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Browse entries in the PDBbind-CN Database

HEADER    HYDROLASE                               22-JUL-15   5CR2              
TITLE     E. COLI MAZF IN COMPLEX WITH SINGLE STRAND DNA SUBSTRATE ANALOG       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDORIBONUCLEASE MAZF;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: TOXIN MAZF,MRNA INTERFERASE MAZF;                           
COMPND   5 EC: 3.1.27.-;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SSDNA SUBSTRATE ANALOG;                                    
COMPND   9 CHAIN: D, E, F;                                                      
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: MAZF, CHPA, CHPAK, B2782, JW2753;                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE MS2;                       
SOURCE  11 ORGANISM_TAXID: 329852                                               
KEYWDS    TOXIN-ANTITOXIN, MRNA INTERFERASE, RIBONUCLEASE, PERSISTENCE,         
KEYWDS   2 BACTERIAL STRESS RESPONSE, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.ZORZINI,R.LORIS                                                     
REVDAT   3   08-JUN-16 5CR2    1       JRNL                                     
REVDAT   2   13-APR-16 5CR2    1       JRNL                                     
REVDAT   1   06-APR-16 5CR2    0                                                
JRNL        AUTH   V.ZORZINI,A.MERNIK,J.LAH,Y.G.STERCKX,N.DE JONGE,             
JRNL        AUTH 2 A.GARCIA-PINO,H.DE GREVE,W.VERSEES,R.LORIS                   
JRNL        TITL   SUBSTRATE RECOGNITION AND ACTIVITY REGULATION OF THE         
JRNL        TITL 2 ESCHERICHIA COLI MRNA ENDONUCLEASE MAZF.                     
JRNL        REF    J.BIOL.CHEM.                  V. 291 10950 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   27026704                                                     
JRNL        DOI    10.1074/JBC.M116.715912                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.1_743                                     
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 7461                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 391                             
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 42.8127 -  4.1883    0.87     2390   126  0.2242 0.2660        
REMARK   3     2  4.1883 -  3.3247    0.88     2339   123  0.2284 0.2962        
REMARK   3     3  3.3247 -  2.9046    0.88     2340   124  0.2488 0.3378        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 32.26                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.870           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.98390                                              
REMARK   3    B22 (A**2) : 3.98390                                              
REMARK   3    B33 (A**2) : -12.93470                                            
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      :  0.003           2687                                  
REMARK   3   ANGLE     :  0.730           3676                                  
REMARK   3   CHIRALITY :  0.049            420                                  
REMARK   3   PLANARITY :  0.003            448                                  
REMARK   3   DIHEDRAL  : 14.912            991                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): 157.0664  21.2731  61.2651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1549 T22:   0.2652                                     
REMARK   3      T33:   0.0141 T12:  -0.0372                                     
REMARK   3      T13:  -0.0169 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7228 L22:   0.6264                                     
REMARK   3      L33:   0.6647 L12:   0.0210                                     
REMARK   3      L13:   0.1649 L23:   0.4329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0920 S12:  -0.1443 S13:  -0.0762                       
REMARK   3      S21:   0.0962 S22:  -0.0138 S23:   0.0033                       
REMARK   3      S31:  -0.0239 S32:  -0.1073 S33:  -0.0202                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): 156.4705  21.8047  41.7447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1485 T22:   0.1835                                     
REMARK   3      T33:   0.0436 T12:   0.0005                                     
REMARK   3      T13:  -0.0221 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8487 L22:   1.9360                                     
REMARK   3      L33:   1.3336 L12:   0.3179                                     
REMARK   3      L13:  -0.5648 L23:  -0.0818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0204 S12:   0.0295 S13:  -0.0890                       
REMARK   3      S21:  -0.0022 S22:   0.0283 S23:   0.0956                       
REMARK   3      S31:   0.1148 S32:   0.0561 S33:  -0.0336                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): 131.9342  -0.2671  53.7438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0736 T22:   0.1205                                     
REMARK   3      T33:   0.0144 T12:  -0.0018                                     
REMARK   3      T13:   0.0003 T23:   0.0544                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3478 L22:   1.3976                                     
REMARK   3      L33:   1.4041 L12:   0.2305                                     
REMARK   3      L13:  -0.1522 L23:  -0.1663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0804 S12:   0.2326 S13:  -0.0963                       
REMARK   3      S21:  -0.1800 S22:  -0.0433 S23:  -0.0923                       
REMARK   3      S31:   0.0612 S32:  -0.0385 S33:   0.0331                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'D'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): 160.6118   6.3284  59.0794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2636 T22:   0.2286                                     
REMARK   3      T33:   0.3711 T12:   0.0278                                     
REMARK   3      T13:  -0.0452 T23:  -0.0555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2978 L22:   8.7544                                     
REMARK   3      L33:   7.2500 L12:   5.0264                                     
REMARK   3      L13:   5.9163 L23:  -0.5768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0349 S12:   0.5200 S13:  -0.0076                       
REMARK   3      S21:  -0.5050 S22:  -0.0284 S23:  -0.4983                       
REMARK   3      S31:   0.0518 S32:   0.7233 S33:  -0.4607                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'E'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): 145.5417  22.1087  34.9737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7216 T22:   0.9911                                     
REMARK   3      T33:   0.5672 T12:   0.1299                                     
REMARK   3      T13:   0.1905 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7052 L22:   8.6737                                     
REMARK   3      L33:   5.0667 L12:   4.2773                                     
REMARK   3      L13:  -4.7513 L23:  -5.4534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5693 S12:   1.5606 S13:  -0.3598                       
REMARK   3      S21:  -0.6391 S22:  -0.1775 S23:   0.1914                       
REMARK   3      S31:  -0.5104 S32:  -0.2391 S33:   0.9437                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'F'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): 140.7763  -8.1014  47.4153              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1235 T22:   0.7856                                     
REMARK   3      T33:   0.6251 T12:  -0.1056                                     
REMARK   3      T13:   0.4233 T23:  -0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6840 L22:   5.4698                                     
REMARK   3      L33:   2.5330 L12:  -3.7963                                     
REMARK   3      L13:   2.0532 L23:  -0.6450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0403 S12:  -0.1361 S13:  -0.0869                       
REMARK   3      S21:  -0.1276 S22:  -0.1306 S23:  -0.1219                       
REMARK   3      S31:   0.6810 S32:   0.8955 S33:   0.0878                       
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 5CR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212064.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 2                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7461                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.801                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 8.950                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.22400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.77800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.250                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4MDX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M SODIUM ACETATE TRIHYDRATE,        
REMARK 280  0.085 M TRIS HYDROCLORIDE PH 8.5, 25.5% W/V PEG4000, 15%            
REMARK 280  GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       15.83667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.67333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.67333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       15.83667            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      126.69333            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     HIS A   114                                                      
REMARK 465     HIS A   115                                                      
REMARK 465     HIS A   116                                                      
REMARK 465     HIS A   117                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     HIS B   113                                                      
REMARK 465     HIS B   114                                                      
REMARK 465     HIS B   115                                                      
REMARK 465     HIS B   116                                                      
REMARK 465     HIS B   117                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     HIS C   113                                                      
REMARK 465     HIS C   114                                                      
REMARK 465     HIS C   115                                                      
REMARK 465     HIS C   116                                                      
REMARK 465     HIS C   117                                                      
REMARK 465      DC E     4                                                      
REMARK 465      DA E     5                                                      
REMARK 465      DU E     6                                                      
REMARK 465      DA E     7                                                      
REMARK 465      DC F     4                                                      
REMARK 465      DA F     5                                                      
REMARK 465      DU F     6                                                      
REMARK 465      DA F     7                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   2    CG1  CG2                                            
REMARK 470     ASP A   8    CG   OD1  OD2                                       
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     MET A  38    CE                                                  
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     TYR A  58    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A  65    OG                                                  
REMARK 470     ARG B   4    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  70    CG   OD1  OD2                                       
REMARK 470     GLN B 100    CG   CD   OE1  NE2                                  
REMARK 470     SER C  23    OG                                                  
REMARK 470     GLN C  54    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 100    CG   CD   OE1  NE2                                  
REMARK 470      DA D   1    O5'  C5'  C4'  O4'  C3'  C2'  C1'                   
REMARK 470      DA D   1    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470      DA D   1    C2   N3   C4                                        
REMARK 470      DA D   7    C5'  C4'  O4'  C3'  O3'  C2'  C1'                   
REMARK 470      DA D   7    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470      DA D   7    C2   N3   C4                                        
REMARK 470      DA E   1    O5'  C5'  C4'  O4'  C3'  C2'  C1'                   
REMARK 470      DA E   1    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470      DA E   1    C2   N3   C4                                        
REMARK 470      DA E   3    C5'  C4'  O4'  C3'  O3'  C2'  C1'                   
REMARK 470      DA E   3    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470      DA E   3    C2   N3   C4                                        
REMARK 470      DA F   1    O5'  C5'  C4'  O4'  C3'  C2'  C1'                   
REMARK 470      DA F   1    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470      DA F   1    C2   N3   C4                                        
REMARK 470      DA F   3    C5'  C4'  O4'  C3'  O3'  C2'  C1'                   
REMARK 470      DA F   3    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470      DA F   3    C2   N3   C4                                        
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   O    ASN C    41     NH2  ARG C    84              2.07            
REMARK 500   OE1  GLN A    25     N4    DC D     4              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLN C    67     NZ   LYS C    90     5556     2.18            
REMARK 500   O    HOH C   201     O    HOH C   201     5556     2.19            
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    PRO B  30     -174.00    -66.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5CR2 A    1   111  UNP    P0AE70   MAZF_ECOLI       1    111             
DBREF  5CR2 B    1   111  UNP    P0AE70   MAZF_ECOLI       1    111             
DBREF  5CR2 C    1   111  UNP    P0AE70   MAZF_ECOLI       1    111             
DBREF  5CR2 D    1     7  PDB    5CR2     5CR2             1      7             
DBREF  5CR2 E    1     7  PDB    5CR2     5CR2             1      7             
DBREF  5CR2 F    1     7  PDB    5CR2     5CR2             1      7             
SEQADV 5CR2 HIS A  112  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS A  113  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS A  114  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS A  115  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS A  116  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS A  117  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS B  112  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS B  113  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS B  114  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS B  115  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS B  116  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS B  117  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS C  112  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS C  113  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS C  114  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS C  115  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS C  116  UNP  P0AE70              EXPRESSION TAG                 
SEQADV 5CR2 HIS C  117  UNP  P0AE70              EXPRESSION TAG                 
SEQRES   1 A  117  MET VAL SER ARG TYR VAL PRO ASP MET GLY ASP LEU ILE          
SEQRES   2 A  117  TRP VAL ASP PHE ASP PRO THR LYS GLY SER GLU GLN ALA          
SEQRES   3 A  117  GLY HIS ARG PRO ALA VAL VAL LEU SER PRO PHE MET TYR          
SEQRES   4 A  117  ASN ASN LYS THR GLY MET CYS LEU CYS VAL PRO CYS THR          
SEQRES   5 A  117  THR GLN SER LYS GLY TYR PRO PHE GLU VAL VAL LEU SER          
SEQRES   6 A  117  GLY GLN GLU ARG ASP GLY VAL ALA LEU ALA ASP GLN VAL          
SEQRES   7 A  117  LYS SER ILE ALA TRP ARG ALA ARG GLY ALA THR LYS LYS          
SEQRES   8 A  117  GLY THR VAL ALA PRO GLU GLU LEU GLN LEU ILE LYS ALA          
SEQRES   9 A  117  LYS ILE ASN VAL LEU ILE GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  117  MET VAL SER ARG TYR VAL PRO ASP MET GLY ASP LEU ILE          
SEQRES   2 B  117  TRP VAL ASP PHE ASP PRO THR LYS GLY SER GLU GLN ALA          
SEQRES   3 B  117  GLY HIS ARG PRO ALA VAL VAL LEU SER PRO PHE MET TYR          
SEQRES   4 B  117  ASN ASN LYS THR GLY MET CYS LEU CYS VAL PRO CYS THR          
SEQRES   5 B  117  THR GLN SER LYS GLY TYR PRO PHE GLU VAL VAL LEU SER          
SEQRES   6 B  117  GLY GLN GLU ARG ASP GLY VAL ALA LEU ALA ASP GLN VAL          
SEQRES   7 B  117  LYS SER ILE ALA TRP ARG ALA ARG GLY ALA THR LYS LYS          
SEQRES   8 B  117  GLY THR VAL ALA PRO GLU GLU LEU GLN LEU ILE LYS ALA          
SEQRES   9 B  117  LYS ILE ASN VAL LEU ILE GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  117  MET VAL SER ARG TYR VAL PRO ASP MET GLY ASP LEU ILE          
SEQRES   2 C  117  TRP VAL ASP PHE ASP PRO THR LYS GLY SER GLU GLN ALA          
SEQRES   3 C  117  GLY HIS ARG PRO ALA VAL VAL LEU SER PRO PHE MET TYR          
SEQRES   4 C  117  ASN ASN LYS THR GLY MET CYS LEU CYS VAL PRO CYS THR          
SEQRES   5 C  117  THR GLN SER LYS GLY TYR PRO PHE GLU VAL VAL LEU SER          
SEQRES   6 C  117  GLY GLN GLU ARG ASP GLY VAL ALA LEU ALA ASP GLN VAL          
SEQRES   7 C  117  LYS SER ILE ALA TRP ARG ALA ARG GLY ALA THR LYS LYS          
SEQRES   8 C  117  GLY THR VAL ALA PRO GLU GLU LEU GLN LEU ILE LYS ALA          
SEQRES   9 C  117  LYS ILE ASN VAL LEU ILE GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 D    7   DA  DU  DA  DC  DA  DU  DA                                  
SEQRES   1 E    7   DA  DU  DA  DC  DA  DU  DA                                  
SEQRES   1 F    7   DA  DU  DA  DC  DA  DU  DA                                  
FORMUL   7  HOH   *31(H2 O)                                                     
HELIX    1 AA1 PRO A   36  GLY A   44  1                                   9    
HELIX    2 AA2 TRP A   83  GLY A   87  1                                   5    
HELIX    3 AA3 ALA A   95  ILE A  110  1                                  16    
HELIX    4 AA4 PRO B   36  GLY B   44  1                                   9    
HELIX    5 AA5 TRP B   83  GLY B   87  1                                   5    
HELIX    6 AA6 ALA B   95  ILE B  110  1                                  16    
HELIX    7 AA7 PRO C   36  GLY C   44  1                                   9    
HELIX    8 AA8 ALA C   95  ILE C  110  1                                  16    
SHEET    1 AA1 4 GLU A  61  LEU A  64  0                                        
SHEET    2 AA1 4 GLY A  71  LEU A  74 -1  O  ALA A  73   N  VAL A  62           
SHEET    3 AA1 4 MET A  45  THR A  52 -1  N  THR A  52   O  VAL A  72           
SHEET    4 AA1 4 LYS A  79  ALA A  82 -1  O  LYS A  79   N  CYS A  48           
SHEET    1 AA2 6 GLU A  61  LEU A  64  0                                        
SHEET    2 AA2 6 GLY A  71  LEU A  74 -1  O  ALA A  73   N  VAL A  62           
SHEET    3 AA2 6 MET A  45  THR A  52 -1  N  THR A  52   O  VAL A  72           
SHEET    4 AA2 6 HIS A  28  VAL A  33 -1  N  PRO A  30   O  CYS A  51           
SHEET    5 AA2 6 ASP A  11  ASP A  16 -1  N  ILE A  13   O  ALA A  31           
SHEET    6 AA2 6 THR A  89  THR A  93 -1  O  LYS A  91   N  LEU A  12           
SHEET    1 AA3 3 HIS B  28  ARG B  29  0                                        
SHEET    2 AA3 3 ASP B  11  ASP B  16 -1  N  VAL B  15   O  ARG B  29           
SHEET    3 AA3 3 THR B  89  THR B  93 -1  O  THR B  89   N  TRP B  14           
SHEET    1 AA4 4 ALA B  31  VAL B  33  0                                        
SHEET    2 AA4 4 MET B  45  THR B  52 -1  O  VAL B  49   N  VAL B  32           
SHEET    3 AA4 4 VAL B  72  LEU B  74 -1  O  VAL B  72   N  THR B  52           
SHEET    4 AA4 4 GLU B  61  VAL B  63 -1  N  VAL B  62   O  ALA B  73           
SHEET    1 AA5 3 ALA B  31  VAL B  33  0                                        
SHEET    2 AA5 3 MET B  45  THR B  52 -1  O  VAL B  49   N  VAL B  32           
SHEET    3 AA5 3 LYS B  79  ALA B  82 -1  O  LYS B  79   N  CYS B  48           
SHEET    1 AA6 4 GLU C  61  VAL C  63  0                                        
SHEET    2 AA6 4 VAL C  72  LEU C  74 -1  O  ALA C  73   N  VAL C  62           
SHEET    3 AA6 4 MET C  45  THR C  52 -1  N  THR C  52   O  VAL C  72           
SHEET    4 AA6 4 LYS C  79  ALA C  82 -1  O  LYS C  79   N  CYS C  48           
SHEET    1 AA7 6 GLU C  61  VAL C  63  0                                        
SHEET    2 AA7 6 VAL C  72  LEU C  74 -1  O  ALA C  73   N  VAL C  62           
SHEET    3 AA7 6 MET C  45  THR C  52 -1  N  THR C  52   O  VAL C  72           
SHEET    4 AA7 6 HIS C  28  VAL C  33 -1  N  PRO C  30   O  CYS C  51           
SHEET    5 AA7 6 ASP C  11  ASP C  16 -1  N  ILE C  13   O  ALA C  31           
SHEET    6 AA7 6 THR C  89  THR C  93 -1  O  THR C  89   N  TRP C  14           
CISPEP   1 ASP A   18    PRO A   19          0         1.22                     
CISPEP   2 ASP B   18    PRO B   19          0        -5.81                     
CISPEP   3 ASP C   18    PRO C   19          0        -0.15                     
CRYST1  113.960  113.960   47.510  90.00  90.00 120.00 P 31 2 1     18          
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      0.008775  0.005066  0.000000        0.00000                         
SCALE2      0.000000  0.010133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021048        0.00000                         
ATOM      1  N   VAL A   2     136.475  25.090  67.837  1.00 90.81           N  
ANISOU    1  N   VAL A   2    10853  13391  10259   -304    298   -475       N  
ATOM      2  CA  VAL A   2     137.854  25.383  67.457  1.00 89.85           C  
ANISOU    2  CA  VAL A   2    10817  13163  10160   -273    265   -431       C  
ATOM      3  C   VAL A   2     138.558  26.248  68.507  1.00 87.47           C  
ANISOU    3  C   VAL A   2    10567  12824   9845   -263    276   -428       C  
ATOM      4  O   VAL A   2     138.283  26.131  69.704  1.00 88.07           O  
ANISOU    4  O   VAL A   2    10629  12946   9887   -307    307   -429       O  
ATOM      5  CB  VAL A   2     137.924  26.093  66.085  1.00 90.55           C  
ANISOU    5  CB  VAL A   2    10916  13208  10282   -190    232   -458       C  
ATOM      6  N   SER A   3     139.467  27.109  68.049  1.00 83.60           N  
ANISOU    6  N   SER A   3    10137  12251   9378   -207    252   -426       N  
ATOM      7  CA  SER A   3     140.193  28.028  68.929  1.00 78.35           C  
ANISOU    7  CA  SER A   3     9521  11546   8703   -192    259   -430       C  
ATOM      8  C   SER A   3     140.668  29.276  68.182  1.00 73.81           C  
ANISOU    8  C   SER A   3     8988  10903   8152   -116    239   -456       C  
ATOM      9  O   SER A   3     140.486  29.391  66.967  1.00 74.60           O  
ANISOU    9  O   SER A   3     9086  10983   8276    -75    217   -466       O  
ATOM     10  CB  SER A   3     141.388  27.321  69.577  1.00 75.22           C  
ANISOU   10  CB  SER A   3     9180  11099   8301   -242    252   -367       C  
ATOM     11  OG  SER A   3     142.336  26.931  68.597  1.00 70.90           O  
ANISOU   11  OG  SER A   3     8677  10474   7789   -232    218   -328       O  
ATOM     12  N   ARG A   4     141.293  30.198  68.913  1.00 67.56           N  
ANISOU   12  N   ARG A   4     8239  10078   7352   -101    246   -468       N  
ATOM     13  CA  ARG A   4     141.804  31.431  68.317  1.00 61.63           C  
ANISOU   13  CA  ARG A   4     7536   9262   6619    -38    230   -492       C  
ATOM     14  C   ARG A   4     143.302  31.318  68.010  1.00 56.01           C  
ANISOU   14  C   ARG A   4     6900   8453   5928    -49    208   -443       C  
ATOM     15  O   ARG A   4     143.917  32.266  67.513  1.00 57.76           O  
ANISOU   15  O   ARG A   4     7172   8612   6164    -10    196   -454       O  
ATOM     16  CB  ARG A   4     141.570  32.627  69.241  1.00 64.11           C  
ANISOU   16  CB  ARG A   4     7848   9598   6912    -12    251   -546       C  
ATOM     17  CG  ARG A   4     141.427  33.964  68.521  1.00 64.20           C  
ANISOU   17  CG  ARG A   4     7880   9576   6937     64    239   -595       C  
ATOM     18  CD  ARG A   4     139.961  34.345  68.357  1.00 64.30           C  
ANISOU   18  CD  ARG A   4     7820   9669   6944    107    247   -661       C  
ATOM     19  NE  ARG A   4     139.627  34.771  66.996  1.00 63.95           N  
ANISOU   19  NE  ARG A   4     7781   9599   6920    173    218   -681       N  
ATOM     20  CZ  ARG A   4     140.206  35.788  66.359  1.00 63.31           C  
ANISOU   20  CZ  ARG A   4     7762   9444   6850    224    199   -690       C  
ATOM     21  NH1 ARG A   4     139.825  36.105  65.122  1.00 61.10           N  
ANISOU   21  NH1 ARG A   4     7486   9146   6583    285    170   -707       N  
ATOM     22  NH2 ARG A   4     141.175  36.483  66.953  1.00 63.95           N  
ANISOU   22  NH2 ARG A   4     7902   9469   6926    214    206   -685       N  
ATOM     23  N   TYR A   5     143.887  30.161  68.303  1.00 49.77           N  
ANISOU   23  N   TYR A   5     6118   7654   5139   -103    202   -390       N  
ATOM     24  CA  TYR A   5     145.326  29.977  68.141  1.00 43.75           C  
ANISOU   24  CA  TYR A   5     5418   6808   4396   -115    181   -350       C  
ATOM     25  C   TYR A   5     145.787  30.096  66.694  1.00 44.59           C  
ANISOU   25  C   TYR A   5     5557   6850   4538    -83    156   -339       C  
ATOM     26  O   TYR A   5     145.138  29.593  65.777  1.00 45.38           O  
ANISOU   26  O   TYR A   5     5626   6967   4648    -75    147   -337       O  
ATOM     27  CB  TYR A   5     145.783  28.641  68.733  1.00 37.35           C  
ANISOU   27  CB  TYR A   5     4604   6007   3579   -174    176   -300       C  
ATOM     28  CG  TYR A   5     147.167  28.229  68.265  1.00 32.86           C  
ANISOU   28  CG  TYR A   5     4086   5359   3038   -180    148   -262       C  
ATOM     29  CD1 TYR A   5     148.304  28.891  68.713  1.00 31.51           C  
ANISOU   29  CD1 TYR A   5     3965   5138   2869   -171    142   -265       C  
ATOM     30  CD2 TYR A   5     147.336  27.177  67.376  1.00 30.80           C  
ANISOU   30  CD2 TYR A   5     3820   5080   2802   -196    127   -229       C  
ATOM     31  CE1 TYR A   5     149.570  28.517  68.284  1.00 28.38           C  
ANISOU   31  CE1 TYR A   5     3606   4677   2498   -176    117   -237       C  
ATOM     32  CE2 TYR A   5     148.595  26.796  66.943  1.00 26.64           C  
ANISOU   32  CE2 TYR A   5     3334   4487   2301   -200    102   -202       C  
ATOM     33  CZ  TYR A   5     149.707  27.468  67.399  1.00 25.33           C  
ANISOU   33  CZ  TYR A   5     3212   4274   2137   -190     98   -207       C  
ATOM     34  OH  TYR A   5     150.956  27.084  66.968  1.00 23.33           O  
ANISOU   34  OH  TYR A   5     2992   3964   1909   -193     73   -186       O  
ATOM     35  N   VAL A   6     146.915  30.775  66.504  1.00 43.29           N  
ANISOU   35  N   VAL A   6     5451   6612   4386    -68    146   -335       N  
ATOM     36  CA  VAL A   6     147.558  30.854  65.200  1.00 38.32           C  
ANISOU   36  CA  VAL A   6     4860   5914   3785    -48    125   -320       C  
ATOM     37  C   VAL A   6     149.030  30.487  65.351  1.00 37.66           C  
ANISOU   37  C   VAL A   6     4819   5771   3717    -74    111   -288       C  
ATOM     38  O   VAL A   6     149.689  30.913  66.304  1.00 39.22           O  
ANISOU   38  O   VAL A   6     5038   5960   3903    -84    118   -295       O  
ATOM     39  CB  VAL A   6     147.476  32.279  64.614  1.00 34.42           C  
ANISOU   39  CB  VAL A   6     4401   5389   3289      2    128   -357       C  
ATOM     40  CG1 VAL A   6     148.288  32.380  63.327  1.00 33.31           C  
ANISOU   40  CG1 VAL A   6     4310   5175   3171     14    109   -337       C  
ATOM     41  CG2 VAL A   6     146.027  32.675  64.386  1.00 32.96           C  
ANISOU   41  CG2 VAL A   6     4169   5265   3090     40    135   -396       C  
ATOM     42  N   PRO A   7     149.560  29.712  64.394  1.00 33.44           N  
ANISOU   42  N   PRO A   7     4296   5201   3210    -82     91   -259       N  
ATOM     43  CA  PRO A   7     150.967  29.298  64.396  1.00 30.65           C  
ANISOU   43  CA  PRO A   7     3975   4796   2875   -101     75   -235       C  
ATOM     44  C   PRO A   7     151.908  30.453  64.072  1.00 32.78           C  
ANISOU   44  C   PRO A   7     4298   5007   3150    -80     77   -252       C  
ATOM     45  O   PRO A   7     151.574  31.310  63.255  1.00 35.20           O  
ANISOU   45  O   PRO A   7     4627   5293   3456    -49     82   -270       O  
ATOM     46  CB  PRO A   7     151.026  28.249  63.281  1.00 26.54           C  
ANISOU   46  CB  PRO A   7     3442   4261   2380   -109     56   -210       C  
ATOM     47  CG  PRO A   7     149.618  27.802  63.090  1.00 26.74           C  
ANISOU   47  CG  PRO A   7     3419   4347   2396   -107     61   -214       C  
ATOM     48  CD  PRO A   7     148.786  29.016  63.355  1.00 29.49           C  
ANISOU   48  CD  PRO A   7     3764   4719   2721    -75     81   -251       C  
ATOM     49  N   ASP A   8     153.068  30.469  64.718  1.00 31.89           N  
ANISOU   49  N   ASP A   8     4205   4871   3039    -96     72   -248       N  
ATOM     50  CA  ASP A   8     154.091  31.466  64.435  1.00 28.77           C  
ANISOU   50  CA  ASP A   8     3857   4425   2649    -83     74   -264       C  
ATOM     51  C   ASP A   8     155.397  30.769  64.083  1.00 25.95           C  
ANISOU   51  C   ASP A   8     3508   4036   2316   -102     55   -246       C  
ATOM     52  O   ASP A   8     155.569  29.585  64.366  1.00 23.46           O  
ANISOU   52  O   ASP A   8     3166   3740   2009   -125     39   -223       O  
ATOM     53  CB  ASP A   8     154.292  32.391  65.636  1.00 27.35           C  
ANISOU   53  CB  ASP A   8     3689   4258   2444    -83     88   -292       C  
ATOM     54  N   MET A   9     156.311  31.500  63.455  1.00 26.16           N  
ANISOU   54  N   MET A   9     3571   4018   2351    -92     57   -258       N  
ATOM     55  CA  MET A   9     157.599  30.934  63.074  1.00 23.90           C  
ANISOU   55  CA  MET A   9     3286   3709   2088   -109     41   -250       C  
ATOM     56  C   MET A   9     158.342  30.393  64.291  1.00 17.24           C  
ANISOU   56  C   MET A   9     2423   2888   1240   -134     27   -248       C  
ATOM     57  O   MET A   9     158.446  31.063  65.319  1.00 13.92           O  
ANISOU   57  O   MET A   9     2010   2481    799   -135     35   -267       O  
ATOM     58  CB  MET A   9     158.460  31.977  62.353  1.00 24.33           C  
ANISOU   58  CB  MET A   9     3379   3721   2143    -97     51   -270       C  
ATOM     59  CG  MET A   9     159.804  31.446  61.868  1.00 22.98           C  
ANISOU   59  CG  MET A   9     3201   3535   1996   -117     38   -268       C  
ATOM     60  SD  MET A   9     160.788  32.688  61.010  1.00133.06           S  
ANISOU   60  SD  MET A   9    17183  17439  15935   -110     57   -294       S  
ATOM     61  CE  MET A   9     159.655  33.172  59.710  1.00107.53           C  
ANISOU   61  CE  MET A   9    13986  14183  12689    -75     70   -282       C  
ATOM     62  N   GLY A  10     158.858  29.175  64.168  1.00 15.59           N  
ANISOU   62  N   GLY A  10     2192   2684   1047   -154      5   -229       N  
ATOM     63  CA  GLY A  10     159.637  28.569  65.230  1.00 18.56           C  
ANISOU   63  CA  GLY A  10     2556   3079   1417   -177    -14   -226       C  
ATOM     64  C   GLY A  10     158.781  27.873  66.267  1.00 22.14           C  
ANISOU   64  C   GLY A  10     2990   3574   1847   -189    -17   -206       C  
ATOM     65  O   GLY A  10     159.275  27.447  67.312  1.00 20.49           O  
ANISOU   65  O   GLY A  10     2778   3386   1621   -206    -32   -201       O  
ATOM     66  N   ASP A  11     157.490  27.755  65.979  1.00 25.33           N  
ANISOU   66  N   ASP A  11     3381   3996   2247   -182     -3   -194       N  
ATOM     67  CA  ASP A  11     156.582  27.090  66.899  1.00 27.14           C  
ANISOU   67  CA  ASP A  11     3588   4273   2451   -199     -1   -176       C  
ATOM     68  C   ASP A  11     156.659  25.579  66.759  1.00 29.32           C  
ANISOU   68  C   ASP A  11     3845   4560   2736   -225    -25   -143       C  
ATOM     69  O   ASP A  11     157.382  25.054  65.912  1.00 30.94           O  
ANISOU   69  O   ASP A  11     4052   4736   2969   -225    -44   -138       O  
ATOM     70  CB  ASP A  11     155.144  27.555  66.673  1.00 27.45           C  
ANISOU   70  CB  ASP A  11     3614   4336   2481   -185     23   -183       C  
ATOM     71  CG  ASP A  11     154.674  28.522  67.742  1.00 31.43           C  
ANISOU   71  CG  ASP A  11     4121   4868   2952   -178     45   -207       C  
ATOM     72  OD1 ASP A  11     155.305  28.553  68.820  1.00 37.01           O  
ANISOU   72  OD1 ASP A  11     4837   5586   3639   -192     41   -210       O  
ATOM     73  OD2 ASP A  11     153.675  29.239  67.512  1.00 29.32           O  
ANISOU   73  OD2 ASP A  11     3847   4615   2677   -158     66   -226       O  
ATOM     74  N   LEU A  12     155.906  24.888  67.604  1.00 30.20           N  
ANISOU   74  N   LEU A  12     3939   4715   2820   -248    -23   -122       N  
ATOM     75  CA  LEU A  12     155.803  23.442  67.524  1.00 28.94           C  
ANISOU   75  CA  LEU A  12     3764   4571   2662   -277    -45    -87       C  
ATOM     76  C   LEU A  12     154.341  23.044  67.669  1.00 32.96           C  
ANISOU   76  C   LEU A  12     4243   5129   3152   -295    -26    -72       C  
ATOM     77  O   LEU A  12     153.720  23.299  68.706  1.00 34.09           O  
ANISOU   77  O   LEU A  12     4381   5313   3260   -307     -6    -73       O  
ATOM     78  CB  LEU A  12     156.655  22.785  68.607  1.00 25.89           C  
ANISOU   78  CB  LEU A  12     3393   4192   2253   -300    -70    -68       C  
ATOM     79  CG  LEU A  12     156.730  21.260  68.587  1.00 26.19           C  
ANISOU   79  CG  LEU A  12     3424   4237   2289   -331   -100    -29       C  
ATOM     80  CD1 LEU A  12     157.221  20.759  67.245  1.00 26.39           C  
ANISOU   80  CD1 LEU A  12     3443   4226   2357   -322   -121    -32       C  
ATOM     81  CD2 LEU A  12     157.633  20.766  69.712  1.00 27.89           C  
ANISOU   81  CD2 LEU A  12     3663   4456   2476   -347   -129    -12       C  
ATOM     82  N   ILE A  13     153.804  22.412  66.630  1.00 35.64           N  
ANISOU   82  N   ILE A  13     4561   5467   3512   -298    -31    -63       N  
ATOM     83  CA  ILE A  13     152.381  22.093  66.571  1.00 34.91           C  
ANISOU   83  CA  ILE A  13     4434   5426   3405   -315    -12    -56       C  
ATOM     84  C   ILE A  13     152.113  20.596  66.482  1.00 30.55           C  
ANISOU   84  C   ILE A  13     3863   4897   2849   -359    -31    -19       C  
ATOM     85  O   ILE A  13     152.968  19.820  66.060  1.00 28.70           O  
ANISOU   85  O   ILE A  13     3641   4629   2634   -366    -63     -2       O  
ATOM     86  CB  ILE A  13     151.691  22.790  65.375  1.00 35.30           C  
ANISOU   86  CB  ILE A  13     4469   5468   3476   -279      1    -84       C  
ATOM     87  CG1 ILE A  13     152.204  22.227  64.048  1.00 34.67           C  
ANISOU   87  CG1 ILE A  13     4393   5348   3433   -269    -24    -78       C  
ATOM     88  CG2 ILE A  13     151.889  24.298  65.441  1.00 34.02           C  
ANISOU   88  CG2 ILE A  13     4331   5281   3314   -239     18   -117       C  
ATOM     89  CD1 ILE A  13     151.519  22.820  62.829  1.00 34.87           C  
ANISOU   89  CD1 ILE A  13     4409   5367   3474   -234    -15   -101       C  
ATOM     90  N   TRP A  14     150.913  20.197  66.883  1.00 29.68           N  
ANISOU   90  N   TRP A  14     3720   4847   2711   -391    -13     -7       N  
ATOM     91  CA  TRP A  14     150.498  18.807  66.769  1.00 28.85           C  
ANISOU   91  CA  TRP A  14     3596   4769   2598   -441    -28     30       C  
ATOM     92  C   TRP A  14     149.523  18.675  65.609  1.00 25.81           C  
ANISOU   92  C   TRP A  14     3171   4407   2230   -434    -22     15       C  
ATOM     93  O   TRP A  14     148.418  19.209  65.665  1.00 26.27           O  
ANISOU   93  O   TRP A  14     3196   4514   2273   -429      7     -8       O  
ATOM     94  CB  TRP A  14     149.838  18.337  68.063  1.00 30.37           C  
ANISOU   94  CB  TRP A  14     3779   5018   2740   -494    -11     59       C  
ATOM     95  CG  TRP A  14     149.505  16.888  68.066  1.00 34.01           C  
ANISOU   95  CG  TRP A  14     4231   5503   3188   -557    -29    106       C  
ATOM     96  CD1 TRP A  14     148.295  16.323  67.782  1.00 37.85           C  
ANISOU   96  CD1 TRP A  14     4674   6045   3660   -598    -14    115       C  
ATOM     97  CD2 TRP A  14     150.392  15.805  68.364  1.00 36.26           C  
ANISOU   97  CD2 TRP A  14     4549   5756   3470   -589    -70    153       C  
ATOM     98  NE1 TRP A  14     148.371  14.954  67.890  1.00 40.04           N  
ANISOU   98  NE1 TRP A  14     4961   6326   3927   -660    -41    168       N  
ATOM     99  CE2 TRP A  14     149.647  14.611  68.246  1.00 38.89           C  
ANISOU   99  CE2 TRP A  14     4865   6124   3789   -654    -78    193       C  
ATOM    100  CE3 TRP A  14     151.742  15.732  68.720  1.00 35.30           C  
ANISOU  100  CE3 TRP A  14     4472   5583   3356   -571   -103    163       C  
ATOM    101  CZ2 TRP A  14     150.212  13.355  68.471  1.00 37.90           C  
ANISOU  101  CZ2 TRP A  14     4770   5973   3657   -700   -121    249       C  
ATOM    102  CZ3 TRP A  14     152.297  14.486  68.947  1.00 36.80           C  
ANISOU  102  CZ3 TRP A  14     4688   5754   3540   -610   -146    212       C  
ATOM    103  CH2 TRP A  14     151.535  13.314  68.818  1.00 37.75           C  
ANISOU  103  CH2 TRP A  14     4796   5900   3647   -674   -157    257       C  
ATOM    104  N   VAL A  15     149.930  17.972  64.556  1.00 21.81           N  
ANISOU  104  N   VAL A  15     2664   3869   1753   -432    -51     22       N  
ATOM    105  CA  VAL A  15     149.096  17.886  63.360  1.00 17.23           C  
ANISOU  105  CA  VAL A  15     2049   3309   1190   -418    -49      3       C  
ATOM    106  C   VAL A  15     149.107  16.496  62.716  1.00 20.17           C  
ANISOU  106  C   VAL A  15     2407   3683   1572   -456    -81     29       C  
ATOM    107  O   VAL A  15     150.056  15.721  62.874  1.00 22.25           O  
ANISOU  107  O   VAL A  15     2699   3911   1845   -476   -113     56       O  
ATOM    108  CB  VAL A  15     149.505  18.953  62.318  1.00 15.28           C  
ANISOU  108  CB  VAL A  15     1818   3011    975   -351    -49    -35       C  
ATOM    109  CG1 VAL A  15     150.851  18.598  61.696  1.00 14.34           C  
ANISOU  109  CG1 VAL A  15     1732   2826    889   -338    -80    -29       C  
ATOM    110  CG2 VAL A  15     148.437  19.095  61.247  1.00 17.77           C  
ANISOU  110  CG2 VAL A  15     2097   3357   1297   -329    -43    -61       C  
ATOM    111  N   ASP A  16     148.034  16.196  61.990  1.00 21.83           N  
ANISOU  111  N   ASP A  16     2574   3939   1780   -464    -77     16       N  
ATOM    112  CA  ASP A  16     147.897  14.935  61.272  1.00 24.62           C  
ANISOU  112  CA  ASP A  16     2910   4300   2144   -499   -109     33       C  
ATOM    113  C   ASP A  16     148.197  15.145  59.787  1.00 24.86           C  
ANISOU  113  C   ASP A  16     2940   4289   2216   -443   -128     -1       C  
ATOM    114  O   ASP A  16     147.509  15.908  59.113  1.00 26.95           O  
ANISOU  114  O   ASP A  16     3183   4572   2485   -400   -111    -38       O  
ATOM    115  CB  ASP A  16     146.479  14.387  61.457  1.00 29.75           C  
ANISOU  115  CB  ASP A  16     3507   5038   2760   -554    -93     39       C  
ATOM    116  CG  ASP A  16     146.291  13.015  60.837  1.00 35.94           C  
ANISOU  116  CG  ASP A  16     4272   5831   3550   -603   -132     60       C  
ATOM    117  OD1 ASP A  16     147.254  12.219  60.834  1.00 38.62           O  
ANISOU  117  OD1 ASP A  16     4648   6117   3909   -622   -173     92       O  
ATOM    118  OD2 ASP A  16     145.170  12.735  60.359  1.00 37.58           O  
ANISOU  118  OD2 ASP A  16     4428   6103   3747   -624   -126     40       O  
ATOM    119  N   PHE A  17     149.225  14.467  59.283  1.00 24.65           N  
ANISOU  119  N   PHE A  17     2939   4207   2219   -441   -166      9       N  
ATOM    120  CA  PHE A  17     149.653  14.635  57.895  1.00 23.14           C  
ANISOU  120  CA  PHE A  17     2753   3972   2067   -389   -183    -24       C  
ATOM    121  C   PHE A  17     149.011  13.636  56.947  1.00 28.10           C  
ANISOU  121  C   PHE A  17     3345   4621   2711   -404   -212    -33       C  
ATOM    122  O   PHE A  17     149.210  13.703  55.734  1.00 28.61           O  
ANISOU  122  O   PHE A  17     3409   4654   2805   -362   -226    -63       O  
ATOM    123  CB  PHE A  17     151.171  14.552  57.788  1.00 21.92           C  
ANISOU  123  CB  PHE A  17     2640   3748   1939   -372   -205    -21       C  
ATOM    124  CG  PHE A  17     151.873  15.755  58.336  1.00 26.93           C  
ANISOU  124  CG  PHE A  17     3309   4355   2569   -341   -179    -29       C  
ATOM    125  CD1 PHE A  17     151.828  16.963  57.660  1.00 27.71           C  
ANISOU  125  CD1 PHE A  17     3418   4435   2675   -291   -156    -60       C  
ATOM    126  CD2 PHE A  17     152.573  15.684  59.528  1.00 28.30           C  
ANISOU  126  CD2 PHE A  17     3506   4519   2728   -364   -182     -6       C  
ATOM    127  CE1 PHE A  17     152.471  18.076  58.159  1.00 27.17           C  
ANISOU  127  CE1 PHE A  17     3381   4338   2603   -269   -136    -67       C  
ATOM    128  CE2 PHE A  17     153.220  16.792  60.030  1.00 26.60           C  
ANISOU  128  CE2 PHE A  17     3319   4280   2510   -337   -161    -18       C  
ATOM    129  CZ  PHE A  17     153.170  17.991  59.345  1.00 26.07           C  
ANISOU  129  CZ  PHE A  17     3260   4193   2453   -291   -138    -49       C  
ATOM    130  N   ASP A  18     148.249  12.704  57.509  1.00 31.92           N  
ANISOU  130  N   ASP A  18     3800   5156   3174   -469   -222     -6       N  
ATOM    131  CA  ASP A  18     147.443  11.789  56.714  1.00 36.04           C  
ANISOU  131  CA  ASP A  18     4277   5704   3712   -491   -250    -20       C  
ATOM    132  C   ASP A  18     146.371  12.581  55.984  1.00 39.39           C  
ANISOU  132  C   ASP A  18     4662   6173   4130   -447   -225    -66       C  
ATOM    133  O   ASP A  18     145.877  13.580  56.506  1.00 42.73           O  
ANISOU  133  O   ASP A  18     5080   6633   4522   -430   -184    -74       O  
ATOM    134  CB  ASP A  18     146.779  10.745  57.611  1.00 34.30           C  
ANISOU  134  CB  ASP A  18     4033   5535   3464   -583   -264     22       C  
ATOM    135  CG  ASP A  18     147.737   9.657  58.047  1.00 30.36           C  
ANISOU  135  CG  ASP A  18     3570   4983   2984   -628   -312     69       C  
ATOM    136  OD1 ASP A  18     148.749   9.438  57.346  1.00 30.39           O  
ANISOU  136  OD1 ASP A  18     3597   4916   3036   -586   -344     54       O  
ATOM    137  OD2 ASP A  18     147.474   9.018  59.088  1.00 26.12           O  
ANISOU  137  OD2 ASP A  18     3038   4475   2412   -707   -319    122       O  
ATOM    138  N   PRO A  19     145.988  12.126  54.782  1.00 37.98           N  
ANISOU  138  N   PRO A  19     4455   5989   3987   -424   -252    -99       N  
ATOM    139  CA  PRO A  19     146.479  10.922  54.101  1.00 41.72           C  
ANISOU  139  CA  PRO A  19     4928   6414   4510   -440   -303    -98       C  
ATOM    140  C   PRO A  19     147.861  11.112  53.486  1.00 47.25           C  
ANISOU  140  C   PRO A  19     5680   7034   5240   -391   -317   -105       C  
ATOM    141  O   PRO A  19     148.288  12.245  53.268  1.00 48.94           O  
ANISOU  141  O   PRO A  19     5923   7229   5441   -340   -288   -117       O  
ATOM    142  CB  PRO A  19     145.443  10.709  52.999  1.00 41.10           C  
ANISOU  142  CB  PRO A  19     4798   6361   4457   -416   -316   -144       C  
ATOM    143  CG  PRO A  19     144.977  12.078  52.681  1.00 39.34           C  
ANISOU  143  CG  PRO A  19     4576   6165   4204   -353   -278   -173       C  
ATOM    144  CD  PRO A  19     144.959  12.819  53.990  1.00 36.06           C  
ANISOU  144  CD  PRO A  19     4176   5785   3740   -375   -237   -145       C  
ATOM    145  N   THR A  20     148.545  10.006  53.211  1.00 52.32           N  
ANISOU  145  N   THR A  20     6328   7628   5924   -410   -363    -99       N  
ATOM    146  CA  THR A  20     149.894  10.048  52.652  1.00 56.33           C  
ANISOU  146  CA  THR A  20     6874   8067   6460   -371   -379   -111       C  
ATOM    147  C   THR A  20     150.128   8.930  51.635  1.00 62.53           C  
ANISOU  147  C   THR A  20     7643   8810   7304   -365   -429   -138       C  
ATOM    148  O   THR A  20     149.698   7.797  51.845  1.00 59.42           O  
ANISOU  148  O   THR A  20     7221   8416   6939   -411   -466   -127       O  
ATOM    149  CB  THR A  20     150.956   9.943  53.764  1.00 55.07           C  
ANISOU  149  CB  THR A  20     6753   7881   6291   -396   -385    -74       C  
ATOM    150  OG1 THR A  20     151.387  11.257  54.141  1.00 51.89           O  
ANISOU  150  OG1 THR A  20     6381   7479   5856   -365   -340    -74       O  
ATOM    151  CG2 THR A  20     152.156   9.134  53.290  1.00 55.31           C  
ANISOU  151  CG2 THR A  20     6800   7847   6370   -385   -432    -87       C  
ATOM    152  N   LYS A  21     150.815   9.247  50.540  1.00 71.85           N  
ANISOU  152  N   LYS A  21     8842   9954   8505   -312   -430   -173       N  
ATOM    153  CA  LYS A  21     151.092   8.245  49.513  1.00 77.52           C  
ANISOU  153  CA  LYS A  21     9545  10631   9278   -301   -475   -204       C  
ATOM    154  C   LYS A  21     152.100   7.202  49.997  1.00 84.44           C  
ANISOU  154  C   LYS A  21    10431  11456  10195   -327   -522   -192       C  
ATOM    155  O   LYS A  21     151.811   6.005  49.993  1.00 92.35           O  
ANISOU  155  O   LYS A  21    11406  12440  11243   -358   -569   -193       O  
ATOM    156  CB  LYS A  21     151.579   8.912  48.224  1.00 75.86           C  
ANISOU  156  CB  LYS A  21     9353  10403   9066   -245   -458   -240       C  
ATOM    157  N   GLY A  22     153.278   7.658  50.415  1.00 73.34           N  
ANISOU  157  N   GLY A  22     9061  10027   8776   -314   -514   -184       N  
ATOM    158  CA  GLY A  22     154.226   6.795  51.097  1.00 64.64           C  
ANISOU  158  CA  GLY A  22     7970   8884   7706   -336   -559   -170       C  
ATOM    159  C   GLY A  22     155.545   7.483  51.379  1.00 59.87           C  
ANISOU  159  C   GLY A  22     7402   8259   7088   -312   -545   -173       C  
ATOM    160  O   GLY A  22     155.915   8.433  50.691  1.00 62.81           O  
ANISOU  160  O   GLY A  22     7788   8633   7442   -277   -508   -196       O  
ATOM    161  N   SER A  23     156.263   6.993  52.383  1.00 54.45           N  
ANISOU  161  N   SER A  23     6730   7551   6409   -333   -577   -150       N  
ATOM    162  CA  SER A  23     157.551   7.567  52.754  1.00 49.14           C  
ANISOU  162  CA  SER A  23     6085   6859   5728   -311   -570   -157       C  
ATOM    163  C   SER A  23     157.423   9.075  52.959  1.00 45.61           C  
ANISOU  163  C   SER A  23     5658   6445   5224   -299   -501   -149       C  
ATOM    164  O   SER A  23     158.401   9.819  52.864  1.00 46.80           O  
ANISOU  164  O   SER A  23     5829   6584   5370   -276   -481   -167       O  
ATOM    165  CB  SER A  23     158.621   7.241  51.718  1.00 46.31           C  
ANISOU  165  CB  SER A  23     5722   6455   5418   -278   -598   -207       C  
ATOM    166  OG  SER A  23     158.980   5.872  51.762  1.00 42.35           O  
ANISOU  166  OG  SER A  23     5202   5912   4975   -284   -670   -220       O  
ATOM    167  N   GLU A  24     156.204   9.506  53.265  1.00 41.51           N  
ANISOU  167  N   GLU A  24     5133   5970   4669   -316   -466   -123       N  
ATOM    168  CA  GLU A  24     155.913  10.889  53.594  1.00 37.80           C  
ANISOU  168  CA  GLU A  24     4680   5531   4153   -304   -406   -115       C  
ATOM    169  C   GLU A  24     155.405  10.849  55.021  1.00 36.47           C  
ANISOU  169  C   GLU A  24     4515   5391   3949   -345   -399    -68       C  
ATOM    170  O   GLU A  24     154.398  10.198  55.295  1.00 38.68           O  
ANISOU  170  O   GLU A  24     4774   5700   4221   -382   -410    -45       O  
ATOM    171  CB  GLU A  24     154.825  11.436  52.670  1.00 37.56           C  
ANISOU  171  CB  GLU A  24     4631   5528   4111   -284   -375   -131       C  
ATOM    172  CG  GLU A  24     155.161  11.359  51.191  1.00 40.78           C  
ANISOU  172  CG  GLU A  24     5035   5912   4547   -250   -383   -172       C  
ATOM    173  CD  GLU A  24     153.941  11.566  50.302  1.00 42.57           C  
ANISOU  173  CD  GLU A  24     5240   6168   4766   -234   -369   -185       C  
ATOM    174  OE1 GLU A  24     154.095  12.105  49.183  1.00 41.05           O  
ANISOU  174  OE1 GLU A  24     5056   5968   4574   -200   -354   -211       O  
ATOM    175  OE2 GLU A  24     152.828  11.178  50.720  1.00 42.85           O  
ANISOU  175  OE2 GLU A  24     5249   6237   4794   -257   -374   -171       O  
ATOM    176  N   GLN A  25     156.092  11.524  55.937  1.00 32.82           N  
ANISOU  176  N   GLN A  25     4080   4925   3465   -343   -381    -56       N  
ATOM    177  CA  GLN A  25     155.772  11.351  57.348  1.00 35.24           C  
ANISOU  177  CA  GLN A  25     4396   5255   3737   -385   -381    -10       C  
ATOM    178  C   GLN A  25     154.278  11.546  57.569  1.00 35.81           C  
ANISOU  178  C   GLN A  25     4446   5382   3777   -410   -348      9       C  
ATOM    179  O   GLN A  25     153.700  12.558  57.167  1.00 35.41           O  
ANISOU  179  O   GLN A  25     4387   5352   3715   -382   -305    -13       O  
ATOM    180  CB  GLN A  25     156.600  12.289  58.228  1.00 35.36           C  
ANISOU  180  CB  GLN A  25     4442   5263   3732   -370   -357     -9       C  
ATOM    181  CG  GLN A  25     158.060  11.868  58.378  1.00 33.35           C  
ANISOU  181  CG  GLN A  25     4204   4965   3502   -359   -400    -21       C  
ATOM    182  CD  GLN A  25     158.223  10.468  58.942  1.00 29.00           C  
ANISOU  182  CD  GLN A  25     3656   4401   2962   -393   -462     12       C  
ATOM    183  OE1 GLN A  25     158.524   9.525  58.213  1.00 27.19           O  
ANISOU  183  OE1 GLN A  25     3412   4142   2775   -388   -508     -4       O  
ATOM    184  NE2 GLN A  25     158.035  10.330  60.247  1.00 29.97           N  
ANISOU  184  NE2 GLN A  25     3798   4542   3047   -428   -465     59       N  
ATOM    185  N   ALA A  26     153.666  10.557  58.212  1.00 35.26           N  
ANISOU  185  N   ALA A  26     4367   5335   3694   -467   -373     50       N  
ATOM    186  CA  ALA A  26     152.214  10.445  58.266  1.00 33.14           C  
ANISOU  186  CA  ALA A  26     4066   5126   3400   -503   -353     63       C  
ATOM    187  C   ALA A  26     151.696  10.340  59.698  1.00 29.58           C  
ANISOU  187  C   ALA A  26     3624   4718   2898   -562   -337    115       C  
ATOM    188  O   ALA A  26     152.475  10.334  60.649  1.00 28.36           O  
ANISOU  188  O   ALA A  26     3504   4542   2728   -572   -346    142       O  
ATOM    189  CB  ALA A  26     151.763   9.243  57.454  1.00 34.92           C  
ANISOU  189  CB  ALA A  26     4261   5344   3662   -527   -399     60       C  
ATOM    190  N   GLY A  27     150.376  10.258  59.841  1.00 29.77           N  
ANISOU  190  N   GLY A  27     3613   4806   2892   -602   -314    125       N  
ATOM    191  CA  GLY A  27     149.747  10.159  61.147  1.00 32.05           C  
ANISOU  191  CA  GLY A  27     3907   5147   3126   -666   -290    173       C  
ATOM    192  C   GLY A  27     149.871  11.439  61.951  1.00 29.34           C  
ANISOU  192  C   GLY A  27     3578   4815   2756   -631   -237    159       C  
ATOM    193  O   GLY A  27     150.373  12.445  61.450  1.00 28.19           O  
ANISOU  193  O   GLY A  27     3439   4639   2634   -563   -220    115       O  
ATOM    194  N   HIS A  28     149.410  11.408  63.198  1.00 30.11           N  
ANISOU  194  N   HIS A  28     3682   4953   2806   -681   -212    196       N  
ATOM    195  CA  HIS A  28     149.553  12.564  64.077  1.00 35.35           C  
ANISOU  195  CA  HIS A  28     4358   5622   3450   -648   -170    179       C  
ATOM    196  C   HIS A  28     150.990  12.685  64.567  1.00 34.02           C  
ANISOU  196  C   HIS A  28     4240   5391   3295   -621   -196    187       C  
ATOM    197  O   HIS A  28     151.637  11.684  64.866  1.00 34.04           O  
ANISOU  197  O   HIS A  28     4271   5365   3298   -653   -242    228       O  
ATOM    198  CB  HIS A  28     148.594  12.477  65.265  1.00 42.23           C  
ANISOU  198  CB  HIS A  28     5218   6558   4269   -708   -134    209       C  
ATOM    199  CG  HIS A  28     147.191  12.879  64.936  1.00 49.80           C  
ANISOU  199  CG  HIS A  28     6120   7589   5212   -715    -92    177       C  
ATOM    200  ND1 HIS A  28     146.273  12.005  64.396  1.00 53.07           N  
ANISOU  200  ND1 HIS A  28     6496   8051   5616   -769    -97    190       N  
ATOM    201  CD2 HIS A  28     146.550  14.064  65.067  1.00 54.09           C  
ANISOU  201  CD2 HIS A  28     6636   8167   5749   -674    -48    131       C  
ATOM    202  CE1 HIS A  28     145.126  12.632  64.212  1.00 55.78           C  
ANISOU  202  CE1 HIS A  28     6787   8462   5946   -759    -54    147       C  
ATOM    203  NE2 HIS A  28     145.267  13.885  64.609  1.00 56.51           N  
ANISOU  203  NE2 HIS A  28     6887   8545   6042   -699    -26    112       N  
ATOM    204  N   ARG A  29     151.486  13.914  64.651  1.00 31.40           N  
ANISOU  204  N   ARG A  29     3919   5039   2973   -562   -172    147       N  
ATOM    205  CA  ARG A  29     152.856  14.135  65.091  1.00 31.78           C  
ANISOU  205  CA  ARG A  29     4007   5035   3031   -534   -194    146       C  
ATOM    206  C   ARG A  29     153.204  15.619  65.196  1.00 30.02           C  
ANISOU  206  C   ARG A  29     3792   4798   2815   -478   -162    101       C  
ATOM    207  O   ARG A  29     152.479  16.479  64.681  1.00 29.62           O  
ANISOU  207  O   ARG A  29     3719   4764   2771   -451   -129     69       O  
ATOM    208  CB  ARG A  29     153.850  13.417  64.165  1.00 33.12           C  
ANISOU  208  CB  ARG A  29     4189   5153   3242   -519   -244    142       C  
ATOM    209  CG  ARG A  29     153.819  13.868  62.712  1.00 33.14           C  
ANISOU  209  CG  ARG A  29     4171   5137   3285   -473   -236     97       C  
ATOM    210  CD  ARG A  29     154.862  13.131  61.879  1.00 29.95           C  
ANISOU  210  CD  ARG A  29     3776   4682   2921   -458   -285     88       C  
ATOM    211  NE  ARG A  29     154.576  11.703  61.761  1.00 28.71           N  
ANISOU  211  NE  ARG A  29     3611   4527   2769   -505   -331    123       N  
ATOM    212  CZ  ARG A  29     155.097  10.766  62.546  1.00 31.06           C  
ANISOU  212  CZ  ARG A  29     3934   4807   3058   -540   -376    165       C  
ATOM    213  NH1 ARG A  29     155.943  11.100  63.513  1.00 30.66           N  
ANISOU  213  NH1 ARG A  29     3915   4743   2991   -530   -380    173       N  
ATOM    214  NH2 ARG A  29     154.779   9.492  62.356  1.00 33.80           N  
ANISOU  214  NH2 ARG A  29     4277   5148   3416   -585   -423    200       N  
ATOM    215  N   PRO A  30     154.318  15.921  65.884  1.00 26.09           N  
ANISOU  215  N   PRO A  30     3329   4271   2314   -462   -175     99       N  
ATOM    216  CA  PRO A  30     154.828  17.290  66.010  1.00 23.80           C  
ANISOU  216  CA  PRO A  30     3050   3961   2030   -416   -152     60       C  
ATOM    217  C   PRO A  30     155.371  17.812  64.680  1.00 20.43           C  
ANISOU  217  C   PRO A  30     2622   3492   1647   -373   -154     23       C  
ATOM    218  O   PRO A  30     155.895  17.041  63.873  1.00 18.08           O  
ANISOU  218  O   PRO A  30     2323   3169   1376   -373   -185     26       O  
ATOM    219  CB  PRO A  30     155.982  17.149  67.016  1.00 20.97           C  
ANISOU  219  CB  PRO A  30     2726   3585   1656   -418   -178     71       C  
ATOM    220  CG  PRO A  30     155.754  15.855  67.711  1.00 20.77           C  
ANISOU  220  CG  PRO A  30     2709   3580   1603   -469   -205    123       C  
ATOM    221  CD  PRO A  30     155.102  14.970  66.689  1.00 21.39           C  
ANISOU  221  CD  PRO A  30     2763   3663   1703   -491   -217    138       C  
ATOM    222  N   ALA A  31     155.247  19.117  64.470  1.00 18.66           N  
ANISOU  222  N   ALA A  31     2400   3260   1429   -337   -123    -10       N  
ATOM    223  CA  ALA A  31     155.778  19.785  63.293  1.00 16.94           C  
ANISOU  223  CA  ALA A  31     2189   3001   1245   -300   -121    -41       C  
ATOM    224  C   ALA A  31     156.329  21.147  63.709  1.00 16.18           C  
ANISOU  224  C   ALA A  31     2118   2886   1145   -274   -101    -67       C  
ATOM    225  O   ALA A  31     155.696  21.863  64.487  1.00 14.00           O  
ANISOU  225  O   ALA A  31     1842   2634    844   -271    -77    -71       O  
ATOM    226  CB  ALA A  31     154.692  19.945  62.239  1.00 14.89           C  
ANISOU  226  CB  ALA A  31     1907   2753    996   -286   -105    -50       C  
ATOM    227  N   VAL A  32     157.503  21.500  63.190  1.00 19.27           N  
ANISOU  227  N   VAL A  32     2526   3239   1558   -257   -111    -86       N  
ATOM    228  CA  VAL A  32     158.099  22.812  63.423  1.00 23.38           C  
ANISOU  228  CA  VAL A  32     3068   3738   2075   -237    -93   -112       C  
ATOM    229  C   VAL A  32     157.658  23.803  62.353  1.00 26.00           C  
ANISOU  229  C   VAL A  32     3409   4049   2419   -208    -70   -131       C  
ATOM    230  O   VAL A  32     157.887  23.588  61.159  1.00 26.43           O  
ANISOU  230  O   VAL A  32     3462   4082   2496   -199    -76   -136       O  
ATOM    231  CB  VAL A  32     159.635  22.756  63.415  1.00 20.45           C  
ANISOU  231  CB  VAL A  32     2710   3342   1717   -239   -114   -126       C  
ATOM    232  CG1 VAL A  32     160.212  24.159  63.561  1.00 17.34           C  
ANISOU  232  CG1 VAL A  32     2337   2930   1321   -223    -94   -155       C  
ATOM    233  CG2 VAL A  32     160.148  21.839  64.515  1.00 20.53           C  
ANISOU  233  CG2 VAL A  32     2720   3369   1711   -261   -145   -108       C  
ATOM    234  N   VAL A  33     157.041  24.895  62.796  1.00 26.40           N  
ANISOU  234  N   VAL A  33     3471   4107   2452   -193    -45   -143       N  
ATOM    235  CA  VAL A  33     156.515  25.915  61.897  1.00 26.13           C  
ANISOU  235  CA  VAL A  33     3453   4054   2422   -164    -25   -159       C  
ATOM    236  C   VAL A  33     157.600  26.847  61.365  1.00 30.08           C  
ANISOU  236  C   VAL A  33     3986   4511   2931   -150    -19   -179       C  
ATOM    237  O   VAL A  33     158.328  27.480  62.134  1.00 30.12           O  
ANISOU  237  O   VAL A  33     4006   4512   2928   -154    -15   -193       O  
ATOM    238  CB  VAL A  33     155.460  26.777  62.601  1.00 22.78           C  
ANISOU  238  CB  VAL A  33     3029   3655   1971   -152     -2   -169       C  
ATOM    239  CG1 VAL A  33     154.982  27.890  61.677  1.00 23.15           C  
ANISOU  239  CG1 VAL A  33     3101   3678   2017   -119     14   -187       C  
ATOM    240  CG2 VAL A  33     154.306  25.918  63.069  1.00 20.86           C  
ANISOU  240  CG2 VAL A  33     2749   3463   1715   -169     -2   -153       C  
ATOM    241  N   LEU A  34     157.690  26.936  60.042  1.00 31.31           N  
ANISOU  241  N   LEU A  34     4153   4641   3102   -137    -19   -182       N  
ATOM    242  CA  LEU A  34     158.663  27.799  59.377  1.00 31.81           C  
ANISOU  242  CA  LEU A  34     4248   4668   3170   -128     -9   -199       C  
ATOM    243  C   LEU A  34     158.034  29.131  58.978  1.00 33.43           C  
ANISOU  243  C   LEU A  34     4491   4854   3355    -99     14   -210       C  
ATOM    244  O   LEU A  34     158.500  30.197  59.383  1.00 35.52           O  
ANISOU  244  O   LEU A  34     4784   5106   3607    -94     28   -228       O  
ATOM    245  CB  LEU A  34     159.276  27.100  58.167  1.00 29.89           C  
ANISOU  245  CB  LEU A  34     3998   4410   2948   -132    -21   -197       C  
ATOM    246  CG  LEU A  34     159.875  25.732  58.493  1.00 28.75           C  
ANISOU  246  CG  LEU A  34     3818   4284   2821   -159    -47   -189       C  
ATOM    247  CD1 LEU A  34     160.603  25.182  57.290  1.00 28.85           C  
ANISOU  247  CD1 LEU A  34     3825   4283   2853   -163    -56   -196       C  
ATOM    248  CD2 LEU A  34     160.804  25.826  59.690  1.00 26.81           C  
ANISOU  248  CD2 LEU A  34     3570   4047   2571   -177    -54   -198       C  
ATOM    249  N   SER A  35     156.990  29.058  58.158  1.00 31.34           N  
ANISOU  249  N   SER A  35     4229   4591   3087    -82     14   -202       N  
ATOM    250  CA  SER A  35     156.293  30.247  57.684  1.00 29.10           C  
ANISOU  250  CA  SER A  35     3986   4291   2780    -54     31   -212       C  
ATOM    251  C   SER A  35     155.929  31.185  58.832  1.00 28.47           C  
ANISOU  251  C   SER A  35     3916   4224   2679    -49     46   -229       C  
ATOM    252  O   SER A  35     155.589  30.737  59.931  1.00 27.13           O  
ANISOU  252  O   SER A  35     3711   4089   2508    -62     43   -227       O  
ATOM    253  CB  SER A  35     155.029  29.854  56.919  1.00 32.92           C  
ANISOU  253  CB  SER A  35     4456   4792   3262    -40     24   -204       C  
ATOM    254  OG  SER A  35     155.113  30.256  55.558  1.00 40.12           O  
ANISOU  254  OG  SER A  35     5407   5671   4166    -25     25   -203       O  
ATOM    255  N   PRO A  36     156.010  32.499  58.570  1.00 27.37           N  
ANISOU  255  N   PRO A  36     3826   4056   2517    -30     63   -246       N  
ATOM    256  CA  PRO A  36     155.782  33.600  59.514  1.00 23.76           C  
ANISOU  256  CA  PRO A  36     3387   3606   2036    -22     79   -271       C  
ATOM    257  C   PRO A  36     154.328  33.698  59.956  1.00 23.55           C  
ANISOU  257  C   PRO A  36     3335   3619   1994     -9     83   -279       C  
ATOM    258  O   PRO A  36     153.445  33.124  59.321  1.00 23.12           O  
ANISOU  258  O   PRO A  36     3256   3584   1944     -1     73   -268       O  
ATOM    259  CB  PRO A  36     156.156  34.842  58.700  1.00 22.44           C  
ANISOU  259  CB  PRO A  36     3285   3394   1847     -4     95   -285       C  
ATOM    260  CG  PRO A  36     157.000  34.328  57.569  1.00 22.74           C  
ANISOU  260  CG  PRO A  36     3332   3407   1900     -7     88   -267       C  
ATOM    261  CD  PRO A  36     156.433  32.991  57.249  1.00 24.45           C  
ANISOU  261  CD  PRO A  36     3504   3647   2141    -17     69   -245       C  
ATOM    262  N   PHE A  37     154.089  34.431  61.037  1.00 24.76           N  
ANISOU  262  N   PHE A  37     3487   3792   2130     -6     95   -304       N  
ATOM    263  CA  PHE A  37     152.751  34.553  61.596  1.00 24.71           C  
ANISOU  263  CA  PHE A  37     3445   3836   2108      9    101   -320       C  
ATOM    264  C   PHE A  37     151.726  35.128  60.621  1.00 25.59           C  
ANISOU  264  C   PHE A  37     3566   3951   2205     42    101   -334       C  
ATOM    265  O   PHE A  37     150.577  34.700  60.608  1.00 29.38           O  
ANISOU  265  O   PHE A  37     3998   4480   2683     57     96   -338       O  
ATOM    266  CB  PHE A  37     152.776  35.395  62.871  1.00 24.91           C  
ANISOU  266  CB  PHE A  37     3473   3879   2114     11    116   -352       C  
ATOM    267  CG  PHE A  37     151.411  35.737  63.389  1.00 25.72           C  
ANISOU  267  CG  PHE A  37     3539   4036   2197     33    126   -380       C  
ATOM    268  CD1 PHE A  37     150.728  36.841  62.902  1.00 23.54           C  
ANISOU  268  CD1 PHE A  37     3283   3758   1904     71    133   -414       C  
ATOM    269  CD2 PHE A  37     150.802  34.950  64.352  1.00 27.13           C  
ANISOU  269  CD2 PHE A  37     3661   4274   2373     18    128   -375       C  
ATOM    270  CE1 PHE A  37     149.467  37.156  63.370  1.00 22.55           C  
ANISOU  270  CE1 PHE A  37     3114   3690   1763    101    140   -448       C  
ATOM    271  CE2 PHE A  37     149.539  35.260  64.823  1.00 24.88           C  
ANISOU  271  CE2 PHE A  37     3336   4049   2069     40    140   -406       C  
ATOM    272  CZ  PHE A  37     148.871  36.364  64.329  1.00 22.73           C  
ANISOU  272  CZ  PHE A  37     3077   3776   1785     84    144   -445       C  
ATOM    273  N   MET A  38     152.136  36.105  59.819  1.00 23.31           N  
ANISOU  273  N   MET A  38     3337   3617   1903     54    107   -345       N  
ATOM    274  CA  MET A  38     151.200  36.796  58.935  1.00 25.60           C  
ANISOU  274  CA  MET A  38     3638   3915   2174     90    104   -363       C  
ATOM    275  C   MET A  38     150.794  35.969  57.712  1.00 27.63           C  
ANISOU  275  C   MET A  38     3879   4176   2441     97     83   -335       C  
ATOM    276  O   MET A  38     149.640  36.015  57.281  1.00 29.07           O  
ANISOU  276  O   MET A  38     4032   4397   2616    138     70   -348       O  
ATOM    277  CB  MET A  38     151.750  38.162  58.516  1.00 26.67           C  
ANISOU  277  CB  MET A  38     3842   4007   2285     96    117   -386       C  
ATOM    278  CG  MET A  38     151.746  39.192  59.636  1.00 26.16           C  
ANISOU  278  CG  MET A  38     3785   3948   2205    107    134   -429       C  
ATOM    279  SD  MET A  38     152.483  40.764  59.152  1.00 86.72           S  
ANISOU  279  SD  MET A  38    11533  11568   9849    108    151   -463       S  
ATOM    280  N   TYR A  39     151.739  35.218  57.155  1.00 22.99           N  
ANISOU  280  N   TYR A  39     3309   3552   1873     65     79   -303       N  
ATOM    281  CA  TYR A  39     151.419  34.296  56.075  1.00 22.35           C  
ANISOU  281  CA  TYR A  39     3209   3477   1806     68     59   -280       C  
ATOM    282  C   TYR A  39     150.488  33.207  56.591  1.00 24.92           C  
ANISOU  282  C   TYR A  39     3459   3861   2148     73     47   -276       C  
ATOM    283  O   TYR A  39     149.468  32.904  55.973  1.00 26.78           O  
ANISOU  283  O   TYR A  39     3662   4132   2381    100     32   -280       O  
ATOM    284  CB  TYR A  39     152.687  33.669  55.497  1.00 24.75           C  
ANISOU  284  CB  TYR A  39     3541   3735   2130     37     58   -253       C  
ATOM    285  CG  TYR A  39     152.404  32.579  54.480  1.00 25.87           C  
ANISOU  285  CG  TYR A  39     3655   3885   2288     38     37   -233       C  
ATOM    286  CD1 TYR A  39     152.246  32.880  53.135  1.00 25.94           C  
ANISOU  286  CD1 TYR A  39     3696   3879   2282     49     30   -229       C  
ATOM    287  CD2 TYR A  39     152.290  31.252  54.871  1.00 22.91           C  
ANISOU  287  CD2 TYR A  39     3222   3540   1942     26     24   -221       C  
ATOM    288  CE1 TYR A  39     151.986  31.887  52.205  1.00 25.19           C  
ANISOU  288  CE1 TYR A  39     3575   3794   2201     52     10   -215       C  
ATOM    289  CE2 TYR A  39     152.031  30.253  53.954  1.00 21.53           C  
ANISOU  289  CE2 TYR A  39     3021   3376   1783     26      5   -208       C  
ATOM    290  CZ  TYR A  39     151.878  30.577  52.623  1.00 23.25           C  
ANISOU  290  CZ  TYR A  39     3272   3576   1988     42     -2   -207       C  
ATOM    291  OH  TYR A  39     151.620  29.586  51.708  1.00 21.04           O  
ANISOU  291  OH  TYR A  39     2964   3308   1721     44    -22   -198       O  
ATOM    292  N   ASN A  40     150.853  32.620  57.727  1.00 25.44           N  
ANISOU  292  N   ASN A  40     3497   3942   2228     46     53   -270       N  
ATOM    293  CA  ASN A  40     150.035  31.599  58.370  1.00 23.93           C  
ANISOU  293  CA  ASN A  40     3236   3811   2046     38     48   -266       C  
ATOM    294  C   ASN A  40     148.616  32.099  58.586  1.00 26.99           C  
ANISOU  294  C   ASN A  40     3587   4256   2411     73     52   -297       C  
ATOM    295  O   ASN A  40     147.648  31.460  58.179  1.00 29.46           O  
ANISOU  295  O   ASN A  40     3852   4615   2726     86     41   -299       O  
ATOM    296  CB  ASN A  40     150.651  31.192  59.710  1.00 21.72           C  
ANISOU  296  CB  ASN A  40     2941   3540   1771      4     57   -259       C  
ATOM    297  CG  ASN A  40     152.062  30.648  59.565  1.00 20.54           C  
ANISOU  297  CG  ASN A  40     2815   3345   1644    -23     48   -236       C  
ATOM    298  OD1 ASN A  40     152.435  30.128  58.514  1.00 24.27           O  
ANISOU  298  OD1 ASN A  40     3297   3792   2134    -24     35   -221       O  
ATOM    299  ND2 ASN A  40     152.853  30.763  60.624  1.00 15.92           N  
ANISOU  299  ND2 ASN A  40     2236   2754   1057    -42     54   -238       N  
ATOM    300  N   ASN A  41     148.507  33.252  59.232  1.00 28.82           N  
ANISOU  300  N   ASN A  41     3838   4489   2622     91     67   -326       N  
ATOM    301  CA  ASN A  41     147.222  33.874  59.511  1.00 33.74           C  
ANISOU  301  CA  ASN A  41     4425   5169   3225    134     71   -366       C  
ATOM    302  C   ASN A  41     146.411  34.127  58.241  1.00 39.17           C  
ANISOU  302  C   ASN A  41     5111   5867   3906    186     50   -378       C  
ATOM    303  O   ASN A  41     145.359  33.518  58.032  1.00 42.63           O  
ANISOU  303  O   ASN A  41     5490   6364   4346    206     39   -388       O  
ATOM    304  CB  ASN A  41     147.438  35.177  60.284  1.00 33.07           C  
ANISOU  304  CB  ASN A  41     4372   5071   3121    149     89   -399       C  
ATOM    305  CG  ASN A  41     146.145  35.771  60.808  1.00 34.11           C  
ANISOU  305  CG  ASN A  41     4458   5269   3234    195     94   -449       C  
ATOM    306  OD1 ASN A  41     145.176  35.056  61.071  1.00 35.71           O  
ANISOU  306  OD1 ASN A  41     4593   5538   3437    197     94   -457       O  
ATOM    307  ND2 ASN A  41     146.123  37.092  60.958  1.00 32.22           N  
ANISOU  307  ND2 ASN A  41     4252   5012   2978    232    100   -489       N  
ATOM    308  N   LYS A  42     146.908  35.022  57.393  1.00 38.20           N  
ANISOU  308  N   LYS A  42     5053   5689   3773    208     44   -378       N  
ATOM    309  CA  LYS A  42     146.196  35.394  56.175  1.00 37.86           C  
ANISOU  309  CA  LYS A  42     5018   5650   3717    268     19   -389       C  
ATOM    310  C   LYS A  42     145.869  34.192  55.292  1.00 36.29           C  
ANISOU  310  C   LYS A  42     4784   5469   3534    261     -2   -364       C  
ATOM    311  O   LYS A  42     144.700  33.848  55.109  1.00 33.92           O  
ANISOU  311  O   LYS A  42     4427   5230   3233    301    -18   -386       O  
ATOM    312  CB  LYS A  42     146.992  36.432  55.378  1.00 39.35           C  
ANISOU  312  CB  LYS A  42     5289   5772   3888    280     17   -383       C  
ATOM    313  N   THR A  43     146.904  33.561  54.746  1.00 36.69           N  
ANISOU  313  N   THR A  43     4866   5471   3602    214     -2   -325       N  
ATOM    314  CA  THR A  43     146.723  32.464  53.800  1.00 33.80           C  
ANISOU  314  CA  THR A  43     4475   5115   3253    209    -22   -304       C  
ATOM    315  C   THR A  43     146.002  31.273  54.422  1.00 33.33           C  
ANISOU  315  C   THR A  43     4335   5118   3210    192    -24   -308       C  
ATOM    316  O   THR A  43     145.321  30.516  53.728  1.00 35.70           O  
ANISOU  316  O   THR A  43     4594   5452   3516    208    -44   -310       O  
ATOM    317  CB  THR A  43     148.068  31.984  53.239  1.00 29.77           C  
ANISOU  317  CB  THR A  43     4010   4541   2759    159    -19   -269       C  
ATOM    318  OG1 THR A  43     148.891  31.513  54.313  1.00 29.93           O  
ANISOU  318  OG1 THR A  43     4026   4549   2799    111     -1   -257       O  
ATOM    319  CG2 THR A  43     148.775  33.121  52.517  1.00 29.09           C  
ANISOU  319  CG2 THR A  43     4001   4401   2651    166    -13   -266       C  
ATOM    320  N   GLY A  44     146.152  31.109  55.732  1.00 28.16           N  
ANISOU  320  N   GLY A  44     3658   4482   2559    159     -2   -310       N  
ATOM    321  CA  GLY A  44     145.563  29.976  56.421  1.00 25.28           C  
ANISOU  321  CA  GLY A  44     3222   4180   2203    131      1   -308       C  
ATOM    322  C   GLY A  44     146.354  28.709  56.161  1.00 24.79           C  
ANISOU  322  C   GLY A  44     3159   4093   2168     84     -7   -272       C  
ATOM    323  O   GLY A  44     145.924  27.607  56.510  1.00 22.85           O  
ANISOU  323  O   GLY A  44     2858   3896   1929     56     -9   -266       O  
ATOM    324  N   MET A  45     147.518  28.876  55.541  1.00 25.62           N  
ANISOU  324  N   MET A  45     3323   4126   2284     74    -12   -251       N  
ATOM    325  CA  MET A  45     148.418  27.766  55.257  1.00 23.34           C  
ANISOU  325  CA  MET A  45     3037   3810   2022     37    -21   -224       C  
ATOM    326  C   MET A  45     149.691  27.940  56.071  1.00 25.16           C  
ANISOU  326  C   MET A  45     3303   3997   2261      7     -8   -211       C  
ATOM    327  O   MET A  45     149.876  28.962  56.726  1.00 26.81           O  
ANISOU  327  O   MET A  45     3540   4192   2454     14      8   -222       O  
ATOM    328  CB  MET A  45     148.791  27.767  53.776  1.00 21.35           C  
ANISOU  328  CB  MET A  45     2819   3517   1777     53    -38   -218       C  
ATOM    329  CG  MET A  45     147.616  27.606  52.828  1.00 17.63           C  
ANISOU  329  CG  MET A  45     2316   3086   1298     91    -57   -232       C  
ATOM    330  SD  MET A  45     147.106  25.886  52.688  1.00 71.11           S  
ANISOU  330  SD  MET A  45     9016   9910   8091     67    -75   -228       S  
ATOM    331  CE  MET A  45     148.611  25.146  52.056  1.00 11.94           C  
ANISOU  331  CE  MET A  45     1560   2353    625     34    -83   -203       C  
ATOM    332  N   CYS A  46     150.580  26.953  56.010  1.00 24.81           N  
ANISOU  332  N   CYS A  46     3254   3933   2239    -23    -18   -191       N  
ATOM    333  CA  CYS A  46     151.871  27.061  56.682  1.00 21.84           C  
ANISOU  333  CA  CYS A  46     2907   3521   1872    -46    -12   -183       C  
ATOM    334  C   CYS A  46     152.920  26.100  56.126  1.00 21.73           C  
ANISOU  334  C   CYS A  46     2893   3481   1884    -65    -28   -169       C  
ATOM    335  O   CYS A  46     152.594  25.101  55.472  1.00 20.45           O  
ANISOU  335  O   CYS A  46     2701   3335   1733    -71    -45   -163       O  
ATOM    336  CB  CYS A  46     151.720  26.876  58.196  1.00 18.21           C  
ANISOU  336  CB  CYS A  46     2420   3096   1403    -68     -2   -181       C  
ATOM    337  SG  CYS A  46     151.613  25.159  58.747  1.00 48.54           S  
ANISOU  337  SG  CYS A  46     6207   6980   5255   -110    -18   -158       S  
ATOM    338  N   LEU A  47     154.181  26.424  56.403  1.00 23.23           N  
ANISOU  338  N   LEU A  47     3112   3634   2080    -75    -23   -169       N  
ATOM    339  CA  LEU A  47     155.316  25.600  56.014  1.00 25.71           C  
ANISOU  339  CA  LEU A  47     3421   3930   2416    -93    -38   -164       C  
ATOM    340  C   LEU A  47     155.932  25.016  57.282  1.00 27.35           C  
ANISOU  340  C   LEU A  47     3608   4154   2628   -122    -44   -157       C  
ATOM    341  O   LEU A  47     156.259  25.751  58.214  1.00 25.32           O  
ANISOU  341  O   LEU A  47     3366   3893   2359   -124    -32   -163       O  
ATOM    342  CB  LEU A  47     156.342  26.448  55.256  1.00 26.90           C  
ANISOU  342  CB  LEU A  47     3618   4037   2567    -83    -28   -174       C  
ATOM    343  CG  LEU A  47     156.890  25.922  53.926  1.00 29.07           C  
ANISOU  343  CG  LEU A  47     3897   4295   2855    -82    -37   -176       C  
ATOM    344  CD1 LEU A  47     155.781  25.334  53.067  1.00 28.67           C  
ANISOU  344  CD1 LEU A  47     3828   4262   2804    -70    -50   -170       C  
ATOM    345  CD2 LEU A  47     157.621  27.025  53.173  1.00 28.45           C  
ANISOU  345  CD2 LEU A  47     3869   4179   2763    -69    -18   -185       C  
ATOM    346  N   CYS A  48     156.083  23.697  57.327  1.00 29.20           N  
ANISOU  346  N   CYS A  48     3811   4407   2877   -144    -66   -145       N  
ATOM    347  CA  CYS A  48     156.548  23.049  58.549  1.00 30.30           C  
ANISOU  347  CA  CYS A  48     3936   4564   3014   -172    -77   -135       C  
ATOM    348  C   CYS A  48     157.303  21.743  58.306  1.00 32.19           C  
ANISOU  348  C   CYS A  48     4157   4802   3271   -194   -106   -127       C  
ATOM    349  O   CYS A  48     157.098  21.064  57.299  1.00 33.98           O  
ANISOU  349  O   CYS A  48     4371   5029   3512   -192   -119   -128       O  
ATOM    350  CB  CYS A  48     155.365  22.786  59.485  1.00 29.71           C  
ANISOU  350  CB  CYS A  48     3837   4533   2918   -185    -71   -121       C  
ATOM    351  SG  CYS A  48     154.127  21.651  58.827  1.00 27.39           S  
ANISOU  351  SG  CYS A  48     3503   4277   2626   -195    -82   -108       S  
ATOM    352  N   VAL A  49     158.169  21.388  59.251  1.00 30.82           N  
ANISOU  352  N   VAL A  49     3985   4631   3095   -213   -120   -123       N  
ATOM    353  CA  VAL A  49     158.895  20.121  59.179  1.00 24.07           C  
ANISOU  353  CA  VAL A  49     3117   3774   2254   -232   -155   -117       C  
ATOM    354  C   VAL A  49     158.402  19.126  60.230  1.00 21.76           C  
ANISOU  354  C   VAL A  49     2813   3512   1945   -260   -174    -87       C  
ATOM    355  O   VAL A  49     158.369  19.435  61.416  1.00 20.62           O  
ANISOU  355  O   VAL A  49     2677   3381   1777   -270   -168    -77       O  
ATOM    356  CB  VAL A  49     160.422  20.321  59.280  1.00 18.36           C  
ANISOU  356  CB  VAL A  49     2407   3029   1542   -233   -166   -137       C  
ATOM    357  CG1 VAL A  49     160.946  20.998  58.027  1.00 16.52           C  
ANISOU  357  CG1 VAL A  49     2180   2771   1324   -217   -150   -163       C  
ATOM    358  CG2 VAL A  49     160.779  21.119  60.519  1.00 15.10           C  
ANISOU  358  CG2 VAL A  49     2009   2620   1108   -236   -156   -139       C  
ATOM    359  N   PRO A  50     157.992  17.931  59.785  1.00 19.91           N  
ANISOU  359  N   PRO A  50     2559   3286   1719   -276   -199    -72       N  
ATOM    360  CA  PRO A  50     157.457  16.897  60.681  1.00 18.02           C  
ANISOU  360  CA  PRO A  50     2310   3076   1461   -311   -219    -37       C  
ATOM    361  C   PRO A  50     158.525  16.364  61.626  1.00 16.26           C  
ANISOU  361  C   PRO A  50     2105   2841   1232   -325   -253    -26       C  
ATOM    362  O   PRO A  50     159.702  16.363  61.275  1.00 16.02           O  
ANISOU  362  O   PRO A  50     2083   2781   1223   -309   -274    -48       O  
ATOM    363  CB  PRO A  50     157.011  15.795  59.717  1.00 17.65           C  
ANISOU  363  CB  PRO A  50     2242   3032   1434   -321   -244    -32       C  
ATOM    364  CG  PRO A  50     157.871  15.993  58.509  1.00 17.89           C  
ANISOU  364  CG  PRO A  50     2275   3026   1496   -291   -251    -67       C  
ATOM    365  CD  PRO A  50     158.068  17.473  58.388  1.00 18.68           C  
ANISOU  365  CD  PRO A  50     2392   3116   1591   -264   -211    -88       C  
ATOM    366  N   CYS A  51     158.114  15.927  62.813  1.00 16.34           N  
ANISOU  366  N   CYS A  51     2121   2877   1210   -355   -260      9       N  
ATOM    367  CA  CYS A  51     159.051  15.429  63.814  1.00 17.68           C  
ANISOU  367  CA  CYS A  51     2313   3038   1367   -366   -297     25       C  
ATOM    368  C   CYS A  51     158.841  13.945  64.093  1.00 21.30           C  
ANISOU  368  C   CYS A  51     2773   3500   1820   -403   -344     68       C  
ATOM    369  O   CYS A  51     157.732  13.431  63.969  1.00 22.62           O  
ANISOU  369  O   CYS A  51     2925   3693   1977   -434   -335     95       O  
ATOM    370  CB  CYS A  51     158.912  16.218  65.117  1.00 17.90           C  
ANISOU  370  CB  CYS A  51     2357   3089   1356   -370   -271     32       C  
ATOM    371  SG  CYS A  51     159.035  18.016  64.922  1.00 55.40           S  
ANISOU  371  SG  CYS A  51     7108   7830   6111   -332   -221    -13       S  
ATOM    372  N   THR A  52     159.910  13.262  64.483  1.00 23.13           N  
ANISOU  372  N   THR A  52     3022   3706   2059   -402   -397     74       N  
ATOM    373  CA  THR A  52     159.835  11.833  64.762  1.00 22.91           C  
ANISOU  373  CA  THR A  52     3004   3671   2032   -436   -453    119       C  
ATOM    374  C   THR A  52     160.735  11.444  65.935  1.00 26.72           C  
ANISOU  374  C   THR A  52     3518   4141   2492   -439   -499    140       C  
ATOM    375  O   THR A  52     161.725  12.123  66.222  1.00 26.22           O  
ANISOU  375  O   THR A  52     3463   4068   2431   -404   -501    105       O  
ATOM    376  CB  THR A  52     160.223  11.007  63.527  1.00 18.02           C  
ANISOU  376  CB  THR A  52     2365   3016   1465   -423   -496     97       C  
ATOM    377  OG1 THR A  52     159.998   9.616  63.785  1.00 20.04           O  
ANISOU  377  OG1 THR A  52     2630   3259   1725   -462   -553    145       O  
ATOM    378  CG2 THR A  52     161.692  11.224  63.179  1.00 14.63           C  
ANISOU  378  CG2 THR A  52     1936   2552   1070   -378   -525     46       C  
ATOM    379  N   THR A  53     160.382  10.352  66.610  1.00 29.45           N  
ANISOU  379  N   THR A  53     3884   4487   2818   -482   -538    201       N  
ATOM    380  CA  THR A  53     161.159   9.860  67.744  1.00 34.18           C  
ANISOU  380  CA  THR A  53     4521   5073   3394   -485   -589    231       C  
ATOM    381  C   THR A  53     162.161   8.794  67.305  1.00 37.62           C  
ANISOU  381  C   THR A  53     4959   5458   3878   -468   -672    225       C  
ATOM    382  O   THR A  53     162.940   8.288  68.114  1.00 36.93           O  
ANISOU  382  O   THR A  53     4899   5351   3780   -461   -728    245       O  
ATOM    383  CB  THR A  53     160.255   9.286  68.843  1.00 35.60           C  
ANISOU  383  CB  THR A  53     4730   5277   3520   -545   -587    307       C  
ATOM    384  OG1 THR A  53     159.511   8.181  68.319  1.00 39.48           O  
ANISOU  384  OG1 THR A  53     5218   5754   4028   -593   -613    352       O  
ATOM    385  CG2 THR A  53     159.298  10.347  69.344  1.00 34.15           C  
ANISOU  385  CG2 THR A  53     4537   5147   3293   -557   -506    302       C  
ATOM    386  N   GLN A  54     162.151   8.467  66.016  1.00 40.72           N  
ANISOU  386  N   GLN A  54     5319   5828   4324   -455   -682    193       N  
ATOM    387  CA  GLN A  54     163.067   7.469  65.476  1.00 41.31           C  
ANISOU  387  CA  GLN A  54     5386   5853   4456   -433   -758    174       C  
ATOM    388  C   GLN A  54     164.227   8.150  64.760  1.00 38.57           C  
ANISOU  388  C   GLN A  54     5008   5498   4148   -372   -754     88       C  
ATOM    389  O   GLN A  54     164.055   8.725  63.684  1.00 34.14           O  
ANISOU  389  O   GLN A  54     4418   4942   3611   -354   -712     42       O  
ATOM    390  CB  GLN A  54     162.336   6.545  64.499  1.00 41.29           C  
ANISOU  390  CB  GLN A  54     5364   5828   4495   -460   -778    188       C  
ATOM    391  CG  GLN A  54     160.972   6.080  64.976  1.00 43.29           C  
ANISOU  391  CG  GLN A  54     5637   6101   4709   -530   -765    266       C  
ATOM    392  CD  GLN A  54     161.046   5.239  66.235  1.00 45.11           C  
ANISOU  392  CD  GLN A  54     5920   6311   4908   -570   -819    344       C  
ATOM    393  OE1 GLN A  54     162.074   4.628  66.532  1.00 45.87           O  
ANISOU  393  OE1 GLN A  54     6036   6361   5032   -546   -890    345       O  
ATOM    394  NE2 GLN A  54     159.954   5.209  66.987  1.00 44.32           N  
ANISOU  394  NE2 GLN A  54     5843   6245   4751   -632   -786    410       N  
ATOM    395  N   SER A  55     165.412   8.074  65.357  1.00 40.16           N  
ANISOU  395  N   SER A  55     5217   5688   4354   -342   -800     67       N  
ATOM    396  CA  SER A  55     166.596   8.685  64.773  1.00 40.54           C  
ANISOU  396  CA  SER A  55     5234   5732   4438   -290   -800    -17       C  
ATOM    397  C   SER A  55     167.399   7.639  64.007  1.00 41.99           C  
ANISOU  397  C   SER A  55     5381   5885   4688   -266   -863    -57       C  
ATOM    398  O   SER A  55     168.020   6.758  64.603  1.00 44.01           O  
ANISOU  398  O   SER A  55     5643   6124   4955   -263   -929    -39       O  
ATOM    399  CB  SER A  55     167.455   9.310  65.874  1.00 39.28           C  
ANISOU  399  CB  SER A  55     5091   5587   4245   -270   -810    -30       C  
ATOM    400  OG  SER A  55     168.668   9.827  65.354  1.00 38.26           O  
ANISOU  400  OG  SER A  55     4932   5452   4155   -226   -820   -112       O  
ATOM    401  N   LYS A  56     167.377   7.741  62.682  1.00 39.95           N  
ANISOU  401  N   LYS A  56     5087   5619   4475   -250   -840   -109       N  
ATOM    402  CA  LYS A  56     168.081   6.790  61.829  1.00 37.43           C  
ANISOU  402  CA  LYS A  56     4720   5285   4218   -229   -884   -157       C  
ATOM    403  C   LYS A  56     169.421   7.322  61.330  1.00 38.47           C  
ANISOU  403  C   LYS A  56     4802   5439   4377   -189   -874   -249       C  
ATOM    404  O   LYS A  56     170.154   6.622  60.628  1.00 42.00           O  
ANISOU  404  O   LYS A  56     5195   5903   4861   -208   -876   -274       O  
ATOM    405  CB  LYS A  56     167.182   6.347  60.675  1.00 35.00           C  
ANISOU  405  CB  LYS A  56     4396   4963   3941   -242   -868   -158       C  
ATOM    406  CG  LYS A  56     165.854   5.775  61.159  1.00 34.83           C  
ANISOU  406  CG  LYS A  56     4413   4927   3893   -293   -875    -69       C  
ATOM    407  CD  LYS A  56     164.901   5.489  60.015  1.00 36.80           C  
ANISOU  407  CD  LYS A  56     4641   5171   4170   -305   -854    -75       C  
ATOM    408  CE  LYS A  56     163.575   4.962  60.534  1.00 38.88           C  
ANISOU  408  CE  LYS A  56     4936   5431   4405   -364   -859     10       C  
ATOM    409  NZ  LYS A  56     162.571   4.770  59.450  1.00 39.08           N  
ANISOU  409  NZ  LYS A  56     4936   5461   4453   -377   -835      0       N  
ATOM    410  N   GLY A  57     169.736   8.560  61.700  1.00 35.27           N  
ANISOU  410  N   GLY A  57     4430   5016   3957   -171   -847   -264       N  
ATOM    411  CA  GLY A  57     171.000   9.172  61.331  1.00 33.77           C  
ANISOU  411  CA  GLY A  57     4252   4756   3822   -153   -855   -309       C  
ATOM    412  C   GLY A  57     171.044   9.712  59.911  1.00 33.40           C  
ANISOU  412  C   GLY A  57     4227   4669   3796   -222   -822   -287       C  
ATOM    413  O   GLY A  57     172.118   9.825  59.317  1.00 33.78           O  
ANISOU  413  O   GLY A  57     4247   4731   3856   -265   -811   -304       O  
ATOM    414  N   TYR A  58     169.881  10.044  59.357  1.00 32.59           N  
ANISOU  414  N   TYR A  58     4121   4595   3666   -211   -777   -289       N  
ATOM    415  CA  TYR A  58     169.818  10.613  58.016  1.00 32.08           C  
ANISOU  415  CA  TYR A  58     4040   4541   3607   -230   -717   -307       C  
ATOM    416  C   TYR A  58     170.385  12.032  58.030  1.00 31.35           C  
ANISOU  416  C   TYR A  58     3946   4480   3485   -235   -647   -332       C  
ATOM    417  O   TYR A  58     170.362  12.703  59.062  1.00 32.56           O  
ANISOU  417  O   TYR A  58     4119   4650   3602   -233   -635   -319       O  
ATOM    418  CB  TYR A  58     168.381  10.604  57.489  1.00 31.65           C  
ANISOU  418  CB  TYR A  58     3985   4508   3532   -226   -675   -286       C  
ATOM    419  N   PRO A  59     170.906  12.490  56.882  1.00 29.25           N  
ANISOU  419  N   PRO A  59     3653   4226   3234   -239   -598   -372       N  
ATOM    420  CA  PRO A  59     171.616  13.771  56.788  1.00 27.29           C  
ANISOU  420  CA  PRO A  59     3396   4006   2968   -243   -537   -406       C  
ATOM    421  C   PRO A  59     170.769  14.973  57.204  1.00 28.23           C  
ANISOU  421  C   PRO A  59     3540   4151   3034   -246   -478   -381       C  
ATOM    422  O   PRO A  59     171.250  15.846  57.925  1.00 26.88           O  
ANISOU  422  O   PRO A  59     3376   3993   2843   -251   -459   -390       O  
ATOM    423  CB  PRO A  59     171.961  13.866  55.296  1.00 26.72           C  
ANISOU  423  CB  PRO A  59     3290   3945   2916   -242   -494   -449       C  
ATOM    424  CG  PRO A  59     171.984  12.456  54.822  1.00 25.48           C  
ANISOU  424  CG  PRO A  59     3117   3762   2804   -237   -550   -449       C  
ATOM    425  CD  PRO A  59     170.894  11.777  55.594  1.00 27.28           C  
ANISOU  425  CD  PRO A  59     3376   3968   3020   -238   -599   -392       C  
ATOM    426  N   PHE A  60     169.518  15.008  56.759  1.00 30.63           N  
ANISOU  426  N   PHE A  60     3855   4465   3318   -244   -449   -350       N  
ATOM    427  CA  PHE A  60     168.665  16.175  56.961  1.00 32.96           C  
ANISOU  427  CA  PHE A  60     4170   4784   3570   -249   -388   -326       C  
ATOM    428  C   PHE A  60     167.895  16.124  58.278  1.00 37.73           C  
ANISOU  428  C   PHE A  60     4798   5394   4144   -250   -403   -283       C  
ATOM    429  O   PHE A  60     167.052  16.979  58.552  1.00 39.55           O  
ANISOU  429  O   PHE A  60     5044   5642   4342   -253   -358   -259       O  
ATOM    430  CB  PHE A  60     167.721  16.357  55.773  1.00 30.76           C  
ANISOU  430  CB  PHE A  60     3889   4514   3285   -245   -347   -318       C  
ATOM    431  CG  PHE A  60     168.427  16.727  54.504  1.00 28.90           C  
ANISOU  431  CG  PHE A  60     3634   4283   3063   -247   -316   -361       C  
ATOM    432  CD1 PHE A  60     169.004  15.752  53.707  1.00 26.91           C  
ANISOU  432  CD1 PHE A  60     3355   4020   2848   -243   -346   -390       C  
ATOM    433  CD2 PHE A  60     168.533  18.052  54.118  1.00 30.15           C  
ANISOU  433  CD2 PHE A  60     3801   4455   3199   -253   -257   -371       C  
ATOM    434  CE1 PHE A  60     169.663  16.091  52.539  1.00 26.16           C  
ANISOU  434  CE1 PHE A  60     3239   3938   2762   -245   -310   -432       C  
ATOM    435  CE2 PHE A  60     169.191  18.400  52.952  1.00 28.92           C  
ANISOU  435  CE2 PHE A  60     3630   4308   3051   -259   -225   -409       C  
ATOM    436  CZ  PHE A  60     169.758  17.417  52.160  1.00 26.04           C  
ANISOU  436  CZ  PHE A  60     3234   3941   2718   -255   -249   -441       C  
ATOM    437  N   GLU A  61     168.185  15.109  59.085  1.00 38.54           N  
ANISOU  437  N   GLU A  61     4904   5481   4258   -247   -469   -272       N  
ATOM    438  CA  GLU A  61     167.631  15.013  60.429  1.00 35.31           C  
ANISOU  438  CA  GLU A  61     4517   5085   3814   -250   -484   -233       C  
ATOM    439  C   GLU A  61     168.243  16.063  61.352  1.00 32.54           C  
ANISOU  439  C   GLU A  61     4180   4747   3438   -252   -465   -244       C  
ATOM    440  O   GLU A  61     169.465  16.189  61.435  1.00 34.08           O  
ANISOU  440  O   GLU A  61     4367   4930   3653   -249   -488   -281       O  
ATOM    441  CB  GLU A  61     167.870  13.616  61.001  1.00 37.13           C  
ANISOU  441  CB  GLU A  61     4748   5296   4063   -243   -565   -220       C  
ATOM    442  CG  GLU A  61     166.965  12.540  60.433  1.00 39.08           C  
ANISOU  442  CG  GLU A  61     4986   5538   4327   -246   -585   -197       C  
ATOM    443  CD  GLU A  61     167.082  11.224  61.190  1.00 43.08           C  
ANISOU  443  CD  GLU A  61     5492   6033   4842   -242   -661   -177       C  
ATOM    444  OE1 GLU A  61     167.864  11.167  62.166  1.00 43.46           O  
ANISOU  444  OE1 GLU A  61     5552   6081   4882   -231   -699   -182       O  
ATOM    445  OE2 GLU A  61     166.391  10.252  60.809  1.00 45.13           O  
ANISOU  445  OE2 GLU A  61     5742   6289   5118   -250   -682   -157       O  
ATOM    446  N   VAL A  62     167.391  16.827  62.030  1.00 31.06           N  
ANISOU  446  N   VAL A  62     4009   4582   3210   -258   -423   -216       N  
ATOM    447  CA  VAL A  62     167.848  17.804  63.017  1.00 27.76           C  
ANISOU  447  CA  VAL A  62     3605   4176   2766   -260   -407   -226       C  
ATOM    448  C   VAL A  62     167.289  17.470  64.399  1.00 28.07           C  
ANISOU  448  C   VAL A  62     3666   4232   2766   -263   -428   -187       C  
ATOM    449  O   VAL A  62     166.074  17.357  64.571  1.00 24.62           O  
ANISOU  449  O   VAL A  62     3235   3811   2307   -273   -403   -148       O  
ATOM    450  CB  VAL A  62     167.421  19.241  62.645  1.00 22.33           C  
ANISOU  450  CB  VAL A  62     2919   3499   2065   -263   -336   -236       C  
ATOM    451  CG1 VAL A  62     167.769  20.212  63.767  1.00 18.06           C  
ANISOU  451  CG1 VAL A  62     2394   2971   1498   -265   -324   -245       C  
ATOM    452  CG2 VAL A  62     168.068  19.673  61.340  1.00 20.33           C  
ANISOU  452  CG2 VAL A  62     2648   3235   1841   -263   -311   -274       C  
ATOM    453  N   VAL A  63     168.172  17.323  65.383  1.00 31.80           N  
ANISOU  453  N   VAL A  63     4150   4704   3230   -258   -472   -197       N  
ATOM    454  CA  VAL A  63     167.761  16.944  66.738  1.00 31.61           C  
ANISOU  454  CA  VAL A  63     4150   4698   3162   -261   -496   -159       C  
ATOM    455  C   VAL A  63     167.115  18.089  67.521  1.00 36.73           C  
ANISOU  455  C   VAL A  63     4813   5374   3769   -269   -441   -149       C  
ATOM    456  O   VAL A  63     167.670  19.187  67.615  1.00 41.65           O  
ANISOU  456  O   VAL A  63     5435   5998   4392   -265   -416   -185       O  
ATOM    457  CB  VAL A  63     168.943  16.379  67.563  1.00 22.32           C  
ANISOU  457  CB  VAL A  63     2982   3511   1986   -245   -571   -175       C  
ATOM    458  CG1 VAL A  63     168.685  16.552  69.056  1.00 19.90           C  
ANISOU  458  CG1 VAL A  63     2706   3232   1623   -248   -577   -147       C  
ATOM    459  CG2 VAL A  63     169.183  14.919  67.224  1.00 19.24           C  
ANISOU  459  CG2 VAL A  63     2584   3099   1626   -234   -639   -166       C  
ATOM    460  N   LEU A  64     165.939  17.815  68.080  1.00 34.91           N  
ANISOU  460  N   LEU A  64     4593   5166   3505   -283   -423   -103       N  
ATOM    461  CA  LEU A  64     165.218  18.790  68.890  1.00 32.71           C  
ANISOU  461  CA  LEU A  64     4326   4914   3188   -289   -375    -95       C  
ATOM    462  C   LEU A  64     165.292  18.446  70.376  1.00 36.13           C  
ANISOU  462  C   LEU A  64     4786   5371   3573   -295   -405    -71       C  
ATOM    463  O   LEU A  64     164.879  17.364  70.796  1.00 36.83           O  
ANISOU  463  O   LEU A  64     4885   5468   3641   -309   -434    -26       O  
ATOM    464  CB  LEU A  64     163.753  18.876  68.454  1.00 29.22           C  
ANISOU  464  CB  LEU A  64     3873   4486   2742   -302   -327    -69       C  
ATOM    465  CG  LEU A  64     163.469  19.337  67.024  1.00 23.71           C  
ANISOU  465  CG  LEU A  64     3155   3771   2084   -293   -293    -90       C  
ATOM    466  CD1 LEU A  64     161.973  19.351  66.755  1.00 23.08           C  
ANISOU  466  CD1 LEU A  64     3065   3709   1997   -303   -255    -64       C  
ATOM    467  CD2 LEU A  64     164.075  20.711  66.772  1.00 21.24           C  
ANISOU  467  CD2 LEU A  64     2842   3446   1782   -278   -263   -133       C  
ATOM    468  N   SER A  65     165.817  19.375  71.170  1.00 38.68           N  
ANISOU  468  N   SER A  65     5120   5703   3873   -285   -399    -98       N  
ATOM    469  CA  SER A  65     165.887  19.193  72.615  1.00 36.10           C  
ANISOU  469  CA  SER A  65     4821   5401   3493   -287   -423    -79       C  
ATOM    470  C   SER A  65     164.759  19.957  73.300  1.00 37.12           C  
ANISOU  470  C   SER A  65     4956   5564   3584   -300   -367    -65       C  
ATOM    471  O   SER A  65     163.967  20.633  72.642  1.00 36.16           O  
ANISOU  471  O   SER A  65     4816   5444   3481   -302   -315    -74       O  
ATOM    472  CB  SER A  65     167.243  19.660  73.150  1.00 32.81           C  
ANISOU  472  CB  SER A  65     4414   4977   3074   -268   -462   -122       C  
ATOM    473  N   GLY A  66     164.693  19.850  74.623  1.00 39.43           N  
ANISOU  473  N   GLY A  66     5274   5886   3822   -305   -381    -47       N  
ATOM    474  CA  GLY A  66     163.672  20.536  75.391  1.00 39.15           C  
ANISOU  474  CA  GLY A  66     5244   5887   3746   -317   -331    -39       C  
ATOM    475  C   GLY A  66     162.263  20.148  74.988  1.00 37.22           C  
ANISOU  475  C   GLY A  66     4982   5657   3502   -341   -291     -3       C  
ATOM    476  O   GLY A  66     161.402  21.008  74.800  1.00 36.88           O  
ANISOU  476  O   GLY A  66     4922   5628   3463   -341   -239    -19       O  
ATOM    477  N   GLN A  67     162.025  18.847  74.856  1.00 36.51           N  
ANISOU  477  N   GLN A  67     4897   5566   3409   -362   -319     44       N  
ATOM    478  CA  GLN A  67     160.697  18.352  74.516  1.00 37.18           C  
ANISOU  478  CA  GLN A  67     4965   5669   3493   -393   -287     80       C  
ATOM    479  C   GLN A  67     160.295  17.205  75.437  1.00 40.46           C  
ANISOU  479  C   GLN A  67     5405   6110   3859   -430   -309    142       C  
ATOM    480  O   GLN A  67     161.071  16.791  76.299  1.00 45.22           O  
ANISOU  480  O   GLN A  67     6040   6712   4428   -426   -353    157       O  
ATOM    481  CB  GLN A  67     160.642  17.916  73.049  1.00 34.45           C  
ANISOU  481  CB  GLN A  67     4593   5290   3205   -391   -291     77       C  
ATOM    482  CG  GLN A  67     159.744  18.791  72.179  1.00 32.80           C  
ANISOU  482  CG  GLN A  67     4353   5086   3025   -383   -236     51       C  
ATOM    483  CD  GLN A  67     160.148  20.260  72.197  1.00 27.13           C  
ANISOU  483  CD  GLN A  67     3634   4359   2315   -351   -210     -1       C  
ATOM    484  OE1 GLN A  67     161.253  20.620  71.787  1.00 24.67           O  
ANISOU  484  OE1 GLN A  67     3327   4016   2030   -329   -229    -32       O  
ATOM    485  NE2 GLN A  67     159.252  21.114  72.682  1.00 25.34           N  
ANISOU  485  NE2 GLN A  67     3401   4162   2066   -352   -166    -12       N  
ATOM    486  N   GLU A  68     159.083  16.694  75.254  1.00 39.03           N  
ANISOU  486  N   GLU A  68     5209   5951   3670   -468   -280    177       N  
ATOM    487  CA  GLU A  68     158.577  15.629  76.114  1.00 41.72           C  
ANISOU  487  CA  GLU A  68     5574   6317   3961   -515   -294    241       C  
ATOM    488  C   GLU A  68     159.166  14.263  75.752  1.00 44.31           C  
ANISOU  488  C   GLU A  68     5922   6608   4306   -530   -359    285       C  
ATOM    489  O   GLU A  68     159.389  13.420  76.624  1.00 46.08           O  
ANISOU  489  O   GLU A  68     6185   6834   4489   -553   -397    336       O  
ATOM    490  CB  GLU A  68     157.046  15.603  76.100  1.00 42.69           C  
ANISOU  490  CB  GLU A  68     5670   6482   4068   -557   -239    260       C  
ATOM    491  CG  GLU A  68     156.417  15.486  74.732  1.00 41.58           C  
ANISOU  491  CG  GLU A  68     5489   6330   3981   -562   -222    249       C  
ATOM    492  CD  GLU A  68     154.935  15.814  74.754  1.00 39.35           C  
ANISOU  492  CD  GLU A  68     5172   6097   3682   -590   -163    247       C  
ATOM    493  OE1 GLU A  68     154.149  15.043  74.165  1.00 42.05           O  
ANISOU  493  OE1 GLU A  68     5493   6448   4035   -629   -159    275       O  
ATOM    494  OE2 GLU A  68     154.558  16.843  75.357  1.00 35.07           O  
ANISOU  494  OE2 GLU A  68     4621   5586   3116   -574   -124    215       O  
ATOM    495  N   ARG A  69     159.412  14.056  74.461  1.00 46.46           N  
ANISOU  495  N   ARG A  69     6169   6845   4639   -516   -373    266       N  
ATOM    496  CA  ARG A  69     160.140  12.881  73.983  1.00 47.03           C  
ANISOU  496  CA  ARG A  69     6255   6874   4739   -519   -441    293       C  
ATOM    497  C   ARG A  69     161.248  13.304  73.026  1.00 42.53           C  
ANISOU  497  C   ARG A  69     5667   6266   4226   -467   -465    233       C  
ATOM    498  O   ARG A  69     160.987  13.956  72.015  1.00 39.72           O  
ANISOU  498  O   ARG A  69     5278   5906   3910   -451   -428    193       O  
ATOM    499  CB  ARG A  69     159.209  11.893  73.272  1.00 51.02           C  
ANISOU  499  CB  ARG A  69     6748   7376   5264   -567   -442    337       C  
ATOM    500  CG  ARG A  69     158.186  11.212  74.164  1.00 56.79           C  
ANISOU  500  CG  ARG A  69     7499   8138   5940   -631   -428    405       C  
ATOM    501  CD  ARG A  69     157.359  10.187  73.369  1.00 60.65           C  
ANISOU  501  CD  ARG A  69     7974   8618   6453   -683   -436    448       C  
ATOM    502  NE  ARG A  69     156.365   9.512  74.202  1.00 66.56           N  
ANISOU  502  NE  ARG A  69     8742   9397   7149   -754   -420    515       N  
ATOM    503  CZ  ARG A  69     155.493   8.613  73.753  1.00 69.06           C  
ANISOU  503  CZ  ARG A  69     9051   9714   7474   -815   -423    561       C  
ATOM    504  NH1 ARG A  69     155.492   8.286  72.461  1.00 67.77           N  
ANISOU  504  NH1 ARG A  69     8859   9523   7366   -809   -443    544       N  
ATOM    505  NH2 ARG A  69     154.623   8.052  74.595  1.00 70.06           N  
ANISOU  505  NH2 ARG A  69     9198   9871   7551   -884   -403    622       N  
ATOM    506  N   ASP A  70     162.483  12.931  73.347  1.00 44.90           N  
ANISOU  506  N   ASP A  70     5989   6541   4530   -440   -528    226       N  
ATOM    507  CA  ASP A  70     163.619  13.235  72.484  1.00 47.21           C  
ANISOU  507  CA  ASP A  70     6261   6800   4876   -394   -556    167       C  
ATOM    508  C   ASP A  70     163.410  12.615  71.109  1.00 49.79           C  
ANISOU  508  C   ASP A  70     6561   7100   5259   -400   -564    164       C  
ATOM    509  O   ASP A  70     163.066  11.439  70.995  1.00 52.74           O  
ANISOU  509  O   ASP A  70     6943   7460   5638   -430   -600    212       O  
ATOM    510  CB  ASP A  70     164.922  12.722  73.096  1.00 48.42           C  
ANISOU  510  CB  ASP A  70     6437   6936   5024   -366   -633    161       C  
ATOM    511  CG  ASP A  70     164.769  12.339  74.552  1.00 51.24           C  
ANISOU  511  CG  ASP A  70     6838   7317   5314   -384   -654    213       C  
ATOM    512  OD1 ASP A  70     163.688  12.595  75.126  1.00 50.41           O  
ANISOU  512  OD1 ASP A  70     6744   7246   5166   -419   -601    247       O  
ATOM    513  OD2 ASP A  70     165.732  11.782  75.122  1.00 53.71           O  
ANISOU  513  OD2 ASP A  70     7173   7618   5618   -362   -723    218       O  
ATOM    514  N   GLY A  71     163.620  13.413  70.068  1.00 48.50           N  
ANISOU  514  N   GLY A  71     6366   6924   5137   -374   -533    108       N  
ATOM    515  CA  GLY A  71     163.395  12.962  68.708  1.00 47.44           C  
ANISOU  515  CA  GLY A  71     6205   6768   5053   -375   -534     98       C  
ATOM    516  C   GLY A  71     164.020  13.887  67.683  1.00 45.47           C  
ANISOU  516  C   GLY A  71     5930   6501   4844   -340   -510     32       C  
ATOM    517  O   GLY A  71     164.835  14.746  68.022  1.00 44.55           O  
ANISOU  517  O   GLY A  71     5819   6384   4725   -317   -505     -5       O  
ATOM    518  N   VAL A  72     163.641  13.710  66.423  1.00 43.73           N  
ANISOU  518  N   VAL A  72     5686   6268   4662   -340   -496     20       N  
ATOM    519  CA  VAL A  72     164.235  14.477  65.338  1.00 41.47           C  
ANISOU  519  CA  VAL A  72     5379   5963   4413   -313   -474    -36       C  
ATOM    520  C   VAL A  72     163.187  15.081  64.405  1.00 38.92           C  
ANISOU  520  C   VAL A  72     5040   5651   4098   -317   -413    -39       C  
ATOM    521  O   VAL A  72     162.135  14.486  64.160  1.00 41.53           O  
ANISOU  521  O   VAL A  72     5362   5994   4424   -338   -407     -7       O  
ATOM    522  CB  VAL A  72     165.197  13.605  64.512  1.00 39.82           C  
ANISOU  522  CB  VAL A  72     5155   5720   4254   -295   -531    -65       C  
ATOM    523  CG1 VAL A  72     165.730  14.389  63.336  1.00 40.16           C  
ANISOU  523  CG1 VAL A  72     5180   5747   4332   -277   -501   -117       C  
ATOM    524  CG2 VAL A  72     166.333  13.098  65.381  1.00 38.24           C  
ANISOU  524  CG2 VAL A  72     4967   5508   4054   -280   -598    -74       C  
ATOM    525  N   ALA A  73     163.481  16.275  63.900  1.00 32.92           N  
ANISOU  525  N   ALA A  73     4275   4886   3348   -299   -372    -76       N  
ATOM    526  CA  ALA A  73     162.649  16.908  62.889  1.00 31.34           C  
ANISOU  526  CA  ALA A  73     4061   4688   3158   -294   -323    -84       C  
ATOM    527  C   ALA A  73     163.314  16.704  61.534  1.00 35.58           C  
ANISOU  527  C   ALA A  73     4583   5201   3736   -280   -334   -117       C  
ATOM    528  O   ALA A  73     164.543  16.669  61.434  1.00 40.87           O  
ANISOU  528  O   ALA A  73     5252   5852   4424   -272   -359   -147       O  
ATOM    529  CB  ALA A  73     162.482  18.384  63.184  1.00 26.29           C  
ANISOU  529  CB  ALA A  73     3430   4058   2502   -284   -273   -100       C  
ATOM    530  N   LEU A  74     162.505  16.547  60.493  1.00 30.65           N  
ANISOU  530  N   LEU A  74     3945   4577   3124   -278   -316   -115       N  
ATOM    531  CA  LEU A  74     163.039  16.250  59.171  1.00 29.23           C  
ANISOU  531  CA  LEU A  74     3750   4376   2979   -266   -326   -145       C  
ATOM    532  C   LEU A  74     163.072  17.502  58.293  1.00 31.72           C  
ANISOU  532  C   LEU A  74     4068   4689   3295   -252   -275   -169       C  
ATOM    533  O   LEU A  74     162.033  18.021  57.886  1.00 31.71           O  
ANISOU  533  O   LEU A  74     4068   4696   3283   -246   -242   -159       O  
ATOM    534  CB  LEU A  74     162.226  15.133  58.516  1.00 26.91           C  
ANISOU  534  CB  LEU A  74     3440   4084   2700   -273   -349   -129       C  
ATOM    535  CG  LEU A  74     161.989  13.900  59.397  1.00 22.99           C  
ANISOU  535  CG  LEU A  74     2946   3592   2199   -294   -398    -95       C  
ATOM    536  CD1 LEU A  74     161.162  12.864  58.660  1.00 23.79           C  
ANISOU  536  CD1 LEU A  74     3027   3693   2318   -304   -420    -84       C  
ATOM    537  CD2 LEU A  74     163.297  13.297  59.874  1.00 21.35           C  
ANISOU  537  CD2 LEU A  74     2743   3359   2010   -287   -454   -110       C  
ATOM    538  N   ALA A  75     164.281  17.974  58.002  1.00 33.59           N  
ANISOU  538  N   ALA A  75     4306   4913   3545   -248   -273   -203       N  
ATOM    539  CA  ALA A  75     164.478  19.251  57.322  1.00 33.03           C  
ANISOU  539  CA  ALA A  75     4242   4839   3470   -241   -226   -224       C  
ATOM    540  C   ALA A  75     164.166  19.197  55.826  1.00 33.43           C  
ANISOU  540  C   ALA A  75     4285   4884   3533   -232   -210   -235       C  
ATOM    541  O   ALA A  75     163.832  20.215  55.226  1.00 34.17           O  
ANISOU  541  O   ALA A  75     4393   4973   3616   -222   -172   -238       O  
ATOM    542  CB  ALA A  75     165.898  19.753  57.552  1.00 34.70           C  
ANISOU  542  CB  ALA A  75     4452   5045   3688   -248   -226   -258       C  
ATOM    543  N   ASP A  76     164.280  18.013  55.230  1.00 35.76           N  
ANISOU  543  N   ASP A  76     4561   5176   3850   -233   -244   -241       N  
ATOM    544  CA  ASP A  76     164.051  17.842  53.796  1.00 40.40           C  
ANISOU  544  CA  ASP A  76     5140   5762   4449   -223   -233   -256       C  
ATOM    545  C   ASP A  76     162.617  17.402  53.520  1.00 46.43           C  
ANISOU  545  C   ASP A  76     5900   6533   5206   -216   -236   -229       C  
ATOM    546  O   ASP A  76     162.212  17.212  52.372  1.00 50.86           O  
ANISOU  546  O   ASP A  76     6455   7096   5774   -205   -232   -238       O  
ATOM    547  CB  ASP A  76     165.026  16.812  53.231  1.00 42.09           C  
ANISOU  547  CB  ASP A  76     5330   5969   4695   -227   -269   -287       C  
ATOM    548  CG  ASP A  76     164.766  15.412  53.758  1.00 44.80           C  
ANISOU  548  CG  ASP A  76     5662   6303   5058   -230   -326   -272       C  
ATOM    549  OD1 ASP A  76     164.201  15.287  54.864  1.00 45.28           O  
ANISOU  549  OD1 ASP A  76     5733   6367   5103   -236   -339   -239       O  
ATOM    550  OD2 ASP A  76     165.125  14.435  53.066  1.00 46.12           O  
ANISOU  550  OD2 ASP A  76     5810   6457   5258   -227   -360   -293       O  
ATOM    551  N   GLN A  77     161.858  17.269  54.598  1.00 46.94           N  
ANISOU  551  N   GLN A  77     5969   6608   5257   -222   -243   -199       N  
ATOM    552  CA  GLN A  77     160.502  16.738  54.585  1.00 47.23           C  
ANISOU  552  CA  GLN A  77     5996   6661   5288   -224   -249   -174       C  
ATOM    553  C   GLN A  77     159.466  17.842  54.373  1.00 50.41           C  
ANISOU  553  C   GLN A  77     6411   7074   5670   -208   -208   -166       C  
ATOM    554  O   GLN A  77     158.273  17.618  54.581  1.00 55.48           O  
ANISOU  554  O   GLN A  77     7042   7736   6301   -210   -206   -147       O  
ATOM    555  CB  GLN A  77     160.218  15.968  55.878  1.00 48.20           C  
ANISOU  555  CB  GLN A  77     6115   6795   5402   -245   -276   -145       C  
ATOM    556  CG  GLN A  77     159.120  14.920  55.757  1.00 47.77           C  
ANISOU  556  CG  GLN A  77     6041   6758   5351   -259   -298   -125       C  
ATOM    557  CD  GLN A  77     159.495  13.775  54.838  1.00 44.84           C  
ANISOU  557  CD  GLN A  77     5653   6369   5015   -257   -341   -144       C  
ATOM    558  OE1 GLN A  77     160.592  13.225  54.922  1.00 44.31           O  
ANISOU  558  OE1 GLN A  77     5588   6278   4972   -257   -376   -159       O  
ATOM    559  NE2 GLN A  77     158.581  13.414  53.947  1.00 42.85           N  
ANISOU  559  NE2 GLN A  77     5383   6127   4770   -253   -341   -148       N  
ATOM    560  N   VAL A  78     159.919  19.031  53.976  1.00 47.62           N  
ANISOU  560  N   VAL A  78     6079   6704   5309   -193   -177   -180       N  
ATOM    561  CA  VAL A  78     159.121  20.246  54.113  1.00 44.59           C  
ANISOU  561  CA  VAL A  78     5717   6319   4906   -177   -145   -172       C  
ATOM    562  C   VAL A  78     157.682  20.039  53.667  1.00 39.64           C  
ANISOU  562  C   VAL A  78     5079   5711   4273   -165   -145   -161       C  
ATOM    563  O   VAL A  78     157.413  19.428  52.632  1.00 37.56           O  
ANISOU  563  O   VAL A  78     4802   5450   4019   -158   -158   -168       O  
ATOM    564  CB  VAL A  78     159.693  21.399  53.259  1.00 46.49           C  
ANISOU  564  CB  VAL A  78     5988   6535   5142   -160   -119   -189       C  
ATOM    565  CG1 VAL A  78     158.841  22.650  53.419  1.00 46.66           C  
ANISOU  565  CG1 VAL A  78     6039   6548   5142   -139    -93   -181       C  
ATOM    566  CG2 VAL A  78     161.142  21.679  53.620  1.00 48.52           C  
ANISOU  566  CG2 VAL A  78     6250   6781   5405   -175   -116   -207       C  
ATOM    567  N   LYS A  79     156.762  20.558  54.474  1.00 37.78           N  
ANISOU  567  N   LYS A  79     4844   5491   4019   -162   -130   -148       N  
ATOM    568  CA  LYS A  79     155.335  20.324  54.295  1.00 35.41           C  
ANISOU  568  CA  LYS A  79     4523   5221   3710   -156   -130   -141       C  
ATOM    569  C   LYS A  79     154.557  21.639  54.217  1.00 33.81           C  
ANISOU  569  C   LYS A  79     4342   5016   3489   -128   -105   -146       C  
ATOM    570  O   LYS A  79     154.646  22.472  55.123  1.00 33.33           O  
ANISOU  570  O   LYS A  79     4298   4951   3415   -127    -88   -144       O  
ATOM    571  CB  LYS A  79     154.785  19.489  55.464  1.00 34.54           C  
ANISOU  571  CB  LYS A  79     4383   5148   3592   -186   -140   -121       C  
ATOM    572  CG  LYS A  79     155.367  18.085  55.612  1.00 36.23           C  
ANISOU  572  CG  LYS A  79     4580   5364   3820   -215   -173   -111       C  
ATOM    573  CD  LYS A  79     154.804  17.138  54.564  1.00 40.12           C  
ANISOU  573  CD  LYS A  79     5047   5869   4327   -215   -195   -117       C  
ATOM    574  CE  LYS A  79     154.883  15.680  55.005  1.00 40.02           C  
ANISOU  574  CE  LYS A  79     5015   5869   4323   -252   -231   -101       C  
ATOM    575  NZ  LYS A  79     154.220  14.784  54.012  1.00 38.67           N  
ANISOU  575  NZ  LYS A  79     4815   5709   4167   -253   -255   -110       N  
ATOM    576  N   SER A  80     153.796  21.818  53.140  1.00 32.01           N  
ANISOU  576  N   SER A  80     4114   4791   3257   -104   -106   -154       N  
ATOM    577  CA  SER A  80     152.824  22.901  53.053  1.00 31.23           C  
ANISOU  577  CA  SER A  80     4030   4699   3137    -76    -90   -159       C  
ATOM    578  C   SER A  80     151.456  22.354  53.439  1.00 32.33           C  
ANISOU  578  C   SER A  80     4120   4897   3268    -80    -95   -159       C  
ATOM    579  O   SER A  80     150.992  21.375  52.858  1.00 34.41           O  
ANISOU  579  O   SER A  80     4350   5186   3540    -85   -114   -161       O  
ATOM    580  CB  SER A  80     152.764  23.473  51.634  1.00 31.92           C  
ANISOU  580  CB  SER A  80     4149   4761   3218    -47    -91   -169       C  
ATOM    581  OG  SER A  80     151.782  24.503  51.536  1.00 31.33           O  
ANISOU  581  OG  SER A  80     4090   4696   3120    -18    -82   -175       O  
ATOM    582  N   ILE A  81     150.811  22.974  54.421  1.00 31.90           N  
ANISOU  582  N   ILE A  81     4058   4867   3194    -78    -78   -160       N  
ATOM    583  CA  ILE A  81     149.532  22.457  54.903  1.00 29.86           C  
ANISOU  583  CA  ILE A  81     3746   4676   2923    -88    -78   -162       C  
ATOM    584  C   ILE A  81     148.516  23.552  55.197  1.00 33.43           C  
ANISOU  584  C   ILE A  81     4193   5157   3350    -58    -61   -181       C  
ATOM    585  O   ILE A  81     148.876  24.709  55.389  1.00 31.69           O  
ANISOU  585  O   ILE A  81     4015   4903   3122    -38    -47   -187       O  
ATOM    586  CB  ILE A  81     149.709  21.620  56.185  1.00 25.15           C  
ANISOU  586  CB  ILE A  81     3125   4107   2323   -135    -75   -143       C  
ATOM    587  CG1 ILE A  81     150.459  22.429  57.243  1.00 22.90           C  
ANISOU  587  CG1 ILE A  81     2874   3796   2031   -139    -58   -139       C  
ATOM    588  CG2 ILE A  81     150.440  20.326  55.889  1.00 25.33           C  
ANISOU  588  CG2 ILE A  81     3141   4117   2367   -165    -99   -128       C  
ATOM    589  CD1 ILE A  81     150.677  21.692  58.549  1.00 22.10           C  
ANISOU  589  CD1 ILE A  81     2757   3720   1920   -184    -57   -118       C  
ATOM    590  N   ALA A  82     147.241  23.182  55.227  1.00 36.76           N  
ANISOU  590  N   ALA A  82     4561   5646   3760    -55    -62   -194       N  
ATOM    591  CA  ALA A  82     146.235  24.079  55.768  1.00 36.60           C  
ANISOU  591  CA  ALA A  82     4521   5670   3714    -31    -45   -217       C  
ATOM    592  C   ALA A  82     146.082  23.680  57.222  1.00 35.18           C  
ANISOU  592  C   ALA A  82     4312   5534   3521    -76    -25   -208       C  
ATOM    593  O   ALA A  82     145.520  22.630  57.531  1.00 34.19           O  
ANISOU  593  O   ALA A  82     4136   5464   3389   -113    -26   -201       O  
ATOM    594  CB  ALA A  82     144.922  23.930  55.026  1.00 37.57           C  
ANISOU  594  CB  ALA A  82     4594   5854   3828      0    -56   -245       C  
ATOM    595  N   TRP A  83     146.582  24.526  58.115  1.00 35.85           N  
ANISOU  595  N   TRP A  83     4430   5593   3597    -76     -7   -207       N  
ATOM    596  CA  TRP A  83     146.621  24.199  59.531  1.00 35.59           C  
ANISOU  596  CA  TRP A  83     4380   5592   3548   -119     10   -195       C  
ATOM    597  C   TRP A  83     145.267  24.446  60.183  1.00 35.08           C  
ANISOU  597  C   TRP A  83     4263   5612   3455   -118     31   -221       C  
ATOM    598  O   TRP A  83     144.857  23.719  61.087  1.00 35.75           O  
ANISOU  598  O   TRP A  83     4310   5751   3522   -165     44   -210       O  
ATOM    599  CB  TRP A  83     147.715  25.006  60.231  1.00 38.44           C  
ANISOU  599  CB  TRP A  83     4796   5898   3911   -116     19   -189       C  
ATOM    600  CG  TRP A  83     147.498  26.476  60.161  1.00 42.07           C  
ANISOU  600  CG  TRP A  83     5282   6342   4360    -72     31   -218       C  
ATOM    601  CD1 TRP A  83     147.956  27.330  59.203  1.00 42.12           C  
ANISOU  601  CD1 TRP A  83     5336   6292   4375    -35     24   -226       C  
ATOM    602  CD2 TRP A  83     146.759  27.274  61.093  1.00 44.65           C  
ANISOU  602  CD2 TRP A  83     5592   6714   4661    -61     54   -244       C  
ATOM    603  NE1 TRP A  83     147.548  28.614  59.481  1.00 42.14           N  
ANISOU  603  NE1 TRP A  83     5355   6299   4358     -3     39   -255       N  
ATOM    604  CE2 TRP A  83     146.811  28.605  60.636  1.00 43.72           C  
ANISOU  604  CE2 TRP A  83     5512   6560   4538    -15     56   -269       C  
ATOM    605  CE3 TRP A  83     146.058  26.990  62.270  1.00 47.34           C  
ANISOU  605  CE3 TRP A  83     5888   7121   4977    -89     73   -251       C  
ATOM    606  CZ2 TRP A  83     146.188  29.649  61.312  1.00 45.84           C  
ANISOU  606  CZ2 TRP A  83     5775   6860   4783     10     75   -304       C  
ATOM    607  CZ3 TRP A  83     145.441  28.029  62.941  1.00 49.39           C  
ANISOU  607  CZ3 TRP A  83     6138   7413   5213    -66     94   -286       C  
ATOM    608  CH2 TRP A  83     145.510  29.342  62.460  1.00 49.00           C  
ANISOU  608  CH2 TRP A  83     6126   7328   5164    -14     93   -315       C  
ATOM    609  N   ARG A  84     144.581  25.485  59.721  1.00 33.45           N  
ANISOU  609  N   ARG A  84     4053   5416   3241    -65     35   -257       N  
ATOM    610  CA  ARG A  84     143.278  25.847  60.259  1.00 31.92           C  
ANISOU  610  CA  ARG A  84     3802   5306   3021    -54     54   -294       C  
ATOM    611  C   ARG A  84     142.252  24.779  59.895  1.00 29.85           C  
ANISOU  611  C   ARG A  84     3469   5121   2753    -75     49   -303       C  
ATOM    612  O   ARG A  84     141.325  24.509  60.655  1.00 29.01           O  
ANISOU  612  O   ARG A  84     3303   5096   2622   -102     71   -322       O  
ATOM    613  CB  ARG A  84     142.852  27.217  59.719  1.00 35.87           C  
ANISOU  613  CB  ARG A  84     4318   5796   3515     17     51   -334       C  
ATOM    614  CG  ARG A  84     141.961  28.025  60.657  1.00 41.38           C  
ANISOU  614  CG  ARG A  84     4980   6555   4186     35     75   -378       C  
ATOM    615  CD  ARG A  84     142.509  29.436  60.892  1.00 44.07           C  
ANISOU  615  CD  ARG A  84     5380   6841   4522     73     80   -393       C  
ATOM    616  NE  ARG A  84     142.599  30.213  59.658  1.00 46.63           N  
ANISOU  616  NE  ARG A  84     5744   7118   4854    133     57   -404       N  
ATOM    617  CZ  ARG A  84     143.023  31.472  59.597  1.00 50.52           C  
ANISOU  617  CZ  ARG A  84     6293   7561   5340    170     57   -419       C  
ATOM    618  NH1 ARG A  84     143.396  32.102  60.704  1.00 51.06           N  
ANISOU  618  NH1 ARG A  84     6379   7621   5398    155     80   -428       N  
ATOM    619  NH2 ARG A  84     143.074  32.100  58.429  1.00 52.23           N  
ANISOU  619  NH2 ARG A  84     6549   7737   5557    220     34   -425       N  
ATOM    620  N   ALA A  85     142.436  24.172  58.726  1.00 31.50           N  
ANISOU  620  N   ALA A  85     3682   5306   2982    -66     22   -292       N  
ATOM    621  CA  ALA A  85     141.574  23.092  58.260  1.00 30.70           C  
ANISOU  621  CA  ALA A  85     3515   5272   2877    -88     13   -302       C  
ATOM    622  C   ALA A  85     141.910  21.765  58.939  1.00 32.83           C  
ANISOU  622  C   ALA A  85     3771   5559   3143   -170     19   -262       C  
ATOM    623  O   ALA A  85     141.015  21.022  59.340  1.00 34.68           O  
ANISOU  623  O   ALA A  85     3944   5878   3356   -215     32   -271       O  
ATOM    624  CB  ALA A  85     141.673  22.953  56.748  1.00 27.17           C  
ANISOU  624  CB  ALA A  85     3082   4790   2453    -45    -21   -308       C  
ATOM    625  N   ARG A  86     143.201  21.470  59.061  1.00 32.64           N  
ANISOU  625  N   ARG A  86     3805   5459   3138   -190      8   -220       N  
ATOM    626  CA  ARG A  86     143.654  20.224  59.677  1.00 36.11           C  
ANISOU  626  CA  ARG A  86     4243   5904   3574   -262      5   -179       C  
ATOM    627  C   ARG A  86     143.654  20.329  61.206  1.00 39.30           C  
ANISOU  627  C   ARG A  86     4649   6335   3950   -305     34   -162       C  
ATOM    628  O   ARG A  86     143.951  19.361  61.910  1.00 41.48           O  
ANISOU  628  O   ARG A  86     4927   6620   4213   -368     33   -124       O  
ATOM    629  CB  ARG A  86     145.056  19.849  59.171  1.00 39.40           C  
ANISOU  629  CB  ARG A  86     4716   6231   4022   -260    -22   -148       C  
ATOM    630  CG  ARG A  86     145.110  19.310  57.734  1.00 41.06           C  
ANISOU  630  CG  ARG A  86     4921   6421   4259   -238    -53   -157       C  
ATOM    631  CD  ARG A  86     146.554  19.064  57.264  1.00 41.72           C  
ANISOU  631  CD  ARG A  86     5059   6418   4374   -232    -75   -135       C  
ATOM    632  NE  ARG A  86     146.618  18.448  55.937  1.00 42.08           N  
ANISOU  632  NE  ARG A  86     5099   6446   4443   -216   -104   -145       N  
ATOM    633  CZ  ARG A  86     146.831  17.153  55.721  1.00 39.92           C  
ANISOU  633  CZ  ARG A  86     4810   6176   4182   -256   -129   -129       C  
ATOM    634  NH1 ARG A  86     146.868  16.680  54.482  1.00 38.37           N  
ANISOU  634  NH1 ARG A  86     4608   5961   4009   -235   -156   -145       N  
ATOM    635  NH2 ARG A  86     147.010  16.328  56.744  1.00 38.73           N  
ANISOU  635  NH2 ARG A  86     4654   6045   4018   -316   -131    -97       N  
ATOM    636  N   GLY A  87     143.315  21.509  61.713  1.00 37.55           N  
ANISOU  636  N   GLY A  87     4429   6123   3715   -269     56   -192       N  
ATOM    637  CA  GLY A  87     143.223  21.721  63.145  1.00 39.14           C  
ANISOU  637  CA  GLY A  87     4630   6355   3888   -303     84   -185       C  
ATOM    638  C   GLY A  87     144.550  21.615  63.871  1.00 43.49           C  
ANISOU  638  C   GLY A  87     5241   6839   4444   -322     76   -147       C  
ATOM    639  O   GLY A  87     144.689  20.833  64.812  1.00 48.50           O  
ANISOU  639  O   GLY A  87     5876   7495   5057   -379     81   -114       O  
ATOM    640  N   ALA A  88     145.531  22.397  63.433  1.00 40.88           N  
ANISOU  640  N   ALA A  88     4962   6430   4139   -275     62   -152       N  
ATOM    641  CA  ALA A  88     146.817  22.441  64.116  1.00 36.82           C  
ANISOU  641  CA  ALA A  88     4500   5860   3631   -286     54   -127       C  
ATOM    642  C   ALA A  88     146.639  22.960  65.540  1.00 34.56           C  
ANISOU  642  C   ALA A  88     4215   5605   3310   -301     79   -133       C  
ATOM    643  O   ALA A  88     145.801  23.824  65.793  1.00 31.50           O  
ANISOU  643  O   ALA A  88     3806   5257   2906   -278    103   -168       O  
ATOM    644  CB  ALA A  88     147.799  23.313  63.350  1.00 36.02           C  
ANISOU  644  CB  ALA A  88     4447   5679   3559   -236     40   -139       C  
ATOM    645  N   THR A  89     147.423  22.413  66.464  1.00 34.79           N  
ANISOU  645  N   THR A  89     4270   5621   3327   -337     73   -101       N  
ATOM    646  CA  THR A  89     147.377  22.802  67.871  1.00 33.55           C  
ANISOU  646  CA  THR A  89     4121   5493   3134   -354     94   -103       C  
ATOM    647  C   THR A  89     148.783  23.049  68.383  1.00 33.08           C  
ANISOU  647  C   THR A  89     4115   5375   3081   -345     77    -91       C  
ATOM    648  O   THR A  89     149.663  22.210  68.201  1.00 35.63           O  
ANISOU  648  O   THR A  89     4458   5662   3418   -362     49    -60       O  
ATOM    649  CB  THR A  89     146.771  21.694  68.741  1.00 34.95           C  
ANISOU  649  CB  THR A  89     4272   5732   3274   -420    105    -70       C  
ATOM    650  OG1 THR A  89     145.369  21.582  68.473  1.00 37.60           O  
ANISOU  650  OG1 THR A  89     4551   6139   3597   -434    128    -90       O  
ATOM    651  CG2 THR A  89     146.978  22.005  70.218  1.00 36.79           C  
ANISOU  651  CG2 THR A  89     4525   5986   3467   -438    122    -66       C  
ATOM    652  N   LYS A  90     149.000  24.192  69.024  1.00 30.83           N  
ANISOU  652  N   LYS A  90     3848   5083   2783   -318     92   -119       N  
ATOM    653  CA  LYS A  90     150.328  24.509  69.526  1.00 29.96           C  
ANISOU  653  CA  LYS A  90     3783   4924   2675   -309     76   -115       C  
ATOM    654  C   LYS A  90     150.793  23.458  70.531  1.00 33.52           C  
ANISOU  654  C   LYS A  90     4245   5392   3099   -354     63    -75       C  
ATOM    655  O   LYS A  90     150.145  23.231  71.551  1.00 35.07           O  
ANISOU  655  O   LYS A  90     4429   5644   3254   -385     82    -67       O  
ATOM    656  CB  LYS A  90     150.320  25.897  70.175  1.00 27.16           C  
ANISOU  656  CB  LYS A  90     3443   4574   2305   -279     97   -154       C  
ATOM    657  CG  LYS A  90     151.556  26.211  71.004  1.00 25.86           C  
ANISOU  657  CG  LYS A  90     3317   4379   2130   -279     84   -154       C  
ATOM    658  CD  LYS A  90     151.734  27.704  71.199  1.00 25.43           C  
ANISOU  658  CD  LYS A  90     3281   4309   2072   -242     99   -198       C  
ATOM    659  CE  LYS A  90     153.043  28.002  71.900  1.00 25.69           C  
ANISOU  659  CE  LYS A  90     3350   4313   2098   -242     83   -201       C  
ATOM    660  NZ  LYS A  90     153.370  29.456  71.867  1.00 23.82           N  
ANISOU  660  NZ  LYS A  90     3134   4050   1865   -209     94   -244       N  
ATOM    661  N   LYS A  91     151.915  22.812  70.223  1.00 36.60           N  
ANISOU  661  N   LYS A  91     4661   5736   3510   -358     30    -52       N  
ATOM    662  CA  LYS A  91     152.535  21.859  71.140  1.00 38.48           C  
ANISOU  662  CA  LYS A  91     4920   5981   3722   -394      8    -15       C  
ATOM    663  C   LYS A  91     153.665  22.461  71.973  1.00 37.04           C  
ANISOU  663  C   LYS A  91     4773   5775   3525   -377     -4    -28       C  
ATOM    664  O   LYS A  91     154.125  21.852  72.940  1.00 38.09           O  
ANISOU  664  O   LYS A  91     4927   5921   3625   -402    -20     -1       O  
ATOM    665  CB  LYS A  91     153.036  20.632  70.368  1.00 39.92           C  
ANISOU  665  CB  LYS A  91     5104   6133   3929   -412    -27     18       C  
ATOM    666  CG  LYS A  91     153.974  19.726  71.150  1.00 41.33           C  
ANISOU  666  CG  LYS A  91     5314   6303   4088   -438    -62     54       C  
ATOM    667  CD  LYS A  91     153.724  18.266  70.821  1.00 43.83           C  
ANISOU  667  CD  LYS A  91     5623   6624   4405   -481    -86    101       C  
ATOM    668  CE  LYS A  91     152.386  17.821  71.376  1.00 48.31           C  
ANISOU  668  CE  LYS A  91     6168   7255   4934   -529    -58    126       C  
ATOM    669  NZ  LYS A  91     152.316  18.052  72.845  1.00 52.34           N  
ANISOU  669  NZ  LYS A  91     6698   7799   5390   -547    -42    137       N  
ATOM    670  N   GLY A  92     154.117  23.653  71.602  1.00 36.05           N  
ANISOU  670  N   GLY A  92     4658   5618   3423   -336      3    -68       N  
ATOM    671  CA  GLY A  92     155.233  24.253  72.309  1.00 37.94           C  
ANISOU  671  CA  GLY A  92     4928   5837   3650   -322     -9    -85       C  
ATOM    672  C   GLY A  92     156.123  25.131  71.452  1.00 39.66           C  
ANISOU  672  C   GLY A  92     5160   6002   3909   -288    -16   -117       C  
ATOM    673  O   GLY A  92     155.706  25.638  70.409  1.00 38.96           O  
ANISOU  673  O   GLY A  92     5061   5892   3849   -267     -2   -132       O  
ATOM    674  N   THR A  93     157.361  25.307  71.902  1.00 40.13           N  
ANISOU  674  N   THR A  93     5243   6041   3965   -283    -38   -126       N  
ATOM    675  CA  THR A  93     158.330  26.129  71.191  1.00 39.01           C  
ANISOU  675  CA  THR A  93     5114   5853   3855   -259    -44   -158       C  
ATOM    676  C   THR A  93     159.642  25.369  70.964  1.00 38.30           C  
ANISOU  676  C   THR A  93     5033   5737   3783   -266    -83   -149       C  
ATOM    677  O   THR A  93     159.951  24.419  71.685  1.00 41.74           O  
ANISOU  677  O   THR A  93     5474   6190   4196   -284   -110   -124       O  
ATOM    678  CB  THR A  93     158.608  27.438  71.964  1.00 38.90           C  
ANISOU  678  CB  THR A  93     5116   5845   3821   -245    -28   -196       C  
ATOM    679  OG1 THR A  93     158.317  28.562  71.126  1.00 40.15           O  
ANISOU  679  OG1 THR A  93     5276   5977   4002   -220     -5   -224       O  
ATOM    680  CG2 THR A  93     160.058  27.507  72.429  1.00 37.95           C  
ANISOU  680  CG2 THR A  93     5013   5709   3698   -247    -57   -211       C  
ATOM    681  N   VAL A  94     160.402  25.781  69.951  1.00 35.29           N  
ANISOU  681  N   VAL A  94     4653   5316   3438   -251    -87   -170       N  
ATOM    682  CA  VAL A  94     161.722  25.204  69.694  1.00 31.52           C  
ANISOU  682  CA  VAL A  94     4180   4818   2980   -256   -122   -174       C  
ATOM    683  C   VAL A  94     162.794  26.295  69.751  1.00 33.20           C  
ANISOU  683  C   VAL A  94     4403   5012   3198   -247   -120   -216       C  
ATOM    684  O   VAL A  94     162.523  27.458  69.454  1.00 33.57           O  
ANISOU  684  O   VAL A  94     4455   5048   3250   -234    -90   -240       O  
ATOM    685  CB  VAL A  94     161.784  24.465  68.337  1.00 28.26           C  
ANISOU  685  CB  VAL A  94     3753   4379   2605   -256   -132   -162       C  
ATOM    686  CG1 VAL A  94     160.388  24.117  67.854  1.00 28.31           C  
ANISOU  686  CG1 VAL A  94     3745   4397   2613   -258   -112   -138       C  
ATOM    687  CG2 VAL A  94     162.516  25.304  67.292  1.00 28.37           C  
ANISOU  687  CG2 VAL A  94     3769   4360   2651   -243   -120   -195       C  
ATOM    688  N   ALA A  95     164.007  25.918  70.144  1.00 33.99           N  
ANISOU  688  N   ALA A  95     4507   5110   3298   -254   -155   -227       N  
ATOM    689  CA  ALA A  95     165.106  26.871  70.245  1.00 32.01           C  
ANISOU  689  CA  ALA A  95     4260   4848   3053   -251   -156   -271       C  
ATOM    690  C   ALA A  95     165.451  27.464  68.880  1.00 30.84           C  
ANISOU  690  C   ALA A  95     4105   4668   2943   -248   -134   -293       C  
ATOM    691  O   ALA A  95     165.395  26.773  67.863  1.00 26.76           O  
ANISOU  691  O   ALA A  95     3578   4137   2454   -249   -139   -278       O  
ATOM    692  CB  ALA A  95     166.328  26.207  70.869  1.00 30.25           C  
ANISOU  692  CB  ALA A  95     4039   4631   2824   -259   -204   -281       C  
ATOM    693  N   PRO A  96     165.809  28.755  68.857  1.00 32.51           N  
ANISOU  693  N   PRO A  96     4325   4871   3157   -245   -111   -331       N  
ATOM    694  CA  PRO A  96     166.136  29.471  67.619  1.00 32.76           C  
ANISOU  694  CA  PRO A  96     4356   4873   3217   -245    -86   -352       C  
ATOM    695  C   PRO A  96     167.229  28.782  66.806  1.00 37.37           C  
ANISOU  695  C   PRO A  96     4922   5446   3832   -259   -106   -362       C  
ATOM    696  O   PRO A  96     167.206  28.856  65.577  1.00 38.76           O  
ANISOU  696  O   PRO A  96     5096   5602   4031   -259    -88   -361       O  
ATOM    697  CB  PRO A  96     166.647  30.824  68.124  1.00 31.18           C  
ANISOU  697  CB  PRO A  96     4169   4671   3007   -247    -69   -395       C  
ATOM    698  CG  PRO A  96     165.997  31.002  69.447  1.00 31.89           C  
ANISOU  698  CG  PRO A  96     4268   4788   3060   -239    -72   -390       C  
ATOM    699  CD  PRO A  96     165.895  29.628  70.041  1.00 32.51           C  
ANISOU  699  CD  PRO A  96     4337   4889   3127   -244   -106   -355       C  
ATOM    700  N   GLU A  97     168.169  28.126  67.479  1.00 39.89           N  
ANISOU  700  N   GLU A  97     5230   5778   4148   -269   -144   -373       N  
ATOM    701  CA  GLU A  97     169.300  27.502  66.797  1.00 42.38           C  
ANISOU  701  CA  GLU A  97     5524   6084   4493   -281   -166   -392       C  
ATOM    702  C   GLU A  97     168.854  26.323  65.942  1.00 42.11           C  
ANISOU  702  C   GLU A  97     5480   6042   4476   -276   -179   -359       C  
ATOM    703  O   GLU A  97     169.361  26.115  64.839  1.00 43.64           O  
ANISOU  703  O   GLU A  97     5659   6223   4698   -283   -174   -373       O  
ATOM    704  CB  GLU A  97     170.359  27.038  67.801  1.00 46.59           C  
ANISOU  704  CB  GLU A  97     6051   6633   5020   -286   -213   -413       C  
ATOM    705  CG  GLU A  97     170.886  28.128  68.713  1.00 52.55           C  
ANISOU  705  CG  GLU A  97     6811   7399   5758   -292   -206   -452       C  
ATOM    706  CD  GLU A  97     169.920  28.473  69.831  1.00 59.13           C  
ANISOU  706  CD  GLU A  97     7668   8250   6550   -280   -199   -430       C  
ATOM    707  OE1 GLU A  97     170.118  29.517  70.489  1.00 60.24           O  
ANISOU  707  OE1 GLU A  97     7817   8398   6675   -282   -185   -462       O  
ATOM    708  OE2 GLU A  97     168.965  27.700  70.055  1.00 62.07           O  
ANISOU  708  OE2 GLU A  97     8050   8630   6905   -270   -207   -385       O  
ATOM    709  N   GLU A  98     167.910  25.552  66.472  1.00 40.93           N  
ANISOU  709  N   GLU A  98     5340   5904   4308   -267   -194   -317       N  
ATOM    710  CA  GLU A  98     167.377  24.379  65.788  1.00 39.08           C  
ANISOU  710  CA  GLU A  98     5097   5663   4087   -265   -210   -284       C  
ATOM    711  C   GLU A  98     166.522  24.777  64.586  1.00 38.70           C  
ANISOU  711  C   GLU A  98     5048   5602   4054   -258   -170   -275       C  
ATOM    712  O   GLU A  98     166.643  24.198  63.504  1.00 38.76           O  
ANISOU  712  O   GLU A  98     5043   5598   4086   -259   -174   -274       O  
ATOM    713  CB  GLU A  98     166.573  23.524  66.771  1.00 38.73           C  
ANISOU  713  CB  GLU A  98     5062   5637   4015   -263   -233   -244       C  
ATOM    714  CG  GLU A  98     167.429  22.871  67.843  1.00 41.30           C  
ANISOU  714  CG  GLU A  98     5394   5972   4324   -266   -285   -246       C  
ATOM    715  CD  GLU A  98     166.694  22.660  69.157  1.00 46.86           C  
ANISOU  715  CD  GLU A  98     6118   6702   4983   -267   -292   -215       C  
ATOM    716  OE1 GLU A  98     165.453  22.814  69.191  1.00 48.24           O  
ANISOU  716  OE1 GLU A  98     6296   6890   5144   -269   -258   -188       O  
ATOM    717  OE2 GLU A  98     167.372  22.345  70.159  1.00 48.82           O  
ANISOU  717  OE2 GLU A  98     6379   6960   5209   -266   -333   -218       O  
ATOM    718  N   LEU A  99     165.660  25.771  64.779  1.00 37.49           N  
ANISOU  718  N   LEU A  99     4910   5449   3885   -249   -135   -270       N  
ATOM    719  CA  LEU A  99     164.892  26.336  63.678  1.00 33.90           C  
ANISOU  719  CA  LEU A  99     4462   4978   3441   -237   -101   -266       C  
ATOM    720  C   LEU A  99     165.859  26.821  62.607  1.00 34.31           C  
ANISOU  720  C   LEU A  99     4512   5010   3514   -244    -89   -296       C  
ATOM    721  O   LEU A  99     165.639  26.616  61.411  1.00 38.26           O  
ANISOU  721  O   LEU A  99     5010   5497   4030   -239    -79   -290       O  
ATOM    722  CB  LEU A  99     164.029  27.495  64.173  1.00 30.57           C  
ANISOU  722  CB  LEU A  99     4061   4557   2997   -222    -72   -267       C  
ATOM    723  CG  LEU A  99     163.209  28.252  63.129  1.00 29.22           C  
ANISOU  723  CG  LEU A  99     3906   4366   2832   -203    -42   -265       C  
ATOM    724  CD1 LEU A  99     162.103  27.371  62.568  1.00 31.01           C  
ANISOU  724  CD1 LEU A  99     4122   4597   3064   -194    -46   -233       C  
ATOM    725  CD2 LEU A  99     162.629  29.529  63.715  1.00 27.24           C  
ANISOU  725  CD2 LEU A  99     3678   4114   2557   -188    -17   -277       C  
ATOM    726  N   GLN A 100     166.942  27.448  63.054  1.00 32.06           N  
ANISOU  726  N   GLN A 100     4226   4726   3228   -257    -88   -330       N  
ATOM    727  CA  GLN A 100     167.964  27.976  62.160  1.00 32.26           C  
ANISOU  727  CA  GLN A 100     4246   4739   3272   -273    -71   -365       C  
ATOM    728  C   GLN A 100     168.675  26.869  61.383  1.00 31.08           C  
ANISOU  728  C   GLN A 100     4070   4591   3148   -284    -92   -371       C  
ATOM    729  O   GLN A 100     169.078  27.071  60.239  1.00 32.06           O  
ANISOU  729  O   GLN A 100     4189   4705   3287   -293    -72   -388       O  
ATOM    730  CB  GLN A 100     168.991  28.788  62.952  1.00 36.09           C  
ANISOU  730  CB  GLN A 100     4730   5231   3752   -290    -68   -406       C  
ATOM    731  CG  GLN A 100     170.094  29.390  62.099  1.00 40.89           C  
ANISOU  731  CG  GLN A 100     5328   5828   4379   -316    -45   -448       C  
ATOM    732  CD  GLN A 100     171.343  29.710  62.897  1.00 44.19           C  
ANISOU  732  CD  GLN A 100     5729   6259   4802   -338    -56   -496       C  
ATOM    733  OE1 GLN A 100     171.792  28.910  63.721  1.00 43.52           O  
ANISOU  733  OE1 GLN A 100     5626   6191   4718   -335    -97   -499       O  
ATOM    734  NE2 GLN A 100     171.911  30.887  62.660  1.00 47.38           N  
ANISOU  734  NE2 GLN A 100     6140   6654   5210   -361    -21   -534       N  
ATOM    735  N   LEU A 101     168.845  25.709  62.010  1.00 28.51           N  
ANISOU  735  N   LEU A 101     3729   4279   2825   -282   -135   -360       N  
ATOM    736  CA  LEU A 101     169.509  24.587  61.354  1.00 25.17           C  
ANISOU  736  CA  LEU A 101     3282   3855   2427   -288   -163   -370       C  
ATOM    737  C   LEU A 101     168.577  23.940  60.338  1.00 23.82           C  
ANISOU  737  C   LEU A 101     3111   3677   2264   -277   -158   -340       C  
ATOM    738  O   LEU A 101     169.008  23.513  59.270  1.00 26.85           O  
ANISOU  738  O   LEU A 101     3478   4056   2669   -282   -158   -356       O  
ATOM    739  CB  LEU A 101     169.985  23.559  62.381  1.00 24.85           C  
ANISOU  739  CB  LEU A 101     3233   3823   2386   -285   -220   -366       C  
ATOM    740  CG  LEU A 101     170.820  22.396  61.840  1.00 24.58           C  
ANISOU  740  CG  LEU A 101     3174   3783   2384   -286   -261   -384       C  
ATOM    741  CD1 LEU A 101     171.749  22.858  60.724  1.00 21.57           C  
ANISOU  741  CD1 LEU A 101     2768   3399   2028   -301   -232   -430       C  
ATOM    742  CD2 LEU A 101     171.614  21.734  62.965  1.00 25.75           C  
ANISOU  742  CD2 LEU A 101     3320   3932   2533   -283   -321   -393       C  
ATOM    743  N   ILE A 102     167.296  23.864  60.681  1.00 24.52           N  
ANISOU  743  N   ILE A 102     3215   3767   2335   -263   -154   -301       N  
ATOM    744  CA  ILE A 102     166.281  23.421  59.735  1.00 24.45           C  
ANISOU  744  CA  ILE A 102     3205   3751   2332   -252   -146   -276       C  
ATOM    745  C   ILE A 102     166.306  24.308  58.500  1.00 24.76           C  
ANISOU  745  C   ILE A 102     3254   3776   2376   -249   -108   -291       C  
ATOM    746  O   ILE A 102     166.576  23.838  57.395  1.00 26.12           O  
ANISOU  746  O   ILE A 102     3415   3944   2565   -251   -108   -301       O  
ATOM    747  CB  ILE A 102     164.873  23.446  60.357  1.00 24.14           C  
ANISOU  747  CB  ILE A 102     3180   3720   2273   -240   -139   -240       C  
ATOM    748  CG1 ILE A 102     164.780  22.440  61.505  1.00 21.77           C  
ANISOU  748  CG1 ILE A 102     2873   3436   1962   -248   -176   -219       C  
ATOM    749  CG2 ILE A 102     163.826  23.150  59.308  1.00 25.22           C  
ANISOU  749  CG2 ILE A 102     3315   3852   2417   -228   -129   -222       C  
ATOM    750  CD1 ILE A 102     163.463  22.466  62.237  1.00 21.03           C  
ANISOU  750  CD1 ILE A 102     2786   3358   1844   -244   -165   -188       C  
ATOM    751  N   LYS A 103     166.006  25.591  58.696  1.00 23.50           N  
ANISOU  751  N   LYS A 103     3120   3607   2200   -242    -77   -294       N  
ATOM    752  CA  LYS A 103     166.020  26.557  57.604  1.00 22.40           C  
ANISOU  752  CA  LYS A 103     3002   3450   2060   -237    -42   -304       C  
ATOM    753  C   LYS A 103     167.330  26.466  56.816  1.00 19.70           C  
ANISOU  753  C   LYS A 103     2642   3108   1733   -262    -36   -339       C  
ATOM    754  O   LYS A 103     167.331  26.554  55.586  1.00 16.47           O  
ANISOU  754  O   LYS A 103     2240   2691   1328   -261    -18   -342       O  
ATOM    755  CB  LYS A 103     165.835  27.984  58.132  1.00 24.27           C  
ANISOU  755  CB  LYS A 103     3269   3676   2276   -231    -15   -311       C  
ATOM    756  CG  LYS A 103     164.611  28.212  59.020  1.00 26.84           C  
ANISOU  756  CG  LYS A 103     3609   4006   2585   -208    -17   -287       C  
ATOM    757  CD  LYS A 103     164.064  29.632  58.833  1.00 28.15           C  
ANISOU  757  CD  LYS A 103     3813   4152   2730   -188     13   -291       C  
ATOM    758  CE  LYS A 103     163.689  30.298  60.153  1.00 28.35           C  
ANISOU  758  CE  LYS A 103     3849   4187   2737   -182     16   -297       C  
ATOM    759  NZ  LYS A 103     164.877  30.864  60.859  1.00 27.67           N  
ANISOU  759  NZ  LYS A 103     3759   4106   2650   -206     19   -330       N  
ATOM    760  N   ALA A 104     168.438  26.281  57.530  1.00 20.22           N  
ANISOU  760  N   ALA A 104     2686   3188   1809   -284    -51   -367       N  
ATOM    761  CA  ALA A 104     169.755  26.200  56.907  1.00 21.00           C  
ANISOU  761  CA  ALA A 104     2761   3293   1926   -311    -43   -409       C  
ATOM    762  C   ALA A 104     169.868  24.981  56.000  1.00 19.76           C  
ANISOU  762  C   ALA A 104     2578   3142   1787   -308    -63   -410       C  
ATOM    763  O   ALA A 104     170.498  25.040  54.948  1.00 17.81           O  
ANISOU  763  O   ALA A 104     2319   2897   1551   -323    -42   -437       O  
ATOM    764  CB  ALA A 104     170.844  26.169  57.976  1.00 21.87           C  
ANISOU  764  CB  ALA A 104     2849   3417   2044   -328    -63   -442       C  
ATOM    765  N   LYS A 105     169.249  23.879  56.412  1.00 21.52           N  
ANISOU  765  N   LYS A 105     2793   3368   2015   -290   -101   -383       N  
ATOM    766  CA  LYS A 105     169.285  22.642  55.641  1.00 24.48           C  
ANISOU  766  CA  LYS A 105     3144   3747   2410   -286   -127   -386       C  
ATOM    767  C   LYS A 105     168.339  22.685  54.452  1.00 31.86           C  
ANISOU  767  C   LYS A 105     4093   4675   3338   -272   -105   -365       C  
ATOM    768  O   LYS A 105     168.577  22.026  53.439  1.00 34.73           O  
ANISOU  768  O   LYS A 105     4438   5042   3715   -273   -110   -380       O  
ATOM    769  CB  LYS A 105     168.960  21.440  56.529  1.00 20.96           C  
ANISOU  769  CB  LYS A 105     2690   3302   1970   -275   -179   -363       C  
ATOM    770  CG  LYS A 105     170.169  20.899  57.260  1.00 20.80           C  
ANISOU  770  CG  LYS A 105     2650   3285   1969   -282   -219   -393       C  
ATOM    771  CD  LYS A 105     169.814  19.741  58.165  1.00 21.20           C  
ANISOU  771  CD  LYS A 105     2704   3329   2022   -271   -277   -364       C  
ATOM    772  CE  LYS A 105     171.050  19.223  58.881  1.00 22.42           C  
ANISOU  772  CE  LYS A 105     2844   3477   2196   -273   -326   -393       C  
ATOM    773  NZ  LYS A 105     170.716  18.141  59.847  1.00 23.71           N  
ANISOU  773  NZ  LYS A 105     3020   3630   2359   -262   -390   -361       N  
ATOM    774  N   ILE A 106     167.267  23.462  54.570  1.00 34.33           N  
ANISOU  774  N   ILE A 106     4438   4976   3629   -257    -85   -334       N  
ATOM    775  CA  ILE A 106     166.322  23.574  53.465  1.00 34.34           C  
ANISOU  775  CA  ILE A 106     4456   4968   3622   -238    -69   -316       C  
ATOM    776  C   ILE A 106     166.919  24.342  52.287  1.00 32.84           C  
ANISOU  776  C   ILE A 106     4280   4770   3426   -247    -34   -337       C  
ATOM    777  O   ILE A 106     166.585  24.075  51.136  1.00 33.45           O  
ANISOU  777  O   ILE A 106     4362   4846   3501   -237    -29   -334       O  
ATOM    778  CB  ILE A 106     164.996  24.223  53.894  1.00 36.74           C  
ANISOU  778  CB  ILE A 106     4791   5261   3908   -215    -60   -282       C  
ATOM    779  CG1 ILE A 106     164.328  23.393  54.990  1.00 38.25           C  
ANISOU  779  CG1 ILE A 106     4967   5465   4102   -212    -89   -259       C  
ATOM    780  CG2 ILE A 106     164.060  24.349  52.706  1.00 35.73           C  
ANISOU  780  CG2 ILE A 106     4683   5123   3771   -191    -48   -267       C  
ATOM    781  CD1 ILE A 106     162.960  23.910  55.386  1.00 37.91           C  
ANISOU  781  CD1 ILE A 106     4943   5419   4041   -191    -78   -232       C  
ATOM    782  N   ASN A 107     167.801  25.295  52.570  1.00 33.89           N  
ANISOU  782  N   ASN A 107     4421   4901   3554   -268     -9   -360       N  
ATOM    783  CA  ASN A 107     168.457  26.044  51.502  1.00 36.13           C  
ANISOU  783  CA  ASN A 107     4718   5179   3829   -286     29   -382       C  
ATOM    784  C   ASN A 107     169.598  25.232  50.901  1.00 38.11           C  
ANISOU  784  C   ASN A 107     4926   5452   4101   -313     25   -422       C  
ATOM    785  O   ASN A 107     170.056  25.503  49.790  1.00 39.46           O  
ANISOU  785  O   ASN A 107     5102   5626   4267   -328     55   -441       O  
ATOM    786  CB  ASN A 107     168.963  27.393  52.016  1.00 39.01           C  
ANISOU  786  CB  ASN A 107     5108   5534   4181   -305     60   -395       C  
ATOM    787  CG  ASN A 107     167.898  28.157  52.779  1.00 41.91           C  
ANISOU  787  CG  ASN A 107     5512   5883   4529   -275     59   -364       C  
ATOM    788  OD1 ASN A 107     168.112  28.564  53.920  1.00 41.10           O  
ANISOU  788  OD1 ASN A 107     5406   5782   4426   -283     55   -372       O  
ATOM    789  ND2 ASN A 107     166.740  28.352  52.151  1.00 43.49           N  
ANISOU  789  ND2 ASN A 107     5744   6068   4713   -239     62   -332       N  
ATOM    790  N   VAL A 108     170.069  24.249  51.662  1.00 39.34           N  
ANISOU  790  N   VAL A 108     5041   5624   4281   -316    -11   -438       N  
ATOM    791  CA  VAL A 108     171.082  23.320  51.179  1.00 42.49           C  
ANISOU  791  CA  VAL A 108     5394   6044   4707   -331    -23   -481       C  
ATOM    792  C   VAL A 108     170.458  22.247  50.295  1.00 44.70           C  
ANISOU  792  C   VAL A 108     5663   6327   4993   -310    -44   -470       C  
ATOM    793  O   VAL A 108     171.064  21.811  49.313  1.00 46.20           O  
ANISOU  793  O   VAL A 108     5827   6531   5195   -320    -36   -503       O  
ATOM    794  CB  VAL A 108     171.831  22.642  52.343  1.00 42.97           C  
ANISOU  794  CB  VAL A 108     5421   6113   4792   -334    -63   -502       C  
ATOM    795  CG1 VAL A 108     172.751  21.548  51.824  1.00 41.13           C  
ANISOU  795  CG1 VAL A 108     5140   5894   4593   -336    -86   -546       C  
ATOM    796  CG2 VAL A 108     172.616  23.673  53.144  1.00 44.59           C  
ANISOU  796  CG2 VAL A 108     5629   6319   4994   -357    -42   -525       C  
ATOM    797  N   LEU A 109     169.236  21.839  50.628  1.00 44.84           N  
ANISOU  797  N   LEU A 109     5700   6334   5005   -283    -69   -427       N  
ATOM    798  CA  LEU A 109     168.553  20.842  49.816  1.00 44.68           C  
ANISOU  798  CA  LEU A 109     5670   6316   4992   -265    -90   -417       C  
ATOM    799  C   LEU A 109     168.110  21.476  48.519  1.00 48.93           C  
ANISOU  799  C   LEU A 109     6234   6851   5507   -259    -56   -411       C  
ATOM    800  O   LEU A 109     168.551  21.057  47.451  1.00 52.64           O  
ANISOU  800  O   LEU A 109     6686   7334   5982   -264    -49   -438       O  
ATOM    801  CB  LEU A 109     167.376  20.192  50.537  1.00 39.39           C  
ANISOU  801  CB  LEU A 109     5006   5637   4322   -245   -125   -377       C  
ATOM    802  CG  LEU A 109     166.744  19.106  49.663  1.00 35.40           C  
ANISOU  802  CG  LEU A 109     4486   5136   3829   -230   -148   -375       C  
ATOM    803  CD1 LEU A 109     167.810  18.253  48.990  1.00 32.43           C  
ANISOU  803  CD1 LEU A 109     4072   4770   3480   -238   -163   -421       C  
ATOM    804  CD2 LEU A 109     165.781  18.243  50.453  1.00 35.93           C  
ANISOU  804  CD2 LEU A 109     4550   5197   3903   -220   -187   -343       C  
ATOM    805  N   ILE A 110     167.237  22.474  48.585  1.00 52.43           N  
ANISOU  805  N   ILE A 110     6722   7275   5923   -244    -35   -376       N  
ATOM    806  CA  ILE A 110     167.069  23.239  47.378  1.00 56.39           C  
ANISOU  806  CA  ILE A 110     7258   7767   6399   -238     -2   -373       C  
ATOM    807  C   ILE A 110     167.809  24.558  47.546  1.00 64.03           C  
ANISOU  807  C   ILE A 110     8253   8725   7351   -259     37   -382       C  
ATOM    808  O   ILE A 110     167.226  25.591  47.883  1.00 60.32           O  
ANISOU  808  O   ILE A 110     7826   8233   6860   -243     52   -357       O  
ATOM    809  CB  ILE A 110     165.571  23.496  47.162  1.00 54.47           C  
ANISOU  809  CB  ILE A 110     7053   7506   6136   -200     -9   -332       C  
ATOM    810  CG1 ILE A 110     164.995  24.349  48.291  1.00 50.78           C  
ANISOU  810  CG1 ILE A 110     6613   7022   5661   -188     -5   -306       C  
ATOM    811  CG2 ILE A 110     164.816  22.175  47.147  1.00 54.11           C  
ANISOU  811  CG2 ILE A 110     6976   7473   6110   -187    -47   -325       C  
ATOM    812  CD1 ILE A 110     163.659  24.965  47.973  1.00 50.56           C  
ANISOU  812  CD1 ILE A 110     6629   6974   5608   -151     -1   -275       C  
ATOM    813  N   GLY A 111     169.114  24.515  47.293  1.00 74.28           N  
ANISOU  813  N   GLY A 111     9522  10041   8661   -296     55   -425       N  
ATOM    814  CA  GLY A 111     169.872  25.670  46.869  1.00 80.14           C  
ANISOU  814  CA  GLY A 111    10288  10777   9384   -326    103   -441       C  
ATOM    815  C   GLY A 111     170.588  25.398  45.565  1.00 86.53           C  
ANISOU  815  C   GLY A 111    11083  11606  10190   -349    127   -472       C  
ATOM    816  O   GLY A 111     171.003  26.323  44.866  1.00 88.74           O  
ANISOU  816  O   GLY A 111    11394  11880  10445   -372    171   -477       O  
ATOM    817  N   HIS A 112     170.686  24.115  45.222  1.00 84.73           N  
ANISOU  817  N   HIS A 112    10808  11401   9984   -341     98   -493       N  
ATOM    818  CA  HIS A 112     171.766  23.631  44.356  1.00 85.88           C  
ANISOU  818  CA  HIS A 112    10912  11577  10142   -372    116   -545       C  
ATOM    819  C   HIS A 112     171.890  24.335  43.012  1.00 89.06           C  
ANISOU  819  C   HIS A 112    11351  11980  10508   -387    163   -544       C  
ATOM    820  O   HIS A 112     172.978  24.761  42.634  1.00 92.26           O  
ANISOU  820  O   HIS A 112    11741  12400  10911   -433    203   -583       O  
ATOM    821  CB  HIS A 112     171.695  22.107  44.183  1.00 86.72           C  
ANISOU  821  CB  HIS A 112    10966  11705  10278   -351     73   -566       C  
ATOM    822  CG  HIS A 112     172.145  21.344  45.393  1.00 90.27           C  
ANISOU  822  CG  HIS A 112    11370  12161  10769   -348     34   -586       C  
ATOM    823  ND1 HIS A 112     173.477  21.202  45.727  1.00 91.88           N  
ANISOU  823  ND1 HIS A 112    11525  12385  11002   -375     41   -641       N  
ATOM    824  CD2 HIS A 112     171.447  20.695  46.354  1.00 90.74           C  
ANISOU  824  CD2 HIS A 112    11429  12206  10843   -321    -13   -557       C  
ATOM    825  CE1 HIS A 112     173.575  20.495  46.841  1.00 91.38           C  
ANISOU  825  CE1 HIS A 112    11437  12314  10967   -358     -5   -642       C  
ATOM    826  NE2 HIS A 112     172.358  20.174  47.239  1.00 90.59           N  
ANISOU  826  NE2 HIS A 112    11369  12194  10857   -328    -38   -590       N  
TER     827      HIS A 112                                                      
ATOM    828  N   ARG B   4     164.299   3.927  33.688  1.00 42.85           N  
ANISOU  828  N   ARG B   4     6580   4891   4809    542    783   -500       N  
ATOM    829  CA  ARG B   4     163.361   4.601  34.581  1.00 41.40           C  
ANISOU  829  CA  ARG B   4     6336   4789   4605    483    650   -450       C  
ATOM    830  C   ARG B   4     163.779   6.048  34.850  1.00 42.02           C  
ANISOU  830  C   ARG B   4     6273   5024   4670    494    560   -408       C  
ATOM    831  O   ARG B   4     164.935   6.319  35.180  1.00 41.98           O  
ANISOU  831  O   ARG B   4     6172   5063   4714    600    579   -364       O  
ATOM    832  CB  ARG B   4     163.227   3.829  35.896  1.00 40.15           C  
ANISOU  832  CB  ARG B   4     6178   4567   4511    556    645   -372       C  
ATOM    833  N   TYR B   5     162.827   6.969  34.708  1.00 40.87           N  
ANISOU  833  N   TYR B   5     6110   4957   4462    384    464   -423       N  
ATOM    834  CA  TYR B   5     163.079   8.404  34.877  1.00 38.26           C  
ANISOU  834  CA  TYR B   5     5665   4763   4110    377    385   -392       C  
ATOM    835  C   TYR B   5     163.106   8.856  36.338  1.00 38.81           C  
ANISOU  835  C   TYR B   5     5637   4893   4218    428    309   -305       C  
ATOM    836  O   TYR B   5     162.314   8.392  37.160  1.00 38.14           O  
ANISOU  836  O   TYR B   5     5580   4767   4145    413    281   -275       O  
ATOM    837  CB  TYR B   5     162.034   9.224  34.099  1.00 34.08           C  
ANISOU  837  CB  TYR B   5     5162   4285   3500    247    315   -436       C  
ATOM    838  CG  TYR B   5     161.835  10.648  34.587  1.00 26.95           C  
ANISOU  838  CG  TYR B   5     4156   3503   2583    226    219   -392       C  
ATOM    839  CD1 TYR B   5     162.548  11.704  34.031  1.00 24.67           C  
ANISOU  839  CD1 TYR B   5     3816   3293   2264    229    218   -398       C  
ATOM    840  CD2 TYR B   5     160.918  10.937  35.591  1.00 21.65           C  
ANISOU  840  CD2 TYR B   5     3446   2854   1926    199    144   -347       C  
ATOM    841  CE1 TYR B   5     162.362  13.004  34.470  1.00 20.45           C  
ANISOU  841  CE1 TYR B   5     3200   2854   1717    207    141   -361       C  
ATOM    842  CE2 TYR B   5     160.727  12.233  36.035  1.00 18.53           C  
ANISOU  842  CE2 TYR B   5     2968   2555   1518    181     71   -311       C  
ATOM    843  CZ  TYR B   5     161.453  13.262  35.473  1.00 17.89           C  
ANISOU  843  CZ  TYR B   5     2842   2547   1407    185     68   -318       C  
ATOM    844  OH  TYR B   5     161.263  14.554  35.916  1.00 18.77           O  
ANISOU  844  OH  TYR B   5     2882   2742   1508    165      5   -285       O  
ATOM    845  N   VAL B   6     164.012   9.783  36.646  1.00 39.95           N  
ANISOU  845  N   VAL B   6     5673   5133   4374    477    281   -270       N  
ATOM    846  CA  VAL B   6     164.070  10.410  37.966  1.00 39.77           C  
ANISOU  846  CA  VAL B   6     5563   5181   4366    508    200   -197       C  
ATOM    847  C   VAL B   6     163.991  11.934  37.829  1.00 37.09           C  
ANISOU  847  C   VAL B   6     5152   4954   3985    446    136   -202       C  
ATOM    848  O   VAL B   6     164.601  12.511  36.928  1.00 35.86           O  
ANISOU  848  O   VAL B   6     4972   4839   3814    435    164   -237       O  
ATOM    849  CB  VAL B   6     165.369  10.027  38.713  1.00 40.07           C  
ANISOU  849  CB  VAL B   6     5529   5228   4469    635    217   -138       C  
ATOM    850  CG1 VAL B   6     165.599  10.940  39.914  1.00 40.39           C  
ANISOU  850  CG1 VAL B   6     5476   5367   4503    648    122    -74       C  
ATOM    851  CG2 VAL B   6     165.333   8.571  39.140  1.00 38.52           C  
ANISOU  851  CG2 VAL B   6     5407   4914   4316    706    268   -110       C  
ATOM    852  N   PRO B   7     163.241  12.593  38.728  1.00 35.65           N  
ANISOU  852  N   PRO B   7     4946   4816   3785    407     61   -166       N  
ATOM    853  CA  PRO B   7     163.078  14.049  38.679  1.00 36.48           C  
ANISOU  853  CA  PRO B   7     4994   5012   3853    350      7   -167       C  
ATOM    854  C   PRO B   7     164.385  14.773  38.979  1.00 40.62           C  
ANISOU  854  C   PRO B   7     5423   5617   4395    399     -1   -145       C  
ATOM    855  O   PRO B   7     165.089  14.406  39.921  1.00 42.73           O  
ANISOU  855  O   PRO B   7     5646   5893   4696    471    -16    -99       O  
ATOM    856  CB  PRO B   7     162.062  14.322  39.793  1.00 33.47           C  
ANISOU  856  CB  PRO B   7     4616   4636   3465    317    -49   -129       C  
ATOM    857  CG  PRO B   7     161.336  13.034  39.969  1.00 32.48           C  
ANISOU  857  CG  PRO B   7     4567   4414   3359    319    -20   -129       C  
ATOM    858  CD  PRO B   7     162.366  11.980  39.739  1.00 33.34           C  
ANISOU  858  CD  PRO B   7     4696   4472   3501    403     39   -129       C  
ATOM    859  N   ASP B   8     164.697  15.799  38.193  1.00 41.52           N  
ANISOU  859  N   ASP B   8     5506   5786   4483    357      4   -175       N  
ATOM    860  CA  ASP B   8     165.919  16.562  38.402  1.00 46.21           C  
ANISOU  860  CA  ASP B   8     6004   6458   5097    385      2   -163       C  
ATOM    861  C   ASP B   8     165.587  18.025  38.682  1.00 44.80           C  
ANISOU  861  C   ASP B   8     5794   6347   4879    316    -51   -157       C  
ATOM    862  O   ASP B   8     164.485  18.486  38.388  1.00 45.55           O  
ANISOU  862  O   ASP B   8     5943   6430   4936    254    -71   -169       O  
ATOM    863  CB  ASP B   8     166.840  16.449  37.184  1.00 51.03           C  
ANISOU  863  CB  ASP B   8     6604   7063   5722    401     85   -206       C  
ATOM    864  CG  ASP B   8     168.283  16.782  37.513  1.00 53.79           C  
ANISOU  864  CG  ASP B   8     6834   7478   6128    454     98   -189       C  
ATOM    865  OD1 ASP B   8     168.526  17.384  38.581  1.00 53.88           O  
ANISOU  865  OD1 ASP B   8     6774   7553   6146    455     26   -149       O  
ATOM    866  OD2 ASP B   8     169.174  16.445  36.703  1.00 54.70           O  
ANISOU  866  OD2 ASP B   8     6926   7579   6279    490    182   -216       O  
ATOM    867  N   MET B   9     166.542  18.746  39.261  1.00 41.66           N  
ANISOU  867  N   MET B   9     5309   6021   4499    328    -73   -139       N  
ATOM    868  CA  MET B   9     166.338  20.152  39.588  1.00 37.08           C  
ANISOU  868  CA  MET B   9     4705   5498   3884    261   -111   -138       C  
ATOM    869  C   MET B   9     165.906  20.930  38.350  1.00 35.44           C  
ANISOU  869  C   MET B   9     4543   5284   3640    199    -76   -175       C  
ATOM    870  O   MET B   9     166.558  20.867  37.306  1.00 37.89           O  
ANISOU  870  O   MET B   9     4852   5593   3954    202    -17   -206       O  
ATOM    871  CB  MET B   9     167.617  20.762  40.166  1.00 35.82           C  
ANISOU  871  CB  MET B   9     4444   5417   3751    271   -130   -126       C  
ATOM    872  CG  MET B   9     167.548  22.270  40.382  1.00 34.61           C  
ANISOU  872  CG  MET B   9     4275   5314   3563    193   -153   -136       C  
ATOM    873  SD  MET B   9     167.113  22.736  42.068  1.00131.25           S  
ANISOU  873  SD  MET B   9    16519  17578  15772    170   -234    -99       S  
ATOM    874  CE  MET B   9     168.498  22.045  42.971  1.00 49.93           C  
ANISOU  874  CE  MET B   9     6121   7338   5513    236   -283    -67       C  
ATOM    875  N   GLY B  10     164.802  21.660  38.470  1.00 32.25           N  
ANISOU  875  N   GLY B  10     4181   4854   3220    142   -108   -164       N  
ATOM    876  CA  GLY B  10     164.302  22.473  37.377  1.00 30.04           C  
ANISOU  876  CA  GLY B  10     3946   4524   2944     83    -87   -175       C  
ATOM    877  C   GLY B  10     163.238  21.785  36.543  1.00 27.33           C  
ANISOU  877  C   GLY B  10     3681   4115   2590     67    -90   -184       C  
ATOM    878  O   GLY B  10     162.477  22.441  35.829  1.00 23.62           O  
ANISOU  878  O   GLY B  10     3254   3598   2123     24   -101   -176       O  
ATOM    879  N   ASP B  11     163.188  20.459  36.630  1.00 27.99           N  
ANISOU  879  N   ASP B  11     3783   4199   2651    110    -83   -201       N  
ATOM    880  CA  ASP B  11     162.206  19.679  35.883  1.00 28.37           C  
ANISOU  880  CA  ASP B  11     3906   4192   2679     85    -87   -220       C  
ATOM    881  C   ASP B  11     160.770  20.028  36.261  1.00 29.36           C  
ANISOU  881  C   ASP B  11     4044   4276   2836     39   -141   -190       C  
ATOM    882  O   ASP B  11     160.462  20.272  37.424  1.00 32.15           O  
ANISOU  882  O   ASP B  11     4360   4634   3223     48   -162   -159       O  
ATOM    883  CB  ASP B  11     162.441  18.176  36.074  1.00 31.92           C  
ANISOU  883  CB  ASP B  11     4382   4616   3130    142    -57   -240       C  
ATOM    884  CG  ASP B  11     163.503  17.625  35.138  1.00 38.17           C  
ANISOU  884  CG  ASP B  11     5194   5389   3920    172     19   -278       C  
ATOM    885  OD1 ASP B  11     163.858  18.321  34.163  1.00 39.75           O  
ANISOU  885  OD1 ASP B  11     5410   5613   4079    140     47   -303       O  
ATOM    886  OD2 ASP B  11     163.973  16.489  35.372  1.00 42.18           O  
ANISOU  886  OD2 ASP B  11     5708   5851   4468    229     61   -281       O  
ATOM    887  N   LEU B  12     159.902  20.057  35.256  1.00 30.40           N  
ANISOU  887  N   LEU B  12     4230   4371   2950     -4   -163   -201       N  
ATOM    888  CA  LEU B  12     158.470  20.242  35.451  1.00 30.80           C  
ANISOU  888  CA  LEU B  12     4281   4398   3023    -30   -217   -181       C  
ATOM    889  C   LEU B  12     157.783  18.904  35.220  1.00 28.83           C  
ANISOU  889  C   LEU B  12     4073   4138   2744    -44   -231   -216       C  
ATOM    890  O   LEU B  12     157.860  18.339  34.126  1.00 27.15           O  
ANISOU  890  O   LEU B  12     3911   3915   2490    -53   -224   -258       O  
ATOM    891  CB  LEU B  12     157.926  21.282  34.468  1.00 32.03           C  
ANISOU  891  CB  LEU B  12     4452   4540   3179    -44   -250   -170       C  
ATOM    892  CG  LEU B  12     156.439  21.632  34.552  1.00 30.06           C  
ANISOU  892  CG  LEU B  12     4174   4294   2955    -60   -309   -151       C  
ATOM    893  CD1 LEU B  12     156.190  22.619  35.678  1.00 26.40           C  
ANISOU  893  CD1 LEU B  12     3656   3838   2537    -54   -304   -112       C  
ATOM    894  CD2 LEU B  12     155.950  22.200  33.230  1.00 32.53           C  
ANISOU  894  CD2 LEU B  12     4505   4611   3243    -66   -348   -153       C  
ATOM    895  N   ILE B  13     157.110  18.398  36.247  1.00 29.27           N  
ANISOU  895  N   ILE B  13     4104   4201   2816    -45   -243   -207       N  
ATOM    896  CA  ILE B  13     156.568  17.048  36.194  1.00 30.84           C  
ANISOU  896  CA  ILE B  13     4346   4351   3019    -67   -235   -235       C  
ATOM    897  C   ILE B  13     155.056  17.008  36.382  1.00 31.68           C  
ANISOU  897  C   ILE B  13     4430   4444   3164   -124   -282   -225       C  
ATOM    898  O   ILE B  13     154.459  17.950  36.902  1.00 30.92           O  
ANISOU  898  O   ILE B  13     4275   4380   3094   -128   -309   -189       O  
ATOM    899  CB  ILE B  13     157.222  16.150  37.258  1.00 28.82           C  
ANISOU  899  CB  ILE B  13     4094   4057   2799     -8   -182   -221       C  
ATOM    900  CG1 ILE B  13     156.675  16.481  38.647  1.00 26.22           C  
ANISOU  900  CG1 ILE B  13     3720   3733   2510      2   -192   -174       C  
ATOM    901  CG2 ILE B  13     158.732  16.303  37.225  1.00 29.68           C  
ANISOU  901  CG2 ILE B  13     4192   4192   2892     56   -143   -220       C  
ATOM    902  CD1 ILE B  13     157.319  15.679  39.761  1.00 26.10           C  
ANISOU  902  CD1 ILE B  13     3718   3684   2514     62   -152   -147       C  
ATOM    903  N   TRP B  14     154.446  15.912  35.940  1.00 34.03           N  
ANISOU  903  N   TRP B  14     4772   4689   3467   -170   -285   -260       N  
ATOM    904  CA  TRP B  14     153.019  15.694  36.129  1.00 35.24           C  
ANISOU  904  CA  TRP B  14     4892   4825   3671   -232   -324   -256       C  
ATOM    905  C   TRP B  14     152.808  14.716  37.279  1.00 38.02           C  
ANISOU  905  C   TRP B  14     5252   5114   4080   -221   -267   -246       C  
ATOM    906  O   TRP B  14     153.327  13.600  37.251  1.00 39.80           O  
ANISOU  906  O   TRP B  14     5546   5279   4297   -207   -217   -272       O  
ATOM    907  CB  TRP B  14     152.381  15.152  34.851  1.00 31.04           C  
ANISOU  907  CB  TRP B  14     4407   4281   3107   -313   -375   -305       C  
ATOM    908  CG  TRP B  14     150.890  15.196  34.872  1.00 29.66           C  
ANISOU  908  CG  TRP B  14     4168   4112   2988   -384   -439   -297       C  
ATOM    909  CD1 TRP B  14     150.042  14.173  35.178  1.00 30.13           C  
ANISOU  909  CD1 TRP B  14     4227   4117   3103   -443   -428   -319       C  
ATOM    910  CD2 TRP B  14     150.064  16.331  34.583  1.00 30.76           C  
ANISOU  910  CD2 TRP B  14     4227   4314   3146   -402   -520   -262       C  
ATOM    911  NE1 TRP B  14     148.737  14.600  35.095  1.00 31.86           N  
ANISOU  911  NE1 TRP B  14     4356   4368   3379   -501   -500   -302       N  
ATOM    912  CE2 TRP B  14     148.725  15.920  34.729  1.00 31.31           C  
ANISOU  912  CE2 TRP B  14     4234   4371   3290   -470   -560   -264       C  
ATOM    913  CE3 TRP B  14     150.327  17.654  34.216  1.00 31.20           C  
ANISOU  913  CE3 TRP B  14     4257   4431   3168   -366   -559   -226       C  
ATOM    914  CZ2 TRP B  14     147.655  16.785  34.519  1.00 30.71           C  
ANISOU  914  CZ2 TRP B  14     4059   4346   3263   -493   -642   -227       C  
ATOM    915  CZ3 TRP B  14     149.262  18.509  34.008  1.00 30.95           C  
ANISOU  915  CZ3 TRP B  14     4142   4440   3177   -385   -637   -187       C  
ATOM    916  CH2 TRP B  14     147.944  18.071  34.157  1.00 30.91           C  
ANISOU  916  CH2 TRP B  14     4064   4427   3254   -444   -680   -186       C  
ATOM    917  N   VAL B  15     152.054  15.141  38.289  1.00 35.03           N  
ANISOU  917  N   VAL B  15     4811   4741   3758   -222   -264   -206       N  
ATOM    918  CA  VAL B  15     151.849  14.333  39.486  1.00 31.23           C  
ANISOU  918  CA  VAL B  15     4346   4199   3321   -211   -201   -188       C  
ATOM    919  C   VAL B  15     150.461  14.547  40.081  1.00 28.22           C  
ANISOU  919  C   VAL B  15     3900   3809   3013   -262   -202   -169       C  
ATOM    920  O   VAL B  15     149.901  15.636  39.988  1.00 27.50           O  
ANISOU  920  O   VAL B  15     3735   3771   2945   -271   -241   -149       O  
ATOM    921  CB  VAL B  15     152.923  14.648  40.552  1.00 32.67           C  
ANISOU  921  CB  VAL B  15     4540   4394   3481   -127   -161   -147       C  
ATOM    922  CG1 VAL B  15     152.983  16.144  40.816  1.00 32.72           C  
ANISOU  922  CG1 VAL B  15     4483   4472   3478   -109   -189   -119       C  
ATOM    923  CG2 VAL B  15     152.656  13.877  41.835  1.00 33.63           C  
ANISOU  923  CG2 VAL B  15     4692   4452   3634   -115   -101   -118       C  
ATOM    924  N   ASP B  16     149.908  13.501  40.685  1.00 28.35           N  
ANISOU  924  N   ASP B  16     3943   3753   3074   -294   -150   -173       N  
ATOM    925  CA  ASP B  16     148.621  13.598  41.362  1.00 29.15           C  
ANISOU  925  CA  ASP B  16     3981   3838   3257   -343   -127   -155       C  
ATOM    926  C   ASP B  16     148.852  13.897  42.839  1.00 27.50           C  
ANISOU  926  C   ASP B  16     3785   3613   3051   -290    -54   -106       C  
ATOM    927  O   ASP B  16     149.386  13.065  43.571  1.00 28.83           O  
ANISOU  927  O   ASP B  16     4034   3723   3196   -260      3    -93       O  
ATOM    928  CB  ASP B  16     147.828  12.297  41.186  1.00 31.07           C  
ANISOU  928  CB  ASP B  16     4251   4005   3548   -425   -101   -191       C  
ATOM    929  CG  ASP B  16     146.505  12.303  41.937  1.00 30.33           C  
ANISOU  929  CG  ASP B  16     4084   3887   3552   -481    -59   -174       C  
ATOM    930  OD1 ASP B  16     146.083  13.381  42.408  1.00 29.88           O  
ANISOU  930  OD1 ASP B  16     3945   3876   3530   -460    -59   -139       O  
ATOM    931  OD2 ASP B  16     145.881  11.224  42.045  1.00 31.17           O  
ANISOU  931  OD2 ASP B  16     4216   3923   3706   -550    -16   -199       O  
ATOM    932  N   PHE B  17     148.447  15.088  43.271  1.00 25.88           N  
ANISOU  932  N   PHE B  17     3511   3454   2870   -278    -57    -78       N  
ATOM    933  CA  PHE B  17     148.696  15.538  44.639  1.00 23.90           C  
ANISOU  933  CA  PHE B  17     3283   3193   2604   -234      9    -38       C  
ATOM    934  C   PHE B  17     147.690  14.976  45.640  1.00 21.22           C  
ANISOU  934  C   PHE B  17     2949   2786   2328   -275     97    -23       C  
ATOM    935  O   PHE B  17     147.913  15.032  46.850  1.00 19.06           O  
ANISOU  935  O   PHE B  17     2731   2485   2026   -247    165      8       O  
ATOM    936  CB  PHE B  17     148.710  17.072  44.705  1.00 25.71           C  
ANISOU  936  CB  PHE B  17     3452   3486   2829   -207    -12    -19       C  
ATOM    937  CG  PHE B  17     150.004  17.692  44.247  1.00 25.89           C  
ANISOU  937  CG  PHE B  17     3500   3565   2770   -156    -64    -22       C  
ATOM    938  CD1 PHE B  17     151.070  17.831  45.123  1.00 23.29           C  
ANISOU  938  CD1 PHE B  17     3230   3244   2375   -106    -41     -2       C  
ATOM    939  CD2 PHE B  17     150.156  18.140  42.944  1.00 26.99           C  
ANISOU  939  CD2 PHE B  17     3604   3751   2898   -162   -137    -42       C  
ATOM    940  CE1 PHE B  17     152.264  18.403  44.708  1.00 22.34           C  
ANISOU  940  CE1 PHE B  17     3117   3178   2193    -67    -85     -7       C  
ATOM    941  CE2 PHE B  17     151.348  18.714  42.523  1.00 26.16           C  
ANISOU  941  CE2 PHE B  17     3521   3693   2724   -121   -169    -46       C  
ATOM    942  CZ  PHE B  17     152.402  18.846  43.407  1.00 24.85           C  
ANISOU  942  CZ  PHE B  17     3398   3536   2508    -75   -141    -30       C  
ATOM    943  N   ASP B  18     146.588  14.437  45.130  1.00 20.42           N  
ANISOU  943  N   ASP B  18     2792   2657   2309   -348     97    -48       N  
ATOM    944  CA  ASP B  18     145.572  13.839  45.984  1.00 20.60           C  
ANISOU  944  CA  ASP B  18     2810   2611   2406   -400    191    -39       C  
ATOM    945  C   ASP B  18     146.138  12.678  46.796  1.00 27.77           C  
ANISOU  945  C   ASP B  18     3849   3438   3264   -385    263    -26       C  
ATOM    946  O   ASP B  18     147.112  12.048  46.391  1.00 28.75           O  
ANISOU  946  O   ASP B  18     4049   3551   3323   -351    228    -35       O  
ATOM    947  CB  ASP B  18     144.382  13.353  45.156  1.00 16.22           C  
ANISOU  947  CB  ASP B  18     2165   2045   1951   -492    163    -75       C  
ATOM    948  CG  ASP B  18     143.567  14.492  44.579  1.00 16.28           C  
ANISOU  948  CG  ASP B  18     2030   2124   2031   -504    102    -71       C  
ATOM    949  OD1 ASP B  18     143.534  15.572  45.205  1.00 15.91           O  
ANISOU  949  OD1 ASP B  18     1950   2103   1993   -455    136    -37       O  
ATOM    950  OD2 ASP B  18     142.960  14.308  43.499  1.00 17.76           O  
ANISOU  950  OD2 ASP B  18     2144   2340   2265   -564     18   -100       O  
ATOM    951  N   PRO B  19     145.521  12.397  47.956  1.00 32.27           N  
ANISOU  951  N   PRO B  19     4451   3945   3866   -408    371     -1       N  
ATOM    952  CA  PRO B  19     144.439  13.224  48.506  1.00 35.35           C  
ANISOU  952  CA  PRO B  19     4751   4344   4336   -438    431     11       C  
ATOM    953  C   PRO B  19     144.990  14.479  49.188  1.00 39.01           C  
ANISOU  953  C   PRO B  19     5228   4857   4738   -370    438     41       C  
ATOM    954  O   PRO B  19     146.096  14.455  49.729  1.00 40.85           O  
ANISOU  954  O   PRO B  19     5565   5092   4863   -313    430     63       O  
ATOM    955  CB  PRO B  19     143.787  12.303  49.550  1.00 35.70           C  
ANISOU  955  CB  PRO B  19     4861   4289   4415   -486    563     25       C  
ATOM    956  CG  PRO B  19     144.315  10.916  49.245  1.00 35.34           C  
ANISOU  956  CG  PRO B  19     4916   4180   4330   -497    553     13       C  
ATOM    957  CD  PRO B  19     145.678  11.140  48.705  1.00 31.61           C  
ANISOU  957  CD  PRO B  19     4490   3764   3758   -416    453     16       C  
ATOM    958  N   THR B  20     144.216  15.560  49.177  1.00 42.53           N  
ANISOU  958  N   THR B  20     5569   5337   5256   -378    453     42       N  
ATOM    959  CA  THR B  20     144.638  16.815  49.802  1.00 45.57           C  
ANISOU  959  CA  THR B  20     5970   5756   5589   -325    472     63       C  
ATOM    960  C   THR B  20     143.478  17.528  50.501  1.00 50.42           C  
ANISOU  960  C   THR B  20     6517   6343   6298   -346    582     73       C  
ATOM    961  O   THR B  20     142.356  17.554  49.994  1.00 53.05           O  
ANISOU  961  O   THR B  20     6722   6674   6760   -387    590     64       O  
ATOM    962  CB  THR B  20     145.312  17.759  48.782  1.00 40.83           C  
ANISOU  962  CB  THR B  20     5318   5240   4956   -282    354     54       C  
ATOM    963  OG1 THR B  20     146.724  17.804  49.029  1.00 37.90           O  
ANISOU  963  OG1 THR B  20     5048   4893   4457   -231    314     61       O  
ATOM    964  CG2 THR B  20     144.739  19.167  48.894  1.00 40.69           C  
ANISOU  964  CG2 THR B  20     5219   5248   4993   -266    381     64       C  
ATOM    965  N   LYS B  21     143.757  18.091  51.675  1.00 52.16           N  
ANISOU  965  N   LYS B  21     6825   6541   6454   -322    669     92       N  
ATOM    966  CA  LYS B  21     142.731  18.760  52.468  1.00 54.14           C  
ANISOU  966  CA  LYS B  21     7036   6750   6783   -338    803     99       C  
ATOM    967  C   LYS B  21     142.975  20.265  52.540  1.00 50.93           C  
ANISOU  967  C   LYS B  21     6610   6383   6358   -291    800    101       C  
ATOM    968  O   LYS B  21     144.121  20.716  52.546  1.00 50.00           O  
ANISOU  968  O   LYS B  21     6570   6307   6122   -254    731    100       O  
ATOM    969  CB  LYS B  21     142.690  18.182  53.886  1.00 57.53           C  
ANISOU  969  CB  LYS B  21     7607   7103   7151   -361    939    114       C  
ATOM    970  CG  LYS B  21     141.284  17.862  54.417  1.00 60.76           C  
ANISOU  970  CG  LYS B  21     7958   7437   7690   -418   1092    114       C  
ATOM    971  CD  LYS B  21     140.325  19.058  54.296  1.00 60.03           C  
ANISOU  971  CD  LYS B  21     7724   7355   7728   -408   1152    108       C  
ATOM    972  CE  LYS B  21     139.455  18.938  53.036  1.00 55.74           C  
ANISOU  972  CE  LYS B  21     6981   6851   7348   -430   1071     98       C  
ATOM    973  NZ  LYS B  21     138.582  20.117  52.841  1.00 57.24           N  
ANISOU  973  NZ  LYS B  21     7022   7055   7671   -403   1111    105       N  
ATOM    974  N   GLY B  22     141.894  21.037  52.592  1.00 49.94           N  
ANISOU  974  N   GLY B  22     6378   6239   6358   -293    879    103       N  
ATOM    975  CA  GLY B  22     141.986  22.473  52.780  1.00 48.78           C  
ANISOU  975  CA  GLY B  22     6223   6105   6206   -250    909    106       C  
ATOM    976  C   GLY B  22     142.304  23.268  51.532  1.00 46.82           C  
ANISOU  976  C   GLY B  22     5884   5928   5978   -209    775    107       C  
ATOM    977  O   GLY B  22     141.870  22.927  50.433  1.00 47.95           O  
ANISOU  977  O   GLY B  22     5910   6106   6203   -217    680    110       O  
ATOM    978  N   SER B  23     143.068  24.341  51.714  1.00 44.09           N  
ANISOU  978  N   SER B  23     5603   5600   5549   -172    767    105       N  
ATOM    979  CA  SER B  23     143.415  25.248  50.624  1.00 41.14           C  
ANISOU  979  CA  SER B  23     5165   5282   5184   -133    660    111       C  
ATOM    980  C   SER B  23     144.597  24.712  49.825  1.00 38.04           C  
ANISOU  980  C   SER B  23     4815   4953   4685   -132    515    100       C  
ATOM    981  O   SER B  23     145.027  25.323  48.843  1.00 38.83           O  
ANISOU  981  O   SER B  23     4879   5101   4772   -107    420    103       O  
ATOM    982  CB  SER B  23     143.772  26.626  51.189  1.00 42.85           C  
ANISOU  982  CB  SER B  23     5445   5479   5357   -103    728    107       C  
ATOM    983  OG  SER B  23     142.762  27.081  52.087  1.00 44.71           O  
ANISOU  983  OG  SER B  23     5666   5642   5679   -102    890    111       O  
ATOM    984  N   GLU B  24     145.118  23.567  50.252  1.00 35.27           N  
ANISOU  984  N   GLU B  24     4547   4596   4259   -158    508     91       N  
ATOM    985  CA  GLU B  24     146.238  22.926  49.578  1.00 31.94           C  
ANISOU  985  CA  GLU B  24     4165   4223   3746   -153    390     82       C  
ATOM    986  C   GLU B  24     145.836  22.511  48.170  1.00 29.06           C  
ANISOU  986  C   GLU B  24     3698   3891   3451   -161    291     78       C  
ATOM    987  O   GLU B  24     144.702  22.090  47.940  1.00 26.10           O  
ANISOU  987  O   GLU B  24     3238   3494   3185   -190    310     81       O  
ATOM    988  CB  GLU B  24     146.692  21.700  50.369  1.00 32.06           C  
ANISOU  988  CB  GLU B  24     4283   4208   3690   -170    416     82       C  
ATOM    989  CG  GLU B  24     146.892  21.953  51.851  1.00 33.21           C  
ANISOU  989  CG  GLU B  24     4541   4314   3762   -174    517     90       C  
ATOM    990  CD  GLU B  24     147.257  20.688  52.610  1.00 34.43           C  
ANISOU  990  CD  GLU B  24     4801   4433   3847   -187    538    103       C  
ATOM    991  OE1 GLU B  24     146.792  20.521  53.760  1.00 31.15           O  
ANISOU  991  OE1 GLU B  24     4460   3959   3415   -209    650    114       O  
ATOM    992  OE2 GLU B  24     148.013  19.862  52.052  1.00 35.98           O  
ANISOU  992  OE2 GLU B  24     5012   4655   4005   -172    450    105       O  
ATOM    993  N   GLN B  25     146.764  22.643  47.227  1.00 29.15           N  
ANISOU  993  N   GLN B  25     3720   3956   3398   -142    187     69       N  
ATOM    994  CA  GLN B  25     146.507  22.250  45.846  1.00 30.90           C  
ANISOU  994  CA  GLN B  25     3872   4212   3657   -156     87     61       C  
ATOM    995  C   GLN B  25     146.234  20.752  45.735  1.00 34.01           C  
ANISOU  995  C   GLN B  25     4277   4577   4067   -198     80     44       C  
ATOM    996  O   GLN B  25     146.989  19.931  46.263  1.00 35.95           O  
ANISOU  996  O   GLN B  25     4614   4801   4243   -195    101     37       O  
ATOM    997  CB  GLN B  25     147.675  22.644  44.938  1.00 27.03           C  
ANISOU  997  CB  GLN B  25     3415   3776   3078   -130     -1     51       C  
ATOM    998  CG  GLN B  25     147.813  24.138  44.726  1.00 25.23           C  
ANISOU  998  CG  GLN B  25     3166   3572   2847    -98     -6     68       C  
ATOM    999  CD  GLN B  25     146.570  24.752  44.109  1.00 25.10           C  
ANISOU  999  CD  GLN B  25     3042   3555   2938    -95    -24     92       C  
ATOM   1000  OE1 GLN B  25     145.894  24.128  43.288  1.00 25.19           O  
ANISOU 1000  OE1 GLN B  25     2991   3580   3001   -121    -89     92       O  
ATOM   1001  NE2 GLN B  25     146.260  25.983  44.505  1.00 24.22           N  
ANISOU 1001  NE2 GLN B  25     2912   3428   2865    -64     30    115       N  
ATOM   1002  N   ALA B  26     145.151  20.406  45.045  1.00 34.38           N  
ANISOU 1002  N   ALA B  26     4231   4622   4210   -238     49     40       N  
ATOM   1003  CA  ALA B  26     144.755  19.014  44.884  1.00 33.20           C  
ANISOU 1003  CA  ALA B  26     4088   4438   4089   -294     47     17       C  
ATOM   1004  C   ALA B  26     144.715  18.612  43.414  1.00 32.61           C  
ANISOU 1004  C   ALA B  26     3979   4402   4009   -326    -71     -8       C  
ATOM   1005  O   ALA B  26     144.982  19.425  42.530  1.00 32.15           O  
ANISOU 1005  O   ALA B  26     3895   4398   3923   -302   -152     -1       O  
ATOM   1006  CB  ALA B  26     143.394  18.780  45.529  1.00 33.55           C  
ANISOU 1006  CB  ALA B  26     4053   4436   4257   -338    131     26       C  
ATOM   1007  N   GLY B  27     144.391  17.348  43.165  1.00 34.48           N  
ANISOU 1007  N   GLY B  27     4231   4603   4265   -387    -76    -37       N  
ATOM   1008  CA  GLY B  27     144.246  16.841  41.813  1.00 36.32           C  
ANISOU 1008  CA  GLY B  27     4448   4863   4490   -437   -181    -70       C  
ATOM   1009  C   GLY B  27     145.540  16.796  41.024  1.00 37.35           C  
ANISOU 1009  C   GLY B  27     4671   5021   4498   -402   -239    -90       C  
ATOM   1010  O   GLY B  27     146.608  17.130  41.538  1.00 37.96           O  
ANISOU 1010  O   GLY B  27     4816   5101   4506   -338   -202    -76       O  
ATOM   1011  N   HIS B  28     145.437  16.376  39.767  1.00 38.59           N  
ANISOU 1011  N   HIS B  28     4832   5199   4631   -451   -328   -124       N  
ATOM   1012  CA  HIS B  28     146.585  16.325  38.871  1.00 39.12           C  
ANISOU 1012  CA  HIS B  28     4987   5289   4587   -426   -374   -148       C  
ATOM   1013  C   HIS B  28     146.989  17.726  38.429  1.00 36.62           C  
ANISOU 1013  C   HIS B  28     4643   5039   4231   -372   -424   -117       C  
ATOM   1014  O   HIS B  28     146.138  18.586  38.213  1.00 38.24           O  
ANISOU 1014  O   HIS B  28     4758   5280   4493   -377   -471    -87       O  
ATOM   1015  CB  HIS B  28     146.271  15.464  37.646  1.00 43.39           C  
ANISOU 1015  CB  HIS B  28     5556   5826   5104   -507   -447   -200       C  
ATOM   1016  CG  HIS B  28     146.104  14.010  37.951  1.00 49.65           C  
ANISOU 1016  CG  HIS B  28     6406   6540   5918   -562   -390   -240       C  
ATOM   1017  ND1 HIS B  28     146.874  13.030  37.369  1.00 53.53           N  
ANISOU 1017  ND1 HIS B  28     7013   6989   6337   -576   -377   -289       N  
ATOM   1018  CD2 HIS B  28     145.245  13.369  38.789  1.00 51.91           C  
ANISOU 1018  CD2 HIS B  28     6656   6773   6295   -607   -328   -238       C  
ATOM   1019  CE1 HIS B  28     146.500  11.848  37.826  1.00 54.71           C  
ANISOU 1019  CE1 HIS B  28     7200   7059   6529   -626   -315   -314       C  
ATOM   1020  NE2 HIS B  28     145.522  12.024  38.687  1.00 54.06           N  
ANISOU 1020  NE2 HIS B  28     7028   6969   6543   -649   -285   -284       N  
ATOM   1021  N   ARG B  29     148.292  17.944  38.295  1.00 33.37           N  
ANISOU 1021  N   ARG B  29     4309   4640   3731   -320   -408   -122       N  
ATOM   1022  CA  ARG B  29     148.822  19.238  37.885  1.00 31.43           C  
ANISOU 1022  CA  ARG B  29     4055   4447   3440   -275   -440    -97       C  
ATOM   1023  C   ARG B  29     150.345  19.172  37.812  1.00 32.08           C  
ANISOU 1023  C   ARG B  29     4221   4534   3433   -230   -407   -114       C  
ATOM   1024  O   ARG B  29     150.962  18.285  38.410  1.00 33.55           O  
ANISOU 1024  O   ARG B  29     4456   4683   3609   -214   -351   -129       O  
ATOM   1025  CB  ARG B  29     148.386  20.331  38.866  1.00 27.73           C  
ANISOU 1025  CB  ARG B  29     3518   3985   3032   -237   -401    -50       C  
ATOM   1026  CG  ARG B  29     148.792  20.073  40.310  1.00 27.06           C  
ANISOU 1026  CG  ARG B  29     3462   3863   2957   -207   -304    -43       C  
ATOM   1027  CD  ARG B  29     148.438  21.249  41.215  1.00 27.59           C  
ANISOU 1027  CD  ARG B  29     3483   3933   3067   -175   -257     -4       C  
ATOM   1028  NE  ARG B  29     147.015  21.302  41.546  1.00 28.28           N  
ANISOU 1028  NE  ARG B  29     3483   3998   3263   -202   -238     14       N  
ATOM   1029  CZ  ARG B  29     146.119  22.036  40.893  1.00 27.19           C  
ANISOU 1029  CZ  ARG B  29     3258   3886   3188   -205   -291     37       C  
ATOM   1030  NH1 ARG B  29     146.495  22.785  39.865  1.00 24.80           N  
ANISOU 1030  NH1 ARG B  29     2959   3626   2836   -186   -366     48       N  
ATOM   1031  NH2 ARG B  29     144.846  22.021  41.269  1.00 27.23           N  
ANISOU 1031  NH2 ARG B  29     3167   3870   3308   -226   -265     55       N  
ATOM   1032  N   PRO B  30     150.959  20.111  37.076  1.00 28.36           N  
ANISOU 1032  N   PRO B  30     3764   4107   2905   -208   -438   -106       N  
ATOM   1033  CA  PRO B  30     152.421  20.153  36.980  1.00 25.97           C  
ANISOU 1033  CA  PRO B  30     3522   3815   2532   -168   -401   -122       C  
ATOM   1034  C   PRO B  30     153.045  20.507  38.323  1.00 27.15           C  
ANISOU 1034  C   PRO B  30     3657   3961   2696   -120   -339    -99       C  
ATOM   1035  O   PRO B  30     152.333  20.612  39.321  1.00 29.65           O  
ANISOU 1035  O   PRO B  30     3938   4260   3068   -120   -315    -76       O  
ATOM   1036  CB  PRO B  30     152.677  21.278  35.968  1.00 23.82           C  
ANISOU 1036  CB  PRO B  30     3253   3557   2239   -150   -430   -109       C  
ATOM   1037  CG  PRO B  30     151.390  21.421  35.211  1.00 24.03           C  
ANISOU 1037  CG  PRO B  30     3247   3601   2283   -196   -511    -99       C  
ATOM   1038  CD  PRO B  30     150.318  21.116  36.210  1.00 24.60           C  
ANISOU 1038  CD  PRO B  30     3249   3670   2428   -221   -511    -81       C  
ATOM   1039  N   ALA B  31     154.360  20.697  38.337  1.00 25.02           N  
ANISOU 1039  N   ALA B  31     3418   3703   2386    -82   -310   -106       N  
ATOM   1040  CA  ALA B  31     155.071  21.096  39.544  1.00 20.43           C  
ANISOU 1040  CA  ALA B  31     2827   3121   1815    -45   -268    -85       C  
ATOM   1041  C   ALA B  31     156.540  21.308  39.216  1.00 23.52           C  
ANISOU 1041  C   ALA B  31     3236   3497   2203    -18   -244    -92       C  
ATOM   1042  O   ALA B  31     157.037  20.813  38.207  1.00 28.28           O  
ANISOU 1042  O   ALA B  31     3869   4094   2783    -19   -245   -116       O  
ATOM   1043  CB  ALA B  31     154.926  20.028  40.619  1.00 17.52           C  
ANISOU 1043  CB  ALA B  31     2472   2730   1454    -35   -240    -80       C  
ATOM   1044  N   VAL B  32     157.237  22.043  40.076  1.00 23.36           N  
ANISOU 1044  N   VAL B  32     3198   3480   2198     -2   -222    -74       N  
ATOM   1045  CA  VAL B  32     158.646  22.340  39.843  1.00 22.04           C  
ANISOU 1045  CA  VAL B  32     3025   3322   2028     12   -204    -82       C  
ATOM   1046  C   VAL B  32     159.504  21.668  40.903  1.00 25.08           C  
ANISOU 1046  C   VAL B  32     3397   3728   2402     44   -196    -75       C  
ATOM   1047  O   VAL B  32     159.295  21.875  42.101  1.00 30.59           O  
ANISOU 1047  O   VAL B  32     4094   4424   3106     45   -197    -54       O  
ATOM   1048  CB  VAL B  32     158.923  23.852  39.856  1.00 20.62           C  
ANISOU 1048  CB  VAL B  32     2828   3141   1865     -2   -195    -73       C  
ATOM   1049  CG1 VAL B  32     160.335  24.132  39.374  1.00 16.04           C  
ANISOU 1049  CG1 VAL B  32     2234   2587   1273      3   -177    -88       C  
ATOM   1050  CG2 VAL B  32     157.900  24.598  39.000  1.00 23.74           C  
ANISOU 1050  CG2 VAL B  32     3235   3522   2265    -20   -211    -67       C  
ATOM   1051  N   VAL B  33     160.471  20.870  40.457  1.00 24.16           N  
ANISOU 1051  N   VAL B  33     3278   3640   2262     77   -188    -91       N  
ATOM   1052  CA  VAL B  33     161.353  20.164  41.374  1.00 25.52           C  
ANISOU 1052  CA  VAL B  33     3433   3848   2417    131   -192    -78       C  
ATOM   1053  C   VAL B  33     162.501  21.077  41.774  1.00 27.89           C  
ANISOU 1053  C   VAL B  33     3679   4193   2724    132   -199    -72       C  
ATOM   1054  O   VAL B  33     163.312  21.473  40.939  1.00 29.86           O  
ANISOU 1054  O   VAL B  33     3900   4481   2967    132   -183    -95       O  
ATOM   1055  CB  VAL B  33     161.932  18.897  40.726  1.00 23.37           C  
ANISOU 1055  CB  VAL B  33     3179   3592   2108    194   -175    -99       C  
ATOM   1056  CG1 VAL B  33     162.845  18.166  41.702  1.00 24.20           C  
ANISOU 1056  CG1 VAL B  33     3262   3702   2233    262   -181    -66       C  
ATOM   1057  CG2 VAL B  33     160.811  17.986  40.242  1.00 21.76           C  
ANISOU 1057  CG2 VAL B  33     3036   3318   1913    173   -162   -114       C  
ATOM   1058  N   LEU B  34     162.567  21.415  43.056  1.00 26.33           N  
ANISOU 1058  N   LEU B  34     3476   3997   2532    125   -220    -46       N  
ATOM   1059  CA  LEU B  34     163.629  22.279  43.543  1.00 28.16           C  
ANISOU 1059  CA  LEU B  34     3660   4277   2764    115   -235    -45       C  
ATOM   1060  C   LEU B  34     164.749  21.435  44.130  1.00 32.18           C  
ANISOU 1060  C   LEU B  34     4126   4854   3248    179   -271    -26       C  
ATOM   1061  O   LEU B  34     165.802  21.949  44.501  1.00 36.86           O  
ANISOU 1061  O   LEU B  34     4659   5510   3835    177   -299    -25       O  
ATOM   1062  CB  LEU B  34     163.070  23.241  44.589  1.00 27.14           C  
ANISOU 1062  CB  LEU B  34     3562   4108   2643     67   -240    -34       C  
ATOM   1063  CG  LEU B  34     161.691  23.799  44.228  1.00 25.43           C  
ANISOU 1063  CG  LEU B  34     3387   3828   2446     34   -211    -40       C  
ATOM   1064  CD1 LEU B  34     161.036  24.448  45.435  1.00 26.46           C  
ANISOU 1064  CD1 LEU B  34     3557   3928   2569     11   -206    -29       C  
ATOM   1065  CD2 LEU B  34     161.775  24.762  43.060  1.00 23.18           C  
ANISOU 1065  CD2 LEU B  34     3086   3542   2177     12   -192    -60       C  
ATOM   1066  N   SER B  35     164.518  20.129  44.200  1.00 29.65           N  
ANISOU 1066  N   SER B  35     3835   4523   2910    243   -275     -7       N  
ATOM   1067  CA  SER B  35     165.502  19.206  44.747  1.00 29.29           C  
ANISOU 1067  CA  SER B  35     3755   4521   2852    330   -311     27       C  
ATOM   1068  C   SER B  35     166.428  18.707  43.644  1.00 29.14           C  
ANISOU 1068  C   SER B  35     3681   4504   2886    378   -271      6       C  
ATOM   1069  O   SER B  35     166.039  18.651  42.476  1.00 28.77           O  
ANISOU 1069  O   SER B  35     3662   4422   2848    358   -217    -34       O  
ATOM   1070  CB  SER B  35     164.802  18.019  45.411  1.00 29.20           C  
ANISOU 1070  CB  SER B  35     3819   4438   2838    371   -309     66       C  
ATOM   1071  OG  SER B  35     163.874  18.444  46.397  1.00 27.20           O  
ANISOU 1071  OG  SER B  35     3621   4151   2561    313   -318     81       O  
ATOM   1072  N   PRO B  36     167.657  18.329  44.016  1.00 29.73           N  
ANISOU 1072  N   PRO B  36     3679   4621   2996    442   -298     34       N  
ATOM   1073  CA  PRO B  36     168.639  17.815  43.055  1.00 31.07           C  
ANISOU 1073  CA  PRO B  36     3785   4790   3232    499   -245     17       C  
ATOM   1074  C   PRO B  36     168.204  16.476  42.476  1.00 35.05           C  
ANISOU 1074  C   PRO B  36     4361   5195   3764    556   -182     14       C  
ATOM   1075  O   PRO B  36     167.173  15.941  42.875  1.00 32.29           O  
ANISOU 1075  O   PRO B  36     4101   4782   3385    548   -188     29       O  
ATOM   1076  CB  PRO B  36     169.894  17.613  43.910  1.00 32.15           C  
ANISOU 1076  CB  PRO B  36     3817   4992   3408    566   -306     65       C  
ATOM   1077  CG  PRO B  36     169.672  18.437  45.144  1.00 32.49           C  
ANISOU 1077  CG  PRO B  36     3867   5092   3385    509   -397     89       C  
ATOM   1078  CD  PRO B  36     168.201  18.414  45.380  1.00 30.92           C  
ANISOU 1078  CD  PRO B  36     3795   4826   3127    463   -382     85       C  
ATOM   1079  N   PHE B  37     168.998  15.945  41.553  1.00 43.75           N  
ANISOU 1079  N   PHE B  37     5425   6277   4922    608   -113     -8       N  
ATOM   1080  CA  PHE B  37     168.747  14.631  40.974  1.00 49.19           C  
ANISOU 1080  CA  PHE B  37     6186   6863   5640    664    -41    -17       C  
ATOM   1081  C   PHE B  37     169.082  13.520  41.956  1.00 54.47           C  
ANISOU 1081  C   PHE B  37     6853   7493   6348    767    -67     52       C  
ATOM   1082  O   PHE B  37     168.308  12.579  42.127  1.00 51.31           O  
ANISOU 1082  O   PHE B  37     6553   7002   5940    784    -46     64       O  
ATOM   1083  CB  PHE B  37     169.571  14.448  39.696  1.00 49.31           C  
ANISOU 1083  CB  PHE B  37     6169   6864   5702    690     56    -65       C  
ATOM   1084  CG  PHE B  37     169.639  13.021  39.210  1.00 50.28           C  
ANISOU 1084  CG  PHE B  37     6354   6879   5869    767    141    -71       C  
ATOM   1085  CD1 PHE B  37     170.576  12.140  39.728  1.00 49.05           C  
ANISOU 1085  CD1 PHE B  37     6138   6704   5796    888    154    -20       C  
ATOM   1086  CD2 PHE B  37     168.777  12.565  38.226  1.00 51.27           C  
ANISOU 1086  CD2 PHE B  37     6604   6921   5957    717    208   -128       C  
ATOM   1087  CE1 PHE B  37     170.646  10.831  39.280  1.00 47.27           C  
ANISOU 1087  CE1 PHE B  37     5980   6365   5617    964    246    -26       C  
ATOM   1088  CE2 PHE B  37     168.846  11.254  37.772  1.00 50.49           C  
ANISOU 1088  CE2 PHE B  37     6577   6712   5895    777    296   -143       C  
ATOM   1089  CZ  PHE B  37     169.780  10.388  38.302  1.00 48.81           C  
ANISOU 1089  CZ  PHE B  37     6309   6469   5768    904    323    -93       C  
ATOM   1090  N   MET B  38     170.240  13.628  42.601  1.00 64.09           N  
ANISOU 1090  N   MET B  38     7957   8782   7613    834   -116     99       N  
ATOM   1091  CA  MET B  38     170.731  12.537  43.437  1.00 70.37           C  
ANISOU 1091  CA  MET B  38     8741   9542   8454    951   -143    175       C  
ATOM   1092  C   MET B  38     169.845  12.271  44.646  1.00 63.83           C  
ANISOU 1092  C   MET B  38     8006   8686   7560    939   -214    229       C  
ATOM   1093  O   MET B  38     169.584  11.118  44.985  1.00 65.20           O  
ANISOU 1093  O   MET B  38     8256   8767   7748   1008   -191    271       O  
ATOM   1094  CB  MET B  38     172.168  12.774  43.896  1.00 79.37           C  
ANISOU 1094  CB  MET B  38     9721  10777   9658   1022   -201    220       C  
ATOM   1095  CG  MET B  38     172.684  11.658  44.794  1.00 86.26           C  
ANISOU 1095  CG  MET B  38    10579  11616  10578   1155   -245    313       C  
ATOM   1096  SD  MET B  38     172.416  10.057  44.004  1.00185.52           S  
ANISOU 1096  SD  MET B  38    23256  24019  23213   1251   -105    307       S  
ATOM   1097  CE  MET B  38     173.357   8.965  45.062  1.00108.74           C  
ANISOU 1097  CE  MET B  38    13475  14277  13564   1427   -165    431       C  
ATOM   1098  N   TYR B  39     169.400  13.337  45.301  1.00 50.54           N  
ANISOU 1098  N   TYR B  39     6325   7075   5804    850   -287    227       N  
ATOM   1099  CA  TYR B  39     168.486  13.210  46.429  1.00 43.55           C  
ANISOU 1099  CA  TYR B  39     5538   6162   4848    823   -337    269       C  
ATOM   1100  C   TYR B  39     167.192  12.514  46.002  1.00 45.48           C  
ANISOU 1100  C   TYR B  39     5910   6291   5080    791   -259    241       C  
ATOM   1101  O   TYR B  39     166.767  11.525  46.612  1.00 48.74           O  
ANISOU 1101  O   TYR B  39     6409   6623   5487    834   -249    288       O  
ATOM   1102  CB  TYR B  39     168.179  14.589  47.018  1.00 38.05           C  
ANISOU 1102  CB  TYR B  39     4828   5553   4078    721   -403    253       C  
ATOM   1103  CG  TYR B  39     166.961  14.616  47.914  1.00 36.87           C  
ANISOU 1103  CG  TYR B  39     4795   5360   3853    668   -415    271       C  
ATOM   1104  CD1 TYR B  39     167.059  14.302  49.261  1.00 39.63           C  
ANISOU 1104  CD1 TYR B  39     5188   5716   4152    700   -482    343       C  
ATOM   1105  CD2 TYR B  39     165.712  14.960  47.411  1.00 34.85           C  
ANISOU 1105  CD2 TYR B  39     4606   5059   3579    585   -357    220       C  
ATOM   1106  CE1 TYR B  39     165.949  14.328  50.082  1.00 38.65           C  
ANISOU 1106  CE1 TYR B  39     5180   5548   3960    647   -474    357       C  
ATOM   1107  CE2 TYR B  39     164.597  14.989  48.225  1.00 33.99           C  
ANISOU 1107  CE2 TYR B  39     4589   4908   3416    537   -354    235       C  
ATOM   1108  CZ  TYR B  39     164.723  14.674  49.560  1.00 34.81           C  
ANISOU 1108  CZ  TYR B  39     4744   5013   3470    566   -404    301       C  
ATOM   1109  OH  TYR B  39     163.620  14.700  50.379  1.00 31.60           O  
ANISOU 1109  OH  TYR B  39     4438   4560   3010    515   -382    315       O  
ATOM   1110  N   ASN B  40     166.571  13.039  44.949  1.00 40.05           N  
ANISOU 1110  N   ASN B  40     5235   5595   4386    710   -208    167       N  
ATOM   1111  CA  ASN B  40     165.335  12.471  44.417  1.00 32.83           C  
ANISOU 1111  CA  ASN B  40     4425   4585   3464    663   -145    131       C  
ATOM   1112  C   ASN B  40     165.502  11.003  44.066  1.00 28.54           C  
ANISOU 1112  C   ASN B  40     3937   3934   2970    740    -78    141       C  
ATOM   1113  O   ASN B  40     164.583  10.204  44.239  1.00 25.24           O  
ANISOU 1113  O   ASN B  40     3619   3424   2546    723    -43    145       O  
ATOM   1114  CB  ASN B  40     164.874  13.239  43.178  1.00 32.37           C  
ANISOU 1114  CB  ASN B  40     4359   4546   3395    578   -113     54       C  
ATOM   1115  CG  ASN B  40     164.750  14.731  43.428  1.00 33.39           C  
ANISOU 1115  CG  ASN B  40     4435   4768   3481    506   -167     44       C  
ATOM   1116  OD1 ASN B  40     164.567  15.169  44.565  1.00 32.95           O  
ANISOU 1116  OD1 ASN B  40     4381   4746   3393    493   -219     82       O  
ATOM   1117  ND2 ASN B  40     164.854  15.521  42.364  1.00 33.15           N  
ANISOU 1117  ND2 ASN B  40     4374   4774   3447    459   -147     -8       N  
ATOM   1118  N   ASN B  41     166.685  10.658  43.570  1.00 30.52           N  
ANISOU 1118  N   ASN B  41     4124   4193   3278    824    -49    143       N  
ATOM   1119  CA  ASN B  41     166.977   9.289  43.173  1.00 31.90           C  
ANISOU 1119  CA  ASN B  41     4351   4258   3512    909     31    150       C  
ATOM   1120  C   ASN B  41     167.171   8.374  44.378  1.00 30.46           C  
ANISOU 1120  C   ASN B  41     4204   4025   3343   1004      3    243       C  
ATOM   1121  O   ASN B  41     166.772   7.211  44.351  1.00 30.07           O  
ANISOU 1121  O   ASN B  41     4257   3854   3316   1039     68    254       O  
ATOM   1122  CB  ASN B  41     168.203   9.241  42.258  1.00 35.73           C  
ANISOU 1122  CB  ASN B  41     4749   4762   4063    975     87    124       C  
ATOM   1123  CG  ASN B  41     168.579   7.825  41.861  1.00 38.78           C  
ANISOU 1123  CG  ASN B  41     5192   5026   4518   1075    185    131       C  
ATOM   1124  OD1 ASN B  41     167.726   6.938  41.787  1.00 37.31           O  
ANISOU 1124  OD1 ASN B  41     5132   4726   4319   1057    236    119       O  
ATOM   1125  ND2 ASN B  41     169.864   7.602  41.614  1.00 40.50           N  
ANISOU 1125  ND2 ASN B  41     5312   5259   4816   1181    220    150       N  
ATOM   1126  N   LYS B  42     167.770   8.910  45.438  1.00 33.93           N  
ANISOU 1126  N   LYS B  42     4570   4556   3764   1039    -96    310       N  
ATOM   1127  CA  LYS B  42     168.011   8.138  46.655  1.00 36.17           C  
ANISOU 1127  CA  LYS B  42     4892   4805   4045   1130   -143    410       C  
ATOM   1128  C   LYS B  42     166.729   7.927  47.453  1.00 37.35           C  
ANISOU 1128  C   LYS B  42     5175   4894   4123   1063   -146    429       C  
ATOM   1129  O   LYS B  42     166.253   6.800  47.597  1.00 38.84           O  
ANISOU 1129  O   LYS B  42     5473   4960   4326   1097    -85    455       O  
ATOM   1130  CB  LYS B  42     169.068   8.815  47.540  1.00 39.16           C  
ANISOU 1130  CB  LYS B  42     5153   5311   4414   1177   -263    474       C  
ATOM   1131  CG  LYS B  42     170.511   8.624  47.059  1.00 46.33           C  
ANISOU 1131  CG  LYS B  42     5921   6260   5422   1287   -260    491       C  
ATOM   1132  CD  LYS B  42     171.531   8.978  48.132  1.00 51.64           C  
ANISOU 1132  CD  LYS B  42     6485   7045   6092   1349   -396    576       C  
ATOM   1133  CE  LYS B  42     171.890  10.462  48.115  1.00 55.28           C  
ANISOU 1133  CE  LYS B  42     6832   7652   6520   1250   -468    529       C  
ATOM   1134  NZ  LYS B  42     172.995  10.779  49.093  1.00 58.67           N  
ANISOU 1134  NZ  LYS B  42     7141   8199   6953   1303   -607    606       N  
ATOM   1135  N   THR B  43     166.176   9.016  47.975  1.00 39.69           N  
ANISOU 1135  N   THR B  43     5464   5270   4346    966   -206    415       N  
ATOM   1136  CA  THR B  43     165.004   8.944  48.840  1.00 42.80           C  
ANISOU 1136  CA  THR B  43     5971   5617   4674    901   -204    436       C  
ATOM   1137  C   THR B  43     163.735   8.537  48.098  1.00 43.54           C  
ANISOU 1137  C   THR B  43     6146   5613   4783    820   -110    370       C  
ATOM   1138  O   THR B  43     162.802   8.013  48.702  1.00 48.25           O  
ANISOU 1138  O   THR B  43     6846   6131   5355    788    -75    392       O  
ATOM   1139  CB  THR B  43     164.748  10.291  49.546  1.00 42.21           C  
ANISOU 1139  CB  THR B  43     5867   5649   4523    816   -278    430       C  
ATOM   1140  OG1 THR B  43     164.699  11.340  48.570  1.00 42.45           O  
ANISOU 1140  OG1 THR B  43     5815   5747   4568    744   -271    348       O  
ATOM   1141  CG2 THR B  43     165.852  10.588  50.550  1.00 41.40           C  
ANISOU 1141  CG2 THR B  43     5712   5636   4385    879   -386    502       C  
ATOM   1142  N   GLY B  44     163.700   8.781  46.793  1.00 39.80           N  
ANISOU 1142  N   GLY B  44     5628   5147   4347    782    -69    290       N  
ATOM   1143  CA  GLY B  44     162.482   8.575  46.033  1.00 37.24           C  
ANISOU 1143  CA  GLY B  44     5366   4755   4030    688     -4    222       C  
ATOM   1144  C   GLY B  44     161.484   9.647  46.412  1.00 32.80           C  
ANISOU 1144  C   GLY B  44     4793   4249   3419    582    -38    203       C  
ATOM   1145  O   GLY B  44     160.289   9.538  46.140  1.00 29.84           O  
ANISOU 1145  O   GLY B  44     4465   3825   3049    499      1    165       O  
ATOM   1146  N   MET B  45     162.004  10.694  47.045  1.00 32.63           N  
ANISOU 1146  N   MET B  45     4707   4330   3359    586   -108    228       N  
ATOM   1147  CA  MET B  45     161.220  11.842  47.470  1.00 31.12           C  
ANISOU 1147  CA  MET B  45     4503   4195   3124    498   -134    213       C  
ATOM   1148  C   MET B  45     161.644  13.044  46.644  1.00 28.53           C  
ANISOU 1148  C   MET B  45     4081   3961   2797    464   -165    163       C  
ATOM   1149  O   MET B  45     162.524  12.936  45.791  1.00 28.93           O  
ANISOU 1149  O   MET B  45     4081   4033   2879    505   -162    141       O  
ATOM   1150  CB  MET B  45     161.500  12.149  48.940  1.00 31.08           C  
ANISOU 1150  CB  MET B  45     4522   4227   3059    519   -186    279       C  
ATOM   1151  CG  MET B  45     160.991  11.105  49.915  1.00 31.27           C  
ANISOU 1151  CG  MET B  45     4659   4159   3065    543   -152    338       C  
ATOM   1152  SD  MET B  45     159.203  11.202  50.103  1.00 61.07           S  
ANISOU 1152  SD  MET B  45     8501   7866   6839    431    -77    305       S  
ATOM   1153  CE  MET B  45     159.012  12.932  50.530  1.00 66.81           C  
ANISOU 1153  CE  MET B  45     9171   8699   7514    363   -120    282       C  
ATOM   1154  N   CYS B  46     161.029  14.193  46.908  1.00 27.34           N  
ANISOU 1154  N   CYS B  46     3914   3861   2615    391   -184    146       N  
ATOM   1155  CA  CYS B  46     161.473  15.443  46.298  1.00 28.03           C  
ANISOU 1155  CA  CYS B  46     3921   4033   2694    359   -214    108       C  
ATOM   1156  C   CYS B  46     160.644  16.634  46.760  1.00 30.43           C  
ANISOU 1156  C   CYS B  46     4227   4368   2966    284   -221     98       C  
ATOM   1157  O   CYS B  46     159.520  16.475  47.238  1.00 32.16           O  
ANISOU 1157  O   CYS B  46     4498   4537   3185    248   -190    105       O  
ATOM   1158  CB  CYS B  46     161.424  15.344  44.772  1.00 25.71           C  
ANISOU 1158  CB  CYS B  46     3606   3727   2437    344   -182     53       C  
ATOM   1159  SG  CYS B  46     159.763  15.084  44.102  1.00 49.66           S  
ANISOU 1159  SG  CYS B  46     6690   6690   5488    266   -143     15       S  
ATOM   1160  N   LEU B  47     161.202  17.829  46.592  1.00 30.36           N  
ANISOU 1160  N   LEU B  47     4158   4427   2952    255   -248     78       N  
ATOM   1161  CA  LEU B  47     160.505  19.060  46.947  1.00 30.24           C  
ANISOU 1161  CA  LEU B  47     4138   4398   2953    171   -236     64       C  
ATOM   1162  C   LEU B  47     160.039  19.774  45.686  1.00 30.45           C  
ANISOU 1162  C   LEU B  47     4132   4421   3015    131   -218     23       C  
ATOM   1163  O   LEU B  47     160.851  20.135  44.830  1.00 31.69           O  
ANISOU 1163  O   LEU B  47     4245   4606   3188    136   -225      2       O  
ATOM   1164  CB  LEU B  47     161.412  19.976  47.773  1.00 27.99           C  
ANISOU 1164  CB  LEU B  47     3830   4140   2664    147   -269     72       C  
ATOM   1165  CG  LEU B  47     161.636  19.567  49.231  1.00 26.54           C  
ANISOU 1165  CG  LEU B  47     3695   3953   2437    157   -295    115       C  
ATOM   1166  CD1 LEU B  47     162.857  20.261  49.812  1.00 25.09           C  
ANISOU 1166  CD1 LEU B  47     3478   3813   2243    146   -350    118       C  
ATOM   1167  CD2 LEU B  47     160.400  19.857  50.060  1.00 28.36           C  
ANISOU 1167  CD2 LEU B  47     3996   4138   2642    105   -254    120       C  
ATOM   1168  N   CYS B  48     158.731  19.968  45.568  1.00 28.48           N  
ANISOU 1168  N   CYS B  48     3906   4144   2772     96   -194     15       N  
ATOM   1169  CA  CYS B  48     158.182  20.595  44.374  1.00 25.41           C  
ANISOU 1169  CA  CYS B  48     3490   3751   2412     65   -190    -13       C  
ATOM   1170  C   CYS B  48     157.165  21.674  44.709  1.00 24.62           C  
ANISOU 1170  C   CYS B  48     3388   3641   2326     30   -174    -10       C  
ATOM   1171  O   CYS B  48     156.533  21.641  45.765  1.00 24.92           O  
ANISOU 1171  O   CYS B  48     3453   3674   2341     24   -151      7       O  
ATOM   1172  CB  CYS B  48     157.533  19.549  43.469  1.00 24.90           C  
ANISOU 1172  CB  CYS B  48     3443   3684   2334     74   -191    -31       C  
ATOM   1173  SG  CYS B  48     156.104  18.732  44.200  1.00 31.04           S  
ANISOU 1173  SG  CYS B  48     4254   4394   3145     51   -159    -14       S  
ATOM   1174  N   VAL B  49     157.023  22.640  43.807  1.00 22.46           N  
ANISOU 1174  N   VAL B  49     3087   3368   2078     12   -178    -24       N  
ATOM   1175  CA  VAL B  49     155.958  23.624  43.926  1.00 21.23           C  
ANISOU 1175  CA  VAL B  49     2919   3218   1929    -10   -163    -18       C  
ATOM   1176  C   VAL B  49     154.866  23.294  42.917  1.00 23.70           C  
ANISOU 1176  C   VAL B  49     3207   3551   2247    -25   -185    -21       C  
ATOM   1177  O   VAL B  49     155.120  23.234  41.714  1.00 23.78           O  
ANISOU 1177  O   VAL B  49     3212   3554   2268    -26   -213    -35       O  
ATOM   1178  CB  VAL B  49     156.461  25.066  43.743  1.00 19.97           C  
ANISOU 1178  CB  VAL B  49     2750   3054   1782    -19   -155    -22       C  
ATOM   1179  CG1 VAL B  49     157.500  25.405  44.795  1.00 20.26           C  
ANISOU 1179  CG1 VAL B  49     2807   3084   1808    -19   -145    -24       C  
ATOM   1180  CG2 VAL B  49     157.033  25.266  42.347  1.00 21.42           C  
ANISOU 1180  CG2 VAL B  49     2921   3236   1982    -18   -176    -34       C  
ATOM   1181  N   PRO B  50     153.642  23.057  43.413  1.00 25.36           N  
ANISOU 1181  N   PRO B  50     3405   3734   2497    -41   -163     -8       N  
ATOM   1182  CA  PRO B  50     152.526  22.711  42.529  1.00 25.88           C  
ANISOU 1182  CA  PRO B  50     3433   3782   2618    -63   -190     -9       C  
ATOM   1183  C   PRO B  50     152.131  23.906  41.673  1.00 27.78           C  
ANISOU 1183  C   PRO B  50     3636   4046   2874    -66   -220      2       C  
ATOM   1184  O   PRO B  50     152.052  25.024  42.186  1.00 26.43           O  
ANISOU 1184  O   PRO B  50     3457   3875   2711    -56   -188     19       O  
ATOM   1185  CB  PRO B  50     151.398  22.349  43.507  1.00 21.68           C  
ANISOU 1185  CB  PRO B  50     2885   3203   2150    -78   -139      6       C  
ATOM   1186  CG  PRO B  50     151.719  23.099  44.747  1.00 21.03           C  
ANISOU 1186  CG  PRO B  50     2832   3117   2044    -65    -83     20       C  
ATOM   1187  CD  PRO B  50     153.225  23.151  44.823  1.00 22.95           C  
ANISOU 1187  CD  PRO B  50     3119   3398   2203    -43   -106      9       C  
ATOM   1188  N   CYS B  51     151.894  23.678  40.385  1.00 28.20           N  
ANISOU 1188  N   CYS B  51     3678   4114   2923    -81   -280     -6       N  
ATOM   1189  CA  CYS B  51     151.508  24.770  39.505  1.00 29.59           C  
ANISOU 1189  CA  CYS B  51     3828   4311   3105    -79   -320     15       C  
ATOM   1190  C   CYS B  51     149.986  24.878  39.443  1.00 31.21           C  
ANISOU 1190  C   CYS B  51     3960   4498   3399    -91   -342     43       C  
ATOM   1191  O   CYS B  51     149.272  24.046  40.004  1.00 31.32           O  
ANISOU 1191  O   CYS B  51     3945   4486   3469   -110   -322     37       O  
ATOM   1192  CB  CYS B  51     152.101  24.558  38.109  1.00 27.24           C  
ANISOU 1192  CB  CYS B  51     3569   4041   2740    -91   -376     -4       C  
ATOM   1193  SG  CYS B  51     153.888  24.294  38.109  1.00 51.53           S  
ANISOU 1193  SG  CYS B  51     6712   7077   5792    -64   -321    -37       S  
ATOM   1194  N   THR B  52     149.498  25.909  38.762  1.00 32.46           N  
ANISOU 1194  N   THR B  52     4086   4670   3576    -77   -380     76       N  
ATOM   1195  CA  THR B  52     148.066  26.122  38.595  1.00 33.74           C  
ANISOU 1195  CA  THR B  52     4159   4824   3835    -78   -414    111       C  
ATOM   1196  C   THR B  52     147.793  26.978  37.362  1.00 31.70           C  
ANISOU 1196  C   THR B  52     3889   4594   3563    -64   -497    149       C  
ATOM   1197  O   THR B  52     148.627  27.792  36.970  1.00 30.71           O  
ANISOU 1197  O   THR B  52     3823   4477   3367    -43   -492    157       O  
ATOM   1198  CB  THR B  52     147.455  26.827  39.814  1.00 36.27           C  
ANISOU 1198  CB  THR B  52     4433   5106   4242    -49   -325    137       C  
ATOM   1199  OG1 THR B  52     146.073  27.108  39.556  1.00 38.91           O  
ANISOU 1199  OG1 THR B  52     4662   5435   4687    -41   -356    177       O  
ATOM   1200  CG2 THR B  52     148.182  28.133  40.083  1.00 35.71           C  
ANISOU 1200  CG2 THR B  52     4410   5027   4130    -12   -275    151       C  
ATOM   1201  N   THR B  53     146.610  26.822  36.776  1.00 32.33           N  
ANISOU 1201  N   THR B  53     3889   4687   3710    -77   -576    176       N  
ATOM   1202  CA  THR B  53     146.228  27.602  35.599  1.00 29.72           C  
ANISOU 1202  CA  THR B  53     3545   4384   3365    -59   -673    225       C  
ATOM   1203  C   THR B  53     145.538  28.902  36.004  1.00 29.64           C  
ANISOU 1203  C   THR B  53     3466   4349   3448      5   -640    290       C  
ATOM   1204  O   THR B  53     145.340  29.801  35.182  1.00 28.91           O  
ANISOU 1204  O   THR B  53     3373   4267   3344     39   -701    344       O  
ATOM   1205  CB  THR B  53     145.283  26.811  34.679  1.00 27.21           C  
ANISOU 1205  CB  THR B  53     3171   4101   3068   -108   -797    226       C  
ATOM   1206  OG1 THR B  53     145.214  27.450  33.399  1.00 31.46           O  
ANISOU 1206  OG1 THR B  53     3736   4673   3543    -99   -905    268       O  
ATOM   1207  CG2 THR B  53     143.886  26.729  35.282  1.00 23.75           C  
ANISOU 1207  CG2 THR B  53     2587   3652   2786   -105   -797    256       C  
ATOM   1208  N   GLN B  54     145.193  28.998  37.284  1.00 29.68           N  
ANISOU 1208  N   GLN B  54     3423   4313   3542     23   -534    286       N  
ATOM   1209  CA  GLN B  54     144.459  30.143  37.803  1.00 29.86           C  
ANISOU 1209  CA  GLN B  54     3378   4297   3670     85   -476    341       C  
ATOM   1210  C   GLN B  54     145.375  31.050  38.610  1.00 30.71           C  
ANISOU 1210  C   GLN B  54     3575   4363   3732    114   -358    329       C  
ATOM   1211  O   GLN B  54     145.843  30.679  39.689  1.00 30.79           O  
ANISOU 1211  O   GLN B  54     3623   4350   3724     92   -266    284       O  
ATOM   1212  CB  GLN B  54     143.298  29.673  38.680  1.00 30.34           C  
ANISOU 1212  CB  GLN B  54     3323   4333   3872     81   -423    343       C  
ATOM   1213  CG  GLN B  54     142.373  28.675  38.016  1.00 32.84           C  
ANISOU 1213  CG  GLN B  54     3542   4690   4244     34   -533    344       C  
ATOM   1214  CD  GLN B  54     141.664  29.253  36.806  1.00 35.29           C  
ANISOU 1214  CD  GLN B  54     3780   5041   4588     62   -669    409       C  
ATOM   1215  OE1 GLN B  54     141.869  30.414  36.440  1.00 34.33           O  
ANISOU 1215  OE1 GLN B  54     3687   4908   4447    125   -676    461       O  
ATOM   1216  NE2 GLN B  54     140.820  28.442  36.176  1.00 36.79           N  
ANISOU 1216  NE2 GLN B  54     3879   5274   4825     12   -782    410       N  
ATOM   1217  N   SER B  55     145.631  32.242  38.083  1.00 31.36           N  
ANISOU 1217  N   SER B  55     3694   4432   3790    157   -364    371       N  
ATOM   1218  CA  SER B  55     146.457  33.216  38.780  1.00 33.79           C  
ANISOU 1218  CA  SER B  55     4086   4694   4057    174   -254    358       C  
ATOM   1219  C   SER B  55     145.574  34.263  39.447  1.00 41.31           C  
ANISOU 1219  C   SER B  55     4987   5580   5130    234   -165    403       C  
ATOM   1220  O   SER B  55     144.880  35.022  38.771  1.00 48.42           O  
ANISOU 1220  O   SER B  55     5839   6465   6092    290   -206    471       O  
ATOM   1221  CB  SER B  55     147.421  33.894  37.806  1.00 32.49           C  
ANISOU 1221  CB  SER B  55     4015   4544   3786    174   -294    369       C  
ATOM   1222  OG  SER B  55     146.722  34.751  36.916  1.00 35.29           O  
ANISOU 1222  OG  SER B  55     4341   4887   4182    227   -352    445       O  
ATOM   1223  N   LYS B  56     145.596  34.299  40.775  1.00 40.12           N  
ANISOU 1223  N   LYS B  56     4852   5384   5008    225    -40    367       N  
ATOM   1224  CA  LYS B  56     144.806  35.273  41.519  1.00 43.98           C  
ANISOU 1224  CA  LYS B  56     5306   5796   5608    280     74    398       C  
ATOM   1225  C   LYS B  56     145.602  36.551  41.755  1.00 45.28           C  
ANISOU 1225  C   LYS B  56     5582   5906   5715    293    158    393       C  
ATOM   1226  O   LYS B  56     145.109  37.503  42.361  1.00 46.32           O  
ANISOU 1226  O   LYS B  56     5715   5960   5924    338    270    413       O  
ATOM   1227  CB  LYS B  56     144.354  34.688  42.858  1.00 46.22           C  
ANISOU 1227  CB  LYS B  56     5566   6049   5947    257    183    359       C  
ATOM   1228  CG  LYS B  56     143.221  33.677  42.758  1.00 49.89           C  
ANISOU 1228  CG  LYS B  56     5897   6539   6519    252    138    375       C  
ATOM   1229  CD  LYS B  56     141.899  34.352  42.428  1.00 52.86           C  
ANISOU 1229  CD  LYS B  56     6141   6885   7059    326    141    447       C  
ATOM   1230  CE  LYS B  56     141.529  35.393  43.479  1.00 52.46           C  
ANISOU 1230  CE  LYS B  56     6106   6738   7088    375    317    454       C  
ATOM   1231  NZ  LYS B  56     140.239  36.076  43.160  1.00 51.37           N  
ANISOU 1231  NZ  LYS B  56     5826   6564   7128    462    329    532       N  
ATOM   1232  N   GLY B  57     146.841  36.564  41.275  1.00 44.91           N  
ANISOU 1232  N   GLY B  57     5629   5897   5537    251    112    364       N  
ATOM   1233  CA  GLY B  57     147.738  37.678  41.515  1.00 43.66           C  
ANISOU 1233  CA  GLY B  57     5581   5694   5315    241    190    346       C  
ATOM   1234  C   GLY B  57     148.331  37.626  42.912  1.00 42.84           C  
ANISOU 1234  C   GLY B  57     5545   5565   5165    189    298    276       C  
ATOM   1235  O   GLY B  57     148.849  38.624  43.412  1.00 44.42           O  
ANISOU 1235  O   GLY B  57     5832   5711   5333    174    388    255       O  
ATOM   1236  N   TYR B  58     148.240  36.462  43.552  1.00 39.50           N  
ANISOU 1236  N   TYR B  58     5092   5179   4735    157    287    241       N  
ATOM   1237  CA  TYR B  58     148.809  36.267  44.882  1.00 39.05           C  
ANISOU 1237  CA  TYR B  58     5108   5109   4620    105    370    180       C  
ATOM   1238  C   TYR B  58     150.300  36.608  44.902  1.00 38.11           C  
ANISOU 1238  C   TYR B  58     5085   5019   4374     49    357    135       C  
ATOM   1239  O   TYR B  58     150.999  36.411  43.910  1.00 36.54           O  
ANISOU 1239  O   TYR B  58     4884   4875   4124     39    269    139       O  
ATOM   1240  CB  TYR B  58     148.564  34.834  45.370  1.00 41.24           C  
ANISOU 1240  CB  TYR B  58     5345   5427   4897     81    341    160       C  
ATOM   1241  CG  TYR B  58     147.135  34.576  45.810  1.00 47.76           C  
ANISOU 1241  CG  TYR B  58     6087   6208   5849    116    400    188       C  
ATOM   1242  CD1 TYR B  58     146.276  35.632  46.105  1.00 51.06           C  
ANISOU 1242  CD1 TYR B  58     6486   6549   6367    164    502    217       C  
ATOM   1243  CD2 TYR B  58     146.648  33.279  45.940  1.00 48.66           C  
ANISOU 1243  CD2 TYR B  58     6142   6353   5993     99    365    184       C  
ATOM   1244  CE1 TYR B  58     144.972  35.402  46.506  1.00 50.52           C  
ANISOU 1244  CE1 TYR B  58     6325   6440   6430    197    567    242       C  
ATOM   1245  CE2 TYR B  58     145.343  33.043  46.344  1.00 49.07           C  
ANISOU 1245  CE2 TYR B  58     6109   6366   6172    122    428    206       C  
ATOM   1246  CZ  TYR B  58     144.511  34.109  46.622  1.00 49.09           C  
ANISOU 1246  CZ  TYR B  58     6077   6296   6277    172    529    236       C  
ATOM   1247  OH  TYR B  58     143.211  33.888  47.021  1.00 48.08           O  
ANISOU 1247  OH  TYR B  58     5848   6129   6290    197    601    259       O  
ATOM   1248  N   PRO B  59     150.785  37.134  46.038  1.00 39.09           N  
ANISOU 1248  N   PRO B  59     5296   5108   4450      6    449     90       N  
ATOM   1249  CA  PRO B  59     152.171  37.591  46.196  1.00 39.57           C  
ANISOU 1249  CA  PRO B  59     5440   5193   4401    -58    444     43       C  
ATOM   1250  C   PRO B  59     153.218  36.542  45.814  1.00 37.77           C  
ANISOU 1250  C   PRO B  59     5192   5061   4095    -91    335     21       C  
ATOM   1251  O   PRO B  59     154.262  36.893  45.262  1.00 35.44           O  
ANISOU 1251  O   PRO B  59     4921   4801   3743   -123    301      4       O  
ATOM   1252  CB  PRO B  59     152.271  37.878  47.699  1.00 40.61           C  
ANISOU 1252  CB  PRO B  59     5656   5282   4493   -105    543     -5       C  
ATOM   1253  CG  PRO B  59     150.882  38.197  48.118  1.00 40.67           C  
ANISOU 1253  CG  PRO B  59     5642   5206   4606    -52    644     24       C  
ATOM   1254  CD  PRO B  59     149.995  37.331  47.266  1.00 40.08           C  
ANISOU 1254  CD  PRO B  59     5445   5163   4620     10    569     78       C  
ATOM   1255  N   PHE B  60     152.947  35.275  46.117  1.00 36.50           N  
ANISOU 1255  N   PHE B  60     4991   4938   3940    -84    293     21       N  
ATOM   1256  CA  PHE B  60     153.927  34.208  45.911  1.00 32.89           C  
ANISOU 1256  CA  PHE B  60     4520   4560   3416   -107    206      1       C  
ATOM   1257  C   PHE B  60     153.801  33.481  44.575  1.00 33.20           C  
ANISOU 1257  C   PHE B  60     4495   4640   3480    -75    119     28       C  
ATOM   1258  O   PHE B  60     154.482  32.483  44.338  1.00 34.34           O  
ANISOU 1258  O   PHE B  60     4625   4838   3583    -84     57     13       O  
ATOM   1259  CB  PHE B  60     153.896  33.213  47.070  1.00 29.57           C  
ANISOU 1259  CB  PHE B  60     4117   4151   2968   -123    213    -16       C  
ATOM   1260  CG  PHE B  60     154.381  33.788  48.366  1.00 31.23           C  
ANISOU 1260  CG  PHE B  60     4413   4342   3112   -172    274    -53       C  
ATOM   1261  CD1 PHE B  60     155.735  33.993  48.584  1.00 30.72           C  
ANISOU 1261  CD1 PHE B  60     4345   4300   3026   -189    217    -78       C  
ATOM   1262  CD2 PHE B  60     153.487  34.130  49.365  1.00 31.41           C  
ANISOU 1262  CD2 PHE B  60     4481   4296   3159   -174    374    -55       C  
ATOM   1263  CE1 PHE B  60     156.187  34.528  49.776  1.00 30.45           C  
ANISOU 1263  CE1 PHE B  60     4359   4241   2970   -224    242   -106       C  
ATOM   1264  CE2 PHE B  60     153.932  34.659  50.560  1.00 29.65           C  
ANISOU 1264  CE2 PHE B  60     4323   4044   2900   -212    409    -88       C  
ATOM   1265  CZ  PHE B  60     155.284  34.859  50.766  1.00 29.17           C  
ANISOU 1265  CZ  PHE B  60     4257   4020   2806   -238    332   -112       C  
ATOM   1266  N   GLU B  61     152.918  33.967  43.713  1.00 30.64           N  
ANISOU 1266  N   GLU B  61     4134   4286   3220    -37    114     69       N  
ATOM   1267  CA  GLU B  61     152.767  33.383  42.388  1.00 30.03           C  
ANISOU 1267  CA  GLU B  61     4012   4245   3151    -16     26     93       C  
ATOM   1268  C   GLU B  61     153.961  33.691  41.492  1.00 26.86           C  
ANISOU 1268  C   GLU B  61     3647   3882   2676    -38     -8     78       C  
ATOM   1269  O   GLU B  61     154.366  34.845  41.358  1.00 29.00           O  
ANISOU 1269  O   GLU B  61     3961   4128   2930    -49     33     81       O  
ATOM   1270  CB  GLU B  61     151.493  33.893  41.725  1.00 34.10           C  
ANISOU 1270  CB  GLU B  61     4480   4725   3753     31     16    148       C  
ATOM   1271  CG  GLU B  61     150.219  33.400  42.367  1.00 38.95           C  
ANISOU 1271  CG  GLU B  61     5028   5309   4460     54     41    165       C  
ATOM   1272  CD  GLU B  61     148.992  33.828  41.590  1.00 41.57           C  
ANISOU 1272  CD  GLU B  61     5288   5620   4888    104     10    225       C  
ATOM   1273  OE1 GLU B  61     149.155  34.350  40.466  1.00 39.29           O  
ANISOU 1273  OE1 GLU B  61     5009   5344   4576    121    -49    257       O  
ATOM   1274  OE2 GLU B  61     147.868  33.647  42.102  1.00 46.31           O  
ANISOU 1274  OE2 GLU B  61     5819   6190   5588    127     45    245       O  
ATOM   1275  N   VAL B  62     154.520  32.651  40.880  1.00 22.39           N  
ANISOU 1275  N   VAL B  62     3068   3369   2072    -47    -71     62       N  
ATOM   1276  CA  VAL B  62     155.582  32.820  39.891  1.00 18.62           C  
ANISOU 1276  CA  VAL B  62     2617   2912   1544    -63    -93     48       C  
ATOM   1277  C   VAL B  62     155.117  32.349  38.519  1.00 17.41           C  
ANISOU 1277  C   VAL B  62     2455   2768   1393    -45   -159     72       C  
ATOM   1278  O   VAL B  62     154.826  31.171  38.327  1.00 11.86           O  
ANISOU 1278  O   VAL B  62     1726   2066    712    -39   -201     61       O  
ATOM   1279  CB  VAL B  62     156.854  32.045  40.263  1.00 18.53           C  
ANISOU 1279  CB  VAL B  62     2603   2880   1558    -72    -91      2       C  
ATOM   1280  CG1 VAL B  62     157.871  32.143  39.139  1.00 14.96           C  
ANISOU 1280  CG1 VAL B  62     2165   2420   1100    -75    -98    -10       C  
ATOM   1281  CG2 VAL B  62     157.440  32.570  41.561  1.00 20.87           C  
ANISOU 1281  CG2 VAL B  62     2911   3168   1850    -93    -47    -20       C  
ATOM   1282  N   VAL B  63     155.069  33.268  37.561  1.00 21.19           N  
ANISOU 1282  N   VAL B  63     2967   3244   1840    -41   -166    104       N  
ATOM   1283  CA  VAL B  63     154.565  32.955  36.228  1.00 21.09           C  
ANISOU 1283  CA  VAL B  63     2961   3232   1820    -27   -236    131       C  
ATOM   1284  C   VAL B  63     155.476  32.007  35.456  1.00 25.34           C  
ANISOU 1284  C   VAL B  63     3526   3743   2361    -35   -245     81       C  
ATOM   1285  O   VAL B  63     156.664  32.280  35.287  1.00 27.70           O  
ANISOU 1285  O   VAL B  63     3854   4026   2645    -44   -198     53       O  
ATOM   1286  CB  VAL B  63     154.360  34.235  35.398  1.00 17.23           C  
ANISOU 1286  CB  VAL B  63     2519   2729   1299    -13   -238    186       C  
ATOM   1287  CG1 VAL B  63     154.157  33.892  33.930  1.00 14.84           C  
ANISOU 1287  CG1 VAL B  63     2248   2423    965     -7   -310    202       C  
ATOM   1288  CG2 VAL B  63     153.179  35.038  35.944  1.00 14.94           C  
ANISOU 1288  CG2 VAL B  63     2191   2388   1097     31   -222    237       C  
ATOM   1289  N   LEU B  64     154.901  30.904  34.981  1.00 24.92           N  
ANISOU 1289  N   LEU B  64     3456   3691   2321    -31   -301     74       N  
ATOM   1290  CA  LEU B  64     155.616  29.954  34.139  1.00 22.70           C  
ANISOU 1290  CA  LEU B  64     3208   3390   2027    -33   -305     35       C  
ATOM   1291  C   LEU B  64     155.337  30.235  32.667  1.00 31.37           C  
ANISOU 1291  C   LEU B  64     4352   4490   3078    -21   -346     51       C  
ATOM   1292  O   LEU B  64     154.190  30.165  32.224  1.00 36.56           O  
ANISOU 1292  O   LEU B  64     4994   5164   3735    -16   -417     80       O  
ATOM   1293  CB  LEU B  64     155.205  28.518  34.473  1.00 15.85           C  
ANISOU 1293  CB  LEU B  64     2311   2523   1190    -38   -332     11       C  
ATOM   1294  CG  LEU B  64     155.468  28.013  35.892  1.00 13.51           C  
ANISOU 1294  CG  LEU B  64     1974   2229    929    -42   -295     -3       C  
ATOM   1295  CD1 LEU B  64     155.301  26.502  35.966  1.00 10.44           C  
ANISOU 1295  CD1 LEU B  64     1579   1837    550    -46   -313    -28       C  
ATOM   1296  CD2 LEU B  64     156.862  28.417  36.342  1.00 15.44           C  
ANISOU 1296  CD2 LEU B  64     2229   2464   1172    -41   -235    -21       C  
ATOM   1297  N   SER B  65     156.383  30.554  31.910  1.00 32.43           N  
ANISOU 1297  N   SER B  65     4531   4620   3170    -16   -302     34       N  
ATOM   1298  CA  SER B  65     156.235  30.839  30.483  1.00 33.09           C  
ANISOU 1298  CA  SER B  65     4654   4726   3194     -6   -326     50       C  
ATOM   1299  C   SER B  65     156.869  29.747  29.627  1.00 33.92           C  
ANISOU 1299  C   SER B  65     4779   4841   3269    -12   -313      4       C  
ATOM   1300  O   SER B  65     157.934  29.223  29.957  1.00 34.85           O  
ANISOU 1300  O   SER B  65     4900   4945   3398    -16   -258    -33       O  
ATOM   1301  CB  SER B  65     156.853  32.198  30.132  1.00 32.44           C  
ANISOU 1301  CB  SER B  65     4605   4648   3071     -9   -275     78       C  
ATOM   1302  OG  SER B  65     156.142  33.262  30.754  1.00 33.13           O  
ANISOU 1302  OG  SER B  65     4687   4729   3171     -4   -288    131       O  
ATOM   1303  N   GLY B  66     156.208  29.406  28.526  1.00 32.62           N  
ANISOU 1303  N   GLY B  66     4631   4701   3062    -22   -365     10       N  
ATOM   1304  CA  GLY B  66     156.745  28.442  27.586  1.00 34.39           C  
ANISOU 1304  CA  GLY B  66     4890   4935   3243    -42   -348    -31       C  
ATOM   1305  C   GLY B  66     156.114  27.063  27.631  1.00 38.04           C  
ANISOU 1305  C   GLY B  66     5336   5397   3721    -56   -393    -65       C  
ATOM   1306  O   GLY B  66     156.538  26.168  26.900  1.00 40.55           O  
ANISOU 1306  O   GLY B  66     5693   5716   3999    -80   -375   -104       O  
ATOM   1307  N   GLN B  67     155.113  26.875  28.486  1.00 38.46           N  
ANISOU 1307  N   GLN B  67     5340   5444   3829    -51   -445    -51       N  
ATOM   1308  CA  GLN B  67     154.441  25.579  28.549  1.00 39.91           C  
ANISOU 1308  CA  GLN B  67     5509   5627   4028    -78   -488    -82       C  
ATOM   1309  C   GLN B  67     153.186  25.517  27.681  1.00 39.96           C  
ANISOU 1309  C   GLN B  67     5516   5657   4012   -108   -582    -64       C  
ATOM   1310  O   GLN B  67     152.788  26.506  27.062  1.00 35.91           O  
ANISOU 1310  O   GLN B  67     5012   5161   3471    -99   -620    -20       O  
ATOM   1311  CB  GLN B  67     154.112  25.179  29.992  1.00 40.77           C  
ANISOU 1311  CB  GLN B  67     5565   5716   4208    -72   -487    -81       C  
ATOM   1312  CG  GLN B  67     155.242  24.457  30.699  1.00 43.29           C  
ANISOU 1312  CG  GLN B  67     5897   6012   4541    -61   -416   -115       C  
ATOM   1313  CD  GLN B  67     156.338  25.404  31.150  1.00 46.16           C  
ANISOU 1313  CD  GLN B  67     6271   6358   4911    -36   -354   -100       C  
ATOM   1314  OE1 GLN B  67     156.247  26.617  30.950  1.00 49.96           O  
ANISOU 1314  OE1 GLN B  67     6753   6844   5384    -28   -357    -69       O  
ATOM   1315  NE2 GLN B  67     157.380  24.854  31.770  1.00 43.08           N  
ANISOU 1315  NE2 GLN B  67     5888   5950   4533    -33   -300   -121       N  
ATOM   1316  N   GLU B  68     152.561  24.343  27.661  1.00 43.70           N  
ANISOU 1316  N   GLU B  68     5980   6128   4496   -147   -623    -96       N  
ATOM   1317  CA  GLU B  68     151.396  24.098  26.821  1.00 48.56           C  
ANISOU 1317  CA  GLU B  68     6595   6764   5091   -188   -721    -88       C  
ATOM   1318  C   GLU B  68     150.223  24.988  27.207  1.00 51.22           C  
ANISOU 1318  C   GLU B  68     6858   7123   5481   -171   -800    -27       C  
ATOM   1319  O   GLU B  68     149.434  25.402  26.357  1.00 53.33           O  
ANISOU 1319  O   GLU B  68     7123   7416   5722   -180   -883      5       O  
ATOM   1320  CB  GLU B  68     150.997  22.622  26.880  1.00 51.47           C  
ANISOU 1320  CB  GLU B  68     6968   7119   5469   -244   -743   -140       C  
ATOM   1321  CG  GLU B  68     151.080  21.999  28.266  1.00 54.90           C  
ANISOU 1321  CG  GLU B  68     7357   7532   5970   -241   -703   -155       C  
ATOM   1322  CD  GLU B  68     150.807  20.505  28.244  1.00 57.66           C  
ANISOU 1322  CD  GLU B  68     7733   7860   6316   -304   -712   -209       C  
ATOM   1323  OE1 GLU B  68     151.112  19.824  29.247  1.00 57.57           O  
ANISOU 1323  OE1 GLU B  68     7712   7825   6337   -306   -664   -227       O  
ATOM   1324  OE2 GLU B  68     150.285  20.011  27.221  1.00 59.42           O  
ANISOU 1324  OE2 GLU B  68     7992   8087   6497   -356   -768   -233       O  
ATOM   1325  N   ARG B  69     150.123  25.284  28.495  1.00 54.56           N  
ANISOU 1325  N   ARG B  69     7221   7534   5974   -148   -775     -7       N  
ATOM   1326  CA  ARG B  69     149.106  26.187  29.003  1.00 60.69           C  
ANISOU 1326  CA  ARG B  69     7922   8326   6812   -128   -834     58       C  
ATOM   1327  C   ARG B  69     149.843  27.254  29.798  1.00 57.42           C  
ANISOU 1327  C   ARG B  69     7515   7893   6408    -82   -761     87       C  
ATOM   1328  O   ARG B  69     150.960  27.017  30.258  1.00 55.05           O  
ANISOU 1328  O   ARG B  69     7253   7569   6093    -75   -674     50       O  
ATOM   1329  CB  ARG B  69     148.139  25.415  29.904  1.00 68.52           C  
ANISOU 1329  CB  ARG B  69     8826   9324   7886   -165   -874     55       C  
ATOM   1330  CG  ARG B  69     146.713  25.958  29.958  1.00 75.92           C  
ANISOU 1330  CG  ARG B  69     9659  10290   8897   -163   -971    118       C  
ATOM   1331  CD  ARG B  69     145.791  25.003  30.718  1.00 80.99           C  
ANISOU 1331  CD  ARG B  69    10205  10943   9626   -217  -1005    106       C  
ATOM   1332  NE  ARG B  69     145.101  24.064  29.832  1.00 85.72           N  
ANISOU 1332  NE  ARG B  69    10799  11556  10214   -276  -1083     69       N  
ATOM   1333  CZ  ARG B  69     145.635  22.942  29.357  1.00 87.32           C  
ANISOU 1333  CZ  ARG B  69    11086  11740  10351   -324  -1059     -2       C  
ATOM   1334  NH1 ARG B  69     146.881  22.611  29.675  1.00 86.11           N  
ANISOU 1334  NH1 ARG B  69    11017  11554  10147   -309   -960    -40       N  
ATOM   1335  NH2 ARG B  69     144.924  22.153  28.559  1.00 88.83           N  
ANISOU 1335  NH2 ARG B  69    11273  11946  10532   -387  -1136    -33       N  
ATOM   1336  N   ASP B  70     149.239  28.423  29.977  1.00 57.81           N  
ANISOU 1336  N   ASP B  70     7528   7951   6486    -52   -796    157       N  
ATOM   1337  CA  ASP B  70     149.911  29.445  30.765  1.00 56.56           C  
ANISOU 1337  CA  ASP B  70     7385   7773   6331    -23   -724    185       C  
ATOM   1338  C   ASP B  70     149.333  29.452  32.170  1.00 53.29           C  
ANISOU 1338  C   ASP B  70     6881   7370   5996    -27   -715    213       C  
ATOM   1339  O   ASP B  70     148.228  29.941  32.408  1.00 54.25           O  
ANISOU 1339  O   ASP B  70     6916   7514   6181    -11   -774    282       O  
ATOM   1340  CB  ASP B  70     149.756  30.821  30.116  1.00 57.15           C  
ANISOU 1340  CB  ASP B  70     7489   7849   6376     15   -749    254       C  
ATOM   1341  N   GLY B  71     150.105  28.896  33.096  1.00 48.55           N  
ANISOU 1341  N   GLY B  71     6289   6761   5395    -43   -636    166       N  
ATOM   1342  CA  GLY B  71     149.723  28.827  34.491  1.00 46.23           C  
ANISOU 1342  CA  GLY B  71     5919   6492   5156    -44   -601    182       C  
ATOM   1343  C   GLY B  71     150.594  29.691  35.374  1.00 43.85           C  
ANISOU 1343  C   GLY B  71     5647   6166   4848    -18   -497    177       C  
ATOM   1344  O   GLY B  71     151.262  30.614  34.907  1.00 44.84           O  
ANISOU 1344  O   GLY B  71     5831   6290   4919     -8   -479    192       O  
ATOM   1345  N   VAL B  72     150.583  29.378  36.664  1.00 40.66           N  
ANISOU 1345  N   VAL B  72     5210   5742   4496    -16   -428    155       N  
ATOM   1346  CA  VAL B  72     151.507  29.979  37.613  1.00 37.47           C  
ANISOU 1346  CA  VAL B  72     4843   5323   4072     -9   -338    136       C  
ATOM   1347  C   VAL B  72     151.916  28.942  38.656  1.00 33.36           C  
ANISOU 1347  C   VAL B  72     4321   4803   3552    -26   -298     93       C  
ATOM   1348  O   VAL B  72     151.074  28.212  39.178  1.00 35.08           O  
ANISOU 1348  O   VAL B  72     4494   5005   3829    -29   -298     94       O  
ATOM   1349  CB  VAL B  72     150.879  31.190  38.324  1.00 37.14           C  
ANISOU 1349  CB  VAL B  72     4776   5238   4099     24   -280    174       C  
ATOM   1350  CG1 VAL B  72     151.818  31.718  39.381  1.00 35.70           C  
ANISOU 1350  CG1 VAL B  72     4640   5039   3885     14   -190    144       C  
ATOM   1351  CG2 VAL B  72     150.537  32.282  37.314  1.00 36.53           C  
ANISOU 1351  CG2 VAL B  72     4707   5149   4021     52   -315    228       C  
ATOM   1352  N   ALA B  73     153.210  28.869  38.953  1.00 28.17           N  
ANISOU 1352  N   ALA B  73     3710   4162   2829    -36   -265     60       N  
ATOM   1353  CA  ALA B  73     153.701  27.985  40.004  1.00 25.49           C  
ANISOU 1353  CA  ALA B  73     3376   3817   2490    -41   -231     30       C  
ATOM   1354  C   ALA B  73     153.559  28.686  41.347  1.00 25.28           C  
ANISOU 1354  C   ALA B  73     3351   3771   2481    -39   -166     37       C  
ATOM   1355  O   ALA B  73     153.797  29.889  41.450  1.00 25.59           O  
ANISOU 1355  O   ALA B  73     3410   3802   2512    -39   -133     44       O  
ATOM   1356  CB  ALA B  73     155.149  27.598  39.751  1.00 25.27           C  
ANISOU 1356  CB  ALA B  73     3386   3748   2468    -39   -216     -3       C  
ATOM   1357  N   LEU B  74     153.166  27.939  42.373  1.00 24.22           N  
ANISOU 1357  N   LEU B  74     3211   3618   2373    -40   -139     32       N  
ATOM   1358  CA  LEU B  74     152.981  28.523  43.694  1.00 20.37           C  
ANISOU 1358  CA  LEU B  74     2744   3101   1896    -44    -68     34       C  
ATOM   1359  C   LEU B  74     154.187  28.212  44.570  1.00 22.64           C  
ANISOU 1359  C   LEU B  74     3080   3412   2110    -58    -58      9       C  
ATOM   1360  O   LEU B  74     154.380  27.074  44.992  1.00 23.67           O  
ANISOU 1360  O   LEU B  74     3220   3548   2226    -54    -72      4       O  
ATOM   1361  CB  LEU B  74     151.708  27.978  44.346  1.00 14.65           C  
ANISOU 1361  CB  LEU B  74     1989   2334   1244    -41    -31     49       C  
ATOM   1362  CG  LEU B  74     150.424  28.045  43.515  1.00 13.94           C  
ANISOU 1362  CG  LEU B  74     1825   2228   1243    -29    -57     77       C  
ATOM   1363  CD1 LEU B  74     149.231  27.521  44.311  1.00 12.54           C  
ANISOU 1363  CD1 LEU B  74     1607   2007   1148    -33     -3     87       C  
ATOM   1364  CD2 LEU B  74     150.166  29.462  43.035  1.00 12.69           C  
ANISOU 1364  CD2 LEU B  74     1652   2059   1111     -6    -48    103       C  
ATOM   1365  N   ALA B  75     154.991  29.233  44.848  1.00 23.59           N  
ANISOU 1365  N   ALA B  75     3230   3529   2203    -71    -38     -5       N  
ATOM   1366  CA  ALA B  75     156.202  29.058  45.639  1.00 22.60           C  
ANISOU 1366  CA  ALA B  75     3134   3379   2075    -72    -44    -24       C  
ATOM   1367  C   ALA B  75     155.888  29.019  47.132  1.00 27.08           C  
ANISOU 1367  C   ALA B  75     3745   3930   2612    -84      0    -25       C  
ATOM   1368  O   ALA B  75     156.700  28.556  47.931  1.00 29.28           O  
ANISOU 1368  O   ALA B  75     4048   4202   2878    -77    -20    -31       O  
ATOM   1369  CB  ALA B  75     157.207  30.156  45.326  1.00 17.35           C  
ANISOU 1369  CB  ALA B  75     2474   2710   1411    -85    -42    -41       C  
ATOM   1370  N   ASP B  76     154.708  29.508  47.502  1.00 29.68           N  
ANISOU 1370  N   ASP B  76     4090   4258   2928   -103     65    -16       N  
ATOM   1371  CA  ASP B  76     154.294  29.527  48.902  1.00 35.29           C  
ANISOU 1371  CA  ASP B  76     4861   4934   3614   -122    132    -19       C  
ATOM   1372  C   ASP B  76     154.034  28.117  49.416  1.00 37.52           C  
ANISOU 1372  C   ASP B  76     5155   5216   3886   -114    122     -4       C  
ATOM   1373  O   ASP B  76     154.154  27.844  50.612  1.00 38.83           O  
ANISOU 1373  O   ASP B  76     5373   5355   4025   -116    147     -4       O  
ATOM   1374  CB  ASP B  76     153.054  30.404  49.094  1.00 35.35           C  
ANISOU 1374  CB  ASP B  76     4869   4877   3684   -121    226    -10       C  
ATOM   1375  CG  ASP B  76     151.859  29.912  48.298  1.00 35.68           C  
ANISOU 1375  CG  ASP B  76     4827   4896   3832    -85    221     20       C  
ATOM   1376  OD1 ASP B  76     152.055  29.416  47.167  1.00 37.58           O  
ANISOU 1376  OD1 ASP B  76     5015   5176   4087    -69    141     28       O  
ATOM   1377  OD2 ASP B  76     150.720  30.024  48.800  1.00 35.60           O  
ANISOU 1377  OD2 ASP B  76     4805   4831   3892    -77    300     33       O  
ATOM   1378  N   GLN B  77     153.666  27.227  48.502  1.00 34.24           N  
ANISOU 1378  N   GLN B  77     4680   4806   3524    -88     81     10       N  
ATOM   1379  CA  GLN B  77     153.462  25.831  48.847  1.00 31.05           C  
ANISOU 1379  CA  GLN B  77     4287   4388   3122    -78     73     23       C  
ATOM   1380  C   GLN B  77     154.629  25.001  48.327  1.00 38.09           C  
ANISOU 1380  C   GLN B  77     5173   5328   3973    -58     -8     19       C  
ATOM   1381  O   GLN B  77     154.742  24.755  47.126  1.00 46.19           O  
ANISOU 1381  O   GLN B  77     6149   6372   5027    -45    -51     13       O  
ATOM   1382  CB  GLN B  77     152.147  25.321  48.248  1.00 23.55           C  
ANISOU 1382  CB  GLN B  77     3277   3399   2270    -73     92     35       C  
ATOM   1383  CG  GLN B  77     150.916  26.114  48.658  1.00 20.60           C  
ANISOU 1383  CG  GLN B  77     2883   2976   1968    -81    176     43       C  
ATOM   1384  CD  GLN B  77     149.624  25.443  48.224  1.00 18.78           C  
ANISOU 1384  CD  GLN B  77     2580   2713   1843    -82    190     57       C  
ATOM   1385  OE1 GLN B  77     149.587  24.234  47.986  1.00 16.65           O  
ANISOU 1385  OE1 GLN B  77     2305   2443   1579    -89    158     57       O  
ATOM   1386  NE2 GLN B  77     148.555  26.228  48.117  1.00 19.47           N  
ANISOU 1386  NE2 GLN B  77     2606   2770   2021    -76    240     70       N  
ATOM   1387  N   VAL B  78     155.487  24.559  49.239  1.00 35.20           N  
ANISOU 1387  N   VAL B  78     4853   4941   3579    -40    -24     24       N  
ATOM   1388  CA  VAL B  78     156.605  23.705  48.878  1.00 33.23           C  
ANISOU 1388  CA  VAL B  78     4597   4694   3336    -13    -86     26       C  
ATOM   1389  C   VAL B  78     156.357  22.338  49.485  1.00 30.47           C  
ANISOU 1389  C   VAL B  78     4291   4335   2949      1    -80     53       C  
ATOM   1390  O   VAL B  78     156.393  22.176  50.706  1.00 30.53           O  
ANISOU 1390  O   VAL B  78     4347   4337   2917     15    -60     71       O  
ATOM   1391  CB  VAL B  78     157.943  24.265  49.401  1.00 36.00           C  
ANISOU 1391  CB  VAL B  78     4959   5046   3675    -10   -122     18       C  
ATOM   1392  CG1 VAL B  78     159.092  23.341  49.014  1.00 37.86           C  
ANISOU 1392  CG1 VAL B  78     5167   5302   3916      7   -178     27       C  
ATOM   1393  CG2 VAL B  78     158.174  25.664  48.864  1.00 35.11           C  
ANISOU 1393  CG2 VAL B  78     4811   4941   3588    -29   -115     -7       C  
ATOM   1394  N   LYS B  79     156.084  21.354  48.637  1.00 30.82           N  
ANISOU 1394  N   LYS B  79     4310   4394   3008     18    -91     56       N  
ATOM   1395  CA  LYS B  79     155.655  20.051  49.130  1.00 33.22           C  
ANISOU 1395  CA  LYS B  79     4661   4651   3311     34    -66     80       C  
ATOM   1396  C   LYS B  79     156.706  18.972  48.897  1.00 28.06           C  
ANISOU 1396  C   LYS B  79     4017   4005   2639     86   -110     94       C  
ATOM   1397  O   LYS B  79     157.185  18.789  47.774  1.00 29.44           O  
ANISOU 1397  O   LYS B  79     4146   4201   2840    104   -140     73       O  
ATOM   1398  CB  LYS B  79     154.320  19.652  48.484  1.00 38.13           C  
ANISOU 1398  CB  LYS B  79     5254   5219   4014      6    -26     68       C  
ATOM   1399  CG  LYS B  79     153.379  20.827  48.249  1.00 42.99           C  
ANISOU 1399  CG  LYS B  79     5821   5838   4674    -30      2     54       C  
ATOM   1400  CD  LYS B  79     152.015  20.619  48.891  1.00 47.70           C  
ANISOU 1400  CD  LYS B  79     6424   6372   5327    -61     80     64       C  
ATOM   1401  CE  LYS B  79     151.270  19.434  48.284  1.00 49.40           C  
ANISOU 1401  CE  LYS B  79     6617   6544   5608    -77     84     59       C  
ATOM   1402  NZ  LYS B  79     149.861  19.361  48.787  1.00 49.25           N  
ANISOU 1402  NZ  LYS B  79     6577   6471   5666   -116    164     65       N  
ATOM   1403  N   SER B  80     157.062  18.262  49.962  1.00 24.23           N  
ANISOU 1403  N   SER B  80     3599   3499   2109    113   -110    133       N  
ATOM   1404  CA  SER B  80     157.935  17.116  49.816  1.00 27.13           C  
ANISOU 1404  CA  SER B  80     3978   3856   2473    176   -142    158       C  
ATOM   1405  C   SER B  80     157.065  15.883  49.629  1.00 31.62           C  
ANISOU 1405  C   SER B  80     4591   4334   3090    175    -87    164       C  
ATOM   1406  O   SER B  80     156.378  15.440  50.551  1.00 33.55           O  
ANISOU 1406  O   SER B  80     4906   4520   3320    159    -40    192       O  
ATOM   1407  CB  SER B  80     158.849  16.946  51.032  1.00 24.53           C  
ANISOU 1407  CB  SER B  80     3681   3544   2094    202   -181    204       C  
ATOM   1408  OG  SER B  80     159.851  15.959  50.771  1.00 21.57           O  
ANISOU 1408  OG  SER B  80     3305   3174   1717    285   -221    234       O  
ATOM   1409  N   ILE B  81     157.106  15.337  48.419  1.00 31.89           N  
ANISOU 1409  N   ILE B  81     4590   4351   3175    184    -89    133       N  
ATOM   1410  CA  ILE B  81     156.266  14.212  48.050  1.00 33.87           C  
ANISOU 1410  CA  ILE B  81     4879   4515   3476    167    -39    124       C  
ATOM   1411  C   ILE B  81     157.096  13.052  47.553  1.00 34.52           C  
ANISOU 1411  C   ILE B  81     4986   4559   3569    229    -42    130       C  
ATOM   1412  O   ILE B  81     158.271  13.211  47.212  1.00 33.88           O  
ANISOU 1412  O   ILE B  81     4869   4529   3474    284    -82    132       O  
ATOM   1413  CB  ILE B  81     155.283  14.582  46.923  1.00 34.10           C  
ANISOU 1413  CB  ILE B  81     4854   4545   3559    101    -31     71       C  
ATOM   1414  CG1 ILE B  81     156.052  15.011  45.672  1.00 34.23           C  
ANISOU 1414  CG1 ILE B  81     4816   4618   3573    116    -78     35       C  
ATOM   1415  CG2 ILE B  81     154.321  15.676  47.377  1.00 34.09           C  
ANISOU 1415  CG2 ILE B  81     4819   4565   3568     48    -15     70       C  
ATOM   1416  CD1 ILE B  81     155.174  15.272  44.472  1.00 34.92           C  
ANISOU 1416  CD1 ILE B  81     4864   4707   3698     56    -86    -10       C  
ATOM   1417  N   ALA B  82     156.465  11.885  47.503  1.00 35.37           N  
ANISOU 1417  N   ALA B  82     5156   4573   3711    217     11    130       N  
ATOM   1418  CA  ALA B  82     157.079  10.729  46.879  1.00 36.16           C  
ANISOU 1418  CA  ALA B  82     5291   4615   3833    268     29    125       C  
ATOM   1419  C   ALA B  82     156.624  10.713  45.431  1.00 37.85           C  
ANISOU 1419  C   ALA B  82     5472   4824   4084    212     35     53       C  
ATOM   1420  O   ALA B  82     155.469  10.413  45.131  1.00 36.29           O  
ANISOU 1420  O   ALA B  82     5291   4580   3920    135     64     21       O  
ATOM   1421  CB  ALA B  82     156.662   9.459  47.584  1.00 35.82           C  
ANISOU 1421  CB  ALA B  82     5349   4461   3802    279     90    162       C  
ATOM   1422  N   TRP B  83     157.553  11.026  44.538  1.00 40.44           N  
ANISOU 1422  N   TRP B  83     5758   5203   4405    247      6     26       N  
ATOM   1423  CA  TRP B  83     157.258  11.121  43.121  1.00 40.12           C  
ANISOU 1423  CA  TRP B  83     5699   5167   4377    194      4    -41       C  
ATOM   1424  C   TRP B  83     157.211   9.726  42.512  1.00 40.29           C  
ANISOU 1424  C   TRP B  83     5799   5087   4424    196     60    -71       C  
ATOM   1425  O   TRP B  83     156.419   9.455  41.609  1.00 41.59           O  
ANISOU 1425  O   TRP B  83     5984   5219   4598    118     68   -127       O  
ATOM   1426  CB  TRP B  83     158.323  11.974  42.438  1.00 37.97           C  
ANISOU 1426  CB  TRP B  83     5365   4979   4080    229    -30    -56       C  
ATOM   1427  CG  TRP B  83     159.705  11.484  42.709  1.00 34.98           C  
ANISOU 1427  CG  TRP B  83     4986   4600   3706    330    -17    -26       C  
ATOM   1428  CD1 TRP B  83     160.521  11.848  43.741  1.00 33.54           C  
ANISOU 1428  CD1 TRP B  83     4767   4467   3510    393    -50     31       C  
ATOM   1429  CD2 TRP B  83     160.433  10.523  41.943  1.00 36.21           C  
ANISOU 1429  CD2 TRP B  83     5174   4699   3884    382     32    -49       C  
ATOM   1430  NE1 TRP B  83     161.715  11.179  43.659  1.00 35.83           N  
ANISOU 1430  NE1 TRP B  83     5048   4743   3822    486    -34     51       N  
ATOM   1431  CE2 TRP B  83     161.685  10.356  42.563  1.00 38.89           C  
ANISOU 1431  CE2 TRP B  83     5479   5060   4237    485     26      3       C  
ATOM   1432  CE3 TRP B  83     160.147   9.789  40.789  1.00 36.05           C  
ANISOU 1432  CE3 TRP B  83     5212   4610   3873    348     83   -109       C  
ATOM   1433  CZ2 TRP B  83     162.651   9.481  42.068  1.00 41.75           C  
ANISOU 1433  CZ2 TRP B  83     5852   5373   4637    568     79     -1       C  
ATOM   1434  CZ3 TRP B  83     161.104   8.926  40.299  1.00 38.06           C  
ANISOU 1434  CZ3 TRP B  83     5498   4811   4153    421    143   -120       C  
ATOM   1435  CH2 TRP B  83     162.342   8.779  40.934  1.00 40.80           C  
ANISOU 1435  CH2 TRP B  83     5798   5177   4528    536    146    -64       C  
ATOM   1436  N   ARG B  84     158.068   8.844  43.015  1.00 37.80           N  
ANISOU 1436  N   ARG B  84     5528   4716   4117    285     96    -32       N  
ATOM   1437  CA  ARG B  84     158.115   7.465  42.546  1.00 35.37           C  
ANISOU 1437  CA  ARG B  84     5309   4293   3836    300    166    -55       C  
ATOM   1438  C   ARG B  84     156.818   6.733  42.864  1.00 33.48           C  
ANISOU 1438  C   ARG B  84     5137   3963   3619    218    205    -65       C  
ATOM   1439  O   ARG B  84     156.278   6.016  42.021  1.00 35.00           O  
ANISOU 1439  O   ARG B  84     5384   4085   3828    153    243   -126       O  
ATOM   1440  CB  ARG B  84     159.298   6.723  43.169  1.00 36.21           C  
ANISOU 1440  CB  ARG B  84     5444   4358   3958    428    195      6       C  
ATOM   1441  CG  ARG B  84     160.348   6.294  42.160  1.00 37.95           C  
ANISOU 1441  CG  ARG B  84     5663   4556   4198    493    235    -28       C  
ATOM   1442  CD  ARG B  84     161.125   5.080  42.638  1.00 40.26           C  
ANISOU 1442  CD  ARG B  84     6017   4751   4531    610    294     25       C  
ATOM   1443  NE  ARG B  84     161.971   5.376  43.790  1.00 41.80           N  
ANISOU 1443  NE  ARG B  84     6155   5004   4724    711    240    117       N  
ATOM   1444  CZ  ARG B  84     163.208   5.852  43.702  1.00 44.71           C  
ANISOU 1444  CZ  ARG B  84     6429   5453   5107    796    206    140       C  
ATOM   1445  NH1 ARG B  84     163.743   6.098  42.514  1.00 44.63           N  
ANISOU 1445  NH1 ARG B  84     6375   5467   5114    794    238     76       N  
ATOM   1446  NH2 ARG B  84     163.910   6.090  44.802  1.00 48.81           N  
ANISOU 1446  NH2 ARG B  84     6898   6028   5619    877    141    225       N  
ATOM   1447  N   ALA B  85     156.321   6.929  44.082  1.00 31.93           N  
ANISOU 1447  N   ALA B  85     4942   3771   3421    213    200     -9       N  
ATOM   1448  CA  ALA B  85     155.088   6.288  44.530  1.00 30.52           C  
ANISOU 1448  CA  ALA B  85     4819   3506   3269    133    249    -12       C  
ATOM   1449  C   ALA B  85     153.868   6.795  43.762  1.00 32.06           C  
ANISOU 1449  C   ALA B  85     4960   3735   3487      8    225    -78       C  
ATOM   1450  O   ALA B  85     152.989   6.014  43.386  1.00 34.43           O  
ANISOU 1450  O   ALA B  85     5302   3956   3822    -76    264   -120       O  
ATOM   1451  CB  ALA B  85     154.899   6.496  46.019  1.00 27.49           C  
ANISOU 1451  CB  ALA B  85     4452   3124   2868    158    257     64       C  
ATOM   1452  N   ARG B  86     153.826   8.104  43.528  1.00 32.42           N  
ANISOU 1452  N   ARG B  86     4910   3893   3514     -6    156    -84       N  
ATOM   1453  CA  ARG B  86     152.714   8.724  42.811  1.00 34.80           C  
ANISOU 1453  CA  ARG B  86     5145   4239   3840   -109    117   -132       C  
ATOM   1454  C   ARG B  86     152.882   8.595  41.298  1.00 34.08           C  
ANISOU 1454  C   ARG B  86     5058   4159   3733   -145     84   -200       C  
ATOM   1455  O   ARG B  86     151.990   8.955  40.527  1.00 32.86           O  
ANISOU 1455  O   ARG B  86     4860   4036   3591   -233     38   -242       O  
ATOM   1456  CB  ARG B  86     152.589  10.203  43.184  1.00 36.97           C  
ANISOU 1456  CB  ARG B  86     5325   4618   4102   -102     65   -105       C  
ATOM   1457  CG  ARG B  86     152.479  10.467  44.667  1.00 38.49           C  
ANISOU 1457  CG  ARG B  86     5526   4807   4294    -72     98    -43       C  
ATOM   1458  CD  ARG B  86     152.412  11.952  44.969  1.00 40.94           C  
ANISOU 1458  CD  ARG B  86     5756   5211   4588    -67     57    -26       C  
ATOM   1459  NE  ARG B  86     152.501  12.200  46.405  1.00 43.50           N  
ANISOU 1459  NE  ARG B  86     6111   5530   4889    -35     92     28       N  
ATOM   1460  CZ  ARG B  86     151.453  12.314  47.214  1.00 43.99           C  
ANISOU 1460  CZ  ARG B  86     6172   5561   4983    -83    144     44       C  
ATOM   1461  NH1 ARG B  86     150.223  12.210  46.725  1.00 41.92           N  
ANISOU 1461  NH1 ARG B  86     5860   5275   4793   -162    162     12       N  
ATOM   1462  NH2 ARG B  86     151.637  12.536  48.511  1.00 45.58           N  
ANISOU 1462  NH2 ARG B  86     6421   5754   5141    -54    180     91       N  
ATOM   1463  N   GLY B  87     154.036   8.090  40.878  1.00 36.04           N  
ANISOU 1463  N   GLY B  87     5360   4381   3951    -74    109   -209       N  
ATOM   1464  CA  GLY B  87     154.325   7.944  39.465  1.00 36.90           C  
ANISOU 1464  CA  GLY B  87     5495   4492   4031   -103     96   -276       C  
ATOM   1465  C   GLY B  87     154.429   9.283  38.760  1.00 36.49           C  
ANISOU 1465  C   GLY B  87     5366   4556   3943   -117     20   -287       C  
ATOM   1466  O   GLY B  87     153.829   9.491  37.707  1.00 38.33           O  
ANISOU 1466  O   GLY B  87     5597   4811   4156   -198    -24   -338       O  
ATOM   1467  N   ALA B  88     155.193  10.196  39.350  1.00 34.44           N  
ANISOU 1467  N   ALA B  88     5048   4368   3670    -42      2   -239       N  
ATOM   1468  CA  ALA B  88     155.397  11.519  38.776  1.00 31.24           C  
ANISOU 1468  CA  ALA B  88     4577   4064   3231    -48    -58   -243       C  
ATOM   1469  C   ALA B  88     156.053  11.410  37.404  1.00 29.73           C  
ANISOU 1469  C   ALA B  88     4426   3876   2994    -53    -52   -296       C  
ATOM   1470  O   ALA B  88     157.101  10.787  37.253  1.00 29.67           O  
ANISOU 1470  O   ALA B  88     4461   3832   2981     11      4   -305       O  
ATOM   1471  CB  ALA B  88     156.249  12.364  39.705  1.00 30.59           C  
ANISOU 1471  CB  ALA B  88     4439   4042   3141     30    -65   -188       C  
ATOM   1472  N   THR B  89     155.437  12.027  36.406  1.00 29.32           N  
ANISOU 1472  N   THR B  89     4363   3867   2908   -125   -109   -329       N  
ATOM   1473  CA  THR B  89     155.943  11.944  35.046  1.00 27.25           C  
ANISOU 1473  CA  THR B  89     4161   3607   2587   -145   -102   -384       C  
ATOM   1474  C   THR B  89     156.470  13.300  34.582  1.00 26.69           C  
ANISOU 1474  C   THR B  89     4043   3626   2472   -127   -138   -368       C  
ATOM   1475  O   THR B  89     155.914  14.340  34.930  1.00 25.01           O  
ANISOU 1475  O   THR B  89     3760   3474   2270   -142   -196   -332       O  
ATOM   1476  CB  THR B  89     154.852  11.423  34.082  1.00 30.52           C  
ANISOU 1476  CB  THR B  89     4632   3989   2976   -256   -141   -440       C  
ATOM   1477  OG1 THR B  89     153.727  12.310  34.097  1.00 33.31           O  
ANISOU 1477  OG1 THR B  89     4910   4406   3342   -315   -233   -417       O  
ATOM   1478  CG2 THR B  89     154.392  10.035  34.504  1.00 30.64           C  
ANISOU 1478  CG2 THR B  89     4705   3902   3036   -284    -90   -463       C  
ATOM   1479  N   LYS B  90     157.518  13.285  33.766  1.00 29.36           N  
ANISOU 1479  N   LYS B  90     4424   3965   2765    -99    -92   -398       N  
ATOM   1480  CA  LYS B  90     158.157  14.519  33.326  1.00 30.35           C  
ANISOU 1480  CA  LYS B  90     4513   4167   2850    -82   -107   -385       C  
ATOM   1481  C   LYS B  90     157.306  15.218  32.269  1.00 29.91           C  
ANISOU 1481  C   LYS B  90     4463   4147   2754   -155   -178   -395       C  
ATOM   1482  O   LYS B  90     156.986  14.633  31.237  1.00 29.98           O  
ANISOU 1482  O   LYS B  90     4534   4120   2735   -203   -180   -438       O  
ATOM   1483  CB  LYS B  90     159.535  14.198  32.740  1.00 31.56           C  
ANISOU 1483  CB  LYS B  90     4706   4302   2982    -31    -18   -416       C  
ATOM   1484  CG  LYS B  90     160.334  15.399  32.259  1.00 31.14           C  
ANISOU 1484  CG  LYS B  90     4621   4320   2893    -18    -12   -407       C  
ATOM   1485  CD  LYS B  90     161.533  14.940  31.443  1.00 33.09           C  
ANISOU 1485  CD  LYS B  90     4917   4536   3118     16     90   -450       C  
ATOM   1486  CE  LYS B  90     162.589  16.024  31.346  1.00 33.93           C  
ANISOU 1486  CE  LYS B  90     4961   4708   3221     47    121   -433       C  
ATOM   1487  NZ  LYS B  90     162.012  17.335  30.943  1.00 33.32           N  
ANISOU 1487  NZ  LYS B  90     4844   4691   3123     -4     47   -404       N  
ATOM   1488  N   LYS B  91     156.892  16.452  32.565  1.00 28.52           N  
ANISOU 1488  N   LYS B  91     4199   4028   2610   -145   -233   -345       N  
ATOM   1489  CA  LYS B  91     156.159  17.274  31.599  1.00 28.58           C  
ANISOU 1489  CA  LYS B  91     4184   4059   2617   -173   -294   -331       C  
ATOM   1490  C   LYS B  91     157.024  18.272  30.822  1.00 29.45           C  
ANISOU 1490  C   LYS B  91     4289   4196   2704   -136   -269   -320       C  
ATOM   1491  O   LYS B  91     156.561  18.878  29.857  1.00 31.46           O  
ANISOU 1491  O   LYS B  91     4551   4462   2941   -155   -309   -312       O  
ATOM   1492  CB  LYS B  91     155.013  18.025  32.293  1.00 30.44           C  
ANISOU 1492  CB  LYS B  91     4346   4317   2904   -183   -363   -284       C  
ATOM   1493  CG  LYS B  91     153.719  18.071  31.485  1.00 34.59           C  
ANISOU 1493  CG  LYS B  91     4867   4846   3430   -243   -444   -286       C  
ATOM   1494  CD  LYS B  91     152.798  19.200  31.940  1.00 39.04           C  
ANISOU 1494  CD  LYS B  91     5350   5440   4042   -235   -502   -232       C  
ATOM   1495  CE  LYS B  91     153.333  20.559  31.509  1.00 42.43           C  
ANISOU 1495  CE  LYS B  91     5769   5888   4464   -180   -491   -199       C  
ATOM   1496  NZ  LYS B  91     152.380  21.671  31.793  1.00 43.71           N  
ANISOU 1496  NZ  LYS B  91     5869   6071   4667   -175   -545   -148       N  
ATOM   1497  N   GLY B  92     158.266  18.464  31.252  1.00 28.49           N  
ANISOU 1497  N   GLY B  92     4158   4085   2580    -86   -205   -318       N  
ATOM   1498  CA  GLY B  92     159.096  19.500  30.661  1.00 28.50           C  
ANISOU 1498  CA  GLY B  92     4158   4106   2566    -60   -178   -304       C  
ATOM   1499  C   GLY B  92     160.135  20.070  31.610  1.00 27.32           C  
ANISOU 1499  C   GLY B  92     3990   3950   2442    -22   -137   -276       C  
ATOM   1500  O   GLY B  92     160.570  19.403  32.545  1.00 25.45           O  
ANISOU 1500  O   GLY B  92     3743   3709   2216    -21   -108   -279       O  
ATOM   1501  N   THR B  93     160.546  21.307  31.354  1.00 29.29           N  
ANISOU 1501  N   THR B  93     4232   4203   2696    -21   -130   -249       N  
ATOM   1502  CA  THR B  93     161.484  21.998  32.230  1.00 29.90           C  
ANISOU 1502  CA  THR B  93     4257   4298   2806    -26    -92   -227       C  
ATOM   1503  C   THR B  93     161.082  23.459  32.378  1.00 29.62           C  
ANISOU 1503  C   THR B  93     4197   4259   2800    -33   -123   -187       C  
ATOM   1504  O   THR B  93     160.501  24.043  31.465  1.00 31.23           O  
ANISOU 1504  O   THR B  93     4434   4452   2979    -29   -150   -179       O  
ATOM   1505  CB  THR B  93     162.920  21.938  31.674  1.00 30.00           C  
ANISOU 1505  CB  THR B  93     4275   4339   2783    -17     -7   -260       C  
ATOM   1506  OG1 THR B  93     163.157  20.651  31.088  1.00 28.50           O  
ANISOU 1506  OG1 THR B  93     4141   4138   2551     -4     37   -309       O  
ATOM   1507  CG2 THR B  93     163.928  22.188  32.787  1.00 31.31           C  
ANISOU 1507  CG2 THR B  93     4340   4571   2987      6     21   -256       C  
ATOM   1508  N   VAL B  94     161.381  24.045  33.533  1.00 29.26           N  
ANISOU 1508  N   VAL B  94     4083   4235   2799    -33   -119   -165       N  
ATOM   1509  CA  VAL B  94     161.154  25.469  33.735  1.00 31.26           C  
ANISOU 1509  CA  VAL B  94     4320   4484   3073    -40   -129   -137       C  
ATOM   1510  C   VAL B  94     162.453  26.223  33.483  1.00 32.76           C  
ANISOU 1510  C   VAL B  94     4495   4707   3245    -49    -73   -149       C  
ATOM   1511  O   VAL B  94     163.536  25.732  33.810  1.00 35.05           O  
ANISOU 1511  O   VAL B  94     4742   5043   3532    -43    -35   -172       O  
ATOM   1512  CB  VAL B  94     160.654  25.774  35.159  1.00 29.50           C  
ANISOU 1512  CB  VAL B  94     4043   4264   2902    -37   -151   -114       C  
ATOM   1513  CG1 VAL B  94     159.403  24.959  35.473  1.00 30.88           C  
ANISOU 1513  CG1 VAL B  94     4221   4418   3093    -34   -194   -106       C  
ATOM   1514  CG2 VAL B  94     161.743  25.491  36.182  1.00 28.46           C  
ANISOU 1514  CG2 VAL B  94     3855   4175   2785    -27   -126   -124       C  
ATOM   1515  N   ALA B  95     162.343  27.410  32.894  1.00 32.13           N  
ANISOU 1515  N   ALA B  95     4444   4616   3147    -59    -66   -133       N  
ATOM   1516  CA  ALA B  95     163.510  28.244  32.640  1.00 31.62           C  
ANISOU 1516  CA  ALA B  95     4368   4583   3063    -78     -6   -144       C  
ATOM   1517  C   ALA B  95     164.249  28.498  33.946  1.00 30.54           C  
ANISOU 1517  C   ALA B  95     4147   4493   2963    -91      5   -151       C  
ATOM   1518  O   ALA B  95     163.632  28.611  35.001  1.00 29.85           O  
ANISOU 1518  O   ALA B  95     4033   4396   2913    -84    -33   -134       O  
ATOM   1519  CB  ALA B  95     163.099  29.555  31.994  1.00 31.55           C  
ANISOU 1519  CB  ALA B  95     4403   4554   3030    -85     -4   -119       C  
ATOM   1520  N   PRO B  96     165.583  28.586  33.878  1.00 31.85           N  
ANISOU 1520  N   PRO B  96     4269   4719   3114   -110     60   -180       N  
ATOM   1521  CA  PRO B  96     166.425  28.758  35.068  1.00 31.19           C  
ANISOU 1521  CA  PRO B  96     4093   4706   3050   -123     60   -194       C  
ATOM   1522  C   PRO B  96     165.979  29.925  35.943  1.00 31.42           C  
ANISOU 1522  C   PRO B  96     4120   4716   3103   -149     35   -173       C  
ATOM   1523  O   PRO B  96     165.925  29.770  37.160  1.00 34.12           O  
ANISOU 1523  O   PRO B  96     4419   5078   3468   -144     -1   -168       O  
ATOM   1524  CB  PRO B  96     167.809  29.045  34.477  1.00 33.47           C  
ANISOU 1524  CB  PRO B  96     4343   5063   3311   -155    138   -231       C  
ATOM   1525  CG  PRO B  96     167.799  28.348  33.157  1.00 34.92           C  
ANISOU 1525  CG  PRO B  96     4592   5211   3466   -135    183   -243       C  
ATOM   1526  CD  PRO B  96     166.380  28.507  32.642  1.00 34.09           C  
ANISOU 1526  CD  PRO B  96     4586   5012   3354   -122    130   -205       C  
ATOM   1527  N   GLU B  97     165.661  31.063  35.330  1.00 32.50           N  
ANISOU 1527  N   GLU B  97     4312   4812   3225   -174     59   -160       N  
ATOM   1528  CA  GLU B  97     165.265  32.254  36.075  1.00 33.84           C  
ANISOU 1528  CA  GLU B  97     4490   4963   3406   -199     54   -146       C  
ATOM   1529  C   GLU B  97     163.953  32.053  36.818  1.00 36.22           C  
ANISOU 1529  C   GLU B  97     4809   5219   3737   -163      4   -119       C  
ATOM   1530  O   GLU B  97     163.687  32.724  37.812  1.00 37.92           O  
ANISOU 1530  O   GLU B  97     5017   5427   3963   -178      1   -115       O  
ATOM   1531  CB  GLU B  97     165.142  33.460  35.142  1.00 35.37           C  
ANISOU 1531  CB  GLU B  97     4747   5123   3569   -223     97   -133       C  
ATOM   1532  CG  GLU B  97     166.301  33.624  34.174  1.00 36.90           C  
ANISOU 1532  CG  GLU B  97     4943   5345   3731   -260    163   -157       C  
ATOM   1533  CD  GLU B  97     166.127  32.804  32.908  1.00 36.89           C  
ANISOU 1533  CD  GLU B  97     4990   5322   3703   -223    168   -152       C  
ATOM   1534  OE1 GLU B  97     167.107  32.658  32.148  1.00 32.87           O  
ANISOU 1534  OE1 GLU B  97     4482   4837   3171   -246    232   -177       O  
ATOM   1535  OE2 GLU B  97     165.006  32.313  32.663  1.00 40.64           O  
ANISOU 1535  OE2 GLU B  97     5505   5759   4179   -175    114   -126       O  
ATOM   1536  N   GLU B  98     163.119  31.147  36.320  1.00 37.49           N  
ANISOU 1536  N   GLU B  98     4994   5348   3903   -123    -27   -104       N  
ATOM   1537  CA  GLU B  98     161.853  30.852  36.978  1.00 37.94           C  
ANISOU 1537  CA  GLU B  98     5057   5372   3986    -98    -67    -83       C  
ATOM   1538  C   GLU B  98     162.086  30.058  38.253  1.00 36.00           C  
ANISOU 1538  C   GLU B  98     4765   5143   3768    -91    -84    -92       C  
ATOM   1539  O   GLU B  98     161.591  30.414  39.325  1.00 35.33           O  
ANISOU 1539  O   GLU B  98     4678   5049   3698    -94    -89    -84       O  
ATOM   1540  CB  GLU B  98     160.925  30.097  36.033  1.00 36.56           C  
ANISOU 1540  CB  GLU B  98     4917   5169   3804    -73   -100    -71       C  
ATOM   1541  CG  GLU B  98     160.541  30.899  34.815  1.00 39.91           C  
ANISOU 1541  CG  GLU B  98     5396   5580   4190    -72    -98    -54       C  
ATOM   1542  CD  GLU B  98     159.726  30.090  33.830  1.00 45.36           C  
ANISOU 1542  CD  GLU B  98     6119   6253   4862    -53   -143    -47       C  
ATOM   1543  OE1 GLU B  98     160.063  28.905  33.607  1.00 47.67           O  
ANISOU 1543  OE1 GLU B  98     6411   6545   5155    -50   -146    -71       O  
ATOM   1544  OE2 GLU B  98     158.746  30.641  33.285  1.00 45.85           O  
ANISOU 1544  OE2 GLU B  98     6208   6310   4905    -43   -176    -19       O  
ATOM   1545  N   LEU B  99     162.847  28.979  38.124  1.00 32.12           N  
ANISOU 1545  N   LEU B  99     4246   4683   3275    -80    -88   -108       N  
ATOM   1546  CA  LEU B  99     163.244  28.190  39.277  1.00 28.84           C  
ANISOU 1546  CA  LEU B  99     3788   4296   2873    -68   -107   -111       C  
ATOM   1547  C   LEU B  99     163.976  29.067  40.284  1.00 30.33           C  
ANISOU 1547  C   LEU B  99     3945   4522   3057    -98   -103   -119       C  
ATOM   1548  O   LEU B  99     163.824  28.895  41.492  1.00 31.20           O  
ANISOU 1548  O   LEU B  99     4050   4630   3175    -95   -125   -112       O  
ATOM   1549  CB  LEU B  99     164.122  27.017  38.841  1.00 27.05           C  
ANISOU 1549  CB  LEU B  99     3530   4119   2630    -44   -104   -129       C  
ATOM   1550  CG  LEU B  99     164.938  26.323  39.927  1.00 27.99           C  
ANISOU 1550  CG  LEU B  99     3590   4300   2746    -22   -127   -131       C  
ATOM   1551  CD1 LEU B  99     164.475  24.893  40.133  1.00 25.30           C  
ANISOU 1551  CD1 LEU B  99     3263   3942   2406     24   -147   -121       C  
ATOM   1552  CD2 LEU B  99     166.412  26.365  39.561  1.00 29.88           C  
ANISOU 1552  CD2 LEU B  99     3759   4641   2953    -23   -108   -160       C  
ATOM   1553  N   GLN B 100     164.750  30.023  39.779  1.00 29.86           N  
ANISOU 1553  N   GLN B 100     3873   4495   2978   -136    -73   -137       N  
ATOM   1554  CA  GLN B 100     165.514  30.929  40.633  1.00 27.77           C  
ANISOU 1554  CA  GLN B 100     3577   4273   2700   -185    -69   -153       C  
ATOM   1555  C   GLN B 100     164.615  31.898  41.401  1.00 28.85           C  
ANISOU 1555  C   GLN B 100     3766   4354   2843   -201    -63   -142       C  
ATOM   1556  O   GLN B 100     164.804  32.115  42.602  1.00 30.63           O  
ANISOU 1556  O   GLN B 100     3984   4591   3061   -223    -79   -149       O  
ATOM   1557  CB  GLN B 100     166.546  31.707  39.811  1.00 21.20           C  
ANISOU 1557  CB  GLN B 100     2722   3493   1841   -236    -25   -181       C  
ATOM   1558  N   LEU B 101     163.649  32.488  40.704  1.00 25.07           N  
ANISOU 1558  N   LEU B 101     3339   3820   2366   -190    -40   -126       N  
ATOM   1559  CA  LEU B 101     162.693  33.376  41.350  1.00 23.27           C  
ANISOU 1559  CA  LEU B 101     3155   3550   2136   -197    -24   -115       C  
ATOM   1560  C   LEU B 101     161.922  32.599  42.410  1.00 26.70           C  
ANISOU 1560  C   LEU B 101     3593   3966   2586   -166    -50   -104       C  
ATOM   1561  O   LEU B 101     161.671  33.101  43.506  1.00 31.40           O  
ANISOU 1561  O   LEU B 101     4210   4551   3170   -185    -38   -110       O  
ATOM   1562  CB  LEU B 101     161.724  33.977  40.327  1.00 19.01           C  
ANISOU 1562  CB  LEU B 101     2661   2973   1589   -179     -4    -91       C  
ATOM   1563  CG  LEU B 101     160.663  34.942  40.874  1.00 13.81           C  
ANISOU 1563  CG  LEU B 101     2045   2284    919   -183     25    -76       C  
ATOM   1564  CD1 LEU B 101     161.328  36.152  41.520  1.00 12.57           C  
ANISOU 1564  CD1 LEU B 101     1909   2123    743   -243     71   -101       C  
ATOM   1565  CD2 LEU B 101     159.705  35.371  39.778  1.00 11.18           C  
ANISOU 1565  CD2 LEU B 101     1748   1933    568   -159     30    -40       C  
ATOM   1566  N   ILE B 102     161.541  31.372  42.071  1.00 25.91           N  
ANISOU 1566  N   ILE B 102     3481   3859   2505   -126    -79    -91       N  
ATOM   1567  CA  ILE B 102     160.836  30.508  43.009  1.00 27.40           C  
ANISOU 1567  CA  ILE B 102     3677   4032   2704   -103    -97    -80       C  
ATOM   1568  C   ILE B 102     161.672  30.280  44.262  1.00 27.38           C  
ANISOU 1568  C   ILE B 102     3664   4052   2687   -117   -113    -90       C  
ATOM   1569  O   ILE B 102     161.193  30.480  45.376  1.00 28.33           O  
ANISOU 1569  O   ILE B 102     3815   4156   2793   -123   -105    -88       O  
ATOM   1570  CB  ILE B 102     160.474  29.155  42.367  1.00 28.03           C  
ANISOU 1570  CB  ILE B 102     3744   4104   2800    -71   -122    -69       C  
ATOM   1571  CG1 ILE B 102     159.428  29.361  41.272  1.00 26.94           C  
ANISOU 1571  CG1 ILE B 102     3622   3947   2667    -63   -122    -56       C  
ATOM   1572  CG2 ILE B 102     159.958  28.186  43.417  1.00 26.70           C  
ANISOU 1572  CG2 ILE B 102     3586   3926   2635    -55   -136    -59       C  
ATOM   1573  CD1 ILE B 102     159.061  28.101  40.530  1.00 26.93           C  
ANISOU 1573  CD1 ILE B 102     3618   3940   2675    -44   -149    -54       C  
ATOM   1574  N   LYS B 103     162.920  29.865  44.070  1.00 26.61           N  
ANISOU 1574  N   LYS B 103     3522   4003   2585   -122   -135   -101       N  
ATOM   1575  CA  LYS B 103     163.856  29.694  45.173  1.00 24.27           C  
ANISOU 1575  CA  LYS B 103     3205   3750   2267   -138   -166   -108       C  
ATOM   1576  C   LYS B 103     163.892  30.944  46.039  1.00 21.71           C  
ANISOU 1576  C   LYS B 103     2910   3421   1917   -188   -150   -124       C  
ATOM   1577  O   LYS B 103     163.839  30.863  47.266  1.00 19.27           O  
ANISOU 1577  O   LYS B 103     2631   3106   1584   -194   -169   -123       O  
ATOM   1578  CB  LYS B 103     165.259  29.412  44.639  1.00 24.24           C  
ANISOU 1578  CB  LYS B 103     3127   3827   2255   -146   -186   -122       C  
ATOM   1579  CG  LYS B 103     165.410  28.090  43.908  1.00 25.30           C  
ANISOU 1579  CG  LYS B 103     3231   3982   2402    -94   -197   -112       C  
ATOM   1580  CD  LYS B 103     165.427  26.922  44.873  1.00 25.81           C  
ANISOU 1580  CD  LYS B 103     3297   4051   2460    -54   -240    -89       C  
ATOM   1581  CE  LYS B 103     165.735  25.622  44.147  1.00 27.36           C  
ANISOU 1581  CE  LYS B 103     3457   4280   2658      2   -247    -82       C  
ATOM   1582  NZ  LYS B 103     167.032  25.694  43.412  1.00 28.49           N  
ANISOU 1582  NZ  LYS B 103     3515   4523   2785      7   -246   -105       N  
ATOM   1583  N   ALA B 104     163.982  32.100  45.388  1.00 21.95           N  
ANISOU 1583  N   ALA B 104     2943   3451   1946   -226   -113   -141       N  
ATOM   1584  CA  ALA B 104     164.064  33.375  46.089  1.00 24.93           C  
ANISOU 1584  CA  ALA B 104     3355   3821   2296   -286    -86   -163       C  
ATOM   1585  C   ALA B 104     162.845  33.611  46.973  1.00 28.47           C  
ANISOU 1585  C   ALA B 104     3870   4213   2736   -271    -60   -154       C  
ATOM   1586  O   ALA B 104     162.975  33.861  48.169  1.00 34.23           O  
ANISOU 1586  O   ALA B 104     4629   4941   3434   -301    -64   -167       O  
ATOM   1587  CB  ALA B 104     164.228  34.515  45.090  1.00 25.62           C  
ANISOU 1587  CB  ALA B 104     3447   3904   2382   -326    -39   -178       C  
ATOM   1588  N   LYS B 105     161.661  33.533  46.376  1.00 25.87           N  
ANISOU 1588  N   LYS B 105     3560   3843   2428   -231    -31   -133       N  
ATOM   1589  CA  LYS B 105     160.425  33.749  47.114  1.00 24.12           C  
ANISOU 1589  CA  LYS B 105     3387   3580   2197   -220      8   -125       C  
ATOM   1590  C   LYS B 105     160.289  32.778  48.286  1.00 21.94           C  
ANISOU 1590  C   LYS B 105     3126   3305   1906   -201    -16   -118       C  
ATOM   1591  O   LYS B 105     159.991  33.186  49.410  1.00 20.14           O  
ANISOU 1591  O   LYS B 105     2946   3061   1647   -225     13   -129       O  
ATOM   1592  CB  LYS B 105     159.223  33.644  46.177  1.00 20.66           C  
ANISOU 1592  CB  LYS B 105     2949   3121   1779   -183     31    -99       C  
ATOM   1593  CG  LYS B 105     159.258  34.658  45.044  1.00 20.74           C  
ANISOU 1593  CG  LYS B 105     2964   3127   1791   -197     57    -96       C  
ATOM   1594  CD  LYS B 105     157.903  34.800  44.375  1.00 23.45           C  
ANISOU 1594  CD  LYS B 105     3320   3456   2135   -170     82    -64       C  
ATOM   1595  CE  LYS B 105     157.931  35.873  43.298  1.00 26.80           C  
ANISOU 1595  CE  LYS B 105     3766   3869   2546   -181    109    -52       C  
ATOM   1596  NZ  LYS B 105     156.569  36.149  42.764  1.00 29.76           N  
ANISOU 1596  NZ  LYS B 105     4159   4230   2917   -157    132     -7       N  
ATOM   1597  N   ILE B 106     160.508  31.494  48.021  1.00 21.35           N  
ANISOU 1597  N   ILE B 106     3021   3245   1847   -161    -63   -101       N  
ATOM   1598  CA  ILE B 106     160.430  30.485  49.071  1.00 24.42           C  
ANISOU 1598  CA  ILE B 106     3433   3631   2214   -140    -87    -89       C  
ATOM   1599  C   ILE B 106     161.361  30.846  50.223  1.00 28.03           C  
ANISOU 1599  C   ILE B 106     3910   4113   2626   -174   -112   -106       C  
ATOM   1600  O   ILE B 106     160.946  30.897  51.379  1.00 28.53           O  
ANISOU 1600  O   ILE B 106     4025   4163   2650   -182    -95   -107       O  
ATOM   1601  CB  ILE B 106     160.804  29.090  48.542  1.00 26.90           C  
ANISOU 1601  CB  ILE B 106     3715   3958   2549   -103   -135    -71       C  
ATOM   1602  CG1 ILE B 106     159.823  28.654  47.453  1.00 26.17           C  
ANISOU 1602  CG1 ILE B 106     3606   3844   2493    -80   -116    -58       C  
ATOM   1603  CG2 ILE B 106     160.828  28.082  49.678  1.00 29.02           C  
ANISOU 1603  CG2 ILE B 106     4020   4222   2783    -82   -160    -54       C  
ATOM   1604  CD1 ILE B 106     160.215  27.381  46.753  1.00 25.55           C  
ANISOU 1604  CD1 ILE B 106     3496   3777   2435    -54   -152    -47       C  
ATOM   1605  N   ASN B 107     162.621  31.105  49.888  1.00 30.26           N  
ANISOU 1605  N   ASN B 107     4149   4439   2909   -202   -152   -120       N  
ATOM   1606  CA  ASN B 107     163.640  31.450  50.870  1.00 28.32           C  
ANISOU 1606  CA  ASN B 107     3908   4233   2617   -247   -192   -138       C  
ATOM   1607  C   ASN B 107     163.352  32.760  51.601  1.00 25.89           C  
ANISOU 1607  C   ASN B 107     3656   3905   2276   -309   -146   -167       C  
ATOM   1608  O   ASN B 107     163.893  33.007  52.676  1.00 24.03           O  
ANISOU 1608  O   ASN B 107     3450   3690   1990   -350   -174   -182       O  
ATOM   1609  CB  ASN B 107     165.014  31.490  50.197  1.00 31.06           C  
ANISOU 1609  CB  ASN B 107     4176   4648   2976   -274   -237   -149       C  
ATOM   1610  CG  ASN B 107     166.051  32.224  51.022  1.00 36.25           C  
ANISOU 1610  CG  ASN B 107     4829   5356   3590   -346   -273   -176       C  
ATOM   1611  OD1 ASN B 107     166.391  31.811  52.132  1.00 38.55           O  
ANISOU 1611  OD1 ASN B 107     5143   5665   3839   -345   -328   -170       O  
ATOM   1612  ND2 ASN B 107     166.573  33.315  50.473  1.00 37.24           N  
ANISOU 1612  ND2 ASN B 107     4925   5505   3718   -414   -246   -208       N  
ATOM   1613  N   VAL B 108     162.507  33.597  51.008  1.00 27.03           N  
ANISOU 1613  N   VAL B 108     3819   4007   2444   -319    -75   -174       N  
ATOM   1614  CA  VAL B 108     162.053  34.820  51.665  1.00 27.36           C  
ANISOU 1614  CA  VAL B 108     3926   4009   2459   -377    -12   -200       C  
ATOM   1615  C   VAL B 108     160.956  34.488  52.669  1.00 29.94           C  
ANISOU 1615  C   VAL B 108     4315   4295   2765   -356     27   -189       C  
ATOM   1616  O   VAL B 108     160.876  35.082  53.745  1.00 30.40           O  
ANISOU 1616  O   VAL B 108     4439   4330   2780   -407     57   -211       O  
ATOM   1617  CB  VAL B 108     161.531  35.859  50.652  1.00 23.15           C  
ANISOU 1617  CB  VAL B 108     3399   3440   1958   -392     55   -207       C  
ATOM   1618  CG1 VAL B 108     160.858  37.019  51.369  1.00 17.97           C  
ANISOU 1618  CG1 VAL B 108     2827   2721   1282   -442    137   -231       C  
ATOM   1619  CG2 VAL B 108     162.667  36.363  49.776  1.00 25.42           C  
ANISOU 1619  CG2 VAL B 108     3639   3766   2253   -434     33   -225       C  
ATOM   1620  N   LEU B 109     160.108  33.531  52.306  1.00 31.21           N  
ANISOU 1620  N   LEU B 109     4458   4447   2955   -290     33   -157       N  
ATOM   1621  CA  LEU B 109     159.078  33.039  53.209  1.00 33.15           C  
ANISOU 1621  CA  LEU B 109     4752   4661   3182   -274     75   -143       C  
ATOM   1622  C   LEU B 109     159.733  32.295  54.369  1.00 36.88           C  
ANISOU 1622  C   LEU B 109     5250   5163   3599   -275     20   -139       C  
ATOM   1623  O   LEU B 109     159.080  31.949  55.352  1.00 39.76           O  
ANISOU 1623  O   LEU B 109     5670   5504   3931   -278     54   -131       O  
ATOM   1624  CB  LEU B 109     158.120  32.110  52.458  1.00 32.30           C  
ANISOU 1624  CB  LEU B 109     4610   4546   3114   -217     88   -111       C  
ATOM   1625  CG  LEU B 109     156.869  31.611  53.191  1.00 33.08           C  
ANISOU 1625  CG  LEU B 109     4753   4609   3206   -211    153    -95       C  
ATOM   1626  CD1 LEU B 109     155.962  32.773  53.577  1.00 31.32           C  
ANISOU 1626  CD1 LEU B 109     4586   4322   2990   -250    258   -114       C  
ATOM   1627  CD2 LEU B 109     156.119  30.606  52.328  1.00 33.27           C  
ANISOU 1627  CD2 LEU B 109     4736   4639   3266   -168    151    -66       C  
ATOM   1628  N   ILE B 110     161.035  32.065  54.244  1.00 37.45           N  
ANISOU 1628  N   ILE B 110     5285   5285   3658   -276    -63   -143       N  
ATOM   1629  CA  ILE B 110     161.801  31.318  55.231  1.00 37.00           C  
ANISOU 1629  CA  ILE B 110     5247   5267   3546   -268   -133   -134       C  
ATOM   1630  C   ILE B 110     163.157  32.000  55.402  1.00 41.51           C  
ANISOU 1630  C   ILE B 110     5799   5884   4089   -326   -194   -162       C  
ATOM   1631  O   ILE B 110     163.353  33.118  54.929  1.00 41.62           O  
ANISOU 1631  O   ILE B 110     5801   5891   4120   -382   -163   -191       O  
ATOM   1632  CB  ILE B 110     162.003  29.851  54.786  1.00 34.58           C  
ANISOU 1632  CB  ILE B 110     4902   4979   3260   -192   -187    -97       C  
ATOM   1633  CG1 ILE B 110     160.710  29.285  54.193  1.00 33.42           C  
ANISOU 1633  CG1 ILE B 110     4752   4791   3155   -149   -127    -76       C  
ATOM   1634  CG2 ILE B 110     162.468  28.986  55.949  1.00 35.66           C  
ANISOU 1634  CG2 ILE B 110     5076   5144   3329   -170   -246    -77       C  
ATOM   1635  CD1 ILE B 110     160.842  27.845  53.739  1.00 32.90           C  
ANISOU 1635  CD1 ILE B 110     4666   4730   3106    -87   -170    -43       C  
ATOM   1636  N   GLY B 111     164.076  31.352  56.110  1.00 43.66           N  
ANISOU 1636  N   GLY B 111     6069   6204   4314   -318   -280   -151       N  
ATOM   1637  CA  GLY B 111     165.436  31.852  56.223  1.00 42.63           C  
ANISOU 1637  CA  GLY B 111     5902   6134   4163   -375   -353   -174       C  
ATOM   1638  C   GLY B 111     165.689  32.703  57.451  1.00 42.58           C  
ANISOU 1638  C   GLY B 111     5964   6135   4079   -456   -359   -205       C  
ATOM   1639  O   GLY B 111     166.826  33.079  57.727  1.00 41.91           O  
ANISOU 1639  O   GLY B 111     5851   6107   3964   -513   -430   -225       O  
TER    1640      GLY B 111                                                      
ATOM   1641  N   SER C   3     135.326  20.624  43.545  1.00 57.19           N  
ANISOU 1641  N   SER C   3     7839   7265   6625    -27   -133   1192       N  
ATOM   1642  CA  SER C   3     135.962  20.439  44.844  1.00 56.76           C  
ANISOU 1642  CA  SER C   3     7727   7185   6656    -55   -121   1142       C  
ATOM   1643  C   SER C   3     136.350  18.981  45.074  1.00 56.06           C  
ANISOU 1643  C   SER C   3     7560   7169   6570    -78    -99   1070       C  
ATOM   1644  O   SER C   3     136.288  18.157  44.161  1.00 54.18           O  
ANISOU 1644  O   SER C   3     7319   6997   6269    -80    -81   1063       O  
ATOM   1645  CB  SER C   3     135.034  20.912  45.964  1.00 56.13           C  
ANISOU 1645  CB  SER C   3     7652   7048   6628     -4   -166   1108       C  
ATOM   1646  OG  SER C   3     133.768  20.286  45.858  1.00 55.61           O  
ANISOU 1646  OG  SER C   3     7577   7023   6532     51   -204   1064       O  
ATOM   1647  N   ARG C   4     136.733  18.667  46.306  1.00 56.81           N  
ANISOU 1647  N   ARG C   4     7600   7250   6735    -94   -101   1020       N  
ATOM   1648  CA  ARG C   4     137.216  17.336  46.637  1.00 53.69           C  
ANISOU 1648  CA  ARG C   4     7133   6913   6354   -113    -79    961       C  
ATOM   1649  C   ARG C   4     136.053  16.358  46.811  1.00 47.46           C  
ANISOU 1649  C   ARG C   4     6324   6161   5550    -69   -105    894       C  
ATOM   1650  O   ARG C   4     134.884  16.732  46.683  1.00 45.95           O  
ANISOU 1650  O   ARG C   4     6167   5954   5336    -26   -142    894       O  
ATOM   1651  CB  ARG C   4     138.095  17.383  47.891  1.00 55.98           C  
ANISOU 1651  CB  ARG C   4     7372   7176   6720   -147    -78    941       C  
ATOM   1652  CG  ARG C   4     138.743  18.745  48.168  1.00 62.03           C  
ANISOU 1652  CG  ARG C   4     8172   7873   7522   -181    -81    999       C  
ATOM   1653  CD  ARG C   4     139.459  19.335  46.945  1.00 69.56           C  
ANISOU 1653  CD  ARG C   4     9165   8827   8437   -216    -39   1078       C  
ATOM   1654  NE  ARG C   4     139.540  20.797  46.996  1.00 74.06           N  
ANISOU 1654  NE  ARG C   4     9797   9313   9028   -231    -48   1141       N  
ATOM   1655  CZ  ARG C   4     139.695  21.587  45.933  1.00 76.31           C  
ANISOU 1655  CZ  ARG C   4    10145   9576   9273   -243    -23   1219       C  
ATOM   1656  NH1 ARG C   4     139.762  22.907  46.090  1.00 76.44           N  
ANISOU 1656  NH1 ARG C   4    10220   9503   9320   -256    -29   1276       N  
ATOM   1657  NH2 ARG C   4     139.781  21.063  44.714  1.00 77.60           N  
ANISOU 1657  NH2 ARG C   4    10319   9802   9363   -244     12   1242       N  
ATOM   1658  N   TYR C   5     136.385  15.104  47.100  1.00 43.13           N  
ANISOU 1658  N   TYR C   5     5718   5657   5013    -81    -84    843       N  
ATOM   1659  CA  TYR C   5     135.396  14.032  47.162  1.00 38.56           C  
ANISOU 1659  CA  TYR C   5     5118   5114   4417    -51    -98    783       C  
ATOM   1660  C   TYR C   5     135.012  13.648  48.589  1.00 40.96           C  
ANISOU 1660  C   TYR C   5     5380   5398   4783    -39   -118    726       C  
ATOM   1661  O   TYR C   5     135.857  13.213  49.371  1.00 43.42           O  
ANISOU 1661  O   TYR C   5     5647   5709   5140    -62   -102    709       O  
ATOM   1662  CB  TYR C   5     135.925  12.793  46.431  1.00 35.53           C  
ANISOU 1662  CB  TYR C   5     4715   4790   3996    -67    -55    766       C  
ATOM   1663  CG  TYR C   5     135.103  11.552  46.678  1.00 32.76           C  
ANISOU 1663  CG  TYR C   5     4338   4469   3640    -46    -64    701       C  
ATOM   1664  CD1 TYR C   5     133.905  11.349  46.005  1.00 32.63           C  
ANISOU 1664  CD1 TYR C   5     4351   4477   3570    -24    -91    689       C  
ATOM   1665  CD2 TYR C   5     135.522  10.584  47.583  1.00 29.85           C  
ANISOU 1665  CD2 TYR C   5     3916   4103   3321    -52    -47    657       C  
ATOM   1666  CE1 TYR C   5     133.143  10.221  46.230  1.00 30.05           C  
ANISOU 1666  CE1 TYR C   5     4001   4175   3241    -13    -98    633       C  
ATOM   1667  CE2 TYR C   5     134.762   9.452  47.816  1.00 26.97           C  
ANISOU 1667  CE2 TYR C   5     3536   3759   2953    -36    -52    603       C  
ATOM   1668  CZ  TYR C   5     133.573   9.278  47.136  1.00 27.91           C  
ANISOU 1668  CZ  TYR C   5     3684   3901   3020    -20    -76    590       C  
ATOM   1669  OH  TYR C   5     132.812   8.152  47.358  1.00 27.50           O  
ANISOU 1669  OH  TYR C   5     3616   3867   2964    -12    -80    539       O  
ATOM   1670  N   VAL C   6     133.731  13.805  48.913  1.00 39.99           N  
ANISOU 1670  N   VAL C   6     5273   5263   4660     -3   -154    702       N  
ATOM   1671  CA  VAL C   6     133.177  13.347  50.186  1.00 36.12           C  
ANISOU 1671  CA  VAL C   6     4751   4759   4213     10   -166    647       C  
ATOM   1672  C   VAL C   6     132.195  12.199  49.957  1.00 33.47           C  
ANISOU 1672  C   VAL C   6     4395   4467   3856     26   -169    603       C  
ATOM   1673  O   VAL C   6     131.197  12.368  49.256  1.00 33.97           O  
ANISOU 1673  O   VAL C   6     4482   4546   3880     51   -195    612       O  
ATOM   1674  CB  VAL C   6     132.442  14.478  50.933  1.00 37.24           C  
ANISOU 1674  CB  VAL C   6     4929   4846   4375     42   -199    653       C  
ATOM   1675  CG1 VAL C   6     131.583  13.903  52.051  1.00 36.29           C  
ANISOU 1675  CG1 VAL C   6     4786   4724   4280     63   -209    595       C  
ATOM   1676  CG2 VAL C   6     133.433  15.500  51.475  1.00 39.68           C  
ANISOU 1676  CG2 VAL C   6     5257   5104   4717     20   -195    686       C  
ATOM   1677  N   PRO C   7     132.476  11.025  50.548  1.00 31.34           N  
ANISOU 1677  N   PRO C   7     4080   4217   3610     12   -147    561       N  
ATOM   1678  CA  PRO C   7     131.625   9.836  50.398  1.00 30.43           C  
ANISOU 1678  CA  PRO C   7     3946   4138   3478     20   -146    520       C  
ATOM   1679  C   PRO C   7     130.159  10.094  50.749  1.00 29.34           C  
ANISOU 1679  C   PRO C   7     3815   3995   3339     49   -180    503       C  
ATOM   1680  O   PRO C   7     129.878  10.788  51.724  1.00 32.53           O  
ANISOU 1680  O   PRO C   7     4224   4360   3775     64   -194    499       O  
ATOM   1681  CB  PRO C   7     132.228   8.849  51.403  1.00 27.07           C  
ANISOU 1681  CB  PRO C   7     3480   3710   3096      5   -121    487       C  
ATOM   1682  CG  PRO C   7     133.654   9.267  51.523  1.00 27.15           C  
ANISOU 1682  CG  PRO C   7     3481   3707   3128    -16   -104    516       C  
ATOM   1683  CD  PRO C   7     133.647  10.762  51.402  1.00 30.14           C  
ANISOU 1683  CD  PRO C   7     3895   4053   3504    -14   -126    555       C  
ATOM   1684  N   ASP C   8     129.243   9.555  49.949  1.00 25.71           N  
ANISOU 1684  N   ASP C   8     3356   3576   2838     57   -195    495       N  
ATOM   1685  CA  ASP C   8     127.820   9.612  50.259  1.00 26.76           C  
ANISOU 1685  CA  ASP C   8     3480   3717   2972     83   -228    479       C  
ATOM   1686  C   ASP C   8     127.320   8.194  50.500  1.00 25.64           C  
ANISOU 1686  C   ASP C   8     3302   3609   2829     68   -214    434       C  
ATOM   1687  O   ASP C   8     127.827   7.243  49.911  1.00 25.75           O  
ANISOU 1687  O   ASP C   8     3316   3649   2818     45   -192    422       O  
ATOM   1688  CB  ASP C   8     127.037  10.272  49.117  1.00 33.36           C  
ANISOU 1688  CB  ASP C   8     4344   4576   3757    105   -272    514       C  
ATOM   1689  CG  ASP C   8     125.534  10.307  49.376  1.00 37.15           C  
ANISOU 1689  CG  ASP C   8     4802   5073   4241    135   -313    502       C  
ATOM   1690  OD1 ASP C   8     125.128  10.341  50.559  1.00 35.73           O  
ANISOU 1690  OD1 ASP C   8     4600   4869   4107    146   -309    478       O  
ATOM   1691  OD2 ASP C   8     124.759  10.294  48.394  1.00 40.38           O  
ANISOU 1691  OD2 ASP C   8     5214   5526   4603    145   -352    518       O  
ATOM   1692  N   MET C   9     126.322   8.051  51.364  1.00 25.23           N  
ANISOU 1692  N   MET C   9     3226   3556   2802     81   -226    412       N  
ATOM   1693  CA  MET C   9     125.813   6.730  51.710  1.00 22.79           C  
ANISOU 1693  CA  MET C   9     2887   3276   2497     64   -212    373       C  
ATOM   1694  C   MET C   9     125.480   5.942  50.452  1.00 25.39           C  
ANISOU 1694  C   MET C   9     3222   3658   2769     48   -225    366       C  
ATOM   1695  O   MET C   9     124.855   6.463  49.530  1.00 28.96           O  
ANISOU 1695  O   MET C   9     3685   4138   3180     61   -264    386       O  
ATOM   1696  CB  MET C   9     124.585   6.850  52.612  1.00 18.03           C  
ANISOU 1696  CB  MET C   9     2258   2677   1916     83   -229    360       C  
ATOM   1697  CG  MET C   9     123.390   6.044  52.151  1.00 14.23           C  
ANISOU 1697  CG  MET C   9     1748   2252   1407     77   -251    342       C  
ATOM   1698  SD  MET C   9     121.950   6.384  53.173  1.00 88.51           S  
ANISOU 1698  SD  MET C   9    11115  11672  10843    106   -271    335       S  
ATOM   1699  CE  MET C   9     121.818   8.164  52.983  1.00 16.87           C  
ANISOU 1699  CE  MET C   9     2068   2564   1778    158   -310    377       C  
ATOM   1700  N   GLY C  10     125.922   4.690  50.412  1.00 24.67           N  
ANISOU 1700  N   GLY C  10     3129   3576   2669     21   -197    337       N  
ATOM   1701  CA  GLY C  10     125.722   3.851  49.246  1.00 26.11           C  
ANISOU 1701  CA  GLY C  10     3330   3804   2787      2   -206    319       C  
ATOM   1702  C   GLY C  10     126.979   3.755  48.405  1.00 27.88           C  
ANISOU 1702  C   GLY C  10     3594   4023   2976     -7   -178    331       C  
ATOM   1703  O   GLY C  10     127.124   2.850  47.585  1.00 25.79           O  
ANISOU 1703  O   GLY C  10     3359   3785   2654    -26   -167    306       O  
ATOM   1704  N   ASP C  11     127.899   4.691  48.615  1.00 29.48           N  
ANISOU 1704  N   ASP C  11     3801   4191   3207      4   -163    365       N  
ATOM   1705  CA  ASP C  11     129.154   4.690  47.875  1.00 28.86           C  
ANISOU 1705  CA  ASP C  11     3754   4112   3100     -5   -131    383       C  
ATOM   1706  C   ASP C  11     130.007   3.470  48.198  1.00 30.90           C  
ANISOU 1706  C   ASP C  11     4014   4358   3369    -17    -85    355       C  
ATOM   1707  O   ASP C  11     129.999   2.965  49.319  1.00 33.91           O  
ANISOU 1707  O   ASP C  11     4367   4713   3805    -16    -77    337       O  
ATOM   1708  CB  ASP C  11     129.951   5.969  48.144  1.00 29.73           C  
ANISOU 1708  CB  ASP C  11     3863   4189   3245      5   -127    427       C  
ATOM   1709  CG  ASP C  11     129.409   7.168  47.380  1.00 32.11           C  
ANISOU 1709  CG  ASP C  11     4190   4500   3510     19   -164    467       C  
ATOM   1710  OD1 ASP C  11     128.487   6.982  46.551  1.00 35.43           O  
ANISOU 1710  OD1 ASP C  11     4627   4961   3874     22   -195    463       O  
ATOM   1711  OD2 ASP C  11     129.912   8.294  47.597  1.00 31.24           O  
ANISOU 1711  OD2 ASP C  11     4088   4357   3425     26   -167    504       O  
ATOM   1712  N   LEU C  12     130.735   2.999  47.194  1.00 30.06           N  
ANISOU 1712  N   LEU C  12     3950   4269   3204    -28    -50    353       N  
ATOM   1713  CA  LEU C  12     131.708   1.934  47.363  1.00 27.30           C  
ANISOU 1713  CA  LEU C  12     3614   3902   2858    -34      7    333       C  
ATOM   1714  C   LEU C  12     133.078   2.580  47.238  1.00 29.71           C  
ANISOU 1714  C   LEU C  12     3914   4195   3181    -33     41    374       C  
ATOM   1715  O   LEU C  12     133.420   3.118  46.188  1.00 32.32           O  
ANISOU 1715  O   LEU C  12     4276   4547   3456    -39     55    398       O  
ATOM   1716  CB  LEU C  12     131.516   0.866  46.285  1.00 25.67           C  
ANISOU 1716  CB  LEU C  12     3467   3722   2563    -46     40    292       C  
ATOM   1717  CG  LEU C  12     132.180  -0.494  46.498  1.00 23.19           C  
ANISOU 1717  CG  LEU C  12     3165   3405   2243    -53    109    262       C  
ATOM   1718  CD1 LEU C  12     131.626  -1.161  47.737  1.00 19.78           C  
ANISOU 1718  CD1 LEU C  12     2697   2951   1867    -53     90    245       C  
ATOM   1719  CD2 LEU C  12     131.978  -1.381  45.279  1.00 25.61           C  
ANISOU 1719  CD2 LEU C  12     3523   3763   2443    -68    149    214       C  
ATOM   1720  N   ILE C  13     133.857   2.541  48.313  1.00 31.02           N  
ANISOU 1720  N   ILE C  13     4038   4329   3420    -26     52    386       N  
ATOM   1721  CA  ILE C  13     135.125   3.261  48.350  1.00 33.96           C  
ANISOU 1721  CA  ILE C  13     4389   4695   3820    -27     74    429       C  
ATOM   1722  C   ILE C  13     136.334   2.335  48.460  1.00 34.54           C  
ANISOU 1722  C   ILE C  13     4454   4762   3909    -28    136    428       C  
ATOM   1723  O   ILE C  13     136.233   1.216  48.960  1.00 36.09           O  
ANISOU 1723  O   ILE C  13     4652   4942   4120    -23    155    399       O  
ATOM   1724  CB  ILE C  13     135.158   4.272  49.517  1.00 35.46           C  
ANISOU 1724  CB  ILE C  13     4530   4860   4085    -22     30    451       C  
ATOM   1725  CG1 ILE C  13     134.996   3.551  50.858  1.00 34.99           C  
ANISOU 1725  CG1 ILE C  13     4435   4776   4082    -13     20    426       C  
ATOM   1726  CG2 ILE C  13     134.073   5.320  49.341  1.00 36.76           C  
ANISOU 1726  CG2 ILE C  13     4707   5025   4236    -20    -15    457       C  
ATOM   1727  CD1 ILE C  13     135.137   4.461  52.062  1.00 33.66           C  
ANISOU 1727  CD1 ILE C  13     4229   4585   3976    -15    -10    440       C  
ATOM   1728  N   TRP C  14     137.479   2.804  47.977  1.00 33.82           N  
ANISOU 1728  N   TRP C  14     4354   4682   3815    -36    174    465       N  
ATOM   1729  CA  TRP C  14     138.725   2.075  48.162  1.00 30.61           C  
ANISOU 1729  CA  TRP C  14     3913   4278   3438    -31    237    477       C  
ATOM   1730  C   TRP C  14     139.497   2.681  49.320  1.00 31.37           C  
ANISOU 1730  C   TRP C  14     3945   4354   3621    -22    202    515       C  
ATOM   1731  O   TRP C  14     139.899   3.843  49.268  1.00 31.49           O  
ANISOU 1731  O   TRP C  14     3942   4374   3649    -35    181    554       O  
ATOM   1732  CB  TRP C  14     139.580   2.106  46.898  1.00 28.40           C  
ANISOU 1732  CB  TRP C  14     3649   4038   3103    -47    316    494       C  
ATOM   1733  CG  TRP C  14     140.703   1.124  46.950  1.00 27.55           C  
ANISOU 1733  CG  TRP C  14     3491   3952   3024    -29    401    501       C  
ATOM   1734  CD1 TRP C  14     141.999   1.367  47.322  1.00 26.77           C  
ANISOU 1734  CD1 TRP C  14     3319   3862   2991    -17    429    553       C  
ATOM   1735  CD2 TRP C  14     140.632  -0.269  46.639  1.00 25.23           C  
ANISOU 1735  CD2 TRP C  14     3209   3673   2703    -15    475    453       C  
ATOM   1736  NE1 TRP C  14     142.738   0.213  47.247  1.00 23.32           N  
ANISOU 1736  NE1 TRP C  14     2842   3441   2579     14    517    544       N  
ATOM   1737  CE2 TRP C  14     141.923  -0.808  46.831  1.00 23.98           C  
ANISOU 1737  CE2 TRP C  14     2979   3525   2607     18    550    478       C  
ATOM   1738  CE3 TRP C  14     139.604  -1.113  46.204  1.00 23.76           C  
ANISOU 1738  CE3 TRP C  14     3085   3491   2450    -26    488    388       C  
ATOM   1739  CZ2 TRP C  14     142.210  -2.155  46.614  1.00 24.95           C  
ANISOU 1739  CZ2 TRP C  14     3092   3653   2735     52    644    435       C  
ATOM   1740  CZ3 TRP C  14     139.892  -2.448  45.986  1.00 25.51           C  
ANISOU 1740  CZ3 TRP C  14     3301   3726   2664     -7    579    339       C  
ATOM   1741  CH2 TRP C  14     141.184  -2.957  46.194  1.00 27.40           C  
ANISOU 1741  CH2 TRP C  14     3469   3965   2975     38    659    361       C  
ATOM   1742  N   VAL C  15     139.691   1.892  50.370  1.00 32.80           N  
ANISOU 1742  N   VAL C  15     4082   4523   3857      1    197    516       N  
ATOM   1743  CA  VAL C  15     140.362   2.377  51.566  1.00 31.71           C  
ANISOU 1743  CA  VAL C  15     3883   4370   3794      7    157    549       C  
ATOM   1744  C   VAL C  15     141.265   1.293  52.155  1.00 36.70           C  
ANISOU 1744  C   VAL C  15     4452   5012   4478     42    193    586       C  
ATOM   1745  O   VAL C  15     141.090   0.105  51.876  1.00 39.73           O  
ANISOU 1745  O   VAL C  15     4851   5398   4848     66    245    572       O  
ATOM   1746  CB  VAL C  15     139.337   2.855  52.614  1.00 27.04           C  
ANISOU 1746  CB  VAL C  15     3292   3756   3225      2     87    523       C  
ATOM   1747  CG1 VAL C  15     138.460   1.701  53.061  1.00 24.67           C  
ANISOU 1747  CG1 VAL C  15     3014   3437   2920     17     87    482       C  
ATOM   1748  CG2 VAL C  15     140.032   3.512  53.800  1.00 26.83           C  
ANISOU 1748  CG2 VAL C  15     3209   3723   3261     -8     50    552       C  
ATOM   1749  N   ASP C  16     142.238   1.716  52.957  1.00 37.67           N  
ANISOU 1749  N   ASP C  16     4506   5142   4665     45    169    638       N  
ATOM   1750  CA  ASP C  16     143.157   0.800  53.619  1.00 37.29           C  
ANISOU 1750  CA  ASP C  16     4386   5100   4683     86    194    693       C  
ATOM   1751  C   ASP C  16     142.845   0.736  55.111  1.00 36.35           C  
ANISOU 1751  C   ASP C  16     4243   4960   4609     82    126    687       C  
ATOM   1752  O   ASP C  16     143.039   1.713  55.831  1.00 36.46           O  
ANISOU 1752  O   ASP C  16     4234   4976   4643     44     71    690       O  
ATOM   1753  CB  ASP C  16     144.601   1.253  53.399  1.00 39.91           C  
ANISOU 1753  CB  ASP C  16     4644   5463   5057     86    219    768       C  
ATOM   1754  CG  ASP C  16     145.608   0.362  54.099  1.00 43.29           C  
ANISOU 1754  CG  ASP C  16     4987   5892   5567    136    241    840       C  
ATOM   1755  OD1 ASP C  16     145.245  -0.776  54.466  1.00 44.54           O  
ANISOU 1755  OD1 ASP C  16     5153   6024   5744    179    264    833       O  
ATOM   1756  OD2 ASP C  16     146.765   0.799  54.277  1.00 44.78           O  
ANISOU 1756  OD2 ASP C  16     5104   6104   5806    130    235    909       O  
ATOM   1757  N   PHE C  17     142.371  -0.418  55.573  1.00 38.26           N  
ANISOU 1757  N   PHE C  17     4497   5179   4861    111    142    673       N  
ATOM   1758  CA  PHE C  17     141.933  -0.568  56.962  1.00 36.07           C  
ANISOU 1758  CA  PHE C  17     4219   4877   4609     92     92    647       C  
ATOM   1759  C   PHE C  17     143.059  -0.864  57.947  1.00 35.86           C  
ANISOU 1759  C   PHE C  17     4105   4864   4656     99     86    717       C  
ATOM   1760  O   PHE C  17     142.816  -0.975  59.149  1.00 36.83           O  
ANISOU 1760  O   PHE C  17     4246   4964   4785     68     50    692       O  
ATOM   1761  CB  PHE C  17     140.866  -1.659  57.076  1.00 33.45           C  
ANISOU 1761  CB  PHE C  17     3947   4509   4253    108    108    604       C  
ATOM   1762  CG  PHE C  17     139.578  -1.321  56.385  1.00 30.77           C  
ANISOU 1762  CG  PHE C  17     3687   4159   3845     83     98    534       C  
ATOM   1763  CD1 PHE C  17     138.592  -0.607  57.044  1.00 30.82           C  
ANISOU 1763  CD1 PHE C  17     3722   4151   3835     49     48    484       C  
ATOM   1764  CD2 PHE C  17     139.351  -1.719  55.078  1.00 27.38           C  
ANISOU 1764  CD2 PHE C  17     3291   3743   3368     94    150    529       C  
ATOM   1765  CE1 PHE C  17     137.407  -0.296  56.414  1.00 29.03           C  
ANISOU 1765  CE1 PHE C  17     3540   3927   3562     36     41    444       C  
ATOM   1766  CE2 PHE C  17     138.168  -1.412  54.445  1.00 25.17           C  
ANISOU 1766  CE2 PHE C  17     3074   3462   3027     64    134    473       C  
ATOM   1767  CZ  PHE C  17     137.195  -0.698  55.112  1.00 26.26           C  
ANISOU 1767  CZ  PHE C  17     3232   3582   3164     40     76    432       C  
ATOM   1768  N   ASP C  18     144.279  -1.007  57.437  1.00 36.24           N  
ANISOU 1768  N   ASP C  18     4069   4946   4756    138    124    806       N  
ATOM   1769  CA  ASP C  18     145.437  -1.277  58.288  1.00 38.50           C  
ANISOU 1769  CA  ASP C  18     4301   5228   5101    128    121    867       C  
ATOM   1770  C   ASP C  18     145.993   0.002  58.886  1.00 38.49           C  
ANISOU 1770  C   ASP C  18     4282   5244   5099     57     56    874       C  
ATOM   1771  O   ASP C  18     145.785   1.083  58.339  1.00 38.20           O  
ANISOU 1771  O   ASP C  18     4258   5225   5033     34     30    853       O  
ATOM   1772  CB  ASP C  18     146.546  -1.976  57.504  1.00 41.93           C  
ANISOU 1772  CB  ASP C  18     4691   5657   5583    205    185    954       C  
ATOM   1773  CG  ASP C  18     146.107  -3.312  56.935  1.00 44.25           C  
ANISOU 1773  CG  ASP C  18     5017   5909   5886    282    270    962       C  
ATOM   1774  OD1 ASP C  18     145.033  -3.811  57.342  1.00 45.76           O  
ANISOU 1774  OD1 ASP C  18     5245   6084   6059    272    267    899       O  
ATOM   1775  OD2 ASP C  18     146.838  -3.857  56.076  1.00 44.24           O  
ANISOU 1775  OD2 ASP C  18     4991   5899   5918    333    364    994       O  
ATOM   1776  N   PRO C  19     146.724  -0.118  60.005  1.00 37.78           N  
ANISOU 1776  N   PRO C  19     4164   5147   5045     23     31    920       N  
ATOM   1777  CA  PRO C  19     147.026  -1.380  60.697  1.00 36.72           C  
ANISOU 1777  CA  PRO C  19     4005   4994   4954     51     54    969       C  
ATOM   1778  C   PRO C  19     145.781  -1.986  61.338  1.00 35.18           C  
ANISOU 1778  C   PRO C  19     3878   4766   4725     56     36    889       C  
ATOM   1779  O   PRO C  19     144.883  -1.240  61.722  1.00 35.81           O  
ANISOU 1779  O   PRO C  19     4021   4836   4750     17    -10    809       O  
ATOM   1780  CB  PRO C  19     148.021  -0.955  61.784  1.00 35.94           C  
ANISOU 1780  CB  PRO C  19     3860   4906   4889     -2     -1   1037       C  
ATOM   1781  CG  PRO C  19     148.576   0.359  61.316  1.00 34.84           C  
ANISOU 1781  CG  PRO C  19     3713   4788   4735    -41    -29   1048       C  
ATOM   1782  CD  PRO C  19     147.442   1.021  60.600  1.00 36.16           C  
ANISOU 1782  CD  PRO C  19     3939   4954   4845    -43    -28    948       C  
ATOM   1783  N   THR C  20     145.728  -3.312  61.444  1.00 32.44           N  
ANISOU 1783  N   THR C  20     3540   4384   4403    113     69    901       N  
ATOM   1784  CA  THR C  20     144.559  -3.980  62.007  1.00 29.71           C  
ANISOU 1784  CA  THR C  20     3276   3994   4017    122     48    827       C  
ATOM   1785  C   THR C  20     144.943  -5.180  62.872  1.00 30.88           C  
ANISOU 1785  C   THR C  20     3424   4105   4206    157     40    863       C  
ATOM   1786  O   THR C  20     146.051  -5.707  62.765  1.00 33.05           O  
ANISOU 1786  O   THR C  20     3633   4377   4549    197     65    938       O  
ATOM   1787  CB  THR C  20     143.594  -4.451  60.901  1.00 31.40           C  
ANISOU 1787  CB  THR C  20     3531   4193   4208    159    103    788       C  
ATOM   1788  OG1 THR C  20     142.258  -4.496  61.415  1.00 36.89           O  
ANISOU 1788  OG1 THR C  20     4315   4859   4844    133     64    705       O  
ATOM   1789  CG2 THR C  20     143.989  -5.828  60.398  1.00 30.34           C  
ANISOU 1789  CG2 THR C  20     3376   4019   4133    236    181    843       C  
ATOM   1790  N   LYS C  21     144.022  -5.603  63.733  1.00 28.42           N  
ANISOU 1790  N   LYS C  21     3184   3759   3854    147      4    811       N  
ATOM   1791  CA  LYS C  21     144.251  -6.762  64.591  1.00 27.69           C  
ANISOU 1791  CA  LYS C  21     3100   3628   3792    182    -10    845       C  
ATOM   1792  C   LYS C  21     143.120  -7.783  64.476  1.00 30.53           C  
ANISOU 1792  C   LYS C  21     3530   3933   4136    206     18    809       C  
ATOM   1793  O   LYS C  21     142.008  -7.455  64.053  1.00 32.30           O  
ANISOU 1793  O   LYS C  21     3806   4157   4309    181     26    746       O  
ATOM   1794  CB  LYS C  21     144.428  -6.335  66.051  1.00 24.75           C  
ANISOU 1794  CB  LYS C  21     2741   3272   3392    142    -86    851       C  
ATOM   1795  CG  LYS C  21     145.659  -5.493  66.311  1.00 25.02           C  
ANISOU 1795  CG  LYS C  21     2707   3349   3451    116   -121    900       C  
ATOM   1796  CD  LYS C  21     145.952  -5.382  67.798  1.00 29.08           C  
ANISOU 1796  CD  LYS C  21     3221   3877   3950     89   -194    936       C  
ATOM   1797  CE  LYS C  21     147.311  -4.722  68.044  1.00 33.24           C  
ANISOU 1797  CE  LYS C  21     3677   4442   4511     68   -235    996       C  
ATOM   1798  NZ  LYS C  21     147.730  -4.811  69.478  1.00 34.54           N  
ANISOU 1798  NZ  LYS C  21     3839   4620   4664     52   -312   1041       N  
ATOM   1799  N   GLY C  22     143.414  -9.023  64.857  1.00 28.58           N  
ANISOU 1799  N   GLY C  22     3285   3636   3937    253     31    853       N  
ATOM   1800  CA  GLY C  22     142.433 -10.091  64.816  1.00 26.50           C  
ANISOU 1800  CA  GLY C  22     3091   3308   3671    271     59    832       C  
ATOM   1801  C   GLY C  22     141.899 -10.374  63.426  1.00 26.65           C  
ANISOU 1801  C   GLY C  22     3123   3299   3705    297    139    809       C  
ATOM   1802  O   GLY C  22     142.620 -10.267  62.431  1.00 26.07           O  
ANISOU 1802  O   GLY C  22     2996   3233   3677    337    197    835       O  
ATOM   1803  N   SER C  23     140.619 -10.727  63.363  1.00 28.51           N  
ANISOU 1803  N   SER C  23     3434   3500   3900    272    146    763       N  
ATOM   1804  CA  SER C  23     139.972 -11.094  62.108  1.00 31.65           C  
ANISOU 1804  CA  SER C  23     3864   3857   4304    291    223    739       C  
ATOM   1805  C   SER C  23     139.387  -9.877  61.399  1.00 34.45           C  
ANISOU 1805  C   SER C  23     4222   4281   4588    249    210    692       C  
ATOM   1806  O   SER C  23     138.767 -10.003  60.343  1.00 34.74           O  
ANISOU 1806  O   SER C  23     4295   4298   4606    253    267    670       O  
ATOM   1807  CB  SER C  23     138.871 -12.124  62.364  1.00 33.25           C  
ANISOU 1807  CB  SER C  23     4148   3981   4503    273    240    718       C  
ATOM   1808  N   GLU C  24     139.580  -8.703  61.992  1.00 36.29           N  
ANISOU 1808  N   GLU C  24     4427   4584   4779    207    139    673       N  
ATOM   1809  CA  GLU C  24     139.133  -7.455  61.384  1.00 34.55           C  
ANISOU 1809  CA  GLU C  24     4208   4420   4500    170    119    625       C  
ATOM   1810  C   GLU C  24     139.762  -7.338  60.001  1.00 34.88           C  
ANISOU 1810  C   GLU C  24     4212   4478   4563    212    186    657       C  
ATOM   1811  O   GLU C  24     140.973  -7.513  59.852  1.00 35.60           O  
ANISOU 1811  O   GLU C  24     4239   4573   4716    256    221    718       O  
ATOM   1812  CB  GLU C  24     139.557  -6.264  62.248  1.00 34.45           C  
ANISOU 1812  CB  GLU C  24     4171   4452   4468    131     54    608       C  
ATOM   1813  CG  GLU C  24     139.187  -6.385  63.727  1.00 33.52           C  
ANISOU 1813  CG  GLU C  24     4078   4323   4334    107      8    603       C  
ATOM   1814  CD  GLU C  24     140.029  -5.483  64.611  1.00 33.10           C  
ANISOU 1814  CD  GLU C  24     3976   4310   4290     83    -34    633       C  
ATOM   1815  OE1 GLU C  24     140.718  -4.595  64.068  1.00 32.22           O  
ANISOU 1815  OE1 GLU C  24     3822   4232   4190     73    -34    640       O  
ATOM   1816  OE2 GLU C  24     140.015  -5.671  65.845  1.00 34.51           O  
ANISOU 1816  OE2 GLU C  24     4164   4485   4462     70    -68    653       O  
ATOM   1817  N   GLN C  25     138.947  -7.040  58.993  1.00 33.99           N  
ANISOU 1817  N   GLN C  25     4141   4377   4395    197    208    618       N  
ATOM   1818  CA  GLN C  25     139.438  -6.996  57.618  1.00 33.58           C  
ANISOU 1818  CA  GLN C  25     4080   4342   4339    232    288    640       C  
ATOM   1819  C   GLN C  25     140.648  -6.076  57.459  1.00 35.47           C  
ANISOU 1819  C   GLN C  25     4238   4635   4603    246    276    682       C  
ATOM   1820  O   GLN C  25     140.631  -4.928  57.902  1.00 35.74           O  
ANISOU 1820  O   GLN C  25     4255   4711   4614    198    199    655       O  
ATOM   1821  CB  GLN C  25     138.325  -6.592  56.650  1.00 33.27           C  
ANISOU 1821  CB  GLN C  25     4104   4332   4206    185    291    572       C  
ATOM   1822  CG  GLN C  25     137.270  -7.662  56.470  1.00 34.39           C  
ANISOU 1822  CG  GLN C  25     4316   4426   4323    169    342    541       C  
ATOM   1823  CD  GLN C  25     137.867  -8.993  56.047  1.00 35.48           C  
ANISOU 1823  CD  GLN C  25     4468   4485   4526    222    452    535       C  
ATOM   1824  OE1 GLN C  25     138.447  -9.113  54.966  1.00 34.07           O  
ANISOU 1824  OE1 GLN C  25     4284   4319   4340    246    527    493       O  
ATOM   1825  NE2 GLN C  25     137.736  -9.998  56.906  1.00 36.02           N  
ANISOU 1825  NE2 GLN C  25     4555   4466   4664    238    454    554       N  
ATOM   1826  N   ALA C  26     141.700  -6.592  56.828  1.00 36.29           N  
ANISOU 1826  N   ALA C  26     4297   4728   4764    311    370    748       N  
ATOM   1827  CA  ALA C  26     142.945  -5.845  56.685  1.00 32.21           C  
ANISOU 1827  CA  ALA C  26     3689   4263   4286    328    368    808       C  
ATOM   1828  C   ALA C  26     143.180  -5.317  55.273  1.00 32.36           C  
ANISOU 1828  C   ALA C  26     3727   4320   4250    316    424    770       C  
ATOM   1829  O   ALA C  26     142.380  -5.540  54.366  1.00 33.52           O  
ANISOU 1829  O   ALA C  26     3948   4465   4323    293    468    691       O  
ATOM   1830  CB  ALA C  26     144.124  -6.703  57.125  1.00 27.31           C  
ANISOU 1830  CB  ALA C  26     2985   3611   3781    396    428    903       C  
ATOM   1831  N   GLY C  27     144.290  -4.602  55.111  1.00 33.43           N  
ANISOU 1831  N   GLY C  27     3792   4494   4415    318    415    819       N  
ATOM   1832  CA  GLY C  27     144.750  -4.153  53.810  1.00 38.11           C  
ANISOU 1832  CA  GLY C  27     4392   5123   4965    302    475    780       C  
ATOM   1833  C   GLY C  27     143.817  -3.186  53.111  1.00 41.97           C  
ANISOU 1833  C   GLY C  27     4955   5644   5347    235    431    713       C  
ATOM   1834  O   GLY C  27     142.818  -2.741  53.680  1.00 39.98           O  
ANISOU 1834  O   GLY C  27     4744   5384   5061    200    346    687       O  
ATOM   1835  N   HIS C  28     144.156  -2.850  51.870  1.00 46.60           N  
ANISOU 1835  N   HIS C  28     5557   6265   5886    216    490    682       N  
ATOM   1836  CA  HIS C  28     143.270  -2.070  51.019  1.00 48.63           C  
ANISOU 1836  CA  HIS C  28     5889   6546   6042    157    462    625       C  
ATOM   1837  C   HIS C  28     142.150  -2.974  50.530  1.00 46.12           C  
ANISOU 1837  C   HIS C  28     5649   6215   5660    153    498    550       C  
ATOM   1838  O   HIS C  28     142.378  -4.149  50.245  1.00 45.03           O  
ANISOU 1838  O   HIS C  28     5512   6059   5539    194    590    523       O  
ATOM   1839  CB  HIS C  28     144.031  -1.495  49.822  1.00 54.68           C  
ANISOU 1839  CB  HIS C  28     6649   7355   6772    134    522    623       C  
ATOM   1840  CG  HIS C  28     144.993  -0.406  50.178  1.00 59.08           C  
ANISOU 1840  CG  HIS C  28     7141   7930   7377    118    482    692       C  
ATOM   1841  ND1 HIS C  28     146.154  -0.635  50.885  1.00 61.61           N  
ANISOU 1841  ND1 HIS C  28     7366   8249   7793    153    492    759       N  
ATOM   1842  CD2 HIS C  28     144.968   0.926  49.919  1.00 59.39           C  
ANISOU 1842  CD2 HIS C  28     7196   7984   7386     67    432    706       C  
ATOM   1843  CE1 HIS C  28     146.802   0.505  51.045  1.00 61.59           C  
ANISOU 1843  CE1 HIS C  28     7323   8268   7809    117    448    808       C  
ATOM   1844  NE2 HIS C  28     146.106   1.465  50.470  1.00 60.72           N  
ANISOU 1844  NE2 HIS C  28     7281   8164   7625     66    415    776       N  
ATOM   1845  N   ARG C  29     140.943  -2.427  50.428  1.00 45.38           N  
ANISOU 1845  N   ARG C  29     5618   6124   5500    107    427    511       N  
ATOM   1846  CA  ARG C  29     139.802  -3.199  49.952  1.00 46.56           C  
ANISOU 1846  CA  ARG C  29     5838   6272   5581     90    447    443       C  
ATOM   1847  C   ARG C  29     138.556  -2.326  49.864  1.00 46.50           C  
ANISOU 1847  C   ARG C  29     5881   6268   5518     41    355    416       C  
ATOM   1848  O   ARG C  29     138.452  -1.306  50.550  1.00 50.16           O  
ANISOU 1848  O   ARG C  29     6324   6715   6018     34    275    442       O  
ATOM   1849  CB  ARG C  29     139.531  -4.393  50.872  1.00 46.61           C  
ANISOU 1849  CB  ARG C  29     5837   6232   5639    127    469    444       C  
ATOM   1850  CG  ARG C  29     138.964  -4.010  52.224  1.00 47.42           C  
ANISOU 1850  CG  ARG C  29     5926   6306   5785    118    366    474       C  
ATOM   1851  CD  ARG C  29     138.507  -5.232  53.012  1.00 50.44           C  
ANISOU 1851  CD  ARG C  29     6322   6640   6203    142    391    475       C  
ATOM   1852  NE  ARG C  29     139.621  -6.054  53.472  1.00 51.40           N  
ANISOU 1852  NE  ARG C  29     6392   6720   6417    208    462    531       N  
ATOM   1853  CZ  ARG C  29     140.055  -7.142  52.846  1.00 52.57           C  
ANISOU 1853  CZ  ARG C  29     6549   6837   6589    253    588    504       C  
ATOM   1854  NH1 ARG C  29     139.467  -7.548  51.729  1.00 53.04           N  
ANISOU 1854  NH1 ARG C  29     6676   6908   6569    231    650    412       N  
ATOM   1855  NH2 ARG C  29     141.077  -7.824  53.340  1.00 53.95           N  
ANISOU 1855  NH2 ARG C  29     6664   6963   6874    322    645    556       N  
ATOM   1856  N   PRO C  30     137.599  -2.730  49.017  1.00 41.15           N  
ANISOU 1856  N   PRO C  30     5269   5610   4757     13    372    358       N  
ATOM   1857  CA  PRO C  30     136.356  -1.973  48.861  1.00 37.69           C  
ANISOU 1857  CA  PRO C  30     4873   5169   4277    -16    290    338       C  
ATOM   1858  C   PRO C  30     135.522  -1.992  50.138  1.00 34.08           C  
ANISOU 1858  C   PRO C  30     4399   4677   3874    -11    220    339       C  
ATOM   1859  O   PRO C  30     135.447  -3.014  50.817  1.00 36.18           O  
ANISOU 1859  O   PRO C  30     4656   4928   4164     -1    245    335       O  
ATOM   1860  CB  PRO C  30     135.635  -2.716  47.733  1.00 38.28           C  
ANISOU 1860  CB  PRO C  30     5015   5274   4253    -38    334    277       C  
ATOM   1861  CG  PRO C  30     136.193  -4.088  47.761  1.00 38.72           C  
ANISOU 1861  CG  PRO C  30     5065   5336   4312    -27    432    243       C  
ATOM   1862  CD  PRO C  30     137.624  -3.934  48.169  1.00 39.38           C  
ANISOU 1862  CD  PRO C  30     5079   5408   4477     13    471    298       C  
ATOM   1863  N   ALA C  31     134.910  -0.858  50.458  1.00 29.18           N  
ANISOU 1863  N   ALA C  31     3774   4040   3274    -14    145    343       N  
ATOM   1864  CA  ALA C  31     134.072  -0.734  51.642  1.00 28.34           C  
ANISOU 1864  CA  ALA C  31     3650   3901   3216    -10     91    332       C  
ATOM   1865  C   ALA C  31     132.803   0.029  51.290  1.00 30.90           C  
ANISOU 1865  C   ALA C  31     3980   4247   3514    -16     42    317       C  
ATOM   1866  O   ALA C  31     132.842   1.006  50.543  1.00 35.00           O  
ANISOU 1866  O   ALA C  31     4501   4788   4011    -17     28    334       O  
ATOM   1867  CB  ALA C  31     134.827  -0.031  52.757  1.00 28.02           C  
ANISOU 1867  CB  ALA C  31     3554   3844   3249      4     66    365       C  
ATOM   1868  N   VAL C  32     131.679  -0.424  51.835  1.00 29.12           N  
ANISOU 1868  N   VAL C  32     3754   4019   3293    -21     19    292       N  
ATOM   1869  CA  VAL C  32     130.390   0.203  51.580  1.00 27.65           C  
ANISOU 1869  CA  VAL C  32     3556   3860   3088    -26    -24    282       C  
ATOM   1870  C   VAL C  32     130.107   1.283  52.616  1.00 24.14           C  
ANISOU 1870  C   VAL C  32     3067   3403   2701    -16    -52    299       C  
ATOM   1871  O   VAL C  32     130.255   1.055  53.819  1.00 26.06           O  
ANISOU 1871  O   VAL C  32     3291   3621   2991    -14    -49    299       O  
ATOM   1872  CB  VAL C  32     129.258  -0.836  51.588  1.00 31.18           C  
ANISOU 1872  CB  VAL C  32     4020   4322   3506    -42    -30    244       C  
ATOM   1873  CG1 VAL C  32     127.907  -0.166  51.370  1.00 35.03           C  
ANISOU 1873  CG1 VAL C  32     4482   4846   3981    -46    -77    239       C  
ATOM   1874  CG2 VAL C  32     129.515  -1.895  50.528  1.00 30.31           C  
ANISOU 1874  CG2 VAL C  32     3946   4252   3318    -62      8    222       C  
ATOM   1875  N   VAL C  33     129.693   2.454  52.139  1.00 20.92           N  
ANISOU 1875  N   VAL C  33     2655   3010   2282    -10    -76    315       N  
ATOM   1876  CA  VAL C  33     129.485   3.616  52.996  1.00 20.68           C  
ANISOU 1876  CA  VAL C  33     2604   2959   2293      0    -93    330       C  
ATOM   1877  C   VAL C  33     128.031   3.705  53.472  1.00 23.20           C  
ANISOU 1877  C   VAL C  33     2912   3290   2614      6   -114    315       C  
ATOM   1878  O   VAL C  33     127.112   3.886  52.672  1.00 27.05           O  
ANISOU 1878  O   VAL C  33     3403   3809   3065     10   -138    315       O  
ATOM   1879  CB  VAL C  33     129.894   4.914  52.271  1.00 17.40           C  
ANISOU 1879  CB  VAL C  33     2204   2544   1864      7   -104    363       C  
ATOM   1880  CG1 VAL C  33     129.694   6.121  53.171  1.00 14.20           C  
ANISOU 1880  CG1 VAL C  33     1796   2107   1493     18   -121    375       C  
ATOM   1881  CG2 VAL C  33     131.341   4.819  51.811  1.00 18.29           C  
ANISOU 1881  CG2 VAL C  33     2323   2653   1974     -1    -78    383       C  
ATOM   1882  N   LEU C  34     127.828   3.531  54.776  1.00 20.42           N  
ANISOU 1882  N   LEU C  34     2542   2917   2298      6   -107    305       N  
ATOM   1883  CA  LEU C  34     126.487   3.557  55.357  1.00 17.75           C  
ANISOU 1883  CA  LEU C  34     2190   2593   1961     12   -120    292       C  
ATOM   1884  C   LEU C  34     126.077   4.935  55.893  1.00 21.87           C  
ANISOU 1884  C   LEU C  34     2716   3097   2495     37   -137    306       C  
ATOM   1885  O   LEU C  34     124.903   5.171  56.181  1.00 24.01           O  
ANISOU 1885  O   LEU C  34     2975   3386   2761     53   -152    301       O  
ATOM   1886  CB  LEU C  34     126.380   2.502  56.466  1.00 14.47           C  
ANISOU 1886  CB  LEU C  34     1763   2169   1566     -2   -102    276       C  
ATOM   1887  CG  LEU C  34     126.211   1.034  56.051  1.00 12.78           C  
ANISOU 1887  CG  LEU C  34     1553   1972   1330    -25    -95    258       C  
ATOM   1888  CD1 LEU C  34     126.898   0.726  54.730  1.00 10.92           C  
ANISOU 1888  CD1 LEU C  34     1341   1745   1061    -29    -92    258       C  
ATOM   1889  CD2 LEU C  34     126.704   0.097  57.142  1.00 12.54           C  
ANISOU 1889  CD2 LEU C  34     1527   1913   1325    -35    -75    256       C  
ATOM   1890  N   SER C  35     127.043   5.847  55.991  1.00 23.81           N  
ANISOU 1890  N   SER C  35     2983   3310   2755     42   -137    323       N  
ATOM   1891  CA  SER C  35     126.830   7.154  56.618  1.00 23.80           C  
ANISOU 1891  CA  SER C  35     3003   3278   2763     65   -155    333       C  
ATOM   1892  C   SER C  35     126.365   8.227  55.639  1.00 24.88           C  
ANISOU 1892  C   SER C  35     3159   3417   2878     90   -187    357       C  
ATOM   1893  O   SER C  35     126.689   8.173  54.454  1.00 24.24           O  
ANISOU 1893  O   SER C  35     3082   3354   2774     83   -190    373       O  
ATOM   1894  CB  SER C  35     128.116   7.631  57.297  1.00 26.65           C  
ANISOU 1894  CB  SER C  35     3381   3599   3146     54   -148    340       C  
ATOM   1895  OG  SER C  35     128.558   6.717  58.288  1.00 29.82           O  
ANISOU 1895  OG  SER C  35     3767   3998   3567     35   -128    323       O  
ATOM   1896  N   PRO C  36     125.605   9.214  56.142  1.00 27.72           N  
ANISOU 1896  N   PRO C  36     3535   3755   3242    123   -213    363       N  
ATOM   1897  CA  PRO C  36     125.140  10.367  55.360  1.00 28.01           C  
ANISOU 1897  CA  PRO C  36     3596   3781   3265    156   -253    393       C  
ATOM   1898  C   PRO C  36     126.293  11.247  54.888  1.00 27.04           C  
ANISOU 1898  C   PRO C  36     3515   3620   3137    151   -255    422       C  
ATOM   1899  O   PRO C  36     127.293  11.377  55.592  1.00 28.90           O  
ANISOU 1899  O   PRO C  36     3766   3825   3390    134   -236    417       O  
ATOM   1900  CB  PRO C  36     124.280  11.150  56.362  1.00 28.90           C  
ANISOU 1900  CB  PRO C  36     3717   3866   3398    193   -277    390       C  
ATOM   1901  CG  PRO C  36     123.893  10.156  57.401  1.00 30.52           C  
ANISOU 1901  CG  PRO C  36     3888   4095   3612    179   -248    357       C  
ATOM   1902  CD  PRO C  36     125.069   9.229  57.513  1.00 29.40           C  
ANISOU 1902  CD  PRO C  36     3745   3954   3472    135   -210    343       C  
ATOM   1903  N   PHE C  37     126.143  11.842  53.709  1.00 24.98           N  
ANISOU 1903  N   PHE C  37     3273   3366   2851    166   -280    457       N  
ATOM   1904  CA  PHE C  37     127.160  12.721  53.144  1.00 22.94           C  
ANISOU 1904  CA  PHE C  37     3056   3077   2582    162   -280    495       C  
ATOM   1905  C   PHE C  37     127.578  13.829  54.117  1.00 23.28           C  
ANISOU 1905  C   PHE C  37     3143   3054   2649    180   -286    501       C  
ATOM   1906  O   PHE C  37     128.761  14.128  54.255  1.00 19.53           O  
ANISOU 1906  O   PHE C  37     2681   2558   2183    156   -263    516       O  
ATOM   1907  CB  PHE C  37     126.662  13.316  51.821  1.00 21.93           C  
ANISOU 1907  CB  PHE C  37     2951   2963   2417    185   -315    538       C  
ATOM   1908  CG  PHE C  37     127.254  14.659  51.499  1.00 19.90           C  
ANISOU 1908  CG  PHE C  37     2752   2655   2154    202   -327    588       C  
ATOM   1909  CD1 PHE C  37     128.447  14.762  50.801  1.00 18.91           C  
ANISOU 1909  CD1 PHE C  37     2641   2533   2011    169   -299    619       C  
ATOM   1910  CD2 PHE C  37     126.615  15.823  51.896  1.00 20.30           C  
ANISOU 1910  CD2 PHE C  37     2844   2651   2218    253   -366    607       C  
ATOM   1911  CE1 PHE C  37     128.994  16.006  50.507  1.00 17.68           C  
ANISOU 1911  CE1 PHE C  37     2538   2329   1851    180   -304    673       C  
ATOM   1912  CE2 PHE C  37     127.158  17.065  51.615  1.00 19.55           C  
ANISOU 1912  CE2 PHE C  37     2810   2500   2117    274   -370    658       C  
ATOM   1913  CZ  PHE C  37     128.349  17.158  50.920  1.00 18.11           C  
ANISOU 1913  CZ  PHE C  37     2640   2325   1918    234   -337    693       C  
ATOM   1914  N   MET C  38     126.601  14.438  54.783  1.00 26.29           N  
ANISOU 1914  N   MET C  38     3545   3403   3043    222   -320    494       N  
ATOM   1915  CA  MET C  38     126.865  15.514  55.733  1.00 30.33           C  
ANISOU 1915  CA  MET C  38     4105   3848   3572    248   -323    493       C  
ATOM   1916  C   MET C  38     127.827  15.073  56.830  1.00 30.51           C  
ANISOU 1916  C   MET C  38     4120   3868   3603    220   -282    466       C  
ATOM   1917  O   MET C  38     128.871  15.691  57.034  1.00 35.11           O  
ANISOU 1917  O   MET C  38     4720   4428   4191    211   -260    493       O  
ATOM   1918  CB  MET C  38     125.557  15.990  56.364  1.00 33.32           C  
ANISOU 1918  CB  MET C  38     4480   4197   3982    278   -368    480       C  
ATOM   1919  CG  MET C  38     124.584  16.624  55.387  1.00 33.66           C  
ANISOU 1919  CG  MET C  38     4519   4240   4031    316   -418    523       C  
ATOM   1920  SD  MET C  38     125.191  18.190  54.739  1.00 93.51           S  
ANISOU 1920  SD  MET C  38    12184  11748  11599    352   -427    569       S  
ATOM   1921  CE  MET C  38     123.861  18.632  53.622  1.00141.15           C  
ANISOU 1921  CE  MET C  38    18194  17794  17642    395   -498    622       C  
ATOM   1922  N   TYR C  39     127.460  14.009  57.538  1.00 26.34           N  
ANISOU 1922  N   TYR C  39     3557   3369   3082    200   -276    427       N  
ATOM   1923  CA  TYR C  39     128.282  13.466  58.614  1.00 26.81           C  
ANISOU 1923  CA  TYR C  39     3606   3431   3149    173   -246    404       C  
ATOM   1924  C   TYR C  39     129.701  13.201  58.120  1.00 25.71           C  
ANISOU 1924  C   TYR C  39     3439   3307   3024    122   -222    425       C  
ATOM   1925  O   TYR C  39     130.681  13.661  58.717  1.00 24.78           O  
ANISOU 1925  O   TYR C  39     3327   3167   2919     99   -218    438       O  
ATOM   1926  CB  TYR C  39     127.651  12.171  59.142  1.00 29.48           C  
ANISOU 1926  CB  TYR C  39     3901   3806   3494    152   -237    369       C  
ATOM   1927  CG  TYR C  39     128.551  11.333  60.025  1.00 31.15           C  
ANISOU 1927  CG  TYR C  39     4091   4030   3716    116   -207    351       C  
ATOM   1928  CD1 TYR C  39     129.355  10.338  59.485  1.00 32.28           C  
ANISOU 1928  CD1 TYR C  39     4187   4204   3874     74   -184    355       C  
ATOM   1929  CD2 TYR C  39     128.584  11.527  61.398  1.00 32.56           C  
ANISOU 1929  CD2 TYR C  39     4298   4187   3887    127   -208    335       C  
ATOM   1930  CE1 TYR C  39     130.177   9.572  60.285  1.00 34.42           C  
ANISOU 1930  CE1 TYR C  39     4435   4482   4162     43   -168    346       C  
ATOM   1931  CE2 TYR C  39     129.402  10.766  62.207  1.00 33.44           C  
ANISOU 1931  CE2 TYR C  39     4385   4312   4007     91   -191    327       C  
ATOM   1932  CZ  TYR C  39     130.198   9.787  61.648  1.00 34.10           C  
ANISOU 1932  CZ  TYR C  39     4419   4421   4115     48   -175    333       C  
ATOM   1933  OH  TYR C  39     131.017   9.023  62.454  1.00 30.78           O  
ANISOU 1933  OH  TYR C  39     3977   4009   3710     15   -168    331       O  
ATOM   1934  N   ASN C  40     129.799  12.443  57.032  1.00 22.88           N  
ANISOU 1934  N   ASN C  40     3045   2988   2662     98   -213    431       N  
ATOM   1935  CA  ASN C  40     131.079  12.097  56.428  1.00 19.49           C  
ANISOU 1935  CA  ASN C  40     2587   2575   2242     55   -194    452       C  
ATOM   1936  C   ASN C  40     131.928  13.317  56.111  1.00 23.00           C  
ANISOU 1936  C   ASN C  40     3062   2986   2690     46   -203    495       C  
ATOM   1937  O   ASN C  40     133.139  13.303  56.305  1.00 25.14           O  
ANISOU 1937  O   ASN C  40     3314   3256   2983      4   -197    510       O  
ATOM   1938  CB  ASN C  40     130.857  11.279  55.157  1.00 17.34           C  
ANISOU 1938  CB  ASN C  40     2289   2348   1950     49   -183    456       C  
ATOM   1939  CG  ASN C  40     130.069  10.016  55.415  1.00 17.31           C  
ANISOU 1939  CG  ASN C  40     2253   2377   1946     51   -171    419       C  
ATOM   1940  OD1 ASN C  40     130.150   9.435  56.497  1.00 18.05           O  
ANISOU 1940  OD1 ASN C  40     2331   2466   2060     41   -161    393       O  
ATOM   1941  ND2 ASN C  40     129.294   9.586  54.424  1.00 16.40           N  
ANISOU 1941  ND2 ASN C  40     2132   2297   1804     60   -176    419       N  
ATOM   1942  N   ASN C  41     131.285  14.377  55.634  1.00 27.42           N  
ANISOU 1942  N   ASN C  41     3669   3518   3231     84   -221    521       N  
ATOM   1943  CA  ASN C  41     132.000  15.586  55.251  1.00 30.92           C  
ANISOU 1943  CA  ASN C  41     4148   3922   3679     76   -226    573       C  
ATOM   1944  C   ASN C  41     132.483  16.359  56.468  1.00 32.49           C  
ANISOU 1944  C   ASN C  41     4367   4072   3906     66   -232    575       C  
ATOM   1945  O   ASN C  41     133.686  16.503  56.676  1.00 32.39           O  
ANISOU 1945  O   ASN C  41     4340   4050   3917     11   -232    592       O  
ATOM   1946  CB  ASN C  41     131.133  16.478  54.361  1.00 34.90           C  
ANISOU 1946  CB  ASN C  41     4701   4406   4155    127   -244    608       C  
ATOM   1947  CG  ASN C  41     131.872  17.712  53.881  1.00 39.10           C  
ANISOU 1947  CG  ASN C  41     5274   4891   4692    116   -243    672       C  
ATOM   1948  OD1 ASN C  41     133.084  17.829  54.064  1.00 42.94           O  
ANISOU 1948  OD1 ASN C  41     5747   5367   5203     60   -231    688       O  
ATOM   1949  ND2 ASN C  41     131.150  18.631  53.249  1.00 39.03           N  
ANISOU 1949  ND2 ASN C  41     5316   4851   4663    168   -259    712       N  
ATOM   1950  N   LYS C  42     131.541  16.848  57.269  1.00 32.54           N  
ANISOU 1950  N   LYS C  42     4402   4051   3909    119   -238    561       N  
ATOM   1951  CA  LYS C  42     131.871  17.642  58.449  1.00 31.70           C  
ANISOU 1951  CA  LYS C  42     4319   3896   3830    110   -243    568       C  
ATOM   1952  C   LYS C  42     132.847  16.937  59.397  1.00 28.20           C  
ANISOU 1952  C   LYS C  42     3845   3468   3402     44   -251    537       C  
ATOM   1953  O   LYS C  42     133.773  17.562  59.912  1.00 28.24           O  
ANISOU 1953  O   LYS C  42     3867   3434   3430     -5   -270    553       O  
ATOM   1954  CB  LYS C  42     130.598  18.040  59.206  1.00 33.38           C  
ANISOU 1954  CB  LYS C  42     4546   4097   4041    182   -237    561       C  
ATOM   1955  CG  LYS C  42     129.696  19.021  58.457  1.00 37.21           C  
ANISOU 1955  CG  LYS C  42     5053   4556   4530    250   -234    605       C  
ATOM   1956  CD  LYS C  42     128.442  19.369  59.260  1.00 41.12           C  
ANISOU 1956  CD  LYS C  42     5511   5053   5060    299   -228    608       C  
ATOM   1957  CE  LYS C  42     127.561  20.379  58.509  1.00 44.38           C  
ANISOU 1957  CE  LYS C  42     5916   5440   5507    355   -231    665       C  
ATOM   1958  NZ  LYS C  42     126.276  20.699  59.225  1.00 44.57           N  
ANISOU 1958  NZ  LYS C  42     5888   5435   5611    365   -274    685       N  
ATOM   1959  N   THR C  43     132.641  15.643  59.628  1.00 24.49           N  
ANISOU 1959  N   THR C  43     3333   3050   2921     41   -240    497       N  
ATOM   1960  CA  THR C  43     133.456  14.920  60.602  1.00 18.84           C  
ANISOU 1960  CA  THR C  43     2588   2350   2220    -10   -247    474       C  
ATOM   1961  C   THR C  43     134.687  14.257  59.989  1.00 18.96           C  
ANISOU 1961  C   THR C  43     2551   2396   2256    -65   -245    490       C  
ATOM   1962  O   THR C  43     135.565  13.785  60.710  1.00 12.74           O  
ANISOU 1962  O   THR C  43     1735   1621   1486   -108   -257    486       O  
ATOM   1963  CB  THR C  43     132.627  13.844  61.327  1.00 12.96           C  
ANISOU 1963  CB  THR C  43     1827   1638   1459     17   -233    430       C  
ATOM   1964  OG1 THR C  43     132.313  12.785  60.414  1.00 10.28           O  
ANISOU 1964  OG1 THR C  43     1450   1338   1117     21   -212    418       O  
ATOM   1965  CG2 THR C  43     131.336  14.444  61.865  1.00 10.83           C  
ANISOU 1965  CG2 THR C  43     1594   1355   1167     82   -228    422       C  
ATOM   1966  N   GLY C  44     134.747  14.214  58.663  1.00 24.27           N  
ANISOU 1966  N   GLY C  44     3212   3087   2924    -59   -229    513       N  
ATOM   1967  CA  GLY C  44     135.839  13.541  57.986  1.00 26.95           C  
ANISOU 1967  CA  GLY C  44     3497   3464   3277    -98   -217    533       C  
ATOM   1968  C   GLY C  44     135.887  12.070  58.357  1.00 29.08           C  
ANISOU 1968  C   GLY C  44     3718   3776   3555   -100   -200    502       C  
ATOM   1969  O   GLY C  44     136.864  11.380  58.073  1.00 29.93           O  
ANISOU 1969  O   GLY C  44     3775   3916   3680   -124   -189    518       O  
ATOM   1970  N   MET C  45     134.818  11.599  58.996  1.00 29.65           N  
ANISOU 1970  N   MET C  45     3804   3847   3615    -70   -196    463       N  
ATOM   1971  CA  MET C  45     134.688  10.207  59.419  1.00 27.98           C  
ANISOU 1971  CA  MET C  45     3556   3666   3410    -70   -178    435       C  
ATOM   1972  C   MET C  45     133.478   9.570  58.750  1.00 25.78           C  
ANISOU 1972  C   MET C  45     3280   3406   3110    -36   -158    413       C  
ATOM   1973  O   MET C  45     132.526  10.266  58.396  1.00 26.51           O  
ANISOU 1973  O   MET C  45     3406   3484   3181     -7   -167    411       O  
ATOM   1974  CB  MET C  45     134.509  10.133  60.937  1.00 26.99           C  
ANISOU 1974  CB  MET C  45     3445   3523   3285    -74   -193    413       C  
ATOM   1975  CG  MET C  45     135.698  10.615  61.746  1.00 25.31           C  
ANISOU 1975  CG  MET C  45     3228   3296   3091   -117   -222    434       C  
ATOM   1976  SD  MET C  45     136.865   9.292  62.099  1.00 43.71           S  
ANISOU 1976  SD  MET C  45     5493   5664   5451   -149   -217    448       S  
ATOM   1977  CE  MET C  45     135.837   8.178  63.056  1.00  6.45           C  
ANISOU 1977  CE  MET C  45      786    950    715   -122   -201    410       C  
ATOM   1978  N   CYS C  46     133.509   8.249  58.590  1.00 24.26           N  
ANISOU 1978  N   CYS C  46     3052   3243   2923    -39   -137    400       N  
ATOM   1979  CA  CYS C  46     132.382   7.526  58.012  1.00 22.90           C  
ANISOU 1979  CA  CYS C  46     2879   3090   2731    -18   -123    379       C  
ATOM   1980  C   CYS C  46     132.276   6.093  58.523  1.00 23.03           C  
ANISOU 1980  C   CYS C  46     2871   3123   2758    -21   -106    359       C  
ATOM   1981  O   CYS C  46     133.284   5.454  58.824  1.00 23.19           O  
ANISOU 1981  O   CYS C  46     2866   3147   2797    -35    -98    368       O  
ATOM   1982  CB  CYS C  46     132.483   7.511  56.487  1.00 19.36           C  
ANISOU 1982  CB  CYS C  46     2428   2665   2262    -14   -115    396       C  
ATOM   1983  SG  CYS C  46     133.713   6.348  55.839  1.00 19.73           S  
ANISOU 1983  SG  CYS C  46     2441   2741   2315    -26    -88    408       S  
ATOM   1984  N   LEU C  47     131.043   5.602  58.623  1.00 22.27           N  
ANISOU 1984  N   LEU C  47     2780   3035   2648     -8   -102    337       N  
ATOM   1985  CA  LEU C  47     130.787   4.200  58.924  1.00 20.25           C  
ANISOU 1985  CA  LEU C  47     2508   2793   2396    -12    -86    322       C  
ATOM   1986  C   LEU C  47     130.856   3.412  57.625  1.00 21.01           C  
ANISOU 1986  C   LEU C  47     2597   2911   2474    -10    -74    323       C  
ATOM   1987  O   LEU C  47     130.321   3.840  56.602  1.00 19.84           O  
ANISOU 1987  O   LEU C  47     2459   2780   2301     -4    -81    324       O  
ATOM   1988  CB  LEU C  47     129.402   4.022  59.555  1.00 15.63           C  
ANISOU 1988  CB  LEU C  47     1928   2212   1799     -3    -89    303       C  
ATOM   1989  CG  LEU C  47     129.101   4.771  60.856  1.00 11.33           C  
ANISOU 1989  CG  LEU C  47     1404   1646   1256      4   -100    298       C  
ATOM   1990  CD1 LEU C  47     127.671   4.509  61.301  1.00  9.11           C  
ANISOU 1990  CD1 LEU C  47     1121   1382    959     16    -98    284       C  
ATOM   1991  CD2 LEU C  47     130.084   4.378  61.949  1.00 12.87           C  
ANISOU 1991  CD2 LEU C  47     1598   1825   1466    -13    -99    303       C  
ATOM   1992  N   CYS C  48     131.511   2.259  57.656  1.00 23.99           N  
ANISOU 1992  N   CYS C  48     2967   3288   2859    -13    -59    324       N  
ATOM   1993  CA  CYS C  48     131.611   1.447  56.450  1.00 26.02           C  
ANISOU 1993  CA  CYS C  48     3237   3561   3088     -9    -45    322       C  
ATOM   1994  C   CYS C  48     131.748  -0.038  56.746  1.00 26.70           C  
ANISOU 1994  C   CYS C  48     3336   3635   3175     -8    -27    315       C  
ATOM   1995  O   CYS C  48     132.248  -0.436  57.803  1.00 28.15           O  
ANISOU 1995  O   CYS C  48     3508   3798   3389     -6    -24    325       O  
ATOM   1996  CB  CYS C  48     132.780   1.915  55.580  1.00 25.88           C  
ANISOU 1996  CB  CYS C  48     3217   3550   3065     -5    -35    346       C  
ATOM   1997  SG  CYS C  48     134.380   1.846  56.405  1.00 30.22           S  
ANISOU 1997  SG  CYS C  48     3734   4087   3661     -4    -26    375       S  
ATOM   1998  N   VAL C  49     131.299  -0.853  55.799  1.00 25.74           N  
ANISOU 1998  N   VAL C  49     3246   3522   3011    -12    -14    300       N  
ATOM   1999  CA  VAL C  49     131.452  -2.294  55.904  1.00 27.85           C  
ANISOU 1999  CA  VAL C  49     3548   3764   3268    -16     17    295       C  
ATOM   2000  C   VAL C  49     132.419  -2.779  54.832  1.00 33.09           C  
ANISOU 2000  C   VAL C  49     4232   4440   3903    -13     60    310       C  
ATOM   2001  O   VAL C  49     132.150  -2.650  53.639  1.00 37.68           O  
ANISOU 2001  O   VAL C  49     4833   5055   4428    -22     70    296       O  
ATOM   2002  CB  VAL C  49     130.096  -3.023  55.796  1.00 28.92           C  
ANISOU 2002  CB  VAL C  49     3700   3921   3366    -39     17    275       C  
ATOM   2003  CG1 VAL C  49     129.228  -2.700  56.998  1.00 28.38           C  
ANISOU 2003  CG1 VAL C  49     3611   3843   3331    -41     -9    267       C  
ATOM   2004  CG2 VAL C  49     129.379  -2.639  54.509  1.00 31.27           C  
ANISOU 2004  CG2 VAL C  49     4003   4269   3609    -50      3    254       C  
ATOM   2005  N   PRO C  50     133.570  -3.313  55.259  1.00 33.93           N  
ANISOU 2005  N   PRO C  50     4321   4527   4044      3     89    343       N  
ATOM   2006  CA  PRO C  50     134.594  -3.801  54.329  1.00 32.24           C  
ANISOU 2006  CA  PRO C  50     4106   4332   3813     18    151    368       C  
ATOM   2007  C   PRO C  50     134.081  -4.955  53.478  1.00 29.79           C  
ANISOU 2007  C   PRO C  50     3837   4042   3439      3    220    341       C  
ATOM   2008  O   PRO C  50     133.250  -5.738  53.939  1.00 29.33           O  
ANISOU 2008  O   PRO C  50     3798   3970   3374    -15    228    330       O  
ATOM   2009  CB  PRO C  50     135.718  -4.280  55.259  1.00 33.29           C  
ANISOU 2009  CB  PRO C  50     4196   4433   4018     54    169    418       C  
ATOM   2010  CG  PRO C  50     135.057  -4.512  56.581  1.00 34.66           C  
ANISOU 2010  CG  PRO C  50     4374   4573   4223     43    124    410       C  
ATOM   2011  CD  PRO C  50     133.971  -3.488  56.665  1.00 35.36           C  
ANISOU 2011  CD  PRO C  50     4478   4671   4284     15     70    361       C  
ATOM   2012  N   CYS C  51     134.565  -5.048  52.245  1.00 29.15           N  
ANISOU 2012  N   CYS C  51     3773   3995   3308      5    279    322       N  
ATOM   2013  CA  CYS C  51     134.137  -6.106  51.341  1.00 31.26           C  
ANISOU 2013  CA  CYS C  51     4089   4287   3502     -9    359    263       C  
ATOM   2014  C   CYS C  51     135.287  -7.069  51.074  1.00 33.92           C  
ANISOU 2014  C   CYS C  51     4428   4577   3883     44    478    256       C  
ATOM   2015  O   CYS C  51     136.447  -6.664  51.049  1.00 35.86           O  
ANISOU 2015  O   CYS C  51     4627   4824   4174     80    498    304       O  
ATOM   2016  CB  CYS C  51     133.623  -5.503  50.034  1.00 30.16           C  
ANISOU 2016  CB  CYS C  51     3990   4200   3268    -44    337    213       C  
ATOM   2017  SG  CYS C  51     132.384  -4.195  50.269  1.00 43.52           S  
ANISOU 2017  SG  CYS C  51     5670   5899   4965    -56    206    226       S  
ATOM   2018  N   THR C  52     134.967  -8.346  50.891  1.00 33.71           N  
ANISOU 2018  N   THR C  52     4447   4483   3877     34    528    172       N  
ATOM   2019  CA  THR C  52     135.992  -9.345  50.607  1.00 32.56           C  
ANISOU 2019  CA  THR C  52     4310   4263   3800     88    636    140       C  
ATOM   2020  C   THR C  52     135.656 -10.114  49.336  1.00 30.99           C  
ANISOU 2020  C   THR C  52     4188   4060   3527     58    706     13       C  
ATOM   2021  O   THR C  52     134.592  -9.920  48.748  1.00 28.38           O  
ANISOU 2021  O   THR C  52     3902   3787   3095    -10    658    -46       O  
ATOM   2022  CB  THR C  52     136.161 -10.343  51.777  1.00 35.80           C  
ANISOU 2022  CB  THR C  52     4709   4556   4336    121    644    167       C  
ATOM   2023  OG1 THR C  52     137.183 -11.295  51.454  1.00 39.20           O  
ANISOU 2023  OG1 THR C  52     5143   4908   4842    187    752    139       O  
ATOM   2024  CG2 THR C  52     134.857 -11.080  52.051  1.00 35.72           C  
ANISOU 2024  CG2 THR C  52     4757   4499   4315     57    612    102       C  
ATOM   2025  N   THR C  53     136.553 -11.004  48.927  1.00 34.50           N  
ANISOU 2025  N   THR C  53     4649   4436   4024    111    818    -33       N  
ATOM   2026  CA  THR C  53     136.348 -11.772  47.701  1.00 37.77           C  
ANISOU 2026  CA  THR C  53     5148   4839   4365     86    898   -167       C  
ATOM   2027  C   THR C  53     136.122 -13.259  47.990  1.00 42.00           C  
ANISOU 2027  C   THR C  53     5741   5231   4987     89    951   -248       C  
ATOM   2028  O   THR C  53     135.060 -13.798  47.677  1.00 42.93           O  
ANISOU 2028  O   THR C  53     5929   5331   5053     12    926   -342       O  
ATOM   2029  CB  THR C  53     137.464 -11.521  46.649  1.00 23.08           C  
ANISOU 2029  CB  THR C  53     3278   3030   2463    132    998   -181       C  
ATOM   2030  OG1 THR C  53     136.862 -11.161  45.400  1.00 26.48           O  
ANISOU 2030  OG1 THR C  53     3756   3559   2748     67    957   -250       O  
ATOM   2031  CG2 THR C  53     138.344 -12.752  46.444  1.00 27.09           C  
ANISOU 2031  CG2 THR C  53     3801   3426   3066    202   1121   -244       C  
ATOM   2032  N   GLN C  54     137.111 -13.921  48.584  1.00 46.50           N  
ANISOU 2032  N   GLN C  54     6278   5697   5693    177   1021   -208       N  
ATOM   2033  CA  GLN C  54     136.930 -15.298  49.018  1.00 49.74           C  
ANISOU 2033  CA  GLN C  54     6743   5953   6205    188   1065   -261       C  
ATOM   2034  C   GLN C  54     135.776 -15.315  50.009  1.00 54.19           C  
ANISOU 2034  C   GLN C  54     7311   6498   6782    116    955   -224       C  
ATOM   2035  O   GLN C  54     135.786 -14.583  51.000  1.00 53.65           O  
ANISOU 2035  O   GLN C  54     7173   6471   6742    127    874   -107       O  
ATOM   2036  CB  GLN C  54     138.208 -15.838  49.661  1.00 48.58           C  
ANISOU 2036  CB  GLN C  54     6540   5707   6213    308   1136   -188       C  
ATOM   2037  N   SER C  55     134.781 -16.149  49.734  1.00 57.45           N  
ANISOU 2037  N   SER C  55     7807   6850   7171     38    956   -330       N  
ATOM   2038  CA  SER C  55     133.530 -16.108  50.477  1.00 58.99           C  
ANISOU 2038  CA  SER C  55     8004   7051   7358    -49    858   -311       C  
ATOM   2039  C   SER C  55     133.264 -17.395  51.250  1.00 61.23           C  
ANISOU 2039  C   SER C  55     8335   7171   7758    -60    887   -321       C  
ATOM   2040  O   SER C  55     133.307 -18.493  50.690  1.00 64.01           O  
ANISOU 2040  O   SER C  55     8768   7410   8142    -69    968   -426       O  
ATOM   2041  CB  SER C  55     132.364 -15.809  49.531  1.00 62.89           C  
ANISOU 2041  CB  SER C  55     8539   7644   7714   -158    807   -412       C  
ATOM   2042  OG  SER C  55     131.144 -15.682  50.241  1.00 66.08           O  
ANISOU 2042  OG  SER C  55     8924   8071   8114   -240    714   -389       O  
ATOM   2043  N   LYS C  56     132.988 -17.239  52.541  1.00 59.61           N  
ANISOU 2043  N   LYS C  56     8085   6949   7613    -62    822   -211       N  
ATOM   2044  CA  LYS C  56     132.708 -18.362  53.426  1.00 57.75           C  
ANISOU 2044  CA  LYS C  56     7891   6565   7486    -76    841   -191       C  
ATOM   2045  C   LYS C  56     131.218 -18.692  53.487  1.00 57.09           C  
ANISOU 2045  C   LYS C  56     7848   6483   7363   -210    794   -254       C  
ATOM   2046  O   LYS C  56     130.826 -19.728  54.024  1.00 58.99           O  
ANISOU 2046  O   LYS C  56     8139   6592   7683   -248    819   -261       O  
ATOM   2047  CB  LYS C  56     133.231 -18.060  54.834  1.00 56.07           C  
ANISOU 2047  CB  LYS C  56     7614   6339   7351    -11    799    -30       C  
ATOM   2048  CG  LYS C  56     134.700 -17.617  54.888  1.00 55.81           C  
ANISOU 2048  CG  LYS C  56     7518   6326   7363    114    826     49       C  
ATOM   2049  CD  LYS C  56     134.850 -16.124  55.195  1.00 52.67           C  
ANISOU 2049  CD  LYS C  56     7033   6085   6893    121    742    133       C  
ATOM   2050  CE  LYS C  56     134.760 -15.844  56.692  1.00 49.89           C  
ANISOU 2050  CE  LYS C  56     6642   5735   6581    126    666    262       C  
ATOM   2051  NZ  LYS C  56     133.460 -16.266  57.292  1.00 48.23           N  
ANISOU 2051  NZ  LYS C  56     6476   5493   6357     33    632    248       N  
ATOM   2052  N   GLY C  57     130.391 -17.813  52.930  1.00 54.88           N  
ANISOU 2052  N   GLY C  57     7539   6348   6963   -281    726   -296       N  
ATOM   2053  CA  GLY C  57     128.950 -17.972  53.013  1.00 53.25           C  
ANISOU 2053  CA  GLY C  57     7341   6171   6719   -407    670   -346       C  
ATOM   2054  C   GLY C  57     128.442 -17.614  54.399  1.00 50.34           C  
ANISOU 2054  C   GLY C  57     6915   5822   6389   -421    611   -228       C  
ATOM   2055  O   GLY C  57     127.337 -17.992  54.793  1.00 50.83           O  
ANISOU 2055  O   GLY C  57     6980   5874   6460   -518    585   -246       O  
ATOM   2056  N   TYR C  58     129.272 -16.884  55.138  1.00 47.25           N  
ANISOU 2056  N   TYR C  58     6470   5463   6020   -327    594   -109       N  
ATOM   2057  CA  TYR C  58     128.954 -16.423  56.489  1.00 44.81           C  
ANISOU 2057  CA  TYR C  58     6111   5182   5732   -327    541      6       C  
ATOM   2058  C   TYR C  58     127.634 -15.655  56.539  1.00 41.39           C  
ANISOU 2058  C   TYR C  58     5630   4874   5220   -412    468    -12       C  
ATOM   2059  O   TYR C  58     127.313 -14.910  55.616  1.00 39.25           O  
ANISOU 2059  O   TYR C  58     5336   4713   4865   -428    432    -68       O  
ATOM   2060  CB  TYR C  58     130.095 -15.544  57.009  1.00 47.99           C  
ANISOU 2060  CB  TYR C  58     6462   5629   6143   -221    521    114       C  
ATOM   2061  CG  TYR C  58     129.957 -15.123  58.449  1.00 52.34           C  
ANISOU 2061  CG  TYR C  58     6976   6199   6712   -213    472    231       C  
ATOM   2062  CD1 TYR C  58     130.282 -15.995  59.481  1.00 55.50           C  
ANISOU 2062  CD1 TYR C  58     7405   6486   7197   -192    498    307       C  
ATOM   2063  CD2 TYR C  58     129.518 -13.848  58.780  1.00 53.59           C  
ANISOU 2063  CD2 TYR C  58     7077   6485   6798   -223    403    267       C  
ATOM   2064  CE1 TYR C  58     130.159 -15.615  60.801  1.00 56.58           C  
ANISOU 2064  CE1 TYR C  58     7517   6648   7332   -189    453    413       C  
ATOM   2065  CE2 TYR C  58     129.396 -13.459  60.096  1.00 54.63           C  
ANISOU 2065  CE2 TYR C  58     7185   6637   6936   -217    365    362       C  
ATOM   2066  CZ  TYR C  58     129.716 -14.346  61.105  1.00 55.87           C  
ANISOU 2066  CZ  TYR C  58     7374   6691   7163   -204    389    433       C  
ATOM   2067  OH  TYR C  58     129.595 -13.965  62.423  1.00 55.18           O  
ANISOU 2067  OH  TYR C  58     7252   6663   7052   -199    312    489       O  
ATOM   2068  N   PRO C  59     126.870 -15.832  57.629  1.00 39.37           N  
ANISOU 2068  N   PRO C  59     5360   4607   4994   -461    450     41       N  
ATOM   2069  CA  PRO C  59     125.538 -15.246  57.818  1.00 35.62           C  
ANISOU 2069  CA  PRO C  59     4829   4240   4463   -541    394     26       C  
ATOM   2070  C   PRO C  59     125.441 -13.752  57.506  1.00 31.42           C  
ANISOU 2070  C   PRO C  59     4232   3860   3849   -502    327     42       C  
ATOM   2071  O   PRO C  59     124.430 -13.318  56.957  1.00 33.65           O  
ANISOU 2071  O   PRO C  59     4475   4237   4075   -560    283    -12       O  
ATOM   2072  CB  PRO C  59     125.277 -15.475  59.307  1.00 33.84           C  
ANISOU 2072  CB  PRO C  59     4596   3974   4287   -552    400    123       C  
ATOM   2073  CG  PRO C  59     126.004 -16.730  59.611  1.00 36.01           C  
ANISOU 2073  CG  PRO C  59     4946   4086   4651   -533    465    146       C  
ATOM   2074  CD  PRO C  59     127.241 -16.716  58.749  1.00 38.17           C  
ANISOU 2074  CD  PRO C  59     5244   4327   4933   -444    490    120       C  
ATOM   2075  N   PHE C  60     126.457 -12.978  57.866  1.00 27.99           N  
ANISOU 2075  N   PHE C  60     3781   3443   3411   -409    316    120       N  
ATOM   2076  CA  PHE C  60     126.394 -11.530  57.696  1.00 25.93           C  
ANISOU 2076  CA  PHE C  60     3465   3306   3081   -373    256    146       C  
ATOM   2077  C   PHE C  60     126.935 -11.063  56.345  1.00 26.12           C  
ANISOU 2077  C   PHE C  60     3496   3378   3050   -343    251     97       C  
ATOM   2078  O   PHE C  60     127.036  -9.865  56.086  1.00 23.39           O  
ANISOU 2078  O   PHE C  60     3115   3122   2650   -308    205    125       O  
ATOM   2079  CB  PHE C  60     127.087 -10.817  58.860  1.00 26.49           C  
ANISOU 2079  CB  PHE C  60     3514   3381   3169   -307    238    253       C  
ATOM   2080  CG  PHE C  60     126.380 -10.988  60.176  1.00 28.00           C  
ANISOU 2080  CG  PHE C  60     3695   3562   3381   -341    234    301       C  
ATOM   2081  CD1 PHE C  60     126.792 -11.952  61.079  1.00 31.32           C  
ANISOU 2081  CD1 PHE C  60     4154   3881   3864   -340    273    354       C  
ATOM   2082  CD2 PHE C  60     125.297 -10.191  60.506  1.00 30.10           C  
ANISOU 2082  CD2 PHE C  60     3913   3921   3605   -372    195    297       C  
ATOM   2083  CE1 PHE C  60     126.141 -12.116  62.297  1.00 33.23           C  
ANISOU 2083  CE1 PHE C  60     4381   4121   4123   -355    268    392       C  
ATOM   2084  CE2 PHE C  60     124.635 -10.351  61.720  1.00 34.25           C  
ANISOU 2084  CE2 PHE C  60     4424   4437   4154   -384    200    324       C  
ATOM   2085  CZ  PHE C  60     125.060 -11.314  62.618  1.00 34.73           C  
ANISOU 2085  CZ  PHE C  60     4522   4401   4271   -372    237    367       C  
ATOM   2086  N   GLU C  61     127.288 -12.020  55.492  1.00 28.51           N  
ANISOU 2086  N   GLU C  61     3853   3615   3364   -357    304     25       N  
ATOM   2087  CA  GLU C  61     127.733 -11.721  54.137  1.00 24.64           C  
ANISOU 2087  CA  GLU C  61     3382   3172   2809   -340    313    -33       C  
ATOM   2088  C   GLU C  61     126.598 -11.141  53.303  1.00 25.75           C  
ANISOU 2088  C   GLU C  61     3499   3429   2855   -403    249    -91       C  
ATOM   2089  O   GLU C  61     125.442 -11.544  53.445  1.00 25.41           O  
ANISOU 2089  O   GLU C  61     3444   3399   2813   -481    222   -133       O  
ATOM   2090  CB  GLU C  61     128.254 -12.988  53.458  1.00 20.80           C  
ANISOU 2090  CB  GLU C  61     2967   2582   2355   -347    395   -114       C  
ATOM   2091  CG  GLU C  61     129.529 -13.553  54.044  1.00 19.09           C  
ANISOU 2091  CG  GLU C  61     2767   2252   2233   -266    462    -57       C  
ATOM   2092  CD  GLU C  61     130.038 -14.743  53.255  1.00 21.34           C  
ANISOU 2092  CD  GLU C  61     3126   2432   2552   -260    551   -147       C  
ATOM   2093  OE1 GLU C  61     129.587 -14.934  52.103  1.00 17.26           O  
ANISOU 2093  OE1 GLU C  61     2650   1949   1961   -315    561   -257       O  
ATOM   2094  OE2 GLU C  61     130.885 -15.488  53.790  1.00 25.16           O  
ANISOU 2094  OE2 GLU C  61     3627   2798   3134   -199    611   -108       O  
ATOM   2095  N   VAL C  62     126.931 -10.182  52.446  1.00 26.78           N  
ANISOU 2095  N   VAL C  62     3620   3648   2907   -369    222    -85       N  
ATOM   2096  CA  VAL C  62     125.973  -9.651  51.488  1.00 28.92           C  
ANISOU 2096  CA  VAL C  62     3876   4032   3081   -419    157   -134       C  
ATOM   2097  C   VAL C  62     126.615  -9.556  50.112  1.00 37.01           C  
ANISOU 2097  C   VAL C  62     4950   5093   4019   -407    182   -183       C  
ATOM   2098  O   VAL C  62     127.563  -8.799  49.908  1.00 41.42           O  
ANISOU 2098  O   VAL C  62     5507   5673   4559   -340    198   -125       O  
ATOM   2099  CB  VAL C  62     125.463  -8.263  51.909  1.00 26.20           C  
ANISOU 2099  CB  VAL C  62     3462   3782   2710   -389     77    -55       C  
ATOM   2100  CG1 VAL C  62     124.563  -7.679  50.836  1.00 26.54           C  
ANISOU 2100  CG1 VAL C  62     3487   3944   2653   -426      4    -92       C  
ATOM   2101  CG2 VAL C  62     124.729  -8.351  53.239  1.00 24.89           C  
ANISOU 2101  CG2 VAL C  62     3249   3592   2615   -406     61    -18       C  
ATOM   2102  N   VAL C  63     126.090 -10.322  49.165  1.00 38.28           N  
ANISOU 2102  N   VAL C  63     5158   5263   4123   -479    187   -292       N  
ATOM   2103  CA  VAL C  63     126.654 -10.355  47.824  1.00 36.80           C  
ANISOU 2103  CA  VAL C  63     5032   5112   3839   -476    221   -353       C  
ATOM   2104  C   VAL C  63     126.480  -9.013  47.127  1.00 36.90           C  
ANISOU 2104  C   VAL C  63     4999   5232   3791   -434    140   -285       C  
ATOM   2105  O   VAL C  63     125.382  -8.455  47.109  1.00 36.92           O  
ANISOU 2105  O   VAL C  63     4945   5293   3790   -453     49   -262       O  
ATOM   2106  CB  VAL C  63     126.009 -11.461  46.970  1.00 36.45           C  
ANISOU 2106  CB  VAL C  63     5052   5054   3744   -572    232   -493       C  
ATOM   2107  CG1 VAL C  63     126.527 -11.402  45.540  1.00 37.35           C  
ANISOU 2107  CG1 VAL C  63     5210   5199   3783   -546    251   -532       C  
ATOM   2108  CG2 VAL C  63     126.281 -12.822  47.583  1.00 37.32           C  
ANISOU 2108  CG2 VAL C  63     5205   5005   3968   -586    315   -544       C  
ATOM   2109  N   LEU C  64     127.563  -8.498  46.550  1.00 38.21           N  
ANISOU 2109  N   LEU C  64     5182   5398   3938   -364    180   -246       N  
ATOM   2110  CA  LEU C  64     127.490  -7.257  45.788  1.00 37.71           C  
ANISOU 2110  CA  LEU C  64     5092   5395   3842   -317    116   -180       C  
ATOM   2111  C   LEU C  64     127.457  -7.575  44.296  1.00 44.51           C  
ANISOU 2111  C   LEU C  64     6009   6292   4609   -340    125   -250       C  
ATOM   2112  O   LEU C  64     128.468  -7.959  43.703  1.00 48.14           O  
ANISOU 2112  O   LEU C  64     6520   6731   5038   -317    208   -280       O  
ATOM   2113  CB  LEU C  64     128.684  -6.357  46.113  1.00 31.15           C  
ANISOU 2113  CB  LEU C  64     4245   4538   3053   -235    150    -85       C  
ATOM   2114  CG  LEU C  64     128.843  -5.982  47.585  1.00 23.78           C  
ANISOU 2114  CG  LEU C  64     3259   3563   2212   -206    139    -12       C  
ATOM   2115  CD1 LEU C  64     130.093  -5.144  47.787  1.00 20.01           C  
ANISOU 2115  CD1 LEU C  64     2771   3051   1780   -138    170     68       C  
ATOM   2116  CD2 LEU C  64     127.615  -5.245  48.087  1.00 21.48           C  
ANISOU 2116  CD2 LEU C  64     2914   3295   1954   -214     44     19       C  
ATOM   2117  N   SER C  65     126.284  -7.394  43.698  1.00 45.69           N  
ANISOU 2117  N   SER C  65     6146   6498   4717   -382     40   -271       N  
ATOM   2118  CA  SER C  65     126.047  -7.788  42.316  1.00 45.82           C  
ANISOU 2118  CA  SER C  65     6218   6556   4637   -417     33   -343       C  
ATOM   2119  C   SER C  65     126.481  -6.726  41.309  1.00 46.94           C  
ANISOU 2119  C   SER C  65     6379   6741   4715   -362     17   -280       C  
ATOM   2120  O   SER C  65     126.401  -5.528  41.583  1.00 46.09           O  
ANISOU 2120  O   SER C  65     6228   6641   4642   -313    -29   -184       O  
ATOM   2121  CB  SER C  65     124.570  -8.135  42.114  1.00 47.02           C  
ANISOU 2121  CB  SER C  65     6344   6751   4770   -492    -54   -392       C  
ATOM   2122  OG  SER C  65     124.352  -8.738  40.846  1.00 51.01           O  
ANISOU 2122  OG  SER C  65     6912   7289   5181   -539    -58   -478       O  
ATOM   2123  N   GLY C  66     126.938  -7.177  40.143  1.00 47.94           N  
ANISOU 2123  N   GLY C  66     6576   6888   4751   -372     62   -341       N  
ATOM   2124  CA  GLY C  66     127.285  -6.283  39.052  1.00 45.25           C  
ANISOU 2124  CA  GLY C  66     6268   6595   4331   -333     51   -291       C  
ATOM   2125  C   GLY C  66     128.477  -5.412  39.382  1.00 42.90           C  
ANISOU 2125  C   GLY C  66     5960   6265   4076   -259    108   -198       C  
ATOM   2126  O   GLY C  66     128.607  -4.294  38.881  1.00 40.17           O  
ANISOU 2126  O   GLY C  66     5618   5940   3703   -225     80   -122       O  
ATOM   2127  N   GLN C  67     129.354  -5.936  40.228  1.00 44.23           N  
ANISOU 2127  N   GLN C  67     6115   6376   4315   -237    191   -204       N  
ATOM   2128  CA  GLN C  67     130.489  -5.171  40.714  1.00 41.96           C  
ANISOU 2128  CA  GLN C  67     5804   6052   4085   -174    243   -114       C  
ATOM   2129  C   GLN C  67     131.731  -5.404  39.861  1.00 41.99           C  
ANISOU 2129  C   GLN C  67     5854   6066   4035   -142    351   -129       C  
ATOM   2130  O   GLN C  67     131.699  -6.158  38.889  1.00 39.56           O  
ANISOU 2130  O   GLN C  67     5598   5791   3641   -165    387   -214       O  
ATOM   2131  CB  GLN C  67     130.770  -5.523  42.175  1.00 39.62           C  
ANISOU 2131  CB  GLN C  67     5458   5696   3900   -163    267    -97       C  
ATOM   2132  CG  GLN C  67     131.095  -4.321  43.035  1.00 37.76           C  
ANISOU 2132  CG  GLN C  67     5173   5424   3748   -124    235     11       C  
ATOM   2133  CD  GLN C  67     130.024  -3.249  42.955  1.00 37.84           C  
ANISOU 2133  CD  GLN C  67     5161   5454   3762   -133    125     52       C  
ATOM   2134  OE1 GLN C  67     130.303  -2.104  42.601  1.00 36.66           O  
ANISOU 2134  OE1 GLN C  67     5017   5300   3614   -110    106    114       O  
ATOM   2135  NE2 GLN C  67     128.788  -3.617  43.284  1.00 39.70           N  
ANISOU 2135  NE2 GLN C  67     5369   5711   4003   -168     59     16       N  
ATOM   2136  N   GLU C  68     132.823  -4.749  40.235  1.00 43.78           N  
ANISOU 2136  N   GLU C  68     6056   6261   4316    -93    406    -48       N  
ATOM   2137  CA  GLU C  68     134.079  -4.868  39.512  1.00 48.61           C  
ANISOU 2137  CA  GLU C  68     6691   6888   4892    -54    519    -45       C  
ATOM   2138  C   GLU C  68     134.509  -6.333  39.449  1.00 51.12           C  
ANISOU 2138  C   GLU C  68     7009   7207   5206    -52    611   -151       C  
ATOM   2139  O   GLU C  68     134.961  -6.818  38.411  1.00 50.40           O  
ANISOU 2139  O   GLU C  68     6958   7153   5039    -47    681   -212       O  
ATOM   2140  CB  GLU C  68     135.144  -4.017  40.203  1.00 51.11           C  
ANISOU 2140  CB  GLU C  68     6972   7149   5298    -22    562     55       C  
ATOM   2141  CG  GLU C  68     136.216  -3.479  39.281  1.00 56.23           C  
ANISOU 2141  CG  GLU C  68     7642   7809   5915     -8    639     92       C  
ATOM   2142  CD  GLU C  68     137.359  -4.452  39.086  1.00 63.48           C  
ANISOU 2142  CD  GLU C  68     8510   8757   6851     45    759     56       C  
ATOM   2143  OE1 GLU C  68     137.234  -5.615  39.524  1.00 65.45           O  
ANISOU 2143  OE1 GLU C  68     8713   9039   7114     50    776    -21       O  
ATOM   2144  OE2 GLU C  68     138.386  -4.051  38.498  1.00 67.62           O  
ANISOU 2144  OE2 GLU C  68     9031   9288   7373     64    833     95       O  
ATOM   2145  N   ARG C  69     134.350  -7.030  40.570  1.00 52.92           N  
ANISOU 2145  N   ARG C  69     7202   7382   5524    -62    613   -180       N  
ATOM   2146  CA  ARG C  69     134.685  -8.446  40.666  1.00 53.71           C  
ANISOU 2146  CA  ARG C  69     7321   7432   5655    -73    702   -291       C  
ATOM   2147  C   ARG C  69     133.748  -9.127  41.656  1.00 52.07           C  
ANISOU 2147  C   ARG C  69     7120   7157   5507   -121    657   -336       C  
ATOM   2148  O   ARG C  69     133.245  -8.486  42.577  1.00 51.53           O  
ANISOU 2148  O   ARG C  69     7006   7089   5483   -127    580   -261       O  
ATOM   2149  CB  ARG C  69     136.135  -8.624  41.120  1.00 57.06           C  
ANISOU 2149  CB  ARG C  69     7684   7829   6168    -15    811   -259       C  
ATOM   2150  CG  ARG C  69     136.487 -10.051  41.515  1.00 63.03           C  
ANISOU 2150  CG  ARG C  69     8468   8472   7007     -7    909   -357       C  
ATOM   2151  CD  ARG C  69     137.844 -10.140  42.208  1.00 67.28           C  
ANISOU 2151  CD  ARG C  69     8933   8959   7670     59    998   -302       C  
ATOM   2152  NE  ARG C  69     138.936 -10.356  41.262  1.00 73.50           N  
ANISOU 2152  NE  ARG C  69     9714   9773   8441     99   1100   -334       N  
ATOM   2153  CZ  ARG C  69     140.182 -10.653  41.618  1.00 78.16           C  
ANISOU 2153  CZ  ARG C  69    10243  10311   9142    163   1192   -309       C  
ATOM   2154  NH1 ARG C  69     141.116 -10.823  40.684  1.00 81.09           N  
ANISOU 2154  NH1 ARG C  69    10605  10717   9487    194   1284   -343       N  
ATOM   2155  NH2 ARG C  69     140.491 -10.769  42.909  1.00 78.11           N  
ANISOU 2155  NH2 ARG C  69    10183  10221   9276    201   1188   -243       N  
ATOM   2156  N   ASP C  70     133.515 -10.423  41.471  1.00 51.68           N  
ANISOU 2156  N   ASP C  70     7131   7043   5463   -157    710   -460       N  
ATOM   2157  CA  ASP C  70     132.677 -11.172  42.400  1.00 51.46           C  
ANISOU 2157  CA  ASP C  70     7117   6938   5498   -208    683   -507       C  
ATOM   2158  C   ASP C  70     133.211 -11.004  43.815  1.00 50.86           C  
ANISOU 2158  C   ASP C  70     6985   6801   5540   -164    712   -423       C  
ATOM   2159  O   ASP C  70     134.382 -11.274  44.083  1.00 54.25           O  
ANISOU 2159  O   ASP C  70     7394   7173   6044    -97    811   -402       O  
ATOM   2160  CB  ASP C  70     132.644 -12.656  42.035  1.00 53.48           C  
ANISOU 2160  CB  ASP C  70     7453   7097   5771   -238    763   -648       C  
ATOM   2161  CG  ASP C  70     131.875 -12.924  40.757  1.00 58.09           C  
ANISOU 2161  CG  ASP C  70     8098   7737   6237   -302    716   -739       C  
ATOM   2162  OD1 ASP C  70     130.807 -12.301  40.558  1.00 57.62           O  
ANISOU 2162  OD1 ASP C  70     8021   7761   6113   -355    597   -712       O  
ATOM   2163  OD2 ASP C  70     132.341 -13.753  39.946  1.00 62.76           O  
ANISOU 2163  OD2 ASP C  70     8751   8289   6805   -295    799   -833       O  
ATOM   2164  N   GLY C  71     132.347 -10.567  44.723  1.00 45.33           N  
ANISOU 2164  N   GLY C  71     6250   6113   4859   -199    623   -373       N  
ATOM   2165  CA  GLY C  71     132.753 -10.328  46.094  1.00 41.41           C  
ANISOU 2165  CA  GLY C  71     5705   5568   4461   -162    638   -283       C  
ATOM   2166  C   GLY C  71     131.583 -10.217  47.046  1.00 39.54           C  
ANISOU 2166  C   GLY C  71     5439   5328   4257   -211    535   -256       C  
ATOM   2167  O   GLY C  71     130.423 -10.201  46.627  1.00 39.01           O  
ANISOU 2167  O   GLY C  71     5392   5318   4111   -285    466   -312       O  
ATOM   2168  N   VAL C  72     131.892 -10.146  48.335  1.00 36.51           N  
ANISOU 2168  N   VAL C  72     4999   4881   3992   -167    522   -169       N  
ATOM   2169  CA  VAL C  72     130.865 -10.060  49.359  1.00 33.47           C  
ANISOU 2169  CA  VAL C  72     4580   4488   3647   -204    438   -136       C  
ATOM   2170  C   VAL C  72     131.226  -9.023  50.414  1.00 29.89           C  
ANISOU 2170  C   VAL C  72     4057   4055   3244   -155    389     -9       C  
ATOM   2171  O   VAL C  72     132.395  -8.866  50.774  1.00 31.47           O  
ANISOU 2171  O   VAL C  72     4232   4221   3504    -90    432     54       O  
ATOM   2172  CB  VAL C  72     130.645 -11.425  50.039  1.00 32.73           C  
ANISOU 2172  CB  VAL C  72     4516   4267   3652   -224    479   -181       C  
ATOM   2173  CG1 VAL C  72     129.565 -11.321  51.086  1.00 29.78           C  
ANISOU 2173  CG1 VAL C  72     4106   3895   3312   -269    402   -144       C  
ATOM   2174  CG2 VAL C  72     130.274 -12.481  49.003  1.00 35.87           C  
ANISOU 2174  CG2 VAL C  72     4994   4630   4004   -282    528   -320       C  
ATOM   2175  N   ALA C  73     130.215  -8.313  50.899  1.00 26.10           N  
ANISOU 2175  N   ALA C  73     3544   3632   2741   -187    300     24       N  
ATOM   2176  CA  ALA C  73     130.393  -7.371  51.991  1.00 24.34           C  
ANISOU 2176  CA  ALA C  73     3267   3420   2563   -150    251    128       C  
ATOM   2177  C   ALA C  73     130.210  -8.085  53.323  1.00 24.60           C  
ANISOU 2177  C   ALA C  73     3289   3370   2690   -151    255    151       C  
ATOM   2178  O   ALA C  73     129.365  -8.973  53.453  1.00 28.45           O  
ANISOU 2178  O   ALA C  73     3796   3821   3191   -203    260     94       O  
ATOM   2179  CB  ALA C  73     129.404  -6.220  51.863  1.00 20.10           C  
ANISOU 2179  CB  ALA C  73     2699   2960   1980   -162    158    145       C  
ATOM   2180  N   LEU C  74     131.009  -7.706  54.312  1.00 19.69           N  
ANISOU 2180  N   LEU C  74     2635   2717   2128   -102    251    239       N  
ATOM   2181  CA  LEU C  74     130.870  -8.280  55.641  1.00 18.78           C  
ANISOU 2181  CA  LEU C  74     2515   2535   2088   -102    248    277       C  
ATOM   2182  C   LEU C  74     130.113  -7.296  56.522  1.00 20.53           C  
ANISOU 2182  C   LEU C  74     2703   2810   2289   -115    175    323       C  
ATOM   2183  O   LEU C  74     130.652  -6.264  56.913  1.00 22.21           O  
ANISOU 2183  O   LEU C  74     2894   3011   2536    -71    127    330       O  
ATOM   2184  CB  LEU C  74     132.252  -8.577  56.228  1.00 17.80           C  
ANISOU 2184  CB  LEU C  74     2377   2344   2041    -38    285    344       C  
ATOM   2185  CG  LEU C  74     133.106  -9.527  55.379  1.00 18.72           C  
ANISOU 2185  CG  LEU C  74     2520   2401   2192     -7    370    299       C  
ATOM   2186  CD1 LEU C  74     134.536  -9.608  55.896  1.00 17.05           C  
ANISOU 2186  CD1 LEU C  74     2271   2146   2062     68    398    378       C  
ATOM   2187  CD2 LEU C  74     132.473 -10.904  55.331  1.00 20.71           C  
ANISOU 2187  CD2 LEU C  74     2825   2565   2477    -43    413    227       C  
ATOM   2188  N   ALA C  75     128.865  -7.622  56.841  1.00 22.62           N  
ANISOU 2188  N   ALA C  75     2967   3085   2543   -168    157    289       N  
ATOM   2189  CA  ALA C  75     127.998  -6.692  57.554  1.00 23.97           C  
ANISOU 2189  CA  ALA C  75     3101   3288   2717   -161     94    291       C  
ATOM   2190  C   ALA C  75     128.278  -6.666  59.051  1.00 26.20           C  
ANISOU 2190  C   ALA C  75     3382   3510   3064   -130     86    321       C  
ATOM   2191  O   ALA C  75     128.222  -5.610  59.673  1.00 25.70           O  
ANISOU 2191  O   ALA C  75     3296   3450   3018    -98     45    309       O  
ATOM   2192  CB  ALA C  75     126.534  -7.015  57.288  1.00 22.88           C  
ANISOU 2192  CB  ALA C  75     2950   3214   2530   -239     83    252       C  
ATOM   2193  N   ASP C  76     128.583  -7.825  59.627  1.00 28.92           N  
ANISOU 2193  N   ASP C  76     3755   3794   3442   -146    131    351       N  
ATOM   2194  CA  ASP C  76     128.833  -7.908  61.064  1.00 31.32           C  
ANISOU 2194  CA  ASP C  76     4066   4048   3785   -123    117    369       C  
ATOM   2195  C   ASP C  76     130.055  -7.084  61.433  1.00 28.44           C  
ANISOU 2195  C   ASP C  76     3689   3677   3441    -71     79    368       C  
ATOM   2196  O   ASP C  76     130.195  -6.624  62.570  1.00 24.69           O  
ANISOU 2196  O   ASP C  76     3210   3195   2976    -57     52    362       O  
ATOM   2197  CB  ASP C  76     129.000  -9.361  61.510  1.00 34.87           C  
ANISOU 2197  CB  ASP C  76     4555   4422   4273   -151    166    404       C  
ATOM   2198  CG  ASP C  76     130.219 -10.022  60.905  1.00 39.12           C  
ANISOU 2198  CG  ASP C  76     5104   4911   4851   -123    197    436       C  
ATOM   2199  OD1 ASP C  76     130.647  -9.604  59.811  1.00 41.48           O  
ANISOU 2199  OD1 ASP C  76     5390   5242   5130   -103    213    427       O  
ATOM   2200  OD2 ASP C  76     130.749 -10.967  61.523  1.00 41.62           O  
ANISOU 2200  OD2 ASP C  76     5439   5153   5223   -107    214    469       O  
ATOM   2201  N   GLN C  77     130.934  -6.893  60.457  1.00 28.08           N  
ANISOU 2201  N   GLN C  77     3634   3639   3396    -52     86    374       N  
ATOM   2202  CA  GLN C  77     132.078  -6.023  60.645  1.00 29.12           C  
ANISOU 2202  CA  GLN C  77     3737   3776   3550    -18     55    373       C  
ATOM   2203  C   GLN C  77     131.722  -4.627  60.142  1.00 31.72           C  
ANISOU 2203  C   GLN C  77     4041   4151   3861    -16     26    341       C  
ATOM   2204  O   GLN C  77     131.575  -4.400  58.944  1.00 35.65           O  
ANISOU 2204  O   GLN C  77     4547   4667   4330    -20     35    327       O  
ATOM   2205  CB  GLN C  77     133.309  -6.581  59.927  1.00 30.59           C  
ANISOU 2205  CB  GLN C  77     3910   3951   3763      9     90    414       C  
ATOM   2206  CG  GLN C  77     133.785  -7.920  60.471  1.00 36.00           C  
ANISOU 2206  CG  GLN C  77     4604   4578   4496     27    125    461       C  
ATOM   2207  CD  GLN C  77     135.269  -8.179  60.198  1.00 41.40           C  
ANISOU 2207  CD  GLN C  77     5248   5246   5235     82    154    509       C  
ATOM   2208  OE1 GLN C  77     136.001  -7.284  59.760  1.00 40.96           O  
ANISOU 2208  OE1 GLN C  77     5154   5234   5177     97    142    509       O  
ATOM   2209  NE2 GLN C  77     135.714  -9.412  60.451  1.00 43.69           N  
ANISOU 2209  NE2 GLN C  77     5547   5466   5586    115    201    553       N  
ATOM   2210  N   VAL C  78     131.575  -3.698  61.078  1.00 30.63           N  
ANISOU 2210  N   VAL C  78     3868   4034   3737    -16     -4    341       N  
ATOM   2211  CA  VAL C  78     131.194  -2.328  60.763  1.00 27.42           C  
ANISOU 2211  CA  VAL C  78     3434   3659   3323    -19    -25    323       C  
ATOM   2212  C   VAL C  78     132.171  -1.399  61.457  1.00 27.20           C  
ANISOU 2212  C   VAL C  78     3379   3635   3321    -17    -40    339       C  
ATOM   2213  O   VAL C  78     132.348  -1.463  62.675  1.00 28.38           O  
ANISOU 2213  O   VAL C  78     3528   3775   3480    -23    -50    350       O  
ATOM   2214  CB  VAL C  78     129.769  -2.010  61.239  1.00 24.05           C  
ANISOU 2214  CB  VAL C  78     3009   3249   2881    -33    -35    305       C  
ATOM   2215  CG1 VAL C  78     129.488  -0.515  61.134  1.00 22.83           C  
ANISOU 2215  CG1 VAL C  78     2834   3113   2725    -30    -50    296       C  
ATOM   2216  CG2 VAL C  78     128.761  -2.806  60.445  1.00 21.54           C  
ANISOU 2216  CG2 VAL C  78     2712   2940   2534    -45    -23    290       C  
ATOM   2217  N   LYS C  79     132.821  -0.544  60.680  1.00 26.95           N  
ANISOU 2217  N   LYS C  79     3330   3616   3293    -15    -42    344       N  
ATOM   2218  CA  LYS C  79     133.894   0.267  61.228  1.00 25.09           C  
ANISOU 2218  CA  LYS C  79     3072   3382   3080    -22    -55    365       C  
ATOM   2219  C   LYS C  79     133.670   1.749  60.962  1.00 23.55           C  
ANISOU 2219  C   LYS C  79     2879   3193   2876    -33    -70    357       C  
ATOM   2220  O   LYS C  79     133.470   2.169  59.816  1.00 21.04           O  
ANISOU 2220  O   LYS C  79     2563   2885   2545    -27    -64    353       O  
ATOM   2221  CB  LYS C  79     135.240  -0.184  60.646  1.00 26.38           C  
ANISOU 2221  CB  LYS C  79     3211   3549   3262    -10    -41    395       C  
ATOM   2222  CG  LYS C  79     135.422  -1.697  60.618  1.00 28.32           C  
ANISOU 2222  CG  LYS C  79     3469   3777   3515     11    -19    407       C  
ATOM   2223  CD  LYS C  79     136.410  -2.144  59.545  1.00 29.95           C  
ANISOU 2223  CD  LYS C  79     3667   3985   3729     35     11    430       C  
ATOM   2224  CE  LYS C  79     137.790  -2.450  60.126  1.00 27.31           C  
ANISOU 2224  CE  LYS C  79     3289   3649   3439     48     15    478       C  
ATOM   2225  NZ  LYS C  79     138.710  -3.018  59.090  1.00 22.09           N  
ANISOU 2225  NZ  LYS C  79     2614   2988   2793     81     58    510       N  
ATOM   2226  N   SER C  80     133.676   2.534  62.034  1.00 23.92           N  
ANISOU 2226  N   SER C  80     2935   3228   2925    -46    -90    357       N  
ATOM   2227  CA  SER C  80     133.762   3.971  61.898  1.00 25.48           C  
ANISOU 2227  CA  SER C  80     3144   3419   3117    -54   -106    359       C  
ATOM   2228  C   SER C  80     135.232   4.263  61.684  1.00 25.32           C  
ANISOU 2228  C   SER C  80     3096   3404   3120    -71   -114    392       C  
ATOM   2229  O   SER C  80     136.057   3.988  62.557  1.00 27.07           O  
ANISOU 2229  O   SER C  80     3303   3626   3358    -86   -127    411       O  
ATOM   2230  CB  SER C  80     133.276   4.667  63.167  1.00 27.95           C  
ANISOU 2230  CB  SER C  80     3491   3714   3417    -58   -126    348       C  
ATOM   2231  OG  SER C  80     133.304   6.080  63.014  1.00 30.87           O  
ANISOU 2231  OG  SER C  80     3885   4067   3778    -59   -144    351       O  
ATOM   2232  N   ILE C  81     135.560   4.813  60.521  1.00 21.36           N  
ANISOU 2232  N   ILE C  81     2586   2911   2617    -69   -109    404       N  
ATOM   2233  CA  ILE C  81     136.949   5.085  60.180  1.00 19.25           C  
ANISOU 2233  CA  ILE C  81     2285   2657   2372    -85   -113    442       C  
ATOM   2234  C   ILE C  81     137.063   6.512  59.706  1.00 20.04           C  
ANISOU 2234  C   ILE C  81     2403   2746   2465   -100   -130    454       C  
ATOM   2235  O   ILE C  81     136.061   7.134  59.361  1.00 21.08           O  
ANISOU 2235  O   ILE C  81     2572   2864   2574    -87   -132    435       O  
ATOM   2236  CB  ILE C  81     137.454   4.179  59.048  1.00 16.16           C  
ANISOU 2236  CB  ILE C  81     1867   2290   1982    -63    -81    457       C  
ATOM   2237  CG1 ILE C  81     136.713   4.505  57.751  1.00 14.09           C  
ANISOU 2237  CG1 ILE C  81     1632   2034   1687    -49    -69    443       C  
ATOM   2238  CG2 ILE C  81     137.295   2.710  59.418  1.00 15.10           C  
ANISOU 2238  CG2 ILE C  81     1728   2155   1854    -42    -63    447       C  
ATOM   2239  CD1 ILE C  81     137.219   3.749  56.553  1.00 12.96           C  
ANISOU 2239  CD1 ILE C  81     1481   1912   1529    -28    -37    457       C  
ATOM   2240  N   ALA C  82     138.283   7.029  59.686  1.00 18.54           N  
ANISOU 2240  N   ALA C  82     2185   2563   2297   -126   -145    492       N  
ATOM   2241  CA  ALA C  82     138.504   8.350  59.141  1.00 16.62           C  
ANISOU 2241  CA  ALA C  82     1961   2307   2048   -142   -161    513       C  
ATOM   2242  C   ALA C  82     138.837   8.145  57.675  1.00 21.95           C  
ANISOU 2242  C   ALA C  82     2618   3008   2712   -126   -131    535       C  
ATOM   2243  O   ALA C  82     139.924   7.675  57.333  1.00 22.63           O  
ANISOU 2243  O   ALA C  82     2659   3122   2817   -129   -117    569       O  
ATOM   2244  CB  ALA C  82     139.653   9.019  59.856  1.00 14.08           C  
ANISOU 2244  CB  ALA C  82     1618   1979   1753   -186   -197    548       C  
ATOM   2245  N   TRP C  83     137.901   8.511  56.808  1.00 25.23           N  
ANISOU 2245  N   TRP C  83     3075   3418   3095   -107   -121    522       N  
ATOM   2246  CA  TRP C  83     138.034   8.224  55.389  1.00 29.31           C  
ANISOU 2246  CA  TRP C  83     3592   3960   3585    -92    -91    538       C  
ATOM   2247  C   TRP C  83     138.952   9.234  54.710  1.00 33.63           C  
ANISOU 2247  C   TRP C  83     4141   4508   4131   -115    -92    588       C  
ATOM   2248  O   TRP C  83     139.624   8.916  53.725  1.00 36.81           O  
ANISOU 2248  O   TRP C  83     4531   4938   4518   -111    -61    615       O  
ATOM   2249  CB  TRP C  83     136.660   8.204  54.721  1.00 26.88           C  
ANISOU 2249  CB  TRP C  83     3327   3650   3237    -68    -87    510       C  
ATOM   2250  CG  TRP C  83     135.907   9.474  54.880  1.00 25.65           C  
ANISOU 2250  CG  TRP C  83     3214   3461   3072    -67   -114    512       C  
ATOM   2251  CD1 TRP C  83     135.011   9.779  55.862  1.00 23.55           C  
ANISOU 2251  CD1 TRP C  83     2969   3167   2813    -56   -134    484       C  
ATOM   2252  CD2 TRP C  83     135.988  10.629  54.036  1.00 26.40           C  
ANISOU 2252  CD2 TRP C  83     3343   3543   3146    -70   -121    549       C  
ATOM   2253  NE1 TRP C  83     134.523  11.049  55.677  1.00 24.40           N  
ANISOU 2253  NE1 TRP C  83     3122   3244   2906    -45   -154    500       N  
ATOM   2254  CE2 TRP C  83     135.108  11.591  54.562  1.00 27.40           C  
ANISOU 2254  CE2 TRP C  83     3511   3630   3270    -55   -148    541       C  
ATOM   2255  CE3 TRP C  83     136.720  10.941  52.886  1.00 24.76           C  
ANISOU 2255  CE3 TRP C  83     3141   3352   2917    -82   -104    592       C  
ATOM   2256  CZ2 TRP C  83     134.938  12.844  53.976  1.00 28.73           C  
ANISOU 2256  CZ2 TRP C  83     3726   3770   3421    -47   -161    578       C  
ATOM   2257  CZ3 TRP C  83     136.549  12.185  52.306  1.00 25.03           C  
ANISOU 2257  CZ3 TRP C  83     3220   3359   2930    -83   -116    629       C  
ATOM   2258  CH2 TRP C  83     135.669  13.121  52.853  1.00 26.99           C  
ANISOU 2258  CH2 TRP C  83     3510   3564   3182    -64   -146    623       C  
ATOM   2259  N   ARG C  84     138.989  10.449  55.248  1.00 30.32           N  
ANISOU 2259  N   ARG C  84     3744   4054   3724   -139   -124    602       N  
ATOM   2260  CA  ARG C  84     139.853  11.490  54.707  1.00 27.13           C  
ANISOU 2260  CA  ARG C  84     3346   3641   3322   -168   -127    655       C  
ATOM   2261  C   ARG C  84     141.298  11.273  55.141  1.00 25.24           C  
ANISOU 2261  C   ARG C  84     3046   3423   3122   -200   -131    690       C  
ATOM   2262  O   ARG C  84     142.231  11.626  54.422  1.00 25.30           O  
ANISOU 2262  O   ARG C  84     3038   3443   3130   -220   -112    739       O  
ATOM   2263  CB  ARG C  84     139.372  12.872  55.150  1.00 29.85           C  
ANISOU 2263  CB  ARG C  84     3744   3930   3666   -181   -161    660       C  
ATOM   2264  CG  ARG C  84     138.942  13.771  54.002  1.00 32.77           C  
ANISOU 2264  CG  ARG C  84     4168   4281   4001   -170   -150    691       C  
ATOM   2265  CD  ARG C  84     138.788  15.219  54.450  1.00 32.80           C  
ANISOU 2265  CD  ARG C  84     4227   4221   4015   -184   -180    713       C  
ATOM   2266  NE  ARG C  84     137.605  15.422  55.280  1.00 31.85           N  
ANISOU 2266  NE  ARG C  84     4143   4067   3890   -149   -202    670       N  
ATOM   2267  CZ  ARG C  84     136.452  15.902  54.827  1.00 30.25           C  
ANISOU 2267  CZ  ARG C  84     3992   3844   3660   -102   -202    668       C  
ATOM   2268  NH1 ARG C  84     136.327  16.230  53.549  1.00 29.37           N  
ANISOU 2268  NH1 ARG C  84     3904   3738   3518    -91   -188    706       N  
ATOM   2269  NH2 ARG C  84     135.426  16.055  55.651  1.00 28.54           N  
ANISOU 2269  NH2 ARG C  84     3801   3601   3441    -65   -217    632       N  
ATOM   2270  N   ALA C  85     141.472  10.688  56.322  1.00 24.79           N  
ANISOU 2270  N   ALA C  85     2954   3370   3096   -205   -154    670       N  
ATOM   2271  CA  ALA C  85     142.799  10.412  56.860  1.00 24.87           C  
ANISOU 2271  CA  ALA C  85     2898   3404   3146   -231   -168    709       C  
ATOM   2272  C   ALA C  85     143.434   9.220  56.154  1.00 28.15           C  
ANISOU 2272  C   ALA C  85     3265   3865   3567   -197   -121    728       C  
ATOM   2273  O   ALA C  85     144.626   9.224  55.856  1.00 31.89           O  
ANISOU 2273  O   ALA C  85     3689   4365   4064   -210   -110    783       O  
ATOM   2274  CB  ALA C  85     142.719  10.161  58.358  1.00 21.14           C  
ANISOU 2274  CB  ALA C  85     2415   2920   2697   -248   -209    685       C  
ATOM   2275  N   ARG C  86     142.626   8.198  55.893  1.00 27.24           N  
ANISOU 2275  N   ARG C  86     3164   3757   3429   -154    -91    686       N  
ATOM   2276  CA  ARG C  86     143.093   6.999  55.206  1.00 27.21           C  
ANISOU 2276  CA  ARG C  86     3133   3782   3422   -115    -41    697       C  
ATOM   2277  C   ARG C  86     143.073   7.213  53.697  1.00 30.49           C  
ANISOU 2277  C   ARG C  86     3587   4209   3791   -109      7    708       C  
ATOM   2278  O   ARG C  86     143.413   6.315  52.922  1.00 31.11           O  
ANISOU 2278  O   ARG C  86     3663   4307   3852    -84     63    712       O  
ATOM   2279  CB  ARG C  86     142.236   5.791  55.591  1.00 26.07           C  
ANISOU 2279  CB  ARG C  86     3001   3632   3271    -80    -31    648       C  
ATOM   2280  CG  ARG C  86     142.251   5.507  57.079  1.00 26.59           C  
ANISOU 2280  CG  ARG C  86     3040   3688   3375    -92    -66    639       C  
ATOM   2281  CD  ARG C  86     141.470   4.257  57.450  1.00 25.76           C  
ANISOU 2281  CD  ARG C  86     2951   3573   3263    -61    -48    600       C  
ATOM   2282  NE  ARG C  86     141.563   4.018  58.886  1.00 25.98           N  
ANISOU 2282  NE  ARG C  86     2962   3590   3319    -80    -76    599       N  
ATOM   2283  CZ  ARG C  86     142.608   3.449  59.477  1.00 26.41           C  
ANISOU 2283  CZ  ARG C  86     2964   3657   3414    -80    -77    641       C  
ATOM   2284  NH1 ARG C  86     143.645   3.049  58.752  1.00 24.09           N  
ANISOU 2284  NH1 ARG C  86     2609   3396   3149    -55    -49    699       N  
ATOM   2285  NH2 ARG C  86     142.617   3.278  60.790  1.00 30.08           N  
ANISOU 2285  NH2 ARG C  86     3429   4109   3892   -105   -105    641       N  
ATOM   2286  N   GLY C  87     142.659   8.410  53.291  1.00 31.70           N  
ANISOU 2286  N   GLY C  87     3781   4344   3920   -136     -9    714       N  
ATOM   2287  CA  GLY C  87     142.625   8.783  51.889  1.00 32.34           C  
ANISOU 2287  CA  GLY C  87     3904   4434   3949   -140     33    732       C  
ATOM   2288  C   GLY C  87     141.664   7.945  51.065  1.00 30.41           C  
ANISOU 2288  C   GLY C  87     3705   4201   3650   -107     62    690       C  
ATOM   2289  O   GLY C  87     141.951   7.620  49.913  1.00 32.69           O  
ANISOU 2289  O   GLY C  87     4016   4513   3893   -106    117    701       O  
ATOM   2290  N   ALA C  88     140.525   7.587  51.651  1.00 26.45           N  
ANISOU 2290  N   ALA C  88     3218   3684   3148    -88     30    642       N  
ATOM   2291  CA  ALA C  88     139.532   6.777  50.949  1.00 22.89           C  
ANISOU 2291  CA  ALA C  88     2809   3243   2647    -64     47    602       C  
ATOM   2292  C   ALA C  88     139.153   7.400  49.608  1.00 24.71           C  
ANISOU 2292  C   ALA C  88     3093   3484   2811    -73     62    618       C  
ATOM   2293  O   ALA C  88     138.923   8.606  49.519  1.00 24.47           O  
ANISOU 2293  O   ALA C  88     3084   3437   2778    -87     35    643       O  
ATOM   2294  CB  ALA C  88     138.303   6.573  51.812  1.00 19.57           C  
ANISOU 2294  CB  ALA C  88     2395   2803   2240    -52      8    556       C  
ATOM   2295  N   THR C  89     139.106   6.574  48.567  1.00 24.96           N  
ANISOU 2295  N   THR C  89     3157   3542   2784    -67    108    604       N  
ATOM   2296  CA  THR C  89     138.740   7.035  47.228  1.00 21.90           C  
ANISOU 2296  CA  THR C  89     2828   3173   2319    -78    124    619       C  
ATOM   2297  C   THR C  89     137.525   6.264  46.693  1.00 20.17           C  
ANISOU 2297  C   THR C  89     2652   2968   2042    -64    115    572       C  
ATOM   2298  O   THR C  89     137.174   5.210  47.216  1.00 20.16           O  
ANISOU 2298  O   THR C  89     2640   2964   2057    -51    116    529       O  
ATOM   2299  CB  THR C  89     139.924   6.933  46.250  1.00 22.88           C  
ANISOU 2299  CB  THR C  89     2963   3323   2406    -99    199    650       C  
ATOM   2300  OG1 THR C  89     139.508   7.340  44.941  1.00 27.38           O  
ANISOU 2300  OG1 THR C  89     3600   3914   2888   -110    216    664       O  
ATOM   2301  CG2 THR C  89     140.456   5.509  46.189  1.00 22.56           C  
ANISOU 2301  CG2 THR C  89     2910   3299   2365    -91    263    615       C  
ATOM   2302  N   LYS C  90     136.882   6.792  45.656  1.00 20.84           N  
ANISOU 2302  N   LYS C  90     2789   3071   2057    -68    105    585       N  
ATOM   2303  CA  LYS C  90     135.609   6.247  45.192  1.00 25.03           C  
ANISOU 2303  CA  LYS C  90     3356   3621   2534    -57     79    547       C  
ATOM   2304  C   LYS C  90     135.767   5.092  44.207  1.00 27.27           C  
ANISOU 2304  C   LYS C  90     3686   3936   2739    -66    136    513       C  
ATOM   2305  O   LYS C  90     136.309   5.264  43.117  1.00 32.78           O  
ANISOU 2305  O   LYS C  90     4429   4659   3368    -81    183    534       O  
ATOM   2306  CB  LYS C  90     134.777   7.359  44.548  1.00 29.47           C  
ANISOU 2306  CB  LYS C  90     3952   4190   3054    -52     32    580       C  
ATOM   2307  CG  LYS C  90     133.389   6.923  44.103  1.00 32.67           C  
ANISOU 2307  CG  LYS C  90     4382   4624   3409    -40     -9    548       C  
ATOM   2308  CD  LYS C  90     132.589   8.100  43.552  1.00 37.22           C  
ANISOU 2308  CD  LYS C  90     4985   5205   3951    -29    -61    591       C  
ATOM   2309  CE  LYS C  90     131.144   7.711  43.269  1.00 41.29           C  
ANISOU 2309  CE  LYS C  90     5507   5752   4428    -15   -113    561       C  
ATOM   2310  NZ  LYS C  90     131.060   6.549  42.343  1.00 45.24           N  
ANISOU 2310  NZ  LYS C  90     6043   6301   4844    -30    -89    522       N  
ATOM   2311  N   LYS C  91     135.293   3.917  44.610  1.00 25.87           N  
ANISOU 2311  N   LYS C  91     3507   3755   2569    -59    140    459       N  
ATOM   2312  CA  LYS C  91     135.301   2.730  43.759  1.00 27.48           C  
ANISOU 2312  CA  LYS C  91     3766   3979   2696    -68    200    412       C  
ATOM   2313  C   LYS C  91     134.093   2.662  42.823  1.00 29.57           C  
ANISOU 2313  C   LYS C  91     4082   4281   2872    -66    161    390       C  
ATOM   2314  O   LYS C  91     134.214   2.246  41.674  1.00 31.77           O  
ANISOU 2314  O   LYS C  91     4423   4591   3056    -73    206    371       O  
ATOM   2315  CB  LYS C  91     135.385   1.459  44.606  1.00 29.01           C  
ANISOU 2315  CB  LYS C  91     3938   4150   2934    -64    229    367       C  
ATOM   2316  CG  LYS C  91     135.684   0.202  43.807  1.00 32.37           C  
ANISOU 2316  CG  LYS C  91     4405   4610   3286    -72    317    320       C  
ATOM   2317  CD  LYS C  91     136.989   0.342  43.031  1.00 34.66           C  
ANISOU 2317  CD  LYS C  91     4704   4919   3546    -86    408    339       C  
ATOM   2318  CE  LYS C  91     137.356  -0.944  42.302  1.00 34.80           C  
ANISOU 2318  CE  LYS C  91     4762   4960   3499    -90    519    276       C  
ATOM   2319  NZ  LYS C  91     138.601  -0.768  41.502  1.00 33.83           N  
ANISOU 2319  NZ  LYS C  91     4642   4863   3350   -109    618    287       N  
ATOM   2320  N   GLY C  92     132.928   3.058  43.329  1.00 30.89           N  
ANISOU 2320  N   GLY C  92     4218   4450   3068    -57     79    390       N  
ATOM   2321  CA  GLY C  92     131.678   2.904  42.602  1.00 33.08           C  
ANISOU 2321  CA  GLY C  92     4524   4770   3275    -58     29    367       C  
ATOM   2322  C   GLY C  92     130.477   3.123  43.508  1.00 34.85           C  
ANISOU 2322  C   GLY C  92     4695   4987   3561    -49    -44    360       C  
ATOM   2323  O   GLY C  92     130.559   3.872  44.480  1.00 35.22           O  
ANISOU 2323  O   GLY C  92     4694   4999   3691    -37    -63    389       O  
ATOM   2324  N   THR C  93     129.347   2.510  43.161  1.00 34.29           N  
ANISOU 2324  N   THR C  93     4632   4952   3446    -56    -82    320       N  
ATOM   2325  CA  THR C  93     128.157   2.538  44.018  1.00 30.56           C  
ANISOU 2325  CA  THR C  93     4106   4477   3029    -52   -139    308       C  
ATOM   2326  C   THR C  93     127.396   1.213  44.025  1.00 32.39           C  
ANISOU 2326  C   THR C  93     4340   4732   3234    -73   -146    242       C  
ATOM   2327  O   THR C  93     127.135   0.636  42.973  1.00 33.51           O  
ANISOU 2327  O   THR C  93     4526   4918   3287    -91   -150    207       O  
ATOM   2328  CB  THR C  93     127.194   3.673  43.636  1.00 29.10           C  
ANISOU 2328  CB  THR C  93     3907   4319   2829    -38   -207    347       C  
ATOM   2329  OG1 THR C  93     127.468   4.095  42.297  1.00 33.05           O  
ANISOU 2329  OG1 THR C  93     4464   4856   3237    -41   -210    374       O  
ATOM   2330  CG2 THR C  93     127.368   4.856  44.578  1.00 28.13           C  
ANISOU 2330  CG2 THR C  93     3748   4150   2791    -13   -214    394       C  
ATOM   2331  N   VAL C  94     127.054   0.736  45.219  1.00 34.73           N  
ANISOU 2331  N   VAL C  94     4593   4999   3604    -74   -146    223       N  
ATOM   2332  CA  VAL C  94     126.281  -0.497  45.372  1.00 37.79           C  
ANISOU 2332  CA  VAL C  94     4967   5421   3970   -109   -154    165       C  
ATOM   2333  C   VAL C  94     124.786  -0.284  45.139  1.00 38.91           C  
ANISOU 2333  C   VAL C  94     5076   5612   4097   -122   -227    156       C  
ATOM   2334  O   VAL C  94     124.270   0.823  45.310  1.00 37.68           O  
ANISOU 2334  O   VAL C  94     4894   5448   3974    -92   -267    198       O  
ATOM   2335  CB  VAL C  94     126.475  -1.124  46.770  1.00 35.78           C  
ANISOU 2335  CB  VAL C  94     4676   5127   3790   -113   -124    157       C  
ATOM   2336  CG1 VAL C  94     127.907  -1.596  46.953  1.00 36.23           C  
ANISOU 2336  CG1 VAL C  94     4763   5148   3855   -104    -52    161       C  
ATOM   2337  CG2 VAL C  94     126.083  -0.131  47.854  1.00 33.72           C  
ANISOU 2337  CG2 VAL C  94     4372   4823   3619    -81   -152    195       C  
ATOM   2338  N   ALA C  95     124.096  -1.352  44.750  1.00 39.66           N  
ANISOU 2338  N   ALA C  95     5167   5764   4139   -173   -243     97       N  
ATOM   2339  CA  ALA C  95     122.649  -1.310  44.567  1.00 40.93           C  
ANISOU 2339  CA  ALA C  95     5285   5980   4287   -195   -314     83       C  
ATOM   2340  C   ALA C  95     121.930  -1.054  45.891  1.00 44.50           C  
ANISOU 2340  C   ALA C  95     5666   6411   4830   -182   -327    102       C  
ATOM   2341  O   ALA C  95     122.339  -1.565  46.933  1.00 44.96           O  
ANISOU 2341  O   ALA C  95     5710   6434   4939   -189   -282     95       O  
ATOM   2342  CB  ALA C  95     122.156  -2.609  43.940  1.00 40.21           C  
ANISOU 2342  CB  ALA C  95     5205   5947   4124   -269   -324      2       C  
ATOM   2343  N   PRO C  96     120.855  -0.253  45.851  1.00 45.06           N  
ANISOU 2343  N   PRO C  96     5696   6509   4917   -159   -386    128       N  
ATOM   2344  CA  PRO C  96     120.081   0.095  47.048  1.00 42.81           C  
ANISOU 2344  CA  PRO C  96     5345   6212   4709   -141   -394    146       C  
ATOM   2345  C   PRO C  96     119.550  -1.133  47.776  1.00 43.32           C  
ANISOU 2345  C   PRO C  96     5364   6308   4787   -200   -379     99       C  
ATOM   2346  O   PRO C  96     119.456  -1.124  49.005  1.00 46.02           O  
ANISOU 2346  O   PRO C  96     5671   6625   5191   -191   -351    112       O  
ATOM   2347  CB  PRO C  96     118.913   0.905  46.482  1.00 42.85           C  
ANISOU 2347  CB  PRO C  96     5317   6264   4701   -118   -469    168       C  
ATOM   2348  CG  PRO C  96     119.434   1.478  45.228  1.00 43.79           C  
ANISOU 2348  CG  PRO C  96     5499   6385   4755   -100   -491    190       C  
ATOM   2349  CD  PRO C  96     120.351   0.440  44.654  1.00 45.74           C  
ANISOU 2349  CD  PRO C  96     5799   6637   4942   -145   -449    147       C  
ATOM   2350  N   GLU C  97     119.194  -2.173  47.031  1.00 42.14           N  
ANISOU 2350  N   GLU C  97     5221   6214   4578   -268   -398     42       N  
ATOM   2351  CA  GLU C  97     118.724  -3.398  47.654  1.00 42.07           C  
ANISOU 2351  CA  GLU C  97     5179   6227   4579   -343   -382    -13       C  
ATOM   2352  C   GLU C  97     119.815  -3.892  48.596  1.00 39.03           C  
ANISOU 2352  C   GLU C  97     4824   5778   4226   -345   -310    -12       C  
ATOM   2353  O   GLU C  97     119.554  -4.265  49.746  1.00 39.04           O  
ANISOU 2353  O   GLU C  97     4788   5771   4273   -366   -288    -11       O  
ATOM   2354  CB  GLU C  97     118.400  -4.454  46.594  1.00 47.47           C  
ANISOU 2354  CB  GLU C  97     5889   6957   5190   -425   -405    -91       C  
ATOM   2355  CG  GLU C  97     117.197  -4.124  45.716  1.00 52.04           C  
ANISOU 2355  CG  GLU C  97     6429   7609   5735   -436   -489    -96       C  
ATOM   2356  CD  GLU C  97     117.468  -2.995  44.740  1.00 54.85           C  
ANISOU 2356  CD  GLU C  97     6821   7971   6048   -369   -526    -45       C  
ATOM   2357  OE1 GLU C  97     116.505  -2.522  44.102  1.00 55.05           O  
ANISOU 2357  OE1 GLU C  97     6813   8054   6051   -363   -602    -32       O  
ATOM   2358  OE2 GLU C  97     118.641  -2.582  44.612  1.00 56.81           O  
ANISOU 2358  OE2 GLU C  97     7131   8168   6287   -325   -480    -16       O  
ATOM   2359  N   GLU C  98     121.048  -3.860  48.102  1.00 36.03           N  
ANISOU 2359  N   GLU C  98     4513   5359   3818   -320   -274     -6       N  
ATOM   2360  CA  GLU C  98     122.204  -4.303  48.871  1.00 34.41           C  
ANISOU 2360  CA  GLU C  98     4342   5095   3640   -313   -209      0       C  
ATOM   2361  C   GLU C  98     122.440  -3.451  50.108  1.00 30.83           C  
ANISOU 2361  C   GLU C  98     3855   4593   3266   -253   -197     67       C  
ATOM   2362  O   GLU C  98     122.736  -3.975  51.178  1.00 32.42           O  
ANISOU 2362  O   GLU C  98     4052   4767   3500   -267   -164     71       O  
ATOM   2363  CB  GLU C  98     123.449  -4.314  47.989  1.00 35.80           C  
ANISOU 2363  CB  GLU C  98     4589   5244   3770   -290   -172     -3       C  
ATOM   2364  CG  GLU C  98     123.352  -5.316  46.860  1.00 40.66           C  
ANISOU 2364  CG  GLU C  98     5254   5895   4301   -354   -165    -86       C  
ATOM   2365  CD  GLU C  98     124.251  -4.976  45.686  1.00 44.75           C  
ANISOU 2365  CD  GLU C  98     5833   6413   4758   -320   -143    -81       C  
ATOM   2366  OE1 GLU C  98     124.814  -3.859  45.660  1.00 45.77           O  
ANISOU 2366  OE1 GLU C  98     5960   6520   4911   -253   -144     -9       O  
ATOM   2367  OE2 GLU C  98     124.391  -5.833  44.787  1.00 44.82           O  
ANISOU 2367  OE2 GLU C  98     5896   6440   4695   -365   -119   -155       O  
ATOM   2368  N   LEU C  99     122.307  -2.138  49.960  1.00 26.33           N  
ANISOU 2368  N   LEU C  99     3273   4007   2722   -191   -223    112       N  
ATOM   2369  CA  LEU C  99     122.486  -1.227  51.084  1.00 21.97           C  
ANISOU 2369  CA  LEU C  99     2702   3400   2244   -139   -210    157       C  
ATOM   2370  C   LEU C  99     121.466  -1.531  52.172  1.00 20.74           C  
ANISOU 2370  C   LEU C  99     2488   3274   2118   -161   -214    153       C  
ATOM   2371  O   LEU C  99     121.809  -1.643  53.352  1.00 20.11           O  
ANISOU 2371  O   LEU C  99     2402   3158   2080   -154   -182    169       O  
ATOM   2372  CB  LEU C  99     122.350   0.222  50.623  1.00 20.57           C  
ANISOU 2372  CB  LEU C  99     2534   3203   2080    -86   -239    189       C  
ATOM   2373  CG  LEU C  99     122.656   1.303  51.656  1.00 21.72           C  
ANISOU 2373  CG  LEU C  99     2669   3296   2287    -44   -222    225       C  
ATOM   2374  CD1 LEU C  99     124.061   1.129  52.216  1.00 23.98           C  
ANISOU 2374  CD1 LEU C  99     2981   3527   2603    -41   -176    233       C  
ATOM   2375  CD2 LEU C  99     122.492   2.674  51.036  1.00 22.52           C  
ANISOU 2375  CD2 LEU C  99     2772   3406   2379    -10   -252    259       C  
ATOM   2376  N   GLN C 100     120.208  -1.666  51.765  1.00 22.71           N  
ANISOU 2376  N   GLN C 100     2692   3593   2343   -189   -255    132       N  
ATOM   2377  CA  GLN C 100     119.142  -2.002  52.698  1.00 23.39           C  
ANISOU 2377  CA  GLN C 100     2712   3723   2451   -217   -258    125       C  
ATOM   2378  C   GLN C 100     119.432  -3.320  53.403  1.00 20.92           C  
ANISOU 2378  C   GLN C 100     2404   3412   2132   -288   -222     98       C  
ATOM   2379  O   GLN C 100     119.194  -3.453  54.605  1.00 20.24           O  
ANISOU 2379  O   GLN C 100     2288   3328   2076   -297   -200    114       O  
ATOM   2380  CB  GLN C 100     117.794  -2.068  51.979  1.00 25.68           C  
ANISOU 2380  CB  GLN C 100     2948   4090   2718   -245   -312     99       C  
ATOM   2381  N   LEU C 101     119.939  -4.294  52.652  1.00 22.73           N  
ANISOU 2381  N   LEU C 101     2679   3641   2317   -344   -215     53       N  
ATOM   2382  CA  LEU C 101     120.292  -5.584  53.236  1.00 26.55           C  
ANISOU 2382  CA  LEU C 101     3189   4110   2789   -423   -178     17       C  
ATOM   2383  C   LEU C 101     121.363  -5.411  54.308  1.00 28.70           C  
ANISOU 2383  C   LEU C 101     3496   4319   3092   -377   -134     74       C  
ATOM   2384  O   LEU C 101     121.283  -6.005  55.385  1.00 28.97           O  
ANISOU 2384  O   LEU C 101     3527   4324   3156   -410   -101     84       O  
ATOM   2385  CB  LEU C 101     120.780  -6.556  52.162  1.00 26.92           C  
ANISOU 2385  CB  LEU C 101     3303   4146   2778   -482   -165    -54       C  
ATOM   2386  CG  LEU C 101     121.124  -7.951  52.684  1.00 23.78           C  
ANISOU 2386  CG  LEU C 101     2957   3675   2402   -558   -103   -106       C  
ATOM   2387  CD1 LEU C 101     120.025  -8.447  53.623  1.00 22.34           C  
ANISOU 2387  CD1 LEU C 101     2713   3490   2285   -619   -101   -114       C  
ATOM   2388  CD2 LEU C 101     121.342  -8.926  51.538  1.00 23.17           C  
ANISOU 2388  CD2 LEU C 101     2948   3576   2279   -620    -83   -201       C  
ATOM   2389  N   ILE C 102     122.375  -4.609  53.991  1.00 29.95           N  
ANISOU 2389  N   ILE C 102     3687   4424   3270   -296   -125    111       N  
ATOM   2390  CA  ILE C 102     123.417  -4.261  54.947  1.00 28.04           C  
ANISOU 2390  CA  ILE C 102     3468   4105   3082   -240    -92    162       C  
ATOM   2391  C   ILE C 102     122.796  -3.718  56.227  1.00 26.13           C  
ANISOU 2391  C   ILE C 102     3182   3861   2887   -221    -96    192       C  
ATOM   2392  O   ILE C 102     122.946  -4.306  57.299  1.00 27.53           O  
ANISOU 2392  O   ILE C 102     3368   4013   3081   -240    -69    211       O  
ATOM   2393  CB  ILE C 102     124.376  -3.202  54.378  1.00 26.98           C  
ANISOU 2393  CB  ILE C 102     3357   3920   2972   -167    -94    182       C  
ATOM   2394  CG1 ILE C 102     124.918  -3.641  53.015  1.00 24.29           C  
ANISOU 2394  CG1 ILE C 102     3059   3597   2572   -182    -85    154       C  
ATOM   2395  CG2 ILE C 102     125.511  -2.943  55.352  1.00 27.31           C  
ANISOU 2395  CG2 ILE C 102     3421   3883   3074   -124    -66    214       C  
ATOM   2396  CD1 ILE C 102     125.766  -4.881  53.070  1.00 25.24           C  
ANISOU 2396  CD1 ILE C 102     3227   3697   2667   -214    -31    139       C  
ATOM   2397  N   LYS C 103     122.101  -2.590  56.109  1.00 22.48           N  
ANISOU 2397  N   LYS C 103     2683   3418   2441   -181   -122    198       N  
ATOM   2398  CA  LYS C 103     121.487  -1.951  57.271  1.00 22.38           C  
ANISOU 2398  CA  LYS C 103     2634   3410   2460   -157   -117    219       C  
ATOM   2399  C   LYS C 103     120.636  -2.919  58.096  1.00 20.09           C  
ANISOU 2399  C   LYS C 103     2301   3186   2147   -224   -108    219       C  
ATOM   2400  O   LYS C 103     120.715  -2.925  59.320  1.00 16.83           O  
ANISOU 2400  O   LYS C 103     1889   2752   1754   -218    -83    244       O  
ATOM   2401  CB  LYS C 103     120.661  -0.734  56.848  1.00 25.02           C  
ANISOU 2401  CB  LYS C 103     2940   3768   2799   -113   -145    220       C  
ATOM   2402  CG  LYS C 103     121.504   0.435  56.373  1.00 27.38           C  
ANISOU 2402  CG  LYS C 103     3289   3991   3121    -57   -150    227       C  
ATOM   2403  CD  LYS C 103     120.637   1.558  55.841  1.00 29.19           C  
ANISOU 2403  CD  LYS C 103     3502   4243   3347    -20   -186    233       C  
ATOM   2404  CE  LYS C 103     121.478   2.754  55.429  1.00 30.35           C  
ANISOU 2404  CE  LYS C 103     3689   4339   3505     16   -190    252       C  
ATOM   2405  NZ  LYS C 103     120.839   3.521  54.320  1.00 32.82           N  
ANISOU 2405  NZ  LYS C 103     3993   4684   3793     37   -234    265       N  
ATOM   2406  N   ALA C 104     119.826  -3.731  57.421  1.00 17.56           N  
ANISOU 2406  N   ALA C 104     1949   2939   1786   -296   -129    181       N  
ATOM   2407  CA  ALA C 104     118.981  -4.713  58.097  1.00 15.62           C  
ANISOU 2407  CA  ALA C 104     1661   2726   1549   -380   -109    157       C  
ATOM   2408  C   ALA C 104     119.831  -5.700  58.891  1.00 16.40           C  
ANISOU 2408  C   ALA C 104     1831   2719   1681   -406    -40    172       C  
ATOM   2409  O   ALA C 104     119.594  -5.940  60.077  1.00 16.98           O  
ANISOU 2409  O   ALA C 104     1899   2767   1787   -418      3    198       O  
ATOM   2410  CB  ALA C 104     118.109  -5.444  57.093  1.00 16.39           C  
ANISOU 2410  CB  ALA C 104     1718   2876   1633   -461   -140     89       C  
ATOM   2411  N   LYS C 105     120.830  -6.264  58.224  1.00 18.02           N  
ANISOU 2411  N   LYS C 105     2105   2865   1878   -409    -28    159       N  
ATOM   2412  CA  LYS C 105     121.740  -7.208  58.858  1.00 22.54           C  
ANISOU 2412  CA  LYS C 105     2745   3330   2490   -419     31    180       C  
ATOM   2413  C   LYS C 105     122.464  -6.575  60.045  1.00 25.20           C  
ANISOU 2413  C   LYS C 105     3099   3630   2844   -350     40    251       C  
ATOM   2414  O   LYS C 105     122.885  -7.269  60.969  1.00 26.20           O  
ANISOU 2414  O   LYS C 105     3264   3674   3018   -346     76    273       O  
ATOM   2415  CB  LYS C 105     122.751  -7.747  57.842  1.00 23.45           C  
ANISOU 2415  CB  LYS C 105     2921   3393   2595   -412     45    152       C  
ATOM   2416  CG  LYS C 105     122.128  -8.578  56.730  1.00 22.95           C  
ANISOU 2416  CG  LYS C 105     2863   3343   2515   -488     41     63       C  
ATOM   2417  CD  LYS C 105     122.903  -9.868  56.501  1.00 26.52           C  
ANISOU 2417  CD  LYS C 105     3391   3683   3004   -512    103     30       C  
ATOM   2418  CE  LYS C 105     122.190 -10.786  55.512  1.00 31.53           C  
ANISOU 2418  CE  LYS C 105     4040   4318   3622   -605    103    -73       C  
ATOM   2419  NZ  LYS C 105     122.814 -12.144  55.455  1.00 34.11           N  
ANISOU 2419  NZ  LYS C 105     4448   4512   4002   -632    175   -111       N  
ATOM   2420  N   ILE C 106     122.607  -5.255  60.015  1.00 25.70           N  
ANISOU 2420  N   ILE C 106     3140   3718   2906   -274     -6    260       N  
ATOM   2421  CA  ILE C 106     123.225  -4.536  61.122  1.00 27.39           C  
ANISOU 2421  CA  ILE C 106     3372   3869   3168   -204     -8    279       C  
ATOM   2422  C   ILE C 106     122.251  -4.371  62.286  1.00 28.72           C  
ANISOU 2422  C   ILE C 106     3511   4065   3335   -217      4    288       C  
ATOM   2423  O   ILE C 106     122.612  -4.570  63.446  1.00 27.15           O  
ANISOU 2423  O   ILE C 106     3348   3809   3161   -202     26    301       O  
ATOM   2424  CB  ILE C 106     123.722  -3.146  60.683  1.00 26.78           C  
ANISOU 2424  CB  ILE C 106     3288   3779   3108   -140    -38    269       C  
ATOM   2425  CG1 ILE C 106     125.074  -3.255  59.974  1.00 25.58           C  
ANISOU 2425  CG1 ILE C 106     3178   3572   2971   -115    -34    265       C  
ATOM   2426  CG2 ILE C 106     123.837  -2.217  61.882  1.00 26.41           C  
ANISOU 2426  CG2 ILE C 106     3248   3698   3088   -101    -37    271       C  
ATOM   2427  CD1 ILE C 106     125.603  -1.926  59.487  1.00 24.17           C  
ANISOU 2427  CD1 ILE C 106     3004   3369   2810    -71    -51    251       C  
ATOM   2428  N   ASN C 107     121.013  -4.012  61.967  1.00 30.77           N  
ANISOU 2428  N   ASN C 107     3704   4424   3562   -245     -7    280       N  
ATOM   2429  CA  ASN C 107     119.999  -3.763  62.982  1.00 31.72           C  
ANISOU 2429  CA  ASN C 107     3785   4589   3679   -253     17    285       C  
ATOM   2430  C   ASN C 107     119.561  -5.054  63.660  1.00 30.73           C  
ANISOU 2430  C   ASN C 107     3672   4429   3575   -320     69    279       C  
ATOM   2431  O   ASN C 107     119.031  -5.036  64.772  1.00 30.42           O  
ANISOU 2431  O   ASN C 107     3628   4385   3544   -320    103    285       O  
ATOM   2432  CB  ASN C 107     118.795  -3.044  62.369  1.00 36.31           C  
ANISOU 2432  CB  ASN C 107     4270   5300   4225   -257     -2    278       C  
ATOM   2433  CG  ASN C 107     119.179  -1.748  61.689  1.00 42.13           C  
ANISOU 2433  CG  ASN C 107     5008   6039   4961   -177    -54    282       C  
ATOM   2434  OD1 ASN C 107     120.230  -1.172  61.973  1.00 41.99           O  
ANISOU 2434  OD1 ASN C 107     5054   5918   4983   -126    -51    283       O  
ATOM   2435  ND2 ASN C 107     118.326  -1.278  60.785  1.00 46.47           N  
ANISOU 2435  ND2 ASN C 107     5501   6653   5501   -163    -86    263       N  
ATOM   2436  N   VAL C 108     119.785  -6.175  62.980  1.00 30.76           N  
ANISOU 2436  N   VAL C 108     3697   4400   3590   -379     83    265       N  
ATOM   2437  CA  VAL C 108     119.510  -7.482  63.564  1.00 33.53           C  
ANISOU 2437  CA  VAL C 108     4073   4689   3977   -441    135    262       C  
ATOM   2438  C   VAL C 108     120.613  -7.858  64.546  1.00 37.94           C  
ANISOU 2438  C   VAL C 108     4713   5145   4559   -393    156    303       C  
ATOM   2439  O   VAL C 108     120.354  -8.456  65.592  1.00 37.78           O  
ANISOU 2439  O   VAL C 108     4712   5083   4558   -407    197    321       O  
ATOM   2440  CB  VAL C 108     119.377  -8.575  62.483  1.00 32.17           C  
ANISOU 2440  CB  VAL C 108     3902   4504   3818   -529    145    224       C  
ATOM   2441  CG1 VAL C 108     119.471  -9.959  63.107  1.00 31.38           C  
ANISOU 2441  CG1 VAL C 108     3854   4300   3768   -576    200    234       C  
ATOM   2442  CG2 VAL C 108     118.064  -8.409  61.721  1.00 32.57           C  
ANISOU 2442  CG2 VAL C 108     3857   4659   3858   -591    120    170       C  
ATOM   2443  N   LEU C 109     121.844  -7.486  64.209  1.00 40.23           N  
ANISOU 2443  N   LEU C 109     5042   5398   4848   -333    127    315       N  
ATOM   2444  CA  LEU C 109     122.989  -7.784  65.063  1.00 41.78           C  
ANISOU 2444  CA  LEU C 109     5299   5508   5067   -282    138    345       C  
ATOM   2445  C   LEU C 109     122.957  -6.985  66.364  1.00 47.17           C  
ANISOU 2445  C   LEU C 109     5991   6196   5736   -241    131    353       C  
ATOM   2446  O   LEU C 109     123.043  -7.556  67.448  1.00 46.92           O  
ANISOU 2446  O   LEU C 109     5995   6124   5709   -245    162    375       O  
ATOM   2447  CB  LEU C 109     124.303  -7.539  64.314  1.00 36.85           C  
ANISOU 2447  CB  LEU C 109     4698   4852   4450   -233    112    346       C  
ATOM   2448  CG  LEU C 109     125.580  -7.814  65.111  1.00 31.99           C  
ANISOU 2448  CG  LEU C 109     4134   4165   3858   -185    117    369       C  
ATOM   2449  CD1 LEU C 109     125.548  -9.209  65.720  1.00 30.66           C  
ANISOU 2449  CD1 LEU C 109     4004   3932   3713   -216    168    401       C  
ATOM   2450  CD2 LEU C 109     126.810  -7.636  64.237  1.00 29.68           C  
ANISOU 2450  CD2 LEU C 109     3850   3851   3575   -149     99    366       C  
ATOM   2451  N   ILE C 110     122.832  -5.665  66.247  1.00 50.86           N  
ANISOU 2451  N   ILE C 110     6429   6711   6185   -207     94    335       N  
ATOM   2452  CA  ILE C 110     122.750  -4.791  67.415  1.00 55.39           C  
ANISOU 2452  CA  ILE C 110     7015   7290   6742   -178     92    334       C  
ATOM   2453  C   ILE C 110     121.299  -4.392  67.688  1.00 62.28           C  
ANISOU 2453  C   ILE C 110     7836   8238   7588   -204    115    328       C  
ATOM   2454  O   ILE C 110     120.690  -3.635  66.929  1.00 65.46           O  
ANISOU 2454  O   ILE C 110     8183   8709   7980   -197     95    315       O  
ATOM   2455  CB  ILE C 110     123.644  -3.543  67.264  1.00 55.04           C  
ANISOU 2455  CB  ILE C 110     6980   7231   6703   -125     49    316       C  
ATOM   2456  CG1 ILE C 110     122.951  -2.303  67.838  1.00 57.30           C  
ANISOU 2456  CG1 ILE C 110     7250   7558   6963   -109     47    307       C  
ATOM   2457  CG2 ILE C 110     123.993  -3.316  65.802  1.00 54.60           C  
ANISOU 2457  CG2 ILE C 110     6898   7184   6665   -115     22    303       C  
ATOM   2458  CD1 ILE C 110     122.704  -1.203  66.810  1.00 58.90           C  
ANISOU 2458  CD1 ILE C 110     7411   7799   7171    -84     19    292       C  
ATOM   2459  N   GLY C 111     120.751  -4.932  68.774  1.00 67.11           N  
ANISOU 2459  N   GLY C 111     8465   8845   8190   -231    163    340       N  
ATOM   2460  CA  GLY C 111     119.377  -4.681  69.173  1.00 73.56           C  
ANISOU 2460  CA  GLY C 111     9229   9732   8988   -258    204    331       C  
ATOM   2461  C   GLY C 111     118.845  -5.914  69.884  1.00 80.66           C  
ANISOU 2461  C   GLY C 111    10143  10606   9900   -312    265    348       C  
ATOM   2462  O   GLY C 111     119.581  -6.890  70.067  1.00 81.30           O  
ANISOU 2462  O   GLY C 111    10278  10615   9999   -321    272    373       O  
ATOM   2463  N   HIS C 112     117.572  -5.869  70.273  1.00 85.58           N  
ANISOU 2463  N   HIS C 112    10711  11288  10518   -344    315    336       N  
ATOM   2464  CA  HIS C 112     116.868  -7.006  70.874  1.00 87.42           C  
ANISOU 2464  CA  HIS C 112    10941  11502  10771   -404    380    353       C  
ATOM   2465  C   HIS C 112     115.761  -6.494  71.795  1.00 87.91           C  
ANISOU 2465  C   HIS C 112    10964  11627  10813   -408    441    344       C  
ATOM   2466  O   HIS C 112     116.003  -5.626  72.644  1.00 86.37           O  
ANISOU 2466  O   HIS C 112    10806  11439  10572   -361    450    345       O  
ATOM   2467  CB  HIS C 112     117.815  -7.914  71.669  1.00 88.70           C  
ANISOU 2467  CB  HIS C 112    11195  11573  10933   -400    394    399       C  
ATOM   2468  CG  HIS C 112     117.502  -9.380  71.548  1.00 89.31           C  
ANISOU 2468  CG  HIS C 112    11272  11605  11058   -464    434    423       C  
ATOM   2469  ND1 HIS C 112     116.737 -10.060  72.472  1.00 89.43           N  
ANISOU 2469  ND1 HIS C 112    11285  11617  11079   -506    501    453       N  
ATOM   2470  CD2 HIS C 112     117.860 -10.291  70.615  1.00 89.06           C  
ANISOU 2470  CD2 HIS C 112    11243  11524  11071   -495    418    424       C  
ATOM   2471  CE1 HIS C 112     116.632 -11.327  72.109  1.00 89.64           C  
ANISOU 2471  CE1 HIS C 112    11310  11591  11158   -562    520    473       C  
ATOM   2472  NE2 HIS C 112     117.312 -11.495  70.987  1.00 89.80           N  
ANISOU 2472  NE2 HIS C 112    11337  11579  11202   -557    471    453       N  
TER    2473      HIS C 112                                                      
ATOM   2474  O3'  DA D   1     152.535  11.033  70.613  1.00164.96           O  
ANISOU 2474  O3'  DA D   1    20031  21598  21048   -430    727  -3563       O  
ATOM   2475  P    DU D   2     152.377   9.506  70.139  1.00 46.42           P  
ANISOU 2475  P    DU D   2     4969   6803   5866   -686    637  -3018       P  
ATOM   2476  OP1  DU D   2     150.936   9.235  69.944  1.00 48.22           O  
ANISOU 2476  OP1  DU D   2     4749   7347   6227   -596    885  -3181       O  
ATOM   2477  OP2  DU D   2     153.168   8.660  71.060  1.00 48.36           O  
ANISOU 2477  OP2  DU D   2     5526   7296   5554  -1224    549  -2733       O  
ATOM   2478  O5'  DU D   2     153.120   9.475  68.722  1.00 57.71           O  
ANISOU 2478  O5'  DU D   2     6529   7684   7713   -405    250  -2575       O  
ATOM   2479  C5'  DU D   2     152.827  10.416  67.695  1.00 55.88           C  
ANISOU 2479  C5'  DU D   2     6172   7046   8015     20    126  -2681       C  
ATOM   2480  C4'  DU D   2     154.034  10.557  66.782  1.00 50.73           C  
ANISOU 2480  C4'  DU D   2     5780   5996   7500     75   -197  -2290       C  
ATOM   2481  O4'  DU D   2     154.794  11.740  67.141  1.00 51.27           O  
ANISOU 2481  O4'  DU D   2     6018   5815   7648    120   -309  -2443       O  
ATOM   2482  C3'  DU D   2     155.029   9.403  66.842  1.00 47.56           C  
ANISOU 2482  C3'  DU D   2     5575   5705   6791   -189   -291  -1876       C  
ATOM   2483  O3'  DU D   2     155.652   9.269  65.574  1.00 44.40           O  
ANISOU 2483  O3'  DU D   2     5242   5046   6582    -54   -483  -1554       O  
ATOM   2484  C2'  DU D   2     156.011   9.880  67.904  1.00 49.31           C  
ANISOU 2484  C2'  DU D   2     5997   5937   6800   -397   -322  -1965       C  
ATOM   2485  C1'  DU D   2     156.082  11.370  67.593  1.00 50.56           C  
ANISOU 2485  C1'  DU D   2     6173   5756   7282   -154   -410  -2209       C  
ATOM   2486  N1   DU D   2     156.435  12.206  68.775  1.00 55.72           N  
ANISOU 2486  N1   DU D   2     7002   6422   7747   -281   -379  -2472       N  
ATOM   2487  C2   DU D   2     157.565  12.998  68.734  1.00 57.23           C  
ANISOU 2487  C2   DU D   2     7409   6329   8006   -334   -635  -2287       C  
ATOM   2488  O2   DU D   2     158.307  13.054  67.769  1.00 55.95           O  
ANISOU 2488  O2   DU D   2     7244   5968   8047   -298   -845  -1935       O  
ATOM   2489  N3   DU D   2     157.800  13.728  69.874  1.00 60.16           N  
ANISOU 2489  N3   DU D   2     8004   6693   8161   -475   -630  -2531       N  
ATOM   2490  C4   DU D   2     157.035  13.744  71.025  1.00 62.87           C  
ANISOU 2490  C4   DU D   2     8371   7322   8195   -553   -355  -2950       C  
ATOM   2491  O4   DU D   2     157.325  14.430  71.999  1.00 65.70           O  
ANISOU 2491  O4   DU D   2     8992   7642   8329   -682   -380  -3162       O  
ATOM   2492  C5   DU D   2     155.874  12.892  70.992  1.00 62.76           C  
ANISOU 2492  C5   DU D   2     8050   7684   8111   -514    -36  -3113       C  
ATOM   2493  C6   DU D   2     155.625  12.171  69.892  1.00 58.99           C  
ANISOU 2493  C6   DU D   2     7365   7173   7875   -388    -86  -2868       C  
ATOM   2494  P    DA D   3     156.883   8.254  65.376  1.00 68.79           P  
ANISOU 2494  P    DA D   3     8462   8146   9530   -180   -603  -1202       P  
ATOM   2495  OP1  DA D   3     156.563   7.001  66.096  1.00 68.61           O  
ANISOU 2495  OP1  DA D   3     8455   8350   9265   -394   -604  -1124       O  
ATOM   2496  OP2  DA D   3     158.130   8.981  65.699  1.00 69.72           O  
ANISOU 2496  OP2  DA D   3     8664   8152   9673   -252   -700  -1148       O  
ATOM   2497  O5'  DA D   3     156.880   7.978  63.799  1.00 29.41           O  
ANISOU 2497  O5'  DA D   3     3469   3006   4699      8   -669  -1011       O  
ATOM   2498  C5'  DA D   3     157.783   7.054  63.203  1.00 29.35           C  
ANISOU 2498  C5'  DA D   3     3512   2992   4647     25   -721   -806       C  
ATOM   2499  C4'  DA D   3     157.030   5.833  62.702  1.00 28.00           C  
ANISOU 2499  C4'  DA D   3     3386   2838   4414     63   -763   -751       C  
ATOM   2500  O4'  DA D   3     155.802   6.231  62.044  1.00 25.99           O  
ANISOU 2500  O4'  DA D   3     3105   2537   4233    125   -757   -798       O  
ATOM   2501  C3'  DA D   3     157.747   5.011  61.643  1.00 28.17           C  
ANISOU 2501  C3'  DA D   3     3483   2783   4436    189   -798   -661       C  
ATOM   2502  O3'  DA D   3     158.731   4.174  62.230  1.00 27.19           O  
ANISOU 2502  O3'  DA D   3     3333   2652   4347    183   -891   -616       O  
ATOM   2503  C2'  DA D   3     156.576   4.216  61.083  1.00 28.61           C  
ANISOU 2503  C2'  DA D   3     3645   2790   4434    199   -890   -643       C  
ATOM   2504  C1'  DA D   3     155.495   5.293  61.031  1.00 25.78           C  
ANISOU 2504  C1'  DA D   3     3197   2443   4155    170   -848   -688       C  
ATOM   2505  N9   DA D   3     155.435   5.974  59.740  1.00 25.17           N  
ANISOU 2505  N9   DA D   3     3195   2241   4128    231   -877   -635       N  
ATOM   2506  C8   DA D   3     155.529   7.315  59.486  1.00 25.91           C  
ANISOU 2506  C8   DA D   3     3241   2245   4358    227   -899   -633       C  
ATOM   2507  N7   DA D   3     155.438   7.619  58.211  1.00 24.64           N  
ANISOU 2507  N7   DA D   3     3215   1982   4164    175  -1010   -498       N  
ATOM   2508  C5   DA D   3     155.278   6.396  57.586  1.00 23.46           C  
ANISOU 2508  C5   DA D   3     3222   1873   3818    177  -1006   -468       C  
ATOM   2509  C6   DA D   3     155.126   6.026  56.234  1.00 26.64           C  
ANISOU 2509  C6   DA D   3     3872   2232   4019     91  -1090   -374       C  
ATOM   2510  N6   DA D   3     155.107   6.904  55.221  1.00 28.54           N  
ANISOU 2510  N6   DA D   3     4236   2410   4198    -84  -1212   -218       N  
ATOM   2511  N1   DA D   3     154.988   4.708  55.960  1.00 27.27           N  
ANISOU 2511  N1   DA D   3     4116   2310   3933    138  -1102   -435       N  
ATOM   2512  C2   DA D   3     155.000   3.833  56.971  1.00 25.80           C  
ANISOU 2512  C2   DA D   3     3839   2145   3821    237  -1092   -518       C  
ATOM   2513  N3   DA D   3     155.139   4.059  58.273  1.00 23.46           N  
ANISOU 2513  N3   DA D   3     3315   1928   3671    255  -1029   -551       N  
ATOM   2514  C4   DA D   3     155.275   5.372  58.513  1.00 23.16           C  
ANISOU 2514  C4   DA D   3     3128   1914   3756    237   -954   -553       C  
ATOM   2515  P    DC D   4     160.215   4.125  61.618  1.00 33.52           P  
ANISOU 2515  P    DC D   4     4012   3452   5271    338   -817   -616       P  
ATOM   2516  OP1  DC D   4     161.024   3.213  62.455  1.00 35.11           O  
ANISOU 2516  OP1  DC D   4     4133   3574   5634    341  -1026   -562       O  
ATOM   2517  OP2  DC D   4     160.664   5.516  61.406  1.00 34.78           O  
ANISOU 2517  OP2  DC D   4     4084   3701   5431    268   -679   -576       O  
ATOM   2518  O5'  DC D   4     160.007   3.461  60.178  1.00 43.12           O  
ANISOU 2518  O5'  DC D   4     5335   4635   6415    523   -733   -722       O  
ATOM   2519  C5'  DC D   4     159.681   2.081  60.056  1.00 44.11           C  
ANISOU 2519  C5'  DC D   4     5597   4597   6566    632   -917   -790       C  
ATOM   2520  C4'  DC D   4     159.435   1.703  58.606  1.00 45.77           C  
ANISOU 2520  C4'  DC D   4     5983   4785   6623    766   -811   -940       C  
ATOM   2521  O4'  DC D   4     158.309   2.461  58.096  1.00 45.16           O  
ANISOU 2521  O4'  DC D   4     6048   4742   6366    597   -790   -835       O  
ATOM   2522  C3'  DC D   4     160.584   1.995  57.651  1.00 48.10           C  
ANISOU 2522  C3'  DC D   4     6138   5269   6869    901   -500  -1104       C  
ATOM   2523  O3'  DC D   4     161.472   0.881  57.613  1.00 50.75           O  
ANISOU 2523  O3'  DC D   4     6358   5511   7413   1188   -525  -1342       O  
ATOM   2524  C2'  DC D   4     159.850   2.158  56.325  1.00 49.21           C  
ANISOU 2524  C2'  DC D   4     6558   5457   6681    811   -407  -1149       C  
ATOM   2525  C1'  DC D   4     158.553   2.841  56.754  1.00 46.22           C  
ANISOU 2525  C1'  DC D   4     6284   4980   6296    593   -606   -902       C  
ATOM   2526  N1   DC D   4     158.611   4.332  56.681  1.00 44.94           N  
ANISOU 2526  N1   DC D   4     6017   4942   6118    411   -519   -740       N  
ATOM   2527  C2   DC D   4     158.655   4.965  55.434  1.00 47.01           C  
ANISOU 2527  C2   DC D   4     6412   5313   6137    243   -436   -676       C  
ATOM   2528  O2   DC D   4     158.642   4.279  54.405  1.00 49.00           O  
ANISOU 2528  O2   DC D   4     6875   5612   6128    246   -365   -800       O  
ATOM   2529  N3   DC D   4     158.712   6.319  55.388  1.00 49.66           N  
ANISOU 2529  N3   DC D   4     6681   5679   6507     37   -484   -478       N  
ATOM   2530  C4   DC D   4     158.720   7.028  56.517  1.00 48.89           C  
ANISOU 2530  C4   DC D   4     6404   5493   6677     58   -571   -423       C  
ATOM   2531  N4   DC D   4     158.771   8.360  56.415  1.00 50.27           N  
ANISOU 2531  N4   DC D   4     6561   5613   6925   -130   -698   -253       N  
ATOM   2532  C5   DC D   4     158.673   6.402  57.797  1.00 46.74           C  
ANISOU 2532  C5   DC D   4     6008   5168   6582    222   -580   -536       C  
ATOM   2533  C6   DC D   4     158.621   5.066  57.831  1.00 45.48           C  
ANISOU 2533  C6   DC D   4     5906   4992   6382    363   -572   -652       C  
ATOM   2534  P    DA D   5     163.055   1.110  57.448  1.00 44.37           P  
ANISOU 2534  P    DA D   5     5123   4945   6791   1358   -236  -1487       P  
ATOM   2535  OP1  DA D   5     163.693  -0.215  57.287  1.00 48.00           O  
ANISOU 2535  OP1  DA D   5     5476   5213   7550   1747   -321  -1829       O  
ATOM   2536  OP2  DA D   5     163.502   2.011  58.531  1.00 42.20           O  
ANISOU 2536  OP2  DA D   5     4616   4742   6678   1165   -311  -1195       O  
ATOM   2537  O5'  DA D   5     163.179   1.905  56.064  1.00 57.61           O  
ANISOU 2537  O5'  DA D   5     6835   7002   8053   1222    191  -1568       O  
ATOM   2538  C5'  DA D   5     162.980   1.228  54.822  1.00 57.08           C  
ANISOU 2538  C5'  DA D   5     6999   6989   7700   1337    369  -1897       C  
ATOM   2539  C4'  DA D   5     163.127   2.188  53.652  1.00 55.30           C  
ANISOU 2539  C4'  DA D   5     6823   7195   6993   1025    731  -1851       C  
ATOM   2540  O4'  DA D   5     162.052   3.162  53.667  1.00 49.51           O  
ANISOU 2540  O4'  DA D   5     6371   6360   6079    659    498  -1457       O  
ATOM   2541  C3'  DA D   5     164.389   3.034  53.668  1.00 53.81           C  
ANISOU 2541  C3'  DA D   5     6162   7443   6841    905   1053  -1763       C  
ATOM   2542  O3'  DA D   5     165.474   2.323  53.112  1.00 55.89           O  
ANISOU 2542  O3'  DA D   5     6089   8006   7140   1187   1449  -2206       O  
ATOM   2543  C2'  DA D   5     163.981   4.215  52.800  1.00 53.78           C  
ANISOU 2543  C2'  DA D   5     6389   7697   6347    398   1127  -1469       C  
ATOM   2544  C1'  DA D   5     162.559   4.433  53.302  1.00 48.10           C  
ANISOU 2544  C1'  DA D   5     6050   6513   5713    316    664  -1212       C  
ATOM   2545  N9   DA D   5     162.467   5.286  54.479  1.00 42.52           N  
ANISOU 2545  N9   DA D   5     5192   5630   5336    241    415   -907       N  
ATOM   2546  C8   DA D   5     162.498   4.889  55.788  1.00 41.12           C  
ANISOU 2546  C8   DA D   5     4868   5210   5547    463    231   -917       C  
ATOM   2547  N7   DA D   5     162.385   5.882  56.643  1.00 38.31           N  
ANISOU 2547  N7   DA D   5     4450   4762   5344    301     54   -672       N  
ATOM   2548  C5   DA D   5     162.270   7.001  55.832  1.00 36.91           C  
ANISOU 2548  C5   DA D   5     4373   4709   4941    -12     66   -474       C  
ATOM   2549  C6   DA D   5     162.122   8.369  56.126  1.00 35.10           C  
ANISOU 2549  C6   DA D   5     4170   4382   4786   -272   -150   -206       C  
ATOM   2550  N6   DA D   5     162.065   8.850  57.371  1.00 32.17           N  
ANISOU 2550  N6   DA D   5     3725   3804   4692   -228   -339   -164       N  
ATOM   2551  N1   DA D   5     162.040   9.222  55.085  1.00 37.94           N  
ANISOU 2551  N1   DA D   5     4671   4840   4905   -613   -211      8       N  
ATOM   2552  C2   DA D   5     162.104   8.736  53.839  1.00 40.22           C  
ANISOU 2552  C2   DA D   5     5082   5389   4810   -732     -1    -51       C  
ATOM   2553  N3   DA D   5     162.242   7.473  53.440  1.00 40.99           N  
ANISOU 2553  N3   DA D   5     5183   5634   4757   -486    282   -372       N  
ATOM   2554  C4   DA D   5     162.321   6.650  54.496  1.00 39.63           C  
ANISOU 2554  C4   DA D   5     4850   5282   4926    -99    276   -572       C  
ATOM   2555  P    DU D   6     166.958   2.567  53.671  1.00120.37           P  
ANISOU 2555  P    DU D   6    13552  16467  15718   1310   1656  -2201       P  
ATOM   2556  OP1  DU D   6     167.801   1.434  53.236  1.00126.54           O  
ANISOU 2556  OP1  DU D   6    14002  17359  16719   1786   1950  -2776       O  
ATOM   2557  OP2  DU D   6     166.850   2.897  55.111  1.00115.45           O  
ANISOU 2557  OP2  DU D   6    12863  15469  15533   1284   1196  -1812       O  
ATOM   2558  O5'  DU D   6     167.426   3.896  52.916  1.00 89.13           O  
ANISOU 2558  O5'  DU D   6     9456  13117  11291    768   1999  -1914       O  
ATOM   2559  C5'  DU D   6     167.179   4.055  51.525  1.00 91.01           C  
ANISOU 2559  C5'  DU D   6     9965  13759  10857    469   2342  -2053       C  
ATOM   2560  C4'  DU D   6     167.238   5.526  51.169  1.00 88.38           C  
ANISOU 2560  C4'  DU D   6     9676  13762  10142   -204   2327  -1514       C  
ATOM   2561  O4'  DU D   6     166.127   6.231  51.774  1.00 81.09           O  
ANISOU 2561  O4'  DU D   6     9179  12305   9325   -390   1758  -1076       O  
ATOM   2562  C3'  DU D   6     168.470   6.224  51.712  1.00 88.74           C  
ANISOU 2562  C3'  DU D   6     9104  14147  10467   -343   2441  -1260       C  
ATOM   2563  O3'  DU D   6     169.531   6.066  50.799  1.00 94.78           O  
ANISOU 2563  O3'  DU D   6     9413  15668  10933   -447   3065  -1535       O  
ATOM   2564  C2'  DU D   6     168.015   7.673  51.800  1.00 86.94           C  
ANISOU 2564  C2'  DU D   6     9164  13820  10048   -946   2048   -626       C  
ATOM   2565  C1'  DU D   6     166.549   7.515  52.197  1.00 81.37           C  
ANISOU 2565  C1'  DU D   6     9040  12430   9447   -782   1577   -591       C  
ATOM   2566  N1   DU D   6     166.299   7.650  53.662  1.00 77.56           N  
ANISOU 2566  N1   DU D   6     8517  11426   9527   -534   1165   -449       N  
ATOM   2567  C2   DU D   6     166.592   8.842  54.291  1.00 77.98           C  
ANISOU 2567  C2   DU D   6     8483  11407   9737   -841    888    -38       C  
ATOM   2568  O2   DU D   6     167.058   9.808  53.712  1.00 81.26           O  
ANISOU 2568  O2   DU D   6     8841  12133   9902  -1321    903    276       O  
ATOM   2569  N3   DU D   6     166.325   8.865  55.637  1.00 75.02           N  
ANISOU 2569  N3   DU D   6     8127  10586   9790   -619    557      0       N  
ATOM   2570  C4   DU D   6     165.802   7.839  56.401  1.00 71.74           C  
ANISOU 2570  C4   DU D   6     7790   9842   9627   -200    467   -260       C  
ATOM   2571  O4   DU D   6     165.595   7.953  57.605  1.00 69.33           O  
ANISOU 2571  O4   DU D   6     7519   9225   9599   -126    185   -192       O  
ATOM   2572  C5   DU D   6     165.521   6.629  55.674  1.00 71.94           C  
ANISOU 2572  C5   DU D   6     7892   9926   9517     81    698   -615       C  
ATOM   2573  C6   DU D   6     165.774   6.583  54.361  1.00 74.94           C  
ANISOU 2573  C6   DU D   6     8276  10697   9501    -62   1037   -727       C  
ATOM   2574  P    DA D   7     170.955   5.538  51.312  1.00 96.34           P  
ANISOU 2574  P    DA D   7     8807  16078  11720    -21   3330  -1769       P  
ATOM   2575  OP1  DA D   7     170.963   4.064  51.192  1.00 99.92           O  
ANISOU 2575  OP1  DA D   7     9325  16186  12455    665   3407  -2357       O  
ATOM   2576  OP2  DA D   7     171.221   6.160  52.626  1.00 91.19           O  
ANISOU 2576  OP2  DA D   7     7892  15142  11613    -71   2893  -1319       O  
ATOM   2577  O5'  DA D   7     171.984   6.151  50.253  1.00 80.75           O  
ANISOU 2577  O5'  DA D   7     6565  14820   9298   -486   3775  -1623       O  
TER    2578       DA D   7                                                      
ATOM   2579  O3'  DA E   1     143.813  18.931  32.022  1.00100.19           O  
ANISOU 2579  O3'  DA E   1    11943  15919  10205    700   2386  -1274       O  
ATOM   2580  P    DU E   2     143.288  18.680  33.520  0.92 76.26           P  
ANISOU 2580  P    DU E   2     8730  12493   7753    984   2413  -1292       P  
ATOM   2581  OP1  DU E   2     143.504  17.251  33.846  0.92 75.49           O  
ANISOU 2581  OP1  DU E   2     8531  12193   7958    914   2944  -1692       O  
ATOM   2582  OP2  DU E   2     141.932  19.261  33.631  0.92 76.77           O  
ANISOU 2582  OP2  DU E   2     8669  12673   7826   1092   1980  -1213       O  
ATOM   2583  O5'  DU E   2     144.263  19.579  34.414  0.92 61.96           O  
ANISOU 2583  O5'  DU E   2     7044  10373   6126   1183   2363   -808       O  
ATOM   2584  C5'  DU E   2     143.945  20.946  34.656  0.92 61.46           C  
ANISOU 2584  C5'  DU E   2     7115  10273   5964   1327   1964   -424       C  
ATOM   2585  C4'  DU E   2     144.822  21.496  35.766  0.92 58.64           C  
ANISOU 2585  C4'  DU E   2     6936   9540   5805   1393   1999    -78       C  
ATOM   2586  O4'  DU E   2     146.200  21.330  35.356  0.92 59.00           O  
ANISOU 2586  O4'  DU E   2     6995   9664   5760   1240   2177     94       O  
ATOM   2587  C3'  DU E   2     144.627  22.976  36.094  0.92 58.57           C  
ANISOU 2587  C3'  DU E   2     7197   9378   5678   1492   1705    310       C  
ATOM   2588  O3'  DU E   2     144.590  23.205  37.508  0.92 56.43           O  
ANISOU 2588  O3'  DU E   2     7126   8646   5667   1535   1767    416       O  
ATOM   2589  C2'  DU E   2     145.832  23.654  35.450  0.92 59.41           C  
ANISOU 2589  C2'  DU E   2     7452   9636   5484   1348   1631    637       C  
ATOM   2590  C1'  DU E   2     146.887  22.557  35.434  0.92 58.87           C  
ANISOU 2590  C1'  DU E   2     7208   9597   5561   1204   1947    548       C  
ATOM   2591  N1   DU E   2     147.789  22.636  34.260  0.92 63.04           N  
ANISOU 2591  N1   DU E   2     7729  10406   5818   1079   2033    666       N  
ATOM   2592  C2   DU E   2     148.784  23.588  34.241  0.92 66.57           C  
ANISOU 2592  C2   DU E   2     8336  10822   6135    996   1903   1123       C  
ATOM   2593  O2   DU E   2     148.960  24.380  35.151  0.92 66.56           O  
ANISOU 2593  O2   DU E   2     8524  10577   6189    965   1706   1418       O  
ATOM   2594  N3   DU E   2     149.567  23.580  33.112  0.92 68.42           N  
ANISOU 2594  N3   DU E   2     8551  11296   6147    902   2049   1211       N  
ATOM   2595  C4   DU E   2     149.450  22.728  32.028  0.92 71.32           C  
ANISOU 2595  C4   DU E   2     8840  11899   6361    843   2346    862       C  
ATOM   2596  O4   DU E   2     150.199  22.795  31.059  0.92 75.66           O  
ANISOU 2596  O4   DU E   2     9454  12601   6692    738   2537    961       O  
ATOM   2597  C5   DU E   2     148.386  21.761  32.125  0.92 69.39           C  
ANISOU 2597  C5   DU E   2     8481  11675   6210    866   2452    368       C  
ATOM   2598  C6   DU E   2     147.613  21.752  33.216  0.92 65.88           C  
ANISOU 2598  C6   DU E   2     7972  11024   6037   1002   2278    305       C  
ATOM   2599  P    DA E   3     143.994  24.582  38.088  1.00 93.44           P  
ANISOU 2599  P    DA E   3    12181  12993  10329   1654   1648    695       P  
ATOM   2600  OP1  DA E   3     142.674  24.809  37.459  1.00 95.70           O  
ANISOU 2600  OP1  DA E   3    12263  13427  10670   1897   1558    642       O  
ATOM   2601  OP2  DA E   3     145.043  25.618  37.976  1.00 93.76           O  
ANISOU 2601  OP2  DA E   3    12541  12998  10085   1477   1528   1076       O  
ATOM   2602  O5'  DA E   3     143.786  24.276  39.645  1.00 72.12           O  
ANISOU 2602  O5'  DA E   3     9697   9788   7917   1630   1847    608       O  
TER    2603       DA E   3                                                      
ATOM   2604  O3'  DA F   1     143.805  -6.720  44.427  0.80 70.38           O  
ANISOU 2604  O3'  DA F   1    11187   8945   6609   -802   4491   -424       O  
ATOM   2605  P    DU F   2     144.031  -7.427  45.852  0.82 85.19           P  
ANISOU 2605  P    DU F   2    13055  10842   8471   -736   4404   -463       P  
ATOM   2606  OP1  DU F   2     145.401  -7.104  46.309  0.82 86.83           O  
ANISOU 2606  OP1  DU F   2    12916  11337   8737   -664   4405   -355       O  
ATOM   2607  OP2  DU F   2     143.606  -8.840  45.732  0.82 84.58           O  
ANISOU 2607  OP2  DU F   2    13308  10579   8250   -512   4425   -515       O  
ATOM   2608  O5'  DU F   2     142.987  -6.682  46.809  0.82 73.09           O  
ANISOU 2608  O5'  DU F   2    11534   9167   7069  -1029   4256   -572       O  
ATOM   2609  C5'  DU F   2     143.045  -6.888  48.218  0.82 70.54           C  
ANISOU 2609  C5'  DU F   2    11190   8880   6730  -1000   4165   -602       C  
ATOM   2610  C4'  DU F   2     141.682  -7.255  48.782  0.82 67.20           C  
ANISOU 2610  C4'  DU F   2    11014   8216   6303  -1082   4153   -673       C  
ATOM   2611  O4'  DU F   2     140.653  -6.582  48.014  0.82 65.66           O  
ANISOU 2611  O4'  DU F   2    10875   7851   6221  -1306   4138   -744       O  
ATOM   2612  C3'  DU F   2     141.341  -8.745  48.756  0.82 67.81           C  
ANISOU 2612  C3'  DU F   2    11358   8109   6296   -893   4236   -635       C  
ATOM   2613  O3'  DU F   2     141.207  -9.239  50.091  0.82 68.42           O  
ANISOU 2613  O3'  DU F   2    11504   8185   6310   -804   4236   -591       O  
ATOM   2614  C2'  DU F   2     140.025  -8.842  47.984  0.82 66.65           C  
ANISOU 2614  C2'  DU F   2    11394   7661   6270  -1041   4239   -699       C  
ATOM   2615  C1'  DU F   2     139.510  -7.407  47.962  0.82 65.15           C  
ANISOU 2615  C1'  DU F   2    11056   7510   6188  -1310   4173   -773       C  
ATOM   2616  N1   DU F   2     138.736  -7.080  46.729  0.82 65.30           N  
ANISOU 2616  N1   DU F   2    11171   7340   6301  -1433   4147   -855       N  
ATOM   2617  C2   DU F   2     137.360  -7.181  46.748  0.82 65.26           C  
ANISOU 2617  C2   DU F   2    11294   7059   6445  -1575   4107   -928       C  
ATOM   2618  O2   DU F   2     136.730  -7.523  47.734  0.82 65.84           O  
ANISOU 2618  O2   DU F   2    11386   7047   6581  -1610   4136   -891       O  
ATOM   2619  N3   DU F   2     136.740  -6.859  45.566  0.82 64.69           N  
ANISOU 2619  N3   DU F   2    11317   6812   6449  -1652   4039  -1030       N  
ATOM   2620  C4   DU F   2     137.347  -6.457  44.390  0.82 66.67           C  
ANISOU 2620  C4   DU F   2    11580   7151   6598  -1576   4039  -1042       C  
ATOM   2621  O4   DU F   2     136.708  -6.190  43.377  0.82 67.99           O  
ANISOU 2621  O4   DU F   2    11880   7147   6807  -1607   3966  -1140       O  
ATOM   2622  C5   DU F   2     138.784  -6.379  44.448  0.82 67.27           C  
ANISOU 2622  C5   DU F   2    11498   7538   6524  -1431   4137   -915       C  
ATOM   2623  C6   DU F   2     139.409  -6.686  45.591  0.82 66.98           C  
ANISOU 2623  C6   DU F   2    11337   7658   6454  -1379   4169   -841       C  
ATOM   2624  P    DA F   3     140.877 -10.791  50.350  0.92 93.53           P  
ANISOU 2624  P    DA F   3    14943  11150   9442   -618   4313   -503       P  
ATOM   2625  OP1  DA F   3     141.175 -11.534  49.103  0.92 94.68           O  
ANISOU 2625  OP1  DA F   3    15198  11192   9582   -493   4317   -523       O  
ATOM   2626  OP2  DA F   3     139.527 -10.875  50.956  0.92 92.22           O  
ANISOU 2626  OP2  DA F   3    14886  10761   9394   -762   4364   -460       O  
ATOM   2627  O5'  DA F   3     141.933 -11.215  51.477  0.92 82.57           O  
ANISOU 2627  O5'  DA F   3    13525   9977   7872   -366   4301   -436       O  
TER    2628       DA F   3                                                      
HETATM 2629  O   HOH A 201     170.611  18.546  66.036  1.00 12.51           O  
HETATM 2630  O   HOH A 202     151.254  15.296  54.435  1.00 32.51           O  
HETATM 2631  O   HOH A 203     170.096  21.108  70.169  1.00 43.29           O  
HETATM 2632  O   HOH A 204     168.282  31.515  72.036  1.00 30.61           O  
HETATM 2633  O   HOH A 205     160.464  24.191  75.212  1.00 22.81           O  
HETATM 2634  O   HOH A 206     172.278   6.097  57.979  1.00  3.61           O  
HETATM 2635  O   HOH A 207     163.688  24.248  73.881  1.00 19.93           O  
HETATM 2636  O   HOH B 201     142.655  22.367  28.255  1.00 15.98           O  
HETATM 2637  O   HOH B 202     141.342  26.571  54.249  1.00 23.03           O  
HETATM 2638  O   HOH B 203     156.551  37.661  46.410  1.00 21.65           O  
HETATM 2639  O   HOH B 204     151.395  40.041  43.945  1.00 44.61           O  
HETATM 2640  O   HOH B 205     153.085  37.783  42.031  1.00 26.74           O  
HETATM 2641  O   HOH B 206     152.689   4.908  40.431  1.00 24.89           O  
HETATM 2642  O   HOH B 207     169.344  27.201  41.719  1.00 23.42           O  
HETATM 2643  O   HOH B 208     137.248  20.694  49.903  1.00 16.39           O  
HETATM 2644  O   HOH B 209     160.871  27.554  29.597  1.00  7.98           O  
HETATM 2645  O   HOH B 210     142.706  25.613  27.899  1.00 18.70           O  
HETATM 2646  O   HOH C 201     127.590   0.579  40.524  1.00  7.61           O  
HETATM 2647  O   HOH C 202     147.098  -7.888  62.151  1.00 16.32           O  
HETATM 2648  O   HOH C 203     117.076  -4.967  50.109  1.00 24.99           O  
HETATM 2649  O   HOH C 204     123.579   3.345  46.093  1.00 30.40           O  
HETATM 2650  O   HOH C 205     130.267  11.835  46.681  1.00 27.53           O  
HETATM 2651  O   HOH C 206     135.239 -13.385  40.123  1.00 20.31           O  
HETATM 2652  O   HOH C 207     136.429 -13.069  42.940  1.00 13.48           O  
HETATM 2653  O   HOH C 208     114.228 -11.109  73.731  1.00 29.85           O  
HETATM 2654  O   HOH C 210     125.301  -1.058  41.243  1.00  6.88           O  
HETATM 2655  O   HOH C 211     140.077 -11.947  58.157  1.00 47.58           O  
HETATM 2656  O   HOH C 212     133.247 -11.440  59.077  1.00 38.51           O  
HETATM 2657  O   HOH C 213     130.784  13.964  46.402  1.00 31.51           O  
HETATM 2658  O   HOH C 214     136.314 -12.261  58.863  1.00 35.19           O  
HETATM 2659  O   HOH D 101     171.514   7.703  55.877  1.00 30.75           O  
MASTER      422    0    0    8   30    0    0    6 2653    6    0   30          
END

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Related entries of code: 5cr2

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	5cr2
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	mRNA Endonuclease MazF
Ligand Name	ssDNA substrate analog AUACAUA
EC.Number	E.C.3.1.27
Resolution	2.9(Å)
Affinity (Kd/Ki/IC50)	Kd=0.52uM
Release Year	2016
Protein/NA Sequence	Check fasta file
Primary Reference	(2016) J.Biol.Chem. Vol. 291: pp. 10950-10960

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): P0AE70
Entrez Gene ID	NCBI Entrez Gene ID: 61731222 947252
ASD	Information of known allosteric effects of PDB entries

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