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Browse entries in the PDBbind-CN Database

HEADER    APOPTOSIS                               02-NOV-09   3KJ1              
TITLE     MCL-1 IN COMPLEX WITH BIM BH3 MUTANT I2DA                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: (UNP 172-322);                                             
COMPND   6 SYNONYM: BCL-2-RELATED PROTEIN EAT/MCL1, MCL1/EAT, BCL-2-LIKE PROTEIN
COMPND   7 3, BCL2-L-3;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: BCL-2-LIKE PROTEIN 11;                                     
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: BH3 REGION OF BIM (UNP 1-21);                              
COMPND  13 SYNONYM: BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL DEATH;         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCL2L3, MCL-1, MCL1;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSV282;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: BCL2L11, BIM;                                                  
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PSV282                                    
KEYWDS    BCL-2, BH3, APOPTOSIS, PROTEIN-PEPTIDE COMPLEX, ALTERNATIVE SPLICING, 
KEYWDS   2 CYTOPLASM, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, ISOPEPTIDE BOND,  
KEYWDS   3 MEMBRANE, MITOCHONDRION, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM,      
KEYWDS   4 TRANSMEMBRANE, UBL CONJUGATION                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.FIRE,R.A.GRANT,A.E.KEATING                                          
REVDAT   3   01-NOV-17 3KJ1    1       REMARK                                   
REVDAT   2   23-MAR-10 3KJ1    1       JRNL                                     
REVDAT   1   16-FEB-10 3KJ1    0                                                
JRNL        AUTH   E.FIRE,S.V.GULLA,R.A.GRANT,A.E.KEATING                       
JRNL        TITL   MCL-1-BIM COMPLEXES ACCOMMODATE SURPRISING POINT MUTATIONS   
JRNL        TITL 2 VIA MINOR STRUCTURAL CHANGES.                                
JRNL        REF    PROTEIN SCI.                  V.  19   507 2010              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   20066663                                                     
JRNL        DOI    10.1002/PRO.329                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.940                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 51.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 16418                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 831                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.8880 -  3.5320    0.55     2829   127  0.1800 0.1940        
REMARK   3     2  3.5320 -  2.8040    0.53     2684   156  0.1860 0.2070        
REMARK   3     3  2.8040 -  2.4500    0.52     2645   145  0.1870 0.2340        
REMARK   3     4  2.4500 -  2.2260    0.52     2614   141  0.1760 0.2090        
REMARK   3     5  2.2260 -  2.0660    0.51     2585   145  0.1720 0.2140        
REMARK   3     6  2.0660 -  1.9450    0.44     2230   117  0.1970 0.2270        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 66.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.85300                                             
REMARK   3    B22 (A**2) : -2.42900                                             
REMARK   3    B33 (A**2) : 4.28100                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           1454                                  
REMARK   3   ANGLE     :  0.995           1954                                  
REMARK   3   CHIRALITY :  0.071            211                                  
REMARK   3   PLANARITY :  0.004            253                                  
REMARK   3   DIHEDRAL  : 14.976            543                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2443  20.6557  41.4334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0947 T22:   0.0354                                     
REMARK   3      T33:   0.1081 T12:  -0.0060                                     
REMARK   3      T13:   0.0108 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5129 L22:   0.3758                                     
REMARK   3      L33:   0.9476 L12:  -0.0212                                     
REMARK   3      L13:   0.6064 L23:   0.1943                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0641 S12:  -0.0340 S13:  -0.1712                       
REMARK   3      S21:   0.0846 S22:   0.0050 S23:   0.0425                       
REMARK   3      S31:   0.1326 S32:   0.0161 S33:  -0.0745                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KJ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : VARIMAXHR                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16418                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 10.20                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 0.2 M ZINC ACETATE,     
REMARK 280  16% PEG 400, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       26.53300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.00350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.92250            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       26.53300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.00350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.92250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       26.53300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       36.00350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.92250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       26.53300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       36.00350            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       58.92250            
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: 2600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8990 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -636.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       72.00700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      117.84500            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       72.00700            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      117.84500            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 328  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A   6  LIES ON A SPECIAL POSITION.                          
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     GLY A   170                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY A   327                                                      
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   OE1  GLU A   240     O    HOH A     9              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A   288     O    HOH A     9     3556     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 286   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 202     -109.17     75.44                                   
REMARK 500    ASN A 223      -21.88     87.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 313   OD1                                                    
REMARK 620 2 GLU A 317   OE2 108.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B  23  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B   9   OE1                                                    
REMARK 620 2 HOH B  24   O    93.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1428                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 328                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 23                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KJ0   RELATED DB: PDB                                   
REMARK 900 MCL-1 IN COMPLEX WITH BIM BH3 MUTANT I2DY                            
REMARK 900 RELATED ID: 3KJ2   RELATED DB: PDB                                   
REMARK 900 MCL-1 IN COMPLEX WITH BIM BH3 MUTANT F4AE                            
REMARK 900 RELATED ID: 2PQK   RELATED DB: PDB                                   
REMARK 900 HUMAN MCL-1 IN COMPLEX WITH WILD-TYPE BIM BH3                        
DBREF  3KJ1 A  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  3KJ1 B    1    21  UNP    O43521   B2L11_HUMAN    143    163             
SEQADV 3KJ1 GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3KJ1 SER A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 3KJ1 ALA B    6  UNP  O43521    ILE   148 ENGINEERED                     
SEQADV 3KJ1 ARG B   22  UNP  O43521              EXPRESSION TAG                 
SEQRES   1 A  158  GLY SER ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 A  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 A  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 A  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 A  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 A  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 A  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 A  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 A  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 A  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 A  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 A  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 A  158  GLY GLY                                                      
SEQRES   1 B   22  ARG PRO GLU ILE TRP ALA ALA GLN GLU LEU ARG ARG ILE          
SEQRES   2 B   22  GLY ASP GLU PHE ASN ALA TYR TYR ARG                          
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HET     ZN  A   5       1                                                       
HET    ACT  A1428       4                                                       
HET     CL  A 328       1                                                       
HET     ZN  B  23       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   ZN    5(ZN 2+)                                                     
FORMUL   7  ACT    C2 H3 O2 1-                                                  
FORMUL   8   CL    CL 1-                                                        
FORMUL  10  HOH   *116(H2 O)                                                    
HELIX    1   1 ASP A  172  GLY A  192  1                                  21    
HELIX    2   2 GLY A  203  ARG A  222  1                                  20    
HELIX    3   3 HIS A  224  ASP A  236  1                                  13    
HELIX    4   4 VAL A  243  PHE A  254  1                                  12    
HELIX    5   5 SER A  255  GLY A  257  5                                   3    
HELIX    6   6 ASN A  260  ASN A  282  1                                  23    
HELIX    7   7 ILE A  287  LYS A  302  1                                  16    
HELIX    8   8 LYS A  302  GLN A  309  1                                   8    
HELIX    9   9 GLY A  311  PHE A  319  1                                   9    
HELIX   10  10 ARG B    1  ARG B   22  1                                  22    
SSBOND   1 CYS A  286    CYS A  286                          1555   3556  2.04  
LINK         ND1 HIS A 277                ZN    ZN A   5     1555   1555  2.39  
LINK         OE2 GLU A 292                ZN    ZN A   2     1555   1555  2.33  
LINK         OD1 ASP A 313                ZN    ZN A   3     1555   1555  2.04  
LINK         OE2 GLU A 317                ZN    ZN A   3     1555   1555  2.01  
LINK         OE1 GLU B   9                ZN    ZN B  23     1555   1555  2.04  
LINK        ZN    ZN A   1                 OXT ACT A1428     1555   1555  1.83  
LINK         SG  CYS A 286                 SG  CYS A 286     1555   3556  2.04  
LINK        ZN    ZN B  23                 O   HOH B  24     1555   1555  2.42  
SITE     1 AC1  4 HIS A 252  ASP A 304  HOH A 329  ACT A1428                    
SITE     1 AC2  3 GLU A 240  ASP A 241  GLU A 292                               
SITE     1 AC3  4 HIS A 224  ASP A 313  GLU A 317  GLU B  16                    
SITE     1 AC4  2 GLN A 229  HIS A 277                                          
SITE     1 AC5  6  ZN A   1  HOH A 111  HIS A 252  ASP A 304                    
SITE     2 AC5  6 GLN B   8  ARG B  11                                          
SITE     1 AC6  1 ARG A 300                                                     
SITE     1 AC7  4 HIS A 320  GLU A 322  GLU B   9  HOH B  24                    
CRYST1   53.066   72.007  117.845  90.00  90.00  90.00 I 2 2 2       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      0.018844  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013888  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008486        0.00000                         
ATOM      1  N   SER A 171     -17.491  26.323  50.162  1.00 74.65           N  
ANISOU    1  N   SER A 171     8738  10276   9349   -317    685   -227       N  
ATOM      2  CA  SER A 171     -17.579  25.291  49.132  1.00 72.10           C  
ANISOU    2  CA  SER A 171     8449   9848   9098   -381    664   -151       C  
ATOM      3  C   SER A 171     -16.783  25.655  47.884  1.00 69.15           C  
ANISOU    3  C   SER A 171     8155   9313   8808   -329    608   -175       C  
ATOM      4  O   SER A 171     -17.184  26.528  47.114  1.00 73.80           O  
ANISOU    4  O   SER A 171     8726   9875   9440   -266    584   -250       O  
ATOM      5  CB  SER A 171     -19.031  25.049  48.736  1.00 68.87           C  
ANISOU    5  CB  SER A 171     7952   9509   8707   -414    683   -166       C  
ATOM      6  OG  SER A 171     -19.087  24.254  47.567  1.00 67.99           O  
ANISOU    6  OG  SER A 171     7875   9280   8677   -456    650   -120       O  
ATOM      7  N   ASP A 172     -15.669  24.962  47.676  1.00 58.76           N  
ANISOU    7  N   ASP A 172     6921   7894   7512   -356    584   -107       N  
ATOM      8  CA  ASP A 172     -14.750  25.289  46.591  1.00 43.05           C  
ANISOU    8  CA  ASP A 172     5003   5769   5584   -311    535   -125       C  
ATOM      9  C   ASP A 172     -14.255  24.002  45.938  1.00 38.62           C  
ANISOU    9  C   ASP A 172     4495   5110   5067   -369    511    -47       C  
ATOM     10  O   ASP A 172     -13.216  23.464  46.326  1.00 36.52           O  
ANISOU   10  O   ASP A 172     4286   4801   4788   -386    502      4       O  
ATOM     11  CB  ASP A 172     -13.580  26.072  47.163  1.00 40.19           C  
ANISOU   11  CB  ASP A 172     4689   5390   5192   -258    525   -150       C  
ATOM     12  CG  ASP A 172     -12.686  26.662  46.093  1.00 37.18           C  
ANISOU   12  CG  ASP A 172     4367   4892   4867   -208    477   -176       C  
ATOM     13  OD1 ASP A 172     -12.798  26.260  44.909  1.00 34.44           O  
ANISOU   13  OD1 ASP A 172     4036   4475   4576   -219    452   -161       O  
ATOM     14  OD2 ASP A 172     -11.856  27.518  46.461  1.00 41.35           O  
ANISOU   14  OD2 ASP A 172     4924   5406   5381   -161    464   -210       O  
ATOM     15  N   GLU A 173     -14.998  23.510  44.952  1.00 36.44           N  
ANISOU   15  N   GLU A 173     4198   4802   4846   -395    496    -45       N  
ATOM     16  CA  GLU A 173     -14.705  22.199  44.370  1.00 40.08           C  
ANISOU   16  CA  GLU A 173     4697   5176   5355   -452    469     17       C  
ATOM     17  C   GLU A 173     -13.357  22.170  43.629  1.00 38.84           C  
ANISOU   17  C   GLU A 173     4619   4909   5229   -413    427     15       C  
ATOM     18  O   GLU A 173     -12.626  21.181  43.696  1.00 34.31           O  
ANISOU   18  O   GLU A 173     4092   4272   4670   -446    406     68       O  
ATOM     19  CB  GLU A 173     -15.862  21.732  43.476  1.00 40.52           C  
ANISOU   19  CB  GLU A 173     4704   5229   5461   -485    460      6       C  
ATOM     20  CG  GLU A 173     -15.594  20.444  42.690  1.00 45.99           C  
ANISOU   20  CG  GLU A 173     5434   5821   6218   -534    420     48       C  
ATOM     21  CD  GLU A 173     -15.347  19.215  43.569  1.00 50.86           C  
ANISOU   21  CD  GLU A 173     6072   6421   6831   -614    422    140       C  
ATOM     22  OE1 GLU A 173     -15.561  19.269  44.799  1.00 52.39           O  
ANISOU   22  OE1 GLU A 173     6240   6701   6965   -646    463    182       O  
ATOM     23  OE2 GLU A 173     -14.933  18.179  43.014  1.00 52.70           O  
ANISOU   23  OE2 GLU A 173     6346   6555   7123   -644    379    170       O  
ATOM     24  N   LEU A 174     -13.011  23.261  42.950  1.00 35.73           N  
ANISOU   24  N   LEU A 174     4238   4494   4844   -344    410    -45       N  
ATOM     25  CA  LEU A 174     -11.750  23.297  42.218  1.00 31.25           C  
ANISOU   25  CA  LEU A 174     3734   3842   4297   -311    373    -48       C  
ATOM     26  C   LEU A 174     -10.583  23.175  43.185  1.00 28.85           C  
ANISOU   26  C   LEU A 174     3476   3530   3956   -310    378    -14       C  
ATOM     27  O   LEU A 174      -9.614  22.458  42.930  1.00 33.02           O  
ANISOU   27  O   LEU A 174     4052   3994   4501   -317    353     14       O  
ATOM     28  CB  LEU A 174     -11.624  24.585  41.398  1.00 31.80           C  
ANISOU   28  CB  LEU A 174     3803   3901   4377   -246    354   -104       C  
ATOM     29  CG  LEU A 174     -10.311  24.703  40.614  1.00 29.89           C  
ANISOU   29  CG  LEU A 174     3617   3590   4148   -218    320   -103       C  
ATOM     30  CD1 LEU A 174     -10.097  23.513  39.649  1.00 29.91           C  
ANISOU   30  CD1 LEU A 174     3638   3541   4187   -243    293    -86       C  
ATOM     31  CD2 LEU A 174     -10.265  26.030  39.879  1.00 28.52           C  
ANISOU   31  CD2 LEU A 174     3440   3412   3984   -165    301   -143       C  
ATOM     32  N   TYR A 175     -10.674  23.887  44.300  1.00 28.93           N  
ANISOU   32  N   TYR A 175     3467   3611   3915   -297    409    -26       N  
ATOM     33  CA  TYR A 175      -9.633  23.827  45.305  1.00 28.29           C  
ANISOU   33  CA  TYR A 175     3423   3536   3790   -295    414      2       C  
ATOM     34  C   TYR A 175      -9.574  22.427  45.911  1.00 31.04           C  
ANISOU   34  C   TYR A 175     3785   3879   4130   -360    417     83       C  
ATOM     35  O   TYR A 175      -8.496  21.855  46.039  1.00 32.16           O  
ANISOU   35  O   TYR A 175     3978   3967   4274   -362    394    119       O  
ATOM     36  CB  TYR A 175      -9.844  24.874  46.413  1.00 30.88           C  
ANISOU   36  CB  TYR A 175     3719   3955   4059   -265    444    -37       C  
ATOM     37  CG  TYR A 175      -8.692  24.887  47.393  1.00 36.19           C  
ANISOU   37  CG  TYR A 175     4430   4636   4684   -257    443    -16       C  
ATOM     38  CD1 TYR A 175      -7.638  25.782  47.253  1.00 40.27           C  
ANISOU   38  CD1 TYR A 175     4981   5114   5205   -205    420    -57       C  
ATOM     39  CD2 TYR A 175      -8.642  23.978  48.436  1.00 41.51           C  
ANISOU   39  CD2 TYR A 175     5105   5356   5310   -306    462     51       C  
ATOM     40  CE1 TYR A 175      -6.571  25.776  48.141  1.00 42.23           C  
ANISOU   40  CE1 TYR A 175     5260   5373   5411   -198    416    -41       C  
ATOM     41  CE2 TYR A 175      -7.588  23.964  49.322  1.00 47.19           C  
ANISOU   41  CE2 TYR A 175     5858   6087   5983   -296    458     72       C  
ATOM     42  CZ  TYR A 175      -6.554  24.858  49.169  1.00 48.35           C  
ANISOU   42  CZ  TYR A 175     6036   6198   6136   -240    435     21       C  
ATOM     43  OH  TYR A 175      -5.508  24.826  50.062  1.00 58.89           O  
ANISOU   43  OH  TYR A 175     7401   7550   7424   -231    428     38       O  
ATOM     44  N   ARG A 176     -10.737  21.901  46.304  1.00 33.28           N  
ANISOU   44  N   ARG A 176     4020   4221   4405   -414    443    113       N  
ATOM     45  CA  ARG A 176     -10.824  20.556  46.895  1.00 34.80           C  
ANISOU   45  CA  ARG A 176     4221   4406   4596   -490    442    204       C  
ATOM     46  C   ARG A 176     -10.203  19.508  45.970  1.00 31.10           C  
ANISOU   46  C   ARG A 176     3804   3812   4201   -503    390    231       C  
ATOM     47  O   ARG A 176      -9.349  18.720  46.382  1.00 34.52           O  
ANISOU   47  O   ARG A 176     4284   4195   4637   -520    365    287       O  
ATOM     48  CB  ARG A 176     -12.284  20.183  47.184  1.00 37.36           C  
ANISOU   48  CB  ARG A 176     4475   4808   4912   -554    475    230       C  
ATOM     49  CG  ARG A 176     -12.440  18.869  47.972  1.00 39.24           C  
ANISOU   49  CG  ARG A 176     4716   5051   5141   -646    475    341       C  
ATOM     50  CD  ARG A 176     -13.742  18.122  47.629  1.00 39.15           C  
ANISOU   50  CD  ARG A 176     4650   5053   5171   -723    481    373       C  
ATOM     51  NE  ARG A 176     -13.783  17.747  46.217  1.00 45.45           N  
ANISOU   51  NE  ARG A 176     5469   5738   6064   -710    435    335       N  
ATOM     52  CZ  ARG A 176     -13.084  16.749  45.678  1.00 46.39           C  
ANISOU   52  CZ  ARG A 176     5646   5730   6249   -725    379    368       C  
ATOM     53  NH1 ARG A 176     -13.188  16.491  44.383  1.00 43.66           N  
ANISOU   53  NH1 ARG A 176     5308   5302   5978   -707    340    317       N  
ATOM     54  NH2 ARG A 176     -12.280  16.006  46.426  1.00 48.31           N  
ANISOU   54  NH2 ARG A 176     5938   5933   6483   -753    359    446       N  
ATOM     55  N   GLN A 177     -10.633  19.516  44.712  1.00 32.13           N  
ANISOU   55  N   GLN A 177     3924   3895   4390   -490    370    185       N  
ATOM     56  CA  GLN A 177     -10.097  18.607  43.703  1.00 32.60           C  
ANISOU   56  CA  GLN A 177     4022   3846   4518   -491    317    187       C  
ATOM     57  C   GLN A 177      -8.575  18.742  43.496  1.00 29.02           C  
ANISOU   57  C   GLN A 177     3628   3336   4061   -436    288    170       C  
ATOM     58  O   GLN A 177      -7.845  17.737  43.466  1.00 29.30           O  
ANISOU   58  O   GLN A 177     3704   3299   4130   -447    248    203       O  
ATOM     59  CB  GLN A 177     -10.839  18.775  42.374  1.00 33.04           C  
ANISOU   59  CB  GLN A 177     4047   3884   4621   -478    303    128       C  
ATOM     60  CG  GLN A 177     -10.463  17.710  41.360  1.00 36.85           C  
ANISOU   60  CG  GLN A 177     4559   4268   5174   -483    248    121       C  
ATOM     61  CD  GLN A 177     -11.006  17.983  39.975  1.00 37.11           C  
ANISOU   61  CD  GLN A 177     4565   4295   5241   -457    230     53       C  
ATOM     62  OE1 GLN A 177     -11.248  19.131  39.598  1.00 35.66           O  
ANISOU   62  OE1 GLN A 177     4358   4162   5028   -415    251      9       O  
ATOM     63  NE2 GLN A 177     -11.175  16.923  39.196  1.00 36.18           N  
ANISOU   63  NE2 GLN A 177     4450   4111   5187   -480    186     43       N  
ATOM     64  N   SER A 178      -8.101  19.980  43.365  1.00 24.54           N  
ANISOU   64  N   SER A 178     3062   2802   3459   -378    303    120       N  
ATOM     65  CA  SER A 178      -6.685  20.250  43.165  1.00 25.07           C  
ANISOU   65  CA  SER A 178     3174   2834   3519   -329    279    102       C  
ATOM     66  C   SER A 178      -5.846  19.754  44.329  1.00 25.99           C  
ANISOU   66  C   SER A 178     3324   2946   3603   -341    276    155       C  
ATOM     67  O   SER A 178      -4.788  19.168  44.130  1.00 25.96           O  
ANISOU   67  O   SER A 178     3360   2886   3619   -324    240    163       O  
ATOM     68  CB  SER A 178      -6.429  21.757  42.949  1.00 24.80           C  
ANISOU   68  CB  SER A 178     3129   2837   3454   -277    295     48       C  
ATOM     69  OG  SER A 178      -7.147  22.212  41.805  1.00 26.74           O  
ANISOU   69  OG  SER A 178     3347   3082   3730   -263    290      6       O  
ATOM     70  N   LEU A 179      -6.318  20.007  45.544  1.00 28.36           N  
ANISOU   70  N   LEU A 179     3605   3320   3852   -367    312    188       N  
ATOM     71  CA  LEU A 179      -5.605  19.588  46.743  1.00 30.10           C  
ANISOU   71  CA  LEU A 179     3852   3554   4029   -380    310    245       C  
ATOM     72  C   LEU A 179      -5.574  18.056  46.829  1.00 29.57           C  
ANISOU   72  C   LEU A 179     3811   3418   4005   -431    274    320       C  
ATOM     73  O   LEU A 179      -4.586  17.474  47.238  1.00 30.66           O  
ANISOU   73  O   LEU A 179     3991   3516   4143   -423    242    357       O  
ATOM     74  CB  LEU A 179      -6.246  20.189  48.002  1.00 30.30           C  
ANISOU   74  CB  LEU A 179     3841   3693   3979   -398    359    261       C  
ATOM     75  CG  LEU A 179      -5.572  19.913  49.353  1.00 32.80           C  
ANISOU   75  CG  LEU A 179     4179   4053   4231   -410    362    319       C  
ATOM     76  CD1 LEU A 179      -4.166  20.516  49.404  1.00 30.30           C  
ANISOU   76  CD1 LEU A 179     3900   3714   3899   -349    341    279       C  
ATOM     77  CD2 LEU A 179      -6.420  20.435  50.502  1.00 33.70           C  
ANISOU   77  CD2 LEU A 179     4241   4300   4265   -433    414    327       C  
ATOM     78  N   GLU A 180      -6.653  17.413  46.415  1.00 29.72           N  
ANISOU   78  N   GLU A 180     3804   3419   4068   -481    272    341       N  
ATOM     79  CA  GLU A 180      -6.708  15.954  46.472  1.00 31.54           C  
ANISOU   79  CA  GLU A 180     4059   3571   4355   -536    228    413       C  
ATOM     80  C   GLU A 180      -5.691  15.350  45.501  1.00 29.18           C  
ANISOU   80  C   GLU A 180     3805   3160   4124   -491    165    376       C  
ATOM     81  O   GLU A 180      -4.906  14.472  45.875  1.00 31.53           O  
ANISOU   81  O   GLU A 180     4144   3391   4444   -493    120    423       O  
ATOM     82  CB  GLU A 180      -8.122  15.472  46.156  1.00 33.51           C  
ANISOU   82  CB  GLU A 180     4264   3826   4644   -603    238    433       C  
ATOM     83  CG  GLU A 180      -8.297  13.967  46.194  1.00 36.89           C  
ANISOU   83  CG  GLU A 180     4713   4161   5144   -670    186    511       C  
ATOM     84  CD  GLU A 180      -9.744  13.558  46.040  1.00 48.96           C  
ANISOU   84  CD  GLU A 180     6188   5710   6703   -748    201    538       C  
ATOM     85  OE1 GLU A 180     -10.463  14.195  45.246  1.00 56.63           O  
ANISOU   85  OE1 GLU A 180     7117   6717   7681   -729    225    464       O  
ATOM     86  OE2 GLU A 180     -10.168  12.600  46.716  1.00 60.42           O  
ANISOU   86  OE2 GLU A 180     7639   7145   8174   -833    185    639       O  
ATOM     87  N   ILE A 181      -5.694  15.854  44.265  1.00 26.16           N  
ANISOU   87  N   ILE A 181     3409   2763   3768   -446    162    291       N  
ATOM     88  CA  ILE A 181      -4.774  15.389  43.230  1.00 29.78           C  
ANISOU   88  CA  ILE A 181     3896   3142   4279   -397    108    239       C  
ATOM     89  C   ILE A 181      -3.313  15.573  43.662  1.00 30.57           C  
ANISOU   89  C   ILE A 181     4033   3237   4346   -346     92    237       C  
ATOM     90  O   ILE A 181      -2.519  14.631  43.632  1.00 25.95           O  
ANISOU   90  O   ILE A 181     3482   2578   3801   -331     38    248       O  
ATOM     91  CB  ILE A 181      -5.039  16.109  41.878  1.00 28.65           C  
ANISOU   91  CB  ILE A 181     3724   3016   4145   -358    116    152       C  
ATOM     92  CG1 ILE A 181      -6.355  15.624  41.258  1.00 28.67           C  
ANISOU   92  CG1 ILE A 181     3692   3004   4198   -403    111    145       C  
ATOM     93  CG2 ILE A 181      -3.867  15.911  40.901  1.00 33.70           C  
ANISOU   93  CG2 ILE A 181     4385   3613   4807   -296     72     90       C  
ATOM     94  CD1 ILE A 181      -6.893  16.563  40.151  1.00 27.27           C  
ANISOU   94  CD1 ILE A 181     3477   2873   4011   -372    131     74       C  
ATOM     95  N   ILE A 182      -2.965  16.796  44.058  1.00 26.93           N  
ANISOU   95  N   ILE A 182     3564   2852   3817   -317    135    217       N  
ATOM     96  CA  ILE A 182      -1.591  17.130  44.447  1.00 23.36           C  
ANISOU   96  CA  ILE A 182     3139   2407   3330   -270    124    207       C  
ATOM     97  C   ILE A 182      -1.140  16.394  45.705  1.00 29.09           C  
ANISOU   97  C   ILE A 182     3895   3119   4039   -291    105    284       C  
ATOM     98  O   ILE A 182      -0.008  15.905  45.763  1.00 26.68           O  
ANISOU   98  O   ILE A 182     3621   2771   3746   -256     62    283       O  
ATOM     99  CB  ILE A 182      -1.426  18.685  44.586  1.00 23.88           C  
ANISOU   99  CB  ILE A 182     3185   2552   3335   -241    170    166       C  
ATOM    100  CG1 ILE A 182      -1.563  19.330  43.202  1.00 26.07           C  
ANISOU  100  CG1 ILE A 182     3441   2830   3636   -213    171     98       C  
ATOM    101  CG2 ILE A 182      -0.087  19.094  45.279  1.00 23.12           C  
ANISOU  101  CG2 ILE A 182     3112   2477   3196   -205    163    165       C  
ATOM    102  CD1 ILE A 182      -1.738  20.870  43.229  1.00 29.64           C  
ANISOU  102  CD1 ILE A 182     3871   3345   4048   -196    209     65       C  
ATOM    103  N   SER A 183      -2.026  16.282  46.692  1.00 30.01           N  
ANISOU  103  N   SER A 183     4000   3278   4124   -347    134    351       N  
ATOM    104  CA  SER A 183      -1.707  15.569  47.943  1.00 30.17           C  
ANISOU  104  CA  SER A 183     4046   3298   4118   -377    117    441       C  
ATOM    105  C   SER A 183      -1.462  14.089  47.704  1.00 31.97           C  
ANISOU  105  C   SER A 183     4309   3412   4426   -395     46    489       C  
ATOM    106  O   SER A 183      -0.538  13.495  48.263  1.00 28.24           O  
ANISOU  106  O   SER A 183     3874   2900   3956   -378      2    530       O  
ATOM    107  CB  SER A 183      -2.850  15.697  48.964  1.00 32.41           C  
ANISOU  107  CB  SER A 183     4299   3668   4348   -444    166    508       C  
ATOM    108  OG  SER A 183      -3.093  17.054  49.285  1.00 33.71           O  
ANISOU  108  OG  SER A 183     4429   3938   4441   -421    224    456       O  
ATOM    109  N   ARG A 184      -2.327  13.491  46.897  1.00 28.48           N  
ANISOU  109  N   ARG A 184     3854   2913   4054   -429     30    481       N  
ATOM    110  CA  ARG A 184      -2.174  12.087  46.558  1.00 32.35           C  
ANISOU  110  CA  ARG A 184     4375   3279   4637   -444    -47    512       C  
ATOM    111  C   ARG A 184      -0.857  11.834  45.854  1.00 33.77           C  
ANISOU  111  C   ARG A 184     4582   3393   4855   -361   -103    441       C  
ATOM    112  O   ARG A 184      -0.158  10.869  46.182  1.00 30.99           O  
ANISOU  112  O   ARG A 184     4269   2960   4546   -350   -170    479       O  
ATOM    113  CB  ARG A 184      -3.346  11.598  45.716  1.00 29.72           C  
ANISOU  113  CB  ARG A 184     4015   2901   4374   -491    -55    498       C  
ATOM    114  CG  ARG A 184      -4.595  11.431  46.540  1.00 33.08           C  
ANISOU  114  CG  ARG A 184     4415   3376   4779   -586    -19    591       C  
ATOM    115  CD  ARG A 184      -5.424  10.261  46.055  1.00 40.40           C  
ANISOU  115  CD  ARG A 184     5338   4204   5807   -650    -69    624       C  
ATOM    116  NE  ARG A 184      -6.625  10.127  46.864  1.00 45.37           N  
ANISOU  116  NE  ARG A 184     5933   4896   6410   -750    -29    719       N  
ATOM    117  CZ  ARG A 184      -7.456   9.094  46.808  1.00 46.22           C  
ANISOU  117  CZ  ARG A 184     6033   4934   6593   -834    -67    784       C  
ATOM    118  NH1 ARG A 184      -7.219   8.092  45.971  1.00 45.95           N  
ANISOU  118  NH1 ARG A 184     6029   4755   6676   -825   -152    755       N  
ATOM    119  NH2 ARG A 184      -8.520   9.071  47.592  1.00 45.06           N  
ANISOU  119  NH2 ARG A 184     5845   4868   6407   -929    -22    874       N  
ATOM    120  N   TYR A 185      -0.503  12.698  44.898  1.00 27.67           N  
ANISOU  120  N   TYR A 185     3788   2659   4065   -304    -79    340       N  
ATOM    121  CA  TYR A 185       0.766  12.522  44.203  1.00 28.08           C  
ANISOU  121  CA  TYR A 185     3854   2674   4140   -226   -125    267       C  
ATOM    122  C   TYR A 185       1.939  12.648  45.177  1.00 27.52           C  
ANISOU  122  C   TYR A 185     3810   2624   4023   -194   -136    299       C  
ATOM    123  O   TYR A 185       2.804  11.782  45.228  1.00 30.00           O  
ANISOU  123  O   TYR A 185     4151   2868   4379   -158   -203    300       O  
ATOM    124  CB  TYR A 185       0.922  13.513  43.048  1.00 26.24           C  
ANISOU  124  CB  TYR A 185     3587   2500   3883   -181    -92    167       C  
ATOM    125  CG  TYR A 185       2.227  13.352  42.285  1.00 30.48           C  
ANISOU  125  CG  TYR A 185     4126   3022   4434   -105   -134     90       C  
ATOM    126  CD1 TYR A 185       2.548  12.142  41.682  1.00 30.21           C  
ANISOU  126  CD1 TYR A 185     4103   2899   4478    -76   -208     53       C  
ATOM    127  CD2 TYR A 185       3.127  14.417  42.147  1.00 32.27           C  
ANISOU  127  CD2 TYR A 185     4338   3328   4597    -63   -102     47       C  
ATOM    128  CE1 TYR A 185       3.731  11.980  40.988  1.00 33.81           C  
ANISOU  128  CE1 TYR A 185     4550   3356   4941      0   -246    -28       C  
ATOM    129  CE2 TYR A 185       4.323  14.256  41.442  1.00 31.06           C  
ANISOU  129  CE2 TYR A 185     4175   3177   4449      3   -137    -23       C  
ATOM    130  CZ  TYR A 185       4.607  13.042  40.860  1.00 35.18           C  
ANISOU  130  CZ  TYR A 185     4702   3622   5041     37   -206    -64       C  
ATOM    131  OH  TYR A 185       5.775  12.856  40.152  1.00 39.42           O  
ANISOU  131  OH  TYR A 185     5221   4176   5579    107   -242   -145       O  
ATOM    132  N   LEU A 186       1.972  13.740  45.938  1.00 29.51           N  
ANISOU  132  N   LEU A 186     4051   2973   4189   -201    -76    317       N  
ATOM    133  CA  LEU A 186       3.037  13.956  46.913  1.00 30.41           C  
ANISOU  133  CA  LEU A 186     4185   3120   4250   -173    -83    344       C  
ATOM    134  C   LEU A 186       3.151  12.804  47.934  1.00 34.44           C  
ANISOU  134  C   LEU A 186     4733   3572   4779   -201   -135    444       C  
ATOM    135  O   LEU A 186       4.253  12.372  48.275  1.00 31.37           O  
ANISOU  135  O   LEU A 186     4370   3154   4397   -157   -185    451       O  
ATOM    136  CB  LEU A 186       2.855  15.304  47.624  1.00 28.06           C  
ANISOU  136  CB  LEU A 186     3866   2934   3862   -184    -12    344       C  
ATOM    137  CG  LEU A 186       3.638  16.500  47.056  1.00 28.30           C  
ANISOU  137  CG  LEU A 186     3875   3017   3859   -132     13    258       C  
ATOM    138  CD1 LEU A 186       3.476  16.622  45.558  1.00 30.06           C  
ANISOU  138  CD1 LEU A 186     4078   3216   4129   -112     10    185       C  
ATOM    139  CD2 LEU A 186       3.265  17.827  47.771  1.00 32.46           C  
ANISOU  139  CD2 LEU A 186     4381   3640   4312   -147     75    254       C  
ATOM    140  N   ARG A 187       2.018  12.304  48.415  1.00 33.31           N  
ANISOU  140  N   ARG A 187     4592   3417   4649   -276   -126    527       N  
ATOM    141  CA  ARG A 187       2.046  11.223  49.384  1.00 34.32           C  
ANISOU  141  CA  ARG A 187     4755   3491   4794   -316   -177    641       C  
ATOM    142  C   ARG A 187       2.566   9.906  48.792  1.00 35.25           C  
ANISOU  142  C   ARG A 187     4907   3463   5023   -288   -276    636       C  
ATOM    143  O   ARG A 187       3.345   9.204  49.441  1.00 36.61           O  
ANISOU  143  O   ARG A 187     5116   3585   5210   -269   -339    692       O  
ATOM    144  CB  ARG A 187       0.671  11.031  50.016  1.00 40.50           C  
ANISOU  144  CB  ARG A 187     5522   4308   5558   -413   -140    736       C  
ATOM    145  CG  ARG A 187       0.691  10.117  51.227  1.00 45.72           C  
ANISOU  145  CG  ARG A 187     6215   4948   6210   -467   -181    877       C  
ATOM    146  CD  ARG A 187      -0.673  10.061  51.903  1.00 52.96           C  
ANISOU  146  CD  ARG A 187     7102   5932   7087   -571   -132    973       C  
ATOM    147  NE  ARG A 187      -0.980  11.280  52.648  1.00 57.71           N  
ANISOU  147  NE  ARG A 187     7664   6700   7564   -575    -43    961       N  
ATOM    148  CZ  ARG A 187      -1.873  12.192  52.268  1.00 58.43           C  
ANISOU  148  CZ  ARG A 187     7704   6872   7624   -586     29    897       C  
ATOM    149  NH1 ARG A 187      -2.563  12.034  51.143  1.00 59.59           N  
ANISOU  149  NH1 ARG A 187     7834   6957   7850   -597     27    844       N  
ATOM    150  NH2 ARG A 187      -2.082  13.266  53.019  1.00 54.39           N  
ANISOU  150  NH2 ARG A 187     7158   6505   7005   -581     99    879       N  
ATOM    151  N   GLU A 188       2.143   9.581  47.568  1.00 34.66           N  
ANISOU  151  N   GLU A 188     4819   3324   5028   -280   -295    564       N  
ATOM    152  CA  GLU A 188       2.629   8.388  46.862  1.00 37.55           C  
ANISOU  152  CA  GLU A 188     5210   3552   5506   -240   -394    529       C  
ATOM    153  C   GLU A 188       4.133   8.465  46.680  1.00 38.87           C  
ANISOU  153  C   GLU A 188     5387   3718   5665   -141   -432    457       C  
ATOM    154  O   GLU A 188       4.867   7.509  46.950  1.00 39.38           O  
ANISOU  154  O   GLU A 188     5485   3691   5786   -107   -519    480       O  
ATOM    155  CB  GLU A 188       2.034   8.296  45.458  1.00 37.38           C  
ANISOU  155  CB  GLU A 188     5159   3495   5548   -232   -397    431       C  
ATOM    156  CG  GLU A 188       0.613   7.879  45.362  1.00 44.85           C  
ANISOU  156  CG  GLU A 188     6094   4407   6539   -320   -388    483       C  
ATOM    157  CD  GLU A 188       0.197   7.645  43.920  1.00 48.54           C  
ANISOU  157  CD  GLU A 188     6535   4829   7078   -298   -410    374       C  
ATOM    158  OE1 GLU A 188       1.005   7.917  43.008  1.00 50.04           O  
ANISOU  158  OE1 GLU A 188     6712   5034   7267   -213   -421    260       O  
ATOM    159  OE2 GLU A 188      -0.935   7.184  43.698  1.00 51.41           O  
ANISOU  159  OE2 GLU A 188     6887   5151   7496   -366   -416    402       O  
ATOM    160  N   GLN A 189       4.582   9.602  46.162  1.00 32.75           N  
ANISOU  160  N   GLN A 189     4577   3042   4824    -95   -372    367       N  
ATOM    161  CA  GLN A 189       5.997   9.812  45.921  1.00 35.12           C  
ANISOU  161  CA  GLN A 189     4874   3365   5107     -7   -398    292       C  
ATOM    162  C   GLN A 189       6.774   9.690  47.225  1.00 35.31           C  
ANISOU  162  C   GLN A 189     4927   3399   5088      2   -421    371       C  
ATOM    163  O   GLN A 189       7.826   9.057  47.278  1.00 35.62           O  
ANISOU  163  O   GLN A 189     4984   3389   5163     65   -493    350       O  
ATOM    164  CB  GLN A 189       6.217  11.181  45.278  1.00 35.30           C  
ANISOU  164  CB  GLN A 189     4853   3503   5057     18   -321    208       C  
ATOM    165  CG  GLN A 189       5.669  11.274  43.862  1.00 36.26           C  
ANISOU  165  CG  GLN A 189     4941   3620   5216     25   -310    122       C  
ATOM    166  CD  GLN A 189       6.618  10.664  42.843  1.00 40.18           C  
ANISOU  166  CD  GLN A 189     5424   4080   5762    106   -373     19       C  
ATOM    167  OE1 GLN A 189       6.302   9.665  42.182  1.00 37.33           O  
ANISOU  167  OE1 GLN A 189     5067   3632   5485    117   -433    -16       O  
ATOM    168  NE2 GLN A 189       7.786  11.273  42.705  1.00 40.81           N  
ANISOU  168  NE2 GLN A 189     5481   4233   5791    163   -362    -36       N  
ATOM    169  N   ALA A 190       6.248  10.297  48.284  1.00 35.35           N  
ANISOU  169  N   ALA A 190     4936   3479   5016    -58   -362    456       N  
ATOM    170  CA  ALA A 190       6.935  10.288  49.573  1.00 40.71           C  
ANISOU  170  CA  ALA A 190     5639   4191   5638    -53   -378    531       C  
ATOM    171  C   ALA A 190       6.984   8.902  50.223  1.00 42.90           C  
ANISOU  171  C   ALA A 190     5964   4358   5978    -71   -468    634       C  
ATOM    172  O   ALA A 190       8.004   8.525  50.802  1.00 40.33           O  
ANISOU  172  O   ALA A 190     5662   4014   5649    -23   -525    657       O  
ATOM    173  CB  ALA A 190       6.308  11.289  50.526  1.00 39.29           C  
ANISOU  173  CB  ALA A 190     5445   4132   5354   -109   -293    585       C  
ATOM    174  N   THR A 191       5.881   8.161  50.144  1.00 43.87           N  
ANISOU  174  N   THR A 191     6100   4408   6162   -141   -484    701       N  
ATOM    175  CA  THR A 191       5.782   6.870  50.823  1.00 46.56           C  
ANISOU  175  CA  THR A 191     6486   4638   6567   -178   -571    822       C  
ATOM    176  C   THR A 191       6.120   5.672  49.926  1.00 49.63           C  
ANISOU  176  C   THR A 191     6897   4862   7097   -130   -680    771       C  
ATOM    177  O   THR A 191       6.510   4.614  50.413  1.00 53.01           O  
ANISOU  177  O   THR A 191     7368   5181   7590   -124   -778    846       O  
ATOM    178  CB  THR A 191       4.388   6.669  51.462  1.00 43.64           C  
ANISOU  178  CB  THR A 191     6117   4285   6181   -297   -535    949       C  
ATOM    179  OG1 THR A 191       3.387   6.629  50.440  1.00 38.50           O  
ANISOU  179  OG1 THR A 191     5440   3599   5591   -332   -512    895       O  
ATOM    180  CG2 THR A 191       4.076   7.800  52.428  1.00 45.83           C  
ANISOU  180  CG2 THR A 191     6366   4732   6315   -335   -435    990       C  
ATOM    181  N   GLY A 192       5.975   5.848  48.619  1.00 49.60           N  
ANISOU  181  N   GLY A 192     6864   4843   7140    -94   -668    643       N  
ATOM    182  CA  GLY A 192       6.241   4.793  47.657  1.00 46.70           C  
ANISOU  182  CA  GLY A 192     6506   4334   6902    -42   -767    568       C  
ATOM    183  C   GLY A 192       5.030   3.914  47.392  1.00 54.17           C  
ANISOU  183  C   GLY A 192     7466   5169   7947   -122   -805    622       C  
ATOM    184  O   GLY A 192       5.098   2.959  46.612  1.00 58.88           O  
ANISOU  184  O   GLY A 192     8072   5634   8664    -88   -896    561       O  
ATOM    185  N   ALA A 193       3.913   4.237  48.036  1.00 53.12           N  
ANISOU  185  N   ALA A 193     7327   5092   7763   -229   -738    730       N  
ATOM    186  CA  ALA A 193       2.723   3.397  47.971  1.00 53.40           C  
ANISOU  186  CA  ALA A 193     7373   5031   7886   -324   -771    807       C  
ATOM    187  C   ALA A 193       1.518   4.159  47.440  1.00 52.32           C  
ANISOU  187  C   ALA A 193     7186   4983   7708   -384   -674    774       C  
ATOM    188  O   ALA A 193       1.293   5.317  47.802  1.00 48.23           O  
ANISOU  188  O   ALA A 193     6638   4615   7071   -399   -569    776       O  
ATOM    189  CB  ALA A 193       2.416   2.810  49.348  1.00 53.12           C  
ANISOU  189  CB  ALA A 193     7375   4968   7840   -414   -799    997       C  
ATOM    190  N   LYS A 194       0.741   3.507  46.583  1.00 46.73           N  
ANISOU  190  N   LYS A 194     6470   4183   7104   -416   -713    737       N  
ATOM    191  CA  LYS A 194      -0.474   4.121  46.061  1.00 57.02           C  
ANISOU  191  CA  LYS A 194     7724   5561   8378   -475   -632    709       C  
ATOM    192  C   LYS A 194      -1.610   4.068  47.087  1.00 57.99           C  
ANISOU  192  C   LYS A 194     7840   5727   8466   -604   -588    864       C  
ATOM    193  O   LYS A 194      -1.681   3.149  47.898  1.00 52.19           O  
ANISOU  193  O   LYS A 194     7141   4910   7778   -665   -650    995       O  
ATOM    194  CB  LYS A 194      -0.894   3.472  44.740  1.00 60.29           C  
ANISOU  194  CB  LYS A 194     8124   5873   8911   -459   -690    604       C  
ATOM    195  CG  LYS A 194       0.085   3.731  43.597  1.00 64.97           C  
ANISOU  195  CG  LYS A 194     8703   6472   9511   -333   -711    434       C  
ATOM    196  CD  LYS A 194      -0.487   3.289  42.261  1.00 66.29           C  
ANISOU  196  CD  LYS A 194     8843   6578   9768   -321   -749    320       C  
ATOM    197  CE  LYS A 194       0.494   3.549  41.125  1.00 67.51           C  
ANISOU  197  CE  LYS A 194     8975   6761   9914   -198   -766    152       C  
ATOM    198  NZ  LYS A 194      -0.026   3.023  39.820  1.00 68.02           N  
ANISOU  198  NZ  LYS A 194     9011   6769  10064   -180   -814     33       N  
ATOM    199  N   ASP A 195      -2.481   5.071  47.051  1.00 58.74           N  
ANISOU  199  N   ASP A 195     7885   5958   8476   -643   -482    851       N  
ATOM    200  CA  ASP A 195      -3.607   5.162  47.974  1.00 66.91           C  
ANISOU  200  CA  ASP A 195     8895   7068   9458   -760   -426    980       C  
ATOM    201  C   ASP A 195      -4.807   4.427  47.390  1.00 75.00           C  
ANISOU  201  C   ASP A 195     9898   8016  10583   -844   -455    996       C  
ATOM    202  O   ASP A 195      -5.359   4.841  46.373  1.00 68.43           O  
ANISOU  202  O   ASP A 195     9026   7207   9767   -826   -424    889       O  
ATOM    203  CB  ASP A 195      -3.960   6.635  48.228  1.00 69.12           C  
ANISOU  203  CB  ASP A 195     9127   7535   9601   -751   -303    943       C  
ATOM    204  CG  ASP A 195      -4.986   6.820  49.338  1.00 73.07           C  
ANISOU  204  CG  ASP A 195     9594   8145  10024   -858   -239   1069       C  
ATOM    205  OD1 ASP A 195      -5.455   5.812  49.902  1.00 76.66           O  
ANISOU  205  OD1 ASP A 195    10062   8538  10526   -951   -284   1197       O  
ATOM    206  OD2 ASP A 195      -5.320   7.983  49.648  1.00 72.96           O  
ANISOU  206  OD2 ASP A 195     9537   8283   9900   -850   -145   1038       O  
ATOM    207  N   THR A 196      -5.204   3.329  48.026  1.00 87.97           N  
ANISOU  207  N   THR A 196    11564   9567  12295   -938   -518   1133       N  
ATOM    208  CA  THR A 196      -6.371   2.580  47.571  1.00101.95           C  
ANISOU  208  CA  THR A 196    13311  11260  14166  -1034   -551   1162       C  
ATOM    209  C   THR A 196      -7.626   3.020  48.319  1.00114.83           C  
ANISOU  209  C   THR A 196    14884  13033  15711  -1152   -458   1265       C  
ATOM    210  O   THR A 196      -8.173   2.283  49.141  1.00119.71           O  
ANISOU  210  O   THR A 196    15506  13628  16351  -1267   -483   1421       O  
ATOM    211  CB  THR A 196      -6.177   1.056  47.707  1.00102.83           C  
ANISOU  211  CB  THR A 196    13476  11169  14425  -1080   -687   1250       C  
ATOM    212  OG1 THR A 196      -4.961   0.669  47.058  1.00100.48           O  
ANISOU  212  OG1 THR A 196    13226  10751  14202   -958   -775   1143       O  
ATOM    213  CG2 THR A 196      -7.341   0.311  47.065  1.00105.70           C  
ANISOU  213  CG2 THR A 196    13812  11442  14907  -1172   -729   1255       C  
ATOM    214  N   LYS A 197      -8.061   4.241  48.035  1.00120.40           N  
ANISOU  214  N   LYS A 197    15535  13892  16319  -1121   -354   1178       N  
ATOM    215  CA  LYS A 197      -9.308   4.771  48.560  1.00126.97           C  
ANISOU  215  CA  LYS A 197    16299  14874  17071  -1213   -262   1238       C  
ATOM    216  C   LYS A 197      -9.947   5.597  47.458  1.00129.23           C  
ANISOU  216  C   LYS A 197    16530  15220  17351  -1171   -208   1093       C  
ATOM    217  O   LYS A 197      -9.310   6.488  46.904  1.00126.57           O  
ANISOU  217  O   LYS A 197    16198  14924  16970  -1062   -178    972       O  
ATOM    218  CB  LYS A 197      -9.058   5.632  49.799  1.00130.46           C  
ANISOU  218  CB  LYS A 197    16729  15483  17357  -1211   -180   1302       C  
ATOM    219  CG  LYS A 197      -8.569   4.855  51.012  1.00135.59           C  
ANISOU  219  CG  LYS A 197    17423  16102  17992  -1267   -226   1465       C  
ATOM    220  CD  LYS A 197      -8.412   5.755  52.232  1.00138.56           C  
ANISOU  220  CD  LYS A 197    17776  16668  18201  -1265   -140   1518       C  
ATOM    221  CE  LYS A 197      -7.314   6.786  52.030  1.00138.44           C  
ANISOU  221  CE  LYS A 197    17783  16697  18123  -1128   -112   1390       C  
ATOM    222  NZ  LYS A 197      -7.155   7.671  53.215  1.00139.10           N  
ANISOU  222  NZ  LYS A 197    17843  16960  18050  -1121    -35   1428       N  
ATOM    223  N   PRO A 198     -11.207   5.290  47.119  1.00135.03           N  
ANISOU  223  N   PRO A 198    17212  15960  18133  -1259   -199   1108       N  
ATOM    224  CA  PRO A 198     -11.897   5.992  46.032  1.00135.33           C  
ANISOU  224  CA  PRO A 198    17196  16050  18174  -1222   -157    976       C  
ATOM    225  C   PRO A 198     -11.752   7.503  46.160  1.00132.27           C  
ANISOU  225  C   PRO A 198    16778  15824  17654  -1143    -59    901       C  
ATOM    226  O   PRO A 198     -11.966   8.054  47.240  1.00131.53           O  
ANISOU  226  O   PRO A 198    16659  15861  17455  -1175      8    971       O  
ATOM    227  CB  PRO A 198     -13.357   5.585  46.232  1.00137.65           C  
ANISOU  227  CB  PRO A 198    17424  16384  18492  -1353   -138   1051       C  
ATOM    228  CG  PRO A 198     -13.281   4.248  46.877  1.00139.75           C  
ANISOU  228  CG  PRO A 198    17729  16529  18840  -1451   -218   1196       C  
ATOM    229  CD  PRO A 198     -12.066   4.282  47.763  1.00138.78           C  
ANISOU  229  CD  PRO A 198    17671  16400  18660  -1403   -229   1258       C  
ATOM    230  N   MET A 199     -11.379   8.163  45.070  1.00129.54           N  
ANISOU  230  N   MET A 199    16433  15471  17313  -1042    -56    761       N  
ATOM    231  CA  MET A 199     -11.278   9.614  45.075  1.00128.06           C  
ANISOU  231  CA  MET A 199    16218  15419  17018   -970     25    688       C  
ATOM    232  C   MET A 199     -12.672  10.222  45.168  1.00132.12           C  
ANISOU  232  C   MET A 199    16652  16060  17489  -1023     95    685       C  
ATOM    233  O   MET A 199     -13.644   9.623  44.712  1.00133.80           O  
ANISOU  233  O   MET A 199    16827  16242  17769  -1090     76    693       O  
ATOM    234  CB  MET A 199     -10.556  10.108  43.825  1.00123.37           C  
ANISOU  234  CB  MET A 199    15644  14784  16446   -860      4    553       C  
ATOM    235  CG  MET A 199      -9.179   9.507  43.642  1.00122.09           C  
ANISOU  235  CG  MET A 199    15551  14510  16328   -800    -66    538       C  
ATOM    236  SD  MET A 199      -8.170  10.450  42.490  1.00 70.50           S  
ANISOU  236  SD  MET A 199     9028   7992   9767   -669    -62    394       S  
ATOM    237  CE  MET A 199      -7.691  11.833  43.506  1.00 66.35           C  
ANISOU  237  CE  MET A 199     8501   7599   9111   -635     20    415       C  
ATOM    238  N   GLY A 200     -12.762  11.409  45.763  1.00133.26           N  
ANISOU  238  N   GLY A 200    16764  16344  17523   -990    173    668       N  
ATOM    239  CA  GLY A 200     -14.040  12.057  46.011  1.00133.94           C  
ANISOU  239  CA  GLY A 200    16768  16566  17556  -1030    241    661       C  
ATOM    240  C   GLY A 200     -14.850  12.333  44.759  1.00133.33           C  
ANISOU  240  C   GLY A 200    16647  16481  17531  -1010    238    564       C  
ATOM    241  O   GLY A 200     -14.632  11.709  43.719  1.00133.41           O  
ANISOU  241  O   GLY A 200    16685  16374  17632   -995    175    521       O  
ATOM    242  N   ARG A 201     -15.793  13.267  44.855  1.00131.46           N  
ANISOU  242  N   ARG A 201    16338  16375  17236  -1005    301    524       N  
ATOM    243  CA  ARG A 201     -16.590  13.642  43.692  1.00128.36           C  
ANISOU  243  CA  ARG A 201    15899  15988  16883   -979    298    431       C  
ATOM    244  C   ARG A 201     -15.666  13.977  42.526  1.00125.00           C  
ANISOU  244  C   ARG A 201    15527  15475  16491   -880    256    339       C  
ATOM    245  O   ARG A 201     -14.537  14.425  42.732  1.00125.83           O  
ANISOU  245  O   ARG A 201    15686  15564  16561   -815    256    328       O  
ATOM    246  CB  ARG A 201     -17.544  14.799  44.005  1.00127.16           C  
ANISOU  246  CB  ARG A 201    15666  15992  16656   -961    368    388       C  
ATOM    247  CG  ARG A 201     -16.899  16.035  44.605  1.00124.34           C  
ANISOU  247  CG  ARG A 201    15323  15710  16209   -878    411    352       C  
ATOM    248  CD  ARG A 201     -17.804  17.246  44.411  1.00122.20           C  
ANISOU  248  CD  ARG A 201    14979  15553  15898   -830    455    268       C  
ATOM    249  NE  ARG A 201     -17.941  17.587  42.995  1.00119.54           N  
ANISOU  249  NE  ARG A 201    14644  15156  15617   -773    420    183       N  
ATOM    250  CZ  ARG A 201     -18.755  18.524  42.518  1.00115.33           C  
ANISOU  250  CZ  ARG A 201    14054  14693  15074   -728    438    108       C  
ATOM    251  NH1 ARG A 201     -19.522  19.227  43.343  1.00115.06           N  
ANISOU  251  NH1 ARG A 201    13950  14790  14978   -727    490     94       N  
ATOM    252  NH2 ARG A 201     -18.804  18.759  41.213  1.00111.90           N  
ANISOU  252  NH2 ARG A 201    13626  14201  14688   -679    400     43       N  
ATOM    253  N   SER A 202     -16.157  13.761  41.309  1.00119.98           N  
ANISOU  253  N   SER A 202    14871  14794  15920   -871    221    274       N  
ATOM    254  CA  SER A 202     -15.307  13.697  40.123  1.00113.18           C  
ANISOU  254  CA  SER A 202    14058  13842  15102   -797    168    199       C  
ATOM    255  C   SER A 202     -14.594  12.349  40.146  1.00109.13           C  
ANISOU  255  C   SER A 202    13601  13200  14663   -830    102    242       C  
ATOM    256  O   SER A 202     -15.220  11.304  39.955  1.00112.80           O  
ANISOU  256  O   SER A 202    14051  13603  15206   -902     60    268       O  
ATOM    257  CB  SER A 202     -14.295  14.847  40.077  1.00108.64           C  
ANISOU  257  CB  SER A 202    13517  13300  14460   -701    192    155       C  
ATOM    258  OG  SER A 202     -14.947  16.106  40.059  1.00107.06           O  
ANISOU  258  OG  SER A 202    13268  13204  14204   -666    242    114       O  
ATOM    259  N   GLY A 203     -13.291  12.371  40.402  1.00 98.47           N  
ANISOU  259  N   GLY A 203    12314  11805  13293   -778     86    249       N  
ATOM    260  CA  GLY A 203     -12.533  11.141  40.539  1.00 86.35           C  
ANISOU  260  CA  GLY A 203    10835  10147  11827   -798     18    289       C  
ATOM    261  C   GLY A 203     -12.116  10.571  39.200  1.00 74.30           C  
ANISOU  261  C   GLY A 203     9328   8526  10377   -749    -54    198       C  
ATOM    262  O   GLY A 203     -11.019  10.030  39.066  1.00 74.08           O  
ANISOU  262  O   GLY A 203     9352   8415  10381   -706   -106    184       O  
ATOM    263  N   ALA A 204     -12.995  10.688  38.209  1.00 64.85           N  
ANISOU  263  N   ALA A 204     8083   7350   9208   -750    -58    130       N  
ATOM    264  CA  ALA A 204     -12.675  10.275  36.846  1.00 59.31           C  
ANISOU  264  CA  ALA A 204     7387   6586   8562   -696   -121     27       C  
ATOM    265  C   ALA A 204     -11.578  11.168  36.261  1.00 51.45           C  
ANISOU  265  C   ALA A 204     6414   5633   7501   -591   -107    -42       C  
ATOM    266  O   ALA A 204     -10.541  10.674  35.806  1.00 47.30           O  
ANISOU  266  O   ALA A 204     5926   5044   7002   -538   -158    -87       O  
ATOM    267  CB  ALA A 204     -13.922  10.307  35.969  1.00 60.12           C  
ANISOU  267  CB  ALA A 204     7427   6721   8694   -722   -124    -27       C  
ATOM    268  N   THR A 205     -11.814  12.481  36.267  1.00 47.03           N  
ANISOU  268  N   THR A 205     5829   5182   6859   -561    -41    -52       N  
ATOM    269  CA  THR A 205     -10.784  13.430  35.839  1.00 44.47           C  
ANISOU  269  CA  THR A 205     5525   4901   6470   -476    -24    -98       C  
ATOM    270  C   THR A 205      -9.623  13.397  36.817  1.00 34.77           C  
ANISOU  270  C   THR A 205     4348   3649   5215   -461    -18    -46       C  
ATOM    271  O   THR A 205      -8.465  13.419  36.410  1.00 37.15           O  
ANISOU  271  O   THR A 205     4679   3932   5504   -400    -41    -86       O  
ATOM    272  CB  THR A 205     -11.306  14.871  35.710  1.00 50.58           C  
ANISOU  272  CB  THR A 205     6264   5783   7173   -452     36   -111       C  
ATOM    273  OG1 THR A 205     -12.165  14.968  34.566  1.00 58.20           O  
ANISOU  273  OG1 THR A 205     7184   6773   8157   -445     20   -172       O  
ATOM    274  CG2 THR A 205     -10.137  15.840  35.525  1.00 42.47           C  
ANISOU  274  CG2 THR A 205     5264   4790   6082   -379     52   -132       C  
ATOM    275  N   SER A 206      -9.928  13.319  38.109  1.00 38.57           N  
ANISOU  275  N   SER A 206     4835   4138   5681   -517     13     41       N  
ATOM    276  CA  SER A 206      -8.862  13.298  39.111  1.00 37.99           C  
ANISOU  276  CA  SER A 206     4809   4051   5577   -504     17     94       C  
ATOM    277  C   SER A 206      -7.940  12.105  38.908  1.00 37.01           C  
ANISOU  277  C   SER A 206     4728   3815   5518   -488    -57     87       C  
ATOM    278  O   SER A 206      -6.732  12.235  39.029  1.00 32.23           O  
ANISOU  278  O   SER A 206     4158   3200   4889   -433    -69     74       O  
ATOM    279  CB  SER A 206      -9.432  13.282  40.528  1.00 38.46           C  
ANISOU  279  CB  SER A 206     4861   4147   5605   -574     58    192       C  
ATOM    280  OG  SER A 206     -10.351  14.344  40.714  1.00 41.16           O  
ANISOU  280  OG  SER A 206     5154   4595   5892   -583    122    185       O  
ATOM    281  N   ARG A 207      -8.508  10.933  38.605  1.00 39.25           N  
ANISOU  281  N   ARG A 207     5009   4014   5891   -534   -113     91       N  
ATOM    282  CA  ARG A 207      -7.670   9.749  38.462  1.00 35.98           C  
ANISOU  282  CA  ARG A 207     4638   3481   5553   -515   -195     81       C  
ATOM    283  C   ARG A 207      -6.785   9.895  37.248  1.00 32.52           C  
ANISOU  283  C   ARG A 207     4200   3042   5113   -421   -227    -36       C  
ATOM    284  O   ARG A 207      -5.600   9.591  37.298  1.00 36.19           O  
ANISOU  284  O   ARG A 207     4699   3469   5583   -366   -263    -57       O  
ATOM    285  CB  ARG A 207      -8.494   8.450  38.379  1.00 41.14           C  
ANISOU  285  CB  ARG A 207     5286   4029   6315   -588   -259    108       C  
ATOM    286  CG  ARG A 207      -8.705   7.794  39.727  1.00 53.33           C  
ANISOU  286  CG  ARG A 207     6856   5527   7882   -673   -267    242       C  
ATOM    287  CD  ARG A 207      -9.339   6.413  39.584  1.00 62.49           C  
ANISOU  287  CD  ARG A 207     8019   6558   9167   -747   -348    272       C  
ATOM    288  NE  ARG A 207     -10.598   6.486  38.850  1.00 66.92           N  
ANISOU  288  NE  ARG A 207     8522   7150   9755   -791   -335    230       N  
ATOM    289  CZ  ARG A 207     -11.748   6.890  39.381  1.00 70.75           C  
ANISOU  289  CZ  ARG A 207     8960   7719  10201   -872   -271    296       C  
ATOM    290  NH1 ARG A 207     -11.804   7.257  40.658  1.00 71.40           N  
ANISOU  290  NH1 ARG A 207     9047   7870  10213   -918   -214    406       N  
ATOM    291  NH2 ARG A 207     -12.842   6.930  38.632  1.00 71.78           N  
ANISOU  291  NH2 ARG A 207     9035   7876  10361   -904   -266    246       N  
ATOM    292  N   LYS A 208      -7.362  10.369  36.151  1.00 33.21           N  
ANISOU  292  N   LYS A 208     4246   3185   5189   -401   -213   -113       N  
ATOM    293  CA  LYS A 208      -6.567  10.594  34.954  1.00 33.68           C  
ANISOU  293  CA  LYS A 208     4296   3271   5229   -316   -235   -220       C  
ATOM    294  C   LYS A 208      -5.509  11.671  35.185  1.00 30.35           C  
ANISOU  294  C   LYS A 208     3888   2929   4716   -261   -187   -217       C  
ATOM    295  O   LYS A 208      -4.409  11.577  34.658  1.00 35.41           O  
ANISOU  295  O   LYS A 208     4537   3573   5345   -195   -215   -277       O  
ATOM    296  CB  LYS A 208      -7.457  10.948  33.759  1.00 42.39           C  
ANISOU  296  CB  LYS A 208     5349   4430   6327   -311   -228   -292       C  
ATOM    297  CG  LYS A 208      -8.272   9.763  33.255  1.00 55.98           C  
ANISOU  297  CG  LYS A 208     7054   6067   8149   -349   -295   -328       C  
ATOM    298  CD  LYS A 208      -9.029  10.103  31.980  1.00 63.13           C  
ANISOU  298  CD  LYS A 208     7908   7037   9042   -332   -295   -413       C  
ATOM    299  CE  LYS A 208      -8.079  10.544  30.869  1.00 60.04           C  
ANISOU  299  CE  LYS A 208     7505   6714   8592   -240   -304   -508       C  
ATOM    300  NZ  LYS A 208      -8.841  10.975  29.660  1.00 54.27           N  
ANISOU  300  NZ  LYS A 208     6723   6063   7834   -225   -301   -577       N  
ATOM    301  N   ALA A 209      -5.843  12.696  35.973  1.00 30.47           N  
ANISOU  301  N   ALA A 209     3899   3010   4666   -289   -118   -151       N  
ATOM    302  CA  ALA A 209      -4.859  13.738  36.304  1.00 30.35           C  
ANISOU  302  CA  ALA A 209     3898   3061   4573   -245    -77   -143       C  
ATOM    303  C   ALA A 209      -3.712  13.157  37.126  1.00 28.29           C  
ANISOU  303  C   ALA A 209     3681   2747   4322   -227   -105   -112       C  
ATOM    304  O   ALA A 209      -2.542  13.472  36.901  1.00 32.28           O  
ANISOU  304  O   ALA A 209     4194   3277   4792   -170   -110   -147       O  
ATOM    305  CB  ALA A 209      -5.525  14.897  37.056  1.00 31.26           C  
ANISOU  305  CB  ALA A 209     3999   3248   4629   -277     -6    -88       C  
ATOM    306  N   LEU A 210      -4.051  12.316  38.096  1.00 28.64           N  
ANISOU  306  N   LEU A 210     3749   2723   4411   -280   -125    -39       N  
ATOM    307  CA  LEU A 210      -3.029  11.654  38.901  1.00 28.05           C  
ANISOU  307  CA  LEU A 210     3717   2588   4352   -265   -164      0       C  
ATOM    308  C   LEU A 210      -2.161  10.713  38.054  1.00 31.78           C  
ANISOU  308  C   LEU A 210     4201   2989   4886   -204   -243    -80       C  
ATOM    309  O   LEU A 210      -0.944  10.653  38.223  1.00 35.23           O  
ANISOU  309  O   LEU A 210     4657   3421   5307   -148   -264    -99       O  
ATOM    310  CB  LEU A 210      -3.685  10.904  40.072  1.00 33.97           C  
ANISOU  310  CB  LEU A 210     4488   3281   5138   -344   -174    107       C  
ATOM    311  CG  LEU A 210      -2.788  10.273  41.133  1.00 37.29           C  
ANISOU  311  CG  LEU A 210     4956   3645   5567   -341   -211    176       C  
ATOM    312  CD1 LEU A 210      -1.806  11.291  41.708  1.00 36.77           C  
ANISOU  312  CD1 LEU A 210     4899   3662   5409   -295   -166    179       C  
ATOM    313  CD2 LEU A 210      -3.637   9.665  42.239  1.00 41.49           C  
ANISOU  313  CD2 LEU A 210     5500   4146   6121   -434   -212    297       C  
ATOM    314  N   GLU A 211      -2.790   9.965  37.146  1.00 34.70           N  
ANISOU  314  N   GLU A 211     4552   3304   5326   -210   -289   -136       N  
ATOM    315  CA  GLU A 211      -2.052   9.118  36.225  1.00 32.28           C  
ANISOU  315  CA  GLU A 211     4246   2942   5077   -144   -366   -235       C  
ATOM    316  C   GLU A 211      -1.127   9.961  35.348  1.00 32.24           C  
ANISOU  316  C   GLU A 211     4214   3041   4996    -65   -340   -323       C  
ATOM    317  O   GLU A 211       0.022   9.609  35.119  1.00 31.06           O  
ANISOU  317  O   GLU A 211     4070   2882   4850      2   -381   -379       O  
ATOM    318  CB  GLU A 211      -3.020   8.293  35.358  1.00 38.06           C  
ANISOU  318  CB  GLU A 211     4956   3612   5893   -167   -417   -290       C  
ATOM    319  CG  GLU A 211      -3.666   7.143  36.114  1.00 49.20           C  
ANISOU  319  CG  GLU A 211     6396   4892   7406   -240   -473   -213       C  
ATOM    320  CD  GLU A 211      -4.909   6.596  35.425  1.00 56.16           C  
ANISOU  320  CD  GLU A 211     7247   5730   8359   -291   -502   -245       C  
ATOM    321  OE1 GLU A 211      -5.163   6.960  34.247  1.00 52.56           O  
ANISOU  321  OE1 GLU A 211     6751   5339   7882   -253   -494   -346       O  
ATOM    322  OE2 GLU A 211      -5.632   5.807  36.078  1.00 57.77           O  
ANISOU  322  OE2 GLU A 211     7467   5841   8639   -372   -535   -164       O  
ATOM    323  N   THR A 212      -1.638  11.082  34.854  1.00 33.45           N  
ANISOU  323  N   THR A 212     4333   3297   5079    -75   -274   -331       N  
ATOM    324  CA  THR A 212      -0.818  11.996  34.068  1.00 32.05           C  
ANISOU  324  CA  THR A 212     4128   3226   4823    -16   -245   -391       C  
ATOM    325  C   THR A 212       0.348  12.534  34.894  1.00 29.80           C  
ANISOU  325  C   THR A 212     3866   2971   4485      8   -220   -352       C  
ATOM    326  O   THR A 212       1.476  12.633  34.421  1.00 31.68           O  
ANISOU  326  O   THR A 212     4090   3254   4692     68   -233   -409       O  
ATOM    327  CB  THR A 212      -1.686  13.168  33.512  1.00 30.45           C  
ANISOU  327  CB  THR A 212     3892   3117   4562    -41   -183   -385       C  
ATOM    328  OG1 THR A 212      -2.742  12.638  32.689  1.00 37.24           O  
ANISOU  328  OG1 THR A 212     4726   3956   5468    -59   -210   -430       O  
ATOM    329  CG2 THR A 212      -0.842  14.167  32.725  1.00 29.00           C  
ANISOU  329  CG2 THR A 212     3681   3043   4295      7   -154   -427       C  
ATOM    330  N   LEU A 213       0.062  12.904  36.133  1.00 29.83           N  
ANISOU  330  N   LEU A 213     3897   2961   4474    -41   -183   -256       N  
ATOM    331  CA  LEU A 213       1.067  13.463  37.028  1.00 31.61           C  
ANISOU  331  CA  LEU A 213     4143   3217   4648    -24   -160   -216       C  
ATOM    332  C   LEU A 213       2.177  12.450  37.334  1.00 36.01           C  
ANISOU  332  C   LEU A 213     4726   3711   5246     21   -224   -234       C  
ATOM    333  O   LEU A 213       3.368  12.802  37.366  1.00 31.02           O  
ANISOU  333  O   LEU A 213     4089   3124   4572     70   -223   -260       O  
ATOM    334  CB  LEU A 213       0.355  13.924  38.305  1.00 35.92           C  
ANISOU  334  CB  LEU A 213     4710   3763   5173    -87   -113   -117       C  
ATOM    335  CG  LEU A 213       0.857  14.997  39.255  1.00 37.72           C  
ANISOU  335  CG  LEU A 213     4948   4054   5330    -90    -63    -70       C  
ATOM    336  CD1 LEU A 213       1.512  16.196  38.535  1.00 28.71           C  
ANISOU  336  CD1 LEU A 213     3780   2999   4129    -52    -31   -119       C  
ATOM    337  CD2 LEU A 213      -0.313  15.407  40.170  1.00 30.61           C  
ANISOU  337  CD2 LEU A 213     4048   3169   4413   -153    -17      1       C  
ATOM    338  N   ARG A 214       1.799  11.184  37.526  1.00 38.58           N  
ANISOU  338  N   ARG A 214     5074   3927   5658      7   -287   -223       N  
ATOM    339  CA  ARG A 214       2.791  10.115  37.668  1.00 37.75           C  
ANISOU  339  CA  ARG A 214     4991   3744   5607     60   -366   -253       C  
ATOM    340  C   ARG A 214       3.712  10.043  36.452  1.00 39.85           C  
ANISOU  340  C   ARG A 214     5219   4059   5864    144   -395   -379       C  
ATOM    341  O   ARG A 214       4.936  10.029  36.584  1.00 36.73           O  
ANISOU  341  O   ARG A 214     4822   3688   5447    203   -414   -410       O  
ATOM    342  CB  ARG A 214       2.123   8.751  37.840  1.00 36.47           C  
ANISOU  342  CB  ARG A 214     4857   3445   5557     28   -441   -230       C  
ATOM    343  CG  ARG A 214       1.334   8.585  39.121  1.00 37.21           C  
ANISOU  343  CG  ARG A 214     4985   3489   5663    -58   -424    -96       C  
ATOM    344  CD  ARG A 214       0.873   7.133  39.319  1.00 40.85           C  
ANISOU  344  CD  ARG A 214     5475   3800   6243    -91   -514    -63       C  
ATOM    345  NE  ARG A 214      -0.023   7.024  40.470  1.00 38.95           N  
ANISOU  345  NE  ARG A 214     5259   3536   6006   -190   -490     75       N  
ATOM    346  CZ  ARG A 214      -1.308   6.710  40.392  1.00 42.96           C  
ANISOU  346  CZ  ARG A 214     5755   4012   6558   -269   -485    114       C  
ATOM    347  NH1 ARG A 214      -1.852   6.428  39.216  1.00 45.73           N  
ANISOU  347  NH1 ARG A 214     6075   4338   6961   -259   -510     22       N  
ATOM    348  NH2 ARG A 214      -2.043   6.647  41.491  1.00 42.46           N  
ANISOU  348  NH2 ARG A 214     5704   3947   6482   -359   -458    243       N  
ATOM    349  N   ARG A 215       3.115   9.982  35.265  1.00 36.64           N  
ANISOU  349  N   ARG A 215     4776   3676   5469    151   -399   -455       N  
ATOM    350  CA  ARG A 215       3.888   9.861  34.036  1.00 34.99           C  
ANISOU  350  CA  ARG A 215     4522   3531   5242    230   -427   -580       C  
ATOM    351  C   ARG A 215       4.806  11.076  33.801  1.00 36.25           C  
ANISOU  351  C   ARG A 215     4649   3832   5293    257   -364   -591       C  
ATOM    352  O   ARG A 215       6.028  10.939  33.664  1.00 31.80           O  
ANISOU  352  O   ARG A 215     4068   3307   4709    321   -388   -646       O  
ATOM    353  CB  ARG A 215       2.954   9.640  32.842  1.00 33.72           C  
ANISOU  353  CB  ARG A 215     4326   3382   5103    225   -439   -652       C  
ATOM    354  CG  ARG A 215       3.634   9.699  31.493  1.00 32.99           C  
ANISOU  354  CG  ARG A 215     4175   3393   4967    300   -454   -781       C  
ATOM    355  CD  ARG A 215       2.706   9.151  30.406  1.00 38.01           C  
ANISOU  355  CD  ARG A 215     4781   4016   5644    302   -490   -862       C  
ATOM    356  NE  ARG A 215       1.353   9.699  30.504  1.00 35.62           N  
ANISOU  356  NE  ARG A 215     4486   3712   5337    221   -441   -788       N  
ATOM    357  CZ  ARG A 215       0.981  10.859  29.970  1.00 36.01           C  
ANISOU  357  CZ  ARG A 215     4504   3878   5298    201   -373   -771       C  
ATOM    358  NH1 ARG A 215       1.859  11.599  29.299  1.00 32.46           N  
ANISOU  358  NH1 ARG A 215     4017   3559   4758    245   -343   -811       N  
ATOM    359  NH2 ARG A 215      -0.267  11.282  30.106  1.00 33.27           N  
ANISOU  359  NH2 ARG A 215     4162   3521   4957    135   -338   -710       N  
ATOM    360  N   VAL A 216       4.225  12.268  33.755  1.00 30.80           N  
ANISOU  360  N   VAL A 216     3948   3216   4537    208   -289   -539       N  
ATOM    361  CA  VAL A 216       5.010  13.443  33.387  1.00 27.53           C  
ANISOU  361  CA  VAL A 216     3500   2930   4029    224   -237   -547       C  
ATOM    362  C   VAL A 216       5.880  13.951  34.538  1.00 31.52           C  
ANISOU  362  C   VAL A 216     4031   3442   4503    220   -214   -483       C  
ATOM    363  O   VAL A 216       6.995  14.430  34.311  1.00 36.42           O  
ANISOU  363  O   VAL A 216     4624   4146   5070    255   -203   -513       O  
ATOM    364  CB  VAL A 216       4.112  14.574  32.817  1.00 35.30           C  
ANISOU  364  CB  VAL A 216     4463   3989   4961    179   -177   -518       C  
ATOM    365  CG1 VAL A 216       3.373  14.077  31.587  1.00 32.77           C  
ANISOU  365  CG1 VAL A 216     4109   3679   4661    191   -204   -591       C  
ATOM    366  CG2 VAL A 216       3.114  15.049  33.852  1.00 43.71           C  
ANISOU  366  CG2 VAL A 216     5565   5002   6039    112   -139   -420       C  
ATOM    367  N   GLY A 217       5.369  13.843  35.763  1.00 32.31           N  
ANISOU  367  N   GLY A 217     4180   3465   4633    175   -207   -397       N  
ATOM    368  CA  GLY A 217       6.083  14.300  36.947  1.00 34.65           C  
ANISOU  368  CA  GLY A 217     4501   3767   4898    168   -188   -336       C  
ATOM    369  C   GLY A 217       7.322  13.474  37.228  1.00 37.13           C  
ANISOU  369  C   GLY A 217     4821   4053   5235    229   -246   -372       C  
ATOM    370  O   GLY A 217       8.370  14.008  37.604  1.00 35.89           O  
ANISOU  370  O   GLY A 217     4655   3953   5030    252   -232   -370       O  
ATOM    371  N   ASP A 218       7.210  12.159  37.042  1.00 34.34           N  
ANISOU  371  N   ASP A 218     4481   3608   4960    258   -317   -409       N  
ATOM    372  CA  ASP A 218       8.376  11.306  37.109  1.00 38.06           C  
ANISOU  372  CA  ASP A 218     4950   4049   5463    331   -385   -463       C  
ATOM    373  C   ASP A 218       9.361  11.722  36.011  1.00 35.17           C  
ANISOU  373  C   ASP A 218     4520   3804   5040    392   -376   -567       C  
ATOM    374  O   ASP A 218      10.560  11.767  36.243  1.00 38.15           O  
ANISOU  374  O   ASP A 218     4880   4224   5391    440   -390   -593       O  
ATOM    375  CB  ASP A 218       8.004   9.811  36.962  1.00 42.54           C  
ANISOU  375  CB  ASP A 218     5540   4483   6138    354   -475   -496       C  
ATOM    376  CG  ASP A 218       7.182   9.267  38.149  1.00 51.81           C  
ANISOU  376  CG  ASP A 218     6777   5538   7371    289   -493   -379       C  
ATOM    377  OD1 ASP A 218       6.767  10.052  39.043  1.00 45.78           O  
ANISOU  377  OD1 ASP A 218     6034   4805   6556    226   -430   -281       O  
ATOM    378  OD2 ASP A 218       6.932   8.033  38.170  1.00 54.46           O  
ANISOU  378  OD2 ASP A 218     7139   5750   7805    299   -575   -388       O  
ATOM    379  N   GLY A 219       8.861  12.017  34.812  1.00 39.31           N  
ANISOU  379  N   GLY A 219     5002   4391   5541    389   -353   -623       N  
ATOM    380  CA  GLY A 219       9.731  12.434  33.715  1.00 35.73           C  
ANISOU  380  CA  GLY A 219     4480   4073   5021    438   -340   -713       C  
ATOM    381  C   GLY A 219      10.485  13.734  33.956  1.00 37.01           C  
ANISOU  381  C   GLY A 219     4620   4348   5094    416   -275   -669       C  
ATOM    382  O   GLY A 219      11.669  13.845  33.648  1.00 36.60           O  
ANISOU  382  O   GLY A 219     4521   4385   4999    463   -281   -723       O  
ATOM    383  N   VAL A 220       9.793  14.738  34.502  1.00 32.58           N  
ANISOU  383  N   VAL A 220     4088   3786   4507    344   -216   -574       N  
ATOM    384  CA  VAL A 220      10.456  15.991  34.892  1.00 28.94           C  
ANISOU  384  CA  VAL A 220     3613   3407   3976    316   -164   -526       C  
ATOM    385  C   VAL A 220      11.554  15.716  35.879  1.00 32.23           C  
ANISOU  385  C   VAL A 220     4043   3805   4397    347   -189   -518       C  
ATOM    386  O   VAL A 220      12.655  16.278  35.813  1.00 33.03           O  
ANISOU  386  O   VAL A 220     4106   3998   4447    363   -176   -536       O  
ATOM    387  CB  VAL A 220       9.465  16.946  35.612  1.00 32.92           C  
ANISOU  387  CB  VAL A 220     4156   3879   4472    242   -113   -429       C  
ATOM    388  CG1 VAL A 220      10.226  18.102  36.283  1.00 36.06           C  
ANISOU  388  CG1 VAL A 220     4550   4332   4817    218    -75   -383       C  
ATOM    389  CG2 VAL A 220       8.464  17.456  34.647  1.00 35.10           C  
ANISOU  389  CG2 VAL A 220     4415   4188   4734    210    -84   -430       C  
ATOM    390  N   GLN A 221      11.249  14.863  36.844  1.00 26.87           N  
ANISOU  390  N   GLN A 221     3418   3011   3779    352   -228   -484       N  
ATOM    391  CA  GLN A 221      12.234  14.594  37.867  1.00 28.82           C  
ANISOU  391  CA  GLN A 221     3682   3238   4029    381   -257   -467       C  
ATOM    392  C   GLN A 221      13.479  13.985  37.204  1.00 44.74           C  
ANISOU  392  C   GLN A 221     5647   5307   6044    464   -305   -569       C  
ATOM    393  O   GLN A 221      14.605  14.194  37.667  1.00 35.91           O  
ANISOU  393  O   GLN A 221     4510   4237   4896    492   -311   -577       O  
ATOM    394  CB  GLN A 221      11.658  13.720  38.981  1.00 40.60           C  
ANISOU  394  CB  GLN A 221     5241   4601   5585    368   -297   -402       C  
ATOM    395  CG  GLN A 221      11.388  14.505  40.249  1.00 45.39           C  
ANISOU  395  CG  GLN A 221     5884   5205   6156    310   -253   -303       C  
ATOM    396  CD  GLN A 221      10.429  13.819  41.196  1.00 49.50           C  
ANISOU  396  CD  GLN A 221     6463   5621   6725    272   -273   -222       C  
ATOM    397  OE1 GLN A 221       9.240  13.706  40.908  1.00 51.35           O  
ANISOU  397  OE1 GLN A 221     6708   5818   6985    229   -257   -201       O  
ATOM    398  NE2 GLN A 221      10.933  13.383  42.347  1.00 48.23           N  
ANISOU  398  NE2 GLN A 221     6336   5421   6569    282   -307   -171       N  
ATOM    399  N   ARG A 222      13.261  13.299  36.080  1.00 45.53           N  
ANISOU  399  N   ARG A 222     5717   5412   6172    503   -336   -654       N  
ATOM    400  CA  ARG A 222      14.340  12.701  35.290  1.00 46.68           C  
ANISOU  400  CA  ARG A 222     5801   5625   6312    590   -381   -771       C  
ATOM    401  C   ARG A 222      15.036  13.686  34.337  1.00 40.23           C  
ANISOU  401  C   ARG A 222     4903   4983   5399    588   -327   -814       C  
ATOM    402  O   ARG A 222      14.397  14.414  33.577  1.00 50.44           O  
ANISOU  402  O   ARG A 222     6176   6339   6649    540   -277   -799       O  
ATOM    403  CB  ARG A 222      13.826  11.474  34.513  1.00 58.74           C  
ANISOU  403  CB  ARG A 222     7326   7082   7912    640   -447   -857       C  
ATOM    404  CG  ARG A 222      13.817  10.174  35.330  1.00 63.50           C  
ANISOU  404  CG  ARG A 222     7985   7524   8620    679   -536   -853       C  
ATOM    405  CD  ARG A 222      13.553   8.937  34.455  1.00 70.27           C  
ANISOU  405  CD  ARG A 222     8827   8315   9556    744   -617   -965       C  
ATOM    406  NE  ARG A 222      12.126   8.639  34.338  1.00 71.83           N  
ANISOU  406  NE  ARG A 222     9068   8413   9810    684   -619   -923       N  
ATOM    407  CZ  ARG A 222      11.369   8.971  33.297  1.00 66.75           C  
ANISOU  407  CZ  ARG A 222     8392   7831   9138    660   -583   -961       C  
ATOM    408  NH1 ARG A 222      11.903   9.603  32.257  1.00 68.64           N  
ANISOU  408  NH1 ARG A 222     8557   8233   9290    688   -543  -1038       N  
ATOM    409  NH2 ARG A 222      10.079   8.662  33.294  1.00 57.68           N  
ANISOU  409  NH2 ARG A 222     7282   6587   8046    604   -589   -920       N  
ATOM    410  N   ASN A 223      16.357  13.680  34.375  1.00 44.26           N  
ANISOU  410  N   ASN A 223     5365   5577   5877    639   -342   -865       N  
ATOM    411  CA  ASN A 223      17.166  14.678  33.681  1.00 48.67           C  
ANISOU  411  CA  ASN A 223     5844   6308   6340    625   -289   -885       C  
ATOM    412  C   ASN A 223      17.394  15.899  34.557  1.00 34.76           C  
ANISOU  412  C   ASN A 223     4103   4566   4538    552   -235   -782       C  
ATOM    413  O   ASN A 223      18.364  16.621  34.375  1.00 42.27           O  
ANISOU  413  O   ASN A 223     4995   5639   5426    543   -208   -789       O  
ATOM    414  CB  ASN A 223      16.563  15.085  32.328  1.00 51.18           C  
ANISOU  414  CB  ASN A 223     6117   6720   6609    599   -252   -914       C  
ATOM    415  CG  ASN A 223      16.942  14.132  31.207  1.00 43.21           C  
ANISOU  415  CG  ASN A 223     5040   5781   5596    686   -298  -1053       C  
ATOM    416  OD1 ASN A 223      17.598  13.113  31.434  1.00 49.27           O  
ANISOU  416  OD1 ASN A 223     5799   6511   6411    770   -364  -1134       O  
ATOM    417  ND2 ASN A 223      16.531  14.458  29.996  1.00 27.04           N  
ANISOU  417  ND2 ASN A 223     2943   3838   3493    670   -268  -1084       N  
ATOM    418  N   HIS A 224      16.529  16.100  35.543  1.00 33.86           N  
ANISOU  418  N   HIS A 224     4068   4334   4462    501   -224   -690       N  
ATOM    419  CA  HIS A 224      16.640  17.306  36.366  1.00 32.13           C  
ANISOU  419  CA  HIS A 224     3869   4132   4208    434   -176   -602       C  
ATOM    420  C   HIS A 224      16.917  16.996  37.831  1.00 35.14           C  
ANISOU  420  C   HIS A 224     4304   4426   4622    444   -205   -558       C  
ATOM    421  O   HIS A 224      16.734  17.842  38.692  1.00 29.31           O  
ANISOU  421  O   HIS A 224     3597   3673   3867    391   -173   -485       O  
ATOM    422  CB  HIS A 224      15.416  18.203  36.153  1.00 27.78           C  
ANISOU  422  CB  HIS A 224     3346   3561   3648    357   -124   -533       C  
ATOM    423  CG  HIS A 224      15.138  18.461  34.706  1.00 25.72           C  
ANISOU  423  CG  HIS A 224     3032   3388   3350    349   -103   -571       C  
ATOM    424  ND1 HIS A 224      14.115  17.850  34.024  1.00 25.46           N  
ANISOU  424  ND1 HIS A 224     3012   3312   3348    358   -115   -596       N  
ATOM    425  CD2 HIS A 224      15.802  19.210  33.792  1.00 23.59           C  
ANISOU  425  CD2 HIS A 224     2693   3258   3014    333    -74   -588       C  
ATOM    426  CE1 HIS A 224      14.138  18.218  32.758  1.00 25.63           C  
ANISOU  426  CE1 HIS A 224     2976   3445   3319    353    -94   -630       C  
ATOM    427  NE2 HIS A 224      15.158  19.042  32.586  1.00 20.57           N  
ANISOU  427  NE2 HIS A 224     2282   2918   2614    336    -68   -622       N  
ATOM    428  N   GLU A 225      17.394  15.780  38.101  1.00 31.25           N  
ANISOU  428  N   GLU A 225     3819   3880   4174    517   -271   -606       N  
ATOM    429  CA  GLU A 225      17.759  15.390  39.461  1.00 36.83           C  
ANISOU  429  CA  GLU A 225     4574   4513   4908    534   -308   -562       C  
ATOM    430  C   GLU A 225      18.826  16.310  40.039  1.00 31.90           C  
ANISOU  430  C   GLU A 225     3918   3977   4227    521   -284   -547       C  
ATOM    431  O   GLU A 225      18.743  16.734  41.191  1.00 31.25           O  
ANISOU  431  O   GLU A 225     3877   3859   4136    487   -274   -477       O  
ATOM    432  CB  GLU A 225      18.257  13.936  39.497  1.00 39.93           C  
ANISOU  432  CB  GLU A 225     4969   4840   5362    625   -395   -624       C  
ATOM    433  CG  GLU A 225      17.348  12.948  38.767  1.00 50.05           C  
ANISOU  433  CG  GLU A 225     6270   6038   6709    646   -432   -661       C  
ATOM    434  CD  GLU A 225      17.598  12.896  37.255  1.00 58.82           C  
ANISOU  434  CD  GLU A 225     7304   7248   7796    684   -426   -772       C  
ATOM    435  OE1 GLU A 225      18.605  13.477  36.778  1.00 60.42           O  
ANISOU  435  OE1 GLU A 225     7434   7589   7934    703   -401   -822       O  
ATOM    436  OE2 GLU A 225      16.788  12.257  36.545  1.00 58.75           O  
ANISOU  436  OE2 GLU A 225     7304   7187   7832    694   -448   -809       O  
ATOM    437  N   THR A 226      19.830  16.629  39.235  1.00 35.89           N  
ANISOU  437  N   THR A 226     4343   4605   4689    546   -276   -615       N  
ATOM    438  CA  THR A 226      20.907  17.493  39.706  1.00 39.71           C  
ANISOU  438  CA  THR A 226     4787   5179   5123    529   -257   -607       C  
ATOM    439  C   THR A 226      20.399  18.893  40.061  1.00 36.47           C  
ANISOU  439  C   THR A 226     4397   4781   4680    434   -194   -526       C  
ATOM    440  O   THR A 226      20.727  19.445  41.114  1.00 37.55           O  
ANISOU  440  O   THR A 226     4554   4909   4804    410   -190   -484       O  
ATOM    441  CB  THR A 226      22.043  17.579  38.673  1.00 43.06           C  
ANISOU  441  CB  THR A 226     5109   5749   5502    565   -255   -693       C  
ATOM    442  OG1 THR A 226      22.609  16.274  38.496  1.00 50.58           O  
ANISOU  442  OG1 THR A 226     6041   6689   6490    666   -323   -781       O  
ATOM    443  CG2 THR A 226      23.127  18.552  39.149  1.00 41.42           C  
ANISOU  443  CG2 THR A 226     4855   5637   5244    533   -233   -678       C  
ATOM    444  N   ALA A 227      19.598  19.462  39.171  1.00 33.98           N  
ANISOU  444  N   ALA A 227     4074   4484   4352    385   -150   -511       N  
ATOM    445  CA  ALA A 227      18.998  20.772  39.409  1.00 32.23           C  
ANISOU  445  CA  ALA A 227     3874   4259   4112    301   -100   -439       C  
ATOM    446  C   ALA A 227      18.090  20.759  40.627  1.00 29.53           C  
ANISOU  446  C   ALA A 227     3614   3806   3801    280   -101   -377       C  
ATOM    447  O   ALA A 227      18.173  21.636  41.478  1.00 32.38           O  
ANISOU  447  O   ALA A 227     3991   4165   4147    241    -84   -337       O  
ATOM    448  CB  ALA A 227      18.230  21.222  38.189  1.00 32.21           C  
ANISOU  448  CB  ALA A 227     3853   4289   4097    263    -64   -434       C  
ATOM    449  N   PHE A 228      17.213  19.762  40.716  1.00 28.47           N  
ANISOU  449  N   PHE A 228     3525   3583   3708    305   -122   -372       N  
ATOM    450  CA  PHE A 228      16.311  19.657  41.860  1.00 27.41           C  
ANISOU  450  CA  PHE A 228     3461   3358   3597    281   -121   -308       C  
ATOM    451  C   PHE A 228      17.083  19.554  43.183  1.00 31.93           C  
ANISOU  451  C   PHE A 228     4052   3924   4157    300   -148   -289       C  
ATOM    452  O   PHE A 228      16.796  20.279  44.136  1.00 32.95           O  
ANISOU  452  O   PHE A 228     4208   4045   4266    262   -126   -242       O  
ATOM    453  CB  PHE A 228      15.360  18.466  41.680  1.00 30.04           C  
ANISOU  453  CB  PHE A 228     3832   3600   3980    301   -148   -304       C  
ATOM    454  CG  PHE A 228      14.147  18.771  40.828  1.00 29.05           C  
ANISOU  454  CG  PHE A 228     3710   3462   3865    261   -113   -295       C  
ATOM    455  CD1 PHE A 228      14.150  19.852  39.957  1.00 29.63           C  
ANISOU  455  CD1 PHE A 228     3743   3610   3904    228    -71   -306       C  
ATOM    456  CD2 PHE A 228      13.002  17.967  40.902  1.00 30.08           C  
ANISOU  456  CD2 PHE A 228     3882   3505   4043    254   -126   -271       C  
ATOM    457  CE1 PHE A 228      13.020  20.142  39.174  1.00 27.49           C  
ANISOU  457  CE1 PHE A 228     3474   3328   3641    195    -44   -295       C  
ATOM    458  CE2 PHE A 228      11.868  18.255  40.129  1.00 30.84           C  
ANISOU  458  CE2 PHE A 228     3976   3593   4147    219    -95   -266       C  
ATOM    459  CZ  PHE A 228      11.886  19.343  39.256  1.00 24.84           C  
ANISOU  459  CZ  PHE A 228     3178   2911   3350    193    -55   -280       C  
ATOM    460  N   GLN A 229      18.070  18.664  43.234  1.00 35.51           N  
ANISOU  460  N   GLN A 229     4487   4385   4621    365   -199   -330       N  
ATOM    461  CA  GLN A 229      18.928  18.543  44.421  1.00 36.53           C  
ANISOU  461  CA  GLN A 229     4627   4519   4735    390   -232   -316       C  
ATOM    462  C   GLN A 229      19.588  19.870  44.755  1.00 38.06           C  
ANISOU  462  C   GLN A 229     4786   4795   4880    351   -198   -315       C  
ATOM    463  O   GLN A 229      19.594  20.298  45.913  1.00 36.86           O  
ANISOU  463  O   GLN A 229     4663   4635   4708    332   -196   -276       O  
ATOM    464  CB  GLN A 229      19.994  17.459  44.230  1.00 45.55           C  
ANISOU  464  CB  GLN A 229     5740   5668   5898    474   -297   -375       C  
ATOM    465  CG  GLN A 229      19.635  16.108  44.863  1.00 57.07           C  
ANISOU  465  CG  GLN A 229     7258   7017   7410    517   -360   -345       C  
ATOM    466  CD  GLN A 229      19.454  16.194  46.381  1.00 61.65           C  
ANISOU  466  CD  GLN A 229     7893   7561   7972    494   -369   -262       C  
ATOM    467  OE1 GLN A 229      18.503  15.646  46.940  1.00 63.99           O  
ANISOU  467  OE1 GLN A 229     8248   7774   8293    472   -379   -195       O  
ATOM    468  NE2 GLN A 229      20.368  16.888  47.046  1.00 65.71           N  
ANISOU  468  NE2 GLN A 229     8382   8147   8437    495   -364   -267       N  
ATOM    469  N   GLY A 230      20.142  20.519  43.733  1.00 37.85           N  
ANISOU  469  N   GLY A 230     4696   4851   4834    337   -174   -358       N  
ATOM    470  CA  GLY A 230      20.705  21.848  43.888  1.00 39.29           C  
ANISOU  470  CA  GLY A 230     4844   5104   4981    286   -144   -352       C  
ATOM    471  C   GLY A 230      19.757  22.815  44.565  1.00 39.70           C  
ANISOU  471  C   GLY A 230     4942   5112   5031    225   -110   -297       C  
ATOM    472  O   GLY A 230      20.128  23.493  45.517  1.00 41.33           O  
ANISOU  472  O   GLY A 230     5153   5331   5219    206   -112   -285       O  
ATOM    473  N   MET A 231      18.520  22.883  44.081  1.00 37.55           N  
ANISOU  473  N   MET A 231     4700   4790   4778    197    -82   -271       N  
ATOM    474  CA  MET A 231      17.534  23.800  44.649  1.00 33.05           C  
ANISOU  474  CA  MET A 231     4167   4182   4208    146    -51   -229       C  
ATOM    475  C   MET A 231      17.119  23.451  46.066  1.00 36.57           C  
ANISOU  475  C   MET A 231     4665   4583   4648    157    -64   -198       C  
ATOM    476  O   MET A 231      16.990  24.334  46.917  1.00 36.33           O  
ANISOU  476  O   MET A 231     4646   4560   4600    129    -52   -186       O  
ATOM    477  CB  MET A 231      16.289  23.880  43.773  1.00 32.55           C  
ANISOU  477  CB  MET A 231     4118   4083   4167    120    -22   -212       C  
ATOM    478  CG  MET A 231      16.550  24.484  42.427  1.00 36.83           C  
ANISOU  478  CG  MET A 231     4610   4680   4704     95     -5   -228       C  
ATOM    479  SD  MET A 231      15.043  24.628  41.461  1.00 41.28           S  
ANISOU  479  SD  MET A 231     5192   5204   5289     67     24   -206       S  
ATOM    480  CE  MET A 231      14.855  22.994  40.800  1.00 26.81           C  
ANISOU  480  CE  MET A 231     3360   3353   3474    123      0   -239       C  
ATOM    481  N   LEU A 232      16.890  22.166  46.310  1.00 34.43           N  
ANISOU  481  N   LEU A 232     4423   4267   4391    196    -91   -184       N  
ATOM    482  CA  LEU A 232      16.553  21.699  47.653  1.00 38.93           C  
ANISOU  482  CA  LEU A 232     5039   4804   4948    204   -107   -141       C  
ATOM    483  C   LEU A 232      17.606  22.178  48.658  1.00 41.44           C  
ANISOU  483  C   LEU A 232     5344   5174   5227    216   -126   -152       C  
ATOM    484  O   LEU A 232      17.281  22.726  49.714  1.00 43.40           O  
ANISOU  484  O   LEU A 232     5613   5433   5444    195   -115   -130       O  
ATOM    485  CB  LEU A 232      16.469  20.175  47.663  1.00 38.18           C  
ANISOU  485  CB  LEU A 232     4972   4652   4884    247   -151   -123       C  
ATOM    486  CG  LEU A 232      16.292  19.457  48.998  1.00 45.63           C  
ANISOU  486  CG  LEU A 232     5961   5563   5813    258   -181    -64       C  
ATOM    487  CD1 LEU A 232      14.935  19.756  49.596  1.00 49.55           C  
ANISOU  487  CD1 LEU A 232     6491   6040   6294    206   -142     -9       C  
ATOM    488  CD2 LEU A 232      16.474  17.965  48.786  1.00 49.00           C  
ANISOU  488  CD2 LEU A 232     6407   5923   6287    305   -240    -54       C  
ATOM    489  N   ARG A 233      18.866  21.980  48.293  1.00 40.16           N  
ANISOU  489  N   ARG A 233     5141   5053   5064    251   -156   -194       N  
ATOM    490  CA  ARG A 233      20.009  22.376  49.113  1.00 47.71           C  
ANISOU  490  CA  ARG A 233     6074   6067   5988    265   -180   -214       C  
ATOM    491  C   ARG A 233      20.030  23.882  49.373  1.00 50.54           C  
ANISOU  491  C   ARG A 233     6414   6464   6326    211   -148   -227       C  
ATOM    492  O   ARG A 233      20.137  24.320  50.521  1.00 50.83           O  
ANISOU  492  O   ARG A 233     6464   6518   6332    206   -155   -221       O  
ATOM    493  CB  ARG A 233      21.310  21.915  48.441  1.00 53.27           C  
ANISOU  493  CB  ARG A 233     6724   6818   6699    311   -213   -266       C  
ATOM    494  CG  ARG A 233      22.586  22.283  49.182  1.00 64.55           C  
ANISOU  494  CG  ARG A 233     8117   8313   8096    328   -241   -294       C  
ATOM    495  CD  ARG A 233      23.798  21.551  48.602  1.00 72.47           C  
ANISOU  495  CD  ARG A 233     9066   9362   9107    388   -282   -346       C  
ATOM    496  NE  ARG A 233      23.842  21.595  47.139  1.00 76.54           N  
ANISOU  496  NE  ARG A 233     9535   9908   9641    381   -257   -383       N  
ATOM    497  CZ  ARG A 233      23.560  20.560  46.352  1.00 79.07           C  
ANISOU  497  CZ  ARG A 233     9858  10193   9990    425   -274   -402       C  
ATOM    498  NH1 ARG A 233      23.215  19.394  46.885  1.00 81.67           N  
ANISOU  498  NH1 ARG A 233    10239  10444  10347    476   -318   -380       N  
ATOM    499  NH2 ARG A 233      23.625  20.683  45.032  1.00 75.96           N  
ANISOU  499  NH2 ARG A 233     9414   9847   9599    417   -250   -440       N  
ATOM    500  N   LYS A 234      19.908  24.668  48.307  1.00 51.26           N  
ANISOU  500  N   LYS A 234     6473   6567   6435    172   -117   -243       N  
ATOM    501  CA  LYS A 234      19.953  26.126  48.410  1.00 51.94           C  
ANISOU  501  CA  LYS A 234     6541   6675   6520    118    -97   -254       C  
ATOM    502  C   LYS A 234      18.770  26.712  49.176  1.00 51.17           C  
ANISOU  502  C   LYS A 234     6488   6535   6419     93    -76   -232       C  
ATOM    503  O   LYS A 234      18.910  27.725  49.858  1.00 52.25           O  
ANISOU  503  O   LYS A 234     6620   6687   6548     69    -79   -251       O  
ATOM    504  CB  LYS A 234      20.028  26.774  47.020  1.00 59.68           C  
ANISOU  504  CB  LYS A 234     7481   7674   7523     78    -74   -261       C  
ATOM    505  CG  LYS A 234      21.156  26.262  46.140  1.00 67.93           C  
ANISOU  505  CG  LYS A 234     8467   8783   8561    100    -88   -290       C  
ATOM    506  CD  LYS A 234      22.444  27.034  46.353  1.00 74.55           C  
ANISOU  506  CD  LYS A 234     9250   9692   9384     78   -104   -316       C  
ATOM    507  CE  LYS A 234      22.435  28.336  45.574  1.00 78.47           C  
ANISOU  507  CE  LYS A 234     9712  10206   9896      1    -81   -302       C  
ATOM    508  NZ  LYS A 234      23.799  28.927  45.506  1.00 82.00           N  
ANISOU  508  NZ  LYS A 234    10091  10734  10332    -28    -97   -324       N  
ATOM    509  N   LEU A 235      17.598  26.100  49.049  1.00 44.56           N  
ANISOU  509  N   LEU A 235     5689   5650   5592     98    -58   -200       N  
ATOM    510  CA  LEU A 235      16.433  26.558  49.803  1.00 42.06           C  
ANISOU  510  CA  LEU A 235     5407   5309   5266     79    -36   -184       C  
ATOM    511  C   LEU A 235      16.483  26.097  51.257  1.00 39.62           C  
ANISOU  511  C   LEU A 235     5122   5020   4910    104    -53   -170       C  
ATOM    512  O   LEU A 235      15.738  26.599  52.089  1.00 48.98           O  
ANISOU  512  O   LEU A 235     6325   6214   6072     91    -37   -168       O  
ATOM    513  CB  LEU A 235      15.125  26.097  49.156  1.00 41.26           C  
ANISOU  513  CB  LEU A 235     5330   5159   5189     69     -8   -153       C  
ATOM    514  CG  LEU A 235      14.800  26.641  47.764  1.00 45.31           C  
ANISOU  514  CG  LEU A 235     5822   5655   5739     42     12   -161       C  
ATOM    515  CD1 LEU A 235      13.512  25.984  47.228  1.00 38.83           C  
ANISOU  515  CD1 LEU A 235     5025   4790   4939     39     33   -133       C  
ATOM    516  CD2 LEU A 235      14.672  28.166  47.791  1.00 43.81           C  
ANISOU  516  CD2 LEU A 235     5617   5466   5561      4     21   -180       C  
ATOM    517  N   ASP A 236      17.334  25.122  51.549  1.00 44.07           N  
ANISOU  517  N   ASP A 236     5687   5599   5459    142    -87   -159       N  
ATOM    518  CA  ASP A 236      17.513  24.630  52.915  1.00 55.90           C  
ANISOU  518  CA  ASP A 236     7208   7124   6908    167   -112   -136       C  
ATOM    519  C   ASP A 236      16.174  24.407  53.617  1.00 57.75           C  
ANISOU  519  C   ASP A 236     7480   7346   7117    150    -86    -90       C  
ATOM    520  O   ASP A 236      15.916  24.978  54.678  1.00 60.50           O  
ANISOU  520  O   ASP A 236     7830   7739   7416    143    -79    -97       O  
ATOM    521  CB  ASP A 236      18.369  25.616  53.728  1.00 63.87           C  
ANISOU  521  CB  ASP A 236     8191   8194   7884    165   -127   -182       C  
ATOM    522  CG  ASP A 236      18.976  24.986  54.981  1.00 72.36           C  
ANISOU  522  CG  ASP A 236     9278   9313   8904    202   -166   -163       C  
ATOM    523  OD1 ASP A 236      18.816  23.761  55.192  1.00 72.97           O  
ANISOU  523  OD1 ASP A 236     9385   9367   8974    228   -185   -108       O  
ATOM    524  OD2 ASP A 236      19.624  25.723  55.755  1.00 78.68           O  
ANISOU  524  OD2 ASP A 236    10057  10168   9670    204   -182   -203       O  
ATOM    525  N   ILE A 237      15.317  23.587  53.021  1.00 56.21           N  
ANISOU  525  N   ILE A 237     7307   7097   6953    144    -74    -48       N  
ATOM    526  CA  ILE A 237      14.014  23.313  53.614  1.00 53.43           C  
ANISOU  526  CA  ILE A 237     6982   6740   6578    121    -48      1       C  
ATOM    527  C   ILE A 237      14.188  22.387  54.816  1.00 57.17           C  
ANISOU  527  C   ILE A 237     7482   7238   7002    137    -78     62       C  
ATOM    528  O   ILE A 237      14.568  21.225  54.669  1.00 61.06           O  
ANISOU  528  O   ILE A 237     7994   7688   7517    159   -117    103       O  
ATOM    529  CB  ILE A 237      13.040  22.723  52.579  1.00 49.88           C  
ANISOU  529  CB  ILE A 237     6545   6225   6182    103    -29     27       C  
ATOM    530  CG1 ILE A 237      12.837  23.724  51.438  1.00 47.39           C  
ANISOU  530  CG1 ILE A 237     6204   5897   5906     85      0    -25       C  
ATOM    531  CG2 ILE A 237      11.708  22.373  53.235  1.00 47.20           C  
ANISOU  531  CG2 ILE A 237     6228   5889   5818     73     -2     83       C  
ATOM    532  CD1 ILE A 237      12.240  23.125  50.182  1.00 52.13           C  
ANISOU  532  CD1 ILE A 237     6808   6441   6560     78      7    -15       C  
ATOM    533  N   LYS A 238      13.912  22.914  56.004  1.00 56.12           N  
ANISOU  533  N   LYS A 238     7347   7175   6800    127    -65     65       N  
ATOM    534  CA  LYS A 238      14.296  22.232  57.235  1.00 66.02           C  
ANISOU  534  CA  LYS A 238     8618   8476   7990    144    -97    119       C  
ATOM    535  C   LYS A 238      13.239  21.285  57.810  1.00 66.12           C  
ANISOU  535  C   LYS A 238     8660   8487   7974    116    -89    217       C  
ATOM    536  O   LYS A 238      13.571  20.334  58.522  1.00 65.91           O  
ANISOU  536  O   LYS A 238     8658   8467   7919    126   -129    289       O  
ATOM    537  CB  LYS A 238      14.784  23.247  58.279  1.00 70.87           C  
ANISOU  537  CB  LYS A 238     9209   9185   8534    154    -98     67       C  
ATOM    538  CG  LYS A 238      16.279  23.542  58.149  1.00 73.72           C  
ANISOU  538  CG  LYS A 238     9549   9554   8908    189   -139     12       C  
ATOM    539  CD  LYS A 238      16.699  24.876  58.745  1.00 74.13           C  
ANISOU  539  CD  LYS A 238     9567   9675   8922    189   -135    -70       C  
ATOM    540  CE  LYS A 238      18.224  25.015  58.673  1.00 76.24           C  
ANISOU  540  CE  LYS A 238     9810   9956   9201    219   -181   -114       C  
ATOM    541  NZ  LYS A 238      18.726  26.414  58.825  1.00 77.51           N  
ANISOU  541  NZ  LYS A 238     9934  10155   9362    209   -181   -205       N  
ATOM    542  N   ASN A 239      11.972  21.530  57.490  1.00 61.60           N  
ANISOU  542  N   ASN A 239     8084   7907   7413     77    -40    223       N  
ATOM    543  CA  ASN A 239      10.904  20.692  58.015  1.00 57.78           C  
ANISOU  543  CA  ASN A 239     7619   7431   6902     39    -27    317       C  
ATOM    544  C   ASN A 239       9.594  20.792  57.231  1.00 53.30           C  
ANISOU  544  C   ASN A 239     7044   6827   6379      1     20    316       C  
ATOM    545  O   ASN A 239       9.439  21.643  56.356  1.00 46.16           O  
ANISOU  545  O   ASN A 239     6121   5900   5518      5     45    240       O  
ATOM    546  CB  ASN A 239      10.688  20.962  59.513  1.00 57.97           C  
ANISOU  546  CB  ASN A 239     7633   7578   6815     29    -14    345       C  
ATOM    547  CG  ASN A 239      10.164  22.360  59.792  1.00 58.19           C  
ANISOU  547  CG  ASN A 239     7621   7687   6800     27     35    256       C  
ATOM    548  OD1 ASN A 239       9.145  22.771  59.247  1.00 51.70           O  
ANISOU  548  OD1 ASN A 239     6785   6851   6007      3     78    231       O  
ATOM    549  ND2 ASN A 239      10.853  23.091  60.661  1.00 64.31           N  
ANISOU  549  ND2 ASN A 239     8378   8547   7510     54     24    202       N  
ATOM    550  N   GLU A 240       8.664  19.900  57.551  1.00 47.16           N  
ANISOU  550  N   GLU A 240     6282   6046   5592    -41     27    407       N  
ATOM    551  CA  GLU A 240       7.389  19.801  56.857  1.00 45.78           C  
ANISOU  551  CA  GLU A 240     6098   5836   5459    -82     65    418       C  
ATOM    552  C   GLU A 240       6.647  21.133  56.794  1.00 43.74           C  
ANISOU  552  C   GLU A 240     5800   5643   5176    -86    123    337       C  
ATOM    553  O   GLU A 240       5.784  21.319  55.935  1.00 41.15           O  
ANISOU  553  O   GLU A 240     5459   5277   4897   -104    150    315       O  
ATOM    554  CB  GLU A 240       6.499  18.768  57.553  1.00 48.86           C  
ANISOU  554  CB  GLU A 240     6501   6245   5820   -136     67    536       C  
ATOM    555  CG  GLU A 240       6.067  19.214  58.935  1.00 53.55           C  
ANISOU  555  CG  GLU A 240     7069   6982   6295   -157    101    562       C  
ATOM    556  CD  GLU A 240       5.236  18.184  59.658  1.00 59.49           C  
ANISOU  556  CD  GLU A 240     7829   7768   7009   -221    103    693       C  
ATOM    557  OE1 GLU A 240       5.043  17.081  59.111  1.00 57.16           O  
ANISOU  557  OE1 GLU A 240     7564   7366   6790   -250     69    767       O  
ATOM    558  OE2 GLU A 240       4.783  18.483  60.781  1.00 64.81           O  
ANISOU  558  OE2 GLU A 240     8474   8578   7575   -244    136    721       O  
ATOM    559  N   ASP A 241       6.973  22.051  57.706  1.00 45.08           N  
ANISOU  559  N   ASP A 241     5948   5908   5271    -65    134    288       N  
ATOM    560  CA  ASP A 241       6.245  23.322  57.826  1.00 47.33           C  
ANISOU  560  CA  ASP A 241     6194   6258   5531    -63    179    206       C  
ATOM    561  C   ASP A 241       6.955  24.492  57.142  1.00 46.06           C  
ANISOU  561  C   ASP A 241     6024   6060   5419    -26    169    101       C  
ATOM    562  O   ASP A 241       6.382  25.572  56.990  1.00 46.43           O  
ANISOU  562  O   ASP A 241     6043   6127   5473    -20    195     28       O  
ATOM    563  CB  ASP A 241       6.011  23.682  59.299  1.00 45.73           C  
ANISOU  563  CB  ASP A 241     5965   6195   5214    -63    198    204       C  
ATOM    564  CG  ASP A 241       4.992  22.784  59.969  1.00 42.60           C  
ANISOU  564  CG  ASP A 241     5563   5864   4760   -113    223    305       C  
ATOM    565  OD1 ASP A 241       3.936  22.520  59.356  1.00 46.80           O  
ANISOU  565  OD1 ASP A 241     6085   6363   5332   -148    252    329       O  
ATOM    566  OD2 ASP A 241       5.251  22.351  61.114  1.00 45.33           O  
ANISOU  566  OD2 ASP A 241     5910   6298   5017   -121    213    365       O  
ATOM    567  N   ASP A 242       8.203  24.271  56.755  1.00 43.20           N  
ANISOU  567  N   ASP A 242     5680   5643   5089     -3    128     96       N  
ATOM    568  CA  ASP A 242       9.033  25.308  56.149  1.00 44.43           C  
ANISOU  568  CA  ASP A 242     5824   5770   5287     22    113     12       C  
ATOM    569  C   ASP A 242       8.718  25.436  54.665  1.00 41.44           C  
ANISOU  569  C   ASP A 242     5445   5305   4994     12    122     -4       C  
ATOM    570  O   ASP A 242       9.476  24.960  53.817  1.00 48.52           O  
ANISOU  570  O   ASP A 242     6353   6144   5938     21     97      6       O  
ATOM    571  CB  ASP A 242      10.513  24.963  56.348  1.00 51.61           C  
ANISOU  571  CB  ASP A 242     6745   6674   6190     49     67     15       C  
ATOM    572  CG  ASP A 242      11.429  26.151  56.107  1.00 60.05           C  
ANISOU  572  CG  ASP A 242     7792   7744   7280     67     52    -70       C  
ATOM    573  OD1 ASP A 242      10.924  27.287  55.976  1.00 60.28           O  
ANISOU  573  OD1 ASP A 242     7801   7779   7324     60     71   -131       O  
ATOM    574  OD2 ASP A 242      12.658  25.946  56.050  1.00 66.10           O  
ANISOU  574  OD2 ASP A 242     8559   8504   8053     87     15    -76       O  
ATOM    575  N   VAL A 243       7.591  26.073  54.357  1.00 38.14           N  
ANISOU  575  N   VAL A 243     5010   4888   4592     -2    156    -30       N  
ATOM    576  CA  VAL A 243       7.077  26.120  52.987  1.00 37.83           C  
ANISOU  576  CA  VAL A 243     4971   4778   4626    -15    166    -35       C  
ATOM    577  C   VAL A 243       6.989  27.538  52.452  1.00 41.01           C  
ANISOU  577  C   VAL A 243     5352   5166   5064     -8    170   -107       C  
ATOM    578  O   VAL A 243       6.666  27.738  51.289  1.00 44.50           O  
ANISOU  578  O   VAL A 243     5791   5554   5561    -17    173   -112       O  
ATOM    579  CB  VAL A 243       5.657  25.506  52.887  1.00 49.93           C  
ANISOU  579  CB  VAL A 243     6500   6310   6159    -42    198      8       C  
ATOM    580  CG1 VAL A 243       5.652  24.061  53.368  1.00 54.13           C  
ANISOU  580  CG1 VAL A 243     7056   6843   6669    -59    188     94       C  
ATOM    581  CG2 VAL A 243       4.649  26.342  53.679  1.00 46.05           C  
ANISOU  581  CG2 VAL A 243     5980   5892   5624    -44    231    -29       C  
ATOM    582  N   LYS A 244       7.254  28.523  53.301  1.00 38.28           N  
ANISOU  582  N   LYS A 244     4991   4866   4688      7    163   -163       N  
ATOM    583  CA  LYS A 244       7.140  29.914  52.878  1.00 40.26           C  
ANISOU  583  CA  LYS A 244     5224   5090   4982     13    155   -231       C  
ATOM    584  C   LYS A 244       8.068  30.222  51.710  1.00 42.53           C  
ANISOU  584  C   LYS A 244     5515   5312   5330      3    130   -231       C  
ATOM    585  O   LYS A 244       7.663  30.895  50.768  1.00 41.25           O  
ANISOU  585  O   LYS A 244     5347   5104   5223     -7    129   -244       O  
ATOM    586  CB  LYS A 244       7.425  30.880  54.031  1.00 44.34           C  
ANISOU  586  CB  LYS A 244     5724   5662   5462     34    141   -301       C  
ATOM    587  CG  LYS A 244       6.290  31.038  55.036  1.00 54.03           C  
ANISOU  587  CG  LYS A 244     6930   6965   6633     47    168   -329       C  
ATOM    588  CD  LYS A 244       6.501  32.299  55.864  1.00 60.09           C  
ANISOU  588  CD  LYS A 244     7675   7770   7388     76    145   -428       C  
ATOM    589  CE  LYS A 244       5.602  32.342  57.092  1.00 65.70           C  
ANISOU  589  CE  LYS A 244     8356   8592   8016     96    171   -464       C  
ATOM    590  NZ  LYS A 244       6.211  31.628  58.255  1.00 66.49           N  
ANISOU  590  NZ  LYS A 244     8458   8785   8020     99    171   -434       N  
ATOM    591  N   SER A 245       9.306  29.732  51.770  1.00 41.23           N  
ANISOU  591  N   SER A 245     5358   5155   5154      7    108   -214       N  
ATOM    592  CA  SER A 245      10.282  30.012  50.715  1.00 40.52           C  
ANISOU  592  CA  SER A 245     5260   5026   5110     -5     87   -215       C  
ATOM    593  C   SER A 245       9.857  29.406  49.384  1.00 39.32           C  
ANISOU  593  C   SER A 245     5112   4834   4995    -17    100   -177       C  
ATOM    594  O   SER A 245      10.057  30.016  48.325  1.00 36.54           O  
ANISOU  594  O   SER A 245     4747   4453   4685    -34     94   -182       O  
ATOM    595  CB  SER A 245      11.686  29.531  51.094  1.00 40.53           C  
ANISOU  595  CB  SER A 245     5259   5056   5085      7     61   -212       C  
ATOM    596  OG  SER A 245      11.785  28.124  50.973  1.00 47.95           O  
ANISOU  596  OG  SER A 245     6215   5996   6008     20     63   -163       O  
ATOM    597  N   LEU A 246       9.253  28.220  49.433  1.00 34.83           N  
ANISOU  597  N   LEU A 246     4559   4264   4410    -11    116   -137       N  
ATOM    598  CA  LEU A 246       8.779  27.580  48.216  1.00 33.11           C  
ANISOU  598  CA  LEU A 246     4344   4010   4228    -20    125   -110       C  
ATOM    599  C   LEU A 246       7.618  28.353  47.587  1.00 30.80           C  
ANISOU  599  C   LEU A 246     4043   3694   3967    -35    144   -122       C  
ATOM    600  O   LEU A 246       7.576  28.511  46.380  1.00 28.04           O  
ANISOU  600  O   LEU A 246     3684   3319   3652    -45    142   -118       O  
ATOM    601  CB  LEU A 246       8.388  26.121  48.457  1.00 37.09           C  
ANISOU  601  CB  LEU A 246     4867   4505   4718    -14    128    -66       C  
ATOM    602  CG  LEU A 246       7.923  25.351  47.223  1.00 40.24           C  
ANISOU  602  CG  LEU A 246     5268   4864   5158    -20    130    -49       C  
ATOM    603  CD1 LEU A 246       8.895  25.555  46.072  1.00 41.61           C  
ANISOU  603  CD1 LEU A 246     5422   5034   5353    -12    113    -72       C  
ATOM    604  CD2 LEU A 246       7.757  23.861  47.523  1.00 44.11           C  
ANISOU  604  CD2 LEU A 246     5780   5333   5648    -14    118     -7       C  
ATOM    605  N  ASER A 247       6.687  28.829  48.411  0.50 29.86           N  
ANISOU  605  N  ASER A 247     3921   3591   3832    -34    161   -138       N  
ATOM    606  N  BSER A 247       6.686  28.823  48.412  0.50 29.85           N  
ANISOU  606  N  BSER A 247     3921   3591   3831    -34    161   -138       N  
ATOM    607  CA ASER A 247       5.578  29.644  47.916  0.50 29.79           C  
ANISOU  607  CA ASER A 247     3901   3564   3856    -39    172   -158       C  
ATOM    608  CA BSER A 247       5.585  29.647  47.922  0.50 29.82           C  
ANISOU  608  CA BSER A 247     3904   3567   3860    -39    172   -158       C  
ATOM    609  C  ASER A 247       6.100  30.907  47.211  0.50 26.87           C  
ANISOU  609  C  ASER A 247     3519   3160   3528    -45    147   -184       C  
ATOM    610  C  BSER A 247       6.122  30.889  47.197  0.50 26.85           C  
ANISOU  610  C  BSER A 247     3518   3158   3526    -46    147   -183       C  
ATOM    611  O  ASER A 247       5.603  31.288  46.151  0.50 26.89           O  
ANISOU  611  O  ASER A 247     3516   3131   3571    -56    145   -176       O  
ATOM    612  O  BSER A 247       5.658  31.239  46.111  0.50 26.87           O  
ANISOU  612  O  BSER A 247     3514   3128   3568    -56    145   -174       O  
ATOM    613  CB ASER A 247       4.627  30.019  49.062  0.50 31.62           C  
ANISOU  613  CB ASER A 247     4122   3836   4057    -28    190   -187       C  
ATOM    614  CB BSER A 247       4.675  30.062  49.083  0.50 31.66           C  
ANISOU  614  CB BSER A 247     4128   3841   4062    -28    189   -189       C  
ATOM    615  OG ASER A 247       3.521  30.771  48.587  0.50 27.49           O  
ANISOU  615  OG ASER A 247     3583   3294   3568    -26    197   -213       O  
ATOM    616  OG BSER A 247       4.214  28.927  49.791  0.50 31.15           O  
ANISOU  616  OG BSER A 247     4069   3816   3952    -33    212   -151       O  
ATOM    617  N   ARG A 248       7.105  31.544  47.804  1.00 28.15           N  
ANISOU  617  N   ARG A 248     3680   3333   3684    -43    124   -211       N  
ATOM    618  CA  ARG A 248       7.711  32.740  47.219  1.00 30.89           C  
ANISOU  618  CA  ARG A 248     4017   3645   4076    -59     94   -227       C  
ATOM    619  C   ARG A 248       8.336  32.438  45.868  1.00 31.96           C  
ANISOU  619  C   ARG A 248     4145   3769   4229    -83     89   -184       C  
ATOM    620  O   ARG A 248       8.238  33.231  44.932  1.00 27.93           O  
ANISOU  620  O   ARG A 248     3626   3227   3760   -105     74   -171       O  
ATOM    621  CB  ARG A 248       8.791  33.317  48.147  1.00 28.79           C  
ANISOU  621  CB  ARG A 248     3745   3396   3797    -57     67   -263       C  
ATOM    622  CG  ARG A 248       8.248  34.054  49.388  1.00 33.86           C  
ANISOU  622  CG  ARG A 248     4385   4052   4429    -33     60   -325       C  
ATOM    623  CD  ARG A 248       9.348  34.893  50.057  1.00 36.61           C  
ANISOU  623  CD  ARG A 248     4724   4403   4783    -36     21   -371       C  
ATOM    624  NE  ARG A 248      10.372  34.061  50.689  1.00 39.70           N  
ANISOU  624  NE  ARG A 248     5117   4849   5120    -30     24   -359       N  
ATOM    625  CZ  ARG A 248      10.333  33.644  51.954  1.00 42.43           C  
ANISOU  625  CZ  ARG A 248     5464   5254   5402     -3     32   -383       C  
ATOM    626  NH1 ARG A 248       9.315  33.970  52.743  1.00 40.19           N  
ANISOU  626  NH1 ARG A 248     5177   4997   5097     20     43   -425       N  
ATOM    627  NH2 ARG A 248      11.313  32.888  52.433  1.00 43.56           N  
ANISOU  627  NH2 ARG A 248     5610   5441   5501      3     26   -364       N  
ATOM    628  N   VAL A 249       9.025  31.306  45.795  1.00 31.82           N  
ANISOU  628  N   VAL A 249     4129   3781   4179    -77     97   -164       N  
ATOM    629  CA  VAL A 249       9.681  30.866  44.569  1.00 30.13           C  
ANISOU  629  CA  VAL A 249     3901   3577   3971    -90     94   -136       C  
ATOM    630  C   VAL A 249       8.625  30.638  43.485  1.00 23.42           C  
ANISOU  630  C   VAL A 249     3051   2708   3140    -95    109   -115       C  
ATOM    631  O   VAL A 249       8.780  31.068  42.349  1.00 25.38           O  
ANISOU  631  O   VAL A 249     3281   2956   3405   -116    102    -96       O  
ATOM    632  CB  VAL A 249      10.516  29.575  44.829  1.00 27.25           C  
ANISOU  632  CB  VAL A 249     3537   3246   3571    -68     94   -132       C  
ATOM    633  CG1 VAL A 249      10.963  28.919  43.521  1.00 27.42           C  
ANISOU  633  CG1 VAL A 249     3539   3286   3595    -68     93   -119       C  
ATOM    634  CG2 VAL A 249      11.716  29.892  45.714  1.00 27.31           C  
ANISOU  634  CG2 VAL A 249     3537   3281   3560    -64     74   -153       C  
ATOM    635  N   MET A 250       7.540  29.964  43.842  1.00 21.95           N  
ANISOU  635  N   MET A 250     2880   2511   2949    -79    129   -114       N  
ATOM    636  CA  MET A 250       6.478  29.691  42.877  1.00 27.95           C  
ANISOU  636  CA  MET A 250     3637   3255   3728    -83    141    -99       C  
ATOM    637  C   MET A 250       5.842  30.988  42.350  1.00 26.23           C  
ANISOU  637  C   MET A 250     3411   3011   3545    -97    132   -100       C  
ATOM    638  O   MET A 250       5.640  31.132  41.155  1.00 23.32           O  
ANISOU  638  O   MET A 250     3030   2639   3190   -109    127    -79       O  
ATOM    639  CB  MET A 250       5.409  28.786  43.496  1.00 27.49           C  
ANISOU  639  CB  MET A 250     3592   3192   3660    -71    162    -97       C  
ATOM    640  CG  MET A 250       5.941  27.402  43.834  1.00 29.01           C  
ANISOU  640  CG  MET A 250     3797   3394   3830    -60    161    -83       C  
ATOM    641  SD  MET A 250       4.682  26.263  44.450  1.00 38.91           S  
ANISOU  641  SD  MET A 250     5066   4638   5081    -62    180    -60       S  
ATOM    642  CE  MET A 250       4.421  26.822  46.128  1.00 33.43           C  
ANISOU  642  CE  MET A 250     4376   3977   4348    -61    194    -67       C  
ATOM    643  N   ILE A 251       5.552  31.929  43.246  1.00 24.02           N  
ANISOU  643  N   ILE A 251     3135   2714   3278    -92    124   -126       N  
ATOM    644  CA  ILE A 251       4.998  33.235  42.835  1.00 23.93           C  
ANISOU  644  CA  ILE A 251     3117   2662   3311    -99    101   -132       C  
ATOM    645  C   ILE A 251       5.982  33.927  41.911  1.00 22.47           C  
ANISOU  645  C   ILE A 251     2922   2467   3146   -131     73   -101       C  
ATOM    646  O   ILE A 251       5.613  34.489  40.876  1.00 22.66           O  
ANISOU  646  O   ILE A 251     2940   2472   3200   -148     58    -71       O  
ATOM    647  CB  ILE A 251       4.741  34.137  44.066  1.00 25.21           C  
ANISOU  647  CB  ILE A 251     3283   2810   3488    -80     88   -183       C  
ATOM    648  CG1 ILE A 251       3.636  33.544  44.947  1.00 32.21           C  
ANISOU  648  CG1 ILE A 251     4168   3724   4345    -53    119   -210       C  
ATOM    649  CG2 ILE A 251       4.391  35.574  43.649  1.00 23.19           C  
ANISOU  649  CG2 ILE A 251     3023   2496   3294    -85     48   -193       C  
ATOM    650  CD1 ILE A 251       2.300  33.449  44.269  1.00 36.49           C  
ANISOU  650  CD1 ILE A 251     4701   4256   4908    -46    131   -203       C  
ATOM    651  N   HIS A 252       7.256  33.879  42.282  1.00 24.28           N  
ANISOU  651  N   HIS A 252     3149   2720   3358   -143     66   -103       N  
ATOM    652  CA  HIS A 252       8.308  34.441  41.449  1.00 24.41           C  
ANISOU  652  CA  HIS A 252     3146   2745   3385   -183     44    -68       C  
ATOM    653  C   HIS A 252       8.380  33.821  40.051  1.00 22.21           C  
ANISOU  653  C   HIS A 252     2849   2506   3084   -197     57    -26       C  
ATOM    654  O   HIS A 252       8.486  34.538  39.064  1.00 20.00           O  
ANISOU  654  O   HIS A 252     2554   2224   2820   -231     39     15       O  
ATOM    655  CB  HIS A 252       9.666  34.323  42.153  1.00 25.02           C  
ANISOU  655  CB  HIS A 252     3215   2854   3439   -190     37    -85       C  
ATOM    656  CG  HIS A 252      10.631  35.371  41.724  1.00 33.87           C  
ANISOU  656  CG  HIS A 252     4315   3969   4586   -238      4    -60       C  
ATOM    657  ND1 HIS A 252      11.007  35.536  40.408  1.00 38.48           N  
ANISOU  657  ND1 HIS A 252     4873   4581   5167   -278      1     -5       N  
ATOM    658  CD2 HIS A 252      11.273  36.332  42.421  1.00 38.96           C  
ANISOU  658  CD2 HIS A 252     4957   4586   5261   -258    -29    -79       C  
ATOM    659  CE1 HIS A 252      11.849  36.546  40.318  1.00 28.18           C  
ANISOU  659  CE1 HIS A 252     3551   3266   3891   -327    -32     18       C  
ATOM    660  NE2 HIS A 252      12.028  37.046  41.524  1.00 39.42           N  
ANISOU  660  NE2 HIS A 252     4990   4649   5341   -316    -52    -29       N  
ATOM    661  N   VAL A 253       8.285  32.489  39.953  1.00 22.75           N  
ANISOU  661  N   VAL A 253     2917   2610   3115   -170     84    -37       N  
ATOM    662  CA  VAL A 253       8.246  31.830  38.644  1.00 22.30           C  
ANISOU  662  CA  VAL A 253     2841   2596   3037   -173     93    -15       C  
ATOM    663  C   VAL A 253       7.161  32.415  37.715  1.00 21.45           C  
ANISOU  663  C   VAL A 253     2732   2466   2953   -185     87     13       C  
ATOM    664  O   VAL A 253       7.405  32.677  36.537  1.00 23.28           O  
ANISOU  664  O   VAL A 253     2939   2734   3172   -211     79     49       O  
ATOM    665  CB  VAL A 253       8.017  30.287  38.769  1.00 22.92           C  
ANISOU  665  CB  VAL A 253     2926   2692   3091   -136    113    -42       C  
ATOM    666  CG1 VAL A 253       7.652  29.686  37.400  1.00 21.63           C  
ANISOU  666  CG1 VAL A 253     2742   2563   2914   -133    118    -34       C  
ATOM    667  CG2 VAL A 253       9.254  29.606  39.357  1.00 22.74           C  
ANISOU  667  CG2 VAL A 253     2897   2701   3041   -121    111    -63       C  
ATOM    668  N   PHE A 254       5.961  32.602  38.255  1.00 22.34           N  
ANISOU  668  N   PHE A 254     2866   2529   3094   -166     90     -4       N  
ATOM    669  CA  PHE A 254       4.857  33.159  37.487  1.00 22.05           C  
ANISOU  669  CA  PHE A 254     2827   2467   3084   -169     79     16       C  
ATOM    670  C   PHE A 254       4.879  34.680  37.301  1.00 26.70           C  
ANISOU  670  C   PHE A 254     3417   3011   3716   -195     41     46       C  
ATOM    671  O   PHE A 254       3.993  35.225  36.632  1.00 26.56           O  
ANISOU  671  O   PHE A 254     3399   2968   3725   -195     23     69       O  
ATOM    672  CB  PHE A 254       3.522  32.739  38.129  1.00 21.01           C  
ANISOU  672  CB  PHE A 254     2709   2309   2966   -137     96    -18       C  
ATOM    673  CG  PHE A 254       3.248  31.241  38.030  1.00 24.49           C  
ANISOU  673  CG  PHE A 254     3149   2780   3377   -120    124    -33       C  
ATOM    674  CD1 PHE A 254       3.142  30.632  36.797  1.00 22.88           C  
ANISOU  674  CD1 PHE A 254     2928   2609   3157   -123    125    -19       C  
ATOM    675  CD2 PHE A 254       3.058  30.478  39.167  1.00 25.35           C  
ANISOU  675  CD2 PHE A 254     3272   2884   3477   -104    143    -59       C  
ATOM    676  CE1 PHE A 254       2.885  29.268  36.688  1.00 31.29           C  
ANISOU  676  CE1 PHE A 254     3992   3689   4208   -108    140    -40       C  
ATOM    677  CE2 PHE A 254       2.784  29.113  39.076  1.00 30.47           C  
ANISOU  677  CE2 PHE A 254     3922   3545   4111    -95    159    -64       C  
ATOM    678  CZ  PHE A 254       2.699  28.509  37.832  1.00 29.72           C  
ANISOU  678  CZ  PHE A 254     3811   3470   4011    -95    155    -59       C  
ATOM    679  N   SER A 255       5.888  35.355  37.850  1.00 24.21           N  
ANISOU  679  N   SER A 255     3103   2682   3413   -217     22     48       N  
ATOM    680  CA  SER A 255       5.909  36.828  37.875  1.00 27.60           C  
ANISOU  680  CA  SER A 255     3538   3048   3901   -242    -25     70       C  
ATOM    681  C   SER A 255       6.266  37.512  36.555  1.00 28.30           C  
ANISOU  681  C   SER A 255     3610   3146   3997   -293    -54    150       C  
ATOM    682  O   SER A 255       6.136  38.741  36.447  1.00 24.69           O  
ANISOU  682  O   SER A 255     3160   2621   3598   -317   -103    180       O  
ATOM    683  CB  SER A 255       6.798  37.375  39.014  1.00 25.58           C  
ANISOU  683  CB  SER A 255     3289   2766   3665   -251    -43     38       C  
ATOM    684  OG  SER A 255       8.192  37.299  38.688  1.00 23.46           O  
ANISOU  684  OG  SER A 255     2999   2546   3369   -294    -43     70       O  
ATOM    685  N   ASP A 256       6.690  36.726  35.559  1.00 24.36           N  
ANISOU  685  N   ASP A 256     3086   2731   3439   -309    -28    182       N  
ATOM    686  CA  ASP A 256       6.877  37.237  34.197  1.00 26.85           C  
ANISOU  686  CA  ASP A 256     3378   3082   3742   -356    -49    262       C  
ATOM    687  C   ASP A 256       5.549  37.301  33.442  1.00 22.37           C  
ANISOU  687  C   ASP A 256     2817   2496   3186   -334    -58    280       C  
ATOM    688  O   ASP A 256       5.479  37.746  32.301  1.00 26.79           O  
ANISOU  688  O   ASP A 256     3361   3084   3735   -367    -79    351       O  
ATOM    689  CB  ASP A 256       7.895  36.406  33.403  1.00 22.46           C  
ANISOU  689  CB  ASP A 256     2782   2644   3109   -377    -19    280       C  
ATOM    690  CG  ASP A 256       7.470  34.933  33.238  1.00 23.44           C  
ANISOU  690  CG  ASP A 256     2900   2822   3185   -324     23    224       C  
ATOM    691  OD1 ASP A 256       6.451  34.506  33.826  1.00 23.93           O  
ANISOU  691  OD1 ASP A 256     2990   2832   3271   -280     32    178       O  
ATOM    692  OD2 ASP A 256       8.182  34.201  32.511  1.00 23.36           O  
ANISOU  692  OD2 ASP A 256     2853   2909   3113   -329     42    224       O  
ATOM    693  N   GLY A 257       4.504  36.817  34.085  1.00 22.99           N  
ANISOU  693  N   GLY A 257     2915   2538   3281   -280    -42    219       N  
ATOM    694  CA  GLY A 257       3.172  36.884  33.528  1.00 29.81           C  
ANISOU  694  CA  GLY A 257     3783   3382   4162   -255    -52    223       C  
ATOM    695  C   GLY A 257       2.818  35.707  32.642  1.00 31.77           C  
ANISOU  695  C   GLY A 257     4009   3710   4350   -240    -20    217       C  
ATOM    696  O   GLY A 257       1.768  35.689  32.011  1.00 32.63           O  
ANISOU  696  O   GLY A 257     4115   3818   4465   -223    -28    224       O  
ATOM    697  N   VAL A 258       3.690  34.714  32.596  1.00 23.96           N  
ANISOU  697  N   VAL A 258     3005   2789   3308   -243     13    197       N  
ATOM    698  CA  VAL A 258       3.447  33.553  31.743  1.00 22.58           C  
ANISOU  698  CA  VAL A 258     2807   2688   3082   -225     37    178       C  
ATOM    699  C   VAL A 258       2.891  32.413  32.586  1.00 23.33           C  
ANISOU  699  C   VAL A 258     2917   2761   3184   -183     66    108       C  
ATOM    700  O   VAL A 258       3.409  32.122  33.671  1.00 23.17           O  
ANISOU  700  O   VAL A 258     2913   2718   3172   -175     80     78       O  
ATOM    701  CB  VAL A 258       4.750  33.085  31.018  1.00 25.02           C  
ANISOU  701  CB  VAL A 258     3082   3098   3327   -248     49    192       C  
ATOM    702  CG1 VAL A 258       4.534  31.759  30.299  1.00 26.46           C  
ANISOU  702  CG1 VAL A 258     3240   3351   3462   -217     69    147       C  
ATOM    703  CG2 VAL A 258       5.255  34.157  30.046  1.00 28.47           C  
ANISOU  703  CG2 VAL A 258     3495   3577   3745   -301     23    277       C  
ATOM    704  N   THR A 259       1.837  31.769  32.087  1.00 23.75           N  
ANISOU  704  N   THR A 259     2964   2823   3235   -161     72     87       N  
ATOM    705  CA  THR A 259       1.260  30.607  32.764  1.00 26.18           C  
ANISOU  705  CA  THR A 259     3283   3113   3552   -132     95     31       C  
ATOM    706  C   THR A 259       1.117  29.448  31.791  1.00 24.71           C  
ANISOU  706  C   THR A 259     3073   2981   3334   -119    100      5       C  
ATOM    707  O   THR A 259       0.558  29.606  30.703  1.00 26.55           O  
ANISOU  707  O   THR A 259     3285   3249   3553   -120     87     19       O  
ATOM    708  CB  THR A 259      -0.146  30.916  33.303  1.00 28.20           C  
ANISOU  708  CB  THR A 259     3550   3315   3851   -116     95     17       C  
ATOM    709  OG1 THR A 259      -0.131  32.177  33.972  1.00 27.15           O  
ANISOU  709  OG1 THR A 259     3431   3133   3751   -121     78     34       O  
ATOM    710  CG2 THR A 259      -0.620  29.818  34.267  1.00 29.11           C  
ANISOU  710  CG2 THR A 259     3675   3410   3975   -100    121    -26       C  
ATOM    711  N   ASN A 260       1.620  28.279  32.166  1.00 24.50           N  
ANISOU  711  N   ASN A 260     3049   2962   3297   -104    113    -35       N  
ATOM    712  CA  ASN A 260       1.385  27.093  31.336  1.00 24.63           C  
ANISOU  712  CA  ASN A 260     3045   3016   3298    -85    109    -76       C  
ATOM    713  C   ASN A 260       1.474  25.823  32.181  1.00 24.69           C  
ANISOU  713  C   ASN A 260     3070   2982   3328    -67    115   -118       C  
ATOM    714  O   ASN A 260       1.899  25.876  33.321  1.00 20.51           O  
ANISOU  714  O   ASN A 260     2566   2415   2812    -69    124   -110       O  
ATOM    715  CB  ASN A 260       2.317  27.057  30.106  1.00 23.36           C  
ANISOU  715  CB  ASN A 260     2846   2949   3080    -85     99    -77       C  
ATOM    716  CG  ASN A 260       3.815  27.038  30.472  1.00 23.93           C  
ANISOU  716  CG  ASN A 260     2913   3052   3126    -87    105    -78       C  
ATOM    717  OD1 ASN A 260       4.258  26.248  31.303  1.00 25.89           O  
ANISOU  717  OD1 ASN A 260     3178   3268   3392    -68    108   -112       O  
ATOM    718  ND2 ASN A 260       4.598  27.912  29.824  1.00 25.02           N  
ANISOU  718  ND2 ASN A 260     3024   3259   3223   -114    102    -35       N  
ATOM    719  N   TRP A 261       1.057  24.693  31.621  1.00 21.95           N  
ANISOU  719  N   TRP A 261     2711   2640   2988    -49    104   -161       N  
ATOM    720  CA  TRP A 261       1.023  23.441  32.350  1.00 22.88           C  
ANISOU  720  CA  TRP A 261     2848   2705   3139    -37     98   -192       C  
ATOM    721  C   TRP A 261       2.416  22.855  32.576  1.00 21.66           C  
ANISOU  721  C   TRP A 261     2696   2566   2970    -15     88   -216       C  
ATOM    722  O   TRP A 261       2.647  22.177  33.555  1.00 22.68           O  
ANISOU  722  O   TRP A 261     2851   2642   3125     -9     84   -218       O  
ATOM    723  CB  TRP A 261       0.111  22.444  31.612  1.00 21.10           C  
ANISOU  723  CB  TRP A 261     2607   2471   2938    -28     79   -235       C  
ATOM    724  CG  TRP A 261      -1.371  22.728  31.831  1.00 25.00           C  
ANISOU  724  CG  TRP A 261     3104   2932   3464    -50     90   -215       C  
ATOM    725  CD1 TRP A 261      -2.278  23.103  30.883  1.00 24.57           C  
ANISOU  725  CD1 TRP A 261     3023   2910   3403    -53     84   -220       C  
ATOM    726  CD2 TRP A 261      -2.090  22.681  33.079  1.00 24.33           C  
ANISOU  726  CD2 TRP A 261     3042   2788   3413    -72    108   -189       C  
ATOM    727  NE1 TRP A 261      -3.510  23.272  31.454  1.00 23.52           N  
ANISOU  727  NE1 TRP A 261     2894   2737   3304    -71     96   -204       N  
ATOM    728  CE2 TRP A 261      -3.425  23.007  32.799  1.00 24.28           C  
ANISOU  728  CE2 TRP A 261     3018   2783   3423    -85    113   -185       C  
ATOM    729  CE3 TRP A 261      -1.728  22.367  34.398  1.00 23.20           C  
ANISOU  729  CE3 TRP A 261     2929   2603   3283    -81    119   -167       C  
ATOM    730  CZ2 TRP A 261      -4.416  23.047  33.791  1.00 24.70           C  
ANISOU  730  CZ2 TRP A 261     3077   2805   3504   -107    132   -166       C  
ATOM    731  CZ3 TRP A 261      -2.692  22.394  35.375  1.00 21.95           C  
ANISOU  731  CZ3 TRP A 261     2778   2415   3146   -106    138   -142       C  
ATOM    732  CH2 TRP A 261      -4.029  22.755  35.072  1.00 24.21           C  
ANISOU  732  CH2 TRP A 261     3041   2711   3447   -119    147   -144       C  
ATOM    733  N   GLY A 262       3.359  23.148  31.690  1.00 21.03           N  
ANISOU  733  N   GLY A 262     2583   2565   2842     -4     83   -229       N  
ATOM    734  CA  GLY A 262       4.732  22.714  31.909  1.00 20.86           C  
ANISOU  734  CA  GLY A 262     2554   2571   2802     19     74   -255       C  
ATOM    735  C   GLY A 262       5.303  23.298  33.202  1.00 23.28           C  
ANISOU  735  C   GLY A 262     2890   2840   3115      4     89   -214       C  
ATOM    736  O   GLY A 262       5.923  22.595  34.011  1.00 21.54           O  
ANISOU  736  O   GLY A 262     2687   2588   2910     23     78   -229       O  
ATOM    737  N   ARG A 263       5.071  24.586  33.425  1.00 23.96           N  
ANISOU  737  N   ARG A 263     2983   2928   3194    -29    107   -163       N  
ATOM    738  CA  ARG A 263       5.522  25.216  34.666  1.00 21.38           C  
ANISOU  738  CA  ARG A 263     2682   2567   2874    -43    117   -134       C  
ATOM    739  C   ARG A 263       4.833  24.600  35.865  1.00 19.48           C  
ANISOU  739  C   ARG A 263     2478   2252   2669    -39    121   -133       C  
ATOM    740  O   ARG A 263       5.458  24.338  36.892  1.00 18.45           O  
ANISOU  740  O   ARG A 263     2368   2102   2540    -31    119   -130       O  
ATOM    741  CB  ARG A 263       5.219  26.719  34.651  1.00 19.11           C  
ANISOU  741  CB  ARG A 263     2395   2279   2586    -77    126    -88       C  
ATOM    742  CG  ARG A 263       6.162  27.506  33.736  1.00 22.69           C  
ANISOU  742  CG  ARG A 263     2814   2806   3003    -97    121    -66       C  
ATOM    743  CD  ARG A 263       5.739  28.954  33.624  1.00 22.38           C  
ANISOU  743  CD  ARG A 263     2778   2748   2976   -132    117    -15       C  
ATOM    744  NE  ARG A 263       6.668  29.669  32.756  1.00 23.30           N  
ANISOU  744  NE  ARG A 263     2860   2935   3057   -163    109     21       N  
ATOM    745  CZ  ARG A 263       6.908  30.970  32.857  1.00 23.32           C  
ANISOU  745  CZ  ARG A 263     2866   2921   3074   -202     97     73       C  
ATOM    746  NH1 ARG A 263       6.281  31.687  33.786  1.00 22.32           N  
ANISOU  746  NH1 ARG A 263     2775   2709   2998   -204     89     79       N  
ATOM    747  NH2 ARG A 263       7.782  31.533  32.045  1.00 23.32           N  
ANISOU  747  NH2 ARG A 263     2830   2992   3039   -239     90    115       N  
ATOM    748  N   ILE A 264       3.531  24.398  35.738  1.00 19.83           N  
ANISOU  748  N   ILE A 264     2530   2266   2740    -46    126   -130       N  
ATOM    749  CA  ILE A 264       2.734  23.903  36.847  1.00 22.93           C  
ANISOU  749  CA  ILE A 264     2949   2602   3159    -53    134   -119       C  
ATOM    750  C   ILE A 264       3.165  22.475  37.239  1.00 22.87           C  
ANISOU  750  C   ILE A 264     2958   2564   3169    -36    114   -134       C  
ATOM    751  O   ILE A 264       3.381  22.176  38.425  1.00 21.54           O  
ANISOU  751  O   ILE A 264     2815   2367   3003    -39    115   -113       O  
ATOM    752  CB  ILE A 264       1.225  23.966  36.510  1.00 24.60           C  
ANISOU  752  CB  ILE A 264     3154   2799   3394    -68    143   -115       C  
ATOM    753  CG1 ILE A 264       0.748  25.430  36.551  1.00 23.77           C  
ANISOU  753  CG1 ILE A 264     3042   2705   3283    -81    158    -95       C  
ATOM    754  CG2 ILE A 264       0.441  23.103  37.504  1.00 19.40           C  
ANISOU  754  CG2 ILE A 264     2513   2095   2761    -82    150   -104       C  
ATOM    755  CD1 ILE A 264      -0.602  25.692  35.890  1.00 19.69           C  
ANISOU  755  CD1 ILE A 264     2508   2189   2785    -87    159    -97       C  
ATOM    756  N   VAL A 265       3.335  21.611  36.243  1.00 23.73           N  
ANISOU  756  N   VAL A 265     3050   2680   3287    -15     89   -173       N  
ATOM    757  CA  VAL A 265       3.721  20.226  36.532  1.00 25.74           C  
ANISOU  757  CA  VAL A 265     3319   2890   3571      8     56   -194       C  
ATOM    758  C   VAL A 265       5.129  20.184  37.118  1.00 25.71           C  
ANISOU  758  C   VAL A 265     3322   2901   3547     32     45   -197       C  
ATOM    759  O   VAL A 265       5.437  19.354  37.970  1.00 26.70           O  
ANISOU  759  O   VAL A 265     3473   2977   3693     43     23   -187       O  
ATOM    760  CB  VAL A 265       3.598  19.304  35.282  1.00 25.17           C  
ANISOU  760  CB  VAL A 265     3222   2822   3520     33     24   -254       C  
ATOM    761  CG1 VAL A 265       4.781  19.469  34.332  1.00 21.86           C  
ANISOU  761  CG1 VAL A 265     2766   2481   3060     70     13   -302       C  
ATOM    762  CG2 VAL A 265       3.492  17.843  35.711  1.00 31.69           C  
ANISOU  762  CG2 VAL A 265     4071   3566   4403     46    -18   -267       C  
ATOM    763  N   THR A 266       5.983  21.110  36.693  1.00 22.91           N  
ANISOU  763  N   THR A 266     2942   2614   3150     37     58   -205       N  
ATOM    764  CA  THR A 266       7.349  21.166  37.210  1.00 19.47           C  
ANISOU  764  CA  THR A 266     2504   2204   2692     58     48   -212       C  
ATOM    765  C   THR A 266       7.352  21.571  38.673  1.00 20.33           C  
ANISOU  765  C   THR A 266     2647   2280   2798     39     62   -166       C  
ATOM    766  O   THR A 266       8.102  21.018  39.478  1.00 21.51           O  
ANISOU  766  O   THR A 266     2811   2412   2948     60     41   -164       O  
ATOM    767  CB  THR A 266       8.232  22.117  36.351  1.00 23.64           C  
ANISOU  767  CB  THR A 266     2988   2821   3173     56     60   -225       C  
ATOM    768  OG1 THR A 266       8.298  21.608  35.016  1.00 25.76           O  
ANISOU  768  OG1 THR A 266     3218   3138   3431     79     46   -273       O  
ATOM    769  CG2 THR A 266       9.655  22.236  36.892  1.00 22.87           C  
ANISOU  769  CG2 THR A 266     2880   2759   3052     72     51   -233       C  
ATOM    770  N   LEU A 267       6.498  22.537  39.029  1.00 22.17           N  
ANISOU  770  N   LEU A 267     2889   2508   3027      5     92   -133       N  
ATOM    771  CA  LEU A 267       6.379  22.961  40.424  1.00 23.82           C  
ANISOU  771  CA  LEU A 267     3124   2699   3228    -10    106   -100       C  
ATOM    772  C   LEU A 267       5.863  21.834  41.291  1.00 25.25           C  
ANISOU  772  C   LEU A 267     3334   2831   3428    -11     95    -77       C  
ATOM    773  O   LEU A 267       6.342  21.621  42.408  1.00 25.50           O  
ANISOU  773  O   LEU A 267     3386   2857   3446     -6     88    -56       O  
ATOM    774  CB  LEU A 267       5.463  24.188  40.564  1.00 21.57           C  
ANISOU  774  CB  LEU A 267     2837   2420   2940    -39    134    -84       C  
ATOM    775  CG  LEU A 267       6.001  25.436  39.854  1.00 24.55           C  
ANISOU  775  CG  LEU A 267     3190   2834   3303    -48    137    -90       C  
ATOM    776  CD1 LEU A 267       5.078  26.627  40.085  1.00 29.55           C  
ANISOU  776  CD1 LEU A 267     3826   3457   3947    -68    153    -78       C  
ATOM    777  CD2 LEU A 267       7.389  25.751  40.378  1.00 26.86           C  
ANISOU  777  CD2 LEU A 267     3479   3152   3573    -41    127    -96       C  
ATOM    778  N   ILE A 268       4.864  21.123  40.787  1.00 21.82           N  
ANISOU  778  N   ILE A 268     2901   2363   3026    -20     91    -76       N  
ATOM    779  CA  ILE A 268       4.296  20.007  41.541  1.00 22.74           C  
ANISOU  779  CA  ILE A 268     3043   2426   3169    -33     76    -42       C  
ATOM    780  C   ILE A 268       5.332  18.890  41.675  1.00 23.38           C  
ANISOU  780  C   ILE A 268     3140   2474   3268      1     29    -51       C  
ATOM    781  O   ILE A 268       5.494  18.312  42.757  1.00 24.25           O  
ANISOU  781  O   ILE A 268     3278   2556   3379     -4     13     -9       O  
ATOM    782  CB  ILE A 268       3.018  19.439  40.898  1.00 24.19           C  
ANISOU  782  CB  ILE A 268     3221   2577   3393    -56     76    -43       C  
ATOM    783  CG1 ILE A 268       1.853  20.438  40.998  1.00 27.67           C  
ANISOU  783  CG1 ILE A 268     3647   3048   3819    -87    119    -29       C  
ATOM    784  CG2 ILE A 268       2.628  18.115  41.604  1.00 29.21           C  
ANISOU  784  CG2 ILE A 268     3884   3149   4067    -74     48     -1       C  
ATOM    785  CD1 ILE A 268       0.660  20.091  40.060  1.00 22.82           C  
ANISOU  785  CD1 ILE A 268     3013   2417   3241   -104    119    -44       C  
ATOM    786  N   SER A 269       6.037  18.595  40.584  1.00 25.95           N  
ANISOU  786  N   SER A 269     3444   2810   3606     38      3   -107       N  
ATOM    787  CA  SER A 269       7.098  17.579  40.613  1.00 26.69           C  
ANISOU  787  CA  SER A 269     3543   2877   3719     83    -48   -132       C  
ATOM    788  C   SER A 269       8.210  17.944  41.587  1.00 28.27           C  
ANISOU  788  C   SER A 269     3752   3106   3883    100    -50   -115       C  
ATOM    789  O   SER A 269       8.744  17.073  42.286  1.00 28.18           O  
ANISOU  789  O   SER A 269     3764   3054   3889    123    -91    -99       O  
ATOM    790  CB  SER A 269       7.728  17.362  39.234  1.00 31.68           C  
ANISOU  790  CB  SER A 269     4137   3545   4357    126    -69   -210       C  
ATOM    791  OG  SER A 269       6.754  16.993  38.289  1.00 39.09           O  
ANISOU  791  OG  SER A 269     5064   4463   5326    117    -73   -235       O  
ATOM    792  N   PHE A 270       8.586  19.223  41.627  1.00 25.81           N  
ANISOU  792  N   PHE A 270     3421   2861   3524     88    -13   -119       N  
ATOM    793  CA  PHE A 270       9.573  19.630  42.614  1.00 22.51           C  
ANISOU  793  CA  PHE A 270     3009   2472   3072     98    -15   -105       C  
ATOM    794  C   PHE A 270       9.026  19.449  44.031  1.00 29.23           C  
ANISOU  794  C   PHE A 270     3898   3293   3914     74    -10    -43       C  
ATOM    795  O   PHE A 270       9.757  19.071  44.941  1.00 30.54           O  
ANISOU  795  O   PHE A 270     4081   3457   4067     93    -36    -24       O  
ATOM    796  CB  PHE A 270      10.074  21.060  42.378  1.00 21.95           C  
ANISOU  796  CB  PHE A 270     2908   2470   2961     84     17   -121       C  
ATOM    797  CG  PHE A 270      11.128  21.502  43.365  1.00 27.75           C  
ANISOU  797  CG  PHE A 270     3644   3236   3663     93     10   -116       C  
ATOM    798  CD1 PHE A 270      12.402  20.958  43.332  1.00 27.50           C  
ANISOU  798  CD1 PHE A 270     3596   3226   3627    135    -25   -146       C  
ATOM    799  CD2 PHE A 270      10.834  22.452  44.342  1.00 29.48           C  
ANISOU  799  CD2 PHE A 270     3876   3468   3856     65     35    -91       C  
ATOM    800  CE1 PHE A 270      13.369  21.359  44.242  1.00 29.65           C  
ANISOU  800  CE1 PHE A 270     3865   3531   3869    144    -34   -144       C  
ATOM    801  CE2 PHE A 270      11.808  22.860  45.260  1.00 29.84           C  
ANISOU  801  CE2 PHE A 270     3920   3547   3872     74     25    -93       C  
ATOM    802  CZ  PHE A 270      13.075  22.304  45.209  1.00 30.02           C  
ANISOU  802  CZ  PHE A 270     3927   3590   3889    112    -10   -117       C  
ATOM    803  N   GLY A 271       7.741  19.729  44.223  1.00 27.28           N  
ANISOU  803  N   GLY A 271     3660   3034   3669     33     22    -12       N  
ATOM    804  CA  GLY A 271       7.110  19.500  45.502  1.00 25.27           C  
ANISOU  804  CA  GLY A 271     3433   2769   3399      5     31     48       C  
ATOM    805  C   GLY A 271       7.232  18.040  45.939  1.00 26.91           C  
ANISOU  805  C   GLY A 271     3671   2916   3639     14    -17     89       C  
ATOM    806  O   GLY A 271       7.506  17.759  47.106  1.00 29.92           O  
ANISOU  806  O   GLY A 271     4074   3302   3993     10    -30    138       O  
ATOM    807  N   ALA A 272       7.017  17.111  45.007  1.00 25.62           N  
ANISOU  807  N   ALA A 272     3508   2694   3535     25    -50     69       N  
ATOM    808  CA  ALA A 272       7.192  15.678  45.295  1.00 27.94           C  
ANISOU  808  CA  ALA A 272     3831   2908   3878     37   -111    102       C  
ATOM    809  C   ALA A 272       8.657  15.353  45.644  1.00 30.60           C  
ANISOU  809  C   ALA A 272     4174   3246   4206     93   -158     84       C  
ATOM    810  O   ALA A 272       8.935  14.535  46.526  1.00 34.09           O  
ANISOU  810  O   ALA A 272     4647   3645   4659     98   -202    139       O  
ATOM    811  CB  ALA A 272       6.719  14.841  44.118  1.00 27.03           C  
ANISOU  811  CB  ALA A 272     3708   2728   3833     45   -143     62       C  
ATOM    812  N   PHE A 273       9.589  15.997  44.948  1.00 28.60           N  
ANISOU  812  N   PHE A 273     3888   3048   3932    133   -150     12       N  
ATOM    813  CA  PHE A 273      11.016  15.816  45.227  1.00 31.46           C  
ANISOU  813  CA  PHE A 273     4243   3429   4281    187   -190    -15       C  
ATOM    814  C   PHE A 273      11.355  16.212  46.666  1.00 33.33           C  
ANISOU  814  C   PHE A 273     4500   3698   4464    174   -182     42       C  
ATOM    815  O   PHE A 273      12.044  15.482  47.389  1.00 34.94           O  
ANISOU  815  O   PHE A 273     4725   3876   4674    205   -233     69       O  
ATOM    816  CB  PHE A 273      11.844  16.652  44.254  1.00 30.49           C  
ANISOU  816  CB  PHE A 273     4070   3382   4132    215   -169    -94       C  
ATOM    817  CG  PHE A 273      13.314  16.367  44.307  1.00 32.86           C  
ANISOU  817  CG  PHE A 273     4350   3711   4425    275   -211   -138       C  
ATOM    818  CD1 PHE A 273      13.862  15.333  43.558  1.00 32.67           C  
ANISOU  818  CD1 PHE A 273     4310   3656   4447    335   -268   -197       C  
ATOM    819  CD2 PHE A 273      14.154  17.149  45.087  1.00 32.65           C  
ANISOU  819  CD2 PHE A 273     4313   3746   4346    276   -198   -130       C  
ATOM    820  CE1 PHE A 273      15.237  15.073  43.590  1.00 37.71           C  
ANISOU  820  CE1 PHE A 273     4920   4330   5078    398   -309   -247       C  
ATOM    821  CE2 PHE A 273      15.523  16.887  45.142  1.00 33.75           C  
ANISOU  821  CE2 PHE A 273     4427   3920   4478    332   -239   -173       C  
ATOM    822  CZ  PHE A 273      16.067  15.846  44.390  1.00 35.42           C  
ANISOU  822  CZ  PHE A 273     4619   4105   4733    395   -293   -231       C  
ATOM    823  N   VAL A 274      10.853  17.370  47.078  1.00 29.25           N  
ANISOU  823  N   VAL A 274     3976   3240   3898    133   -122     58       N  
ATOM    824  CA  VAL A 274      11.053  17.860  48.431  1.00 29.91           C  
ANISOU  824  CA  VAL A 274     4073   3369   3923    119   -109    101       C  
ATOM    825  C   VAL A 274      10.414  16.898  49.441  1.00 37.83           C  
ANISOU  825  C   VAL A 274     5116   4330   4928     94   -132    189       C  
ATOM    826  O   VAL A 274      11.037  16.531  50.441  1.00 35.27           O  
ANISOU  826  O   VAL A 274     4810   4015   4575    110   -165    230       O  
ATOM    827  CB  VAL A 274      10.471  19.281  48.609  1.00 33.25           C  
ANISOU  827  CB  VAL A 274     4477   3855   4302     82    -46     88       C  
ATOM    828  CG1 VAL A 274      10.542  19.726  50.081  1.00 30.30           C  
ANISOU  828  CG1 VAL A 274     4114   3534   3863     69    -35    124       C  
ATOM    829  CG2 VAL A 274      11.204  20.277  47.698  1.00 29.19           C  
ANISOU  829  CG2 VAL A 274     3926   3381   3786     97    -31     17       C  
ATOM    830  N   ALA A 275       9.175  16.490  49.166  1.00 31.38           N  
ANISOU  830  N   ALA A 275     4309   3472   4143     52   -117    224       N  
ATOM    831  CA  ALA A 275       8.459  15.560  50.033  1.00 36.77           C  
ANISOU  831  CA  ALA A 275     5025   4116   4832     13   -136    319       C  
ATOM    832  C   ALA A 275       9.240  14.262  50.258  1.00 37.34           C  
ANISOU  832  C   ALA A 275     5128   4111   4949     49   -219    354       C  
ATOM    833  O   ALA A 275       9.323  13.779  51.382  1.00 42.28           O  
ANISOU  833  O   ALA A 275     5780   4737   5547     34   -245    437       O  
ATOM    834  CB  ALA A 275       7.066  15.253  49.467  1.00 33.00           C  
ANISOU  834  CB  ALA A 275     4545   3599   4397    -37   -113    340       C  
ATOM    835  N   LYS A 276       9.782  13.682  49.190  1.00 38.86           N  
ANISOU  835  N   LYS A 276     5314   4239   5210     97   -265    291       N  
ATOM    836  CA  LYS A 276      10.619  12.488  49.327  1.00 40.13           C  
ANISOU  836  CA  LYS A 276     5501   4322   5424    146   -354    305       C  
ATOM    837  C   LYS A 276      11.784  12.736  50.282  1.00 40.30           C  
ANISOU  837  C   LYS A 276     5526   4397   5389    184   -375    317       C  
ATOM    838  O   LYS A 276      12.089  11.905  51.134  1.00 43.35           O  
ANISOU  838  O   LYS A 276     5947   4741   5784    193   -434    390       O  
ATOM    839  CB  LYS A 276      11.199  12.054  47.982  1.00 44.40           C  
ANISOU  839  CB  LYS A 276     6019   4816   6033    208   -394    202       C  
ATOM    840  CG  LYS A 276      10.245  11.387  47.040  1.00 53.61           C  
ANISOU  840  CG  LYS A 276     7189   5903   7276    187   -408    186       C  
ATOM    841  CD  LYS A 276      11.029  10.866  45.849  1.00 62.52           C  
ANISOU  841  CD  LYS A 276     8292   7000   8463    264   -461     75       C  
ATOM    842  CE  LYS A 276      10.164  10.733  44.618  1.00 65.09           C  
ANISOU  842  CE  LYS A 276     8597   7298   8835    249   -447     19       C  
ATOM    843  NZ  LYS A 276      10.995  10.570  43.396  1.00 65.72           N  
ANISOU  843  NZ  LYS A 276     8635   7398   8938    326   -477   -106       N  
ATOM    844  N   HIS A 277      12.447  13.873  50.126  1.00 39.02           N  
ANISOU  844  N   HIS A 277     5327   4327   5171    206   -331    248       N  
ATOM    845  CA  HIS A 277      13.624  14.177  50.925  1.00 44.06           C  
ANISOU  845  CA  HIS A 277     5959   5023   5757    245   -352    243       C  
ATOM    846  C   HIS A 277      13.265  14.411  52.397  1.00 46.61           C  
ANISOU  846  C   HIS A 277     6307   5395   6008    203   -335    334       C  
ATOM    847  O   HIS A 277      14.021  14.051  53.298  1.00 53.06           O  
ANISOU  847  O   HIS A 277     7140   6224   6797    231   -381    373       O  
ATOM    848  CB  HIS A 277      14.382  15.378  50.340  1.00 44.89           C  
ANISOU  848  CB  HIS A 277     6014   5213   5827    267   -310    147       C  
ATOM    849  CG  HIS A 277      15.528  15.841  51.189  1.00 53.97           C  
ANISOU  849  CG  HIS A 277     7152   6433   6921    298   -325    137       C  
ATOM    850  ND1 HIS A 277      16.767  15.242  51.158  1.00 59.45           N  
ANISOU  850  ND1 HIS A 277     7836   7119   7634    366   -390    104       N  
ATOM    851  CD2 HIS A 277      15.618  16.852  52.087  1.00 55.17           C  
ANISOU  851  CD2 HIS A 277     7296   6667   6999    274   -287    147       C  
ATOM    852  CE1 HIS A 277      17.574  15.858  52.006  1.00 57.49           C  
ANISOU  852  CE1 HIS A 277     7574   6947   7325    378   -390    100       C  
ATOM    853  NE2 HIS A 277      16.901  16.836  52.583  1.00 55.82           N  
ANISOU  853  NE2 HIS A 277     7364   6789   7057    322   -329    125       N  
ATOM    854  N   LEU A 278      12.103  15.005  52.640  1.00 39.07           N  
ANISOU  854  N   LEU A 278     5351   4476   5018    140   -270    366       N  
ATOM    855  CA  LEU A 278      11.659  15.245  54.001  1.00 40.45           C  
ANISOU  855  CA  LEU A 278     5538   4716   5113     99   -247    445       C  
ATOM    856  C   LEU A 278      11.315  13.941  54.725  1.00 44.21           C  
ANISOU  856  C   LEU A 278     6058   5133   5608     75   -301    564       C  
ATOM    857  O   LEU A 278      11.475  13.840  55.941  1.00 45.70           O  
ANISOU  857  O   LEU A 278     6261   5375   5729     64   -314    637       O  
ATOM    858  CB  LEU A 278      10.472  16.197  54.013  1.00 40.53           C  
ANISOU  858  CB  LEU A 278     5527   4786   5085     44   -166    437       C  
ATOM    859  CG  LEU A 278      10.826  17.644  53.655  1.00 41.99           C  
ANISOU  859  CG  LEU A 278     5674   5040   5239     60   -118    338       C  
ATOM    860  CD1 LEU A 278       9.625  18.536  53.904  1.00 39.50           C  
ANISOU  860  CD1 LEU A 278     5341   4784   4884     12    -49    336       C  
ATOM    861  CD2 LEU A 278      12.032  18.119  54.459  1.00 42.89           C  
ANISOU  861  CD2 LEU A 278     5780   5219   5296     98   -138    314       C  
ATOM    862  N   LYS A 279      10.847  12.955  53.966  1.00 46.54           N  
ANISOU  862  N   LYS A 279     6372   5318   5994     66   -338    584       N  
ATOM    863  CA  LYS A 279      10.533  11.634  54.504  1.00 57.72           C  
ANISOU  863  CA  LYS A 279     7831   6649   7449     39   -403    700       C  
ATOM    864  C   LYS A 279      11.774  10.860  54.929  1.00 63.51           C  
ANISOU  864  C   LYS A 279     8590   7336   8204    103   -496    721       C  
ATOM    865  O   LYS A 279      11.719  10.052  55.853  1.00 62.56           O  
ANISOU  865  O   LYS A 279     8507   7187   8077     80   -548    838       O  
ATOM    866  CB  LYS A 279       9.747  10.805  53.486  1.00 61.55           C  
ANISOU  866  CB  LYS A 279     8327   7017   8041     15   -427    699       C  
ATOM    867  CG  LYS A 279       8.241  10.912  53.618  1.00 66.18           C  
ANISOU  867  CG  LYS A 279     8908   7624   8614    -76   -369    761       C  
ATOM    868  CD  LYS A 279       7.754  10.300  54.919  1.00 69.77           C  
ANISOU  868  CD  LYS A 279     9390   8094   9026   -141   -386    913       C  
ATOM    869  CE  LYS A 279       6.242  10.140  54.917  1.00 72.19           C  
ANISOU  869  CE  LYS A 279     9685   8404   9339   -235   -341    979       C  
ATOM    870  NZ  LYS A 279       5.544  11.409  54.563  1.00 73.75           N  
ANISOU  870  NZ  LYS A 279     9835   8705   9481   -250   -241    898       N  
ATOM    871  N   THR A 280      12.888  11.092  54.246  1.00 69.62           N  
ANISOU  871  N   THR A 280     9342   8107   9003    182   -519    612       N  
ATOM    872  CA  THR A 280      14.136  10.433  54.608  1.00 76.42           C  
ANISOU  872  CA  THR A 280    10219   8935   9884    254   -608    615       C  
ATOM    873  C   THR A 280      14.679  10.998  55.920  1.00 82.34           C  
ANISOU  873  C   THR A 280    10967   9794  10524    254   -596    661       C  
ATOM    874  O   THR A 280      15.131  10.252  56.786  1.00 88.61           O  
ANISOU  874  O   THR A 280    11794  10564  11312    271   -668    745       O  
ATOM    875  CB  THR A 280      15.199  10.547  53.496  1.00 74.50           C  
ANISOU  875  CB  THR A 280     9939   8677   9689    339   -632    476       C  
ATOM    876  OG1 THR A 280      15.692  11.891  53.429  1.00 72.97           O  
ANISOU  876  OG1 THR A 280     9699   8607   9419    347   -562    397       O  
ATOM    877  CG2 THR A 280      14.605  10.148  52.152  1.00 72.95           C  
ANISOU  877  CG2 THR A 280     9735   8399   9583    338   -632    416       C  
ATOM    878  N   ILE A 281      14.622  12.317  56.068  1.00 80.69           N  
ANISOU  878  N   ILE A 281    10721   9703  10233    237   -513    605       N  
ATOM    879  CA  ILE A 281      15.064  12.962  57.298  1.00 83.29           C  
ANISOU  879  CA  ILE A 281    11043  10148  10454    236   -498    632       C  
ATOM    880  C   ILE A 281      14.149  12.616  58.468  1.00 86.32           C  
ANISOU  880  C   ILE A 281    11457  10566  10776    168   -489    768       C  
ATOM    881  O   ILE A 281      14.610  12.343  59.574  1.00 88.81           O  
ANISOU  881  O   ILE A 281    11788  10927  11029    177   -529    841       O  
ATOM    882  CB  ILE A 281      15.133  14.486  57.135  1.00 83.24           C  
ANISOU  882  CB  ILE A 281    10990  10249  10387    230   -416    533       C  
ATOM    883  CG1 ILE A 281      16.287  14.856  56.202  1.00 85.81           C  
ANISOU  883  CG1 ILE A 281    11280  10568  10754    294   -432    415       C  
ATOM    884  CG2 ILE A 281      15.302  15.159  58.487  1.00 81.20           C  
ANISOU  884  CG2 ILE A 281    10724  10113  10016    217   -396    562       C  
ATOM    885  CD1 ILE A 281      16.260  16.291  55.739  1.00 87.43           C  
ANISOU  885  CD1 ILE A 281    11441  10848  10930    278   -358    321       C  
ATOM    886  N   ASN A 282      12.847  12.625  58.215  1.00 87.93           N  
ANISOU  886  N   ASN A 282    11663  10757  10992     99   -437    804       N  
ATOM    887  CA  ASN A 282      11.867  12.274  59.231  1.00 90.54           C  
ANISOU  887  CA  ASN A 282    12011  11130  11262     24   -421    936       C  
ATOM    888  C   ASN A 282      10.716  11.480  58.623  1.00 91.12           C  
ANISOU  888  C   ASN A 282    12101  11103  11416    -37   -421    996       C  
ATOM    889  O   ASN A 282       9.884  12.029  57.904  1.00 89.57           O  
ANISOU  889  O   ASN A 282    11880  10914  11237    -67   -356    939       O  
ATOM    890  CB  ASN A 282      11.344  13.535  59.922  1.00 91.31           C  
ANISOU  890  CB  ASN A 282    12069  11384  11241     -9   -331    907       C  
ATOM    891  CG  ASN A 282      10.242  13.238  60.916  1.00 92.25           C  
ANISOU  891  CG  ASN A 282    12192  11574  11285    -90   -303   1034       C  
ATOM    892  OD1 ASN A 282      10.084  12.103  61.364  1.00 93.32           O  
ANISOU  892  OD1 ASN A 282    12363  11656  11438   -123   -359   1164       O  
ATOM    893  ND2 ASN A 282       9.471  14.261  61.267  1.00 90.84           N  
ANISOU  893  ND2 ASN A 282    11973  11519  11024   -123   -218    996       N  
ATOM    894  N   GLN A 283      10.675  10.184  58.912  1.00 93.66           N  
ANISOU  894  N   GLN A 283    12467  11328  11791    -56   -501   1113       N  
ATOM    895  CA  GLN A 283       9.673   9.299  58.322  1.00 96.80           C  
ANISOU  895  CA  GLN A 283    12885  11611  12284   -114   -519   1172       C  
ATOM    896  C   GLN A 283       8.249   9.591  58.799  1.00 90.87           C  
ANISOU  896  C   GLN A 283    12113  10945  11469   -216   -441   1248       C  
ATOM    897  O   GLN A 283       7.296   8.970  58.329  1.00 89.05           O  
ANISOU  897  O   GLN A 283    11890  10636  11310   -277   -444   1296       O  
ATOM    898  CB  GLN A 283      10.032   7.831  58.581  1.00105.69           C  
ANISOU  898  CB  GLN A 283    14065  12601  13493   -111   -638   1284       C  
ATOM    899  CG  GLN A 283      11.047   7.249  57.602  1.00109.88           C  
ANISOU  899  CG  GLN A 283    14611  12996  14142    -15   -724   1189       C  
ATOM    900  CD  GLN A 283      10.423   6.853  56.271  1.00111.72           C  
ANISOU  900  CD  GLN A 283    14840  13112  14495    -23   -728   1121       C  
ATOM    901  OE1 GLN A 283       9.219   6.614  56.183  1.00111.89           O  
ANISOU  901  OE1 GLN A 283    14864  13112  14539   -109   -699   1185       O  
ATOM    902  NE2 GLN A 283      11.246   6.777  55.230  1.00112.31           N  
ANISOU  902  NE2 GLN A 283    14904  13124  14645     66   -766    989       N  
ATOM    903  N   GLU A 284       8.108  10.536  59.724  1.00 88.06           N  
ANISOU  903  N   GLU A 284    11727  10754  10980   -233   -372   1252       N  
ATOM    904  CA  GLU A 284       6.800  10.901  60.265  1.00 88.90           C  
ANISOU  904  CA  GLU A 284    11801  10970  11008   -321   -293   1311       C  
ATOM    905  C   GLU A 284       6.327  12.247  59.709  1.00 80.45           C  
ANISOU  905  C   GLU A 284    10680   9983   9906   -308   -198   1173       C  
ATOM    906  O   GLU A 284       5.378  12.849  60.215  1.00 79.53           O  
ANISOU  906  O   GLU A 284    10523   9987   9707   -359   -125   1185       O  
ATOM    907  CB  GLU A 284       6.846  10.934  61.798  1.00 98.66           C  
ANISOU  907  CB  GLU A 284    13033  12347  12107   -354   -287   1421       C  
ATOM    908  CG  GLU A 284       5.476  11.000  62.472  1.00107.05           C  
ANISOU  908  CG  GLU A 284    14061  13527  13087   -455   -219   1513       C  
ATOM    909  CD  GLU A 284       5.493  10.489  63.906  1.00112.78           C  
ANISOU  909  CD  GLU A 284    14794  14355  13700   -505   -243   1673       C  
ATOM    910  OE1 GLU A 284       6.533  10.631  64.583  1.00114.39           O  
ANISOU  910  OE1 GLU A 284    15013  14607  13842   -448   -280   1672       O  
ATOM    911  OE2 GLU A 284       4.462   9.944  64.356  1.00114.77           O  
ANISOU  911  OE2 GLU A 284    15035  14648  13924   -604   -225   1803       O  
ATOM    912  N   SER A 285       6.998  12.709  58.660  1.00 72.00           N  
ANISOU  912  N   SER A 285     9606   8848   8902   -238   -204   1042       N  
ATOM    913  CA  SER A 285       6.699  14.000  58.054  1.00 64.35           C  
ANISOU  913  CA  SER A 285     8594   7940   7916   -219   -129    914       C  
ATOM    914  C   SER A 285       5.364  13.983  57.289  1.00 57.33           C  
ANISOU  914  C   SER A 285     7685   7021   7076   -274    -83    908       C  
ATOM    915  O   SER A 285       5.111  13.078  56.503  1.00 55.22           O  
ANISOU  915  O   SER A 285     7440   6632   6909   -290   -124    933       O  
ATOM    916  CB  SER A 285       7.846  14.392  57.124  1.00 62.69           C  
ANISOU  916  CB  SER A 285     8387   7671   7764   -137   -155    795       C  
ATOM    917  OG  SER A 285       7.831  15.777  56.846  1.00 65.04           O  
ANISOU  917  OG  SER A 285     8644   8044   8022   -116    -92    684       O  
ATOM    918  N   CYS A 286       4.514  14.976  57.550  1.00 58.72           N  
ANISOU  918  N   CYS A 286     7817   7311   7183   -300     -5    871       N  
ATOM    919  CA  CYS A 286       3.260  15.183  56.818  1.00 60.92           C  
ANISOU  919  CA  CYS A 286     8066   7581   7500   -343     44    845       C  
ATOM    920  C   CYS A 286       3.569  15.915  55.482  1.00 42.45           C  
ANISOU  920  C   CYS A 286     5718   5183   5230   -287     53    713       C  
ATOM    921  O   CYS A 286       4.307  16.901  55.469  1.00 38.33           O  
ANISOU  921  O   CYS A 286     5185   4704   4676   -234     67    627       O  
ATOM    922  CB  CYS A 286       2.280  16.030  57.671  1.00 34.35           C  
ANISOU  922  CB  CYS A 286     4649   4373   4028   -381    121    846       C  
ATOM    923  SG  CYS A 286       1.012  15.232  58.812  1.00 71.64           S  
ANISOU  923  SG  CYS A 286     9349   9193   8677   -488    147   1002       S  
ATOM    924  N   ILE A 287       3.017  15.441  54.365  1.00 39.52           N  
ANISOU  924  N   ILE A 287     5349   4717   4951   -303     44    699       N  
ATOM    925  CA  ILE A 287       3.169  16.144  53.080  1.00 40.51           C  
ANISOU  925  CA  ILE A 287     5459   4803   5128   -259     57    584       C  
ATOM    926  C   ILE A 287       2.141  17.258  52.893  1.00 36.34           C  
ANISOU  926  C   ILE A 287     4886   4353   4569   -276    128    529       C  
ATOM    927  O   ILE A 287       2.187  18.006  51.914  1.00 35.27           O  
ANISOU  927  O   ILE A 287     4734   4200   4465   -244    143    441       O  
ATOM    928  CB  ILE A 287       3.082  15.191  51.851  1.00 41.14           C  
ANISOU  928  CB  ILE A 287     5557   4755   5319   -257     11    576       C  
ATOM    929  CG1 ILE A 287       1.752  14.412  51.832  1.00 39.49           C  
ANISOU  929  CG1 ILE A 287     5343   4518   5146   -333     17    649       C  
ATOM    930  CG2 ILE A 287       4.282  14.245  51.815  1.00 38.79           C  
ANISOU  930  CG2 ILE A 287     5299   4372   5067   -215    -68    594       C  
ATOM    931  CD1 ILE A 287       0.623  15.077  51.086  1.00 34.19           C  
ANISOU  931  CD1 ILE A 287     4629   3875   4485   -355     72    594       C  
ATOM    932  N   GLU A 288       1.210  17.370  53.829  1.00 35.78           N  
ANISOU  932  N   GLU A 288     4790   4373   4432   -325    169    581       N  
ATOM    933  CA  GLU A 288       0.091  18.291  53.651  1.00 35.32           C  
ANISOU  933  CA  GLU A 288     4684   4386   4352   -340    230    529       C  
ATOM    934  C   GLU A 288       0.455  19.784  53.606  1.00 33.75           C  
ANISOU  934  C   GLU A 288     4462   4245   4118   -285    258    422       C  
ATOM    935  O   GLU A 288      -0.052  20.516  52.765  1.00 35.10           O  
ANISOU  935  O   GLU A 288     4609   4403   4323   -271    280    352       O  
ATOM    936  CB  GLU A 288      -1.030  17.974  54.642  1.00 43.91           C  
ANISOU  936  CB  GLU A 288     5740   5569   5377   -408    267    609       C  
ATOM    937  CG  GLU A 288      -1.817  16.755  54.177  1.00 56.44           C  
ANISOU  937  CG  GLU A 288     7334   7079   7033   -474    247    690       C  
ATOM    938  CD  GLU A 288      -2.623  16.098  55.263  1.00 72.56           C  
ANISOU  938  CD  GLU A 288     9355   9201   9014   -555    265    807       C  
ATOM    939  OE1 GLU A 288      -3.630  16.700  55.693  1.00 79.46           O  
ANISOU  939  OE1 GLU A 288    10171  10196   9825   -582    326    793       O  
ATOM    940  OE2 GLU A 288      -2.269  14.965  55.661  1.00 77.08           O  
ANISOU  940  OE2 GLU A 288     9965   9716   9605   -592    216    914       O  
ATOM    941  N   PRO A 289       1.329  20.245  54.503  1.00 38.42           N  
ANISOU  941  N   PRO A 289     5060   4894   4644   -254    252    409       N  
ATOM    942  CA  PRO A 289       1.707  21.667  54.389  1.00 40.82           C  
ANISOU  942  CA  PRO A 289     5344   5235   4932   -204    269    303       C  
ATOM    943  C   PRO A 289       2.245  22.031  52.998  1.00 37.10           C  
ANISOU  943  C   PRO A 289     4885   4668   4544   -171    248    240       C  
ATOM    944  O   PRO A 289       1.880  23.067  52.438  1.00 34.98           O  
ANISOU  944  O   PRO A 289     4593   4404   4294   -154    268    169       O  
ATOM    945  CB  PRO A 289       2.811  21.820  55.439  1.00 41.14           C  
ANISOU  945  CB  PRO A 289     5398   5327   4906   -177    248    307       C  
ATOM    946  CG  PRO A 289       2.501  20.781  56.465  1.00 41.43           C  
ANISOU  946  CG  PRO A 289     5443   5414   4886   -221    246    415       C  
ATOM    947  CD  PRO A 289       1.808  19.631  55.755  1.00 42.39           C  
ANISOU  947  CD  PRO A 289     5580   5450   5078   -268    235    489       C  
ATOM    948  N   LEU A 290       3.118  21.190  52.457  1.00 35.73           N  
ANISOU  948  N   LEU A 290     4745   4414   4416   -160    204    266       N  
ATOM    949  CA  LEU A 290       3.672  21.385  51.121  1.00 35.51           C  
ANISOU  949  CA  LEU A 290     4723   4312   4456   -131    184    213       C  
ATOM    950  C   LEU A 290       2.571  21.368  50.055  1.00 34.94           C  
ANISOU  950  C   LEU A 290     4634   4204   4437   -152    203    199       C  
ATOM    951  O   LEU A 290       2.491  22.259  49.209  1.00 26.59           O  
ANISOU  951  O   LEU A 290     3559   3139   3404   -135    214    139       O  
ATOM    952  CB  LEU A 290       4.690  20.282  50.832  1.00 43.70           C  
ANISOU  952  CB  LEU A 290     5793   5282   5530   -114    131    243       C  
ATOM    953  CG  LEU A 290       5.818  20.481  49.830  1.00 50.37           C  
ANISOU  953  CG  LEU A 290     6639   6086   6414    -71    103    185       C  
ATOM    954  CD1 LEU A 290       6.576  21.755  50.128  1.00 48.96           C  
ANISOU  954  CD1 LEU A 290     6443   5961   6196    -46    115    130       C  
ATOM    955  CD2 LEU A 290       6.751  19.278  49.904  1.00 53.83           C  
ANISOU  955  CD2 LEU A 290     7104   6473   6875    -48     47    217       C  
ATOM    956  N   ALA A 291       1.720  20.349  50.100  1.00 31.51           N  
ANISOU  956  N   ALA A 291     4204   3748   4022   -193    203    259       N  
ATOM    957  CA  ALA A 291       0.647  20.220  49.124  1.00 27.54           C  
ANISOU  957  CA  ALA A 291     3681   3212   3569   -216    216    247       C  
ATOM    958  C   ALA A 291      -0.316  21.406  49.212  1.00 28.40           C  
ANISOU  958  C   ALA A 291     3750   3389   3650   -219    264    202       C  
ATOM    959  O   ALA A 291      -0.773  21.915  48.198  1.00 30.10           O  
ANISOU  959  O   ALA A 291     3950   3584   3904   -209    271    156       O  
ATOM    960  CB  ALA A 291      -0.106  18.891  49.310  1.00 25.86           C  
ANISOU  960  CB  ALA A 291     3478   2965   3384   -268    203    325       C  
ATOM    961  N   GLU A 292      -0.611  21.850  50.428  1.00 30.89           N  
ANISOU  961  N   GLU A 292     4049   3791   3897   -227    293    213       N  
ATOM    962  CA  GLU A 292      -1.489  23.000  50.618  1.00 30.58           C  
ANISOU  962  CA  GLU A 292     3967   3821   3831   -219    332    157       C  
ATOM    963  C   GLU A 292      -0.872  24.291  50.085  1.00 31.41           C  
ANISOU  963  C   GLU A 292     4071   3909   3953   -170    323     76       C  
ATOM    964  O   GLU A 292      -1.565  25.151  49.533  1.00 29.36           O  
ANISOU  964  O   GLU A 292     3785   3653   3717   -156    335     24       O  
ATOM    965  CB  GLU A 292      -1.889  23.123  52.093  1.00 34.25           C  
ANISOU  965  CB  GLU A 292     4408   4397   4210   -235    362    179       C  
ATOM    966  CG  GLU A 292      -2.836  22.019  52.503  1.00 40.76           C  
ANISOU  966  CG  GLU A 292     5217   5250   5018   -299    379    265       C  
ATOM    967  CD  GLU A 292      -3.027  21.887  54.004  1.00 46.49           C  
ANISOU  967  CD  GLU A 292     5923   6096   5646   -324    404    311       C  
ATOM    968  OE1 GLU A 292      -2.402  22.644  54.783  1.00 47.79           O  
ANISOU  968  OE1 GLU A 292     6085   6324   5751   -285    407    269       O  
ATOM    969  OE2 GLU A 292      -3.811  21.002  54.397  1.00 50.54           O  
ANISOU  969  OE2 GLU A 292     6420   6643   6141   -386    419    394       O  
ATOM    970  N   SER A 293       0.440  24.411  50.222  1.00 31.01           N  
ANISOU  970  N   SER A 293     4048   3838   3896   -144    295     68       N  
ATOM    971  CA  SER A 293       1.149  25.603  49.767  1.00 35.22           C  
ANISOU  971  CA  SER A 293     4580   4353   4447   -108    281      2       C  
ATOM    972  C   SER A 293       1.141  25.690  48.245  1.00 29.25           C  
ANISOU  972  C   SER A 293     3827   3529   3758   -105    267    -13       C  
ATOM    973  O   SER A 293       0.963  26.762  47.659  1.00 26.92           O  
ANISOU  973  O   SER A 293     3517   3223   3487    -89    266    -58       O  
ATOM    974  CB  SER A 293       2.592  25.572  50.286  1.00 37.51           C  
ANISOU  974  CB  SER A 293     4895   4645   4714    -89    254      3       C  
ATOM    975  OG  SER A 293       3.362  26.609  49.717  1.00 48.50           O  
ANISOU  975  OG  SER A 293     6284   6011   6132    -65    236    -50       O  
ATOM    976  N   ILE A 294       1.364  24.555  47.598  1.00 22.71           N  
ANISOU  976  N   ILE A 294     3016   2654   2957   -117    251     25       N  
ATOM    977  CA  ILE A 294       1.373  24.501  46.153  1.00 23.17           C  
ANISOU  977  CA  ILE A 294     3073   2663   3068   -112    237     10       C  
ATOM    978  C   ILE A 294      -0.035  24.728  45.600  1.00 25.19           C  
ANISOU  978  C   ILE A 294     3303   2920   3346   -127    258      0       C  
ATOM    979  O   ILE A 294      -0.229  25.489  44.636  1.00 25.79           O  
ANISOU  979  O   ILE A 294     3365   2983   3450   -116    254    -31       O  
ATOM    980  CB  ILE A 294       1.948  23.128  45.680  1.00 26.47           C  
ANISOU  980  CB  ILE A 294     3513   3034   3511   -114    208     40       C  
ATOM    981  CG1 ILE A 294       3.436  23.037  46.051  1.00 27.91           C  
ANISOU  981  CG1 ILE A 294     3713   3217   3674    -89    182     37       C  
ATOM    982  CG2 ILE A 294       1.729  22.919  44.168  1.00 25.58           C  
ANISOU  982  CG2 ILE A 294     3389   2885   3444   -110    196     18       C  
ATOM    983  CD1 ILE A 294       3.983  21.604  46.015  1.00 27.32           C  
ANISOU  983  CD1 ILE A 294     3661   3100   3619    -83    147     68       C  
ATOM    984  N   THR A 295      -1.017  24.059  46.197  1.00 24.83           N  
ANISOU  984  N   THR A 295     3248   2897   3291   -156    277     32       N  
ATOM    985  CA  THR A 295      -2.389  24.156  45.707  1.00 24.62           C  
ANISOU  985  CA  THR A 295     3190   2879   3286   -173    296     23       C  
ATOM    986  C   THR A 295      -2.877  25.605  45.852  1.00 24.46           C  
ANISOU  986  C   THR A 295     3142   2897   3254   -148    312    -30       C  
ATOM    987  O   THR A 295      -3.545  26.147  44.976  1.00 25.03           O  
ANISOU  987  O   THR A 295     3195   2957   3359   -139    310    -57       O  
ATOM    988  CB  THR A 295      -3.344  23.212  46.478  1.00 26.13           C  
ANISOU  988  CB  THR A 295     3368   3100   3461   -217    317     72       C  
ATOM    989  OG1 THR A 295      -2.930  21.847  46.294  1.00 30.72           O  
ANISOU  989  OG1 THR A 295     3978   3626   4069   -241    290    123       O  
ATOM    990  CG2 THR A 295      -4.771  23.387  45.970  1.00 26.54           C  
ANISOU  990  CG2 THR A 295     3378   3170   3534   -234    337     56       C  
ATOM    991  N   ASP A 296      -2.535  26.220  46.976  1.00 26.86           N  
ANISOU  991  N   ASP A 296     3444   3247   3514   -134    322    -46       N  
ATOM    992  CA  ASP A 296      -2.892  27.626  47.216  1.00 30.49           C  
ANISOU  992  CA  ASP A 296     3880   3736   3970   -102    326   -108       C  
ATOM    993  C   ASP A 296      -2.382  28.558  46.107  1.00 31.13           C  
ANISOU  993  C   ASP A 296     3971   3757   4101    -78    295   -138       C  
ATOM    994  O   ASP A 296      -3.142  29.366  45.569  1.00 31.05           O  
ANISOU  994  O   ASP A 296     3939   3738   4121    -62    290   -171       O  
ATOM    995  CB  ASP A 296      -2.371  28.076  48.582  1.00 33.33           C  
ANISOU  995  CB  ASP A 296     4238   4151   4274    -87    332   -130       C  
ATOM    996  CG  ASP A 296      -2.518  29.566  48.792  1.00 43.98           C  
ANISOU  996  CG  ASP A 296     5567   5512   5632    -46    322   -207       C  
ATOM    997  OD1 ASP A 296      -3.658  30.016  49.022  1.00 43.62           O  
ANISOU  997  OD1 ASP A 296     5481   5510   5582    -34    339   -245       O  
ATOM    998  OD2 ASP A 296      -1.497  30.284  48.714  1.00 47.77           O  
ANISOU  998  OD2 ASP A 296     6066   5955   6128    -27    292   -231       O  
ATOM    999  N   VAL A 297      -1.108  28.436  45.738  1.00 28.90           N  
ANISOU  999  N   VAL A 297     3718   3438   3825    -77    272   -122       N  
ATOM   1000  CA  VAL A 297      -0.559  29.251  44.653  1.00 29.59           C  
ANISOU 1000  CA  VAL A 297     3811   3481   3951    -66    244   -135       C  
ATOM   1001  C   VAL A 297      -1.299  29.000  43.355  1.00 33.61           C  
ANISOU 1001  C   VAL A 297     4309   3965   4494    -74    241   -123       C  
ATOM   1002  O   VAL A 297      -1.746  29.928  42.697  1.00 30.63           O  
ANISOU 1002  O   VAL A 297     3919   3572   4147    -63    226   -141       O  
ATOM   1003  CB  VAL A 297       0.961  29.025  44.422  1.00 36.82           C  
ANISOU 1003  CB  VAL A 297     4750   4378   4860    -69    224   -118       C  
ATOM   1004  CG1 VAL A 297       1.417  29.702  43.127  1.00 39.36           C  
ANISOU 1004  CG1 VAL A 297     5070   4669   5217    -71    199   -117       C  
ATOM   1005  CG2 VAL A 297       1.745  29.561  45.588  1.00 32.95           C  
ANISOU 1005  CG2 VAL A 297     4267   3909   4342    -58    218   -140       C  
ATOM   1006  N   LEU A 298      -1.437  27.736  42.987  1.00 25.77           N  
ANISOU 1006  N   LEU A 298     3322   2970   3501    -92    248    -94       N  
ATOM   1007  CA  LEU A 298      -2.112  27.401  41.745  1.00 27.85           C  
ANISOU 1007  CA  LEU A 298     3572   3216   3794    -99    242    -89       C  
ATOM   1008  C   LEU A 298      -3.579  27.877  41.691  1.00 27.28           C  
ANISOU 1008  C   LEU A 298     3468   3160   3737    -96    254   -108       C  
ATOM   1009  O   LEU A 298      -3.972  28.594  40.779  1.00 29.81           O  
ANISOU 1009  O   LEU A 298     3775   3467   4083    -84    238   -121       O  
ATOM   1010  CB  LEU A 298      -2.030  25.887  41.509  1.00 26.06           C  
ANISOU 1010  CB  LEU A 298     3355   2977   3571   -117    241    -64       C  
ATOM   1011  CG  LEU A 298      -2.897  25.297  40.395  1.00 36.46           C  
ANISOU 1011  CG  LEU A 298     4655   4282   4917   -127    235    -67       C  
ATOM   1012  CD1 LEU A 298      -2.494  25.855  39.020  1.00 40.43           C  
ANISOU 1012  CD1 LEU A 298     5151   4781   5430   -111    213    -81       C  
ATOM   1013  CD2 LEU A 298      -2.801  23.760  40.405  1.00 41.26           C  
ANISOU 1013  CD2 LEU A 298     5275   4864   5538   -146    226    -47       C  
ATOM   1014  N   VAL A 299      -4.386  27.479  42.665  1.00 22.79           N  
ANISOU 1014  N   VAL A 299     2883   2625   3150   -108    281   -108       N  
ATOM   1015  CA  VAL A 299      -5.809  27.721  42.582  1.00 26.24           C  
ANISOU 1015  CA  VAL A 299     3281   3089   3600   -107    295   -128       C  
ATOM   1016  C   VAL A 299      -6.142  29.189  42.843  1.00 29.81           C  
ANISOU 1016  C   VAL A 299     3714   3553   4059    -70    287   -176       C  
ATOM   1017  O   VAL A 299      -6.918  29.795  42.109  1.00 29.60           O  
ANISOU 1017  O   VAL A 299     3666   3518   4064    -52    273   -197       O  
ATOM   1018  CB  VAL A 299      -6.607  26.757  43.493  1.00 25.45           C  
ANISOU 1018  CB  VAL A 299     3160   3035   3474   -141    328   -107       C  
ATOM   1019  CG1 VAL A 299      -8.081  27.063  43.432  1.00 23.37           C  
ANISOU 1019  CG1 VAL A 299     2845   2814   3220   -141    345   -134       C  
ATOM   1020  CG2 VAL A 299      -6.346  25.295  43.038  1.00 25.71           C  
ANISOU 1020  CG2 VAL A 299     3214   3032   3523   -178    320    -60       C  
ATOM   1021  N   ARG A 300      -5.530  29.760  43.870  1.00 26.21           N  
ANISOU 1021  N   ARG A 300     3268   3113   3577    -54    289   -196       N  
ATOM   1022  CA  ARG A 300      -5.813  31.140  44.245  1.00 33.12           C  
ANISOU 1022  CA  ARG A 300     4125   3992   4465    -14    274   -253       C  
ATOM   1023  C   ARG A 300      -5.261  32.118  43.192  1.00 30.11           C  
ANISOU 1023  C   ARG A 300     3764   3543   4135      3    228   -254       C  
ATOM   1024  O   ARG A 300      -5.973  32.994  42.724  1.00 28.73           O  
ANISOU 1024  O   ARG A 300     3571   3349   3998     30    204   -283       O  
ATOM   1025  CB  ARG A 300      -5.259  31.438  45.651  1.00 31.53           C  
ANISOU 1025  CB  ARG A 300     3927   3832   4221     -2    284   -282       C  
ATOM   1026  CG  ARG A 300      -5.599  32.813  46.224  1.00 36.16           C  
ANISOU 1026  CG  ARG A 300     4489   4429   4822     46    264   -359       C  
ATOM   1027  CD  ARG A 300      -5.039  32.990  47.664  1.00 41.80           C  
ANISOU 1027  CD  ARG A 300     5202   5199   5483     58    275   -394       C  
ATOM   1028  NE  ARG A 300      -3.616  32.661  47.760  1.00 38.90           N  
ANISOU 1028  NE  ARG A 300     4879   4800   5101     37    265   -355       N  
ATOM   1029  CZ  ARG A 300      -2.630  33.462  47.375  1.00 41.73           C  
ANISOU 1029  CZ  ARG A 300     5264   5094   5499     46    224   -364       C  
ATOM   1030  NH1 ARG A 300      -2.892  34.677  46.891  1.00 36.27           N  
ANISOU 1030  NH1 ARG A 300     4565   4349   4866     74    184   -407       N  
ATOM   1031  NH2 ARG A 300      -1.375  33.049  47.482  1.00 43.41           N  
ANISOU 1031  NH2 ARG A 300     5509   5293   5694     26    218   -329       N  
ATOM   1032  N   THR A 301      -4.017  31.938  42.767  1.00 26.65           N  
ANISOU 1032  N   THR A 301     3360   3070   3695    -15    213   -219       N  
ATOM   1033  CA  THR A 301      -3.436  32.922  41.850  1.00 29.98           C  
ANISOU 1033  CA  THR A 301     3797   3438   4157     -9    171   -209       C  
ATOM   1034  C   THR A 301      -3.753  32.665  40.366  1.00 29.49           C  
ANISOU 1034  C   THR A 301     3731   3359   4115    -21    158   -172       C  
ATOM   1035  O   THR A 301      -3.668  33.593  39.548  1.00 26.03           O  
ANISOU 1035  O   THR A 301     3294   2885   3710    -16    121   -160       O  
ATOM   1036  CB  THR A 301      -1.909  33.162  42.100  1.00 31.61           C  
ANISOU 1036  CB  THR A 301     4031   3626   4354    -22    156   -195       C  
ATOM   1037  OG1 THR A 301      -1.142  32.115  41.517  1.00 27.08           O  
ANISOU 1037  OG1 THR A 301     3471   3061   3756    -48    167   -152       O  
ATOM   1038  CG2 THR A 301      -1.595  33.245  43.592  1.00 34.18           C  
ANISOU 1038  CG2 THR A 301     4358   3979   4649     -9    169   -233       C  
ATOM   1039  N   LYS A 302      -4.154  31.438  40.019  1.00 22.89           N  
ANISOU 1039  N   LYS A 302     2887   2550   3260    -38    184   -155       N  
ATOM   1040  CA  LYS A 302      -4.510  31.131  38.625  1.00 24.26           C  
ANISOU 1040  CA  LYS A 302     3052   2719   3446    -46    171   -131       C  
ATOM   1041  C   LYS A 302      -5.951  30.672  38.477  1.00 25.05           C  
ANISOU 1041  C   LYS A 302     3121   2842   3556    -42    185   -148       C  
ATOM   1042  O   LYS A 302      -6.288  30.003  37.515  1.00 23.13           O  
ANISOU 1042  O   LYS A 302     2867   2605   3314    -54    182   -135       O  
ATOM   1043  CB  LYS A 302      -3.574  30.075  38.014  1.00 27.76           C  
ANISOU 1043  CB  LYS A 302     3511   3170   3866    -68    175   -103       C  
ATOM   1044  CG  LYS A 302      -2.109  30.475  38.007  1.00 29.12           C  
ANISOU 1044  CG  LYS A 302     3704   3334   4025    -75    161    -86       C  
ATOM   1045  CD  LYS A 302      -1.884  31.753  37.234  1.00 29.68           C  
ANISOU 1045  CD  LYS A 302     3774   3387   4117    -74    127    -66       C  
ATOM   1046  CE  LYS A 302      -0.491  32.289  37.531  1.00 39.05           C  
ANISOU 1046  CE  LYS A 302     4976   4565   5296    -88    115    -52       C  
ATOM   1047  NZ  LYS A 302      -0.097  33.348  36.576  1.00 39.73           N  
ANISOU 1047  NZ  LYS A 302     5059   4637   5400   -103     79    -13       N  
ATOM   1048  N   ARG A 303      -6.802  31.056  39.419  1.00 25.61           N  
ANISOU 1048  N   ARG A 303     3170   2931   3631    -26    199   -184       N  
ATOM   1049  CA  ARG A 303      -8.195  30.617  39.432  1.00 23.17           C  
ANISOU 1049  CA  ARG A 303     2820   2657   3326    -26    218   -203       C  
ATOM   1050  C   ARG A 303      -8.904  30.683  38.073  1.00 24.58           C  
ANISOU 1050  C   ARG A 303     2981   2828   3533    -20    193   -197       C  
ATOM   1051  O   ARG A 303      -9.393  29.679  37.574  1.00 21.95           O  
ANISOU 1051  O   ARG A 303     2633   2511   3197    -43    204   -187       O  
ATOM   1052  CB  ARG A 303      -8.975  31.460  40.457  1.00 25.10           C  
ANISOU 1052  CB  ARG A 303     3034   2930   3573      6    225   -254       C  
ATOM   1053  CG  ARG A 303     -10.476  31.241  40.433  1.00 30.20           C  
ANISOU 1053  CG  ARG A 303     3626   3623   4226     11    241   -281       C  
ATOM   1054  CD  ARG A 303     -10.904  30.000  41.152  1.00 34.07           C  
ANISOU 1054  CD  ARG A 303     4096   4169   4681    -31    288   -266       C  
ATOM   1055  NE  ARG A 303     -10.603  30.026  42.583  1.00 36.39           N  
ANISOU 1055  NE  ARG A 303     4388   4507   4932    -33    317   -278       N  
ATOM   1056  CZ  ARG A 303     -11.024  29.099  43.443  1.00 36.96           C  
ANISOU 1056  CZ  ARG A 303     4437   4641   4965    -72    358   -259       C  
ATOM   1057  NH1 ARG A 303     -11.791  28.097  43.023  1.00 33.32           N  
ANISOU 1057  NH1 ARG A 303     3952   4195   4512   -114    372   -230       N  
ATOM   1058  NH2 ARG A 303     -10.693  29.176  44.722  1.00 35.01           N  
ANISOU 1058  NH2 ARG A 303     4189   4445   4670    -72    382   -267       N  
ATOM   1059  N   ASP A 304      -8.982  31.872  37.479  1.00 23.18           N  
ANISOU 1059  N   ASP A 304     2803   2622   3383     10    153   -201       N  
ATOM   1060  CA  ASP A 304      -9.759  32.032  36.254  1.00 24.01           C  
ANISOU 1060  CA  ASP A 304     2887   2728   3510     21    126   -194       C  
ATOM   1061  C   ASP A 304      -9.099  31.347  35.057  1.00 24.11           C  
ANISOU 1061  C   ASP A 304     2916   2741   3504     -5    116   -153       C  
ATOM   1062  O   ASP A 304      -9.792  30.844  34.170  1.00 22.64           O  
ANISOU 1062  O   ASP A 304     2707   2577   3320     -9    109   -154       O  
ATOM   1063  CB  ASP A 304     -10.010  33.510  35.950  1.00 23.88           C  
ANISOU 1063  CB  ASP A 304     2867   2674   3532     60     77   -201       C  
ATOM   1064  CG  ASP A 304     -10.988  34.140  36.917  1.00 28.65           C  
ANISOU 1064  CG  ASP A 304     3438   3290   4159    100     79   -263       C  
ATOM   1065  OD1 ASP A 304     -11.722  33.376  37.588  1.00 25.03           O  
ANISOU 1065  OD1 ASP A 304     2946   2886   3679     92    121   -294       O  
ATOM   1066  OD2 ASP A 304     -11.040  35.381  36.990  1.00 27.98           O  
ANISOU 1066  OD2 ASP A 304     3356   3162   4114    139     34   -281       O  
ATOM   1067  N   TRP A 305      -7.771  31.336  35.036  1.00 23.95           N  
ANISOU 1067  N   TRP A 305     2931   2705   3465    -21    114   -125       N  
ATOM   1068  CA  TRP A 305      -7.015  30.609  34.012  1.00 24.11           C  
ANISOU 1068  CA  TRP A 305     2960   2741   3458    -42    110    -98       C  
ATOM   1069  C   TRP A 305      -7.373  29.103  34.063  1.00 24.13           C  
ANISOU 1069  C   TRP A 305     2952   2765   3451    -60    136   -118       C  
ATOM   1070  O   TRP A 305      -7.592  28.470  33.035  1.00 21.72           O  
ANISOU 1070  O   TRP A 305     2631   2481   3139    -64    124   -121       O  
ATOM   1071  CB  TRP A 305      -5.511  30.826  34.227  1.00 23.98           C  
ANISOU 1071  CB  TRP A 305     2974   2713   3422    -54    109    -73       C  
ATOM   1072  CG  TRP A 305      -4.622  30.228  33.169  1.00 22.32           C  
ANISOU 1072  CG  TRP A 305     2766   2535   3179    -69    102    -51       C  
ATOM   1073  CD1 TRP A 305      -4.208  30.831  32.018  1.00 27.01           C  
ANISOU 1073  CD1 TRP A 305     3354   3152   3756    -75     74    -15       C  
ATOM   1074  CD2 TRP A 305      -4.037  28.919  33.171  1.00 24.97           C  
ANISOU 1074  CD2 TRP A 305     3106   2890   3492    -79    120    -68       C  
ATOM   1075  NE1 TRP A 305      -3.404  29.983  31.301  1.00 26.41           N  
ANISOU 1075  NE1 TRP A 305     3272   3124   3641    -84     79    -16       N  
ATOM   1076  CE2 TRP A 305      -3.279  28.802  31.986  1.00 27.66           C  
ANISOU 1076  CE2 TRP A 305     3436   3273   3799    -83    104    -53       C  
ATOM   1077  CE3 TRP A 305      -4.056  27.849  34.073  1.00 20.97           C  
ANISOU 1077  CE3 TRP A 305     2609   2369   2990    -84    143    -90       C  
ATOM   1078  CZ2 TRP A 305      -2.553  27.645  31.666  1.00 25.33           C  
ANISOU 1078  CZ2 TRP A 305     3139   3006   3480    -82    109    -76       C  
ATOM   1079  CZ3 TRP A 305      -3.317  26.683  33.751  1.00 22.93           C  
ANISOU 1079  CZ3 TRP A 305     2861   2629   3222    -87    142   -103       C  
ATOM   1080  CH2 TRP A 305      -2.589  26.597  32.560  1.00 20.96           C  
ANISOU 1080  CH2 TRP A 305     2599   2421   2944    -82    124   -104       C  
ATOM   1081  N   LEU A 306      -7.449  28.543  35.263  1.00 25.30           N  
ANISOU 1081  N   LEU A 306     3106   2908   3600    -71    166   -130       N  
ATOM   1082  CA  LEU A 306      -7.847  27.137  35.421  1.00 25.18           C  
ANISOU 1082  CA  LEU A 306     3081   2899   3586    -95    183   -139       C  
ATOM   1083  C   LEU A 306      -9.306  26.923  35.029  1.00 29.50           C  
ANISOU 1083  C   LEU A 306     3587   3466   4155    -99    183   -159       C  
ATOM   1084  O   LEU A 306      -9.620  25.983  34.286  1.00 27.90           O  
ANISOU 1084  O   LEU A 306     3372   3268   3962   -114    173   -168       O  
ATOM   1085  CB  LEU A 306      -7.644  26.678  36.861  1.00 23.14           C  
ANISOU 1085  CB  LEU A 306     2838   2637   3320   -112    213   -133       C  
ATOM   1086  CG  LEU A 306      -6.213  26.645  37.373  1.00 28.33           C  
ANISOU 1086  CG  LEU A 306     3532   3277   3955   -111    214   -117       C  
ATOM   1087  CD1 LEU A 306      -6.217  26.586  38.881  1.00 26.83           C  
ANISOU 1087  CD1 LEU A 306     3350   3096   3750   -120    241   -112       C  
ATOM   1088  CD2 LEU A 306      -5.438  25.432  36.750  1.00 25.35           C  
ANISOU 1088  CD2 LEU A 306     3171   2884   3576   -122    200   -111       C  
ATOM   1089  N   VAL A 307     -10.199  27.796  35.512  1.00 23.73           N  
ANISOU 1089  N   VAL A 307     2831   2750   3435    -81    189   -174       N  
ATOM   1090  CA  VAL A 307     -11.628  27.648  35.223  1.00 26.66           C  
ANISOU 1090  CA  VAL A 307     3154   3150   3826    -82    189   -198       C  
ATOM   1091  C   VAL A 307     -11.882  27.644  33.721  1.00 30.32           C  
ANISOU 1091  C   VAL A 307     3605   3618   4298    -71    153   -200       C  
ATOM   1092  O   VAL A 307     -12.658  26.828  33.220  1.00 30.80           O  
ANISOU 1092  O   VAL A 307     3637   3696   4371    -89    150   -216       O  
ATOM   1093  CB  VAL A 307     -12.486  28.770  35.872  1.00 31.92           C  
ANISOU 1093  CB  VAL A 307     3790   3837   4503    -50    193   -225       C  
ATOM   1094  CG1 VAL A 307     -13.945  28.704  35.369  1.00 32.50           C  
ANISOU 1094  CG1 VAL A 307     3806   3947   4597    -44    186   -253       C  
ATOM   1095  CG2 VAL A 307     -12.439  28.679  37.390  1.00 27.97           C  
ANISOU 1095  CG2 VAL A 307     3287   3357   3984    -62    232   -232       C  
ATOM   1096  N   LYS A 308     -11.227  28.546  32.992  1.00 25.37           N  
ANISOU 1096  N   LYS A 308     2998   2980   3661    -46    124   -182       N  
ATOM   1097  CA  LYS A 308     -11.552  28.719  31.577  1.00 31.25           C  
ANISOU 1097  CA  LYS A 308     3726   3745   4403    -33     88   -178       C  
ATOM   1098  C   LYS A 308     -11.376  27.400  30.823  1.00 41.90           C  
ANISOU 1098  C   LYS A 308     5069   5112   5739    -56     86   -191       C  
ATOM   1099  O   LYS A 308     -12.016  27.140  29.807  1.00 40.28           O  
ANISOU 1099  O   LYS A 308     4835   4936   5533    -51     63   -207       O  
ATOM   1100  CB  LYS A 308     -10.681  29.810  30.943  1.00 35.52           C  
ANISOU 1100  CB  LYS A 308     4292   4275   4929    -15     57   -139       C  
ATOM   1101  CG  LYS A 308     -11.191  30.249  29.576  1.00 51.25           C  
ANISOU 1101  CG  LYS A 308     6261   6297   6914      2     15   -125       C  
ATOM   1102  CD  LYS A 308     -10.297  31.307  28.944  1.00 62.30           C  
ANISOU 1102  CD  LYS A 308     7685   7690   8296      7    -17    -68       C  
ATOM   1103  CE  LYS A 308     -10.690  31.574  27.496  1.00 66.00           C  
ANISOU 1103  CE  LYS A 308     8132   8204   8742     16    -59    -42       C  
ATOM   1104  NZ  LYS A 308      -9.695  32.459  26.820  1.00 69.10           N  
ANISOU 1104  NZ  LYS A 308     8545   8602   9107      6    -88     28       N  
ATOM   1105  N   GLN A 309     -10.537  26.554  31.401  1.00 42.71           N  
ANISOU 1105  N   GLN A 309     5198   5194   5835    -78    107   -189       N  
ATOM   1106  CA  GLN A 309      -9.940  25.403  30.758  1.00 42.79           C  
ANISOU 1106  CA  GLN A 309     5215   5208   5835    -90     97   -205       C  
ATOM   1107  C   GLN A 309     -10.534  24.121  31.292  1.00 37.71           C  
ANISOU 1107  C   GLN A 309     4562   4543   5225   -122    108   -227       C  
ATOM   1108  O   GLN A 309      -9.976  23.042  31.097  1.00 43.80           O  
ANISOU 1108  O   GLN A 309     5344   5295   6002   -133     98   -243       O  
ATOM   1109  CB  GLN A 309      -8.490  25.449  31.186  1.00 37.93           C  
ANISOU 1109  CB  GLN A 309     4639   4575   5196    -90    106   -184       C  
ATOM   1110  CG  GLN A 309      -7.583  24.574  30.508  1.00 53.39           C  
ANISOU 1110  CG  GLN A 309     6604   6545   7137    -88     91   -202       C  
ATOM   1111  CD  GLN A 309      -6.215  25.080  30.719  1.00 43.25           C  
ANISOU 1111  CD  GLN A 309     5347   5264   5821    -80     97   -177       C  
ATOM   1112  OE1 GLN A 309      -6.006  26.011  31.513  1.00 43.70           O  
ANISOU 1112  OE1 GLN A 309     5422   5303   5879    -81    111   -146       O  
ATOM   1113  NE2 GLN A 309      -5.273  24.536  29.982  1.00 43.35           N  
ANISOU 1113  NE2 GLN A 309     5358   5306   5806    -70     82   -195       N  
ATOM   1114  N   ARG A 310     -11.660  24.247  31.979  1.00 33.20           N  
ANISOU 1114  N   ARG A 310     3964   3974   4677   -136    126   -228       N  
ATOM   1115  CA  ARG A 310     -12.248  23.152  32.748  1.00 33.39           C  
ANISOU 1115  CA  ARG A 310     3976   3979   4731   -180    143   -230       C  
ATOM   1116  C   ARG A 310     -11.214  22.484  33.651  1.00 29.41           C  
ANISOU 1116  C   ARG A 310     3515   3435   4224   -199    156   -205       C  
ATOM   1117  O   ARG A 310     -11.157  21.254  33.754  1.00 24.56           O  
ANISOU 1117  O   ARG A 310     2907   2785   3638   -230    145   -206       O  
ATOM   1118  CB  ARG A 310     -12.964  22.118  31.851  1.00 37.92           C  
ANISOU 1118  CB  ARG A 310     4519   4552   5336   -200    115   -264       C  
ATOM   1119  CG  ARG A 310     -14.346  22.543  31.379  1.00 42.39           C  
ANISOU 1119  CG  ARG A 310     5031   5162   5915   -196    109   -287       C  
ATOM   1120  CD  ARG A 310     -15.161  21.335  30.897  1.00 45.43           C  
ANISOU 1120  CD  ARG A 310     5381   5539   6342   -234     87   -318       C  
ATOM   1121  NE  ARG A 310     -14.401  20.529  29.945  1.00 43.67           N  
ANISOU 1121  NE  ARG A 310     5178   5292   6122   -224     49   -348       N  
ATOM   1122  CZ  ARG A 310     -14.194  20.891  28.687  1.00 49.07           C  
ANISOU 1122  CZ  ARG A 310     5853   6014   6776   -184     19   -379       C  
ATOM   1123  NH1 ARG A 310     -14.694  22.041  28.241  1.00 49.96           N  
ANISOU 1123  NH1 ARG A 310     5943   6177   6861   -153     19   -372       N  
ATOM   1124  NH2 ARG A 310     -13.488  20.113  27.879  1.00 49.17           N  
ANISOU 1124  NH2 ARG A 310     5876   6018   6786   -172    -14   -417       N  
ATOM   1125  N   GLY A 311     -10.394  23.314  34.295  1.00 23.74           N  
ANISOU 1125  N   GLY A 311     2827   2717   3477   -179    173   -183       N  
ATOM   1126  CA  GLY A 311      -9.524  22.875  35.370  1.00 22.33           C  
ANISOU 1126  CA  GLY A 311     2684   2511   3290   -194    189   -155       C  
ATOM   1127  C   GLY A 311      -8.567  21.792  34.924  1.00 21.03           C  
ANISOU 1127  C   GLY A 311     2546   2308   3135   -196    162   -161       C  
ATOM   1128  O   GLY A 311      -7.828  21.958  33.945  1.00 21.95           O  
ANISOU 1128  O   GLY A 311     2669   2432   3237   -166    140   -182       O  
ATOM   1129  N   TRP A 312      -8.624  20.658  35.614  1.00 21.50           N  
ANISOU 1129  N   TRP A 312     2617   2329   3221   -231    161   -142       N  
ATOM   1130  CA  TRP A 312      -7.689  19.562  35.348  1.00 24.09           C  
ANISOU 1130  CA  TRP A 312     2974   2609   3571   -227    127   -152       C  
ATOM   1131  C   TRP A 312      -7.838  18.876  33.998  1.00 27.10           C  
ANISOU 1131  C   TRP A 312     3338   2980   3980   -215     85   -205       C  
ATOM   1132  O   TRP A 312      -6.917  18.184  33.557  1.00 23.49           O  
ANISOU 1132  O   TRP A 312     2898   2496   3532   -192     52   -233       O  
ATOM   1133  CB  TRP A 312      -7.715  18.556  36.501  1.00 26.09           C  
ANISOU 1133  CB  TRP A 312     3248   2814   3851   -270    127   -107       C  
ATOM   1134  CG  TRP A 312      -7.125  19.203  37.720  1.00 28.61           C  
ANISOU 1134  CG  TRP A 312     3591   3154   4127   -267    160    -66       C  
ATOM   1135  CD1 TRP A 312      -7.793  19.884  38.700  1.00 28.96           C  
ANISOU 1135  CD1 TRP A 312     3618   3243   4142   -287    202    -37       C  
ATOM   1136  CD2 TRP A 312      -5.735  19.284  38.050  1.00 26.07           C  
ANISOU 1136  CD2 TRP A 312     3305   2819   3780   -237    152    -59       C  
ATOM   1137  NE1 TRP A 312      -6.902  20.355  39.637  1.00 27.06           N  
ANISOU 1137  NE1 TRP A 312     3405   3015   3862   -272    218    -14       N  
ATOM   1138  CE2 TRP A 312      -5.634  19.991  39.267  1.00 27.71           C  
ANISOU 1138  CE2 TRP A 312     3521   3059   3947   -244    188    -24       C  
ATOM   1139  CE3 TRP A 312      -4.562  18.793  37.450  1.00 27.13           C  
ANISOU 1139  CE3 TRP A 312     3462   2924   3922   -203    116    -87       C  
ATOM   1140  CZ2 TRP A 312      -4.398  20.247  39.890  1.00 27.60           C  
ANISOU 1140  CZ2 TRP A 312     3538   3045   3902   -220    187    -12       C  
ATOM   1141  CZ3 TRP A 312      -3.343  19.049  38.065  1.00 32.57           C  
ANISOU 1141  CZ3 TRP A 312     4178   3615   4580   -180    118    -73       C  
ATOM   1142  CH2 TRP A 312      -3.272  19.771  39.274  1.00 31.32           C  
ANISOU 1142  CH2 TRP A 312     4031   3486   4385   -190    153    -33       C  
ATOM   1143  N   ASP A 313      -8.974  19.077  33.326  1.00 25.81           N  
ANISOU 1143  N   ASP A 313     3134   2844   3828   -224     84   -227       N  
ATOM   1144  CA  ASP A 313      -9.086  18.601  31.945  1.00 28.00           C  
ANISOU 1144  CA  ASP A 313     3389   3129   4119   -204     43   -287       C  
ATOM   1145  C   ASP A 313      -8.023  19.257  31.045  1.00 29.52           C  
ANISOU 1145  C   ASP A 313     3588   3370   4259   -152     35   -311       C  
ATOM   1146  O   ASP A 313      -7.482  18.626  30.130  1.00 23.63           O  
ANISOU 1146  O   ASP A 313     2836   2631   3513   -126      0   -363       O  
ATOM   1147  CB  ASP A 313     -10.475  18.857  31.352  1.00 24.89           C  
ANISOU 1147  CB  ASP A 313     2949   2771   3738   -218     43   -306       C  
ATOM   1148  CG  ASP A 313     -10.618  18.235  29.986  1.00 26.33           C  
ANISOU 1148  CG  ASP A 313     3107   2965   3934   -199     -3   -372       C  
ATOM   1149  OD1 ASP A 313     -10.275  17.036  29.877  1.00 24.07           O  
ANISOU 1149  OD1 ASP A 313     2831   2623   3690   -206    -39   -404       O  
ATOM   1150  OD2 ASP A 313     -11.030  18.915  29.026  1.00 24.56           O  
ANISOU 1150  OD2 ASP A 313     2852   2802   3678   -174     -9   -396       O  
ATOM   1151  N   GLY A 314      -7.716  20.525  31.301  1.00 22.39           N  
ANISOU 1151  N   GLY A 314     2692   2504   3311   -138     65   -276       N  
ATOM   1152  CA  GLY A 314      -6.675  21.193  30.525  1.00 21.11           C  
ANISOU 1152  CA  GLY A 314     2533   2391   3098   -102     58   -283       C  
ATOM   1153  C   GLY A 314      -5.341  20.484  30.662  1.00 23.88           C  
ANISOU 1153  C   GLY A 314     2908   2724   3443    -86     45   -299       C  
ATOM   1154  O   GLY A 314      -4.631  20.289  29.683  1.00 24.71           O  
ANISOU 1154  O   GLY A 314     2997   2871   3519    -57     23   -338       O  
ATOM   1155  N   PHE A 315      -5.005  20.120  31.898  1.00 23.84           N  
ANISOU 1155  N   PHE A 315     2934   2664   3460   -102     58   -270       N  
ATOM   1156  CA  PHE A 315      -3.793  19.374  32.239  1.00 23.55           C  
ANISOU 1156  CA  PHE A 315     2922   2599   3427    -85     41   -281       C  
ATOM   1157  C   PHE A 315      -3.783  18.012  31.539  1.00 26.63           C  
ANISOU 1157  C   PHE A 315     3303   2959   3858    -71     -7   -343       C  
ATOM   1158  O   PHE A 315      -2.840  17.663  30.834  1.00 24.47           O  
ANISOU 1158  O   PHE A 315     3020   2711   3566    -31    -32   -393       O  
ATOM   1159  CB  PHE A 315      -3.766  19.181  33.756  1.00 21.55           C  
ANISOU 1159  CB  PHE A 315     2702   2292   3194   -112     60   -230       C  
ATOM   1160  CG  PHE A 315      -2.595  18.376  34.277  1.00 24.42           C  
ANISOU 1160  CG  PHE A 315     3095   2616   3568    -95     37   -232       C  
ATOM   1161  CD1 PHE A 315      -1.310  18.923  34.331  1.00 27.22           C  
ANISOU 1161  CD1 PHE A 315     3458   3006   3879    -65     43   -234       C  
ATOM   1162  CD2 PHE A 315      -2.792  17.095  34.765  1.00 27.90           C  
ANISOU 1162  CD2 PHE A 315     3553   2982   4065   -112      6   -228       C  
ATOM   1163  CE1 PHE A 315      -0.234  18.182  34.830  1.00 26.24           C  
ANISOU 1163  CE1 PHE A 315     3356   2849   3765    -44     19   -240       C  
ATOM   1164  CE2 PHE A 315      -1.719  16.337  35.274  1.00 26.89           C  
ANISOU 1164  CE2 PHE A 315     3454   2810   3953    -91    -24   -228       C  
ATOM   1165  CZ  PHE A 315      -0.445  16.872  35.303  1.00 25.67           C  
ANISOU 1165  CZ  PHE A 315     3305   2697   3752    -53    -17   -238       C  
ATOM   1166  N   VAL A 316      -4.855  17.252  31.734  1.00 26.44           N  
ANISOU 1166  N   VAL A 316     3275   2881   3891   -104    -21   -344       N  
ATOM   1167  CA  VAL A 316      -4.989  15.931  31.115  1.00 27.04           C  
ANISOU 1167  CA  VAL A 316     3341   2910   4022    -96    -76   -406       C  
ATOM   1168  C   VAL A 316      -4.787  15.990  29.597  1.00 27.92           C  
ANISOU 1168  C   VAL A 316     3415   3093   4102    -51   -101   -486       C  
ATOM   1169  O   VAL A 316      -3.997  15.229  29.037  1.00 24.17           O  
ANISOU 1169  O   VAL A 316     2934   2615   3634    -10   -142   -553       O  
ATOM   1170  CB  VAL A 316      -6.350  15.293  31.471  1.00 26.02           C  
ANISOU 1170  CB  VAL A 316     3205   2723   3959   -151    -85   -388       C  
ATOM   1171  CG1 VAL A 316      -6.615  14.049  30.600  1.00 28.57           C  
ANISOU 1171  CG1 VAL A 316     3511   3000   4346   -143   -150   -465       C  
ATOM   1172  CG2 VAL A 316      -6.367  14.914  32.947  1.00 27.39           C  
ANISOU 1172  CG2 VAL A 316     3414   2829   4163   -195    -72   -312       C  
ATOM   1173  N   GLU A 317      -5.468  16.924  28.936  1.00 25.37           N  
ANISOU 1173  N   GLU A 317     3062   2842   3736    -55    -77   -480       N  
ATOM   1174  CA  GLU A 317      -5.388  17.001  27.481  1.00 23.74           C  
ANISOU 1174  CA  GLU A 317     2815   2717   3488    -18   -101   -546       C  
ATOM   1175  C   GLU A 317      -4.031  17.523  27.008  1.00 24.32           C  
ANISOU 1175  C   GLU A 317     2882   2869   3488     23    -93   -557       C  
ATOM   1176  O   GLU A 317      -3.511  17.076  25.991  1.00 27.01           O  
ANISOU 1176  O   GLU A 317     3192   3269   3800     63   -123   -631       O  
ATOM   1177  CB  GLU A 317      -6.529  17.842  26.913  1.00 27.48           C  
ANISOU 1177  CB  GLU A 317     3259   3245   3938    -35    -85   -528       C  
ATOM   1178  CG  GLU A 317      -7.921  17.312  27.308  1.00 27.79           C  
ANISOU 1178  CG  GLU A 317     3290   3222   4046    -77    -92   -525       C  
ATOM   1179  CD  GLU A 317      -8.177  15.877  26.839  1.00 28.93           C  
ANISOU 1179  CD  GLU A 317     3422   3317   4255    -76   -148   -603       C  
ATOM   1180  OE1 GLU A 317      -7.473  15.391  25.943  1.00 27.01           O  
ANISOU 1180  OE1 GLU A 317     3163   3106   3993    -32   -185   -678       O  
ATOM   1181  OE2 GLU A 317      -9.109  15.238  27.371  1.00 26.32           O  
ANISOU 1181  OE2 GLU A 317     3090   2915   3993   -122   -159   -591       O  
ATOM   1182  N   PHE A 318      -3.440  18.448  27.758  1.00 21.49           N  
ANISOU 1182  N   PHE A 318     2548   2518   3098     12    -53   -487       N  
ATOM   1183  CA  PHE A 318      -2.161  19.013  27.332  1.00 24.27           C  
ANISOU 1183  CA  PHE A 318     2890   2951   3382     40    -44   -488       C  
ATOM   1184  C   PHE A 318      -1.105  17.917  27.258  1.00 23.95           C  
ANISOU 1184  C   PHE A 318     2847   2901   3353     80    -77   -557       C  
ATOM   1185  O   PHE A 318      -0.294  17.871  26.342  1.00 24.99           O  
ANISOU 1185  O   PHE A 318     2942   3122   3429    117    -89   -609       O  
ATOM   1186  CB  PHE A 318      -1.702  20.158  28.265  1.00 25.53           C  
ANISOU 1186  CB  PHE A 318     3078   3105   3518     18     -3   -405       C  
ATOM   1187  CG  PHE A 318      -0.416  20.807  27.826  1.00 28.31           C  
ANISOU 1187  CG  PHE A 318     3413   3541   3802     35      7   -397       C  
ATOM   1188  CD1 PHE A 318      -0.402  21.676  26.747  1.00 30.49           C  
ANISOU 1188  CD1 PHE A 318     3654   3915   4014     33     12   -381       C  
ATOM   1189  CD2 PHE A 318       0.783  20.513  28.462  1.00 26.82           C  
ANISOU 1189  CD2 PHE A 318     3240   3340   3611     50      8   -403       C  
ATOM   1190  CE1 PHE A 318       0.791  22.259  26.320  1.00 33.60           C  
ANISOU 1190  CE1 PHE A 318     4027   4398   4343     38     21   -365       C  
ATOM   1191  CE2 PHE A 318       1.981  21.096  28.040  1.00 27.86           C  
ANISOU 1191  CE2 PHE A 318     3347   3561   3679     60     17   -397       C  
ATOM   1192  CZ  PHE A 318       1.981  21.972  26.974  1.00 29.15           C  
ANISOU 1192  CZ  PHE A 318     3473   3824   3778     50     26   -375       C  
ATOM   1193  N   PHE A 319      -1.131  17.025  28.238  1.00 24.72           N  
ANISOU 1193  N   PHE A 319     2979   2891   3521     73    -94   -557       N  
ATOM   1194  CA  PHE A 319      -0.131  15.977  28.345  1.00 23.68           C  
ANISOU 1194  CA  PHE A 319     2853   2729   3416    115   -134   -617       C  
ATOM   1195  C   PHE A 319      -0.582  14.634  27.768  1.00 25.80           C  
ANISOU 1195  C   PHE A 319     3109   2946   3750    138   -196   -706       C  
ATOM   1196  O   PHE A 319       0.094  13.629  27.942  1.00 28.06           O  
ANISOU 1196  O   PHE A 319     3404   3178   4080    174   -242   -759       O  
ATOM   1197  CB  PHE A 319       0.277  15.803  29.799  1.00 22.16           C  
ANISOU 1197  CB  PHE A 319     2710   2448   3261     97   -126   -556       C  
ATOM   1198  CG  PHE A 319       1.102  16.958  30.325  1.00 23.21           C  
ANISOU 1198  CG  PHE A 319     2852   2635   3333     91    -80   -495       C  
ATOM   1199  CD1 PHE A 319       2.356  17.213  29.803  1.00 25.38           C  
ANISOU 1199  CD1 PHE A 319     3099   2993   3550    129    -80   -530       C  
ATOM   1200  CD2 PHE A 319       0.605  17.791  31.317  1.00 24.10           C  
ANISOU 1200  CD2 PHE A 319     2994   2719   3445     46    -38   -411       C  
ATOM   1201  CE1 PHE A 319       3.139  18.287  30.279  1.00 27.57           C  
ANISOU 1201  CE1 PHE A 319     3381   3317   3777    116    -42   -473       C  
ATOM   1202  CE2 PHE A 319       1.375  18.857  31.805  1.00 24.15           C  
ANISOU 1202  CE2 PHE A 319     3008   2767   3402     40     -4   -364       C  
ATOM   1203  CZ  PHE A 319       2.642  19.106  31.282  1.00 27.69           C  
ANISOU 1203  CZ  PHE A 319     3432   3291   3800     72     -7   -392       C  
ATOM   1204  N   HIS A 320      -1.722  14.642  27.095  1.00 27.70           N  
ANISOU 1204  N   HIS A 320     3327   3200   4000    119   -201   -724       N  
ATOM   1205  CA  HIS A 320      -2.275  13.414  26.541  1.00 26.91           C  
ANISOU 1205  CA  HIS A 320     3211   3044   3968    133   -264   -811       C  
ATOM   1206  C   HIS A 320      -1.391  12.866  25.431  1.00 32.72           C  
ANISOU 1206  C   HIS A 320     3905   3856   4673    206   -307   -931       C  
ATOM   1207  O   HIS A 320      -1.077  13.575  24.482  1.00 35.08           O  
ANISOU 1207  O   HIS A 320     4160   4291   4879    230   -285   -955       O  
ATOM   1208  CB  HIS A 320      -3.681  13.660  25.992  1.00 26.90           C  
ANISOU 1208  CB  HIS A 320     3187   3060   3974     97   -258   -808       C  
ATOM   1209  CG  HIS A 320      -4.357  12.416  25.527  1.00 28.53           C  
ANISOU 1209  CG  HIS A 320     3378   3198   4262    101   -325   -893       C  
ATOM   1210  ND1 HIS A 320      -4.722  11.405  26.395  1.00 32.76           N  
ANISOU 1210  ND1 HIS A 320     3950   3592   4906     67   -362   -876       N  
ATOM   1211  CD2 HIS A 320      -4.714  11.997  24.290  1.00 26.40           C  
ANISOU 1211  CD2 HIS A 320     3062   2983   3987    132   -367   -995       C  
ATOM   1212  CE1 HIS A 320      -5.279  10.422  25.711  1.00 31.00           C  
ANISOU 1212  CE1 HIS A 320     3703   3326   4748     75   -427   -965       C  
ATOM   1213  NE2 HIS A 320      -5.283  10.756  24.436  1.00 32.37           N  
ANISOU 1213  NE2 HIS A 320     3826   3619   4853    118   -431  -1045       N  
ATOM   1214  N   VAL A 321      -1.017  11.594  25.555  1.00 33.53           N  
ANISOU 1214  N   VAL A 321     4016   3870   4853    241   -374  -1007       N  
ATOM   1215  CA  VAL A 321      -0.267  10.903  24.509  1.00 41.43           C  
ANISOU 1215  CA  VAL A 321     4970   4935   5837    321   -427  -1145       C  
ATOM   1216  C   VAL A 321      -1.020   9.647  24.047  1.00 43.49           C  
ANISOU 1216  C   VAL A 321     5222   5106   6197    333   -508  -1244       C  
ATOM   1217  O   VAL A 321      -1.801   9.068  24.805  1.00 47.03           O  
ANISOU 1217  O   VAL A 321     5712   5411   6748    282   -533  -1198       O  
ATOM   1218  CB  VAL A 321       1.128  10.505  24.998  1.00 39.91           C  
ANISOU 1218  CB  VAL A 321     4789   4725   5650    373   -447  -1172       C  
ATOM   1219  CG1 VAL A 321       1.965  11.744  25.270  1.00 35.63           C  
ANISOU 1219  CG1 VAL A 321     4243   4291   5005    365   -374  -1093       C  
ATOM   1220  CG2 VAL A 321       1.018   9.634  26.249  1.00 44.43           C  
ANISOU 1220  CG2 VAL A 321     5425   5114   6341    349   -488  -1125       C  
ATOM   1221  N   GLU A 322      -0.793   9.237  22.804  1.00 47.48           N  
ANISOU 1221  N   GLU A 322     5669   5701   6670    398   -550  -1381       N  
ATOM   1222  CA  GLU A 322      -1.494   8.076  22.244  1.00 58.62           C  
ANISOU 1222  CA  GLU A 322     7064   7035   8175    415   -634  -1493       C  
ATOM   1223  C   GLU A 322      -0.736   6.771  22.490  1.00 68.69           C  
ANISOU 1223  C   GLU A 322     8353   8195   9550    477   -724  -1591       C  
ATOM   1224  O   GLU A 322      -0.949   6.092  23.497  1.00 74.19           O  
ANISOU 1224  O   GLU A 322     9107   8719  10364    441   -761  -1536       O  
ATOM   1225  CB  GLU A 322      -1.746   8.260  20.739  1.00 55.33           C  
ANISOU 1225  CB  GLU A 322     6572   6777   7672    457   -642  -1604       C  
ATOM   1226  CG  GLU A 322      -2.335   9.610  20.343  1.00 51.13           C  
ANISOU 1226  CG  GLU A 322     6021   6378   7029    410   -562  -1512       C  
ATOM   1227  CD  GLU A 322      -3.627   9.929  21.079  1.00 49.74           C  
ANISOU 1227  CD  GLU A 322     5887   6100   6914    321   -534  -1397       C  
ATOM   1228  OE1 GLU A 322      -4.207   9.009  21.693  1.00 47.14           O  
ANISOU 1228  OE1 GLU A 322     5590   5613   6709    291   -582  -1400       O  
ATOM   1229  OE2 GLU A 322      -4.062  11.098  21.044  1.00 51.16           O  
ANISOU 1229  OE2 GLU A 322     6063   6358   7018    282   -469  -1303       O  
TER    1230      GLU A 322                                                      
ATOM   1231  N   ARG B   1      20.637  35.543  45.233  1.00 61.24           N  
ANISOU 1231  N   ARG B   1     7554   7787   7929   -341   -110   -200       N  
ATOM   1232  CA  ARG B   1      19.772  34.909  46.221  1.00 58.47           C  
ANISOU 1232  CA  ARG B   1     7257   7402   7559   -273   -100   -235       C  
ATOM   1233  C   ARG B   1      19.356  33.525  45.751  1.00 53.19           C  
ANISOU 1233  C   ARG B   1     6601   6763   6848   -221    -66   -221       C  
ATOM   1234  O   ARG B   1      19.074  33.329  44.566  1.00 46.04           O  
ANISOU 1234  O   ARG B   1     5683   5868   5943   -237    -46   -184       O  
ATOM   1235  CB  ARG B   1      18.523  35.751  46.474  1.00 64.52           C  
ANISOU 1235  CB  ARG B   1     8066   8078   8371   -279   -107   -238       C  
ATOM   1236  CG  ARG B   1      17.460  35.015  47.269  1.00 69.81           C  
ANISOU 1236  CG  ARG B   1     8783   8730   9013   -215    -86   -263       C  
ATOM   1237  CD  ARG B   1      16.077  35.523  46.941  1.00 79.38           C  
ANISOU 1237  CD  ARG B   1    10025   9873  10261   -217    -77   -251       C  
ATOM   1238  NE  ARG B   1      15.819  36.843  47.505  1.00 88.31           N  
ANISOU 1238  NE  ARG B   1    11163  10945  11445   -236   -114   -287       N  
ATOM   1239  CZ  ARG B   1      14.694  37.525  47.318  1.00 96.17           C  
ANISOU 1239  CZ  ARG B   1    12181  11874  12486   -235   -121   -289       C  
ATOM   1240  NH1 ARG B   1      13.720  37.011  46.576  1.00 97.17           N  
ANISOU 1240  NH1 ARG B   1    12323  11992  12607   -222    -89   -253       N  
ATOM   1241  NH2 ARG B   1      14.541  38.722  47.871  1.00101.20           N  
ANISOU 1241  NH2 ARG B   1    12820  12452  13178   -244   -164   -334       N  
ATOM   1242  N   PRO B   2      19.316  32.561  46.686  1.00 51.90           N  
ANISOU 1242  N   PRO B   2     6461   6611   6647   -161    -63   -249       N  
ATOM   1243  CA  PRO B   2      18.954  31.177  46.369  1.00 48.89           C  
ANISOU 1243  CA  PRO B   2     6096   6244   6237   -111    -42   -237       C  
ATOM   1244  C   PRO B   2      17.526  31.074  45.863  1.00 43.18           C  
ANISOU 1244  C   PRO B   2     5409   5465   5531   -110    -16   -211       C  
ATOM   1245  O   PRO B   2      17.237  30.184  45.078  1.00 41.64           O  
ANISOU 1245  O   PRO B   2     5214   5278   5328    -90      0   -196       O  
ATOM   1246  CB  PRO B   2      19.079  30.464  47.718  1.00 50.69           C  
ANISOU 1246  CB  PRO B   2     6351   6478   6432    -59    -55   -261       C  
ATOM   1247  CG  PRO B   2      20.021  31.313  48.508  1.00 53.21           C  
ANISOU 1247  CG  PRO B   2     6644   6823   6749    -78    -85   -294       C  
ATOM   1248  CD  PRO B   2      19.727  32.714  48.092  1.00 51.46           C  
ANISOU 1248  CD  PRO B   2     6414   6562   6576   -139    -88   -291       C  
ATOM   1249  N   GLU B   3      16.650  31.968  46.312  1.00 41.11           N  
ANISOU 1249  N   GLU B   3     5174   5150   5296   -127    -16   -214       N  
ATOM   1250  CA  GLU B   3      15.242  31.908  45.924  1.00 40.67           C  
ANISOU 1250  CA  GLU B   3     5149   5046   5257   -123      6   -194       C  
ATOM   1251  C   GLU B   3      15.014  32.392  44.497  1.00 35.31           C  
ANISOU 1251  C   GLU B   3     4451   4358   4607   -163     13   -159       C  
ATOM   1252  O   GLU B   3      14.192  31.835  43.782  1.00 33.92           O  
ANISOU 1252  O   GLU B   3     4286   4171   4430   -151     34   -139       O  
ATOM   1253  CB  GLU B   3      14.355  32.660  46.926  1.00 45.25           C  
ANISOU 1253  CB  GLU B   3     5757   5583   5852   -118      2   -219       C  
ATOM   1254  CG  GLU B   3      14.157  31.901  48.246  1.00 46.96           C  
ANISOU 1254  CG  GLU B   3     5997   5821   6023    -75      7   -240       C  
ATOM   1255  CD  GLU B   3      13.311  32.656  49.262  1.00 50.61           C  
ANISOU 1255  CD  GLU B   3     6475   6265   6487    -66      5   -276       C  
ATOM   1256  OE1 GLU B   3      12.477  33.501  48.863  1.00 43.49           O  
ANISOU 1256  OE1 GLU B   3     5577   5320   5628    -81      6   -283       O  
ATOM   1257  OE2 GLU B   3      13.478  32.394  50.471  1.00 57.48           O  
ANISOU 1257  OE2 GLU B   3     7352   7172   7314    -40      0   -301       O  
ATOM   1258  N   ILE B   4      15.748  33.422  44.084  1.00 31.57           N  
ANISOU 1258  N   ILE B   4     3947   3892   4157   -212     -7   -148       N  
ATOM   1259  CA  ILE B   4      15.697  33.905  42.708  1.00 31.61           C  
ANISOU 1259  CA  ILE B   4     3927   3903   4179   -258     -5   -102       C  
ATOM   1260  C   ILE B   4      16.282  32.867  41.753  1.00 34.60           C  
ANISOU 1260  C   ILE B   4     4272   4362   4514   -246     15    -90       C  
ATOM   1261  O   ILE B   4      15.762  32.645  40.656  1.00 28.21           O  
ANISOU 1261  O   ILE B   4     3455   3565   3698   -252     31    -62       O  
ATOM   1262  CB  ILE B   4      16.465  35.247  42.558  1.00 48.61           C  
ANISOU 1262  CB  ILE B   4     6052   6048   6370   -324    -37    -82       C  
ATOM   1263  CG1 ILE B   4      15.736  36.370  43.299  1.00 50.82           C  
ANISOU 1263  CG1 ILE B   4     6366   6236   6708   -333    -66    -99       C  
ATOM   1264  CG2 ILE B   4      16.639  35.623  41.093  1.00 42.22           C  
ANISOU 1264  CG2 ILE B   4     5208   5272   5562   -379    -34    -18       C  
ATOM   1265  CD1 ILE B   4      16.490  37.692  43.276  1.00 59.16           C  
ANISOU 1265  CD1 ILE B   4     7399   7264   7815   -399   -111    -85       C  
ATOM   1266  N   TRP B   5      17.368  32.227  42.171  1.00 36.23           N  
ANISOU 1266  N   TRP B   5     4453   4625   4689   -223     10   -120       N  
ATOM   1267  CA  TRP B   5      17.986  31.207  41.338  1.00 36.12           C  
ANISOU 1267  CA  TRP B   5     4399   4690   4634   -199     23   -127       C  
ATOM   1268  C   TRP B   5      17.070  29.987  41.184  1.00 30.65           C  
ANISOU 1268  C   TRP B   5     3740   3972   3932   -142     38   -140       C  
ATOM   1269  O   TRP B   5      16.943  29.429  40.092  1.00 29.83           O  
ANISOU 1269  O   TRP B   5     3614   3908   3813   -133     50   -137       O  
ATOM   1270  CB  TRP B   5      19.368  30.793  41.868  1.00 38.28           C  
ANISOU 1270  CB  TRP B   5     4636   5029   4881   -179      7   -162       C  
ATOM   1271  CG  TRP B   5      19.893  29.606  41.110  1.00 37.98           C  
ANISOU 1271  CG  TRP B   5     4559   5066   4806   -135     14   -187       C  
ATOM   1272  CD1 TRP B   5      20.489  29.613  39.877  1.00 43.11           C  
ANISOU 1272  CD1 TRP B   5     5145   5809   5427   -157     24   -181       C  
ATOM   1273  CD2 TRP B   5      19.822  28.236  41.513  1.00 39.27           C  
ANISOU 1273  CD2 TRP B   5     4745   5218   4959    -59      6   -225       C  
ATOM   1274  NE1 TRP B   5      20.806  28.329  39.499  1.00 41.48           N  
ANISOU 1274  NE1 TRP B   5     4916   5652   5192    -91     23   -228       N  
ATOM   1275  CE2 TRP B   5      20.401  27.466  40.483  1.00 40.20           C  
ANISOU 1275  CE2 TRP B   5     4809   5416   5048    -31      8   -252       C  
ATOM   1276  CE3 TRP B   5      19.328  27.583  42.646  1.00 42.74           C  
ANISOU 1276  CE3 TRP B   5     5241   5589   5408    -14     -5   -234       C  
ATOM   1277  CZ2 TRP B   5      20.503  26.080  40.557  1.00 45.33           C  
ANISOU 1277  CZ2 TRP B   5     5466   6065   5694     45     -9   -296       C  
ATOM   1278  CZ3 TRP B   5      19.432  26.209  42.715  1.00 44.19           C  
ANISOU 1278  CZ3 TRP B   5     5433   5771   5585     52    -21   -261       C  
ATOM   1279  CH2 TRP B   5      20.016  25.472  41.678  1.00 42.88           C  
ANISOU 1279  CH2 TRP B   5     5218   5670   5405     84    -26   -295       C  
ATOM   1280  N   ALA B   6      16.424  29.578  42.269  1.00 30.88           N  
ANISOU 1280  N   ALA B   6     3819   3941   3972   -108     36   -153       N  
ATOM   1281  CA  ALA B   6      15.490  28.459  42.197  1.00 30.05           C  
ANISOU 1281  CA  ALA B   6     3748   3803   3867    -66     47   -156       C  
ATOM   1282  C   ALA B   6      14.322  28.755  41.251  1.00 29.00           C  
ANISOU 1282  C   ALA B   6     3624   3642   3753    -87     65   -131       C  
ATOM   1283  O   ALA B   6      13.893  27.898  40.472  1.00 27.66           O  
ANISOU 1283  O   ALA B   6     3451   3479   3578    -65     72   -135       O  
ATOM   1284  CB  ALA B   6      14.980  28.099  43.589  1.00 28.83           C  
ANISOU 1284  CB  ALA B   6     3641   3600   3715    -39     43   -161       C  
ATOM   1285  N   ALA B   7      13.807  29.977  41.309  1.00 26.80           N  
ANISOU 1285  N   ALA B   7     3355   3330   3499   -128     67   -108       N  
ATOM   1286  CA  ALA B   7      12.720  30.360  40.412  1.00 27.14           C  
ANISOU 1286  CA  ALA B   7     3404   3346   3560   -147     78    -82       C  
ATOM   1287  C   ALA B   7      13.179  30.338  38.956  1.00 24.95           C  
ANISOU 1287  C   ALA B   7     3082   3135   3262   -168     81    -63       C  
ATOM   1288  O   ALA B   7      12.481  29.840  38.076  1.00 25.68           O  
ANISOU 1288  O   ALA B   7     3172   3236   3348   -157     92    -58       O  
ATOM   1289  CB  ALA B   7      12.171  31.726  40.790  1.00 27.84           C  
ANISOU 1289  CB  ALA B   7     3510   3381   3687   -180     67    -66       C  
ATOM   1290  N   GLN B   8      14.356  30.891  38.692  1.00 28.03           N  
ANISOU 1290  N   GLN B   8     3430   3582   3637   -201     72    -52       N  
ATOM   1291  CA  GLN B   8      14.906  30.866  37.340  1.00 28.15           C  
ANISOU 1291  CA  GLN B   8     3391   3686   3617   -225     78    -33       C  
ATOM   1292  C   GLN B   8      15.030  29.408  36.831  1.00 25.19           C  
ANISOU 1292  C   GLN B   8     2999   3364   3208   -167     87    -79       C  
ATOM   1293  O   GLN B   8      14.761  29.115  35.672  1.00 25.33           O  
ANISOU 1293  O   GLN B   8     2989   3433   3200   -166     96    -75       O  
ATOM   1294  CB  GLN B   8      16.278  31.511  37.350  1.00 31.65           C  
ANISOU 1294  CB  GLN B   8     3786   4193   4045   -267     67    -21       C  
ATOM   1295  CG  GLN B   8      16.631  32.276  36.102  1.00 51.42           C  
ANISOU 1295  CG  GLN B   8     6239   6770   6527   -332     69     36       C  
ATOM   1296  CD  GLN B   8      17.732  33.299  36.355  1.00 65.64           C  
ANISOU 1296  CD  GLN B   8     8004   8598   8336   -397     51     67       C  
ATOM   1297  OE1 GLN B   8      18.053  33.616  37.507  1.00 65.15           O  
ANISOU 1297  OE1 GLN B   8     7965   8481   8307   -395     34     43       O  
ATOM   1298  NE2 GLN B   8      18.314  33.822  35.277  1.00 71.30           N  
ANISOU 1298  NE2 GLN B   8     8663   9406   9022   -460     54    121       N  
ATOM   1299  N   GLU B   9      15.490  28.524  37.706  1.00 25.92           N  
ANISOU 1299  N   GLU B   9     3103   3446   3299   -119     79   -123       N  
ATOM   1300  CA  GLU B   9      15.716  27.121  37.353  1.00 30.90           C  
ANISOU 1300  CA  GLU B   9     3718   4110   3911    -58     74   -174       C  
ATOM   1301  C   GLU B   9      14.381  26.403  37.077  1.00 24.63           C  
ANISOU 1301  C   GLU B   9     2965   3255   3140    -32     78   -179       C  
ATOM   1302  O   GLU B   9      14.238  25.708  36.072  1.00 23.14           O  
ANISOU 1302  O   GLU B   9     2749   3107   2935     -8     78   -207       O  
ATOM   1303  CB  GLU B   9      16.473  26.414  38.484  1.00 31.82           C  
ANISOU 1303  CB  GLU B   9     3847   4211   4032    -13     54   -210       C  
ATOM   1304  CG  GLU B   9      17.053  25.065  38.097  1.00 36.20           C  
ANISOU 1304  CG  GLU B   9     4374   4808   4572     52     35   -268       C  
ATOM   1305  CD  GLU B   9      18.236  25.214  37.154  1.00 39.82           C  
ANISOU 1305  CD  GLU B   9     4751   5395   4985     48     37   -296       C  
ATOM   1306  OE1 GLU B   9      19.140  26.020  37.449  1.00 43.88           O  
ANISOU 1306  OE1 GLU B   9     5232   5958   5482     12     39   -280       O  
ATOM   1307  OE2 GLU B   9      18.265  24.537  36.117  1.00 40.89           O  
ANISOU 1307  OE2 GLU B   9     4848   5590   5098     80     36   -336       O  
ATOM   1308  N   LEU B  10      13.401  26.590  37.964  1.00 23.95           N  
ANISOU 1308  N   LEU B  10     2934   3078   3087    -38     82   -157       N  
ATOM   1309  CA  LEU B  10      12.091  25.940  37.804  1.00 26.00           C  
ANISOU 1309  CA  LEU B  10     3227   3280   3371    -21     87   -158       C  
ATOM   1310  C   LEU B  10      11.358  26.475  36.580  1.00 23.54           C  
ANISOU 1310  C   LEU B  10     2898   2991   3055    -49     99   -138       C  
ATOM   1311  O   LEU B  10      10.682  25.734  35.851  1.00 22.29           O  
ANISOU 1311  O   LEU B  10     2737   2832   2900    -28     98   -157       O  
ATOM   1312  CB  LEU B  10      11.251  26.138  39.056  1.00 29.37           C  
ANISOU 1312  CB  LEU B  10     3706   3627   3826    -27     92   -137       C  
ATOM   1313  CG  LEU B  10      11.733  25.296  40.232  1.00 31.54           C  
ANISOU 1313  CG  LEU B  10     4005   3878   4102      6     77   -151       C  
ATOM   1314  CD1 LEU B  10      11.221  25.894  41.555  1.00 29.00           C  
ANISOU 1314  CD1 LEU B  10     3719   3513   3786    -10     85   -128       C  
ATOM   1315  CD2 LEU B  10      11.264  23.849  40.053  1.00 27.44           C  
ANISOU 1315  CD2 LEU B  10     3501   3324   3601     42     62   -168       C  
ATOM   1316  N   ARG B  11      11.502  27.773  36.333  1.00 23.61           N  
ANISOU 1316  N   ARG B  11     2893   3020   3059    -96    105    -97       N  
ATOM   1317  CA  ARG B  11      10.925  28.343  35.126  1.00 22.89           C  
ANISOU 1317  CA  ARG B  11     2781   2958   2957   -125    110    -67       C  
ATOM   1318  C   ARG B  11      11.557  27.790  33.840  1.00 20.77           C  
ANISOU 1318  C   ARG B  11     2457   2797   2640   -114    111    -88       C  
ATOM   1319  O   ARG B  11      10.847  27.499  32.879  1.00 22.01           O  
ANISOU 1319  O   ARG B  11     2602   2976   2784   -107    113    -93       O  
ATOM   1320  CB  ARG B  11      11.036  29.870  35.149  1.00 21.46           C  
ANISOU 1320  CB  ARG B  11     2599   2767   2789   -181    106    -11       C  
ATOM   1321  CG  ARG B  11      10.283  30.536  34.002  1.00 21.52           C  
ANISOU 1321  CG  ARG B  11     2595   2789   2794   -212    104     35       C  
ATOM   1322  CD  ARG B  11      10.652  32.047  33.895  1.00 30.34           C  
ANISOU 1322  CD  ARG B  11     3704   3899   3927   -274     87    100       C  
ATOM   1323  NE  ARG B  11       9.977  32.838  34.924  1.00 27.98           N  
ANISOU 1323  NE  ARG B  11     3451   3492   3689   -278     73    105       N  
ATOM   1324  CZ  ARG B  11      10.339  34.063  35.304  1.00 26.68           C  
ANISOU 1324  CZ  ARG B  11     3292   3288   3559   -320     48    139       C  
ATOM   1325  NH1 ARG B  11      11.404  34.654  34.762  1.00 21.90           N  
ANISOU 1325  NH1 ARG B  11     2648   2738   2936   -373     37    183       N  
ATOM   1326  NH2 ARG B  11       9.642  34.692  36.239  1.00 23.87           N  
ANISOU 1326  NH2 ARG B  11     2974   2838   3257   -310     33    124       N  
ATOM   1327  N   ARG B  12      12.886  27.662  33.818  1.00 25.71           N  
ANISOU 1327  N   ARG B  12     3040   3496   3231   -111    108   -108       N  
ATOM   1328  CA  ARG B  12      13.589  27.076  32.679  1.00 26.05           C  
ANISOU 1328  CA  ARG B  12     3019   3660   3219    -92    110   -143       C  
ATOM   1329  C   ARG B  12      13.035  25.680  32.402  1.00 23.55           C  
ANISOU 1329  C   ARG B  12     2711   3325   2911    -27     99   -211       C  
ATOM   1330  O   ARG B  12      12.681  25.361  31.276  1.00 24.10           O  
ANISOU 1330  O   ARG B  12     2750   3456   2951    -17    100   -232       O  
ATOM   1331  CB  ARG B  12      15.108  27.003  32.942  1.00 27.92           C  
ANISOU 1331  CB  ARG B  12     3208   3975   3425    -88    106   -168       C  
ATOM   1332  CG  ARG B  12      15.921  26.472  31.757  1.00 27.53           C  
ANISOU 1332  CG  ARG B  12     3078   4074   3309    -66    109   -213       C  
ATOM   1333  CD  ARG B  12      17.400  26.345  32.113  1.00 24.36           C  
ANISOU 1333  CD  ARG B  12     2625   3751   2881    -55    104   -246       C  
ATOM   1334  NE  ARG B  12      17.669  25.333  33.153  1.00 27.02           N  
ANISOU 1334  NE  ARG B  12     2994   4016   3256     14     81   -308       N  
ATOM   1335  CZ  ARG B  12      17.809  24.026  32.909  1.00 27.63           C  
ANISOU 1335  CZ  ARG B  12     3057   4109   3332     92     60   -392       C  
ATOM   1336  NH1 ARG B  12      17.675  23.565  31.669  1.00 24.94           N  
ANISOU 1336  NH1 ARG B  12     2668   3858   2952    116     62   -435       N  
ATOM   1337  NH2 ARG B  12      18.076  23.177  33.900  1.00 24.04           N  
ANISOU 1337  NH2 ARG B  12     2636   3580   2918    148     31   -432       N  
ATOM   1338  N   ILE B  13      12.965  24.853  33.439  1.00 23.31           N  
ANISOU 1338  N   ILE B  13     2723   3211   2923     14     85   -245       N  
ATOM   1339  CA  ILE B  13      12.553  23.455  33.265  1.00 22.73           C  
ANISOU 1339  CA  ILE B  13     2659   3106   2871     74     64   -308       C  
ATOM   1340  C   ILE B  13      11.072  23.407  32.878  1.00 23.26           C  
ANISOU 1340  C   ILE B  13     2758   3116   2965     61     69   -291       C  
ATOM   1341  O   ILE B  13      10.668  22.668  31.977  1.00 23.32           O  
ANISOU 1341  O   ILE B  13     2744   3148   2967     90     58   -337       O  
ATOM   1342  CB  ILE B  13      12.865  22.632  34.530  1.00 20.44           C  
ANISOU 1342  CB  ILE B  13     2409   2734   2622    112     41   -329       C  
ATOM   1343  CG1 ILE B  13      14.380  22.507  34.699  1.00 20.73           C  
ANISOU 1343  CG1 ILE B  13     2403   2845   2630    138     29   -363       C  
ATOM   1344  CG2 ILE B  13      12.229  21.217  34.457  1.00 22.81           C  
ANISOU 1344  CG2 ILE B  13     2733   2968   2965    163     11   -379       C  
ATOM   1345  CD1 ILE B  13      14.817  22.167  36.112  1.00 20.64           C  
ANISOU 1345  CD1 ILE B  13     2431   2764   2648    159     10   -358       C  
ATOM   1346  N   GLY B  14      10.281  24.263  33.519  1.00 24.02           N  
ANISOU 1346  N   GLY B  14     2895   3143   3087     20     85   -230       N  
ATOM   1347  CA  GLY B  14       8.863  24.331  33.244  1.00 23.55           C  
ANISOU 1347  CA  GLY B  14     2861   3034   3054      6     91   -212       C  
ATOM   1348  C   GLY B  14       8.550  24.676  31.810  1.00 25.17           C  
ANISOU 1348  C   GLY B  14     3026   3317   3222     -6     95   -210       C  
ATOM   1349  O   GLY B  14       7.710  24.019  31.200  1.00 24.04           O  
ANISOU 1349  O   GLY B  14     2881   3166   3089     12     86   -240       O  
ATOM   1350  N   ASP B  15       9.238  25.691  31.265  1.00 23.10           N  
ANISOU 1350  N   ASP B  15     2728   3135   2915    -42    105   -171       N  
ATOM   1351  CA  ASP B  15       9.007  26.106  29.882  1.00 23.38           C  
ANISOU 1351  CA  ASP B  15     2720   3260   2902    -60    107   -153       C  
ATOM   1352  C   ASP B  15       9.542  25.075  28.890  1.00 21.40           C  
ANISOU 1352  C   ASP B  15     2415   3113   2603    -17     99   -228       C  
ATOM   1353  O   ASP B  15       9.011  24.902  27.797  1.00 24.53           O  
ANISOU 1353  O   ASP B  15     2783   3570   2968    -10     95   -244       O  
ATOM   1354  CB  ASP B  15       9.627  27.485  29.622  1.00 25.97           C  
ANISOU 1354  CB  ASP B  15     3025   3642   3198   -120    116    -77       C  
ATOM   1355  CG  ASP B  15       8.801  28.613  30.238  1.00 28.90           C  
ANISOU 1355  CG  ASP B  15     3445   3915   3621   -159    114    -10       C  
ATOM   1356  OD1 ASP B  15       7.619  28.361  30.555  1.00 26.85           O  
ANISOU 1356  OD1 ASP B  15     3223   3574   3403   -141    112    -21       O  
ATOM   1357  OD2 ASP B  15       9.313  29.739  30.421  1.00 29.59           O  
ANISOU 1357  OD2 ASP B  15     3530   4003   3711   -207    111     50       O  
ATOM   1358  N   GLU B  16      10.622  24.411  29.273  1.00 24.26           N  
ANISOU 1358  N   GLU B  16     2758   3501   2957     18     92   -280       N  
ATOM   1359  CA  GLU B  16      11.178  23.344  28.453  1.00 26.91           C  
ANISOU 1359  CA  GLU B  16     3040   3929   3256     74     76   -371       C  
ATOM   1360  C   GLU B  16      10.149  22.222  28.307  1.00 26.86           C  
ANISOU 1360  C   GLU B  16     3061   3849   3297    119     52   -433       C  
ATOM   1361  O   GLU B  16       9.884  21.735  27.208  1.00 30.12           O  
ANISOU 1361  O   GLU B  16     3432   4334   3677    146     40   -487       O  
ATOM   1362  CB  GLU B  16      12.478  22.838  29.105  1.00 26.76           C  
ANISOU 1362  CB  GLU B  16     3002   3928   3236    109     66   -417       C  
ATOM   1363  CG  GLU B  16      13.009  21.545  28.510  1.00 33.00           C  
ANISOU 1363  CG  GLU B  16     3746   4781   4011    187     37   -531       C  
ATOM   1364  CD  GLU B  16      13.791  20.783  29.541  1.00 37.38           C  
ANISOU 1364  CD  GLU B  16     4318   5274   4609    235     11   -575       C  
ATOM   1365  OE1 GLU B  16      14.736  21.381  30.092  1.00 32.20           O  
ANISOU 1365  OE1 GLU B  16     3649   4652   3934    213     24   -542       O  
ATOM   1366  OE2 GLU B  16      13.438  19.621  29.823  1.00 34.91           O  
ANISOU 1366  OE2 GLU B  16     4037   4874   4355    290    -27   -636       O  
ATOM   1367  N   PHE B  17       9.547  21.837  29.425  1.00 29.14           N  
ANISOU 1367  N   PHE B  17     3414   3997   3660    123     42   -421       N  
ATOM   1368  CA  PHE B  17       8.564  20.767  29.434  1.00 32.80           C  
ANISOU 1368  CA  PHE B  17     3906   4375   4180    154     16   -468       C  
ATOM   1369  C   PHE B  17       7.296  21.184  28.702  1.00 37.01           C  
ANISOU 1369  C   PHE B  17     4441   4912   4710    125     26   -442       C  
ATOM   1370  O   PHE B  17       6.681  20.389  28.002  1.00 41.18           O  
ANISOU 1370  O   PHE B  17     4956   5442   5251    153      3   -501       O  
ATOM   1371  CB  PHE B  17       8.247  20.357  30.874  1.00 38.70           C  
ANISOU 1371  CB  PHE B  17     4720   4985   5000    152      8   -441       C  
ATOM   1372  CG  PHE B  17       8.360  18.886  31.112  1.00 44.32           C  
ANISOU 1372  CG  PHE B  17     5444   5633   5764    205    -38   -511       C  
ATOM   1373  CD1 PHE B  17       7.236  18.109  31.293  1.00 51.95           C  
ANISOU 1373  CD1 PHE B  17     6444   6499   6794    204    -59   -518       C  
ATOM   1374  CD2 PHE B  17       9.600  18.281  31.137  1.00 54.04           C  
ANISOU 1374  CD2 PHE B  17     6647   6901   6984    257    -64   -570       C  
ATOM   1375  CE1 PHE B  17       7.353  16.751  31.498  1.00 58.45           C  
ANISOU 1375  CE1 PHE B  17     7282   7250   7677    249   -111   -577       C  
ATOM   1376  CE2 PHE B  17       9.721  16.935  31.338  1.00 54.25           C  
ANISOU 1376  CE2 PHE B  17     6687   6857   7070    311   -117   -636       C  
ATOM   1377  CZ  PHE B  17       8.600  16.167  31.518  1.00 57.55           C  
ANISOU 1377  CZ  PHE B  17     7145   7164   7557    305   -143   -636       C  
ATOM   1378  N   ASN B  18       6.917  22.449  28.845  1.00 34.60           N  
ANISOU 1378  N   ASN B  18     4150   4606   4390     72     54   -357       N  
ATOM   1379  CA  ASN B  18       5.778  22.935  28.104  1.00 32.55           C  
ANISOU 1379  CA  ASN B  18     3887   4358   4124     49     59   -330       C  
ATOM   1380  C   ASN B  18       6.032  22.841  26.609  1.00 37.24           C  
ANISOU 1380  C   ASN B  18     4417   5088   4646     64     51   -367       C  
ATOM   1381  O   ASN B  18       5.214  22.284  25.862  1.00 33.75           O  
ANISOU 1381  O   ASN B  18     3961   4657   4205     83     35   -412       O  
ATOM   1382  CB  ASN B  18       5.402  24.370  28.505  1.00 29.01           C  
ANISOU 1382  CB  ASN B  18     3463   3882   3679     -5     80   -235       C  
ATOM   1383  CG  ASN B  18       3.944  24.650  28.260  1.00 35.06           C  
ANISOU 1383  CG  ASN B  18     4247   4604   4473    -19     78   -213       C  
ATOM   1384  OD1 ASN B  18       3.086  24.192  29.019  1.00 32.31           O  
ANISOU 1384  OD1 ASN B  18     3933   4161   4181    -14     77   -223       O  
ATOM   1385  ND2 ASN B  18       3.644  25.368  27.179  1.00 29.63           N  
ANISOU 1385  ND2 ASN B  18     3529   3990   3740    -37     76   -180       N  
ATOM   1386  N   ALA B  19       7.175  23.371  26.178  1.00 34.33           N  
ANISOU 1386  N   ALA B  19     4004   4831   4210     53     63   -352       N  
ATOM   1387  CA  ALA B  19       7.545  23.348  24.758  1.00 35.08           C  
ANISOU 1387  CA  ALA B  19     4027   5085   4216     63     61   -382       C  
ATOM   1388  C   ALA B  19       7.583  21.921  24.220  1.00 35.92           C  
ANISOU 1388  C   ALA B  19     4102   5222   4322    133     32   -508       C  
ATOM   1389  O   ALA B  19       7.168  21.663  23.086  1.00 37.91           O  
ANISOU 1389  O   ALA B  19     4312   5564   4528    151     21   -551       O  
ATOM   1390  CB  ALA B  19       8.894  24.079  24.519  1.00 30.80           C  
ANISOU 1390  CB  ALA B  19     3435   4665   3601     35     81   -343       C  
ATOM   1391  N   TYR B  20       8.061  20.993  25.045  1.00 37.51           N  
ANISOU 1391  N   TYR B  20     4325   5347   4580    175     14   -568       N  
ATOM   1392  CA  TYR B  20       8.122  19.582  24.667  1.00 39.91           C  
ANISOU 1392  CA  TYR B  20     4607   5651   4906    247    -27   -693       C  
ATOM   1393  C   TYR B  20       6.743  19.011  24.276  1.00 42.67           C  
ANISOU 1393  C   TYR B  20     4977   5934   5302    255    -51   -726       C  
ATOM   1394  O   TYR B  20       6.608  18.363  23.235  1.00 41.39           O  
ANISOU 1394  O   TYR B  20     4766   5848   5110    297    -77   -817       O  
ATOM   1395  CB  TYR B  20       8.737  18.746  25.794  1.00 40.88           C  
ANISOU 1395  CB  TYR B  20     4765   5668   5100    284    -51   -731       C  
ATOM   1396  CG  TYR B  20       9.163  17.366  25.345  1.00 52.92           C  
ANISOU 1396  CG  TYR B  20     6255   7209   6643    367   -102   -866       C  
ATOM   1397  CD1 TYR B  20      10.313  17.192  24.582  1.00 59.63           C  
ANISOU 1397  CD1 TYR B  20     7026   8213   7418    414   -106   -945       C  
ATOM   1398  CD2 TYR B  20       8.412  16.240  25.666  1.00 59.98           C  
ANISOU 1398  CD2 TYR B  20     7191   7967   7632    397   -149   -920       C  
ATOM   1399  CE1 TYR B  20      10.708  15.935  24.156  1.00 66.90           C  
ANISOU 1399  CE1 TYR B  20     7910   9150   8360    500   -160  -1085       C  
ATOM   1400  CE2 TYR B  20       8.798  14.977  25.242  1.00 64.88           C  
ANISOU 1400  CE2 TYR B  20     7781   8588   8283    476   -208  -1051       C  
ATOM   1401  CZ  TYR B  20       9.946  14.831  24.488  1.00 69.17           C  
ANISOU 1401  CZ  TYR B  20     8246   9283   8752    533   -215  -1139       C  
ATOM   1402  OH  TYR B  20      10.338  13.580  24.070  1.00 76.03           O  
ANISOU 1402  OH  TYR B  20     9080  10153   9655    622   -280  -1284       O  
ATOM   1403  N   TYR B  21       5.726  19.254  25.103  1.00 38.43           N  
ANISOU 1403  N   TYR B  21     4505   5262   4834    215    -44   -659       N  
ATOM   1404  CA  TYR B  21       4.387  18.711  24.845  1.00 40.96           C  
ANISOU 1404  CA  TYR B  21     4843   5514   5206    216    -66   -685       C  
ATOM   1405  C   TYR B  21       3.556  19.619  23.955  1.00 44.00           C  
ANISOU 1405  C   TYR B  21     5206   5973   5539    181    -48   -638       C  
ATOM   1406  O   TYR B  21       2.519  19.214  23.423  1.00 46.40           O  
ANISOU 1406  O   TYR B  21     5505   6261   5864    187    -69   -673       O  
ATOM   1407  CB  TYR B  21       3.649  18.393  26.146  1.00 36.95           C  
ANISOU 1407  CB  TYR B  21     4404   4838   4796    192    -70   -644       C  
ATOM   1408  CG  TYR B  21       4.160  17.143  26.803  1.00 35.77           C  
ANISOU 1408  CG  TYR B  21     4276   4603   4713    232   -109   -705       C  
ATOM   1409  CD1 TYR B  21       5.249  17.191  27.656  1.00 34.72           C  
ANISOU 1409  CD1 TYR B  21     4159   4454   4580    243   -103   -685       C  
ATOM   1410  CD2 TYR B  21       3.570  15.900  26.550  1.00 38.63           C  
ANISOU 1410  CD2 TYR B  21     4639   4896   5141    261   -160   -784       C  
ATOM   1411  CE1 TYR B  21       5.738  16.050  28.250  1.00 36.15           C  
ANISOU 1411  CE1 TYR B  21     4359   4552   4822    284   -146   -736       C  
ATOM   1412  CE2 TYR B  21       4.059  14.744  27.150  1.00 36.90           C  
ANISOU 1412  CE2 TYR B  21     4442   4584   4992    299   -207   -834       C  
ATOM   1413  CZ  TYR B  21       5.147  14.827  27.995  1.00 38.12           C  
ANISOU 1413  CZ  TYR B  21     4615   4726   5144    312   -201   -808       C  
ATOM   1414  OH  TYR B  21       5.653  13.698  28.610  1.00 42.33           O  
ANISOU 1414  OH  TYR B  21     5172   5164   5748    353   -255   -851       O  
ATOM   1415  N   ARG B  22       4.020  20.856  23.829  1.00 40.45           N  
ANISOU 1415  N   ARG B  22     4745   5599   5027    144    -14   -554       N  
ATOM   1416  CA  ARG B  22       3.605  21.779  22.778  1.00 53.18           C  
ANISOU 1416  CA  ARG B  22     6323   7316   6566    116     -3   -505       C  
ATOM   1417  C   ARG B  22       2.565  22.780  23.237  1.00 59.71           C  
ANISOU 1417  C   ARG B  22     7195   8062   7431     68     11   -407       C  
ATOM   1418  O   ARG B  22       2.903  23.928  23.519  1.00 62.96           O  
ANISOU 1418  O   ARG B  22     7618   8480   7823     27     32   -317       O  
ATOM   1419  CB  ARG B  22       3.139  21.049  21.515  1.00 59.33           C  
ANISOU 1419  CB  ARG B  22     7052   8185   7307    155    -32   -594       C  
ATOM   1420  CG  ARG B  22       2.526  21.976  20.486  1.00 65.82           C  
ANISOU 1420  CG  ARG B  22     7844   9106   8057    125    -26   -534       C  
ATOM   1421  CD  ARG B  22       1.893  21.224  19.320  1.00 76.17           C  
ANISOU 1421  CD  ARG B  22     9108  10497   9335    164    -58   -627       C  
ATOM   1422  NE  ARG B  22       0.673  20.507  19.697  1.00 79.83           N  
ANISOU 1422  NE  ARG B  22     9607  10830   9894    174    -83   -671       N  
ATOM   1423  CZ  ARG B  22       0.579  19.182  19.781  1.00 81.90           C  
ANISOU 1423  CZ  ARG B  22     9867  11037  10213    218   -118   -786       C  
ATOM   1424  NH1 ARG B  22       1.632  18.419  19.518  1.00 85.00           N  
ANISOU 1424  NH1 ARG B  22    10225  11491  10580    267   -134   -878       N  
ATOM   1425  NH2 ARG B  22      -0.569  18.617  20.124  1.00 81.45           N  
ANISOU 1425  NH2 ARG B  22     9841  10863  10244    213   -141   -809       N  
TER    1426      ARG B  22                                                      
HETATM 1427 ZN    ZN A   1      12.897  37.758  38.937  1.00 40.90          ZN  
ANISOU 1427 ZN    ZN A   1     5117   4899   5524   -428    -68    113      ZN  
HETATM 1428 ZN    ZN A   2      -3.481  20.947  56.701  1.00 58.13          ZN  
ANISOU 1428 ZN    ZN A   2     7360   7796   6929   -406    443    463      ZN  
HETATM 1429 ZN    ZN A   3     -10.720  16.222  28.056  1.00 28.16          ZN  
ANISOU 1429 ZN    ZN A   3     3302   3168   4228   -180   -106   -513      ZN  
HETATM 1430 ZN    ZN A   5      17.174  13.712  49.362  1.00 79.17          ZN  
ANISOU 1430 ZN    ZN A   5    10317   9506  10259    447   -470     17      ZN  
HETATM 1431  C   ACT A1428      13.618  35.281  37.426  1.00 42.83           C  
ANISOU 1431  C   ACT A1428     5300   5347   5625   -389     11    115       C  
HETATM 1432  O   ACT A1428      14.660  35.645  36.834  1.00 51.37           O  
ANISOU 1432  O   ACT A1428     6335   6495   6686   -441      4    152       O  
HETATM 1433  OXT ACT A1428      13.032  36.205  37.976  1.00 30.01           O  
ANISOU 1433  OXT ACT A1428     3710   3635   4059   -399    -15    118       O  
HETATM 1434  CH3 ACT A1428      13.095  33.865  37.495  1.00 27.90           C  
ANISOU 1434  CH3 ACT A1428     3424   3479   3699   -322     42     68       C  
HETATM 1435 CL    CL A 328       0.000  36.004  46.219  0.50 45.33          CL  
ANISOU 1435 CL    CL A 328     5776   5365   6082     44      0      0      CL  
HETATM 1436 ZN    ZN B  23      20.606  26.374  36.072  1.00 42.54          ZN  
ANISOU 1436 ZN    ZN B  23     4938   5986   5241    -15     51   -301      ZN  
HETATM 1437  O   HOH A   4       3.720  29.516  27.625  1.00 32.95           O  
ANISOU 1437  O   HOH A   4     3984   4362   4172   -161     77     66       O  
HETATM 1438  O   HOH A   6       0.000  36.004  34.974  0.50 14.92           O  
ANISOU 1438  O   HOH A   6     1915   1429   2327   -136      0      0       O  
HETATM 1439  O   HOH A   7       7.314  39.146  30.867  1.00 33.09           O  
ANISOU 1439  O   HOH A   7     4110   3958   4504   -505   -126    520       O  
HETATM 1440  O   HOH A   8       0.433  38.145  31.845  1.00 35.56           O  
ANISOU 1440  O   HOH A   8     4511   4041   4959   -221   -130    288       O  
HETATM 1441  O   HOH A   9       4.061  15.661  60.342  1.00 34.68           O  
ANISOU 1441  O   HOH A   9     4726   4572   3879   -352     60    976       O  
HETATM 1442  O   HOH A  10     -10.949  20.197  37.166  1.00 34.13           O  
ANISOU 1442  O   HOH A  10     4157   3962   4847   -321    209    -96       O  
HETATM 1443  O   HOH A  11       0.107  24.565  28.926  1.00 33.85           O  
ANISOU 1443  O   HOH A  11     4151   4266   4447    -36     75   -196       O  
HETATM 1444  O   HOH A  12      10.030  35.201  30.984  1.00 38.52           O  
ANISOU 1444  O   HOH A  12     4693   4979   4963   -437     27    340       O  
HETATM 1445  O   HOH A  13      -5.655  15.965  23.899  1.00 38.02           O  
ANISOU 1445  O   HOH A  13     4506   4707   5232     72   -200   -774       O  
HETATM 1446  O   HOH A  15      -4.946  21.471  27.260  1.00 31.53           O  
ANISOU 1446  O   HOH A  15     3796   3891   4293    -26      5   -363       O  
HETATM 1447  O   HOH A  16      -6.875  17.766  22.415  1.00 37.10           O  
ANISOU 1447  O   HOH A  16     4331   4763   5002     65   -173   -727       O  
HETATM 1448  O   HOH A  17      -2.926  13.064  30.057  1.00 32.92           O  
ANISOU 1448  O   HOH A  17     4094   3551   4861     10   -227   -588       O  
HETATM 1449  O   HOH A  18      -1.685   9.550  31.754  1.00 43.39           O  
ANISOU 1449  O   HOH A  18     5517   4544   6427     32   -407   -606       O  
HETATM 1450  O   HOH A  19      -9.035  17.932  49.010  1.00 33.25           O  
ANISOU 1450  O   HOH A  19     4131   4142   4360   -600    396    441       O  
HETATM 1451  O   HOH A  20      -6.919  29.192  30.199  1.00 46.27           O  
ANISOU 1451  O   HOH A  20     5723   5657   6199    -54     62    -76       O  
HETATM 1452  O   HOH A  21      -2.193   7.466  45.620  1.00 40.99           O  
ANISOU 1452  O   HOH A  21     5565   3920   6091   -513   -337    610       O  
HETATM 1453  O   HOH A  22     -16.833  23.589  28.895  1.00 45.67           O  
ANISOU 1453  O   HOH A  22     5328   5689   6335   -142     43   -361       O  
HETATM 1454  O   HOH A  23       6.666  35.065  52.305  1.00 40.91           O  
ANISOU 1454  O   HOH A  23     5252   5045   5247     43     66   -479       O  
HETATM 1455  O   HOH A  24       7.661  35.804  45.442  1.00 29.95           O  
ANISOU 1455  O   HOH A  24     3879   3397   4104   -111     16   -230       O  
HETATM 1456  O   HOH A  25       4.902   6.784  39.548  1.00 57.80           O  
ANISOU 1456  O   HOH A  25     7645   5960   8355    150   -621   -194       O  
HETATM 1457  O   HOH A  28      -9.175  31.091  46.405  1.00 50.35           O  
ANISOU 1457  O   HOH A  28     6160   6399   6571      7    360   -353       O  
HETATM 1458  O   HOH A  30       3.708  37.663  29.979  1.00 39.37           O  
ANISOU 1458  O   HOH A  30     4932   4741   5287   -356   -100    429       O  
HETATM 1459  O   HOH A  31       2.202  39.747  29.341  1.00 52.23           O  
ANISOU 1459  O   HOH A  31     6591   6227   7026   -365   -208    531       O  
HETATM 1460  O   HOH A  32       9.458  17.220  58.903  1.00 49.90           O  
ANISOU 1460  O   HOH A  32     6703   6340   5916    -52    -89    635       O  
HETATM 1461  O   HOH A  35       4.793  19.372  54.009  1.00 35.02           O  
ANISOU 1461  O   HOH A  35     4717   4310   4279   -153    123    397       O  
HETATM 1462  O   HOH A  37     -13.637  27.663  40.872  1.00 33.96           O  
ANISOU 1462  O   HOH A  37     3972   4261   4669   -124    344   -244       O  
HETATM 1463  O   HOH A  38      -2.059   9.754  27.549  1.00 47.61           O  
ANISOU 1463  O   HOH A  38     5895   5327   6867    160   -450   -928       O  
HETATM 1464  O   HOH A  39      -4.121  11.118  28.995  1.00 42.60           O  
ANISOU 1464  O   HOH A  39     5293   4669   6223      5   -337   -709       O  
HETATM 1465  O   HOH A  40     -10.209  15.272  31.952  1.00 36.00           O  
ANISOU 1465  O   HOH A  40     4393   3982   5303   -292    -49   -328       O  
HETATM 1466  O   HOH A  42       8.051  37.457  43.171  1.00 30.62           O  
ANISOU 1466  O   HOH A  42     3950   3397   4288   -188    -45   -144       O  
HETATM 1467  O   HOH A  43       9.755  39.462  44.228  1.00 38.80           O  
ANISOU 1467  O   HOH A  43     4975   4363   5403   -236   -136   -189       O  
HETATM 1468  O   HOH A  45       2.251  29.003  51.633  1.00 50.43           O  
ANISOU 1468  O   HOH A  45     6472   6380   6309    -30    264   -174       O  
HETATM 1469  O   HOH A  46      -6.013  29.044  49.049  1.00 59.06           O  
ANISOU 1469  O   HOH A  46     7367   7557   7518    -72    396   -221       O  
HETATM 1470  O   HOH A  47     -14.130  18.161  30.929  1.00 37.78           O  
ANISOU 1470  O   HOH A  47     4460   4432   5462   -308     32   -340       O  
HETATM 1471  O   HOH A  48      -2.644  18.339  23.200  1.00 62.64           O  
ANISOU 1471  O   HOH A  48     7604   8083   8115    122   -122   -686       O  
HETATM 1472  O   HOH A  51     -17.564  24.586  44.540  1.00 61.76           O  
ANISOU 1472  O   HOH A  51     7248   8157   8061   -363    525   -155       O  
HETATM 1473  O   HOH A  52      -0.011   7.286  49.209  1.00 43.12           O  
ANISOU 1473  O   HOH A  52     5930   4257   6196   -507   -366    874       O  
HETATM 1474  O   HOH A  53      -0.664   5.398  36.857  1.00 53.74           O  
ANISOU 1474  O   HOH A  53     7060   5281   8077    -91   -643   -252       O  
HETATM 1475  O   HOH A  54     -14.578  25.774  42.479  1.00 41.10           O  
ANISOU 1475  O   HOH A  54     4824   5269   5524   -235    416   -183       O  
HETATM 1476  O   HOH A  55       0.961  19.594  59.712  1.00 54.10           O  
ANISOU 1476  O   HOH A  55     6996   7319   6241   -344    301    641       O  
HETATM 1477  O   HOH A  56      -9.271   6.036  43.160  1.00 64.12           O  
ANISOU 1477  O   HOH A  56     8278   6803   9281   -914   -295    629       O  
HETATM 1478  O   HOH A  57      -1.406   9.043  47.801  1.00 41.86           O  
ANISOU 1478  O   HOH A  57     5678   4245   5980   -508   -225    715       O  
HETATM 1479  O   HOH A  59       1.084  25.075  53.901  1.00 39.17           O  
ANISOU 1479  O   HOH A  59     5060   5099   4723   -127    320     67       O  
HETATM 1480  O   HOH A  60       0.650  15.854  24.638  1.00 42.79           O  
ANISOU 1480  O   HOH A  60     5124   5456   5678    224   -181   -829       O  
HETATM 1481  O   HOH A  61       1.369  29.234  48.988  1.00 42.40           O  
ANISOU 1481  O   HOH A  61     5455   5239   5418    -44    257   -165       O  
HETATM 1482  O   HOH A  62      -5.450  36.173  47.367  1.00 36.61           O  
ANISOU 1482  O   HOH A  62     4521   4438   4952    165    169   -551       O  
HETATM 1483  O   HOH A  63     -10.519  12.884  30.488  1.00 37.57           O  
ANISOU 1483  O   HOH A  63     4571   4067   5635   -298   -177   -453       O  
HETATM 1484  O   HOH A  64     -16.378  20.988  47.296  1.00 54.90           O  
ANISOU 1484  O   HOH A  64     6447   7313   7097   -619    576    151       O  
HETATM 1485  O   HOH A  65       1.342  35.531  37.896  1.00 50.57           O  
ANISOU 1485  O   HOH A  65     6456   5931   6827   -120     25    -16       O  
HETATM 1486  O   HOH A  67       2.048  33.946  35.248  1.00 37.78           O  
ANISOU 1486  O   HOH A  67     4803   4430   5121   -160     49     66       O  
HETATM 1487  O   HOH A  68       5.645  32.796  51.374  1.00 45.36           O  
ANISOU 1487  O   HOH A  68     5835   5630   5770     18    138   -348       O  
HETATM 1488  O   HOH A  69      17.314  18.915  54.126  1.00 65.60           O  
ANISOU 1488  O   HOH A  69     8572   8188   8164    286   -270    101       O  
HETATM 1489  O   HOH A  70      -3.241   9.961  49.571  1.00 45.41           O  
ANISOU 1489  O   HOH A  70     6067   4912   6276   -652    -89    864       O  
HETATM 1490  O   HOH A  71      -0.604  28.675  28.365  1.00 56.77           O  
ANISOU 1490  O   HOH A  71     7057   7183   7330   -100     66     -8       O  
HETATM 1491  O   HOH A  72      14.582  14.008  47.246  1.00 48.80           O  
ANISOU 1491  O   HOH A  72     6466   5598   6479    349   -370     -9       O  
HETATM 1492  O   HOH A  74      23.496  20.266  42.295  1.00 64.57           O  
ANISOU 1492  O   HOH A  74     7881   8490   8162    433   -219   -525       O  
HETATM 1493  O   HOH A  76       0.731   6.786  35.018  1.00 50.61           O  
ANISOU 1493  O   HOH A  76     6588   5104   7537     63   -584   -462       O  
HETATM 1494  O   HOH A  77      -6.586  34.755  50.309  1.00 65.73           O  
ANISOU 1494  O   HOH A  77     8119   8415   8439    166    289   -610       O  
HETATM 1495  O   HOH A  78       1.402   8.213  21.319  1.00 72.32           O  
ANISOU 1495  O   HOH A  78     8716   9016   9745    584   -635  -1653       O  
HETATM 1496  O   HOH A  79      10.206  26.555  51.803  1.00 46.38           O  
ANISOU 1496  O   HOH A  79     6052   5806   5767     22     92    -89       O  
HETATM 1497  O   HOH A  80     -11.849  14.186  42.954  1.00 54.91           O  
ANISOU 1497  O   HOH A  80     6840   6454   7571   -720    199    337       O  
HETATM 1498  O   HOH A  81       4.587  33.614  48.893  1.00 50.62           O  
ANISOU 1498  O   HOH A  81     6499   6172   6562     -4    127   -321       O  
HETATM 1499  O   HOH A  82      -4.722   7.095  44.446  1.00 48.80           O  
ANISOU 1499  O   HOH A  82     6482   4887   7172   -638   -313    591       O  
HETATM 1500  O   HOH A  83       1.170  34.670  40.537  1.00 57.75           O  
ANISOU 1500  O   HOH A  83     7377   6864   7703    -76     76   -116       O  
HETATM 1501  O   HOH A  84      -6.675   7.004  41.999  1.00 74.58           O  
ANISOU 1501  O   HOH A  84     9660   8129  10550   -665   -316    420       O  
HETATM 1502  O   HOH A  85       3.539   6.283  35.033  1.00 53.57           O  
ANISOU 1502  O   HOH A  85     6968   5487   7898    237   -666   -576       O  
HETATM 1503  O   HOH A  86       0.141   6.445  32.468  1.00 66.98           O  
ANISOU 1503  O   HOH A  86     8576   7238   9635    130   -630   -691       O  
HETATM 1504  O   HOH A  87      14.530  12.132  45.205  1.00 49.07           O  
ANISOU 1504  O   HOH A  87     6483   5504   6657    431   -467   -125       O  
HETATM 1505  O   HOH A  88      10.525  31.745  55.437  1.00 59.14           O  
ANISOU 1505  O   HOH A  88     7589   7587   7294     60     56   -380       O  
HETATM 1506  O   HOH A  89       1.886  12.459  54.555  1.00 52.19           O  
ANISOU 1506  O   HOH A  89     7007   6142   6679   -434    -56    940       O  
HETATM 1507  O   HOH A  90       0.257  15.483  56.119  1.00 49.31           O  
ANISOU 1507  O   HOH A  90     6513   6173   6049   -463    155    850       O  
HETATM 1508  O   HOH A  91      23.630  27.866  42.474  1.00 70.17           O  
ANISOU 1508  O   HOH A  91     8515   9336   8810    -17    -52   -320       O  
HETATM 1509  O   HOH A  92      13.964  28.025  52.682  1.00 57.39           O  
ANISOU 1509  O   HOH A  92     7400   7275   7131     56      7   -192       O  
HETATM 1510  O   HOH A  93     -12.437  18.730  34.913  1.00 44.86           O  
ANISOU 1510  O   HOH A  93     5458   5287   6301   -351    139   -169       O  
HETATM 1511  O   HOH A  94       3.723   7.996  42.207  1.00 53.31           O  
ANISOU 1511  O   HOH A  94     7127   5465   7665    -21   -488     91       O  
HETATM 1512  O   HOH A  95      23.251  25.221  43.236  1.00 69.98           O  
ANISOU 1512  O   HOH A  95     8557   9239   8791    145    -95   -375       O  
HETATM 1513  O   HOH A  96       5.399   6.141  44.012  1.00 53.34           O  
ANISOU 1513  O   HOH A  96     7223   5289   7757     29   -654    213       O  
HETATM 1514  O   HOH A  97     -13.019  17.360  37.019  1.00 58.24           O  
ANISOU 1514  O   HOH A  97     7154   6947   8027   -465    167    -65       O  
HETATM 1515  O   HOH A  98       9.224  25.775  60.009  1.00 59.49           O  
ANISOU 1515  O   HOH A  98     7698   7973   6933     48    113      3       O  
HETATM 1516  O   HOH A  99     -13.734  20.115  39.995  1.00 70.62           O  
ANISOU 1516  O   HOH A  99     8668   8730   9434   -447    312    -13       O  
HETATM 1517  O   HOH A 100      13.190  28.741  57.212  1.00 66.43           O  
ANISOU 1517  O   HOH A 100     8545   8634   8059     97      5   -247       O  
HETATM 1518  O   HOH A 101      -4.209  17.028  51.809  1.00 51.77           O  
ANISOU 1518  O   HOH A 101     6670   6421   6579   -516    293    589       O  
HETATM 1519  O   HOH A 102     -14.665  22.780  39.722  1.00 67.62           O  
ANISOU 1519  O   HOH A 102     8222   8463   9006   -341    343   -112       O  
HETATM 1520  O   HOH A 103      14.537  29.345  54.891  1.00 50.69           O  
ANISOU 1520  O   HOH A 103     6533   6523   6205     73    -20   -273       O  
HETATM 1521  O   HOH A 104     -13.172  22.092  36.834  1.00 37.32           O  
ANISOU 1521  O   HOH A 104     4463   4484   5234   -294    245   -145       O  
HETATM 1522  O   HOH A 105     -13.148  17.026  33.114  1.00 40.78           O  
ANISOU 1522  O   HOH A 105     4909   4712   5875   -374     56   -246       O  
HETATM 1523  O   HOH A 106      -6.851  16.341  50.247  1.00 44.09           O  
ANISOU 1523  O   HOH A 106     5621   5409   5723   -616    317    586       O  
HETATM 1524  O   HOH A 107       1.448  35.502  28.811  1.00 54.65           O  
ANISOU 1524  O   HOH A 107     6844   6770   7152   -258    -51    335       O  
HETATM 1525  O   HOH A 108     -12.932  34.671  34.288  1.00 43.26           O  
ANISOU 1525  O   HOH A 108     5233   5144   6061    141     -4   -241       O  
HETATM 1526  O   HOH A 109       7.157   9.640  66.933  1.00 73.15           O  
ANISOU 1526  O   HOH A 109     9822   9536   8437   -495   -363   1942       O  
HETATM 1527  O   HOH A 111     -15.251  35.743  34.629  1.00 49.33           O  
ANISOU 1527  O   HOH A 111     5913   5939   6892    233    -42   -341       O  
HETATM 1528  O   HOH A 112      -5.852  15.270  55.331  1.00 80.76           O  
ANISOU 1528  O   HOH A 112    10283  10347  10055   -741    345    925       O  
HETATM 1529  O   HOH A 113      -6.349  23.366  52.779  1.00 54.37           O  
ANISOU 1529  O   HOH A 113     6781   7189   6690   -331    490    176       O  
HETATM 1530  O   HOH A 115     -12.723  32.063  34.089  1.00 51.57           O  
ANISOU 1530  O   HOH A 115     6279   6269   7045     58     77   -224       O  
HETATM 1531  O   HOH A 329     -14.145  32.639  39.850  1.00 33.49           O  
ANISOU 1531  O   HOH A 329     3891   4126   4709    103    212   -406       O  
HETATM 1532  O   HOH A 330       3.344  35.728  40.119  1.00 26.27           O  
ANISOU 1532  O   HOH A 330     3398   2854   3732   -127     29    -70       O  
HETATM 1533  O   HOH A 331       0.883  32.651  29.426  1.00 32.22           O  
ANISOU 1533  O   HOH A 331     3993   3979   4269   -183     26    173       O  
HETATM 1534  O   HOH B  24      19.322  28.091  34.961  1.00 48.90           O  
ANISOU 1534  O   HOH B  24     5759   6774   6046   -135     86   -183       O  
HETATM 1535  O   HOH B  25       7.805  27.153  26.458  1.00 42.24           O  
ANISOU 1535  O   HOH B  25     5016   5866   5165   -109    104    -84       O  
HETATM 1536  O   HOH B  26      13.221  26.917  28.890  1.00 33.67           O  
ANISOU 1536  O   HOH B  26     3847   4910   4035   -107    126   -149       O  
HETATM 1537  O   HOH B  27       1.189  25.928  26.013  1.00 38.60           O  
ANISOU 1537  O   HOH B  27     4660   5115   4892    -48     57   -149       O  
HETATM 1538  O   HOH B  29      11.776  30.457  30.047  1.00 43.63           O  
ANISOU 1538  O   HOH B  29     5222   5941   5413   -269    115     89       O  
HETATM 1539  O   HOH B  33      14.497  30.893  33.631  1.00 36.16           O  
ANISOU 1539  O   HOH B  33     4305   4891   4541   -276    102     38       O  
HETATM 1540  O   HOH B  34      11.677  21.425  25.160  1.00 33.72           O  
ANISOU 1540  O   HOH B  34     3725   5116   3969    195     41   -598       O  
HETATM 1541  O   HOH B  36       5.698  26.415  25.145  1.00 43.77           O  
ANISOU 1541  O   HOH B  36     5209   6061   5361    -72     83   -129       O  
HETATM 1542  O   HOH B  41      -0.012  19.461  24.027  1.00 46.75           O  
ANISOU 1542  O   HOH B  41     5608   6141   6013    128    -68   -604       O  
HETATM 1543  O   HOH B  44      13.326  33.995  32.488  1.00 55.00           O  
ANISOU 1543  O   HOH B  44     6711   7199   6986   -429     64    233       O  
HETATM 1544  O   HOH B  49       4.495  11.233  28.192  1.00 46.38           O  
ANISOU 1544  O   HOH B  49     5704   5481   6438    398   -388   -987       O  
HETATM 1545  O   HOH B  50      11.960  34.933  46.681  1.00 44.00           O  
ANISOU 1545  O   HOH B  50     5627   5297   5795   -144    -10   -238       O  
HETATM 1546  O   HOH B  58       8.118  31.359  28.085  1.00 48.53           O  
ANISOU 1546  O   HOH B  58     5893   6485   6063   -281     88    185       O  
HETATM 1547  O   HOH B  66      12.095  40.445  47.923  1.00 59.35           O  
ANISOU 1547  O   HOH B  66     7558   6998   7993   -209   -209   -390       O  
HETATM 1548  O   HOH B  73       8.016  26.087  36.764  1.00 36.62           O  
ANISOU 1548  O   HOH B  73     4628   4504   4781    -50    117   -115       O  
HETATM 1549  O   HOH B  75      11.250  30.126  26.860  1.00 59.54           O  
ANISOU 1549  O   HOH B  75     7132   8210   7281   -280    123    116       O  
HETATM 1550  O   HOH B 110       7.435  12.745  30.505  1.00 49.09           O  
ANISOU 1550  O   HOH B 110     6083   5897   6673    408   -308   -835       O  
HETATM 1551  O   HOH B 114       6.679  23.465  21.408  1.00 50.30           O  
ANISOU 1551  O   HOH B 114     5825   7323   5964     72     47   -419       O  
HETATM 1552  O   HOH B 116       5.985  25.896  22.433  1.00 51.98           O  
ANISOU 1552  O   HOH B 116     6123   7392   6234    -48     72   -184       O  
CONECT  850 1430                                                                
CONECT  969 1428                                                                
CONECT 1149 1429                                                                
CONECT 1181 1429                                                                
CONECT 1306 1436                                                                
CONECT 1427 1433                                                                
CONECT 1428  969                                                                
CONECT 1429 1149 1181                                                           
CONECT 1430  850                                                                
CONECT 1431 1432 1433 1434                                                      
CONECT 1432 1431                                                                
CONECT 1433 1427 1431                                                           
CONECT 1434 1431                                                                
CONECT 1436 1306 1534                                                           
CONECT 1534 1436                                                                
MASTER      393    0    7   10    0    0    8    6 1544    2   15   15          
END

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Related entries of code: 3kj1

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3kj0	RCSB PDB PDBbind	27aa, >3KJ0_2\|Chain... *
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
1qur	RCSB PDB PDBbind	22-mer
1smf	RCSB PDB PDBbind	22-mer
3dvm	RCSB PDB PDBbind	22-mer
3kj2	RCSB PDB PDBbind	22-mer
3o34	RCSB PDB PDBbind	22-mer

Entry Information

PDB ID	3kj1
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	Induced myeloid leukemia cell differentiation protein Mcl-1
Ligand Name	22-mer
EC.Number	E.C.-.-.-.-
Resolution	1.95(Å)
Affinity (Kd/Ki/IC50)	Kd=2nM
Release Year	2010
Protein/NA Sequence	Check fasta file
Primary Reference	(2010) Protein Sci. Vol. 19: pp. 507-519

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): O43521 Q07820
Entrez Gene ID	NCBI Entrez Gene ID: 10018 4170
ASD	Information of known allosteric effects of PDB entries

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