   1580       O  
ATOM   1493  CB  ILE B  43     -49.839   4.450 -42.020  1.00 38.62           C  
ANISOU 1493  CB  ILE B  43     2814   8841   3019   1124    142   1183       C  
ATOM   1494  CG1 ILE B  43     -50.651   3.672 -40.970  1.00 37.62           C  
ANISOU 1494  CG1 ILE B  43     2688   8649   2956   1065    135   1008       C  
ATOM   1495  CG2 ILE B  43     -49.835   5.953 -41.712  1.00 39.54           C  
ANISOU 1495  CG2 ILE B  43     3073   8777   3174   1291    141   1439       C  
ATOM   1496  CD1 ILE B  43     -52.156   3.969 -40.958  1.00 39.94           C  
ANISOU 1496  CD1 ILE B  43     2862   9194   3119   1188    124   1042       C  
ATOM   1497  N   GLY B  44     -48.399   4.183 -44.900  1.00 40.63           N  
ANISOU 1497  N   GLY B  44     2824   9620   2991   1041    154   1237       N  
ATOM   1498  CA  GLY B  44     -47.403   4.745 -45.815  1.00 41.58           C  
ANISOU 1498  CA  GLY B  44     2927   9831   3039   1036    165   1389       C  
ATOM   1499  C   GLY B  44     -46.174   3.863 -45.913  1.00 40.81           C  
ANISOU 1499  C   GLY B  44     2819   9699   2987    898    176   1221       C  
ATOM   1500  O   GLY B  44     -46.139   2.772 -45.323  1.00 40.04           O  
ANISOU 1500  O   GLY B  44     2742   9496   2976    821    171    983       O  
ATOM   1501  N   GLU B  45     -45.167   4.355 -46.639  1.00 41.26           N  
ANISOU 1501  N   GLU B  45     2851   9849   2976    873    190   1355       N  
ATOM   1502  CA  GLU B  45     -43.946   3.616 -46.951  1.00 40.53           C  
ANISOU 1502  CA  GLU B  45     2706   9820   2873    776    201   1215       C  
ATOM   1503  C   GLU B  45     -43.081   3.335 -45.725  1.00 38.75           C  
ANISOU 1503  C   GLU B  45     2638   9239   2849    709    206   1129       C  
ATOM   1504  O   GLU B  45     -42.626   4.254 -45.037  1.00 37.83           O  
ANISOU 1504  O   GLU B  45     2662   8873   2840    695    212   1302       O  
ATOM   1505  N   VAL B  46     -42.861   2.049 -45.470  1.00 37.96           N  
ANISOU 1505  N   VAL B  46     2519   9116   2789    670    199    857       N  
ATOM   1506  CA  VAL B  46     -42.057   1.597 -44.340  1.00 36.11           C  
ANISOU 1506  CA  VAL B  46     2417   8577   2726    626    199    750       C  
ATOM   1507  C   VAL B  46     -40.620   1.291 -44.776  1.00 36.32           C  
ANISOU 1507  C   VAL B  46     2380   8722   2698    595    211    698       C  
ATOM   1508  O   VAL B  46     -40.388   0.429 -45.640  1.00 37.52           O  
ANISOU 1508  O   VAL B  46     2406   9127   2724    612    207    528       O  
ATOM   1509  CB  VAL B  46     -42.700   0.362 -43.654  1.00 35.12           C  
ANISOU 1509  CB  VAL B  46     2347   8311   2684    610    179    496       C  
ATOM   1510  CG1 VAL B  46     -41.761  -0.236 -42.621  1.00 33.33           C  
ANISOU 1510  CG1 VAL B  46     2246   7809   2607    582    176    378       C  
ATOM   1511  CG2 VAL B  46     -44.026   0.740 -43.009  1.00 34.47           C  
ANISOU 1511  CG2 VAL B  46     2323   8113   2661    629    171    560       C  
ATOM   1512  N   GLU B  47     -39.663   2.002 -44.175  1.00 35.42           N  
ANISOU 1512  N   GLU B  47     2347   8445   2666    551    224    837       N  
ATOM   1513  CA  GLU B  47     -38.232   1.780 -44.438  0.50 35.19           C  
ANISOU 1513  CA  GLU B  47     2246   8546   2580    518    236    799       C  
ATOM   1514  C   GLU B  47     -37.759   0.432 -43.877  1.00 34.11           C  
ANISOU 1514  C   GLU B  47     2137   8313   2510    559    222    518       C  
ATOM   1515  O   GLU B  47     -36.996  -0.298 -44.535  1.00 34.75           O  
ANISOU 1515  O   GLU B  47     2103   8625   2476    599    222    371       O  
ATOM   1516  CB  GLU B  47     -37.397   2.939 -43.869  1.00 35.21           C  
ANISOU 1516  CB  GLU B  47     2331   8400   2645    429    250   1026       C  
ATOM   1517  CG  GLU B  47     -35.885   2.877 -44.158  1.00 36.46           C  
ANISOU 1517  CG  GLU B  47     2385   8753   2714    370    266   1022       C  
ATOM   1518  CD  GLU B  47     -35.085   2.092 -43.123  1.00 37.08           C  
ANISOU 1518  CD  GLU B  47     2519   8665   2906    388    259    842       C  
ATOM   1519  OE1 GLU B  47     -35.470   2.065 -41.924  1.00 34.13           O  
ANISOU 1519  OE1 GLU B  47     2309   7947   2711    391    247    815       O  
ATOM   1520  OE2 GLU B  47     -34.049   1.509 -43.519  1.00 39.16           O  
ANISOU 1520  OE2 GLU B  47     2653   9165   3063    412    264    730       O  
ATOM   1521  N   SER B  48     -38.205   0.119 -42.657  1.00 31.86           N  
ANISOU 1521  N   SER B  48     2012   7692   2401    561    208    448       N  
ATOM   1522  CA  SER B  48     -37.909  -1.156 -42.011  1.00 30.76           C  
ANISOU 1522  CA  SER B  48     1944   7406   2340    603    189    202       C  
ATOM   1523  C   SER B  48     -38.878  -1.442 -40.861  1.00 29.30           C  
ANISOU 1523  C   SER B  48     1920   6895   2317    586    173    155       C  
ATOM   1524  O   SER B  48     -39.456  -0.527 -40.263  1.00 28.21           O  
ANISOU 1524  O   SER B  48     1851   6606   2262    552    180    322       O  
ATOM   1525  CB  SER B  48     -36.467  -1.187 -41.491  1.00 30.23           C  
ANISOU 1525  CB  SER B  48     1883   7300   2301    613    195    195       C  
ATOM   1526  OG  SER B  48     -36.290  -0.243 -40.451  1.00 28.54           O  
ANISOU 1526  OG  SER B  48     1775   6850   2217    543    204    369       O  
ATOM   1527  N   ALA B  49     -39.055  -2.726 -40.580  1.00 28.99           N  
ANISOU 1527  N   ALA B  49     1946   6756   2311    612    149    -74       N  
ATOM   1528  CA  ALA B  49     -39.869  -3.185 -39.472  1.00 27.97           C  
ANISOU 1528  CA  ALA B  49     1969   6338   2321    576    131   -137       C  
ATOM   1529  C   ALA B  49     -39.188  -4.421 -38.896  1.00 27.86           C  
ANISOU 1529  C   ALA B  49     2065   6155   2366    619    108   -339       C  
ATOM   1530  O   ALA B  49     -38.705  -5.279 -39.647  1.00 29.71           O  
ANISOU 1530  O   ALA B  49     2260   6525   2503    682     94   -509       O  
ATOM   1531  CB  ALA B  49     -41.293  -3.504 -39.949  1.00 28.53           C  
ANISOU 1531  CB  ALA B  49     2009   6501   2332    530    120   -196       C  
ATOM   1532  N   LYS B  50     -39.088  -4.489 -37.574  1.00 26.01           N  
ANISOU 1532  N   LYS B  50     1970   5632   2279    604    101   -319       N  
ATOM   1533  CA  LYS B  50     -38.452  -5.629 -36.934  1.00 26.05           C  
ANISOU 1533  CA  LYS B  50     2101   5454   2342    662     75   -486       C  
ATOM   1534  C   LYS B  50     -39.284  -6.133 -35.763  1.00 25.21           C  
ANISOU 1534  C   LYS B  50     2164   5051   2363    593     55   -519       C  
ATOM   1535  O   LYS B  50     -39.521  -5.397 -34.812  1.00 23.94           O  
ANISOU 1535  O   LYS B  50     2041   4753   2301    548     69   -379       O  
ATOM   1536  CB  LYS B  50     -37.037  -5.261 -36.468  1.00 25.86           C  
ANISOU 1536  CB  LYS B  50     2058   5426   2342    735     85   -423       C  
ATOM   1537  CG  LYS B  50     -36.223  -6.436 -35.954  1.00 26.60           C  
ANISOU 1537  CG  LYS B  50     2260   5386   2462    847     56   -594       C  
ATOM   1538  CD  LYS B  50     -34.732  -6.151 -36.030  1.00 28.61           C  
ANISOU 1538  CD  LYS B  50     2411   5805   2655    946     67   -566       C  
ATOM   1539  CE  LYS B  50     -33.932  -7.340 -35.532  1.00 30.05           C  
ANISOU 1539  CE  LYS B  50     2699   5873   2846   1103     33   -739       C  
ATOM   1540  NZ  LYS B  50     -32.473  -7.041 -35.413  1.00 32.42           N  
ANISOU 1540  NZ  LYS B  50     2883   6355   3081   1203     43   -704       N  
ATOM   1541  N   LEU B  51     -39.730  -7.385 -35.841  1.00 25.87           N  
ANISOU 1541  N   LEU B  51     2354   5040   2435    575     23   -706       N  
ATOM   1542  CA  LEU B  51     -40.366  -8.021 -34.701  1.00 25.57           C  
ANISOU 1542  CA  LEU B  51     2492   4717   2506    495      1   -742       C  
ATOM   1543  C   LEU B  51     -39.281  -8.505 -33.757  1.00 25.40           C  
ANISOU 1543  C   LEU B  51     2599   4482   2568    594    -15   -773       C  
ATOM   1544  O   LEU B  51     -38.322  -9.154 -34.188  1.00 26.06           O  
ANISOU 1544  O   LEU B  51     2702   4600   2600    724    -32   -894       O  
ATOM   1545  CB  LEU B  51     -41.251  -9.183 -35.146  1.00 26.85           C  
ANISOU 1545  CB  LEU B  51     2741   4846   2614    404    -32   -923       C  
ATOM   1546  CG  LEU B  51     -42.000  -9.900 -34.020  1.00 27.26           C  
ANISOU 1546  CG  LEU B  51     2980   4619   2758    279    -57   -953       C  
ATOM   1547  CD1 LEU B  51     -42.974  -8.956 -33.315  1.00 26.44           C  
ANISOU 1547  CD1 LEU B  51     2806   4537   2701    172    -30   -780       C  
ATOM   1548  CD2 LEU B  51     -42.728 -11.105 -34.580  1.00 29.42           C  
ANISOU 1548  CD2 LEU B  51     3356   4862   2961    166    -94  -1146       C  
ATOM   1549  N   ILE B  52     -39.413  -8.182 -32.472  1.00 24.32           N  
ANISOU 1549  N   ILE B  52     2543   4151   2548    551    -11   -666       N  
ATOM   1550  CA  ILE B  52     -38.389  -8.579 -31.502  1.00 24.21           C  
ANISOU 1550  CA  ILE B  52     2639   3956   2605    648    -27   -678       C  
ATOM   1551  C   ILE B  52     -38.700  -9.951 -30.901  1.00 25.43           C  
ANISOU 1551  C   ILE B  52     3014   3846   2802    631    -70   -808       C  
ATOM   1552  O   ILE B  52     -39.814 -10.202 -30.427  1.00 25.05           O  
ANISOU 1552  O   ILE B  52     3049   3675   2792    480    -78   -797       O  
ATOM   1553  CB  ILE B  52     -38.158  -7.485 -30.409  1.00 22.79           C  
ANISOU 1553  CB  ILE B  52     2427   3716   2515    624     -1   -498       C  
ATOM   1554  CG1 ILE B  52     -37.816  -6.130 -31.058  1.00 22.78           C  
ANISOU 1554  CG1 ILE B  52     2245   3945   2467    625     36   -366       C  
ATOM   1555  CG2 ILE B  52     -37.081  -7.899 -29.392  1.00 21.99           C  
ANISOU 1555  CG2 ILE B  52     2420   3466   2471    725    -19   -510       C  
ATOM   1556  CD1 ILE B  52     -36.717  -6.152 -32.113  1.00 20.93           C  
ANISOU 1556  CD1 ILE B  52     1892   3938   2122    728     41   -414       C  
ATOM   1557  N   ARG B  53     -37.705 -10.837 -30.942  1.00 26.51           N  
ANISOU 1557  N   ARG B  53     3248   3906   2917    788   -101   -928       N  
ATOM   1558  CA  ARG B  53     -37.860 -12.181 -30.424  1.00 28.44           C  
ANISOU 1558  CA  ARG B  53     3742   3869   3196    796   -149  -1049       C  
ATOM   1559  C   ARG B  53     -36.929 -12.446 -29.249  1.00 28.45           C  
ANISOU 1559  C   ARG B  53     3854   3691   3265    927   -167  -1006       C  
ATOM   1560  O   ARG B  53     -35.935 -11.751 -29.062  1.00 27.89           O  
ANISOU 1560  O   ARG B  53     3651   3758   3187   1045   -146   -930       O  
ATOM   1561  CB  ARG B  53     -37.621 -13.226 -31.529  1.00 30.58           C  
ANISOU 1561  CB  ARG B  53     4090   4162   3369    895   -184  -1263       C  
ATOM   1562  CG  ARG B  53     -38.538 -13.068 -32.716  1.00 31.20           C  
ANISOU 1562  CG  ARG B  53     4058   4435   3362    764   -172  -1324       C  
ATOM   1563  CD  ARG B  53     -38.293 -14.098 -33.799  1.00 33.86           C  
ANISOU 1563  CD  ARG B  53     4473   4798   3593    860   -208  -1554       C  
ATOM   1564  NE  ARG B  53     -39.347 -13.985 -34.799  1.00 36.11           N  
ANISOU 1564  NE  ARG B  53     4661   5263   3796    694   -199  -1608       N  
ATOM   1565  CZ  ARG B  53     -40.538 -14.570 -34.715  1.00 35.36           C  
ANISOU 1565  CZ  ARG B  53     4691   5036   3707    479   -222  -1667       C  
ATOM   1566  NH1 ARG B  53     -40.842 -15.353 -33.688  1.00 36.34           N  
ANISOU 1566  NH1 ARG B  53     5063   4824   3918    391   -257  -1677       N  
ATOM   1567  NH2 ARG B  53     -41.424 -14.376 -35.671  1.00 36.44           N  
ANISOU 1567  NH2 ARG B  53     4698   5401   3749    341   -212  -1711       N  
ATOM   1568  N   ASP B  54     -37.266 -13.475 -28.477  1.00 29.67           N  
ANISOU 1568  N   ASP B  54     4253   3548   3472    894   -208  -1051       N  
ATOM   1569  CA  ASP B  54     -36.477 -13.917 -27.330  1.00 30.24           C  
ANISOU 1569  CA  ASP B  54     4465   3426   3598   1025   -234  -1014       C  
ATOM   1570  C   ASP B  54     -35.110 -14.428 -27.792  1.00 31.64           C  
ANISOU 1570  C   ASP B  54     4651   3671   3702   1314   -259  -1128       C  
ATOM   1571  O   ASP B  54     -35.017 -15.234 -28.708  1.00 32.83           O  
ANISOU 1571  O   ASP B  54     4885   3809   3780   1406   -288  -1297       O  
ATOM   1572  CB  ASP B  54     -37.263 -14.996 -26.560  1.00 31.53           C  
ANISOU 1572  CB  ASP B  54     4913   3252   3816    902   -278  -1036       C  
ATOM   1573  CG  ASP B  54     -36.426 -15.728 -25.511  1.00 33.53           C  
ANISOU 1573  CG  ASP B  54     5361   3275   4105   1072   -318  -1019       C  
ATOM   1574  OD1 ASP B  54     -35.506 -15.127 -24.915  1.00 36.12           O  
ANISOU 1574  OD1 ASP B  54     5571   3709   4445   1212   -301   -929       O  
ATOM   1575  OD2 ASP B  54     -36.712 -16.914 -25.265  1.00 35.13           O  
ANISOU 1575  OD2 ASP B  54     5845   3187   4316   1056   -370  -1091       O  
ATOM   1576  N   LYS B  55     -34.058 -13.933 -27.145  1.00 31.45           N  
ANISOU 1576  N   LYS B  55     4527   3740   3681   1457   -247  -1041       N  
ATOM   1577  CA  LYS B  55     -32.682 -14.279 -27.479  1.00 32.65           C  
ANISOU 1577  CA  LYS B  55     4635   4029   3743   1746   -265  -1130       C  
ATOM   1578  C   LYS B  55     -32.365 -15.735 -27.181  1.00 35.07           C  
ANISOU 1578  C   LYS B  55     5230   4056   4037   1942   -332  -1258       C  
ATOM   1579  O   LYS B  55     -31.477 -16.317 -27.817  1.00 37.03           O  
ANISOU 1579  O   LYS B  55     5487   4397   4184   2203   -358  -1399       O  
ATOM   1580  CB  LYS B  55     -31.709 -13.378 -26.718  1.00 32.09           C  
ANISOU 1580  CB  LYS B  55     4384   4137   3671   1812   -238   -994       C  
ATOM   1581  N   VAL B  56     -33.092 -16.323 -26.226  1.00 34.97           N  
ANISOU 1581  N   VAL B  56     5461   3709   4118   1823   -360  -1208       N  
ATOM   1582  CA  VAL B  56     -32.860 -17.726 -25.825  1.00 36.99           C  
ANISOU 1582  CA  VAL B  56     6046   3636   4372   1990   -430  -1303       C  
ATOM   1583  C   VAL B  56     -33.627 -18.731 -26.682  1.00 38.59           C  
ANISOU 1583  C   VAL B  56     6478   3633   4553   1919   -469  -1476       C  
ATOM   1584  O   VAL B  56     -33.015 -19.620 -27.274  1.00 41.31           O  
ANISOU 1584  O   VAL B  56     6966   3909   4822   2164   -515  -1648       O  
ATOM   1585  CB  VAL B  56     -33.176 -17.995 -24.317  1.00 36.77           C  
ANISOU 1585  CB  VAL B  56     6203   3328   4438   1902   -450  -1155       C  
ATOM   1586  CG1 VAL B  56     -32.926 -19.474 -23.962  1.00 39.16           C  
ANISOU 1586  CG1 VAL B  56     6882   3266   4732   2082   -528  -1241       C  
ATOM   1587  CG2 VAL B  56     -32.366 -17.080 -23.416  1.00 34.89           C  
ANISOU 1587  CG2 VAL B  56     5757   3289   4212   1981   -418  -1004       C  
ATOM   1588  N   ALA B  57     -34.953 -18.592 -26.738  1.00 37.31           N  
ANISOU 1588  N   ALA B  57     6347   3385   4444   1589   -454  -1439       N  
ATOM   1589  CA  ALA B  57     -35.805 -19.572 -27.420  1.00 38.91           C  
ANISOU 1589  CA  ALA B  57     6782   3377   4624   1456   -494  -1595       C  
ATOM   1590  C   ALA B  57     -36.606 -19.028 -28.609  1.00 37.85           C  
ANISOU 1590  C   ALA B  57     6449   3493   4440   1263   -457  -1662       C  
ATOM   1591  O   ALA B  57     -37.492 -19.708 -29.128  1.00 39.28           O  
ANISOU 1591  O   ALA B  57     6788   3539   4598   1083   -484  -1778       O  
ATOM   1592  CB  ALA B  57     -36.725 -20.262 -26.426  1.00 39.75           C  
ANISOU 1592  CB  ALA B  57     7175   3120   4807   1222   -528  -1519       C  
ATOM   1593  N   GLY B  58     -36.297 -17.802 -29.020  1.00 35.64           N  
ANISOU 1593  N   GLY B  58     5829   3580   4135   1290   -397  -1583       N  
ATOM   1594  CA  GLY B  58     -36.756 -17.258 -30.300  1.00 34.93           C  
ANISOU 1594  CA  GLY B  58     5524   3779   3967   1195   -364  -1649       C  
ATOM   1595  C   GLY B  58     -38.222 -16.930 -30.499  1.00 34.08           C  
ANISOU 1595  C   GLY B  58     5366   3709   3874    865   -342  -1604       C  
ATOM   1596  O   GLY B  58     -38.625 -16.585 -31.615  1.00 33.95           O  
ANISOU 1596  O   GLY B  58     5186   3935   3778    800   -321  -1670       O  
ATOM   1597  N   HIS B  59     -39.030 -17.044 -29.448  1.00 33.37           N  
ANISOU 1597  N   HIS B  59     5399   3413   3867    662   -348  -1494       N  
ATOM   1598  CA  HIS B  59     -40.430 -16.629 -29.541  1.00 32.86           C  
ANISOU 1598  CA  HIS B  59     5243   3443   3799    357   -323  -1434       C  
ATOM   1599  C   HIS B  59     -40.560 -15.110 -29.569  1.00 30.32           C  
ANISOU 1599  C   HIS B  59     4602   3433   3487    338   -257  -1270       C  
ATOM   1600  O   HIS B  59     -39.728 -14.400 -29.007  1.00 28.81           O  
ANISOU 1600  O   HIS B  59     4315   3291   3342    482   -233  -1156       O  
ATOM   1601  CB  HIS B  59     -41.285 -17.201 -28.400  1.00 33.34           C  
ANISOU 1601  CB  HIS B  59     5513   3232   3924    133   -347  -1361       C  
ATOM   1602  CG  HIS B  59     -42.757 -17.113 -28.665  1.00 34.58           C  
ANISOU 1602  CG  HIS B  59     5607   3495   4036   -184   -335  -1356       C  
ATOM   1603  ND1 HIS B  59     -43.504 -15.987 -28.379  1.00 33.46           N  
ANISOU 1603  ND1 HIS B  59     5222   3591   3900   -307   -284  -1204       N  
ATOM   1604  CD2 HIS B  59     -43.613 -17.994 -29.236  1.00 36.68           C  
ANISOU 1604  CD2 HIS B  59     6012   3690   4235   -397   -371  -1494       C  
ATOM   1605  CE1 HIS B  59     -44.759 -16.189 -28.740  1.00 33.20           C  
ANISOU 1605  CE1 HIS B  59     5162   3654   3798   -568   -286  -1242       C  
ATOM   1606  NE2 HIS B  59     -44.850 -17.397 -29.270  1.00 36.32           N  
ANISOU 1606  NE2 HIS B  59     5782   3872   4147   -647   -338  -1417       N  
ATOM   1607  N   SER B  60     -41.607 -14.620 -30.230  1.00 30.14           N  
ANISOU 1607  N   SER B  60     4425   3618   3408    161   -232  -1260       N  
ATOM   1608  CA  SER B  60     -41.922 -13.193 -30.237  1.00 27.78           C  
ANISOU 1608  CA  SER B  60     3861   3579   3113    133   -177  -1097       C  
ATOM   1609  C   SER B  60     -42.068 -12.616 -28.831  1.00 26.11           C  
ANISOU 1609  C   SER B  60     3656   3264   3001     89   -158   -924       C  
ATOM   1610  O   SER B  60     -42.636 -13.253 -27.934  1.00 26.77           O  
ANISOU 1610  O   SER B  60     3901   3145   3124    -47   -180   -910       O  
ATOM   1611  CB  SER B  60     -43.204 -12.929 -31.028  1.00 28.06           C  
ANISOU 1611  CB  SER B  60     3764   3833   3063    -55   -162  -1115       C  
ATOM   1612  OG  SER B  60     -43.691 -11.629 -30.747  1.00 26.55           O  
ANISOU 1612  OG  SER B  60     3373   3827   2887    -84   -116   -941       O  
ATOM   1613  N   LEU B  61     -41.567 -11.401 -28.648  1.00 23.91           N  
ANISOU 1613  N   LEU B  61     3205   3128   2751    189   -118   -793       N  
ATOM   1614  CA  LEU B  61     -41.721 -10.705 -27.379  1.00 22.52           C  
ANISOU 1614  CA  LEU B  61     3014   2886   2657    154    -98   -639       C  
ATOM   1615  C   LEU B  61     -42.954  -9.808 -27.388  1.00 21.88           C  
ANISOU 1615  C   LEU B  61     2787   2974   2553     18    -66   -545       C  
ATOM   1616  O   LEU B  61     -43.217  -9.075 -26.423  1.00 21.20           O  
ANISOU 1616  O   LEU B  61     2663   2872   2518     -4    -45   -423       O  
ATOM   1617  CB  LEU B  61     -40.449  -9.931 -27.023  1.00 21.14           C  
ANISOU 1617  CB  LEU B  61     2767   2740   2525    327    -79   -558       C  
ATOM   1618  CG  LEU B  61     -39.255 -10.847 -26.744  1.00 22.07           C  
ANISOU 1618  CG  LEU B  61     3026   2703   2658    483   -113   -639       C  
ATOM   1619  CD1 LEU B  61     -37.983 -10.053 -26.485  1.00 22.37           C  
ANISOU 1619  CD1 LEU B  61     2953   2838   2709    636    -94   -565       C  
ATOM   1620  CD2 LEU B  61     -39.545 -11.770 -25.568  1.00 24.24           C  
ANISOU 1620  CD2 LEU B  61     3517   2703   2991    421   -147   -637       C  
ATOM   1621  N   GLY B  62     -43.713  -9.904 -28.473  1.00 22.20           N  
ANISOU 1621  N   GLY B  62     2746   3187   2503    -59    -65   -611       N  
ATOM   1622  CA  GLY B  62     -44.929  -9.126 -28.658  1.00 22.56           C  
ANISOU 1622  CA  GLY B  62     2636   3440   2494   -161    -39   -536       C  
ATOM   1623  C   GLY B  62     -44.712  -7.633 -28.817  1.00 20.85           C  
ANISOU 1623  C   GLY B  62     2253   3384   2286    -43      1   -397       C  
ATOM   1624  O   GLY B  62     -45.584  -6.828 -28.458  1.00 20.57           O  
ANISOU 1624  O   GLY B  62     2127   3450   2238    -78     21   -299       O  
ATOM   1625  N   TYR B  63     -43.541  -7.258 -29.326  1.00 20.38           N  
ANISOU 1625  N   TYR B  63     2161   3347   2237     98      9   -388       N  
ATOM   1626  CA  TYR B  63     -43.260  -5.860 -29.643  1.00 19.27           C  
ANISOU 1626  CA  TYR B  63     1884   3348   2091    187     41   -254       C  
ATOM   1627  C   TYR B  63     -42.281  -5.800 -30.801  1.00 19.65           C  
ANISOU 1627  C   TYR B  63     1861   3526   2078    282     45   -290       C  
ATOM   1628  O   TYR B  63     -41.569  -6.768 -31.081  1.00 20.61           O  
ANISOU 1628  O   TYR B  63     2050   3594   2186    323     22   -416       O  
ATOM   1629  CB  TYR B  63     -42.779  -5.045 -28.414  1.00 17.73           C  
ANISOU 1629  CB  TYR B  63     1727   3012   1996    230     56   -134       C  
ATOM   1630  CG  TYR B  63     -41.314  -5.210 -28.012  1.00 17.26           C  
ANISOU 1630  CG  TYR B  63     1730   2837   1993    315     49   -146       C  
ATOM   1631  CD1 TYR B  63     -40.919  -6.221 -27.146  1.00 18.53           C  
ANISOU 1631  CD1 TYR B  63     2027   2806   2206    315     23   -216       C  
ATOM   1632  CD2 TYR B  63     -40.337  -4.324 -28.472  1.00 18.03           C  
ANISOU 1632  CD2 TYR B  63     1744   3032   2075    391     67    -74       C  
ATOM   1633  CE1 TYR B  63     -39.576  -6.373 -26.764  1.00 18.04           C  
ANISOU 1633  CE1 TYR B  63     2003   2674   2175    417     15   -226       C  
ATOM   1634  CE2 TYR B  63     -38.999  -4.460 -28.103  1.00 16.67           C  
ANISOU 1634  CE2 TYR B  63     1596   2807   1929    461     61    -86       C  
ATOM   1635  CZ  TYR B  63     -38.630  -5.492 -27.248  1.00 18.89           C  
ANISOU 1635  CZ  TYR B  63     1999   2919   2257    487     35   -166       C  
ATOM   1636  OH  TYR B  63     -37.317  -5.645 -26.881  1.00 21.71           O  
ANISOU 1636  OH  TYR B  63     2366   3261   2622    579     27   -179       O  
ATOM   1637  N   GLY B  64     -42.270  -4.665 -31.481  1.00 19.16           N  
ANISOU 1637  N   GLY B  64     1668   3641   1969    324     70   -178       N  
ATOM   1638  CA  GLY B  64     -41.359  -4.458 -32.597  1.00 19.62           C  
ANISOU 1638  CA  GLY B  64     1635   3869   1952    398     78   -183       C  
ATOM   1639  C   GLY B  64     -41.157  -2.990 -32.878  1.00 19.16           C  
ANISOU 1639  C   GLY B  64     1483   3919   1878    428    107     -2       C  
ATOM   1640  O   GLY B  64     -41.738  -2.128 -32.211  1.00 18.38           O  
ANISOU 1640  O   GLY B  64     1406   3745   1832    412    118    117       O  
ATOM   1641  N   PHE B  65     -40.335  -2.714 -33.883  1.00 19.95           N  
ANISOU 1641  N   PHE B  65     1487   4198   1895    472    117     19       N  
ATOM   1642  CA  PHE B  65     -40.013  -1.353 -34.270  1.00 20.14           C  
ANISOU 1642  CA  PHE B  65     1440   4322   1889    479    140    202       C  
ATOM   1643  C   PHE B  65     -40.401  -1.153 -35.728  1.00 21.40           C  
ANISOU 1643  C   PHE B  65     1466   4759   1906    492    148    226       C  
ATOM   1644  O   PHE B  65     -40.178  -2.027 -36.567  1.00 22.10           O  
ANISOU 1644  O   PHE B  65     1489   5001   1905    512    139     89       O  
ATOM   1645  CB  PHE B  65     -38.512  -1.075 -34.112  1.00 19.59           C  
ANISOU 1645  CB  PHE B  65     1360   4255   1828    492    148    239       C  
ATOM   1646  CG  PHE B  65     -38.043  -1.002 -32.683  1.00 18.82           C  
ANISOU 1646  CG  PHE B  65     1375   3919   1856    478    143    251       C  
ATOM   1647  CD1 PHE B  65     -38.095   0.199 -31.978  1.00 17.76           C  
ANISOU 1647  CD1 PHE B  65     1295   3664   1789    434    155    404       C  
ATOM   1648  CD2 PHE B  65     -37.517  -2.126 -32.050  1.00 18.65           C  
ANISOU 1648  CD2 PHE B  65     1416   3793   1877    517    123    108       C  
ATOM   1649  CE1 PHE B  65     -37.655   0.280 -30.655  1.00 17.34           C  
ANISOU 1649  CE1 PHE B  65     1337   3413   1840    415    150    406       C  
ATOM   1650  CE2 PHE B  65     -37.062  -2.057 -30.715  1.00 17.91           C  
ANISOU 1650  CE2 PHE B  65     1415   3505   1886    509    118    126       C  
ATOM   1651  CZ  PHE B  65     -37.139  -0.850 -30.022  1.00 17.98           C  
ANISOU 1651  CZ  PHE B  65     1456   3420   1957    451    132    271       C  
ATOM   1652  N   VAL B  66     -40.987   0.002 -36.014  1.00 22.10           N  
ANISOU 1652  N   VAL B  66     1522   4908   1966    495    161    397       N  
ATOM   1653  CA  VAL B  66     -41.348   0.374 -37.377  1.00 24.15           C  
ANISOU 1653  CA  VAL B  66     1653   5444   2081    516    169    461       C  
ATOM   1654  C   VAL B  66     -40.781   1.761 -37.662  1.00 24.76           C  
ANISOU 1654  C   VAL B  66     1724   5549   2134    515    186    685       C  
ATOM   1655  O   VAL B  66     -41.139   2.740 -37.003  1.00 24.11           O  
ANISOU 1655  O   VAL B  66     1737   5299   2123    522    189    826       O  
ATOM   1656  CB  VAL B  66     -42.882   0.376 -37.593  1.00 24.54           C  
ANISOU 1656  CB  VAL B  66     1665   5576   2082    532    162    460       C  
ATOM   1657  CG1 VAL B  66     -43.206   0.586 -39.076  1.00 26.62           C  
ANISOU 1657  CG1 VAL B  66     1775   6165   2173    561    166    504       C  
ATOM   1658  CG2 VAL B  66     -43.507  -0.920 -37.090  1.00 24.51           C  
ANISOU 1658  CG2 VAL B  66     1700   5500   2114    484    143    256       C  
ATOM   1659  N   ASN B  67     -39.880   1.822 -38.639  1.00 26.57           N  
ANISOU 1659  N   ASN B  67     1850   5991   2255    500    196    712       N  
ATOM   1660  CA  ASN B  67     -39.276   3.071 -39.085  1.00 28.21           C  
ANISOU 1660  CA  ASN B  67     2046   6261   2410    462    211    933       C  
ATOM   1661  C   ASN B  67     -39.806   3.407 -40.475  1.00 29.93           C  
ANISOU 1661  C   ASN B  67     2139   6769   2464    493    216   1025       C  
ATOM   1662  O   ASN B  67     -39.635   2.640 -41.426  1.00 30.77           O  
ANISOU 1662  O   ASN B  67     2104   7140   2448    508    217    908       O  
ATOM   1663  CB  ASN B  67     -37.746   2.946 -39.114  1.00 28.57           C  
ANISOU 1663  CB  ASN B  67     2047   6377   2432    399    221    916       C  
ATOM   1664  CG  ASN B  67     -37.048   4.283 -39.357  1.00 29.88           C  
ANISOU 1664  CG  ASN B  67     2231   6568   2556    305    235   1156       C  
ATOM   1665  OD1 ASN B  67     -37.347   5.272 -38.703  1.00 31.11           O  
ANISOU 1665  OD1 ASN B  67     2530   6491   2798    273    232   1303       O  
ATOM   1666  ND2 ASN B  67     -36.103   4.305 -40.299  1.00 31.82           N  
ANISOU 1666  ND2 ASN B  67     2335   7097   2657    253    248   1193       N  
ATOM   1667  N   TYR B  68     -40.468   4.551 -40.583  1.00 31.02           N  
ANISOU 1667  N   TYR B  68     2336   6859   2591    519    217   1229       N  
ATOM   1668  CA  TYR B  68     -41.055   4.970 -41.845  1.00 32.59           C  
ANISOU 1668  CA  TYR B  68     2425   7328   2628    568    218   1346       C  
ATOM   1669  C   TYR B  68     -40.020   5.701 -42.674  1.00 34.22           C  
ANISOU 1669  C   TYR B  68     2584   7691   2727    491    232   1522       C  
ATOM   1670  O   TYR B  68     -38.982   6.117 -42.156  1.00 34.19           O  
ANISOU 1670  O   TYR B  68     2655   7550   2784    394    240   1587       O  
ATOM   1671  CB  TYR B  68     -42.259   5.875 -41.586  1.00 32.52           C  
ANISOU 1671  CB  TYR B  68     2511   7203   2642    663    208   1495       C  
ATOM   1672  CG  TYR B  68     -43.524   5.115 -41.287  1.00 32.01           C  
ANISOU 1672  CG  TYR B  68     2403   7169   2589    740    195   1335       C  
ATOM   1673  CD1 TYR B  68     -43.857   4.761 -39.976  1.00 30.16           C  
ANISOU 1673  CD1 TYR B  68     2278   6676   2506    738    189   1224       C  
ATOM   1674  CD2 TYR B  68     -44.386   4.739 -42.312  1.00 31.46           C  
ANISOU 1674  CD2 TYR B  68     2175   7415   2364    795    190   1296       C  
ATOM   1675  CE1 TYR B  68     -45.015   4.051 -39.702  1.00 30.01           C  
ANISOU 1675  CE1 TYR B  68     2210   6712   2480    775    178   1087       C  
ATOM   1676  CE2 TYR B  68     -45.548   4.036 -42.053  1.00 31.94           C  
ANISOU 1676  CE2 TYR B  68     2183   7536   2416    829    178   1149       C  
ATOM   1677  CZ  TYR B  68     -45.863   3.697 -40.746  1.00 30.46           C  
ANISOU 1677  CZ  TYR B  68     2107   7089   2378    812    172   1049       C  
ATOM   1678  OH  TYR B  68     -47.010   3.002 -40.489  1.00 30.23           O  
ANISOU 1678  OH  TYR B  68     2018   7145   2323    816    161    914       O  
ATOM   1679  N   VAL B  69     -40.303   5.849 -43.964  1.00 35.95           N  
ANISOU 1679  N   VAL B  69     2665   8224   2769    522    236   1602       N  
ATOM   1680  CA  VAL B  69     -39.510   6.731 -44.811  1.00 37.91           C  
ANISOU 1680  CA  VAL B  69     2876   8634   2892    443    248   1825       C  
ATOM   1681  C   VAL B  69     -39.735   8.174 -44.356  1.00 38.72           C  
ANISOU 1681  C   VAL B  69     3187   8462   3063    432    241   2095       C  
ATOM   1682  O   VAL B  69     -38.782   8.946 -44.236  1.00 39.31           O  
ANISOU 1682  O   VAL B  69     3346   8444   3145    299    247   2254       O  
ATOM   1683  CB  VAL B  69     -39.867   6.575 -46.306  1.00 39.18           C  
ANISOU 1683  CB  VAL B  69     2841   9211   2835    490    251   1859       C  
ATOM   1684  N   THR B  70     -40.996   8.511 -44.065  1.00 38.68           N  
ANISOU 1684  N   THR B  70     3269   8327   3101    571    224   2135       N  
ATOM   1685  CA  THR B  70     -41.394   9.886 -43.753  1.00 39.77           C  
ANISOU 1685  CA  THR B  70     3617   8212   3280    618    210   2385       C  
ATOM   1686  C   THR B  70     -41.850  10.058 -42.304  1.00 38.64           C  
ANISOU 1686  C   THR B  70     3663   7688   3330    675    198   2315       C  
ATOM   1687  O   THR B  70     -42.571   9.206 -41.771  1.00 37.30           O  
ANISOU 1687  O   THR B  70     3436   7517   3220    755    195   2114       O  
ATOM   1688  CB  THR B  70     -42.528  10.358 -44.691  1.00 41.61           C  
ANISOU 1688  CB  THR B  70     3802   8641   3369    782    198   2530       C  
ATOM   1689  N   ALA B  71     -41.441  11.163 -41.675  1.00 38.95           N  
ANISOU 1689  N   ALA B  71     3931   7412   3456    623    190   2481       N  
ATOM   1690  CA  ALA B  71     -41.863  11.476 -40.305  1.00 37.71           C  
ANISOU 1690  CA  ALA B  71     3967   6894   3469    686    177   2428       C  
ATOM   1691  C   ALA B  71     -43.370  11.722 -40.211  1.00 38.31           C  
ANISOU 1691  C   ALA B  71     4073   6956   3526    926    159   2443       C  
ATOM   1692  O   ALA B  71     -44.012  11.360 -39.213  1.00 36.97           O  
ANISOU 1692  O   ALA B  71     3934   6655   3458   1010    154   2296       O  
ATOM   1693  CB  ALA B  71     -41.098  12.672 -39.775  1.00 38.81           C  
ANISOU 1693  CB  ALA B  71     4355   6710   3680    570    168   2604       C  
ATOM   1694  N   LYS B  72     -43.925  12.338 -41.256  1.00 40.08           N  
ANISOU 1694  N   LYS B  72     4276   7347   3605   1039    149   2628       N  
ATOM   1695  CA  LYS B  72     -45.355  12.572 -41.349  1.00 40.89           C  
ANISOU 1695  CA  LYS B  72     4366   7524   3646   1289    131   2656       C  
ATOM   1696  C   LYS B  72     -46.144  11.268 -41.296  1.00 39.34           C  
ANISOU 1696  C   LYS B  72     3935   7589   3423   1335    139   2407       C  
ATOM   1697  O   LYS B  72     -47.183  11.202 -40.644  1.00 39.20           O  
ANISOU 1697  O   LYS B  72     3925   7536   3432   1485    129   2330       O  
ATOM   1698  N   ASP B  73     -45.654  10.239 -41.984  1.00 38.89           N  
ANISOU 1698  N   ASP B  73     3676   7800   3302   1203    157   2278       N  
ATOM   1699  CA  ASP B  73     -46.306   8.926 -41.970  1.00 38.21           C  
ANISOU 1699  CA  ASP B  73     3393   7936   3188   1204    161   2029       C  
ATOM   1700  C   ASP B  73     -46.195   8.277 -40.578  1.00 36.15           C  
ANISOU 1700  C   ASP B  73     3209   7421   3106   1138    164   1834       C  
ATOM   1701  O   ASP B  73     -47.119   7.595 -40.128  1.00 35.64           O  
ANISOU 1701  O   ASP B  73     3071   7422   3048   1184    159   1682       O  
ATOM   1702  CB  ASP B  73     -45.731   8.007 -43.065  1.00 38.39           C  
ANISOU 1702  CB  ASP B  73     3213   8280   3094   1086    174   1929       C  
ATOM   1703  CG  ASP B  73     -46.184   8.398 -44.474  1.00 41.49           C  
ANISOU 1703  CG  ASP B  73     3470   9020   3276   1171    169   2078       C  
ATOM   1704  OD1 ASP B  73     -47.405   8.434 -44.727  1.00 43.99           O  
ANISOU 1704  OD1 ASP B  73     3703   9514   3496   1316    156   2083       O  
ATOM   1705  OD2 ASP B  73     -45.316   8.649 -45.339  1.00 43.30           O  
ANISOU 1705  OD2 ASP B  73     3657   9377   3417   1090    179   2189       O  
ATOM   1706  N   ALA B  74     -45.073   8.517 -39.897  1.00 35.57           N  
ANISOU 1706  N   ALA B  74     3277   7077   3163   1021    171   1850       N  
ATOM   1707  CA  ALA B  74     -44.870   8.028 -38.531  1.00 34.13           C  
ANISOU 1707  CA  ALA B  74     3181   6640   3146    964    172   1694       C  
ATOM   1708  C   ALA B  74     -45.873   8.642 -37.551  1.00 34.40           C  
ANISOU 1708  C   ALA B  74     3340   6485   3247   1108    159   1724       C  
ATOM   1709  O   ALA B  74     -46.416   7.933 -36.706  1.00 33.24           O  
ANISOU 1709  O   ALA B  74     3166   6303   3161   1113    158   1563       O  
ATOM   1710  CB  ALA B  74     -43.434   8.261 -38.071  1.00 33.65           C  
ANISOU 1710  CB  ALA B  74     3231   6372   3184    813    181   1722       C  
ATOM   1711  N   GLU B  75     -46.144   9.945 -37.690  1.00 36.37           N  
ANISOU 1711  N   GLU B  75     3726   6624   3468   1231    147   1930       N  
ATOM   1712  CA  GLU B  75     -47.155  10.626 -36.859  1.00 36.89           C  
ANISOU 1712  CA  GLU B  75     3911   6537   3569   1419    131   1962       C  
ATOM   1713  C   GLU B  75     -48.554  10.055 -37.096  1.00 37.30           C  
ANISOU 1713  C   GLU B  75     3777   6888   3508   1561    126   1873       C  
ATOM   1714  O   GLU B  75     -49.293   9.779 -36.143  1.00 36.77           O  
ANISOU 1714  O   GLU B  75     3703   6783   3484   1624    124   1758       O  
ATOM   1715  CB  GLU B  75     -47.161  12.136 -37.121  1.00 38.89           C  
ANISOU 1715  CB  GLU B  75     4369   6613   3794   1547    112   2207       C  
ATOM   1716  N   ARG B  76     -48.898   9.891 -38.372  1.00 38.52           N  
ANISOU 1716  N   ARG B  76     3769   7364   3502   1596    126   1928       N  
ATOM   1717  CA  ARG B  76     -50.187   9.348 -38.789  1.00 39.19           C  
ANISOU 1717  CA  ARG B  76     3647   7799   3443   1704    120   1850       C  
ATOM   1718  C   ARG B  76     -50.388   7.929 -38.262  1.00 37.21           C  
ANISOU 1718  C   ARG B  76     3264   7639   3234   1549    130   1595       C  
ATOM   1719  O   ARG B  76     -51.480   7.569 -37.836  1.00 37.21           O  
ANISOU 1719  O   ARG B  76     3169   7785   3186   1613    125   1502       O  
ATOM   1720  N   ALA B  77     -49.322   7.135 -38.289  1.00 36.09           N  
ANISOU 1720  N   ALA B  77     3122   7417   3172   1347    143   1488       N  
ATOM   1721  CA  ALA B  77     -49.343   5.781 -37.737  1.00 34.46           C  
ANISOU 1721  CA  ALA B  77     2847   7223   3023   1194    147   1255       C  
ATOM   1722  C   ALA B  77     -49.718   5.782 -36.257  1.00 33.49           C  
ANISOU 1722  C   ALA B  77     2828   6874   3023   1210    145   1191       C  
ATOM   1723  O   ALA B  77     -50.493   4.926 -35.806  1.00 33.49           O  
ANISOU 1723  O   ALA B  77     2741   6982   3003   1157    143   1046       O  
ATOM   1724  CB  ALA B  77     -47.996   5.110 -37.938  1.00 33.53           C  
ANISOU 1724  CB  ALA B  77     2753   7012   2975   1026    157   1174       C  
ATOM   1725  N   ILE B  78     -49.175   6.737 -35.501  1.00 32.91           N  
ANISOU 1725  N   ILE B  78     2941   6498   3064   1267    146   1299       N  
ATOM   1726  CA  ILE B  78     -49.488   6.824 -34.077  1.00 32.09           C  
ANISOU 1726  CA  ILE B  78     2937   6186   3069   1294    144   1240       C  
ATOM   1727  C   ILE B  78     -50.955   7.213 -33.900  1.00 33.34           C  
ANISOU 1727  C   ILE B  78     3022   6526   3121   1480    135   1263       C  
ATOM   1728  O   ILE B  78     -51.641   6.679 -33.031  1.00 32.98           O  
ANISOU 1728  O   ILE B  78     2927   6519   3085   1462    135   1147       O  
ATOM   1729  CB  ILE B  78     -48.579   7.810 -33.304  1.00 31.38           C  
ANISOU 1729  CB  ILE B  78     3071   5737   3115   1309    143   1338       C  
ATOM   1730  CG1 ILE B  78     -47.117   7.363 -33.357  1.00 30.32           C  
ANISOU 1730  CG1 ILE B  78     2981   5468   3071   1118    153   1302       C  
ATOM   1731  CG2 ILE B  78     -49.032   7.915 -31.827  1.00 30.85           C  
ANISOU 1731  CG2 ILE B  78     3091   5494   3138   1359    141   1265       C  
ATOM   1732  CD1 ILE B  78     -46.147   8.379 -32.776  1.00 28.69           C  
ANISOU 1732  CD1 ILE B  78     2976   4953   2970   1095    151   1408       C  
ATOM   1733  N   ASN B  79     -51.432   8.137 -34.727  1.00 35.26           N  
ANISOU 1733  N   ASN B  79     3250   6899   3247   1664    125   1417       N  
ATOM   1734  CA  ASN B  79     -52.828   8.559 -34.637  1.00 37.05           C  
ANISOU 1734  CA  ASN B  79     3389   7342   3345   1883    114   1446       C  
ATOM   1735  C   ASN B  79     -53.803   7.498 -35.135  1.00 37.42           C  
ANISOU 1735  C   ASN B  79     3174   7803   3242   1815    115   1320       C  
ATOM   1736  O   ASN B  79     -54.891   7.356 -34.593  1.00 38.22           O  
ANISOU 1736  O   ASN B  79     3171   8086   3266   1894    112   1257       O  
ATOM   1737  CB  ASN B  79     -53.060   9.893 -35.352  1.00 38.94           C  
ANISOU 1737  CB  ASN B  79     3711   7589   3495   2131     97   1661       C  
ATOM   1738  CG  ASN B  79     -52.235  11.029 -34.761  1.00 39.69           C  
ANISOU 1738  CG  ASN B  79     4098   7253   3729   2191     90   1783       C  
ATOM   1739  OD1 ASN B  79     -51.810  11.930 -35.484  1.00 42.55           O  
ANISOU 1739  OD1 ASN B  79     4583   7518   4065   2263     79   1966       O  
ATOM   1740  ND2 ASN B  79     -51.999  10.988 -33.451  1.00 37.92           N  
ANISOU 1740  ND2 ASN B  79     3991   6773   3644   2145     94   1687       N  
ATOM   1741  N   THR B  80     -53.409   6.737 -36.148  1.00 37.16           N  
ANISOU 1741  N   THR B  80     3030   7932   3157   1658    120   1272       N  
ATOM   1742  CA  THR B  80     -54.323   5.746 -36.715  1.00 37.66           C  
ANISOU 1742  CA  THR B  80     2856   8390   3064   1571    117   1146       C  
ATOM   1743  C   THR B  80     -54.289   4.407 -35.977  1.00 36.11           C  
ANISOU 1743  C   THR B  80     2633   8147   2942   1323    122    935       C  
ATOM   1744  O   THR B  80     -55.345   3.810 -35.741  1.00 36.47           O  
ANISOU 1744  O   THR B  80     2532   8443   2884   1270    118    835       O  
ATOM   1745  CB  THR B  80     -54.051   5.506 -38.206  1.00 38.34           C  
ANISOU 1745  CB  THR B  80     2824   8715   3030   1524    115   1172       C  
ATOM   1746  OG1 THR B  80     -54.617   6.576 -38.968  1.00 41.05           O  
ANISOU 1746  OG1 THR B  80     3118   9251   3227   1767    105   1359       O  
ATOM   1747  N   LEU B  81     -53.088   3.947 -35.609  1.00 33.99           N  
ANISOU 1747  N   LEU B  81     2506   7569   2838   1171    130    877       N  
ATOM   1748  CA  LEU B  81     -52.921   2.577 -35.115  1.00 32.54           C  
ANISOU 1748  CA  LEU B  81     2321   7328   2716    936    129    684       C  
ATOM   1749  C   LEU B  81     -52.698   2.425 -33.603  1.00 31.23           C  
ANISOU 1749  C   LEU B  81     2293   6868   2705    884    133    639       C  
ATOM   1750  O   LEU B  81     -52.863   1.324 -33.068  1.00 30.85           O  
ANISOU 1750  O   LEU B  81     2239   6801   2681    704    129    497       O  
ATOM   1751  CB  LEU B  81     -51.846   1.815 -35.919  1.00 32.16           C  
ANISOU 1751  CB  LEU B  81     2292   7228   2698    796    129    606       C  
ATOM   1752  CG  LEU B  81     -51.951   1.824 -37.457  1.00 33.05           C  
ANISOU 1752  CG  LEU B  81     2258   7648   2650    821    126    629       C  
ATOM   1753  CD1 LEU B  81     -50.912   0.913 -38.092  1.00 31.94           C  
ANISOU 1753  CD1 LEU B  81     2137   7462   2535    681    125    508       C  
ATOM   1754  CD2 LEU B  81     -53.336   1.451 -37.946  1.00 34.47           C  
ANISOU 1754  CD2 LEU B  81     2240   8216   2641    805    115    567       C  
ATOM   1755  N   ASN B  82     -52.333   3.506 -32.911  1.00 30.32           N  
ANISOU 1755  N   ASN B  82     2313   6522   2686   1030    139    757       N  
ATOM   1756  CA  ASN B  82     -52.312   3.459 -31.448  1.00 29.55           C  
ANISOU 1756  CA  ASN B  82     2319   6204   2704   1005    142    715       C  
ATOM   1757  C   ASN B  82     -53.692   3.031 -30.954  1.00 30.56           C  
ANISOU 1757  C   ASN B  82     2308   6585   2719    990    139    643       C  
ATOM   1758  O   ASN B  82     -54.706   3.603 -31.362  1.00 32.13           O  
ANISOU 1758  O   ASN B  82     2381   7057   2772   1144    136    702       O  
ATOM   1759  CB  ASN B  82     -51.908   4.800 -30.808  1.00 28.91           C  
ANISOU 1759  CB  ASN B  82     2397   5874   2712   1182    144    844       C  
ATOM   1760  CG  ASN B  82     -51.610   4.670 -29.312  1.00 27.15           C  
ANISOU 1760  CG  ASN B  82     2293   5402   2622   1129    147    785       C  
ATOM   1761  OD1 ASN B  82     -50.998   3.708 -28.886  1.00 23.48           O  
ANISOU 1761  OD1 ASN B  82     1861   4820   2239    951    149    687       O  
ATOM   1762  ND2 ASN B  82     -52.039   5.643 -28.522  1.00 26.59           N  
ANISOU 1762  ND2 ASN B  82     2290   5253   2560   1300    146    842       N  
ATOM   1763  N   GLY B  83     -53.720   2.013 -30.099  1.00 29.87           N  
ANISOU 1763  N   GLY B  83     2239   6426   2686    801    139    523       N  
ATOM   1764  CA  GLY B  83     -54.966   1.512 -29.537  1.00 31.35           C  
ANISOU 1764  CA  GLY B  83     2294   6858   2761    732    137    455       C  
ATOM   1765  C   GLY B  83     -55.807   0.629 -30.444  1.00 32.63           C  
ANISOU 1765  C   GLY B  83     2272   7369   2754    584    128    370       C  
ATOM   1766  O   GLY B  83     -56.989   0.448 -30.179  1.00 34.11           O  
ANISOU 1766  O   GLY B  83     2307   7853   2801    552    127    340       O  
ATOM   1767  N   LEU B  84     -55.210   0.080 -31.506  1.00 32.61           N  
ANISOU 1767  N   LEU B  84     2277   7359   2753    487    121    325       N  
ATOM   1768  CA  LEU B  84     -55.924  -0.840 -32.401  1.00 34.32           C  
ANISOU 1768  CA  LEU B  84     2339   7890   2811    317    109    219       C  
ATOM   1769  C   LEU B  84     -56.211  -2.165 -31.710  1.00 34.63           C  
ANISOU 1769  C   LEU B  84     2411   7886   2861     29     99     77       C  
ATOM   1770  O   LEU B  84     -55.307  -2.787 -31.136  1.00 33.41           O  
ANISOU 1770  O   LEU B  84     2440   7394   2861    -79     95     25       O  
ATOM   1771  CB  LEU B  84     -55.152  -1.109 -33.701  1.00 34.16           C  
ANISOU 1771  CB  LEU B  84     2328   7867   2785    294    103    190       C  
ATOM   1772  CG  LEU B  84     -55.733  -2.183 -34.643  1.00 35.64           C  
ANISOU 1772  CG  LEU B  84     2386   8337   2819     92     86     46       C  
ATOM   1773  CD1 LEU B  84     -57.018  -1.706 -35.323  1.00 37.30           C  
ANISOU 1773  CD1 LEU B  84     2350   9020   2803    174     84     90       C  
ATOM   1774  CD2 LEU B  84     -54.716  -2.626 -35.697  1.00 35.86           C  
ANISOU 1774  CD2 LEU B  84     2471   8277   2876     56     79    -18       C  
ATOM   1775  N  AARG B  85     -57.464  -2.598 -31.781  0.70 36.08           N  
ANISOU 1775  N  AARG B  85     2419   8422   2866    -98     92     21       N  
ATOM   1776  N  BARG B  85     -57.466  -2.594 -31.806  0.30 35.97           N  
ANISOU 1776  N  BARG B  85     2403   8413   2851    -97     92     21       N  
ATOM   1777  CA AARG B  85     -57.882  -3.830 -31.131  0.70 37.13           C  
ANISOU 1777  CA AARG B  85     2582   8544   2982   -406     79    -98       C  
ATOM   1778  CA BARG B  85     -57.947  -3.823 -31.194  0.30 36.66           C  
ANISOU 1778  CA BARG B  85     2508   8513   2909   -406     79    -99       C  
ATOM   1779  C  AARG B  85     -57.792  -5.021 -32.089  0.70 37.87           C  
ANISOU 1779  C  AARG B  85     2691   8679   3018   -653     56   -246       C  
ATOM   1780  C  BARG B  85     -57.742  -5.003 -32.143  0.30 37.53           C  
ANISOU 1780  C  BARG B  85     2651   8630   2978   -644     56   -245       C  
ATOM   1781  O  AARG B  85     -58.415  -5.030 -33.149  0.70 39.47           O  
ANISOU 1781  O  AARG B  85     2719   9226   3051   -671     49   -281       O  
ATOM   1782  O  BARG B  85     -58.245  -4.987 -33.268  0.30 38.92           O  
ANISOU 1782  O  BARG B  85     2665   9124   2997   -648     49   -279       O  
ATOM   1783  CB AARG B  85     -59.288  -3.684 -30.536  0.70 38.45           C  
ANISOU 1783  CB AARG B  85     2552   9080   2976   -449     85    -80       C  
ATOM   1784  CB BARG B  85     -59.432  -3.670 -30.866  0.30 38.10           C  
ANISOU 1784  CB BARG B  85     2461   9126   2888   -446     83    -87       C  
ATOM   1785  CG AARG B  85     -59.487  -4.509 -29.277  0.70 39.55           C  
ANISOU 1785  CG AARG B  85     2778   9088   3159   -692     81   -128       C  
ATOM   1786  CG BARG B  85     -59.879  -4.374 -29.604  0.30 37.83           C  
ANISOU 1786  CG BARG B  85     2465   9048   2859   -673     81   -127       C  
ATOM   1787  CD AARG B  85     -60.707  -4.078 -28.453  0.70 41.49           C  
ANISOU 1787  CD AARG B  85     2831   9681   3251   -663     94    -79       C  
ATOM   1788  CD BARG B  85     -61.282  -3.930 -29.208  0.30 37.42           C  
ANISOU 1788  CD BARG B  85     2158   9464   2597   -636     91    -88       C  
ATOM   1789  NE AARG B  85     -60.654  -4.708 -27.135  0.70 41.64           N  
ANISOU 1789  NE AARG B  85     2967   9511   3345   -857     95    -94       N  
ATOM   1790  NE BARG B  85     -61.421  -2.476 -29.204  0.30 35.96           N  
ANISOU 1790  NE BARG B  85     1887   9385   2392   -241    108     35       N  
ATOM   1791  CZ AARG B  85     -60.268  -4.102 -26.013  0.70 41.29           C  
ANISOU 1791  CZ AARG B  85     3013   9257   3417   -697    111    -20       C  
ATOM   1792  CZ BARG B  85     -61.144  -1.700 -28.161  0.30 34.69           C  
ANISOU 1792  CZ BARG B  85     1815   9028   2338    -39    123    113       C  
ATOM   1793  NH1AARG B  85     -59.930  -2.818 -26.018  0.70 40.82           N  
ANISOU 1793  NH1AARG B  85     2955   9137   3419   -344    125     68       N  
ATOM   1794  NH1BARG B  85     -60.712  -2.237 -27.028  0.30 33.37           N  
ANISOU 1794  NH1BARG B  85     1800   8578   2300   -196    126     88       N  
ATOM   1795  NH2AARG B  85     -60.235  -4.783 -24.875  0.70 40.75           N  
ANISOU 1795  NH2AARG B  85     3043   9042   3398   -899    109    -33       N  
ATOM   1796  NH2BARG B  85     -61.299  -0.386 -28.249  0.30 34.30           N  
ANISOU 1796  NH2BARG B  85     1714   9059   2261    322    132    215       N  
ATOM   1797  N   LEU B  86     -57.010  -6.020 -31.687  1.00 37.10           N  
ANISOU 1797  N   LEU B  86     2812   8228   3056   -829     41   -336       N  
ATOM   1798  CA  LEU B  86     -56.695  -7.185 -32.519  1.00 38.14           C  
ANISOU 1798  CA  LEU B  86     3030   8296   3167  -1034     13   -494       C  
ATOM   1799  C   LEU B  86     -56.401  -8.401 -31.636  1.00 38.56           C  
ANISOU 1799  C   LEU B  86     3312   8021   3318  -1282     -9   -585       C  
ATOM   1800  O   LEU B  86     -55.500  -8.350 -30.799  1.00 36.69           O  
ANISOU 1800  O   LEU B  86     3254   7431   3256  -1196     -4   -537       O  
ATOM   1801  CB  LEU B  86     -55.470  -6.874 -33.408  1.00 37.12           C  
ANISOU 1801  CB  LEU B  86     2975   8001   3129   -841     16   -493       C  
ATOM   1802  CG  LEU B  86     -55.094  -7.808 -34.565  1.00 38.23           C  
ANISOU 1802  CG  LEU B  86     3161   8149   3217   -959    -10   -657       C  
ATOM   1803  CD1 LEU B  86     -56.198  -7.844 -35.618  1.00 40.31           C  
ANISOU 1803  CD1 LEU B  86     3191   8873   3252  -1049    -17   -713       C  
ATOM   1804  CD2 LEU B  86     -53.784  -7.378 -35.196  1.00 36.53           C  
ANISOU 1804  CD2 LEU B  86     3012   7769   3099   -741     -1   -630       C  
ATOM   1805  N   GLN B  87     -57.159  -9.487 -31.827  1.00 40.86           N  
ANISOU 1805  N   GLN B  87     3605   8431   3490  -1597    -36   -711       N  
ATOM   1806  CA  GLN B  87     -56.946 -10.761 -31.098  1.00 41.50           C  
ANISOU 1806  CA  GLN B  87     3937   8186   3645  -1866    -66   -799       C  
ATOM   1807  C   GLN B  87     -56.867 -10.586 -29.572  1.00 39.97           C  
ANISOU 1807  C   GLN B  87     3833   7793   3559  -1857    -53   -683       C  
ATOM   1808  O   GLN B  87     -55.971 -11.130 -28.925  1.00 39.07           O  
ANISOU 1808  O   GLN B  87     3968   7276   3601  -1865    -67   -691       O  
ATOM   1809  CB  GLN B  87     -55.673 -11.476 -31.594  1.00 41.12           C  
ANISOU 1809  CB  GLN B  87     4138   7758   3727  -1820    -91   -910       C  
ATOM   1810  CG  GLN B  87     -55.679 -11.903 -33.053  1.00 43.71           C  
ANISOU 1810  CG  GLN B  87     4420   8243   3946  -1866   -112  -1061       C  
ATOM   1811  CD  GLN B  87     -54.378 -12.588 -33.467  1.00 44.90           C  
ANISOU 1811  CD  GLN B  87     4815   8028   4217  -1780   -137  -1178       C  
ATOM   1812  OE1 GLN B  87     -53.607 -12.057 -34.270  1.00 44.66           O  
ANISOU 1812  OE1 GLN B  87     4727   8033   4210  -1543   -124  -1176       O  
ATOM   1813  NE2 GLN B  87     -54.124 -13.766 -32.906  1.00 46.55           N  
ANISOU 1813  NE2 GLN B  87     5302   7891   4493  -1966   -174  -1273       N  
ATOM   1814  N   SER B  88     -57.807  -9.825 -29.016  1.00 39.84           N  
ANISOU 1814  N   SER B  88     3607   8085   3446  -1825    -27   -579       N  
ATOM   1815  CA  SER B  88     -57.840  -9.484 -27.582  1.00 38.52           C  
ANISOU 1815  CA  SER B  88     3477   7807   3353  -1787     -9   -466       C  
ATOM   1816  C   SER B  88     -56.643  -8.663 -27.091  1.00 35.66           C  
ANISOU 1816  C   SER B  88     3227   7133   3188  -1474     10   -375       C  
ATOM   1817  O   SER B  88     -56.426  -8.552 -25.884  1.00 34.51           O  
ANISOU 1817  O   SER B  88     3165   6817   3129  -1455     18   -304       O  
ATOM   1818  CB  SER B  88     -58.023 -10.737 -26.706  1.00 40.01           C  
ANISOU 1818  CB  SER B  88     3851   7800   3551  -2126    -36   -507       C  
ATOM   1819  N   LYS B  89     -55.876  -8.100 -28.024  1.00 33.78           N  
ANISOU 1819  N   LYS B  89     2985   6843   3008  -1250     16   -376       N  
ATOM   1820  CA  LYS B  89     -54.806  -7.159 -27.687  1.00 31.79           C  
ANISOU 1820  CA  LYS B  89     2803   6362   2913   -965     35   -282       C  
ATOM   1821  C   LYS B  89     -55.237  -5.747 -28.064  1.00 31.08           C  
ANISOU 1821  C   LYS B  89     2514   6539   2756   -718     62   -179       C  
ATOM   1822  O   LYS B  89     -56.020  -5.560 -28.989  1.00 32.27           O  
ANISOU 1822  O   LYS B  89     2487   7020   2754   -717     63   -196       O  
ATOM   1823  CB  LYS B  89     -53.494  -7.509 -28.414  1.00 30.38           C  
ANISOU 1823  CB  LYS B  89     2779   5918   2847   -890     22   -343       C  
ATOM   1824  CG  LYS B  89     -52.890  -8.879 -28.073  1.00 31.28           C  
ANISOU 1824  CG  LYS B  89     3132   5714   3040  -1068    -11   -447       C  
ATOM   1825  CD  LYS B  89     -51.940  -8.842 -26.864  1.00 29.56           C  
ANISOU 1825  CD  LYS B  89     3086   5161   2985   -981     -9   -382       C  
ATOM   1826  CE  LYS B  89     -52.649  -9.221 -25.591  1.00 30.13           C  
ANISOU 1826  CE  LYS B  89     3197   5209   3044  -1154    -12   -339       C  
ATOM   1827  NZ  LYS B  89     -51.713  -9.475 -24.470  1.00 27.88           N  
ANISOU 1827  NZ  LYS B  89     3103   4589   2900  -1107    -19   -296       N  
ATOM   1828  N   THR B  90     -54.727  -4.761 -27.332  1.00 29.57           N  
ANISOU 1828  N   THR B  90     2364   6200   2671   -506     82    -74       N  
ATOM   1829  CA  THR B  90     -54.848  -3.354 -27.725  1.00 28.92           C  
ANISOU 1829  CA  THR B  90     2168   6261   2558   -234    101     31       C  
ATOM   1830  C   THR B  90     -53.431  -2.825 -27.967  1.00 26.53           C  
ANISOU 1830  C   THR B  90     2007   5662   2411    -77    106     78       C  
ATOM   1831  O   THR B  90     -52.723  -2.515 -27.026  1.00 24.90           O  
ANISOU 1831  O   THR B  90     1925   5202   2335    -17    112    120       O  
ATOM   1832  CB  THR B  90     -55.614  -2.536 -26.641  1.00 29.17           C  
ANISOU 1832  CB  THR B  90     2123   6408   2553   -120    117    109       C  
ATOM   1833  OG1 THR B  90     -56.951  -3.048 -26.526  1.00 32.85           O  
ANISOU 1833  OG1 THR B  90     2420   7220   2841   -278    114     65       O  
ATOM   1834  CG2 THR B  90     -55.696  -1.056 -26.992  1.00 29.28           C  
ANISOU 1834  CG2 THR B  90     2071   6510   2543    187    131    218       C  
ATOM   1835  N   ILE B  91     -53.002  -2.756 -29.227  1.00 26.18           N  
ANISOU 1835  N   ILE B  91     1933   5675   2340    -29    102     67       N  
ATOM   1836  CA  ILE B  91     -51.608  -2.377 -29.514  1.00 24.79           C  
ANISOU 1836  CA  ILE B  91     1876   5256   2289     81    106    106       C  
ATOM   1837  C   ILE B  91     -51.329  -0.930 -29.079  1.00 23.82           C  
ANISOU 1837  C   ILE B  91     1776   5048   2225    293    124    249       C  
ATOM   1838  O   ILE B  91     -52.251  -0.101 -29.023  1.00 24.64           O  
ANISOU 1838  O   ILE B  91     1784   5334   2245    413    131    322       O  
ATOM   1839  CB  ILE B  91     -51.204  -2.602 -31.009  1.00 25.20           C  
ANISOU 1839  CB  ILE B  91     1873   5426   2276     85    100     65       C  
ATOM   1840  CG1 ILE B  91     -51.873  -1.581 -31.927  1.00 26.41           C  
ANISOU 1840  CG1 ILE B  91     1867   5866   2301    233    110    165       C  
ATOM   1841  CG2 ILE B  91     -51.528  -4.034 -31.459  1.00 26.00           C  
ANISOU 1841  CG2 ILE B  91     1972   5598   2309   -126     78    -99       C  
ATOM   1842  N   LYS B  92     -50.077  -0.655 -28.719  1.00 22.37           N  
ANISOU 1842  N   LYS B  92     1729   4593   2178    336    127    282       N  
ATOM   1843  CA  LYS B  92     -49.629   0.708 -28.465  1.00 21.70           C  
ANISOU 1843  CA  LYS B  92     1698   4397   2151    506    139    410       C  
ATOM   1844  C   LYS B  92     -48.582   1.097 -29.498  1.00 21.50           C  
ANISOU 1844  C   LYS B  92     1693   4334   2141    550    142    463       C  
ATOM   1845  O   LYS B  92     -47.671   0.329 -29.795  1.00 21.68           O  
ANISOU 1845  O   LYS B  92     1753   4282   2204    464    137    392       O  
ATOM   1846  CB  LYS B  92     -49.059   0.853 -27.048  1.00 20.67           C  
ANISOU 1846  CB  LYS B  92     1699   4005   2150    499    141    414       C  
ATOM   1847  CG  LYS B  92     -48.548   2.264 -26.729  1.00 20.29           C  
ANISOU 1847  CG  LYS B  92     1735   3810   2163    647    149    531       C  
ATOM   1848  CD  LYS B  92     -48.166   2.427 -25.254  1.00 19.97           C  
ANISOU 1848  CD  LYS B  92     1805   3554   2228    638    150    519       C  
ATOM   1849  CE  LYS B  92     -47.333   3.691 -25.061  1.00 20.92           C  
ANISOU 1849  CE  LYS B  92     2041   3488   2420    733    152    613       C  
ATOM   1850  NZ  LYS B  92     -47.086   3.975 -23.621  1.00 21.77           N  
ANISOU 1850  NZ  LYS B  92     2246   3416   2610    736    152    594       N  
ATOM   1851  N   VAL B  93     -48.723   2.295 -30.047  1.00 21.68           N  
ANISOU 1851  N   VAL B  93     1696   4421   2119    692    148    592       N  
ATOM   1852  CA  VAL B  93     -47.787   2.805 -31.033  1.00 21.40           C  
ANISOU 1852  CA  VAL B  93     1675   4376   2078    724    152    672       C  
ATOM   1853  C   VAL B  93     -47.269   4.125 -30.494  1.00 21.04           C  
ANISOU 1853  C   VAL B  93     1760   4124   2109    819    156    807       C  
ATOM   1854  O   VAL B  93     -48.047   5.017 -30.203  1.00 21.46           O  
ANISOU 1854  O   VAL B  93     1836   4181   2135    950    154    886       O  
ATOM   1855  CB  VAL B  93     -48.466   3.032 -32.401  1.00 22.71           C  
ANISOU 1855  CB  VAL B  93     1704   4832   2092    789    151    724       C  
ATOM   1856  CG1 VAL B  93     -47.422   3.440 -33.456  1.00 21.99           C  
ANISOU 1856  CG1 VAL B  93     1617   4756   1982    793    156    807       C  
ATOM   1857  CG2 VAL B  93     -49.206   1.794 -32.841  1.00 23.35           C  
ANISOU 1857  CG2 VAL B  93     1657   5134   2080    683    143    578       C  
ATOM   1858  N   SER B  94     -45.958   4.226 -30.322  1.00 20.05           N  
ANISOU 1858  N   SER B  94     1725   3823   2072    752    159    822       N  
ATOM   1859  CA  SER B  94     -45.345   5.436 -29.782  1.00 20.08           C  
ANISOU 1859  CA  SER B  94     1870   3612   2149    794    160    937       C  
ATOM   1860  C   SER B  94     -43.956   5.612 -30.387  1.00 20.27           C  
ANISOU 1860  C   SER B  94     1916   3599   2186    706    165    991       C  
ATOM   1861  O   SER B  94     -43.425   4.692 -31.005  1.00 19.21           O  
ANISOU 1861  O   SER B  94     1692   3589   2020    633    168    913       O  
ATOM   1862  CB  SER B  94     -45.254   5.356 -28.254  1.00 19.44           C  
ANISOU 1862  CB  SER B  94     1885   3326   2176    772    158    872       C  
ATOM   1863  OG  SER B  94     -44.384   4.305 -27.854  1.00 18.05           O  
ANISOU 1863  OG  SER B  94     1703   3095   2060    648    158    765       O  
ATOM   1864  N   TYR B  95     -43.381   6.798 -30.216  1.00 21.30           N  
ANISOU 1864  N   TYR B  95     2171   3569   2352    711    164   1118       N  
ATOM   1865  CA  TYR B  95     -42.051   7.079 -30.738  1.00 22.53           C  
ANISOU 1865  CA  TYR B  95     2341   3715   2503    600    169   1186       C  
ATOM   1866  C   TYR B  95     -41.011   6.304 -29.951  1.00 21.66           C  
ANISOU 1866  C   TYR B  95     2229   3533   2469    491    171   1069       C  
ATOM   1867  O   TYR B  95     -41.045   6.273 -28.721  1.00 21.31           O  
ANISOU 1867  O   TYR B  95     2265   3318   2513    487    166   1011       O  
ATOM   1868  CB  TYR B  95     -41.736   8.570 -30.676  1.00 23.97           C  
ANISOU 1868  CB  TYR B  95     2685   3723   2701    600    163   1355       C  
ATOM   1869  CG  TYR B  95     -42.419   9.387 -31.751  1.00 27.44           C  
ANISOU 1869  CG  TYR B  95     3133   4252   3040    703    159   1511       C  
ATOM   1870  CD1 TYR B  95     -42.163   9.156 -33.104  1.00 30.32           C  
ANISOU 1870  CD1 TYR B  95     3369   4857   3293    670    167   1569       C  
ATOM   1871  CD2 TYR B  95     -43.321  10.391 -31.414  1.00 30.25           C  
ANISOU 1871  CD2 TYR B  95     3627   4466   3402    854    145   1598       C  
ATOM   1872  CE1 TYR B  95     -42.795   9.905 -34.095  1.00 32.74           C  
ANISOU 1872  CE1 TYR B  95     3681   5263   3495    772    161   1726       C  
ATOM   1873  CE2 TYR B  95     -43.947  11.143 -32.388  1.00 32.62           C  
ANISOU 1873  CE2 TYR B  95     3945   4848   3601    977    137   1751       C  
ATOM   1874  CZ  TYR B  95     -43.682  10.899 -33.727  1.00 34.01           C  
ANISOU 1874  CZ  TYR B  95     3989   5266   3666    930    145   1822       C  
ATOM   1875  OH  TYR B  95     -44.312  11.652 -34.698  1.00 37.52           O  
ANISOU 1875  OH  TYR B  95     4450   5808   3999   1060    135   1988       O  
ATOM   1876  N   ALA B  96     -40.105   5.663 -30.672  1.00 21.74           N  
ANISOU 1876  N   ALA B  96     2137   3694   2429    420    177   1032       N  
ATOM   1877  CA  ALA B  96     -38.999   4.968 -30.049  1.00 21.62           C  
ANISOU 1877  CA  ALA B  96     2110   3645   2461    344    176    934       C  
ATOM   1878  C   ALA B  96     -38.004   5.993 -29.560  1.00 22.32           C  
ANISOU 1878  C   ALA B  96     2288   3609   2583    246    177   1034       C  
ATOM   1879  O   ALA B  96     -37.729   6.981 -30.250  1.00 23.36           O  
ANISOU 1879  O   ALA B  96     2446   3767   2661    195    181   1178       O  
ATOM   1880  CB  ALA B  96     -38.348   4.009 -31.046  1.00 21.80           C  
ANISOU 1880  CB  ALA B  96     1990   3895   2396    330    180    857       C  
ATOM   1881  N   ARG B  97     -37.494   5.774 -28.352  1.00 22.01           N  
ANISOU 1881  N   ARG B  97     2303   3435   2625    208    171    962       N  
ATOM   1882  CA  ARG B  97     -36.410   6.588 -27.801  1.00 22.70           C  
ANISOU 1882  CA  ARG B  97     2458   3434   2734     85    169   1025       C  
ATOM   1883  C   ARG B  97     -35.079   6.022 -28.262  1.00 22.83           C  
ANISOU 1883  C   ARG B  97     2341   3654   2678      7    174    991       C  
ATOM   1884  O   ARG B  97     -35.014   4.840 -28.603  1.00 22.50           O  
ANISOU 1884  O   ARG B  97     2191   3754   2605     81    175    878       O  
ATOM   1885  CB  ARG B  97     -36.467   6.542 -26.276  1.00 21.91           C  
ANISOU 1885  CB  ARG B  97     2451   3139   2734     87    159    950       C  
ATOM   1886  CG  ARG B  97     -37.763   7.097 -25.698  1.00 22.36           C  
ANISOU 1886  CG  ARG B  97     2627   3020   2848    181    154    966       C  
ATOM   1887  CD  ARG B  97     -37.962   6.572 -24.274  1.00 19.88           C  
ANISOU 1887  CD  ARG B  97     2349   2592   2612    208    146    854       C  
ATOM   1888  NE  ARG B  97     -38.501   5.208 -24.243  1.00 17.93           N  
ANISOU 1888  NE  ARG B  97     2012   2438   2364    277    146    746       N  
ATOM   1889  CZ  ARG B  97     -38.287   4.339 -23.262  1.00 17.54           C  
ANISOU 1889  CZ  ARG B  97     1956   2352   2357    274    139    648       C  
ATOM   1890  NH1 ARG B  97     -38.833   3.125 -23.315  1.00 16.07           N  
ANISOU 1890  NH1 ARG B  97     1719   2223   2162    318    136    563       N  
ATOM   1891  NH2 ARG B  97     -37.501   4.664 -22.237  1.00 16.62           N  
ANISOU 1891  NH2 ARG B  97     1891   2142   2280    216    133    638       N  
ATOM   1892  N   PRO B  98     -34.003   6.843 -28.259  1.00 23.76           N  
ANISOU 1892  N   PRO B  98     2471   3797   2759   -143    177   1081       N  
ATOM   1893  CA  PRO B  98     -32.684   6.292 -28.568  1.00 23.95           C  
ANISOU 1893  CA  PRO B  98     2343   4062   2696   -209    182   1038       C  
ATOM   1894  C   PRO B  98     -32.378   5.047 -27.749  1.00 22.84           C  
ANISOU 1894  C   PRO B  98     2146   3938   2592   -112    172    871       C  
ATOM   1895  O   PRO B  98     -32.680   5.006 -26.553  1.00 21.94           O  
ANISOU 1895  O   PRO B  98     2131   3630   2576    -92    162    823       O  
ATOM   1896  CB  PRO B  98     -31.732   7.423 -28.157  1.00 25.45           C  
ANISOU 1896  CB  PRO B  98     2591   4211   2867   -411    180   1143       C  
ATOM   1897  CG  PRO B  98     -32.502   8.658 -28.437  1.00 26.39           C  
ANISOU 1897  CG  PRO B  98     2876   4136   3014   -457    178   1291       C  
ATOM   1898  CD  PRO B  98     -33.948   8.310 -28.071  1.00 24.95           C  
ANISOU 1898  CD  PRO B  98     2775   3779   2927   -265    172   1227       C  
ATOM   1899  N   SER B  99     -31.799   4.035 -28.388  1.00 22.63           N  
ANISOU 1899  N   SER B  99     1974   4143   2482    -40    174    784       N  
ATOM   1900  CA  SER B  99     -31.423   2.811 -27.687  1.00 22.04           C  
ANISOU 1900  CA  SER B  99     1866   4080   2428     74    159    632       C  
ATOM   1901  C   SER B  99     -30.271   3.059 -26.721  1.00 22.29           C  
ANISOU 1901  C   SER B  99     1875   4144   2451     -6    153    632       C  
ATOM   1902  O   SER B  99     -29.265   3.661 -27.081  1.00 23.08           O  
ANISOU 1902  O   SER B  99     1879   4435   2453   -129    161    699       O  
ATOM   1903  CB  SER B  99     -31.048   1.712 -28.683  1.00 22.82           C  
ANISOU 1903  CB  SER B  99     1832   4415   2424    194    158    531       C  
ATOM   1904  OG  SER B  99     -30.771   0.506 -28.006  1.00 21.85           O  
ANISOU 1904  OG  SER B  99     1719   4256   2326    329    138    388       O  
ATOM   1905  N   SER B 100     -30.433   2.617 -25.482  1.00 21.65           N  
ANISOU 1905  N   SER B 100     1873   3895   2458     49    137    561       N  
ATOM   1906  CA  SER B 100     -29.369   2.757 -24.490  1.00 22.41           C  
ANISOU 1906  CA  SER B 100     1937   4043   2537    -11    128    547       C  
ATOM   1907  C   SER B 100     -29.524   1.758 -23.363  1.00 21.57           C  
ANISOU 1907  C   SER B 100     1884   3815   2497    122    107    442       C  
ATOM   1908  O   SER B 100     -30.589   1.150 -23.182  1.00 20.78           O  
ANISOU 1908  O   SER B 100     1880   3538   2478    217    102    398       O  
ATOM   1909  CB  SER B 100     -29.335   4.177 -23.907  1.00 22.84           C  
ANISOU 1909  CB  SER B 100     2081   3968   2630   -206    132    653       C  
ATOM   1910  OG  SER B 100     -30.437   4.373 -23.034  1.00 22.51           O  
ANISOU 1910  OG  SER B 100     2199   3640   2714   -173    126    643       O  
ATOM   1911  N   GLU B 101     -28.457   1.606 -22.588  1.00 21.86           N  
ANISOU 1911  N   GLU B 101     1855   3964   2488    116     96    412       N  
ATOM   1912  CA  GLU B 101     -28.501   0.761 -21.409  1.00 21.54           C  
ANISOU 1912  CA  GLU B 101     1871   3815   2500    233     74    336       C  
ATOM   1913  C   GLU B 101     -29.395   1.326 -20.310  1.00 19.41           C  
ANISOU 1913  C   GLU B 101     1746   3281   2348    161     72    366       C  
ATOM   1914  O   GLU B 101     -30.078   0.566 -19.615  1.00 17.82           O  
ANISOU 1914  O   GLU B 101     1631   2924   2214    261     60    318       O  
ATOM   1915  CB  GLU B 101     -27.092   0.505 -20.863  1.00 23.58           C  
ANISOU 1915  CB  GLU B 101     2001   4301   2655    259     59    303       C  
ATOM   1916  CG  GLU B 101     -26.951  -0.888 -20.238  1.00 26.39           C  
ANISOU 1916  CG  GLU B 101     2382   4632   3013    481     31    209       C  
ATOM   1917  CD  GLU B 101     -27.118  -1.986 -21.272  1.00 30.31           C  
ANISOU 1917  CD  GLU B 101     2872   5170   3474    663     24    135       C  
ATOM   1918  OE1 GLU B 101     -26.295  -2.069 -22.205  1.00 33.34           O  
ANISOU 1918  OE1 GLU B 101     3111   5822   3735    707     30    113       O  
ATOM   1919  OE2 GLU B 101     -28.086  -2.758 -21.159  1.00 32.53           O  
ANISOU 1919  OE2 GLU B 101     3293   5226   3840    751     13     94       O  
ATOM   1920  N   VAL B 102     -29.409   2.652 -20.163  1.00 18.88           N  
ANISOU 1920  N   VAL B 102     1716   3162   2297    -12     84    443       N  
ATOM   1921  CA  VAL B 102     -30.145   3.275 -19.039  1.00 18.20           C  
ANISOU 1921  CA  VAL B 102     1764   2846   2306    -67     80    454       C  
ATOM   1922  C   VAL B 102     -31.684   3.181 -19.177  1.00 16.93           C  
ANISOU 1922  C   VAL B 102     1716   2482   2234      7     87    458       C  
ATOM   1923  O   VAL B 102     -32.412   3.284 -18.189  1.00 16.13           O  
ANISOU 1923  O   VAL B 102     1706   2224   2200     23     82    440       O  
ATOM   1924  CB  VAL B 102     -29.634   4.726 -18.726  1.00 19.18           C  
ANISOU 1924  CB  VAL B 102     1923   2949   2415   -272     83    517       C  
ATOM   1925  CG1 VAL B 102     -30.120   5.759 -19.764  1.00 18.87           C  
ANISOU 1925  CG1 VAL B 102     1952   2838   2382   -366     99    613       C  
ATOM   1926  CG2 VAL B 102     -30.004   5.149 -17.304  1.00 19.69           C  
ANISOU 1926  CG2 VAL B 102     2096   2837   2547   -302     72    486       C  
ATOM   1927  N   ILE B 103     -32.172   2.941 -20.392  1.00 16.47           N  
ANISOU 1927  N   ILE B 103     1634   2466   2159     54     98    476       N  
ATOM   1928  CA  ILE B 103     -33.614   2.822 -20.591  1.00 16.15           C  
ANISOU 1928  CA  ILE B 103     1671   2290   2177    117    103    478       C  
ATOM   1929  C   ILE B 103     -34.121   1.398 -20.377  1.00 16.50           C  
ANISOU 1929  C   ILE B 103     1719   2313   2239    233     92    393       C  
ATOM   1930  O   ILE B 103     -35.321   1.200 -20.254  1.00 16.36           O  
ANISOU 1930  O   ILE B 103     1758   2196   2262    263     94    384       O  
ATOM   1931  CB  ILE B 103     -34.080   3.343 -21.977  1.00 16.30           C  
ANISOU 1931  CB  ILE B 103     1671   2361   2162    103    119    545       C  
ATOM   1932  CG1 ILE B 103     -33.587   2.423 -23.112  1.00 16.51           C  
ANISOU 1932  CG1 ILE B 103     1582   2579   2111    160    120    505       C  
ATOM   1933  CG2 ILE B 103     -33.653   4.797 -22.179  1.00 15.87           C  
ANISOU 1933  CG2 ILE B 103     1656   2285   2091    -26    126    649       C  
ATOM   1934  CD1 ILE B 103     -34.272   2.661 -24.475  1.00 18.06           C  
ANISOU 1934  CD1 ILE B 103     1749   2845   2266    173    133    553       C  
ATOM   1935  N   LYS B 104     -33.213   0.416 -20.335  1.00 17.26           N  
ANISOU 1935  N   LYS B 104     1759   2506   2293    297     77    333       N  
ATOM   1936  CA  LYS B 104     -33.626  -0.991 -20.334  1.00 17.70           C  
ANISOU 1936  CA  LYS B 104     1850   2518   2356    405     61    256       C  
ATOM   1937  C   LYS B 104     -34.243  -1.438 -19.009  1.00 17.02           C  
ANISOU 1937  C   LYS B 104     1860   2274   2332    415     48    240       C  
ATOM   1938  O   LYS B 104     -35.351  -1.987 -19.002  1.00 17.20           O  
ANISOU 1938  O   LYS B 104     1947   2203   2385    421     45    221       O  
ATOM   1939  CB  LYS B 104     -32.487  -1.925 -20.738  1.00 18.83           C  
ANISOU 1939  CB  LYS B 104     1928   2800   2426    510     44    192       C  
ATOM   1940  CG  LYS B 104     -32.048  -1.785 -22.193  1.00 21.06           C  
ANISOU 1940  CG  LYS B 104     2105   3269   2628    521     56    187       C  
ATOM   1941  CD  LYS B 104     -31.146  -2.945 -22.584  1.00 25.75           C  
ANISOU 1941  CD  LYS B 104     2651   3989   3143    673     35     93       C  
ATOM   1942  CE  LYS B 104     -30.230  -2.598 -23.756  1.00 28.31           C  
ANISOU 1942  CE  LYS B 104     2819   4586   3351    678     49     96       C  
ATOM   1943  NZ  LYS B 104     -29.183  -3.659 -23.983  1.00 29.90           N  
ANISOU 1943  NZ  LYS B 104     2957   4950   3456    861     26     -6       N  
ATOM   1944  N   ASP B 105     -33.552  -1.194 -17.897  1.00 16.08           N  
ANISOU 1944  N   ASP B 105     1741   2150   2217    402     39    251       N  
ATOM   1945  CA  ASP B 105     -34.032  -1.676 -16.604  1.00 15.14           C  
ANISOU 1945  CA  ASP B 105     1702   1912   2140    415     26    242       C  
ATOM   1946  C   ASP B 105     -34.583  -0.555 -15.720  1.00 14.04           C  
ANISOU 1946  C   ASP B 105     1590   1705   2041    328     39    280       C  
ATOM   1947  O   ASP B 105     -34.140  -0.364 -14.587  1.00 13.33           O  
ANISOU 1947  O   ASP B 105     1506   1609   1950    312     30    280       O  
ATOM   1948  CB  ASP B 105     -32.965  -2.516 -15.883  1.00 15.67           C  
ANISOU 1948  CB  ASP B 105     1761   2023   2169    502     -1    214       C  
ATOM   1949  CG  ASP B 105     -31.584  -1.851 -15.888  1.00 16.98           C  
ANISOU 1949  CG  ASP B 105     1815   2364   2274    485      0    222       C  
ATOM   1950  OD1 ASP B 105     -31.456  -0.710 -16.409  1.00 14.43           O  
ANISOU 1950  OD1 ASP B 105     1440   2099   1945    378     21    256       O  
ATOM   1951  OD2 ASP B 105     -30.628  -2.481 -15.382  1.00 15.25           O  
ANISOU 1951  OD2 ASP B 105     1561   2233   2002    576    -22    200       O  
ATOM   1952  N   ALA B 106     -35.574   0.159 -16.257  1.00 13.36           N  
ANISOU 1952  N   ALA B 106     1522   1576   1978    289     58    306       N  
ATOM   1953  CA  ALA B 106     -36.161   1.341 -15.620  1.00 13.02           C  
ANISOU 1953  CA  ALA B 106     1520   1464   1964    240     69    334       C  
ATOM   1954  C   ALA B 106     -37.596   1.073 -15.137  1.00 12.53           C  
ANISOU 1954  C   ALA B 106     1499   1341   1921    263     73    325       C  
ATOM   1955  O   ALA B 106     -38.368   2.010 -14.920  1.00 11.71           O  
ANISOU 1955  O   ALA B 106     1423   1200   1827    262     84    341       O  
ATOM   1956  CB  ALA B 106     -36.134   2.536 -16.622  1.00 13.35           C  
ANISOU 1956  CB  ALA B 106     1557   1516   2000    198     84    383       C  
ATOM   1957  N   ASN B 107     -37.931  -0.213 -14.970  1.00 12.42           N  
ANISOU 1957  N   ASN B 107     1494   1324   1900    284     62    301       N  
ATOM   1958  CA  ASN B 107     -39.303  -0.671 -14.718  1.00 12.52           C  
ANISOU 1958  CA  ASN B 107     1527   1323   1907    273     65    297       C  
ATOM   1959  C   ASN B 107     -39.478  -1.118 -13.260  1.00 12.06           C  
ANISOU 1959  C   ASN B 107     1502   1233   1846    255     55    295       C  
ATOM   1960  O   ASN B 107     -38.747  -1.978 -12.764  1.00 12.04           O  
ANISOU 1960  O   ASN B 107     1531   1204   1842    265     35    291       O  
ATOM   1961  CB  ASN B 107     -39.635  -1.809 -15.700  1.00 12.92           C  
ANISOU 1961  CB  ASN B 107     1582   1389   1939    270     57    274       C  
ATOM   1962  CG  ASN B 107     -41.085  -2.262 -15.647  1.00 13.20           C  
ANISOU 1962  CG  ASN B 107     1622   1447   1949    220     61    270       C  
ATOM   1963  OD1 ASN B 107     -41.374  -3.449 -15.867  1.00 16.04           O  
ANISOU 1963  OD1 ASN B 107     2023   1782   2291    179     46    244       O  
ATOM   1964  ND2 ASN B 107     -41.993  -1.353 -15.363  1.00 11.80           N  
ANISOU 1964  ND2 ASN B 107     1405   1321   1756    223     79    291       N  
ATOM   1965  N   LEU B 108     -40.436  -0.501 -12.581  1.00 12.07           N  
ANISOU 1965  N   LEU B 108     1496   1254   1836    245     67    300       N  
ATOM   1966  CA  LEU B 108     -40.641  -0.700 -11.147  1.00 12.63           C  
ANISOU 1966  CA  LEU B 108     1580   1329   1888    225     62    301       C  
ATOM   1967  C   LEU B 108     -41.881  -1.525 -10.840  1.00 13.02           C  
ANISOU 1967  C   LEU B 108     1626   1427   1895    173     63    313       C  
ATOM   1968  O   LEU B 108     -42.920  -1.359 -11.480  1.00 13.88           O  
ANISOU 1968  O   LEU B 108     1695   1601   1976    164     76    311       O  
ATOM   1969  CB  LEU B 108     -40.771   0.664 -10.448  1.00 12.07           C  
ANISOU 1969  CB  LEU B 108     1500   1269   1816    254     73    283       C  
ATOM   1970  CG  LEU B 108     -39.566   1.602 -10.500  1.00 11.77           C  
ANISOU 1970  CG  LEU B 108     1481   1184   1809    260     70    271       C  
ATOM   1971  CD1 LEU B 108     -39.947   2.990  -9.974  1.00 12.13           C  
ANISOU 1971  CD1 LEU B 108     1556   1202   1852    286     78    242       C  
ATOM   1972  CD2 LEU B 108     -38.419   1.024  -9.686  1.00 11.75           C  
ANISOU 1972  CD2 LEU B 108     1475   1190   1799    237     51    267       C  
ATOM   1973  N   TYR B 109     -41.776  -2.383  -9.836  1.00 13.23           N  
ANISOU 1973  N   TYR B 109     1687   1438   1900    131     47    334       N  
ATOM   1974  CA  TYR B 109     -42.933  -3.027  -9.238  1.00 13.83           C  
ANISOU 1974  CA  TYR B 109     1757   1581   1917     48     49    360       C  
ATOM   1975  C   TYR B 109     -43.182  -2.342  -7.891  1.00 14.22           C  
ANISOU 1975  C   TYR B 109     1762   1714   1927     63     58    359       C  
ATOM   1976  O   TYR B 109     -42.258  -2.214  -7.080  1.00 14.22           O  
ANISOU 1976  O   TYR B 109     1784   1678   1941     94     47    361       O  
ATOM   1977  CB  TYR B 109     -42.639  -4.523  -9.060  1.00 14.76           C  
ANISOU 1977  CB  TYR B 109     1971   1608   2030    -20     21    397       C  
ATOM   1978  CG  TYR B 109     -43.739  -5.337  -8.434  1.00 16.02           C  
ANISOU 1978  CG  TYR B 109     2146   1822   2118   -153     18    442       C  
ATOM   1979  CD1 TYR B 109     -44.829  -5.785  -9.192  1.00 17.97           C  
ANISOU 1979  CD1 TYR B 109     2379   2125   2326   -259     23    436       C  
ATOM   1980  CD2 TYR B 109     -43.674  -5.706  -7.091  1.00 18.36           C  
ANISOU 1980  CD2 TYR B 109     2468   2134   2373   -191      7    496       C  
ATOM   1981  CE1 TYR B 109     -45.833  -6.567  -8.614  1.00 18.70           C  
ANISOU 1981  CE1 TYR B 109     2481   2289   2335   -421     19    483       C  
ATOM   1982  CE2 TYR B 109     -44.679  -6.499  -6.505  1.00 19.29           C  
ANISOU 1982  CE2 TYR B 109     2602   2316   2411   -344      4    554       C  
ATOM   1983  CZ  TYR B 109     -45.750  -6.908  -7.270  1.00 20.31           C  
ANISOU 1983  CZ  TYR B 109     2715   2502   2499   -467     10    547       C  
ATOM   1984  OH  TYR B 109     -46.735  -7.679  -6.680  1.00 24.31           O  
ANISOU 1984  OH  TYR B 109     3231   3096   2910   -653      6    610       O  
ATOM   1985  N   ILE B 110     -44.422  -1.903  -7.665  1.00 14.06           N  
ANISOU 1985  N   ILE B 110     1669   1830   1844     51     78    350       N  
ATOM   1986  CA  ILE B 110     -44.809  -1.142  -6.477  1.00 14.35           C  
ANISOU 1986  CA  ILE B 110     1650   1975   1825     91     89    328       C  
ATOM   1987  C   ILE B 110     -45.970  -1.843  -5.765  1.00 15.86           C  
ANISOU 1987  C   ILE B 110     1782   2332   1911     -9     95    365       C  
ATOM   1988  O   ILE B 110     -46.933  -2.245  -6.418  1.00 15.85           O  
ANISOU 1988  O   ILE B 110     1738   2420   1864    -75    102    378       O  
ATOM   1989  CB  ILE B 110     -45.206   0.327  -6.874  1.00 14.43           C  
ANISOU 1989  CB  ILE B 110     1622   2022   1839    216    107    267       C  
ATOM   1990  CG1 ILE B 110     -44.023   1.030  -7.563  1.00 14.75           C  
ANISOU 1990  CG1 ILE B 110     1732   1899   1974    273    100    248       C  
ATOM   1991  CG2 ILE B 110     -45.648   1.158  -5.656  1.00 14.31           C  
ANISOU 1991  CG2 ILE B 110     1563   2116   1757    285    116    220       C  
ATOM   1992  CD1 ILE B 110     -44.448   1.913  -8.712  1.00 17.84           C  
ANISOU 1992  CD1 ILE B 110     2120   2277   2381    353    112    234       C  
ATOM   1993  N  ASER B 111     -45.870  -2.005  -4.445  0.50 16.43           N  
ANISOU 1993  N  ASER B 111     1844   2468   1931    -35     91    385       N  
ATOM   1994  N  BSER B 111     -45.867  -1.984  -4.441  0.50 16.61           N  
ANISOU 1994  N  BSER B 111     1865   2490   1954    -33     91    383       N  
ATOM   1995  CA ASER B 111     -46.965  -2.577  -3.649  0.50 18.02           C  
ANISOU 1995  CA ASER B 111     1973   2863   2010   -144     98    429       C  
ATOM   1996  CA BSER B 111     -46.926  -2.588  -3.622  0.50 18.40           C  
ANISOU 1996  CA BSER B 111     2024   2907   2060   -144     97    430       C  
ATOM   1997  C  ASER B 111     -47.270  -1.704  -2.434  0.50 19.00           C  
ANISOU 1997  C  ASER B 111     2009   3157   2053    -65    112    383       C  
ATOM   1998  C  BSER B 111     -47.268  -1.696  -2.431  0.50 19.20           C  
ANISOU 1998  C  BSER B 111     2034   3183   2078    -64    112    382       C  
ATOM   1999  O  ASER B 111     -46.549  -0.747  -2.163  0.50 18.49           O  
ANISOU 1999  O  ASER B 111     1966   3023   2038     58    111    316       O  
ATOM   2000  O  BSER B 111     -46.573  -0.717  -2.173  0.50 18.70           O  
ANISOU 2000  O  BSER B 111     1990   3052   2063     61    111    314       O  
ATOM   2001  CB ASER B 111     -46.639  -4.007  -3.205  0.50 18.38           C  
ANISOU 2001  CB ASER B 111     2109   2830   2043   -294     74    527       C  
ATOM   2002  CB BSER B 111     -46.498  -3.971  -3.129  0.50 18.74           C  
ANISOU 2002  CB BSER B 111     2161   2864   2096   -283     72    526       C  
ATOM   2003  OG ASER B 111     -45.743  -4.004  -2.113  0.50 17.82           O  
ANISOU 2003  OG ASER B 111     2072   2723   1976   -254     60    548       O  
ATOM   2004  OG BSER B 111     -45.971  -4.732  -4.197  0.50 19.43           O  
ANISOU 2004  OG BSER B 111     2360   2756   2268   -316     53    546       O  
ATOM   2005  N   GLY B 112     -48.334  -2.045  -1.709  1.00 20.92           N  
ANISOU 2005  N   GLY B 112     2152   3635   2161   -149    124    414       N  
ATOM   2006  CA  GLY B 112     -48.758  -1.297  -0.515  1.00 22.45           C  
ANISOU 2006  CA  GLY B 112     2243   4041   2248    -70    138    363       C  
ATOM   2007  C   GLY B 112     -49.391   0.062  -0.786  1.00 23.79           C  
ANISOU 2007  C   GLY B 112     2334   4318   2387    120    158    248       C  
ATOM   2008  O   GLY B 112     -49.421   0.922   0.100  1.00 24.44           O  
ANISOU 2008  O   GLY B 112     2375   4496   2414    241    163    168       O  
ATOM   2009  N   LEU B 113     -49.896   0.264  -2.002  1.00 23.89           N  
ANISOU 2009  N   LEU B 113     2335   4315   2427    158    165    235       N  
ATOM   2010  CA  LEU B 113     -50.608   1.499  -2.344  1.00 25.63           C  
ANISOU 2010  CA  LEU B 113     2492   4642   2604    361    180    143       C  
ATOM   2011  C   LEU B 113     -52.071   1.444  -1.883  1.00 28.03           C  
ANISOU 2011  C   LEU B 113     2610   5326   2716    366    200    133       C  
ATOM   2012  O   LEU B 113     -52.710   0.396  -1.966  1.00 28.55           O  
ANISOU 2012  O   LEU B 113     2597   5551   2700    175    205    214       O  
ATOM   2013  CB  LEU B 113     -50.550   1.767  -3.860  1.00 24.08           C  
ANISOU 2013  CB  LEU B 113     2349   4301   2500    415    178    145       C  
ATOM   2014  CG  LEU B 113     -49.190   1.989  -4.551  1.00 23.50           C  
ANISOU 2014  CG  LEU B 113     2434   3897   2598    428    161    148       C  
ATOM   2015  CD1 LEU B 113     -49.325   1.893  -6.074  1.00 21.06           C  
ANISOU 2015  CD1 LEU B 113     2142   3516   2342    429    161    177       C  
ATOM   2016  CD2 LEU B 113     -48.531   3.320  -4.185  1.00 21.96           C  
ANISOU 2016  CD2 LEU B 113     2325   3563   2456    591    155     64       C  
ATOM   2017  N   PRO B 114     -52.615   2.572  -1.396  1.00 30.53           N  
ANISOU 2017  N   PRO B 114     2858   5797   2944    583    210     31       N  
ATOM   2018  CA  PRO B 114     -54.053   2.595  -1.086  1.00 33.15           C  
ANISOU 2018  CA  PRO B 114     2985   6541   3071    624    230     13       C  
ATOM   2019  C   PRO B 114     -54.894   2.049  -2.240  1.00 34.41           C  
ANISOU 2019  C   PRO B 114     3055   6836   3184    537    238     72       C  
ATOM   2020  O   PRO B 114     -54.621   2.348  -3.412  1.00 33.96           O  
ANISOU 2020  O   PRO B 114     3083   6585   3236    605    230     71       O  
ATOM   2021  CB  PRO B 114     -54.329   4.075  -0.875  1.00 33.99           C  
ANISOU 2021  CB  PRO B 114     3092   6686   3136    945    232   -123       C  
ATOM   2022  CG  PRO B 114     -53.075   4.582  -0.286  1.00 32.90           C  
ANISOU 2022  CG  PRO B 114     3126   6245   3129    983    215   -175       C  
ATOM   2023  CD  PRO B 114     -51.945   3.800  -0.934  1.00 30.63           C  
ANISOU 2023  CD  PRO B 114     2975   5644   3018    785    201    -77       C  
ATOM   2024  N   ARG B 115     -55.888   1.232  -1.905  1.00 36.39           N  
ANISOU 2024  N   ARG B 115     3132   7431   3262    364    251    126       N  
ATOM   2025  CA  ARG B 115     -56.742   0.582  -2.897  1.00 38.11           C  
ANISOU 2025  CA  ARG B 115     3246   7826   3407    225    257    180       C  
ATOM   2026  C   ARG B 115     -57.619   1.592  -3.646  1.00 38.76           C  
ANISOU 2026  C   ARG B 115     3210   8114   3402    490    266    104       C  
ATOM   2027  O   ARG B 115     -58.174   1.281  -4.704  1.00 39.19           O  
ANISOU 2027  O   ARG B 115     3198   8271   3422    428    267    133       O  
ATOM   2028  CB  ARG B 115     -57.626  -0.474  -2.221  1.00 40.33           C  
ANISOU 2028  CB  ARG B 115     3365   8461   3498    -50    268    255       C  
ATOM   2029  CG  ARG B 115     -56.955  -1.210  -1.052  1.00 42.88           C  
ANISOU 2029  CG  ARG B 115     3774   8675   3844   -236    260    326       C  
ATOM   2030  CD  ARG B 115     -55.934  -2.240  -1.537  1.00 45.63           C  
ANISOU 2030  CD  ARG B 115     4341   8622   4373   -448    235    417       C  
ATOM   2031  NE  ARG B 115     -56.570  -3.526  -1.828  1.00 49.18           N  
ANISOU 2031  NE  ARG B 115     4761   9190   4735   -776    230    518       N  
ATOM   2032  CZ  ARG B 115     -55.943  -4.701  -1.794  1.00 49.85           C  
ANISOU 2032  CZ  ARG B 115     5021   9016   4902  -1018    206    619       C  
ATOM   2033  NH1 ARG B 115     -54.654  -4.765  -1.474  1.00 48.68           N  
ANISOU 2033  NH1 ARG B 115     5064   8515   4918   -949    187    634       N  
ATOM   2034  NH2 ARG B 115     -56.609  -5.817  -2.073  1.00 51.32           N  
ANISOU 2034  NH2 ARG B 115     5198   9305   4996  -1328    199    702       N  
ATOM   2035  N   THR B 116     -57.729   2.796  -3.085  1.00 39.40           N  
ANISOU 2035  N   THR B 116     3276   8252   3440    793    270      3       N  
ATOM   2036  CA  THR B 116     -58.552   3.867  -3.644  1.00 40.28           C  
ANISOU 2036  CA  THR B 116     3298   8551   3456   1106    275    -74       C  
ATOM   2037  C   THR B 116     -57.863   4.599  -4.804  1.00 38.97           C  
ANISOU 2037  C   THR B 116     3325   8011   3473   1271    257    -82       C  
ATOM   2038  O   THR B 116     -58.536   5.200  -5.635  1.00 39.69           O  
ANISOU 2038  O   THR B 116     3354   8231   3497   1472    257   -101       O  
ATOM   2039  CB  THR B 116     -58.940   4.886  -2.559  1.00 41.64           C  
ANISOU 2039  CB  THR B 116     3409   8909   3503   1391    280   -191       C  
ATOM   2040  N   MET B 117     -56.529   4.529  -4.856  1.00 36.91           N  
ANISOU 2040  N   MET B 117     3284   7316   3424   1183    243    -60       N  
ATOM   2041  CA  MET B 117     -55.723   5.241  -5.862  1.00 35.59           C  
ANISOU 2041  CA  MET B 117     3309   6783   3429   1308    226    -60       C  
ATOM   2042  C   MET B 117     -55.947   4.757  -7.287  1.00 34.52           C  
ANISOU 2042  C   MET B 117     3142   6654   3318   1221    226     12       C  
ATOM   2043  O   MET B 117     -55.817   3.562  -7.558  1.00 33.73           O  
ANISOU 2043  O   MET B 117     3013   6563   3240    946    227     78       O  
ATOM   2044  CB  MET B 117     -54.233   5.097  -5.555  1.00 34.24           C  
ANISOU 2044  CB  MET B 117     3340   6217   3452   1182    213    -46       C  
ATOM   2045  CG  MET B 117     -53.673   6.091  -4.579  1.00 36.08           C  
ANISOU 2045  CG  MET B 117     3689   6300   3719   1342    204   -138       C  
ATOM   2046  SD  MET B 117     -51.883   5.925  -4.544  1.00 37.31           S  
ANISOU 2046  SD  MET B 117     4061   6023   4093   1181    185   -110       S  
ATOM   2047  CE  MET B 117     -51.461   7.413  -3.647  1.00 38.55           C  
ANISOU 2047  CE  MET B 117     4357   6027   4263   1404    171   -242       C  
ATOM   2048  N   THR B 118     -56.242   5.694  -8.192  1.00 34.37           N  
ANISOU 2048  N   THR B 118     3151   6614   3295   1460    220     -2       N  
ATOM   2049  CA  THR B 118     -56.414   5.387  -9.617  1.00 33.55           C  
ANISOU 2049  CA  THR B 118     3020   6519   3209   1410    217     62       C  
ATOM   2050  C   THR B 118     -55.085   5.427 -10.371  1.00 31.77           C  
ANISOU 2050  C   THR B 118     3005   5873   3193   1336    203    105       C  
ATOM   2051  O   THR B 118     -54.100   5.991  -9.874  1.00 30.81           O  
ANISOU 2051  O   THR B 118     3055   5457   3194   1381    194     81       O  
ATOM   2052  CB  THR B 118     -57.380   6.383 -10.298  1.00 35.49           C  
ANISOU 2052  CB  THR B 118     3187   6967   3330   1721    215     44       C  
ATOM   2053  OG1 THR B 118     -56.796   7.691 -10.298  1.00 35.20           O  
ANISOU 2053  OG1 THR B 118     3356   6627   3390   1983    199     13       O  
ATOM   2054  CG2 THR B 118     -58.727   6.423  -9.571  0.40 36.90           C  
ANISOU 2054  CG2 THR B 118     3130   7620   3272   1833    229     -8       C  
ATOM   2055  N   GLN B 119     -55.066   4.835 -11.571  1.00 30.51           N  
ANISOU 2055  N   GLN B 119     2819   5715   3058   1218    202    162       N  
ATOM   2056  CA  GLN B 119     -53.892   4.884 -12.459  1.00 28.72           C  
ANISOU 2056  CA  GLN B 119     2759   5153   3001   1164    190    205       C  
ATOM   2057  C   GLN B 119     -53.338   6.301 -12.601  1.00 28.11           C  
ANISOU 2057  C   GLN B 119     2847   4831   3001   1398    179    198       C  
ATOM   2058  O   GLN B 119     -52.128   6.511 -12.458  1.00 26.90           O  
ANISOU 2058  O   GLN B 119     2859   4373   2990   1339    170    204       O  
ATOM   2059  CB  GLN B 119     -54.210   4.299 -13.845  1.00 28.74           C  
ANISOU 2059  CB  GLN B 119     2683   5262   2974   1077    190    251       C  
ATOM   2060  CG  GLN B 119     -52.973   3.815 -14.629  1.00 27.65           C  
ANISOU 2060  CG  GLN B 119     2675   4840   2990    930    181    287       C  
ATOM   2061  CD  GLN B 119     -53.300   3.437 -16.063  1.00 28.07           C  
ANISOU 2061  CD  GLN B 119     2655   5006   3002    888    180    319       C  
ATOM   2062  N   LYS B 120     -54.225   7.262 -12.868  1.00 28.90           N  
ANISOU 2062  N   LYS B 120     2911   5072   2998   1662    177    188       N  
ATOM   2063  CA  LYS B 120     -53.838   8.673 -12.956  1.00 28.79           C  
ANISOU 2063  CA  LYS B 120     3087   4811   3041   1901    161    183       C  
ATOM   2064  C   LYS B 120     -53.238   9.168 -11.635  1.00 28.14           C  
ANISOU 2064  C   LYS B 120     3134   4540   3017   1924    154    106       C  
ATOM   2065  O   LYS B 120     -52.292   9.957 -11.653  1.00 27.15           O  
ANISOU 2065  O   LYS B 120     3218   4089   3008   1953    138    107       O  
ATOM   2066  CB  LYS B 120     -55.020   9.557 -13.386  1.00 30.69           C  
ANISOU 2066  CB  LYS B 120     3266   5260   3135   2217    155    183       C  
ATOM   2067  N   ASP B 121     -53.775   8.684 -10.505  1.00 28.03           N  
ANISOU 2067  N   ASP B 121     2991   4746   2913   1888    166     41       N  
ATOM   2068  CA  ASP B 121     -53.288   9.078  -9.173  1.00 28.14           C  
ANISOU 2068  CA  ASP B 121     3098   4637   2957   1907    161    -43       C  
ATOM   2069  C   ASP B 121     -51.864   8.557  -8.981  1.00 25.10           C  
ANISOU 2069  C   ASP B 121     2829   3975   2733   1654    156    -17       C  
ATOM   2070  O   ASP B 121     -50.988   9.297  -8.548  1.00 24.64           O  
ANISOU 2070  O   ASP B 121     2944   3655   2763   1679    142    -57       O  
ATOM   2071  CB  ASP B 121     -54.183   8.552  -8.034  1.00 29.42           C  
ANISOU 2071  CB  ASP B 121     3067   5143   2967   1898    177   -103       C  
ATOM   2072  CG  ASP B 121     -55.500   9.320  -7.885  1.00 34.34           C  
ANISOU 2072  CG  ASP B 121     3583   6058   3408   2208    179   -165       C  
ATOM   2073  OD1 ASP B 121     -55.571  10.536  -8.203  1.00 39.18           O  
ANISOU 2073  OD1 ASP B 121     4339   6520   4028   2487    160   -197       O  
ATOM   2074  OD2 ASP B 121     -56.477   8.695  -7.410  1.00 37.38           O  
ANISOU 2074  OD2 ASP B 121     3739   6835   3629   2174    197   -180       O  
ATOM   2075  N   VAL B 122     -51.643   7.287  -9.317  1.00 23.28           N  
ANISOU 2075  N   VAL B 122     2506   3810   2530   1416    166     45       N  
ATOM   2076  CA  VAL B 122     -50.306   6.678  -9.214  1.00 21.20           C  
ANISOU 2076  CA  VAL B 122     2335   3319   2402   1202    160     74       C  
ATOM   2077  C   VAL B 122     -49.289   7.333 -10.168  1.00 20.23           C  
ANISOU 2077  C   VAL B 122     2373   2912   2403   1212    147    112       C  
ATOM   2078  O   VAL B 122     -48.154   7.602  -9.772  1.00 19.09           O  
ANISOU 2078  O   VAL B 122     2349   2554   2350   1140    136     97       O  
ATOM   2079  CB  VAL B 122     -50.348   5.123  -9.355  1.00 20.45           C  
ANISOU 2079  CB  VAL B 122     2128   3345   2296    969    168    126       C  
ATOM   2080  CG1 VAL B 122     -48.937   4.527  -9.341  1.00 18.71           C  
ANISOU 2080  CG1 VAL B 122     2011   2893   2206    801    157    154       C  
ATOM   2081  CG2 VAL B 122     -51.180   4.510  -8.225  1.00 21.03           C  
ANISOU 2081  CG2 VAL B 122     2067   3675   2247    914    178    101       C  
ATOM   2082  N   GLU B 123     -49.701   7.603 -11.404  1.00 20.73           N  
ANISOU 2082  N   GLU B 123     2426   2999   2450   1292    147    165       N  
ATOM   2083  CA  GLU B 123     -48.857   8.338 -12.364  1.00 21.14           C  
ANISOU 2083  CA  GLU B 123     2627   2811   2596   1310    136    218       C  
ATOM   2084  C   GLU B 123     -48.441   9.721 -11.864  1.00 21.50           C  
ANISOU 2084  C   GLU B 123     2862   2629   2678   1439    119    178       C  
ATOM   2085  O   GLU B 123     -47.267  10.071 -11.944  1.00 20.41           O  
ANISOU 2085  O   GLU B 123     2859   2261   2637   1333    108    194       O  
ATOM   2086  CB  GLU B 123     -49.533   8.481 -13.736  1.00 22.07           C  
ANISOU 2086  CB  GLU B 123     2694   3030   2664   1405    138    287       C  
ATOM   2087  CG  GLU B 123     -49.280   7.290 -14.648  1.00 24.65           C  
ANISOU 2087  CG  GLU B 123     2919   3437   3009   1221    146    336       C  
ATOM   2088  CD  GLU B 123     -49.791   7.481 -16.075  1.00 29.54           C  
ANISOU 2088  CD  GLU B 123     3492   4154   3579   1300    147    404       C  
ATOM   2089  OE1 GLU B 123     -50.481   8.492 -16.371  1.00 33.22           O  
ANISOU 2089  OE1 GLU B 123     3988   4652   3982   1516    141    426       O  
ATOM   2090  OE2 GLU B 123     -49.507   6.593 -16.909  1.00 31.73           O  
ANISOU 2090  OE2 GLU B 123     3704   4481   3871   1157    151    433       O  
ATOM   2091  N   ASP B 124     -49.410  10.503 -11.378  1.00 22.48           N  
ANISOU 2091  N   ASP B 124     2998   2828   2714   1666    114    121       N  
ATOM   2092  CA  ASP B 124     -49.133  11.828 -10.835  1.00 23.91           C  
ANISOU 2092  CA  ASP B 124     3387   2779   2919   1808     93     61       C  
ATOM   2093  C   ASP B 124     -48.146  11.710  -9.677  1.00 22.77           C  
ANISOU 2093  C   ASP B 124     3303   2512   2838   1647     88    -12       C  
ATOM   2094  O   ASP B 124     -47.196  12.496  -9.581  1.00 22.62           O  
ANISOU 2094  O   ASP B 124     3475   2224   2897   1594     69    -26       O  
ATOM   2095  CB  ASP B 124     -50.421  12.497 -10.353  1.00 26.39           C  
ANISOU 2095  CB  ASP B 124     3676   3247   3104   2104     89    -12       C  
ATOM   2096  CG  ASP B 124     -50.180  13.883  -9.766  1.00 29.66           C  
ANISOU 2096  CG  ASP B 124     4339   3395   3537   2275     61    -94       C  
ATOM   2097  OD1 ASP B 124     -50.276  14.002  -8.528  1.00 33.13           O  
ANISOU 2097  OD1 ASP B 124     4774   3878   3936   2314     59   -213       O  
ATOM   2098  OD2 ASP B 124     -49.895  14.837 -10.535  1.00 30.11           O  
ANISOU 2098  OD2 ASP B 124     4602   3196   3640   2361     39    -39       O  
ATOM   2099  N   MET B 125     -48.373  10.715  -8.818  1.00 21.09           N  
ANISOU 2099  N   MET B 125     2924   2508   2580   1556    104    -51       N  
ATOM   2100  CA  MET B 125     -47.530  10.482  -7.650  1.00 20.49           C  
ANISOU 2100  CA  MET B 125     2871   2373   2539   1416    100   -115       C  
ATOM   2101  C   MET B 125     -46.077  10.233  -8.064  1.00 19.08           C  
ANISOU 2101  C   MET B 125     2770   2001   2480   1200     92    -61       C  
ATOM   2102  O   MET B 125     -45.149  10.764  -7.446  1.00 19.35           O  
ANISOU 2102  O   MET B 125     2920   1873   2558   1127     77   -112       O  
ATOM   2103  CB  MET B 125     -48.077   9.311  -6.809  1.00 19.66           C  
ANISOU 2103  CB  MET B 125     2567   2547   2355   1342    118   -130       C  
ATOM   2104  CG  MET B 125     -47.138   8.805  -5.721  1.00 20.35           C  
ANISOU 2104  CG  MET B 125     2653   2604   2476   1175    114   -163       C  
ATOM   2105  SD  MET B 125     -47.925   7.539  -4.686  1.00 23.29           S  
ANISOU 2105  SD  MET B 125     2816   3301   2732   1101    132   -161       S  
ATOM   2106  CE  MET B 125     -46.492   6.703  -4.022  1.00 22.11           C  
ANISOU 2106  CE  MET B 125     2691   3051   2659    878    122   -132       C  
ATOM   2107  N   PHE B 126     -45.883   9.428  -9.104  1.00 17.98           N  
ANISOU 2107  N   PHE B 126     2556   1900   2374   1097    102     35       N  
ATOM   2108  CA  PHE B 126     -44.519   9.045  -9.511  1.00 16.95           C  
ANISOU 2108  CA  PHE B 126     2461   1646   2332    906     96     83       C  
ATOM   2109  C   PHE B 126     -43.894   9.987 -10.551  1.00 17.49           C  
ANISOU 2109  C   PHE B 126     2672   1516   2457    899     85    138       C  
ATOM   2110  O   PHE B 126     -42.685   9.924 -10.802  1.00 17.04           O  
ANISOU 2110  O   PHE B 126     2653   1365   2456    743     79    167       O  
ATOM   2111  CB  PHE B 126     -44.467   7.579  -9.951  1.00 15.62           C  
ANISOU 2111  CB  PHE B 126     2150   1620   2166    790    109    140       C  
ATOM   2112  CG  PHE B 126     -44.440   6.617  -8.797  1.00 15.11           C  
ANISOU 2112  CG  PHE B 126     1998   1670   2072    712    111    107       C  
ATOM   2113  CD1 PHE B 126     -43.227   6.089  -8.347  1.00 14.44           C  
ANISOU 2113  CD1 PHE B 126     1924   1529   2032    580    102    109       C  
ATOM   2114  CD2 PHE B 126     -45.614   6.268  -8.131  1.00 15.53           C  
ANISOU 2114  CD2 PHE B 126     1955   1908   2036    774    122     79       C  
ATOM   2115  CE1 PHE B 126     -43.177   5.215  -7.249  1.00 14.16           C  
ANISOU 2115  CE1 PHE B 126     1824   1595   1962    521    100     94       C  
ATOM   2116  CE2 PHE B 126     -45.577   5.392  -7.026  1.00 15.44           C  
ANISOU 2116  CE2 PHE B 126     1873   2005   1988    687    123     66       C  
ATOM   2117  CZ  PHE B 126     -44.343   4.863  -6.594  1.00 14.56           C  
ANISOU 2117  CZ  PHE B 126     1794   1807   1931    565    111     79       C  
ATOM   2118  N   SER B 127     -44.707  10.888 -11.108  1.00 18.69           N  
ANISOU 2118  N   SER B 127     2903   1618   2579   1070     81    155       N  
ATOM   2119  CA  SER B 127     -44.245  11.823 -12.145  1.00 19.67           C  
ANISOU 2119  CA  SER B 127     3181   1550   2744   1071     68    231       C  
ATOM   2120  C   SER B 127     -43.196  12.846 -11.684  1.00 21.36           C  
ANISOU 2120  C   SER B 127     3596   1511   3007    973     45    199       C  
ATOM   2121  O   SER B 127     -42.476  13.383 -12.521  1.00 21.81           O  
ANISOU 2121  O   SER B 127     3762   1423   3101    877     36    278       O  
ATOM   2122  CB  SER B 127     -45.424  12.544 -12.829  1.00 21.08           C  
ANISOU 2122  CB  SER B 127     3409   1738   2865   1308     64    268       C  
ATOM   2123  OG  SER B 127     -46.191  13.276 -11.890  1.00 22.22           O  
ANISOU 2123  OG  SER B 127     3628   1858   2957   1503     53    172       O  
ATOM   2124  N   ARG B 128     -43.092  13.122 -10.381  1.00 22.73           N  
ANISOU 2124  N   ARG B 128     3817   1647   3172    977     36     84       N  
ATOM   2125  CA  ARG B 128     -42.049  14.049  -9.896  1.00 25.00           C  
ANISOU 2125  CA  ARG B 128     4293   1707   3498    846     11     38       C  
ATOM   2126  C   ARG B 128     -40.627  13.546 -10.204  1.00 24.03           C  
ANISOU 2126  C   ARG B 128     4113   1599   3418    578     14     92       C  
ATOM   2127  O   ARG B 128     -39.679  14.322 -10.235  1.00 25.01           O  
ANISOU 2127  O   ARG B 128     4381   1555   3566    424     -5     95       O  
ATOM   2128  CB  ARG B 128     -42.188  14.332  -8.394  1.00 26.48           C  
ANISOU 2128  CB  ARG B 128     4517   1893   3654    893      0   -112       C  
ATOM   2129  CG  ARG B 128     -41.887  13.144  -7.485  1.00 27.00           C  
ANISOU 2129  CG  ARG B 128     4376   2182   3700    792     16   -155       C  
ATOM   2130  CD  ARG B 128     -41.826  13.540  -6.002  1.00 31.25           C  
ANISOU 2130  CD  ARG B 128     4959   2716   4198    807      2   -301       C  
ATOM   2131  NE  ARG B 128     -40.460  13.740  -5.499  1.00 34.37           N  
ANISOU 2131  NE  ARG B 128     5408   3032   4619    583    -15   -340       N  
ATOM   2132  CZ  ARG B 128     -40.076  13.514  -4.239  1.00 35.31           C  
ANISOU 2132  CZ  ARG B 128     5469   3251   4699    519    -20   -439       C  
ATOM   2133  NH1 ARG B 128     -38.816  13.722  -3.874  1.00 36.49           N  
ANISOU 2133  NH1 ARG B 128     5653   3355   4857    309    -37   -470       N  
ATOM   2134  NH2 ARG B 128     -40.941  13.064  -3.338  1.00 34.25           N  
ANISOU 2134  NH2 ARG B 128     5223   3291   4499    656     -9   -503       N  
ATOM   2135  N   PHE B 129     -40.490  12.248 -10.447  1.00 22.15           N  
ANISOU 2135  N   PHE B 129     3668   1569   3179    522     35    132       N  
ATOM   2136  CA  PHE B 129     -39.172  11.668 -10.661  1.00 21.65           C  
ANISOU 2136  CA  PHE B 129     3526   1562   3137    313     36    169       C  
ATOM   2137  C   PHE B 129     -38.711  11.680 -12.112  1.00 21.43           C  
ANISOU 2137  C   PHE B 129     3493   1524   3124    239     41    287       C  
ATOM   2138  O   PHE B 129     -37.529  11.489 -12.374  1.00 21.60           O  
ANISOU 2138  O   PHE B 129     3474   1586   3148     66     39    317       O  
ATOM   2139  CB  PHE B 129     -39.112  10.256 -10.083  1.00 20.34           C  
ANISOU 2139  CB  PHE B 129     3170   1603   2956    299     49    144       C  
ATOM   2140  CG  PHE B 129     -39.541  10.185  -8.656  1.00 21.35           C  
ANISOU 2140  CG  PHE B 129     3283   1776   3054    357     45     43       C  
ATOM   2141  CD1 PHE B 129     -38.826  10.849  -7.669  1.00 23.12           C  
ANISOU 2141  CD1 PHE B 129     3587   1929   3269    272     27    -39       C  
ATOM   2142  CD2 PHE B 129     -40.677   9.477  -8.297  1.00 21.22           C  
ANISOU 2142  CD2 PHE B 129     3167   1893   3001    484     59     28       C  
ATOM   2143  CE1 PHE B 129     -39.229  10.787  -6.344  1.00 22.88           C  
ANISOU 2143  CE1 PHE B 129     3533   1965   3197    331     23   -137       C  
ATOM   2144  CE2 PHE B 129     -41.083   9.412  -6.978  1.00 20.36           C  
ANISOU 2144  CE2 PHE B 129     3031   1858   2846    533     57    -57       C  
ATOM   2145  CZ  PHE B 129     -40.367  10.069  -6.007  1.00 22.49           C  
ANISOU 2145  CZ  PHE B 129     3377   2059   3109    468     40   -141       C  
ATOM   2146  N   GLY B 130     -39.631  11.907 -13.049  1.00 21.27           N  
ANISOU 2146  N   GLY B 130     3501   1483   3098    374     48    353       N  
ATOM   2147  CA  GLY B 130     -39.272  11.923 -14.459  1.00 20.93           C  
ANISOU 2147  CA  GLY B 130     3444   1454   3055    315     54    469       C  
ATOM   2148  C   GLY B 130     -40.354  11.403 -15.381  1.00 20.21           C  
ANISOU 2148  C   GLY B 130     3258   1482   2938    468     70    523       C  
ATOM   2149  O   GLY B 130     -41.501  11.232 -14.976  1.00 19.40           O  
ANISOU 2149  O   GLY B 130     3123   1435   2812    631     74    478       O  
ATOM   2150  N   ARG B 131     -39.982  11.166 -16.630  1.00 19.95           N  
ANISOU 2150  N   ARG B 131     3170   1517   2894    408     78    616       N  
ATOM   2151  CA  ARG B 131     -40.926  10.723 -17.644  1.00 20.25           C  
ANISOU 2151  CA  ARG B 131     3116   1683   2896    531     90    668       C  
ATOM   2152  C   ARG B 131     -41.404   9.296 -17.402  1.00 18.80           C  
ANISOU 2152  C   ARG B 131     2751   1692   2698    557    104    603       C  
ATOM   2153  O   ARG B 131     -40.612   8.364 -17.303  1.00 17.64           O  
ANISOU 2153  O   ARG B 131     2515   1623   2566    446    108    575       O  
ATOM   2154  CB  ARG B 131     -40.308  10.858 -19.039  1.00 20.78           C  
ANISOU 2154  CB  ARG B 131     3168   1786   2941    446     94    781       C  
ATOM   2155  CG  ARG B 131     -41.138  10.252 -20.165  1.00 21.82           C  
ANISOU 2155  CG  ARG B 131     3176   2092   3023    547    107    826       C  
ATOM   2156  CD  ARG B 131     -40.567  10.627 -21.547  1.00 24.86           C  
ANISOU 2156  CD  ARG B 131     3566   2509   3373    476    109    949       C  
ATOM   2157  NE  ARG B 131     -41.268   9.915 -22.623  1.00 26.34           N  
ANISOU 2157  NE  ARG B 131     3610   2898   3502    556    121    974       N  
ATOM   2158  CZ  ARG B 131     -40.846   9.826 -23.883  1.00 28.26           C  
ANISOU 2158  CZ  ARG B 131     3789   3255   3695    501    127   1056       C  
ATOM   2159  NH1 ARG B 131     -41.565   9.147 -24.771  1.00 29.34           N  
ANISOU 2159  NH1 ARG B 131     3792   3584   3771    578    136   1056       N  
ATOM   2160  NH2 ARG B 131     -39.714  10.408 -24.264  1.00 28.44           N  
ANISOU 2160  NH2 ARG B 131     3870   3223   3714    356    125   1135       N  
ATOM   2161  N   ILE B 132     -42.716   9.143 -17.307  1.00 18.89           N  
ANISOU 2161  N   ILE B 132     2720   1787   2673    706    109    581       N  
ATOM   2162  CA  ILE B 132     -43.318   7.826 -17.239  1.00 17.96           C  
ANISOU 2162  CA  ILE B 132     2445   1853   2526    706    121    535       C  
ATOM   2163  C   ILE B 132     -43.668   7.362 -18.653  1.00 17.46           C  
ANISOU 2163  C   ILE B 132     2290   1925   2420    718    129    592       C  
ATOM   2164  O   ILE B 132     -44.353   8.062 -19.407  1.00 17.27           O  
ANISOU 2164  O   ILE B 132     2285   1926   2351    830    128    652       O  
ATOM   2165  CB  ILE B 132     -44.547   7.803 -16.292  1.00 18.49           C  
ANISOU 2165  CB  ILE B 132     2481   1994   2552    825    123    474       C  
ATOM   2166  CG1 ILE B 132     -44.064   7.976 -14.841  1.00 19.25           C  
ANISOU 2166  CG1 ILE B 132     2639   1993   2683    786    116    402       C  
ATOM   2167  CG2 ILE B 132     -45.343   6.486 -16.460  1.00 16.68           C  
ANISOU 2167  CG2 ILE B 132     2094   1974   2272    799    134    449       C  
ATOM   2168  CD1 ILE B 132     -45.124   8.464 -13.878  1.00 21.94           C  
ANISOU 2168  CD1 ILE B 132     2991   2373   2973    930    115    343       C  
ATOM   2169  N   ILE B 133     -43.153   6.185 -18.985  1.00 16.28           N  
ANISOU 2169  N   ILE B 133     2048   1860   2277    612    132    567       N  
ATOM   2170  CA  ILE B 133     -43.364   5.532 -20.269  1.00 16.45           C  
ANISOU 2170  CA  ILE B 133     1975   2022   2254    601    138    591       C  
ATOM   2171  C   ILE B 133     -44.682   4.737 -20.267  1.00 16.87           C  
ANISOU 2171  C   ILE B 133     1927   2236   2246    640    142    546       C  
ATOM   2172  O   ILE B 133     -45.433   4.767 -21.236  1.00 17.77           O  
ANISOU 2172  O   ILE B 133     1974   2486   2294    694    146    575       O  
ATOM   2173  CB  ILE B 133     -42.175   4.575 -20.566  1.00 15.30           C  
ANISOU 2173  CB  ILE B 133     1791   1890   2134    484    136    562       C  
ATOM   2174  CG1 ILE B 133     -40.882   5.365 -20.830  1.00 15.88           C  
ANISOU 2174  CG1 ILE B 133     1922   1880   2232    424    134    617       C  
ATOM   2175  CG2 ILE B 133     -42.478   3.644 -21.727  1.00 14.92           C  
ANISOU 2175  CG2 ILE B 133     1644   1993   2033    473    139    546       C  
ATOM   2176  CD1 ILE B 133     -40.975   6.410 -21.960  1.00 15.88           C  
ANISOU 2176  CD1 ILE B 133     1953   1887   2195    455    137    722       C  
ATOM   2177  N   ASN B 134     -44.930   4.011 -19.182  1.00 16.83           N  
ANISOU 2177  N   ASN B 134     1908   2235   2254    596    141    480       N  
ATOM   2178  CA  ASN B 134     -46.144   3.219 -19.019  1.00 18.59           C  
ANISOU 2178  CA  ASN B 134     2037   2618   2408    587    144    440       C  
ATOM   2179  C   ASN B 134     -46.398   2.934 -17.551  1.00 18.48           C  
ANISOU 2179  C   ASN B 134     2037   2581   2403    559    142    395       C  
ATOM   2180  O   ASN B 134     -45.470   2.950 -16.742  1.00 18.27           O  
ANISOU 2180  O   ASN B 134     2083   2417   2443    521    137    382       O  
ATOM   2181  CB  ASN B 134     -46.101   1.910 -19.830  1.00 18.68           C  
ANISOU 2181  CB  ASN B 134     1987   2713   2397    477    139    406       C  
ATOM   2182  CG  ASN B 134     -45.124   0.904 -19.273  1.00 19.80           C  
ANISOU 2182  CG  ASN B 134     2184   2737   2600    374    128    362       C  
ATOM   2183  N   SER B 135     -47.663   2.692 -17.218  1.00 19.38           N  
ANISOU 2183  N   SER B 135     2065   2863   2433    576    148    376       N  
ATOM   2184  CA  SER B 135     -48.082   2.433 -15.855  1.00 20.09           C  
ANISOU 2184  CA  SER B 135     2144   2988   2503    548    149    342       C  
ATOM   2185  C   SER B 135     -49.312   1.532 -15.862  1.00 20.76           C  
ANISOU 2185  C   SER B 135     2107   3300   2480    465    153    323       C  
ATOM   2186  O   SER B 135     -50.081   1.526 -16.831  1.00 21.47           O  
ANISOU 2186  O   SER B 135     2109   3555   2495    487    157    332       O  
ATOM   2187  CB  SER B 135     -48.439   3.737 -15.151  1.00 21.56           C  
ANISOU 2187  CB  SER B 135     2358   3165   2670    712    153    338       C  
ATOM   2188  OG  SER B 135     -49.563   4.340 -15.779  1.00 23.99           O  
ANISOU 2188  OG  SER B 135     2587   3644   2882    850    159    354       O  
ATOM   2189  N   ARG B 136     -49.492   0.792 -14.771  1.00 19.90           N  
ANISOU 2189  N   ARG B 136     1991   3217   2353    356    151    304       N  
ATOM   2190  CA  ARG B 136     -50.615  -0.109 -14.619  1.00 20.77           C  
ANISOU 2190  CA  ARG B 136     1996   3544   2352    227    153    294       C  
ATOM   2191  C   ARG B 136     -50.873  -0.367 -13.142  1.00 20.77           C  
ANISOU 2191  C   ARG B 136     1985   3590   2315    169    156    291       C  
ATOM   2192  O   ARG B 136     -49.983  -0.822 -12.426  1.00 19.47           O  
ANISOU 2192  O   ARG B 136     1921   3248   2227    102    146    298       O  
ATOM   2193  CB  ARG B 136     -50.333  -1.443 -15.327  1.00 20.82           C  
ANISOU 2193  CB  ARG B 136     2043   3491   2378     41    139    286       C  
ATOM   2194  CG  ARG B 136     -51.563  -2.345 -15.481  1.00 22.28           C  
ANISOU 2194  CG  ARG B 136     2124   3908   2433   -129    138    274       C  
ATOM   2195  CD  ARG B 136     -52.373  -1.976 -16.721  1.00 24.01           C  
ANISOU 2195  CD  ARG B 136     2218   4342   2563    -75    145    262       C  
ATOM   2196  N   VAL B 137     -52.081  -0.061 -12.685  1.00 21.55           N  
ANISOU 2196  N   VAL B 137     1951   3956   2283    207    169    282       N  
ATOM   2197  CA  VAL B 137     -52.523  -0.553 -11.388  1.00 22.41           C  
ANISOU 2197  CA  VAL B 137     2015   4183   2318    102    173    285       C  
ATOM   2198  C   VAL B 137     -53.197  -1.903 -11.631  1.00 23.60           C  
ANISOU 2198  C   VAL B 137     2113   4470   2384   -156    167    306       C  
ATOM   2199  O   VAL B 137     -54.127  -2.011 -12.441  1.00 23.73           O  
ANISOU 2199  O   VAL B 137     2010   4708   2297   -192    171    297       O  
ATOM   2200  CB  VAL B 137     -53.476   0.427 -10.669  1.00 23.67           C  
ANISOU 2200  CB  VAL B 137     2046   4594   2355    271    189    257       C  
ATOM   2201  CG1 VAL B 137     -53.793  -0.070  -9.257  1.00 23.98           C  
ANISOU 2201  CG1 VAL B 137     2036   4760   2314    158    194    264       C  
ATOM   2202  CG2 VAL B 137     -52.864   1.835 -10.629  1.00 22.90           C  
ANISOU 2202  CG2 VAL B 137     2037   4325   2340    529    189    227       C  
ATOM   2203  N   LEU B 138     -52.702  -2.930 -10.947  1.00 23.40           N  
ANISOU 2203  N   LEU B 138     2189   4304   2396   -337    153    337       N  
ATOM   2204  CA  LEU B 138     -53.182  -4.285 -11.152  1.00 25.38           C  
ANISOU 2204  CA  LEU B 138     2454   4605   2585   -609    139    361       C  
ATOM   2205  C   LEU B 138     -54.454  -4.518 -10.339  1.00 27.26           C  
ANISOU 2205  C   LEU B 138     2536   5180   2642   -745    152    385       C  
ATOM   2206  O   LEU B 138     -54.585  -4.002  -9.229  1.00 27.54           O  
ANISOU 2206  O   LEU B 138     2513   5317   2632   -664    165    396       O  
ATOM   2207  CB  LEU B 138     -52.098  -5.322 -10.795  1.00 24.91           C  
ANISOU 2207  CB  LEU B 138     2600   4229   2637   -730    112    394       C  
ATOM   2208  CG  LEU B 138     -50.683  -5.230 -11.399  1.00 24.54           C  
ANISOU 2208  CG  LEU B 138     2703   3869   2753   -603     97    373       C  
ATOM   2209  CD1 LEU B 138     -50.024  -6.618 -11.437  1.00 25.57           C  
ANISOU 2209  CD1 LEU B 138     3017   3761   2938   -758     64    393       C  
ATOM   2210  CD2 LEU B 138     -50.640  -4.601 -12.796  1.00 24.39           C  
ANISOU 2210  CD2 LEU B 138     2636   3867   2764   -481    105    326       C  
ATOM   2211  N   VAL B 139     -55.384  -5.283 -10.907  1.00 29.39           N  
ANISOU 2211  N   VAL B 139     2729   5644   2795   -960    148    387       N  
ATOM   2212  CA  VAL B 139     -56.650  -5.617 -10.250  1.00 32.24           C  
ANISOU 2212  CA  VAL B 139     2920   6377   2955  -1141    160    415       C  
ATOM   2213  C   VAL B 139     -56.789  -7.136 -10.173  1.00 34.04           C  
ANISOU 2213  C   VAL B 139     3262   6523   3147  -1511    135    464       C  
ATOM   2214  O   VAL B 139     -56.212  -7.849 -11.003  1.00 33.95           O  
ANISOU 2214  O   VAL B 139     3420   6242   3238  -1601    110    447       O  
ATOM   2215  CB  VAL B 139     -57.872  -5.072 -11.051  1.00 33.37           C  
ANISOU 2215  CB  VAL B 139     2822   6921   2934  -1085    177    372       C  
ATOM   2216  CG2 VAL B 139     -57.843  -3.554 -11.141  1.00 32.75           C  
ANISOU 2216  CG2 VAL B 139     2654   6917   2874   -705    196    330       C  
ATOM   2217  N   ASP B 140     -57.557  -7.630  -9.198  1.00 36.62           N  
ANISOU 2217  N   ASP B 140     3507   7083   3323  -1727    140    524       N  
ATOM   2218  CA  ASP B 140     -57.934  -9.054  -9.158  1.00 39.25           C  
ANISOU 2218  CA  ASP B 140     3942   7387   3584  -2125    115    581       C  
ATOM   2219  C   ASP B 140     -58.718  -9.385 -10.419  1.00 41.01           C  
ANISOU 2219  C   ASP B 140     4079   7786   3717  -2279    110    522       C  
ATOM   2220  O   ASP B 140     -59.649  -8.662 -10.775  1.00 41.77           O  
ANISOU 2220  O   ASP B 140     3916   8282   3672  -2191    134    480       O  
ATOM   2221  CB  ASP B 140     -58.782  -9.385  -7.926  1.00 41.27           C  
ANISOU 2221  CB  ASP B 140     4078   7950   3653  -2342    127    664       C  
ATOM   2222  N   GLN B 141     -58.339 -10.472 -11.089  1.00 42.00           N  
ANISOU 2222  N   GLN B 141     4421   7622   3913  -2493     75    512       N  
ATOM   2223  CA  GLN B 141     -58.900 -10.806 -12.392  1.00 43.50           C  
ANISOU 2223  CA  GLN B 141     4561   7928   4040  -2628     64    436       C  
ATOM   2224  C   GLN B 141     -60.372 -11.218 -12.371  1.00 46.31           C  
ANISOU 2224  C   GLN B 141     4707   8749   4141  -2956     71    448       C  
ATOM   2225  O   GLN B 141     -60.996 -11.306 -13.421  1.00 47.45           O  
ANISOU 2225  O   GLN B 141     4739   9097   4194  -3048     67    377       O  
ATOM   2226  CB  GLN B 141     -58.031 -11.839 -13.120  1.00 43.62           C  
ANISOU 2226  CB  GLN B 141     4883   7489   4200  -2742     21    400       C  
ATOM   2227  CG  GLN B 141     -56.765 -11.241 -13.732  1.00 42.29           C  
ANISOU 2227  CG  GLN B 141     4824   7006   4238  -2390     20    346       C  
ATOM   2228  CD  GLN B 141     -57.058 -10.177 -14.789  1.00 42.99           C  
ANISOU 2228  CD  GLN B 141     4700   7332   4302  -2158     45    273       C  
ATOM   2229  OE1 GLN B 141     -56.855  -8.984 -14.560  1.00 43.43           O  
ANISOU 2229  OE1 GLN B 141     4635   7473   4395  -1859     73    283       O  
ATOM   2230  NE2 GLN B 141     -57.539 -10.610 -15.948  1.00 44.67           N  
ANISOU 2230  NE2 GLN B 141     4880   7648   4446  -2300     32    199       N  
ATOM   2231  N   THR B 142     -60.933 -11.459 -11.190  1.00 47.82           N  
ANISOU 2231  N   THR B 142     4826   9143   4201  -3139     80    537       N  
ATOM   2232  CA  THR B 142     -62.361 -11.783 -11.104  1.00 50.63           C  
ANISOU 2232  CA  THR B 142     4941  10012   4284  -3459     90    554       C  
ATOM   2233  C   THR B 142     -63.184 -10.660 -10.459  1.00 50.66           C  
ANISOU 2233  C   THR B 142     4593  10541   4116  -3247    135    561       C  
ATOM   2234  O   THR B 142     -64.270 -10.332 -10.938  1.00 52.42           O  
ANISOU 2234  O   THR B 142     4529  11255   4134  -3281    151    518       O  
ATOM   2235  CB  THR B 142     -62.622 -13.152 -10.407  1.00 53.02           C  
ANISOU 2235  CB  THR B 142     5417  10223   4504  -3944     61    653       C  
ATOM   2236  OG1 THR B 142     -62.683 -12.979  -8.985  1.00 53.72           O  
ANISOU 2236  OG1 THR B 142     5450  10428   4531  -3939     80    761       O  
ATOM   2237  N   THR B 143     -62.653 -10.069  -9.390  1.00 49.01           N  
ANISOU 2237  N   THR B 143     4405  10238   3980  -3013    151    607       N  
ATOM   2238  CA  THR B 143     -63.345  -8.992  -8.673  1.00 48.78           C  
ANISOU 2238  CA  THR B 143     4074  10667   3793  -2777    190    600       C  
ATOM   2239  C   THR B 143     -63.258  -7.643  -9.396  1.00 46.73           C  
ANISOU 2239  C   THR B 143     3686  10481   3589  -2317    209    504       C  
ATOM   2240  O   THR B 143     -64.196  -6.844  -9.343  1.00 48.17           O  
ANISOU 2240  O   THR B 143     3575  11144   3581  -2150    234    468       O  
ATOM   2241  CB  THR B 143     -62.814  -8.833  -7.235  1.00 48.16           C  
ANISOU 2241  CB  THR B 143     4069  10470   3762  -2694    199    672       C  
ATOM   2242  OG1 THR B 143     -61.537  -8.183  -7.265  1.00 45.01           O  
ANISOU 2242  OG1 THR B 143     3862   9623   3617  -2346    194    637       O  
ATOM   2243  N   GLY B 144     -62.134  -7.403 -10.067  1.00 43.54           N  
ANISOU 2243  N   GLY B 144     3504   9608   3431  -2113    194    468       N  
ATOM   2244  CA  GLY B 144     -61.870  -6.125 -10.736  1.00 40.91           C  
ANISOU 2244  CA  GLY B 144     3109   9257   3178  -1687    207    397       C  
ATOM   2245  C   GLY B 144     -61.363  -5.054  -9.785  1.00 38.96           C  
ANISOU 2245  C   GLY B 144     2871   8927   3004  -1347    224    394       C  
ATOM   2246  O   GLY B 144     -61.145  -3.906 -10.187  1.00 37.77           O  
ANISOU 2246  O   GLY B 144     2693   8743   2914   -989    233    343       O  
ATOM   2247  N   LEU B 145     -61.171  -5.435  -8.523  1.00 38.37           N  
ANISOU 2247  N   LEU B 145     2848   8811   2917  -1469    226    450       N  
ATOM   2248  CA  LEU B 145     -60.791  -4.495  -7.475  1.00 37.17           C  
ANISOU 2248  CA  LEU B 145     2687   8634   2800  -1187    242    436       C  
ATOM   2249  C   LEU B 145     -59.277  -4.311  -7.385  1.00 34.64           C  
ANISOU 2249  C   LEU B 145     2643   7772   2747  -1043    226    437       C  
ATOM   2250  O   LEU B 145     -58.509  -5.258  -7.610  1.00 33.37           O  
ANISOU 2250  O   LEU B 145     2693   7269   2718  -1239    202    481       O  
ATOM   2251  CB  LEU B 145     -61.357  -4.933  -6.119  1.00 38.65           C  
ANISOU 2251  CB  LEU B 145     2763   9105   2816  -1378    254    496       C  
ATOM   2252  CG  LEU B 145     -62.880  -4.933  -5.939  1.00 41.47           C  
ANISOU 2252  CG  LEU B 145     2795  10095   2867  -1487    275    493       C  
ATOM   2253  CD1 LEU B 145     -63.251  -5.425  -4.539  1.00 41.32           C  
ANISOU 2253  CD1 LEU B 145     2693  10315   2692  -1699    286    567       C  
ATOM   2254  CD2 LEU B 145     -63.473  -3.550  -6.186  1.00 41.50           C  
ANISOU 2254  CD2 LEU B 145     2584  10410   2772  -1072    296    395       C  
ATOM   2255  N   SER B 146     -58.869  -3.085  -7.061  1.00 33.46           N  
ANISOU 2255  N   SER B 146     2494   7559   2662   -698    237    382       N  
ATOM   2256  CA  SER B 146     -57.456  -2.715  -6.984  1.00 32.06           C  
ANISOU 2256  CA  SER B 146     2545   6923   2715   -544    224    371       C  
ATOM   2257  C   SER B 146     -56.710  -3.483  -5.892  1.00 31.67           C  
ANISOU 2257  C   SER B 146     2634   6672   2726   -713    212    435       C  
ATOM   2258  O   SER B 146     -57.226  -3.690  -4.785  1.00 32.06           O  
ANISOU 2258  O   SER B 146     2584   6958   2638   -807    222    468       O  
ATOM   2259  CB  SER B 146     -57.298  -1.209  -6.751  1.00 31.42           C  
ANISOU 2259  CB  SER B 146     2435   6845   2660   -171    236    295       C  
ATOM   2260  OG  SER B 146     -55.943  -0.895  -6.461  1.00 30.96           O  
ANISOU 2260  OG  SER B 146     2582   6386   2796    -75    223    288       O  
ATOM   2261  N   ARG B 147     -55.485  -3.884  -6.221  1.00 30.41           N  
ANISOU 2261  N   ARG B 147     2696   6098   2759   -736    190    455       N  
ATOM   2262  CA  ARG B 147     -54.657  -4.677  -5.317  1.00 30.09           C  
ANISOU 2262  CA  ARG B 147     2812   5836   2785   -872    172    524       C  
ATOM   2263  C   ARG B 147     -53.649  -3.834  -4.550  1.00 28.67           C  
ANISOU 2263  C   ARG B 147     2701   5485   2708   -648    173    492       C  
ATOM   2264  O   ARG B 147     -52.942  -4.346  -3.679  1.00 28.77           O  
ANISOU 2264  O   ARG B 147     2818   5354   2758   -719    159    546       O  
ATOM   2265  CB  ARG B 147     -53.946  -5.793  -6.086  1.00 29.91           C  
ANISOU 2265  CB  ARG B 147     2992   5490   2884  -1039    142    564       C  
ATOM   2266  CG  ARG B 147     -54.894  -6.772  -6.748  1.00 33.19           C  
ANISOU 2266  CG  ARG B 147     3373   6045   3194  -1314    135    591       C  
ATOM   2267  CD  ARG B 147     -54.374  -8.195  -6.674  1.00 36.76           C  
ANISOU 2267  CD  ARG B 147     4051   6217   3700  -1562    100    666       C  
ATOM   2268  NE  ARG B 147     -53.380  -8.496  -7.698  1.00 37.37           N  
ANISOU 2268  NE  ARG B 147     4313   5943   3944  -1490     76    627       N  
ATOM   2269  CZ  ARG B 147     -52.081  -8.670  -7.471  1.00 37.47           C  
ANISOU 2269  CZ  ARG B 147     4507   5630   4101  -1375     55    641       C  
ATOM   2270  NH1 ARG B 147     -51.275  -8.945  -8.485  1.00 37.96           N  
ANISOU 2270  NH1 ARG B 147     4705   5433   4286  -1307     35    595       N  
ATOM   2271  NH2 ARG B 147     -51.584  -8.578  -6.244  1.00 36.80           N  
ANISOU 2271  NH2 ARG B 147     4454   5506   4023  -1324     54    698       N  
ATOM   2272  N   GLY B 148     -53.595  -2.543  -4.862  1.00 27.59           N  
ANISOU 2272  N   GLY B 148     2513   5366   2605   -383    186    406       N  
ATOM   2273  CA  GLY B 148     -52.547  -1.668  -4.339  1.00 25.99           C  
ANISOU 2273  CA  GLY B 148     2402   4961   2513   -186    182    359       C  
ATOM   2274  C   GLY B 148     -51.176  -1.963  -4.939  1.00 23.97           C  
ANISOU 2274  C   GLY B 148     2334   4332   2442   -191    160    376       C  
ATOM   2275  O   GLY B 148     -50.151  -1.517  -4.424  1.00 22.97           O  
ANISOU 2275  O   GLY B 148     2293   4034   2402    -96    152    355       O  
ATOM   2276  N   VAL B 149     -51.168  -2.718  -6.032  1.00 23.10           N  
ANISOU 2276  N   VAL B 149     2276   4126   2376   -304    150    405       N  
ATOM   2277  CA  VAL B 149     -49.941  -3.092  -6.717  1.00 21.22           C  
ANISOU 2277  CA  VAL B 149     2197   3577   2289   -301    129    413       C  
ATOM   2278  C   VAL B 149     -49.898  -2.381  -8.067  1.00 19.85           C  
ANISOU 2278  C   VAL B 149     2013   3356   2174   -176    135    365       C  
ATOM   2279  O   VAL B 149     -50.927  -2.252  -8.742  1.00 19.93           O  
ANISOU 2279  O   VAL B 149     1917   3553   2102   -184    147    351       O  
ATOM   2280  CB  VAL B 149     -49.833  -4.637  -6.892  1.00 21.71           C  
ANISOU 2280  CB  VAL B 149     2364   3529   2355   -523    105    480       C  
ATOM   2281  CG1 VAL B 149     -48.742  -5.000  -7.880  1.00 21.73           C  
ANISOU 2281  CG1 VAL B 149     2507   3259   2491   -486     84    466       C  
ATOM   2282  CG2 VAL B 149     -49.569  -5.317  -5.551  1.00 22.29           C  
ANISOU 2282  CG2 VAL B 149     2494   3582   2393   -625     92    551       C  
ATOM   2283  N   ALA B 150     -48.721  -1.899  -8.451  1.00 17.67           N  
ANISOU 2283  N   ALA B 150     1832   2858   2022    -66    127    345       N  
ATOM   2284  CA  ALA B 150     -48.578  -1.250  -9.754  1.00 16.70           C  
ANISOU 2284  CA  ALA B 150     1712   2683   1952     37    131    317       C  
ATOM   2285  C   ALA B 150     -47.240  -1.529 -10.417  1.00 15.65           C  
ANISOU 2285  C   ALA B 150     1694   2315   1938     41    115    321       C  
ATOM   2286  O   ALA B 150     -46.270  -1.869  -9.743  1.00 14.39           O  
ANISOU 2286  O   ALA B 150     1612   2026   1830     23    101    334       O  
ATOM   2287  CB  ALA B 150     -48.814   0.259  -9.632  1.00 17.07           C  
ANISOU 2287  CB  ALA B 150     1715   2784   1986    231    146    277       C  
ATOM   2288  N   PHE B 151     -47.210  -1.409 -11.751  1.00 15.47           N  
ANISOU 2288  N   PHE B 151     1667   2270   1940     70    116    312       N  
ATOM   2289  CA  PHE B 151     -45.953  -1.315 -12.515  1.00 15.02           C  
ANISOU 2289  CA  PHE B 151     1687   2042   1979    114    106    308       C  
ATOM   2290  C   PHE B 151     -45.838   0.114 -12.995  1.00 14.65           C  
ANISOU 2290  C   PHE B 151     1622   1992   1953    251    119    302       C  
ATOM   2291  O   PHE B 151     -46.838   0.694 -13.452  1.00 15.14           O  
ANISOU 2291  O   PHE B 151     1615   2182   1956    314    131    302       O  
ATOM   2292  CB  PHE B 151     -45.959  -2.221 -13.761  1.00 15.00           C  
ANISOU 2292  CB  PHE B 151     1698   2025   1977     46     96    299       C  
ATOM   2293  CG  PHE B 151     -45.700  -3.672 -13.479  1.00 16.68           C  
ANISOU 2293  CG  PHE B 151     1995   2149   2194    -77     73    301       C  
ATOM   2294  CD1 PHE B 151     -44.400  -4.141 -13.318  1.00 15.35           C  
ANISOU 2294  CD1 PHE B 151     1923   1816   2091    -47     54    300       C  
ATOM   2295  CD2 PHE B 151     -46.758  -4.586 -13.448  1.00 18.01           C  
ANISOU 2295  CD2 PHE B 151     2153   2403   2287   -225     68    303       C  
ATOM   2296  CE1 PHE B 151     -44.157  -5.481 -13.081  1.00 17.38           C  
ANISOU 2296  CE1 PHE B 151     2289   1967   2348   -128     27    304       C  
ATOM   2297  CE2 PHE B 151     -46.525  -5.937 -13.201  1.00 20.10           C  
ANISOU 2297  CE2 PHE B 151     2538   2544   2555   -347     41    311       C  
ATOM   2298  CZ  PHE B 151     -45.220  -6.383 -13.014  1.00 20.14           C  
ANISOU 2298  CZ  PHE B 151     2663   2355   2635   -282     19    312       C  
ATOM   2299  N   ILE B 152     -44.641   0.690 -12.878  1.00 13.74           N  
ANISOU 2299  N   ILE B 152     1572   1740   1909    295    114    302       N  
ATOM   2300  CA  ILE B 152     -44.345   1.999 -13.449  1.00 13.32           C  
ANISOU 2300  CA  ILE B 152     1541   1638   1883    391    120    310       C  
ATOM   2301  C   ILE B 152     -43.020   1.859 -14.169  1.00 12.98           C  
ANISOU 2301  C   ILE B 152     1537   1495   1897    358    112    324       C  
ATOM   2302  O   ILE B 152     -41.992   1.495 -13.552  1.00 11.80           O  
ANISOU 2302  O   ILE B 152     1421   1281   1781    317    100    314       O  
ATOM   2303  CB  ILE B 152     -44.199   3.157 -12.400  1.00 13.55           C  
ANISOU 2303  CB  ILE B 152     1617   1610   1920    460    121    289       C  
ATOM   2304  CG1 ILE B 152     -45.524   3.470 -11.671  1.00 15.84           C  
ANISOU 2304  CG1 ILE B 152     1855   2031   2134    533    131    263       C  
ATOM   2305  CG2 ILE B 152     -43.657   4.432 -13.075  1.00 13.37           C  
ANISOU 2305  CG2 ILE B 152     1666   1478   1936    523    121    307       C  
ATOM   2306  CD1 ILE B 152     -46.453   4.433 -12.374  1.00 17.12           C  
ANISOU 2306  CD1 ILE B 152     2000   2256   2250    671    139    270       C  
ATOM   2307  N   ARG B 153     -43.042   2.123 -15.477  1.00 12.44           N  
ANISOU 2307  N   ARG B 153     1451   1449   1825    382    117    349       N  
ATOM   2308  CA  ARG B 153     -41.800   2.181 -16.247  1.00 12.00           C  
ANISOU 2308  CA  ARG B 153     1415   1342   1804    358    112    366       C  
ATOM   2309  C   ARG B 153     -41.406   3.631 -16.471  1.00 12.41           C  
ANISOU 2309  C   ARG B 153     1516   1327   1872    392    117    406       C  
ATOM   2310  O   ARG B 153     -42.150   4.414 -17.082  1.00 12.92           O  
ANISOU 2310  O   ARG B 153     1588   1409   1913    459    124    442       O  
ATOM   2311  CB  ARG B 153     -41.920   1.457 -17.589  1.00 12.44           C  
ANISOU 2311  CB  ARG B 153     1421   1474   1833    346    113    367       C  
ATOM   2312  CG  ARG B 153     -40.686   1.636 -18.489  1.00 13.52           C  
ANISOU 2312  CG  ARG B 153     1553   1605   1981    335    111    387       C  
ATOM   2313  CD  ARG B 153     -40.742   0.801 -19.749  1.00 12.56           C  
ANISOU 2313  CD  ARG B 153     1378   1573   1821    331    109    367       C  
ATOM   2314  NE  ARG B 153     -40.411  -0.614 -19.512  1.00 13.18           N  
ANISOU 2314  NE  ARG B 153     1473   1634   1903    307     93    302       N  
ATOM   2315  CZ  ARG B 153     -39.168  -1.122 -19.468  1.00 14.19           C  
ANISOU 2315  CZ  ARG B 153     1610   1741   2039    320     80    276       C  
ATOM   2316  NH1 ARG B 153     -38.073  -0.362 -19.608  1.00 12.18           N  
ANISOU 2316  NH1 ARG B 153     1329   1513   1785    325     85    308       N  
ATOM   2317  NH2 ARG B 153     -39.011  -2.418 -19.285  1.00 14.54           N  
ANISOU 2317  NH2 ARG B 153     1697   1748   2080    327     60    218       N  
ATOM   2318  N   PHE B 154     -40.241   3.998 -15.953  1.00 12.40           N  
ANISOU 2318  N   PHE B 154     1556   1252   1902    342    109    403       N  
ATOM   2319  CA  PHE B 154     -39.706   5.317 -16.260  1.00 13.05           C  
ANISOU 2319  CA  PHE B 154     1706   1254   1996    326    109    446       C  
ATOM   2320  C   PHE B 154     -38.931   5.259 -17.563  1.00 13.20           C  
ANISOU 2320  C   PHE B 154     1687   1328   2000    279    112    496       C  
ATOM   2321  O   PHE B 154     -38.608   4.180 -18.049  1.00 13.25           O  
ANISOU 2321  O   PHE B 154     1615   1428   1990    268    112    475       O  
ATOM   2322  CB  PHE B 154     -38.806   5.827 -15.132  1.00 13.29           C  
ANISOU 2322  CB  PHE B 154     1793   1206   2050    261     99    415       C  
ATOM   2323  CG  PHE B 154     -39.558   6.380 -13.950  1.00 13.54           C  
ANISOU 2323  CG  PHE B 154     1887   1172   2086    318     96    369       C  
ATOM   2324  CD1 PHE B 154     -40.095   7.652 -13.990  1.00 14.61           C  
ANISOU 2324  CD1 PHE B 154     2128   1201   2221    379     95    381       C  
ATOM   2325  CD2 PHE B 154     -39.718   5.625 -12.796  1.00 13.21           C  
ANISOU 2325  CD2 PHE B 154     1805   1176   2037    320     93    315       C  
ATOM   2326  CE1 PHE B 154     -40.779   8.179 -12.883  1.00 14.96           C  
ANISOU 2326  CE1 PHE B 154     2229   1198   2256    457     90    320       C  
ATOM   2327  CE2 PHE B 154     -40.388   6.141 -11.687  1.00 13.47           C  
ANISOU 2327  CE2 PHE B 154     1879   1184   2057    375     91    266       C  
ATOM   2328  CZ  PHE B 154     -40.923   7.420 -11.738  1.00 14.41           C  
ANISOU 2328  CZ  PHE B 154     2094   1209   2173    451     91    259       C  
ATOM   2329  N   ASP B 155     -38.626   6.432 -18.105  1.00 14.37           N  
ANISOU 2329  N   ASP B 155     1901   1415   2145    250    113    561       N  
ATOM   2330  CA  ASP B 155     -37.765   6.572 -19.266  1.00 14.68           C  
ANISOU 2330  CA  ASP B 155     1903   1523   2153    179    117    624       C  
ATOM   2331  C   ASP B 155     -36.376   5.988 -18.918  1.00 14.48           C  
ANISOU 2331  C   ASP B 155     1810   1573   2117     84    111    586       C  
ATOM   2332  O   ASP B 155     -35.867   5.103 -19.613  1.00 14.06           O  
ANISOU 2332  O   ASP B 155     1657   1658   2030     88    113    573       O  
ATOM   2333  CB  ASP B 155     -37.716   8.070 -19.653  1.00 16.35           C  
ANISOU 2333  CB  ASP B 155     2237   1616   2361    143    114    714       C  
ATOM   2334  CG  ASP B 155     -36.791   8.370 -20.831  1.00 17.99           C  
ANISOU 2334  CG  ASP B 155     2410   1907   2520     37    118    801       C  
ATOM   2335  OD1 ASP B 155     -36.399   9.548 -20.948  1.00 20.08           O  
ANISOU 2335  OD1 ASP B 155     2791   2058   2779    -53    111    878       O  
ATOM   2336  OD2 ASP B 155     -36.454   7.462 -21.628  1.00 16.90           O  
ANISOU 2336  OD2 ASP B 155     2137   1942   2340     37    127    793       O  
ATOM   2337  N   LYS B 156     -35.790   6.462 -17.825  1.00 14.48           N  
ANISOU 2337  N   LYS B 156     1864   1502   2138     16    101    559       N  
ATOM   2338  CA  LYS B 156     -34.427   6.110 -17.462  1.00 14.64           C  
ANISOU 2338  CA  LYS B 156     1812   1622   2128    -74     94    532       C  
ATOM   2339  C   LYS B 156     -34.340   5.497 -16.074  1.00 14.08           C  
ANISOU 2339  C   LYS B 156     1733   1540   2077    -44     82    454       C  
ATOM   2340  O   LYS B 156     -35.085   5.878 -15.178  1.00 13.95           O  
ANISOU 2340  O   LYS B 156     1796   1409   2097    -14     80    427       O  
ATOM   2341  CB  LYS B 156     -33.533   7.354 -17.501  1.00 15.87           C  
ANISOU 2341  CB  LYS B 156     2023   1746   2259   -236     89    583       C  
ATOM   2342  CG  LYS B 156     -33.435   8.039 -18.838  1.00 17.92           C  
ANISOU 2342  CG  LYS B 156     2299   2026   2483   -298     98    684       C  
ATOM   2343  CD  LYS B 156     -32.443   9.184 -18.753  1.00 22.59           C  
ANISOU 2343  CD  LYS B 156     2957   2587   3041   -503     89    737       C  
ATOM   2344  CE  LYS B 156     -32.890  10.403 -19.573  1.00 26.57           C  
ANISOU 2344  CE  LYS B 156     3610   2941   3546   -555     89    851       C  
ATOM   2345  NZ  LYS B 156     -32.708  10.221 -21.043  1.00 27.56           N  
ANISOU 2345  NZ  LYS B 156     3642   3224   3607   -568    104    945       N  
ATOM   2346  N   ARG B 157     -33.398   4.569 -15.893  1.00 13.95           N  
ANISOU 2346  N   ARG B 157     1617   1658   2023    -41     74    420       N  
ATOM   2347  CA  ARG B 157     -33.175   3.939 -14.586  1.00 13.63           C  
ANISOU 2347  CA  ARG B 157     1566   1627   1987     -8     60    363       C  
ATOM   2348  C   ARG B 157     -32.885   4.961 -13.485  1.00 14.17           C  
ANISOU 2348  C   ARG B 157     1692   1634   2059   -105     53    344       C  
ATOM   2349  O   ARG B 157     -33.252   4.758 -12.330  1.00 13.89           O  
ANISOU 2349  O   ARG B 157     1683   1556   2039    -69     45    301       O  
ATOM   2350  CB  ARG B 157     -32.029   2.903 -14.646  1.00 13.82           C  
ANISOU 2350  CB  ARG B 157     1478   1821   1951     31     48    339       C  
ATOM   2351  CG  ARG B 157     -31.913   2.072 -13.355  1.00 13.74           C  
ANISOU 2351  CG  ARG B 157     1467   1816   1939     99     29    297       C  
ATOM   2352  CD  ARG B 157     -30.902   0.942 -13.497  1.00 15.01           C  
ANISOU 2352  CD  ARG B 157     1539   2130   2035    193     12    277       C  
ATOM   2353  NE  ARG B 157     -30.765   0.124 -12.293  1.00 15.76           N  
ANISOU 2353  NE  ARG B 157     1646   2223   2118    272     -9    256       N  
ATOM   2354  CZ  ARG B 157     -31.498  -0.950 -11.999  1.00 16.06           C  
ANISOU 2354  CZ  ARG B 157     1757   2158   2186    372    -20    254       C  
ATOM   2355  NH1 ARG B 157     -32.497  -1.354 -12.782  1.00 15.29           N  
ANISOU 2355  NH1 ARG B 157     1721   1955   2135    395    -10    256       N  
ATOM   2356  NH2 ARG B 157     -31.236  -1.626 -10.892  1.00 18.00           N  
ANISOU 2356  NH2 ARG B 157     2016   2415   2406    435    -42    253       N  
ATOM   2357  N   SER B 158     -32.212   6.048 -13.834  1.00 15.14           N  
ANISOU 2357  N   SER B 158     1837   1757   2157   -241     53    374       N  
ATOM   2358  CA  SER B 158     -31.904   7.079 -12.848  1.00 15.95           C  
ANISOU 2358  CA  SER B 158     2018   1785   2259   -358     42    342       C  
ATOM   2359  C   SER B 158     -33.171   7.717 -12.250  1.00 15.83           C  
ANISOU 2359  C   SER B 158     2144   1567   2303   -292     43    315       C  
ATOM   2360  O   SER B 158     -33.184   8.096 -11.074  1.00 16.16           O  
ANISOU 2360  O   SER B 158     2235   1560   2344   -316     31    251       O  
ATOM   2361  CB  SER B 158     -30.983   8.135 -13.447  1.00 17.32           C  
ANISOU 2361  CB  SER B 158     2214   1980   2388   -550     39    388       C  
ATOM   2362  OG  SER B 158     -31.487   8.574 -14.689  1.00 18.35           O  
ANISOU 2362  OG  SER B 158     2401   2033   2538   -544     52    468       O  
ATOM   2363  N   GLU B 159     -34.230   7.813 -13.053  1.00 15.49           N  
ANISOU 2363  N   GLU B 159     2153   1437   2296   -196     55    357       N  
ATOM   2364  CA  GLU B 159     -35.523   8.284 -12.554  1.00 15.47           C  
ANISOU 2364  CA  GLU B 159     2255   1294   2329    -89     57    329       C  
ATOM   2365  C   GLU B 159     -36.162   7.234 -11.633  1.00 14.50           C  
ANISOU 2365  C   GLU B 159     2062   1241   2207     15     59    275       C  
ATOM   2366  O   GLU B 159     -36.690   7.572 -10.570  1.00 14.72           O  
ANISOU 2366  O   GLU B 159     2139   1219   2235     54     54    217       O  
ATOM   2367  CB  GLU B 159     -36.456   8.617 -13.708  1.00 15.56           C  
ANISOU 2367  CB  GLU B 159     2313   1243   2355     -4     68    395       C  
ATOM   2368  CG  GLU B 159     -35.933   9.712 -14.629  1.00 17.25           C  
ANISOU 2368  CG  GLU B 159     2621   1371   2562   -106     65    472       C  
ATOM   2369  CD  GLU B 159     -36.634   9.734 -15.978  1.00 18.59           C  
ANISOU 2369  CD  GLU B 159     2786   1550   2726    -23     77    558       C  
ATOM   2370  OE1 GLU B 159     -37.122   8.673 -16.422  1.00 18.07           O  
ANISOU 2370  OE1 GLU B 159     2601   1613   2653     65     89    554       O  
ATOM   2371  OE2 GLU B 159     -36.696  10.817 -16.601  1.00 22.22           O  
ANISOU 2371  OE2 GLU B 159     3373   1887   3183    -51     71    631       O  
ATOM   2372  N   ALA B 160     -36.113   5.968 -12.044  1.00 13.64           N  
ANISOU 2372  N   ALA B 160     1848   1245   2090     55     64    294       N  
ATOM   2373  CA  ALA B 160     -36.615   4.874 -11.190  1.00 12.97           C  
ANISOU 2373  CA  ALA B 160     1714   1215   1998    122     62    262       C  
ATOM   2374  C   ALA B 160     -35.862   4.829  -9.865  1.00 13.21           C  
ANISOU 2374  C   ALA B 160     1730   1286   2005     77     47    215       C  
ATOM   2375  O   ALA B 160     -36.469   4.651  -8.818  1.00 13.14           O  
ANISOU 2375  O   ALA B 160     1727   1280   1984    115     45    182       O  
ATOM   2376  CB  ALA B 160     -36.535   3.544 -11.908  1.00 12.37           C  
ANISOU 2376  CB  ALA B 160     1567   1217   1916    158     62    287       C  
ATOM   2377  N   GLU B 161     -34.545   5.035  -9.917  1.00 13.67           N  
ANISOU 2377  N   GLU B 161     1753   1403   2038    -12     37    215       N  
ATOM   2378  CA  GLU B 161     -33.717   5.068  -8.711  1.00 14.12           C  
ANISOU 2378  CA  GLU B 161     1778   1533   2053    -65     20    169       C  
ATOM   2379  C   GLU B 161     -34.209   6.113  -7.701  1.00 14.70           C  
ANISOU 2379  C   GLU B 161     1939   1517   2130    -94     17    107       C  
ATOM   2380  O   GLU B 161     -34.245   5.848  -6.495  1.00 14.77           O  
ANISOU 2380  O   GLU B 161     1923   1581   2107    -76      8     63       O  
ATOM   2381  CB  GLU B 161     -32.251   5.342  -9.067  1.00 14.85           C  
ANISOU 2381  CB  GLU B 161     1807   1736   2098   -178     11    177       C  
ATOM   2382  CG  GLU B 161     -31.517   4.134  -9.698  1.00 14.57           C  
ANISOU 2382  CG  GLU B 161     1657   1850   2027   -114      7    211       C  
ATOM   2383  CD  GLU B 161     -30.157   4.496 -10.312  1.00 15.48           C  
ANISOU 2383  CD  GLU B 161     1684   2120   2076   -221      3    224       C  
ATOM   2384  OE1 GLU B 161     -29.415   3.565 -10.707  1.00 15.56           O  
ANISOU 2384  OE1 GLU B 161     1588   2290   2033   -149     -4    235       O  
ATOM   2385  OE2 GLU B 161     -29.832   5.707 -10.409  1.00 16.32           O  
ANISOU 2385  OE2 GLU B 161     1834   2193   2173   -379      4    223       O  
ATOM   2386  N   GLU B 162     -34.586   7.293  -8.189  1.00 15.30           N  
ANISOU 2386  N   GLU B 162     2125   1454   2236   -127     22    103       N  
ATOM   2387  CA  GLU B 162     -34.970   8.362  -7.270  1.00 16.20           C  
ANISOU 2387  CA  GLU B 162     2348   1462   2346   -139     14     26       C  
ATOM   2388  C   GLU B 162     -36.300   8.052  -6.610  1.00 15.78           C  
ANISOU 2388  C   GLU B 162     2297   1406   2292      9     22     -7       C  
ATOM   2389  O   GLU B 162     -36.496   8.411  -5.461  1.00 16.33           O  
ANISOU 2389  O   GLU B 162     2392   1481   2330     23     14    -86       O  
ATOM   2390  CB  GLU B 162     -34.992   9.743  -7.944  1.00 17.35           C  
ANISOU 2390  CB  GLU B 162     2649   1426   2518   -202      9     32       C  
ATOM   2391  CG  GLU B 162     -33.639  10.183  -8.490  1.00 18.16           C  
ANISOU 2391  CG  GLU B 162     2751   1551   2599   -397     -1     66       C  
ATOM   2392  CD  GLU B 162     -32.563  10.439  -7.414  1.00 23.67           C  
ANISOU 2392  CD  GLU B 162     3419   2334   3239   -549    -20    -12       C  
ATOM   2393  OE1 GLU B 162     -32.883  10.701  -6.226  1.00 24.99           O  
ANISOU 2393  OE1 GLU B 162     3629   2475   3391   -520    -31   -106       O  
ATOM   2394  N   ALA B 163     -37.186   7.375  -7.343  1.00 14.96           N  
ANISOU 2394  N   ALA B 163     2155   1321   2208    107     39     51       N  
ATOM   2395  CA  ALA B 163     -38.471   6.893  -6.819  1.00 14.63           C  
ANISOU 2395  CA  ALA B 163     2080   1333   2145    225     49     36       C  
ATOM   2396  C   ALA B 163     -38.276   5.878  -5.676  1.00 14.26           C  
ANISOU 2396  C   ALA B 163     1944   1419   2056    209     44     23       C  
ATOM   2397  O   ALA B 163     -38.924   5.959  -4.614  1.00 14.62           O  
ANISOU 2397  O   ALA B 163     1978   1520   2056    256     45    -26       O  
ATOM   2398  CB  ALA B 163     -39.305   6.291  -7.957  1.00 13.99           C  
ANISOU 2398  CB  ALA B 163     1961   1272   2080    289     65    104       C  
ATOM   2399  N   ILE B 164     -37.368   4.935  -5.895  1.00 13.75           N  
ANISOU 2399  N   ILE B 164     1817   1414   1993    157     36     71       N  
ATOM   2400  CA  ILE B 164     -37.020   3.968  -4.866  1.00 13.64           C  
ANISOU 2400  CA  ILE B 164     1738   1511   1934    151     25     78       C  
ATOM   2401  C   ILE B 164     -36.541   4.688  -3.595  1.00 14.42           C  
ANISOU 2401  C   ILE B 164     1840   1653   1986    112     13      2       C  
ATOM   2402  O   ILE B 164     -37.078   4.483  -2.506  1.00 14.65           O  
ANISOU 2402  O   ILE B 164     1844   1758   1966    143     12    -23       O  
ATOM   2403  CB  ILE B 164     -35.950   2.985  -5.389  1.00 13.32           C  
ANISOU 2403  CB  ILE B 164     1648   1517   1895    133     13    133       C  
ATOM   2404  CG1 ILE B 164     -36.565   2.094  -6.487  1.00 12.70           C  
ANISOU 2404  CG1 ILE B 164     1574   1400   1851    178     22    190       C  
ATOM   2405  CG2 ILE B 164     -35.346   2.137  -4.234  1.00 13.57           C  
ANISOU 2405  CG2 ILE B 164     1628   1660   1868    142     -7    145       C  
ATOM   2406  CD1 ILE B 164     -35.580   1.069  -7.071  1.00 12.60           C  
ANISOU 2406  CD1 ILE B 164     1529   1423   1833    197      7    228       C  
ATOM   2407  N   THR B 165     -35.547   5.556  -3.757  1.00 14.99           N  
ANISOU 2407  N   THR B 165     1941   1692   2064     27      2    -37       N  
ATOM   2408  CA  THR B 165     -34.957   6.275  -2.632  1.00 15.95           C  
ANISOU 2408  CA  THR B 165     2069   1858   2133    -41    -13   -123       C  
ATOM   2409  C   THR B 165     -36.008   7.112  -1.888  1.00 16.57           C  
ANISOU 2409  C   THR B 165     2222   1876   2197     17     -8   -210       C  
ATOM   2410  O   THR B 165     -36.002   7.172  -0.657  1.00 17.13           O  
ANISOU 2410  O   THR B 165     2263   2042   2203     18    -17   -275       O  
ATOM   2411  CB  THR B 165     -33.768   7.143  -3.117  1.00 16.72           C  
ANISOU 2411  CB  THR B 165     2199   1921   2233   -181    -25   -147       C  
ATOM   2412  OG1 THR B 165     -32.801   6.283  -3.715  1.00 16.31           O  
ANISOU 2412  OG1 THR B 165     2046   1983   2168   -206    -30    -75       O  
ATOM   2413  CG2 THR B 165     -33.111   7.899  -1.967  1.00 17.94           C  
ANISOU 2413  CG2 THR B 165     2364   2130   2324   -283    -45   -250       C  
ATOM   2414  N   SER B 166     -36.923   7.733  -2.623  1.00 16.62           N  
ANISOU 2414  N   SER B 166     2317   1748   2249     85      4   -212       N  
ATOM   2415  CA  SER B 166     -37.868   8.642  -1.988  1.00 17.55           C  
ANISOU 2415  CA  SER B 166     2515   1811   2341    173      5   -307       C  
ATOM   2416  C   SER B 166     -38.973   7.919  -1.249  1.00 17.24           C  
ANISOU 2416  C   SER B 166     2385   1920   2245    283     19   -306       C  
ATOM   2417  O   SER B 166     -39.410   8.394  -0.211  1.00 18.12           O  
ANISOU 2417  O   SER B 166     2505   2087   2294    337     16   -401       O  
ATOM   2418  CB  SER B 166     -38.468   9.633  -2.996  1.00 18.41           C  
ANISOU 2418  CB  SER B 166     2760   1733   2502    238      9   -308       C  
ATOM   2419  OG  SER B 166     -37.441  10.331  -3.689  1.00 21.11           O  
ANISOU 2419  OG  SER B 166     3196   1938   2887    106     -4   -294       O  
ATOM   2420  N   PHE B 167     -39.410   6.776  -1.776  1.00 16.20           N  
ANISOU 2420  N   PHE B 167     2169   1861   2124    304     33   -202       N  
ATOM   2421  CA  PHE B 167     -40.620   6.104  -1.268  1.00 16.12           C  
ANISOU 2421  CA  PHE B 167     2077   1994   2052    380     48   -183       C  
ATOM   2422  C   PHE B 167     -40.452   4.727  -0.641  1.00 15.63           C  
ANISOU 2422  C   PHE B 167     1918   2075   1947    323     46   -105       C  
ATOM   2423  O   PHE B 167     -41.235   4.362   0.239  1.00 16.04           O  
ANISOU 2423  O   PHE B 167     1904   2273   1917    349     53   -107       O  
ATOM   2424  CB  PHE B 167     -41.683   5.977  -2.368  1.00 15.77           C  
ANISOU 2424  CB  PHE B 167     2032   1929   2033    452     66   -131       C  
ATOM   2425  CG  PHE B 167     -42.238   7.295  -2.859  1.00 16.59           C  
ANISOU 2425  CG  PHE B 167     2232   1922   2150    563     68   -196       C  
ATOM   2426  CD1 PHE B 167     -42.186   8.437  -2.075  1.00 18.10           C  
ANISOU 2426  CD1 PHE B 167     2507   2057   2312    620     57   -313       C  
ATOM   2427  CD2 PHE B 167     -42.834   7.375  -4.112  1.00 16.57           C  
ANISOU 2427  CD2 PHE B 167     2246   1869   2182    621     79   -141       C  
ATOM   2428  CE1 PHE B 167     -42.705   9.659  -2.548  1.00 20.39           C  
ANISOU 2428  CE1 PHE B 167     2924   2208   2614    746     53   -369       C  
ATOM   2429  CE2 PHE B 167     -43.358   8.579  -4.587  1.00 17.91           C  
ANISOU 2429  CE2 PHE B 167     2519   1930   2357    748     77   -184       C  
ATOM   2430  CZ  PHE B 167     -43.290   9.719  -3.805  1.00 18.66           C  
ANISOU 2430  CZ  PHE B 167     2724   1938   2430    817     62   -295       C  
ATOM   2431  N   ASN B 168     -39.485   3.942  -1.107  1.00 14.98           N  
ANISOU 2431  N   ASN B 168     1828   1957   1906    256     35    -32       N  
ATOM   2432  CA  ASN B 168     -39.400   2.547  -0.648  1.00 14.73           C  
ANISOU 2432  CA  ASN B 168     1741   2020   1837    225     28     59       C  
ATOM   2433  C   ASN B 168     -39.318   2.419   0.866  1.00 15.48           C  
ANISOU 2433  C   ASN B 168     1783   2262   1838    216     19     38       C  
ATOM   2434  O   ASN B 168     -38.443   3.030   1.500  1.00 15.90           O  
ANISOU 2434  O   ASN B 168     1831   2341   1868    198      5    -28       O  
ATOM   2435  CB  ASN B 168     -38.229   1.798  -1.273  1.00 14.26           C  
ANISOU 2435  CB  ASN B 168     1691   1905   1822    194     11    122       C  
ATOM   2436  CG  ASN B 168     -38.281   0.299  -0.966  1.00 14.25           C  
ANISOU 2436  CG  ASN B 168     1679   1949   1788    188     -1    224       C  
ATOM   2437  OD1 ASN B 168     -39.342  -0.301  -1.014  1.00 14.27           O  
ANISOU 2437  OD1 ASN B 168     1686   1965   1773    174      9    271       O  
ATOM   2438  ND2 ASN B 168     -37.145  -0.286  -0.623  1.00 14.47           N  
ANISOU 2438  ND2 ASN B 168     1697   2005   1795    195    -25    259       N  
ATOM   2439  N   GLY B 169     -40.222   1.618   1.434  1.00 15.69           N  
ANISOU 2439  N   GLY B 169     1765   2400   1798    210     26     99       N  
ATOM   2440  CA  GLY B 169     -40.279   1.402   2.886  1.00 17.47           C  
ANISOU 2440  CA  GLY B 169     1928   2797   1914    198     20     99       C  
ATOM   2441  C   GLY B 169     -41.091   2.426   3.677  1.00 19.15           C  
ANISOU 2441  C   GLY B 169     2097   3129   2050    249     35    -16       C  
ATOM   2442  O   GLY B 169     -41.291   2.263   4.878  1.00 20.01           O  
ANISOU 2442  O   GLY B 169     2139   3414   2051    242     33    -21       O  
ATOM   2443  N   HIS B 170     -41.582   3.473   3.018  1.00 20.00           N  
ANISOU 2443  N   HIS B 170     2248   3149   2202    316     47   -107       N  
ATOM   2444  CA  HIS B 170     -42.325   4.523   3.725  1.00 22.66           C  
ANISOU 2444  CA  HIS B 170     2566   3581   2463    406     57   -237       C  
ATOM   2445  C   HIS B 170     -43.817   4.266   3.856  1.00 23.91           C  
ANISOU 2445  C   HIS B 170     2639   3914   2531    461     80   -218       C  
ATOM   2446  O   HIS B 170     -44.464   3.799   2.920  1.00 23.20           O  
ANISOU 2446  O   HIS B 170     2541   3801   2474    453     93   -144       O  
ATOM   2447  CB  HIS B 170     -42.059   5.898   3.109  1.00 22.91           C  
ANISOU 2447  CB  HIS B 170     2713   3424   2568    472     51   -355       C  
ATOM   2448  CG  HIS B 170     -40.606   6.242   3.058  1.00 24.49           C  
ANISOU 2448  CG  HIS B 170     2981   3496   2829    385     29   -382       C  
ATOM   2449  ND1 HIS B 170     -40.067   7.065   2.100  1.00 26.25           N  
ANISOU 2449  ND1 HIS B 170     3317   3510   3145    370     21   -414       N  
ATOM   2450  CD2 HIS B 170     -39.573   5.839   3.835  1.00 26.05           C  
ANISOU 2450  CD2 HIS B 170     3134   3774   2990    300     11   -372       C  
ATOM   2451  CE1 HIS B 170     -38.764   7.171   2.296  1.00 28.15           C  
ANISOU 2451  CE1 HIS B 170     3573   3721   3400    262      2   -429       C  
ATOM   2452  NE2 HIS B 170     -38.439   6.435   3.342  1.00 27.90           N  
ANISOU 2452  NE2 HIS B 170     3441   3871   3290    229     -6   -408       N  
ATOM   2453  N   LYS B 171     -44.345   4.579   5.035  1.00 26.47           N  
ANISOU 2453  N   LYS B 171     2886   4445   2727    511     85   -292       N  
ATOM   2454  CA  LYS B 171     -45.761   4.394   5.336  1.00 29.06           C  
ANISOU 2454  CA  LYS B 171     3098   5013   2931    563    108   -286       C  
ATOM   2455  C   LYS B 171     -46.566   5.660   5.067  1.00 31.25           C  
ANISOU 2455  C   LYS B 171     3397   5294   3182    752    118   -430       C  
ATOM   2456  O   LYS B 171     -46.202   6.744   5.544  1.00 32.57           O  
ANISOU 2456  O   LYS B 171     3637   5392   3345    851    105   -577       O  
ATOM   2457  CB  LYS B 171     -45.957   3.991   6.804  1.00 30.08           C  
ANISOU 2457  CB  LYS B 171     3109   5416   2903    525    110   -281       C  
ATOM   2458  CG  LYS B 171     -45.421   2.618   7.167  1.00 30.53           C  
ANISOU 2458  CG  LYS B 171     3142   5508   2951    357    100   -112       C  
ATOM   2459  CD  LYS B 171     -45.398   2.430   8.677  1.00 33.54           C  
ANISOU 2459  CD  LYS B 171     3423   6144   3178    331     97   -116       C  
ATOM   2460  CE  LYS B 171     -44.540   1.228   9.076  1.00 34.40           C  
ANISOU 2460  CE  LYS B 171     3550   6229   3289    197     77     47       C  
ATOM   2461  NZ  LYS B 171     -44.610   0.947  10.556  1.00 35.41           N  
ANISOU 2461  NZ  LYS B 171     3570   6638   3246    163     74     72       N  
ATOM   2462  N   PRO B 172     -47.675   5.527   4.319  1.00 32.26           N  
ANISOU 2462  N   PRO B 172     3467   5509   3281    808    137   -392       N  
ATOM   2463  CA  PRO B 172     -48.657   6.602   4.227  1.00 34.31           C  
ANISOU 2463  CA  PRO B 172     3714   5855   3469   1026    146   -518       C  
ATOM   2464  C   PRO B 172     -49.176   6.981   5.619  1.00 36.74           C  
ANISOU 2464  C   PRO B 172     3917   6440   3603   1122    151   -633       C  
ATOM   2465  O   PRO B 172     -49.397   6.093   6.445  1.00 37.43           O  
ANISOU 2465  O   PRO B 172     3867   6775   3581   1001    161   -559       O  
ATOM   2466  CB  PRO B 172     -49.783   5.976   3.399  1.00 34.45           C  
ANISOU 2466  CB  PRO B 172     3619   6032   3438   1016    167   -421       C  
ATOM   2467  CG  PRO B 172     -49.106   4.923   2.579  1.00 32.42           C  
ANISOU 2467  CG  PRO B 172     3412   5599   3308    814    161   -272       C  
ATOM   2468  CD  PRO B 172     -48.012   4.386   3.448  1.00 31.36           C  
ANISOU 2468  CD  PRO B 172     3311   5404   3201    678    146   -237       C  
ATOM   2469  N   PRO B 173     -49.348   8.290   5.891  1.00 38.55           N  
ANISOU 2469  N   PRO B 173     4225   6622   3801   1339    141   -812       N  
ATOM   2470  CA  PRO B 173     -49.927   8.748   7.161  1.00 40.65           C  
ANISOU 2470  CA  PRO B 173     4391   7168   3886   1472    146   -950       C  
ATOM   2471  C   PRO B 173     -51.211   8.003   7.503  1.00 41.78           C  
ANISOU 2471  C   PRO B 173     4291   7741   3841   1472    176   -882       C  
ATOM   2472  O   PRO B 173     -52.064   7.794   6.629  1.00 41.85           O  
ANISOU 2472  O   PRO B 173     4235   7832   3833   1513    191   -816       O  
ATOM   2473  CB  PRO B 173     -50.240  10.219   6.889  1.00 42.07           C  
ANISOU 2473  CB  PRO B 173     4716   7197   4071   1750    131  -1133       C  
ATOM   2474  CG  PRO B 173     -49.210  10.632   5.907  1.00 40.86           C  
ANISOU 2474  CG  PRO B 173     4788   6610   4125   1683    109  -1106       C  
ATOM   2475  CD  PRO B 173     -48.898   9.420   5.058  1.00 38.60           C  
ANISOU 2475  CD  PRO B 173     4443   6284   3939   1461    121   -896       C  
ATOM   2476  N   GLY B 174     -51.331   7.589   8.762  1.00 42.88           N  
ANISOU 2476  N   GLY B 174     4289   8174   3830   1408    184   -891       N  
ATOM   2477  CA  GLY B 174     -52.501   6.843   9.222  1.00 44.32           C  
ANISOU 2477  CA  GLY B 174     4228   8805   3808   1363    212   -815       C  
ATOM   2478  C   GLY B 174     -52.399   5.345   8.981  1.00 43.23           C  
ANISOU 2478  C   GLY B 174     4023   8705   3695   1060    221   -581       C  
ATOM   2479  O   GLY B 174     -53.041   4.555   9.684  1.00 44.31           O  
ANISOU 2479  O   GLY B 174     3981   9195   3661    933    239   -491       O  
ATOM   2480  N   SER B 175     -51.592   4.957   7.989  1.00 41.05           N  
ANISOU 2480  N   SER B 175     3904   8069   3625    942    207   -482       N  
ATOM   2481  CA  SER B 175     -51.410   3.551   7.628  1.00 39.76           C  
ANISOU 2481  CA  SER B 175     3730   7869   3508    675    208   -273       C  
ATOM   2482  C   SER B 175     -50.166   2.929   8.258  1.00 38.43           C  
ANISOU 2482  C   SER B 175     3647   7545   3410    522    187   -194       C  
ATOM   2483  O   SER B 175     -49.128   3.579   8.390  1.00 37.76           O  
ANISOU 2483  O   SER B 175     3683   7237   3429    592    167   -284       O  
ATOM   2484  CB  SER B 175     -51.339   3.392   6.112  1.00 38.53           C  
ANISOU 2484  CB  SER B 175     3677   7450   3512    651    205   -213       C  
ATOM   2485  OG  SER B 175     -51.210   2.025   5.762  1.00 38.75           O  
ANISOU 2485  OG  SER B 175     3713   7435   3576    403    202    -30       O  
ATOM   2486  N   SER B 176     -50.286   1.657   8.626  1.00 38.08           N  
ANISOU 2486  N   SER B 176     3543   7625   3299    309    189    -19       N  
ATOM   2487  CA  SER B 176     -49.165   0.893   9.167  1.00 37.15           C  
ANISOU 2487  CA  SER B 176     3508   7372   3234    173    166     89       C  
ATOM   2488  C   SER B 176     -48.549  -0.046   8.120  1.00 35.10           C  
ANISOU 2488  C   SER B 176     3392   6805   3140     41    149    230       C  
ATOM   2489  O   SER B 176     -47.657  -0.836   8.436  1.00 35.33           O  
ANISOU 2489  O   SER B 176     3501   6714   3210    -59    126    341       O  
ATOM   2490  CB  SER B 176     -49.603   0.113  10.416  1.00 38.60           C  
ANISOU 2490  CB  SER B 176     3561   7885   3222     40    172    197       C  
ATOM   2491  OG  SER B 176     -50.605  -0.839  10.099  1.00 39.71           O  
ANISOU 2491  OG  SER B 176     3630   8180   3277   -133    187    343       O  
ATOM   2492  N   GLU B 177     -49.028   0.043   6.881  1.00 33.61           N  
ANISOU 2492  N   GLU B 177     3235   6503   3032     59    157    222       N  
ATOM   2493  CA  GLU B 177     -48.471  -0.741   5.765  1.00 31.14           C  
ANISOU 2493  CA  GLU B 177     3060   5899   2875    -41    141    324       C  
ATOM   2494  C   GLU B 177     -47.579   0.117   4.853  1.00 28.69           C  
ANISOU 2494  C   GLU B 177     2866   5295   2738     95    131    223       C  
ATOM   2495  O   GLU B 177     -48.040   1.115   4.294  1.00 28.38           O  
ANISOU 2495  O   GLU B 177     2811   5253   2717    231    144    110       O  
ATOM   2496  CB  GLU B 177     -49.588  -1.413   4.954  1.00 31.48           C  
ANISOU 2496  CB  GLU B 177     3056   6031   2876   -160    156    403       C  
ATOM   2497  N   PRO B 178     -46.298  -0.264   4.708  1.00 26.86           N  
ANISOU 2497  N   PRO B 178     2753   4833   2621     61    106    268       N  
ATOM   2498  CA  PRO B 178     -45.384   0.551   3.917  1.00 25.23           C  
ANISOU 2498  CA  PRO B 178     2642   4386   2557    160     96    180       C  
ATOM   2499  C   PRO B 178     -45.564   0.386   2.412  1.00 24.01           C  
ANISOU 2499  C   PRO B 178     2548   4063   2510    152    100    208       C  
ATOM   2500  O   PRO B 178     -46.011  -0.670   1.933  1.00 23.67           O  
ANISOU 2500  O   PRO B 178     2511   4021   2462     41    100    313       O  
ATOM   2501  CB  PRO B 178     -44.004   0.034   4.344  1.00 24.79           C  
ANISOU 2501  CB  PRO B 178     2653   4217   2548    115     69    234       C  
ATOM   2502  CG  PRO B 178     -44.232  -1.363   4.723  1.00 25.69           C  
ANISOU 2502  CG  PRO B 178     2766   4393   2600    -10     60    391       C  
ATOM   2503  CD  PRO B 178     -45.605  -1.406   5.334  1.00 26.85           C  
ANISOU 2503  CD  PRO B 178     2795   4804   2602    -56     84    402       C  
ATOM   2504  N   ILE B 179     -45.220   1.438   1.678  1.00 22.97           N  
ANISOU 2504  N   ILE B 179     2471   3789   2468    260    101    112       N  
ATOM   2505  CA  ILE B 179     -45.071   1.357   0.237  1.00 21.60           C  
ANISOU 2505  CA  ILE B 179     2363   3439   2404    259    101    138       C  
ATOM   2506  C   ILE B 179     -43.747   0.655  -0.033  1.00 20.66           C  
ANISOU 2506  C   ILE B 179     2327   3149   2374    193     78    201       C  
ATOM   2507  O   ILE B 179     -42.718   0.972   0.586  1.00 20.79           O  
ANISOU 2507  O   ILE B 179     2366   3129   2404    208     63    168       O  
ATOM   2508  CB  ILE B 179     -45.079   2.749  -0.412  1.00 21.64           C  
ANISOU 2508  CB  ILE B 179     2414   3346   2465    392    107     33       C  
ATOM   2509  CG1 ILE B 179     -46.456   3.400  -0.238  1.00 23.56           C  
ANISOU 2509  CG1 ILE B 179     2576   3769   2605    503    127    -30       C  
ATOM   2510  CG2 ILE B 179     -44.742   2.656  -1.899  1.00 21.66           C  
ANISOU 2510  CG2 ILE B 179     2482   3172   2576    381    105     72       C  
ATOM   2511  CD1 ILE B 179     -46.442   4.933  -0.202  1.00 25.52           C  
ANISOU 2511  CD1 ILE B 179     2890   3941   2866    672    125   -159       C  
ATOM   2512  N   THR B 180     -43.778  -0.327  -0.924  1.00 18.71           N  
ANISOU 2512  N   THR B 180     2117   2819   2172    125     73    283       N  
ATOM   2513  CA  THR B 180     -42.546  -0.909  -1.406  1.00 17.67           C  
ANISOU 2513  CA  THR B 180     2064   2526   2122    107     51    324       C  
ATOM   2514  C   THR B 180     -42.391  -0.543  -2.871  1.00 15.81           C  
ANISOU 2514  C   THR B 180     1866   2164   1977    142     56    298       C  
ATOM   2515  O   THR B 180     -43.366  -0.564  -3.634  1.00 14.87           O  
ANISOU 2515  O   THR B 180     1727   2071   1853    134     71    302       O  
ATOM   2516  CB  THR B 180     -42.495  -2.423  -1.212  1.00 18.05           C  
ANISOU 2516  CB  THR B 180     2160   2552   2147     18     32    436       C  
ATOM   2517  OG1 THR B 180     -43.548  -3.029  -1.955  1.00 19.96           O  
ANISOU 2517  OG1 THR B 180     2407   2801   2377    -58     41    474       O  
ATOM   2518  CG2 THR B 180     -42.647  -2.776   0.262  1.00 19.31           C  
ANISOU 2518  CG2 THR B 180     2283   2851   2204    -23     26    483       C  
ATOM   2519  N   VAL B 181     -41.168  -0.152  -3.228  1.00 14.03           N  
ANISOU 2519  N   VAL B 181     1678   1834   1816    176     45    272       N  
ATOM   2520  CA  VAL B 181     -40.812   0.211  -4.590  1.00 13.02           C  
ANISOU 2520  CA  VAL B 181     1582   1601   1765    200     48    258       C  
ATOM   2521  C   VAL B 181     -39.502  -0.498  -4.874  1.00 12.81           C  
ANISOU 2521  C   VAL B 181     1586   1509   1771    195     26    290       C  
ATOM   2522  O   VAL B 181     -38.535  -0.301  -4.163  1.00 13.00           O  
ANISOU 2522  O   VAL B 181     1599   1560   1781    202     12    275       O  
ATOM   2523  CB  VAL B 181     -40.541   1.717  -4.750  1.00 13.07           C  
ANISOU 2523  CB  VAL B 181     1599   1568   1798    247     56    184       C  
ATOM   2524  CG1 VAL B 181     -40.212   2.021  -6.193  1.00 12.66           C  
ANISOU 2524  CG1 VAL B 181     1577   1422   1811    256     60    193       C  
ATOM   2525  CG2 VAL B 181     -41.733   2.589  -4.238  1.00 13.64           C  
ANISOU 2525  CG2 VAL B 181     1650   1711   1820    303     73    129       C  
ATOM   2526  N   LYS B 182     -39.476  -1.319  -5.921  1.00 12.57           N  
ANISOU 2526  N   LYS B 182     1588   1416   1774    190     21    324       N  
ATOM   2527  CA  LYS B 182     -38.279  -2.086  -6.264  1.00 12.61           C  
ANISOU 2527  CA  LYS B 182     1621   1373   1795    221     -2    346       C  
ATOM   2528  C   LYS B 182     -38.278  -2.352  -7.759  1.00 12.32           C  
ANISOU 2528  C   LYS B 182     1604   1275   1800    235      1    340       C  
ATOM   2529  O   LYS B 182     -39.322  -2.232  -8.401  1.00 12.15           O  
ANISOU 2529  O   LYS B 182     1581   1249   1788    205     18    336       O  
ATOM   2530  CB  LYS B 182     -38.264  -3.406  -5.493  1.00 13.20           C  
ANISOU 2530  CB  LYS B 182     1749   1435   1830    216    -26    409       C  
ATOM   2531  CG  LYS B 182     -39.318  -4.396  -5.908  1.00 14.96           C  
ANISOU 2531  CG  LYS B 182     2037   1600   2049    155    -28    449       C  
ATOM   2532  CD  LYS B 182     -39.253  -5.645  -5.013  1.00 19.87           C  
ANISOU 2532  CD  LYS B 182     2743   2182   2624    134    -57    528       C  
ATOM   2533  CE  LYS B 182     -40.524  -6.500  -5.142  1.00 23.86           C  
ANISOU 2533  CE  LYS B 182     3312   2650   3101     10    -57    574       C  
ATOM   2534  NZ  LYS B 182     -41.633  -6.112  -4.199  1.00 24.82           N  
ANISOU 2534  NZ  LYS B 182     3360   2915   3155    -85    -35    598       N  
ATOM   2535  N   PHE B 183     -37.126  -2.701  -8.317  1.00 12.39           N  
ANISOU 2535  N   PHE B 183     1617   1271   1820    286    -15    335       N  
ATOM   2536  CA  PHE B 183     -37.086  -2.987  -9.735  1.00 12.70           C  
ANISOU 2536  CA  PHE B 183     1665   1276   1884    307    -12    321       C  
ATOM   2537  C   PHE B 183     -37.870  -4.274 -10.011  1.00 14.14           C  
ANISOU 2537  C   PHE B 183     1929   1382   2062    289    -25    339       C  
ATOM   2538  O   PHE B 183     -37.821  -5.222  -9.219  1.00 13.19           O  
ANISOU 2538  O   PHE B 183     1879   1214   1918    293    -48    374       O  
ATOM   2539  CB  PHE B 183     -35.647  -3.025 -10.269  1.00 12.97           C  
ANISOU 2539  CB  PHE B 183     1663   1355   1908    375    -25    303       C  
ATOM   2540  CG  PHE B 183     -34.998  -1.659 -10.314  1.00 12.37           C  
ANISOU 2540  CG  PHE B 183     1513   1356   1833    338     -9    286       C  
ATOM   2541  CD1 PHE B 183     -35.373  -0.733 -11.285  1.00 13.43           C  
ANISOU 2541  CD1 PHE B 183     1629   1481   1993    295     13    280       C  
ATOM   2542  CD2 PHE B 183     -34.073  -1.291  -9.368  1.00 13.13           C  
ANISOU 2542  CD2 PHE B 183     1567   1528   1894    333    -20    280       C  
ATOM   2543  CE1 PHE B 183     -34.813   0.546 -11.319  1.00 13.34           C  
ANISOU 2543  CE1 PHE B 183     1585   1504   1980    237     23    275       C  
ATOM   2544  CE2 PHE B 183     -33.488  -0.006  -9.383  1.00 14.40           C  
ANISOU 2544  CE2 PHE B 183     1678   1745   2048    260    -10    259       C  
ATOM   2545  CZ  PHE B 183     -33.868   0.909 -10.361  1.00 13.13           C  
ANISOU 2545  CZ  PHE B 183     1527   1541   1921    206     11    260       C  
ATOM   2546  N   ALA B 184     -38.616  -4.256 -11.108  1.00 15.39           N  
ANISOU 2546  N   ALA B 184     2084   1531   2234    257    -11    320       N  
ATOM   2547  CA  ALA B 184     -39.463  -5.367 -11.535  1.00 18.93           C  
ANISOU 2547  CA  ALA B 184     2607   1916   2671    203    -22    321       C  
ATOM   2548  C   ALA B 184     -38.639  -6.601 -11.896  1.00 21.54           C  
ANISOU 2548  C   ALA B 184     3039   2147   2999    270    -57    306       C  
ATOM   2549  O   ALA B 184     -37.569  -6.477 -12.490  1.00 21.95           O  
ANISOU 2549  O   ALA B 184     3060   2223   3055    372    -62    274       O  
ATOM   2550  CB  ALA B 184     -40.315  -4.930 -12.729  1.00 18.88           C  
ANISOU 2550  CB  ALA B 184     2547   1961   2665    164     -1    293       C  
ATOM   2551  N   ALA B 185     -39.154  -7.785 -11.553  1.00 24.79           N  
ANISOU 2551  N   ALA B 185     3576   2450   3393    214    -82    330       N  
ATOM   2552  CA  ALA B 185     -38.461  -9.072 -11.787  1.00 28.01           C  
ANISOU 2552  CA  ALA B 185     4131   2717   3794    296   -123    315       C  
ATOM   2553  C   ALA B 185     -37.990  -9.314 -13.225  1.00 29.61           C  
ANISOU 2553  C   ALA B 185     4337   2910   4003    380   -129    231       C  
ATOM   2554  O   ALA B 185     -37.174 -10.215 -13.463  1.00 31.36           O  
ANISOU 2554  O   ALA B 185     4664   3040   4212    506   -164    199       O  
ATOM   2555  CB  ALA B 185     -39.314 -10.253 -11.284  1.00 29.46           C  
ANISOU 2555  CB  ALA B 185     4481   2757   3956    175   -150    360       C  
ATOM   2556  N   ASN B 186     -38.503  -8.523 -14.176  1.00 29.83           N  
ANISOU 2556  N   ASN B 186     4252   3042   4039    327    -97    195       N  
ATOM   2557  CA  ASN B 186     -37.991  -8.515 -15.558  1.00 31.13           C  
ANISOU 2557  CA  ASN B 186     4377   3254   4196    408    -96    120       C  
ATOM   2558  CB  ASN B 186     -38.329  -9.821 -16.297  1.00 32.28           C  
ANISOU 2558  CB  ASN B 186     4671   3271   4324    395   -128     53       C  
ATOM   2559  CG  ASN B 186     -37.096 -10.515 -16.859  1.00 34.93           C  
ANISOU 2559  CG  ASN B 186     5067   3569   4637    584   -158    -17       C  
ATOM   2560  ND2 ASN B 186     -36.124 -10.808 -15.994  1.00 37.19           N  
ANISOU 2560  ND2 ASN B 186     5398   3817   4917    715   -181     16       N  
TER    2561      ASN B 186                                                      
ATOM   2562  O3'   U C   2     -49.301 -11.825  -8.535  1.00 95.37           O  
ANISOU 2562  O3'   U C   2    15234  12825   8176  -3293   3959   2609       O  
ATOM   2563  P     U C   3     -47.867 -11.110  -8.532  1.00 89.98           P  
ANISOU 2563  P     U C   3    14521  12316   7350  -2462   3392   2542       P  
ATOM   2564  OP1   U C   3     -46.966 -11.947  -7.704  1.00 96.08           O  
ANISOU 2564  OP1   U C   3    15786  12951   7770  -2041   3495   3436       O  
ATOM   2565  OP2   U C   3     -48.049  -9.678  -8.197  1.00 85.06           O  
ANISOU 2565  OP2   U C   3    13249  12637   6434  -2285   3060   1868       O  
ATOM   2566  O5'   U C   3     -47.410 -11.204 -10.065  1.00 84.08           O  
ANISOU 2566  O5'   U C   3    13895  10720   7332  -2405   3156   2160       O  
ATOM   2567  C5'   U C   3     -48.077 -10.452 -11.073  1.00 78.14           C  
ANISOU 2567  C5'   U C   3    12709  10045   6935  -2662   3001   1390       C  
ATOM   2568  C4'   U C   3     -47.077  -9.780 -11.997  1.00 71.40           C  
ANISOU 2568  C4'   U C   3    11747   9020   6364  -2185   2527   1064       C  
ATOM   2569  O4'   U C   3     -46.140  -9.001 -11.209  1.00 70.38           O  
ANISOU 2569  O4'   U C   3    11478   9398   5865  -1633   2215   1124       O  
ATOM   2570  C3'   U C   3     -46.268 -10.735 -12.869  1.00 71.17           C  
ANISOU 2570  C3'   U C   3    12152   8151   6738  -2044   2514   1284       C  
ATOM   2571  O3'   U C   3     -46.486 -10.405 -14.272  1.00 66.39           O  
ANISOU 2571  O3'   U C   3    11286   7377   6561  -2166   2355    725       O  
ATOM   2572  C2'   U C   3     -44.812 -10.585 -12.381  1.00 70.27           C  
ANISOU 2572  C2'   U C   3    12213   8107   6381  -1366   2212   1607       C  
ATOM   2573  O2'   U C   3     -43.897 -10.398 -13.443  1.00 66.47           O  
ANISOU 2573  O2'   U C   3    11707   7322   6226  -1056   1899   1361       O  
ATOM   2574  C1'   U C   3     -44.794  -9.331 -11.503  1.00 67.86           C  
ANISOU 2574  C1'   U C   3    11457   8685   5643  -1150   1995   1375       C  
ATOM   2575  N1    U C   3     -44.016  -9.353 -10.182  1.00 70.02           N  
ANISOU 2575  N1    U C   3    11814   9457   5334   -687   1932   1783       N  
ATOM   2576  C2    U C   3     -42.760  -8.759 -10.071  1.00 66.50           C  
ANISOU 2576  C2    U C   3    11223   9265   4778   -112   1553   1642       C  
ATOM   2577  O2    U C   3     -42.180  -8.213 -10.989  1.00 59.71           O  
ANISOU 2577  O2    U C   3    10205   8184   4299     26   1282   1266       O  
ATOM   2578  N3    U C   3     -42.175  -8.834  -8.823  1.00 71.20           N  
ANISOU 2578  N3    U C   3    11824  10470   4757    308   1515   1962       N  
ATOM   2579  C4    U C   3     -42.703  -9.421  -7.683  1.00 78.51           C  
ANISOU 2579  C4    U C   3    12899  11806   5124    237   1822   2499       C  
ATOM   2580  O4    U C   3     -42.071  -9.416  -6.626  1.00 82.97           O  
ANISOU 2580  O4    U C   3    13401  13057   5066    711   1738   2764       O  
ATOM   2581  C5    U C   3     -44.009 -10.005  -7.866  1.00 81.01           C  
ANISOU 2581  C5    U C   3    13391  11768   5623   -422   2244   2687       C  
ATOM   2582  C6    U C   3     -44.595  -9.945  -9.073  1.00 76.41           C  
ANISOU 2582  C6    U C   3    12781  10575   5675   -852   2274   2280       C  
ATOM   2583  P     U C   4     -47.776 -10.895 -15.118  1.00 67.40           P  
ANISOU 2583  P     U C   4    11260   7325   7025  -2798   2650    317       P  
ATOM   2584  OP1   U C   4     -48.703 -11.606 -14.205  1.00 73.21           O  
ANISOU 2584  OP1   U C   4    12152   8036   7628  -3300   3121    581       O  
ATOM   2585  OP2   U C   4     -47.239 -11.586 -16.309  1.00 67.23           O  
ANISOU 2585  OP2   U C   4    11390   6721   7432  -2733   2591    166       O  
ATOM   2586  O5'   U C   4     -48.467  -9.539 -15.657  1.00 59.98           O  
ANISOU 2586  O5'   U C   4     9692   7057   6041  -2808   2398   -278       O  
ATOM   2587  C5'   U C   4     -49.845  -9.197 -15.371  1.00 57.63           C  
ANISOU 2587  C5'   U C   4     9028   7254   5616  -3235   2590   -613       C  
ATOM   2588  C4'   U C   4     -50.183  -7.711 -15.550  1.00 50.97           C  
ANISOU 2588  C4'   U C   4     7635   7035   4694  -2993   2259  -1029       C  
ATOM   2589  O4'   U C   4     -49.026  -6.846 -15.339  1.00 44.67           O  
ANISOU 2589  O4'   U C   4     6835   6267   3869  -2432   1894   -870       O  
ATOM   2590  C3'   U C   4     -50.753  -7.280 -16.905  1.00 47.63           C  
ANISOU 2590  C3'   U C   4     6816   6771   4510  -3015   2113  -1508       C  
ATOM   2591  O3'   U C   4     -51.731  -6.245 -16.715  1.00 47.40           O  
ANISOU 2591  O3'   U C   4     6278   7359   4373  -3024   2022  -1895       O  
ATOM   2592  C2'   U C   4     -49.513  -6.739 -17.615  1.00 42.54           C  
ANISOU 2592  C2'   U C   4     6222   5915   4028  -2489   1748  -1346       C  
ATOM   2593  O2'   U C   4     -49.788  -5.840 -18.673  1.00 40.38           O  
ANISOU 2593  O2'   U C   4     5520   5936   3885  -2287   1506  -1622       O  
ATOM   2594  C1'   U C   4     -48.844  -6.000 -16.460  1.00 40.21           C  
ANISOU 2594  C1'   U C   4     5969   5741   3567  -2176   1594  -1124       C  
ATOM   2595  N1    U C   4     -47.381  -5.734 -16.636  1.00 35.10           N  
ANISOU 2595  N1    U C   4     5496   4820   3019  -1724   1333   -865       N  
ATOM   2596  C2    U C   4     -46.914  -4.428 -16.745  1.00 31.03           C  
ANISOU 2596  C2    U C   4     4664   4472   2654  -1373   1034   -977       C  
ATOM   2597  O2    U C   4     -47.626  -3.448 -16.719  1.00 28.85           O  
ANISOU 2597  O2    U C   4     3991   4497   2474  -1355    948  -1257       O  
ATOM   2598  N3    U C   4     -45.549  -4.296 -16.888  1.00 29.29           N  
ANISOU 2598  N3    U C   4     4588   4018   2522  -1033    848   -770       N  
ATOM   2599  C4    U C   4     -44.629  -5.331 -16.934  1.00 31.64           C  
ANISOU 2599  C4    U C   4     5302   3987   2732   -947    893   -483       C  
ATOM   2600  O4    U C   4     -43.438  -5.077 -17.077  1.00 32.16           O  
ANISOU 2600  O4    U C   4     5401   3952   2865   -625    703   -381       O  
ATOM   2601  C5    U C   4     -45.181  -6.660 -16.815  1.00 34.45           C  
ANISOU 2601  C5    U C   4     6000   4113   2976  -1262   1187   -352       C  
ATOM   2602  C6    U C   4     -46.508  -6.810 -16.674  1.00 35.86           C  
ANISOU 2602  C6    U C   4     6049   4470   3105  -1666   1412   -537       C  
ATOM   2603  P     U C   5     -53.303  -6.488 -16.972  1.00 52.41           P  
ANISOU 2603  P     U C   5     6528   8437   4950  -3518   2274  -2410       P  
ATOM   2604  OP1   U C   5     -54.026  -5.277 -16.525  1.00 51.69           O  
ANISOU 2604  OP1   U C   5     5945   8969   4726  -3350   2102  -2743       O  
ATOM   2605  OP2   U C   5     -53.683  -7.803 -16.406  1.00 55.57           O  
ANISOU 2605  OP2   U C   5     7240   8582   5294  -4103   2749  -2275       O  
ATOM   2606  O5'   U C   5     -53.335  -6.544 -18.577  1.00 48.92           O  
ANISOU 2606  O5'   U C   5     5882   7976   4729  -3401   2121  -2675       O  
ATOM   2607  C5'   U C   5     -54.046  -7.570 -19.248  1.00 51.58           C  
ANISOU 2607  C5'   U C   5     6138   8310   5151  -3872   2405  -3038       C  
ATOM   2608  C4'   U C   5     -53.707  -7.633 -20.730  1.00 48.98           C  
ANISOU 2608  C4'   U C   5     5636   8014   4958  -3628   2203  -3226       C  
ATOM   2609  O4'   U C   5     -53.817  -6.325 -21.341  1.00 44.77           O  
ANISOU 2609  O4'   U C   5     4674   8009   4328  -3116   1826  -3284       O  
ATOM   2610  C3'   U C   5     -52.307  -8.128 -21.066  1.00 45.90           C  
ANISOU 2610  C3'   U C   5     5694   7006   4740  -3379   2104  -2824       C  
ATOM   2611  O3'   U C   5     -52.435  -9.248 -21.917  1.00 50.64           O  
ANISOU 2611  O3'   U C   5     6281   7432   5528  -3678   2296  -3182       O  
ATOM   2612  C2'   U C   5     -51.668  -6.945 -21.804  1.00 40.30           C  
ANISOU 2612  C2'   U C   5     4756   6577   3981  -2765   1676  -2652       C  
ATOM   2613  O2'   U C   5     -50.781  -7.333 -22.835  1.00 36.73           O  
ANISOU 2613  O2'   U C   5     4374   5968   3615  -2553   1555  -2590       O  
ATOM   2614  C1'   U C   5     -52.902  -6.278 -22.402  1.00 40.61           C  
ANISOU 2614  C1'   U C   5     4183   7367   3878  -2751   1604  -3100       C  
ATOM   2615  N1    U C   5     -52.709  -4.858 -22.841  1.00 36.13           N  
ANISOU 2615  N1    U C   5     3317   7129   3281  -2172   1239  -2882       N  
ATOM   2616  C2    U C   5     -52.919  -4.513 -24.167  1.00 35.92           C  
ANISOU 2616  C2    U C   5     2873   7629   3147  -1878   1063  -2996       C  
ATOM   2617  O2    U C   5     -53.255  -5.306 -25.036  1.00 37.24           O  
ANISOU 2617  O2    U C   5     2838   8113   3199  -2058   1163  -3381       O  
ATOM   2618  N3    U C   5     -52.703  -3.183 -24.451  1.00 34.13           N  
ANISOU 2618  N3    U C   5     2438   7564   2967  -1343    773  -2642       N  
ATOM   2619  C4    U C   5     -52.320  -2.183 -23.565  1.00 33.88           C  
ANISOU 2619  C4    U C   5     2535   7176   3162  -1116    647  -2322       C  
ATOM   2620  O4    U C   5     -52.170  -1.034 -23.967  1.00 33.51           O  
ANISOU 2620  O4    U C   5     2268   7201   3262   -657    422  -2028       O  
ATOM   2621  C5    U C   5     -52.127  -2.616 -22.201  1.00 32.95           C  
ANISOU 2621  C5    U C   5     2785   6635   3100  -1445    817  -2363       C  
ATOM   2622  C6    U C   5     -52.325  -3.910 -21.906  1.00 34.18           C  
ANISOU 2622  C6    U C   5     3184   6671   3131  -1931   1101  -2571       C  
ATOM   2623  P     U C   6     -52.452 -10.765 -21.405  1.00 56.48           P  
ANISOU 2623  P     U C   6     7460   7433   6565  -4230   2748  -3175       P  
ATOM   2624  OP1   U C   6     -52.254 -11.606 -22.604  1.00 59.01           O  
ANISOU 2624  OP1   U C   6     7661   7603   7158  -4307   2782  -3631       O  
ATOM   2625  OP2   U C   6     -53.641 -10.967 -20.545  1.00 62.63           O  
ANISOU 2625  OP2   U C   6     8142   8373   7282  -4788   3112  -3334       O  
ATOM   2626  O5'   U C   6     -51.163 -10.854 -20.468  1.00 55.19           O  
ANISOU 2626  O5'   U C   6     7928   6632   6409  -3910   2674  -2408       O  
ATOM   2627  C5'   U C   6     -49.864 -10.833 -21.026  1.00 51.23           C  
ANISOU 2627  C5'   U C   6     7620   5862   5985  -3424   2389  -2182       C  
ATOM   2628  C4'   U C   6     -48.847 -10.497 -19.953  1.00 48.95           C  
ANISOU 2628  C4'   U C   6     7750   5299   5549  -3060   2259  -1530       C  
ATOM   2629  O4'   U C   6     -48.322 -11.713 -19.377  1.00 53.59           O  
ANISOU 2629  O4'   U C   6     8889   5144   6329  -3167   2510  -1182       O  
ATOM   2630  C3'   U C   6     -47.649  -9.733 -20.498  1.00 44.45           C  
ANISOU 2630  C3'   U C   6     7127   4840   4921  -2476   1847  -1367       C  
ATOM   2631  O3'   U C   6     -47.737  -8.370 -20.040  1.00 39.38           O  
ANISOU 2631  O3'   U C   6     6232   4658   4072  -2241   1628  -1261       O  
ATOM   2632  C2'   U C   6     -46.418 -10.470 -19.970  1.00 45.70           C  
ANISOU 2632  C2'   U C   6     7814   4397   5152  -2230   1847   -937       C  
ATOM   2633  O2'   U C   6     -45.911  -9.893 -18.778  1.00 45.61           O  
ANISOU 2633  O2'   U C   6     7975   4463   4893  -1974   1751   -514       O  
ATOM   2634  C1'   U C   6     -46.948 -11.865 -19.678  1.00 52.59           C  
ANISOU 2634  C1'   U C   6     9013   4697   6273  -2677   2260   -944       C  
ATOM   2635  N1    U C   6     -46.748 -12.906 -20.771  1.00 56.44           N  
ANISOU 2635  N1    U C   6     9522   4763   7159  -2775   2339  -1325       N  
ATOM   2636  C2    U C   6     -45.476 -13.403 -21.036  1.00 57.36           C  
ANISOU 2636  C2    U C   6     9921   4454   7421  -2361   2175  -1160       C  
ATOM   2637  O2    U C   6     -44.465 -13.040 -20.446  1.00 55.41           O  
ANISOU 2637  O2    U C   6     9906   4178   6969  -1909   1963   -704       O  
ATOM   2638  N3    U C   6     -45.423 -14.353 -22.039  1.00 60.79           N  
ANISOU 2638  N3    U C   6    10288   4556   8253  -2481   2260  -1649       N  
ATOM   2639  C4    U C   6     -46.486 -14.844 -22.785  1.00 64.51           C  
ANISOU 2639  C4    U C   6    10418   5108   8986  -2981   2496  -2312       C  
ATOM   2640  O4    U C   6     -46.296 -15.694 -23.648  1.00 69.58           O  
ANISOU 2640  O4    U C   6    10966   5469  10004  -3033   2546  -2821       O  
ATOM   2641  C5    U C   6     -47.772 -14.291 -22.453  1.00 64.26           C  
ANISOU 2641  C5    U C   6    10104   5557   8755  -3401   2662  -2433       C  
ATOM   2642  C6    U C   6     -47.843 -13.369 -21.481  1.00 60.34           C  
ANISOU 2642  C6    U C   6     9694   5357   7874  -3271   2574  -1928       C  
ATOM   2643  P     A C   7     -47.590  -7.185 -21.105  1.00 35.67           P  
ANISOU 2643  P     A C   7     5305   4645   3605  -1900   1302  -1391       P  
ATOM   2644  OP1   A C   7     -47.929  -5.918 -20.420  1.00 34.25           O  
ANISOU 2644  OP1   A C   7     4890   4768   3356  -1756   1170  -1338       O  
ATOM   2645  OP2   A C   7     -48.289  -7.571 -22.357  1.00 36.23           O  
ANISOU 2645  OP2   A C   7     5053   5008   3706  -2068   1355  -1806       O  
ATOM   2646  O5'   A C   7     -46.022  -7.228 -21.437  1.00 32.43           O  
ANISOU 2646  O5'   A C   7     5113   3950   3258  -1501   1095  -1098       O  
ATOM   2647  C5'   A C   7     -45.029  -7.118 -20.415  1.00 30.37           C  
ANISOU 2647  C5'   A C   7     5165   3423   2953  -1270   1022   -759       C  
ATOM   2648  C4'   A C   7     -43.698  -7.592 -20.947  1.00 28.18           C  
ANISOU 2648  C4'   A C   7     5077   2894   2736   -979    890   -628       C  
ATOM   2649  O4'   A C   7     -43.785  -8.998 -21.318  1.00 32.12           O  
ANISOU 2649  O4'   A C   7     5833   3023   3348  -1166   1081   -757       O  
ATOM   2650  C3'   A C   7     -43.271  -6.834 -22.201  1.00 26.42           C  
ANISOU 2650  C3'   A C   7     4479   2999   2560   -765    676   -694       C  
ATOM   2651  O3'   A C   7     -42.005  -6.244 -21.974  1.00 25.37           O  
ANISOU 2651  O3'   A C   7     4373   2828   2439   -429    484   -468       O  
ATOM   2652  C2'   A C   7     -43.208  -7.904 -23.288  1.00 27.81           C  
ANISOU 2652  C2'   A C   7     4656   3133   2776   -840    740   -947       C  
ATOM   2653  O2'   A C   7     -42.139  -7.672 -24.189  1.00 26.74           O  
ANISOU 2653  O2'   A C   7     4362   3188   2612   -537    546   -900       O  
ATOM   2654  C1'   A C   7     -43.021  -9.192 -22.483  1.00 29.94           C  
ANISOU 2654  C1'   A C   7     5426   2810   3141   -955    928   -905       C  
ATOM   2655  N9    A C   7     -43.451 -10.403 -23.179  1.00 33.42           N  
ANISOU 2655  N9    A C   7     5901   3027   3769  -1205   1113  -1276       N  
ATOM   2656  C8    A C   7     -44.597 -10.584 -23.904  1.00 35.19           C  
ANISOU 2656  C8    A C   7     5792   3539   4039  -1547   1252  -1720       C  
ATOM   2657  N7    A C   7     -44.709 -11.774 -24.441  1.00 38.28           N  
ANISOU 2657  N7    A C   7     6232   3629   4684  -1740   1416  -2121       N  
ATOM   2658  C5    A C   7     -43.563 -12.435 -24.042  1.00 39.29           C  
ANISOU 2658  C5    A C   7     6796   3169   4963  -1472   1375  -1866       C  
ATOM   2659  C6    A C   7     -43.074 -13.748 -24.285  1.00 43.92           C  
ANISOU 2659  C6    A C   7     7638   3132   5919  -1456   1485  -2091       C  
ATOM   2660  N6    A C   7     -43.727 -14.657 -25.013  1.00 48.07           N  
ANISOU 2660  N6    A C   7     7981   3503   6782  -1797   1691  -2714       N  
ATOM   2661  N1    A C   7     -41.881 -14.097 -23.744  1.00 43.74           N  
ANISOU 2661  N1    A C   7     8026   2650   5944  -1050   1371  -1714       N  
ATOM   2662  C2    A C   7     -41.230 -13.188 -23.008  1.00 40.22           C  
ANISOU 2662  C2    A C   7     7684   2435   5163   -728   1172  -1207       C  
ATOM   2663  N3    A C   7     -41.588 -11.927 -22.718  1.00 36.79           N  
ANISOU 2663  N3    A C   7     7009   2546   4423   -760   1073  -1022       N  
ATOM   2664  C4    A C   7     -42.775 -11.605 -23.268  1.00 35.85           C  
ANISOU 2664  C4    A C   7     6530   2797   4296  -1127   1180  -1341       C  
ATOM   2665  P     U C   8     -41.860  -4.705 -21.556  1.00 27.47           P  
ANISOU 2665  P     U C   8     4354   3281   2804   -282    340   -351       P  
ATOM   2666  OP1   U C   8     -40.526  -4.605 -20.931  1.00 26.33           O  
ANISOU 2666  OP1   U C   8     4348   3004   2654    -25    224   -236       O  
ATOM   2667  OP2   U C   8     -43.038  -4.231 -20.794  1.00 25.96           O  
ANISOU 2667  OP2   U C   8     4061   3189   2616   -470    425   -460       O  
ATOM   2668  O5'   U C   8     -41.855  -3.980 -22.982  1.00 21.92           O  
ANISOU 2668  O5'   U C   8     3255   2880   2192   -193    244   -290       O  
ATOM   2669  C5'   U C   8     -40.938  -4.426 -23.970  1.00 21.29           C  
ANISOU 2669  C5'   U C   8     3148   2898   2041    -56    183   -246       C  
ATOM   2670  C4'   U C   8     -40.024  -3.317 -24.451  1.00 19.89           C  
ANISOU 2670  C4'   U C   8     2697   2861   2001    146     61     15       C  
ATOM   2671  O4'   U C   8     -40.818  -2.218 -24.967  1.00 18.40           O  
ANISOU 2671  O4'   U C   8     2161   2884   1944    146     59    194       O  
ATOM   2672  C3'   U C   8     -39.120  -2.709 -23.382  1.00 19.31           C  
ANISOU 2672  C3'   U C   8     2699   2527   2110    253     -5     66       C  
ATOM   2673  O3'   U C   8     -37.881  -2.455 -23.990  1.00 21.18           O  
ANISOU 2673  O3'   U C   8     2790   2872   2385    400    -74    189       O  
ATOM   2674  C2'   U C   8     -39.820  -1.414 -22.982  1.00 18.39           C  
ANISOU 2674  C2'   U C   8     2340   2356   2293    210     -3    126       C  
ATOM   2675  O2'   U C   8     -38.941  -0.377 -22.576  1.00 19.62           O  
ANISOU 2675  O2'   U C   8     2315   2358   2781    303    -60    175       O  
ATOM   2676  C1'   U C   8     -40.476  -1.012 -24.305  1.00 17.84           C  
ANISOU 2676  C1'   U C   8     1983   2571   2225    217     15    345       C  
ATOM   2677  N1    U C   8     -41.716  -0.180 -24.136  1.00 16.72           N  
ANISOU 2677  N1    U C   8     1643   2443   2267    192     28    351       N  
ATOM   2678  C2    U C   8     -41.723   1.150 -24.532  1.00 17.96           C  
ANISOU 2678  C2    U C   8     1491   2528   2804    332     -1    661       C  
ATOM   2679  O2    U C   8     -40.759   1.733 -25.026  1.00 18.99           O  
ANISOU 2679  O2    U C   8     1493   2575   3146    418      0    973       O  
ATOM   2680  N3    U C   8     -42.930   1.782 -24.319  1.00 19.11           N  
ANISOU 2680  N3    U C   8     1468   2685   3110    367    -10    597       N  
ATOM   2681  C4    U C   8     -44.081   1.221 -23.759  1.00 18.02           C  
ANISOU 2681  C4    U C   8     1401   2704   2740    232     17    222       C  
ATOM   2682  O4    U C   8     -45.088   1.896 -23.628  1.00 21.70           O  
ANISOU 2682  O4    U C   8     1648   3233   3362    304     -8    145       O  
ATOM   2683  C5    U C   8     -43.997  -0.162 -23.379  1.00 17.43           C  
ANISOU 2683  C5    U C   8     1650   2691   2280     15     93    -45       C  
ATOM   2684  C6    U C   8     -42.834  -0.803 -23.579  1.00 15.50           C  
ANISOU 2684  C6    U C   8     1612   2353   1925     28     90     48       C  
ATOM   2685  P     U C   9     -36.534  -2.816 -23.223  1.00 22.41           P  
ANISOU 2685  P     U C   9     3113   2910   2492    569   -155     59       P  
ATOM   2686  OP1   U C   9     -36.585  -4.249 -22.883  1.00 23.99           O  
ANISOU 2686  OP1   U C   9     3704   2985   2425    628   -145    -90       O  
ATOM   2687  OP2   U C   9     -36.340  -1.793 -22.173  1.00 24.25           O  
ANISOU 2687  OP2   U C   9     3221   3008   2986    574   -182     -7       O  
ATOM   2688  O5'   U C   9     -35.463  -2.581 -24.373  1.00 22.64           O  
ANISOU 2688  O5'   U C   9     2866   3221   2515    656   -191    181       O  
ATOM   2689  C5'   U C   9     -35.285  -3.542 -25.417  1.00 21.08           C  
ANISOU 2689  C5'   U C   9     2676   3294   2040    715   -201    119       C  
ATOM   2690  C4'   U C   9     -34.470  -2.931 -26.535  1.00 21.50           C  
ANISOU 2690  C4'   U C   9     2332   3759   2077    747   -197    319       C  
ATOM   2691  O4'   U C   9     -35.221  -1.885 -27.208  1.00 19.78           O  
ANISOU 2691  O4'   U C   9     1824   3690   2001    629   -107    700       O  
ATOM   2692  C3'   U C   9     -33.145  -2.280 -26.136  1.00 21.61           C  
ANISOU 2692  C3'   U C   9     2191   3756   2264    804   -227    323       C  
ATOM   2693  O3'   U C   9     -32.271  -2.428 -27.249  1.00 27.28           O  
ANISOU 2693  O3'   U C   9     2627   4961   2779    860   -223    371       O  
ATOM   2694  C2'   U C   9     -33.556  -0.815 -25.940  1.00 19.71           C  
ANISOU 2694  C2'   U C   9     1729   3299   2462    635   -128    625       C  
ATOM   2695  O2'   U C   9     -32.485   0.100 -26.003  1.00 21.09           O  
ANISOU 2695  O2'   U C   9     1596   3491   2927    571    -69    720       O  
ATOM   2696  C1'   U C   9     -34.514  -0.648 -27.119  1.00 20.01           C  
ANISOU 2696  C1'   U C   9     1607   3614   2383    583    -53    978       C  
ATOM   2697  N1    U C   9     -35.502   0.505 -27.068  1.00 18.20           N  
ANISOU 2697  N1    U C   9     1247   3148   2521    500     25   1313       N  
ATOM   2698  C2    U C   9     -35.275   1.646 -27.817  1.00 19.70           C  
ANISOU 2698  C2    U C   9     1102   3391   2993    466    143   1834       C  
ATOM   2699  O2    U C   9     -34.295   1.811 -28.518  1.00 22.56           O  
ANISOU 2699  O2    U C   9     1242   4035   3295    444    215   2054       O  
ATOM   2700  N3    U C   9     -36.231   2.618 -27.702  1.00 18.43           N  
ANISOU 2700  N3    U C   9      857   2927   3217    466    193   2116       N  
ATOM   2701  C4    U C   9     -37.390   2.569 -26.939  1.00 18.39           C  
ANISOU 2701  C4    U C   9     1020   2676   3290    483    125   1859       C  
ATOM   2702  O4    U C   9     -38.175   3.516 -26.935  1.00 19.73           O  
ANISOU 2702  O4    U C   9     1054   2612   3832    532    159   2108       O  
ATOM   2703  C5    U C   9     -37.566   1.352 -26.187  1.00 15.56           C  
ANISOU 2703  C5    U C   9      987   2353   2572    454     32   1323       C  
ATOM   2704  C6    U C   9     -36.634   0.394 -26.274  1.00 15.78           C  
ANISOU 2704  C6    U C   9     1147   2571   2279    472     -7   1117       C  
ATOM   2705  P     U C  10     -31.328  -3.711 -27.457  1.00 29.21           P  
ANISOU 2705  P     U C  10     2959   5454   2686   1100   -348    -34       P  
ATOM   2706  OP1   U C  10     -31.525  -4.670 -26.344  1.00 26.67           O  
ANISOU 2706  OP1   U C  10     3106   4682   2345   1262   -444   -319       O  
ATOM   2707  OP2   U C  10     -29.999  -3.158 -27.798  1.00 31.39           O  
ANISOU 2707  OP2   U C  10     2873   6089   2966   1116   -338    -20       O  
ATOM   2708  O5'   U C  10     -31.829  -4.372 -28.821  1.00 30.89           O  
ANISOU 2708  O5'   U C  10     3000   6154   2583   1104   -326    -71       O  
ATOM   2709  C5'   U C  10     -33.101  -4.970 -28.927  1.00 31.06           C  
ANISOU 2709  C5'   U C  10     3206   6039   2555   1039   -301   -170       C  
ATOM   2710  C4'   U C  10     -33.465  -5.287 -30.376  1.00 32.51           C  
ANISOU 2710  C4'   U C  10     3016   6925   2413   1038   -273   -241       C  
ATOM   2711  O4'   U C  10     -34.260  -4.218 -30.949  1.00 30.97           O  
ANISOU 2711  O4'   U C  10     2537   7035   2195    913   -171    246       O  
ATOM   2712  C3'   U C  10     -32.336  -5.570 -31.363  1.00 36.39           C  
ANISOU 2712  C3'   U C  10     3127   8101   2597   1187   -321   -407       C  
ATOM   2713  O3'   U C  10     -32.701  -6.733 -32.143  1.00 43.54           O  
ANISOU 2713  O3'   U C  10     3916   9368   3258   1274   -367   -940       O  
ATOM   2714  C2'   U C  10     -32.275  -4.284 -32.193  1.00 36.08           C  
ANISOU 2714  C2'   U C  10     2636   8631   2443   1081   -198    206       C  
ATOM   2715  O2'   U C  10     -31.869  -4.496 -33.522  1.00 39.75           O  
ANISOU 2715  O2'   U C  10     2603  10056   2444   1167   -184    153       O  
ATOM   2716  C1'   U C  10     -33.742  -3.855 -32.210  1.00 32.88           C  
ANISOU 2716  C1'   U C  10     2284   8098   2112    973   -131    478       C  
ATOM   2717  N1    U C  10     -34.016  -2.401 -32.386  1.00 30.43           N  
ANISOU 2717  N1    U C  10     1777   7811   1975    886     -6   1215       N  
ATOM   2718  C2    U C  10     -34.691  -1.959 -33.509  1.00 33.51           C  
ANISOU 2718  C2    U C  10     1779   8904   2050    946     64   1619       C  
ATOM   2719  O2    U C  10     -35.076  -2.687 -34.402  1.00 35.04           O  
ANISOU 2719  O2    U C  10     1716   9828   1769   1050     21   1326       O  
ATOM   2720  N3    U C  10     -34.908  -0.606 -33.559  1.00 34.70           N  
ANISOU 2720  N3    U C  10     1813   8894   2478    911    189   2371       N  
ATOM   2721  C4    U C  10     -34.532   0.330 -32.608  1.00 32.81           C  
ANISOU 2721  C4    U C  10     1769   7835   2861    775    258   2635       C  
ATOM   2722  O4    U C  10     -34.789   1.515 -32.784  1.00 36.13           O  
ANISOU 2722  O4    U C  10     2045   8086   3595    760    388   3296       O  
ATOM   2723  C5    U C  10     -33.838  -0.201 -31.470  1.00 28.68           C  
ANISOU 2723  C5    U C  10     1580   6739   2578    696    170   2076       C  
ATOM   2724  C6    U C  10     -33.619  -1.516 -31.404  1.00 28.44           C  
ANISOU 2724  C6    U C  10     1705   6878   2221    779     40   1462       C  
ATOM   2725  P     U C  11     -32.292  -8.232 -31.703  1.00 47.45           P  
ANISOU 2725  P     U C  11     4738   9407   3882   1464   -481  -1619       P  
ATOM   2726  OP1   U C  11     -30.902  -8.174 -31.203  1.00 47.46           O  
ANISOU 2726  OP1   U C  11     4808   9309   3917   1675   -584  -1626       O  
ATOM   2727  OP2   U C  11     -32.627  -9.145 -32.819  1.00 52.06           O  
ANISOU 2727  OP2   U C  11     4986  10542   4253   1511   -495  -2197       O  
ATOM   2728  O5'   U C  11     -33.273  -8.604 -30.482  1.00 47.03           O  
ANISOU 2728  O5'   U C  11     5274   8403   4194   1334   -424  -1590       O  
ATOM   2729  C5'   U C  11     -32.841  -9.410 -29.372  1.00 49.24           C  
ANISOU 2729  C5'   U C  11     6065   7923   4722   1501   -481  -1740       C  
ATOM   2730  C4'   U C  11     -33.146  -8.689 -28.070  1.00 47.84           C  
ANISOU 2730  C4'   U C  11     6236   7229   4712   1401   -436  -1292       C  
ATOM   2731  O4'   U C  11     -34.431  -9.108 -27.545  1.00 48.23           O  
ANISOU 2731  O4'   U C  11     6599   6792   4932   1177   -304  -1292       O  
ATOM   2732  C3'   U C  11     -32.230  -8.921 -26.876  1.00 48.84           C  
ANISOU 2732  C3'   U C  11     6715   6927   4915   1674   -536  -1238       C  
ATOM   2733  O3'   U C  11     -30.968  -8.268 -27.019  1.00 48.91           O  
ANISOU 2733  O3'   U C  11     6426   7365   4795   1847   -647  -1210       O  
ATOM   2734  C2'   U C  11     -33.087  -8.264 -25.791  1.00 46.89           C  
ANISOU 2734  C2'   U C  11     6711   6314   4791   1467   -440   -895       C  
ATOM   2735  C1'   U C  11     -34.491  -8.733 -26.183  1.00 46.43           C  
ANISOU 2735  C1'   U C  11     6723   6105   4813   1177   -288   -983       C  
TER    2736        U C  11                                                      
ATOM   2737  C4    U D   2      -9.052 -11.316 -19.229  1.00 51.50           C  
ANISOU 2737  C4    U D   2     6743   6641   6183  -2158   2263  -2542       C  
ATOM   2738  O4    U D   2      -8.065 -11.241 -18.173  1.00 47.99           O  
ANISOU 2738  O4    U D   2     6491   5550   6193  -1820   2247  -2112       O  
ATOM   2739  P     U D   3      -8.173 -12.237 -16.924  1.00 46.40           P  
ANISOU 2739  P     U D   3     6308   4774   6546  -1686   2528  -2006       P  
ATOM   2740  OP1   U D   3      -6.907 -12.205 -16.158  1.00 43.96           O  
ANISOU 2740  OP1   U D   3     6067   4071   6566  -1340   2547  -1584       O  
ATOM   2741  OP2   U D   3      -8.691 -13.519 -17.448  1.00 49.88           O  
ANISOU 2741  OP2   U D   3     6617   5088   7247  -2086   3085  -2569       O  
ATOM   2742  O5'   U D   3      -9.344 -11.546 -16.056  1.00 40.39           O  
ANISOU 2742  O5'   U D   3     5572   4252   5524  -1507   2131  -1764       O  
ATOM   2743  C5'   U D   3      -9.129 -10.393 -15.247  1.00 33.89           C  
ANISOU 2743  C5'   U D   3     4852   3475   4549  -1169   1713  -1301       C  
ATOM   2744  C4'   U D   3     -10.339 -10.103 -14.368  1.00 30.11           C  
ANISOU 2744  C4'   U D   3     4374   3113   3953  -1060   1497  -1166       C  
ATOM   2745  O4'   U D   3     -11.417  -9.557 -15.172  1.00 29.88           O  
ANISOU 2745  O4'   U D   3     4272   3611   3470  -1205   1320  -1327       O  
ATOM   2746  C3'   U D   3     -10.945 -11.298 -13.639  1.00 30.63           C  
ANISOU 2746  C3'   U D   3     4388   2881   4369  -1097   1806  -1262       C  
ATOM   2747  O3'   U D   3     -11.271 -10.899 -12.314  1.00 27.99           O  
ANISOU 2747  O3'   U D   3     4094   2486   4054   -808   1580   -895       O  
ATOM   2748  C2'   U D   3     -12.198 -11.649 -14.446  1.00 32.09           C  
ANISOU 2748  C2'   U D   3     4445   3420   4326  -1457   1904  -1739       C  
ATOM   2749  O2'   U D   3     -13.207 -12.127 -13.597  1.00 32.37           O  
ANISOU 2749  O2'   U D   3     4454   3333   4511  -1451   1996  -1761       O  
ATOM   2750  C1'   U D   3     -12.623 -10.287 -14.981  1.00 30.12           C  
ANISOU 2750  C1'   U D   3     4184   3757   3504  -1379   1436  -1595       C  
ATOM   2751  N1    U D   3     -13.423 -10.270 -16.259  1.00 29.84           N  
ANISOU 2751  N1    U D   3     3922   4426   2991  -1674   1434  -1985       N  
ATOM   2752  C2    U D   3     -14.702  -9.740 -16.256  1.00 29.96           C  
ANISOU 2752  C2    U D   3     3791   4997   2593  -1630   1188  -1947       C  
ATOM   2753  O2    U D   3     -15.248  -9.296 -15.260  1.00 27.87           O  
ANISOU 2753  O2    U D   3     3620   4574   2393  -1394    993  -1643       O  
ATOM   2754  N3    U D   3     -15.339  -9.752 -17.474  1.00 32.43           N  
ANISOU 2754  N3    U D   3     3790   6165   2366  -1872   1189  -2287       N  
ATOM   2755  C4    U D   3     -14.838 -10.230 -18.672  1.00 36.97           C  
ANISOU 2755  C4    U D   3     4191   7088   2767  -2196   1413  -2710       C  
ATOM   2756  O4    U D   3     -15.528 -10.180 -19.685  1.00 41.54           O  
ANISOU 2756  O4    U D   3     4402   8640   2743  -2399   1377  -3010       O  
ATOM   2757  C5    U D   3     -13.501 -10.761 -18.610  1.00 36.33           C  
ANISOU 2757  C5    U D   3     4332   6264   3207  -2255   1687  -2756       C  
ATOM   2758  C6    U D   3     -12.868 -10.757 -17.429  1.00 33.83           C  
ANISOU 2758  C6    U D   3     4309   5126   3419  -1971   1682  -2370       C  
ATOM   2759  P     U D   4     -10.762 -11.738 -11.049  1.00 28.46           P  
ANISOU 2759  P     U D   4     4120   2162   4531   -514   1838   -557       P  
ATOM   2760  OP1   U D   4     -10.105 -12.975 -11.535  1.00 31.02           O  
ANISOU 2760  OP1   U D   4     4404   2092   5290   -586   2407   -679       O  
ATOM   2761  OP2   U D   4     -11.892 -11.800 -10.098  1.00 29.96           O  
ANISOU 2761  OP2   U D   4     4308   2371   4703   -432   1765   -453       O  
ATOM   2762  O5'   U D   4      -9.653 -10.800 -10.369  1.00 25.61           O  
ANISOU 2762  O5'   U D   4     3727   1979   4026   -229   1517   -200       O  
ATOM   2763  C5'   U D   4      -8.482 -10.376 -11.075  1.00 24.83           C  
ANISOU 2763  C5'   U D   4     3625   1932   3878   -269   1483   -251       C  
ATOM   2764  C4'   U D   4      -8.098  -8.952 -10.693  1.00 22.88           C  
ANISOU 2764  C4'   U D   4     3376   1974   3345   -209   1109   -164       C  
ATOM   2765  O4'   U D   4      -9.212  -8.051 -10.962  1.00 21.45           O  
ANISOU 2765  O4'   U D   4     3313   1924   2912   -328    891   -262       O  
ATOM   2766  C3'   U D   4      -7.719  -8.730  -9.227  1.00 21.78           C  
ANISOU 2766  C3'   U D   4     3055   2052   3167     42    982     97       C  
ATOM   2767  O3'   U D   4      -6.719  -7.734  -9.130  1.00 23.02           O  
ANISOU 2767  O3'   U D   4     3119   2446   3181      9    846     27       O  
ATOM   2768  C2'   U D   4      -9.011  -8.176  -8.630  1.00 20.93           C  
ANISOU 2768  C2'   U D   4     3019   2030   2902     14    778     93       C  
ATOM   2769  O2'   U D   4      -8.791  -7.391  -7.469  1.00 17.78           O  
ANISOU 2769  O2'   U D   4     2469   1945   2340    105    591    169       O  
ATOM   2770  C1'   U D   4      -9.545  -7.334  -9.799  1.00 19.35           C  
ANISOU 2770  C1'   U D   4     3008   1792   2554   -205    693   -121       C  
ATOM   2771  N1    U D   4     -11.018  -7.122  -9.738  1.00 18.89           N  
ANISOU 2771  N1    U D   4     3025   1780   2371   -242    584   -140       N  
ATOM   2772  C2    U D   4     -11.495  -5.858  -9.435  1.00 17.95           C  
ANISOU 2772  C2    U D   4     2956   1764   2100   -222    427    -94       C  
ATOM   2773  O2    U D   4     -10.767  -4.924  -9.246  1.00 18.54           O  
ANISOU 2773  O2    U D   4     3024   1847   2172   -227    430   -104       O  
ATOM   2774  N3    U D   4     -12.861  -5.717  -9.380  1.00 17.58           N  
ANISOU 2774  N3    U D   4     2944   1794   1940   -213    341    -69       N  
ATOM   2775  C4    U D   4     -13.782  -6.730  -9.591  1.00 19.31           C  
ANISOU 2775  C4    U D   4     3130   2050   2158   -277    384   -162       C  
ATOM   2776  O4    U D   4     -14.985  -6.487  -9.515  1.00 20.62           O  
ANISOU 2776  O4    U D   4     3285   2363   2186   -273    291   -158       O  
ATOM   2777  C5    U D   4     -13.222  -8.021  -9.905  1.00 19.24           C  
ANISOU 2777  C5    U D   4     3079   1880   2353   -361    617   -288       C  
ATOM   2778  C6    U D   4     -11.890  -8.166  -9.965  1.00 18.61           C  
ANISOU 2778  C6    U D   4     2985   1676   2411   -313    714   -234       C  
ATOM   2779  P     U D   5      -5.160  -8.065  -9.033  1.00 25.88           P  
ANISOU 2779  P     U D   5     3242   2981   3610    135    964    106       P  
ATOM   2780  OP1   U D   5      -4.426  -6.813  -9.264  1.00 24.71           O  
ANISOU 2780  OP1   U D   5     3065   3007   3316    -62    863   -155       O  
ATOM   2781  OP2   U D   5      -4.863  -9.258  -9.837  1.00 25.01           O  
ANISOU 2781  OP2   U D   5     3187   2529   3785    184   1273    174       O  
ATOM   2782  O5'   U D   5      -5.042  -8.513  -7.500  1.00 26.42           O  
ANISOU 2782  O5'   U D   5     2979   3474   3586    460    926    435       O  
ATOM   2783  C5'   U D   5      -5.400  -7.595  -6.492  1.00 24.97           C  
ANISOU 2783  C5'   U D   5     2663   3699   3127    408    685    344       C  
ATOM   2784  C4'   U D   5      -5.418  -8.332  -5.173  1.00 27.18           C  
ANISOU 2784  C4'   U D   5     2615   4423   3290    775    697    745       C  
ATOM   2785  O4'   U D   5      -5.245  -7.396  -4.083  1.00 27.35           O  
ANISOU 2785  O4'   U D   5     2320   5136   2937    697    475    574       O  
ATOM   2786  C3'   U D   5      -6.731  -9.061  -4.917  1.00 26.79           C  
ANISOU 2786  C3'   U D   5     2767   4011   3400    897    787    970       C  
ATOM   2787  O3'   U D   5      -6.421 -10.283  -4.282  1.00 30.28           O  
ANISOU 2787  O3'   U D   5     2981   4562   3962   1344   1062   1498       O  
ATOM   2788  C2'   U D   5      -7.494  -8.093  -4.016  1.00 23.97           C  
ANISOU 2788  C2'   U D   5     2366   3982   2760    763    513    803       C  
ATOM   2789  O2'   U D   5      -8.405  -8.737  -3.152  1.00 24.61           O  
ANISOU 2789  O2'   U D   5     2421   4085   2845    987    557   1109       O  
ATOM   2790  C1'   U D   5      -6.342  -7.494  -3.211  1.00 26.66           C  
ANISOU 2790  C1'   U D   5     2250   5120   2758    789    392    721       C  
ATOM   2791  N1    U D   5      -6.606  -6.142  -2.677  1.00 26.30           N  
ANISOU 2791  N1    U D   5     2132   5384   2475    450    214    268       N  
ATOM   2792  C2    U D   5      -6.401  -5.911  -1.326  1.00 27.97           C  
ANISOU 2792  C2    U D   5     1880   6450   2298    512    107    252       C  
ATOM   2793  O2    U D   5      -6.000  -6.759  -0.550  1.00 30.22           O  
ANISOU 2793  O2    U D   5     1789   7327   2367    905    116    690       O  
ATOM   2794  N3    U D   5      -6.680  -4.627  -0.924  1.00 28.17           N  
ANISOU 2794  N3    U D   5     1862   6648   2194    105     55   -288       N  
ATOM   2795  C4    U D   5      -7.134  -3.597  -1.737  1.00 27.78           C  
ANISOU 2795  C4    U D   5     2206   5929   2420   -257    156   -678       C  
ATOM   2796  O4    U D   5      -7.342  -2.509  -1.244  1.00 31.76           O  
ANISOU 2796  O4    U D   5     2627   6572   2868   -584    233  -1126       O  
ATOM   2797  C5    U D   5      -7.332  -3.907  -3.134  1.00 25.86           C  
ANISOU 2797  C5    U D   5     2414   4902   2511   -204    228   -508       C  
ATOM   2798  C6    U D   5      -7.062  -5.152  -3.544  1.00 24.33           C  
ANISOU 2798  C6    U D   5     2247   4598   2400     98    231   -108       C  
ATOM   2799  P     U D   6      -6.311 -11.667  -5.086  1.00 34.04           P  
ANISOU 2799  P     U D   6     3612   4371   4949   1507   1577   1731       P  
ATOM   2800  OP1   U D   6      -6.468 -12.736  -4.081  1.00 35.79           O  
ANISOU 2800  OP1   U D   6     3631   4657   5312   2013   1926   2355       O  
ATOM   2801  OP2   U D   6      -5.128 -11.622  -5.958  1.00 33.94           O  
ANISOU 2801  OP2   U D   6     3554   4322   5018   1437   1652   1602       O  
ATOM   2802  O5'   U D   6      -7.608 -11.670  -6.017  1.00 30.96           O  
ANISOU 2802  O5'   U D   6     3649   3348   4765   1099   1615   1311       O  
ATOM   2803  C5'   U D   6      -8.861 -11.586  -5.450  1.00 31.36           C  
ANISOU 2803  C5'   U D   6     3800   3361   4754   1054   1519   1296       C  
ATOM   2804  C4'   U D   6      -9.908 -11.662  -6.523  1.00 31.10           C  
ANISOU 2804  C4'   U D   6     4066   2882   4867    667   1587    865       C  
ATOM   2805  O4'   U D   6     -10.197 -13.057  -6.774  1.00 34.84           O  
ANISOU 2805  O4'   U D   6     4585   2847   5804    710   2174    924       O  
ATOM   2806  C3'   U D   6     -11.193 -11.041  -6.010  1.00 28.93           C  
ANISOU 2806  C3'   U D   6     3877   2735   4379    554   1301    754       C  
ATOM   2807  O3'   U D   6     -11.235  -9.680  -6.434  1.00 25.18           O  
ANISOU 2807  O3'   U D   6     3477   2494   3597    335    903    491       O  
ATOM   2808  C2'   U D   6     -12.317 -11.930  -6.557  1.00 32.15           C  
ANISOU 2808  C2'   U D   6     4426   2734   5055    355   1631    527       C  
ATOM   2809  O2'   U D   6     -13.009 -11.380  -7.662  1.00 32.15           O  
ANISOU 2809  O2'   U D   6     4546   2792   4877    -12   1451     81       O  
ATOM   2810  C1'   U D   6     -11.582 -13.213  -6.974  1.00 36.42           C  
ANISOU 2810  C1'   U D   6     4929   2859   6048    441   2225    616       C  
ATOM   2811  N1    U D   6     -11.990 -14.399  -6.206  1.00 42.67           N  
ANISOU 2811  N1    U D   6     5679   3287   7245    679   2774    917       N  
ATOM   2812  C2    U D   6     -11.746 -14.524  -4.837  1.00 46.00           C  
ANISOU 2812  C2    U D   6     5939   3925   7614   1168   2778   1532       C  
ATOM   2813  O2    U D   6     -11.187 -13.688  -4.139  1.00 44.74           O  
ANISOU 2813  O2    U D   6     5616   4339   7043   1372   2315   1771       O  
ATOM   2814  N3    U D   6     -12.191 -15.706  -4.286  1.00 50.41           N  
ANISOU 2814  N3    U D   6     6488   4043   8624   1403   3429   1844       N  
ATOM   2815  C4    U D   6     -12.840 -16.743  -4.942  1.00 54.02           C  
ANISOU 2815  C4    U D   6     7085   3810   9630   1128   4119   1505       C  
ATOM   2816  O4    U D   6     -13.191 -17.740  -4.316  1.00 57.36           O  
ANISOU 2816  O4    U D   6     7495   3795  10504   1380   4787   1841       O  
ATOM   2817  C5    U D   6     -13.055 -16.536  -6.354  1.00 51.88           C  
ANISOU 2817  C5    U D   6     6929   3447   9335    538   4041    742       C  
ATOM   2818  C6    U D   6     -12.631 -15.396  -6.917  1.00 47.41           C  
ANISOU 2818  C6    U D   6     6371   3369   8274    381   3358    540       C  
ATOM   2819  P     A D   7     -11.450  -8.504  -5.363  1.00 23.03           P  
ANISOU 2819  P     A D   7     3115   2609   3026    375    561    528       P  
ATOM   2820  OP1   A D   7     -11.193  -7.262  -6.124  1.00 19.93           O  
ANISOU 2820  OP1   A D   7     2823   2253   2498    158    398    269       O  
ATOM   2821  OP2   A D   7     -10.767  -8.834  -4.084  1.00 22.79           O  
ANISOU 2821  OP2   A D   7     2794   2952   2912    668    581    845       O  
ATOM   2822  O5'   A D   7     -13.006  -8.632  -5.030  1.00 21.66           O  
ANISOU 2822  O5'   A D   7     3054   2318   2857    328    525    501       O  
ATOM   2823  C5'   A D   7     -14.013  -8.349  -5.991  1.00 20.89           C  
ANISOU 2823  C5'   A D   7     3126   2084   2726    105    477    251       C  
ATOM   2824  C4'   A D   7     -15.314  -9.007  -5.587  1.00 21.66           C  
ANISOU 2824  C4'   A D   7     3246   2080   2903     92    567    238       C  
ATOM   2825  O4'   A D   7     -15.089 -10.423  -5.336  1.00 23.43           O  
ANISOU 2825  O4'   A D   7     3423   2035   3445    199    967    366       O  
ATOM   2826  C3'   A D   7     -15.929  -8.425  -4.308  1.00 22.29           C  
ANISOU 2826  C3'   A D   7     3280   2339   2851    207    372    381       C  
ATOM   2827  O3'   A D   7     -17.269  -8.123  -4.556  1.00 25.40           O  
ANISOU 2827  O3'   A D   7     3747   2737   3166     79    281    222       O  
ATOM   2828  C2'   A D   7     -15.859  -9.578  -3.305  1.00 23.57           C  
ANISOU 2828  C2'   A D   7     3341   2420   3194    434    624    665       C  
ATOM   2829  O2'   A D   7     -16.989  -9.693  -2.465  1.00 23.05           O  
ANISOU 2829  O2'   A D   7     3280   2364   3116    470    612    720       O  
ATOM   2830  C1'   A D   7     -15.865 -10.784  -4.227  1.00 23.44           C  
ANISOU 2830  C1'   A D   7     3388   2017   3499    341   1032    551       C  
ATOM   2831  N9    A D   7     -15.350 -11.993  -3.605  1.00 26.91           N  
ANISOU 2831  N9    A D   7     3740   2233   4252    624   1477    908       N  
ATOM   2832  C8    A D   7     -14.323 -12.135  -2.709  1.00 27.13           C  
ANISOU 2832  C8    A D   7     3580   2499   4229   1008   1514   1380       C  
ATOM   2833  N7    A D   7     -14.134 -13.380  -2.328  1.00 30.69           N  
ANISOU 2833  N7    A D   7     3966   2655   5039   1305   2063   1763       N  
ATOM   2834  C5    A D   7     -15.099 -14.099  -3.011  1.00 32.49           C  
ANISOU 2834  C5    A D   7     4376   2337   5632   1013   2449   1412       C  
ATOM   2835  C6    A D   7     -15.434 -15.477  -3.062  1.00 38.26           C  
ANISOU 2835  C6    A D   7     5150   2452   6934   1059   3233   1481       C  
ATOM   2836  N6    A D   7     -14.809 -16.444  -2.372  1.00 41.59           N  
ANISOU 2836  N6    A D   7     5460   2634   7708   1551   3820   2115       N  
ATOM   2837  N1    A D   7     -16.466 -15.835  -3.860  1.00 39.98           N  
ANISOU 2837  N1    A D   7     5490   2336   7363    581   3478    867       N  
ATOM   2838  C2    A D   7     -17.110 -14.899  -4.571  1.00 35.35           C  
ANISOU 2838  C2    A D   7     4950   2105   6379    180   2928    342       C  
ATOM   2839  N3    A D   7     -16.884 -13.582  -4.602  1.00 31.52           N  
ANISOU 2839  N3    A D   7     4459   2132   5385    194   2218    362       N  
ATOM   2840  C4    A D   7     -15.860 -13.250  -3.796  1.00 29.69           C  
ANISOU 2840  C4    A D   7     4141   2114   5027    581   2041    861       C  
ATOM   2841  P     U D   8     -17.785  -6.694  -5.031  1.00 26.45           P  
ANISOU 2841  P     U D   8     3936   3035   3079     10     45    138       P  
ATOM   2842  OP1   U D   8     -19.168  -6.935  -5.487  1.00 26.30           O  
ANISOU 2842  OP1   U D   8     3908   3101   2986    -80     40      9       O  
ATOM   2843  OP2   U D   8     -16.801  -6.053  -5.937  1.00 27.03           O  
ANISOU 2843  OP2   U D   8     4048   3121   3102    -23     41    111       O  
ATOM   2844  O5'   U D   8     -17.771  -5.845  -3.663  1.00 23.09           O  
ANISOU 2844  O5'   U D   8     3463   2708   2602     98    -75    240       O  
ATOM   2845  C5'   U D   8     -18.591  -6.258  -2.571  1.00 21.44           C  
ANISOU 2845  C5'   U D   8     3206   2537   2404    159    -89    312       C  
ATOM   2846  C4'   U D   8     -19.530  -5.151  -2.128  1.00 19.07           C  
ANISOU 2846  C4'   U D   8     2928   2299   2020    128   -204    261       C  
ATOM   2847  O4'   U D   8     -18.768  -4.087  -1.490  1.00 18.06           O  
ANISOU 2847  O4'   U D   8     2731   2282   1849     87   -210    194       O  
ATOM   2848  C3'   U D   8     -20.359  -4.488  -3.224  1.00 18.86           C  
ANISOU 2848  C3'   U D   8     2979   2247   1941    104   -226    226       C  
ATOM   2849  O3'   U D   8     -21.638  -4.274  -2.707  1.00 19.58           O  
ANISOU 2849  O3'   U D   8     3053   2383   2004    130   -275    238       O  
ATOM   2850  C2'   U D   8     -19.631  -3.173  -3.478  1.00 18.60           C  
ANISOU 2850  C2'   U D   8     2987   2153   1929    105   -156    235       C  
ATOM   2851  O2'   U D   8     -20.480  -2.131  -3.909  1.00 20.95           O  
ANISOU 2851  O2'   U D   8     3325   2416   2220    194    -84    342       O  
ATOM   2852  C1'   U D   8     -19.085  -2.846  -2.090  1.00 17.04           C  
ANISOU 2852  C1'   U D   8     2696   2015   1765     39   -141    133       C  
ATOM   2853  N1    U D   8     -17.862  -2.021  -2.114  1.00 15.31           N  
ANISOU 2853  N1    U D   8     2435   1790   1594    -69     -7    -14       N  
ATOM   2854  C2    U D   8     -17.870  -0.725  -1.609  1.00 15.33           C  
ANISOU 2854  C2    U D   8     2411   1709   1704   -197    202   -201       C  
ATOM   2855  O2    U D   8     -18.838  -0.183  -1.108  1.00 16.03           O  
ANISOU 2855  O2    U D   8     2520   1712   1858   -194    273   -210       O  
ATOM   2856  N3    U D   8     -16.669  -0.060  -1.686  1.00 15.60           N  
ANISOU 2856  N3    U D   8     2376   1741   1812   -366    403   -436       N  
ATOM   2857  C4    U D   8     -15.490  -0.564  -2.229  1.00 15.60           C  
ANISOU 2857  C4    U D   8     2329   1847   1749   -377    351   -449       C  
ATOM   2858  O4    U D   8     -14.483   0.141  -2.249  1.00 18.28           O  
ANISOU 2858  O4    U D   8     2582   2199   2163   -566    567   -718       O  
ATOM   2859  C5    U D   8     -15.563  -1.902  -2.750  1.00 15.90           C  
ANISOU 2859  C5    U D   8     2416   1944   1684   -196    117   -188       C  
ATOM   2860  C6    U D   8     -16.719  -2.586  -2.675  1.00 14.69           C  
ANISOU 2860  C6    U D   8     2328   1760   1492    -71    -17    -10       C  
ATOM   2861  P     U D   9     -22.936  -4.585  -3.570  1.00 22.07           P  
ANISOU 2861  P     U D   9     3315   2871   2200    126   -307    199       P  
ATOM   2862  OP1   U D   9     -22.814  -5.908  -4.194  1.00 23.35           O  
ANISOU 2862  OP1   U D   9     3431   3064   2376    -10   -223     22       O  
ATOM   2863  OP2   U D   9     -23.162  -3.409  -4.450  1.00 24.04           O  
ANISOU 2863  OP2   U D   9     3552   3252   2329    257   -298    357       O  
ATOM   2864  O5'   U D   9     -24.057  -4.625  -2.428  1.00 20.36           O  
ANISOU 2864  O5'   U D   9     3067   2648   2020    139   -346    192       O  
ATOM   2865  C5'   U D   9     -24.152  -5.707  -1.491  1.00 19.85           C  
ANISOU 2865  C5'   U D   9     2997   2481   2066     87   -287    140       C  
ATOM   2866  C4'   U D   9     -24.965  -5.303  -0.258  1.00 19.55           C  
ANISOU 2866  C4'   U D   9     2943   2447   2037    126   -333    182       C  
ATOM   2867  O4'   U D   9     -24.232  -4.330   0.544  1.00 17.48           O  
ANISOU 2867  O4'   U D   9     2684   2189   1768    154   -358    232       O  
ATOM   2868  C3'   U D   9     -26.331  -4.659  -0.520  1.00 18.62           C  
ANISOU 2868  C3'   U D   9     2775   2456   1843    149   -396    155       C  
ATOM   2869  O3'   U D   9     -27.243  -5.018   0.539  1.00 21.46           O  
ANISOU 2869  O3'   U D   9     3110   2792   2251    125   -385    116       O  
ATOM   2870  C2'   U D   9     -25.982  -3.174  -0.503  1.00 18.25           C  
ANISOU 2870  C2'   U D   9     2769   2351   1814    245   -380    275       C  
ATOM   2871  O2'   U D   9     -27.117  -2.356  -0.292  1.00 18.20           O  
ANISOU 2871  O2'   U D   9     2720   2378   1819    340   -352    349       O  
ATOM   2872  C1'   U D   9     -24.980  -3.131   0.660  1.00 16.27           C  
ANISOU 2872  C1'   U D   9     2539   2015   1631    170   -349    218       C  
ATOM   2873  N1    U D   9     -24.048  -1.941   0.677  1.00 14.23           N  
ANISOU 2873  N1    U D   9     2295   1670   1441    129   -224    168       N  
ATOM   2874  C2    U D   9     -24.317  -0.901   1.543  1.00 13.01           C  
ANISOU 2874  C2    U D   9     2109   1450   1385     55    -77     49       C  
ATOM   2875  O2    U D   9     -25.261  -0.897   2.308  1.00 13.37           O  
ANISOU 2875  O2    U D   9     2121   1527   1433     50    -96     24       O  
ATOM   2876  N3    U D   9     -23.437   0.148   1.508  1.00 12.80           N  
ANISOU 2876  N3    U D   9     2078   1296   1490    -57    165   -101       N  
ATOM   2877  C4    U D   9     -22.328   0.264   0.700  1.00 12.31           C  
ANISOU 2877  C4    U D   9     2049   1178   1449    -74    232   -104       C  
ATOM   2878  O4    U D   9     -21.638   1.265   0.784  1.00 12.97           O  
ANISOU 2878  O4    U D   9     2115   1113   1699   -221    531   -306       O  
ATOM   2879  C5    U D   9     -22.099  -0.854  -0.195  1.00 13.09           C  
ANISOU 2879  C5    U D   9     2192   1377   1404     45      3     78       C  
ATOM   2880  C6    U D   9     -22.945  -1.897  -0.184  1.00 12.60           C  
ANISOU 2880  C6    U D   9     2124   1426   1237    123   -186    181       C  
ATOM   2881  P     U D  10     -28.274  -6.249   0.380  1.00 24.89           P  
ANISOU 2881  P     U D  10     3467   3271   2718      3   -285    -70       P  
ATOM   2882  OP1   U D  10     -27.937  -7.028  -0.817  1.00 21.29           O  
ANISOU 2882  OP1   U D  10     2960   2881   2248   -122   -181   -245       O  
ATOM   2883  OP2   U D  10     -29.630  -5.708   0.554  1.00 24.40           O  
ANISOU 2883  OP2   U D  10     3310   3387   2576     21   -363   -114       O  
ATOM   2884  O5'   U D  10     -27.978  -7.128   1.683  1.00 24.54           O  
ANISOU 2884  O5'   U D  10     3485   3000   2838     26   -123     25       O  
ATOM   2885  C5'   U D  10     -26.901  -8.038   1.782  1.00 26.05           C  
ANISOU 2885  C5'   U D  10     3716   3028   3156     78     67    149       C  
ATOM   2886  C4'   U D  10     -26.631  -8.367   3.237  1.00 26.61           C  
ANISOU 2886  C4'   U D  10     3770   3092   3247    247    161    422       C  
ATOM   2887  O4'   U D  10     -25.785  -7.331   3.795  1.00 25.60           O  
ANISOU 2887  O4'   U D  10     3587   3229   2912    323    -61    525       O  
ATOM   2888  C3'   U D  10     -27.860  -8.405   4.136  1.00 29.56           C  
ANISOU 2888  C3'   U D  10     4130   3471   3632    229    192    396       C  
ATOM   2889  O3'   U D  10     -27.794  -9.481   5.043  1.00 36.82           O  
ANISOU 2889  O3'   U D  10     5036   4267   4686    384    509    657       O  
ATOM   2890  C2'   U D  10     -27.793  -7.111   4.918  1.00 26.72           C  
ANISOU 2890  C2'   U D  10     3720   3378   3054    255    -76    419       C  
ATOM   2891  O2'   U D  10     -28.424  -7.200   6.179  1.00 28.79           O  
ANISOU 2891  O2'   U D  10     3932   3741   3267    302    -31    504       O  
ATOM   2892  C1'   U D  10     -26.284  -6.960   5.065  1.00 24.18           C  
ANISOU 2892  C1'   U D  10     3333   3240   2613    356   -113    577       C  
ATOM   2893  N1    U D  10     -25.971  -5.536   5.371  1.00 20.72           N  
ANISOU 2893  N1    U D  10     2830   3026   2016    257   -293    415       N  
ATOM   2894  C2    U D  10     -25.470  -5.195   6.607  1.00 19.96           C  
ANISOU 2894  C2    U D  10     2548   3337   1700    265   -315    433       C  
ATOM   2895  O2    U D  10     -25.226  -6.015   7.470  1.00 20.80           O  
ANISOU 2895  O2    U D  10     2522   3712   1671    436   -241    691       O  
ATOM   2896  N3    U D  10     -25.240  -3.852   6.791  1.00 18.46           N  
ANISOU 2896  N3    U D  10     2289   3275   1449     68   -355    136       N  
ATOM   2897  C4    U D  10     -25.479  -2.853   5.864  1.00 16.51           C  
ANISOU 2897  C4    U D  10     2181   2696   1398    -43   -321    -44       C  
ATOM   2898  O4    U D  10     -25.235  -1.690   6.148  1.00 18.77           O  
ANISOU 2898  O4    U D  10     2400   3016   1714   -219   -207   -307       O  
ATOM   2899  C5    U D  10     -26.010  -3.286   4.604  1.00 17.99           C  
ANISOU 2899  C5    U D  10     2541   2559   1735     58   -352     87       C  
ATOM   2900  C6    U D  10     -26.239  -4.585   4.406  1.00 17.38           C  
ANISOU 2900  C6    U D  10     2496   2436   1672    156   -357    242       C  
ATOM   2901  P     U D  11     -28.886 -10.645   4.941  1.00 43.88           P  
ANISOU 2901  P     U D  11     5974   4802   5897    269    928    508       P  
ATOM   2902  OP1   U D  11     -29.184 -11.126   6.324  1.00 44.75           O  
ANISOU 2902  OP1   U D  11     6067   4890   6047    478   1155    845       O  
ATOM   2903  OP2   U D  11     -28.356 -11.558   3.895  1.00 45.28           O  
ANISOU 2903  OP2   U D  11     6182   4687   6337    179   1267    388       O  
ATOM   2904  O5'   U D  11     -30.192  -9.934   4.342  1.00 43.84           O  
ANISOU 2904  O5'   U D  11     5933   4933   5791     -2    679     69       O  
ATOM   2905  C5'   U D  11     -31.234  -9.469   5.175  1.00 44.83           C  
ANISOU 2905  C5'   U D  11     6032   5166   5837    -12    564     40       C  
ATOM   2906  C4'   U D  11     -32.421  -9.162   4.287  1.00 46.95           C  
ANISOU 2906  C4'   U D  11     6198   5589   6053   -240    455   -364       C  
ATOM   2907  O4'   U D  11     -33.641  -9.618   4.930  1.00 48.41           O  
ANISOU 2907  O4'   U D  11     6341   5701   6353   -341    643   -514       O  
ATOM   2908  C3'   U D  11     -32.625  -7.680   3.985  1.00 45.89           C  
ANISOU 2908  C3'   U D  11     6009   5761   5666   -173     52   -342       C  
ATOM   2909  O3'   U D  11     -31.900  -7.287   2.815  1.00 45.40           O  
ANISOU 2909  O3'   U D  11     5925   5831   5494   -160    -75   -351       O  
ATOM   2910  C2'   U D  11     -34.136  -7.637   3.770  1.00 47.11           C  
ANISOU 2910  C2'   U D  11     6003   6119   5775   -300     42   -609       C  
ATOM   2911  C1'   U D  11     -34.614  -8.595   4.861  1.00 47.97           C  
ANISOU 2911  C1'   U D  11     6175   5951   6100   -365    338   -636       C  
TER    2912        U D  11                                                      
HETATM 2913  C1  GOL A 201     -23.624   9.503  17.403  1.00 33.78           C  
HETATM 2914  O1  GOL A 201     -22.298   9.133  17.666  1.00 30.27           O  
HETATM 2915  C2  GOL A 201     -24.209   8.559  16.371  1.00 36.09           C  
HETATM 2916  O2  GOL A 201     -24.683   7.403  17.024  1.00 36.03           O  
HETATM 2917  C3  GOL A 201     -25.339   9.259  15.620  1.00 38.27           C  
HETATM 2918  O3  GOL A 201     -25.475   8.704  14.322  1.00 40.62           O  
HETATM 2919  C1  GOL A 202      -2.241   2.540 -13.092  1.00 33.46           C  
HETATM 2920  O1  GOL A 202      -2.014   3.563 -12.136  1.00 32.20           O  
HETATM 2921  C2  GOL A 202      -1.256   1.378 -12.962  1.00 34.18           C  
HETATM 2922  O2  GOL A 202      -0.647   1.201 -14.230  1.00 35.25           O  
HETATM 2923  C3  GOL A 202      -2.007   0.076 -12.659  1.00 33.80           C  
HETATM 2924  O3  GOL A 202      -2.623   0.001 -11.383  1.00 33.38           O  
HETATM 2925  C1  GOL A 203      -0.589  -5.837 -21.860  1.00 48.33           C  
HETATM 2926  O1  GOL A 203       0.503  -5.214 -21.208  1.00 46.15           O  
HETATM 2927  C2  GOL A 203      -0.484  -7.356 -21.811  1.00 48.59           C  
HETATM 2928  O2  GOL A 203      -1.487  -7.875 -20.971  1.00 49.63           O  
HETATM 2929  C3  GOL A 203      -0.677  -7.915 -23.214  1.00 49.15           C  
HETATM 2930  O3  GOL A 203       0.541  -8.496 -23.616  1.00 49.47           O  
HETATM 2931  C1  GOL A 204      -7.469   0.272 -38.986  1.00 55.65           C  
HETATM 2932  O1  GOL A 204      -6.581   1.168 -39.617  1.00 55.51           O  
HETATM 2933  C2  GOL A 204      -6.857  -1.127 -38.971  1.00 55.58           C  
HETATM 2934  O2  GOL A 204      -7.706  -2.021 -39.650  1.00 55.73           O  
HETATM 2935  C3  GOL A 204      -6.601  -1.629 -37.548  1.00 55.88           C  
HETATM 2936  O3  GOL A 204      -7.782  -1.672 -36.771  1.00 55.70           O  
HETATM 2937  C1  GOL A 205     -11.027  -7.297 -26.304  1.00 49.36           C  
HETATM 2938  O1  GOL A 205     -12.421  -7.084 -26.213  1.00 50.53           O  
HETATM 2939  C2  GOL A 205     -10.262  -6.199 -25.566  1.00 48.95           C  
HETATM 2940  O2  GOL A 205     -10.797  -4.915 -25.824  1.00 47.65           O  
HETATM 2941  C3  GOL A 205      -8.780  -6.260 -25.930  1.00 49.10           C  
HETATM 2942  O3  GOL A 205      -8.434  -5.176 -26.766  1.00 49.59           O  
HETATM 2943  C1  M2M A 206      -6.878  -0.436   1.265  1.00 40.34           C  
HETATM 2944  O1  M2M A 206      -7.795   0.661   1.401  1.00 41.88           O  
HETATM 2945  C2  M2M A 206      -7.159   1.938   1.452  1.00 41.79           C  
HETATM 2946  C3  M2M A 206      -7.948   2.999   0.669  1.00 42.92           C  
HETATM 2947  O2  M2M A 206      -9.279   3.161   1.182  1.00 42.65           O  
HETATM 2948  C4  M2M A 206      -9.665   4.513   1.423  1.00 40.84           C  
HETATM 2949  C5  M2M A 206     -11.116   4.534   1.916  1.00 40.26           C  
HETATM 2950  O3  M2M A 206     -11.197   4.539   3.347  1.00 38.18           O  
HETATM 2951  C6  M2M A 206     -12.086   5.550   3.810  1.00 37.36           C  
HETATM 2952  C1  EDO A 207      -5.268  10.004 -19.981  1.00 34.75           C  
HETATM 2953  O1  EDO A 207      -6.143   9.754 -21.078  1.00 36.41           O  
HETATM 2954  C2  EDO A 207      -3.839  10.152 -20.476  1.00 36.04           C  
HETATM 2955  O2  EDO A 207      -3.012   9.171 -19.844  1.00 35.91           O  
HETATM 2956  C1  EDO A 208     -12.502   9.418   7.097  1.00 46.05           C  
HETATM 2957  O1  EDO A 208     -12.736  10.050   8.357  1.00 48.48           O  
HETATM 2958  C2  EDO A 208     -13.773   9.523   6.266  1.00 45.61           C  
HETATM 2959  O2  EDO A 208     -13.639   8.759   5.064  1.00 44.05           O  
HETATM 2960  C1  GOL D 101      -4.132  -9.063 -12.938  1.00 45.01           C  
HETATM 2961  O1  GOL D 101      -3.214  -8.759 -13.971  1.00 44.07           O  
HETATM 2962  C2  GOL D 101      -4.438 -10.556 -12.914  1.00 45.73           C  
HETATM 2963  O2  GOL D 101      -4.120 -11.108 -11.655  1.00 46.55           O  
HETATM 2964  C3  GOL D 101      -5.917 -10.775 -13.216  1.00 45.51           C  
HETATM 2965  O3  GOL D 101      -6.210 -12.151 -13.282  1.00 44.35           O  
HETATM 2966  C1  GOL D 102     -11.385  -2.444  -7.164  1.00 30.57           C  
HETATM 2967  O1  GOL D 102     -11.917  -2.459  -8.468  1.00 28.30           O  
HETATM 2968  C2  GOL D 102     -10.967  -3.857  -6.791  1.00 30.62           C  
HETATM 2969  O2  GOL D 102      -9.645  -3.848  -6.303  1.00 31.71           O  
HETATM 2970  C3  GOL D 102     -11.904  -4.410  -5.730  1.00 30.46           C  
HETATM 2971  O3  GOL D 102     -12.941  -5.180  -6.268  1.00 31.18           O  
HETATM 2972  O   HOH A 301     -14.401  -0.385   2.373  1.00  2.00           O  
HETATM 2973  O   HOH A 302     -15.010  -3.046  22.349  1.00  2.00           O  
HETATM 2974  O   HOH A 303     -29.400  -4.309  -9.271  1.00  4.31           O  
HETATM 2975  O   HOH A 304      -7.933   2.698 -26.436  1.00  2.00           O  
HETATM 2976  O   HOH A 305     -23.895   5.208   9.424  1.00  3.48           O  
HETATM 2977  O   HOH A 306     -22.091   0.950  -5.928  1.00  2.00           O  
HETATM 2978  O   HOH A 307     -28.769  -1.538  -9.003  1.00  2.00           O  
HETATM 2979  O   HOH A 308     -22.098   5.016   7.236  1.00  2.00           O  
HETATM 2980  O   HOH A 309     -12.666  -0.932  22.928  1.00  4.56           O  
HETATM 2981  O   HOH A 310     -17.075   2.874  22.686  1.00  4.61           O  
HETATM 2982  O   HOH A 311     -10.256   2.479  -5.756  1.00  8.11           O  
HETATM 2983  O   HOH A 312      -4.042   1.563 -18.847  1.00  2.00           O  
HETATM 2984  O   HOH A 313      -0.732   5.766 -25.403  1.00  2.00           O  
HETATM 2985  O   HOH A 314     -24.209  -2.849   9.154  1.00  2.00           O  
HETATM 2986  O   HOH A 315     -16.559   2.565  -0.104  1.00  4.03           O  
HETATM 2987  O   HOH A 316     -19.772   3.049  23.821  1.00  5.99           O  
HETATM 2988  O   HOH A 317     -23.360  -4.785  11.059  1.00  4.62           O  
HETATM 2989  O   HOH A 318     -27.087   4.252 -20.847  1.00  6.96           O  
HETATM 2990  O   HOH A 319      -6.732  -4.392 -22.819  1.00  2.03           O  
HETATM 2991  O   HOH A 320     -18.376   9.283  11.756  1.00  3.76           O  
HETATM 2992  O   HOH A 321     -15.845  10.356  -7.961  1.00  5.07           O  
HETATM 2993  O   HOH A 322     -35.821  -5.791  -7.668  1.00  2.00           O  
HETATM 2994  O   HOH A 323     -21.456  -3.367 -22.712  1.00  4.66           O  
HETATM 2995  O   HOH A 324     -18.684   3.121  19.555  1.00  2.00           O  
HETATM 2996  O   HOH A 325      -3.046   6.733 -26.414  1.00  6.96           O  
HETATM 2997  O   HOH A 326     -13.661  -7.998  -0.670  1.00  9.45           O  
HETATM 2998  O   HOH A 327     -15.114   6.487   4.079  1.00  4.44           O  
HETATM 2999  O   HOH A 328     -33.951  -0.770  -2.116  1.00  5.94           O  
HETATM 3000  O   HOH A 329     -21.788  -4.734 -11.682  1.00  5.05           O  
HETATM 3001  O   HOH A 330      -2.823   6.873 -10.843  1.00  2.00           O  
HETATM 3002  O   HOH A 331      -2.243  -7.112   0.337  1.00 13.20           O  
HETATM 3003  O   HOH A 332     -29.207  -5.390 -12.026  1.00  9.37           O  
HETATM 3004  O   HOH A 333       1.524   7.090 -25.873  1.00 13.98           O  
HETATM 3005  O   HOH A 334      -4.332   7.899 -24.262  1.00 16.19           O  
HETATM 3006  O   HOH A 335     -28.865   1.663   5.451  1.00 14.80           O  
HETATM 3007  O   HOH A 336     -25.129   2.575   6.106  1.00  6.65           O  
HETATM 3008  O   HOH A 337      -0.852  -7.570 -11.183  1.00 10.20           O  
HETATM 3009  O   HOH A 338      -6.285  12.528 -16.868  1.00  3.58           O  
HETATM 3010  O   HOH A 339     -21.878   7.129   3.458  1.00 14.79           O  
HETATM 3011  O   HOH A 340     -13.929 -13.754   5.132  1.00  3.06           O  
HETATM 3012  O   HOH A 341     -14.703   6.516 -31.532  1.00 14.65           O  
HETATM 3013  O   HOH A 342     -12.787   9.885  15.745  1.00  7.97           O  
HETATM 3014  O   HOH A 343     -17.541  -3.995  21.322  1.00  4.48           O  
HETATM 3015  O   HOH A 344     -19.810  10.116  18.539  1.00  8.26           O  
HETATM 3016  O   HOH A 345      -0.725  -6.248   9.792  1.00 16.11           O  
HETATM 3017  O   HOH A 346      -8.159   1.626 -35.302  1.00  8.62           O  
HETATM 3018  O   HOH A 347     -11.389   8.926 -30.621  1.00  9.96           O  
HETATM 3019  O   HOH A 348       4.378   2.483 -22.361  1.00 11.48           O  
HETATM 3020  O   HOH A 349       1.681   0.783 -18.479  1.00  3.33           O  
HETATM 3021  O   HOH A 350     -35.882  -1.545  -3.858  1.00  2.00           O  
HETATM 3022  O   HOH A 351     -32.139  -4.292  -9.718  1.00  7.02           O  
HETATM 3023  O   HOH A 352     -24.381 -13.223   4.432  1.00 12.54           O  
HETATM 3024  O   HOH A 353     -12.325  14.414 -15.336  1.00 11.15           O  
HETATM 3025  O   HOH A 354      -8.918   9.235  14.280  1.00 17.14           O  
HETATM 3026  O   HOH A 355      -5.016   0.462 -10.159  1.00 11.08           O  
HETATM 3027  O   HOH A 356      -1.732   9.986 -13.575  1.00  7.00           O  
HETATM 3028  O   HOH A 357     -29.396  -2.425 -18.207  1.00 14.28           O  
HETATM 3029  O   HOH A 358     -17.561  -3.277 -27.379  1.00 10.58           O  
HETATM 3030  O   HOH A 359     -22.792  -4.835 -20.087  1.00 15.32           O  
HETATM 3031  O   HOH A 360       2.864 -11.333 -20.051  1.00 20.11           O  
HETATM 3032  O   HOH A 361      -2.391   7.939 -22.064  1.00 11.82           O  
HETATM 3033  O   HOH A 362     -14.940  12.006 -19.422  1.00 15.59           O  
HETATM 3034  O   HOH A 363     -24.623   9.323 -15.180  1.00  9.55           O  
HETATM 3035  O   HOH A 364      -5.112 -13.908   2.276  1.00  8.79           O  
HETATM 3036  O   HOH A 365      -7.273 -14.908   1.546  1.00  6.58           O  
HETATM 3037  O   HOH A 366      -6.713  -0.412  16.960  1.00 16.26           O  
HETATM 3038  O   HOH A 367     -14.943  12.476 -16.951  1.00 12.47           O  
HETATM 3039  O   HOH A 368     -12.600  -7.540 -23.141  1.00 16.15           O  
HETATM 3040  O   HOH A 369      -8.075  -1.555  22.581  1.00 11.15           O  
HETATM 3041  O   HOH A 370     -21.587  -6.086  -9.374  1.00 27.25           O  
HETATM 3042  O   HOH A 371     -20.493  -5.792 -24.210  1.00 22.55           O  
HETATM 3043  O   HOH A 372     -18.118  -7.312 -24.995  1.00 19.06           O  
HETATM 3044  O   HOH A 373      -8.012  10.810 -18.548  1.00  3.41           O  
HETATM 3045  O   HOH A 374     -10.860   8.259   4.541  1.00 23.26           O  
HETATM 3046  O   HOH A 375     -17.732  -9.693 -11.210  1.00 20.42           O  
HETATM 3047  O   HOH A 376      -4.304   3.359  -5.929  1.00 26.76           O  
HETATM 3048  O   HOH A 377     -19.259  -6.987 -10.300  1.00 22.78           O  
HETATM 3049  O   HOH A 378     -26.152  -6.357 -16.214  1.00 25.15           O  
HETATM 3050  O   HOH A 379     -22.658 -20.535  -4.910  1.00 30.18           O  
HETATM 3051  O   HOH A 380      -2.037  -3.200 -22.560  1.00 17.61           O  
HETATM 3052  O   HOH A 381     -31.827  -6.578  -6.799  1.00 25.53           O  
HETATM 3053  O   HOH A 382     -15.309  11.186   9.190  1.00 19.83           O  
HETATM 3054  O   HOH A 383     -22.900  -9.195 -14.245  1.00 19.38           O  
HETATM 3055  O   HOH A 384     -21.424  10.688 -24.549  1.00 16.10           O  
HETATM 3056  O   HOH A 385     -20.030   7.222   1.448  1.00 22.08           O  
HETATM 3057  O   HOH A 386     -13.460   4.363  22.000  1.00 14.28           O  
HETATM 3058  O   HOH A 387     -15.322   7.966  -1.075  1.00 26.16           O  
HETATM 3059  O   HOH A 388     -19.854 -16.554  -5.073  1.00 20.17           O  
HETATM 3060  O   HOH A 389      -7.588   2.214  -5.732  1.00 18.00           O  
HETATM 3061  O   HOH A 390     -25.837   1.243 -25.273  1.00 23.51           O  
HETATM 3062  O   HOH A 391     -16.367   7.732  -3.789  1.00 12.73           O  
HETATM 3063  O   HOH A 392      -5.531   4.052   8.012  1.00 16.45           O  
HETATM 3064  O   HOH A 393     -10.941 -11.142  -0.201  1.00 18.11           O  
HETATM 3065  O   HOH A 394     -16.971  11.449  -9.882  1.00 23.62           O  
HETATM 3066  O   HOH A 395     -27.579   4.664  -0.923  1.00  8.79           O  
HETATM 3067  O   HOH A 396      -9.106   2.069  20.977  1.00 20.16           O  
HETATM 3068  O   HOH A 397     -24.526  -8.399 -16.297  1.00 19.77           O  
HETATM 3069  O   HOH A 398     -10.786   2.273  -3.086  1.00 18.27           O  
HETATM 3070  O   HOH A 399     -20.745 -10.468  15.212  1.00 17.01           O  
HETATM 3071  O   HOH A 400     -23.891   9.298  -7.256  1.00 14.20           O  
HETATM 3072  O   HOH A 401      -9.729 -10.785  14.960  1.00  5.46           O  
HETATM 3073  O   HOH A 402     -22.231  -9.363  -2.456  1.00 13.44           O  
HETATM 3074  O   HOH A 403      -6.118   5.360   5.712  1.00 15.33           O  
HETATM 3075  O   HOH A 404      -1.986   9.704 -28.947  1.00 12.22           O  
HETATM 3076  O   HOH A 405     -29.440 -20.469  -0.835  1.00 18.04           O  
HETATM 3077  O   HOH A 406       0.394 -10.421 -13.997  1.00 12.64           O  
HETATM 3078  O   HOH A 407     -23.975  12.074 -12.754  1.00 21.67           O  
HETATM 3079  O   HOH A 408     -22.798  -8.423  15.553  1.00 13.49           O  
HETATM 3080  O   HOH A 409      -4.215 -10.298  -1.972  1.00 19.55           O  
HETATM 3081  O   HOH A 410      -3.093  -3.393 -10.327  1.00 11.00           O  
HETATM 3082  O   HOH A 411     -12.408 -13.995  17.365  1.00 17.65           O  
HETATM 3083  O   HOH A 412     -21.644   2.570 -27.037  1.00 10.02           O  
HETATM 3084  O   HOH A 413      -2.918   2.353  12.025  1.00 22.32           O  
HETATM 3085  O   HOH A 414     -25.819  13.561 -14.319  1.00 31.37           O  
HETATM 3086  O   HOH A 415     -14.555 -17.801  14.554  1.00 14.92           O  
HETATM 3087  O   HOH A 416     -16.905   7.425  21.410  1.00 18.03           O  
HETATM 3088  O   HOH A 417     -25.541 -15.055   3.580  1.00 15.73           O  
HETATM 3089  O   HOH A 418     -30.223  -4.388   3.136  1.00 16.75           O  
HETATM 3090  O   HOH A 419     -18.763   9.829  21.125  1.00 17.94           O  
HETATM 3091  O   HOH A 420      -7.951  14.273 -11.487  1.00 28.59           O  
HETATM 3092  O   HOH A 421     -20.472  -6.535  19.264  1.00 11.83           O  
HETATM 3093  O   HOH A 422     -24.388   8.157 -21.989  1.00 19.27           O  
HETATM 3094  O   HOH A 423       1.618   6.354 -17.739  1.00 24.40           O  
HETATM 3095  O   HOH A 424      -7.225   8.734 -23.613  1.00 22.38           O  
HETATM 3096  O   HOH A 425     -29.949   5.739  -0.651  1.00 14.01           O  
HETATM 3097  O   HOH A 426     -16.176 -10.988  19.373  1.00 30.41           O  
HETATM 3098  O   HOH A 427       2.314   0.474 -14.261  1.00 16.39           O  
HETATM 3099  O   HOH A 428     -31.322   6.191   1.544  1.00 25.45           O  
HETATM 3100  O   HOH A 429     -25.831   5.932  12.825  1.00  6.53           O  
HETATM 3101  O   HOH A 430     -36.806  -3.508  -2.070  1.00 14.08           O  
HETATM 3102  O   HOH A 431      -7.774  10.937 -31.391  1.00 14.23           O  
HETATM 3103  O   HOH A 432      -8.911   8.372 -31.654  1.00 12.65           O  
HETATM 3104  O   HOH A 433     -12.426  -3.307 -27.331  1.00 21.90           O  
HETATM 3105  O   HOH A 434     -27.343   8.481 -13.862  1.00  9.47           O  
HETATM 3106  O   HOH A 435     -28.793   8.491 -16.003  1.00  9.54           O  
HETATM 3107  O  AHOH A 436     -18.245  12.241   8.595  0.50 10.24           O  
HETATM 3108  O  BHOH A 436     -20.036  11.164   9.143  0.50  2.00           O  
HETATM 3109  O   HOH A 437     -17.802 -22.711  -0.794  1.00 16.79           O  
HETATM 3110  O   HOH A 438       2.713  -6.326 -20.580  1.00  9.25           O  
HETATM 3111  O   HOH A 439     -22.192  -2.088  -6.843  1.00 15.64           O  
HETATM 3112  O   HOH A 440       7.732 -10.366 -12.668  1.00 13.84           O  
HETATM 3113  O   HOH A 441     -11.422  11.850 -10.977  1.00 18.75           O  
HETATM 3114  O   HOH A 442     -21.794  -4.852  23.962  1.00 30.44           O  
HETATM 3115  O   HOH A 443     -19.212  -4.629  23.251  1.00 21.91           O  
HETATM 3116  O   HOH A 444       1.806  -3.826 -23.897  1.00 16.86           O  
HETATM 3117  O   HOH A 445     -25.371   6.004  -2.314  1.00  7.13           O  
HETATM 3118  O   HOH A 446     -24.719   7.790  -0.726  1.00 15.95           O  
HETATM 3119  O   HOH A 447     -26.446   7.642  -4.079  1.00 24.00           O  
HETATM 3120  O   HOH B 201     -37.704   2.446 -20.171  1.00  2.00           O  
HETATM 3121  O   HOH B 202     -38.098   9.705 -29.193  1.00 15.44           O  
HETATM 3122  O   HOH B 203     -44.250  -1.628 -16.910  1.00  2.00           O  
HETATM 3123  O   HOH B 204     -39.741  -7.183  -8.068  1.00 14.09           O  
HETATM 3124  O   HOH B 205     -45.557   1.833 -28.236  1.00  2.00           O  
HETATM 3125  O   HOH B 206     -38.524   7.864 -32.752  1.00  2.00           O  
HETATM 3126  O   HOH B 207     -29.898   1.118  -9.758  1.00  3.56           O  
HETATM 3127  O   HOH B 208     -43.014   6.793 -44.774  1.00 16.84           O  
HETATM 3128  O   HOH B 209     -36.254   4.682   0.686  1.00  2.00           O  
HETATM 3129  O   HOH B 210     -43.483  13.121  -3.380  1.00  2.00           O  
HETATM 3130  O   HOH B 211     -56.218   6.554  -2.251  1.00 18.26           O  
HETATM 3131  O   HOH B 212     -30.913  -4.663 -13.917  1.00  2.00           O  
HETATM 3132  O   HOH B 213     -33.190  -4.282 -12.177  1.00  3.71           O  
HETATM 3133  O   HOH B 214     -36.513  -2.837 -14.529  1.00 11.05           O  
HETATM 3134  O   HOH B 215     -43.249   4.396 -25.508  1.00  6.15           O  
HETATM 3135  O   HOH B 216     -36.582  11.310 -19.167  1.00  3.58           O  
HETATM 3136  O   HOH B 217     -44.397  11.627 -16.945  1.00  8.97           O  
HETATM 3137  O   HOH B 218     -42.582  -3.527  -4.236  1.00  7.58           O  
HETATM 3138  O   HOH B 219     -45.480   8.732 -28.871  1.00 15.62           O  
HETATM 3139  O   HOH B 220     -36.126   0.846 -35.782  1.00  2.00           O  
HETATM 3140  O   HOH B 221     -50.601  -3.738  -1.901  1.00  9.97           O  
HETATM 3141  O   HOH B 222     -34.602   1.160  -0.336  1.00  6.25           O  
HETATM 3142  O   HOH B 223     -50.272  15.126 -13.251  1.00  4.56           O  
HETATM 3143  O   HOH B 224     -45.115  12.441  -5.531  1.00  2.61           O  
HETATM 3144  O   HOH B 225     -32.162   4.345  -2.170  1.00  2.18           O  
HETATM 3145  O   HOH B 226     -45.734 -11.188 -32.405  1.00  4.86           O  
HETATM 3146  O   HOH B 227     -51.958   8.308 -43.732  1.00  6.33           O  
HETATM 3147  O   HOH B 228     -54.537   1.061  -6.017  1.00  5.57           O  
HETATM 3148  O   HOH B 229     -30.568   8.256  -9.650  1.00  5.49           O  
HETATM 3149  O   HOH B 230     -35.223   5.793 -32.211  1.00  6.89           O  
HETATM 3150  O   HOH B 231     -60.295  -7.009 -32.797  1.00  6.86           O  
HETATM 3151  O   HOH B 232     -59.674  -8.749 -30.412  1.00 17.46           O  
HETATM 3152  O   HOH B 233     -33.045  11.925 -12.519  1.00 20.99           O  
HETATM 3153  O   HOH B 234     -32.483   6.847 -24.843  1.00 11.07           O  
HETATM 3154  O   HOH B 235     -36.099  -5.598 -39.713  1.00 19.12           O  
HETATM 3155  O   HOH B 236     -39.302  -5.605 -16.549  1.00 14.05           O  
HETATM 3156  O   HOH B 237     -49.960  -2.198 -19.219  1.00 22.45           O  
HETATM 3157  O   HOH B 238     -35.145  10.547  -4.444  1.00 15.12           O  
HETATM 3158  O   HOH B 239     -66.113  -7.587  -7.742  1.00  5.21           O  
HETATM 3159  O   HOH B 240     -53.949   0.530 -14.812  1.00 10.21           O  
HETATM 3160  O   HOH B 241     -44.071   9.161 -21.908  1.00 12.19           O  
HETATM 3161  O   HOH B 242     -49.205  12.965 -39.859  1.00  2.00           O  
HETATM 3162  O   HOH B 243     -45.923  -6.894 -25.680  1.00 11.77           O  
HETATM 3163  O   HOH B 244     -49.549   3.554 -19.257  1.00  9.11           O  
HETATM 3164  O   HOH B 245     -43.081 -16.280 -32.227  1.00  7.64           O  
HETATM 3165  O   HOH B 246     -34.453   8.293 -23.564  1.00 14.67           O  
HETATM 3166  O   HOH B 247     -31.009   7.530  -5.642  1.00 18.61           O  
HETATM 3167  O   HOH B 248     -44.798  -4.672 -24.986  1.00 12.57           O  
HETATM 3168  O   HOH B 249     -49.784   1.318   2.550  1.00  9.61           O  
HETATM 3169  O   HOH B 250     -37.535   3.101   4.045  1.00 24.93           O  
HETATM 3170  O   HOH B 251     -29.161 -16.718 -25.598  1.00  9.05           O  
HETATM 3171  O   HOH B 252     -43.897  -0.588 -47.265  1.00 13.12           O  
HETATM 3172  O   HOH B 253     -50.492   6.013 -25.755  1.00 28.51           O  
HETATM 3173  O   HOH B 254     -52.361   2.981 -26.276  1.00  4.68           O  
HETATM 3174  O   HOH B 255     -52.048  -7.948  -3.534  1.00 21.12           O  
HETATM 3175  O   HOH B 256     -35.466  -4.875 -13.408  1.00 21.91           O  
HETATM 3176  O   HOH B 257     -40.898  13.982 -34.497  1.00  6.19           O  
HETATM 3177  O   HOH B 258     -43.324  14.653 -33.057  1.00 12.25           O  
HETATM 3178  O   HOH B 259     -36.245  -4.308 -19.852  1.00 10.67           O  
HETATM 3179  O   HOH B 260     -28.094   6.638 -27.290  1.00 17.96           O  
HETATM 3180  O   HOH B 261     -52.881   0.621   8.644  1.00 17.05           O  
HETATM 3181  O   HOH B 262     -31.105   4.099 -31.243  1.00 18.78           O  
HETATM 3182  O   HOH B 263     -42.433  13.301 -43.431  1.00  7.46           O  
HETATM 3183  O   HOH B 264     -36.729  -1.236 -37.692  1.00 14.23           O  
HETATM 3184  O   HOH B 265     -49.245  10.685 -43.528  1.00 12.73           O  
HETATM 3185  O   HOH B 266     -33.840   7.088   1.466  1.00 16.13           O  
HETATM 3186  O   HOH B 267     -43.049  -1.692 -19.396  1.00 14.50           O  
HETATM 3187  O   HOH B 268     -35.757  10.205 -25.080  1.00  9.30           O  
HETATM 3188  O   HOH B 269     -49.214   3.699 -21.762  1.00 13.93           O  
HETATM 3189  O   HOH B 270     -52.633  -2.127  -0.376  1.00 19.50           O  
HETATM 3190  O   HOH B 271     -51.476  -1.902   2.198  1.00  8.79           O  
HETATM 3191  O   HOH B 272     -52.931  -2.040   7.428  1.00 11.56           O  
HETATM 3192  O   HOH B 273     -37.530 -10.440 -36.243  1.00  7.29           O  
HETATM 3193  O   HOH B 274     -32.702  10.774 -15.069  1.00 11.72           O  
HETATM 3194  O   HOH B 275     -35.462  11.926 -10.816  1.00 11.20           O  
HETATM 3195  O   HOH B 276     -37.333  10.662 -23.183  1.00 14.97           O  
HETATM 3196  O   HOH C 101     -45.105  -3.318 -22.654  1.00  9.01           O  
HETATM 3197  O   HOH C 102     -40.536   4.702 -26.314  1.00 13.85           O  
HETATM 3198  O   HOH C 103     -33.989   3.724 -31.084  1.00  3.51           O  
HETATM 3199  O   HOH C 104     -34.834  -2.749 -37.247  1.00 18.31           O  
HETATM 3200  O   HOH C 105     -52.814   0.339 -26.273  1.00 10.34           O  
HETATM 3201  O   HOH C 106     -52.012   1.328 -22.251  1.00 21.00           O  
HETATM 3202  O   HOH C 107     -37.136  -6.316 -24.299  1.00 27.05           O  
HETATM 3203  O   HOH C 108     -34.342  -5.643 -22.176  1.00 19.03           O  
HETATM 3204  O   HOH C 109     -39.377  -7.725 -23.234  1.00 15.49           O  
HETATM 3205  O   HOH C 110     -46.215  -3.660 -20.002  1.00 24.14           O  
HETATM 3206  O   HOH C 111     -27.853  -1.949 -26.277  1.00 25.82           O  
HETATM 3207  O   HOH D 201     -25.903   0.580   4.786  1.00  2.00           O  
HETATM 3208  O   HOH D 202     -23.512  -5.592  -6.814  1.00 11.53           O  
HETATM 3209  O   HOH D 203     -19.070   2.709   0.222  1.00  4.77           O  
HETATM 3210  O   HOH D 204     -17.749  -8.786 -18.039  1.00  7.64           O  
HETATM 3211  O   HOH D 205     -12.177  -9.697  -2.028  1.00 11.21           O  
HETATM 3212  O   HOH D 206     -19.842 -10.103  -3.527  1.00  7.13           O  
HETATM 3213  O   HOH D 207     -32.936  -3.206  -0.581  1.00 17.02           O  
HETATM 3214  O   HOH D 208      -2.102  -6.555  -8.059  1.00  9.66           O  
HETATM 3215  O   HOH D 209     -14.320  -3.486  -8.952  1.00 13.83           O  
HETATM 3216  O   HOH D 210      -7.684  -4.871  -6.884  1.00 16.63           O  
HETATM 3217  O   HOH D 211     -14.905  -5.153  -4.255  1.00 15.06           O  
HETATM 3218  O   HOH D 212      -2.956  -5.992 -11.349  1.00 16.82           O  
HETATM 3219  O   HOH D 213      -1.905  -7.878  -3.437  1.00 11.79           O  
HETATM 3220  O   HOH D 214     -26.114  -8.760  -1.919  1.00 11.17           O  
HETATM 3221  O   HOH D 215     -30.332  -3.592  -1.238  1.00 23.57           O  
HETATM 3222  O   HOH D 216      -5.234 -11.946  -8.916  1.00 15.40           O  
HETATM 3223  O   HOH D 217     -25.562  -6.023  10.607  1.00 23.26           O  
HETATM 3224  O   HOH D 218     -16.674  -8.056  -8.803  1.00 20.23           O  
CONECT 2913 2914 2915                                                           
CONECT 2914 2913                                                                
CONECT 2915 2913 2916 2917                                                      
CONECT 2916 2915                                                                
CONECT 2917 2915 2918                                                           
CONECT 2918 2917                                                                
CONECT 2919 2920 2921                                                           
CONECT 2920 2919                                                                
CONECT 2921 2919 2922 2923                                                      
CONECT 2922 2921                                                                
CONECT 2923 2921 2924                                                           
CONECT 2924 2923                                                                
CONECT 2925 2926 2927                                                           
CONECT 2926 2925                                                                
CONECT 2927 2925 2928 2929                                                      
CONECT 2928 2927                                                                
CONECT 2929 2927 2930                                                           
CONECT 2930 2929                                                                
CONECT 2931 2932 2933                                                           
CONECT 2932 2931                                                                
CONECT 2933 2931 2934 2935                                                      
CONECT 2934 2933                                                                
CONECT 2935 2933 2936                                                           
CONECT 2936 2935                                                                
CONECT 2937 2938 2939                                                           
CONECT 2938 2937                                                                
CONECT 2939 2937 2940 2941                                                      
CONECT 2940 2939                                                                
CONECT 2941 2939 2942                                                           
CONECT 2942 2941                                                                
CONECT 2943 2944                                                                
CONECT 2944 2943 2945                                                           
CONECT 2945 2944 2946                                                           
CONECT 2946 2945 2947                                                           
CONECT 2947 2946 2948                                                           
CONECT 2948 2947 2949                                                           
CONECT 2949 2948 2950                                                           
CONECT 2950 2949 2951                                                           
CONECT 2951 2950                                                                
CONECT 2952 2953 2954                                                           
CONECT 2953 2952                                                                
CONECT 2954 2952 2955                                                           
CONECT 2955 2954                                                                
CONECT 2956 2957 2958                                                           
CONECT 2957 2956                                                                
CONECT 2958 2956 2959                                                           
CONECT 2959 2958                                                                
CONECT 2960 2961 2962                                                           
CONECT 2961 2960                                                                
CONECT 2962 2960 2963 2964                                                      
CONECT 2963 2962                                                                
CONECT 2964 2962 2965                                                           
CONECT 2965 2964                                                                
CONECT 2966 2967 2968                                                           
CONECT 2967 2966                                                                
CONECT 2968 2966 2969 2970                                                      
CONECT 2969 2968                                                                
CONECT 2970 2968 2971                                                           
CONECT 2971 2970                                                                
MASTER      485    0   10   11   20    0   18    6 3186    4   59   30          
END

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Related entries of code: 4ed5

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
6gc5	RCSB PDB PDBbind	11aa, >6GC5_2\|Chains... at 100%
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	4ed5
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	RRM1 and RRM2 domain of Human RNA-binding protein (HuR)
Ligand Name	11-mer AU rich RNA
EC.Number	E.C.-.-.-.-
Resolution	2(Å)
Affinity (Kd/Ki/IC50)	Kd=169nM
Release Year	2012
Protein/NA Sequence	Check fasta file
Primary Reference	(2013) Acta Crystallogr.,Sect.D Vol. 69: pp. 373-380

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): Q15717
Entrez Gene ID	NCBI Entrez Gene ID: 1994
ASD	Information of known allosteric effects of PDB entries

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