CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  HYDROLASE/VIRAL PROTEIN 19-MAR-22 7XB0  ***

elNémo ID: 23022000321414153

Job options:

ID        	=	 23022000321414153
JOBID     	=	 HYDROLASE/VIRAL PROTEIN 19-MAR-22 7XB0
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE/VIRAL PROTEIN                 19-MAR-22   7XB0              
TITLE     CRYSTAL STRUCTURE OF OMICRON BA.2 RBD COMPLEXED WITH HACE2            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME 2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACE-RELATED CARBOXYPEPTIDASE,ANGIOTENSIN-CONVERTING ENZYME  
COMPND   5 HOMOLOG;                                                             
COMPND   6 EC: 3.4.17.23,3.4.17.-;                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SPIKE PROTEIN S1;                                          
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: OMICRON BA.2 RBD;                                          
COMPND  12 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACE2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR EGFP-MCS-PCDNA3.1;    
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 2021194;                                    
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  10 2;                                                                   
SOURCE  11 ORGANISM_TAXID: 2697049;                                             
SOURCE  12 GENE: S, 2;                                                          
SOURCE  13 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR EGFP-MCS-PCDNA3.1;    
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 2021194                                     
KEYWDS    SARS-COV-2, OMICRON, RBD, HACE2, COMPLEX STRUCTURE, VIRAL PROTEIN,    
KEYWDS   2 HYDROLASE-VIRAL PROTEIN COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LI,H.LIAO,Y.MENG,W.LI                                               
REVDAT   2   20-JUL-22 7XB0    1       JRNL                                     
REVDAT   1   06-JUL-22 7XB0    0                                                
JRNL        AUTH   L.LI,H.LIAO,Y.MENG,W.LI,P.HAN,K.LIU,Q.WANG,D.LI,Y.ZHANG,     
JRNL        AUTH 2 L.WANG,Z.FAN,Y.ZHANG,Q.WANG,X.ZHAO,Y.SUN,N.HUANG,J.QI,       
JRNL        AUTH 3 G.F.GAO                                                      
JRNL        TITL   STRUCTURAL BASIS OF HUMAN ACE2 HIGHER BINDING AFFINITY TO    
JRNL        TITL 2 CURRENTLY CIRCULATING OMICRON SARS-COV-2 SUB-VARIANTS BA.2   
JRNL        TITL 3 AND BA.1.1.                                                  
JRNL        REF    CELL                                       2022              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   35809570                                                     
JRNL        DOI    10.1016/J.CELL.2022.06.023                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26098                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1302                            
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 19.6600 -  5.9900    0.94     2924   163  0.1991 0.2471        
REMARK   3     2  5.9900 -  4.7700    0.96     2865   136  0.1978 0.2487        
REMARK   3     3  4.7700 -  4.1800    0.96     2817   141  0.1811 0.1800        
REMARK   3     4  4.1800 -  3.8000    0.97     2803   150  0.2045 0.2253        
REMARK   3     5  3.8000 -  3.5300    0.97     2800   153  0.2189 0.2837        
REMARK   3     6  3.5300 -  3.3200    0.97     2789   139  0.2460 0.3095        
REMARK   3     7  3.3200 -  3.1500    0.97     2786   151  0.2557 0.2925        
REMARK   3     8  3.1500 -  3.0200    0.95     2731   129  0.2787 0.3520        
REMARK   3     9  3.0200 -  2.9000    0.81     2281   140  0.2792 0.3076        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.284            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.945           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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           6741                                  
REMARK   3   ANGLE     :  0.535           9163                                  
REMARK   3   CHIRALITY :  0.041            985                                  
REMARK   3   PLANARITY :  0.004           1175                                  
REMARK   3   DIHEDRAL  : 16.315           2448                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2254  15.8636 -24.7481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1412 T22:   0.2413                                     
REMARK   3      T33:   0.2114 T12:   0.0042                                     
REMARK   3      T13:  -0.0049 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2775 L22:   0.6354                                     
REMARK   3      L33:   0.8468 L12:   0.0715                                     
REMARK   3      L13:  -0.1858 L23:   0.1342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0049 S12:  -0.0057 S13:   0.0045                       
REMARK   3      S21:   0.0049 S22:   0.0443 S23:   0.0831                       
REMARK   3      S31:   0.0081 S32:   0.0511 S33:   0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -32.7968  25.0244  20.4809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3204 T22:   0.4533                                     
REMARK   3      T33:   0.3705 T12:   0.0548                                     
REMARK   3      T13:   0.0614 T23:  -0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1457 L22:   0.1659                                     
REMARK   3      L33:   0.2287 L12:  -0.1214                                     
REMARK   3      L13:  -0.1722 L23:  -0.0161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0143 S12:  -0.1207 S13:   0.0001                       
REMARK   3      S21:   0.0849 S22:   0.1293 S23:  -0.0221                       
REMARK   3      S31:  -0.1371 S32:   0.1879 S33:   0.0000                       
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 7XB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAR-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300028448.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-22                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL10U2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 S 16M               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26827                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.3000                            
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) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6LZG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 0.1 M BIS        
REMARK 280  -TRIS, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.42500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       51.63050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       51.63050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.21250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       51.63050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       51.63050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      168.63750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       51.63050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.63050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.21250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       51.63050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.63050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      168.63750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      112.42500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   607     OD1  ASP A   609              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    GLU A  87       37.07    -98.42                                   
REMARK 500    LEU A  91       -8.65     71.47                                   
REMARK 500    ASP A 136       16.53     49.53                                   
REMARK 500    ASN A 137       81.80   -161.84                                   
REMARK 500    PRO A 138        0.42    -67.53                                   
REMARK 500    ASN A 290      143.45     75.35                                   
REMARK 500    ASN A 338     -120.03     44.06                                   
REMARK 500    PRO B 337       56.99    -91.01                                   
REMARK 500    ALA B 352       41.34   -104.45                                   
REMARK 500    PHE B 371      -10.75     71.27                                   
REMARK 500    PRO B 373      108.62    -49.94                                   
REMARK 500    ASN B 422      -50.55   -120.47                                   
REMARK 500    ASP B 428       52.40    -93.47                                   
REMARK 500    ASN B 487        9.87     59.85                                   
REMARK 500    ALA B 522       69.82     60.05                                   
REMARK 500    THR B 523       32.75    -97.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 374   NE2                                                    
REMARK 620 2 HIS A 378   NE2  93.5                                              
REMARK 620 3 GLU A 402   OE2  96.9  98.2                                        
REMARK 620 N                    1     2                                         
DBREF  7XB0 A   19   614  UNP    Q9BYF1   ACE2_HUMAN      19    614             
DBREF  7XB0 B  333   527  UNP    P0DTC2   SPIKE_SARS2    333    527             
SEQADV 7XB0 ASP B  339  UNP  P0DTC2    GLY   339 VARIANT                        
SEQADV 7XB0 PHE B  371  UNP  P0DTC2    SER   371 VARIANT                        
SEQADV 7XB0 PRO B  373  UNP  P0DTC2    SER   373 VARIANT                        
SEQADV 7XB0 PHE B  375  UNP  P0DTC2    SER   375 VARIANT                        
SEQADV 7XB0 ALA B  376  UNP  P0DTC2    THR   376 VARIANT                        
SEQADV 7XB0 ASN B  405  UNP  P0DTC2    ASP   405 VARIANT                        
SEQADV 7XB0 SER B  408  UNP  P0DTC2    ARG   408 VARIANT                        
SEQADV 7XB0 ASN B  417  UNP  P0DTC2    LYS   417 VARIANT                        
SEQADV 7XB0 LYS B  440  UNP  P0DTC2    ASN   440 VARIANT                        
SEQADV 7XB0 ASN B  477  UNP  P0DTC2    SER   477 VARIANT                        
SEQADV 7XB0 LYS B  478  UNP  P0DTC2    THR   478 VARIANT                        
SEQADV 7XB0 ALA B  484  UNP  P0DTC2    GLU   484 VARIANT                        
SEQADV 7XB0 ARG B  493  UNP  P0DTC2    GLN   493 VARIANT                        
SEQADV 7XB0 ARG B  498  UNP  P0DTC2    GLN   498 VARIANT                        
SEQADV 7XB0 TYR B  501  UNP  P0DTC2    ASN   501 VARIANT                        
SEQADV 7XB0 HIS B  505  UNP  P0DTC2    TYR   505 VARIANT                        
SEQRES   1 A  596  SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS          
SEQRES   2 A  596  PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER          
SEQRES   3 A  596  LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU          
SEQRES   4 A  596  ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER          
SEQRES   5 A  596  ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR          
SEQRES   6 A  596  PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN          
SEQRES   7 A  596  LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER          
SEQRES   8 A  596  GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR          
SEQRES   9 A  596  MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO          
SEQRES  10 A  596  ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU          
SEQRES  11 A  596  ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG          
SEQRES  12 A  596  LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS          
SEQRES  13 A  596  GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS          
SEQRES  14 A  596  ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY          
SEQRES  15 A  596  ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP          
SEQRES  16 A  596  GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL          
SEQRES  17 A  596  GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS          
SEQRES  18 A  596  LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR          
SEQRES  19 A  596  PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS          
SEQRES  20 A  596  LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU          
SEQRES  21 A  596  TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE          
SEQRES  22 A  596  ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA          
SEQRES  23 A  596  GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER          
SEQRES  24 A  596  VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN          
SEQRES  25 A  596  SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL          
SEQRES  26 A  596  CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE          
SEQRES  27 A  596  ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE          
SEQRES  28 A  596  LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP          
SEQRES  29 A  596  MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY          
SEQRES  30 A  596  ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET          
SEQRES  31 A  596  SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE          
SEQRES  32 A  596  GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR          
SEQRES  33 A  596  GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL          
SEQRES  34 A  596  GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG          
SEQRES  35 A  596  TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP          
SEQRES  36 A  596  MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY          
SEQRES  37 A  596  VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP          
SEQRES  38 A  596  PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE          
SEQRES  39 A  596  ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE          
SEQRES  40 A  596  GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO          
SEQRES  41 A  596  LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY          
SEQRES  42 A  596  GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU          
SEQRES  43 A  596  PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS          
SEQRES  44 A  596  ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO          
SEQRES  45 A  596  LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE          
SEQRES  46 A  596  VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA                  
SEQRES   1 B  195  THR ASN LEU CYS PRO PHE ASP GLU VAL PHE ASN ALA THR          
SEQRES   2 B  195  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES   3 B  195  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE          
SEQRES   4 B  195  ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES   5 B  195  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES   6 B  195  ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN ILE          
SEQRES   7 B  195  ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR          
SEQRES   8 B  195  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES   9 B  195  ASN SER ASN LYS LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  10 B  195  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  11 B  195  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  12 B  195  GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY PHE ASN CYS          
SEQRES  13 B  195  TYR PHE PRO LEU ARG SER TYR GLY PHE ARG PRO THR TYR          
SEQRES  14 B  195  GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  15 B  195  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET     ZN  A 701       1                                                       
HET    NAG  A 702      14                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM      ZN ZINC ION                                                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
FORMUL   3  NAG    9(C8 H15 N O6)                                               
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   6   ZN    ZN 2+                                                        
HELIX    1 AA1 THR A   20  ASN A   53  1                                  34    
HELIX    2 AA2 THR A   55  MET A   82  1                                  28    
HELIX    3 AA3 PRO A   84  ILE A   88  5                                   5    
HELIX    4 AA4 THR A   92  GLY A  104  1                                  13    
HELIX    5 AA5 SER A  105  LEU A  108  5                                   4    
HELIX    6 AA6 SER A  109  GLY A  130  1                                  22    
HELIX    7 AA7 PRO A  146  SER A  155  1                                  10    
HELIX    8 AA8 ASP A  157  VAL A  172  1                                  16    
HELIX    9 AA9 VAL A  172  ASN A  194  1                                  23    
HELIX   10 AB1 ASP A  198  GLY A  205  1                                   8    
HELIX   11 AB2 ASP A  206  GLU A  208  5                                   3    
HELIX   12 AB3 SER A  218  TYR A  252  1                                  35    
HELIX   13 AB4 HIS A  265  LEU A  267  5                                   3    
HELIX   14 AB5 TRP A  275  ASN A  277  5                                   3    
HELIX   15 AB6 LEU A  278  VAL A  283  1                                   6    
HELIX   16 AB7 VAL A  293  GLN A  300  1                                   8    
HELIX   17 AB8 ASP A  303  SER A  317  1                                  15    
HELIX   18 AB9 THR A  324  SER A  331  1                                   8    
HELIX   19 AC1 THR A  365  TYR A  385  1                                  21    
HELIX   20 AC2 PRO A  389  ARG A  393  5                                   5    
HELIX   21 AC3 GLY A  399  THR A  414  1                                  16    
HELIX   22 AC4 THR A  414  ILE A  421  1                                   8    
HELIX   23 AC5 ASP A  431  LYS A  465  1                                  35    
HELIX   24 AC6 PRO A  469  ASP A  471  5                                   3    
HELIX   25 AC7 GLN A  472  ILE A  484  1                                  13    
HELIX   26 AC8 ASP A  499  SER A  502  5                                   4    
HELIX   27 AC9 LEU A  503  ASN A  508  1                                   6    
HELIX   28 AD1 PHE A  512  ALA A  533  1                                  22    
HELIX   29 AD2 PRO A  538  CYS A  542  5                                   5    
HELIX   30 AD3 SER A  547  ARG A  559  1                                  13    
HELIX   31 AD4 PRO A  565  GLY A  575  1                                  11    
HELIX   32 AD5 VAL A  581  PHE A  588  1                                   8    
HELIX   33 AD6 PHE A  588  ASN A  599  1                                  12    
HELIX   34 AD7 PRO B  337  ASN B  343  1                                   7    
HELIX   35 AD8 ASN B  405  ILE B  410  5                                   6    
HELIX   36 AD9 GLY B  416  ASN B  422  1                                   7    
HELIX   37 AE1 SER B  438  SER B  443  1                                   6    
HELIX   38 AE2 GLY B  502  HIS B  505  5                                   4    
SHEET    1 AA1 2 LYS A 131  CYS A 133  0                                        
SHEET    2 AA1 2 CYS A 141  LEU A 143 -1  O  LEU A 142   N  VAL A 132           
SHEET    1 AA2 2 LEU A 262  PRO A 263  0                                        
SHEET    2 AA2 2 VAL A 487  VAL A 488  1  O  VAL A 488   N  LEU A 262           
SHEET    1 AA3 2 THR A 347  GLY A 352  0                                        
SHEET    2 AA3 2 ASP A 355  LEU A 359 -1  O  ARG A 357   N  TRP A 349           
SHEET    1 AA4 5 LYS B 356  ILE B 358  0                                        
SHEET    2 AA4 5 VAL B 395  ARG B 403 -1  O  VAL B 395   N  ILE B 358           
SHEET    3 AA4 5 PRO B 507  PHE B 515 -1  O  SER B 514   N  TYR B 396           
SHEET    4 AA4 5 GLY B 431  ASN B 437 -1  N  ILE B 434   O  VAL B 511           
SHEET    5 AA4 5 ALA B 376  TYR B 380 -1  N  TYR B 380   O  GLY B 431           
SHEET    1 AA5 2 LEU B 452  ARG B 454  0                                        
SHEET    2 AA5 2 LEU B 492  SER B 494 -1  O  ARG B 493   N  TYR B 453           
SHEET    1 AA6 2 TYR B 473  GLN B 474  0                                        
SHEET    2 AA6 2 CYS B 488  TYR B 489 -1  O  TYR B 489   N  TYR B 473           
SSBOND   1 CYS A  133    CYS A  141                          1555   1555  2.03  
SSBOND   2 CYS A  344    CYS A  361                          1555   1555  2.03  
SSBOND   3 CYS A  530    CYS A  542                          1555   1555  2.03  
SSBOND   4 CYS B  336    CYS B  361                          1555   1555  2.03  
SSBOND   5 CYS B  379    CYS B  432                          1555   1555  2.03  
SSBOND   6 CYS B  391    CYS B  525                          1555   1555  2.03  
SSBOND   7 CYS B  480    CYS B  488                          1555   1555  2.03  
LINK         ND2 ASN A  53                 C1  NAG A 702     1555   1555  1.44  
LINK         ND2 ASN A  90                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN A 322                 C1  NAG A 703     1555   1555  1.45  
LINK         ND2 ASN A 432                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN A 546                 C1  NAG A 704     1555   1555  1.44  
LINK         ND2 ASN B 343                 C1  NAG E   1     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         NE2 HIS A 374                ZN    ZN A 701     1555   1555  2.10  
LINK         NE2 HIS A 378                ZN    ZN A 701     1555   1555  2.10  
LINK         OE2 GLU A 402                ZN    ZN A 701     1555   1555  2.00  
CISPEP   1 GLU A  145    PRO A  146          0         0.35                     
CRYST1  103.261  103.261  224.850  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009684  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009684  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004447        0.00000                         
ATOM      1  N   SER A  19     -32.784  51.640   2.813  1.00 63.91           N  
ANISOU    1  N   SER A  19     9440   7017   7826   -163   1796  -1264       N  
ATOM      2  CA  SER A  19     -32.156  50.418   2.320  1.00 72.67           C  
ANISOU    2  CA  SER A  19    10449   8230   8932   -192   1703  -1246       C  
ATOM      3  C   SER A  19     -31.943  50.488   0.811  1.00 71.45           C  
ANISOU    3  C   SER A  19    10249   8077   8824   -171   1645  -1205       C  
ATOM      4  O   SER A  19     -32.805  50.969   0.078  1.00 58.11           O  
ANISOU    4  O   SER A  19     8555   6324   7199    -87   1672  -1171       O  
ATOM      5  CB  SER A  19     -33.005  49.198   2.679  1.00 69.35           C  
ANISOU    5  CB  SER A  19     9929   7869   8551   -131   1692  -1215       C  
ATOM      6  OG  SER A  19     -33.893  48.868   1.626  1.00 64.68           O  
ANISOU    6  OG  SER A  19     9249   7275   8050    -38   1672  -1158       O  
ATOM      7  N   THR A  20     -30.793  50.002   0.351  1.00 78.85           N  
ANISOU    7  N   THR A  20    11150   9085   9724   -244   1565  -1209       N  
ATOM      8  CA  THR A  20     -30.453  50.093  -1.058  1.00 75.70           C  
ANISOU    8  CA  THR A  20    10717   8688   9357   -238   1512  -1175       C  
ATOM      9  C   THR A  20     -31.206  49.041  -1.867  1.00 73.91           C  
ANISOU    9  C   THR A  20    10367   8510   9204   -154   1460  -1114       C  
ATOM     10  O   THR A  20     -31.882  48.159  -1.329  1.00 76.98           O  
ANISOU   10  O   THR A  20    10692   8940   9616   -112   1460  -1099       O  
ATOM     11  CB  THR A  20     -28.950  49.924  -1.272  1.00 68.43           C  
ANISOU   11  CB  THR A  20     9796   7831   8373   -347   1448  -1203       C  
ATOM     12  OG1 THR A  20     -28.650  50.064  -2.666  1.00 81.25           O  
ANISOU   12  OG1 THR A  20    11394   9450  10027   -341   1406  -1171       O  
ATOM     13  CG2 THR A  20     -28.504  48.550  -0.818  1.00 68.62           C  
ANISOU   13  CG2 THR A  20     9729   7969   8375   -372   1381  -1202       C  
ATOM     14  N   ILE A  21     -31.070  49.145  -3.189  1.00 77.58           N  
ANISOU   14  N   ILE A  21    10804   8970   9703   -136   1417  -1079       N  
ATOM     15  CA  ILE A  21     -31.752  48.232  -4.098  1.00 75.41           C  
ANISOU   15  CA  ILE A  21    10419   8738   9496    -60   1365  -1022       C  
ATOM     16  C   ILE A  21     -31.007  46.906  -4.240  1.00 74.38           C  
ANISOU   16  C   ILE A  21    10198   8718   9347   -105   1281  -1015       C  
ATOM     17  O   ILE A  21     -31.595  45.914  -4.690  1.00 72.65           O  
ANISOU   17  O   ILE A  21     9882   8546   9177    -50   1240   -975       O  
ATOM     18  CB  ILE A  21     -31.956  48.949  -5.446  1.00 79.27           C  
ANISOU   18  CB  ILE A  21    10926   9168  10023    -18   1356   -987       C  
ATOM     19  CG1 ILE A  21     -32.674  48.057  -6.465  1.00 67.91           C  
ANISOU   19  CG1 ILE A  21     9377   7774   8654     58   1297   -928       C  
ATOM     20  CG2 ILE A  21     -30.628  49.462  -5.980  1.00 87.36           C  
ANISOU   20  CG2 ILE A  21    12007  10193  10994   -111   1329  -1010       C  
ATOM     21  CD1 ILE A  21     -34.182  48.098  -6.353  1.00 64.70           C  
ANISOU   21  CD1 ILE A  21     8936   7330   8317    168   1338   -899       C  
ATOM     22  N   GLU A  22     -29.735  46.847  -3.841  1.00 84.78           N  
ANISOU   22  N   GLU A  22    11541  10078  10594   -202   1255  -1055       N  
ATOM     23  CA  GLU A  22     -29.011  45.580  -3.880  1.00 82.99           C  
ANISOU   23  CA  GLU A  22    11230   9956  10347   -238   1178  -1051       C  
ATOM     24  C   GLU A  22     -29.355  44.706  -2.679  1.00 82.28           C  
ANISOU   24  C   GLU A  22    11110   9910  10242   -228   1186  -1060       C  
ATOM     25  O   GLU A  22     -29.657  43.518  -2.835  1.00 78.11           O  
ANISOU   25  O   GLU A  22    10495   9441   9741   -194   1142  -1028       O  
ATOM     26  CB  GLU A  22     -27.502  45.824  -3.942  1.00 84.14           C  
ANISOU   26  CB  GLU A  22    11406  10139  10425   -341   1143  -1090       C  
ATOM     27  CG  GLU A  22     -26.679  44.626  -3.483  1.00 80.20           C  
ANISOU   27  CG  GLU A  22    10840   9746   9887   -384   1079  -1101       C  
ATOM     28  CD  GLU A  22     -25.226  44.707  -3.905  1.00 88.08           C  
ANISOU   28  CD  GLU A  22    11835  10795  10836   -472   1029  -1130       C  
ATOM     29  OE1 GLU A  22     -24.959  45.103  -5.059  1.00 88.15           O  
ANISOU   29  OE1 GLU A  22    11842  10785  10865   -478   1015  -1115       O  
ATOM     30  OE2 GLU A  22     -24.349  44.367  -3.082  1.00 79.98           O1-
ANISOU   30  OE2 GLU A  22    10808   9832   9751   -534   1004  -1167       O1-
ATOM     31  N   GLU A  23     -29.310  45.278  -1.472  1.00 88.46           N  
ANISOU   31  N   GLU A  23    11971  10662  10976   -261   1244  -1103       N  
ATOM     32  CA  GLU A  23     -29.634  44.501  -0.280  1.00 80.35           C  
ANISOU   32  CA  GLU A  23    10929   9672   9927   -255   1257  -1112       C  
ATOM     33  C   GLU A  23     -31.093  44.064  -0.279  1.00 74.88           C  
ANISOU   33  C   GLU A  23    10187   8956   9306   -161   1292  -1073       C  
ATOM     34  O   GLU A  23     -31.431  43.038   0.323  1.00 75.06           O  
ANISOU   34  O   GLU A  23    10162   9027   9329   -145   1283  -1063       O  
ATOM     35  CB  GLU A  23     -29.313  45.301   0.985  1.00 81.63           C  
ANISOU   35  CB  GLU A  23    11194   9800  10021   -311   1315  -1168       C  
ATOM     36  CG  GLU A  23     -27.829  45.313   1.340  1.00 91.64           C  
ANISOU   36  CG  GLU A  23    12489  11124  11205   -414   1268  -1212       C  
ATOM     37  CD  GLU A  23     -27.429  46.500   2.198  1.00100.99           C  
ANISOU   37  CD  GLU A  23    13791  12255  12327   -479   1327  -1270       C  
ATOM     38  OE1 GLU A  23     -28.096  47.553   2.114  1.00 86.61           O  
ANISOU   38  OE1 GLU A  23    12038  10338  10530   -450   1400  -1275       O  
ATOM     39  OE2 GLU A  23     -26.444  46.375   2.958  1.00102.92           O1-
ANISOU   39  OE2 GLU A  23    14059  12551  12494   -558   1299  -1312       O1-
ATOM     40  N   GLN A  24     -31.969  44.826  -0.939  1.00 70.92           N  
ANISOU   40  N   GLN A  24     9696   8383   8866    -97   1333  -1051       N  
ATOM     41  CA  GLN A  24     -33.331  44.354  -1.165  1.00 71.80           C  
ANISOU   41  CA  GLN A  24     9740   8486   9055     -5   1353  -1011       C  
ATOM     42  C   GLN A  24     -33.330  43.080  -1.996  1.00 67.19           C  
ANISOU   42  C   GLN A  24     9045   7977   8506     13   1273   -969       C  
ATOM     43  O   GLN A  24     -34.076  42.136  -1.710  1.00 72.35           O  
ANISOU   43  O   GLN A  24     9634   8665   9192     51   1274   -948       O  
ATOM     44  CB  GLN A  24     -34.156  45.437  -1.861  1.00 69.33           C  
ANISOU   44  CB  GLN A  24     9455   8088   8800     62   1399   -993       C  
ATOM     45  CG  GLN A  24     -34.609  46.568  -0.962  1.00 75.20           C  
ANISOU   45  CG  GLN A  24    10296   8747   9528     74   1496  -1028       C  
ATOM     46  CD  GLN A  24     -35.403  47.618  -1.714  1.00 81.21           C  
ANISOU   46  CD  GLN A  24    11086   9423  10348    150   1537  -1006       C  
ATOM     47  OE1 GLN A  24     -35.915  47.362  -2.804  1.00 69.49           O  
ANISOU   47  OE1 GLN A  24     9531   7947   8925    210   1497   -960       O  
ATOM     48  NE2 GLN A  24     -35.506  48.809  -1.136  1.00 84.87           N  
ANISOU   48  NE2 GLN A  24    11656   9800  10788    149   1616  -1040       N  
ATOM     49  N   ALA A  25     -32.496  43.041  -3.036  1.00 62.17           N  
ANISOU   49  N   ALA A  25     8391   7366   7864    -16   1208   -957       N  
ATOM     50  CA  ALA A  25     -32.407  41.861  -3.886  1.00 60.42           C  
ANISOU   50  CA  ALA A  25     8072   7214   7671     -3   1131   -920       C  
ATOM     51  C   ALA A  25     -31.732  40.697  -3.173  1.00 60.21           C  
ANISOU   51  C   ALA A  25     8014   7266   7598    -49   1091   -932       C  
ATOM     52  O   ALA A  25     -32.090  39.538  -3.411  1.00 59.05           O  
ANISOU   52  O   ALA A  25     7789   7167   7480    -22   1054   -903       O  
ATOM     53  CB  ALA A  25     -31.659  42.208  -5.168  1.00 61.23           C  
ANISOU   53  CB  ALA A  25     8172   7317   7774    -24   1079   -908       C  
ATOM     54  N   LYS A  26     -30.750  40.982  -2.313  1.00 63.16           N  
ANISOU   54  N   LYS A  26     8449   7652   7896   -119   1096   -976       N  
ATOM     55  CA  LYS A  26     -30.164  39.934  -1.483  1.00 57.60           C  
ANISOU   55  CA  LYS A  26     7725   7019   7141   -156   1062   -988       C  
ATOM     56  C   LYS A  26     -31.228  39.288  -0.607  1.00 62.52           C  
ANISOU   56  C   LYS A  26     8332   7640   7784   -112   1104   -976       C  
ATOM     57  O   LYS A  26     -31.294  38.060  -0.485  1.00 60.88           O  
ANISOU   57  O   LYS A  26     8068   7486   7579   -102   1068   -955       O  
ATOM     58  CB  LYS A  26     -29.046  40.514  -0.616  1.00 64.79           C  
ANISOU   58  CB  LYS A  26     8712   7939   7967   -235   1067  -1040       C  
ATOM     59  CG  LYS A  26     -27.666  40.451  -1.234  1.00 62.71           C  
ANISOU   59  CG  LYS A  26     8433   7728   7666   -296    997  -1053       C  
ATOM     60  CD  LYS A  26     -26.656  41.232  -0.411  1.00 65.74           C  
ANISOU   60  CD  LYS A  26     8895   8114   7970   -377   1010  -1110       C  
ATOM     61  CE  LYS A  26     -25.280  41.211  -1.056  1.00 73.86           C  
ANISOU   61  CE  LYS A  26     9900   9199   8966   -440    944  -1127       C  
ATOM     62  NZ  LYS A  26     -24.405  42.296  -0.533  1.00 74.47           N  
ANISOU   62  NZ  LYS A  26    10056   9260   8978   -523    966  -1183       N  
ATOM     63  N   THR A  27     -32.072  40.114   0.012  1.00 60.89           N  
ANISOU   63  N   THR A  27     8177   7367   7590    -86   1186   -990       N  
ATOM     64  CA  THR A  27     -33.170  39.600   0.821  1.00 55.35           C  
ANISOU   64  CA  THR A  27     7461   6658   6912    -44   1239   -980       C  
ATOM     65  C   THR A  27     -34.186  38.854  -0.036  1.00 52.60           C  
ANISOU   65  C   THR A  27     7016   6321   6648     22   1223   -932       C  
ATOM     66  O   THR A  27     -34.736  37.832   0.392  1.00 49.01           O  
ANISOU   66  O   THR A  27     6517   5898   6206     39   1227   -917       O  
ATOM     67  CB  THR A  27     -33.832  40.751   1.577  1.00 56.80           C  
ANISOU   67  CB  THR A  27     7722   6764   7095    -28   1335  -1008       C  
ATOM     68  OG1 THR A  27     -32.836  41.471   2.315  1.00 61.06           O  
ANISOU   68  OG1 THR A  27     8354   7293   7552    -98   1346  -1056       O  
ATOM     69  CG2 THR A  27     -34.880  40.232   2.540  1.00 62.69           C  
ANISOU   69  CG2 THR A  27     8458   7506   7856      6   1397  -1006       C  
ATOM     70  N   PHE A  28     -34.450  39.350  -1.248  1.00 54.52           N  
ANISOU   70  N   PHE A  28     7230   6540   6947     58   1205   -909       N  
ATOM     71  CA  PHE A  28     -35.387  38.670  -2.137  1.00 51.81           C  
ANISOU   71  CA  PHE A  28     6793   6212   6682    119   1182   -865       C  
ATOM     72  C   PHE A  28     -34.884  37.284  -2.518  1.00 52.69           C  
ANISOU   72  C   PHE A  28     6837   6398   6784     97   1106   -844       C  
ATOM     73  O   PHE A  28     -35.652  36.315  -2.517  1.00 50.69           O  
ANISOU   73  O   PHE A  28     6520   6171   6570    126   1103   -820       O  
ATOM     74  CB  PHE A  28     -35.628  39.507  -3.393  1.00 50.37           C  
ANISOU   74  CB  PHE A  28     6600   5990   6549    158   1168   -845       C  
ATOM     75  CG  PHE A  28     -36.342  38.764  -4.485  1.00 51.32           C  
ANISOU   75  CG  PHE A  28     6623   6139   6739    208   1123   -800       C  
ATOM     76  CD1 PHE A  28     -37.663  38.379  -4.329  1.00 55.11           C  
ANISOU   76  CD1 PHE A  28     7042   6616   7280    266   1158   -782       C  
ATOM     77  CD2 PHE A  28     -35.691  38.444  -5.665  1.00 58.77           C  
ANISOU   77  CD2 PHE A  28     7533   7114   7684    194   1046   -780       C  
ATOM     78  CE1 PHE A  28     -38.324  37.694  -5.331  1.00 57.41           C  
ANISOU   78  CE1 PHE A  28     7241   6937   7633    307   1113   -744       C  
ATOM     79  CE2 PHE A  28     -36.346  37.758  -6.670  1.00 57.32           C  
ANISOU   79  CE2 PHE A  28     7264   6956   7560    237   1002   -741       C  
ATOM     80  CZ  PHE A  28     -37.664  37.383  -6.503  1.00 59.24           C  
ANISOU   80  CZ  PHE A  28     7447   7198   7863    292   1034   -724       C  
ATOM     81  N   LEU A  29     -33.597  37.172  -2.854  1.00 61.07           N  
ANISOU   81  N   LEU A  29     7915   7494   7796     44   1045   -854       N  
ATOM     82  CA  LEU A  29     -33.036  35.868  -3.188  1.00 59.21           C  
ANISOU   82  CA  LEU A  29     7623   7328   7548     26    974   -837       C  
ATOM     83  C   LEU A  29     -33.042  34.938  -1.984  1.00 55.76           C  
ANISOU   83  C   LEU A  29     7193   6923   7071      9    987   -845       C  
ATOM     84  O   LEU A  29     -33.221  33.724  -2.137  1.00 55.24           O  
ANISOU   84  O   LEU A  29     7071   6897   7019     20    954   -821       O  
ATOM     85  CB  LEU A  29     -31.617  36.024  -3.733  1.00 62.53           C  
ANISOU   85  CB  LEU A  29     8059   7779   7921    -25    913   -851       C  
ATOM     86  CG  LEU A  29     -31.495  36.657  -5.119  1.00 59.48           C  
ANISOU   86  CG  LEU A  29     7658   7372   7571    -13    885   -835       C  
ATOM     87  CD1 LEU A  29     -30.051  37.017  -5.414  1.00 57.11           C  
ANISOU   87  CD1 LEU A  29     7389   7096   7215    -76    845   -860       C  
ATOM     88  CD2 LEU A  29     -32.043  35.721  -6.180  1.00 48.59           C  
ANISOU   88  CD2 LEU A  29     6193   6019   6248     28    839   -793       C  
ATOM     89  N   ASP A  30     -32.843  35.486  -0.784  1.00 53.67           N  
ANISOU   89  N   ASP A  30     7002   6638   6753    -19   1036   -880       N  
ATOM     90  CA  ASP A  30     -32.945  34.677   0.426  1.00 48.82           C  
ANISOU   90  CA  ASP A  30     6405   6046   6097    -32   1057   -887       C  
ATOM     91  C   ASP A  30     -34.332  34.062   0.547  1.00 53.80           C  
ANISOU   91  C   ASP A  30     6989   6664   6789     17   1102   -861       C  
ATOM     92  O   ASP A  30     -34.473  32.865   0.823  1.00 53.65           O  
ANISOU   92  O   ASP A  30     6940   6682   6764     17   1084   -843       O  
ATOM     93  CB  ASP A  30     -32.624  35.528   1.655  1.00 53.73           C  
ANISOU   93  CB  ASP A  30     7121   6640   6653    -68   1110   -930       C  
ATOM     94  CG  ASP A  30     -31.653  34.847   2.596  1.00 63.45           C  
ANISOU   94  CG  ASP A  30     8388   7923   7799   -116   1075   -948       C  
ATOM     95  OD1 ASP A  30     -31.583  33.601   2.577  1.00 64.01           O  
ANISOU   95  OD1 ASP A  30     8415   8039   7866   -108   1034   -923       O  
ATOM     96  OD2 ASP A  30     -30.963  35.558   3.355  1.00 77.57           O1-
ANISOU   96  OD2 ASP A  30    10249   9705   9521   -161   1088   -987       O1-
ATOM     97  N   LYS A  31     -35.374  34.867   0.331  1.00 59.41           N  
ANISOU   97  N   LYS A  31     7692   7323   7559     60   1160   -858       N  
ATOM     98  CA  LYS A  31     -36.727  34.326   0.322  1.00 63.73           C  
ANISOU   98  CA  LYS A  31     8178   7863   8172    107   1201   -834       C  
ATOM     99  C   LYS A  31     -36.896  33.306  -0.796  1.00 64.26           C  
ANISOU   99  C   LYS A  31     8156   7972   8289    125   1135   -797       C  
ATOM    100  O   LYS A  31     -37.409  32.205  -0.573  1.00 61.80           O  
ANISOU  100  O   LYS A  31     7803   7687   7992    128   1137   -780       O  
ATOM    101  CB  LYS A  31     -37.747  35.454   0.175  1.00 65.31           C  
ANISOU  101  CB  LYS A  31     8380   8004   8431    157   1269   -838       C  
ATOM    102  CG  LYS A  31     -39.185  34.982   0.254  1.00 59.58           C  
ANISOU  102  CG  LYS A  31     7587   7274   7776    205   1318   -820       C  
ATOM    103  CD  LYS A  31     -40.124  35.897  -0.510  1.00 63.88           C  
ANISOU  103  CD  LYS A  31     8094   7778   8398    270   1346   -809       C  
ATOM    104  CE  LYS A  31     -40.132  35.583  -1.998  1.00 73.39           C  
ANISOU  104  CE  LYS A  31     9223   9009   9654    293   1267   -774       C  
ATOM    105  NZ  LYS A  31     -40.810  36.654  -2.782  1.00 74.64           N  
ANISOU  105  NZ  LYS A  31     9363   9123   9873    355   1283   -763       N  
ATOM    106  N   PHE A  32     -36.438  33.648  -2.004  1.00 55.44           N  
ANISOU  106  N   PHE A  32     7014   6859   7192    131   1077   -784       N  
ATOM    107  CA  PHE A  32     -36.639  32.770  -3.152  1.00 51.49           C  
ANISOU  107  CA  PHE A  32     6432   6393   6739    149   1016   -750       C  
ATOM    108  C   PHE A  32     -36.005  31.405  -2.922  1.00 52.44           C  
ANISOU  108  C   PHE A  32     6540   6567   6820    115    968   -742       C  
ATOM    109  O   PHE A  32     -36.644  30.370  -3.140  1.00 56.76           O  
ANISOU  109  O   PHE A  32     7030   7136   7402    129    959   -719       O  
ATOM    110  CB  PHE A  32     -36.072  33.417  -4.417  1.00 46.20           C  
ANISOU  110  CB  PHE A  32     5755   5718   6082    153    962   -741       C  
ATOM    111  CG  PHE A  32     -35.995  32.481  -5.592  1.00 42.31           C  
ANISOU  111  CG  PHE A  32     5190   5266   5619    160    890   -711       C  
ATOM    112  CD1 PHE A  32     -37.105  32.260  -6.390  1.00 44.98           C  
ANISOU  112  CD1 PHE A  32     5458   5601   6031    206    887   -683       C  
ATOM    113  CD2 PHE A  32     -34.815  31.821  -5.897  1.00 40.96           C  
ANISOU  113  CD2 PHE A  32     5023   5138   5403    121    826   -712       C  
ATOM    114  CE1 PHE A  32     -37.041  31.399  -7.469  1.00 44.06           C  
ANISOU  114  CE1 PHE A  32     5281   5521   5938    208    821   -657       C  
ATOM    115  CE2 PHE A  32     -34.747  30.957  -6.972  1.00 40.51           C  
ANISOU  115  CE2 PHE A  32     4906   5115   5371    127    764   -686       C  
ATOM    116  CZ  PHE A  32     -35.859  30.747  -7.760  1.00 43.27           C  
ANISOU  116  CZ  PHE A  32     5192   5458   5791    168    762   -659       C  
ATOM    117  N   ASN A  33     -34.750  31.384  -2.466  1.00 53.93           N  
ANISOU  117  N   ASN A  33     6781   6776   6934     72    938   -762       N  
ATOM    118  CA  ASN A  33     -34.025  30.123  -2.328  1.00 47.02           C  
ANISOU  118  CA  ASN A  33     5895   5952   6018     47    885   -754       C  
ATOM    119  C   ASN A  33     -34.756  29.159  -1.403  1.00 52.75           C  
ANISOU  119  C   ASN A  33     6620   6681   6741     52    925   -745       C  
ATOM    120  O   ASN A  33     -34.991  27.999  -1.758  1.00 55.46           O  
ANISOU  120  O   ASN A  33     6918   7049   7103     58    896   -720       O  
ATOM    121  CB  ASN A  33     -32.609  30.386  -1.815  1.00 45.29           C  
ANISOU  121  CB  ASN A  33     5735   5756   5717      3    854   -781       C  
ATOM    122  CG  ASN A  33     -31.753  31.130  -2.819  1.00 47.22           C  
ANISOU  122  CG  ASN A  33     5975   6005   5961    -11    808   -789       C  
ATOM    123  OD1 ASN A  33     -32.029  31.116  -4.019  1.00 48.42           O  
ANISOU  123  OD1 ASN A  33     6076   6155   6166     12    781   -767       O  
ATOM    124  ND2 ASN A  33     -30.707  31.787  -2.333  1.00 42.49           N  
ANISOU  124  ND2 ASN A  33     5431   5414   5300    -52    800   -821       N  
ATOM    125  N   HIS A  34     -35.135  29.627  -0.212  1.00 53.88           N  
ANISOU  125  N   HIS A  34     6817   6797   6857     46    994   -766       N  
ATOM    126  CA  HIS A  34     -35.833  28.758   0.730  1.00 48.10           C  
ANISOU  126  CA  HIS A  34     6093   6065   6117     45   1040   -759       C  
ATOM    127  C   HIS A  34     -37.181  28.313   0.177  1.00 56.12           C  
ANISOU  127  C   HIS A  34     7033   7071   7218     79   1069   -735       C  
ATOM    128  O   HIS A  34     -37.569  27.149   0.333  1.00 51.83           O  
ANISOU  128  O   HIS A  34     6466   6545   6681     74   1070   -717       O  
ATOM    129  CB  HIS A  34     -35.999  29.470   2.073  1.00 44.45           C  
ANISOU  129  CB  HIS A  34     5708   5572   5610     32   1115   -790       C  
ATOM    130  CG  HIS A  34     -34.703  29.764   2.762  1.00 47.32           C  
ANISOU  130  CG  HIS A  34     6146   5951   5881     -8   1086   -816       C  
ATOM    131  ND1 HIS A  34     -34.363  29.209   3.977  1.00 58.63           N  
ANISOU  131  ND1 HIS A  34     7640   7397   7240    -33   1099   -825       N  
ATOM    132  CD2 HIS A  34     -33.659  30.547   2.402  1.00 43.26           C  
ANISOU  132  CD2 HIS A  34     5654   5445   5336    -28   1042   -835       C  
ATOM    133  CE1 HIS A  34     -33.168  29.642   4.338  1.00 53.32           C  
ANISOU  133  CE1 HIS A  34     7020   6744   6494    -66   1060   -850       C  
ATOM    134  NE2 HIS A  34     -32.720  30.456   3.400  1.00 50.35           N  
ANISOU  134  NE2 HIS A  34     6620   6366   6145    -67   1028   -858       N  
ATOM    135  N   GLU A  35     -37.840  29.224  -0.525  1.00 51.75           N  
ANISOU  135  N   GLU A  35     6442   6492   6728    112   1088   -734       N  
ATOM    136  CA  GLU A  35     -39.151  28.933  -1.136  1.00 52.89           C  
ANISOU  136  CA  GLU A  35     6504   6633   6959    147   1110   -713       C  
ATOM    137  C   GLU A  35     -38.943  27.996  -2.323  1.00 55.53           C  
ANISOU  137  C   GLU A  35     6775   7004   7320    147   1031   -685       C  
ATOM    138  O   GLU A  35     -39.674  27.032  -2.435  1.00 57.75           O  
ANISOU  138  O   GLU A  35     7006   7300   7636    148   1038   -669       O  
ATOM    139  CB  GLU A  35     -39.778  30.243  -1.603  1.00 57.58           C  
ANISOU  139  CB  GLU A  35     7081   7190   7607    189   1142   -719       C  
ATOM    140  CG  GLU A  35     -41.160  30.502  -1.046  1.00 67.43           C  
ANISOU  140  CG  GLU A  35     8301   8412   8908    221   1230   -724       C  
ATOM    141  CD  GLU A  35     -41.465  31.961  -0.776  1.00 74.87           C  
ANISOU  141  CD  GLU A  35     9280   9304   9862    253   1287   -745       C  
ATOM    142  OE1 GLU A  35     -40.623  32.624  -0.189  1.00 74.16           O  
ANISOU  142  OE1 GLU A  35     9275   9194   9709    228   1297   -769       O  
ATOM    143  OE2 GLU A  35     -42.544  32.425  -1.149  1.00 79.93           O1-
ANISOU  143  OE2 GLU A  35     9867   9928  10575    302   1322   -738       O1-
ATOM    144  N   ALA A  36     -37.952  28.277  -3.163  1.00 60.46           N  
ANISOU  144  N   ALA A  36     7405   7641   7927    140    963   -683       N  
ATOM    145  CA  ALA A  36     -37.715  27.491  -4.371  1.00 53.63           C  
ANISOU  145  CA  ALA A  36     6484   6807   7085    141    889   -659       C  
ATOM    146  C   ALA A  36     -37.272  26.073  -4.038  1.00 54.94           C  
ANISOU  146  C   ALA A  36     6656   7005   7213    114    861   -650       C  
ATOM    147  O   ALA A  36     -37.743  25.111  -4.654  1.00 53.39           O  
ANISOU  147  O   ALA A  36     6407   6827   7054    117    838   -629       O  
ATOM    148  CB  ALA A  36     -36.677  28.176  -5.261  1.00 43.21           C  
ANISOU  148  CB  ALA A  36     5178   5492   5747    137    830   -662       C  
ATOM    149  N   GLU A  37     -36.375  25.920  -3.059  1.00 51.95           N  
ANISOU  149  N   GLU A  37     6345   6634   6760     87    863   -665       N  
ATOM    150  CA  GLU A  37     -35.870  24.592  -2.722  1.00 53.16           C  
ANISOU  150  CA  GLU A  37     6514   6814   6871     67    833   -654       C  
ATOM    151  C   GLU A  37     -36.993  23.670  -2.265  1.00 56.95           C  
ANISOU  151  C   GLU A  37     6973   7285   7380     68    882   -640       C  
ATOM    152  O   GLU A  37     -37.039  22.497  -2.656  1.00 56.40           O  
ANISOU  152  O   GLU A  37     6878   7233   7318     62    852   -621       O  
ATOM    153  CB  GLU A  37     -34.791  24.695  -1.644  1.00 46.21           C  
ANISOU  153  CB  GLU A  37     5711   5943   5903     44    830   -674       C  
ATOM    154  CG  GLU A  37     -33.479  25.291  -2.126  1.00 54.36           C  
ANISOU  154  CG  GLU A  37     6758   6997   6898     32    770   -688       C  
ATOM    155  CD  GLU A  37     -32.413  25.294  -1.049  1.00 62.76           C  
ANISOU  155  CD  GLU A  37     7892   8080   7875      7    759   -708       C  
ATOM    156  OE1 GLU A  37     -32.351  24.320  -0.270  1.00 59.65           O  
ANISOU  156  OE1 GLU A  37     7527   7697   7441      3    762   -700       O  
ATOM    157  OE2 GLU A  37     -31.641  26.273  -0.978  1.00 56.91           O1-
ANISOU  157  OE2 GLU A  37     7179   7342   7102     -9    747   -733       O1-
ATOM    158  N   ASP A  38     -37.906  24.179  -1.436  1.00 59.91           N  
ANISOU  158  N   ASP A  38     7360   7633   7771     73    961   -652       N  
ATOM    159  CA  ASP A  38     -39.023  23.362  -0.975  1.00 55.06           C  
ANISOU  159  CA  ASP A  38     6724   7011   7186     68   1016   -642       C  
ATOM    160  C   ASP A  38     -39.953  22.996  -2.127  1.00 52.41           C  
ANISOU  160  C   ASP A  38     6294   6684   6935     83   1001   -624       C  
ATOM    161  O   ASP A  38     -40.358  21.836  -2.266  1.00 57.51           O  
ANISOU  161  O   ASP A  38     6915   7342   7596     68    997   -609       O  
ATOM    162  CB  ASP A  38     -39.790  24.096   0.126  1.00 50.26           C  
ANISOU  162  CB  ASP A  38     6145   6372   6579     72   1109   -662       C  
ATOM    163  CG  ASP A  38     -40.997  23.318   0.613  1.00 60.52           C  
ANISOU  163  CG  ASP A  38     7418   7665   7913     63   1176   -655       C  
ATOM    164  OD1 ASP A  38     -40.807  22.235   1.205  1.00 56.57           O  
ANISOU  164  OD1 ASP A  38     6956   7170   7368     36   1181   -646       O  
ATOM    165  OD2 ASP A  38     -42.134  23.790   0.403  1.00 64.21           O1-
ANISOU  165  OD2 ASP A  38     7825   8122   8451     84   1226   -659       O1-
ATOM    166  N   LEU A  39     -40.302  23.976  -2.965  1.00 45.40           N  
ANISOU  166  N   LEU A  39     5358   5792   6102    113    990   -626       N  
ATOM    167  CA  LEU A  39     -41.204  23.702  -4.081  1.00 50.78           C  
ANISOU  167  CA  LEU A  39     5948   6485   6861    130    970   -609       C  
ATOM    168  C   LEU A  39     -40.522  22.863  -5.155  1.00 48.50           C  
ANISOU  168  C   LEU A  39     5639   6224   6566    118    885   -592       C  
ATOM    169  O   LEU A  39     -41.159  22.001  -5.771  1.00 45.22           O  
ANISOU  169  O   LEU A  39     5166   5824   6192    112    869   -577       O  
ATOM    170  CB  LEU A  39     -41.734  25.011  -4.669  1.00 52.22           C  
ANISOU  170  CB  LEU A  39     6092   6653   7097    171    979   -614       C  
ATOM    171  CG  LEU A  39     -42.801  25.737  -3.845  1.00 60.73           C  
ANISOU  171  CG  LEU A  39     7162   7705   8209    194   1069   -628       C  
ATOM    172  CD1 LEU A  39     -42.426  27.191  -3.608  1.00 58.35           C  
ANISOU  172  CD1 LEU A  39     6909   7371   7890    219   1090   -645       C  
ATOM    173  CD2 LEU A  39     -44.161  25.640  -4.518  1.00 49.33           C  
ANISOU  173  CD2 LEU A  39     5616   6273   6854    221   1083   -618       C  
ATOM    174  N   PHE A  40     -39.230  23.103  -5.400  1.00 54.94           N  
ANISOU  174  N   PHE A  40     6499   7046   7329    113    831   -594       N  
ATOM    175  CA  PHE A  40     -38.500  22.290  -6.369  1.00 50.43           C  
ANISOU  175  CA  PHE A  40     5914   6502   6747    103    754   -580       C  
ATOM    176  C   PHE A  40     -38.391  20.844  -5.901  1.00 48.33           C  
ANISOU  176  C   PHE A  40     5668   6245   6452     78    754   -571       C  
ATOM    177  O   PHE A  40     -38.457  19.915  -6.715  1.00 52.54           O  
ANISOU  177  O   PHE A  40     6167   6793   7004     70    714   -556       O  
ATOM    178  CB  PHE A  40     -37.113  22.883  -6.619  1.00 46.57           C  
ANISOU  178  CB  PHE A  40     5468   6021   6207    102    705   -589       C  
ATOM    179  CG  PHE A  40     -36.276  22.093  -7.582  1.00 46.42           C  
ANISOU  179  CG  PHE A  40     5436   6029   6173     93    632   -577       C  
ATOM    180  CD1 PHE A  40     -36.436  22.249  -8.948  1.00 50.12           C  
ANISOU  180  CD1 PHE A  40     5853   6506   6684    105    587   -566       C  
ATOM    181  CD2 PHE A  40     -35.318  21.204  -7.121  1.00 46.50           C  
ANISOU  181  CD2 PHE A  40     5489   6056   6124     76    607   -578       C  
ATOM    182  CE1 PHE A  40     -35.663  21.528  -9.838  1.00 46.63           C  
ANISOU  182  CE1 PHE A  40     5403   6087   6227     97    524   -558       C  
ATOM    183  CE2 PHE A  40     -34.542  20.479  -8.006  1.00 42.19           C  
ANISOU  183  CE2 PHE A  40     4930   5533   5565     74    543   -568       C  
ATOM    184  CZ  PHE A  40     -34.715  20.642  -9.366  1.00 42.10           C  
ANISOU  184  CZ  PHE A  40     4869   5529   5598     82    504   -560       C  
ATOM    185  N   TYR A  41     -38.210  20.635  -4.594  1.00 42.11           N  
ANISOU  185  N   TYR A  41     4941   5446   5613     64    798   -579       N  
ATOM    186  CA  TYR A  41     -38.176  19.276  -4.063  1.00 40.02           C  
ANISOU  186  CA  TYR A  41     4707   5183   5317     42    805   -568       C  
ATOM    187  C   TYR A  41     -39.511  18.573  -4.273  1.00 47.06           C  
ANISOU  187  C   TYR A  41     5543   6067   6269     31    843   -558       C  
ATOM    188  O   TYR A  41     -39.547  17.386  -4.618  1.00 48.32           O  
ANISOU  188  O   TYR A  41     5697   6232   6430     14    822   -545       O  
ATOM    189  CB  TYR A  41     -37.804  19.298  -2.580  1.00 40.00           C  
ANISOU  189  CB  TYR A  41     4786   5168   5246     31    850   -579       C  
ATOM    190  CG  TYR A  41     -37.402  17.948  -2.028  1.00 40.23           C  
ANISOU  190  CG  TYR A  41     4866   5196   5222     14    842   -565       C  
ATOM    191  CD1 TYR A  41     -38.358  16.992  -1.709  1.00 35.82           C  
ANISOU  191  CD1 TYR A  41     4304   4622   4685     -5    889   -554       C  
ATOM    192  CD2 TYR A  41     -36.066  17.628  -1.827  1.00 39.55           C  
ANISOU  192  CD2 TYR A  41     4834   5128   5066     18    787   -563       C  
ATOM    193  CE1 TYR A  41     -37.995  15.758  -1.209  1.00 36.84           C  
ANISOU  193  CE1 TYR A  41     4490   4744   4763    -19    885   -539       C  
ATOM    194  CE2 TYR A  41     -35.695  16.396  -1.325  1.00 38.36           C  
ANISOU  194  CE2 TYR A  41     4735   4974   4865     11    778   -548       C  
ATOM    195  CZ  TYR A  41     -36.664  15.465  -1.017  1.00 37.85           C  
ANISOU  195  CZ  TYR A  41     4676   4887   4821     -7    828   -535       C  
ATOM    196  OH  TYR A  41     -36.303  14.236  -0.516  1.00 42.15           O  
ANISOU  196  OH  TYR A  41     5282   5421   5313    -13    822   -517       O  
ATOM    197  N   GLN A  42     -40.606  19.291  -4.097  1.00 52.23           N  
ANISOU  197  N   GLN A  42     6157   6712   6978     40    900   -567       N  
ATOM    198  CA  GLN A  42     -41.916  18.647  -4.313  1.00 48.69           C  
ANISOU  198  CA  GLN A  42     5644   6265   6592     26    937   -561       C  
ATOM    199  C   GLN A  42     -42.032  18.285  -5.790  1.00 46.38           C  
ANISOU  199  C   GLN A  42     5282   5994   6346     30    869   -549       C  
ATOM    200  O   GLN A  42     -42.479  17.194  -6.078  1.00 49.17           O  
ANISOU  200  O   GLN A  42     5612   6354   6718      3    865   -540       O  
ATOM    201  CB  GLN A  42     -43.023  19.581  -3.848  1.00 52.52           C  
ANISOU  201  CB  GLN A  42     6091   6739   7126     42   1010   -575       C  
ATOM    202  CG  GLN A  42     -42.748  20.203  -2.498  1.00 48.84           C  
ANISOU  202  CG  GLN A  42     5700   6249   6607     44   1070   -591       C  
ATOM    203  CD  GLN A  42     -44.019  20.812  -1.985  1.00 56.84           C  
ANISOU  203  CD  GLN A  42     6673   7250   7674     55   1156   -605       C  
ATOM    204  OE1 GLN A  42     -45.061  20.184  -2.004  1.00 64.52           O  
ANISOU  204  OE1 GLN A  42     7592   8230   8695     39   1194   -602       O  
ATOM    205  NE2 GLN A  42     -43.945  22.048  -1.538  1.00 47.56           N  
ANISOU  205  NE2 GLN A  42     5522   6057   6492     82   1188   -621       N  
ATOM    206  N   SER A  43     -41.655  19.190  -6.685  1.00 45.25           N  
ANISOU  206  N   SER A  43     5113   5861   6220     58    819   -549       N  
ATOM    207  CA  SER A  43     -41.721  18.874  -8.107  1.00 47.02           C  
ANISOU  207  CA  SER A  43     5278   6105   6482     62    752   -537       C  
ATOM    208  C   SER A  43     -40.811  17.703  -8.456  1.00 49.58           C  
ANISOU  208  C   SER A  43     5639   6438   6762     38    700   -527       C  
ATOM    209  O   SER A  43     -41.200  16.816  -9.226  1.00 49.70           O  
ANISOU  209  O   SER A  43     5616   6464   6804     21    673   -518       O  
ATOM    210  CB  SER A  43     -41.353  20.106  -8.933  1.00 47.28           C  
ANISOU  210  CB  SER A  43     5294   6142   6529     97    710   -537       C  
ATOM    211  OG  SER A  43     -41.322  19.803 -10.316  1.00 49.99           O  
ANISOU  211  OG  SER A  43     5591   6505   6898     99    643   -525       O  
ATOM    212  N   SER A  44     -39.597  17.682  -7.901  1.00 47.52           N  
ANISOU  212  N   SER A  44     5452   6173   6432     39    685   -530       N  
ATOM    213  CA  SER A  44     -38.650  16.622  -8.233  1.00 42.63           C  
ANISOU  213  CA  SER A  44     4867   5561   5769     27    635   -521       C  
ATOM    214  C   SER A  44     -39.093  15.276  -7.670  1.00 45.91           C  
ANISOU  214  C   SER A  44     5307   5964   6175     -2    667   -513       C  
ATOM    215  O   SER A  44     -39.014  14.254  -8.361  1.00 45.56           O  
ANISOU  215  O   SER A  44     5254   5922   6133    -16    633   -503       O  
ATOM    216  CB  SER A  44     -37.256  16.985  -7.722  1.00 39.53           C  
ANISOU  216  CB  SER A  44     4541   5173   5306     38    611   -527       C  
ATOM    217  OG  SER A  44     -36.764  18.147  -8.366  1.00 49.59           O  
ANISOU  217  OG  SER A  44     5797   6458   6587     57    579   -535       O  
ATOM    218  N   LEU A  45     -39.555  15.253  -6.416  1.00 43.81           N  
ANISOU  218  N   LEU A  45     5075   5680   5892    -12    736   -517       N  
ATOM    219  CA  LEU A  45     -39.963  13.990  -5.806  1.00 37.02           C  
ANISOU  219  CA  LEU A  45     4248   4802   5016    -43    773   -509       C  
ATOM    220  C   LEU A  45     -41.201  13.419  -6.486  1.00 40.17           C  
ANISOU  220  C   LEU A  45     4576   5203   5484    -70    789   -507       C  
ATOM    221  O   LEU A  45     -41.300  12.202  -6.684  1.00 43.88           O  
ANISOU  221  O   LEU A  45     5060   5663   5947    -97    784   -498       O  
ATOM    222  CB  LEU A  45     -40.211  14.178  -4.310  1.00 34.39           C  
ANISOU  222  CB  LEU A  45     3972   4448   4648    -51    848   -516       C  
ATOM    223  CG  LEU A  45     -40.374  12.886  -3.501  1.00 30.48           C  
ANISOU  223  CG  LEU A  45     3539   3928   4115    -81    887   -505       C  
ATOM    224  CD1 LEU A  45     -39.415  11.806  -3.990  1.00 36.22           C  
ANISOU  224  CD1 LEU A  45     4307   4654   4801    -79    825   -489       C  
ATOM    225  CD2 LEU A  45     -40.180  13.144  -2.017  1.00 35.13           C  
ANISOU  225  CD2 LEU A  45     4207   4499   4644    -81    943   -509       C  
ATOM    226  N   ALA A  46     -42.160  14.277  -6.840  1.00 44.43           N  
ANISOU  226  N   ALA A  46     5038   5755   6089    -61    809   -516       N  
ATOM    227  CA  ALA A  46     -43.319  13.810  -7.591  1.00 48.76           C  
ANISOU  227  CA  ALA A  46     5505   6315   6705    -85    814   -516       C  
ATOM    228  C   ALA A  46     -42.902  13.271  -8.952  1.00 48.25           C  
ANISOU  228  C   ALA A  46     5417   6267   6650    -88    734   -508       C  
ATOM    229  O   ALA A  46     -43.423  12.247  -9.411  1.00 47.74           O  
ANISOU  229  O   ALA A  46     5330   6203   6607   -124    730   -505       O  
ATOM    230  CB  ALA A  46     -44.338  14.939  -7.743  1.00 50.22           C  
ANISOU  230  CB  ALA A  46     5609   6515   6957    -64    842   -526       C  
ATOM    231  N   SER A  47     -41.964  13.953  -9.615  1.00 57.83           N  
ANISOU  231  N   SER A  47     6636   7490   7844    -54    673   -505       N  
ATOM    232  CA  SER A  47     -41.425  13.447 -10.873  1.00 58.62           C  
ANISOU  232  CA  SER A  47     6725   7604   7943    -56    599   -498       C  
ATOM    233  C   SER A  47     -40.697  12.126 -10.667  1.00 52.78           C  
ANISOU  233  C   SER A  47     6055   6849   7152    -78    588   -491       C  
ATOM    234  O   SER A  47     -40.819  11.207 -11.486  1.00 52.14           O  
ANISOU  234  O   SER A  47     5960   6768   7082   -100    558   -488       O  
ATOM    235  CB  SER A  47     -40.488  14.481 -11.495  1.00 52.69           C  
ANISOU  235  CB  SER A  47     5976   6866   7176    -19    545   -498       C  
ATOM    236  OG  SER A  47     -40.961  15.795 -11.264  1.00 63.82           O  
ANISOU  236  OG  SER A  47     7354   8278   8616      7    571   -504       O  
ATOM    237  N   TRP A  48     -39.928  12.016  -9.581  1.00 49.54           N  
ANISOU  237  N   TRP A  48     5720   6421   6681    -69    611   -489       N  
ATOM    238  CA  TRP A  48     -39.226  10.770  -9.294  1.00 46.98           C  
ANISOU  238  CA  TRP A  48     5468   6078   6304    -80    602   -480       C  
ATOM    239  C   TRP A  48     -40.204   9.624  -9.081  1.00 52.42           C  
ANISOU  239  C   TRP A  48     6160   6746   7013   -124    647   -477       C  
ATOM    240  O   TRP A  48     -39.991   8.514  -9.584  1.00 54.77           O  
ANISOU  240  O   TRP A  48     6481   7030   7298   -142    624   -470       O  
ATOM    241  CB  TRP A  48     -38.333  10.937  -8.064  1.00 49.06           C  
ANISOU  241  CB  TRP A  48     5810   6330   6499    -60    620   -478       C  
ATOM    242  CG  TRP A  48     -37.832   9.632  -7.525  1.00 49.24           C  
ANISOU  242  CG  TRP A  48     5912   6328   6467    -68    625   -465       C  
ATOM    243  CD1 TRP A  48     -38.471   8.804  -6.646  1.00 52.98           C  
ANISOU  243  CD1 TRP A  48     6430   6771   6928    -97    685   -459       C  
ATOM    244  CD2 TRP A  48     -36.587   8.999  -7.840  1.00 46.03           C  
ANISOU  244  CD2 TRP A  48     5554   5925   6012    -44    570   -457       C  
ATOM    245  NE1 TRP A  48     -37.701   7.694  -6.397  1.00 56.58           N  
ANISOU  245  NE1 TRP A  48     6964   7205   7327    -91    669   -445       N  
ATOM    246  CE2 TRP A  48     -36.538   7.792  -7.115  1.00 51.31           C  
ANISOU  246  CE2 TRP A  48     6297   6559   6638    -55    597   -444       C  
ATOM    247  CE3 TRP A  48     -35.509   9.336  -8.663  1.00 44.34           C  
ANISOU  247  CE3 TRP A  48     5326   5738   5785    -14    503   -461       C  
ATOM    248  CZ2 TRP A  48     -35.453   6.922  -7.189  1.00 50.80           C  
ANISOU  248  CZ2 TRP A  48     6294   6488   6522    -30    557   -433       C  
ATOM    249  CZ3 TRP A  48     -34.433   8.471  -8.734  1.00 50.33           C  
ANISOU  249  CZ3 TRP A  48     6137   6492   6493      8    465   -452       C  
ATOM    250  CH2 TRP A  48     -34.412   7.279  -8.001  1.00 48.35           C  
ANISOU  250  CH2 TRP A  48     5959   6207   6202      3    491   -438       C  
ATOM    251  N   ASN A  49     -41.278   9.871  -8.328  1.00 55.99           N  
ANISOU  251  N   ASN A  49     6588   7190   7494   -145    715   -483       N  
ATOM    252  CA  ASN A  49     -42.251   8.819  -8.058  1.00 53.59           C  
ANISOU  252  CA  ASN A  49     6286   6867   7210   -196    767   -483       C  
ATOM    253  C   ASN A  49     -42.930   8.345  -9.335  1.00 55.74           C  
ANISOU  253  C   ASN A  49     6486   7154   7538   -225    734   -487       C  
ATOM    254  O   ASN A  49     -43.249   7.158  -9.461  1.00 61.95           O  
ANISOU  254  O   ASN A  49     7294   7920   8322   -268    747   -485       O  
ATOM    255  CB  ASN A  49     -43.287   9.308  -7.046  1.00 51.87           C  
ANISOU  255  CB  ASN A  49     6047   6644   7018   -212    850   -492       C  
ATOM    256  CG  ASN A  49     -42.705   9.480  -5.655  1.00 48.16           C  
ANISOU  256  CG  ASN A  49     5666   6150   6481   -197    893   -487       C  
ATOM    257  OD1 ASN A  49     -41.698   8.860  -5.311  1.00 47.31           O  
ANISOU  257  OD1 ASN A  49     5644   6025   6308   -186    870   -475       O  
ATOM    258  ND2 ASN A  49     -43.336  10.325  -4.849  1.00 51.02           N  
ANISOU  258  ND2 ASN A  49     6010   6516   6861   -194    954   -498       N  
ATOM    259  N   TYR A  50     -43.164   9.251 -10.287  1.00 48.58           N  
ANISOU  259  N   TYR A  50     5498   6282   6679   -204    691   -493       N  
ATOM    260  CA  TYR A  50     -43.709   8.836 -11.575  1.00 58.24           C  
ANISOU  260  CA  TYR A  50     6656   7525   7948   -229    648   -498       C  
ATOM    261  C   TYR A  50     -42.713   7.974 -12.339  1.00 60.37           C  
ANISOU  261  C   TYR A  50     6977   7782   8177   -229    589   -490       C  
ATOM    262  O   TYR A  50     -43.071   6.920 -12.876  1.00 66.83           O  
ANISOU  262  O   TYR A  50     7796   8591   9004   -271    582   -493       O  
ATOM    263  CB  TYR A  50     -44.104  10.057 -12.407  1.00 58.81           C  
ANISOU  263  CB  TYR A  50     6639   7634   8072   -198    611   -502       C  
ATOM    264  CG  TYR A  50     -44.446   9.711 -13.840  1.00 64.51           C  
ANISOU  264  CG  TYR A  50     7303   8380   8830   -216    550   -505       C  
ATOM    265  CD1 TYR A  50     -45.722   9.293 -14.182  1.00 71.09           C  
ANISOU  265  CD1 TYR A  50     8062   9231   9719   -259    566   -515       C  
ATOM    266  CD2 TYR A  50     -43.491   9.798 -14.849  1.00 58.55           C  
ANISOU  266  CD2 TYR A  50     6565   7631   8049   -192    477   -499       C  
ATOM    267  CE1 TYR A  50     -46.041   8.968 -15.483  1.00 75.35           C  
ANISOU  267  CE1 TYR A  50     8550   9793  10285   -278    507   -519       C  
ATOM    268  CE2 TYR A  50     -43.804   9.474 -16.157  1.00 64.01           C  
ANISOU  268  CE2 TYR A  50     7211   8344   8767   -210    422   -502       C  
ATOM    269  CZ  TYR A  50     -45.084   9.062 -16.467  1.00 70.11           C  
ANISOU  269  CZ  TYR A  50     7912   9133   9592   -253    435   -512       C  
ATOM    270  OH  TYR A  50     -45.416   8.738 -17.762  1.00 78.63           O  
ANISOU  270  OH  TYR A  50     8947  10236  10694   -274    377   -516       O  
ATOM    271  N   ASN A  51     -41.454   8.412 -12.401  1.00 53.34           N  
ANISOU  271  N   ASN A  51     6132   6894   7242   -184    548   -483       N  
ATOM    272  CA  ASN A  51     -40.443   7.703 -13.174  1.00 47.49           C  
ANISOU  272  CA  ASN A  51     5434   6146   6464   -176    492   -478       C  
ATOM    273  C   ASN A  51     -40.038   6.377 -12.544  1.00 53.59           C  
ANISOU  273  C   ASN A  51     6294   6879   7188   -193    517   -471       C  
ATOM    274  O   ASN A  51     -39.350   5.585 -13.198  1.00 58.93           O  
ANISOU  274  O   ASN A  51     7007   7545   7838   -190    478   -468       O  
ATOM    275  CB  ASN A  51     -39.214   8.594 -13.360  1.00 49.54           C  
ANISOU  275  CB  ASN A  51     5710   6423   6690   -124    446   -476       C  
ATOM    276  CG  ASN A  51     -39.451   9.722 -14.347  1.00 44.47           C  
ANISOU  276  CG  ASN A  51     4993   5813   6090   -107    407   -481       C  
ATOM    277  OD1 ASN A  51     -38.839   9.766 -15.413  1.00 42.00           O  
ANISOU  277  OD1 ASN A  51     4674   5514   5771    -96    350   -481       O  
ATOM    278  ND2 ASN A  51     -40.337  10.645 -13.991  1.00 53.47           N  
ANISOU  278  ND2 ASN A  51     6082   6964   7271   -104    439   -485       N  
ATOM    279  N   THR A  52     -40.441   6.118 -11.298  1.00 54.99           N  
ANISOU  279  N   THR A  52     6511   7033   7350   -209    582   -467       N  
ATOM    280  CA  THR A  52     -40.230   4.827 -10.661  1.00 54.44           C  
ANISOU  280  CA  THR A  52     6530   6920   7236   -229    614   -458       C  
ATOM    281  C   THR A  52     -41.516   4.041 -10.457  1.00 60.06           C  
ANISOU  281  C   THR A  52     7229   7610   7982   -294    673   -463       C  
ATOM    282  O   THR A  52     -41.456   2.815 -10.316  1.00 66.84           O  
ANISOU  282  O   THR A  52     8156   8429   8812   -322    691   -457       O  
ATOM    283  CB  THR A  52     -39.541   5.004  -9.299  1.00 58.01           C  
ANISOU  283  CB  THR A  52     7059   7355   7628   -197    644   -447       C  
ATOM    284  OG1 THR A  52     -40.396   5.749  -8.421  1.00 67.64           O  
ANISOU  284  OG1 THR A  52     8249   8580   8869   -211    704   -453       O  
ATOM    285  CG2 THR A  52     -38.222   5.743  -9.461  1.00 48.23           C  
ANISOU  285  CG2 THR A  52     5831   6142   6353   -139    586   -444       C  
ATOM    286  N   ASN A  53     -42.667   4.712 -10.439  1.00 66.21           N  
ANISOU  286  N   ASN A  53     7924   8414   8820   -319    705   -476       N  
ATOM    287  CA  ASN A  53     -43.971   4.069 -10.268  1.00 74.29           C  
ANISOU  287  CA  ASN A  53     8917   9427   9884   -386    764   -486       C  
ATOM    288  C   ASN A  53     -44.933   4.771 -11.221  1.00 73.48           C  
ANISOU  288  C   ASN A  53     8690   9372   9858   -399    740   -502       C  
ATOM    289  O   ASN A  53     -45.380   5.888 -10.946  1.00 78.94           O  
ANISOU  289  O   ASN A  53     9318  10092  10582   -375    756   -507       O  
ATOM    290  CB  ASN A  53     -44.443   4.161  -8.821  1.00 78.39           C  
ANISOU  290  CB  ASN A  53     9472   9925  10388   -399    849   -484       C  
ATOM    291  CG  ASN A  53     -45.692   3.341  -8.551  1.00 85.33           C  
ANISOU  291  CG  ASN A  53    10333  10788  11300   -475    919   -495       C  
ATOM    292  OD1 ASN A  53     -46.167   2.600  -9.412  1.00 84.43           O  
ANISOU  292  OD1 ASN A  53    10189  10675  11216   -522    902   -504       O  
ATOM    293  ND2 ASN A  53     -46.226   3.470  -7.340  1.00 89.63           N  
ANISOU  293  ND2 ASN A  53    10900  11317  11838   -493   1001   -496       N  
ATOM    294  N   ILE A  54     -45.245   4.120 -12.340  1.00 80.43           N  
ANISOU  294  N   ILE A  54     9536  10260  10763   -434    701   -510       N  
ATOM    295  CA  ILE A  54     -46.036   4.734 -13.401  1.00 85.12           C  
ANISOU  295  CA  ILE A  54    10015  10904  11423   -442    661   -523       C  
ATOM    296  C   ILE A  54     -47.502   4.400 -13.141  1.00 88.48           C  
ANISOU  296  C   ILE A  54    10374  11341  11904   -506    720   -540       C  
ATOM    297  O   ILE A  54     -47.978   3.314 -13.473  1.00 91.18           O  
ANISOU  297  O   ILE A  54    10722  11669  12252   -571    730   -550       O  
ATOM    298  CB  ILE A  54     -45.582   4.274 -14.787  1.00 81.05           C  
ANISOU  298  CB  ILE A  54     9498  10396  10902   -446    583   -525       C  
ATOM    299  CG1 ILE A  54     -44.171   4.791 -15.079  1.00 75.53           C  
ANISOU  299  CG1 ILE A  54     8847   9695  10156   -379    527   -511       C  
ATOM    300  CG2 ILE A  54     -46.548   4.766 -15.857  1.00 83.22           C  
ANISOU  300  CG2 ILE A  54     9656  10722  11242   -462    543   -538       C  
ATOM    301  CD1 ILE A  54     -43.748   4.655 -16.527  1.00 69.09           C  
ANISOU  301  CD1 ILE A  54     8014   8895   9340   -374    449   -514       C  
ATOM    302  N   THR A  55     -48.213   5.339 -12.518  1.00 72.12           N  
ANISOU  302  N   THR A  55     8238   9293   9870   -491    762   -545       N  
ATOM    303  CA  THR A  55     -49.658   5.278 -12.353  1.00 75.65           C  
ANISOU  303  CA  THR A  55     8595   9767  10382   -542    815   -564       C  
ATOM    304  C   THR A  55     -50.240   6.631 -12.730  1.00 78.62           C  
ANISOU  304  C   THR A  55     8859  10197  10818   -495    792   -569       C  
ATOM    305  O   THR A  55     -49.567   7.658 -12.619  1.00 73.72           O  
ANISOU  305  O   THR A  55     8252   9578  10181   -427    768   -558       O  
ATOM    306  CB  THR A  55     -50.078   4.932 -10.913  1.00 81.95           C  
ANISOU  306  CB  THR A  55     9439  10533  11166   -574    918   -566       C  
ATOM    307  OG1 THR A  55     -50.203   6.139 -10.149  1.00 84.78           O  
ANISOU  307  OG1 THR A  55     9769  10905  11537   -523    953   -565       O  
ATOM    308  CG2 THR A  55     -49.061   4.020 -10.244  1.00 81.97           C  
ANISOU  308  CG2 THR A  55     9585  10474  11087   -580    937   -550       C  
ATOM    309  N   GLU A  56     -51.504   6.627 -13.166  1.00104.25           N  
ANISOU  309  N   GLU A  56    11992  13485  14132   -533    799   -588       N  
ATOM    310  CA  GLU A  56     -52.139   7.876 -13.581  1.00104.28           C  
ANISOU  310  CA  GLU A  56    11885  13541  14197   -483    774   -592       C  
ATOM    311  C   GLU A  56     -52.199   8.883 -12.439  1.00 98.10           C  
ANISOU  311  C   GLU A  56    11106  12750  13417   -434    839   -589       C  
ATOM    312  O   GLU A  56     -52.177  10.095 -12.682  1.00101.96           O  
ANISOU  312  O   GLU A  56    11549  13261  13929   -368    811   -583       O  
ATOM    313  CB  GLU A  56     -53.539   7.604 -14.136  1.00102.55           C  
ANISOU  313  CB  GLU A  56    11541  13373  14051   -534    776   -614       C  
ATOM    314  CG  GLU A  56     -54.210   8.820 -14.773  1.00110.40           C  
ANISOU  314  CG  GLU A  56    12412  14425  15108   -477    734   -616       C  
ATOM    315  CD  GLU A  56     -53.531   9.278 -16.055  1.00114.67           C  
ANISOU  315  CD  GLU A  56    12954  14981  15634   -430    626   -601       C  
ATOM    316  OE1 GLU A  56     -52.739   8.502 -16.630  1.00105.65           O  
ANISOU  316  OE1 GLU A  56    11883  13814  14444   -456    581   -596       O  
ATOM    317  OE2 GLU A  56     -53.792  10.421 -16.488  1.00113.33           O1-
ANISOU  317  OE2 GLU A  56    12715  14844  15500   -366    590   -595       O1-
ATOM    318  N   GLU A  57     -52.273   8.409 -11.193  1.00 75.96           N  
ANISOU  318  N   GLU A  57     8364   9911  10588   -466    928   -592       N  
ATOM    319  CA  GLU A  57     -52.163   9.325 -10.062  1.00 78.50           C  
ANISOU  319  CA  GLU A  57     8711  10217  10898   -421    989   -589       C  
ATOM    320  C   GLU A  57     -50.779   9.957 -10.003  1.00 78.82           C  
ANISOU  320  C   GLU A  57     8839  10231  10877   -356    943   -570       C  
ATOM    321  O   GLU A  57     -50.649  11.159  -9.742  1.00 75.61           O  
ANISOU  321  O   GLU A  57     8419   9832  10479   -297    947   -567       O  
ATOM    322  CB  GLU A  57     -52.476   8.600  -8.751  1.00 75.02           C  
ANISOU  322  CB  GLU A  57     8330   9740  10432   -473   1092   -596       C  
ATOM    323  CG  GLU A  57     -51.589   9.032  -7.586  1.00 90.27           C  
ANISOU  323  CG  GLU A  57    10370  11630  12297   -435   1132   -583       C  
ATOM    324  CD  GLU A  57     -51.686   8.106  -6.397  1.00 99.00           C  
ANISOU  324  CD  GLU A  57    11563  12693  13360   -490   1220   -584       C  
ATOM    325  OE1 GLU A  57     -51.796   6.884  -6.611  1.00 94.96           O  
ANISOU  325  OE1 GLU A  57    11081  12164  12836   -552   1223   -584       O  
ATOM    326  OE2 GLU A  57     -51.643   8.598  -5.250  1.00 94.79           O1-
ANISOU  326  OE2 GLU A  57    11074  12140  12801   -472   1287   -585       O1-
ATOM    327  N   ASN A  58     -49.732   9.164 -10.251  1.00 68.76           N  
ANISOU  327  N   ASN A  58     7657   8928   9542   -368    901   -557       N  
ATOM    328  CA  ASN A  58     -48.376   9.697 -10.190  1.00 57.36           C  
ANISOU  328  CA  ASN A  58     6291   7464   8038   -312    858   -541       C  
ATOM    329  C   ASN A  58     -48.117  10.703 -11.304  1.00 61.76           C  
ANISOU  329  C   ASN A  58     6790   8053   8621   -260    779   -537       C  
ATOM    330  O   ASN A  58     -47.328  11.637 -11.116  1.00 57.25           O  
ANISOU  330  O   ASN A  58     6254   7476   8023   -207    761   -529       O  
ATOM    331  CB  ASN A  58     -47.358   8.559 -10.237  1.00 55.12           C  
ANISOU  331  CB  ASN A  58     6110   7146   7688   -334    831   -529       C  
ATOM    332  CG  ASN A  58     -47.010   8.036  -8.856  1.00 65.99           C  
ANISOU  332  CG  ASN A  58     7587   8479   9007   -349    901   -524       C  
ATOM    333  OD1 ASN A  58     -47.320   8.668  -7.845  1.00 64.73           O  
ANISOU  333  OD1 ASN A  58     7432   8315   8848   -336    963   -528       O  
ATOM    334  ND2 ASN A  58     -46.363   6.879  -8.805  1.00 64.52           N  
ANISOU  334  ND2 ASN A  58     7487   8259   8768   -373    891   -514       N  
ATOM    335  N   VAL A  59     -48.756  10.534 -12.466  1.00 78.45           N  
ANISOU  335  N   VAL A  59     8821  10201  10784   -276    730   -542       N  
ATOM    336  CA  VAL A  59     -48.726  11.588 -13.477  1.00 71.93           C  
ANISOU  336  CA  VAL A  59     7935   9408   9989   -224    663   -537       C  
ATOM    337  C   VAL A  59     -49.420  12.834 -12.947  1.00 77.41           C  
ANISOU  337  C   VAL A  59     8570  10116  10727   -180    705   -542       C  
ATOM    338  O   VAL A  59     -48.890  13.948 -13.032  1.00 76.92           O  
ANISOU  338  O   VAL A  59     8521  10051  10655   -122    682   -534       O  
ATOM    339  CB  VAL A  59     -49.379  11.117 -14.790  1.00 78.67           C  
ANISOU  339  CB  VAL A  59     8710  10297  10884   -253    603   -542       C  
ATOM    340  CG1 VAL A  59     -48.746  11.827 -15.978  1.00 77.74           C  
ANISOU  340  CG1 VAL A  59     8584  10195  10759   -206    514   -530       C  
ATOM    341  CG2 VAL A  59     -49.288   9.617 -14.947  1.00 83.06           C  
ANISOU  341  CG2 VAL A  59     9308  10836  11415   -323    603   -548       C  
ATOM    342  N   GLN A  60     -50.617  12.657 -12.382  1.00 91.65           N  
ANISOU  342  N   GLN A  60    10310  11934  12580   -209    771   -556       N  
ATOM    343  CA  GLN A  60     -51.373  13.793 -11.870  1.00 91.91           C  
ANISOU  343  CA  GLN A  60    10280  11981  12659   -164    818   -563       C  
ATOM    344  C   GLN A  60     -50.603  14.510 -10.770  1.00 87.46           C  
ANISOU  344  C   GLN A  60     9804  11379  12047   -127    865   -559       C  
ATOM    345  O   GLN A  60     -50.538  15.744 -10.753  1.00 87.29           O  
ANISOU  345  O   GLN A  60     9768  11358  12039    -67    862   -557       O  
ATOM    346  CB  GLN A  60     -52.736  13.327 -11.357  1.00 98.11           C  
ANISOU  346  CB  GLN A  60    10987  12789  13502   -210    891   -583       C  
ATOM    347  CG  GLN A  60     -53.729  12.968 -12.453  1.00 97.44           C  
ANISOU  347  CG  GLN A  60    10785  12756  13480   -236    846   -592       C  
ATOM    348  CD  GLN A  60     -54.593  14.142 -12.867  1.00120.15           C  
ANISOU  348  CD  GLN A  60    13548  15675  16426   -175    832   -595       C  
ATOM    349  OE1 GLN A  60     -54.970  14.973 -12.041  1.00122.28           O  
ANISOU  349  OE1 GLN A  60    13801  15940  16718   -135    896   -600       O  
ATOM    350  NE2 GLN A  60     -54.912  14.216 -14.154  1.00122.84           N  
ANISOU  350  NE2 GLN A  60    13815  16058  16801   -164    747   -591       N  
ATOM    351  N   ASN A  61     -50.004  13.752  -9.849  1.00 67.35           N  
ANISOU  351  N   ASN A  61     7352   8796   9441   -163    907   -558       N  
ATOM    352  CA  ASN A  61     -49.204  14.364  -8.792  1.00 65.24           C  
ANISOU  352  CA  ASN A  61     7174   8495   9119   -133    945   -556       C  
ATOM    353  C   ASN A  61     -47.988  15.084  -9.362  1.00 62.37           C  
ANISOU  353  C   ASN A  61     6857   8124   8716    -85    872   -543       C  
ATOM    354  O   ASN A  61     -47.655  16.193  -8.929  1.00 59.95           O  
ANISOU  354  O   ASN A  61     6574   7807   8398    -40    887   -545       O  
ATOM    355  CB  ASN A  61     -48.772  13.303  -7.781  1.00 62.77           C  
ANISOU  355  CB  ASN A  61     6958   8148   8745   -180    994   -554       C  
ATOM    356  CG  ASN A  61     -49.838  13.020  -6.740  1.00 66.29           C  
ANISOU  356  CG  ASN A  61     7384   8588   9215   -216   1096   -569       C  
ATOM    357  OD1 ASN A  61     -50.359  11.908  -6.655  1.00 73.76           O  
ANISOU  357  OD1 ASN A  61     8326   9532  10169   -276   1125   -572       O  
ATOM    358  ND2 ASN A  61     -50.167  14.028  -5.939  1.00 66.54           N  
ANISOU  358  ND2 ASN A  61     7408   8615   9258   -183   1155   -578       N  
ATOM    359  N   MET A  62     -47.307  14.465 -10.331  1.00 69.49           N  
ANISOU  359  N   MET A  62     7775   9032   9595    -97    796   -533       N  
ATOM    360  CA  MET A  62     -46.112  15.074 -10.908  1.00 64.90           C  
ANISOU  360  CA  MET A  62     7237   8446   8974    -58    729   -523       C  
ATOM    361  C   MET A  62     -46.447  16.380 -11.617  1.00 65.56           C  
ANISOU  361  C   MET A  62     7258   8549   9104     -7    700   -522       C  
ATOM    362  O   MET A  62     -45.747  17.386 -11.454  1.00 67.15           O  
ANISOU  362  O   MET A  62     7498   8736   9278     32    692   -520       O  
ATOM    363  CB  MET A  62     -45.436  14.090 -11.865  1.00 64.38           C  
ANISOU  363  CB  MET A  62     7195   8385   8883    -82    660   -514       C  
ATOM    364  CG  MET A  62     -44.473  14.725 -12.858  1.00 62.13           C  
ANISOU  364  CG  MET A  62     6921   8107   8577    -46    583   -506       C  
ATOM    365  SD  MET A  62     -43.757  13.505 -13.977  1.00 68.84           S  
ANISOU  365  SD  MET A  62     7796   8961   9398    -76    511   -499       S  
ATOM    366  CE  MET A  62     -42.277  14.354 -14.522  1.00 65.73           C  
ANISOU  366  CE  MET A  62     7451   8567   8956    -33    451   -492       C  
ATOM    367  N   ASN A  63     -47.521  16.384 -12.409  1.00 73.27           N  
ANISOU  367  N   ASN A  63     8138   9556  10145     -8    682   -523       N  
ATOM    368  CA  ASN A  63     -47.937  17.616 -13.072  1.00 66.35           C  
ANISOU  368  CA  ASN A  63     7202   8696   9314     47    654   -519       C  
ATOM    369  C   ASN A  63     -48.467  18.632 -12.068  1.00 74.27           C  
ANISOU  369  C   ASN A  63     8195   9686  10340     84    728   -528       C  
ATOM    370  O   ASN A  63     -48.245  19.838 -12.226  1.00 73.54           O  
ANISOU  370  O   ASN A  63     8109   9584  10250    137    717   -524       O  
ATOM    371  CB  ASN A  63     -48.987  17.315 -14.142  1.00 74.53           C  
ANISOU  371  CB  ASN A  63     8133   9772  10411     39    612   -518       C  
ATOM    372  CG  ASN A  63     -48.430  16.495 -15.293  1.00 79.41           C  
ANISOU  372  CG  ASN A  63     8764  10403  11006     10    532   -510       C  
ATOM    373  OD1 ASN A  63     -48.697  15.299 -15.406  1.00 73.06           O  
ANISOU  373  OD1 ASN A  63     7950   9606  10202    -46    532   -516       O  
ATOM    374  ND2 ASN A  63     -47.649  17.138 -16.152  1.00 71.34           N  
ANISOU  374  ND2 ASN A  63     7767   9377   9960     45    468   -497       N  
ATOM    375  N   ASN A  64     -49.170  18.166 -11.030  1.00 86.11           N  
ANISOU  375  N   ASN A  64     9683  11181  11853     54    808   -541       N  
ATOM    376  CA  ASN A  64     -49.693  19.084 -10.022  1.00 85.74           C  
ANISOU  376  CA  ASN A  64     9631  11121  11826     87    887   -552       C  
ATOM    377  C   ASN A  64     -48.567  19.825  -9.314  1.00 88.51           C  
ANISOU  377  C   ASN A  64    10085  11432  12112    111    901   -552       C  
ATOM    378  O   ASN A  64     -48.652  21.040  -9.100  1.00 90.64           O  
ANISOU  378  O   ASN A  64    10356  11689  12395    160    922   -556       O  
ATOM    379  CB  ASN A  64     -50.552  18.325  -9.009  1.00 85.10           C  
ANISOU  379  CB  ASN A  64     9531  11041  11762     41    974   -568       C  
ATOM    380  CG  ASN A  64     -51.956  18.060  -9.517  1.00 92.15           C  
ANISOU  380  CG  ASN A  64    10299  11978  12738     31    982   -576       C  
ATOM    381  OD1 ASN A  64     -52.518  18.856 -10.270  1.00 94.16           O  
ANISOU  381  OD1 ASN A  64    10472  12257  13046     80    948   -573       O  
ATOM    382  ND2 ASN A  64     -52.529  16.933  -9.112  1.00 90.63           N  
ANISOU  382  ND2 ASN A  64    10088  11793  12554    -34   1026   -586       N  
ATOM    383  N   ALA A  65     -47.500  19.113  -8.948  1.00 71.95           N  
ANISOU  383  N   ALA A  65     8076   9318   9944     76    888   -548       N  
ATOM    384  CA  ALA A  65     -46.338  19.772  -8.364  1.00 68.42           C  
ANISOU  384  CA  ALA A  65     7723   8842   9432     94    889   -550       C  
ATOM    385  C   ALA A  65     -45.509  20.493  -9.418  1.00 63.17           C  
ANISOU  385  C   ALA A  65     7067   8180   8755    127    810   -539       C  
ATOM    386  O   ALA A  65     -44.887  21.518  -9.115  1.00 69.08           O  
ANISOU  386  O   ALA A  65     7865   8908   9476    156    816   -544       O  
ATOM    387  CB  ALA A  65     -45.474  18.756  -7.616  1.00 58.31           C  
ANISOU  387  CB  ALA A  65     6530   7547   8080     52    898   -549       C  
ATOM    388  N   GLY A  66     -45.477  19.972 -10.646  1.00 50.83           N  
ANISOU  388  N   GLY A  66     5463   6640   7210    119    739   -527       N  
ATOM    389  CA  GLY A  66     -44.784  20.669 -11.716  1.00 52.51           C  
ANISOU  389  CA  GLY A  66     5681   6855   7413    149    668   -517       C  
ATOM    390  C   GLY A  66     -45.469  21.965 -12.106  1.00 64.22           C  
ANISOU  390  C   GLY A  66     7116   8337   8947    203    671   -515       C  
ATOM    391  O   GLY A  66     -44.807  22.964 -12.398  1.00 63.44           O  
ANISOU  391  O   GLY A  66     7055   8221   8827    234    649   -512       O  
ATOM    392  N   ASP A  67     -46.805  21.963 -12.130  1.00 80.01           N  
ANISOU  392  N   ASP A  67     9031  10354  11014    215    700   -517       N  
ATOM    393  CA  ASP A  67     -47.541  23.190 -12.417  1.00 77.72           C  
ANISOU  393  CA  ASP A  67     8693  10063  10775    276    709   -515       C  
ATOM    394  C   ASP A  67     -47.294  24.242 -11.345  1.00 79.09           C  
ANISOU  394  C   ASP A  67     8926  10197  10927    304    776   -527       C  
ATOM    395  O   ASP A  67     -47.073  25.418 -11.658  1.00 80.34           O  
ANISOU  395  O   ASP A  67     9104  10334  11087    351    764   -522       O  
ATOM    396  CB  ASP A  67     -49.034  22.891 -12.539  1.00 79.25           C  
ANISOU  396  CB  ASP A  67     8777  10290  11046    282    732   -518       C  
ATOM    397  CG  ASP A  67     -49.385  22.184 -13.832  1.00 83.75           C  
ANISOU  397  CG  ASP A  67     9278  10899  11643    266    654   -506       C  
ATOM    398  OD1 ASP A  67     -48.504  22.073 -14.711  1.00 75.70           O  
ANISOU  398  OD1 ASP A  67     8298   9879  10587    260    583   -494       O  
ATOM    399  OD2 ASP A  67     -50.543  21.736 -13.968  1.00 80.32           O1-
ANISOU  399  OD2 ASP A  67     8751  10500  11267    257    665   -512       O1-
ATOM    400  N   LYS A  68     -47.323  23.838 -10.071  1.00 67.95           N  
ANISOU  400  N   LYS A  68     7550   8773   9494    274    848   -542       N  
ATOM    401  CA  LYS A  68     -47.047  24.769  -8.984  1.00 68.34           C  
ANISOU  401  CA  LYS A  68     7666   8785   9516    294    914   -557       C  
ATOM    402  C   LYS A  68     -45.607  25.258  -8.992  1.00 69.22           C  
ANISOU  402  C   LYS A  68     7873   8872   9556    289    879   -557       C  
ATOM    403  O   LYS A  68     -45.322  26.311  -8.413  1.00 69.47           O  
ANISOU  403  O   LYS A  68     7958   8872   9568    313    917   -568       O  
ATOM    404  CB  LYS A  68     -47.362  24.118  -7.635  1.00 68.89           C  
ANISOU  404  CB  LYS A  68     7759   8849   9569    256    996   -574       C  
ATOM    405  CG  LYS A  68     -48.820  23.731  -7.450  1.00 78.35           C  
ANISOU  405  CG  LYS A  68     8863  10069  10838    256   1048   -580       C  
ATOM    406  CD  LYS A  68     -48.982  22.726  -6.319  1.00 71.25           C  
ANISOU  406  CD  LYS A  68     7993   9167   9911    201   1115   -591       C  
ATOM    407  CE  LYS A  68     -50.202  23.038  -5.469  1.00 68.67           C  
ANISOU  407  CE  LYS A  68     7618   8839   9633    214   1214   -609       C  
ATOM    408  NZ  LYS A  68     -50.221  22.243  -4.210  1.00 55.93           N  
ANISOU  408  NZ  LYS A  68     6060   7212   7979    161   1289   -621       N  
ATOM    409  N   TRP A  69     -44.695  24.522  -9.629  1.00 67.81           N  
ANISOU  409  N   TRP A  69     7718   8709   9339    257    811   -547       N  
ATOM    410  CA  TRP A  69     -43.299  24.939  -9.671  1.00 61.14           C  
ANISOU  410  CA  TRP A  69     6954   7849   8428    249    777   -549       C  
ATOM    411  C   TRP A  69     -43.070  26.007 -10.734  1.00 58.78           C  
ANISOU  411  C   TRP A  69     6650   7540   8143    288    730   -539       C  
ATOM    412  O   TRP A  69     -42.443  27.038 -10.463  1.00 62.92           O  
ANISOU  412  O   TRP A  69     7234   8036   8637    301    743   -548       O  
ATOM    413  CB  TRP A  69     -42.397  23.729  -9.920  1.00 59.74           C  
ANISOU  413  CB  TRP A  69     6803   7692   8204    205    727   -543       C  
ATOM    414  CG  TRP A  69     -40.981  24.094 -10.239  1.00 65.98           C  
ANISOU  414  CG  TRP A  69     7656   8478   8936    198    679   -545       C  
ATOM    415  CD1 TRP A  69     -40.301  23.812 -11.387  1.00 65.51           C  
ANISOU  415  CD1 TRP A  69     7589   8435   8865    192    606   -533       C  
ATOM    416  CD2 TRP A  69     -40.068  24.811  -9.399  1.00 57.44           C  
ANISOU  416  CD2 TRP A  69     6651   7376   7798    193    702   -561       C  
ATOM    417  NE1 TRP A  69     -39.022  24.308 -11.315  1.00 64.55           N  
ANISOU  417  NE1 TRP A  69     7532   8308   8688    184    585   -542       N  
ATOM    418  CE2 TRP A  69     -38.854  24.926 -10.104  1.00 55.10           C  
ANISOU  418  CE2 TRP A  69     6386   7089   7462    182    641   -560       C  
ATOM    419  CE3 TRP A  69     -40.159  25.367  -8.119  1.00 55.99           C  
ANISOU  419  CE3 TRP A  69     6513   7169   7593    194    771   -579       C  
ATOM    420  CZ2 TRP A  69     -37.740  25.572  -9.572  1.00 54.38           C  
ANISOU  420  CZ2 TRP A  69     6362   6987   7312    170    644   -576       C  
ATOM    421  CZ3 TRP A  69     -39.053  26.009  -7.593  1.00 55.81           C  
ANISOU  421  CZ3 TRP A  69     6564   7132   7508    181    771   -596       C  
ATOM    422  CH2 TRP A  69     -37.859  26.106  -8.319  1.00 50.10           C  
ANISOU  422  CH2 TRP A  69     5864   6423   6748    168    707   -594       C  
ATOM    423  N   SER A  70     -43.566  25.775 -11.952  1.00 60.84           N  
ANISOU  423  N   SER A  70     6845   7824   8448    303    676   -521       N  
ATOM    424  CA  SER A  70     -43.438  26.778 -13.004  1.00 65.46           C  
ANISOU  424  CA  SER A  70     7427   8398   9045    342    631   -508       C  
ATOM    425  C   SER A  70     -44.226  28.037 -12.664  1.00 69.65           C  
ANISOU  425  C   SER A  70     7949   8899   9615    398    682   -511       C  
ATOM    426  O   SER A  70     -43.763  29.154 -12.924  1.00 64.08           O  
ANISOU  426  O   SER A  70     7292   8162   8894    425    676   -510       O  
ATOM    427  CB  SER A  70     -43.898  26.199 -14.342  1.00 67.40           C  
ANISOU  427  CB  SER A  70     7604   8678   9327    346    562   -489       C  
ATOM    428  OG  SER A  70     -44.194  24.819 -14.226  1.00 73.44           O  
ANISOU  428  OG  SER A  70     8331   9474  10099    304    557   -491       O  
ATOM    429  N   ALA A  71     -45.420  27.875 -12.089  1.00 85.69           N  
ANISOU  429  N   ALA A  71     9921  10939  11699    415    735   -517       N  
ATOM    430  CA  ALA A  71     -46.197  29.034 -11.661  1.00 82.45           C  
ANISOU  430  CA  ALA A  71     9501  10499  11327    472    792   -522       C  
ATOM    431  C   ALA A  71     -45.473  29.804 -10.564  1.00 78.81           C  
ANISOU  431  C   ALA A  71     9137   9994  10815    466    852   -543       C  
ATOM    432  O   ALA A  71     -45.550  31.037 -10.505  1.00 85.31           O  
ANISOU  432  O   ALA A  71     9992  10777  11645    511    878   -546       O  
ATOM    433  CB  ALA A  71     -47.582  28.594 -11.186  1.00 80.37           C  
ANISOU  433  CB  ALA A  71     9149  10260  11128    485    844   -528       C  
ATOM    434  N   PHE A  72     -44.773  29.090  -9.679  1.00 56.74           N  
ANISOU  434  N   PHE A  72     6392   7202   7966    410    873   -558       N  
ATOM    435  CA  PHE A  72     -43.958  29.759  -8.670  1.00 54.90           C  
ANISOU  435  CA  PHE A  72     6254   6932   7673    395    919   -580       C  
ATOM    436  C   PHE A  72     -42.842  30.568  -9.317  1.00 52.82           C  
ANISOU  436  C   PHE A  72     6054   6648   7368    395    871   -577       C  
ATOM    437  O   PHE A  72     -42.584  31.710  -8.922  1.00 57.53           O  
ANISOU  437  O   PHE A  72     6710   7202   7947    412    907   -590       O  
ATOM    438  CB  PHE A  72     -43.383  28.727  -7.699  1.00 54.37           C  
ANISOU  438  CB  PHE A  72     6226   6880   7552    336    937   -593       C  
ATOM    439  CG  PHE A  72     -42.268  29.251  -6.838  1.00 50.39           C  
ANISOU  439  CG  PHE A  72     5822   6350   6973    310    958   -614       C  
ATOM    440  CD1 PHE A  72     -42.541  30.010  -5.713  1.00 56.76           C  
ANISOU  440  CD1 PHE A  72     6675   7122   7768    320   1037   -636       C  
ATOM    441  CD2 PHE A  72     -40.946  28.973  -7.148  1.00 47.84           C  
ANISOU  441  CD2 PHE A  72     5546   6041   6591    274    898   -613       C  
ATOM    442  CE1 PHE A  72     -41.518  30.487  -4.915  1.00 54.06           C  
ANISOU  442  CE1 PHE A  72     6426   6759   7354    291   1053   -658       C  
ATOM    443  CE2 PHE A  72     -39.918  29.451  -6.356  1.00 47.81           C  
ANISOU  443  CE2 PHE A  72     5627   6020   6518    247    913   -635       C  
ATOM    444  CZ  PHE A  72     -40.205  30.207  -5.238  1.00 42.17           C  
ANISOU  444  CZ  PHE A  72     4960   5271   5790    254    989   -658       C  
ATOM    445  N   LEU A  73     -42.173  29.993 -10.320  1.00 58.46           N  
ANISOU  445  N   LEU A  73     6757   7389   8066    373    793   -562       N  
ATOM    446  CA  LEU A  73     -41.067  30.691 -10.969  1.00 56.65           C  
ANISOU  446  CA  LEU A  73     6586   7143   7795    365    750   -560       C  
ATOM    447  C   LEU A  73     -41.551  31.915 -11.736  1.00 60.76           C  
ANISOU  447  C   LEU A  73     7102   7630   8352    421    746   -548       C  
ATOM    448  O   LEU A  73     -40.909  32.969 -11.695  1.00 64.37           O  
ANISOU  448  O   LEU A  73     7630   8049   8779    424    758   -557       O  
ATOM    449  CB  LEU A  73     -40.314  29.738 -11.895  1.00 50.25           C  
ANISOU  449  CB  LEU A  73     5759   6370   6962    331    672   -547       C  
ATOM    450  CG  LEU A  73     -39.293  28.828 -11.210  1.00 55.94           C  
ANISOU  450  CG  LEU A  73     6518   7114   7622    276    665   -562       C  
ATOM    451  CD1 LEU A  73     -38.705  27.838 -12.202  1.00 63.43           C  
ANISOU  451  CD1 LEU A  73     7442   8099   8558    252    592   -548       C  
ATOM    452  CD2 LEU A  73     -38.198  29.652 -10.550  1.00 49.55           C  
ANISOU  452  CD2 LEU A  73     5794   6282   6752    254    685   -585       C  
ATOM    453  N   LYS A  74     -42.681  31.797 -12.441  1.00 74.49           N  
ANISOU  453  N   LYS A  74     8762   9384  10158    466    729   -527       N  
ATOM    454  CA  LYS A  74     -43.206  32.939 -13.184  1.00 82.06           C  
ANISOU  454  CA  LYS A  74     9716  10310  11152    529    722   -510       C  
ATOM    455  C   LYS A  74     -43.546  34.090 -12.247  1.00 84.63           C  
ANISOU  455  C   LYS A  74    10089  10584  11484    565    803   -527       C  
ATOM    456  O   LYS A  74     -43.291  35.258 -12.566  1.00 89.17           O  
ANISOU  456  O   LYS A  74    10721  11112  12050    596    807   -524       O  
ATOM    457  CB  LYS A  74     -44.435  32.526 -13.994  1.00 82.01           C  
ANISOU  457  CB  LYS A  74     9607  10338  11216    573    689   -487       C  
ATOM    458  CG  LYS A  74     -44.906  33.590 -14.976  1.00 90.15           C  
ANISOU  458  CG  LYS A  74    10631  11342  12279    642    662   -463       C  
ATOM    459  CD  LYS A  74     -46.121  33.128 -15.765  1.00 95.94           C  
ANISOU  459  CD  LYS A  74    11254  12118  13079    684    622   -442       C  
ATOM    460  CE  LYS A  74     -47.379  33.156 -14.912  1.00112.69           C  
ANISOU  460  CE  LYS A  74    13307  14246  15261    722    689   -453       C  
ATOM    461  NZ  LYS A  74     -48.511  32.449 -15.572  1.00117.24           N  
ANISOU  461  NZ  LYS A  74    13765  14880  15902    744    649   -438       N  
ATOM    462  N   GLU A  75     -44.132  33.781 -11.090  1.00 58.68           N  
ANISOU  462  N   GLU A  75     6784   7301   8212    562    870   -546       N  
ATOM    463  CA  GLU A  75     -44.364  34.808 -10.081  1.00 60.55           C  
ANISOU  463  CA  GLU A  75     7075   7486   8446    588    953   -568       C  
ATOM    464  C   GLU A  75     -43.045  35.395  -9.592  1.00 57.82           C  
ANISOU  464  C   GLU A  75     6842   7105   8023    542    965   -589       C  
ATOM    465  O   GLU A  75     -42.883  36.619  -9.529  1.00 55.71           O  
ANISOU  465  O   GLU A  75     6639   6783   7745    568    995   -597       O  
ATOM    466  CB  GLU A  75     -45.161  34.224  -8.915  1.00 60.60           C  
ANISOU  466  CB  GLU A  75     7044   7508   8475    582   1024   -586       C  
ATOM    467  CG  GLU A  75     -45.269  35.145  -7.710  1.00 69.32           C  
ANISOU  467  CG  GLU A  75     8216   8562   9563    596   1117   -614       C  
ATOM    468  CD  GLU A  75     -46.629  35.075  -7.043  1.00 82.04           C  
ANISOU  468  CD  GLU A  75     9760  10176  11235    637   1190   -621       C  
ATOM    469  OE1 GLU A  75     -47.439  34.206  -7.430  1.00 83.08           O  
ANISOU  469  OE1 GLU A  75     9793  10357  11419    644   1170   -607       O  
ATOM    470  OE2 GLU A  75     -46.886  35.887  -6.130  1.00 87.09           O1-
ANISOU  470  OE2 GLU A  75    10448  10771  11870    660   1272   -644       O1-
ATOM    471  N   GLN A  76     -42.081  34.533  -9.262  1.00 59.92           N  
ANISOU  471  N   GLN A  76     7132   7403   8234    474    940   -600       N  
ATOM    472  CA  GLN A  76     -40.812  35.018  -8.729  1.00 57.06           C  
ANISOU  472  CA  GLN A  76     6866   7017   7796    425    948   -624       C  
ATOM    473  C   GLN A  76     -39.955  35.670  -9.805  1.00 52.78           C  
ANISOU  473  C   GLN A  76     6364   6459   7231    419    893   -614       C  
ATOM    474  O   GLN A  76     -39.130  36.536  -9.493  1.00 51.54           O  
ANISOU  474  O   GLN A  76     6290   6266   7026    394    913   -635       O  
ATOM    475  CB  GLN A  76     -40.049  33.875  -8.059  1.00 50.40           C  
ANISOU  475  CB  GLN A  76     6032   6217   6901    360    933   -638       C  
ATOM    476  CG  GLN A  76     -40.778  33.265  -6.875  1.00 49.71           C  
ANISOU  476  CG  GLN A  76     5927   6139   6823    357    995   -650       C  
ATOM    477  CD  GLN A  76     -40.927  34.230  -5.716  1.00 56.16           C  
ANISOU  477  CD  GLN A  76     6811   6908   7620    364   1079   -678       C  
ATOM    478  OE1 GLN A  76     -40.019  35.005  -5.418  1.00 55.23           O  
ANISOU  478  OE1 GLN A  76     6775   6762   7448    339   1085   -699       O  
ATOM    479  NE2 GLN A  76     -42.078  34.186  -5.053  1.00 63.34           N  
ANISOU  479  NE2 GLN A  76     7687   7808   8571    396   1147   -683       N  
ATOM    480  N   SER A  77     -40.120  35.267 -11.067  1.00 58.09           N  
ANISOU  480  N   SER A  77     6981   7158   7934    436    827   -585       N  
ATOM    481  CA  SER A  77     -39.399  35.938 -12.144  1.00 61.92           C  
ANISOU  481  CA  SER A  77     7505   7624   8398    434    780   -573       C  
ATOM    482  C   SER A  77     -39.903  37.362 -12.337  1.00 61.60           C  
ANISOU  482  C   SER A  77     7507   7518   8381    491    817   -568       C  
ATOM    483  O   SER A  77     -39.106  38.290 -12.523  1.00 63.18           O  
ANISOU  483  O   SER A  77     7787   7676   8541    473    821   -577       O  
ATOM    484  CB  SER A  77     -39.524  35.147 -13.444  1.00 67.34           C  
ANISOU  484  CB  SER A  77     8125   8353   9109    440    702   -543       C  
ATOM    485  OG  SER A  77     -38.842  35.804 -14.497  1.00 72.54           O  
ANISOU  485  OG  SER A  77     8826   8991   9745    437    661   -531       O  
ATOM    486  N   THR A  78     -41.224  37.553 -12.302  1.00 75.51           N  
ANISOU  486  N   THR A  78     9215   9269  10207    560    845   -554       N  
ATOM    487  CA  THR A  78     -41.781  38.897 -12.417  1.00 75.67           C  
ANISOU  487  CA  THR A  78     9276   9224  10253    625    884   -548       C  
ATOM    488  C   THR A  78     -41.359  39.770 -11.242  1.00 79.11           C  
ANISOU  488  C   THR A  78     9804   9605  10648    605    963   -584       C  
ATOM    489  O   THR A  78     -41.006  40.941 -11.425  1.00 88.10           O  
ANISOU  489  O   THR A  78    11026  10682  11766    617    983   -587       O  
ATOM    490  CB  THR A  78     -43.305  38.827 -12.514  1.00 73.66           C  
ANISOU  490  CB  THR A  78     8932   8978  10078    705    901   -529       C  
ATOM    491  OG1 THR A  78     -43.677  37.962 -13.595  1.00 79.88           O  
ANISOU  491  OG1 THR A  78     9632   9821  10898    715    824   -499       O  
ATOM    492  CG2 THR A  78     -43.887  40.212 -12.758  1.00 67.07           C  
ANISOU  492  CG2 THR A  78     8137   8075   9271    785    934   -518       C  
ATOM    493  N   LEU A  79     -41.389  39.217 -10.027  1.00 71.31           N  
ANISOU  493  N   LEU A  79     8812   8637   9646    572   1009   -611       N  
ATOM    494  CA  LEU A  79     -40.934  39.973  -8.865  1.00 76.40           C  
ANISOU  494  CA  LEU A  79     9549   9235  10245    544   1081   -648       C  
ATOM    495  C   LEU A  79     -39.433  40.229  -8.918  1.00 77.47           C  
ANISOU  495  C   LEU A  79     9767   9365  10304    468   1054   -667       C  
ATOM    496  O   LEU A  79     -38.951  41.203  -8.331  1.00 81.65           O  
ANISOU  496  O   LEU A  79    10388   9842  10793    448   1102   -695       O  
ATOM    497  CB  LEU A  79     -41.307  39.240  -7.576  1.00 76.56           C  
ANISOU  497  CB  LEU A  79     9546   9283  10262    523   1133   -671       C  
ATOM    498  CG  LEU A  79     -42.788  38.904  -7.381  1.00 80.34           C  
ANISOU  498  CG  LEU A  79     9936   9774  10816    587   1170   -658       C  
ATOM    499  CD1 LEU A  79     -42.966  37.807  -6.341  1.00 78.10           C  
ANISOU  499  CD1 LEU A  79     9621   9534  10521    547   1199   -674       C  
ATOM    500  CD2 LEU A  79     -43.587  40.141  -7.003  1.00 79.20           C  
ANISOU  500  CD2 LEU A  79     9826   9562  10704    656   1246   -667       C  
ATOM    501  N   ALA A  80     -38.682  39.365  -9.604  1.00 76.28           N  
ANISOU  501  N   ALA A  80     9584   9268  10131    424    979   -655       N  
ATOM    502  CA  ALA A  80     -37.250  39.597  -9.761  1.00 68.55           C  
ANISOU  502  CA  ALA A  80     8671   8291   9084    354    950   -674       C  
ATOM    503  C   ALA A  80     -36.982  40.757 -10.711  1.00 71.50           C  
ANISOU  503  C   ALA A  80     9102   8609   9455    370    942   -663       C  
ATOM    504  O   ALA A  80     -36.025  41.517 -10.518  1.00 74.96           O  
ANISOU  504  O   ALA A  80     9625   9017   9840    321    958   -688       O  
ATOM    505  CB  ALA A  80     -36.560  38.326 -10.254  1.00 66.47           C  
ANISOU  505  CB  ALA A  80     8353   8101   8802    309    877   -664       C  
ATOM    506  N   GLN A  81     -37.816  40.908 -11.744  1.00 77.47           N  
ANISOU  506  N   GLN A  81     9815   9354  10266    438    916   -625       N  
ATOM    507  CA  GLN A  81     -37.629  41.992 -12.703  1.00 77.56           C  
ANISOU  507  CA  GLN A  81     9886   9309  10274    460    906   -609       C  
ATOM    508  C   GLN A  81     -37.817  43.364 -12.071  1.00 81.20           C  
ANISOU  508  C   GLN A  81    10440   9685  10727    483    983   -628       C  
ATOM    509  O   GLN A  81     -37.325  44.358 -12.616  1.00 79.41           O  
ANISOU  509  O   GLN A  81    10294   9403  10475    476    987   -626       O  
ATOM    510  CB  GLN A  81     -38.589  41.825 -13.883  1.00 70.37           C  
ANISOU  510  CB  GLN A  81     8908   8407   9423    535    859   -562       C  
ATOM    511  CG  GLN A  81     -38.150  40.784 -14.898  1.00 76.79           C  
ANISOU  511  CG  GLN A  81     9661   9284  10230    504    775   -541       C  
ATOM    512  CD  GLN A  81     -39.321  40.072 -15.546  1.00 82.25           C  
ANISOU  512  CD  GLN A  81    10250  10015  10987    568    734   -506       C  
ATOM    513  OE1 GLN A  81     -39.421  38.846 -15.498  1.00 81.35           O  
ANISOU  513  OE1 GLN A  81    10060   9965  10884    545    702   -505       O  
ATOM    514  NE2 GLN A  81     -40.218  40.841 -16.153  1.00 80.61           N  
ANISOU  514  NE2 GLN A  81    10040   9767  10821    647    736   -478       N  
ATOM    515  N   MET A  82     -38.511  43.442 -10.935  1.00 79.47           N  
ANISOU  515  N   MET A  82    10216   9452  10526    508   1048   -647       N  
ATOM    516  CA  MET A  82     -38.695  44.717 -10.253  1.00 75.44           C  
ANISOU  516  CA  MET A  82     9800   8859  10007    530   1128   -670       C  
ATOM    517  C   MET A  82     -37.418  45.213  -9.598  1.00 76.92           C  
ANISOU  517  C   MET A  82    10088   9024  10116    439   1154   -714       C  
ATOM    518  O   MET A  82     -37.397  46.345  -9.098  1.00 78.78           O  
ANISOU  518  O   MET A  82    10416   9184  10332    443   1219   -737       O  
ATOM    519  CB  MET A  82     -39.818  44.597  -9.220  1.00 71.43           C  
ANISOU  519  CB  MET A  82     9254   8345   9540    582   1194   -680       C  
ATOM    520  CG  MET A  82     -41.206  44.443  -9.834  1.00 79.72           C  
ANISOU  520  CG  MET A  82    10214   9403  10674    683   1183   -641       C  
ATOM    521  SD  MET A  82     -42.420  43.766  -8.686  1.00 99.53           S  
ANISOU  521  SD  MET A  82    12639  11944  13234    721   1244   -654       S  
ATOM    522  CE  MET A  82     -43.480  45.188  -8.426  1.00 84.53           C  
ANISOU  522  CE  MET A  82    10784   9952  11380    824   1329   -654       C  
ATOM    523  N   TYR A  83     -36.374  44.383  -9.559  1.00 78.07           N  
ANISOU  523  N   TYR A  83    10214   9235  10215    357   1106   -728       N  
ATOM    524  CA  TYR A  83     -35.051  44.789  -9.100  1.00 80.15           C  
ANISOU  524  CA  TYR A  83    10559   9491  10402    265   1115   -769       C  
ATOM    525  C   TYR A  83     -34.190  44.961 -10.321  1.00 83.10           C  
ANISOU  525  C   TYR A  83    10949   9870  10756    230   1058   -754       C  
ATOM    526  O   TYR A  83     -33.780  43.955 -10.924  1.00 82.81           O  
ANISOU  526  O   TYR A  83    10842   9903  10718    208    990   -738       O  
ATOM    527  CB  TYR A  83     -34.433  43.752  -8.156  1.00 77.09           C  
ANISOU  527  CB  TYR A  83    10139   9177   9975    200   1100   -796       C  
ATOM    528  CG  TYR A  83     -35.260  43.416  -6.953  1.00 78.10           C  
ANISOU  528  CG  TYR A  83    10248   9308  10118    228   1153   -809       C  
ATOM    529  CD1 TYR A  83     -35.154  44.144  -5.777  1.00 78.79           C  
ANISOU  529  CD1 TYR A  83    10417   9351  10168    204   1225   -850       C  
ATOM    530  CD2 TYR A  83     -36.145  42.353  -6.996  1.00 74.15           C  
ANISOU  530  CD2 TYR A  83     9650   8855   9669    274   1134   -782       C  
ATOM    531  CE1 TYR A  83     -35.906  43.808  -4.667  1.00 71.19           C  
ANISOU  531  CE1 TYR A  83     9441   8393   9216    226   1278   -863       C  
ATOM    532  CE2 TYR A  83     -36.901  42.012  -5.895  1.00 69.93           C  
ANISOU  532  CE2 TYR A  83     9098   8325   9148    295   1188   -794       C  
ATOM    533  CZ  TYR A  83     -36.779  42.741  -4.733  1.00 65.14           C  
ANISOU  533  CZ  TYR A  83     8575   7674   8502    272   1260   -834       C  
ATOM    534  OH  TYR A  83     -37.526  42.417  -3.624  1.00 74.20           O  
ANISOU  534  OH  TYR A  83     9711   8823   9658    290   1319   -848       O  
ATOM    535  N   PRO A  84     -33.893  46.196 -10.727  1.00 80.93           N  
ANISOU  535  N   PRO A  84    10768   9520  10463    224   1086   -759       N  
ATOM    536  CA  PRO A  84     -33.108  46.401 -11.937  1.00 81.77           C  
ANISOU  536  CA  PRO A  84    10894   9626  10548    191   1038   -744       C  
ATOM    537  C   PRO A  84     -31.633  46.073 -11.721  1.00 76.46           C  
ANISOU  537  C   PRO A  84    10236   9006   9809     80   1013   -781       C  
ATOM    538  O   PRO A  84     -31.044  46.351 -10.670  1.00 77.28           O  
ANISOU  538  O   PRO A  84    10388   9107   9867     20   1050   -827       O  
ATOM    539  CB  PRO A  84     -33.376  47.871 -12.261  1.00 78.82           C  
ANISOU  539  CB  PRO A  84    10626   9146  10175    223   1090   -739       C  
ATOM    540  CG  PRO A  84     -33.632  48.557 -10.881  1.00 77.19           C  
ANISOU  540  CG  PRO A  84    10487   8888   9954    220   1174   -779       C  
ATOM    541  CD  PRO A  84     -34.118  47.419  -9.948  1.00 78.23           C  
ANISOU  541  CD  PRO A  84    10526   9091  10106    233   1169   -786       C  
ATOM    542  N   LEU A  85     -31.032  45.460 -12.752  1.00 70.09           N  
ANISOU  542  N   LEU A  85     9384   8251   8997     55    946   -762       N  
ATOM    543  CA  LEU A  85     -29.728  44.819 -12.577  1.00 71.23           C  
ANISOU  543  CA  LEU A  85     9508   8468   9090    -36    910   -793       C  
ATOM    544  C   LEU A  85     -28.619  45.847 -12.429  1.00 76.26           C  
ANISOU  544  C   LEU A  85    10239   9068   9667   -122    942   -835       C  
ATOM    545  O   LEU A  85     -27.653  45.621 -11.695  1.00 71.19           O  
ANISOU  545  O   LEU A  85     9600   8473   8976   -199    940   -878       O  
ATOM    546  CB  LEU A  85     -29.444  43.889 -13.755  1.00 69.04           C  
ANISOU  546  CB  LEU A  85     9155   8250   8826    -34    836   -762       C  
ATOM    547  CG  LEU A  85     -29.602  42.378 -13.532  1.00 61.94           C  
ANISOU  547  CG  LEU A  85     8151   7438   7946    -21    788   -752       C  
ATOM    548  CD1 LEU A  85     -28.743  41.611 -14.520  1.00 70.22           C  
ANISOU  548  CD1 LEU A  85     9153   8550   8980    -58    723   -743       C  
ATOM    549  CD2 LEU A  85     -29.257  41.986 -12.101  1.00 64.40           C  
ANISOU  549  CD2 LEU A  85     8458   7784   8225    -59    809   -791       C  
ATOM    550  N   GLN A  86     -28.758  46.993 -13.100  1.00 80.54           N  
ANISOU  550  N   GLN A  86    10863   9527  10210   -109    973   -823       N  
ATOM    551  CA  GLN A  86     -27.633  47.908 -13.242  1.00 84.69           C  
ANISOU  551  CA  GLN A  86    11478  10022  10680   -198    997   -859       C  
ATOM    552  C   GLN A  86     -27.187  48.493 -11.909  1.00 84.88           C  
ANISOU  552  C   GLN A  86    11566  10026  10659   -260   1052   -915       C  
ATOM    553  O   GLN A  86     -26.023  48.882 -11.773  1.00 79.25           O  
ANISOU  553  O   GLN A  86    10896   9324   9890   -358   1059   -958       O  
ATOM    554  CB  GLN A  86     -27.991  49.024 -14.224  1.00 89.16           C  
ANISOU  554  CB  GLN A  86    12128  10491  11257   -165   1024   -830       C  
ATOM    555  CG  GLN A  86     -29.293  49.730 -13.913  1.00 84.69           C  
ANISOU  555  CG  GLN A  86    11606   9839  10732    -69   1074   -808       C  
ATOM    556  CD  GLN A  86     -30.295  49.614 -15.043  1.00 91.69           C  
ANISOU  556  CD  GLN A  86    12459  10705  11674     32   1041   -745       C  
ATOM    557  OE1 GLN A  86     -30.615  48.514 -15.494  1.00 92.58           O  
ANISOU  557  OE1 GLN A  86    12467  10889  11819     66    981   -716       O  
ATOM    558  NE2 GLN A  86     -30.802  50.752 -15.504  1.00 73.73           N  
ANISOU  558  NE2 GLN A  86    10275   8331   9409     82   1080   -723       N  
ATOM    559  N   GLU A  87     -28.075  48.573 -10.918  1.00102.85           N  
ANISOU  559  N   GLU A  87    13850  12275  12956   -209   1094   -920       N  
ATOM    560  CA  GLU A  87     -27.704  49.110  -9.607  1.00102.27           C  
ANISOU  560  CA  GLU A  87    13842  12181  12835   -266   1148   -975       C  
ATOM    561  C   GLU A  87     -27.395  48.006  -8.606  1.00 97.59           C  
ANISOU  561  C   GLU A  87    13176  11681  12222   -294   1118   -998       C  
ATOM    562  O   GLU A  87     -27.723  48.114  -7.420  1.00 97.39           O  
ANISOU  562  O   GLU A  87    13177  11644  12183   -292   1160  -1024       O  
ATOM    563  CB  GLU A  87     -28.787  50.035  -9.061  1.00100.48           C  
ANISOU  563  CB  GLU A  87    13689  11855  12633   -199   1224   -972       C  
ATOM    564  CG  GLU A  87     -29.432  50.914 -10.094  1.00 98.35           C  
ANISOU  564  CG  GLU A  87    13474  11496  12400   -133   1245   -933       C  
ATOM    565  CD  GLU A  87     -30.758  50.339 -10.494  1.00103.85           C  
ANISOU  565  CD  GLU A  87    14090  12198  13169    -14   1225   -878       C  
ATOM    566  OE1 GLU A  87     -30.801  49.105 -10.643  1.00102.65           O  
ANISOU  566  OE1 GLU A  87    13829  12136  13038     -4   1165   -860       O  
ATOM    567  OE2 GLU A  87     -31.746  51.080 -10.634  1.00100.26           O1-
ANISOU  567  OE2 GLU A  87    13679  11663  12753     70   1268   -855       O1-
ATOM    568  N   ILE A  88     -26.767  46.927  -9.066  1.00 87.67           N  
ANISOU  568  N   ILE A  88    11831  10517  10962   -319   1047   -988       N  
ATOM    569  CA  ILE A  88     -26.335  45.832  -8.207  1.00 86.74           C  
ANISOU  569  CA  ILE A  88    11647  10491  10820   -347   1011  -1008       C  
ATOM    570  C   ILE A  88     -24.897  45.489  -8.566  1.00 84.03           C  
ANISOU  570  C   ILE A  88    11277  10221  10431   -434    959  -1033       C  
ATOM    571  O   ILE A  88     -24.599  45.176  -9.725  1.00 84.53           O  
ANISOU  571  O   ILE A  88    11299  10308  10512   -432    917  -1007       O  
ATOM    572  CB  ILE A  88     -27.253  44.609  -8.343  1.00 86.22           C  
ANISOU  572  CB  ILE A  88    11484  10469  10809   -266    975   -963       C  
ATOM    573  CG1 ILE A  88     -28.603  44.939  -7.715  1.00 84.56           C  
ANISOU  573  CG1 ILE A  88    11296  10197  10638   -190   1034   -950       C  
ATOM    574  CG2 ILE A  88     -26.636  43.383  -7.686  1.00 81.29           C  
ANISOU  574  CG2 ILE A  88    10791   9941  10154   -298    928   -978       C  
ATOM    575  CD1 ILE A  88     -29.504  43.777  -7.599  1.00 70.57           C  
ANISOU  575  CD1 ILE A  88     9434   8468   8912   -123   1010   -916       C  
ATOM    576  N   GLN A  89     -24.009  45.554  -7.575  1.00 95.50           N  
ANISOU  576  N   GLN A  89    12750  11711  11823   -511    963  -1085       N  
ATOM    577  CA  GLN A  89     -22.580  45.386  -7.793  1.00 97.63           C  
ANISOU  577  CA  GLN A  89    12998  12051  12045   -601    920  -1118       C  
ATOM    578  C   GLN A  89     -22.067  44.007  -7.408  1.00 95.79           C  
ANISOU  578  C   GLN A  89    12670  11928  11798   -605    855  -1119       C  
ATOM    579  O   GLN A  89     -20.990  43.615  -7.872  1.00 95.82           O  
ANISOU  579  O   GLN A  89    12628  12001  11780   -656    807  -1133       O  
ATOM    580  CB  GLN A  89     -21.801  46.435  -6.989  1.00102.55           C  
ANISOU  580  CB  GLN A  89    13709  12651  12606   -695    963  -1180       C  
ATOM    581  CG  GLN A  89     -22.158  47.878  -7.316  1.00100.87           C  
ANISOU  581  CG  GLN A  89    13606  12324  12396   -703   1033  -1186       C  
ATOM    582  CD  GLN A  89     -23.193  48.454  -6.365  1.00104.01           C  
ANISOU  582  CD  GLN A  89    14074  12643  12802   -657   1099  -1190       C  
ATOM    583  OE1 GLN A  89     -24.318  47.961  -6.277  1.00100.21           O  
ANISOU  583  OE1 GLN A  89    13557  12147  12370   -563   1104  -1150       O  
ATOM    584  NE2 GLN A  89     -22.812  49.500  -5.641  1.00 99.23           N  
ANISOU  584  NE2 GLN A  89    13567  11988  12148   -725   1154  -1242       N  
ATOM    585  N   ASN A  90     -22.816  43.266  -6.588  1.00109.84           N  
ANISOU  585  N   ASN A  90    14421  13723  13592   -549    854  -1104       N  
ATOM    586  CA  ASN A  90     -22.265  42.090  -5.919  1.00103.85           C  
ANISOU  586  CA  ASN A  90    13596  13058  12803   -561    801  -1113       C  
ATOM    587  C   ASN A  90     -21.763  41.039  -6.904  1.00106.24           C  
ANISOU  587  C   ASN A  90    13807  13432  13126   -548    732  -1087       C  
ATOM    588  O   ASN A  90     -20.832  40.292  -6.581  1.00108.16           O  
ANISOU  588  O   ASN A  90    14002  13760  13333   -581    682  -1106       O  
ATOM    589  CB  ASN A  90     -23.317  41.494  -4.981  1.00 97.46           C  
ANISOU  589  CB  ASN A  90    12780  12239  12010   -497    820  -1094       C  
ATOM    590  CG  ASN A  90     -22.864  40.194  -4.345  1.00 96.42           C  
ANISOU  590  CG  ASN A  90    12586  12198  11851   -497    765  -1095       C  
ATOM    591  OD1 ASN A  90     -23.069  39.119  -4.902  1.00101.16           O  
ANISOU  591  OD1 ASN A  90    13113  12837  12485   -451    722  -1058       O  
ATOM    592  ND2 ASN A  90     -22.239  40.288  -3.178  1.00 96.76           N  
ANISOU  592  ND2 ASN A  90    12662  12272  11829   -548    766  -1138       N  
ATOM    593  N   LEU A  91     -22.385  40.936  -8.081  1.00 79.62           N  
ANISOU  593  N   LEU A  91    10411  10030   9811   -496    726  -1042       N  
ATOM    594  CA  LEU A  91     -22.055  40.073  -9.213  1.00 75.28           C  
ANISOU  594  CA  LEU A  91     9786   9531   9286   -480    670  -1014       C  
ATOM    595  C   LEU A  91     -22.361  38.599  -8.945  1.00 67.50           C  
ANISOU  595  C   LEU A  91     8724   8605   8317   -429    625   -987       C  
ATOM    596  O   LEU A  91     -22.241  37.787  -9.863  1.00 65.94           O  
ANISOU  596  O   LEU A  91     8465   8444   8145   -405    581   -960       O  
ATOM    597  CB  LEU A  91     -20.585  40.198  -9.654  1.00 68.90           C  
ANISOU  597  CB  LEU A  91     8963   8780   8437   -559    639  -1048       C  
ATOM    598  CG  LEU A  91     -20.213  40.100 -11.133  1.00 65.84           C  
ANISOU  598  CG  LEU A  91     8544   8401   8072   -563    613  -1028       C  
ATOM    599  CD1 LEU A  91     -21.195  40.897 -11.942  1.00 65.17           C  
ANISOU  599  CD1 LEU A  91     8509   8223   8028   -522    650   -994       C  
ATOM    600  CD2 LEU A  91     -18.823  40.661 -11.293  1.00 59.12           C  
ANISOU  600  CD2 LEU A  91     7705   7586   7173   -657    609  -1075       C  
ATOM    601  N   THR A  92     -22.708  38.215  -7.721  1.00 70.05           N  
ANISOU  601  N   THR A  92     9053   8939   8623   -414    637   -996       N  
ATOM    602  CA  THR A  92     -23.303  36.916  -7.431  1.00 63.19           C  
ANISOU  602  CA  THR A  92     8129   8104   7777   -357    610   -964       C  
ATOM    603  C   THR A  92     -24.800  37.046  -7.217  1.00 66.57           C  
ANISOU  603  C   THR A  92     8573   8467   8254   -293    657   -935       C  
ATOM    604  O   THR A  92     -25.564  36.160  -7.609  1.00 66.75           O  
ANISOU  604  O   THR A  92     8544   8497   8321   -238    640   -897       O  
ATOM    605  CB  THR A  92     -22.652  36.273  -6.191  1.00 67.07           C  
ANISOU  605  CB  THR A  92     8616   8657   8212   -383    589   -991       C  
ATOM    606  OG1 THR A  92     -21.226  36.308  -6.319  1.00 66.35           O  
ANISOU  606  OG1 THR A  92     8508   8628   8074   -445    548  -1025       O  
ATOM    607  CG2 THR A  92     -23.100  34.817  -6.019  1.00 54.17           C  
ANISOU  607  CG2 THR A  92     6925   7061   6596   -328    556   -957       C  
ATOM    608  N   VAL A  93     -25.224  38.154  -6.607  1.00 72.44           N  
ANISOU  608  N   VAL A  93     9388   9148   8989   -302    718   -955       N  
ATOM    609  CA  VAL A  93     -26.629  38.540  -6.633  1.00 70.90           C  
ANISOU  609  CA  VAL A  93     9209   8883   8848   -239    769   -928       C  
ATOM    610  C   VAL A  93     -27.059  38.855  -8.058  1.00 70.18           C  
ANISOU  610  C   VAL A  93     9098   8757   8809   -204    758   -894       C  
ATOM    611  O   VAL A  93     -28.147  38.464  -8.497  1.00 69.74           O  
ANISOU  611  O   VAL A  93     9004   8685   8811   -139    760   -856       O  
ATOM    612  CB  VAL A  93     -26.863  39.738  -5.695  1.00 68.41           C  
ANISOU  612  CB  VAL A  93     8981   8504   8506   -258    839   -962       C  
ATOM    613  CG1 VAL A  93     -28.323  40.157  -5.711  1.00 72.59           C  
ANISOU  613  CG1 VAL A  93     9524   8962   9095   -187    895   -935       C  
ATOM    614  CG2 VAL A  93     -26.401  39.400  -4.293  1.00 67.83           C  
ANISOU  614  CG2 VAL A  93     8931   8469   8374   -296    844   -996       C  
ATOM    615  N   LYS A  94     -26.209  39.569  -8.801  1.00 79.47           N  
ANISOU  615  N   LYS A  94    10304   9926   9966   -250    748   -908       N  
ATOM    616  CA  LYS A  94     -26.534  39.921 -10.180  1.00 70.82           C  
ANISOU  616  CA  LYS A  94     9201   8796   8911   -221    737   -876       C  
ATOM    617  C   LYS A  94     -26.713  38.677 -11.040  1.00 74.68           C  
ANISOU  617  C   LYS A  94     9604   9338   9435   -185    677   -839       C  
ATOM    618  O   LYS A  94     -27.620  38.621 -11.879  1.00 74.81           O  
ANISOU  618  O   LYS A  94     9597   9326   9502   -128    672   -800       O  
ATOM    619  CB  LYS A  94     -25.444  40.824 -10.759  1.00 74.43           C  
ANISOU  619  CB  LYS A  94     9708   9241   9331   -288    737   -902       C  
ATOM    620  CG  LYS A  94     -25.711  41.295 -12.179  1.00 75.65           C  
ANISOU  620  CG  LYS A  94     9872   9354   9518   -264    730   -869       C  
ATOM    621  CD  LYS A  94     -24.943  42.569 -12.494  1.00 81.90           C  
ANISOU  621  CD  LYS A  94    10746  10100  10274   -327    761   -897       C  
ATOM    622  CE  LYS A  94     -25.203  43.027 -13.921  1.00 96.33           C  
ANISOU  622  CE  LYS A  94    12591  11882  12127   -301    754   -861       C  
ATOM    623  NZ  LYS A  94     -24.967  44.487 -14.098  1.00 95.64           N  
ANISOU  623  NZ  LYS A  94    12608  11713  12016   -337    806   -878       N  
ATOM    624  N   LEU A  95     -25.856  37.671 -10.851  1.00 70.19           N  
ANISOU  624  N   LEU A  95     8988   8845   8837   -216    631   -850       N  
ATOM    625  CA  LEU A  95     -25.987  36.433 -11.614  1.00 67.89           C  
ANISOU  625  CA  LEU A  95     8620   8601   8574   -184    578   -818       C  
ATOM    626  C   LEU A  95     -27.281  35.706 -11.270  1.00 66.36           C  
ANISOU  626  C   LEU A  95     8390   8399   8426   -120    586   -787       C  
ATOM    627  O   LEU A  95     -28.031  35.294 -12.162  1.00 64.85           O  
ANISOU  627  O   LEU A  95     8157   8200   8282    -74    566   -751       O  
ATOM    628  CB  LEU A  95     -24.781  35.529 -11.356  1.00 67.68           C  
ANISOU  628  CB  LEU A  95     8557   8655   8504   -226    532   -839       C  
ATOM    629  CG  LEU A  95     -24.212  34.769 -12.556  1.00 56.54           C  
ANISOU  629  CG  LEU A  95     7091   7289   7101   -228    478   -823       C  
ATOM    630  CD1 LEU A  95     -24.373  35.570 -13.841  1.00 55.46           C  
ANISOU  630  CD1 LEU A  95     6976   7108   6988   -226    483   -806       C  
ATOM    631  CD2 LEU A  95     -22.752  34.414 -12.320  1.00 58.88           C  
ANISOU  631  CD2 LEU A  95     7371   7655   7347   -283    446   -857       C  
ATOM    632  N   GLN A  96     -27.557  35.538  -9.973  1.00 66.36           N  
ANISOU  632  N   GLN A  96     8404   8399   8409   -118    617   -803       N  
ATOM    633  CA  GLN A  96     -28.764  34.831  -9.558  1.00 56.82           C  
ANISOU  633  CA  GLN A  96     7161   7185   7242    -64    632   -778       C  
ATOM    634  C   GLN A  96     -30.018  35.554 -10.032  1.00 60.17           C  
ANISOU  634  C   GLN A  96     7591   7546   7724    -11    668   -754       C  
ATOM    635  O   GLN A  96     -30.955  34.923 -10.535  1.00 61.30           O  
ANISOU  635  O   GLN A  96     7679   7693   7919     37    655   -721       O  
ATOM    636  CB  GLN A  96     -28.784  34.668  -8.039  1.00 51.61           C  
ANISOU  636  CB  GLN A  96     6531   6532   6547    -78    666   -802       C  
ATOM    637  CG  GLN A  96     -27.681  33.782  -7.490  1.00 51.78           C  
ANISOU  637  CG  GLN A  96     6540   6620   6513   -117    625   -820       C  
ATOM    638  CD  GLN A  96     -27.698  33.710  -5.977  1.00 58.53           C  
ANISOU  638  CD  GLN A  96     7435   7479   7326   -131    658   -844       C  
ATOM    639  OE1 GLN A  96     -26.723  34.068  -5.316  1.00 53.37           O  
ANISOU  639  OE1 GLN A  96     6819   6846   6612   -180    654   -879       O  
ATOM    640  NE2 GLN A  96     -28.812  33.249  -5.419  1.00 61.05           N  
ANISOU  640  NE2 GLN A  96     7744   7779   7674    -92    693   -826       N  
ATOM    641  N   LEU A  97     -30.055  36.878  -9.879  1.00 50.06           N  
ANISOU  641  N   LEU A  97     6375   6208   6436    -17    713   -770       N  
ATOM    642  CA  LEU A  97     -31.201  37.636 -10.366  1.00 55.38           C  
ANISOU  642  CA  LEU A  97     7058   6820   7164     41    746   -746       C  
ATOM    643  C   LEU A  97     -31.325  37.535 -11.878  1.00 56.73           C  
ANISOU  643  C   LEU A  97     7194   6994   7368     65    698   -712       C  
ATOM    644  O   LEU A  97     -32.427  37.341 -12.404  1.00 58.08           O  
ANISOU  644  O   LEU A  97     7321   7151   7595    125    694   -679       O  
ATOM    645  CB  LEU A  97     -31.082  39.094  -9.946  1.00 54.87           C  
ANISOU  645  CB  LEU A  97     7081   6688   7077     26    804   -772       C  
ATOM    646  CG  LEU A  97     -31.550  39.407  -8.535  1.00 54.65           C  
ANISOU  646  CG  LEU A  97     7092   6634   7038     31    868   -797       C  
ATOM    647  CD1 LEU A  97     -30.990  40.741  -8.195  1.00 54.06           C  
ANISOU  647  CD1 LEU A  97     7112   6504   6922     -8    912   -831       C  
ATOM    648  CD2 LEU A  97     -33.065  39.422  -8.450  1.00 58.74           C  
ANISOU  648  CD2 LEU A  97     7579   7118   7621    109    906   -771       C  
ATOM    649  N   GLN A  98     -30.202  37.651 -12.592  1.00 80.99           N  
ANISOU  649  N   GLN A  98    10281  10085  10405     18    662   -721       N  
ATOM    650  CA  GLN A  98     -30.243  37.605 -14.050  1.00 83.16           C  
ANISOU  650  CA  GLN A  98    10533  10360  10704     36    619   -690       C  
ATOM    651  C   GLN A  98     -30.873  36.309 -14.541  1.00 85.98           C  
ANISOU  651  C   GLN A  98    10805  10762  11100     72    574   -659       C  
ATOM    652  O   GLN A  98     -31.687  36.321 -15.471  1.00 88.79           O  
ANISOU  652  O   GLN A  98    11135  11103  11500    120    555   -625       O  
ATOM    653  CB  GLN A  98     -28.835  37.767 -14.620  1.00 81.39           C  
ANISOU  653  CB  GLN A  98    10335  10160  10431    -31    592   -710       C  
ATOM    654  CG  GLN A  98     -28.791  37.964 -16.123  1.00 87.14           C  
ANISOU  654  CG  GLN A  98    11061  10876  11172    -20    558   -682       C  
ATOM    655  CD  GLN A  98     -28.147  36.795 -16.840  1.00 95.70           C  
ANISOU  655  CD  GLN A  98    12086  12029  12249    -40    498   -675       C  
ATOM    656  OE1 GLN A  98     -27.210  36.180 -16.330  1.00 96.99           O  
ANISOU  656  OE1 GLN A  98    12231  12245  12377    -85    484   -701       O  
ATOM    657  NE2 GLN A  98     -28.648  36.480 -18.028  1.00 90.90           N  
ANISOU  657  NE2 GLN A  98    11448  11420  11670     -5    462   -639       N  
ATOM    658  N   ALA A  99     -30.517  35.182 -13.920  1.00 72.60           N  
ANISOU  658  N   ALA A  99     9071   9124   9389     51    555   -670       N  
ATOM    659  CA  ALA A  99     -31.138  33.912 -14.282  1.00 69.31           C  
ANISOU  659  CA  ALA A  99     8581   8746   9008     81    519   -643       C  
ATOM    660  C   ALA A  99     -32.631  33.919 -13.978  1.00 75.71           C  
ANISOU  660  C   ALA A  99     9363   9529   9874    140    549   -623       C  
ATOM    661  O   ALA A  99     -33.436  33.417 -14.772  1.00 85.85           O  
ANISOU  661  O   ALA A  99    10594  10822  11204    177    521   -594       O  
ATOM    662  CB  ALA A  99     -30.445  32.763 -13.551  1.00 62.08           C  
ANISOU  662  CB  ALA A  99     7642   7887   8059     49    500   -660       C  
ATOM    663  N   LEU A 100     -33.021  34.479 -12.831  1.00 69.18           N  
ANISOU  663  N   LEU A 100     8569   8671   9045    147    608   -641       N  
ATOM    664  CA  LEU A 100     -34.434  34.517 -12.466  1.00 72.45           C  
ANISOU  664  CA  LEU A 100     8953   9062   9514    202    645   -626       C  
ATOM    665  C   LEU A 100     -35.222  35.441 -13.390  1.00 81.04           C  
ANISOU  665  C   LEU A 100    10041  10104  10646    255    648   -602       C  
ATOM    666  O   LEU A 100     -36.302  35.078 -13.870  1.00 72.59           O  
ANISOU  666  O   LEU A 100     8910   9041   9631    304    635   -575       O  
ATOM    667  CB  LEU A 100     -34.588  34.952 -11.008  1.00 62.89           C  
ANISOU  667  CB  LEU A 100     7785   7826   8284    195    713   -654       C  
ATOM    668  CG  LEU A 100     -35.182  33.916 -10.050  1.00 54.35           C  
ANISOU  668  CG  LEU A 100     6664   6774   7213    199    734   -655       C  
ATOM    669  CD1 LEU A 100     -35.280  34.480  -8.640  1.00 61.00           C  
ANISOU  669  CD1 LEU A 100     7562   7586   8029    190    804   -685       C  
ATOM    670  CD2 LEU A 100     -36.542  33.444 -10.539  1.00 45.04           C  
ANISOU  670  CD2 LEU A 100     5410   5598   6105    253    732   -626       C  
ATOM    671  N   GLN A 101     -34.699  36.644 -13.649  1.00 84.00           N  
ANISOU  671  N   GLN A 101    10486  10433  10996    246    663   -610       N  
ATOM    672  CA  GLN A 101     -35.391  37.577 -14.535  1.00 82.33           C  
ANISOU  672  CA  GLN A 101    10287  10172  10820    300    665   -585       C  
ATOM    673  C   GLN A 101     -35.452  37.049 -15.963  1.00 89.92           C  
ANISOU  673  C   GLN A 101    11203  11162  11801    314    595   -552       C  
ATOM    674  O   GLN A 101     -36.454  37.248 -16.660  1.00 89.41           O  
ANISOU  674  O   GLN A 101    11106  11082  11784    375    581   -522       O  
ATOM    675  CB  GLN A 101     -34.708  38.946 -14.508  1.00 77.66           C  
ANISOU  675  CB  GLN A 101     9795   9522  10192    279    699   -603       C  
ATOM    676  CG  GLN A 101     -34.451  39.501 -13.118  1.00 82.55           C  
ANISOU  676  CG  GLN A 101    10473  10114  10780    251    765   -641       C  
ATOM    677  CD  GLN A 101     -33.720  40.828 -13.149  1.00 80.63           C  
ANISOU  677  CD  GLN A 101    10329   9810  10496    220    797   -662       C  
ATOM    678  OE1 GLN A 101     -33.703  41.563 -12.164  1.00 80.27           O  
ANISOU  678  OE1 GLN A 101    10345   9724  10431    209    858   -691       O  
ATOM    679  NE2 GLN A 101     -33.112  41.141 -14.286  1.00 76.98           N  
ANISOU  679  NE2 GLN A 101     9891   9341  10018    202    760   -649       N  
ATOM    680  N   GLN A 102     -34.388  36.382 -16.416  1.00106.81           N  
ANISOU  680  N   GLN A 102    13338  13344  13901    259    550   -559       N  
ATOM    681  CA  GLN A 102     -34.346  35.882 -17.788  1.00112.91           C  
ANISOU  681  CA  GLN A 102    14075  14142  14684    266    486   -531       C  
ATOM    682  C   GLN A 102     -35.449  34.864 -18.047  1.00118.39           C  
ANISOU  682  C   GLN A 102    14681  14871  15430    307    457   -507       C  
ATOM    683  O   GLN A 102     -36.005  34.806 -19.150  1.00125.65           O  
ANISOU  683  O   GLN A 102    15570  15793  16376    341    415   -477       O  
ATOM    684  CB  GLN A 102     -32.975  35.267 -18.073  1.00109.29           C  
ANISOU  684  CB  GLN A 102    13624  13726  14174    199    452   -548       C  
ATOM    685  CG  GLN A 102     -32.877  34.508 -19.383  1.00106.13           C  
ANISOU  685  CG  GLN A 102    13184  13361  13779    199    388   -524       C  
ATOM    686  CD  GLN A 102     -31.782  35.044 -20.281  1.00104.98           C  
ANISOU  686  CD  GLN A 102    13091  13207  13591    159    369   -528       C  
ATOM    687  OE1 GLN A 102     -31.274  36.145 -20.069  1.00101.24           O  
ANISOU  687  OE1 GLN A 102    12685  12691  13090    139    405   -544       O  
ATOM    688  NE2 GLN A 102     -31.410  34.266 -21.290  1.00 95.64           N  
ANISOU  688  NE2 GLN A 102    11878  12062  12400    145    318   -517       N  
ATOM    689  N   ASN A 103     -35.786  34.060 -17.035  1.00125.60           N  
ANISOU  689  N   ASN A 103    15555  15813  16355    301    479   -520       N  
ATOM    690  CA  ASN A 103     -36.723  32.958 -17.230  1.00140.10           C  
ANISOU  690  CA  ASN A 103    17308  17687  18236    324    454   -502       C  
ATOM    691  C   ASN A 103     -38.096  33.451 -17.671  1.00141.56           C  
ANISOU  691  C   ASN A 103    17454  17850  18482    393    457   -476       C  
ATOM    692  O   ASN A 103     -38.751  32.814 -18.505  1.00144.23           O  
ANISOU  692  O   ASN A 103    17729  18218  18854    414    411   -453       O  
ATOM    693  CB  ASN A 103     -36.843  32.140 -15.945  1.00138.95           C  
ANISOU  693  CB  ASN A 103    17142  17566  18088    304    489   -521       C  
ATOM    694  CG  ASN A 103     -37.505  30.794 -16.170  1.00146.96           C  
ANISOU  694  CG  ASN A 103    18079  18624  19136    306    459   -508       C  
ATOM    695  OD1 ASN A 103     -38.731  30.686 -16.170  1.00138.60           O  
ANISOU  695  OD1 ASN A 103    16966  17567  18131    345    471   -494       O  
ATOM    696  ND2 ASN A 103     -36.694  29.760 -16.360  1.00148.05           N  
ANISOU  696  ND2 ASN A 103    18212  18800  19241    264    422   -512       N  
ATOM    697  N   GLY A 104     -38.550  34.575 -17.121  1.00132.39           N  
ANISOU  697  N   GLY A 104    16328  16640  17336    430    510   -481       N  
ATOM    698  CA  GLY A 104     -39.895  35.051 -17.385  1.00132.17           C  
ANISOU  698  CA  GLY A 104    16258  16593  17368    503    519   -459       C  
ATOM    699  C   GLY A 104     -40.194  35.272 -18.853  1.00136.52           C  
ANISOU  699  C   GLY A 104    16792  17144  17936    539    457   -425       C  
ATOM    700  O   GLY A 104     -39.702  36.227 -19.462  1.00131.12           O  
ANISOU  700  O   GLY A 104    16175  16419  17227    547    449   -416       O  
ATOM    701  N   SER A 105     -41.012  34.393 -19.429  1.00122.01           N  
ANISOU  701  N   SER A 105    14867  15352  16140    558    412   -406       N  
ATOM    702  CA  SER A 105     -41.399  34.486 -20.829  1.00121.75           C  
ANISOU  702  CA  SER A 105    14810  15327  16122    593    346   -374       C  
ATOM    703  C   SER A 105     -42.599  35.399 -21.043  1.00119.11           C  
ANISOU  703  C   SER A 105    14452  14965  15840    680    355   -352       C  
ATOM    704  O   SER A 105     -43.258  35.307 -22.085  1.00112.53           O  
ANISOU  704  O   SER A 105    13572  14151  15034    720    297   -323       O  
ATOM    705  CB  SER A 105     -41.691  33.096 -21.396  1.00116.74           C  
ANISOU  705  CB  SER A 105    14095  14757  15503    568    289   -367       C  
ATOM    706  OG  SER A 105     -41.786  33.137 -22.810  1.00 91.08           O  
ANISOU  706  OG  SER A 105    10837  11517  12250    586    219   -339       O  
ATOM    707  N   SER A 106     -42.899  36.274 -20.076  1.00150.89           N  
ANISOU  707  N   SER A 106    18508  18944  19879    713    426   -364       N  
ATOM    708  CA  SER A 106     -43.913  37.316 -20.228  1.00151.15           C  
ANISOU  708  CA  SER A 106    18534  18939  19957    803    443   -345       C  
ATOM    709  C   SER A 106     -43.408  38.325 -21.245  1.00151.12           C  
ANISOU  709  C   SER A 106    18614  18885  19920    826    412   -320       C  
ATOM    710  O   SER A 106     -44.084  39.306 -21.579  1.00159.00           O  
ANISOU  710  O   SER A 106    19628  19842  20944    905    417   -298       O  
ATOM    711  CB  SER A 106     -44.208  38.004 -18.894  1.00145.18           C  
ANISOU  711  CB  SER A 106    17805  18140  19216    826    535   -369       C  
ATOM    712  OG  SER A 106     -45.520  38.545 -18.863  1.00151.12           O  
ANISOU  712  OG  SER A 106    18505  18881  20033    917    554   -354       O  
ATOM    713  N   VAL A 107     -42.184  38.084 -21.718  1.00 96.54           N  
ANISOU  713  N   VAL A 107    11758  11975  12946    756    383   -326       N  
ATOM    714  CA  VAL A 107     -41.590  38.906 -22.759  1.00 97.91           C  
ANISOU  714  CA  VAL A 107    12014  12106  13081    763    352   -304       C  
ATOM    715  C   VAL A 107     -42.436  38.863 -24.025  1.00 92.63           C  
ANISOU  715  C   VAL A 107    11299  11456  12441    825    280   -262       C  
ATOM    716  O   VAL A 107     -42.485  39.839 -24.784  1.00 87.08           O  
ANISOU  716  O   VAL A 107    10657  10704  11725    871    265   -235       O  
ATOM    717  CB  VAL A 107     -40.145  38.437 -23.004  1.00 96.68           C  
ANISOU  717  CB  VAL A 107    11908  11966  12859    670    335   -322       C  
ATOM    718  CG1 VAL A 107     -40.101  36.926 -23.180  1.00 89.91           C  
ANISOU  718  CG1 VAL A 107    10967  11187  12008    626    289   -327       C  
ATOM    719  CG2 VAL A 107     -39.570  39.119 -24.197  1.00 84.37           C  
ANISOU  719  CG2 VAL A 107    10424  10372  11259    669    300   -298       C  
ATOM    720  N   LEU A 108     -43.132  37.755 -24.262  1.00 66.16           N  
ANISOU  720  N   LEU A 108     7840   8173   9125    827    236   -257       N  
ATOM    721  CA  LEU A 108     -44.042  37.617 -25.389  1.00 57.83           C  
ANISOU  721  CA  LEU A 108     6725   7146   8100    884    163   -221       C  
ATOM    722  C   LEU A 108     -45.485  37.725 -24.911  1.00 59.63           C  
ANISOU  722  C   LEU A 108     6863   7391   8404    963    180   -216       C  
ATOM    723  O   LEU A 108     -45.797  37.431 -23.755  1.00 61.39           O  
ANISOU  723  O   LEU A 108     7044   7625   8658    953    239   -243       O  
ATOM    724  CB  LEU A 108     -43.830  36.278 -26.101  1.00 49.92           C  
ANISOU  724  CB  LEU A 108     5666   6214   7087    827     96   -222       C  
ATOM    725  CG  LEU A 108     -42.809  36.235 -27.239  1.00 53.25           C  
ANISOU  725  CG  LEU A 108     6157   6630   7444    783     46   -209       C  
ATOM    726  CD1 LEU A 108     -42.936  34.935 -28.017  1.00 42.06           C  
ANISOU  726  CD1 LEU A 108     4671   5283   6028    746    -24   -206       C  
ATOM    727  CD2 LEU A 108     -42.988  37.432 -28.158  1.00 59.60           C  
ANISOU  727  CD2 LEU A 108     7029   7382   8235    847     20   -173       C  
ATOM    728  N   SER A 109     -46.365  38.159 -25.813  1.00 52.26           N  
ANISOU  728  N   SER A 109     5898   6460   7500   1042    128   -180       N  
ATOM    729  CA  SER A 109     -47.785  38.225 -25.491  1.00 38.97           C  
ANISOU  729  CA  SER A 109     4113   4802   5892   1122    135   -173       C  
ATOM    730  C   SER A 109     -48.304  36.836 -25.140  1.00 48.60           C  
ANISOU  730  C   SER A 109     5212   6103   7149   1076    124   -195       C  
ATOM    731  O   SER A 109     -47.851  35.827 -25.687  1.00 53.54           O  
ANISOU  731  O   SER A 109     5821   6774   7748   1008     73   -198       O  
ATOM    732  CB  SER A 109     -48.574  38.801 -26.667  1.00 47.11           C  
ANISOU  732  CB  SER A 109     5125   5833   6941   1212     64   -130       C  
ATOM    733  OG  SER A 109     -48.762  37.824 -27.677  1.00 49.51           O  
ANISOU  733  OG  SER A 109     5363   6206   7241   1184    -24   -117       O  
ATOM    734  N   GLU A 110     -49.253  36.785 -24.199  1.00 75.84           N  
ANISOU  734  N   GLU A 110     8584   9570  10661   1111    176   -211       N  
ATOM    735  CA  GLU A 110     -49.744  35.489 -23.740  1.00 76.41           C  
ANISOU  735  CA  GLU A 110     8551   9714  10768   1060    179   -234       C  
ATOM    736  C   GLU A 110     -50.351  34.687 -24.881  1.00 68.75           C  
ANISOU  736  C   GLU A 110     7491   8813   9816   1060     84   -216       C  
ATOM    737  O   GLU A 110     -50.339  33.453 -24.841  1.00 66.42           O  
ANISOU  737  O   GLU A 110     7140   8572   9523    990     67   -233       O  
ATOM    738  CB  GLU A 110     -50.761  35.653 -22.609  1.00 78.75           C  
ANISOU  738  CB  GLU A 110     8775  10016  11130   1104    253   -253       C  
ATOM    739  CG  GLU A 110     -51.956  36.523 -22.936  1.00100.14           C  
ANISOU  739  CG  GLU A 110    11426  12724  13899   1218    243   -230       C  
ATOM    740  CD  GLU A 110     -53.229  36.046 -22.261  1.00104.26           C  
ANISOU  740  CD  GLU A 110    11813  13300  14499   1243    278   -248       C  
ATOM    741  OE1 GLU A 110     -53.143  35.159 -21.386  1.00105.49           O  
ANISOU  741  OE1 GLU A 110    11939  13482  14659   1171    326   -280       O  
ATOM    742  OE2 GLU A 110     -54.317  36.557 -22.604  1.00 84.66           O1-
ANISOU  742  OE2 GLU A 110     9257  10837  12075   1336    259   -230       O1-
ATOM    743  N   ASP A 111     -50.886  35.362 -25.903  1.00 51.02           N  
ANISOU  743  N   ASP A 111     5237   6566   7583   1137     22   -181       N  
ATOM    744  CA  ASP A 111     -51.322  34.651 -27.100  1.00 51.56           C  
ANISOU  744  CA  ASP A 111     5237   6698   7655   1131    -76   -162       C  
ATOM    745  C   ASP A 111     -50.136  34.047 -27.840  1.00 50.33           C  
ANISOU  745  C   ASP A 111     5156   6541   7426   1048   -122   -161       C  
ATOM    746  O   ASP A 111     -50.132  32.852 -28.155  1.00 49.77           O  
ANISOU  746  O   ASP A 111     5031   6527   7351    982   -161   -174       O  
ATOM    747  CB  ASP A 111     -52.099  35.592 -28.020  1.00 55.52           C  
ANISOU  747  CB  ASP A 111     5724   7194   8178   1238   -135   -122       C  
ATOM    748  CG  ASP A 111     -52.565  34.908 -29.287  1.00 53.36           C  
ANISOU  748  CG  ASP A 111     5383   6989   7904   1233   -243   -103       C  
ATOM    749  OD1 ASP A 111     -53.411  33.995 -29.188  1.00 51.24           O  
ANISOU  749  OD1 ASP A 111     4990   6794   7684   1213   -262   -120       O  
ATOM    750  OD2 ASP A 111     -52.081  35.273 -30.379  1.00 47.66           O1-
ANISOU  750  OD2 ASP A 111     4734   6244   7129   1244   -307    -74       O1-
ATOM    751  N   LYS A 112     -49.111  34.859 -28.116  1.00 48.36           N  
ANISOU  751  N   LYS A 112     5031   6226   7117   1047   -114   -149       N  
ATOM    752  CA  LYS A 112     -47.922  34.345 -28.788  1.00 41.14           C  
ANISOU  752  CA  LYS A 112     4189   5309   6133    968   -148   -150       C  
ATOM    753  C   LYS A 112     -47.172  33.358 -27.906  1.00 42.36           C  
ANISOU  753  C   LYS A 112     4346   5479   6271    876   -100   -188       C  
ATOM    754  O   LYS A 112     -46.585  32.395 -28.413  1.00 37.12           O  
ANISOU  754  O   LYS A 112     3684   4846   5572    807   -138   -196       O  
ATOM    755  CB  LYS A 112     -47.011  35.499 -29.209  1.00 33.66           C  
ANISOU  755  CB  LYS A 112     3374   4287   5128    986   -140   -131       C  
ATOM    756  CG  LYS A 112     -47.555  36.314 -30.374  1.00 47.09           C  
ANISOU  756  CG  LYS A 112     5094   5973   6826   1067   -206    -87       C  
ATOM    757  CD  LYS A 112     -46.581  37.397 -30.816  1.00 35.27           C  
ANISOU  757  CD  LYS A 112     3738   4397   5265   1073   -194    -69       C  
ATOM    758  CE  LYS A 112     -47.043  38.055 -32.109  1.00 50.45           C  
ANISOU  758  CE  LYS A 112     5688   6307   7173   1145   -269    -22       C  
ATOM    759  NZ  LYS A 112     -46.247  39.268 -32.446  1.00 62.71           N  
ANISOU  759  NZ  LYS A 112     7384   7772   8670   1162   -245     -1       N  
ATOM    760  N   SER A 113     -47.171  33.584 -26.591  1.00 48.53           N  
ANISOU  760  N   SER A 113     5130   6236   7073    874    -16   -212       N  
ATOM    761  CA  SER A 113     -46.647  32.579 -25.673  1.00 43.41           C  
ANISOU  761  CA  SER A 113     4471   5609   6415    795     27   -247       C  
ATOM    762  C   SER A 113     -47.479  31.303 -25.730  1.00 51.94           C  
ANISOU  762  C   SER A 113     5439   6760   7537    768     -2   -256       C  
ATOM    763  O   SER A 113     -46.929  30.195 -25.740  1.00 51.76           O  
ANISOU  763  O   SER A 113     5413   6764   7487    694    -14   -273       O  
ATOM    764  CB  SER A 113     -46.608  33.138 -24.250  1.00 52.80           C  
ANISOU  764  CB  SER A 113     5686   6758   7618    805    121   -269       C  
ATOM    765  OG  SER A 113     -46.865  32.124 -23.295  1.00 61.30           O  
ANISOU  765  OG  SER A 113     6702   7870   8717    760    161   -297       O  
ATOM    766  N   LYS A 114     -48.808  31.437 -25.767  1.00 46.95           N  
ANISOU  766  N   LYS A 114     4712   6158   6969    827    -12   -247       N  
ATOM    767  CA  LYS A 114     -49.664  30.265 -25.929  1.00 40.94           C  
ANISOU  767  CA  LYS A 114     3840   5468   6249    798    -44   -257       C  
ATOM    768  C   LYS A 114     -49.533  29.679 -27.330  1.00 41.85           C  
ANISOU  768  C   LYS A 114     3947   5619   6336    773   -141   -241       C  
ATOM    769  O   LYS A 114     -49.566  28.454 -27.500  1.00 38.02           O  
ANISOU  769  O   LYS A 114     3418   5178   5849    707   -165   -256       O  
ATOM    770  CB  LYS A 114     -51.120  30.623 -25.632  1.00 46.45           C  
ANISOU  770  CB  LYS A 114     4430   6193   7024    868    -31   -254       C  
ATOM    771  CG  LYS A 114     -51.623  30.113 -24.291  1.00 48.20           C  
ANISOU  771  CG  LYS A 114     4594   6430   7289    843     52   -285       C  
ATOM    772  CD  LYS A 114     -52.535  31.126 -23.613  1.00 57.40           C  
ANISOU  772  CD  LYS A 114     5720   7578   8513    929    108   -284       C  
ATOM    773  CE  LYS A 114     -53.802  31.363 -24.418  1.00 51.62           C  
ANISOU  773  CE  LYS A 114     4880   6895   7839   1002     48   -264       C  
ATOM    774  NZ  LYS A 114     -54.743  32.288 -23.727  1.00 41.18           N  
ANISOU  774  NZ  LYS A 114     3508   5559   6578   1091    107   -265       N  
ATOM    775  N   ARG A 115     -49.395  30.538 -28.344  1.00 55.59           N  
ANISOU  775  N   ARG A 115     5734   7336   8051    823   -195   -210       N  
ATOM    776  CA  ARG A 115     -49.158  30.054 -29.701  1.00 49.19           C  
ANISOU  776  CA  ARG A 115     4933   6554   7203    798   -284   -194       C  
ATOM    777  C   ARG A 115     -47.893  29.208 -29.760  1.00 52.29           C  
ANISOU  777  C   ARG A 115     5394   6940   7535    707   -279   -212       C  
ATOM    778  O   ARG A 115     -47.892  28.106 -30.320  1.00 56.06           O  
ANISOU  778  O   ARG A 115     5839   7460   8001    652   -324   -221       O  
ATOM    779  CB  ARG A 115     -49.048  31.232 -30.671  1.00 51.57           C  
ANISOU  779  CB  ARG A 115     5300   6819   7477    866   -331   -156       C  
ATOM    780  CG  ARG A 115     -50.367  31.769 -31.200  1.00 60.97           C  
ANISOU  780  CG  ARG A 115     6410   8038   8717    956   -382   -130       C  
ATOM    781  CD  ARG A 115     -50.192  32.332 -32.604  1.00 65.59           C  
ANISOU  781  CD  ARG A 115     7054   8610   9256    993   -464    -92       C  
ATOM    782  NE  ARG A 115     -49.524  33.628 -32.597  1.00 71.20           N  
ANISOU  782  NE  ARG A 115     7882   9240   9930   1039   -432    -71       N  
ATOM    783  CZ  ARG A 115     -48.858  34.133 -33.627  1.00 75.28           C  
ANISOU  783  CZ  ARG A 115     8497   9724  10385   1043   -476    -44       C  
ATOM    784  NH1 ARG A 115     -48.750  33.476 -34.771  1.00 84.34           N  
ANISOU  784  NH1 ARG A 115     9640  10909  11494   1009   -556    -34       N  
ATOM    785  NH2 ARG A 115     -48.284  35.327 -33.507  1.00 67.29           N  
ANISOU  785  NH2 ARG A 115     7592   8633   9343   1080   -436    -27       N  
ATOM    786  N   LEU A 116     -46.804  29.713 -29.177  1.00 44.59           N  
ANISOU  786  N   LEU A 116     4512   5909   6519    690   -223   -220       N  
ATOM    787  CA  LEU A 116     -45.532  28.998 -29.217  1.00 39.67           C  
ANISOU  787  CA  LEU A 116     3954   5280   5839    612   -217   -238       C  
ATOM    788  C   LEU A 116     -45.601  27.686 -28.447  1.00 37.59           C  
ANISOU  788  C   LEU A 116     3637   5052   5592    550   -188   -268       C  
ATOM    789  O   LEU A 116     -45.091  26.660 -28.913  1.00 38.36           O  
ANISOU  789  O   LEU A 116     3742   5173   5660    491   -219   -278       O  
ATOM    790  CB  LEU A 116     -44.421  29.889 -28.664  1.00 39.38           C  
ANISOU  790  CB  LEU A 116     4019   5182   5761    609   -161   -242       C  
ATOM    791  CG  LEU A 116     -43.034  29.262 -28.528  1.00 34.60           C  
ANISOU  791  CG  LEU A 116     3477   4571   5099    533   -145   -264       C  
ATOM    792  CD1 LEU A 116     -42.501  28.846 -29.890  1.00 37.50           C  
ANISOU  792  CD1 LEU A 116     3874   4955   5421    504   -213   -252       C  
ATOM    793  CD2 LEU A 116     -42.080  30.229 -27.846  1.00 28.49           C  
ANISOU  793  CD2 LEU A 116     2790   3743   4292    532    -86   -272       C  
ATOM    794  N   ASN A 117     -46.228  27.696 -27.267  1.00 49.84           N  
ANISOU  794  N   ASN A 117     5140   6605   7191    563   -127   -282       N  
ATOM    795  CA  ASN A 117     -46.297  26.484 -26.456  1.00 42.29           C  
ANISOU  795  CA  ASN A 117     4144   5676   6248    504    -93   -310       C  
ATOM    796  C   ASN A 117     -47.081  25.388 -27.166  1.00 47.58           C  
ANISOU  796  C   ASN A 117     4732   6402   6942    476   -149   -311       C  
ATOM    797  O   ASN A 117     -46.716  24.209 -27.096  1.00 45.26           O  
ANISOU  797  O   ASN A 117     4440   6127   6631    410   -150   -329       O  
ATOM    798  CB  ASN A 117     -46.913  26.798 -25.094  1.00 45.68           C  
ANISOU  798  CB  ASN A 117     4540   6095   6723    528    -14   -323       C  
ATOM    799  CG  ASN A 117     -45.879  27.240 -24.077  1.00 60.58           C  
ANISOU  799  CG  ASN A 117     6513   7934   8572    513     53   -337       C  
ATOM    800  OD1 ASN A 117     -45.662  26.575 -23.064  1.00 68.71           O  
ANISOU  800  OD1 ASN A 117     7544   8965   9597    472    104   -359       O  
ATOM    801  ND2 ASN A 117     -45.230  28.368 -24.345  1.00 62.76           N  
ANISOU  801  ND2 ASN A 117     6864   8167   8817    544     52   -325       N  
ATOM    802  N   THR A 118     -48.167  25.756 -27.850  1.00 44.04           N  
ANISOU  802  N   THR A 118     4214   5983   6535    524   -196   -294       N  
ATOM    803  CA  THR A 118     -48.882  24.785 -28.671  1.00 36.65           C  
ANISOU  803  CA  THR A 118     3204   5105   5617    494   -260   -296       C  
ATOM    804  C   THR A 118     -47.994  24.264 -29.795  1.00 38.56           C  
ANISOU  804  C   THR A 118     3507   5347   5796    450   -322   -291       C  
ATOM    805  O   THR A 118     -47.995  23.064 -30.093  1.00 43.01           O  
ANISOU  805  O   THR A 118     4050   5942   6351    388   -345   -307       O  
ATOM    806  CB  THR A 118     -50.156  25.411 -29.240  1.00 39.73           C  
ANISOU  806  CB  THR A 118     3509   5529   6058    562   -307   -277       C  
ATOM    807  OG1 THR A 118     -51.020  25.801 -28.165  1.00 45.73           O  
ANISOU  807  OG1 THR A 118     4203   6292   6881    601   -243   -286       O  
ATOM    808  CG2 THR A 118     -50.887  24.422 -30.137  1.00 28.73           C  
ANISOU  808  CG2 THR A 118     2037   4200   4680    526   -379   -282       C  
ATOM    809  N   ILE A 119     -47.223  25.154 -30.424  1.00 39.05           N  
ANISOU  809  N   ILE A 119     3652   5374   5813    480   -344   -270       N  
ATOM    810  CA  ILE A 119     -46.299  24.735 -31.475  1.00 37.87           C  
ANISOU  810  CA  ILE A 119     3568   5220   5600    439   -394   -266       C  
ATOM    811  C   ILE A 119     -45.240  23.796 -30.910  1.00 35.67           C  
ANISOU  811  C   ILE A 119     3337   4930   5287    369   -352   -293       C  
ATOM    812  O   ILE A 119     -44.910  22.771 -31.518  1.00 39.37           O  
ANISOU  812  O   ILE A 119     3813   5419   5728    316   -385   -303       O  
ATOM    813  CB  ILE A 119     -45.668  25.967 -32.151  1.00 35.33           C  
ANISOU  813  CB  ILE A 119     3330   4858   5237    484   -414   -240       C  
ATOM    814  CG1 ILE A 119     -46.718  26.720 -32.971  1.00 42.48           C  
ANISOU  814  CG1 ILE A 119     4193   5779   6168    554   -474   -210       C  
ATOM    815  CG2 ILE A 119     -44.500  25.557 -33.034  1.00 40.20           C  
ANISOU  815  CG2 ILE A 119     4026   5465   5783    435   -444   -241       C  
ATOM    816  CD1 ILE A 119     -46.251  28.070 -33.468  1.00 47.54           C  
ANISOU  816  CD1 ILE A 119     4919   6371   6775    609   -482   -180       C  
ATOM    817  N   LEU A 120     -44.694  24.128 -29.736  1.00 42.76           N  
ANISOU  817  N   LEU A 120     4269   5795   6184    370   -279   -304       N  
ATOM    818  CA  LEU A 120     -43.724  23.243 -29.098  1.00 40.49           C  
ANISOU  818  CA  LEU A 120     4022   5498   5865    312   -239   -328       C  
ATOM    819  C   LEU A 120     -44.347  21.895 -28.757  1.00 47.09           C  
ANISOU  819  C   LEU A 120     4794   6369   6728    266   -234   -347       C  
ATOM    820  O   LEU A 120     -43.739  20.844 -28.993  1.00 53.29           O  
ANISOU  820  O   LEU A 120     5606   7161   7482    213   -245   -360       O  
ATOM    821  CB  LEU A 120     -43.162  23.900 -27.837  1.00 33.26           C  
ANISOU  821  CB  LEU A 120     3147   4545   4945    325   -165   -337       C  
ATOM    822  CG  LEU A 120     -42.335  25.173 -28.010  1.00 36.07           C  
ANISOU  822  CG  LEU A 120     3581   4860   5266    355   -156   -325       C  
ATOM    823  CD1 LEU A 120     -41.948  25.741 -26.654  1.00 41.58           C  
ANISOU  823  CD1 LEU A 120     4308   5525   5964    363    -81   -338       C  
ATOM    824  CD2 LEU A 120     -41.100  24.903 -28.854  1.00 39.12           C  
ANISOU  824  CD2 LEU A 120     4034   5241   5589    318   -187   -326       C  
ATOM    825  N   ASN A 121     -45.561  21.906 -28.200  1.00 56.20           N  
ANISOU  825  N   ASN A 121     5867   7543   7942    284   -215   -349       N  
ATOM    826  CA  ASN A 121     -46.227  20.655 -27.849  1.00 59.90           C  
ANISOU  826  CA  ASN A 121     6275   8044   8440    235   -204   -368       C  
ATOM    827  C   ASN A 121     -46.541  19.830 -29.090  1.00 59.60           C  
ANISOU  827  C   ASN A 121     6209   8041   8393    201   -278   -369       C  
ATOM    828  O   ASN A 121     -46.347  18.609 -29.096  1.00 57.01           O  
ANISOU  828  O   ASN A 121     5887   7723   8051    140   -277   -387       O  
ATOM    829  CB  ASN A 121     -47.505  20.943 -27.061  1.00 62.00           C  
ANISOU  829  CB  ASN A 121     6454   8328   8774    264   -167   -372       C  
ATOM    830  CG  ASN A 121     -47.226  21.515 -25.685  1.00 70.30           C  
ANISOU  830  CG  ASN A 121     7535   9343   9831    284    -83   -378       C  
ATOM    831  OD1 ASN A 121     -46.141  21.336 -25.134  1.00 66.62           O  
ANISOU  831  OD1 ASN A 121     7145   8846   9321    260    -49   -386       O  
ATOM    832  ND2 ASN A 121     -48.209  22.211 -25.124  1.00 71.08           N  
ANISOU  832  ND2 ASN A 121     7573   9448   9984    331    -50   -376       N  
ATOM    833  N   THR A 122     -47.033  20.479 -30.148  1.00 45.00           N  
ANISOU  833  N   THR A 122     4335   6212   6550    239   -343   -349       N  
ATOM    834  CA  THR A 122     -47.365  19.752 -31.370  1.00 44.55           C  
ANISOU  834  CA  THR A 122     4255   6192   6482    206   -418   -350       C  
ATOM    835  C   THR A 122     -46.121  19.146 -32.006  1.00 47.70           C  
ANISOU  835  C   THR A 122     4742   6571   6812    162   -437   -355       C  
ATOM    836  O   THR A 122     -46.136  17.986 -32.432  1.00 41.83           O  
ANISOU  836  O   THR A 122     3994   5846   6055    104   -460   -372       O  
ATOM    837  CB  THR A 122     -48.076  20.676 -32.358  1.00 42.42           C  
ANISOU  837  CB  THR A 122     3949   5944   6224    264   -487   -324       C  
ATOM    838  OG1 THR A 122     -49.127  21.379 -31.685  1.00 53.48           O  
ANISOU  838  OG1 THR A 122     5271   7358   7689    318   -462   -318       O  
ATOM    839  CG2 THR A 122     -48.671  19.870 -33.503  1.00 43.62           C  
ANISOU  839  CG2 THR A 122     4057   6145   6372    227   -566   -328       C  
ATOM    840  N   MET A 123     -45.031  19.915 -32.076  1.00 49.18           N  
ANISOU  840  N   MET A 123     5011   6719   6955    186   -425   -344       N  
ATOM    841  CA  MET A 123     -43.792  19.389 -32.640  1.00 39.10           C  
ANISOU  841  CA  MET A 123     3816   5425   5616    147   -436   -351       C  
ATOM    842  C   MET A 123     -43.254  18.233 -31.807  1.00 39.88           C  
ANISOU  842  C   MET A 123     3932   5515   5707     96   -386   -377       C  
ATOM    843  O   MET A 123     -42.795  17.224 -32.356  1.00 44.60           O  
ANISOU  843  O   MET A 123     4557   6118   6272     49   -406   -390       O  
ATOM    844  CB  MET A 123     -42.749  20.501 -32.752  1.00 36.76           C  
ANISOU  844  CB  MET A 123     3597   5091   5280    181   -422   -336       C  
ATOM    845  CG  MET A 123     -43.041  21.519 -33.839  1.00 44.44           C  
ANISOU  845  CG  MET A 123     4580   6064   6240    225   -479   -309       C  
ATOM    846  SD  MET A 123     -41.554  22.346 -34.435  1.00 45.71           S  
ANISOU  846  SD  MET A 123     4854   6184   6331    231   -476   -298       S  
ATOM    847  CE  MET A 123     -40.874  22.967 -32.900  1.00 36.53           C  
ANISOU  847  CE  MET A 123     3718   4983   5178    244   -387   -309       C  
ATOM    848  N   SER A 124     -43.294  18.365 -30.479  1.00 46.07           N  
ANISOU  848  N   SER A 124     4705   6284   6517    105   -320   -384       N  
ATOM    849  CA  SER A 124     -42.854  17.275 -29.615  1.00 50.19           C  
ANISOU  849  CA  SER A 124     5244   6795   7030     61   -272   -405       C  
ATOM    850  C   SER A 124     -43.739  16.046 -29.784  1.00 56.87           C  
ANISOU  850  C   SER A 124     6037   7668   7901     13   -287   -419       C  
ATOM    851  O   SER A 124     -43.241  14.916 -29.844  1.00 54.46           O  
ANISOU  851  O   SER A 124     5767   7357   7569    -34   -282   -435       O  
ATOM    852  CB  SER A 124     -42.843  17.737 -28.158  1.00 45.31           C  
ANISOU  852  CB  SER A 124     4625   6158   6434     82   -201   -408       C  
ATOM    853  OG  SER A 124     -42.335  16.726 -27.305  1.00 52.61           O  
ANISOU  853  OG  SER A 124     5578   7069   7342     44   -157   -425       O  
ATOM    854  N   THR A 125     -45.058  16.247 -29.857  1.00 54.64           N  
ANISOU  854  N   THR A 125     5672   7417   7672     23   -303   -416       N  
ATOM    855  CA  THR A 125     -45.969  15.124 -30.053  1.00 56.06           C  
ANISOU  855  CA  THR A 125     5795   7628   7879    -29   -318   -432       C  
ATOM    856  C   THR A 125     -45.771  14.481 -31.419  1.00 53.73           C  
ANISOU  856  C   THR A 125     5520   7347   7546    -64   -387   -436       C  
ATOM    857  O   THR A 125     -45.808  13.251 -31.543  1.00 53.46           O  
ANISOU  857  O   THR A 125     5493   7315   7502   -124   -386   -456       O  
ATOM    858  CB  THR A 125     -47.417  15.584 -29.886  1.00 53.05           C  
ANISOU  858  CB  THR A 125     5309   7283   7563     -7   -324   -429       C  
ATOM    859  OG1 THR A 125     -47.497  16.542 -28.823  1.00 63.28           O  
ANISOU  859  OG1 THR A 125     6597   8562   8886     43   -267   -421       O  
ATOM    860  CG2 THR A 125     -48.315  14.400 -29.563  1.00 47.94           C  
ANISOU  860  CG2 THR A 125     4602   6662   6950    -70   -306   -453       C  
ATOM    861  N   ILE A 126     -45.567  15.295 -32.457  1.00 40.41           N  
ANISOU  861  N   ILE A 126     3850   5667   5837    -29   -444   -418       N  
ATOM    862  CA  ILE A 126     -45.347  14.756 -33.796  1.00 35.58           C  
ANISOU  862  CA  ILE A 126     3266   5068   5184    -61   -510   -421       C  
ATOM    863  C   ILE A 126     -44.084  13.905 -33.825  1.00 40.65           C  
ANISOU  863  C   ILE A 126     3996   5678   5772    -98   -486   -436       C  
ATOM    864  O   ILE A 126     -44.046  12.842 -34.454  1.00 46.62           O  
ANISOU  864  O   ILE A 126     4768   6440   6506   -150   -510   -453       O  
ATOM    865  CB  ILE A 126     -45.296  15.898 -34.829  1.00 36.33           C  
ANISOU  865  CB  ILE A 126     3374   5171   5259    -11   -570   -395       C  
ATOM    866  CG1 ILE A 126     -46.704  16.420 -35.118  1.00 41.57           C  
ANISOU  866  CG1 ILE A 126     3942   5878   5972     19   -614   -383       C  
ATOM    867  CG2 ILE A 126     -44.656  15.438 -36.120  1.00 33.63           C  
ANISOU  867  CG2 ILE A 126     3093   4829   4856    -41   -623   -398       C  
ATOM    868  CD1 ILE A 126     -46.727  17.614 -36.044  1.00 37.27           C  
ANISOU  868  CD1 ILE A 126     3414   5337   5409     79   -672   -353       C  
ATOM    869  N   TYR A 127     -43.031  14.354 -33.140  1.00 45.70           N  
ANISOU  869  N   TYR A 127     4692   6283   6390    -73   -438   -431       N  
ATOM    870  CA  TYR A 127     -41.797  13.577 -33.089  1.00 42.69           C  
ANISOU  870  CA  TYR A 127     4386   5873   5960   -100   -414   -445       C  
ATOM    871  C   TYR A 127     -41.991  12.281 -32.310  1.00 49.83           C  
ANISOU  871  C   TYR A 127     5285   6770   6878   -146   -373   -466       C  
ATOM    872  O   TYR A 127     -41.605  11.202 -32.773  1.00 55.94           O  
ANISOU  872  O   TYR A 127     6098   7536   7622   -187   -382   -482       O  
ATOM    873  CB  TYR A 127     -40.683  14.420 -32.468  1.00 42.77           C  
ANISOU  873  CB  TYR A 127     4447   5856   5947    -61   -374   -437       C  
ATOM    874  CG  TYR A 127     -39.329  13.747 -32.443  1.00 39.87           C  
ANISOU  874  CG  TYR A 127     4153   5467   5531    -80   -353   -450       C  
ATOM    875  CD1 TYR A 127     -38.448  13.880 -33.507  1.00 39.24           C  
ANISOU  875  CD1 TYR A 127     4124   5383   5402    -81   -384   -450       C  
ATOM    876  CD2 TYR A 127     -38.929  12.986 -31.352  1.00 41.17           C  
ANISOU  876  CD2 TYR A 127     4334   5614   5695    -94   -300   -464       C  
ATOM    877  CE1 TYR A 127     -37.209  13.271 -33.487  1.00 37.08           C  
ANISOU  877  CE1 TYR A 127     3910   5094   5087    -94   -362   -464       C  
ATOM    878  CE2 TYR A 127     -37.693  12.373 -31.324  1.00 41.68           C  
ANISOU  878  CE2 TYR A 127     4460   5661   5715   -102   -284   -475       C  
ATOM    879  CZ  TYR A 127     -36.837  12.518 -32.394  1.00 42.64           C  
ANISOU  879  CZ  TYR A 127     4624   5783   5794   -101   -314   -477       C  
ATOM    880  OH  TYR A 127     -35.601  11.912 -32.368  1.00 36.62           O  
ANISOU  880  OH  TYR A 127     3916   5007   4990   -106   -295   -490       O  
ATOM    881  N   SER A 128     -42.592  12.367 -31.122  1.00 46.74           N  
ANISOU  881  N   SER A 128     4853   6378   6530   -139   -325   -466       N  
ATOM    882  CA  SER A 128     -42.660  11.200 -30.248  1.00 39.88           C  
ANISOU  882  CA  SER A 128     3993   5493   5667   -180   -276   -484       C  
ATOM    883  C   SER A 128     -43.700  10.191 -30.718  1.00 47.48           C  
ANISOU  883  C   SER A 128     4911   6476   6652   -237   -299   -500       C  
ATOM    884  O   SER A 128     -43.527   8.985 -30.508  1.00 58.10           O  
ANISOU  884  O   SER A 128     6291   7801   7983   -283   -275   -516       O  
ATOM    885  CB  SER A 128     -42.950  11.637 -28.813  1.00 46.80           C  
ANISOU  885  CB  SER A 128     4846   6360   6577   -158   -213   -480       C  
ATOM    886  OG  SER A 128     -43.884  12.701 -28.785  1.00 57.24           O  
ANISOU  886  OG  SER A 128     6098   7706   7944   -123   -224   -468       O  
ATOM    887  N   THR A 129     -44.782  10.652 -31.342  1.00 39.91           N  
ANISOU  887  N   THR A 129     3878   5557   5728   -235   -344   -495       N  
ATOM    888  CA  THR A 129     -45.841   9.769 -31.809  1.00 39.95           C  
ANISOU  888  CA  THR A 129     3831   5591   5758   -293   -370   -513       C  
ATOM    889  C   THR A 129     -45.817   9.550 -33.315  1.00 44.04           C  
ANISOU  889  C   THR A 129     4360   6128   6244   -314   -447   -517       C  
ATOM    890  O   THR A 129     -46.619   8.759 -33.822  1.00 55.34           O  
ANISOU  890  O   THR A 129     5756   7585   7688   -370   -476   -535       O  
ATOM    891  CB  THR A 129     -47.213  10.315 -31.396  1.00 38.36           C  
ANISOU  891  CB  THR A 129     3523   5429   5624   -282   -367   -510       C  
ATOM    892  OG1 THR A 129     -47.569  11.412 -32.248  1.00 40.87           O  
ANISOU  892  OG1 THR A 129     3800   5780   5950   -234   -430   -492       O  
ATOM    893  CG2 THR A 129     -47.189  10.784 -29.947  1.00 41.28           C  
ANISOU  893  CG2 THR A 129     3885   5778   6021   -250   -291   -504       C  
ATOM    894  N   GLY A 130     -44.931  10.228 -34.040  1.00 69.23           N  
ANISOU  894  N   GLY A 130     7603   9310   9392   -276   -480   -502       N  
ATOM    895  CA  GLY A 130     -44.854  10.071 -35.479  1.00 68.56           C  
ANISOU  895  CA  GLY A 130     7540   9242   9270   -294   -551   -504       C  
ATOM    896  C   GLY A 130     -44.530   8.657 -35.904  1.00 71.16           C  
ANISOU  896  C   GLY A 130     7920   9554   9565   -360   -550   -530       C  
ATOM    897  O   GLY A 130     -43.541   8.071 -35.452  1.00 69.68           O  
ANISOU  897  O   GLY A 130     7802   9325   9348   -366   -504   -538       O  
ATOM    898  N   LYS A 131     -45.362   8.100 -36.778  1.00 56.27           N  
ANISOU  898  N   LYS A 131     6000   7699   7681   -409   -603   -545       N  
ATOM    899  CA  LYS A 131     -45.213   6.729 -37.234  1.00 52.35           C  
ANISOU  899  CA  LYS A 131     5550   7186   7154   -480   -604   -574       C  
ATOM    900  C   LYS A 131     -45.176   6.703 -38.753  1.00 52.71           C  
ANISOU  900  C   LYS A 131     5621   7253   7156   -497   -681   -578       C  
ATOM    901  O   LYS A 131     -45.697   7.601 -39.420  1.00 56.38           O  
ANISOU  901  O   LYS A 131     6040   7757   7626   -468   -741   -562       O  
ATOM    902  CB  LYS A 131     -46.359   5.840 -36.730  1.00 56.09           C  
ANISOU  902  CB  LYS A 131     5963   7676   7673   -544   -585   -597       C  
ATOM    903  CG  LYS A 131     -47.741   6.449 -36.926  1.00 69.30           C  
ANISOU  903  CG  LYS A 131     7521   9411   9397   -542   -632   -593       C  
ATOM    904  CD  LYS A 131     -48.795   5.378 -37.164  1.00 80.94           C  
ANISOU  904  CD  LYS A 131     8947  10913  10893   -630   -647   -625       C  
ATOM    905  CE  LYS A 131     -49.944   5.910 -38.010  1.00 87.09           C  
ANISOU  905  CE  LYS A 131     9628  11764  11697   -632   -729   -624       C  
ATOM    906  NZ  LYS A 131     -49.489   6.365 -39.354  1.00 75.11           N  
ANISOU  906  NZ  LYS A 131     8154  10259  10126   -608   -808   -612       N  
ATOM    907  N   VAL A 132     -44.544   5.666 -39.293  1.00 43.26           N  
ANISOU  907  N   VAL A 132     4500   6026   5910   -543   -677   -601       N  
ATOM    908  CA  VAL A 132     -44.559   5.396 -40.723  1.00 44.38           C  
ANISOU  908  CA  VAL A 132     4673   6184   6005   -575   -744   -612       C  
ATOM    909  C   VAL A 132     -44.826   3.912 -40.927  1.00 54.94           C  
ANISOU  909  C   VAL A 132     6039   7506   7330   -659   -734   -649       C  
ATOM    910  O   VAL A 132     -44.341   3.070 -40.164  1.00 53.58           O  
ANISOU  910  O   VAL A 132     5913   7288   7157   -677   -668   -662       O  
ATOM    911  CB  VAL A 132     -43.248   5.826 -41.414  1.00 41.06           C  
ANISOU  911  CB  VAL A 132     4340   5738   5524   -536   -750   -601       C  
ATOM    912  CG1 VAL A 132     -42.068   4.989 -40.934  1.00 37.78           C  
ANISOU  912  CG1 VAL A 132     4008   5266   5079   -542   -682   -616       C  
ATOM    913  CG2 VAL A 132     -43.407   5.716 -42.915  1.00 60.06           C  
ANISOU  913  CG2 VAL A 132     6773   8167   7882   -566   -823   -610       C  
ATOM    914  N   CYS A 133     -45.621   3.599 -41.944  1.00 72.17           N  
ANISOU  914  N   CYS A 133     8196   9725   9500   -711   -800   -666       N  
ATOM    915  CA  CYS A 133     -46.032   2.236 -42.238  1.00 76.57           C  
ANISOU  915  CA  CYS A 133     8775  10272  10046   -800   -798   -705       C  
ATOM    916  C   CYS A 133     -45.384   1.776 -43.537  1.00 82.99           C  
ANISOU  916  C   CYS A 133     9677  11069  10786   -826   -836   -721       C  
ATOM    917  O   CYS A 133     -45.203   2.570 -44.468  1.00 80.63           O  
ANISOU  917  O   CYS A 133     9386  10797  10454   -794   -895   -705       O  
ATOM    918  CB  CYS A 133     -47.557   2.143 -42.325  1.00 80.99           C  
ANISOU  918  CB  CYS A 133     9228  10892  10652   -852   -843   -718       C  
ATOM    919  SG  CYS A 133     -48.404   3.214 -41.128  1.00 88.37           S  
ANISOU  919  SG  CYS A 133    10040  11866  11671   -795   -822   -690       S  
ATOM    920  N   ASN A 134     -45.028   0.494 -43.592  1.00116.83           N  
ANISOU  920  N   ASN A 134    14037  15310  15044   -884   -799   -753       N  
ATOM    921  CA  ASN A 134     -44.214  -0.017 -44.681  1.00121.40           C  
ANISOU  921  CA  ASN A 134    14715  15860  15551   -903   -815   -771       C  
ATOM    922  C   ASN A 134     -44.993  -0.037 -45.998  1.00132.41           C  
ANISOU  922  C   ASN A 134    16091  17303  16916   -955   -904   -787       C  
ATOM    923  O   ASN A 134     -46.226  -0.051 -46.004  1.00134.78           O  
ANISOU  923  O   ASN A 134    16304  17652  17252   -998   -945   -795       O  
ATOM    924  CB  ASN A 134     -43.669  -1.404 -44.312  1.00122.41           C  
ANISOU  924  CB  ASN A 134    14928  15921  15660   -947   -747   -800       C  
ATOM    925  CG  ASN A 134     -44.698  -2.525 -44.444  1.00133.15           C  
ANISOU  925  CG  ASN A 134    16275  17284  17032  -1047   -754   -838       C  
ATOM    926  OD1 ASN A 134     -45.406  -2.631 -45.433  1.00140.84           O  
ANISOU  926  OD1 ASN A 134    17229  18298  17987  -1101   -822   -857       O  
ATOM    927  ND2 ASN A 134     -44.773  -3.371 -43.424  1.00127.92           N  
ANISOU  927  ND2 ASN A 134    15628  16579  16398  -1074   -684   -850       N  
ATOM    928  N   PRO A 135     -44.288  -0.014 -47.128  1.00119.27           N  
ANISOU  928  N   PRO A 135    14505  15629  15184   -952   -935   -792       N  
ATOM    929  CA  PRO A 135     -44.962  -0.124 -48.427  1.00126.76           C  
ANISOU  929  CA  PRO A 135    15450  16620  16092  -1006  -1020   -809       C  
ATOM    930  C   PRO A 135     -45.516  -1.522 -48.655  1.00131.64           C  
ANISOU  930  C   PRO A 135    16093  17224  16701  -1108  -1016   -857       C  
ATOM    931  O   PRO A 135     -45.114  -2.493 -48.013  1.00131.00           O  
ANISOU  931  O   PRO A 135    16064  17085  16626  -1134   -942   -878       O  
ATOM    932  CB  PRO A 135     -43.854   0.208 -49.434  1.00124.34           C  
ANISOU  932  CB  PRO A 135    15240  16292  15712   -972  -1033   -803       C  
ATOM    933  CG  PRO A 135     -42.579  -0.043 -48.697  1.00110.70           C  
ANISOU  933  CG  PRO A 135    13580  14500  13982   -929   -942   -799       C  
ATOM    934  CD  PRO A 135     -42.858   0.310 -47.271  1.00101.64           C  
ANISOU  934  CD  PRO A 135    12357  13353  12908   -891   -897   -777       C  
ATOM    935  N   ASP A 136     -46.475  -1.598 -49.583  1.00170.92           N  
ANISOU  935  N   ASP A 136    21030  22253  21659  -1167  -1099   -875       N  
ATOM    936  CA  ASP A 136     -47.236  -2.808 -49.935  1.00182.13           C  
ANISOU  936  CA  ASP A 136    22457  23676  23069  -1277  -1113   -924       C  
ATOM    937  C   ASP A 136     -47.809  -3.523 -48.709  1.00178.14           C  
ANISOU  937  C   ASP A 136    21904  23152  22630  -1319  -1048   -939       C  
ATOM    938  O   ASP A 136     -48.214  -4.687 -48.799  1.00170.93           O  
ANISOU  938  O   ASP A 136    21019  22218  21708  -1412  -1032   -982       O  
ATOM    939  CB  ASP A 136     -46.421  -3.790 -50.798  1.00185.14           C  
ANISOU  939  CB  ASP A 136    22974  24000  23372  -1323  -1095   -958       C  
ATOM    940  CG  ASP A 136     -45.184  -4.324 -50.102  1.00184.80           C  
ANISOU  940  CG  ASP A 136    23023  23870  23322  -1286   -994   -958       C  
ATOM    941  OD1 ASP A 136     -45.293  -5.348 -49.395  1.00183.68           O  
ANISOU  941  OD1 ASP A 136    22904  23683  23202  -1333   -932   -982       O  
ATOM    942  OD2 ASP A 136     -44.106  -3.713 -50.253  1.00176.01           O1-
ANISOU  942  OD2 ASP A 136    21959  22736  22180  -1210   -976   -933       O1-
ATOM    943  N   ASN A 137     -47.863  -2.838 -47.564  1.00154.56           N  
ANISOU  943  N   ASN A 137    18848  20171  19706  -1255  -1009   -906       N  
ATOM    944  CA  ASN A 137     -48.526  -3.322 -46.359  1.00153.05           C  
ANISOU  944  CA  ASN A 137    18598  19973  19581  -1289   -951   -916       C  
ATOM    945  C   ASN A 137     -48.786  -2.143 -45.423  1.00147.30           C  
ANISOU  945  C   ASN A 137    17771  19280  18917  -1207   -942   -874       C  
ATOM    946  O   ASN A 137     -47.990  -1.900 -44.507  1.00137.68           O  
ANISOU  946  O   ASN A 137    16584  18016  17713  -1144   -873   -850       O  
ATOM    947  CB  ASN A 137     -47.682  -4.413 -45.689  1.00151.82           C  
ANISOU  947  CB  ASN A 137    18548  19727  19411  -1307   -854   -932       C  
ATOM    948  CG  ASN A 137     -48.357  -5.030 -44.477  1.00148.86           C  
ANISOU  948  CG  ASN A 137    18130  19336  19096  -1352   -790   -943       C  
ATOM    949  OD1 ASN A 137     -48.698  -4.340 -43.518  1.00139.56           O  
ANISOU  949  OD1 ASN A 137    16869  18182  17975  -1307   -768   -917       O  
ATOM    950  ND2 ASN A 137     -48.553  -6.341 -44.517  1.00145.09           N  
ANISOU  950  ND2 ASN A 137    17712  18814  18602  -1444   -756   -984       N  
ATOM    951  N   PRO A 138     -49.863  -1.359 -45.630  1.00118.08           N  
ANISOU  951  N   PRO A 138    13951  15659  15253  -1201  -1010   -863       N  
ATOM    952  CA  PRO A 138     -50.114  -0.215 -44.736  1.00110.50           C  
ANISOU  952  CA  PRO A 138    12902  14729  14355  -1119   -997   -824       C  
ATOM    953  C   PRO A 138     -50.480  -0.618 -43.314  1.00101.49           C  
ANISOU  953  C   PRO A 138    11718  13566  13277  -1136   -913   -829       C  
ATOM    954  O   PRO A 138     -50.718   0.243 -42.460  1.00 87.57           O  
ANISOU  954  O   PRO A 138     9883  11822  11566  -1074   -891   -801       O  
ATOM    955  CB  PRO A 138     -51.273   0.523 -45.419  1.00103.12           C  
ANISOU  955  CB  PRO A 138    11853  13886  13442  -1119  -1095   -819       C  
ATOM    956  CG  PRO A 138     -51.239   0.076 -46.837  1.00106.71           C  
ANISOU  956  CG  PRO A 138    12363  14355  13827  -1172  -1169   -842       C  
ATOM    957  CD  PRO A 138     -50.761  -1.348 -46.797  1.00115.95           C  
ANISOU  957  CD  PRO A 138    13634  15459  14964  -1254  -1110   -882       C  
ATOM    958  N   GLN A 139     -50.521  -1.925 -43.048  1.00117.04           N  
ANISOU  958  N   GLN A 139    13738  15492  15239  -1221   -862   -865       N  
ATOM    959  CA  GLN A 139     -50.905  -2.408 -41.725  1.00119.73           C  
ANISOU  959  CA  GLN A 139    14050  15809  15634  -1248   -779   -872       C  
ATOM    960  C   GLN A 139     -49.800  -2.158 -40.703  1.00111.66           C  
ANISOU  960  C   GLN A 139    13093  14721  14611  -1169   -699   -842       C  
ATOM    961  O   GLN A 139     -50.017  -1.493 -39.683  1.00 98.84           O  
ANISOU  961  O   GLN A 139    11407  13109  13038  -1120   -663   -818       O  
ATOM    962  CB  GLN A 139     -51.253  -3.897 -41.792  1.00115.12           C  
ANISOU  962  CB  GLN A 139    13514  15190  15036  -1364   -747   -919       C  
ATOM    963  CG  GLN A 139     -52.636  -4.192 -42.348  1.00117.50           C  
ANISOU  963  CG  GLN A 139    13718  15565  15363  -1457   -806   -954       C  
ATOM    964  CD  GLN A 139     -53.741  -3.845 -41.367  1.00125.93           C  
ANISOU  964  CD  GLN A 139    14653  16683  16513  -1467   -781   -951       C  
ATOM    965  OE1 GLN A 139     -54.100  -4.651 -40.508  1.00129.44           O  
ANISOU  965  OE1 GLN A 139    15099  17096  16985  -1530   -706   -972       O  
ATOM    966  NE2 GLN A 139     -54.287  -2.641 -41.493  1.00115.09           N  
ANISOU  966  NE2 GLN A 139    13167  15385  15176  -1403   -839   -926       N  
ATOM    967  N   GLU A 140     -48.604  -2.682 -40.962  1.00109.15           N  
ANISOU  967  N   GLU A 140    12900  14337  14236  -1156   -672   -844       N  
ATOM    968  CA  GLU A 140     -47.504  -2.601 -40.006  1.00 99.78           C  
ANISOU  968  CA  GLU A 140    11779  13088  13042  -1088   -598   -820       C  
ATOM    969  C   GLU A 140     -46.885  -1.211 -40.069  1.00 94.13           C  
ANISOU  969  C   GLU A 140    11044  12397  12326   -985   -624   -781       C  
ATOM    970  O   GLU A 140     -46.267  -0.841 -41.073  1.00 88.72           O  
ANISOU  970  O   GLU A 140    10400  11717  11594   -958   -672   -775       O  
ATOM    971  CB  GLU A 140     -46.466  -3.681 -40.297  1.00105.38           C  
ANISOU  971  CB  GLU A 140    12624  13723  13693  -1108   -561   -839       C  
ATOM    972  CG  GLU A 140     -45.155  -3.506 -39.543  1.00107.01           C  
ANISOU  972  CG  GLU A 140    12901  13874  13882  -1026   -501   -813       C  
ATOM    973  CD  GLU A 140     -44.126  -4.558 -39.911  1.00109.71           C  
ANISOU  973  CD  GLU A 140    13371  14146  14166  -1036   -469   -832       C  
ATOM    974  OE1 GLU A 140     -44.509  -5.737 -40.066  1.00101.61           O  
ANISOU  974  OE1 GLU A 140    12391  13087  13129  -1116   -450   -864       O  
ATOM    975  OE2 GLU A 140     -42.936  -4.205 -40.047  1.00 92.22           O1-
ANISOU  975  OE2 GLU A 140    11212  11908  11917   -966   -461   -815       O1-
ATOM    976  N   CYS A 141     -47.046  -0.441 -38.998  1.00103.16           N  
ANISOU  976  N   CYS A 141    12127  13551  13517   -932   -590   -755       N  
ATOM    977  CA  CYS A 141     -46.457   0.883 -38.879  1.00 95.18           C  
ANISOU  977  CA  CYS A 141    11101  12555  12508   -837   -603   -718       C  
ATOM    978  C   CYS A 141     -45.347   0.856 -37.836  1.00 87.34           C  
ANISOU  978  C   CYS A 141    10174  11505  11507   -785   -528   -702       C  
ATOM    979  O   CYS A 141     -45.321   0.001 -36.946  1.00 90.69           O  
ANISOU  979  O   CYS A 141    10628  11888  11941   -814   -464   -713       O  
ATOM    980  CB  CYS A 141     -47.516   1.926 -38.505  1.00 92.47           C  
ANISOU  980  CB  CYS A 141    10636  12273  12226   -809   -628   -700       C  
ATOM    981  SG  CYS A 141     -48.945   1.966 -39.618  1.00117.39           S  
ANISOU  981  SG  CYS A 141    13694  15509  15400   -866   -722   -719       S  
ATOM    982  N   LEU A 142     -44.420   1.803 -37.957  1.00 49.69           N  
ANISOU  982  N   LEU A 142     5430   6733   6716   -709   -537   -677       N  
ATOM    983  CA  LEU A 142     -43.243   1.845 -37.101  1.00 48.69           C  
ANISOU  983  CA  LEU A 142     5367   6560   6574   -656   -476   -663       C  
ATOM    984  C   LEU A 142     -43.048   3.250 -36.554  1.00 40.00           C  
ANISOU  984  C   LEU A 142     4220   5481   5497   -581   -474   -631       C  
ATOM    985  O   LEU A 142     -43.078   4.225 -37.311  1.00 36.15           O  
ANISOU  985  O   LEU A 142     3707   5027   5002   -549   -526   -617       O  
ATOM    986  CB  LEU A 142     -41.990   1.406 -37.867  1.00 44.98           C  
ANISOU  986  CB  LEU A 142     4995   6054   6040   -646   -479   -671       C  
ATOM    987  CG  LEU A 142     -41.734  -0.100 -37.955  1.00 43.45           C  
ANISOU  987  CG  LEU A 142     4879   5811   5818   -700   -446   -700       C  
ATOM    988  CD1 LEU A 142     -40.455  -0.377 -38.728  1.00 38.24           C  
ANISOU  988  CD1 LEU A 142     4311   5122   5098   -677   -449   -707       C  
ATOM    989  CD2 LEU A 142     -41.677  -0.724 -36.571  1.00 50.00           C  
ANISOU  989  CD2 LEU A 142     5727   6600   6671   -701   -373   -699       C  
ATOM    990  N   LEU A 143     -42.849   3.347 -35.243  1.00 44.28           N  
ANISOU  990  N   LEU A 143     4760   6002   6064   -553   -412   -621       N  
ATOM    991  CA  LEU A 143     -42.426   4.591 -34.626  1.00 40.59           C  
ANISOU  991  CA  LEU A 143     4270   5542   5609   -482   -399   -594       C  
ATOM    992  C   LEU A 143     -40.923   4.776 -34.816  1.00 44.18           C  
ANISOU  992  C   LEU A 143     4804   5969   6013   -437   -389   -587       C  
ATOM    993  O   LEU A 143     -40.218   3.893 -35.311  1.00 49.28           O  
ANISOU  993  O   LEU A 143     5520   6587   6618   -457   -386   -603       O  
ATOM    994  CB  LEU A 143     -42.776   4.604 -33.139  1.00 37.26           C  
ANISOU  994  CB  LEU A 143     3820   5109   5228   -473   -335   -588       C  
ATOM    995  CG  LEU A 143     -44.251   4.705 -32.750  1.00 41.01           C  
ANISOU  995  CG  LEU A 143     4202   5618   5762   -504   -334   -591       C  
ATOM    996  CD1 LEU A 143     -44.421   4.466 -31.257  1.00 35.74           C  
ANISOU  996  CD1 LEU A 143     3531   4927   5122   -504   -258   -589       C  
ATOM    997  CD2 LEU A 143     -44.818   6.058 -33.145  1.00 41.15           C  
ANISOU  997  CD2 LEU A 143     4144   5684   5809   -461   -380   -573       C  
ATOM    998  N   LEU A 144     -40.427   5.950 -34.423  1.00 46.31           N  
ANISOU  998  N   LEU A 144     5063   6247   6287   -378   -382   -566       N  
ATOM    999  CA  LEU A 144     -38.983   6.157 -34.419  1.00 43.55           C  
ANISOU  999  CA  LEU A 144     4778   5874   5894   -338   -365   -561       C  
ATOM   1000  C   LEU A 144     -38.314   5.271 -33.376  1.00 46.52           C  
ANISOU 1000  C   LEU A 144     5203   6212   6260   -336   -305   -569       C  
ATOM   1001  O   LEU A 144     -37.343   4.566 -33.674  1.00 50.23           O  
ANISOU 1001  O   LEU A 144     5739   6657   6690   -334   -295   -580       O  
ATOM   1002  CB  LEU A 144     -38.658   7.626 -34.164  1.00 42.62           C  
ANISOU 1002  CB  LEU A 144     4637   5772   5784   -281   -368   -539       C  
ATOM   1003  CG  LEU A 144     -37.161   7.926 -34.101  1.00 45.74           C  
ANISOU 1003  CG  LEU A 144     5091   6151   6137   -244   -348   -537       C  
ATOM   1004  CD1 LEU A 144     -36.527   7.803 -35.478  1.00 44.62           C  
ANISOU 1004  CD1 LEU A 144     4994   6011   5949   -254   -385   -545       C  
ATOM   1005  CD2 LEU A 144     -36.923   9.301 -33.522  1.00 39.39           C  
ANISOU 1005  CD2 LEU A 144     4264   5356   5346   -197   -336   -518       C  
ATOM   1006  N   GLU A 145     -38.825   5.293 -32.147  1.00 49.27           N  
ANISOU 1006  N   GLU A 145     5522   6555   6644   -332   -264   -562       N  
ATOM   1007  CA  GLU A 145     -38.345   4.423 -31.085  1.00 51.03           C  
ANISOU 1007  CA  GLU A 145     5791   6740   6857   -332   -208   -567       C  
ATOM   1008  C   GLU A 145     -39.430   3.415 -30.741  1.00 53.59           C  
ANISOU 1008  C   GLU A 145     6103   7052   7209   -390   -187   -579       C  
ATOM   1009  O   GLU A 145     -40.540   3.819 -30.364  1.00 55.26           O  
ANISOU 1009  O   GLU A 145     6245   7286   7464   -406   -184   -575       O  
ATOM   1010  CB  GLU A 145     -37.957   5.233 -29.849  1.00 37.32           C  
ANISOU 1010  CB  GLU A 145     4046   5004   5132   -284   -170   -550       C  
ATOM   1011  CG  GLU A 145     -37.463   4.389 -28.684  1.00 50.58           C  
ANISOU 1011  CG  GLU A 145     5776   6646   6796   -278   -116   -551       C  
ATOM   1012  CD  GLU A 145     -36.148   3.693 -28.981  1.00 56.16           C  
ANISOU 1012  CD  GLU A 145     6556   7327   7453   -258   -114   -559       C  
ATOM   1013  OE1 GLU A 145     -35.301   4.289 -29.680  1.00 55.13           O  
ANISOU 1013  OE1 GLU A 145     6434   7213   7298   -230   -142   -559       O  
ATOM   1014  OE2 GLU A 145     -35.961   2.549 -28.516  1.00 57.74           O1-
ANISOU 1014  OE2 GLU A 145     6809   7491   7638   -270    -83   -565       O1-
ATOM   1015  N   PRO A 146     -39.167   2.105 -30.848  1.00 37.92           N  
ANISOU 1015  N   PRO A 146     4181   5030   5198   -423   -169   -594       N  
ATOM   1016  CA  PRO A 146     -37.879   1.556 -31.275  1.00 46.65           C  
ANISOU 1016  CA  PRO A 146     5365   6106   6252   -400   -168   -601       C  
ATOM   1017  C   PRO A 146     -37.794   1.274 -32.773  1.00 48.03           C  
ANISOU 1017  C   PRO A 146     5558   6289   6402   -427   -217   -617       C  
ATOM   1018  O   PRO A 146     -36.720   0.931 -33.264  1.00 45.26           O  
ANISOU 1018  O   PRO A 146     5267   5920   6010   -405   -218   -624       O  
ATOM   1019  CB  PRO A 146     -37.801   0.252 -30.488  1.00 38.22           C  
ANISOU 1019  CB  PRO A 146     4360   4989   5175   -421   -117   -608       C  
ATOM   1020  CG  PRO A 146     -39.229  -0.210 -30.449  1.00 40.67           C  
ANISOU 1020  CG  PRO A 146     4629   5302   5522   -490   -113   -619       C  
ATOM   1021  CD  PRO A 146     -40.090   1.041 -30.413  1.00 37.67           C  
ANISOU 1021  CD  PRO A 146     4152   4976   5187   -484   -138   -608       C  
ATOM   1022  N   GLY A 147     -38.912   1.427 -33.481  1.00 51.74           N  
ANISOU 1022  N   GLY A 147     5974   6788   6895   -472   -256   -624       N  
ATOM   1023  CA  GLY A 147     -39.035   0.956 -34.848  1.00 55.31           C  
ANISOU 1023  CA  GLY A 147     6448   7246   7322   -513   -300   -643       C  
ATOM   1024  C   GLY A 147     -37.982   1.424 -35.831  1.00 52.87           C  
ANISOU 1024  C   GLY A 147     6176   6944   6970   -477   -331   -642       C  
ATOM   1025  O   GLY A 147     -37.174   0.622 -36.309  1.00 59.70           O  
ANISOU 1025  O   GLY A 147     7113   7778   7794   -480   -321   -658       O  
ATOM   1026  N   LEU A 148     -37.979   2.720 -36.148  1.00 39.64           N  
ANISOU 1026  N   LEU A 148     4454   5306   5301   -443   -365   -624       N  
ATOM   1027  CA  LEU A 148     -37.058   3.219 -37.164  1.00 34.44           C  
ANISOU 1027  CA  LEU A 148     3830   4656   4600   -417   -393   -624       C  
ATOM   1028  C   LEU A 148     -35.629   3.295 -36.643  1.00 34.28           C  
ANISOU 1028  C   LEU A 148     3857   4613   4553   -365   -352   -620       C  
ATOM   1029  O   LEU A 148     -34.680   3.131 -37.419  1.00 35.26           O  
ANISOU 1029  O   LEU A 148     4032   4730   4635   -354   -357   -630       O  
ATOM   1030  CB  LEU A 148     -37.519   4.585 -37.666  1.00 39.18           C  
ANISOU 1030  CB  LEU A 148     4374   5299   5213   -397   -440   -604       C  
ATOM   1031  CG  LEU A 148     -38.783   4.604 -38.527  1.00 38.51           C  
ANISOU 1031  CG  LEU A 148     4244   5245   5142   -442   -498   -608       C  
ATOM   1032  CD1 LEU A 148     -38.859   5.894 -39.326  1.00 36.91           C  
ANISOU 1032  CD1 LEU A 148     4016   5077   4930   -411   -550   -588       C  
ATOM   1033  CD2 LEU A 148     -38.829   3.397 -39.450  1.00 41.89           C  
ANISOU 1033  CD2 LEU A 148     4722   5658   5536   -499   -515   -637       C  
ATOM   1034  N   ASN A 149     -35.454   3.546 -35.344  1.00 35.09           N  
ANISOU 1034  N   ASN A 149     3943   4709   4680   -333   -312   -607       N  
ATOM   1035  CA  ASN A 149     -34.111   3.572 -34.775  1.00 34.68           C  
ANISOU 1035  CA  ASN A 149     3932   4642   4604   -284   -276   -605       C  
ATOM   1036  C   ASN A 149     -33.442   2.208 -34.886  1.00 38.38           C  
ANISOU 1036  C   ASN A 149     4471   5072   5041   -291   -251   -625       C  
ATOM   1037  O   ASN A 149     -32.243   2.118 -35.172  1.00 44.62           O  
ANISOU 1037  O   ASN A 149     5301   5856   5797   -258   -241   -632       O  
ATOM   1038  CB  ASN A 149     -34.163   4.029 -33.318  1.00 35.34           C  
ANISOU 1038  CB  ASN A 149     3986   4726   4717   -254   -240   -589       C  
ATOM   1039  CG  ASN A 149     -34.279   5.534 -33.185  1.00 33.13           C  
ANISOU 1039  CG  ASN A 149     3654   4478   4454   -226   -256   -571       C  
ATOM   1040  OD1 ASN A 149     -33.823   6.282 -34.050  1.00 38.52           O  
ANISOU 1040  OD1 ASN A 149     4339   5180   5118   -214   -284   -569       O  
ATOM   1041  ND2 ASN A 149     -34.891   5.986 -32.097  1.00 29.40           N  
ANISOU 1041  ND2 ASN A 149     3142   4011   4019   -217   -234   -558       N  
ATOM   1042  N   GLU A 150     -34.205   1.135 -34.665  1.00 48.07           N  
ANISOU 1042  N   GLU A 150     5714   6271   6280   -333   -237   -635       N  
ATOM   1043  CA  GLU A 150     -33.654  -0.209 -34.807  1.00 47.67           C  
ANISOU 1043  CA  GLU A 150     5738   6175   6198   -341   -212   -653       C  
ATOM   1044  C   GLU A 150     -33.194  -0.467 -36.236  1.00 44.21           C  
ANISOU 1044  C   GLU A 150     5339   5738   5722   -355   -239   -673       C  
ATOM   1045  O   GLU A 150     -32.159  -1.106 -36.457  1.00 44.65           O  
ANISOU 1045  O   GLU A 150     5455   5767   5743   -330   -218   -685       O  
ATOM   1046  CB  GLU A 150     -34.693  -1.245 -34.377  1.00 40.43           C  
ANISOU 1046  CB  GLU A 150     4833   5226   5301   -396   -192   -661       C  
ATOM   1047  CG  GLU A 150     -34.122  -2.613 -34.049  1.00 49.59           C  
ANISOU 1047  CG  GLU A 150     6078   6329   6436   -392   -150   -673       C  
ATOM   1048  CD  GLU A 150     -33.914  -3.467 -35.282  1.00 47.58           C  
ANISOU 1048  CD  GLU A 150     5882   6050   6146   -424   -163   -700       C  
ATOM   1049  OE1 GLU A 150     -34.776  -3.427 -36.186  1.00 49.38           O  
ANISOU 1049  OE1 GLU A 150     6087   6296   6379   -482   -200   -713       O  
ATOM   1050  OE2 GLU A 150     -32.887  -4.175 -35.352  1.00 47.48           O1-
ANISOU 1050  OE2 GLU A 150     5939   6002   6099   -389   -138   -709       O1-
ATOM   1051  N   ILE A 151     -33.957   0.015 -37.219  1.00 36.99           N  
ANISOU 1051  N   ILE A 151     4392   4853   4811   -394   -287   -676       N  
ATOM   1052  CA  ILE A 151     -33.564  -0.148 -38.617  1.00 32.41           C  
ANISOU 1052  CA  ILE A 151     3851   4274   4189   -411   -315   -694       C  
ATOM   1053  C   ILE A 151     -32.272   0.609 -38.896  1.00 36.04           C  
ANISOU 1053  C   ILE A 151     4323   4750   4621   -356   -310   -689       C  
ATOM   1054  O   ILE A 151     -31.310   0.056 -39.440  1.00 36.15           O  
ANISOU 1054  O   ILE A 151     4395   4745   4597   -342   -294   -706       O  
ATOM   1055  CB  ILE A 151     -34.696   0.316 -39.549  1.00 32.02           C  
ANISOU 1055  CB  ILE A 151     3760   4260   4148   -460   -373   -695       C  
ATOM   1056  CG1 ILE A 151     -35.855  -0.682 -39.529  1.00 37.26           C  
ANISOU 1056  CG1 ILE A 151     4422   4907   4829   -528   -378   -711       C  
ATOM   1057  CG2 ILE A 151     -34.175   0.512 -40.964  1.00 32.37           C  
ANISOU 1057  CG2 ILE A 151     3842   4314   4144   -466   -406   -707       C  
ATOM   1058  CD1 ILE A 151     -37.102  -0.172 -40.213  1.00 37.56           C  
ANISOU 1058  CD1 ILE A 151     4398   4988   4885   -573   -438   -710       C  
ATOM   1059  N   MET A 152     -32.226   1.886 -38.512  1.00 38.04           N  
ANISOU 1059  N   MET A 152     4522   5037   4893   -325   -321   -666       N  
ATOM   1060  CA  MET A 152     -31.061   2.710 -38.812  1.00 34.68           C  
ANISOU 1060  CA  MET A 152     4104   4629   4442   -282   -316   -663       C  
ATOM   1061  C   MET A 152     -29.829   2.285 -38.027  1.00 33.17           C  
ANISOU 1061  C   MET A 152     3941   4421   4240   -234   -268   -668       C  
ATOM   1062  O   MET A 152     -28.708   2.601 -38.439  1.00 38.89           O  
ANISOU 1062  O   MET A 152     4684   5157   4936   -206   -258   -676       O  
ATOM   1063  CB  MET A 152     -31.377   4.179 -38.532  1.00 32.76           C  
ANISOU 1063  CB  MET A 152     3802   4422   4223   -264   -336   -638       C  
ATOM   1064  CG  MET A 152     -32.519   4.729 -39.366  1.00 33.11           C  
ANISOU 1064  CG  MET A 152     3816   4489   4277   -299   -389   -629       C  
ATOM   1065  SD  MET A 152     -32.269   4.470 -41.131  1.00 30.54           S  
ANISOU 1065  SD  MET A 152     3542   4164   3896   -331   -425   -648       S  
ATOM   1066  CE  MET A 152     -30.970   5.656 -41.454  1.00 29.60           C  
ANISOU 1066  CE  MET A 152     3438   4063   3747   -288   -413   -639       C  
ATOM   1067  N   ALA A 153     -30.008   1.571 -36.918  1.00 41.23           N  
ANISOU 1067  N   ALA A 153     4967   5417   5282   -225   -238   -665       N  
ATOM   1068  CA  ALA A 153     -28.890   1.168 -36.078  1.00 37.59           C  
ANISOU 1068  CA  ALA A 153     4531   4942   4810   -174   -198   -667       C  
ATOM   1069  C   ALA A 153     -28.346  -0.212 -36.414  1.00 42.16           C  
ANISOU 1069  C   ALA A 153     5180   5481   5360   -170   -175   -688       C  
ATOM   1070  O   ALA A 153     -27.186  -0.496 -36.095  1.00 46.63           O  
ANISOU 1070  O   ALA A 153     5768   6041   5907   -119   -148   -694       O  
ATOM   1071  CB  ALA A 153     -29.304   1.193 -34.603  1.00 39.67           C  
ANISOU 1071  CB  ALA A 153     4769   5198   5104   -158   -177   -648       C  
ATOM   1072  N   ASN A 154     -29.142  -1.074 -37.045  1.00 41.80           N  
ANISOU 1072  N   ASN A 154     5167   5406   5310   -220   -184   -702       N  
ATOM   1073  CA  ASN A 154     -28.745  -2.468 -37.197  1.00 36.52           C  
ANISOU 1073  CA  ASN A 154     4572   4687   4616   -218   -155   -722       C  
ATOM   1074  C   ASN A 154     -28.819  -2.955 -38.639  1.00 41.92           C  
ANISOU 1074  C   ASN A 154     5300   5359   5269   -258   -172   -748       C  
ATOM   1075  O   ASN A 154     -28.010  -3.793 -39.052  1.00 55.81           O  
ANISOU 1075  O   ASN A 154     7121   7088   6997   -238   -147   -768       O  
ATOM   1076  CB  ASN A 154     -29.611  -3.351 -36.297  1.00 42.47           C  
ANISOU 1076  CB  ASN A 154     5344   5400   5392   -243   -135   -716       C  
ATOM   1077  CG  ASN A 154     -29.483  -2.985 -34.832  1.00 39.36           C  
ANISOU 1077  CG  ASN A 154     4920   5012   5022   -202   -113   -692       C  
ATOM   1078  OD1 ASN A 154     -30.430  -2.495 -34.217  1.00 49.03           O  
ANISOU 1078  OD1 ASN A 154     6097   6251   6281   -227   -120   -676       O  
ATOM   1079  ND2 ASN A 154     -28.304  -3.217 -34.265  1.00 35.94           N  
ANISOU 1079  ND2 ASN A 154     4513   4570   4571   -136    -86   -689       N  
ATOM   1080  N   SER A 155     -29.785  -2.456 -39.407  1.00 31.15           N  
ANISOU 1080  N   SER A 155     3906   4018   3910   -314   -215   -748       N  
ATOM   1081  CA  SER A 155     -29.957  -2.927 -40.776  1.00 36.47           C  
ANISOU 1081  CA  SER A 155     4624   4682   4549   -360   -235   -773       C  
ATOM   1082  C   SER A 155     -28.730  -2.602 -41.616  1.00 41.07           C  
ANISOU 1082  C   SER A 155     5233   5278   5093   -324   -229   -786       C  
ATOM   1083  O   SER A 155     -28.209  -1.485 -41.575  1.00 34.23           O  
ANISOU 1083  O   SER A 155     4325   4452   4229   -292   -237   -771       O  
ATOM   1084  CB  SER A 155     -31.203  -2.302 -41.404  1.00 32.83           C  
ANISOU 1084  CB  SER A 155     4118   4254   4102   -418   -290   -768       C  
ATOM   1085  OG  SER A 155     -31.285  -2.607 -42.786  1.00 39.08           O  
ANISOU 1085  OG  SER A 155     4952   5044   4853   -460   -317   -791       O  
ATOM   1086  N   LEU A 156     -28.260  -3.595 -42.366  1.00 46.14           N  
ANISOU 1086  N   LEU A 156     5948   5884   5698   -332   -209   -814       N  
ATOM   1087  CA  LEU A 156     -27.219  -3.400 -43.363  1.00 41.35           C  
ANISOU 1087  CA  LEU A 156     5373   5289   5050   -311   -201   -832       C  
ATOM   1088  C   LEU A 156     -27.784  -3.277 -44.770  1.00 45.25           C  
ANISOU 1088  C   LEU A 156     5890   5792   5510   -372   -241   -847       C  
ATOM   1089  O   LEU A 156     -27.020  -3.069 -45.718  1.00 51.82           O  
ANISOU 1089  O   LEU A 156     6752   6633   6302   -364   -235   -863       O  
ATOM   1090  CB  LEU A 156     -26.208  -4.549 -43.305  1.00 40.12           C  
ANISOU 1090  CB  LEU A 156     5284   5087   4871   -270   -149   -855       C  
ATOM   1091  CG  LEU A 156     -25.478  -4.720 -41.971  1.00 57.40           C  
ANISOU 1091  CG  LEU A 156     7457   7269   7084   -200   -112   -840       C  
ATOM   1092  CD1 LEU A 156     -25.176  -6.185 -41.694  1.00 58.87           C  
ANISOU 1092  CD1 LEU A 156     7719   7391   7259   -178    -70   -857       C  
ATOM   1093  CD2 LEU A 156     -24.204  -3.896 -41.948  1.00 44.52           C  
ANISOU 1093  CD2 LEU A 156     5791   5680   5445   -140    -97   -838       C  
ATOM   1094  N   ASP A 157     -29.101  -3.396 -44.924  1.00 33.36           N  
ANISOU 1094  N   ASP A 157     4371   4287   4019   -434   -280   -844       N  
ATOM   1095  CA  ASP A 157     -29.736  -3.309 -46.230  1.00 36.60           C  
ANISOU 1095  CA  ASP A 157     4802   4710   4395   -495   -326   -859       C  
ATOM   1096  C   ASP A 157     -29.887  -1.846 -46.628  1.00 36.98           C  
ANISOU 1096  C   ASP A 157     4794   4813   4443   -489   -371   -834       C  
ATOM   1097  O   ASP A 157     -30.497  -1.058 -45.897  1.00 37.13           O  
ANISOU 1097  O   ASP A 157     4743   4860   4505   -481   -392   -806       O  
ATOM   1098  CB  ASP A 157     -31.093  -4.005 -46.206  1.00 36.72           C  
ANISOU 1098  CB  ASP A 157     4816   4710   4426   -564   -354   -867       C  
ATOM   1099  CG  ASP A 157     -31.857  -3.827 -47.496  1.00 39.81           C  
ANISOU 1099  CG  ASP A 157     5217   5124   4785   -628   -413   -880       C  
ATOM   1100  OD1 ASP A 157     -31.544  -4.535 -48.476  1.00 45.02           O  
ANISOU 1100  OD1 ASP A 157     5952   5757   5394   -656   -407   -911       O  
ATOM   1101  OD2 ASP A 157     -32.773  -2.979 -47.531  1.00 45.30           O1-
ANISOU 1101  OD2 ASP A 157     5847   5864   5503   -649   -466   -858       O1-
ATOM   1102  N   TYR A 158     -29.338  -1.489 -47.790  1.00 33.51           N  
ANISOU 1102  N   TYR A 158     4392   4386   3955   -494   -381   -846       N  
ATOM   1103  CA  TYR A 158     -29.349  -0.098 -48.234  1.00 29.72           C  
ANISOU 1103  CA  TYR A 158     3875   3951   3468   -486   -417   -822       C  
ATOM   1104  C   TYR A 158     -30.772   0.429 -48.376  1.00 38.37           C  
ANISOU 1104  C   TYR A 158     4920   5074   4582   -526   -484   -802       C  
ATOM   1105  O   TYR A 158     -31.099   1.512 -47.875  1.00 39.75           O  
ANISOU 1105  O   TYR A 158     5032   5280   4790   -503   -505   -771       O  
ATOM   1106  CB  TYR A 158     -28.592   0.020 -49.558  1.00 31.59           C  
ANISOU 1106  CB  TYR A 158     4174   4189   3640   -494   -413   -841       C  
ATOM   1107  CG  TYR A 158     -28.458   1.425 -50.106  1.00 36.29           C  
ANISOU 1107  CG  TYR A 158     4749   4824   4217   -486   -443   -817       C  
ATOM   1108  CD1 TYR A 158     -29.470   1.997 -50.869  1.00 41.25           C  
ANISOU 1108  CD1 TYR A 158     5368   5475   4828   -525   -510   -803       C  
ATOM   1109  CD2 TYR A 158     -27.309   2.171 -49.879  1.00 30.36           C  
ANISOU 1109  CD2 TYR A 158     3988   4086   3463   -439   -402   -810       C  
ATOM   1110  CE1 TYR A 158     -29.347   3.275 -51.378  1.00 32.78           C  
ANISOU 1110  CE1 TYR A 158     4287   4431   3736   -513   -536   -778       C  
ATOM   1111  CE2 TYR A 158     -27.176   3.450 -50.388  1.00 37.07           C  
ANISOU 1111  CE2 TYR A 158     4828   4963   4293   -436   -424   -789       C  
ATOM   1112  CZ  TYR A 158     -28.198   3.996 -51.136  1.00 37.99           C  
ANISOU 1112  CZ  TYR A 158     4945   5097   4392   -471   -490   -772       C  
ATOM   1113  OH  TYR A 158     -28.070   5.270 -51.640  1.00 47.66           O  
ANISOU 1113  OH  TYR A 158     6170   6345   5595   -464   -510   -748       O  
ATOM   1114  N   ASN A 159     -31.637  -0.328 -49.055  1.00 43.59           N  
ANISOU 1114  N   ASN A 159     5609   5727   5226   -587   -518   -822       N  
ATOM   1115  CA  ASN A 159     -32.979   0.162 -49.350  1.00 42.82           C  
ANISOU 1115  CA  ASN A 159     5463   5665   5143   -627   -589   -806       C  
ATOM   1116  C   ASN A 159     -33.823   0.295 -48.088  1.00 40.02           C  
ANISOU 1116  C   ASN A 159     5028   5320   4858   -619   -591   -786       C  
ATOM   1117  O   ASN A 159     -34.603   1.246 -47.956  1.00 35.50           O  
ANISOU 1117  O   ASN A 159     4389   4786   4313   -614   -636   -759       O  
ATOM   1118  CB  ASN A 159     -33.660  -0.758 -50.363  1.00 47.06           C  
ANISOU 1118  CB  ASN A 159     6047   6192   5640   -699   -625   -838       C  
ATOM   1119  CG  ASN A 159     -33.114  -0.580 -51.766  1.00 52.62           C  
ANISOU 1119  CG  ASN A 159     6822   6899   6272   -712   -643   -851       C  
ATOM   1120  OD1 ASN A 159     -32.666   0.505 -52.137  1.00 47.94           O  
ANISOU 1120  OD1 ASN A 159     6223   6331   5660   -680   -655   -829       O  
ATOM   1121  ND2 ASN A 159     -33.146  -1.649 -52.554  1.00 59.85           N  
ANISOU 1121  ND2 ASN A 159     7810   7787   7143   -764   -641   -889       N  
ATOM   1122  N   GLU A 160     -33.693  -0.651 -47.154  1.00 39.77           N  
ANISOU 1122  N   GLU A 160     5004   5252   4853   -617   -541   -798       N  
ATOM   1123  CA  GLU A 160     -34.475  -0.581 -45.923  1.00 38.79           C  
ANISOU 1123  CA  GLU A 160     4811   5135   4793   -613   -535   -781       C  
ATOM   1124  C   GLU A 160     -34.106   0.651 -45.107  1.00 40.54           C  
ANISOU 1124  C   GLU A 160     4976   5382   5047   -550   -524   -746       C  
ATOM   1125  O   GLU A 160     -34.984   1.372 -44.618  1.00 42.69           O  
ANISOU 1125  O   GLU A 160     5175   5684   5360   -548   -552   -724       O  
ATOM   1126  CB  GLU A 160     -34.278  -1.852 -45.099  1.00 35.98           C  
ANISOU 1126  CB  GLU A 160     4491   4728   4450   -620   -478   -799       C  
ATOM   1127  CG  GLU A 160     -34.850  -1.752 -43.698  1.00 34.52           C  
ANISOU 1127  CG  GLU A 160     4245   4545   4326   -607   -457   -780       C  
ATOM   1128  CD  GLU A 160     -34.872  -3.081 -42.979  1.00 49.68           C  
ANISOU 1128  CD  GLU A 160     6209   6412   6256   -627   -406   -797       C  
ATOM   1129  OE1 GLU A 160     -34.068  -3.967 -43.338  1.00 52.25           O  
ANISOU 1129  OE1 GLU A 160     6615   6694   6543   -622   -374   -820       O  
ATOM   1130  OE2 GLU A 160     -35.689  -3.239 -42.047  1.00 47.17           O1-
ANISOU 1130  OE2 GLU A 160     5848   6093   5982   -645   -396   -789       O1-
ATOM   1131  N   ARG A 161     -32.805   0.908 -44.946  1.00 33.94           N  
ANISOU 1131  N   ARG A 161     4170   4534   4192   -498   -483   -744       N  
ATOM   1132  CA  ARG A 161     -32.376   2.128 -44.269  1.00 26.45           C  
ANISOU 1132  CA  ARG A 161     3174   3610   3267   -444   -473   -716       C  
ATOM   1133  C   ARG A 161     -32.808   3.362 -45.046  1.00 30.56           C  
ANISOU 1133  C   ARG A 161     3667   4169   3777   -446   -527   -695       C  
ATOM   1134  O   ARG A 161     -33.228   4.363 -44.455  1.00 33.94           O  
ANISOU 1134  O   ARG A 161     4035   4619   4240   -422   -540   -668       O  
ATOM   1135  CB  ARG A 161     -30.861   2.130 -44.080  1.00 30.80           C  
ANISOU 1135  CB  ARG A 161     3763   4147   3795   -396   -422   -723       C  
ATOM   1136  CG  ARG A 161     -30.294   0.863 -43.480  1.00 26.42           C  
ANISOU 1136  CG  ARG A 161     3248   3551   3240   -385   -371   -743       C  
ATOM   1137  CD  ARG A 161     -28.779   0.911 -43.492  1.00 26.38           C  
ANISOU 1137  CD  ARG A 161     3274   3541   3208   -336   -327   -752       C  
ATOM   1138  NE  ARG A 161     -28.278   2.075 -42.772  1.00 24.73           N  
ANISOU 1138  NE  ARG A 161     3014   3362   3020   -292   -318   -730       N  
ATOM   1139  CZ  ARG A 161     -28.175   2.149 -41.452  1.00 25.70           C  
ANISOU 1139  CZ  ARG A 161     3103   3484   3179   -258   -294   -716       C  
ATOM   1140  NH1 ARG A 161     -28.513   1.134 -40.674  1.00 26.85           N  
ANISOU 1140  NH1 ARG A 161     3260   3598   3344   -260   -273   -720       N  
ATOM   1141  NH2 ARG A 161     -27.721   3.270 -40.899  1.00 28.14           N  
ANISOU 1141  NH2 ARG A 161     3370   3821   3502   -224   -288   -698       N  
ATOM   1142  N   LEU A 162     -32.704   3.310 -46.377  1.00 33.57           N  
ANISOU 1142  N   LEU A 162     4095   4553   4106   -474   -558   -708       N  
ATOM   1143  CA  LEU A 162     -33.146   4.429 -47.201  1.00 31.89           C  
ANISOU 1143  CA  LEU A 162     3867   4373   3876   -476   -614   -687       C  
ATOM   1144  C   LEU A 162     -34.631   4.699 -47.006  1.00 33.67           C  
ANISOU 1144  C   LEU A 162     4025   4627   4142   -497   -668   -670       C  
ATOM   1145  O   LEU A 162     -35.054   5.859 -46.934  1.00 34.51           O  
ANISOU 1145  O   LEU A 162     4086   4759   4266   -470   -699   -641       O  
ATOM   1146  CB  LEU A 162     -32.836   4.150 -48.672  1.00 31.52           C  
ANISOU 1146  CB  LEU A 162     3892   4323   3760   -508   -637   -706       C  
ATOM   1147  CG  LEU A 162     -33.423   5.118 -49.702  1.00 24.80           C  
ANISOU 1147  CG  LEU A 162     3039   3504   2880   -519   -704   -686       C  
ATOM   1148  CD1 LEU A 162     -33.025   6.548 -49.391  1.00 26.09           C  
ANISOU 1148  CD1 LEU A 162     3177   3682   3055   -469   -699   -652       C  
ATOM   1149  CD2 LEU A 162     -32.986   4.735 -51.107  1.00 38.54           C  
ANISOU 1149  CD2 LEU A 162     4863   5236   4545   -552   -718   -708       C  
ATOM   1150  N   TRP A 163     -35.441   3.641 -46.920  1.00 36.60           N  
ANISOU 1150  N   TRP A 163     4387   4991   4528   -544   -679   -690       N  
ATOM   1151  CA  TRP A 163     -36.865   3.832 -46.669  1.00 38.55           C  
ANISOU 1151  CA  TRP A 163     4560   5269   4820   -566   -726   -679       C  
ATOM   1152  C   TRP A 163     -37.095   4.494 -45.317  1.00 39.07           C  
ANISOU 1152  C   TRP A 163     4555   5342   4949   -523   -699   -654       C  
ATOM   1153  O   TRP A 163     -37.757   5.532 -45.229  1.00 42.62           O  
ANISOU 1153  O   TRP A 163     4946   5824   5425   -500   -735   -627       O  
ATOM   1154  CB  TRP A 163     -37.604   2.496 -46.739  1.00 40.30           C  
ANISOU 1154  CB  TRP A 163     4787   5478   5046   -632   -732   -710       C  
ATOM   1155  CG  TRP A 163     -38.981   2.572 -46.152  1.00 42.02           C  
ANISOU 1155  CG  TRP A 163     4917   5727   5322   -655   -761   -702       C  
ATOM   1156  CD1 TRP A 163     -40.096   3.087 -46.746  1.00 45.39           C  
ANISOU 1156  CD1 TRP A 163     5287   6202   5757   -675   -834   -693       C  
ATOM   1157  CD2 TRP A 163     -39.385   2.138 -44.847  1.00 45.95           C  
ANISOU 1157  CD2 TRP A 163     5370   6212   5876   -657   -716   -703       C  
ATOM   1158  NE1 TRP A 163     -41.172   2.992 -45.896  1.00 47.25           N  
ANISOU 1158  NE1 TRP A 163     5439   6458   6056   -690   -835   -691       N  
ATOM   1159  CE2 TRP A 163     -40.761   2.414 -44.723  1.00 48.65           C  
ANISOU 1159  CE2 TRP A 163     5626   6597   6263   -683   -761   -697       C  
ATOM   1160  CE3 TRP A 163     -38.718   1.539 -43.774  1.00 43.50           C  
ANISOU 1160  CE3 TRP A 163     5086   5859   5583   -639   -642   -708       C  
ATOM   1161  CZ2 TRP A 163     -41.482   2.112 -43.570  1.00 52.01           C  
ANISOU 1161  CZ2 TRP A 163     5990   7022   6748   -695   -728   -697       C  
ATOM   1162  CZ3 TRP A 163     -39.436   1.240 -42.630  1.00 49.20           C  
ANISOU 1162  CZ3 TRP A 163     5755   6578   6360   -651   -613   -706       C  
ATOM   1163  CH2 TRP A 163     -40.803   1.527 -42.537  1.00 47.90           C  
ANISOU 1163  CH2 TRP A 163     5505   6455   6238   -681   -653   -701       C  
ATOM   1164  N   ALA A 164     -36.522   3.923 -44.253  1.00 36.29           N  
ANISOU 1164  N   ALA A 164     4212   4958   4617   -508   -634   -661       N  
ATOM   1165  CA  ALA A 164     -36.736   4.465 -42.915  1.00 35.32           C  
ANISOU 1165  CA  ALA A 164     4029   4840   4550   -471   -604   -640       C  
ATOM   1166  C   ALA A 164     -36.214   5.891 -42.807  1.00 36.22           C  
ANISOU 1166  C   ALA A 164     4128   4970   4665   -414   -605   -612       C  
ATOM   1167  O   ALA A 164     -36.818   6.735 -42.134  1.00 39.55           O  
ANISOU 1167  O   ALA A 164     4487   5410   5129   -388   -611   -589       O  
ATOM   1168  CB  ALA A 164     -36.069   3.568 -41.872  1.00 33.13           C  
ANISOU 1168  CB  ALA A 164     3781   4524   4284   -462   -535   -653       C  
ATOM   1169  N   TRP A 165     -35.087   6.175 -43.459  1.00 34.67           N  
ANISOU 1169  N   TRP A 165     3988   4764   4420   -396   -596   -615       N  
ATOM   1170  CA  TRP A 165     -34.549   7.530 -43.466  1.00 35.55           C  
ANISOU 1170  CA  TRP A 165     4094   4888   4526   -351   -595   -590       C  
ATOM   1171  C   TRP A 165     -35.469   8.485 -44.217  1.00 40.25           C  
ANISOU 1171  C   TRP A 165     4661   5512   5120   -351   -660   -568       C  
ATOM   1172  O   TRP A 165     -35.820   9.556 -43.708  1.00 38.96           O  
ANISOU 1172  O   TRP A 165     4453   5362   4988   -316   -666   -541       O  
ATOM   1173  CB  TRP A 165     -33.154   7.518 -44.089  1.00 33.35           C  
ANISOU 1173  CB  TRP A 165     3885   4595   4193   -342   -568   -603       C  
ATOM   1174  CG  TRP A 165     -32.420   8.810 -43.998  1.00 33.60           C  
ANISOU 1174  CG  TRP A 165     3918   4633   4216   -302   -554   -584       C  
ATOM   1175  CD1 TRP A 165     -31.490   9.160 -43.064  1.00 34.07           C  
ANISOU 1175  CD1 TRP A 165     3971   4686   4288   -268   -502   -582       C  
ATOM   1176  CD2 TRP A 165     -32.536   9.925 -44.888  1.00 33.49           C  
ANISOU 1176  CD2 TRP A 165     3916   4633   4174   -296   -592   -563       C  
ATOM   1177  NE1 TRP A 165     -31.025  10.427 -43.313  1.00 35.15           N  
ANISOU 1177  NE1 TRP A 165     4115   4831   4409   -247   -503   -565       N  
ATOM   1178  CE2 TRP A 165     -31.652  10.919 -44.427  1.00 28.43           C  
ANISOU 1178  CE2 TRP A 165     3280   3990   3534   -262   -555   -552       C  
ATOM   1179  CE3 TRP A 165     -33.304  10.182 -46.028  1.00 34.49           C  
ANISOU 1179  CE3 TRP A 165     4056   4775   4276   -317   -654   -553       C  
ATOM   1180  CZ2 TRP A 165     -31.516  12.146 -45.064  1.00 25.63           C  
ANISOU 1180  CZ2 TRP A 165     2945   3640   3153   -249   -574   -530       C  
ATOM   1181  CZ3 TRP A 165     -33.168  11.403 -46.658  1.00 40.05           C  
ANISOU 1181  CZ3 TRP A 165     4780   5485   4953   -298   -676   -529       C  
ATOM   1182  CH2 TRP A 165     -32.281  12.371 -46.175  1.00 34.65           C  
ANISOU 1182  CH2 TRP A 165     4104   4792   4269   -265   -634   -518       C  
ATOM   1183  N   GLU A 166     -35.870   8.113 -45.435  1.00 42.97           N  
ANISOU 1183  N   GLU A 166     5033   5867   5427   -388   -710   -577       N  
ATOM   1184  CA  GLU A 166     -36.726   8.985 -46.234  1.00 36.75           C  
ANISOU 1184  CA  GLU A 166     4223   5110   4632   -385   -779   -554       C  
ATOM   1185  C   GLU A 166     -38.139   9.049 -45.667  1.00 41.38           C  
ANISOU 1185  C   GLU A 166     4722   5722   5277   -388   -812   -544       C  
ATOM   1186  O   GLU A 166     -38.769  10.113 -45.676  1.00 45.90           O  
ANISOU 1186  O   GLU A 166     5251   6318   5871   -354   -847   -515       O  
ATOM   1187  CB  GLU A 166     -36.747   8.509 -47.687  1.00 39.01           C  
ANISOU 1187  CB  GLU A 166     4567   5401   4855   -426   -825   -570       C  
ATOM   1188  CG  GLU A 166     -37.804   9.175 -48.556  1.00 46.94           C  
ANISOU 1188  CG  GLU A 166     5546   6441   5849   -429   -909   -549       C  
ATOM   1189  CD  GLU A 166     -37.601  10.673 -48.686  1.00 48.11           C  
ANISOU 1189  CD  GLU A 166     5697   6593   5990   -374   -921   -511       C  
ATOM   1190  OE1 GLU A 166     -36.437  11.126 -48.643  1.00 44.78           O  
ANISOU 1190  OE1 GLU A 166     5326   6146   5542   -353   -874   -508       O  
ATOM   1191  OE2 GLU A 166     -38.608  11.398 -48.831  1.00 49.55           O1-
ANISOU 1191  OE2 GLU A 166     5831   6804   6194   -354   -978   -485       O1-
ATOM   1192  N   SER A 167     -38.655   7.921 -45.173  1.00 46.07           N  
ANISOU 1192  N   SER A 167     5291   6314   5901   -427   -798   -568       N  
ATOM   1193  CA  SER A 167     -40.010   7.900 -44.630  1.00 47.94           C  
ANISOU 1193  CA  SER A 167     5440   6580   6196   -438   -823   -563       C  
ATOM   1194  C   SER A 167     -40.136   8.814 -43.420  1.00 52.37           C  
ANISOU 1194  C   SER A 167     5944   7142   6811   -384   -788   -538       C  
ATOM   1195  O   SER A 167     -41.127   9.541 -43.280  1.00 61.45           O  
ANISOU 1195  O   SER A 167     7025   8323   8000   -363   -823   -518       O  
ATOM   1196  CB  SER A 167     -40.400   6.472 -44.256  1.00 47.87           C  
ANISOU 1196  CB  SER A 167     5425   6560   6203   -496   -800   -595       C  
ATOM   1197  OG  SER A 167     -40.888   5.757 -45.377  1.00 62.30           O  
ANISOU 1197  OG  SER A 167     7273   8401   7996   -554   -853   -617       O  
ATOM   1198  N   TRP A 168     -39.141   8.788 -42.531  1.00 42.88           N  
ANISOU 1198  N   TRP A 168     4772   5908   5613   -360   -720   -539       N  
ATOM   1199  CA  TRP A 168     -39.194   9.613 -41.329  1.00 39.55           C  
ANISOU 1199  CA  TRP A 168     4306   5485   5238   -314   -683   -519       C  
ATOM   1200  C   TRP A 168     -39.206  11.096 -41.678  1.00 40.96           C  
ANISOU 1200  C   TRP A 168     4475   5675   5412   -264   -712   -488       C  
ATOM   1201  O   TRP A 168     -39.906  11.887 -41.035  1.00 46.52           O  
ANISOU 1201  O   TRP A 168     5121   6393   6163   -230   -712   -469       O  
ATOM   1202  CB  TRP A 168     -38.011   9.282 -40.418  1.00 37.76           C  
ANISOU 1202  CB  TRP A 168     4120   5223   5004   -299   -611   -529       C  
ATOM   1203  CG  TRP A 168     -37.957  10.109 -39.171  1.00 34.65           C  
ANISOU 1203  CG  TRP A 168     3690   4825   4650   -255   -570   -511       C  
ATOM   1204  CD1 TRP A 168     -37.040  11.071 -38.868  1.00 30.15           C  
ANISOU 1204  CD1 TRP A 168     3144   4245   4067   -213   -544   -498       C  
ATOM   1205  CD2 TRP A 168     -38.854  10.043 -38.056  1.00 42.56           C  
ANISOU 1205  CD2 TRP A 168     4628   5833   5709   -253   -548   -508       C  
ATOM   1206  NE1 TRP A 168     -37.312  11.613 -37.635  1.00 29.39           N  
ANISOU 1206  NE1 TRP A 168     3006   4146   4015   -184   -509   -487       N  
ATOM   1207  CE2 TRP A 168     -38.421  10.999 -37.115  1.00 38.30           C  
ANISOU 1207  CE2 TRP A 168     4082   5285   5187   -206   -509   -492       C  
ATOM   1208  CE3 TRP A 168     -39.982   9.270 -37.761  1.00 44.47           C  
ANISOU 1208  CE3 TRP A 168     4820   6087   5989   -290   -553   -519       C  
ATOM   1209  CZ2 TRP A 168     -39.076  11.203 -35.902  1.00 41.58           C  
ANISOU 1209  CZ2 TRP A 168     4444   5702   5653   -192   -476   -486       C  
ATOM   1210  CZ3 TRP A 168     -40.631   9.475 -36.556  1.00 45.03           C  
ANISOU 1210  CZ3 TRP A 168     4835   6162   6113   -277   -518   -512       C  
ATOM   1211  CH2 TRP A 168     -40.176  10.434 -35.642  1.00 43.73           C  
ANISOU 1211  CH2 TRP A 168     4667   5987   5962   -226   -479   -496       C  
ATOM   1212  N   ARG A 169     -38.440  11.494 -42.693  1.00 40.99           N  
ANISOU 1212  N   ARG A 169     4542   5672   5359   -258   -732   -483       N  
ATOM   1213  CA  ARG A 169     -38.357  12.905 -43.051  1.00 46.76           C  
ANISOU 1213  CA  ARG A 169     5281   6407   6080   -213   -753   -453       C  
ATOM   1214  C   ARG A 169     -39.534  13.363 -43.904  1.00 46.64           C  
ANISOU 1214  C   ARG A 169     5230   6424   6068   -208   -831   -434       C  
ATOM   1215  O   ARG A 169     -39.878  14.550 -43.888  1.00 51.46           O  
ANISOU 1215  O   ARG A 169     5821   7039   6691   -160   -850   -405       O  
ATOM   1216  CB  ARG A 169     -37.040  13.181 -43.775  1.00 52.10           C  
ANISOU 1216  CB  ARG A 169     6042   7062   6692   -212   -738   -455       C  
ATOM   1217  CG  ARG A 169     -35.865  13.370 -42.832  1.00 45.35           C  
ANISOU 1217  CG  ARG A 169     5209   6181   5840   -193   -665   -462       C  
ATOM   1218  CD  ARG A 169     -34.555  12.960 -43.477  1.00 37.73           C  
ANISOU 1218  CD  ARG A 169     4318   5201   4818   -212   -640   -481       C  
ATOM   1219  NE  ARG A 169     -33.486  12.848 -42.492  1.00 40.56           N  
ANISOU 1219  NE  ARG A 169     4685   5544   5183   -198   -574   -494       N  
ATOM   1220  CZ  ARG A 169     -33.312  11.808 -41.689  1.00 42.61           C  
ANISOU 1220  CZ  ARG A 169     4930   5795   5463   -209   -539   -514       C  
ATOM   1221  NH1 ARG A 169     -34.111  10.754 -41.738  1.00 44.28           N  
ANISOU 1221  NH1 ARG A 169     5124   6010   5690   -238   -558   -526       N  
ATOM   1222  NH2 ARG A 169     -32.309  11.823 -40.815  1.00 38.64           N  
ANISOU 1222  NH2 ARG A 169     4436   5282   4963   -190   -485   -523       N  
ATOM   1223  N   SER A 170     -40.162  12.453 -44.649  1.00 44.43           N  
ANISOU 1223  N   SER A 170     4941   6165   5774   -254   -878   -452       N  
ATOM   1224  CA  SER A 170     -41.254  12.832 -45.535  1.00 44.21           C  
ANISOU 1224  CA  SER A 170     4879   6176   5744   -251   -961   -436       C  
ATOM   1225  C   SER A 170     -42.608  12.848 -44.841  1.00 48.91           C  
ANISOU 1225  C   SER A 170     5368   6805   6409   -243   -980   -432       C  
ATOM   1226  O   SER A 170     -43.476  13.645 -45.214  1.00 56.12           O  
ANISOU 1226  O   SER A 170     6237   7750   7338   -208  -1037   -408       O  
ATOM   1227  CB  SER A 170     -41.315  11.885 -46.737  1.00 37.32           C  
ANISOU 1227  CB  SER A 170     4047   5315   4817   -309  -1008   -459       C  
ATOM   1228  OG  SER A 170     -42.282  10.869 -46.534  1.00 53.33           O  
ANISOU 1228  OG  SER A 170     6015   7369   6880   -357  -1027   -483       O  
ATOM   1229  N   GLU A 171     -42.817  11.991 -43.843  1.00 53.10           N  
ANISOU 1229  N   GLU A 171     5858   7332   6984   -272   -932   -455       N  
ATOM   1230  CA  GLU A 171     -44.104  11.897 -43.173  1.00 61.68           C  
ANISOU 1230  CA  GLU A 171     6843   8453   8140   -274   -942   -456       C  
ATOM   1231  C   GLU A 171     -44.107  12.496 -41.774  1.00 59.51           C  
ANISOU 1231  C   GLU A 171     6528   8162   7920   -229   -877   -444       C  
ATOM   1232  O   GLU A 171     -45.186  12.698 -41.208  1.00 67.95           O  
ANISOU 1232  O   GLU A 171     7508   9260   9048   -216   -883   -440       O  
ATOM   1233  CB  GLU A 171     -44.559  10.432 -43.109  1.00 62.39           C  
ANISOU 1233  CB  GLU A 171     6914   8553   8240   -350   -937   -493       C  
ATOM   1234  CG  GLU A 171     -44.819   9.829 -44.481  1.00 60.08           C  
ANISOU 1234  CG  GLU A 171     6648   8283   7897   -400  -1008   -509       C  
ATOM   1235  CD  GLU A 171     -44.974   8.324 -44.442  1.00 71.60           C  
ANISOU 1235  CD  GLU A 171     8116   9736   9354   -481   -990   -549       C  
ATOM   1236  OE1 GLU A 171     -45.765   7.828 -43.613  1.00 77.53           O  
ANISOU 1236  OE1 GLU A 171     8798  10500  10160   -508   -966   -563       O  
ATOM   1237  OE2 GLU A 171     -44.301   7.637 -45.239  1.00 67.52           O1-
ANISOU 1237  OE2 GLU A 171     7680   9198   8778   -519   -997   -568       O1-
ATOM   1238  N   VAL A 172     -42.939  12.783 -41.207  1.00 49.49           N  
ANISOU 1238  N   VAL A 172     5319   6852   6634   -206   -816   -440       N  
ATOM   1239  CA  VAL A 172     -42.833  13.485 -39.938  1.00 44.24           C  
ANISOU 1239  CA  VAL A 172     4628   6170   6012   -162   -758   -428       C  
ATOM   1240  C   VAL A 172     -42.153  14.838 -40.104  1.00 38.45           C  
ANISOU 1240  C   VAL A 172     3938   5416   5255   -104   -755   -400       C  
ATOM   1241  O   VAL A 172     -42.606  15.835 -39.538  1.00 42.42           O  
ANISOU 1241  O   VAL A 172     4402   5921   5795    -53   -746   -379       O  
ATOM   1242  CB  VAL A 172     -42.094  12.620 -38.894  1.00 44.63           C  
ANISOU 1242  CB  VAL A 172     4704   6187   6064   -188   -683   -450       C  
ATOM   1243  CG1 VAL A 172     -42.277  13.189 -37.502  1.00 38.66           C  
ANISOU 1243  CG1 VAL A 172     3908   5422   5358   -151   -626   -441       C  
ATOM   1244  CG2 VAL A 172     -42.602  11.192 -38.953  1.00 51.54           C  
ANISOU 1244  CG2 VAL A 172     5562   7072   6947   -253   -686   -478       C  
ATOM   1245  N   GLY A 173     -41.069  14.891 -40.881  1.00 40.95           N  
ANISOU 1245  N   GLY A 173     4337   5712   5509   -111   -760   -400       N  
ATOM   1246  CA  GLY A 173     -40.395  16.158 -41.111  1.00 40.35           C  
ANISOU 1246  CA  GLY A 173     4310   5615   5407    -65   -755   -376       C  
ATOM   1247  C   GLY A 173     -41.263  17.161 -41.845  1.00 44.05           C  
ANISOU 1247  C   GLY A 173     4756   6102   5878    -24   -818   -345       C  
ATOM   1248  O   GLY A 173     -41.281  18.347 -41.504  1.00 44.87           O  
ANISOU 1248  O   GLY A 173     4861   6191   5996     28   -806   -320       O  
ATOM   1249  N   LYS A 174     -41.992  16.702 -42.868  1.00 46.99           N  
ANISOU 1249  N   LYS A 174     5112   6508   6236    -47   -889   -346       N  
ATOM   1250  CA  LYS A 174     -42.902  17.593 -43.582  1.00 45.60           C  
ANISOU 1250  CA  LYS A 174     4908   6355   6063     -4   -959   -315       C  
ATOM   1251  C   LYS A 174     -44.015  18.097 -42.675  1.00 48.80           C  
ANISOU 1251  C   LYS A 174     5218   6780   6543     40   -954   -303       C  
ATOM   1252  O   LYS A 174     -44.493  19.224 -42.848  1.00 56.59           O  
ANISOU 1252  O   LYS A 174     6192   7769   7541    102   -983   -272       O  
ATOM   1253  CB  LYS A 174     -43.490  16.886 -44.804  1.00 43.91           C  
ANISOU 1253  CB  LYS A 174     4689   6178   5816    -43  -1038   -323       C  
ATOM   1254  CG  LYS A 174     -42.486  16.610 -45.909  1.00 47.07           C  
ANISOU 1254  CG  LYS A 174     5190   6558   6134    -77  -1052   -330       C  
ATOM   1255  CD  LYS A 174     -43.187  16.217 -47.199  1.00 48.41           C  
ANISOU 1255  CD  LYS A 174     5360   6767   6268   -103  -1142   -330       C  
ATOM   1256  CE  LYS A 174     -42.192  15.774 -48.256  1.00 48.53           C  
ANISOU 1256  CE  LYS A 174     5478   6762   6200   -146  -1147   -343       C  
ATOM   1257  NZ  LYS A 174     -42.753  15.848 -49.633  1.00 63.15           N  
ANISOU 1257  NZ  LYS A 174     7351   8643   8000   -154  -1239   -332       N  
ATOM   1258  N   GLN A 175     -44.445  17.278 -41.711  1.00 35.25           N  
ANISOU 1258  N   GLN A 175     3437   5078   4879     11   -916   -328       N  
ATOM   1259  CA  GLN A 175     -45.396  17.750 -40.711  1.00 40.56           C  
ANISOU 1259  CA  GLN A 175     4021   5765   5624     51   -895   -320       C  
ATOM   1260  C   GLN A 175     -44.809  18.896 -39.899  1.00 44.96           C  
ANISOU 1260  C   GLN A 175     4611   6280   6191    108   -837   -301       C  
ATOM   1261  O   GLN A 175     -45.508  19.863 -39.572  1.00 52.96           O  
ANISOU 1261  O   GLN A 175     5580   7298   7243    168   -841   -279       O  
ATOM   1262  CB  GLN A 175     -45.800  16.604 -39.784  1.00 47.08           C  
ANISOU 1262  CB  GLN A 175     4788   6605   6494      0   -852   -352       C  
ATOM   1263  CG  GLN A 175     -46.736  15.579 -40.398  1.00 43.04           C  
ANISOU 1263  CG  GLN A 175     4219   6141   5992    -54   -907   -373       C  
ATOM   1264  CD  GLN A 175     -47.261  14.596 -39.369  1.00 46.46           C  
ANISOU 1264  CD  GLN A 175     4590   6585   6477   -101   -857   -402       C  
ATOM   1265  OE1 GLN A 175     -47.982  14.972 -38.445  1.00 47.84           O  
ANISOU 1265  OE1 GLN A 175     4692   6772   6713    -73   -825   -398       O  
ATOM   1266  NE2 GLN A 175     -46.895  13.329 -39.521  1.00 51.91           N  
ANISOU 1266  NE2 GLN A 175     5314   7267   7141   -172   -845   -431       N  
ATOM   1267  N   LEU A 176     -43.523  18.804 -39.564  1.00 47.00           N  
ANISOU 1267  N   LEU A 176     4946   6498   6413     89   -782   -311       N  
ATOM   1268  CA  LEU A 176     -42.869  19.777 -38.702  1.00 43.26           C  
ANISOU 1268  CA  LEU A 176     4507   5985   5946    130   -720   -300       C  
ATOM   1269  C   LEU A 176     -42.450  21.048 -39.431  1.00 42.42           C  
ANISOU 1269  C   LEU A 176     4464   5853   5801    175   -743   -270       C  
ATOM   1270  O   LEU A 176     -42.123  22.037 -38.767  1.00 48.87           O  
ANISOU 1270  O   LEU A 176     5303   6637   6627    215   -699   -258       O  
ATOM   1271  CB  LEU A 176     -41.642  19.139 -38.046  1.00 36.25           C  
ANISOU 1271  CB  LEU A 176     3670   5070   5034     89   -656   -325       C  
ATOM   1272  CG  LEU A 176     -41.915  17.928 -37.151  1.00 37.45           C  
ANISOU 1272  CG  LEU A 176     3775   5234   5220     48   -620   -352       C  
ATOM   1273  CD1 LEU A 176     -40.705  17.007 -37.097  1.00 36.11           C  
ANISOU 1273  CD1 LEU A 176     3667   5045   5007      2   -587   -376       C  
ATOM   1274  CD2 LEU A 176     -42.307  18.375 -35.758  1.00 38.30           C  
ANISOU 1274  CD2 LEU A 176     3838   5332   5381     78   -563   -351       C  
ATOM   1275  N   ARG A 177     -42.441  21.047 -40.765  1.00 39.59           N  
ANISOU 1275  N   ARG A 177     4142   5506   5395    168   -808   -258       N  
ATOM   1276  CA  ARG A 177     -41.978  22.226 -41.497  1.00 38.71           C  
ANISOU 1276  CA  ARG A 177     4105   5364   5239    207   -826   -228       C  
ATOM   1277  C   ARG A 177     -42.837  23.461 -41.250  1.00 45.02           C  
ANISOU 1277  C   ARG A 177     4873   6157   6077    283   -839   -196       C  
ATOM   1278  O   ARG A 177     -42.272  24.511 -40.897  1.00 45.54           O  
ANISOU 1278  O   ARG A 177     4993   6179   6133    317   -797   -181       O  
ATOM   1279  CB  ARG A 177     -41.877  21.900 -42.992  1.00 36.25           C  
ANISOU 1279  CB  ARG A 177     3840   5068   4866    181   -895   -222       C  
ATOM   1280  CG  ARG A 177     -41.424  23.073 -43.852  1.00 38.56           C  
ANISOU 1280  CG  ARG A 177     4219   5328   5104    217   -916   -189       C  
ATOM   1281  CD  ARG A 177     -40.140  23.692 -43.317  1.00 36.25           C  
ANISOU 1281  CD  ARG A 177     3999   4985   4788    213   -839   -193       C  
ATOM   1282  NE  ARG A 177     -39.726  24.856 -44.091  1.00 38.80           N  
ANISOU 1282  NE  ARG A 177     4409   5272   5061    243   -851   -162       N  
ATOM   1283  CZ  ARG A 177     -38.820  24.828 -45.060  1.00 40.10           C  
ANISOU 1283  CZ  ARG A 177     4660   5421   5155    209   -856   -163       C  
ATOM   1284  NH1 ARG A 177     -38.210  23.706 -45.404  1.00 39.61           N  
ANISOU 1284  NH1 ARG A 177     4610   5377   5064    147   -851   -194       N  
ATOM   1285  NH2 ARG A 177     -38.522  25.954 -45.702  1.00 40.04           N  
ANISOU 1285  NH2 ARG A 177     4733   5377   5103    237   -863   -133       N  
ATOM   1286  N   PRO A 178     -44.167  23.432 -41.414  1.00 54.03           N  
ANISOU 1286  N   PRO A 178     5930   7339   7260    314   -893   -184       N  
ATOM   1287  CA  PRO A 178     -44.945  24.649 -41.125  1.00 50.51           C  
ANISOU 1287  CA  PRO A 178     5455   6884   6853    397   -900   -153       C  
ATOM   1288  C   PRO A 178     -44.863  25.080 -39.673  1.00 51.89           C  
ANISOU 1288  C   PRO A 178     5606   7030   7078    420   -816   -162       C  
ATOM   1289  O   PRO A 178     -44.901  26.283 -39.387  1.00 57.45           O  
ANISOU 1289  O   PRO A 178     6338   7699   7792    482   -795   -138       O  
ATOM   1290  CB  PRO A 178     -46.374  24.254 -41.522  1.00 51.68           C  
ANISOU 1290  CB  PRO A 178     5500   7094   7043    414   -973   -149       C  
ATOM   1291  CG  PRO A 178     -46.404  22.780 -41.372  1.00 50.00           C  
ANISOU 1291  CG  PRO A 178     5242   6917   6838    334   -969   -187       C  
ATOM   1292  CD  PRO A 178     -45.048  22.316 -41.811  1.00 48.80           C  
ANISOU 1292  CD  PRO A 178     5192   6734   6617    277   -948   -201       C  
ATOM   1293  N   LEU A 179     -44.753  24.128 -38.744  1.00 44.44           N  
ANISOU 1293  N   LEU A 179     4620   6100   6165    371   -767   -196       N  
ATOM   1294  CA  LEU A 179     -44.638  24.481 -37.334  1.00 45.70           C  
ANISOU 1294  CA  LEU A 179     4763   6234   6366    388   -686   -206       C  
ATOM   1295  C   LEU A 179     -43.281  25.100 -37.026  1.00 47.46           C  
ANISOU 1295  C   LEU A 179     5086   6402   6545    381   -629   -207       C  
ATOM   1296  O   LEU A 179     -43.196  26.077 -36.274  1.00 47.15           O  
ANISOU 1296  O   LEU A 179     5065   6328   6523    422   -582   -198       O  
ATOM   1297  CB  LEU A 179     -44.871  23.247 -36.467  1.00 43.70           C  
ANISOU 1297  CB  LEU A 179     4446   6009   6149    335   -650   -240       C  
ATOM   1298  CG  LEU A 179     -46.229  22.562 -36.620  1.00 46.80           C  
ANISOU 1298  CG  LEU A 179     4732   6459   6592    330   -695   -246       C  
ATOM   1299  CD1 LEU A 179     -46.252  21.262 -35.839  1.00 44.75           C  
ANISOU 1299  CD1 LEU A 179     4432   6216   6355    264   -653   -281       C  
ATOM   1300  CD2 LEU A 179     -47.348  23.486 -36.166  1.00 50.74           C  
ANISOU 1300  CD2 LEU A 179     5159   6968   7152    404   -693   -228       C  
ATOM   1301  N   TYR A 180     -42.209  24.543 -37.596  1.00 48.71           N  
ANISOU 1301  N   TYR A 180     5309   6553   6645    327   -632   -220       N  
ATOM   1302  CA  TYR A 180     -40.877  25.069 -37.319  1.00 44.01           C  
ANISOU 1302  CA  TYR A 180     4800   5913   6007    313   -579   -225       C  
ATOM   1303  C   TYR A 180     -40.699  26.473 -37.875  1.00 45.44           C  
ANISOU 1303  C   TYR A 180     5049   6056   6161    360   -589   -194       C  
ATOM   1304  O   TYR A 180     -39.980  27.284 -37.280  1.00 42.91           O  
ANISOU 1304  O   TYR A 180     4781   5694   5830    369   -533   -195       O  
ATOM   1305  CB  TYR A 180     -39.802  24.145 -37.884  1.00 39.10           C  
ANISOU 1305  CB  TYR A 180     4226   5298   5332    248   -582   -246       C  
ATOM   1306  CG  TYR A 180     -38.489  24.264 -37.149  1.00 44.34           C  
ANISOU 1306  CG  TYR A 180     4943   5933   5972    222   -513   -266       C  
ATOM   1307  CD1 TYR A 180     -38.312  23.667 -35.910  1.00 42.54           C  
ANISOU 1307  CD1 TYR A 180     4681   5710   5774    203   -461   -291       C  
ATOM   1308  CD2 TYR A 180     -37.434  24.992 -37.684  1.00 37.91           C  
ANISOU 1308  CD2 TYR A 180     4213   5087   5103    215   -501   -261       C  
ATOM   1309  CE1 TYR A 180     -37.119  23.778 -35.229  1.00 43.15           C  
ANISOU 1309  CE1 TYR A 180     4801   5766   5826    181   -405   -310       C  
ATOM   1310  CE2 TYR A 180     -36.234  25.110 -37.009  1.00 34.88           C  
ANISOU 1310  CE2 TYR A 180     3870   4685   4700    188   -440   -282       C  
ATOM   1311  CZ  TYR A 180     -36.083  24.501 -35.781  1.00 42.56           C  
ANISOU 1311  CZ  TYR A 180     4802   5667   5702    173   -396   -306       C  
ATOM   1312  OH  TYR A 180     -34.891  24.614 -35.102  1.00 45.40           O  
ANISOU 1312  OH  TYR A 180     5197   6013   6039    148   -342   -328       O  
ATOM   1313  N   GLU A 181     -41.330  26.776 -39.011  1.00 49.04           N  
ANISOU 1313  N   GLU A 181     5509   6522   6601    390   -659   -166       N  
ATOM   1314  CA  GLU A 181     -41.259  28.130 -39.545  1.00 47.50           C  
ANISOU 1314  CA  GLU A 181     5383   6284   6379    442   -670   -131       C  
ATOM   1315  C   GLU A 181     -41.831  29.131 -38.551  1.00 46.26           C  
ANISOU 1315  C   GLU A 181     5203   6100   6274    506   -629   -120       C  
ATOM   1316  O   GLU A 181     -41.175  30.118 -38.204  1.00 42.86           O  
ANISOU 1316  O   GLU A 181     4843   5616   5825    520   -579   -113       O  
ATOM   1317  CB  GLU A 181     -41.991  28.203 -40.885  1.00 51.29           C  
ANISOU 1317  CB  GLU A 181     5863   6787   6837    470   -760   -102       C  
ATOM   1318  CG  GLU A 181     -41.297  27.431 -41.998  1.00 47.45           C  
ANISOU 1318  CG  GLU A 181     5427   6316   6286    409   -796   -111       C  
ATOM   1319  CD  GLU A 181     -42.103  27.394 -43.280  1.00 56.68           C  
ANISOU 1319  CD  GLU A 181     6591   7515   7431    432   -890    -84       C  
ATOM   1320  OE1 GLU A 181     -43.278  27.815 -43.258  1.00 66.38           O  
ANISOU 1320  OE1 GLU A 181     7759   8762   8702    495   -932    -61       O  
ATOM   1321  OE2 GLU A 181     -41.559  26.939 -44.308  1.00 62.29           O1-
ANISOU 1321  OE2 GLU A 181     7357   8231   8079    389   -922    -87       O1-
ATOM   1322  N   GLU A 182     -43.039  28.866 -38.044  1.00 50.55           N  
ANISOU 1322  N   GLU A 182     5645   6678   6882    540   -643   -120       N  
ATOM   1323  CA  GLU A 182     -43.621  29.734 -37.025  1.00 59.48           C  
ANISOU 1323  CA  GLU A 182     6748   7785   8067    601   -597   -113       C  
ATOM   1324  C   GLU A 182     -42.869  29.633 -35.704  1.00 55.26           C  
ANISOU 1324  C   GLU A 182     6226   7226   7543    565   -509   -144       C  
ATOM   1325  O   GLU A 182     -42.824  30.606 -34.942  1.00 46.17           O  
ANISOU 1325  O   GLU A 182     5102   6032   6408    603   -456   -140       O  
ATOM   1326  CB  GLU A 182     -45.096  29.394 -36.820  1.00 64.64           C  
ANISOU 1326  CB  GLU A 182     7282   8489   8789    642   -632   -109       C  
ATOM   1327  CG  GLU A 182     -45.976  30.605 -36.551  1.00 76.20           C  
ANISOU 1327  CG  GLU A 182     8728   9930  10295    737   -627    -81       C  
ATOM   1328  CD  GLU A 182     -47.426  30.231 -36.312  1.00 91.68           C  
ANISOU 1328  CD  GLU A 182    10558  11948  12328    776   -658    -82       C  
ATOM   1329  OE1 GLU A 182     -47.795  29.070 -36.591  1.00 78.99           O  
ANISOU 1329  OE1 GLU A 182     8882  10400  10732    727   -696   -100       O  
ATOM   1330  OE2 GLU A 182     -48.195  31.098 -35.846  1.00 97.17           O1-
ANISOU 1330  OE2 GLU A 182    11220  12630  13069    854   -640    -66       O1-
ATOM   1331  N   TYR A 183     -42.285  28.467 -35.412  1.00 50.88           N  
ANISOU 1331  N   TYR A 183     5656   6698   6978    494   -492   -175       N  
ATOM   1332  CA  TYR A 183     -41.460  28.328 -34.216  1.00 45.14           C  
ANISOU 1332  CA  TYR A 183     4948   5951   6251    458   -415   -204       C  
ATOM   1333  C   TYR A 183     -40.269  29.276 -34.268  1.00 46.04           C  
ANISOU 1333  C   TYR A 183     5167   6013   6314    451   -379   -202       C  
ATOM   1334  O   TYR A 183     -39.898  29.877 -33.253  1.00 49.31           O  
ANISOU 1334  O   TYR A 183     5605   6395   6737    456   -316   -213       O  
ATOM   1335  CB  TYR A 183     -41.006  26.873 -34.071  1.00 45.98           C  
ANISOU 1335  CB  TYR A 183     5029   6094   6348    389   -414   -234       C  
ATOM   1336  CG  TYR A 183     -39.744  26.650 -33.260  1.00 46.19           C  
ANISOU 1336  CG  TYR A 183     5102   6101   6346    343   -352   -261       C  
ATOM   1337  CD1 TYR A 183     -38.494  26.634 -33.869  1.00 45.00           C  
ANISOU 1337  CD1 TYR A 183     5025   5937   6135    304   -353   -268       C  
ATOM   1338  CD2 TYR A 183     -39.805  26.423 -31.891  1.00 44.16           C  
ANISOU 1338  CD2 TYR A 183     4813   5843   6122    337   -294   -282       C  
ATOM   1339  CE1 TYR A 183     -37.342  26.421 -33.135  1.00 35.50           C  
ANISOU 1339  CE1 TYR A 183     3856   4725   4908    265   -302   -294       C  
ATOM   1340  CE2 TYR A 183     -38.658  26.206 -31.150  1.00 40.46           C  
ANISOU 1340  CE2 TYR A 183     4386   5363   5625    298   -245   -306       C  
ATOM   1341  CZ  TYR A 183     -37.430  26.206 -31.778  1.00 40.64           C  
ANISOU 1341  CZ  TYR A 183     4474   5376   5590    263   -251   -312       C  
ATOM   1342  OH  TYR A 183     -36.283  25.992 -31.047  1.00 41.18           O  
ANISOU 1342  OH  TYR A 183     4575   5440   5632    227   -206   -338       O  
ATOM   1343  N   VAL A 184     -39.661  29.423 -35.446  1.00 36.27           N  
ANISOU 1343  N   VAL A 184     3993   4766   5021    434   -416   -189       N  
ATOM   1344  CA  VAL A 184     -38.547  30.354 -35.602  1.00 31.92           C  
ANISOU 1344  CA  VAL A 184     3542   4166   4420    421   -382   -186       C  
ATOM   1345  C   VAL A 184     -39.011  31.793 -35.397  1.00 33.60           C  
ANISOU 1345  C   VAL A 184     3792   4328   4647    487   -363   -160       C  
ATOM   1346  O   VAL A 184     -38.338  32.585 -34.726  1.00 37.93           O  
ANISOU 1346  O   VAL A 184     4396   4833   5183    480   -302   -170       O  
ATOM   1347  CB  VAL A 184     -37.881  30.158 -36.978  1.00 35.45           C  
ANISOU 1347  CB  VAL A 184     4048   4616   4803    388   -425   -178       C  
ATOM   1348  CG1 VAL A 184     -36.953  31.320 -37.296  1.00 34.37           C  
ANISOU 1348  CG1 VAL A 184     4018   4424   4617    383   -394   -168       C  
ATOM   1349  CG2 VAL A 184     -37.122  28.842 -37.013  1.00 30.50           C  
ANISOU 1349  CG2 VAL A 184     3404   4027   4157    319   -423   -210       C  
ATOM   1350  N   VAL A 185     -40.168  32.154 -35.965  1.00 40.70           N  
ANISOU 1350  N   VAL A 185     4661   5233   5572    552   -414   -128       N  
ATOM   1351  CA  VAL A 185     -40.648  33.534 -35.864  1.00 44.81           C  
ANISOU 1351  CA  VAL A 185     5221   5700   6105    624   -400   -100       C  
ATOM   1352  C   VAL A 185     -40.905  33.910 -34.410  1.00 45.48           C  
ANISOU 1352  C   VAL A 185     5275   5766   6239    646   -329   -118       C  
ATOM   1353  O   VAL A 185     -40.519  34.992 -33.953  1.00 45.78           O  
ANISOU 1353  O   VAL A 185     5383   5745   6266    664   -277   -115       O  
ATOM   1354  CB  VAL A 185     -41.909  33.743 -36.723  1.00 38.51           C  
ANISOU 1354  CB  VAL A 185     4382   4921   5329    697   -475    -62       C  
ATOM   1355  CG1 VAL A 185     -42.133  35.225 -36.961  1.00 50.64           C  
ANISOU 1355  CG1 VAL A 185     5994   6392   6856    771   -468    -26       C  
ATOM   1356  CG2 VAL A 185     -41.775  33.040 -38.051  1.00 35.93           C  
ANISOU 1356  CG2 VAL A 185     4065   4630   4958    665   -549    -51       C  
ATOM   1357  N   LEU A 186     -41.562  33.022 -33.661  1.00 38.40           N  
ANISOU 1357  N   LEU A 186     4279   4917   5395    641   -324   -137       N  
ATOM   1358  CA  LEU A 186     -41.912  33.347 -32.282  1.00 42.72           C  
ANISOU 1358  CA  LEU A 186     4794   5447   5989    664   -257   -154       C  
ATOM   1359  C   LEU A 186     -40.690  33.309 -31.373  1.00 43.16           C  
ANISOU 1359  C   LEU A 186     4903   5481   6015    601   -188   -188       C  
ATOM   1360  O   LEU A 186     -40.550  34.154 -30.481  1.00 47.09           O  
ANISOU 1360  O   LEU A 186     5436   5934   6520    619   -127   -196       O  
ATOM   1361  CB  LEU A 186     -42.994  32.395 -31.776  1.00 41.92           C  
ANISOU 1361  CB  LEU A 186     4574   5404   5950    673   -268   -165       C  
ATOM   1362  CG  LEU A 186     -44.370  32.581 -32.417  1.00 37.46           C  
ANISOU 1362  CG  LEU A 186     3940   4866   5429    745   -328   -136       C  
ATOM   1363  CD1 LEU A 186     -45.343  31.519 -31.933  1.00 45.18           C  
ANISOU 1363  CD1 LEU A 186     4794   5906   6465    736   -336   -153       C  
ATOM   1364  CD2 LEU A 186     -44.908  33.977 -32.138  1.00 40.76           C  
ANISOU 1364  CD2 LEU A 186     4385   5232   5871    832   -301   -113       C  
ATOM   1365  N   LYS A 187     -39.796  32.339 -31.579  1.00 47.79           N  
ANISOU 1365  N   LYS A 187     5495   6098   6567    529   -198   -209       N  
ATOM   1366  CA  LYS A 187     -38.581  32.281 -30.773  1.00 45.68           C  
ANISOU 1366  CA  LYS A 187     5273   5816   6267    471   -140   -241       C  
ATOM   1367  C   LYS A 187     -37.698  33.496 -31.025  1.00 47.78           C  
ANISOU 1367  C   LYS A 187     5644   6025   6487    466   -112   -235       C  
ATOM   1368  O   LYS A 187     -37.091  34.037 -30.092  1.00 51.59           O  
ANISOU 1368  O   LYS A 187     6166   6477   6960    448    -52   -257       O  
ATOM   1369  CB  LYS A 187     -37.816  30.989 -31.061  1.00 36.07           C  
ANISOU 1369  CB  LYS A 187     4039   4644   5022    404   -161   -262       C  
ATOM   1370  CG  LYS A 187     -38.440  29.747 -30.443  1.00 38.11           C  
ANISOU 1370  CG  LYS A 187     4209   4950   5322    392   -165   -277       C  
ATOM   1371  CD  LYS A 187     -38.363  29.778 -28.926  1.00 37.01           C  
ANISOU 1371  CD  LYS A 187     4056   4802   5205    386    -98   -301       C  
ATOM   1372  CE  LYS A 187     -38.747  28.433 -28.330  1.00 36.04           C  
ANISOU 1372  CE  LYS A 187     3861   4723   5109    361    -97   -319       C  
ATOM   1373  NZ  LYS A 187     -38.517  28.384 -26.860  1.00 41.86           N  
ANISOU 1373  NZ  LYS A 187     4597   5452   5855    348    -32   -343       N  
ATOM   1374  N   ASN A 188     -37.605  33.935 -32.282  1.00 44.15           N  
ANISOU 1374  N   ASN A 188     5233   5548   5993    478   -155   -208       N  
ATOM   1375  CA  ASN A 188     -36.865  35.156 -32.586  1.00 48.02           C  
ANISOU 1375  CA  ASN A 188     5830   5977   6439    475   -127   -200       C  
ATOM   1376  C   ASN A 188     -37.532  36.371 -31.954  1.00 54.81           C  
ANISOU 1376  C   ASN A 188     6715   6781   7328    539    -88   -186       C  
ATOM   1377  O   ASN A 188     -36.861  37.213 -31.346  1.00 57.84           O  
ANISOU 1377  O   ASN A 188     7167   7117   7692    521    -29   -202       O  
ATOM   1378  CB  ASN A 188     -36.742  35.334 -34.099  1.00 51.39           C  
ANISOU 1378  CB  ASN A 188     6306   6396   6823    478   -182   -170       C  
ATOM   1379  CG  ASN A 188     -35.610  34.520 -34.691  1.00 48.31           C  
ANISOU 1379  CG  ASN A 188     5934   6038   6383    401   -194   -191       C  
ATOM   1380  OD1 ASN A 188     -34.619  34.232 -34.020  1.00 50.04           O  
ANISOU 1380  OD1 ASN A 188     6160   6266   6586    344   -150   -226       O  
ATOM   1381  ND2 ASN A 188     -35.749  34.146 -35.958  1.00 50.16           N  
ANISOU 1381  ND2 ASN A 188     6177   6291   6591    401   -254   -170       N  
ATOM   1382  N   GLU A 189     -38.860  36.470 -32.077  1.00 57.16           N  
ANISOU 1382  N   GLU A 189     6956   7085   7675    615   -120   -160       N  
ATOM   1383  CA  GLU A 189     -39.583  37.576 -31.456  1.00 62.71           C  
ANISOU 1383  CA  GLU A 189     7677   7738   8413    686    -82   -147       C  
ATOM   1384  C   GLU A 189     -39.352  37.606 -29.952  1.00 58.97           C  
ANISOU 1384  C   GLU A 189     7190   7255   7961    664     -6   -184       C  
ATOM   1385  O   GLU A 189     -39.233  38.682 -29.353  1.00 67.97           O  
ANISOU 1385  O   GLU A 189     8393   8334   9098    685     50   -187       O  
ATOM   1386  CB  GLU A 189     -41.078  37.468 -31.762  1.00 64.58           C  
ANISOU 1386  CB  GLU A 189     7831   8000   8707    770   -131   -117       C  
ATOM   1387  CG  GLU A 189     -41.488  37.987 -33.130  1.00 77.34           C  
ANISOU 1387  CG  GLU A 189     9484   9600  10301    823   -197    -72       C  
ATOM   1388  CD  GLU A 189     -42.964  37.774 -33.411  1.00 82.10           C  
ANISOU 1388  CD  GLU A 189     9989  10244  10962    903   -253    -47       C  
ATOM   1389  OE1 GLU A 189     -43.682  37.309 -32.500  1.00 68.95           O  
ANISOU 1389  OE1 GLU A 189     8229   8612   9356    918   -231    -66       O  
ATOM   1390  OE2 GLU A 189     -43.407  38.070 -34.541  1.00 86.31           O1-
ANISOU 1390  OE2 GLU A 189    10539  10776  11480    950   -319     -9       O1-
ATOM   1391  N   MET A 190     -39.293  36.431 -29.323  1.00 60.53           N  
ANISOU 1391  N   MET A 190     7311   7510   8178    621     -3   -211       N  
ATOM   1392  CA  MET A 190     -39.013  36.362 -27.893  1.00 65.16           C  
ANISOU 1392  CA  MET A 190     7889   8093   8777    594     65   -247       C  
ATOM   1393  C   MET A 190     -37.597  36.835 -27.585  1.00 65.36           C  
ANISOU 1393  C   MET A 190     8005   8086   8745    528    109   -272       C  
ATOM   1394  O   MET A 190     -37.386  37.644 -26.674  1.00 78.13           O  
ANISOU 1394  O   MET A 190     9667   9658  10359    530    171   -289       O  
ATOM   1395  CB  MET A 190     -39.226  34.934 -27.392  1.00 63.54           C  
ANISOU 1395  CB  MET A 190     7590   7955   8597    560     54   -267       C  
ATOM   1396  CG  MET A 190     -38.709  34.682 -25.987  1.00 72.78           C  
ANISOU 1396  CG  MET A 190     8761   9128   9765    518    118   -304       C  
ATOM   1397  SD  MET A 190     -37.239  33.639 -25.976  1.00 85.12           S  
ANISOU 1397  SD  MET A 190    10338  10729  11273    425    109   -334       S  
ATOM   1398  CE  MET A 190     -37.933  32.081 -25.428  1.00 83.87           C  
ANISOU 1398  CE  MET A 190    10076  10634  11156    415     96   -344       C  
ATOM   1399  N   ALA A 191     -36.611  36.337 -28.335  1.00 47.40           N  
ANISOU 1399  N   ALA A 191     5754   5834   6423    469     79   -278       N  
ATOM   1400  CA  ALA A 191     -35.221  36.693 -28.067  1.00 41.64           C  
ANISOU 1400  CA  ALA A 191     5097   5085   5640    401    118   -306       C  
ATOM   1401  C   ALA A 191     -34.958  38.171 -28.326  1.00 49.81           C  
ANISOU 1401  C   ALA A 191     6234   6044   6647    415    150   -294       C  
ATOM   1402  O   ALA A 191     -34.208  38.811 -27.579  1.00 56.76           O  
ANISOU 1402  O   ALA A 191     7171   6892   7503    377    207   -322       O  
ATOM   1403  CB  ALA A 191     -34.287  35.828 -28.911  1.00 37.48           C  
ANISOU 1403  CB  ALA A 191     4567   4601   5072    340     80   -313       C  
ATOM   1404  N   ARG A 192     -35.551  38.728 -29.387  1.00 54.27           N  
ANISOU 1404  N   ARG A 192     6828   6579   7213    467    114   -255       N  
ATOM   1405  CA  ARG A 192     -35.344  40.142 -29.687  1.00 56.68           C  
ANISOU 1405  CA  ARG A 192     7241   6804   7489    485    145   -240       C  
ATOM   1406  C   ARG A 192     -35.887  41.028 -28.577  1.00 63.24           C  
ANISOU 1406  C   ARG A 192     8093   7585   8353    530    205   -247       C  
ATOM   1407  O   ARG A 192     -35.235  41.998 -28.172  1.00 65.41           O  
ANISOU 1407  O   ARG A 192     8456   7801   8597    502    262   -263       O  
ATOM   1408  CB  ARG A 192     -35.993  40.507 -31.022  1.00 55.13           C  
ANISOU 1408  CB  ARG A 192     7071   6587   7289    544     89   -190       C  
ATOM   1409  CG  ARG A 192     -35.074  40.344 -32.218  1.00 53.18           C  
ANISOU 1409  CG  ARG A 192     6877   6347   6981    489     57   -184       C  
ATOM   1410  CD  ARG A 192     -35.658  39.373 -33.224  1.00 55.49           C  
ANISOU 1410  CD  ARG A 192     7104   6696   7283    511    -23   -159       C  
ATOM   1411  NE  ARG A 192     -34.661  38.903 -34.177  1.00 63.13           N  
ANISOU 1411  NE  ARG A 192     8106   7687   8195    443    -46   -164       N  
ATOM   1412  CZ  ARG A 192     -34.950  38.355 -35.349  1.00 70.05           C  
ANISOU 1412  CZ  ARG A 192     8967   8593   9057    453   -113   -139       C  
ATOM   1413  NH1 ARG A 192     -36.201  38.192 -35.745  1.00 71.99           N  
ANISOU 1413  NH1 ARG A 192     9160   8854   9338    527   -169   -106       N  
ATOM   1414  NH2 ARG A 192     -33.959  37.956 -36.141  1.00 58.75           N  
ANISOU 1414  NH2 ARG A 192     7571   7178   7571    387   -123   -149       N  
ATOM   1415  N   ALA A 193     -37.080  40.716 -28.072  1.00 63.50           N  
ANISOU 1415  N   ALA A 193     8044   7637   8445    595    198   -238       N  
ATOM   1416  CA  ALA A 193     -37.614  41.475 -26.953  1.00 75.40           C  
ANISOU 1416  CA  ALA A 193     9565   9100   9985    637    261   -249       C  
ATOM   1417  C   ALA A 193     -36.907  41.146 -25.643  1.00 74.14           C  
ANISOU 1417  C   ALA A 193     9398   8957   9816    571    317   -298       C  
ATOM   1418  O   ALA A 193     -37.069  41.889 -24.668  1.00 80.32           O  
ANISOU 1418  O   ALA A 193    10215   9694  10608    587    379   -314       O  
ATOM   1419  CB  ALA A 193     -39.121  41.245 -26.841  1.00 69.60           C  
ANISOU 1419  CB  ALA A 193     8740   8385   9319    729    238   -225       C  
ATOM   1420  N   ASN A 194     -36.131  40.063 -25.600  1.00 58.08           N  
ANISOU 1420  N   ASN A 194     7322   6985   7759    499    295   -320       N  
ATOM   1421  CA  ASN A 194     -35.146  39.834 -24.552  1.00 54.53           C  
ANISOU 1421  CA  ASN A 194     6886   6551   7282    426    340   -366       C  
ATOM   1422  C   ASN A 194     -33.819  40.516 -24.859  1.00 57.70           C  
ANISOU 1422  C   ASN A 194     7382   6921   7621    357    361   -383       C  
ATOM   1423  O   ASN A 194     -32.828  40.261 -24.166  1.00 50.81           O  
ANISOU 1423  O   ASN A 194     6517   6072   6718    287    386   -422       O  
ATOM   1424  CB  ASN A 194     -34.921  38.332 -24.343  1.00 54.09           C  
ANISOU 1424  CB  ASN A 194     6743   6577   7233    386    307   -381       C  
ATOM   1425  CG  ASN A 194     -36.034  37.681 -23.547  1.00 59.05           C  
ANISOU 1425  CG  ASN A 194     7286   7234   7917    430    313   -380       C  
ATOM   1426  OD1 ASN A 194     -36.689  36.753 -24.020  1.00 61.94           O  
ANISOU 1426  OD1 ASN A 194     7575   7647   8314    451    266   -363       O  
ATOM   1427  ND2 ASN A 194     -36.251  38.164 -22.330  1.00 60.58           N  
ANISOU 1427  ND2 ASN A 194     7494   7401   8123    440    374   -401       N  
ATOM   1428  N   HIS A 195     -33.784  41.359 -25.895  1.00 59.53           N  
ANISOU 1428  N   HIS A 195     7684   7103   7832    376    349   -356       N  
ATOM   1429  CA  HIS A 195     -32.613  42.146 -26.282  1.00 60.61           C  
ANISOU 1429  CA  HIS A 195     7921   7200   7910    312    375   -369       C  
ATOM   1430  C   HIS A 195     -31.467  41.275 -26.791  1.00 57.87           C  
ANISOU 1430  C   HIS A 195     7551   6914   7523    232    345   -388       C  
ATOM   1431  O   HIS A 195     -30.298  41.652 -26.687  1.00 59.63           O  
ANISOU 1431  O   HIS A 195     7829   7129   7700    157    376   -418       O  
ATOM   1432  CB  HIS A 195     -32.146  43.050 -25.137  1.00 62.84           C  
ANISOU 1432  CB  HIS A 195     8268   7434   8175    279    449   -406       C  
ATOM   1433  CG  HIS A 195     -33.257  43.818 -24.491  1.00 70.13           C  
ANISOU 1433  CG  HIS A 195     9208   8298   9138    357    486   -393       C  
ATOM   1434  ND1 HIS A 195     -33.892  43.388 -23.346  1.00 64.07           N  
ANISOU 1434  ND1 HIS A 195     8376   7556   8412    384    508   -409       N  
ATOM   1435  CD2 HIS A 195     -33.858  44.980 -24.841  1.00 68.20           C  
ANISOU 1435  CD2 HIS A 195     9040   7973   8902    419    508   -365       C  
ATOM   1436  CE1 HIS A 195     -34.830  44.257 -23.013  1.00 66.60           C  
ANISOU 1436  CE1 HIS A 195     8727   7814   8764    458    544   -394       C  
ATOM   1437  NE2 HIS A 195     -34.830  45.232 -23.903  1.00 74.38           N  
ANISOU 1437  NE2 HIS A 195     9797   8733   9730    484    543   -367       N  
ATOM   1438  N   TYR A 196     -31.792  40.114 -27.347  1.00 45.73           N  
ANISOU 1438  N   TYR A 196     5932   5438   6004    246    286   -373       N  
ATOM   1439  CA  TYR A 196     -30.841  39.296 -28.085  1.00 39.87           C  
ANISOU 1439  CA  TYR A 196     5173   4749   5228    185    253   -383       C  
ATOM   1440  C   TYR A 196     -31.032  39.515 -29.582  1.00 46.47           C  
ANISOU 1440  C   TYR A 196     6046   5566   6046    207    210   -345       C  
ATOM   1441  O   TYR A 196     -32.100  39.931 -30.040  1.00 46.12           O  
ANISOU 1441  O   TYR A 196     6009   5488   6026    280    188   -306       O  
ATOM   1442  CB  TYR A 196     -31.010  37.812 -27.745  1.00 34.74           C  
ANISOU 1442  CB  TYR A 196     4419   4177   4604    182    218   -394       C  
ATOM   1443  CG  TYR A 196     -30.586  37.439 -26.340  1.00 40.79           C  
ANISOU 1443  CG  TYR A 196     5153   4971   5374    149    255   -434       C  
ATOM   1444  CD1 TYR A 196     -31.470  37.547 -25.274  1.00 40.98           C  
ANISOU 1444  CD1 TYR A 196     5149   4982   5438    192    282   -435       C  
ATOM   1445  CD2 TYR A 196     -29.304  36.973 -26.082  1.00 38.22           C  
ANISOU 1445  CD2 TYR A 196     4824   4686   5010     76    263   -470       C  
ATOM   1446  CE1 TYR A 196     -31.087  37.203 -23.990  1.00 38.14           C  
ANISOU 1446  CE1 TYR A 196     4768   4647   5076    161    315   -470       C  
ATOM   1447  CE2 TYR A 196     -28.913  36.627 -24.801  1.00 36.23           C  
ANISOU 1447  CE2 TYR A 196     4545   4462   4757     49    291   -504       C  
ATOM   1448  CZ  TYR A 196     -29.807  36.744 -23.760  1.00 38.71           C  
ANISOU 1448  CZ  TYR A 196     4841   4760   5107     91    316   -504       C  
ATOM   1449  OH  TYR A 196     -29.420  36.401 -22.485  1.00 51.98           O  
ANISOU 1449  OH  TYR A 196     6503   6467   6782     63    344   -537       O  
ATOM   1450  N   GLU A 197     -29.973  39.236 -30.347  1.00 53.74           N  
ANISOU 1450  N   GLU A 197     6991   6509   6920    143    199   -356       N  
ATOM   1451  CA  GLU A 197     -30.058  39.378 -31.799  1.00 51.99           C  
ANISOU 1451  CA  GLU A 197     6811   6272   6672    155    159   -321       C  
ATOM   1452  C   GLU A 197     -31.121  38.452 -32.375  1.00 49.94           C  
ANISOU 1452  C   GLU A 197     6476   6053   6448    213     92   -290       C  
ATOM   1453  O   GLU A 197     -31.944  38.864 -33.200  1.00 59.50           O  
ANISOU 1453  O   GLU A 197     7710   7233   7663    271     57   -249       O  
ATOM   1454  CB  GLU A 197     -28.702  39.085 -32.442  1.00 49.49           C  
ANISOU 1454  CB  GLU A 197     6520   5982   6301     71    164   -345       C  
ATOM   1455  CG  GLU A 197     -27.557  39.958 -31.969  1.00 54.36           C  
ANISOU 1455  CG  GLU A 197     7207   6568   6880      0    229   -380       C  
ATOM   1456  CD  GLU A 197     -26.219  39.473 -32.495  1.00 70.50           C  
ANISOU 1456  CD  GLU A 197     9251   8657   8879    -83    233   -410       C  
ATOM   1457  OE1 GLU A 197     -26.204  38.482 -33.255  1.00 69.08           O  
ANISOU 1457  OE1 GLU A 197     9025   8526   8697    -81    188   -401       O  
ATOM   1458  OE2 GLU A 197     -25.184  40.081 -32.150  1.00 73.63           O1-
ANISOU 1458  OE2 GLU A 197     9693   9041   9243   -151    284   -444       O1-
ATOM   1459  N   ASP A 198     -31.120  37.197 -31.941  1.00 52.15           N  
ANISOU 1459  N   ASP A 198     6664   6400   6750    199     71   -310       N  
ATOM   1460  CA  ASP A 198     -32.041  36.188 -32.442  1.00 52.87           C  
ANISOU 1460  CA  ASP A 198     6680   6536   6874    239     10   -288       C  
ATOM   1461  C   ASP A 198     -32.086  35.054 -31.427  1.00 51.55           C  
ANISOU 1461  C   ASP A 198     6424   6425   6740    225     14   -316       C  
ATOM   1462  O   ASP A 198     -31.433  35.108 -30.381  1.00 49.21           O  
ANISOU 1462  O   ASP A 198     6128   6131   6438    190     60   -349       O  
ATOM   1463  CB  ASP A 198     -31.615  35.693 -33.827  1.00 57.12           C  
ANISOU 1463  CB  ASP A 198     7235   7095   7371    213    -36   -276       C  
ATOM   1464  CG  ASP A 198     -30.139  35.355 -33.895  1.00 60.31           C  
ANISOU 1464  CG  ASP A 198     7662   7524   7730    131    -10   -312       C  
ATOM   1465  OD1 ASP A 198     -29.738  34.316 -33.331  1.00 59.42           O  
ANISOU 1465  OD1 ASP A 198     7486   7464   7628    101     -9   -341       O  
ATOM   1466  OD2 ASP A 198     -29.378  36.131 -34.511  1.00 63.71           O1-
ANISOU 1466  OD2 ASP A 198     8174   7920   8113     96     12   -312       O1-
ATOM   1467  N   TYR A 199     -32.868  34.020 -31.742  1.00 44.02           N  
ANISOU 1467  N   TYR A 199     5396   5513   5815    250    -35   -304       N  
ATOM   1468  CA  TYR A 199     -32.971  32.885 -30.833  1.00 43.36           C  
ANISOU 1468  CA  TYR A 199     5234   5479   5761    237    -31   -328       C  
ATOM   1469  C   TYR A 199     -31.645  32.148 -30.703  1.00 43.90           C  
ANISOU 1469  C   TYR A 199     5305   5583   5793    169    -19   -362       C  
ATOM   1470  O   TYR A 199     -31.342  31.607 -29.633  1.00 39.53           O  
ANISOU 1470  O   TYR A 199     4717   5054   5250    150      7   -388       O  
ATOM   1471  CB  TYR A 199     -34.069  31.930 -31.295  1.00 40.57           C  
ANISOU 1471  CB  TYR A 199     4807   5163   5444    270    -86   -308       C  
ATOM   1472  CG  TYR A 199     -34.419  30.888 -30.261  1.00 39.89           C  
ANISOU 1472  CG  TYR A 199     4645   5115   5395    265    -75   -328       C  
ATOM   1473  CD1 TYR A 199     -34.577  31.237 -28.926  1.00 39.64           C  
ANISOU 1473  CD1 TYR A 199     4605   5070   5389    275    -23   -343       C  
ATOM   1474  CD2 TYR A 199     -34.589  29.558 -30.615  1.00 37.82           C  
ANISOU 1474  CD2 TYR A 199     4329   4901   5141    247   -113   -332       C  
ATOM   1475  CE1 TYR A 199     -34.896  30.290 -27.973  1.00 42.20           C  
ANISOU 1475  CE1 TYR A 199     4866   5425   5741    268    -10   -360       C  
ATOM   1476  CE2 TYR A 199     -34.911  28.605 -29.670  1.00 37.80           C  
ANISOU 1476  CE2 TYR A 199     4266   4928   5169    240   -100   -349       C  
ATOM   1477  CZ  TYR A 199     -35.060  28.975 -28.350  1.00 37.67           C  
ANISOU 1477  CZ  TYR A 199     4242   4897   5175    251    -48   -362       C  
ATOM   1478  OH  TYR A 199     -35.379  28.029 -27.404  1.00 42.73           O  
ANISOU 1478  OH  TYR A 199     4830   5564   5841    243    -31   -377       O  
ATOM   1479  N   GLY A 200     -30.851  32.106 -31.773  1.00 41.39           N  
ANISOU 1479  N   GLY A 200     5026   5270   5430    134    -37   -361       N  
ATOM   1480  CA  GLY A 200     -29.517  31.538 -31.666  1.00 39.14           C  
ANISOU 1480  CA  GLY A 200     4744   5018   5109     73    -20   -395       C  
ATOM   1481  C   GLY A 200     -28.620  32.348 -30.750  1.00 41.42           C  
ANISOU 1481  C   GLY A 200     5070   5287   5378     39     36   -424       C  
ATOM   1482  O   GLY A 200     -27.828  31.789 -29.987  1.00 38.32           O  
ANISOU 1482  O   GLY A 200     4652   4930   4978      5     56   -456       O  
ATOM   1483  N   ASP A 201     -28.731  33.678 -30.814  1.00 43.93           N  
ANISOU 1483  N   ASP A 201     5454   5550   5687     49     63   -412       N  
ATOM   1484  CA  ASP A 201     -27.997  34.530 -29.885  1.00 38.25           C  
ANISOU 1484  CA  ASP A 201     4775   4808   4952     15    119   -440       C  
ATOM   1485  C   ASP A 201     -28.437  34.277 -28.450  1.00 41.36           C  
ANISOU 1485  C   ASP A 201     5122   5212   5380     34    141   -455       C  
ATOM   1486  O   ASP A 201     -27.616  34.305 -27.525  1.00 43.32           O  
ANISOU 1486  O   ASP A 201     5372   5476   5613     -6    175   -490       O  
ATOM   1487  CB  ASP A 201     -28.193  35.999 -30.259  1.00 44.01           C  
ANISOU 1487  CB  ASP A 201     5591   5466   5667     28    145   -421       C  
ATOM   1488  CG  ASP A 201     -27.205  36.915 -29.566  1.00 43.50           C  
ANISOU 1488  CG  ASP A 201     5581   5375   5571    -26    203   -455       C  
ATOM   1489  OD1 ASP A 201     -26.125  36.434 -29.165  1.00 42.99           O  
ANISOU 1489  OD1 ASP A 201     5494   5356   5484    -84    216   -492       O  
ATOM   1490  OD2 ASP A 201     -27.510  38.118 -29.421  1.00 46.36           O1-
ANISOU 1490  OD2 ASP A 201     6011   5672   5931    -10    236   -445       O1-
ATOM   1491  N   TYR A 202     -29.734  34.030 -28.247  1.00 39.06           N  
ANISOU 1491  N   TYR A 202     4790   4914   5135     94    123   -431       N  
ATOM   1492  CA  TYR A 202     -30.231  33.669 -26.924  1.00 39.94           C  
ANISOU 1492  CA  TYR A 202     4855   5039   5281    112    145   -444       C  
ATOM   1493  C   TYR A 202     -29.568  32.393 -26.421  1.00 44.59           C  
ANISOU 1493  C   TYR A 202     5392   5689   5862     77    136   -470       C  
ATOM   1494  O   TYR A 202     -29.163  32.311 -25.255  1.00 47.32           O  
ANISOU 1494  O   TYR A 202     5732   6046   6203     58    168   -497       O  
ATOM   1495  CB  TYR A 202     -31.755  33.514 -26.975  1.00 45.39           C  
ANISOU 1495  CB  TYR A 202     5501   5720   6024    180    124   -413       C  
ATOM   1496  CG  TYR A 202     -32.409  32.994 -25.708  1.00 49.51           C  
ANISOU 1496  CG  TYR A 202     5968   6259   6585    200    146   -424       C  
ATOM   1497  CD1 TYR A 202     -32.399  31.639 -25.393  1.00 51.31           C  
ANISOU 1497  CD1 TYR A 202     6134   6539   6823    185    127   -434       C  
ATOM   1498  CD2 TYR A 202     -33.059  33.860 -24.837  1.00 56.73           C  
ANISOU 1498  CD2 TYR A 202     6898   7133   7524    234    189   -424       C  
ATOM   1499  CE1 TYR A 202     -32.998  31.165 -24.243  1.00 59.93           C  
ANISOU 1499  CE1 TYR A 202     7182   7642   7945    199    151   -443       C  
ATOM   1500  CE2 TYR A 202     -33.665  33.394 -23.684  1.00 68.67           C  
ANISOU 1500  CE2 TYR A 202     8364   8659   9069    250    214   -434       C  
ATOM   1501  CZ  TYR A 202     -33.631  32.046 -23.393  1.00 73.64           C  
ANISOU 1501  CZ  TYR A 202     8934   9341   9705    231    195   -444       C  
ATOM   1502  OH  TYR A 202     -34.232  31.575 -22.248  1.00 90.65           O  
ANISOU 1502  OH  TYR A 202    11048  11506  11887    243    224   -454       O  
ATOM   1503  N   TRP A 203     -29.451  31.386 -27.289  1.00 46.35           N  
ANISOU 1503  N   TRP A 203     5582   5948   6080     70     92   -463       N  
ATOM   1504  CA  TRP A 203     -28.863  30.114 -26.882  1.00 33.88           C  
ANISOU 1504  CA  TRP A 203     3957   4422   4493     44     81   -484       C  
ATOM   1505  C   TRP A 203     -27.396  30.273 -26.507  1.00 35.27           C  
ANISOU 1505  C   TRP A 203     4158   4617   4625     -9    106   -520       C  
ATOM   1506  O   TRP A 203     -26.937  29.704 -25.510  1.00 39.33           O  
ANISOU 1506  O   TRP A 203     4647   5162   5135    -23    119   -543       O  
ATOM   1507  CB  TRP A 203     -29.020  29.089 -28.001  1.00 35.62           C  
ANISOU 1507  CB  TRP A 203     4148   4670   4714     47     32   -470       C  
ATOM   1508  CG  TRP A 203     -30.281  28.302 -27.910  1.00 30.57           C  
ANISOU 1508  CG  TRP A 203     3454   4041   4120     85      7   -451       C  
ATOM   1509  CD1 TRP A 203     -31.127  28.227 -26.843  1.00 32.33           C  
ANISOU 1509  CD1 TRP A 203     3645   4258   4380    112     28   -449       C  
ATOM   1510  CD2 TRP A 203     -30.847  27.474 -28.930  1.00 34.77           C  
ANISOU 1510  CD2 TRP A 203     3957   4591   4663     96    -41   -432       C  
ATOM   1511  NE1 TRP A 203     -32.185  27.401 -27.135  1.00 33.75           N  
ANISOU 1511  NE1 TRP A 203     3773   4453   4596    137     -3   -432       N  
ATOM   1512  CE2 TRP A 203     -32.036  26.926 -28.411  1.00 33.27           C  
ANISOU 1512  CE2 TRP A 203     3713   4407   4519    127    -48   -422       C  
ATOM   1513  CE3 TRP A 203     -30.462  27.142 -30.232  1.00 34.89           C  
ANISOU 1513  CE3 TRP A 203     3988   4618   4650     79    -77   -426       C  
ATOM   1514  CZ2 TRP A 203     -32.842  26.063 -29.148  1.00 40.06           C  
ANISOU 1514  CZ2 TRP A 203     4533   5287   5400    138    -92   -406       C  
ATOM   1515  CZ3 TRP A 203     -31.265  26.290 -30.962  1.00 36.16           C  
ANISOU 1515  CZ3 TRP A 203     4114   4796   4829     93   -122   -410       C  
ATOM   1516  CH2 TRP A 203     -32.442  25.760 -30.419  1.00 39.82           C  
ANISOU 1516  CH2 TRP A 203     4522   5268   5341    120   -130   -401       C  
ATOM   1517  N   ARG A 204     -26.644  31.043 -27.294  1.00 29.19           N  
ANISOU 1517  N   ARG A 204     3437   3831   3821    -40    113   -524       N  
ATOM   1518  CA  ARG A 204     -25.230  31.252 -27.012  1.00 29.62           C  
ANISOU 1518  CA  ARG A 204     3510   3909   3835    -96    138   -560       C  
ATOM   1519  C   ARG A 204     -24.997  32.060 -25.743  1.00 35.54           C  
ANISOU 1519  C   ARG A 204     4283   4642   4580   -112    181   -584       C  
ATOM   1520  O   ARG A 204     -23.858  32.111 -25.265  1.00 33.83           O  
ANISOU 1520  O   ARG A 204     4068   4455   4331   -158    199   -618       O  
ATOM   1521  CB  ARG A 204     -24.558  31.938 -28.202  1.00 23.76           C  
ANISOU 1521  CB  ARG A 204     2819   3150   3058   -130    141   -559       C  
ATOM   1522  CG  ARG A 204     -24.714  31.175 -29.506  1.00 25.23           C  
ANISOU 1522  CG  ARG A 204     2992   3353   3242   -120     99   -539       C  
ATOM   1523  CD  ARG A 204     -23.847  31.760 -30.603  1.00 21.53           C  
ANISOU 1523  CD  ARG A 204     2575   2874   2730   -163    108   -544       C  
ATOM   1524  NE  ARG A 204     -24.342  33.051 -31.064  1.00 27.73           N  
ANISOU 1524  NE  ARG A 204     3431   3596   3510   -153    123   -520       N  
ATOM   1525  CZ  ARG A 204     -25.288  33.208 -31.979  1.00 32.14           C  
ANISOU 1525  CZ  ARG A 204     4011   4123   4079   -112     93   -480       C  
ATOM   1526  NH1 ARG A 204     -25.873  32.170 -32.553  1.00 32.14           N  
ANISOU 1526  NH1 ARG A 204     3967   4150   4095    -83     46   -463       N  
ATOM   1527  NH2 ARG A 204     -25.657  34.438 -32.326  1.00 35.78           N  
ANISOU 1527  NH2 ARG A 204     4543   4523   4531   -100    109   -458       N  
ATOM   1528  N   GLY A 205     -26.037  32.683 -25.189  1.00 29.25           N  
ANISOU 1528  N   GLY A 205     3501   3801   3812    -74    199   -567       N  
ATOM   1529  CA  GLY A 205     -25.907  33.405 -23.935  1.00 33.41           C  
ANISOU 1529  CA  GLY A 205     4052   4309   4333    -86    243   -590       C  
ATOM   1530  C   GLY A 205     -25.601  32.524 -22.742  1.00 32.65           C  
ANISOU 1530  C   GLY A 205     3911   4259   4235    -94    244   -614       C  
ATOM   1531  O   GLY A 205     -25.219  33.047 -21.689  1.00 35.21           O  
ANISOU 1531  O   GLY A 205     4258   4580   4543   -117    278   -640       O  
ATOM   1532  N   ASP A 206     -25.768  31.205 -22.876  1.00 41.74           N  
ANISOU 1532  N   ASP A 206     5006   5453   5401    -76    210   -605       N  
ATOM   1533  CA  ASP A 206     -25.404  30.300 -21.793  1.00 47.32           C  
ANISOU 1533  CA  ASP A 206     5677   6203   6100    -81    209   -625       C  
ATOM   1534  C   ASP A 206     -23.912  30.361 -21.494  1.00 46.79           C  
ANISOU 1534  C   ASP A 206     5616   6176   5986   -134    214   -663       C  
ATOM   1535  O   ASP A 206     -23.496  30.138 -20.351  1.00 52.67           O  
ANISOU 1535  O   ASP A 206     6352   6946   6714   -146    224   -686       O  
ATOM   1536  CB  ASP A 206     -25.819  28.870 -22.141  1.00 43.98           C  
ANISOU 1536  CB  ASP A 206     5201   5812   5698    -54    171   -608       C  
ATOM   1537  CG  ASP A 206     -25.616  27.907 -20.988  1.00 50.13           C  
ANISOU 1537  CG  ASP A 206     5950   6626   6471    -51    172   -622       C  
ATOM   1538  OD1 ASP A 206     -26.500  27.833 -20.110  1.00 50.87           O  
ANISOU 1538  OD1 ASP A 206     6039   6703   6588    -26    190   -614       O  
ATOM   1539  OD2 ASP A 206     -24.571  27.223 -20.961  1.00 44.81           O1-
ANISOU 1539  OD2 ASP A 206     5261   5997   5769    -72    155   -640       O1-
ATOM   1540  N   TYR A 207     -23.096  30.663 -22.501  1.00 39.44           N  
ANISOU 1540  N   TYR A 207     4699   5254   5033   -167    206   -671       N  
ATOM   1541  CA  TYR A 207     -21.658  30.814 -22.331  1.00 38.84           C  
ANISOU 1541  CA  TYR A 207     4622   5219   4914   -222    213   -709       C  
ATOM   1542  C   TYR A 207     -21.242  32.255 -22.063  1.00 42.33           C  
ANISOU 1542  C   TYR A 207     5121   5629   5334   -266    253   -731       C  
ATOM   1543  O   TYR A 207     -20.046  32.517 -21.898  1.00 44.13           O  
ANISOU 1543  O   TYR A 207     5350   5892   5527   -320    263   -768       O  
ATOM   1544  CB  TYR A 207     -20.923  30.294 -23.571  1.00 45.31           C  
ANISOU 1544  CB  TYR A 207     5424   6072   5722   -239    189   -710       C  
ATOM   1545  CG  TYR A 207     -21.265  28.868 -23.944  1.00 35.78           C  
ANISOU 1545  CG  TYR A 207     4169   4893   4534   -199    151   -692       C  
ATOM   1546  CD1 TYR A 207     -20.551  27.801 -23.416  1.00 33.45           C  
ANISOU 1546  CD1 TYR A 207     3830   4655   4227   -197    134   -710       C  
ATOM   1547  CD2 TYR A 207     -22.300  28.590 -24.828  1.00 35.81           C  
ANISOU 1547  CD2 TYR A 207     4174   4867   4566   -164    132   -656       C  
ATOM   1548  CE1 TYR A 207     -20.859  26.497 -23.756  1.00 35.43           C  
ANISOU 1548  CE1 TYR A 207     4045   4924   4492   -162    103   -694       C  
ATOM   1549  CE2 TYR A 207     -22.616  27.290 -25.173  1.00 31.19           C  
ANISOU 1549  CE2 TYR A 207     3550   4305   3997   -135     99   -641       C  
ATOM   1550  CZ  TYR A 207     -21.892  26.247 -24.635  1.00 31.60           C  
ANISOU 1550  CZ  TYR A 207     3565   4407   4036   -135     87   -660       C  
ATOM   1551  OH  TYR A 207     -22.202  24.951 -24.975  1.00 28.14           O  
ANISOU 1551  OH  TYR A 207     3096   3985   3612   -107     59   -647       O  
ATOM   1552  N   GLU A 208     -22.190  33.188 -22.020  1.00 46.88           N  
ANISOU 1552  N   GLU A 208     5744   6139   5929   -246    278   -712       N  
ATOM   1553  CA  GLU A 208     -21.851  34.593 -21.845  1.00 44.10           C  
ANISOU 1553  CA  GLU A 208     5458   5744   5554   -287    321   -731       C  
ATOM   1554  C   GLU A 208     -21.367  34.870 -20.427  1.00 43.82           C  
ANISOU 1554  C   GLU A 208     5429   5726   5496   -318    345   -768       C  
ATOM   1555  O   GLU A 208     -21.934  34.373 -19.449  1.00 41.80           O  
ANISOU 1555  O   GLU A 208     5150   5478   5256   -285    343   -765       O  
ATOM   1556  CB  GLU A 208     -23.055  35.478 -22.167  1.00 41.97           C  
ANISOU 1556  CB  GLU A 208     5239   5395   5312   -246    340   -697       C  
ATOM   1557  CG  GLU A 208     -22.766  36.968 -22.059  1.00 44.21           C  
ANISOU 1557  CG  GLU A 208     5604   5622   5572   -285    388   -714       C  
ATOM   1558  CD  GLU A 208     -23.803  37.819 -22.762  1.00 56.40           C  
ANISOU 1558  CD  GLU A 208     7202   7088   7139   -240    401   -675       C  
ATOM   1559  OE1 GLU A 208     -24.965  37.376 -22.869  1.00 60.19           O  
ANISOU 1559  OE1 GLU A 208     7653   7557   7661   -172    380   -640       O  
ATOM   1560  OE2 GLU A 208     -23.455  38.933 -23.207  1.00 60.81           O1-
ANISOU 1560  OE2 GLU A 208     7834   7597   7674   -273    432   -680       O1-
ATOM   1561  N   VAL A 209     -20.307  35.668 -20.323  1.00 38.56           N  
ANISOU 1561  N   VAL A 209     4794   5066   4791   -386    369   -806       N  
ATOM   1562  CA  VAL A 209     -19.759  36.114 -19.047  1.00 36.58           C  
ANISOU 1562  CA  VAL A 209     4559   4830   4512   -427    394   -847       C  
ATOM   1563  C   VAL A 209     -19.522  37.615 -19.133  1.00 43.16           C  
ANISOU 1563  C   VAL A 209     5472   5603   5322   -479    442   -866       C  
ATOM   1564  O   VAL A 209     -18.961  38.102 -20.122  1.00 43.39           O  
ANISOU 1564  O   VAL A 209     5527   5623   5337   -518    450   -869       O  
ATOM   1565  CB  VAL A 209     -18.453  35.378 -18.693  1.00 34.81           C  
ANISOU 1565  CB  VAL A 209     4276   4694   4254   -470    367   -884       C  
ATOM   1566  CG1 VAL A 209     -17.816  35.994 -17.459  1.00 39.69           C  
ANISOU 1566  CG1 VAL A 209     4917   5329   4836   -522    390   -930       C  
ATOM   1567  CG2 VAL A 209     -18.717  33.896 -18.479  1.00 26.47           C  
ANISOU 1567  CG2 VAL A 209     3152   3689   3218   -415    323   -865       C  
ATOM   1568  N   ASN A 210     -19.949  38.345 -18.105  1.00 54.30           N  
ANISOU 1568  N   ASN A 210     6931   6973   6730   -480    478   -878       N  
ATOM   1569  CA  ASN A 210     -19.797  39.791 -18.060  1.00 57.22           C  
ANISOU 1569  CA  ASN A 210     7387   7277   7078   -527    530   -898       C  
ATOM   1570  C   ASN A 210     -19.266  40.217 -16.699  1.00 60.28           C  
ANISOU 1570  C   ASN A 210     7795   7680   7430   -578    555   -946       C  
ATOM   1571  O   ASN A 210     -19.392  39.500 -15.703  1.00 66.77           O  
ANISOU 1571  O   ASN A 210     8576   8542   8251   -556    537   -953       O  
ATOM   1572  CB  ASN A 210     -21.125  40.510 -18.340  1.00 61.48           C  
ANISOU 1572  CB  ASN A 210     7986   7722   7652   -466    558   -858       C  
ATOM   1573  CG  ASN A 210     -21.654  40.237 -19.733  1.00 61.51           C  
ANISOU 1573  CG  ASN A 210     7979   7707   7684   -419    532   -811       C  
ATOM   1574  OD1 ASN A 210     -22.635  39.514 -19.906  1.00 71.12           O  
ANISOU 1574  OD1 ASN A 210     9154   8926   8942   -347    504   -773       O  
ATOM   1575  ND2 ASN A 210     -21.008  40.819 -20.737  1.00 62.40           N  
ANISOU 1575  ND2 ASN A 210     8132   7803   7774   -465    541   -814       N  
ATOM   1576  N   GLY A 211     -18.658  41.401 -16.676  1.00 74.15           N  
ANISOU 1576  N   GLY A 211     9621   9400   9153   -649    597   -979       N  
ATOM   1577  CA  GLY A 211     -18.240  42.023 -15.437  1.00 80.62           C  
ANISOU 1577  CA  GLY A 211    10478  10219   9936   -703    627  -1027       C  
ATOM   1578  C   GLY A 211     -17.113  41.338 -14.704  1.00 70.29           C  
ANISOU 1578  C   GLY A 211     9104   9012   8591   -754    594  -1071       C  
ATOM   1579  O   GLY A 211     -16.847  41.686 -13.550  1.00 80.08           O  
ANISOU 1579  O   GLY A 211    10366  10260   9799   -791    610  -1108       O  
ATOM   1580  N   VAL A 212     -16.434  40.381 -15.324  1.00 32.21           N  
ANISOU 1580  N   VAL A 212     4201   4266   3770   -756    547  -1068       N  
ATOM   1581  CA  VAL A 212     -15.320  39.696 -14.685  1.00 43.27           C  
ANISOU 1581  CA  VAL A 212     5534   5768   5138   -796    510  -1108       C  
ATOM   1582  C   VAL A 212     -14.101  39.916 -15.568  1.00 46.91           C  
ANISOU 1582  C   VAL A 212     5972   6273   5579   -870    507  -1136       C  
ATOM   1583  O   VAL A 212     -14.015  39.358 -16.671  1.00 49.03           O  
ANISOU 1583  O   VAL A 212     6202   6559   5869   -847    487  -1111       O  
ATOM   1584  CB  VAL A 212     -15.596  38.202 -14.472  1.00 39.60           C  
ANISOU 1584  CB  VAL A 212     4988   5364   4696   -723    456  -1080       C  
ATOM   1585  CG1 VAL A 212     -14.315  37.487 -14.133  1.00 43.38           C  
ANISOU 1585  CG1 VAL A 212     5392   5949   5141   -760    413  -1117       C  
ATOM   1586  CG2 VAL A 212     -16.620  37.999 -13.370  1.00 28.22           C  
ANISOU 1586  CG2 VAL A 212     3568   3891   3264   -668    463  -1063       C  
ATOM   1587  N   ASP A 213     -13.172  40.747 -15.098  1.00 72.13           N  
ANISOU 1587  N   ASP A 213     9191   9485   8730   -963    531  -1192       N  
ATOM   1588  CA  ASP A 213     -11.993  41.083 -15.885  1.00 67.65           C  
ANISOU 1588  CA  ASP A 213     8605   8957   8140  -1045    539  -1226       C  
ATOM   1589  C   ASP A 213     -11.161  39.838 -16.160  1.00 68.10           C  
ANISOU 1589  C   ASP A 213     8550   9125   8200  -1031    483  -1232       C  
ATOM   1590  O   ASP A 213     -10.862  39.060 -15.249  1.00 69.93           O  
ANISOU 1590  O   ASP A 213     8722   9429   8420  -1011    441  -1246       O  
ATOM   1591  CB  ASP A 213     -11.151  42.132 -15.156  1.00 76.10           C  
ANISOU 1591  CB  ASP A 213     9717  10036   9163  -1151    572  -1290       C  
ATOM   1592  CG  ASP A 213     -11.997  43.155 -14.424  1.00 92.92           C  
ANISOU 1592  CG  ASP A 213    11951  12067  11286  -1152    621  -1289       C  
ATOM   1593  OD1 ASP A 213     -13.000  43.624 -15.002  1.00 82.48           O  
ANISOU 1593  OD1 ASP A 213    10698  10648   9993  -1105    653  -1246       O  
ATOM   1594  OD2 ASP A 213     -11.658  43.491 -13.269  1.00 93.56           O1-
ANISOU 1594  OD2 ASP A 213    12048  12170  11332  -1198    626  -1333       O1-
ATOM   1595  N   GLY A 214     -10.793  39.648 -17.425  1.00 50.86           N  
ANISOU 1595  N   GLY A 214     6342   6952   6029  -1040    483  -1220       N  
ATOM   1596  CA  GLY A 214      -9.973  38.527 -17.824  1.00 54.13           C  
ANISOU 1596  CA  GLY A 214     6654   7464   6446  -1027    437  -1228       C  
ATOM   1597  C   GLY A 214     -10.707  37.220 -18.027  1.00 55.69           C  
ANISOU 1597  C   GLY A 214     6805   7673   6680   -922    392  -1177       C  
ATOM   1598  O   GLY A 214     -10.106  36.267 -18.539  1.00 59.23           O  
ANISOU 1598  O   GLY A 214     7178   8192   7135   -903    359  -1177       O  
ATOM   1599  N   TYR A 215     -11.984  37.135 -17.656  1.00 54.87           N  
ANISOU 1599  N   TYR A 215     6743   7503   6601   -853    394  -1135       N  
ATOM   1600  CA  TYR A 215     -12.754  35.910 -17.818  1.00 48.99           C  
ANISOU 1600  CA  TYR A 215     5959   6765   5891   -758    355  -1088       C  
ATOM   1601  C   TYR A 215     -14.039  36.114 -18.605  1.00 46.65           C  
ANISOU 1601  C   TYR A 215     5714   6377   5632   -705    372  -1034       C  
ATOM   1602  O   TYR A 215     -14.839  35.175 -18.706  1.00 44.45           O  
ANISOU 1602  O   TYR A 215     5410   6095   5384   -630    344   -995       O  
ATOM   1603  CB  TYR A 215     -13.104  35.309 -16.452  1.00 49.90           C  
ANISOU 1603  CB  TYR A 215     6054   6903   6001   -716    330  -1087       C  
ATOM   1604  CG  TYR A 215     -11.942  34.735 -15.680  1.00 50.20           C  
ANISOU 1604  CG  TYR A 215     6026   7043   6006   -742    294  -1129       C  
ATOM   1605  CD1 TYR A 215     -11.340  33.545 -16.064  1.00 51.87           C  
ANISOU 1605  CD1 TYR A 215     6157   7329   6223   -709    249  -1125       C  
ATOM   1606  CD2 TYR A 215     -11.445  35.390 -14.560  1.00 56.42           C  
ANISOU 1606  CD2 TYR A 215     6832   7852   6754   -797    302  -1173       C  
ATOM   1607  CE1 TYR A 215     -10.279  33.019 -15.347  1.00 60.05           C  
ANISOU 1607  CE1 TYR A 215     7129   8460   7228   -724    213  -1161       C  
ATOM   1608  CE2 TYR A 215     -10.388  34.877 -13.843  1.00 55.56           C  
ANISOU 1608  CE2 TYR A 215     6659   7840   6611   -818    263  -1210       C  
ATOM   1609  CZ  TYR A 215      -9.807  33.689 -14.243  1.00 55.45           C  
ANISOU 1609  CZ  TYR A 215     6561   7900   6605   -778    217  -1203       C  
ATOM   1610  OH  TYR A 215      -8.751  33.157 -13.544  1.00 65.34           O  
ANISOU 1610  OH  TYR A 215     7747   9253   7826   -789    175  -1239       O  
ATOM   1611  N   ASP A 216     -14.272  37.306 -19.146  1.00 49.82           N  
ANISOU 1611  N   ASP A 216     6191   6707   6030   -741    416  -1032       N  
ATOM   1612  CA  ASP A 216     -15.497  37.565 -19.883  1.00 53.04           C  
ANISOU 1612  CA  ASP A 216     6649   7030   6472   -686    429   -981       C  
ATOM   1613  C   ASP A 216     -15.531  36.746 -21.170  1.00 48.34           C  
ANISOU 1613  C   ASP A 216     6017   6455   5897   -653    400   -950       C  
ATOM   1614  O   ASP A 216     -14.504  36.291 -21.680  1.00 39.30           O  
ANISOU 1614  O   ASP A 216     4823   5372   4735   -688    386   -973       O  
ATOM   1615  CB  ASP A 216     -15.633  39.055 -20.200  1.00 53.75           C  
ANISOU 1615  CB  ASP A 216     6836   7038   6548   -733    483   -986       C  
ATOM   1616  CG  ASP A 216     -16.122  39.861 -19.014  1.00 52.71           C  
ANISOU 1616  CG  ASP A 216     6760   6857   6409   -737    516  -1000       C  
ATOM   1617  OD1 ASP A 216     -16.471  39.250 -17.983  1.00 53.23           O  
ANISOU 1617  OD1 ASP A 216     6792   6950   6483   -700    496  -1001       O  
ATOM   1618  OD2 ASP A 216     -16.157  41.107 -19.112  1.00 64.38           O1-
ANISOU 1618  OD2 ASP A 216     8323   8267   7873   -779    564  -1011       O1-
ATOM   1619  N   TYR A 217     -16.742  36.557 -21.690  1.00 50.49           N  
ANISOU 1619  N   TYR A 217     6308   6672   6204   -585    391   -900       N  
ATOM   1620  CA  TYR A 217     -16.949  35.731 -22.876  1.00 47.24           C  
ANISOU 1620  CA  TYR A 217     5865   6273   5811   -547    360   -868       C  
ATOM   1621  C   TYR A 217     -18.222  36.199 -23.561  1.00 45.88           C  
ANISOU 1621  C   TYR A 217     5748   6019   5667   -497    367   -819       C  
ATOM   1622  O   TYR A 217     -19.305  36.105 -22.977  1.00 48.18           O  
ANISOU 1622  O   TYR A 217     6042   6278   5987   -441    362   -795       O  
ATOM   1623  CB  TYR A 217     -17.045  34.254 -22.493  1.00 37.68           C  
ANISOU 1623  CB  TYR A 217     4575   5124   4618   -496    314   -860       C  
ATOM   1624  CG  TYR A 217     -16.866  33.291 -23.643  1.00 43.77           C  
ANISOU 1624  CG  TYR A 217     5305   5927   5398   -476    283   -842       C  
ATOM   1625  CD1 TYR A 217     -17.950  32.890 -24.413  1.00 45.05           C  
ANISOU 1625  CD1 TYR A 217     5476   6051   5592   -419    264   -796       C  
ATOM   1626  CD2 TYR A 217     -15.615  32.773 -23.951  1.00 45.50           C  
ANISOU 1626  CD2 TYR A 217     5477   6217   5595   -512    273   -874       C  
ATOM   1627  CE1 TYR A 217     -17.792  32.005 -25.461  1.00 45.08           C  
ANISOU 1627  CE1 TYR A 217     5447   6081   5598   -403    236   -782       C  
ATOM   1628  CE2 TYR A 217     -15.448  31.888 -24.998  1.00 54.34           C  
ANISOU 1628  CE2 TYR A 217     6564   7363   6722   -492    249   -860       C  
ATOM   1629  CZ  TYR A 217     -16.539  31.508 -25.750  1.00 51.80           C  
ANISOU 1629  CZ  TYR A 217     6258   6997   6426   -440    231   -814       C  
ATOM   1630  OH  TYR A 217     -16.379  30.626 -26.793  1.00 43.83           O  
ANISOU 1630  OH  TYR A 217     5222   6012   5420   -423    208   -803       O  
ATOM   1631  N   SER A 218     -18.098  36.704 -24.785  1.00 39.37           N  
ANISOU 1631  N   SER A 218     4965   5162   4832   -517    377   -806       N  
ATOM   1632  CA  SER A 218     -19.261  37.206 -25.497  1.00 41.62           C  
ANISOU 1632  CA  SER A 218     5304   5370   5138   -468    379   -758       C  
ATOM   1633  C   SER A 218     -20.018  36.062 -26.167  1.00 48.74           C  
ANISOU 1633  C   SER A 218     6157   6291   6071   -402    330   -720       C  
ATOM   1634  O   SER A 218     -19.486  34.969 -26.385  1.00 39.57           O  
ANISOU 1634  O   SER A 218     4933   5194   4908   -404    301   -729       O  
ATOM   1635  CB  SER A 218     -18.851  38.247 -26.540  1.00 39.79           C  
ANISOU 1635  CB  SER A 218     5151   5091   4878   -515    410   -756       C  
ATOM   1636  OG  SER A 218     -18.078  37.664 -27.573  1.00 48.42           O  
ANISOU 1636  OG  SER A 218     6215   6229   5952   -544    394   -762       O  
ATOM   1637  N   ARG A 219     -21.285  36.329 -26.489  1.00 50.62           N  
ANISOU 1637  N   ARG A 219     6424   6472   6338   -341    322   -676       N  
ATOM   1638  CA  ARG A 219     -22.099  35.332 -27.177  1.00 43.96           C  
ANISOU 1638  CA  ARG A 219     5538   5642   5524   -283    275   -640       C  
ATOM   1639  C   ARG A 219     -21.559  35.047 -28.572  1.00 51.16           C  
ANISOU 1639  C   ARG A 219     6456   6570   6412   -306    257   -632       C  
ATOM   1640  O   ARG A 219     -21.596  33.902 -29.036  1.00 49.10           O  
ANISOU 1640  O   ARG A 219     6143   6352   6160   -286    219   -624       O  
ATOM   1641  CB  ARG A 219     -23.553  35.798 -27.243  1.00 43.94           C  
ANISOU 1641  CB  ARG A 219     5561   5577   5555   -216    270   -598       C  
ATOM   1642  CG  ARG A 219     -24.114  36.238 -25.901  1.00 46.28           C  
ANISOU 1642  CG  ARG A 219     5862   5850   5874   -194    298   -606       C  
ATOM   1643  CD  ARG A 219     -25.622  36.405 -25.955  1.00 44.10           C  
ANISOU 1643  CD  ARG A 219     5586   5528   5641   -117    287   -564       C  
ATOM   1644  NE  ARG A 219     -26.018  37.631 -26.636  1.00 43.77           N  
ANISOU 1644  NE  ARG A 219     5623   5414   5593   -102    305   -540       N  
ATOM   1645  CZ  ARG A 219     -26.265  38.782 -26.024  1.00 54.21           C  
ANISOU 1645  CZ  ARG A 219     7006   6677   6916    -97    350   -545       C  
ATOM   1646  NH1 ARG A 219     -26.164  38.902 -24.710  1.00 58.26           N  
ANISOU 1646  NH1 ARG A 219     7510   7193   7432   -109    383   -574       N  
ATOM   1647  NH2 ARG A 219     -26.624  39.838 -26.748  1.00 55.84           N  
ANISOU 1647  NH2 ARG A 219     7289   6814   7115    -77    364   -519       N  
ATOM   1648  N   GLY A 220     -21.060  36.077 -29.259  1.00 51.50           N  
ANISOU 1648  N   GLY A 220     6570   6574   6422   -349    286   -636       N  
ATOM   1649  CA  GLY A 220     -20.465  35.872 -30.567  1.00 48.05           C  
ANISOU 1649  CA  GLY A 220     6148   6151   5958   -378    277   -632       C  
ATOM   1650  C   GLY A 220     -19.129  35.162 -30.525  1.00 49.11           C  
ANISOU 1650  C   GLY A 220     6230   6361   6069   -433    282   -675       C  
ATOM   1651  O   GLY A 220     -18.731  34.551 -31.523  1.00 53.14           O  
ANISOU 1651  O   GLY A 220     6726   6899   6565   -443    265   -673       O  
ATOM   1652  N   GLN A 221     -18.426  35.230 -29.392  1.00 41.22           N  
ANISOU 1652  N   GLN A 221     5200   5395   5065   -468    303   -716       N  
ATOM   1653  CA  GLN A 221     -17.149  34.534 -29.271  1.00 39.22           C  
ANISOU 1653  CA  GLN A 221     4888   5221   4793   -513    303   -758       C  
ATOM   1654  C   GLN A 221     -17.327  33.024 -29.358  1.00 39.72           C  
ANISOU 1654  C   GLN A 221     4877   5338   4878   -464    257   -748       C  
ATOM   1655  O   GLN A 221     -16.403  32.313 -29.771  1.00 44.34           O  
ANISOU 1655  O   GLN A 221     5420   5981   5449   -487    250   -772       O  
ATOM   1656  CB  GLN A 221     -16.462  34.917 -27.959  1.00 36.56           C  
ANISOU 1656  CB  GLN A 221     4533   4912   4447   -553    327   -801       C  
ATOM   1657  CG  GLN A 221     -15.050  34.368 -27.799  1.00 48.39           C  
ANISOU 1657  CG  GLN A 221     5968   6495   5922   -604    329   -849       C  
ATOM   1658  CD  GLN A 221     -14.059  34.982 -28.773  1.00 64.17           C  
ANISOU 1658  CD  GLN A 221     7997   8498   7887   -676    363   -872       C  
ATOM   1659  OE1 GLN A 221     -14.300  36.051 -29.334  1.00 63.14           O  
ANISOU 1659  OE1 GLN A 221     7948   8301   7741   -704    395   -859       O  
ATOM   1660  NE2 GLN A 221     -12.934  34.304 -28.976  1.00 56.47           N  
ANISOU 1660  NE2 GLN A 221     6958   7600   6898   -707    360   -906       N  
ATOM   1661  N   LEU A 222     -18.503  32.518 -28.977  1.00 40.88           N  
ANISOU 1661  N   LEU A 222     5007   5466   5060   -398    227   -716       N  
ATOM   1662  CA  LEU A 222     -18.761  31.087 -29.100  1.00 33.89           C  
ANISOU 1662  CA  LEU A 222     4061   4622   4195   -354    186   -706       C  
ATOM   1663  C   LEU A 222     -18.705  30.643 -30.554  1.00 38.19           C  
ANISOU 1663  C   LEU A 222     4614   5168   4728   -353    168   -690       C  
ATOM   1664  O   LEU A 222     -18.144  29.586 -30.866  1.00 36.85           O  
ANISOU 1664  O   LEU A 222     4399   5049   4554   -352    151   -703       O  
ATOM   1665  CB  LEU A 222     -20.116  30.737 -28.489  1.00 32.22           C  
ANISOU 1665  CB  LEU A 222     3836   4384   4023   -291    164   -674       C  
ATOM   1666  CG  LEU A 222     -20.523  29.270 -28.652  1.00 29.34           C  
ANISOU 1666  CG  LEU A 222     3416   4051   3679   -248    123   -660       C  
ATOM   1667  CD1 LEU A 222     -19.643  28.370 -27.797  1.00 26.96           C  
ANISOU 1667  CD1 LEU A 222     3061   3812   3371   -256    120   -692       C  
ATOM   1668  CD2 LEU A 222     -21.992  29.069 -28.319  1.00 20.49           C  
ANISOU 1668  CD2 LEU A 222     2290   2897   2599   -193    105   -625       C  
ATOM   1669  N   ILE A 223     -19.283  31.435 -31.460  1.00 42.15           N  
ANISOU 1669  N   ILE A 223     5178   5613   5223   -352    172   -661       N  
ATOM   1670  CA  ILE A 223     -19.206  31.108 -32.881  1.00 39.00           C  
ANISOU 1670  CA  ILE A 223     4800   5214   4806   -356    157   -646       C  
ATOM   1671  C   ILE A 223     -17.752  31.049 -33.326  1.00 44.20           C  
ANISOU 1671  C   ILE A 223     5451   5916   5428   -418    185   -685       C  
ATOM   1672  O   ILE A 223     -17.309  30.064 -33.925  1.00 44.93           O  
ANISOU 1672  O   ILE A 223     5509   6050   5513   -417    170   -694       O  
ATOM   1673  CB  ILE A 223     -20.012  32.118 -33.716  1.00 45.49           C  
ANISOU 1673  CB  ILE A 223     5700   5966   5620   -346    158   -608       C  
ATOM   1674  CG1 ILE A 223     -21.384  32.358 -33.086  1.00 42.74           C  
ANISOU 1674  CG1 ILE A 223     5352   5577   5311   -285    138   -575       C  
ATOM   1675  CG2 ILE A 223     -20.167  31.623 -35.146  1.00 38.83           C  
ANISOU 1675  CG2 ILE A 223     4875   5122   4758   -339    130   -586       C  
ATOM   1676  CD1 ILE A 223     -22.208  33.410 -33.794  1.00 45.72           C  
ANISOU 1676  CD1 ILE A 223     5804   5885   5684   -264    138   -536       C  
ATOM   1677  N   GLU A 224     -16.975  32.086 -33.000  1.00 50.82           N  
ANISOU 1677  N   GLU A 224     6320   6747   6244   -474    229   -712       N  
ATOM   1678  CA  GLU A 224     -15.568  32.095 -33.388  1.00 44.05           C  
ANISOU 1678  CA  GLU A 224     5449   5936   5353   -539    260   -753       C  
ATOM   1679  C   GLU A 224     -14.821  30.917 -32.778  1.00 38.41           C  
ANISOU 1679  C   GLU A 224     4644   5301   4648   -530    244   -786       C  
ATOM   1680  O   GLU A 224     -14.010  30.272 -33.450  1.00 41.83           O  
ANISOU 1680  O   GLU A 224     5047   5780   5066   -548    248   -806       O  
ATOM   1681  CB  GLU A 224     -14.910  33.412 -32.976  1.00 48.12           C  
ANISOU 1681  CB  GLU A 224     6008   6432   5846   -605    310   -780       C  
ATOM   1682  CG  GLU A 224     -15.790  34.636 -33.147  1.00 67.37           C  
ANISOU 1682  CG  GLU A 224     8536   8781   8280   -600    326   -747       C  
ATOM   1683  CD  GLU A 224     -15.078  35.918 -32.760  1.00 81.79           C  
ANISOU 1683  CD  GLU A 224    10412  10583  10079   -673    381   -778       C  
ATOM   1684  OE1 GLU A 224     -13.837  35.971 -32.884  1.00 84.01           O  
ANISOU 1684  OE1 GLU A 224    10673  10912  10335   -742    411   -821       O  
ATOM   1685  OE2 GLU A 224     -15.760  36.874 -32.331  1.00 74.34           O1-
ANISOU 1685  OE2 GLU A 224     9530   9575   9142   -662    395   -760       O1-
ATOM   1686  N   ASP A 225     -15.094  30.610 -31.508  1.00 37.30           N  
ANISOU 1686  N   ASP A 225     4462   5178   4533   -500    229   -791       N  
ATOM   1687  CA  ASP A 225     -14.369  29.535 -30.838  1.00 41.77           C  
ANISOU 1687  CA  ASP A 225     4947   5817   5104   -488    213   -820       C  
ATOM   1688  C   ASP A 225     -14.795  28.165 -31.352  1.00 42.27           C  
ANISOU 1688  C   ASP A 225     4978   5897   5185   -432    175   -799       C  
ATOM   1689  O   ASP A 225     -13.959  27.265 -31.493  1.00 40.81           O  
ANISOU 1689  O   ASP A 225     4743   5769   4994   -431    169   -823       O  
ATOM   1690  CB  ASP A 225     -14.568  29.634 -29.328  1.00 46.71           C  
ANISOU 1690  CB  ASP A 225     5550   6453   5746   -473    207   -829       C  
ATOM   1691  CG  ASP A 225     -13.595  30.598 -28.678  1.00 54.17           C  
ANISOU 1691  CG  ASP A 225     6497   7419   6667   -538    242   -871       C  
ATOM   1692  OD1 ASP A 225     -12.416  30.618 -29.091  1.00 56.10           O  
ANISOU 1692  OD1 ASP A 225     6716   7712   6888   -587    261   -907       O  
ATOM   1693  OD2 ASP A 225     -14.008  31.338 -27.761  1.00 58.10           O1-
ANISOU 1693  OD2 ASP A 225     7021   7886   7168   -543    253   -871       O1-
ATOM   1694  N   VAL A 226     -16.088  27.978 -31.624  1.00 41.74           N  
ANISOU 1694  N   VAL A 226     4938   5780   5139   -387    149   -757       N  
ATOM   1695  CA  VAL A 226     -16.548  26.698 -32.159  1.00 38.02           C  
ANISOU 1695  CA  VAL A 226     4443   5320   4683   -342    114   -738       C  
ATOM   1696  C   VAL A 226     -15.963  26.464 -33.547  1.00 38.85           C  
ANISOU 1696  C   VAL A 226     4564   5436   4761   -366    121   -745       C  
ATOM   1697  O   VAL A 226     -15.443  25.383 -33.846  1.00 40.34           O  
ANISOU 1697  O   VAL A 226     4715   5666   4947   -353    111   -760       O  
ATOM   1698  CB  VAL A 226     -18.086  26.636 -32.172  1.00 38.73           C  
ANISOU 1698  CB  VAL A 226     4555   5358   4802   -295     85   -694       C  
ATOM   1699  CG1 VAL A 226     -18.566  25.528 -33.092  1.00 34.55           C  
ANISOU 1699  CG1 VAL A 226     4018   4831   4278   -265     52   -675       C  
ATOM   1700  CG2 VAL A 226     -18.617  26.416 -30.766  1.00 35.24           C  
ANISOU 1700  CG2 VAL A 226     4083   4919   4389   -263     77   -691       C  
ATOM   1701  N   GLU A 227     -16.030  27.479 -34.414  1.00 43.16           N  
ANISOU 1701  N   GLU A 227     5171   5942   5285   -400    141   -734       N  
ATOM   1702  CA  GLU A 227     -15.477  27.336 -35.760  1.00 40.72           C  
ANISOU 1702  CA  GLU A 227     4887   5639   4944   -428    153   -740       C  
ATOM   1703  C   GLU A 227     -13.958  27.202 -35.733  1.00 46.65           C  
ANISOU 1703  C   GLU A 227     5598   6452   5674   -474    188   -790       C  
ATOM   1704  O   GLU A 227     -13.390  26.423 -36.506  1.00 49.77           O  
ANISOU 1704  O   GLU A 227     5977   6879   6056   -476    191   -804       O  
ATOM   1705  CB  GLU A 227     -15.907  28.509 -36.646  1.00 40.26           C  
ANISOU 1705  CB  GLU A 227     4912   5521   4863   -455    168   -715       C  
ATOM   1706  CG  GLU A 227     -17.398  28.806 -36.601  1.00 46.02           C  
ANISOU 1706  CG  GLU A 227     5676   6192   5615   -407    133   -667       C  
ATOM   1707  CD  GLU A 227     -17.771  30.084 -37.329  1.00 63.89           C  
ANISOU 1707  CD  GLU A 227     8026   8394   7854   -427    149   -642       C  
ATOM   1708  OE1 GLU A 227     -17.020  31.073 -37.203  1.00 65.27           O  
ANISOU 1708  OE1 GLU A 227     8234   8558   8006   -479    194   -662       O  
ATOM   1709  OE2 GLU A 227     -18.829  30.114 -37.995  1.00 60.87           O1-
ANISOU 1709  OE2 GLU A 227     7680   7972   7475   -391    115   -601       O1-
ATOM   1710  N   HIS A 228     -13.280  27.952 -34.859  1.00 50.34           N  
ANISOU 1710  N   HIS A 228     6050   6939   6139   -511    216   -818       N  
ATOM   1711  CA  HIS A 228     -11.825  27.853 -34.783  1.00 47.70           C  
ANISOU 1711  CA  HIS A 228     5668   6671   5786   -556    248   -868       C  
ATOM   1712  C   HIS A 228     -11.391  26.473 -34.300  1.00 45.88           C  
ANISOU 1712  C   HIS A 228     5357   6503   5573   -510    222   -886       C  
ATOM   1713  O   HIS A 228     -10.486  25.858 -34.876  1.00 53.10           O  
ANISOU 1713  O   HIS A 228     6236   7464   6474   -520    236   -913       O  
ATOM   1714  CB  HIS A 228     -11.264  28.941 -33.868  1.00 47.70           C  
ANISOU 1714  CB  HIS A 228     5665   6679   5778   -607    278   -896       C  
ATOM   1715  CG  HIS A 228      -9.769  28.999 -33.848  1.00 63.55           C  
ANISOU 1715  CG  HIS A 228     7623   8758   7766   -663    312   -950       C  
ATOM   1716  ND1 HIS A 228      -9.004  28.173 -33.053  1.00 67.30           N  
ANISOU 1716  ND1 HIS A 228     8010   9309   8252   -644    297   -983       N  
ATOM   1717  CD2 HIS A 228      -8.898  29.781 -34.528  1.00 57.71           C  
ANISOU 1717  CD2 HIS A 228     6906   8026   6997   -738    362   -979       C  
ATOM   1718  CE1 HIS A 228      -7.725  28.445 -33.243  1.00 63.27           C  
ANISOU 1718  CE1 HIS A 228     7463   8856   7722   -703    333  -1030       C  
ATOM   1719  NE2 HIS A 228      -7.633  29.416 -34.133  1.00 62.77           N  
ANISOU 1719  NE2 HIS A 228     7464   8752   7633   -764    375  -1030       N  
ATOM   1720  N   THR A 229     -12.026  25.971 -33.239  1.00 45.98           N  
ANISOU 1720  N   THR A 229     5342   6515   5613   -460    188   -871       N  
ATOM   1721  CA  THR A 229     -11.697  24.636 -32.752  1.00 45.12           C  
ANISOU 1721  CA  THR A 229     5169   6458   5518   -411    163   -883       C  
ATOM   1722  C   THR A 229     -12.110  23.560 -33.747  1.00 42.67           C  
ANISOU 1722  C   THR A 229     4868   6134   5212   -373    144   -863       C  
ATOM   1723  O   THR A 229     -11.466  22.508 -33.823  1.00 44.46           O  
ANISOU 1723  O   THR A 229     5049   6405   5438   -346    139   -882       O  
ATOM   1724  CB  THR A 229     -12.359  24.383 -31.398  1.00 33.28           C  
ANISOU 1724  CB  THR A 229     3651   4952   4044   -368    134   -868       C  
ATOM   1725  OG1 THR A 229     -13.753  24.706 -31.475  1.00 38.46           O  
ANISOU 1725  OG1 THR A 229     4358   5539   4716   -348    120   -825       O  
ATOM   1726  CG2 THR A 229     -11.702  25.229 -30.315  1.00 35.02           C  
ANISOU 1726  CG2 THR A 229     3850   5201   4255   -405    151   -898       C  
ATOM   1727  N   PHE A 230     -13.177  23.802 -34.513  1.00 43.19           N  
ANISOU 1727  N   PHE A 230     4993   6140   5279   -367    133   -826       N  
ATOM   1728  CA  PHE A 230     -13.610  22.826 -35.506  1.00 39.35           C  
ANISOU 1728  CA  PHE A 230     4520   5639   4791   -339    114   -809       C  
ATOM   1729  C   PHE A 230     -12.623  22.715 -36.659  1.00 45.03           C  
ANISOU 1729  C   PHE A 230     5246   6385   5480   -372    144   -836       C  
ATOM   1730  O   PHE A 230     -12.465  21.632 -37.233  1.00 48.13           O  
ANISOU 1730  O   PHE A 230     5626   6792   5869   -347    136   -841       O  
ATOM   1731  CB  PHE A 230     -14.997  23.186 -36.033  1.00 38.22           C  
ANISOU 1731  CB  PHE A 230     4436   5432   4656   -327     90   -765       C  
ATOM   1732  CG  PHE A 230     -15.545  22.190 -37.008  1.00 41.00           C  
ANISOU 1732  CG  PHE A 230     4804   5768   5004   -301     64   -748       C  
ATOM   1733  CD1 PHE A 230     -15.840  20.901 -36.603  1.00 38.09           C  
ANISOU 1733  CD1 PHE A 230     4401   5414   4658   -256     38   -746       C  
ATOM   1734  CD2 PHE A 230     -15.757  22.539 -38.331  1.00 42.12           C  
ANISOU 1734  CD2 PHE A 230     5002   5882   5119   -325     67   -734       C  
ATOM   1735  CE1 PHE A 230     -16.339  19.978 -37.497  1.00 35.54           C  
ANISOU 1735  CE1 PHE A 230     4096   5075   4331   -238     16   -734       C  
ATOM   1736  CE2 PHE A 230     -16.259  21.619 -39.230  1.00 35.21           C  
ANISOU 1736  CE2 PHE A 230     4145   4996   4238   -306     41   -722       C  
ATOM   1737  CZ  PHE A 230     -16.550  20.337 -38.812  1.00 33.38           C  
ANISOU 1737  CZ  PHE A 230     3875   4777   4029   -264     17   -723       C  
ATOM   1738  N   GLU A 231     -11.962  23.819 -37.019  1.00 47.65           N  
ANISOU 1738  N   GLU A 231     5600   6719   5787   -432    183   -853       N  
ATOM   1739  CA  GLU A 231     -10.976  23.770 -38.095  1.00 42.92           C  
ANISOU 1739  CA  GLU A 231     5005   6146   5156   -470    220   -881       C  
ATOM   1740  C   GLU A 231      -9.837  22.820 -37.752  1.00 43.81           C  
ANISOU 1740  C   GLU A 231     5040   6332   5275   -454    230   -922       C  
ATOM   1741  O   GLU A 231      -9.320  22.115 -38.627  1.00 52.43           O  
ANISOU 1741  O   GLU A 231     6125   7445   6352   -450    245   -939       O  
ATOM   1742  CB  GLU A 231     -10.439  25.173 -38.382  1.00 39.48           C  
ANISOU 1742  CB  GLU A 231     4607   5700   4694   -544    265   -895       C  
ATOM   1743  CG  GLU A 231     -11.441  26.099 -39.051  1.00 54.52           C  
ANISOU 1743  CG  GLU A 231     6603   7528   6584   -559    261   -854       C  
ATOM   1744  CD  GLU A 231     -11.462  25.951 -40.561  1.00 67.87           C  
ANISOU 1744  CD  GLU A 231     8351   9198   8240   -576    272   -844       C  
ATOM   1745  OE1 GLU A 231     -10.757  25.063 -41.086  1.00 65.89           O  
ANISOU 1745  OE1 GLU A 231     8068   8988   7979   -573    285   -870       O  
ATOM   1746  OE2 GLU A 231     -12.185  26.725 -41.224  1.00 74.41           O1-
ANISOU 1746  OE2 GLU A 231     9257   9966   9048   -589    268   -810       O1-
ATOM   1747  N   GLU A 232      -9.431  22.787 -36.481  1.00 35.16           N  
ANISOU 1747  N   GLU A 232     3885   5277   4198   -440    222   -940       N  
ATOM   1748  CA  GLU A 232      -8.406  21.847 -36.049  1.00 42.04           C  
ANISOU 1748  CA  GLU A 232     4677   6220   5076   -412    224   -976       C  
ATOM   1749  C   GLU A 232      -8.929  20.418 -35.978  1.00 40.11           C  
ANISOU 1749  C   GLU A 232     4422   5969   4851   -337    187   -957       C  
ATOM   1750  O   GLU A 232      -8.128  19.479 -35.926  1.00 43.51           O  
ANISOU 1750  O   GLU A 232     4801   6448   5283   -304    190   -983       O  
ATOM   1751  CB  GLU A 232      -7.851  22.272 -34.689  1.00 50.49           C  
ANISOU 1751  CB  GLU A 232     5692   7335   6156   -419    220   -999       C  
ATOM   1752  CG  GLU A 232      -7.724  23.780 -34.526  1.00 53.40           C  
ANISOU 1752  CG  GLU A 232     6089   7689   6511   -492    249  -1008       C  
ATOM   1753  CD  GLU A 232      -6.768  24.171 -33.417  1.00 65.55           C  
ANISOU 1753  CD  GLU A 232     7563   9293   8050   -517    256  -1048       C  
ATOM   1754  OE1 GLU A 232      -5.718  23.509 -33.276  1.00 54.79           O  
ANISOU 1754  OE1 GLU A 232     6126   8004   6686   -504    259  -1083       O  
ATOM   1755  OE2 GLU A 232      -7.065  25.142 -32.690  1.00 72.80           O1-
ANISOU 1755  OE2 GLU A 232     8504  10190   8968   -549    257  -1044       O1-
ATOM   1756  N   ILE A 233     -10.251  20.234 -35.970  1.00 45.86           N  
ANISOU 1756  N   ILE A 233     5197   6636   5592   -310    154   -915       N  
ATOM   1757  CA  ILE A 233     -10.825  18.893 -35.956  1.00 44.68           C  
ANISOU 1757  CA  ILE A 233     5046   6473   5458   -248    123   -897       C  
ATOM   1758  C   ILE A 233     -10.882  18.305 -37.362  1.00 45.88           C  
ANISOU 1758  C   ILE A 233     5235   6607   5593   -249    132   -896       C  
ATOM   1759  O   ILE A 233     -10.732  17.088 -37.534  1.00 43.28           O  
ANISOU 1759  O   ILE A 233     4891   6287   5267   -207    124   -902       O  
ATOM   1760  CB  ILE A 233     -12.218  18.921 -35.302  1.00 36.65           C  
ANISOU 1760  CB  ILE A 233     4056   5404   4464   -222     86   -856       C  
ATOM   1761  CG1 ILE A 233     -12.110  18.713 -33.794  1.00 38.95           C  
ANISOU 1761  CG1 ILE A 233     4303   5721   4775   -191     70   -859       C  
ATOM   1762  CG2 ILE A 233     -13.140  17.868 -35.904  1.00 37.39           C  
ANISOU 1762  CG2 ILE A 233     4180   5459   4566   -187     60   -830       C  
ATOM   1763  CD1 ILE A 233     -13.338  19.165 -33.038  1.00 46.25           C  
ANISOU 1763  CD1 ILE A 233     5252   6600   5720   -183     48   -825       C  
ATOM   1764  N   LYS A 234     -11.059  19.152 -38.379  1.00 40.19           N  
ANISOU 1764  N   LYS A 234     4566   5857   4848   -299    151   -888       N  
ATOM   1765  CA  LYS A 234     -11.275  18.689 -39.750  1.00 28.60           C  
ANISOU 1765  CA  LYS A 234     3146   4364   3356   -305    155   -883       C  
ATOM   1766  C   LYS A 234     -10.267  17.644 -40.216  1.00 38.43           C  
ANISOU 1766  C   LYS A 234     4359   5651   4592   -285    180   -918       C  
ATOM   1767  O   LYS A 234     -10.696  16.633 -40.795  1.00 38.43           O  
ANISOU 1767  O   LYS A 234     4384   5629   4589   -255    164   -910       O  
ATOM   1768  CB  LYS A 234     -11.285  19.895 -40.700  1.00 24.49           C  
ANISOU 1768  CB  LYS A 234     2683   3817   2804   -366    181   -877       C  
ATOM   1769  CG  LYS A 234     -12.419  20.882 -40.463  1.00 30.07           C  
ANISOU 1769  CG  LYS A 234     3436   4472   3519   -377    156   -837       C  
ATOM   1770  CD  LYS A 234     -12.438  21.964 -41.535  1.00 42.85           C  
ANISOU 1770  CD  LYS A 234     5124   6058   5100   -431    180   -827       C  
ATOM   1771  CE  LYS A 234     -13.583  22.942 -41.324  1.00 41.90           C  
ANISOU 1771  CE  LYS A 234     5051   5881   4987   -432    154   -785       C  
ATOM   1772  NZ  LYS A 234     -13.695  23.915 -42.447  1.00 54.50           N  
ANISOU 1772  NZ  LYS A 234     6727   7438   6542   -476    172   -770       N  
ATOM   1773  N   PRO A 235      -8.950  17.800 -40.009  1.00 33.35           N  
ANISOU 1773  N   PRO A 235     3661   5067   3943   -300    217   -959       N  
ATOM   1774  CA  PRO A 235      -8.035  16.721 -40.426  1.00 31.63           C  
ANISOU 1774  CA  PRO A 235     3409   4890   3720   -270    240   -993       C  
ATOM   1775  C   PRO A 235      -8.355  15.376 -39.797  1.00 31.14           C  
ANISOU 1775  C   PRO A 235     3324   4825   3682   -195    206   -984       C  
ATOM   1776  O   PRO A 235      -8.330  14.352 -40.491  1.00 31.58           O  
ANISOU 1776  O   PRO A 235     3398   4870   3730   -166    210   -990       O  
ATOM   1777  CB  PRO A 235      -6.660  17.240 -39.982  1.00 27.72           C  
ANISOU 1777  CB  PRO A 235     2842   4468   3224   -295    277  -1036       C  
ATOM   1778  CG  PRO A 235      -6.808  18.710 -39.935  1.00 22.45           C  
ANISOU 1778  CG  PRO A 235     2201   3785   2545   -363    291  -1029       C  
ATOM   1779  CD  PRO A 235      -8.209  18.958 -39.474  1.00 27.49           C  
ANISOU 1779  CD  PRO A 235     2887   4360   3198   -348    244   -981       C  
ATOM   1780  N   LEU A 236      -8.676  15.350 -38.502  1.00 35.89           N  
ANISOU 1780  N   LEU A 236     3894   5433   4311   -164    174   -970       N  
ATOM   1781  CA  LEU A 236      -9.036  14.090 -37.860  1.00 30.82           C  
ANISOU 1781  CA  LEU A 236     3241   4781   3688    -95    143   -958       C  
ATOM   1782  C   LEU A 236     -10.346  13.546 -38.414  1.00 32.54           C  
ANISOU 1782  C   LEU A 236     3526   4931   3908    -86    116   -923       C  
ATOM   1783  O   LEU A 236     -10.487  12.334 -38.617  1.00 36.90           O  
ANISOU 1783  O   LEU A 236     4091   5468   4463    -44    108   -923       O  
ATOM   1784  CB  LEU A 236      -9.128  14.275 -36.345  1.00 30.46           C  
ANISOU 1784  CB  LEU A 236     3155   4754   3666    -71    116   -949       C  
ATOM   1785  CG  LEU A 236      -9.630  13.082 -35.527  1.00 24.56           C  
ANISOU 1785  CG  LEU A 236     2405   3988   2937     -3     84   -930       C  
ATOM   1786  CD1 LEU A 236      -8.763  11.854 -35.766  1.00 24.13           C  
ANISOU 1786  CD1 LEU A 236     2327   3963   2879     51     96   -954       C  
ATOM   1787  CD2 LEU A 236      -9.674  13.428 -34.047  1.00 20.56           C  
ANISOU 1787  CD2 LEU A 236     1864   3502   2446     13     61   -922       C  
ATOM   1788  N   TYR A 237     -11.316  14.427 -38.665  1.00 38.20           N  
ANISOU 1788  N   TYR A 237     4285   5606   4622   -126    101   -894       N  
ATOM   1789  CA  TYR A 237     -12.600  13.979 -39.193  1.00 35.77           C  
ANISOU 1789  CA  TYR A 237     4034   5241   4317   -122     71   -862       C  
ATOM   1790  C   TYR A 237     -12.482  13.536 -40.645  1.00 34.47           C  
ANISOU 1790  C   TYR A 237     3913   5061   4122   -138     87   -873       C  
ATOM   1791  O   TYR A 237     -13.040  12.502 -41.028  1.00 41.00           O  
ANISOU 1791  O   TYR A 237     4770   5859   4949   -115     70   -865       O  
ATOM   1792  CB  TYR A 237     -13.640  15.088 -39.062  1.00 36.74           C  
ANISOU 1792  CB  TYR A 237     4185   5329   4447   -153     49   -829       C  
ATOM   1793  CG  TYR A 237     -14.992  14.708 -39.614  1.00 31.67           C  
ANISOU 1793  CG  TYR A 237     3590   4634   3808   -150     14   -797       C  
ATOM   1794  CD1 TYR A 237     -15.738  13.689 -39.035  1.00 35.11           C  
ANISOU 1794  CD1 TYR A 237     4021   5050   4268   -112    -14   -782       C  
ATOM   1795  CD2 TYR A 237     -15.522  15.364 -40.717  1.00 31.77           C  
ANISOU 1795  CD2 TYR A 237     3656   4619   3798   -188      8   -781       C  
ATOM   1796  CE1 TYR A 237     -16.977  13.338 -39.535  1.00 31.18           C  
ANISOU 1796  CE1 TYR A 237     3561   4511   3775   -116    -46   -757       C  
ATOM   1797  CE2 TYR A 237     -16.760  15.020 -41.223  1.00 33.02           C  
ANISOU 1797  CE2 TYR A 237     3851   4736   3959   -186    -29   -754       C  
ATOM   1798  CZ  TYR A 237     -17.483  14.007 -40.629  1.00 35.46           C  
ANISOU 1798  CZ  TYR A 237     4146   5031   4295   -152    -56   -743       C  
ATOM   1799  OH  TYR A 237     -18.715  13.663 -41.132  1.00 32.74           O  
ANISOU 1799  OH  TYR A 237     3833   4652   3954   -155    -94   -719       O  
ATOM   1800  N   GLU A 238     -11.765  14.307 -41.469  1.00 37.75           N  
ANISOU 1800  N   GLU A 238     4339   5494   4508   -182    122   -892       N  
ATOM   1801  CA  GLU A 238     -11.632  13.957 -42.880  1.00 39.52           C  
ANISOU 1801  CA  GLU A 238     4613   5704   4698   -203    141   -903       C  
ATOM   1802  C   GLU A 238     -10.976  12.594 -43.051  1.00 44.61           C  
ANISOU 1802  C   GLU A 238     5242   6367   5342   -159    159   -931       C  
ATOM   1803  O   GLU A 238     -11.367  11.814 -43.927  1.00 48.33           O  
ANISOU 1803  O   GLU A 238     5761   6806   5795   -155    155   -930       O  
ATOM   1804  CB  GLU A 238     -10.834  15.031 -43.623  1.00 36.67           C  
ANISOU 1804  CB  GLU A 238     4264   5364   4306   -259    185   -921       C  
ATOM   1805  CG  GLU A 238     -11.540  16.373 -43.743  1.00 43.62           C  
ANISOU 1805  CG  GLU A 238     5184   6212   5177   -304    171   -891       C  
ATOM   1806  CD  GLU A 238     -10.794  17.346 -44.635  1.00 63.29           C  
ANISOU 1806  CD  GLU A 238     7705   8713   7629   -364    219   -908       C  
ATOM   1807  OE1 GLU A 238      -9.610  17.088 -44.939  1.00 57.63           O  
ANISOU 1807  OE1 GLU A 238     6958   8039   6899   -373    266   -948       O  
ATOM   1808  OE2 GLU A 238     -11.390  18.371 -45.030  1.00 71.12           O1-
ANISOU 1808  OE2 GLU A 238     8751   9669   8604   -400    210   -881       O1-
ATOM   1809  N   HIS A 239      -9.976  12.288 -42.223  1.00 38.65           N  
ANISOU 1809  N   HIS A 239     4419   5660   4605   -125    178   -957       N  
ATOM   1810  CA  HIS A 239      -9.336  10.979 -42.299  1.00 41.05           C  
ANISOU 1810  CA  HIS A 239     4706   5980   4911    -72    194   -982       C  
ATOM   1811  C   HIS A 239     -10.242   9.887 -41.743  1.00 39.20           C  
ANISOU 1811  C   HIS A 239     4492   5705   4698    -23    155   -958       C  
ATOM   1812  O   HIS A 239     -10.269   8.768 -42.269  1.00 41.16           O  
ANISOU 1812  O   HIS A 239     4771   5931   4937      5    161   -968       O  
ATOM   1813  CB  HIS A 239      -7.996  11.010 -41.567  1.00 46.18           C  
ANISOU 1813  CB  HIS A 239     5274   6699   5573    -45    221  -1016       C  
ATOM   1814  CG  HIS A 239      -6.902  11.664 -42.351  1.00 43.80           C  
ANISOU 1814  CG  HIS A 239     4952   6441   5248    -89    274  -1053       C  
ATOM   1815  ND1 HIS A 239      -6.237  11.026 -43.375  1.00 41.92           N  
ANISOU 1815  ND1 HIS A 239     4726   6212   4988    -82    316  -1083       N  
ATOM   1816  CD2 HIS A 239      -6.365  12.905 -42.270  1.00 44.53           C  
ANISOU 1816  CD2 HIS A 239     5017   6569   5334   -143    296  -1065       C  
ATOM   1817  CE1 HIS A 239      -5.334  11.842 -43.888  1.00 52.81           C  
ANISOU 1817  CE1 HIS A 239     6083   7633   6349   -131    363  -1112       C  
ATOM   1818  NE2 HIS A 239      -5.391  12.989 -43.235  1.00 53.76           N  
ANISOU 1818  NE2 HIS A 239     6179   7770   6479   -170    352  -1102       N  
ATOM   1819  N   LEU A 240     -10.987  10.187 -40.675  1.00 35.15           N  
ANISOU 1819  N   LEU A 240     3964   5179   4210    -15    118   -929       N  
ATOM   1820  CA  LEU A 240     -11.993   9.243 -40.198  1.00 33.76           C  
ANISOU 1820  CA  LEU A 240     3815   4959   4053     20     83   -904       C  
ATOM   1821  C   LEU A 240     -13.113   9.079 -41.218  1.00 37.27           C  
ANISOU 1821  C   LEU A 240     4328   5350   4483    -14     64   -885       C  
ATOM   1822  O   LEU A 240     -13.576   7.960 -41.467  1.00 37.94           O  
ANISOU 1822  O   LEU A 240     4447   5400   4566      8     55   -883       O  
ATOM   1823  CB  LEU A 240     -12.555   9.701 -38.852  1.00 25.72           C  
ANISOU 1823  CB  LEU A 240     2767   3941   3064     30     53   -878       C  
ATOM   1824  CG  LEU A 240     -13.821   8.980 -38.378  1.00 28.33           C  
ANISOU 1824  CG  LEU A 240     3129   4222   3415     48     18   -847       C  
ATOM   1825  CD1 LEU A 240     -13.515   7.535 -38.020  1.00 26.15           C  
ANISOU 1825  CD1 LEU A 240     2857   3937   3142    106     23   -857       C  
ATOM   1826  CD2 LEU A 240     -14.452   9.706 -37.200  1.00 23.46           C  
ANISOU 1826  CD2 LEU A 240     2488   3604   2822     44     -5   -822       C  
ATOM   1827  N   HIS A 241     -13.557  10.186 -41.819  1.00 36.11           N  
ANISOU 1827  N   HIS A 241     4203   5195   4322    -66     57   -871       N  
ATOM   1828  CA  HIS A 241     -14.583  10.111 -42.854  1.00 32.85           C  
ANISOU 1828  CA  HIS A 241     3853   4738   3891    -98     34   -854       C  
ATOM   1829  C   HIS A 241     -14.094   9.313 -44.055  1.00 36.44           C  
ANISOU 1829  C   HIS A 241     4348   5186   4311   -102     60   -880       C  
ATOM   1830  O   HIS A 241     -14.836   8.493 -44.609  1.00 36.37           O  
ANISOU 1830  O   HIS A 241     4386   5140   4292   -104     41   -875       O  
ATOM   1831  CB  HIS A 241     -14.998  11.523 -43.273  1.00 28.94           C  
ANISOU 1831  CB  HIS A 241     3374   4238   3382   -147     25   -834       C  
ATOM   1832  CG  HIS A 241     -15.992  11.562 -44.391  1.00 33.70           C  
ANISOU 1832  CG  HIS A 241     4040   4804   3962   -179     -4   -815       C  
ATOM   1833  ND1 HIS A 241     -15.636  11.387 -45.711  1.00 39.99           N  
ANISOU 1833  ND1 HIS A 241     4886   5595   4714   -205     16   -832       N  
ATOM   1834  CD2 HIS A 241     -17.330  11.771 -44.387  1.00 34.25           C  
ANISOU 1834  CD2 HIS A 241     4130   4841   4043   -188    -51   -781       C  
ATOM   1835  CE1 HIS A 241     -16.713  11.479 -46.471  1.00 38.07           C  
ANISOU 1835  CE1 HIS A 241     4693   5319   4454   -229    -23   -809       C  
ATOM   1836  NE2 HIS A 241     -17.754  11.712 -45.693  1.00 36.41           N  
ANISOU 1836  NE2 HIS A 241     4462   5093   4278   -219    -65   -778       N  
ATOM   1837  N   ALA A 242     -12.846   9.541 -44.474  1.00 41.20           N  
ANISOU 1837  N   ALA A 242     4934   5826   4894   -107    107   -912       N  
ATOM   1838  CA  ALA A 242     -12.294   8.794 -45.599  1.00 35.67           C  
ANISOU 1838  CA  ALA A 242     4272   5121   4159   -108    140   -942       C  
ATOM   1839  C   ALA A 242     -12.162   7.312 -45.271  1.00 39.05           C  
ANISOU 1839  C   ALA A 242     4700   5536   4601    -52    144   -956       C  
ATOM   1840  O   ALA A 242     -12.480   6.456 -46.105  1.00 47.95           O  
ANISOU 1840  O   ALA A 242     5884   6629   5706    -54    146   -964       O  
ATOM   1841  CB  ALA A 242     -10.941   9.376 -46.005  1.00 40.69           C  
ANISOU 1841  CB  ALA A 242     4880   5805   4776   -124    196   -976       C  
ATOM   1842  N   TYR A 243     -11.686   6.987 -44.066  1.00 40.47           N  
ANISOU 1842  N   TYR A 243     4822   5740   4813     -1    145   -959       N  
ATOM   1843  CA  TYR A 243     -11.563   5.584 -43.683  1.00 39.81           C  
ANISOU 1843  CA  TYR A 243     4744   5639   4742     59    149   -969       C  
ATOM   1844  C   TYR A 243     -12.927   4.915 -43.584  1.00 36.21           C  
ANISOU 1844  C   TYR A 243     4340   5124   4294     54    108   -941       C  
ATOM   1845  O   TYR A 243     -13.103   3.782 -44.048  1.00 43.64           O  
ANISOU 1845  O   TYR A 243     5328   6028   5223     70    115   -952       O  
ATOM   1846  CB  TYR A 243     -10.815   5.455 -42.358  1.00 38.15           C  
ANISOU 1846  CB  TYR A 243     4464   5468   4562    116    152   -973       C  
ATOM   1847  CG  TYR A 243     -10.874   4.058 -41.787  1.00 37.11           C  
ANISOU 1847  CG  TYR A 243     4347   5308   4443    181    148   -972       C  
ATOM   1848  CD1 TYR A 243     -10.178   3.015 -42.383  1.00 39.92           C  
ANISOU 1848  CD1 TYR A 243     4726   5658   4784    221    183  -1002       C  
ATOM   1849  CD2 TYR A 243     -11.640   3.776 -40.663  1.00 35.90           C  
ANISOU 1849  CD2 TYR A 243     4192   5132   4317    204    112   -942       C  
ATOM   1850  CE1 TYR A 243     -10.233   1.734 -41.872  1.00 37.91           C  
ANISOU 1850  CE1 TYR A 243     4494   5370   4540    283    181  -1000       C  
ATOM   1851  CE2 TYR A 243     -11.702   2.498 -40.144  1.00 41.23           C  
ANISOU 1851  CE2 TYR A 243     4890   5776   5000    261    111   -940       C  
ATOM   1852  CZ  TYR A 243     -10.997   1.481 -40.753  1.00 39.65           C  
ANISOU 1852  CZ  TYR A 243     4716   5566   4784    302    145   -968       C  
ATOM   1853  OH  TYR A 243     -11.054   0.206 -40.243  1.00 41.47           O  
ANISOU 1853  OH  TYR A 243     4978   5757   5021    362    146   -965       O  
ATOM   1854  N   VAL A 244     -13.902   5.596 -42.978  1.00 32.02           N  
ANISOU 1854  N   VAL A 244     3798   4583   3784     30     68   -907       N  
ATOM   1855  CA  VAL A 244     -15.250   5.042 -42.886  1.00 33.52           C  
ANISOU 1855  CA  VAL A 244     4028   4722   3984     19     30   -882       C  
ATOM   1856  C   VAL A 244     -15.841   4.862 -44.277  1.00 37.75           C  
ANISOU 1856  C   VAL A 244     4629   5228   4487    -28     22   -886       C  
ATOM   1857  O   VAL A 244     -16.465   3.836 -44.576  1.00 45.09           O  
ANISOU 1857  O   VAL A 244     5605   6117   5412    -28     11   -888       O  
ATOM   1858  CB  VAL A 244     -16.136   5.938 -42.001  1.00 33.96           C  
ANISOU 1858  CB  VAL A 244     4054   4781   4070      2     -7   -847       C  
ATOM   1859  CG1 VAL A 244     -17.608   5.616 -42.213  1.00 33.43           C  
ANISOU 1859  CG1 VAL A 244     4023   4668   4009    -27    -46   -824       C  
ATOM   1860  CG2 VAL A 244     -15.756   5.771 -40.542  1.00 33.32           C  
ANISOU 1860  CG2 VAL A 244     3923   4718   4020     51     -4   -842       C  
ATOM   1861  N   ARG A 245     -15.644   5.851 -45.151  1.00 32.44           N  
ANISOU 1861  N   ARG A 245     3965   4573   3787    -69     27   -889       N  
ATOM   1862  CA  ARG A 245     -16.142   5.745 -46.518  1.00 28.27           C  
ANISOU 1862  CA  ARG A 245     3503   4020   3220   -114     18   -893       C  
ATOM   1863  C   ARG A 245     -15.516   4.562 -47.244  1.00 35.43           C  
ANISOU 1863  C   ARG A 245     4453   4911   4099    -97     54   -928       C  
ATOM   1864  O   ARG A 245     -16.208   3.825 -47.955  1.00 44.70           O  
ANISOU 1864  O   ARG A 245     5685   6046   5252   -118     38   -931       O  
ATOM   1865  CB  ARG A 245     -15.868   7.042 -47.276  1.00 28.08           C  
ANISOU 1865  CB  ARG A 245     3485   4017   3166   -156     25   -890       C  
ATOM   1866  CG  ARG A 245     -16.305   7.020 -48.727  1.00 38.86           C  
ANISOU 1866  CG  ARG A 245     4924   5360   4483   -202     15   -893       C  
ATOM   1867  CD  ARG A 245     -16.008   8.348 -49.393  1.00 37.30           C  
ANISOU 1867  CD  ARG A 245     4738   5180   4254   -241     24   -886       C  
ATOM   1868  NE  ARG A 245     -14.618   8.742 -49.200  1.00 39.44           N  
ANISOU 1868  NE  ARG A 245     4971   5490   4524   -229     83   -912       N  
ATOM   1869  CZ  ARG A 245     -14.172   9.985 -49.304  1.00 38.36           C  
ANISOU 1869  CZ  ARG A 245     4823   5377   4376   -257    100   -907       C  
ATOM   1870  NH1 ARG A 245     -14.982  10.988 -49.601  1.00 34.26           N  
ANISOU 1870  NH1 ARG A 245     4331   4841   3844   -292     65   -874       N  
ATOM   1871  NH2 ARG A 245     -12.880  10.230 -49.103  1.00 44.15           N  
ANISOU 1871  NH2 ARG A 245     5515   6150   5110   -250    155   -936       N  
ATOM   1872  N   ALA A 246     -14.206   4.364 -47.076  1.00 31.84           N  
ANISOU 1872  N   ALA A 246     3968   4486   3644    -59    104   -957       N  
ATOM   1873  CA  ALA A 246     -13.535   3.247 -47.734  1.00 32.06           C  
ANISOU 1873  CA  ALA A 246     4034   4500   3648    -35    145   -993       C  
ATOM   1874  C   ALA A 246     -14.076   1.909 -47.244  1.00 43.08           C  
ANISOU 1874  C   ALA A 246     5457   5851   5061      0    132   -990       C  
ATOM   1875  O   ALA A 246     -14.296   0.991 -48.042  1.00 50.49           O  
ANISOU 1875  O   ALA A 246     6461   6750   5972     -9    142  -1008       O  
ATOM   1876  CB  ALA A 246     -12.026   3.334 -47.507  1.00 29.93           C  
ANISOU 1876  CB  ALA A 246     3711   4278   3382      7    199  -1023       C  
ATOM   1877  N   LYS A 247     -14.291   1.779 -45.933  1.00 40.57           N  
ANISOU 1877  N   LYS A 247     5095   5534   4784     37    112   -970       N  
ATOM   1878  CA  LYS A 247     -14.836   0.536 -45.395  1.00 46.72           C  
ANISOU 1878  CA  LYS A 247     5906   6266   5579     67    103   -965       C  
ATOM   1879  C   LYS A 247     -16.278   0.325 -45.840  1.00 43.87           C  
ANISOU 1879  C   LYS A 247     5597   5860   5211     11     61   -947       C  
ATOM   1880  O   LYS A 247     -16.674  -0.800 -46.168  1.00 49.15           O  
ANISOU 1880  O   LYS A 247     6324   6481   5868     10     64   -959       O  
ATOM   1881  CB  LYS A 247     -14.735   0.535 -43.870  1.00 44.88           C  
ANISOU 1881  CB  LYS A 247     5616   6047   5387    117     92   -945       C  
ATOM   1882  CG  LYS A 247     -13.317   0.680 -43.346  1.00 38.45           C  
ANISOU 1882  CG  LYS A 247     4745   5284   4582    175    127   -963       C  
ATOM   1883  CD  LYS A 247     -12.512  -0.590 -43.561  1.00 32.37           C  
ANISOU 1883  CD  LYS A 247     4004   4495   3800    235    167   -992       C  
ATOM   1884  CE  LYS A 247     -12.957  -1.690 -42.615  1.00 37.14           C  
ANISOU 1884  CE  LYS A 247     4634   5053   4423    281    155   -977       C  
ATOM   1885  NZ  LYS A 247     -12.110  -2.908 -42.744  1.00 51.14           N  
ANISOU 1885  NZ  LYS A 247     6438   6805   6186    350    195  -1003       N  
ATOM   1886  N   LEU A 248     -17.079   1.393 -45.851  1.00 38.01           N  
ANISOU 1886  N   LEU A 248     4833   5133   4476    -35     21   -920       N  
ATOM   1887  CA  LEU A 248     -18.458   1.277 -46.316  1.00 38.36           C  
ANISOU 1887  CA  LEU A 248     4917   5145   4515    -88    -24   -904       C  
ATOM   1888  C   LEU A 248     -18.516   1.013 -47.816  1.00 44.16           C  
ANISOU 1888  C   LEU A 248     5718   5862   5198   -130    -20   -927       C  
ATOM   1889  O   LEU A 248     -19.364   0.243 -48.283  1.00 50.53           O  
ANISOU 1889  O   LEU A 248     6576   6631   5992   -161    -41   -931       O  
ATOM   1890  CB  LEU A 248     -19.242   2.539 -45.960  1.00 34.66           C  
ANISOU 1890  CB  LEU A 248     4404   4699   4066   -117    -67   -870       C  
ATOM   1891  CG  LEU A 248     -19.509   2.806 -44.478  1.00 36.59           C  
ANISOU 1891  CG  LEU A 248     4590   4953   4359    -87    -78   -845       C  
ATOM   1892  CD1 LEU A 248     -20.429   4.005 -44.311  1.00 35.08           C  
ANISOU 1892  CD1 LEU A 248     4367   4777   4185   -120   -120   -813       C  
ATOM   1893  CD2 LEU A 248     -20.094   1.576 -43.804  1.00 34.03           C  
ANISOU 1893  CD2 LEU A 248     4285   4589   4057    -71    -81   -843       C  
ATOM   1894  N   MET A 249     -17.628   1.648 -48.586  1.00 39.62           N  
ANISOU 1894  N   MET A 249     5147   5316   4592   -136      8   -943       N  
ATOM   1895  CA  MET A 249     -17.599   1.418 -50.028  1.00 40.17           C  
ANISOU 1895  CA  MET A 249     5286   5371   4607   -176     17   -966       C  
ATOM   1896  C   MET A 249     -17.255  -0.028 -50.355  1.00 40.74           C  
ANISOU 1896  C   MET A 249     5414   5404   4662   -155     52  -1000       C  
ATOM   1897  O   MET A 249     -17.744  -0.572 -51.350  1.00 49.32           O  
ANISOU 1897  O   MET A 249     6571   6459   5710   -195     43  -1015       O  
ATOM   1898  CB  MET A 249     -16.602   2.368 -50.693  1.00 45.01           C  
ANISOU 1898  CB  MET A 249     5890   6020   5189   -184     51   -978       C  
ATOM   1899  CG  MET A 249     -16.565   2.283 -52.209  1.00 44.73           C  
ANISOU 1899  CG  MET A 249     5932   5972   5092   -230     62   -999       C  
ATOM   1900  SD  MET A 249     -15.075   3.015 -52.914  1.00 47.93           S  
ANISOU 1900  SD  MET A 249     6332   6417   5462   -229    129  -1026       S  
ATOM   1901  CE  MET A 249     -13.930   2.860 -51.544  1.00 52.50           C  
ANISOU 1901  CE  MET A 249     6821   7031   6097   -155    172  -1037       C  
ATOM   1902  N   ASN A 250     -16.415  -0.664 -49.537  1.00 45.01           N  
ANISOU 1902  N   ASN A 250     5927   5945   5229    -90     92  -1012       N  
ATOM   1903  CA  ASN A 250     -16.147  -2.086 -49.723  1.00 48.71           C  
ANISOU 1903  CA  ASN A 250     6453   6369   5686    -61    125  -1041       C  
ATOM   1904  C   ASN A 250     -17.415  -2.908 -49.526  1.00 47.48           C  
ANISOU 1904  C   ASN A 250     6341   6161   5539    -90     88  -1030       C  
ATOM   1905  O   ASN A 250     -17.670  -3.860 -50.273  1.00 57.36           O  
ANISOU 1905  O   ASN A 250     7668   7367   6759   -112     98  -1054       O  
ATOM   1906  CB  ASN A 250     -15.050  -2.544 -48.763  1.00 42.69           C  
ANISOU 1906  CB  ASN A 250     5648   5620   4954     22    168  -1051       C  
ATOM   1907  CG  ASN A 250     -13.689  -1.984 -49.126  1.00 52.06           C  
ANISOU 1907  CG  ASN A 250     6797   6857   6128     49    216  -1075       C  
ATOM   1908  OD1 ASN A 250     -13.496  -1.444 -50.215  1.00 59.39           O  
ANISOU 1908  OD1 ASN A 250     7748   7799   7017      5    228  -1090       O  
ATOM   1909  ND2 ASN A 250     -12.735  -2.108 -48.210  1.00 55.79           N  
ANISOU 1909  ND2 ASN A 250     7210   7358   6630    119    242  -1080       N  
ATOM   1910  N   ALA A 251     -18.222  -2.554 -48.524  1.00 38.84           N  
ANISOU 1910  N   ALA A 251     5200   5072   4485    -94     46   -995       N  
ATOM   1911  CA  ALA A 251     -19.481  -3.246 -48.283  1.00 48.55           C  
ANISOU 1911  CA  ALA A 251     6461   6257   5727   -129     11   -984       C  
ATOM   1912  C   ALA A 251     -20.603  -2.769 -49.197  1.00 47.86           C  
ANISOU 1912  C   ALA A 251     6397   6173   5617   -207    -40   -976       C  
ATOM   1913  O   ALA A 251     -21.578  -3.503 -49.389  1.00 50.49           O  
ANISOU 1913  O   ALA A 251     6771   6468   5945   -248    -65   -979       O  
ATOM   1914  CB  ALA A 251     -19.902  -3.078 -46.822  1.00 42.31           C  
ANISOU 1914  CB  ALA A 251     5613   5474   4990   -102     -7   -951       C  
ATOM   1915  N   TYR A 252     -20.494  -1.565 -49.755  1.00 54.25           N  
ANISOU 1915  N   TYR A 252     7180   7024   6410   -229    -58   -965       N  
ATOM   1916  CA  TYR A 252     -21.504  -1.007 -50.654  1.00 52.53           C  
ANISOU 1916  CA  TYR A 252     6982   6812   6165   -296   -112   -954       C  
ATOM   1917  C   TYR A 252     -20.817  -0.437 -51.889  1.00 53.58           C  
ANISOU 1917  C   TYR A 252     7151   6964   6244   -314    -95   -970       C  
ATOM   1918  O   TYR A 252     -20.766   0.784 -52.081  1.00 56.29           O  
ANISOU 1918  O   TYR A 252     7463   7342   6581   -324   -113   -950       O  
ATOM   1919  CB  TYR A 252     -22.334   0.065 -49.945  1.00 49.43           C  
ANISOU 1919  CB  TYR A 252     6520   6449   5812   -305   -162   -913       C  
ATOM   1920  CG  TYR A 252     -23.020  -0.418 -48.686  1.00 55.17           C  
ANISOU 1920  CG  TYR A 252     7210   7161   6593   -290   -173   -896       C  
ATOM   1921  CD1 TYR A 252     -24.239  -1.080 -48.746  1.00 55.51           C  
ANISOU 1921  CD1 TYR A 252     7273   7177   6642   -334   -210   -895       C  
ATOM   1922  CD2 TYR A 252     -22.449  -0.209 -47.437  1.00 57.30           C  
ANISOU 1922  CD2 TYR A 252     7425   7443   6903   -235   -148   -883       C  
ATOM   1923  CE1 TYR A 252     -24.870  -1.521 -47.598  1.00 59.38           C  
ANISOU 1923  CE1 TYR A 252     7732   7651   7180   -324   -214   -880       C  
ATOM   1924  CE2 TYR A 252     -23.073  -0.646 -46.283  1.00 52.04           C  
ANISOU 1924  CE2 TYR A 252     6732   6760   6280   -222   -156   -867       C  
ATOM   1925  CZ  TYR A 252     -24.283  -1.302 -46.370  1.00 57.22           C  
ANISOU 1925  CZ  TYR A 252     7411   7386   6943   -268   -186   -865       C  
ATOM   1926  OH  TYR A 252     -24.908  -1.740 -45.225  1.00 60.11           O  
ANISOU 1926  OH  TYR A 252     7752   7734   7351   -260   -188   -850       O  
ATOM   1927  N   PRO A 253     -20.263  -1.300 -52.747  1.00 55.49           N  
ANISOU 1927  N   PRO A 253     7462   7180   6442   -318    -57  -1008       N  
ATOM   1928  CA  PRO A 253     -19.543  -0.788 -53.928  1.00 52.51           C  
ANISOU 1928  CA  PRO A 253     7123   6819   6009   -336    -32  -1026       C  
ATOM   1929  C   PRO A 253     -20.422  -0.004 -54.886  1.00 55.68           C  
ANISOU 1929  C   PRO A 253     7552   7232   6370   -400    -90  -1009       C  
ATOM   1930  O   PRO A 253     -19.969   0.991 -55.465  1.00 55.84           O  
ANISOU 1930  O   PRO A 253     7574   7280   6362   -410    -83  -1003       O  
ATOM   1931  CB  PRO A 253     -18.985  -2.063 -54.583  1.00 43.99           C  
ANISOU 1931  CB  PRO A 253     6120   5700   4894   -330     18  -1072       C  
ATOM   1932  CG  PRO A 253     -19.165  -3.160 -53.570  1.00 57.64           C  
ANISOU 1932  CG  PRO A 253     7841   7394   6667   -292     29  -1075       C  
ATOM   1933  CD  PRO A 253     -20.338  -2.769 -52.739  1.00 56.18           C  
ANISOU 1933  CD  PRO A 253     7605   7215   6525   -312    -33  -1036       C  
ATOM   1934  N   SER A 254     -21.675  -0.420 -55.063  1.00 41.62           N  
ANISOU 1934  N   SER A 254     5794   5432   4588   -442   -147  -1001       N  
ATOM   1935  CA  SER A 254     -22.566   0.229 -56.014  1.00 41.46           C  
ANISOU 1935  CA  SER A 254     5802   5425   4527   -500   -210   -986       C  
ATOM   1936  C   SER A 254     -23.213   1.489 -55.461  1.00 41.18           C  
ANISOU 1936  C   SER A 254     5696   5423   4526   -497   -262   -939       C  
ATOM   1937  O   SER A 254     -23.841   2.229 -56.226  1.00 44.39           O  
ANISOU 1937  O   SER A 254     6121   5846   4900   -532   -313   -921       O  
ATOM   1938  CB  SER A 254     -23.658  -0.748 -56.457  1.00 50.61           C  
ANISOU 1938  CB  SER A 254     7008   6553   5668   -550   -254  -1000       C  
ATOM   1939  OG  SER A 254     -24.263  -1.375 -55.339  1.00 54.80           O  
ANISOU 1939  OG  SER A 254     7495   7068   6259   -537   -264   -992       O  
ATOM   1940  N   TYR A 255     -23.072   1.756 -54.162  1.00 50.86           N  
ANISOU 1940  N   TYR A 255     6848   6661   5817   -452   -249   -920       N  
ATOM   1941  CA  TYR A 255     -23.824   2.817 -53.511  1.00 46.69           C  
ANISOU 1941  CA  TYR A 255     6253   6159   5328   -448   -297   -878       C  
ATOM   1942  C   TYR A 255     -22.984   4.002 -53.056  1.00 49.47           C  
ANISOU 1942  C   TYR A 255     6562   6540   5696   -414   -268   -860       C  
ATOM   1943  O   TYR A 255     -23.555   5.059 -52.769  1.00 61.24           O  
ANISOU 1943  O   TYR A 255     8013   8050   7206   -415   -306   -825       O  
ATOM   1944  CB  TYR A 255     -24.571   2.258 -52.291  1.00 49.19           C  
ANISOU 1944  CB  TYR A 255     6516   6465   5708   -434   -313   -866       C  
ATOM   1945  CG  TYR A 255     -25.677   1.283 -52.629  1.00 46.38           C  
ANISOU 1945  CG  TYR A 255     6190   6085   5346   -479   -353   -878       C  
ATOM   1946  CD1 TYR A 255     -26.801   1.695 -53.333  1.00 35.69           C  
ANISOU 1946  CD1 TYR A 255     4842   4747   3973   -526   -424   -863       C  
ATOM   1947  CD2 TYR A 255     -25.603  -0.045 -52.231  1.00 46.35           C  
ANISOU 1947  CD2 TYR A 255     6211   6046   5356   -476   -322   -904       C  
ATOM   1948  CE1 TYR A 255     -27.817   0.809 -53.639  1.00 45.12           C  
ANISOU 1948  CE1 TYR A 255     6058   5925   5161   -573   -462   -877       C  
ATOM   1949  CE2 TYR A 255     -26.614  -0.939 -52.531  1.00 52.05           C  
ANISOU 1949  CE2 TYR A 255     6963   6744   6070   -525   -355   -918       C  
ATOM   1950  CZ  TYR A 255     -27.719  -0.507 -53.235  1.00 54.28           C  
ANISOU 1950  CZ  TYR A 255     7244   7047   6335   -577   -426   -906       C  
ATOM   1951  OH  TYR A 255     -28.729  -1.391 -53.537  1.00 54.39           O  
ANISOU 1951  OH  TYR A 255     7282   7043   6342   -633   -461   -922       O  
ATOM   1952  N   ILE A 256     -21.663   3.864 -52.978  1.00 32.23           N  
ANISOU 1952  N   ILE A 256     4381   4359   3504   -384   -201   -884       N  
ATOM   1953  CA  ILE A 256     -20.810   4.883 -52.378  1.00 29.91           C  
ANISOU 1953  CA  ILE A 256     4038   4095   3230   -354   -169   -872       C  
ATOM   1954  C   ILE A 256     -19.672   5.218 -53.332  1.00 29.66           C  
ANISOU 1954  C   ILE A 256     4047   4074   3146   -363   -119   -895       C  
ATOM   1955  O   ILE A 256     -18.958   4.321 -53.795  1.00 32.86           O  
ANISOU 1955  O   ILE A 256     4490   4467   3527   -357    -74   -932       O  
ATOM   1956  CB  ILE A 256     -20.261   4.423 -51.014  1.00 33.96           C  
ANISOU 1956  CB  ILE A 256     4491   4613   3800   -302   -134   -877       C  
ATOM   1957  CG1 ILE A 256     -21.361   4.508 -49.956  1.00 35.37           C  
ANISOU 1957  CG1 ILE A 256     4620   4787   4031   -295   -180   -846       C  
ATOM   1958  CG2 ILE A 256     -19.057   5.259 -50.607  1.00 32.49           C  
ANISOU 1958  CG2 ILE A 256     4263   4459   3621   -274    -88   -881       C  
ATOM   1959  CD1 ILE A 256     -21.130   3.620 -48.764  1.00 36.12           C  
ANISOU 1959  CD1 ILE A 256     4682   4872   4171   -252   -156   -854       C  
ATOM   1960  N   SER A 257     -19.509   6.511 -53.626  1.00 42.19           N  
ANISOU 1960  N   SER A 257     5631   5682   4717   -378   -123   -875       N  
ATOM   1961  CA  SER A 257     -18.388   6.999 -54.417  1.00 39.39           C  
ANISOU 1961  CA  SER A 257     5309   5342   4316   -391    -69   -895       C  
ATOM   1962  C   SER A 257     -17.123   7.056 -53.561  1.00 42.75           C  
ANISOU 1962  C   SER A 257     5675   5794   4776   -351     -5   -915       C  
ATOM   1963  O   SER A 257     -17.191   7.382 -52.373  1.00 45.21           O  
ANISOU 1963  O   SER A 257     5917   6118   5140   -322    -14   -898       O  
ATOM   1964  CB  SER A 257     -18.692   8.385 -54.982  1.00 41.14           C  
ANISOU 1964  CB  SER A 257     5553   5571   4507   -424    -94   -865       C  
ATOM   1965  OG  SER A 257     -17.501   9.075 -55.317  1.00 42.16           O  
ANISOU 1965  OG  SER A 257     5690   5719   4610   -431    -33   -880       O  
ATOM   1966  N   PRO A 258     -15.956   6.750 -54.138  1.00 48.69           N  
ANISOU 1966  N   PRO A 258     6447   6555   5496   -349     60   -953       N  
ATOM   1967  CA  PRO A 258     -14.705   6.861 -53.372  1.00 50.01           C  
ANISOU 1967  CA  PRO A 258     6549   6756   5695   -312    119   -974       C  
ATOM   1968  C   PRO A 258     -14.300   8.294 -53.072  1.00 44.34           C  
ANISOU 1968  C   PRO A 258     5794   6070   4984   -328    130   -957       C  
ATOM   1969  O   PRO A 258     -13.409   8.504 -52.239  1.00 45.15           O  
ANISOU 1969  O   PRO A 258     5829   6206   5120   -299    166   -970       O  
ATOM   1970  CB  PRO A 258     -13.678   6.174 -54.278  1.00 47.02           C  
ANISOU 1970  CB  PRO A 258     6210   6380   5275   -312    185  -1020       C  
ATOM   1971  CG  PRO A 258     -14.223   6.351 -55.655  1.00 48.52           C  
ANISOU 1971  CG  PRO A 258     6491   6545   5400   -366    167  -1016       C  
ATOM   1972  CD  PRO A 258     -15.723   6.305 -55.523  1.00 44.83           C  
ANISOU 1972  CD  PRO A 258     6041   6050   4941   -382     84   -979       C  
ATOM   1973  N   ILE A 259     -14.916   9.278 -53.723  1.00 37.63           N  
ANISOU 1973  N   ILE A 259     4986   5209   4101   -371     99   -929       N  
ATOM   1974  CA  ILE A 259     -14.582  10.682 -53.515  1.00 40.82           C  
ANISOU 1974  CA  ILE A 259     5370   5634   4507   -391    112   -912       C  
ATOM   1975  C   ILE A 259     -15.754  11.500 -52.999  1.00 40.18           C  
ANISOU 1975  C   ILE A 259     5279   5538   4450   -395     46   -864       C  
ATOM   1976  O   ILE A 259     -15.565  12.683 -52.677  1.00 44.62           O  
ANISOU 1976  O   ILE A 259     5824   6111   5018   -407     54   -847       O  
ATOM   1977  CB  ILE A 259     -14.029  11.325 -54.805  1.00 42.74           C  
ANISOU 1977  CB  ILE A 259     5681   5876   4682   -440    150   -923       C  
ATOM   1978  CG1 ILE A 259     -15.126  11.386 -55.870  1.00 36.41           C  
ANISOU 1978  CG1 ILE A 259     4965   5038   3829   -473     96   -897       C  
ATOM   1979  CG2 ILE A 259     -12.825  10.549 -55.314  1.00 46.30           C  
ANISOU 1979  CG2 ILE A 259     6137   6344   5110   -436    224   -974       C  
ATOM   1980  CD1 ILE A 259     -15.099  12.640 -56.711  1.00 37.10           C  
ANISOU 1980  CD1 ILE A 259     5114   5118   3864   -518    101   -877       C  
ATOM   1981  N   GLY A 260     -16.955  10.927 -52.913  1.00 41.76           N  
ANISOU 1981  N   GLY A 260     5489   5714   4664   -386    -16   -843       N  
ATOM   1982  CA  GLY A 260     -18.140  11.671 -52.554  1.00 43.42           C  
ANISOU 1982  CA  GLY A 260     5691   5912   4895   -388    -79   -799       C  
ATOM   1983  C   GLY A 260     -18.488  11.571 -51.075  1.00 37.60           C  
ANISOU 1983  C   GLY A 260     4876   5182   4228   -349    -96   -786       C  
ATOM   1984  O   GLY A 260     -17.841  10.886 -50.286  1.00 39.78           O  
ANISOU 1984  O   GLY A 260     5106   5473   4536   -319    -64   -809       O  
ATOM   1985  N   CYS A 261     -19.549  12.287 -50.712  1.00 42.31           N  
ANISOU 1985  N   CYS A 261     5460   5769   4846   -348   -147   -748       N  
ATOM   1986  CA  CYS A 261     -20.020  12.304 -49.337  1.00 35.63           C  
ANISOU 1986  CA  CYS A 261     4547   4928   4064   -316   -165   -732       C  
ATOM   1987  C   CYS A 261     -20.675  10.974 -48.973  1.00 38.86           C  
ANISOU 1987  C   CYS A 261     4940   5325   4499   -298   -190   -739       C  
ATOM   1988  O   CYS A 261     -21.079  10.188 -49.834  1.00 41.28           O  
ANISOU 1988  O   CYS A 261     5292   5617   4777   -316   -209   -748       O  
ATOM   1989  CB  CYS A 261     -21.011  13.448 -49.125  1.00 43.02           C  
ANISOU 1989  CB  CYS A 261     5477   5854   5014   -318   -210   -690       C  
ATOM   1990  SG  CYS A 261     -20.306  15.099 -49.317  1.00 49.78           S  
ANISOU 1990  SG  CYS A 261     6354   6715   5846   -337   -177   -678       S  
ATOM   1991  N   LEU A 262     -20.772  10.731 -47.674  1.00 36.71           N  
ANISOU 1991  N   LEU A 262     4608   5058   4279   -267   -187   -735       N  
ATOM   1992  CA  LEU A 262     -21.425   9.528 -47.174  1.00 33.95           C  
ANISOU 1992  CA  LEU A 262     4245   4694   3959   -251   -207   -739       C  
ATOM   1993  C   LEU A 262     -22.939   9.675 -47.273  1.00 39.79           C  
ANISOU 1993  C   LEU A 262     4985   5420   4714   -267   -269   -709       C  
ATOM   1994  O   LEU A 262     -23.480  10.711 -46.873  1.00 33.61           O  
ANISOU 1994  O   LEU A 262     4176   4642   3952   -263   -291   -680       O  
ATOM   1995  CB  LEU A 262     -21.020   9.262 -45.729  1.00 32.36           C  
ANISOU 1995  CB  LEU A 262     3987   4504   3806   -212   -182   -742       C  
ATOM   1996  CG  LEU A 262     -19.564   8.839 -45.539  1.00 33.35           C  
ANISOU 1996  CG  LEU A 262     4102   4648   3921   -188   -126   -775       C  
ATOM   1997  CD1 LEU A 262     -19.271   8.521 -44.082  1.00 32.28           C  
ANISOU 1997  CD1 LEU A 262     3912   4524   3829   -146   -112   -776       C  
ATOM   1998  CD2 LEU A 262     -19.268   7.644 -46.423  1.00 34.34           C  
ANISOU 1998  CD2 LEU A 262     4276   4758   4015   -192   -111   -804       C  
ATOM   1999  N   PRO A 263     -23.648   8.682 -47.810  1.00 34.73           N  
ANISOU 1999  N   PRO A 263     4371   4761   4062   -285   -297   -717       N  
ATOM   2000  CA  PRO A 263     -25.114   8.736 -47.788  1.00 27.00           C  
ANISOU 2000  CA  PRO A 263     3378   3776   3104   -300   -357   -692       C  
ATOM   2001  C   PRO A 263     -25.628   8.848 -46.360  1.00 30.14           C  
ANISOU 2001  C   PRO A 263     3711   4177   3565   -273   -359   -674       C  
ATOM   2002  O   PRO A 263     -25.118   8.201 -45.443  1.00 30.51           O  
ANISOU 2002  O   PRO A 263     3737   4221   3637   -249   -323   -688       O  
ATOM   2003  CB  PRO A 263     -25.528   7.413 -48.440  1.00 34.39           C  
ANISOU 2003  CB  PRO A 263     4354   4694   4020   -326   -372   -714       C  
ATOM   2004  CG  PRO A 263     -24.360   7.038 -49.296  1.00 34.65           C  
ANISOU 2004  CG  PRO A 263     4442   4723   4002   -332   -329   -745       C  
ATOM   2005  CD  PRO A 263     -23.146   7.511 -48.548  1.00 29.69           C  
ANISOU 2005  CD  PRO A 263     3782   4110   3389   -296   -274   -750       C  
ATOM   2006  N   ALA A 264     -26.655   9.683 -46.180  1.00 35.16           N  
ANISOU 2006  N   ALA A 264     4318   4818   4224   -274   -401   -644       N  
ATOM   2007  CA  ALA A 264     -27.097  10.036 -44.835  1.00 27.59           C  
ANISOU 2007  CA  ALA A 264     3298   3863   3321   -248   -397   -626       C  
ATOM   2008  C   ALA A 264     -27.728   8.857 -44.106  1.00 32.61           C  
ANISOU 2008  C   ALA A 264     3910   4488   3992   -249   -399   -634       C  
ATOM   2009  O   ALA A 264     -27.731   8.826 -42.871  1.00 38.81           O  
ANISOU 2009  O   ALA A 264     4655   5272   4817   -225   -377   -629       O  
ATOM   2010  CB  ALA A 264     -28.079  11.205 -44.897  1.00 29.90           C  
ANISOU 2010  CB  ALA A 264     3568   4163   3630   -246   -440   -592       C  
ATOM   2011  N   HIS A 265     -28.260   7.885 -44.840  1.00 35.75           N  
ANISOU 2011  N   HIS A 265     4337   4875   4373   -280   -423   -648       N  
ATOM   2012  CA  HIS A 265     -28.950   6.754 -44.234  1.00 36.37           C  
ANISOU 2012  CA  HIS A 265     4399   4937   4481   -290   -424   -657       C  
ATOM   2013  C   HIS A 265     -28.027   5.585 -43.917  1.00 34.12           C  
ANISOU 2013  C   HIS A 265     4146   4631   4186   -279   -376   -684       C  
ATOM   2014  O   HIS A 265     -28.503   4.560 -43.418  1.00 34.92           O  
ANISOU 2014  O   HIS A 265     4247   4712   4307   -288   -370   -693       O  
ATOM   2015  CB  HIS A 265     -30.079   6.278 -45.149  1.00 36.02           C  
ANISOU 2015  CB  HIS A 265     4369   4892   4425   -335   -476   -660       C  
ATOM   2016  CG  HIS A 265     -29.603   5.709 -46.447  1.00 37.63           C  
ANISOU 2016  CG  HIS A 265     4641   5087   4570   -363   -480   -684       C  
ATOM   2017  ND1 HIS A 265     -28.975   6.471 -47.408  1.00 37.44           N  
ANISOU 2017  ND1 HIS A 265     4653   5073   4500   -362   -484   -682       N  
ATOM   2018  CD2 HIS A 265     -29.661   4.450 -46.942  1.00 37.46           C  
ANISOU 2018  CD2 HIS A 265     4664   5044   4526   -394   -476   -712       C  
ATOM   2019  CE1 HIS A 265     -28.668   5.707 -48.440  1.00 35.21           C  
ANISOU 2019  CE1 HIS A 265     4432   4777   4168   -391   -483   -708       C  
ATOM   2020  NE2 HIS A 265     -29.074   4.477 -48.183  1.00 39.45           N  
ANISOU 2020  NE2 HIS A 265     4976   5294   4719   -410   -479   -727       N  
ATOM   2021  N   LEU A 266     -26.729   5.707 -44.191  1.00 38.32           N  
ANISOU 2021  N   LEU A 266     4705   5167   4688   -258   -340   -699       N  
ATOM   2022  CA  LEU A 266     -25.773   4.628 -43.978  1.00 43.14           C  
ANISOU 2022  CA  LEU A 266     5346   5760   5287   -238   -294   -726       C  
ATOM   2023  C   LEU A 266     -24.807   4.936 -42.837  1.00 43.12           C  
ANISOU 2023  C   LEU A 266     5309   5770   5305   -190   -254   -724       C  
ATOM   2024  O   LEU A 266     -23.675   4.449 -42.829  1.00 45.13           O  
ANISOU 2024  O   LEU A 266     5582   6024   5543   -163   -215   -745       O  
ATOM   2025  CB  LEU A 266     -24.992   4.350 -45.262  1.00 37.79           C  
ANISOU 2025  CB  LEU A 266     4725   5078   4554   -252   -281   -751       C  
ATOM   2026  CG  LEU A 266     -25.764   3.855 -46.486  1.00 39.37           C  
ANISOU 2026  CG  LEU A 266     4973   5264   4722   -301   -317   -761       C  
ATOM   2027  CD1 LEU A 266     -24.825   3.695 -47.672  1.00 46.40           C  
ANISOU 2027  CD1 LEU A 266     5922   6152   5554   -309   -294   -787       C  
ATOM   2028  CD2 LEU A 266     -26.475   2.546 -46.184  1.00 40.05           C  
ANISOU 2028  CD2 LEU A 266     5075   5319   4823   -319   -321   -774       C  
ATOM   2029  N   LEU A 267     -25.237   5.742 -41.866  1.00 38.03           N  
ANISOU 2029  N   LEU A 267     4614   5139   4698   -177   -262   -699       N  
ATOM   2030  CA  LEU A 267     -24.335   6.285 -40.858  1.00 33.65           C  
ANISOU 2030  CA  LEU A 267     4025   4603   4157   -137   -231   -696       C  
ATOM   2031  C   LEU A 267     -24.577   5.736 -39.456  1.00 37.02           C  
ANISOU 2031  C   LEU A 267     4428   5019   4620   -112   -217   -689       C  
ATOM   2032  O   LEU A 267     -23.984   6.243 -38.498  1.00 45.40           O  
ANISOU 2032  O   LEU A 267     5457   6097   5694    -81   -198   -683       O  
ATOM   2033  CB  LEU A 267     -24.430   7.810 -40.844  1.00 29.20           C  
ANISOU 2033  CB  LEU A 267     3432   4062   3599   -142   -244   -676       C  
ATOM   2034  CG  LEU A 267     -24.006   8.490 -42.143  1.00 28.79           C  
ANISOU 2034  CG  LEU A 267     3411   4022   3507   -164   -250   -682       C  
ATOM   2035  CD1 LEU A 267     -24.360   9.962 -42.101  1.00 31.78           C  
ANISOU 2035  CD1 LEU A 267     3769   4414   3893   -170   -268   -657       C  
ATOM   2036  CD2 LEU A 267     -22.518   8.294 -42.383  1.00 32.40           C  
ANISOU 2036  CD2 LEU A 267     3883   4493   3934   -148   -207   -709       C  
ATOM   2037  N   GLY A 268     -25.423   4.722 -39.305  1.00 33.69           N  
ANISOU 2037  N   GLY A 268     4022   4568   4212   -126   -226   -689       N  
ATOM   2038  CA  GLY A 268     -25.585   4.049 -38.033  1.00 39.62           C  
ANISOU 2038  CA  GLY A 268     4762   5301   4989   -104   -207   -683       C  
ATOM   2039  C   GLY A 268     -26.739   4.527 -37.175  1.00 37.75           C  
ANISOU 2039  C   GLY A 268     4485   5066   4793   -116   -222   -659       C  
ATOM   2040  O   GLY A 268     -27.082   3.844 -36.203  1.00 37.28           O  
ANISOU 2040  O   GLY A 268     4426   4986   4753   -107   -206   -654       O  
ATOM   2041  N   ASP A 269     -27.338   5.674 -37.487  1.00 33.37           N  
ANISOU 2041  N   ASP A 269     3898   4532   4249   -133   -249   -643       N  
ATOM   2042  CA  ASP A 269     -28.575   6.082 -36.835  1.00 37.99           C  
ANISOU 2042  CA  ASP A 269     4442   5118   4875   -146   -265   -622       C  
ATOM   2043  C   ASP A 269     -29.376   6.942 -37.805  1.00 39.15           C  
ANISOU 2043  C   ASP A 269     4572   5280   5022   -173   -308   -611       C  
ATOM   2044  O   ASP A 269     -28.999   7.121 -38.966  1.00 43.97           O  
ANISOU 2044  O   ASP A 269     5210   5897   5599   -185   -324   -619       O  
ATOM   2045  CB  ASP A 269     -28.309   6.787 -35.493  1.00 41.30           C  
ANISOU 2045  CB  ASP A 269     4827   5548   5317   -113   -241   -609       C  
ATOM   2046  CG  ASP A 269     -27.440   8.028 -35.621  1.00 43.04           C  
ANISOU 2046  CG  ASP A 269     5035   5794   5522    -94   -238   -606       C  
ATOM   2047  OD1 ASP A 269     -27.442   8.679 -36.685  1.00 48.64           O  
ANISOU 2047  OD1 ASP A 269     5752   6514   6215   -109   -260   -605       O  
ATOM   2048  OD2 ASP A 269     -26.751   8.362 -34.634  1.00 40.97           O1-
ANISOU 2048  OD2 ASP A 269     4761   5542   5264    -65   -213   -606       O1-
ATOM   2049  N   MET A 270     -30.494   7.478 -37.309  1.00 31.78           N  
ANISOU 2049  N   MET A 270     3594   4353   4127   -179   -324   -592       N  
ATOM   2050  CA  MET A 270     -31.468   8.130 -38.181  1.00 36.14           C  
ANISOU 2050  CA  MET A 270     4127   4920   4685   -202   -371   -580       C  
ATOM   2051  C   MET A 270     -30.885   9.345 -38.893  1.00 42.92           C  
ANISOU 2051  C   MET A 270     4995   5794   5517   -188   -384   -570       C  
ATOM   2052  O   MET A 270     -31.328   9.688 -39.995  1.00 46.56           O  
ANISOU 2052  O   MET A 270     5467   6263   5961   -206   -424   -565       O  
ATOM   2053  CB  MET A 270     -32.703   8.523 -37.367  1.00 31.50           C  
ANISOU 2053  CB  MET A 270     3481   4338   4148   -202   -379   -562       C  
ATOM   2054  CG  MET A 270     -33.774   9.258 -38.154  1.00 31.89           C  
ANISOU 2054  CG  MET A 270     3499   4407   4209   -214   -430   -546       C  
ATOM   2055  SD  MET A 270     -34.280   8.365 -39.633  1.00 44.48           S  
ANISOU 2055  SD  MET A 270     5122   6005   5774   -263   -479   -562       S  
ATOM   2056  CE  MET A 270     -35.261   7.054 -38.912  1.00 33.22           C  
ANISOU 2056  CE  MET A 270     3671   4568   4385   -300   -466   -576       C  
ATOM   2057  N   TRP A 271     -29.888   9.999 -38.298  1.00 35.16           N  
ANISOU 2057  N   TRP A 271     4015   4816   4529   -158   -351   -570       N  
ATOM   2058  CA  TRP A 271     -29.379  11.252 -38.835  1.00 39.96           C  
ANISOU 2058  CA  TRP A 271     4632   5435   5116   -149   -356   -560       C  
ATOM   2059  C   TRP A 271     -27.882  11.269 -39.094  1.00 40.28           C  
ANISOU 2059  C   TRP A 271     4707   5480   5118   -142   -325   -579       C  
ATOM   2060  O   TRP A 271     -27.391  12.245 -39.672  1.00 44.07           O  
ANISOU 2060  O   TRP A 271     5204   5968   5574   -143   -325   -574       O  
ATOM   2061  CB  TRP A 271     -29.717  12.413 -37.888  1.00 36.63           C  
ANISOU 2061  CB  TRP A 271     4174   5018   4728   -126   -348   -539       C  
ATOM   2062  CG  TRP A 271     -31.067  12.292 -37.262  1.00 33.30           C  
ANISOU 2062  CG  TRP A 271     3707   4594   4353   -125   -363   -525       C  
ATOM   2063  CD1 TRP A 271     -32.217  12.896 -37.675  1.00 37.07           C  
ANISOU 2063  CD1 TRP A 271     4158   5077   4851   -127   -401   -506       C  
ATOM   2064  CD2 TRP A 271     -31.413  11.513 -36.111  1.00 33.72           C  
ANISOU 2064  CD2 TRP A 271     3735   4639   4437   -122   -338   -530       C  
ATOM   2065  NE1 TRP A 271     -33.258  12.544 -36.852  1.00 38.31           N  
ANISOU 2065  NE1 TRP A 271     4268   5234   5053   -127   -400   -500       N  
ATOM   2066  CE2 TRP A 271     -32.791  11.695 -35.884  1.00 38.31           C  
ANISOU 2066  CE2 TRP A 271     4272   5224   5059   -127   -359   -515       C  
ATOM   2067  CE3 TRP A 271     -30.692  10.679 -35.250  1.00 33.20           C  
ANISOU 2067  CE3 TRP A 271     3682   4565   4368   -114   -300   -545       C  
ATOM   2068  CZ2 TRP A 271     -33.463  11.075 -34.832  1.00 35.68           C  
ANISOU 2068  CZ2 TRP A 271     3909   4885   4764   -131   -338   -516       C  
ATOM   2069  CZ3 TRP A 271     -31.360  10.064 -34.208  1.00 33.83           C  
ANISOU 2069  CZ3 TRP A 271     3738   4634   4480   -115   -282   -543       C  
ATOM   2070  CH2 TRP A 271     -32.731  10.265 -34.007  1.00 32.52           C  
ANISOU 2070  CH2 TRP A 271     3531   4472   4355   -126   -299   -529       C  
ATOM   2071  N   GLY A 272     -27.144  10.236 -38.701  1.00 30.54           N  
ANISOU 2071  N   GLY A 272     3486   4242   3877   -134   -296   -600       N  
ATOM   2072  CA  GLY A 272     -25.702  10.342 -38.706  1.00 29.62           C  
ANISOU 2072  CA  GLY A 272     3385   4138   3733   -119   -262   -618       C  
ATOM   2073  C   GLY A 272     -25.155  11.146 -37.554  1.00 37.21           C  
ANISOU 2073  C   GLY A 272     4315   5113   4710    -95   -236   -614       C  
ATOM   2074  O   GLY A 272     -24.012  11.610 -37.622  1.00 35.09           O  
ANISOU 2074  O   GLY A 272     4052   4862   4420    -89   -212   -627       O  
ATOM   2075  N   ARG A 273     -25.949  11.337 -36.496  1.00 35.50           N  
ANISOU 2075  N   ARG A 273     4067   4890   4531    -85   -238   -597       N  
ATOM   2076  CA  ARG A 273     -25.462  12.052 -35.322  1.00 36.80           C  
ANISOU 2076  CA  ARG A 273     4207   5066   4708    -64   -212   -595       C  
ATOM   2077  C   ARG A 273     -24.275  11.330 -34.703  1.00 37.66           C  
ANISOU 2077  C   ARG A 273     4318   5188   4803    -42   -183   -616       C  
ATOM   2078  O   ARG A 273     -23.299  11.965 -34.291  1.00 30.47           O  
ANISOU 2078  O   ARG A 273     3398   4300   3881    -32   -163   -626       O  
ATOM   2079  CB  ARG A 273     -26.584  12.215 -34.297  1.00 28.18           C  
ANISOU 2079  CB  ARG A 273     3085   3963   3657    -56   -216   -576       C  
ATOM   2080  CG  ARG A 273     -26.151  12.940 -33.033  1.00 29.44           C  
ANISOU 2080  CG  ARG A 273     3225   4133   3828    -37   -189   -574       C  
ATOM   2081  CD  ARG A 273     -27.272  13.030 -32.013  1.00 31.07           C  
ANISOU 2081  CD  ARG A 273     3406   4326   4073    -30   -187   -557       C  
ATOM   2082  NE  ARG A 273     -26.835  13.725 -30.808  1.00 39.95           N  
ANISOU 2082  NE  ARG A 273     4518   5459   5203    -14   -160   -558       N  
ATOM   2083  CZ  ARG A 273     -27.388  13.576 -29.612  1.00 37.30           C  
ANISOU 2083  CZ  ARG A 273     4167   5115   4891     -2   -144   -550       C  
ATOM   2084  NH1 ARG A 273     -28.411  12.760 -29.420  1.00 37.39           N  
ANISOU 2084  NH1 ARG A 273     4169   5110   4926     -7   -149   -542       N  
ATOM   2085  NH2 ARG A 273     -26.900  14.262 -28.582  1.00 39.10           N  
ANISOU 2085  NH2 ARG A 273     4390   5352   5116     10   -121   -554       N  
ATOM   2086  N   PHE A 274     -24.339  10.006 -34.631  1.00 33.07           N  
ANISOU 2086  N   PHE A 274     3751   4593   4221    -34   -181   -624       N  
ATOM   2087  CA  PHE A 274     -23.223   9.193 -34.175  1.00 26.64           C  
ANISOU 2087  CA  PHE A 274     2944   3787   3390     -5   -157   -643       C  
ATOM   2088  C   PHE A 274     -22.959   8.096 -35.192  1.00 31.44           C  
ANISOU 2088  C   PHE A 274     3587   4382   3976     -9   -158   -659       C  
ATOM   2089  O   PHE A 274     -23.894   7.486 -35.719  1.00 38.88           O  
ANISOU 2089  O   PHE A 274     4550   5299   4924    -31   -176   -654       O  
ATOM   2090  CB  PHE A 274     -23.499   8.577 -32.800  1.00 31.23           C  
ANISOU 2090  CB  PHE A 274     3517   4358   3992     20   -146   -635       C  
ATOM   2091  CG  PHE A 274     -23.802   9.587 -31.732  1.00 32.09           C  
ANISOU 2091  CG  PHE A 274     3594   4476   4121     24   -142   -620       C  
ATOM   2092  CD1 PHE A 274     -22.796  10.375 -31.200  1.00 33.46           C  
ANISOU 2092  CD1 PHE A 274     3750   4680   4282     38   -128   -630       C  
ATOM   2093  CD2 PHE A 274     -25.092   9.744 -31.256  1.00 28.05           C  
ANISOU 2093  CD2 PHE A 274     3072   3945   3640     11   -149   -600       C  
ATOM   2094  CE1 PHE A 274     -23.071  11.304 -30.215  1.00 29.82           C  
ANISOU 2094  CE1 PHE A 274     3269   4226   3837     39   -121   -619       C  
ATOM   2095  CE2 PHE A 274     -25.374  10.671 -30.270  1.00 27.27           C  
ANISOU 2095  CE2 PHE A 274     2949   3852   3559     16   -140   -589       C  
ATOM   2096  CZ  PHE A 274     -24.362  11.452 -29.750  1.00 30.39           C  
ANISOU 2096  CZ  PHE A 274     3334   4274   3940     30   -126   -598       C  
ATOM   2097  N   TRP A 275     -21.680   7.855 -35.470  1.00 34.33           N  
ANISOU 2097  N   TRP A 275     3960   4767   4316     10   -138   -682       N  
ATOM   2098  CA  TRP A 275     -21.265   6.765 -36.338  1.00 33.05           C  
ANISOU 2098  CA  TRP A 275     3835   4592   4131     14   -131   -701       C  
ATOM   2099  C   TRP A 275     -20.961   5.494 -35.555  1.00 31.44           C  
ANISOU 2099  C   TRP A 275     3645   4371   3930     54   -115   -707       C  
ATOM   2100  O   TRP A 275     -20.229   4.629 -36.049  1.00 40.08           O  
ANISOU 2100  O   TRP A 275     4765   5460   5003     74    -99   -727       O  
ATOM   2101  CB  TRP A 275     -20.048   7.183 -37.169  1.00 31.79           C  
ANISOU 2101  CB  TRP A 275     3675   4462   3940     15   -113   -724       C  
ATOM   2102  CG  TRP A 275     -20.308   8.335 -38.103  1.00 28.87           C  
ANISOU 2102  CG  TRP A 275     3309   4102   3559    -26   -126   -718       C  
ATOM   2103  CD1 TRP A 275     -21.457   9.065 -38.211  1.00 27.34           C  
ANISOU 2103  CD1 TRP A 275     3113   3895   3381    -54   -154   -694       C  
ATOM   2104  CD2 TRP A 275     -19.394   8.886 -39.060  1.00 25.94           C  
ANISOU 2104  CD2 TRP A 275     2947   3754   3157    -41   -109   -737       C  
ATOM   2105  NE1 TRP A 275     -21.315  10.034 -39.174  1.00 29.81           N  
ANISOU 2105  NE1 TRP A 275     3437   4217   3671    -82   -159   -693       N  
ATOM   2106  CE2 TRP A 275     -20.058   9.946 -39.710  1.00 28.71           C  
ANISOU 2106  CE2 TRP A 275     3308   4099   3503    -78   -130   -720       C  
ATOM   2107  CE3 TRP A 275     -18.079   8.587 -39.430  1.00 24.71           C  
ANISOU 2107  CE3 TRP A 275     2789   3621   2977    -25    -76   -767       C  
ATOM   2108  CZ2 TRP A 275     -19.453  10.705 -40.709  1.00 32.26           C  
ANISOU 2108  CZ2 TRP A 275     3775   4562   3920   -104   -117   -729       C  
ATOM   2109  CZ3 TRP A 275     -17.480   9.342 -40.422  1.00 29.15           C  
ANISOU 2109  CZ3 TRP A 275     3363   4202   3510    -54    -61   -780       C  
ATOM   2110  CH2 TRP A 275     -18.166  10.389 -41.049  1.00 29.85           C  
ANISOU 2110  CH2 TRP A 275     3471   4281   3592    -95    -81   -760       C  
ATOM   2111  N   THR A 276     -21.526   5.364 -34.349  1.00 28.56           N  
ANISOU 2111  N   THR A 276     3268   3995   3589     67   -117   -689       N  
ATOM   2112  CA  THR A 276     -21.194   4.251 -33.464  1.00 32.82           C  
ANISOU 2112  CA  THR A 276     3825   4516   4127    109   -101   -690       C  
ATOM   2113  C   THR A 276     -21.472   2.904 -34.118  1.00 30.68           C  
ANISOU 2113  C   THR A 276     3608   4203   3846    106    -96   -699       C  
ATOM   2114  O   THR A 276     -20.646   1.986 -34.042  1.00 26.59           O  
ANISOU 2114  O   THR A 276     3115   3676   3312    147    -78   -713       O  
ATOM   2115  CB  THR A 276     -21.990   4.366 -32.163  1.00 23.67           C  
ANISOU 2115  CB  THR A 276     2653   3346   2994    111   -104   -667       C  
ATOM   2116  OG1 THR A 276     -22.128   5.745 -31.796  1.00 29.00           O  
ANISOU 2116  OG1 THR A 276     3285   4051   3682     97   -112   -657       O  
ATOM   2117  CG2 THR A 276     -21.310   3.590 -31.044  1.00 25.26           C  
ANISOU 2117  CG2 THR A 276     2867   3544   3188    164    -87   -666       C  
ATOM   2118  N   ASN A 277     -22.622   2.770 -34.768  1.00 35.44           N  
ANISOU 2118  N   ASN A 277     4228   4779   4458     58   -113   -694       N  
ATOM   2119  CA  ASN A 277     -23.068   1.491 -35.299  1.00 34.84           C  
ANISOU 2119  CA  ASN A 277     4206   4657   4373     43   -109   -703       C  
ATOM   2120  C   ASN A 277     -22.444   1.160 -36.646  1.00 33.49           C  
ANISOU 2120  C   ASN A 277     4067   4486   4171     37   -104   -728       C  
ATOM   2121  O   ASN A 277     -22.821   0.156 -37.260  1.00 40.41           O  
ANISOU 2121  O   ASN A 277     4994   5324   5036     18   -102   -740       O  
ATOM   2122  CB  ASN A 277     -24.592   1.486 -35.387  1.00 32.35           C  
ANISOU 2122  CB  ASN A 277     3890   4321   4082    -11   -131   -689       C  
ATOM   2123  CG  ASN A 277     -25.239   1.729 -34.040  1.00 31.26           C  
ANISOU 2123  CG  ASN A 277     3724   4180   3973     -5   -127   -666       C  
ATOM   2124  OD1 ASN A 277     -24.681   1.375 -33.000  1.00 31.19           O  
ANISOU 2124  OD1 ASN A 277     3722   4167   3964     37   -106   -661       O  
ATOM   2125  ND2 ASN A 277     -26.402   2.363 -34.046  1.00 39.39           N  
ANISOU 2125  ND2 ASN A 277     4721   5214   5029    -46   -148   -652       N  
ATOM   2126  N   LEU A 278     -21.508   1.980 -37.116  1.00 37.49           N  
ANISOU 2126  N   LEU A 278     4548   5033   4662     49   -100   -739       N  
ATOM   2127  CA  LEU A 278     -20.658   1.630 -38.243  1.00 32.55           C  
ANISOU 2127  CA  LEU A 278     3953   4411   4005     54    -85   -766       C  
ATOM   2128  C   LEU A 278     -19.427   0.848 -37.812  1.00 39.39           C  
ANISOU 2128  C   LEU A 278     4828   5279   4860    117    -52   -783       C  
ATOM   2129  O   LEU A 278     -18.607   0.496 -38.665  1.00 49.67           O  
ANISOU 2129  O   LEU A 278     6150   6585   6136    130    -32   -808       O  
ATOM   2130  CB  LEU A 278     -20.225   2.891 -38.997  1.00 30.54           C  
ANISOU 2130  CB  LEU A 278     3669   4198   3736     32    -91   -770       C  
ATOM   2131  CG  LEU A 278     -21.339   3.848 -39.416  1.00 31.53           C  
ANISOU 2131  CG  LEU A 278     3782   4326   3871    -21   -126   -751       C  
ATOM   2132  CD1 LEU A 278     -20.779   4.996 -40.242  1.00 32.96           C  
ANISOU 2132  CD1 LEU A 278     3952   4541   4031    -39   -126   -756       C  
ATOM   2133  CD2 LEU A 278     -22.411   3.097 -40.187  1.00 34.96           C  
ANISOU 2133  CD2 LEU A 278     4261   4723   4299    -61   -147   -752       C  
ATOM   2134  N   TYR A 279     -19.287   0.566 -36.514  1.00 31.64           N  
ANISOU 2134  N   TYR A 279     3831   4295   3895    160    -47   -769       N  
ATOM   2135  CA  TYR A 279     -18.091  -0.108 -36.019  1.00 36.32           C  
ANISOU 2135  CA  TYR A 279     4426   4896   4477    229    -22   -782       C  
ATOM   2136  C   TYR A 279     -17.927  -1.483 -36.652  1.00 39.71           C  
ANISOU 2136  C   TYR A 279     4922   5278   4887    248      0   -800       C  
ATOM   2137  O   TYR A 279     -16.812  -1.878 -37.007  1.00 44.85           O  
ANISOU 2137  O   TYR A 279     5577   5943   5522    294     24   -823       O  
ATOM   2138  CB  TYR A 279     -18.145  -0.223 -34.495  1.00 31.36           C  
ANISOU 2138  CB  TYR A 279     3781   4268   3866    268    -25   -760       C  
ATOM   2139  CG  TYR A 279     -16.936  -0.898 -33.887  1.00 30.68           C  
ANISOU 2139  CG  TYR A 279     3695   4195   3768    347     -7   -769       C  
ATOM   2140  CD1 TYR A 279     -15.692  -0.281 -33.898  1.00 31.60           C  
ANISOU 2140  CD1 TYR A 279     3757   4373   3877    380     -1   -786       C  
ATOM   2141  CD2 TYR A 279     -17.040  -2.153 -33.300  1.00 35.13           C  
ANISOU 2141  CD2 TYR A 279     4312   4708   4327    389      4   -761       C  
ATOM   2142  CE1 TYR A 279     -14.584  -0.895 -33.343  1.00 33.16           C  
ANISOU 2142  CE1 TYR A 279     3947   4589   4066    458     11   -795       C  
ATOM   2143  CE2 TYR A 279     -15.938  -2.775 -32.742  1.00 35.88           C  
ANISOU 2143  CE2 TYR A 279     4408   4814   4410    471     17   -767       C  
ATOM   2144  CZ  TYR A 279     -14.713  -2.142 -32.767  1.00 36.64           C  
ANISOU 2144  CZ  TYR A 279     4442   4978   4501    507     18   -784       C  
ATOM   2145  OH  TYR A 279     -13.615  -2.758 -32.212  1.00 43.31           O  
ANISOU 2145  OH  TYR A 279     5280   5841   5335    592     27   -791       O  
ATOM   2146  N   SER A 280     -19.027  -2.224 -36.808  1.00 45.31           N  
ANISOU 2146  N   SER A 280     5684   5931   5600    212     -6   -792       N  
ATOM   2147  CA  SER A 280     -18.941  -3.560 -37.391  1.00 44.55           C  
ANISOU 2147  CA  SER A 280     5662   5782   5485    224     16   -811       C  
ATOM   2148  C   SER A 280     -18.371  -3.512 -38.803  1.00 51.13           C  
ANISOU 2148  C   SER A 280     6511   6626   6291    210     29   -841       C  
ATOM   2149  O   SER A 280     -17.515  -4.328 -39.164  1.00 57.50           O  
ANISOU 2149  O   SER A 280     7353   7417   7079    255     60   -864       O  
ATOM   2150  CB  SER A 280     -20.318  -4.222 -37.390  1.00 44.24           C  
ANISOU 2150  CB  SER A 280     5672   5685   5454    170      6   -800       C  
ATOM   2151  OG  SER A 280     -21.260  -3.438 -38.102  1.00 52.81           O  
ANISOU 2151  OG  SER A 280     6736   6786   6545     96    -24   -797       O  
ATOM   2152  N   LEU A 281     -18.829  -2.560 -39.616  1.00 42.02           N  
ANISOU 2152  N   LEU A 281     5334   5498   5133    150      7   -842       N  
ATOM   2153  CA  LEU A 281     -18.330  -2.422 -40.977  1.00 38.97           C  
ANISOU 2153  CA  LEU A 281     4966   5123   4716    130     19   -869       C  
ATOM   2154  C   LEU A 281     -17.022  -1.647 -41.060  1.00 40.93           C  
ANISOU 2154  C   LEU A 281     5163   5430   4957    166     38   -883       C  
ATOM   2155  O   LEU A 281     -16.381  -1.665 -42.116  1.00 44.38           O  
ANISOU 2155  O   LEU A 281     5618   5877   5367    161     60   -910       O  
ATOM   2156  CB  LEU A 281     -19.379  -1.738 -41.857  1.00 37.74           C  
ANISOU 2156  CB  LEU A 281     4816   4970   4554     51    -15   -863       C  
ATOM   2157  CG  LEU A 281     -20.597  -2.569 -42.262  1.00 39.13           C  
ANISOU 2157  CG  LEU A 281     5050   5093   4726      0    -33   -863       C  
ATOM   2158  CD1 LEU A 281     -21.535  -1.743 -43.126  1.00 43.89           C  
ANISOU 2158  CD1 LEU A 281     5644   5711   5321    -70    -74   -855       C  
ATOM   2159  CD2 LEU A 281     -20.168  -3.835 -42.986  1.00 36.66           C  
ANISOU 2159  CD2 LEU A 281     4812   4734   4382     12     -1   -894       C  
ATOM   2160  N   THR A 282     -16.609  -0.975 -39.985  1.00 40.25           N  
ANISOU 2160  N   THR A 282     5014   5385   4894    198     33   -867       N  
ATOM   2161  CA  THR A 282     -15.404  -0.154 -40.003  1.00 39.21           C  
ANISOU 2161  CA  THR A 282     4825   5315   4758    223     49   -882       C  
ATOM   2162  C   THR A 282     -14.367  -0.582 -38.973  1.00 41.38           C  
ANISOU 2162  C   THR A 282     5067   5614   5043    303     67   -886       C  
ATOM   2163  O   THR A 282     -13.367   0.124 -38.799  1.00 50.40           O  
ANISOU 2163  O   THR A 282     6150   6815   6186    324     77   -898       O  
ATOM   2164  CB  THR A 282     -15.752   1.323 -39.781  1.00 38.49           C  
ANISOU 2164  CB  THR A 282     4682   5263   4679    180     24   -863       C  
ATOM   2165  OG1 THR A 282     -16.384   1.479 -38.505  1.00 43.19           O  
ANISOU 2165  OG1 THR A 282     5253   5853   5302    190      1   -834       O  
ATOM   2166  CG2 THR A 282     -16.682   1.828 -40.873  1.00 37.49           C  
ANISOU 2166  CG2 THR A 282     4585   5120   4539    109      4   -858       C  
ATOM   2167  N   VAL A 283     -14.571  -1.702 -38.282  1.00 40.36           N  
ANISOU 2167  N   VAL A 283     4975   5441   4920    347     69   -877       N  
ATOM   2168  CA  VAL A 283     -13.625  -2.130 -37.253  1.00 39.52           C  
ANISOU 2168  CA  VAL A 283     4840   5355   4819    429     79   -877       C  
ATOM   2169  C   VAL A 283     -12.282  -2.411 -37.918  1.00 44.54           C  
ANISOU 2169  C   VAL A 283     5461   6023   5439    477    114   -912       C  
ATOM   2170  O   VAL A 283     -12.203  -3.235 -38.841  1.00 50.31           O  
ANISOU 2170  O   VAL A 283     6248   6716   6152    481    139   -933       O  
ATOM   2171  CB  VAL A 283     -14.142  -3.353 -36.474  1.00 31.54           C  
ANISOU 2171  CB  VAL A 283     3889   4282   3814    467     78   -858       C  
ATOM   2172  CG1 VAL A 283     -14.699  -4.409 -37.421  1.00 46.25           C  
ANISOU 2172  CG1 VAL A 283     5837   6075   5661    444     96   -871       C  
ATOM   2173  CG2 VAL A 283     -13.042  -3.931 -35.594  1.00 42.75           C  
ANISOU 2173  CG2 VAL A 283     5291   5720   5232    564     90   -860       C  
ATOM   2174  N   PRO A 284     -11.215  -1.723 -37.504  1.00 39.78           N  
ANISOU 2174  N   PRO A 284     4782   5492   4842    509    118   -923       N  
ATOM   2175  CA  PRO A 284      -9.911  -1.934 -38.156  1.00 41.45           C  
ANISOU 2175  CA  PRO A 284     4967   5741   5040    552    154   -960       C  
ATOM   2176  C   PRO A 284      -9.424  -3.368 -38.097  1.00 43.24           C  
ANISOU 2176  C   PRO A 284     5239   5931   5261    635    178   -971       C  
ATOM   2177  O   PRO A 284      -8.880  -3.878 -39.084  1.00 49.97           O  
ANISOU 2177  O   PRO A 284     6116   6774   6097    650    214  -1001       O  
ATOM   2178  CB  PRO A 284      -8.986  -0.994 -37.373  1.00 40.33           C  
ANISOU 2178  CB  PRO A 284     4730   5685   4911    574    145   -964       C  
ATOM   2179  CG  PRO A 284      -9.887   0.071 -36.849  1.00 40.52           C  
ANISOU 2179  CG  PRO A 284     4736   5712   4946    510    111   -936       C  
ATOM   2180  CD  PRO A 284     -11.185  -0.612 -36.539  1.00 33.98           C  
ANISOU 2180  CD  PRO A 284     3979   4809   4123    496     91   -906       C  
ATOM   2181  N   PHE A 285      -9.613  -4.037 -36.963  1.00 47.22           N  
ANISOU 2181  N   PHE A 285     5761   6408   5774    690    160   -946       N  
ATOM   2182  CA  PHE A 285      -9.132  -5.400 -36.753  1.00 50.86           C  
ANISOU 2182  CA  PHE A 285     6269   6828   6227    779    181   -951       C  
ATOM   2183  C   PHE A 285     -10.294  -6.207 -36.181  1.00 56.02           C  
ANISOU 2183  C   PHE A 285     7006   7397   6881    771    166   -919       C  
ATOM   2184  O   PHE A 285     -10.440  -6.328 -34.961  1.00 53.79           O  
ANISOU 2184  O   PHE A 285     6719   7112   6607    807    143   -890       O  
ATOM   2185  CB  PHE A 285      -7.911  -5.401 -35.839  1.00 55.19           C  
ANISOU 2185  CB  PHE A 285     6746   7440   6782    872    176   -955       C  
ATOM   2186  CG  PHE A 285      -6.850  -4.419 -36.255  1.00 50.38           C  
ANISOU 2186  CG  PHE A 285     6040   6925   6177    864    187   -986       C  
ATOM   2187  CD1 PHE A 285      -6.052  -4.668 -37.360  1.00 51.06           C  
ANISOU 2187  CD1 PHE A 285     6120   7027   6253    879    230  -1025       C  
ATOM   2188  CD2 PHE A 285      -6.668  -3.236 -35.558  1.00 50.74           C  
ANISOU 2188  CD2 PHE A 285     6005   7042   6234    836    158   -978       C  
ATOM   2189  CE1 PHE A 285      -5.081  -3.764 -37.752  1.00 50.38           C  
ANISOU 2189  CE1 PHE A 285     5946   7028   6170    865    246  -1056       C  
ATOM   2190  CE2 PHE A 285      -5.700  -2.326 -35.946  1.00 51.78           C  
ANISOU 2190  CE2 PHE A 285     6049   7256   6367    820    172  -1009       C  
ATOM   2191  CZ  PHE A 285      -4.905  -2.591 -37.044  1.00 52.47           C  
ANISOU 2191  CZ  PHE A 285     6128   7361   6446    833    217  -1048       C  
ATOM   2192  N   GLY A 286     -11.118  -6.761 -37.073  1.00 59.87           N  
ANISOU 2192  N   GLY A 286     7572   7816   7358    719    181   -924       N  
ATOM   2193  CA  GLY A 286     -12.278  -7.526 -36.652  1.00 54.38           C  
ANISOU 2193  CA  GLY A 286     6958   7040   6663    696    171   -899       C  
ATOM   2194  C   GLY A 286     -11.941  -8.832 -35.967  1.00 63.09           C  
ANISOU 2194  C   GLY A 286     8122   8090   7759    786    188   -890       C  
ATOM   2195  O   GLY A 286     -12.809  -9.416 -35.311  1.00 65.43           O  
ANISOU 2195  O   GLY A 286     8478   8324   8057    775    180   -864       O  
ATOM   2196  N   GLN A 287     -10.702  -9.310 -36.113  1.00 73.92           N  
ANISOU 2196  N   GLN A 287     9481   9483   9124    875    213   -912       N  
ATOM   2197  CA  GLN A 287     -10.279 -10.499 -35.383  1.00 78.96           C  
ANISOU 2197  CA  GLN A 287    10174  10073   9754    975    226   -900       C  
ATOM   2198  C   GLN A 287     -10.093 -10.206 -33.901  1.00 77.48           C  
ANISOU 2198  C   GLN A 287     9942   9921   9576   1025    192   -866       C  
ATOM   2199  O   GLN A 287     -10.327 -11.085 -33.063  1.00 75.73           O  
ANISOU 2199  O   GLN A 287     9786   9641   9347   1075    191   -840       O  
ATOM   2200  CB  GLN A 287      -8.990 -11.056 -35.987  1.00 87.74           C  
ANISOU 2200  CB  GLN A 287    11278  11203  10857   1063    263   -934       C  
ATOM   2201  CG  GLN A 287      -8.980 -11.083 -37.507  1.00 72.48           C  
ANISOU 2201  CG  GLN A 287     9369   9257   8912   1010    298   -973       C  
ATOM   2202  CD  GLN A 287      -9.508 -12.388 -38.072  1.00 66.76           C  
ANISOU 2202  CD  GLN A 287     8772   8425   8168   1010    332   -981       C  
ATOM   2203  OE1 GLN A 287     -10.293 -13.084 -37.428  1.00 74.54           O  
ANISOU 2203  OE1 GLN A 287     9832   9338   9151   1007    324   -954       O  
ATOM   2204  NE2 GLN A 287      -9.079 -12.726 -39.283  1.00 73.29           N  
ANISOU 2204  NE2 GLN A 287     9627   9239   8980   1009    373  -1020       N  
ATOM   2205  N   LYS A 288      -9.677  -8.989 -33.560  1.00 84.81           N  
ANISOU 2205  N   LYS A 288    10766  10941  10517   1010    165   -867       N  
ATOM   2206  CA  LYS A 288      -9.587  -8.606 -32.162  1.00 81.85           C  
ANISOU 2206  CA  LYS A 288    10349  10602  10147   1044    129   -837       C  
ATOM   2207  C   LYS A 288     -10.983  -8.587 -31.539  1.00 82.74           C  
ANISOU 2207  C   LYS A 288    10516  10657  10263    977    113   -802       C  
ATOM   2208  O   LYS A 288     -11.922  -8.040 -32.128  1.00 85.39           O  
ANISOU 2208  O   LYS A 288    10855  10980  10608    879    111   -804       O  
ATOM   2209  CB  LYS A 288      -8.929  -7.235 -32.022  1.00 78.57           C  
ANISOU 2209  CB  LYS A 288     9816  10295   9744   1024    107   -849       C  
ATOM   2210  CG  LYS A 288      -7.551  -7.146 -32.668  1.00 83.42           C  
ANISOU 2210  CG  LYS A 288    10364  10975  10357   1079    127   -888       C  
ATOM   2211  CD  LYS A 288      -6.478  -7.786 -31.798  1.00 92.52           C  
ANISOU 2211  CD  LYS A 288    11494  12157  11504   1203    118   -884       C  
ATOM   2212  CE  LYS A 288      -5.552  -8.672 -32.619  1.00 89.15           C  
ANISOU 2212  CE  LYS A 288    11080  11722  11071   1280    158   -915       C  
ATOM   2213  NZ  LYS A 288      -4.250  -8.896 -31.931  1.00 83.62           N  
ANISOU 2213  NZ  LYS A 288    10313  11088  10370   1397    145   -922       N  
ATOM   2214  N   PRO A 289     -11.147  -9.163 -30.345  1.00104.93           N  
ANISOU 2214  N   PRO A 289    13368  13435  13067   1028    101   -770       N  
ATOM   2215  CA  PRO A 289     -12.490  -9.432 -29.815  1.00104.96           C  
ANISOU 2215  CA  PRO A 289    13440  13367  13070    968     98   -740       C  
ATOM   2216  C   PRO A 289     -13.176  -8.288 -29.082  1.00103.79           C  
ANISOU 2216  C   PRO A 289    13238  13260  12937    903     68   -719       C  
ATOM   2217  O   PRO A 289     -14.372  -8.427 -28.788  1.00108.10           O  
ANISOU 2217  O   PRO A 289    13833  13752  13489    842     69   -699       O  
ATOM   2218  CB  PRO A 289     -12.248 -10.597 -28.835  1.00 99.84           C  
ANISOU 2218  CB  PRO A 289    12869  12664  12403   1060    104   -714       C  
ATOM   2219  CG  PRO A 289     -10.747 -10.742 -28.691  1.00100.85           C  
ANISOU 2219  CG  PRO A 289    12947  12849  12521   1173     98   -727       C  
ATOM   2220  CD  PRO A 289     -10.078  -9.653 -29.462  1.00 99.20           C  
ANISOU 2220  CD  PRO A 289    12631  12734  12328   1145     91   -761       C  
ATOM   2221  N   ASN A 290     -12.466  -7.199 -28.753  1.00 73.26           N  
ANISOU 2221  N   ASN A 290     9274   9484   9077    914     43   -726       N  
ATOM   2222  CA  ASN A 290     -13.015  -6.052 -28.025  1.00 70.98           C  
ANISOU 2222  CA  ASN A 290     8932   9236   8800    858     17   -709       C  
ATOM   2223  C   ASN A 290     -13.170  -6.428 -26.552  1.00 71.09           C  
ANISOU 2223  C   ASN A 290     8980   9230   8801    903      3   -675       C  
ATOM   2224  O   ASN A 290     -13.512  -7.568 -26.218  1.00 68.78           O  
ANISOU 2224  O   ASN A 290     8775   8862   8494    936     18   -657       O  
ATOM   2225  CB  ASN A 290     -14.334  -5.581 -28.675  1.00 72.54           C  
ANISOU 2225  CB  ASN A 290     9145   9402   9016    749     22   -708       C  
ATOM   2226  CG  ASN A 290     -15.223  -4.704 -27.761  1.00 86.85           C  
ANISOU 2226  CG  ASN A 290    10932  11226  10841    695      2   -683       C  
ATOM   2227  OD1 ASN A 290     -14.907  -4.406 -26.611  1.00 84.80           O  
ANISOU 2227  OD1 ASN A 290    10649  10997  10575    731    -14   -667       O  
ATOM   2228  ND2 ASN A 290     -16.365  -4.297 -28.307  1.00 86.71           N  
ANISOU 2228  ND2 ASN A 290    10920  11184  10842    608      4   -681       N  
ATOM   2229  N   ILE A 291     -12.918  -5.467 -25.666  1.00 54.79           N  
ANISOU 2229  N   ILE A 291     6851   7230   6737    903    -25   -666       N  
ATOM   2230  CA  ILE A 291     -12.960  -5.703 -24.226  1.00 48.75           C  
ANISOU 2230  CA  ILE A 291     6112   6458   5953    947    -41   -635       C  
ATOM   2231  C   ILE A 291     -14.400  -5.587 -23.744  1.00 51.62           C  
ANISOU 2231  C   ILE A 291     6523   6766   6325    873    -33   -610       C  
ATOM   2232  O   ILE A 291     -15.022  -4.525 -23.858  1.00 47.93           O  
ANISOU 2232  O   ILE A 291     6008   6324   5878    796    -39   -613       O  
ATOM   2233  CB  ILE A 291     -12.054  -4.715 -23.478  1.00 47.27           C  
ANISOU 2233  CB  ILE A 291     5836   6365   5758    975    -75   -641       C  
ATOM   2234  CG1 ILE A 291     -10.582  -5.035 -23.738  1.00 57.33           C  
ANISOU 2234  CG1 ILE A 291     7066   7694   7022   1065    -84   -664       C  
ATOM   2235  CG2 ILE A 291     -12.356  -4.739 -21.988  1.00 46.25           C  
ANISOU 2235  CG2 ILE A 291     5736   6227   5608    996    -93   -608       C  
ATOM   2236  CD1 ILE A 291      -9.629  -4.309 -22.817  1.00 59.34           C  
ANISOU 2236  CD1 ILE A 291     7243   8042   7264   1106   -121   -668       C  
ATOM   2237  N   ASP A 292     -14.927  -6.675 -23.185  1.00 58.81           N  
ANISOU 2237  N   ASP A 292     7527   7599   7221    896    -17   -584       N  
ATOM   2238  CA  ASP A 292     -16.272  -6.692 -22.616  1.00 50.18           C  
ANISOU 2238  CA  ASP A 292     6481   6450   6133    829     -4   -560       C  
ATOM   2239  C   ASP A 292     -16.212  -7.466 -21.307  1.00 54.68           C  
ANISOU 2239  C   ASP A 292     7123   6982   6671    890     -3   -527       C  
ATOM   2240  O   ASP A 292     -16.029  -8.687 -21.315  1.00 60.35           O  
ANISOU 2240  O   ASP A 292     7923   7638   7370    944     14   -518       O  
ATOM   2241  CB  ASP A 292     -17.278  -7.321 -23.581  1.00 47.92           C  
ANISOU 2241  CB  ASP A 292     6251   6092   5864    764     27   -567       C  
ATOM   2242  CG  ASP A 292     -18.701  -6.877 -23.309  1.00 54.51           C  
ANISOU 2242  CG  ASP A 292     7090   6901   6720    671     36   -554       C  
ATOM   2243  OD1 ASP A 292     -18.997  -6.497 -22.157  1.00 53.55           O  
ANISOU 2243  OD1 ASP A 292     6966   6790   6593    670     31   -532       O  
ATOM   2244  OD2 ASP A 292     -19.523  -6.906 -24.248  1.00 59.24           O1-
ANISOU 2244  OD2 ASP A 292     7694   7472   7340    600     49   -567       O1-
ATOM   2245  N   VAL A 293     -16.368  -6.760 -20.189  1.00 52.19           N  
ANISOU 2245  N   VAL A 293     6783   6700   6348    883    -19   -509       N  
ATOM   2246  CA  VAL A 293     -16.266  -7.371 -18.868  1.00 50.94           C  
ANISOU 2246  CA  VAL A 293     6690   6512   6152    941    -22   -477       C  
ATOM   2247  C   VAL A 293     -17.648  -7.790 -18.386  1.00 52.24           C  
ANISOU 2247  C   VAL A 293     6933   6596   6318    877     12   -453       C  
ATOM   2248  O   VAL A 293     -17.832  -8.120 -17.209  1.00 60.25           O  
ANISOU 2248  O   VAL A 293     8006   7584   7303    901     16   -423       O  
ATOM   2249  CB  VAL A 293     -15.598  -6.416 -17.862  1.00 50.88           C  
ANISOU 2249  CB  VAL A 293     6619   6587   6126    970    -60   -472       C  
ATOM   2250  CG1 VAL A 293     -14.229  -5.991 -18.367  1.00 52.40           C  
ANISOU 2250  CG1 VAL A 293     6726   6864   6320   1026    -92   -500       C  
ATOM   2251  CG2 VAL A 293     -16.482  -5.204 -17.611  1.00 48.56           C  
ANISOU 2251  CG2 VAL A 293     6275   6319   5856    878    -57   -475       C  
ATOM   2252  N   THR A 294     -18.629  -7.777 -19.292  1.00 52.05           N  
ANISOU 2252  N   THR A 294     6911   6538   6328    792     37   -466       N  
ATOM   2253  CA  THR A 294     -19.972  -8.217 -18.928  1.00 53.02           C  
ANISOU 2253  CA  THR A 294     7100   6587   6457    725     73   -448       C  
ATOM   2254  C   THR A 294     -19.963  -9.663 -18.453  1.00 58.99           C  
ANISOU 2254  C   THR A 294     7978   7256   7178    773     99   -425       C  
ATOM   2255  O   THR A 294     -20.589  -9.995 -17.439  1.00 61.22           O  
ANISOU 2255  O   THR A 294     8325   7494   7443    760    120   -398       O  
ATOM   2256  CB  THR A 294     -20.923  -8.055 -20.115  1.00 53.78           C  
ANISOU 2256  CB  THR A 294     7174   6666   6595    633     90   -470       C  
ATOM   2257  OG1 THR A 294     -21.011  -6.671 -20.477  1.00 53.25           O  
ANISOU 2257  OG1 THR A 294     7002   6673   6557    588     66   -487       O  
ATOM   2258  CG2 THR A 294     -22.311  -8.574 -19.763  1.00 47.80           C  
ANISOU 2258  CG2 THR A 294     6480   5837   5846    560    128   -455       C  
ATOM   2259  N   ASP A 295     -19.249 -10.535 -19.167  1.00 61.83           N  
ANISOU 2259  N   ASP A 295     8377   7589   7528    831    101   -435       N  
ATOM   2260  CA  ASP A 295     -19.164 -11.932 -18.756  1.00 59.85           C  
ANISOU 2260  CA  ASP A 295     8249   7249   7242    886    127   -413       C  
ATOM   2261  C   ASP A 295     -18.494 -12.067 -17.395  1.00 55.38           C  
ANISOU 2261  C   ASP A 295     7717   6695   6632    973    108   -380       C  
ATOM   2262  O   ASP A 295     -18.970 -12.815 -16.533  1.00 57.94           O  
ANISOU 2262  O   ASP A 295     8141   6946   6926    979    134   -350       O  
ATOM   2263  CB  ASP A 295     -18.413 -12.746 -19.809  1.00 57.61           C  
ANISOU 2263  CB  ASP A 295     7992   6940   6955    940    132   -433       C  
ATOM   2264  CG  ASP A 295     -19.298 -13.153 -20.970  1.00 64.86           C  
ANISOU 2264  CG  ASP A 295     8939   7803   7900    853    165   -456       C  
ATOM   2265  OD1 ASP A 295     -20.510 -12.855 -20.927  1.00 58.74           O  
ANISOU 2265  OD1 ASP A 295     8161   7011   7147    753    182   -455       O  
ATOM   2266  OD2 ASP A 295     -18.783 -13.773 -21.924  1.00 68.61           O1-
ANISOU 2266  OD2 ASP A 295     9439   8256   8375    885    174   -477       O1-
ATOM   2267  N   ALA A 296     -17.396 -11.338 -17.179  1.00 45.50           N  
ANISOU 2267  N   ALA A 296     6382   5533   5373   1038     62   -387       N  
ATOM   2268  CA  ALA A 296     -16.677 -11.436 -15.912  1.00 48.71           C  
ANISOU 2268  CA  ALA A 296     6813   5961   5734   1126     35   -358       C  
ATOM   2269  C   ALA A 296     -17.549 -10.990 -14.746  1.00 53.60           C  
ANISOU 2269  C   ALA A 296     7456   6571   6340   1072     45   -333       C  
ATOM   2270  O   ALA A 296     -17.478 -11.564 -13.653  1.00 52.73           O  
ANISOU 2270  O   ALA A 296     7428   6422   6183   1121     46   -299       O  
ATOM   2271  CB  ALA A 296     -15.393 -10.610 -15.972  1.00 48.78           C  
ANISOU 2271  CB  ALA A 296     6712   6081   5743   1189    -17   -378       C  
ATOM   2272  N   MET A 297     -18.374  -9.962 -14.958  1.00 64.11           N  
ANISOU 2272  N   MET A 297     8717   7935   7709    972     52   -349       N  
ATOM   2273  CA  MET A 297     -19.283  -9.518 -13.907  1.00 53.20           C  
ANISOU 2273  CA  MET A 297     7353   6541   6318    915     69   -329       C  
ATOM   2274  C   MET A 297     -20.299 -10.599 -13.562  1.00 57.94           C  
ANISOU 2274  C   MET A 297     8075   7033   6904    880    122   -305       C  
ATOM   2275  O   MET A 297     -20.574 -10.849 -12.382  1.00 65.87           O  
ANISOU 2275  O   MET A 297     9150   8006   7872    890    135   -274       O  
ATOM   2276  CB  MET A 297     -19.990  -8.234 -14.337  1.00 51.46           C  
ANISOU 2276  CB  MET A 297     7034   6374   6146    820     69   -353       C  
ATOM   2277  CG  MET A 297     -19.145  -6.992 -14.164  1.00 62.67           C  
ANISOU 2277  CG  MET A 297     8348   7896   7566    842     23   -369       C  
ATOM   2278  SD  MET A 297     -19.443  -5.748 -15.429  1.00 51.78           S  
ANISOU 2278  SD  MET A 297     6848   6577   6248    762     16   -408       S  
ATOM   2279  CE  MET A 297     -20.911  -4.977 -14.763  1.00 50.59           C  
ANISOU 2279  CE  MET A 297     6692   6411   6119    665     47   -398       C  
ATOM   2280  N   VAL A 298     -20.870 -11.251 -14.578  1.00 51.59           N  
ANISOU 2280  N   VAL A 298     7302   6172   6129    833    154   -319       N  
ATOM   2281  CA  VAL A 298     -21.784 -12.359 -14.322  1.00 57.52           C  
ANISOU 2281  CA  VAL A 298     8173   6816   6867    796    207   -300       C  
ATOM   2282  C   VAL A 298     -21.037 -13.543 -13.720  1.00 62.94           C  
ANISOU 2282  C   VAL A 298     8977   7442   7497    898    209   -270       C  
ATOM   2283  O   VAL A 298     -21.587 -14.274 -12.887  1.00 64.06           O  
ANISOU 2283  O   VAL A 298     9228   7506   7605    890    246   -240       O  
ATOM   2284  CB  VAL A 298     -22.532 -12.752 -15.609  1.00 63.50           C  
ANISOU 2284  CB  VAL A 298     8931   7531   7665    718    236   -327       C  
ATOM   2285  CG1 VAL A 298     -23.653 -13.728 -15.293  1.00 68.64           C  
ANISOU 2285  CG1 VAL A 298     9693   8079   8308    654    296   -312       C  
ATOM   2286  CG2 VAL A 298     -23.092 -11.515 -16.288  1.00 56.24           C  
ANISOU 2286  CG2 VAL A 298     7887   6682   6798    635    222   -356       C  
ATOM   2287  N   ASP A 299     -19.784 -13.758 -14.131  1.00 61.76           N  
ANISOU 2287  N   ASP A 299     8808   7324   7335    998    172   -277       N  
ATOM   2288  CA  ASP A 299     -18.974 -14.810 -13.523  1.00 66.15           C  
ANISOU 2288  CA  ASP A 299     9468   7831   7837   1111    167   -247       C  
ATOM   2289  C   ASP A 299     -18.804 -14.576 -12.028  1.00 67.99           C  
ANISOU 2289  C   ASP A 299     9732   8081   8021   1153    149   -211       C  
ATOM   2290  O   ASP A 299     -18.823 -15.525 -11.235  1.00 61.83           O  
ANISOU 2290  O   ASP A 299     9078   7224   7191   1201    168   -175       O  
ATOM   2291  CB  ASP A 299     -17.608 -14.890 -14.206  1.00 61.03           C  
ANISOU 2291  CB  ASP A 299     8767   7234   7189   1214    126   -265       C  
ATOM   2292  CG  ASP A 299     -17.702 -15.305 -15.661  1.00 64.97           C  
ANISOU 2292  CG  ASP A 299     9257   7703   7724   1184    149   -298       C  
ATOM   2293  OD1 ASP A 299     -18.642 -16.049 -16.013  1.00 66.80           O  
ANISOU 2293  OD1 ASP A 299     9574   7844   7964   1117    198   -298       O  
ATOM   2294  OD2 ASP A 299     -16.834 -14.884 -16.455  1.00 60.57           O1-
ANISOU 2294  OD2 ASP A 299     8611   7215   7188   1222    118   -327       O1-
ATOM   2295  N   GLN A 300     -18.639 -13.318 -11.624  1.00 54.19           N  
ANISOU 2295  N   GLN A 300     7878   6430   6283   1134    113   -220       N  
ATOM   2296  CA  GLN A 300     -18.466 -12.953 -10.226  1.00 54.15           C  
ANISOU 2296  CA  GLN A 300     7893   6452   6230   1167     92   -191       C  
ATOM   2297  C   GLN A 300     -19.782 -12.596  -9.544  1.00 52.81           C  
ANISOU 2297  C   GLN A 300     7752   6249   6064   1062    136   -180       C  
ATOM   2298  O   GLN A 300     -19.763 -12.051  -8.435  1.00 52.46           O  
ANISOU 2298  O   GLN A 300     7709   6238   5987   1068    122   -163       O  
ATOM   2299  CB  GLN A 300     -17.474 -11.793 -10.109  1.00 43.49           C  
ANISOU 2299  CB  GLN A 300     6414   5226   4883   1207     28   -210       C  
ATOM   2300  CG  GLN A 300     -16.123 -12.086 -10.745  1.00 42.05           C  
ANISOU 2300  CG  GLN A 300     6191   5088   4699   1311    -16   -224       C  
ATOM   2301  CD  GLN A 300     -15.319 -10.831 -11.021  1.00 42.97           C  
ANISOU 2301  CD  GLN A 300     6160   5330   4839   1316    -67   -256       C  
ATOM   2302  OE1 GLN A 300     -15.414  -9.845 -10.292  1.00 48.93           O  
ANISOU 2302  OE1 GLN A 300     6863   6143   5584   1283    -87   -257       O  
ATOM   2303  NE2 GLN A 300     -14.519 -10.863 -12.082  1.00 39.05           N  
ANISOU 2303  NE2 GLN A 300     5596   4871   4369   1354    -84   -285       N  
ATOM   2304  N   ALA A 301     -20.916 -12.886 -10.188  1.00 53.74           N  
ANISOU 2304  N   ALA A 301     7892   6306   6222    965    190   -192       N  
ATOM   2305  CA  ALA A 301     -22.244 -12.724  -9.591  1.00 60.04           C  
ANISOU 2305  CA  ALA A 301     8724   7063   7026    865    242   -182       C  
ATOM   2306  C   ALA A 301     -22.498 -11.284  -9.150  1.00 58.31           C  
ANISOU 2306  C   ALA A 301     8398   6930   6826    817    224   -195       C  
ATOM   2307  O   ALA A 301     -23.146 -11.032  -8.132  1.00 58.68           O  
ANISOU 2307  O   ALA A 301     8479   6964   6853    778    251   -178       O  
ATOM   2308  CB  ALA A 301     -22.446 -13.692  -8.424  1.00 58.13           C  
ANISOU 2308  CB  ALA A 301     8631   6735   6720    895    275   -139       C  
ATOM   2309  N   TRP A 302     -21.980 -10.330  -9.923  1.00 60.77           N  
ANISOU 2309  N   TRP A 302     8584   7328   7176    818    181   -227       N  
ATOM   2310  CA  TRP A 302     -22.236  -8.924  -9.644  1.00 56.18           C  
ANISOU 2310  CA  TRP A 302     7901   6824   6619    769    167   -242       C  
ATOM   2311  C   TRP A 302     -23.721  -8.618  -9.784  1.00 61.35           C  
ANISOU 2311  C   TRP A 302     8544   7449   7318    654    220   -251       C  
ATOM   2312  O   TRP A 302     -24.365  -9.034 -10.751  1.00 59.30           O  
ANISOU 2312  O   TRP A 302     8282   7150   7098    600    246   -266       O  
ATOM   2313  CB  TRP A 302     -21.433  -8.035 -10.597  1.00 57.53           C  
ANISOU 2313  CB  TRP A 302     7949   7084   6825    785    118   -276       C  
ATOM   2314  CG  TRP A 302     -20.013  -7.791 -10.183  1.00 58.48           C  
ANISOU 2314  CG  TRP A 302     8041   7272   6907    883     60   -274       C  
ATOM   2315  CD1 TRP A 302     -19.203  -8.637  -9.483  1.00 58.12           C  
ANISOU 2315  CD1 TRP A 302     8074   7207   6804    979     40   -247       C  
ATOM   2316  CD2 TRP A 302     -19.234  -6.617 -10.448  1.00 56.52           C  
ANISOU 2316  CD2 TRP A 302     7676   7125   6675    893     13   -301       C  
ATOM   2317  NE1 TRP A 302     -17.967  -8.063  -9.297  1.00 61.25           N  
ANISOU 2317  NE1 TRP A 302     8401   7692   7181   1049    -20   -257       N  
ATOM   2318  CE2 TRP A 302     -17.962  -6.823  -9.879  1.00 51.55           C  
ANISOU 2318  CE2 TRP A 302     7053   6538   5997    994    -35   -291       C  
ATOM   2319  CE3 TRP A 302     -19.491  -5.412 -11.109  1.00 54.35           C  
ANISOU 2319  CE3 TRP A 302     7295   6908   6448    827      8   -332       C  
ATOM   2320  CZ2 TRP A 302     -16.949  -5.868  -9.953  1.00 54.61           C  
ANISOU 2320  CZ2 TRP A 302     7339   7026   6386   1023    -86   -315       C  
ATOM   2321  CZ3 TRP A 302     -18.483  -4.466 -11.182  1.00 53.91           C  
ANISOU 2321  CZ3 TRP A 302     7148   6944   6392    856    -40   -353       C  
ATOM   2322  CH2 TRP A 302     -17.229  -4.699 -10.606  1.00 54.05           C  
ANISOU 2322  CH2 TRP A 302     7169   7006   6362    949    -85   -346       C  
ATOM   2323  N   ASP A 303     -24.267  -7.901  -8.811  1.00 69.04           N  
ANISOU 2323  N   ASP A 303     9509   8441   8283    616    236   -243       N  
ATOM   2324  CA  ASP A 303     -25.597  -7.324  -8.919  1.00 67.55           C  
ANISOU 2324  CA  ASP A 303     9278   8245   8141    512    281   -256       C  
ATOM   2325  C   ASP A 303     -25.466  -5.821  -9.142  1.00 61.14           C  
ANISOU 2325  C   ASP A 303     8343   7524   7365    492    249   -281       C  
ATOM   2326  O   ASP A 303     -24.362  -5.271  -9.186  1.00 55.71           O  
ANISOU 2326  O   ASP A 303     7607   6900   6662    551    196   -289       O  
ATOM   2327  CB  ASP A 303     -26.440  -7.645  -7.681  1.00 64.67           C  
ANISOU 2327  CB  ASP A 303     9000   7827   7745    478    335   -231       C  
ATOM   2328  CG  ASP A 303     -25.647  -7.561  -6.392  1.00 78.56           C  
ANISOU 2328  CG  ASP A 303    10812   9602   9433    549    312   -205       C  
ATOM   2329  OD1 ASP A 303     -24.463  -7.164  -6.438  1.00 83.76           O  
ANISOU 2329  OD1 ASP A 303    11430  10324  10073    622    251   -210       O  
ATOM   2330  OD2 ASP A 303     -26.214  -7.894  -5.331  1.00 82.19           O1-
ANISOU 2330  OD2 ASP A 303    11356  10015   9856    530    356   -181       O1-
ATOM   2331  N   ALA A 304     -26.612  -5.153  -9.289  1.00 56.83           N  
ANISOU 2331  N   ALA A 304     7745   6981   6865    408    282   -294       N  
ATOM   2332  CA  ALA A 304     -26.592  -3.723  -9.582  1.00 55.26           C  
ANISOU 2332  CA  ALA A 304     7435   6859   6703    385    258   -318       C  
ATOM   2333  C   ALA A 304     -25.960  -2.930  -8.445  1.00 58.90           C  
ANISOU 2333  C   ALA A 304     7890   7366   7121    423    237   -311       C  
ATOM   2334  O   ALA A 304     -25.210  -1.977  -8.688  1.00 55.14           O  
ANISOU 2334  O   ALA A 304     7340   6960   6651    446    194   -329       O  
ATOM   2335  CB  ALA A 304     -28.005  -3.221  -9.864  1.00 52.80           C  
ANISOU 2335  CB  ALA A 304     7076   6538   6449    295    300   -330       C  
ATOM   2336  N   GLN A 305     -26.254  -3.304  -7.197  1.00 53.06           N  
ANISOU 2336  N   GLN A 305     7233   6590   6336    427    269   -287       N  
ATOM   2337  CA  GLN A 305     -25.666  -2.604  -6.059  1.00 54.12           C  
ANISOU 2337  CA  GLN A 305     7373   6768   6422    461    248   -281       C  
ATOM   2338  C   GLN A 305     -24.147  -2.704  -6.065  1.00 52.14           C  
ANISOU 2338  C   GLN A 305     7118   6564   6130    550    182   -280       C  
ATOM   2339  O   GLN A 305     -23.461  -1.755  -5.667  1.00 45.62           O  
ANISOU 2339  O   GLN A 305     6242   5804   5285    570    145   -292       O  
ATOM   2340  CB  GLN A 305     -26.232  -3.158  -4.751  1.00 53.93           C  
ANISOU 2340  CB  GLN A 305     7454   6688   6348    452    296   -252       C  
ATOM   2341  CG  GLN A 305     -25.852  -2.352  -3.521  1.00 50.85           C  
ANISOU 2341  CG  GLN A 305     7073   6340   5909    471    284   -248       C  
ATOM   2342  CD  GLN A 305     -25.482  -3.228  -2.341  1.00 69.26           C  
ANISOU 2342  CD  GLN A 305     9526   8632   8158    522    288   -214       C  
ATOM   2343  OE1 GLN A 305     -24.382  -3.126  -1.798  1.00 65.78           O  
ANISOU 2343  OE1 GLN A 305     9100   8232   7662    590    234   -206       O  
ATOM   2344  NE2 GLN A 305     -26.403  -4.096  -1.937  1.00 72.86           N  
ANISOU 2344  NE2 GLN A 305    10071   9008   8603    487    351   -192       N  
ATOM   2345  N   ARG A 306     -23.604  -3.838  -6.515  1.00 56.85           N  
ANISOU 2345  N   ARG A 306     7765   7127   6711    602    167   -268       N  
ATOM   2346  CA  ARG A 306     -22.157  -3.968  -6.650  1.00 53.11           C  
ANISOU 2346  CA  ARG A 306     7274   6701   6205    690    104   -270       C  
ATOM   2347  C   ARG A 306     -21.609  -2.970  -7.663  1.00 49.14           C  
ANISOU 2347  C   ARG A 306     6650   6275   5747    681     66   -305       C  
ATOM   2348  O   ARG A 306     -20.543  -2.380  -7.451  1.00 48.19           O  
ANISOU 2348  O   ARG A 306     6481   6225   5603    727     16   -316       O  
ATOM   2349  CB  ARG A 306     -21.796  -5.397  -7.059  1.00 57.53           C  
ANISOU 2349  CB  ARG A 306     7910   7202   6746    746    103   -252       C  
ATOM   2350  CG  ARG A 306     -20.306  -5.646  -7.260  1.00 49.90           C  
ANISOU 2350  CG  ARG A 306     6925   6283   5751    845     41   -254       C  
ATOM   2351  CD  ARG A 306     -19.464  -5.053  -6.132  1.00 58.53           C  
ANISOU 2351  CD  ARG A 306     8009   7441   6789    896     -4   -247       C  
ATOM   2352  NE  ARG A 306     -18.040  -5.353  -6.260  1.00 60.30           N  
ANISOU 2352  NE  ARG A 306     8211   7715   6984    995    -65   -249       N  
ATOM   2353  CZ  ARG A 306     -17.507  -6.568  -6.305  1.00 58.78           C  
ANISOU 2353  CZ  ARG A 306     8092   7480   6762   1076    -75   -227       C  
ATOM   2354  NH1 ARG A 306     -18.247  -7.660  -6.192  1.00 44.11           N  
ANISOU 2354  NH1 ARG A 306     6345   5522   4893   1069    -27   -199       N  
ATOM   2355  NH2 ARG A 306     -16.192  -6.691  -6.465  1.00 56.45           N  
ANISOU 2355  NH2 ARG A 306     7757   7244   6447   1166   -132   -234       N  
ATOM   2356  N   ILE A 307     -22.325  -2.772  -8.771  1.00 48.80           N  
ANISOU 2356  N   ILE A 307     6558   6219   5767    621     88   -324       N  
ATOM   2357  CA  ILE A 307     -21.859  -1.862  -9.814  1.00 43.30           C  
ANISOU 2357  CA  ILE A 307     5756   5587   5112    609     57   -356       C  
ATOM   2358  C   ILE A 307     -21.719  -0.448  -9.265  1.00 39.76           C  
ANISOU 2358  C   ILE A 307     5243   5204   4662    586     42   -371       C  
ATOM   2359  O   ILE A 307     -20.733   0.247  -9.540  1.00 43.68           O  
ANISOU 2359  O   ILE A 307     5672   5768   5155    611     -1   -391       O  
ATOM   2360  CB  ILE A 307     -22.809  -1.915 -11.025  1.00 41.58           C  
ANISOU 2360  CB  ILE A 307     5507   5337   4956    543     85   -369       C  
ATOM   2361  CG1 ILE A 307     -22.677  -3.256 -11.748  1.00 45.16           C  
ANISOU 2361  CG1 ILE A 307     6015   5735   5407    571     91   -362       C  
ATOM   2362  CG2 ILE A 307     -22.528  -0.771 -11.978  1.00 44.75           C  
ANISOU 2362  CG2 ILE A 307     5804   5802   5397    518     59   -400       C  
ATOM   2363  CD1 ILE A 307     -23.614  -3.409 -12.924  1.00 43.43           C  
ANISOU 2363  CD1 ILE A 307     5774   5484   5242    504    116   -377       C  
ATOM   2364  N   PHE A 308     -22.699   0.000  -8.478  1.00 42.39           N  
ANISOU 2364  N   PHE A 308     5595   5515   4997    535     80   -363       N  
ATOM   2365  CA  PHE A 308     -22.632   1.335  -7.894  1.00 44.88           C  
ANISOU 2365  CA  PHE A 308     5860   5884   5308    512     72   -378       C  
ATOM   2366  C   PHE A 308     -21.679   1.403  -6.708  1.00 39.81           C  
ANISOU 2366  C   PHE A 308     5251   5277   4597    566     39   -369       C  
ATOM   2367  O   PHE A 308     -21.041   2.440  -6.496  1.00 39.14           O  
ANISOU 2367  O   PHE A 308     5111   5257   4502    566      9   -390       O  
ATOM   2368  CB  PHE A 308     -24.028   1.795  -7.480  1.00 43.34           C  
ANISOU 2368  CB  PHE A 308     5673   5653   5140    442    128   -374       C  
ATOM   2369  CG  PHE A 308     -24.935   2.066  -8.640  1.00 34.91           C  
ANISOU 2369  CG  PHE A 308     4549   4571   4143    385    150   -388       C  
ATOM   2370  CD1 PHE A 308     -25.701   1.052  -9.186  1.00 42.17           C  
ANISOU 2370  CD1 PHE A 308     5504   5433   5088    363    179   -378       C  
ATOM   2371  CD2 PHE A 308     -25.007   3.330  -9.197  1.00 32.72           C  
ANISOU 2371  CD2 PHE A 308     4188   4338   3904    354    140   -412       C  
ATOM   2372  CE1 PHE A 308     -26.531   1.295 -10.259  1.00 39.28           C  
ANISOU 2372  CE1 PHE A 308     5084   5059   4783    311    193   -391       C  
ATOM   2373  CE2 PHE A 308     -25.835   3.580 -10.272  1.00 35.83           C  
ANISOU 2373  CE2 PHE A 308     4533   4720   4359    307    154   -422       C  
ATOM   2374  CZ  PHE A 308     -26.598   2.560 -10.803  1.00 40.90           C  
ANISOU 2374  CZ  PHE A 308     5205   5311   5025    286    179   -412       C  
ATOM   2375  N   LYS A 309     -21.571   0.325  -5.926  1.00 43.66           N  
ANISOU 2375  N   LYS A 309     5831   5723   5034    610     44   -340       N  
ATOM   2376  CA  LYS A 309     -20.610   0.310  -4.827  1.00 47.37           C  
ANISOU 2376  CA  LYS A 309     6336   6230   5434    670      5   -330       C  
ATOM   2377  C   LYS A 309     -19.185   0.439  -5.349  1.00 46.92           C  
ANISOU 2377  C   LYS A 309     6215   6244   5367    730    -61   -348       C  
ATOM   2378  O   LYS A 309     -18.360   1.147  -4.759  1.00 51.92           O  
ANISOU 2378  O   LYS A 309     6816   6946   5966    750   -102   -361       O  
ATOM   2379  CB  LYS A 309     -20.770  -0.966  -4.000  1.00 51.15           C  
ANISOU 2379  CB  LYS A 309     6934   6643   5859    711     22   -291       C  
ATOM   2380  CG  LYS A 309     -21.893  -0.911  -2.974  1.00 53.63           C  
ANISOU 2380  CG  LYS A 309     7317   6906   6153    660     80   -274       C  
ATOM   2381  CD  LYS A 309     -21.783   0.324  -2.094  1.00 56.78           C  
ANISOU 2381  CD  LYS A 309     7686   7360   6528    637     70   -289       C  
ATOM   2382  CE  LYS A 309     -22.814   0.303  -0.976  1.00 50.28           C  
ANISOU 2382  CE  LYS A 309     6942   6486   5677    594    130   -271       C  
ATOM   2383  NZ  LYS A 309     -22.461   1.243   0.123  1.00 52.77           N  
ANISOU 2383  NZ  LYS A 309     7259   6850   5942    593    114   -280       N  
ATOM   2384  N   GLU A 310     -18.875  -0.244  -6.453  1.00 54.69           N  
ANISOU 2384  N   GLU A 310     7182   7217   6382    757    -70   -352       N  
ATOM   2385  CA  GLU A 310     -17.573  -0.070  -7.087  1.00 60.44           C  
ANISOU 2385  CA  GLU A 310     7838   8015   7110    808   -124   -374       C  
ATOM   2386  C   GLU A 310     -17.448   1.313  -7.714  1.00 54.35           C  
ANISOU 2386  C   GLU A 310     6962   7306   6381    752   -133   -411       C  
ATOM   2387  O   GLU A 310     -16.379   1.932  -7.656  1.00 55.15           O  
ANISOU 2387  O   GLU A 310     7002   7486   6466    776   -177   -433       O  
ATOM   2388  CB  GLU A 310     -17.348  -1.160  -8.134  1.00 57.16           C  
ANISOU 2388  CB  GLU A 310     7437   7564   6718    847   -123   -369       C  
ATOM   2389  CG  GLU A 310     -15.919  -1.672  -8.190  1.00 65.92           C  
ANISOU 2389  CG  GLU A 310     8530   8721   7794    942   -176   -372       C  
ATOM   2390  CD  GLU A 310     -15.614  -2.679  -7.096  1.00 75.15           C  
ANISOU 2390  CD  GLU A 310     9798   9859   8899   1019   -191   -335       C  
ATOM   2391  OE1 GLU A 310     -16.525  -2.994  -6.301  1.00 70.07           O  
ANISOU 2391  OE1 GLU A 310     9239   9151   8233    992   -155   -308       O  
ATOM   2392  OE2 GLU A 310     -14.461  -3.154  -7.031  1.00 84.96           O1-
ANISOU 2392  OE2 GLU A 310    11032  11140  10111   1107   -237   -334       O1-
ATOM   2393  N   ALA A 311     -18.528   1.810  -8.323  1.00 44.79           N  
ANISOU 2393  N   ALA A 311     5731   6065   5224    677    -91   -419       N  
ATOM   2394  CA  ALA A 311     -18.523   3.177  -8.833  1.00 38.41           C  
ANISOU 2394  CA  ALA A 311     4837   5307   4451    623    -94   -450       C  
ATOM   2395  C   ALA A 311     -18.341   4.176  -7.701  1.00 43.76           C  
ANISOU 2395  C   ALA A 311     5507   6026   5094    607   -104   -458       C  
ATOM   2396  O   ALA A 311     -17.611   5.163  -7.845  1.00 40.88           O  
ANISOU 2396  O   ALA A 311     5075   5728   4729    596   -132   -487       O  
ATOM   2397  CB  ALA A 311     -19.814   3.462  -9.600  1.00 32.79           C  
ANISOU 2397  CB  ALA A 311     4113   4548   3799    553    -48   -452       C  
ATOM   2398  N   GLU A 312     -19.002   3.935  -6.567  1.00 44.91           N  
ANISOU 2398  N   GLU A 312     5726   6132   5207    602    -78   -436       N  
ATOM   2399  CA  GLU A 312     -18.763   4.747  -5.379  1.00 40.95           C  
ANISOU 2399  CA  GLU A 312     5231   5667   4660    593    -89   -442       C  
ATOM   2400  C   GLU A 312     -17.292   4.711  -4.990  1.00 46.83           C  
ANISOU 2400  C   GLU A 312     5956   6485   5354    654   -153   -452       C  
ATOM   2401  O   GLU A 312     -16.655   5.758  -4.831  1.00 41.66           O  
ANISOU 2401  O   GLU A 312     5244   5897   4689    636   -180   -481       O  
ATOM   2402  CB  GLU A 312     -19.646   4.252  -4.232  1.00 48.01           C  
ANISOU 2402  CB  GLU A 312     6220   6502   5519    586    -50   -412       C  
ATOM   2403  CG  GLU A 312     -19.467   4.988  -2.916  1.00 46.17           C  
ANISOU 2403  CG  GLU A 312     6012   6300   5232    578    -56   -417       C  
ATOM   2404  CD  GLU A 312     -20.307   4.387  -1.804  1.00 62.10           C  
ANISOU 2404  CD  GLU A 312     8131   8255   7210    574    -14   -386       C  
ATOM   2405  OE1 GLU A 312     -20.167   3.173  -1.544  1.00 63.27           O  
ANISOU 2405  OE1 GLU A 312     8349   8367   7324    624    -20   -355       O  
ATOM   2406  OE2 GLU A 312     -21.109   5.125  -1.194  1.00 64.06           O1-
ANISOU 2406  OE2 GLU A 312     8392   8488   7459    522     29   -391       O1-
ATOM   2407  N   LYS A 313     -16.726   3.505  -4.886  1.00 48.37           N  
ANISOU 2407  N   LYS A 313     6193   6669   5517    728   -179   -430       N  
ATOM   2408  CA  LYS A 313     -15.322   3.348  -4.518  1.00 45.07           C  
ANISOU 2408  CA  LYS A 313     5752   6322   5050    797   -244   -437       C  
ATOM   2409  C   LYS A 313     -14.397   4.115  -5.455  1.00 48.29           C  
ANISOU 2409  C   LYS A 313     6050   6808   5490    788   -277   -477       C  
ATOM   2410  O   LYS A 313     -13.331   4.578  -5.032  1.00 53.25           O  
ANISOU 2410  O   LYS A 313     6633   7516   6084    812   -326   -497       O  
ATOM   2411  CB  LYS A 313     -14.963   1.861  -4.510  1.00 44.65           C  
ANISOU 2411  CB  LYS A 313     5760   6233   4970    882   -260   -405       C  
ATOM   2412  CG  LYS A 313     -13.524   1.543  -4.136  1.00 44.85           C  
ANISOU 2412  CG  LYS A 313     5763   6331   4946    968   -330   -408       C  
ATOM   2413  CD  LYS A 313     -13.271   0.039  -4.152  1.00 57.44           C  
ANISOU 2413  CD  LYS A 313     7429   7877   6517   1057   -339   -374       C  
ATOM   2414  CE  LYS A 313     -14.483  -0.740  -3.656  1.00 67.43           C  
ANISOU 2414  CE  LYS A 313     8814   9037   7771   1040   -284   -334       C  
ATOM   2415  NZ  LYS A 313     -14.144  -2.148  -3.307  1.00 72.18           N  
ANISOU 2415  NZ  LYS A 313     9506   9592   8328   1133   -298   -296       N  
ATOM   2416  N   PHE A 314     -14.785   4.262  -6.724  1.00 44.35           N  
ANISOU 2416  N   PHE A 314     5507   6289   5055    752   -249   -490       N  
ATOM   2417  CA  PHE A 314     -13.953   4.986  -7.679  1.00 39.25           C  
ANISOU 2417  CA  PHE A 314     4763   5710   4440    738   -272   -527       C  
ATOM   2418  C   PHE A 314     -13.792   6.447  -7.274  1.00 42.59           C  
ANISOU 2418  C   PHE A 314     5138   6188   4858    678   -278   -558       C  
ATOM   2419  O   PHE A 314     -12.679   6.987  -7.279  1.00 43.84           O  
ANISOU 2419  O   PHE A 314     5230   6427   4999    687   -319   -587       O  
ATOM   2420  CB  PHE A 314     -14.557   4.873  -9.080  1.00 40.51           C  
ANISOU 2420  CB  PHE A 314     4901   5828   4664    704   -238   -532       C  
ATOM   2421  CG  PHE A 314     -14.011   5.871 -10.061  1.00 37.07           C  
ANISOU 2421  CG  PHE A 314     4374   5449   4263    665   -246   -570       C  
ATOM   2422  CD1 PHE A 314     -12.764   5.690 -10.632  1.00 36.50           C  
ANISOU 2422  CD1 PHE A 314     4242   5439   4187    708   -281   -591       C  
ATOM   2423  CD2 PHE A 314     -14.751   6.986 -10.421  1.00 38.21           C  
ANISOU 2423  CD2 PHE A 314     4494   5582   4443    587   -215   -584       C  
ATOM   2424  CE1 PHE A 314     -12.260   6.604 -11.537  1.00 36.34           C  
ANISOU 2424  CE1 PHE A 314     4142   5468   4196    667   -283   -627       C  
ATOM   2425  CE2 PHE A 314     -14.252   7.904 -11.325  1.00 40.81           C  
ANISOU 2425  CE2 PHE A 314     4749   5957   4800    550   -220   -617       C  
ATOM   2426  CZ  PHE A 314     -13.005   7.712 -11.884  1.00 37.52           C  
ANISOU 2426  CZ  PHE A 314     4277   5602   4378    587   -252   -639       C  
ATOM   2427  N   PHE A 315     -14.897   7.105  -6.914  1.00 45.71           N  
ANISOU 2427  N   PHE A 315     5563   6540   5266    615   -236   -553       N  
ATOM   2428  CA  PHE A 315     -14.816   8.506  -6.511  1.00 39.79           C  
ANISOU 2428  CA  PHE A 315     4777   5831   4510    557   -235   -582       C  
ATOM   2429  C   PHE A 315     -14.216   8.662  -5.119  1.00 47.37           C  
ANISOU 2429  C   PHE A 315     5764   6834   5399    579   -269   -584       C  
ATOM   2430  O   PHE A 315     -13.589   9.686  -4.831  1.00 50.89           O  
ANISOU 2430  O   PHE A 315     6165   7342   5827    548   -290   -616       O  
ATOM   2431  CB  PHE A 315     -16.195   9.159  -6.577  1.00 38.70           C  
ANISOU 2431  CB  PHE A 315     4663   5632   4410    491   -177   -576       C  
ATOM   2432  CG  PHE A 315     -16.810   9.139  -7.948  1.00 39.60           C  
ANISOU 2432  CG  PHE A 315     4746   5709   4591    464   -149   -576       C  
ATOM   2433  CD1 PHE A 315     -16.492  10.112  -8.881  1.00 37.10           C  
ANISOU 2433  CD1 PHE A 315     4362   5426   4308    425   -151   -606       C  
ATOM   2434  CD2 PHE A 315     -17.710   8.149  -8.303  1.00 38.53           C  
ANISOU 2434  CD2 PHE A 315     4654   5505   4480    475   -120   -547       C  
ATOM   2435  CE1 PHE A 315     -17.057  10.096 -10.141  1.00 30.61           C  
ANISOU 2435  CE1 PHE A 315     3516   4571   3541    402   -128   -605       C  
ATOM   2436  CE2 PHE A 315     -18.277   8.125  -9.564  1.00 37.92           C  
ANISOU 2436  CE2 PHE A 315     4549   5398   4460    449    -99   -549       C  
ATOM   2437  CZ  PHE A 315     -17.952   9.101 -10.483  1.00 35.23           C  
ANISOU 2437  CZ  PHE A 315     4142   5093   4151    414   -105   -577       C  
ATOM   2438  N   VAL A 316     -14.401   7.675  -4.238  1.00 49.97           N  
ANISOU 2438  N   VAL A 316     6170   7132   5685    629   -274   -550       N  
ATOM   2439  CA  VAL A 316     -13.712   7.719  -2.950  1.00 51.62           C  
ANISOU 2439  CA  VAL A 316     6407   7388   5820    659   -317   -550       C  
ATOM   2440  C   VAL A 316     -12.206   7.660  -3.154  1.00 54.10           C  
ANISOU 2440  C   VAL A 316     6649   7794   6111    708   -384   -573       C  
ATOM   2441  O   VAL A 316     -11.441   8.259  -2.387  1.00 61.45           O  
ANISOU 2441  O   VAL A 316     7557   8795   6994    705   -426   -595       O  
ATOM   2442  CB  VAL A 316     -14.201   6.591  -2.020  1.00 45.35           C  
ANISOU 2442  CB  VAL A 316     5717   6535   4979    708   -308   -505       C  
ATOM   2443  CG1 VAL A 316     -13.756   6.863  -0.595  1.00 53.45           C  
ANISOU 2443  CG1 VAL A 316     6783   7600   5924    721   -342   -505       C  
ATOM   2444  CG2 VAL A 316     -15.710   6.489  -2.059  1.00 50.44           C  
ANISOU 2444  CG2 VAL A 316     6420   7087   5657    660   -235   -483       C  
ATOM   2445  N   SER A 317     -11.755   6.950  -4.190  1.00 44.47           N  
ANISOU 2445  N   SER A 317     5390   6579   4926    751   -396   -571       N  
ATOM   2446  CA  SER A 317     -10.328   6.830  -4.458  1.00 46.04           C  
ANISOU 2446  CA  SER A 317     5515   6868   5111    802   -455   -595       C  
ATOM   2447  C   SER A 317      -9.695   8.150  -4.881  1.00 43.59           C  
ANISOU 2447  C   SER A 317     5109   6633   4820    739   -466   -645       C  
ATOM   2448  O   SER A 317      -8.470   8.286  -4.798  1.00 49.22           O  
ANISOU 2448  O   SER A 317     5755   7436   5509    767   -519   -672       O  
ATOM   2449  CB  SER A 317     -10.086   5.767  -5.531  1.00 45.13           C  
ANISOU 2449  CB  SER A 317     5386   6730   5032    861   -454   -582       C  
ATOM   2450  OG  SER A 317     -10.338   6.281  -6.827  1.00 39.89           O  
ANISOU 2450  OG  SER A 317     4666   6057   4433    806   -419   -605       O  
ATOM   2451  N   VAL A 318     -10.487   9.121  -5.328  1.00 39.60           N  
ANISOU 2451  N   VAL A 318     4595   6095   4355    655   -418   -660       N  
ATOM   2452  CA  VAL A 318      -9.964  10.425  -5.715  1.00 44.27           C  
ANISOU 2452  CA  VAL A 318     5111   6748   4964    588   -420   -706       C  
ATOM   2453  C   VAL A 318     -10.311  11.494  -4.680  1.00 48.49           C  
ANISOU 2453  C   VAL A 318     5673   7286   5464    526   -411   -720       C  
ATOM   2454  O   VAL A 318     -10.285  12.684  -4.986  1.00 47.72           O  
ANISOU 2454  O   VAL A 318     5538   7209   5387    455   -393   -754       O  
ATOM   2455  CB  VAL A 318     -10.444  10.836  -7.118  1.00 43.45           C  
ANISOU 2455  CB  VAL A 318     4972   6609   4930    540   -376   -717       C  
ATOM   2456  CG1 VAL A 318      -9.804   9.962  -8.168  1.00 43.75           C  
ANISOU 2456  CG1 VAL A 318     4965   6663   4993    593   -391   -716       C  
ATOM   2457  CG2 VAL A 318     -11.955  10.766  -7.217  1.00 46.47           C  
ANISOU 2457  CG2 VAL A 318     5421   6892   5343    510   -319   -686       C  
ATOM   2458  N   GLY A 319     -10.631  11.088  -3.454  1.00 59.74           N  
ANISOU 2458  N   GLY A 319     7172   8691   6836    553   -420   -696       N  
ATOM   2459  CA  GLY A 319     -10.963  12.048  -2.422  1.00 61.56           C  
ANISOU 2459  CA  GLY A 319     7438   8924   7029    498   -409   -709       C  
ATOM   2460  C   GLY A 319     -12.336  12.666  -2.533  1.00 59.23           C  
ANISOU 2460  C   GLY A 319     7187   8546   6772    435   -338   -701       C  
ATOM   2461  O   GLY A 319     -12.553  13.760  -2.005  1.00 69.11           O  
ANISOU 2461  O   GLY A 319     8448   9802   8009    375   -319   -725       O  
ATOM   2462  N   LEU A 320     -13.274  12.004  -3.221  1.00 43.88           N  
ANISOU 2462  N   LEU A 320     5269   6527   4877    448   -296   -670       N  
ATOM   2463  CA  LEU A 320     -14.649  12.471  -3.255  1.00 39.75           C  
ANISOU 2463  CA  LEU A 320     4787   5926   4389    398   -230   -659       C  
ATOM   2464  C   LEU A 320     -15.501  11.664  -2.281  1.00 44.53           C  
ANISOU 2464  C   LEU A 320     5484   6472   4964    424   -207   -620       C  
ATOM   2465  O   LEU A 320     -15.249  10.474  -2.067  1.00 46.94           O  
ANISOU 2465  O   LEU A 320     5822   6770   5243    487   -231   -592       O  
ATOM   2466  CB  LEU A 320     -15.226  12.356  -4.669  1.00 39.27           C  
ANISOU 2466  CB  LEU A 320     4692   5824   4404    384   -198   -652       C  
ATOM   2467  CG  LEU A 320     -14.597  13.280  -5.715  1.00 39.13           C  
ANISOU 2467  CG  LEU A 320     4595   5851   4422    346   -207   -689       C  
ATOM   2468  CD1 LEU A 320     -15.139  12.979  -7.103  1.00 36.21           C  
ANISOU 2468  CD1 LEU A 320     4200   5439   4118    342   -182   -678       C  
ATOM   2469  CD2 LEU A 320     -14.824  14.740  -5.351  1.00 35.66           C  
ANISOU 2469  CD2 LEU A 320     4151   5416   3980    276   -182   -718       C  
ATOM   2470  N   PRO A 321     -16.513  12.279  -1.671  1.00 47.52           N  
ANISOU 2470  N   PRO A 321     5909   6804   5343    378   -156   -618       N  
ATOM   2471  CA  PRO A 321     -17.255  11.594  -0.608  1.00 57.48           C  
ANISOU 2471  CA  PRO A 321     7260   8013   6565    396   -130   -585       C  
ATOM   2472  C   PRO A 321     -18.033  10.398  -1.131  1.00 47.70           C  
ANISOU 2472  C   PRO A 321     6052   6708   5362    426   -101   -547       C  
ATOM   2473  O   PRO A 321     -18.455  10.359  -2.290  1.00 48.86           O  
ANISOU 2473  O   PRO A 321     6158   6832   5576    412    -81   -547       O  
ATOM   2474  CB  PRO A 321     -18.202  12.678  -0.081  1.00 55.14           C  
ANISOU 2474  CB  PRO A 321     6990   7684   6278    332    -72   -598       C  
ATOM   2475  CG  PRO A 321     -18.386  13.601  -1.236  1.00 41.80           C  
ANISOU 2475  CG  PRO A 321     5229   5996   4657    289    -54   -623       C  
ATOM   2476  CD  PRO A 321     -17.073  13.610  -1.968  1.00 38.66           C  
ANISOU 2476  CD  PRO A 321     4761   5669   4260    308   -114   -644       C  
ATOM   2477  N   ASN A 322     -18.215   9.411  -0.258  1.00 51.47           N  
ANISOU 2477  N   ASN A 322     6610   7156   5791    465   -100   -515       N  
ATOM   2478  CA  ASN A 322     -19.084   8.300  -0.604  1.00 54.08           C  
ANISOU 2478  CA  ASN A 322     6985   7414   6151    482    -63   -480       C  
ATOM   2479  C   ASN A 322     -20.534   8.774  -0.650  1.00 56.81           C  
ANISOU 2479  C   ASN A 322     7344   7698   6544    421     13   -478       C  
ATOM   2480  O   ASN A 322     -20.909   9.778  -0.037  1.00 60.94           O  
ANISOU 2480  O   ASN A 322     7871   8224   7058    378     40   -495       O  
ATOM   2481  CB  ASN A 322     -18.921   7.135   0.379  1.00 59.99           C  
ANISOU 2481  CB  ASN A 322     7825   8139   6831    538    -76   -445       C  
ATOM   2482  CG  ASN A 322     -18.896   7.574   1.840  1.00 80.73           C  
ANISOU 2482  CG  ASN A 322    10514  10778   9383    528    -75   -445       C  
ATOM   2483  OD1 ASN A 322     -19.322   8.676   2.188  1.00 74.89           O  
ANISOU 2483  OD1 ASN A 322     9762  10043   8649    471    -44   -468       O  
ATOM   2484  ND2 ASN A 322     -18.389   6.687   2.702  1.00 93.72           N  
ANISOU 2484  ND2 ASN A 322    12230  12423  10954    586   -108   -418       N  
ATOM   2485  N   MET A 323     -21.347   8.045  -1.410  1.00 56.06           N  
ANISOU 2485  N   MET A 323     7253   7548   6501    417     47   -458       N  
ATOM   2486  CA  MET A 323     -22.736   8.436  -1.604  1.00 53.14           C  
ANISOU 2486  CA  MET A 323     6881   7126   6185    362    115   -458       C  
ATOM   2487  C   MET A 323     -23.470   8.492  -0.271  1.00 59.19           C  
ANISOU 2487  C   MET A 323     7722   7856   6909    343    163   -446       C  
ATOM   2488  O   MET A 323     -23.228   7.680   0.626  1.00 61.59           O  
ANISOU 2488  O   MET A 323     8103   8147   7151    376    156   -423       O  
ATOM   2489  CB  MET A 323     -23.434   7.458  -2.548  1.00 54.60           C  
ANISOU 2489  CB  MET A 323     7064   7260   6423    363    137   -438       C  
ATOM   2490  CG  MET A 323     -22.815   7.376  -3.932  1.00 47.95           C  
ANISOU 2490  CG  MET A 323     6150   6445   5622    378     97   -450       C  
ATOM   2491  SD  MET A 323     -23.256   8.765  -4.995  1.00 45.93           S  
ANISOU 2491  SD  MET A 323     5803   6209   5440    324    110   -480       S  
ATOM   2492  CE  MET A 323     -21.787   9.781  -4.858  1.00 39.99           C  
ANISOU 2492  CE  MET A 323     5006   5539   4651    336     54   -512       C  
ATOM   2493  N   THR A 324     -24.364   9.469  -0.145  1.00 47.18           N  
ANISOU 2493  N   THR A 324     6183   6320   5423    291    214   -461       N  
ATOM   2494  CA  THR A 324     -25.134   9.631   1.077  1.00 46.35           C  
ANISOU 2494  CA  THR A 324     6146   6182   5284    267    270   -455       C  
ATOM   2495  C   THR A 324     -25.978   8.388   1.344  1.00 49.01           C  
ANISOU 2495  C   THR A 324     6547   6455   5618    271    315   -421       C  
ATOM   2496  O   THR A 324     -26.233   7.571   0.455  1.00 56.71           O  
ANISOU 2496  O   THR A 324     7505   7405   6636    279    314   -407       O  
ATOM   2497  CB  THR A 324     -26.038  10.861   0.985  1.00 42.74           C  
ANISOU 2497  CB  THR A 324     5648   5714   4877    216    323   -478       C  
ATOM   2498  OG1 THR A 324     -27.054  10.635  -0.001  1.00 35.31           O  
ANISOU 2498  OG1 THR A 324     4663   4737   4017    195    359   -471       O  
ATOM   2499  CG2 THR A 324     -25.228  12.090   0.596  1.00 43.48           C  
ANISOU 2499  CG2 THR A 324     5681   5863   4977    207    284   -512       C  
ATOM   2500  N   GLN A 325     -26.403   8.244   2.601  1.00 53.35           N  
ANISOU 2500  N   GLN A 325     7179   6977   6115    262    356   -410       N  
ATOM   2501  CA  GLN A 325     -27.289   7.140   2.949  1.00 59.20           C  
ANISOU 2501  CA  GLN A 325     7989   7653   6852    254    411   -379       C  
ATOM   2502  C   GLN A 325     -28.598   7.231   2.177  1.00 62.43           C  
ANISOU 2502  C   GLN A 325     8346   8024   7349    207    472   -384       C  
ATOM   2503  O   GLN A 325     -29.150   6.209   1.750  1.00 70.43           O  
ANISOU 2503  O   GLN A 325     9376   8994   8388    201    494   -364       O  
ATOM   2504  CB  GLN A 325     -27.546   7.128   4.456  1.00 64.56           C  
ANISOU 2504  CB  GLN A 325     8764   8310   7456    246    451   -369       C  
ATOM   2505  CG  GLN A 325     -28.588   6.115   4.900  1.00 65.86           C  
ANISOU 2505  CG  GLN A 325     9005   8404   7616    225    522   -341       C  
ATOM   2506  CD  GLN A 325     -29.472   6.643   6.011  1.00 90.95           C  
ANISOU 2506  CD  GLN A 325    12231  11555  10770    182    601   -348       C  
ATOM   2507  OE1 GLN A 325     -29.213   6.407   7.191  1.00 83.63           O  
ANISOU 2507  OE1 GLN A 325    11399  10618   9758    194    608   -334       O  
ATOM   2508  NE2 GLN A 325     -30.520   7.371   5.639  1.00 86.36           N  
ANISOU 2508  NE2 GLN A 325    11585  10963  10263    134    660   -368       N  
ATOM   2509  N   GLY A 326     -29.100   8.450   1.973  1.00 57.15           N  
ANISOU 2509  N   GLY A 326     7614   7372   6727    172    498   -411       N  
ATOM   2510  CA  GLY A 326     -30.293   8.642   1.170  1.00 59.87           C  
ANISOU 2510  CA  GLY A 326     7896   7692   7160    133    546   -417       C  
ATOM   2511  C   GLY A 326     -30.128   8.224  -0.276  1.00 57.67           C  
ANISOU 2511  C   GLY A 326     7552   7421   6938    143    504   -415       C  
ATOM   2512  O   GLY A 326     -31.125   7.931  -0.944  1.00 66.61           O  
ANISOU 2512  O   GLY A 326     8649   8525   8133    114    539   -413       O  
ATOM   2513  N   PHE A 327     -28.893   8.199  -0.781  1.00 47.60           N  
ANISOU 2513  N   PHE A 327     6258   6186   5641    181    431   -419       N  
ATOM   2514  CA  PHE A 327     -28.662   7.683  -2.126  1.00 49.51           C  
ANISOU 2514  CA  PHE A 327     6449   6433   5929    193    392   -417       C  
ATOM   2515  C   PHE A 327     -29.009   6.202  -2.204  1.00 48.35           C  
ANISOU 2515  C   PHE A 327     6358   6238   5776    200    409   -390       C  
ATOM   2516  O   PHE A 327     -29.673   5.757  -3.145  1.00 47.39           O  
ANISOU 2516  O   PHE A 327     6202   6093   5712    178    422   -388       O  
ATOM   2517  CB  PHE A 327     -27.207   7.924  -2.538  1.00 44.12           C  
ANISOU 2517  CB  PHE A 327     5740   5805   5219    234    316   -428       C  
ATOM   2518  CG  PHE A 327     -26.830   7.297  -3.855  1.00 43.70           C  
ANISOU 2518  CG  PHE A 327     5646   5757   5202    252    277   -426       C  
ATOM   2519  CD1 PHE A 327     -27.001   7.993  -5.041  1.00 40.33           C  
ANISOU 2519  CD1 PHE A 327     5137   5349   4837    232    266   -444       C  
ATOM   2520  CD2 PHE A 327     -26.294   6.018  -3.907  1.00 44.24           C  
ANISOU 2520  CD2 PHE A 327     5763   5809   5238    292    253   -405       C  
ATOM   2521  CE1 PHE A 327     -26.652   7.423  -6.252  1.00 38.73           C  
ANISOU 2521  CE1 PHE A 327     4902   5150   4663    246    232   -443       C  
ATOM   2522  CE2 PHE A 327     -25.945   5.444  -5.115  1.00 41.56           C  
ANISOU 2522  CE2 PHE A 327     5389   5472   4929    309    221   -405       C  
ATOM   2523  CZ  PHE A 327     -26.124   6.148  -6.289  1.00 43.96           C  
ANISOU 2523  CZ  PHE A 327     5613   5797   5295    284    211   -425       C  
ATOM   2524  N   TRP A 328     -28.572   5.422  -1.218  1.00 52.99           N  
ANISOU 2524  N   TRP A 328     7034   6807   6292    228    407   -369       N  
ATOM   2525  CA  TRP A 328     -28.801   3.983  -1.267  1.00 51.05           C  
ANISOU 2525  CA  TRP A 328     6854   6509   6034    238    422   -342       C  
ATOM   2526  C   TRP A 328     -30.242   3.622  -0.927  1.00 51.70           C  
ANISOU 2526  C   TRP A 328     6965   6535   6144    182    505   -334       C  
ATOM   2527  O   TRP A 328     -30.828   2.738  -1.563  1.00 55.16           O  
ANISOU 2527  O   TRP A 328     7409   6934   6617    162    526   -325       O  
ATOM   2528  CB  TRP A 328     -27.822   3.275  -0.334  1.00 54.34           C  
ANISOU 2528  CB  TRP A 328     7362   6923   6361    294    390   -320       C  
ATOM   2529  CG  TRP A 328     -26.411   3.508  -0.749  1.00 52.19           C  
ANISOU 2529  CG  TRP A 328     7052   6711   6067    349    309   -330       C  
ATOM   2530  CD1 TRP A 328     -25.477   4.266  -0.106  1.00 55.92           C  
ANISOU 2530  CD1 TRP A 328     7518   7239   6491    376    266   -342       C  
ATOM   2531  CD2 TRP A 328     -25.777   3.004  -1.929  1.00 54.36           C  
ANISOU 2531  CD2 TRP A 328     7285   6998   6370    381    262   -332       C  
ATOM   2532  NE1 TRP A 328     -24.295   4.253  -0.806  1.00 55.89           N  
ANISOU 2532  NE1 TRP A 328     7466   7285   6485    422    196   -352       N  
ATOM   2533  CE2 TRP A 328     -24.454   3.485  -1.930  1.00 54.54           C  
ANISOU 2533  CE2 TRP A 328     7273   7087   6361    427    194   -345       C  
ATOM   2534  CE3 TRP A 328     -26.199   2.186  -2.982  1.00 54.86           C  
ANISOU 2534  CE3 TRP A 328     7337   7025   6482    372    273   -326       C  
ATOM   2535  CZ2 TRP A 328     -23.549   3.177  -2.942  1.00 48.82           C  
ANISOU 2535  CZ2 TRP A 328     6504   6394   5653    467    141   -353       C  
ATOM   2536  CZ3 TRP A 328     -25.300   1.880  -3.984  1.00 47.10           C  
ANISOU 2536  CZ3 TRP A 328     6316   6069   5512    412    219   -333       C  
ATOM   2537  CH2 TRP A 328     -23.990   2.373  -3.957  1.00 48.21           C  
ANISOU 2537  CH2 TRP A 328     6421   6275   5621    460    156   -346       C  
ATOM   2538  N   GLU A 329     -30.829   4.291   0.067  1.00 54.02           N  
ANISOU 2538  N   GLU A 329     7278   6826   6423    154    555   -340       N  
ATOM   2539  CA  GLU A 329     -32.195   3.967   0.463  1.00 60.06           C  
ANISOU 2539  CA  GLU A 329     8068   7541   7214    100    640   -334       C  
ATOM   2540  C   GLU A 329     -33.202   4.386  -0.600  1.00 57.16           C  
ANISOU 2540  C   GLU A 329     7600   7177   6941     55    664   -353       C  
ATOM   2541  O   GLU A 329     -34.160   3.654  -0.877  1.00 60.02           O  
ANISOU 2541  O   GLU A 329     7965   7500   7339     15    710   -347       O  
ATOM   2542  CB  GLU A 329     -32.532   4.637   1.795  1.00 64.84           C  
ANISOU 2542  CB  GLU A 329     8716   8144   7777     84    690   -338       C  
ATOM   2543  CG  GLU A 329     -31.788   4.077   2.990  1.00 69.79           C  
ANISOU 2543  CG  GLU A 329     9458   8757   8303    119    680   -315       C  
ATOM   2544  CD  GLU A 329     -31.837   5.009   4.182  1.00 73.58           C  
ANISOU 2544  CD  GLU A 329     9968   9251   8737    110    709   -326       C  
ATOM   2545  OE1 GLU A 329     -32.076   6.219   3.979  1.00 66.25           O  
ANISOU 2545  OE1 GLU A 329     8964   8356   7850     91    716   -354       O  
ATOM   2546  OE2 GLU A 329     -31.639   4.536   5.321  1.00 83.53           O1-
ANISOU 2546  OE2 GLU A 329    11333  10488   9917    121    726   -307       O1-
ATOM   2547  N   ASN A 330     -33.005   5.554  -1.209  1.00 52.86           N  
ANISOU 2547  N   ASN A 330     6968   6680   6437     60    632   -376       N  
ATOM   2548  CA  ASN A 330     -34.058   6.181  -1.994  1.00 51.44           C  
ANISOU 2548  CA  ASN A 330     6696   6506   6342     20    660   -393       C  
ATOM   2549  C   ASN A 330     -33.870   6.069  -3.503  1.00 50.86           C  
ANISOU 2549  C   ASN A 330     6551   6452   6322     25    607   -400       C  
ATOM   2550  O   ASN A 330     -34.833   6.299  -4.241  1.00 49.16           O  
ANISOU 2550  O   ASN A 330     6267   6236   6176     -9    627   -409       O  
ATOM   2551  CB  ASN A 330     -34.184   7.660  -1.612  1.00 46.50           C  
ANISOU 2551  CB  ASN A 330     6027   5912   5729     17    673   -414       C  
ATOM   2552  CG  ASN A 330     -34.372   7.866  -0.123  1.00 52.14           C  
ANISOU 2552  CG  ASN A 330     6814   6610   6388     10    727   -412       C  
ATOM   2553  OD1 ASN A 330     -35.193   7.202   0.508  1.00 53.86           O  
ANISOU 2553  OD1 ASN A 330     7078   6788   6600    -19    791   -401       O  
ATOM   2554  ND2 ASN A 330     -33.611   8.794   0.446  1.00 51.38           N  
ANISOU 2554  ND2 ASN A 330     6729   6544   6250     32    704   -424       N  
ATOM   2555  N   SER A 331     -32.676   5.730  -3.984  1.00 61.78           N  
ANISOU 2555  N   SER A 331     7946   7853   7674     67    540   -395       N  
ATOM   2556  CA  SER A 331     -32.495   5.584  -5.421  1.00 58.01           C  
ANISOU 2556  CA  SER A 331     7408   7391   7244     70    495   -402       C  
ATOM   2557  C   SER A 331     -33.164   4.304  -5.915  1.00 57.17           C  
ANISOU 2557  C   SER A 331     7324   7240   7159     44    517   -390       C  
ATOM   2558  O   SER A 331     -33.620   3.462  -5.136  1.00 64.78           O  
ANISOU 2558  O   SER A 331     8357   8160   8096     27    563   -375       O  
ATOM   2559  CB  SER A 331     -31.013   5.555  -5.793  1.00 52.94           C  
ANISOU 2559  CB  SER A 331     6770   6781   6562    122    423   -402       C  
ATOM   2560  OG  SER A 331     -30.358   6.753  -5.419  1.00 52.83           O  
ANISOU 2560  OG  SER A 331     6732   6812   6530    139    401   -417       O  
ATOM   2561  N   MET A 332     -33.218   4.165  -7.239  1.00 44.23           N  
ANISOU 2561  N   MET A 332     5629   5611   5566     36    483   -398       N  
ATOM   2562  CA  MET A 332     -33.653   2.930  -7.882  1.00 42.28           C  
ANISOU 2562  CA  MET A 332     5404   5325   5336     12    492   -391       C  
ATOM   2563  C   MET A 332     -32.545   2.490  -8.828  1.00 44.57           C  
ANISOU 2563  C   MET A 332     5696   5628   5611     53    428   -391       C  
ATOM   2564  O   MET A 332     -32.321   3.119  -9.868  1.00 49.50           O  
ANISOU 2564  O   MET A 332     6250   6288   6270     56    388   -406       O  
ATOM   2565  CB  MET A 332     -34.976   3.114  -8.623  1.00 45.30           C  
ANISOU 2565  CB  MET A 332     5714   5706   5792    -45    519   -403       C  
ATOM   2566  CG  MET A 332     -35.760   1.817  -8.748  1.00 59.59           C  
ANISOU 2566  CG  MET A 332     7564   7465   7611    -90    557   -397       C  
ATOM   2567  SD  MET A 332     -37.261   1.938  -9.736  1.00 72.44           S  
ANISOU 2567  SD  MET A 332     9097   9100   9325   -159    578   -415       S  
ATOM   2568  CE  MET A 332     -36.661   2.757 -11.197  1.00 43.31           C  
ANISOU 2568  CE  MET A 332     5325   5462   5668   -131    498   -429       C  
ATOM   2569  N   LEU A 333     -31.849   1.416  -8.461  1.00 43.66           N  
ANISOU 2569  N   LEU A 333     5664   5482   5443     86    421   -375       N  
ATOM   2570  CA  LEU A 333     -30.734   0.911  -9.247  1.00 38.50           C  
ANISOU 2570  CA  LEU A 333     5020   4838   4770    132    366   -375       C  
ATOM   2571  C   LEU A 333     -31.083  -0.336 -10.047  1.00 50.52           C  
ANISOU 2571  C   LEU A 333     6575   6314   6308    112    374   -371       C  
ATOM   2572  O   LEU A 333     -30.308  -0.723 -10.925  1.00 55.91           O  
ANISOU 2572  O   LEU A 333     7254   7004   6986    143    332   -376       O  
ATOM   2573  CB  LEU A 333     -29.537   0.620  -8.334  1.00 41.95           C  
ANISOU 2573  CB  LEU A 333     5524   5280   5134    197    342   -360       C  
ATOM   2574  CG  LEU A 333     -29.189   1.745  -7.357  1.00 43.11           C  
ANISOU 2574  CG  LEU A 333     5656   5469   5255    212    337   -364       C  
ATOM   2575  CD1 LEU A 333     -28.041   1.341  -6.444  1.00 31.73           C  
ANISOU 2575  CD1 LEU A 333     4284   4034   3738    275    310   -348       C  
ATOM   2576  CD2 LEU A 333     -28.862   3.029  -8.105  1.00 33.72           C  
ANISOU 2576  CD2 LEU A 333     4370   4339   4102    209    301   -388       C  
ATOM   2577  N   THR A 334     -32.221  -0.966  -9.774  1.00 60.75           N  
ANISOU 2577  N   THR A 334     7901   7560   7619     58    429   -366       N  
ATOM   2578  CA  THR A 334     -32.698  -2.095 -10.553  1.00 56.15           C  
ANISOU 2578  CA  THR A 334     7347   6932   7055     24    442   -367       C  
ATOM   2579  C   THR A 334     -34.068  -1.772 -11.131  1.00 67.19           C  
ANISOU 2579  C   THR A 334     8673   8335   8520    -52    470   -384       C  
ATOM   2580  O   THR A 334     -34.765  -0.867 -10.666  1.00 69.91           O  
ANISOU 2580  O   THR A 334     8966   8705   8892    -78    495   -389       O  
ATOM   2581  CB  THR A 334     -32.794  -3.375  -9.709  1.00 63.94           C  
ANISOU 2581  CB  THR A 334     8451   7848   7994     24    486   -344       C  
ATOM   2582  OG1 THR A 334     -33.555  -3.113  -8.523  1.00 68.92           O  
ANISOU 2582  OG1 THR A 334     9104   8466   8616     -8    542   -335       O  
ATOM   2583  CG2 THR A 334     -31.416  -3.868  -9.321  1.00 46.68           C  
ANISOU 2583  CG2 THR A 334     6338   5656   5743    108    450   -327       C  
ATOM   2584  N   ASP A 335     -34.443  -2.518 -12.157  1.00 62.50           N  
ANISOU 2584  N   ASP A 335     8077   7719   7952    -87    466   -393       N  
ATOM   2585  CA  ASP A 335     -35.803  -2.443 -12.664  1.00 67.71           C  
ANISOU 2585  CA  ASP A 335     8675   8379   8671   -164    493   -409       C  
ATOM   2586  C   ASP A 335     -36.730  -3.130 -11.672  1.00 71.27           C  
ANISOU 2586  C   ASP A 335     9184   8781   9116   -215    567   -400       C  
ATOM   2587  O   ASP A 335     -36.516  -4.307 -11.353  1.00 66.81           O  
ANISOU 2587  O   ASP A 335     8718   8156   8510   -215    591   -387       O  
ATOM   2588  CB  ASP A 335     -35.903  -3.103 -14.038  1.00 68.92           C  
ANISOU 2588  CB  ASP A 335     8816   8522   8847   -191    465   -424       C  
ATOM   2589  CG  ASP A 335     -37.162  -2.705 -14.792  1.00 68.42           C  
ANISOU 2589  CG  ASP A 335     8662   8485   8850   -261    469   -445       C  
ATOM   2590  OD1 ASP A 335     -38.230  -2.570 -14.159  1.00 69.39           O  
ANISOU 2590  OD1 ASP A 335     8762   8604   8999   -310    519   -446       O  
ATOM   2591  OD2 ASP A 335     -37.083  -2.531 -16.026  1.00 74.63           O1-
ANISOU 2591  OD2 ASP A 335     9399   9297   9661   -267    423   -459       O1-
ATOM   2592  N   PRO A 336     -37.750  -2.446 -11.148  1.00 66.09           N  
ANISOU 2592  N   PRO A 336     8472   8144   8495   -256    608   -406       N  
ATOM   2593  CA  PRO A 336     -38.724  -3.136 -10.289  1.00 68.55           C  
ANISOU 2593  CA  PRO A 336     8833   8409   8804   -315    685   -401       C  
ATOM   2594  C   PRO A 336     -39.464  -4.244 -11.013  1.00 79.13           C  
ANISOU 2594  C   PRO A 336    10189   9710  10167   -384    706   -413       C  
ATOM   2595  O   PRO A 336     -39.977  -5.159 -10.357  1.00 81.37           O  
ANISOU 2595  O   PRO A 336    10547   9937  10431   -429    768   -406       O  
ATOM   2596  CB  PRO A 336     -39.672  -2.010  -9.850  1.00 68.63           C  
ANISOU 2596  CB  PRO A 336     8754   8462   8861   -343    717   -412       C  
ATOM   2597  CG  PRO A 336     -39.496  -0.936 -10.873  1.00 63.94           C  
ANISOU 2597  CG  PRO A 336     8055   7930   8310   -319    654   -427       C  
ATOM   2598  CD  PRO A 336     -38.072  -1.022 -11.330  1.00 58.88           C  
ANISOU 2598  CD  PRO A 336     7452   7294   7627   -252    589   -419       C  
ATOM   2599  N   GLY A 337     -39.537  -4.185 -12.342  1.00 91.21           N  
ANISOU 2599  N   GLY A 337    11655  11266  11736   -398    657   -432       N  
ATOM   2600  CA  GLY A 337     -40.075  -5.240 -13.173  1.00 94.05           C  
ANISOU 2600  CA  GLY A 337    12032  11592  12112   -461    664   -446       C  
ATOM   2601  C   GLY A 337     -41.522  -5.545 -12.846  1.00107.10           C  
ANISOU 2601  C   GLY A 337    13659  13232  13804   -554    731   -459       C  
ATOM   2602  O   GLY A 337     -42.293  -4.679 -12.416  1.00107.95           O  
ANISOU 2602  O   GLY A 337    13686  13380  13950   -573    755   -465       O  
ATOM   2603  N   ASN A 338     -41.886  -6.816 -13.037  1.00120.76           N  
ANISOU 2603  N   ASN A 338    15458  14903  15522   -613    764   -465       N  
ATOM   2604  CA  ASN A 338     -43.228  -7.324 -12.772  1.00125.35           C  
ANISOU 2604  CA  ASN A 338    16026  15465  16136   -713    832   -480       C  
ATOM   2605  C   ASN A 338     -44.307  -6.382 -13.293  1.00122.80           C  
ANISOU 2605  C   ASN A 338    15552  15217  15889   -757    821   -506       C  
ATOM   2606  O   ASN A 338     -44.364  -6.096 -14.494  1.00116.14           O  
ANISOU 2606  O   ASN A 338    14634  14414  15079   -761    760   -523       O  
ATOM   2607  CB  ASN A 338     -43.415  -7.567 -11.271  1.00130.39           C  
ANISOU 2607  CB  ASN A 338    16742  16060  16739   -720    912   -461       C  
ATOM   2608  CG  ASN A 338     -42.494  -8.650 -10.738  1.00132.25           C  
ANISOU 2608  CG  ASN A 338    17136  16215  16898   -683    928   -434       C  
ATOM   2609  OD1 ASN A 338     -42.126  -9.579 -11.458  1.00121.10           O  
ANISOU 2609  OD1 ASN A 338    15785  14760  15468   -689    908   -438       O  
ATOM   2610  ND2 ASN A 338     -42.119  -8.535  -9.469  1.00120.20           N  
ANISOU 2610  ND2 ASN A 338    15681  14665  15324   -642    964   -408       N  
ATOM   2611  N   VAL A 339     -45.159  -5.891 -12.398  1.00117.85           N  
ANISOU 2611  N   VAL A 339    14881  14608  15289   -787    879   -508       N  
ATOM   2612  CA  VAL A 339     -46.224  -4.971 -12.784  1.00114.74           C  
ANISOU 2612  CA  VAL A 339    14341  14286  14970   -821    874   -530       C  
ATOM   2613  C   VAL A 339     -45.741  -3.528 -12.774  1.00104.04           C  
ANISOU 2613  C   VAL A 339    12914  12989  13627   -738    826   -521       C  
ATOM   2614  O   VAL A 339     -45.977  -2.777 -13.726  1.00101.82           O  
ANISOU 2614  O   VAL A 339    12529  12765  13391   -728    769   -534       O  
ATOM   2615  CB  VAL A 339     -47.445  -5.159 -11.858  1.00124.86           C  
ANISOU 2615  CB  VAL A 339    15604  15559  16278   -896    967   -540       C  
ATOM   2616  CG1 VAL A 339     -48.522  -4.137 -12.187  1.00118.26           C  
ANISOU 2616  CG1 VAL A 339    14610  14802  15521   -919    961   -563       C  
ATOM   2617  CG2 VAL A 339     -47.988  -6.573 -11.978  1.00124.54           C  
ANISOU 2617  CG2 VAL A 339    15630  15462  16229   -990   1014   -553       C  
ATOM   2618  N   GLN A 340     -45.059  -3.122 -11.701  1.00 87.88           N  
ANISOU 2618  N   GLN A 340    10925  10926  11537   -679    848   -499       N  
ATOM   2619  CA  GLN A 340     -44.632  -1.739 -11.522  1.00 86.48           C  
ANISOU 2619  CA  GLN A 340    10691  10800  11369   -608    815   -492       C  
ATOM   2620  C   GLN A 340     -43.721  -1.283 -12.655  1.00 80.05           C  
ANISOU 2620  C   GLN A 340     9848  10016  10552   -552    723   -491       C  
ATOM   2621  O   GLN A 340     -42.589  -1.761 -12.785  1.00 80.27           O  
ANISOU 2621  O   GLN A 340     9957  10015  10528   -509    690   -478       O  
ATOM   2622  CB  GLN A 340     -43.927  -1.576 -10.174  1.00 76.52           C  
ANISOU 2622  CB  GLN A 340     9516   9508  10048   -559    851   -469       C  
ATOM   2623  CG  GLN A 340     -43.562  -0.142  -9.830  1.00 72.00           C  
ANISOU 2623  CG  GLN A 340     8891   8983   9482   -495    829   -466       C  
ATOM   2624  CD  GLN A 340     -42.513  -0.054  -8.739  1.00 73.38           C  
ANISOU 2624  CD  GLN A 340     9164   9132   9585   -438    838   -443       C  
ATOM   2625  OE1 GLN A 340     -42.244  -1.032  -8.041  1.00 83.90           O  
ANISOU 2625  OE1 GLN A 340    10603  10411  10865   -447    874   -428       O  
ATOM   2626  NE2 GLN A 340     -41.915   1.122  -8.585  1.00 61.19           N  
ANISOU 2626  NE2 GLN A 340     7587   7626   8036   -378    805   -441       N  
ATOM   2627  N   LYS A 341     -44.207  -0.353 -13.471  1.00 90.36           N  
ANISOU 2627  N   LYS A 341    11039  11380  11913   -549    682   -505       N  
ATOM   2628  CA  LYS A 341     -43.461   0.147 -14.615  1.00 84.80           C  
ANISOU 2628  CA  LYS A 341    10304  10707  11210   -504    599   -506       C  
ATOM   2629  C   LYS A 341     -42.597   1.335 -14.213  1.00 80.71           C  
ANISOU 2629  C   LYS A 341     9780  10214  10672   -426    575   -493       C  
ATOM   2630  O   LYS A 341     -42.913   2.069 -13.273  1.00 76.00           O  
ANISOU 2630  O   LYS A 341     9165   9628  10085   -413    616   -490       O  
ATOM   2631  CB  LYS A 341     -44.413   0.551 -15.742  1.00 86.58           C  
ANISOU 2631  CB  LYS A 341    10416  10982  11500   -540    563   -526       C  
ATOM   2632  CG  LYS A 341     -45.174  -0.612 -16.359  1.00 99.10           C  
ANISOU 2632  CG  LYS A 341    12001  12549  13102   -621    572   -543       C  
ATOM   2633  CD  LYS A 341     -46.524  -0.166 -16.901  1.00104.87           C  
ANISOU 2633  CD  LYS A 341    12607  13333  13904   -669    568   -564       C  
ATOM   2634  CE  LYS A 341     -47.255  -1.316 -17.576  1.00 97.74           C  
ANISOU 2634  CE  LYS A 341    11702  12418  13017   -757    571   -586       C  
ATOM   2635  NZ  LYS A 341     -48.731  -1.114 -17.579  1.00 86.85           N  
ANISOU 2635  NZ  LYS A 341    10212  11082  11705   -819    599   -607       N  
ATOM   2636  N   ALA A 342     -41.496   1.518 -14.939  1.00 65.36           N  
ANISOU 2636  N   ALA A 342     7854   8278   8701   -378    511   -488       N  
ATOM   2637  CA  ALA A 342     -40.570   2.604 -14.657  1.00 57.18           C  
ANISOU 2637  CA  ALA A 342     6815   7266   7643   -310    484   -479       C  
ATOM   2638  C   ALA A 342     -39.947   3.091 -15.956  1.00 56.05           C  
ANISOU 2638  C   ALA A 342     6636   7156   7507   -281    410   -484       C  
ATOM   2639  O   ALA A 342     -39.851   2.345 -16.934  1.00 56.79           O  
ANISOU 2639  O   ALA A 342     6738   7240   7598   -301    378   -490       O  
ATOM   2640  CB  ALA A 342     -39.475   2.167 -13.677  1.00 56.09           C  
ANISOU 2640  CB  ALA A 342     6779   7094   7437   -270    500   -463       C  
ATOM   2641  N   VAL A 343     -39.523   4.351 -15.952  1.00 62.93           N  
ANISOU 2641  N   VAL A 343     7468   8060   8381   -236    385   -481       N  
ATOM   2642  CA  VAL A 343     -38.808   4.940 -17.078  1.00 61.42           C  
ANISOU 2642  CA  VAL A 343     7250   7898   8188   -205    320   -484       C  
ATOM   2643  C   VAL A 343     -37.327   4.636 -16.879  1.00 58.67           C  
ANISOU 2643  C   VAL A 343     6976   7536   7780   -160    300   -477       C  
ATOM   2644  O   VAL A 343     -36.698   5.145 -15.948  1.00 60.74           O  
ANISOU 2644  O   VAL A 343     7264   7800   8012   -125    314   -471       O  
ATOM   2645  CB  VAL A 343     -39.066   6.447 -17.185  1.00 56.72           C  
ANISOU 2645  CB  VAL A 343     6584   7340   7625   -180    307   -485       C  
ATOM   2646  CG1 VAL A 343     -38.125   7.078 -18.199  1.00 55.61           C  
ANISOU 2646  CG1 VAL A 343     6435   7224   7470   -146    245   -486       C  
ATOM   2647  CG2 VAL A 343     -40.518   6.709 -17.560  1.00 59.64           C  
ANISOU 2647  CG2 VAL A 343     6872   7729   8058   -216    316   -493       C  
ATOM   2648  N   CYS A 344     -36.769   3.810 -17.760  1.00 61.86           N  
ANISOU 2648  N   CYS A 344     7410   7929   8164   -162    267   -481       N  
ATOM   2649  CA  CYS A 344     -35.459   3.208 -17.550  1.00 62.22           C  
ANISOU 2649  CA  CYS A 344     7529   7957   8154   -122    254   -475       C  
ATOM   2650  C   CYS A 344     -34.308   4.045 -18.092  1.00 60.88           C  
ANISOU 2650  C   CYS A 344     7343   7822   7966    -75    207   -478       C  
ATOM   2651  O   CYS A 344     -33.168   3.570 -18.096  1.00 62.98           O  
ANISOU 2651  O   CYS A 344     7658   8082   8190    -39    190   -477       O  
ATOM   2652  CB  CYS A 344     -35.421   1.811 -18.173  1.00 62.07           C  
ANISOU 2652  CB  CYS A 344     7560   7901   8122   -145    251   -479       C  
ATOM   2653  SG  CYS A 344     -36.122   0.520 -17.122  1.00 95.25           S  
ANISOU 2653  SG  CYS A 344    11833  12045  12312   -183    316   -470       S  
ATOM   2654  N   HIS A 345     -34.570   5.261 -18.553  1.00 70.68           N  
ANISOU 2654  N   HIS A 345     8519   9099   9238    -74    187   -483       N  
ATOM   2655  CA  HIS A 345     -33.495   6.137 -19.000  1.00 69.97           C  
ANISOU 2655  CA  HIS A 345     8416   9040   9129    -36    149   -487       C  
ATOM   2656  C   HIS A 345     -32.586   6.460 -17.818  1.00 62.46           C  
ANISOU 2656  C   HIS A 345     7501   8094   8138      2    164   -482       C  
ATOM   2657  O   HIS A 345     -33.067   6.993 -16.806  1.00 59.92           O  
ANISOU 2657  O   HIS A 345     7174   7771   7823     -1    198   -478       O  
ATOM   2658  CB  HIS A 345     -34.070   7.420 -19.600  1.00 74.06           C  
ANISOU 2658  CB  HIS A 345     8865   9588   9687    -44    132   -490       C  
ATOM   2659  CG  HIS A 345     -33.038   8.349 -20.164  1.00 81.80           C  
ANISOU 2659  CG  HIS A 345     9835  10597  10649    -14     97   -495       C  
ATOM   2660  ND1 HIS A 345     -31.731   7.971 -20.381  1.00 77.04           N  
ANISOU 2660  ND1 HIS A 345     9268  10000  10004     12     76   -500       N  
ATOM   2661  CD2 HIS A 345     -33.124   9.643 -20.555  1.00 85.02           C  
ANISOU 2661  CD2 HIS A 345    10201  11028  11075     -7     82   -496       C  
ATOM   2662  CE1 HIS A 345     -31.056   8.991 -20.881  1.00 78.13           C  
ANISOU 2662  CE1 HIS A 345     9385  10166  10135     27     52   -506       C  
ATOM   2663  NE2 HIS A 345     -31.879  10.018 -20.997  1.00 89.87           N  
ANISOU 2663  NE2 HIS A 345    10830  11661  11657     16     55   -503       N  
ATOM   2664  N   PRO A 346     -31.292   6.148 -17.889  1.00 43.27           N  
ANISOU 2664  N   PRO A 346     5105   5671   5665     37    141   -484       N  
ATOM   2665  CA  PRO A 346     -30.395   6.457 -16.764  1.00 44.01           C  
ANISOU 2665  CA  PRO A 346     5228   5775   5717     73    148   -482       C  
ATOM   2666  C   PRO A 346     -30.309   7.956 -16.523  1.00 42.67           C  
ANISOU 2666  C   PRO A 346     5017   5638   5558     77    146   -488       C  
ATOM   2667  O   PRO A 346     -29.969   8.731 -17.420  1.00 45.73           O  
ANISOU 2667  O   PRO A 346     5367   6052   5957     78    117   -497       O  
ATOM   2668  CB  PRO A 346     -29.050   5.873 -17.211  1.00 43.14           C  
ANISOU 2668  CB  PRO A 346     5146   5676   5569    110    115   -487       C  
ATOM   2669  CG  PRO A 346     -29.395   4.852 -18.242  1.00 43.94           C  
ANISOU 2669  CG  PRO A 346     5258   5752   5685     92    107   -488       C  
ATOM   2670  CD  PRO A 346     -30.618   5.362 -18.936  1.00 46.74           C  
ANISOU 2670  CD  PRO A 346     5562   6107   6090     46    110   -491       C  
ATOM   2671  N   THR A 347     -30.624   8.362 -15.295  1.00 50.56           N  
ANISOU 2671  N   THR A 347     6029   6632   6549     78    180   -483       N  
ATOM   2672  CA  THR A 347     -30.627   9.767 -14.918  1.00 47.13           C  
ANISOU 2672  CA  THR A 347     5564   6220   6121     79    186   -491       C  
ATOM   2673  C   THR A 347     -30.120   9.915 -13.493  1.00 44.38           C  
ANISOU 2673  C   THR A 347     5259   5874   5730     97    207   -489       C  
ATOM   2674  O   THR A 347     -30.378   9.060 -12.641  1.00 44.01           O  
ANISOU 2674  O   THR A 347     5257   5802   5663     98    234   -478       O  
ATOM   2675  CB  THR A 347     -32.030  10.380 -15.028  1.00 45.93           C  
ANISOU 2675  CB  THR A 347     5370   6057   6024     51    214   -488       C  
ATOM   2676  OG1 THR A 347     -33.011   9.406 -14.648  1.00 52.46           O  
ANISOU 2676  OG1 THR A 347     6212   6854   6866     28    248   -479       O  
ATOM   2677  CG2 THR A 347     -32.304  10.842 -16.452  1.00 51.66           C  
ANISOU 2677  CG2 THR A 347     6044   6796   6786     41    181   -493       C  
ATOM   2678  N   ALA A 348     -29.399  11.002 -13.245  1.00 36.17           N  
ANISOU 2678  N   ALA A 348     4207   4863   4671    109    195   -501       N  
ATOM   2679  CA  ALA A 348     -28.947  11.359 -11.908  1.00 28.94           C  
ANISOU 2679  CA  ALA A 348     3327   3955   3713    121    212   -504       C  
ATOM   2680  C   ALA A 348     -29.828  12.491 -11.397  1.00 37.24           C  
ANISOU 2680  C   ALA A 348     4361   4999   4792    102    250   -509       C  
ATOM   2681  O   ALA A 348     -29.946  13.533 -12.052  1.00 32.24           O  
ANISOU 2681  O   ALA A 348     3687   4376   4186     94    242   -518       O  
ATOM   2682  CB  ALA A 348     -27.477  11.770 -11.917  1.00 29.69           C  
ANISOU 2682  CB  ALA A 348     3424   4091   3766    144    172   -519       C  
ATOM   2683  N   TRP A 349     -30.443  12.287 -10.238  1.00 45.33           N  
ANISOU 2683  N   TRP A 349     5419   6000   5804     95    295   -502       N  
ATOM   2684  CA  TRP A 349     -31.441  13.204  -9.708  1.00 42.51           C  
ANISOU 2684  CA  TRP A 349     5047   5630   5476     78    342   -506       C  
ATOM   2685  C   TRP A 349     -30.864  13.984  -8.536  1.00 42.74           C  
ANISOU 2685  C   TRP A 349     5112   5669   5459     85    356   -518       C  
ATOM   2686  O   TRP A 349     -30.371  13.392  -7.571  1.00 46.59           O  
ANISOU 2686  O   TRP A 349     5652   6156   5893     95    360   -514       O  
ATOM   2687  CB  TRP A 349     -32.699  12.449  -9.272  1.00 46.49           C  
ANISOU 2687  CB  TRP A 349     5559   6100   6006     59    391   -494       C  
ATOM   2688  CG  TRP A 349     -33.457  11.846 -10.413  1.00 48.11           C  
ANISOU 2688  CG  TRP A 349     5721   6296   6263     43    380   -487       C  
ATOM   2689  CD1 TRP A 349     -33.032  10.852 -11.246  1.00 49.98           C  
ANISOU 2689  CD1 TRP A 349     5962   6532   6495     46    343   -481       C  
ATOM   2690  CD2 TRP A 349     -34.775  12.199 -10.851  1.00 50.88           C  
ANISOU 2690  CD2 TRP A 349     6016   6638   6678     22    407   -487       C  
ATOM   2691  NE1 TRP A 349     -34.002  10.564 -12.174  1.00 54.77           N  
ANISOU 2691  NE1 TRP A 349     6524   7131   7156     23    343   -478       N  
ATOM   2692  CE2 TRP A 349     -35.083  11.377 -11.953  1.00 56.76           C  
ANISOU 2692  CE2 TRP A 349     6734   7381   7451      9    379   -482       C  
ATOM   2693  CE3 TRP A 349     -35.724  13.129 -10.417  1.00 50.67           C  
ANISOU 2693  CE3 TRP A 349     5958   6607   6687     16    450   -492       C  
ATOM   2694  CZ2 TRP A 349     -36.299  11.458 -12.627  1.00 53.25           C  
ANISOU 2694  CZ2 TRP A 349     6230   6935   7068    -13    389   -482       C  
ATOM   2695  CZ3 TRP A 349     -36.931  13.208 -11.088  1.00 57.56           C  
ANISOU 2695  CZ3 TRP A 349     6768   7478   7623      0    462   -491       C  
ATOM   2696  CH2 TRP A 349     -37.208  12.377 -12.180  1.00 52.67           C  
ANISOU 2696  CH2 TRP A 349     6121   6862   7031    -15    429   -486       C  
ATOM   2697  N   ASP A 350     -30.929  15.310  -8.628  1.00 43.95           N  
ANISOU 2697  N   ASP A 350     5240   5831   5629     80    364   -533       N  
ATOM   2698  CA  ASP A 350     -30.579  16.211  -7.534  1.00 44.70           C  
ANISOU 2698  CA  ASP A 350     5369   5931   5686     78    387   -548       C  
ATOM   2699  C   ASP A 350     -31.862  16.946  -7.156  1.00 51.16           C  
ANISOU 2699  C   ASP A 350     6172   6720   6545     66    446   -550       C  
ATOM   2700  O   ASP A 350     -32.140  18.037  -7.658  1.00 57.73           O  
ANISOU 2700  O   ASP A 350     6973   7551   7412     65    452   -559       O  
ATOM   2701  CB  ASP A 350     -29.462  17.178  -7.933  1.00 53.53           C  
ANISOU 2701  CB  ASP A 350     6476   7081   6783     80    348   -567       C  
ATOM   2702  CG  ASP A 350     -29.149  18.191  -6.846  1.00 57.15           C  
ANISOU 2702  CG  ASP A 350     6968   7542   7202     71    373   -587       C  
ATOM   2703  OD1 ASP A 350     -29.435  17.911  -5.662  1.00 62.24           O  
ANISOU 2703  OD1 ASP A 350     7658   8174   7816     69    407   -585       O  
ATOM   2704  OD2 ASP A 350     -28.616  19.271  -7.177  1.00 60.07           O1-
ANISOU 2704  OD2 ASP A 350     7327   7927   7571     62    360   -606       O1-
ATOM   2705  N   LEU A 351     -32.647  16.333  -6.269  1.00 41.28           N  
ANISOU 2705  N   LEU A 351     4949   5446   5291     59    494   -541       N  
ATOM   2706  CA  LEU A 351     -33.899  16.927  -5.817  1.00 44.38           C  
ANISOU 2706  CA  LEU A 351     5326   5812   5723     50    559   -544       C  
ATOM   2707  C   LEU A 351     -33.685  18.129  -4.911  1.00 40.38           C  
ANISOU 2707  C   LEU A 351     4852   5303   5188     50    590   -564       C  
ATOM   2708  O   LEU A 351     -34.644  18.865  -4.652  1.00 48.11           O  
ANISOU 2708  O   LEU A 351     5814   6261   6204     48    642   -570       O  
ATOM   2709  CB  LEU A 351     -34.744  15.887  -5.074  1.00 42.80           C  
ANISOU 2709  CB  LEU A 351     5151   5588   5522     36    607   -531       C  
ATOM   2710  CG  LEU A 351     -35.106  14.573  -5.768  1.00 45.10           C  
ANISOU 2710  CG  LEU A 351     5424   5873   5838     28    591   -513       C  
ATOM   2711  CD1 LEU A 351     -33.994  13.556  -5.621  1.00 38.82           C  
ANISOU 2711  CD1 LEU A 351     4682   5085   4982     39    549   -503       C  
ATOM   2712  CD2 LEU A 351     -36.398  14.022  -5.194  1.00 46.24           C  
ANISOU 2712  CD2 LEU A 351     5568   5990   6010      5    659   -506       C  
ATOM   2713  N   GLY A 352     -32.465  18.349  -4.434  1.00 39.10           N  
ANISOU 2713  N   GLY A 352     4733   5162   4963     52    559   -575       N  
ATOM   2714  CA  GLY A 352     -32.226  19.332  -3.401  1.00 38.59           C  
ANISOU 2714  CA  GLY A 352     4711   5093   4858     44    590   -596       C  
ATOM   2715  C   GLY A 352     -32.405  18.737  -2.022  1.00 39.96           C  
ANISOU 2715  C   GLY A 352     4948   5253   4980     38    631   -592       C  
ATOM   2716  O   GLY A 352     -32.749  17.564  -1.843  1.00 38.45           O  
ANISOU 2716  O   GLY A 352     4771   5053   4787     39    639   -572       O  
ATOM   2717  N   LYS A 353     -32.152  19.578  -1.018  1.00 44.48           N  
ANISOU 2717  N   LYS A 353     5568   5824   5510     29    658   -613       N  
ATOM   2718  CA  LYS A 353     -32.258  19.188   0.388  1.00 41.11           C  
ANISOU 2718  CA  LYS A 353     5213   5384   5023     21    699   -613       C  
ATOM   2719  C   LYS A 353     -31.360  17.996   0.713  1.00 34.46           C  
ANISOU 2719  C   LYS A 353     4412   4563   4118     31    650   -597       C  
ATOM   2720  O   LYS A 353     -31.686  17.176   1.574  1.00 40.06           O  
ANISOU 2720  O   LYS A 353     5174   5254   4793     29    681   -582       O  
ATOM   2721  CB  LYS A 353     -33.708  18.883   0.777  1.00 39.26           C  
ANISOU 2721  CB  LYS A 353     4975   5111   4830     14    778   -603       C  
ATOM   2722  CG  LYS A 353     -34.683  20.028   0.539  1.00 38.22           C  
ANISOU 2722  CG  LYS A 353     4802   4958   4762     13    831   -618       C  
ATOM   2723  CD  LYS A 353     -34.089  21.365   0.946  1.00 46.88           C  
ANISOU 2723  CD  LYS A 353     5928   6057   5827     10    833   -646       C  
ATOM   2724  CE  LYS A 353     -35.166  22.333   1.406  1.00 52.30           C  
ANISOU 2724  CE  LYS A 353     6614   6709   6550      9    916   -662       C  
ATOM   2725  NZ  LYS A 353     -34.797  23.002   2.686  1.00 48.16           N  
ANISOU 2725  NZ  LYS A 353     6169   6175   5956     -6    952   -687       N  
ATOM   2726  N   GLY A 354     -30.228  17.887   0.020  1.00 48.97           N  
ANISOU 2726  N   GLY A 354     6228   6438   5941     43    576   -598       N  
ATOM   2727  CA  GLY A 354     -29.312  16.788   0.246  1.00 48.30           C  
ANISOU 2727  CA  GLY A 354     6176   6377   5800     61    524   -584       C  
ATOM   2728  C   GLY A 354     -29.761  15.455  -0.304  1.00 48.30           C  
ANISOU 2728  C   GLY A 354     6165   6359   5829     74    520   -554       C  
ATOM   2729  O   GLY A 354     -29.120  14.438  -0.023  1.00 47.87           O  
ANISOU 2729  O   GLY A 354     6148   6313   5726     94    487   -538       O  
ATOM   2730  N   ASP A 355     -30.843  15.425  -1.080  1.00 51.01           N  
ANISOU 2730  N   ASP A 355     6458   6675   6247     64    553   -547       N  
ATOM   2731  CA  ASP A 355     -31.378  14.182  -1.632  1.00 52.00           C  
ANISOU 2731  CA  ASP A 355     6573   6781   6405     67    554   -522       C  
ATOM   2732  C   ASP A 355     -30.792  13.985  -3.024  1.00 53.50           C  
ANISOU 2732  C   ASP A 355     6706   6995   6627     81    491   -521       C  
ATOM   2733  O   ASP A 355     -31.213  14.631  -3.987  1.00 56.27           O  
ANISOU 2733  O   ASP A 355     6995   7348   7038     73    489   -528       O  
ATOM   2734  CB  ASP A 355     -32.902  14.221  -1.666  1.00 49.60           C  
ANISOU 2734  CB  ASP A 355     6242   6441   6162     44    624   -518       C  
ATOM   2735  CG  ASP A 355     -33.515  12.887  -2.055  1.00 53.22           C  
ANISOU 2735  CG  ASP A 355     6699   6875   6645     37    634   -496       C  
ATOM   2736  OD1 ASP A 355     -32.763  11.905  -2.226  1.00 55.54           O  
ANISOU 2736  OD1 ASP A 355     7025   7175   6905     53    591   -482       O  
ATOM   2737  OD2 ASP A 355     -34.755  12.822  -2.188  1.00 47.68           O1-
ANISOU 2737  OD2 ASP A 355     5966   6151   5999     14    686   -494       O1-
ATOM   2738  N   PHE A 356     -29.819  13.087  -3.132  1.00 49.42           N  
ANISOU 2738  N   PHE A 356     6214   6495   6068    104    441   -510       N  
ATOM   2739  CA  PHE A 356     -29.203  12.735  -4.403  1.00 39.82           C  
ANISOU 2739  CA  PHE A 356     4952   5300   4876    119    384   -508       C  
ATOM   2740  C   PHE A 356     -29.563  11.298  -4.748  1.00 44.34           C  
ANISOU 2740  C   PHE A 356     5542   5845   5459    126    386   -485       C  
ATOM   2741  O   PHE A 356     -29.331  10.386  -3.947  1.00 50.46           O  
ANISOU 2741  O   PHE A 356     6382   6605   6184    141    390   -469       O  
ATOM   2742  CB  PHE A 356     -27.684  12.906  -4.345  1.00 38.92           C  
ANISOU 2742  CB  PHE A 356     4845   5233   4709    144    323   -520       C  
ATOM   2743  CG  PHE A 356     -27.248  14.263  -3.876  1.00 46.61           C  
ANISOU 2743  CG  PHE A 356     5813   6233   5662    131    323   -546       C  
ATOM   2744  CD1 PHE A 356     -27.315  15.356  -4.724  1.00 46.25           C  
ANISOU 2744  CD1 PHE A 356     5712   6198   5662    114    320   -564       C  
ATOM   2745  CD2 PHE A 356     -26.775  14.447  -2.588  1.00 47.49           C  
ANISOU 2745  CD2 PHE A 356     5981   6358   5708    134    327   -553       C  
ATOM   2746  CE1 PHE A 356     -26.915  16.607  -4.296  1.00 40.62           C  
ANISOU 2746  CE1 PHE A 356     5001   5503   4929     98    324   -589       C  
ATOM   2747  CE2 PHE A 356     -26.375  15.696  -2.154  1.00 40.33           C  
ANISOU 2747  CE2 PHE A 356     5072   5473   4780    115    328   -580       C  
ATOM   2748  CZ  PHE A 356     -26.446  16.777  -3.009  1.00 43.45           C  
ANISOU 2748  CZ  PHE A 356     5414   5875   5222     96    329   -599       C  
ATOM   2749  N   ARG A 357     -30.130  11.101  -5.935  1.00 34.36           N  
ANISOU 2749  N   ARG A 357     4227   4572   4257    114    381   -482       N  
ATOM   2750  CA  ARG A 357     -30.581   9.791  -6.374  1.00 37.22           C  
ANISOU 2750  CA  ARG A 357     4602   4904   4635    112    386   -464       C  
ATOM   2751  C   ARG A 357     -30.101   9.520  -7.789  1.00 39.88           C  
ANISOU 2751  C   ARG A 357     4894   5258   4999    122    335   -466       C  
ATOM   2752  O   ARG A 357     -29.861  10.443  -8.572  1.00 38.37           O  
ANISOU 2752  O   ARG A 357     4649   5095   4836    120    310   -481       O  
ATOM   2753  CB  ARG A 357     -32.109   9.673  -6.336  1.00 35.70           C  
ANISOU 2753  CB  ARG A 357     4394   4677   4494     74    446   -459       C  
ATOM   2754  CG  ARG A 357     -32.756  10.327  -5.139  1.00 42.03           C  
ANISOU 2754  CG  ARG A 357     5217   5466   5286     59    505   -463       C  
ATOM   2755  CD  ARG A 357     -33.836   9.448  -4.557  1.00 44.20           C  
ANISOU 2755  CD  ARG A 357     5527   5700   5569     31    567   -450       C  
ATOM   2756  NE  ARG A 357     -34.615  10.149  -3.545  1.00 45.07           N  
ANISOU 2756  NE  ARG A 357     5646   5798   5680     12    632   -457       N  
ATOM   2757  CZ  ARG A 357     -35.931  10.059  -3.419  1.00 45.04           C  
ANISOU 2757  CZ  ARG A 357     5618   5771   5724    -21    694   -458       C  
ATOM   2758  NH1 ARG A 357     -36.651   9.303  -4.228  1.00 43.29           N  
ANISOU 2758  NH1 ARG A 357     5361   5537   5551    -44    699   -452       N  
ATOM   2759  NH2 ARG A 357     -36.539  10.740  -2.452  1.00 52.22           N  
ANISOU 2759  NH2 ARG A 357     6539   6672   6630    -33    755   -467       N  
ATOM   2760  N   ILE A 358     -29.969   8.236  -8.108  1.00 45.44           N  
ANISOU 2760  N   ILE A 358     5629   5942   5694    132    323   -452       N  
ATOM   2761  CA  ILE A 358     -29.707   7.779  -9.464  1.00 44.50           C  
ANISOU 2761  CA  ILE A 358     5476   5828   5603    136    286   -454       C  
ATOM   2762  C   ILE A 358     -30.841   6.852  -9.870  1.00 48.35           C  
ANISOU 2762  C   ILE A 358     5968   6274   6128    105    317   -443       C  
ATOM   2763  O   ILE A 358     -31.153   5.891  -9.157  1.00 56.33           O  
ANISOU 2763  O   ILE A 358     7040   7249   7116    101    348   -428       O  
ATOM   2764  CB  ILE A 358     -28.347   7.067  -9.584  1.00 43.83           C  
ANISOU 2764  CB  ILE A 358     5423   5760   5470    181    238   -451       C  
ATOM   2765  CG1 ILE A 358     -27.235   8.091  -9.806  1.00 44.69           C  
ANISOU 2765  CG1 ILE A 358     5494   5923   5564    201    196   -470       C  
ATOM   2766  CG2 ILE A 358     -28.369   6.058 -10.723  1.00 36.77           C  
ANISOU 2766  CG2 ILE A 358     4525   4847   4597    183    221   -446       C  
ATOM   2767  CD1 ILE A 358     -25.893   7.471 -10.109  1.00 38.80           C  
ANISOU 2767  CD1 ILE A 358     4759   5203   4780    246    148   -471       C  
ATOM   2768  N   LEU A 359     -31.462   7.152 -11.001  1.00 43.85           N  
ANISOU 2768  N   LEU A 359     5337   5709   5614     80    308   -451       N  
ATOM   2769  CA  LEU A 359     -32.492   6.306 -11.584  1.00 44.41           C  
ANISOU 2769  CA  LEU A 359     5400   5749   5724     45    329   -446       C  
ATOM   2770  C   LEU A 359     -31.869   5.550 -12.751  1.00 45.94           C  
ANISOU 2770  C   LEU A 359     5596   5944   5917     57    284   -448       C  
ATOM   2771  O   LEU A 359     -31.486   6.152 -13.757  1.00 46.69           O  
ANISOU 2771  O   LEU A 359     5642   6068   6029     63    246   -459       O  
ATOM   2772  CB  LEU A 359     -33.689   7.147 -12.021  1.00 48.44           C  
ANISOU 2772  CB  LEU A 359     5839   6268   6297     10    348   -455       C  
ATOM   2773  CG  LEU A 359     -35.061   6.478 -12.006  1.00 43.06           C  
ANISOU 2773  CG  LEU A 359     5148   5556   5655    -36    392   -451       C  
ATOM   2774  CD1 LEU A 359     -36.104   7.463 -12.436  1.00 45.23           C  
ANISOU 2774  CD1 LEU A 359     5343   5851   5991    -58    402   -460       C  
ATOM   2775  CD2 LEU A 359     -35.062   5.314 -12.970  1.00 46.33           C  
ANISOU 2775  CD2 LEU A 359     5576   5953   6075    -52    369   -450       C  
ATOM   2776  N   MET A 360     -31.776   4.229 -12.614  1.00 36.15           N  
ANISOU 2776  N   MET A 360     4417   4667   4652     59    294   -437       N  
ATOM   2777  CA  MET A 360     -31.197   3.403 -13.664  1.00 42.99           C  
ANISOU 2777  CA  MET A 360     5294   5526   5512     72    258   -440       C  
ATOM   2778  C   MET A 360     -31.700   1.978 -13.509  1.00 46.85           C  
ANISOU 2778  C   MET A 360     5847   5960   5992     52    289   -429       C  
ATOM   2779  O   MET A 360     -31.684   1.430 -12.403  1.00 47.99           O  
ANISOU 2779  O   MET A 360     6058   6075   6101     62    320   -414       O  
ATOM   2780  CB  MET A 360     -29.665   3.440 -13.610  1.00 45.07           C  
ANISOU 2780  CB  MET A 360     5579   5817   5730    131    217   -441       C  
ATOM   2781  CG  MET A 360     -28.990   2.858 -14.840  1.00 56.49           C  
ANISOU 2781  CG  MET A 360     7021   7266   7175    148    180   -449       C  
ATOM   2782  SD  MET A 360     -27.188   2.909 -14.764  1.00 64.39           S  
ANISOU 2782  SD  MET A 360     8034   8306   8125    218    135   -453       S  
ATOM   2783  CE  MET A 360     -26.922   4.349 -13.733  1.00 42.09           C  
ANISOU 2783  CE  MET A 360     5178   5527   5288    224    135   -458       C  
ATOM   2784  N   CYS A 361     -32.155   1.389 -14.616  1.00 48.37           N  
ANISOU 2784  N   CYS A 361     6026   6137   6215     21    280   -436       N  
ATOM   2785  CA  CYS A 361     -32.482  -0.035 -14.659  1.00 50.65           C  
ANISOU 2785  CA  CYS A 361     6382   6371   6493      1    305   -430       C  
ATOM   2786  C   CYS A 361     -31.202  -0.777 -15.027  1.00 52.51           C  
ANISOU 2786  C   CYS A 361     6670   6597   6686     56    272   -427       C  
ATOM   2787  O   CYS A 361     -30.958  -1.141 -16.179  1.00 51.09           O  
ANISOU 2787  O   CYS A 361     6480   6417   6517     54    245   -438       O  
ATOM   2788  CB  CYS A 361     -33.608  -0.305 -15.648  1.00 53.05           C  
ANISOU 2788  CB  CYS A 361     6645   6663   6847    -63    312   -442       C  
ATOM   2789  SG  CYS A 361     -35.095   0.686 -15.377  1.00 57.37           S  
ANISOU 2789  SG  CYS A 361     7110   7235   7454   -119    344   -449       S  
ATOM   2790  N   THR A 362     -30.361  -0.988 -14.018  1.00 51.29           N  
ANISOU 2790  N   THR A 362     6571   6435   6480    108    273   -412       N  
ATOM   2791  CA  THR A 362     -29.021  -1.512 -14.242  1.00 50.75           C  
ANISOU 2791  CA  THR A 362     6541   6372   6371    174    237   -409       C  
ATOM   2792  C   THR A 362     -29.082  -3.000 -14.556  1.00 51.04           C  
ANISOU 2792  C   THR A 362     6656   6343   6392    175    254   -402       C  
ATOM   2793  O   THR A 362     -29.603  -3.792 -13.763  1.00 56.18           O  
ANISOU 2793  O   THR A 362     7380   6941   7024    160    296   -386       O  
ATOM   2794  CB  THR A 362     -28.135  -1.269 -13.023  1.00 47.85           C  
ANISOU 2794  CB  THR A 362     6207   6023   5953    232    229   -395       C  
ATOM   2795  OG1 THR A 362     -28.377   0.045 -12.504  1.00 42.69           O  
ANISOU 2795  OG1 THR A 362     5495   5413   5313    216    231   -401       O  
ATOM   2796  CG2 THR A 362     -26.667  -1.400 -13.392  1.00 53.42           C  
ANISOU 2796  CG2 THR A 362     6912   6759   6627    303    181   -400       C  
ATOM   2797  N   LYS A 363     -28.554  -3.372 -15.713  1.00 53.77           N  
ANISOU 2797  N   LYS A 363     6994   6693   6745    189    225   -416       N  
ATOM   2798  CA  LYS A 363     -28.250  -4.759 -16.013  1.00 53.76           C  
ANISOU 2798  CA  LYS A 363     7076   6633   6718    210    234   -411       C  
ATOM   2799  C   LYS A 363     -26.801  -5.037 -15.635  1.00 50.70           C  
ANISOU 2799  C   LYS A 363     6724   6258   6281    303    206   -401       C  
ATOM   2800  O   LYS A 363     -25.989  -4.121 -15.483  1.00 49.16           O  
ANISOU 2800  O   LYS A 363     6474   6126   6079    342    171   -406       O  
ATOM   2801  CB  LYS A 363     -28.482  -5.061 -17.495  1.00 58.00           C  
ANISOU 2801  CB  LYS A 363     7588   7164   7286    175    221   -433       C  
ATOM   2802  CG  LYS A 363     -29.639  -4.297 -18.122  1.00 55.42           C  
ANISOU 2802  CG  LYS A 363     7182   6861   7012     97    223   -449       C  
ATOM   2803  CD  LYS A 363     -30.976  -4.738 -17.548  1.00 59.57           C  
ANISOU 2803  CD  LYS A 363     7734   7342   7555     29    273   -442       C  
ATOM   2804  CE  LYS A 363     -32.037  -3.665 -17.736  1.00 64.64           C  
ANISOU 2804  CE  LYS A 363     8284   8027   8250    -29    274   -452       C  
ATOM   2805  NZ  LYS A 363     -33.414  -4.232 -17.751  1.00 75.47           N  
ANISOU 2805  NZ  LYS A 363     9664   9362   9651   -109    315   -456       N  
ATOM   2806  N   VAL A 364     -26.472  -6.318 -15.491  1.00 53.23           N  
ANISOU 2806  N   VAL A 364     7138   6518   6567    339    220   -388       N  
ATOM   2807  CA  VAL A 364     -25.106  -6.672 -15.132  1.00 51.06           C  
ANISOU 2807  CA  VAL A 364     6899   6255   6247    436    192   -378       C  
ATOM   2808  C   VAL A 364     -24.296  -6.718 -16.419  1.00 46.79           C  
ANISOU 2808  C   VAL A 364     6319   5741   5719    465    159   -402       C  
ATOM   2809  O   VAL A 364     -24.060  -7.790 -16.987  1.00 57.15           O  
ANISOU 2809  O   VAL A 364     7692   7004   7020    487    168   -404       O  
ATOM   2810  CB  VAL A 364     -25.049  -8.013 -14.379  1.00 59.85           C  
ANISOU 2810  CB  VAL A 364     8138   7289   7315    472    221   -351       C  
ATOM   2811  CG1 VAL A 364     -23.660  -8.239 -13.800  1.00 54.16           C  
ANISOU 2811  CG1 VAL A 364     7446   6590   6544    581    186   -337       C  
ATOM   2812  CG2 VAL A 364     -26.107  -8.048 -13.287  1.00 57.22           C  
ANISOU 2812  CG2 VAL A 364     7848   6918   6974    420    266   -331       C  
ATOM   2813  N   THR A 365     -23.867  -5.543 -16.883  1.00 44.32           N  
ANISOU 2813  N   THR A 365     5908   5504   5427    463    125   -421       N  
ATOM   2814  CA  THR A 365     -23.172  -5.390 -18.153  1.00 47.15           C  
ANISOU 2814  CA  THR A 365     6218   5897   5801    479     98   -446       C  
ATOM   2815  C   THR A 365     -22.109  -4.312 -18.017  1.00 49.32           C  
ANISOU 2815  C   THR A 365     6416   6256   6069    522     59   -456       C  
ATOM   2816  O   THR A 365     -22.190  -3.433 -17.155  1.00 52.13           O  
ANISOU 2816  O   THR A 365     6738   6647   6420    514     53   -449       O  
ATOM   2817  CB  THR A 365     -24.112  -5.002 -19.313  1.00 48.39           C  
ANISOU 2817  CB  THR A 365     6328   6054   6005    396    104   -466       C  
ATOM   2818  OG1 THR A 365     -24.368  -3.592 -19.272  1.00 50.57           O  
ANISOU 2818  OG1 THR A 365     6517   6391   6307    362     88   -474       O  
ATOM   2819  CG2 THR A 365     -25.433  -5.760 -19.260  1.00 45.78           C  
ANISOU 2819  CG2 THR A 365     6053   5654   5689    330    144   -458       C  
ATOM   2820  N   MET A 366     -21.113  -4.381 -18.903  1.00 50.25           N  
ANISOU 2820  N   MET A 366     6505   6404   6184    563     36   -475       N  
ATOM   2821  CA  MET A 366     -20.078  -3.353 -18.934  1.00 47.56           C  
ANISOU 2821  CA  MET A 366     6085   6147   5841    594      2   -491       C  
ATOM   2822  C   MET A 366     -20.664  -1.991 -19.287  1.00 45.06           C  
ANISOU 2822  C   MET A 366     5690   5871   5558    523     -3   -504       C  
ATOM   2823  O   MET A 366     -20.201  -0.959 -18.785  1.00 45.19           O  
ANISOU 2823  O   MET A 366     5654   5947   5570    530    -22   -509       O  
ATOM   2824  CB  MET A 366     -18.987  -3.745 -19.930  1.00 47.10           C  
ANISOU 2824  CB  MET A 366     6010   6109   5777    643    -14   -512       C  
ATOM   2825  CG  MET A 366     -17.828  -2.768 -20.005  1.00 42.73           C  
ANISOU 2825  CG  MET A 366     5373   5643   5219    674    -46   -532       C  
ATOM   2826  SD  MET A 366     -16.503  -3.362 -21.072  1.00 47.45           S  
ANISOU 2826  SD  MET A 366     5955   6265   5809    740    -56   -557       S  
ATOM   2827  CE  MET A 366     -15.786  -1.812 -21.609  1.00 48.64           C  
ANISOU 2827  CE  MET A 366     5992   6513   5976    712    -79   -588       C  
ATOM   2828  N   ASP A 367     -21.682  -1.968 -20.151  1.00 50.61           N  
ANISOU 2828  N   ASP A 367     6390   6545   6295    457     12   -510       N  
ATOM   2829  CA  ASP A 367     -22.288  -0.704 -20.560  1.00 49.76           C  
ANISOU 2829  CA  ASP A 367     6213   6473   6221    396      6   -521       C  
ATOM   2830  C   ASP A 367     -22.899   0.026 -19.369  1.00 51.73           C  
ANISOU 2830  C   ASP A 367     6451   6731   6473    375     16   -505       C  
ATOM   2831  O   ASP A 367     -22.637   1.216 -19.154  1.00 50.02           O  
ANISOU 2831  O   ASP A 367     6178   6565   6261    368      2   -513       O  
ATOM   2832  CB  ASP A 367     -23.346  -0.956 -21.635  1.00 54.59           C  
ANISOU 2832  CB  ASP A 367     6829   7049   6866    333     18   -527       C  
ATOM   2833  CG  ASP A 367     -22.740  -1.191 -23.005  1.00 63.23           C  
ANISOU 2833  CG  ASP A 367     7912   8152   7960    340      4   -549       C  
ATOM   2834  OD1 ASP A 367     -21.594  -0.751 -23.235  1.00 54.09           O  
ANISOU 2834  OD1 ASP A 367     6719   7044   6788    380    -15   -563       O  
ATOM   2835  OD2 ASP A 367     -23.412  -1.816 -23.853  1.00 61.99           O1-
ANISOU 2835  OD2 ASP A 367     7781   7955   7815    302     13   -555       O1-
ATOM   2836  N   ASP A 368     -23.719  -0.673 -18.581  1.00 57.15           N  
ANISOU 2836  N   ASP A 368     7196   7365   7155    362     44   -485       N  
ATOM   2837  CA  ASP A 368     -24.319  -0.054 -17.404  1.00 55.83           C  
ANISOU 2837  CA  ASP A 368     7025   7201   6987    342     60   -471       C  
ATOM   2838  C   ASP A 368     -23.273   0.262 -16.344  1.00 53.47           C  
ANISOU 2838  C   ASP A 368     6729   6940   6646    400     42   -466       C  
ATOM   2839  O   ASP A 368     -23.423   1.237 -15.598  1.00 55.12           O  
ANISOU 2839  O   ASP A 368     6909   7178   6855    386     44   -465       O  
ATOM   2840  CB  ASP A 368     -25.405  -0.961 -16.827  1.00 56.97           C  
ANISOU 2840  CB  ASP A 368     7235   7278   7132    313    100   -452       C  
ATOM   2841  CG  ASP A 368     -26.614  -1.072 -17.734  1.00 56.35           C  
ANISOU 2841  CG  ASP A 368     7139   7173   7099    243    117   -460       C  
ATOM   2842  OD1 ASP A 368     -26.512  -0.674 -18.914  1.00 60.67           O  
ANISOU 2842  OD1 ASP A 368     7638   7745   7670    227     94   -478       O  
ATOM   2843  OD2 ASP A 368     -27.666  -1.556 -17.267  1.00 62.41           O1-
ANISOU 2843  OD2 ASP A 368     7941   7896   7877    202    153   -449       O1-
ATOM   2844  N   PHE A 369     -22.218  -0.552 -16.259  1.00 45.43           N  
ANISOU 2844  N   PHE A 369     5746   5921   5592    466     25   -463       N  
ATOM   2845  CA  PHE A 369     -21.137  -0.279 -15.318  1.00 41.40           C  
ANISOU 2845  CA  PHE A 369     5232   5457   5042    525      0   -460       C  
ATOM   2846  C   PHE A 369     -20.488   1.069 -15.608  1.00 39.27           C  
ANISOU 2846  C   PHE A 369     4876   5263   4782    516    -27   -484       C  
ATOM   2847  O   PHE A 369     -20.219   1.849 -14.687  1.00 36.34           O  
ANISOU 2847  O   PHE A 369     4486   4929   4392    520    -37   -484       O  
ATOM   2848  CB  PHE A 369     -20.109  -1.411 -15.378  1.00 41.18           C  
ANISOU 2848  CB  PHE A 369     5249   5419   4980    604    -17   -455       C  
ATOM   2849  CG  PHE A 369     -18.851  -1.142 -14.602  1.00 39.48           C  
ANISOU 2849  CG  PHE A 369     5014   5263   4724    671    -53   -456       C  
ATOM   2850  CD1 PHE A 369     -18.782  -1.431 -13.250  1.00 43.13           C  
ANISOU 2850  CD1 PHE A 369     5532   5715   5143    705    -55   -432       C  
ATOM   2851  CD2 PHE A 369     -17.729  -0.627 -15.231  1.00 37.53           C  
ANISOU 2851  CD2 PHE A 369     4696   5084   4480    698    -85   -482       C  
ATOM   2852  CE1 PHE A 369     -17.623  -1.196 -12.536  1.00 48.86           C  
ANISOU 2852  CE1 PHE A 369     6237   6499   5827    768    -94   -434       C  
ATOM   2853  CE2 PHE A 369     -16.569  -0.387 -14.522  1.00 38.48           C  
ANISOU 2853  CE2 PHE A 369     4791   5266   4563    757   -121   -486       C  
ATOM   2854  CZ  PHE A 369     -16.515  -0.674 -13.174  1.00 42.82           C  
ANISOU 2854  CZ  PHE A 369     5392   5807   5069    793   -129   -462       C  
ATOM   2855  N   LEU A 370     -20.228   1.358 -16.884  1.00 50.12           N  
ANISOU 2855  N   LEU A 370     6202   6659   6184    500    -38   -505       N  
ATOM   2856  CA  LEU A 370     -19.721   2.674 -17.259  1.00 47.99           C  
ANISOU 2856  CA  LEU A 370     5856   6454   5926    479    -57   -528       C  
ATOM   2857  C   LEU A 370     -20.755   3.761 -16.995  1.00 47.70           C  
ANISOU 2857  C   LEU A 370     5795   6414   5916    416    -40   -526       C  
ATOM   2858  O   LEU A 370     -20.412   4.852 -16.525  1.00 44.49           O  
ANISOU 2858  O   LEU A 370     5350   6052   5503    407    -49   -536       O  
ATOM   2859  CB  LEU A 370     -19.310   2.675 -18.730  1.00 47.17           C  
ANISOU 2859  CB  LEU A 370     5715   6364   5842    472    -66   -550       C  
ATOM   2860  CG  LEU A 370     -18.229   1.667 -19.120  1.00 48.54           C  
ANISOU 2860  CG  LEU A 370     5905   6544   5994    537    -79   -556       C  
ATOM   2861  CD1 LEU A 370     -17.816   1.863 -20.570  1.00 45.53           C  
ANISOU 2861  CD1 LEU A 370     5483   6182   5632    523    -83   -581       C  
ATOM   2862  CD2 LEU A 370     -17.034   1.787 -18.190  1.00 47.31           C  
ANISOU 2862  CD2 LEU A 370     5732   6442   5802    598   -104   -560       C  
ATOM   2863  N   THR A 371     -22.026   3.481 -17.297  1.00 41.91           N  
ANISOU 2863  N   THR A 371     5082   5629   5212    373    -14   -515       N  
ATOM   2864  CA  THR A 371     -23.077   4.472 -17.087  1.00 39.64           C  
ANISOU 2864  CA  THR A 371     4768   5338   4955    319      4   -513       C  
ATOM   2865  C   THR A 371     -23.228   4.811 -15.609  1.00 39.45           C  
ANISOU 2865  C   THR A 371     4765   5316   4907    325     18   -501       C  
ATOM   2866  O   THR A 371     -23.509   5.961 -15.254  1.00 41.18           O  
ANISOU 2866  O   THR A 371     4952   5556   5137    298     24   -508       O  
ATOM   2867  CB  THR A 371     -24.399   3.964 -17.662  1.00 39.31           C  
ANISOU 2867  CB  THR A 371     4741   5245   4949    274     28   -504       C  
ATOM   2868  OG1 THR A 371     -24.214   3.601 -19.036  1.00 41.08           O  
ANISOU 2868  OG1 THR A 371     4953   5467   5188    269     13   -516       O  
ATOM   2869  CG2 THR A 371     -25.473   5.038 -17.573  1.00 39.74           C  
ANISOU 2869  CG2 THR A 371     4757   5302   5040    225     44   -504       C  
ATOM   2870  N   ALA A 372     -23.045   3.819 -14.732  1.00 40.10           N  
ANISOU 2870  N   ALA A 372     4909   5372   4954    361     25   -484       N  
ATOM   2871  CA  ALA A 372     -23.114   4.082 -13.299  1.00 42.47           C  
ANISOU 2871  CA  ALA A 372     5239   5675   5223    370     37   -473       C  
ATOM   2872  C   ALA A 372     -22.038   5.072 -12.869  1.00 35.94           C  
ANISOU 2872  C   ALA A 372     4373   4913   4369    391      6   -490       C  
ATOM   2873  O   ALA A 372     -22.312   6.002 -12.103  1.00 34.07           O  
ANISOU 2873  O   ALA A 372     4126   4691   4128    367     18   -493       O  
ATOM   2874  CB  ALA A 372     -22.987   2.776 -12.518  1.00 40.62           C  
ANISOU 2874  CB  ALA A 372     5085   5401   4949    412     45   -450       C  
ATOM   2875  N   HIS A 373     -20.807   4.889 -13.354  1.00 37.86           N  
ANISOU 2875  N   HIS A 373     4593   5198   4596    432    -30   -503       N  
ATOM   2876  CA  HIS A 373     -19.756   5.866 -13.086  1.00 38.62           C  
ANISOU 2876  CA  HIS A 373     4640   5362   4670    442    -59   -524       C  
ATOM   2877  C   HIS A 373     -20.095   7.214 -13.706  1.00 39.41           C  
ANISOU 2877  C   HIS A 373     4684   5484   4807    386    -51   -544       C  
ATOM   2878  O   HIS A 373     -19.865   8.265 -13.095  1.00 42.81           O  
ANISOU 2878  O   HIS A 373     5094   5948   5225    368    -54   -556       O  
ATOM   2879  CB  HIS A 373     -18.416   5.360 -13.617  1.00 31.23           C  
ANISOU 2879  CB  HIS A 373     3682   4468   3716    495    -95   -537       C  
ATOM   2880  CG  HIS A 373     -17.868   4.188 -12.865  1.00 31.33           C  
ANISOU 2880  CG  HIS A 373     3748   4470   3684    564   -110   -519       C  
ATOM   2881  ND1 HIS A 373     -18.507   2.968 -12.821  1.00 40.68           N  
ANISOU 2881  ND1 HIS A 373     5002   5587   4868    581    -89   -493       N  
ATOM   2882  CD2 HIS A 373     -16.738   4.048 -12.132  1.00 41.56           C  
ANISOU 2882  CD2 HIS A 373     5041   5815   4935    620   -146   -522       C  
ATOM   2883  CE1 HIS A 373     -17.797   2.128 -12.090  1.00 50.42           C  
ANISOU 2883  CE1 HIS A 373     6280   6823   6056    649   -109   -478       C  
ATOM   2884  NE2 HIS A 373     -16.718   2.758 -11.661  1.00 44.24           N  
ANISOU 2884  NE2 HIS A 373     5450   6112   5245    676   -146   -495       N  
ATOM   2885  N   HIS A 374     -20.634   7.200 -14.926  1.00 35.29           N  
ANISOU 2885  N   HIS A 374     4142   4940   4328    358    -42   -547       N  
ATOM   2886  CA  HIS A 374     -21.000   8.440 -15.602  1.00 31.34           C  
ANISOU 2886  CA  HIS A 374     3594   4453   3860    310    -36   -562       C  
ATOM   2887  C   HIS A 374     -22.092   9.181 -14.839  1.00 36.23           C  
ANISOU 2887  C   HIS A 374     4223   5048   4495    274     -6   -553       C  
ATOM   2888  O   HIS A 374     -22.009  10.399 -14.638  1.00 36.17           O  
ANISOU 2888  O   HIS A 374     4188   5064   4489    250     -3   -566       O  
ATOM   2889  CB  HIS A 374     -21.443   8.127 -17.033  1.00 39.35           C  
ANISOU 2889  CB  HIS A 374     4594   5445   4912    291    -34   -562       C  
ATOM   2890  CG  HIS A 374     -22.180   9.243 -17.707  1.00 38.62           C  
ANISOU 2890  CG  HIS A 374     4468   5350   4858    242    -24   -568       C  
ATOM   2891  ND1 HIS A 374     -21.601  10.041 -18.670  1.00 41.24           N  
ANISOU 2891  ND1 HIS A 374     4760   5713   5196    226    -38   -587       N  
ATOM   2892  CD2 HIS A 374     -23.457   9.676 -17.580  1.00 35.03           C  
ANISOU 2892  CD2 HIS A 374     4014   4862   4434    208      0   -556       C  
ATOM   2893  CE1 HIS A 374     -22.482  10.929 -19.093  1.00 36.00           C  
ANISOU 2893  CE1 HIS A 374     4080   5034   4565    188    -27   -584       C  
ATOM   2894  NE2 HIS A 374     -23.616  10.729 -18.447  1.00 41.34           N  
ANISOU 2894  NE2 HIS A 374     4776   5673   5258    179     -5   -566       N  
ATOM   2895  N   GLU A 375     -23.126   8.459 -14.401  1.00 45.89           N  
ANISOU 2895  N   GLU A 375     5486   6222   5728    269     21   -531       N  
ATOM   2896  CA  GLU A 375     -24.232   9.110 -13.706  1.00 42.80           C  
ANISOU 2896  CA  GLU A 375     5100   5806   5354    236     56   -524       C  
ATOM   2897  C   GLU A 375     -23.845   9.490 -12.282  1.00 44.94           C  
ANISOU 2897  C   GLU A 375     5398   6095   5582    248     61   -525       C  
ATOM   2898  O   GLU A 375     -24.268  10.538 -11.779  1.00 44.13           O  
ANISOU 2898  O   GLU A 375     5286   5996   5487    223     81   -532       O  
ATOM   2899  CB  GLU A 375     -25.465   8.206 -13.712  1.00 39.08           C  
ANISOU 2899  CB  GLU A 375     4659   5281   4908    220     86   -504       C  
ATOM   2900  CG  GLU A 375     -26.094   8.033 -15.087  1.00 42.94           C  
ANISOU 2900  CG  GLU A 375     5117   5754   5443    195     82   -505       C  
ATOM   2901  CD  GLU A 375     -26.684   9.323 -15.631  1.00 48.19           C  
ANISOU 2901  CD  GLU A 375     5731   6431   6148    162     86   -514       C  
ATOM   2902  OE1 GLU A 375     -27.002  10.225 -14.827  1.00 51.31           O  
ANISOU 2902  OE1 GLU A 375     6121   6830   6543    152    107   -516       O  
ATOM   2903  OE2 GLU A 375     -26.829   9.435 -16.866  1.00 46.64           O1-
ANISOU 2903  OE2 GLU A 375     5505   6238   5979    148     69   -520       O1-
ATOM   2904  N   MET A 376     -23.050   8.652 -11.613  1.00 38.03           N  
ANISOU 2904  N   MET A 376     4560   5228   4660    290     44   -518       N  
ATOM   2905  CA  MET A 376     -22.537   9.037 -10.303  1.00 35.99           C  
ANISOU 2905  CA  MET A 376     4327   4995   4353    304     40   -521       C  
ATOM   2906  C   MET A 376     -21.591  10.224 -10.413  1.00 40.08           C  
ANISOU 2906  C   MET A 376     4796   5571   4859    296     13   -549       C  
ATOM   2907  O   MET A 376     -21.430  10.982  -9.449  1.00 39.42           O  
ANISOU 2907  O   MET A 376     4723   5508   4748    285     18   -558       O  
ATOM   2908  CB  MET A 376     -21.839   7.853  -9.637  1.00 36.62           C  
ANISOU 2908  CB  MET A 376     4457   5074   4382    357     19   -506       C  
ATOM   2909  CG  MET A 376     -21.533   8.066  -8.169  1.00 33.60           C  
ANISOU 2909  CG  MET A 376     4115   4707   3944    372     18   -502       C  
ATOM   2910  SD  MET A 376     -20.865   6.585  -7.401  1.00 48.72           S  
ANISOU 2910  SD  MET A 376     6101   6612   5798    440     -6   -477       S  
ATOM   2911  CE  MET A 376     -22.363   5.658  -7.082  1.00 39.26           C  
ANISOU 2911  CE  MET A 376     4975   5326   4616    419     53   -445       C  
ATOM   2912  N   GLY A 377     -20.959  10.401 -11.576  1.00 45.13           N  
ANISOU 2912  N   GLY A 377     5388   6239   5519    296    -11   -565       N  
ATOM   2913  CA  GLY A 377     -20.209  11.621 -11.818  1.00 41.58           C  
ANISOU 2913  CA  GLY A 377     4892   5839   5066    274    -27   -593       C  
ATOM   2914  C   GLY A 377     -21.093  12.852 -11.782  1.00 40.43           C  
ANISOU 2914  C   GLY A 377     4738   5674   4950    225      6   -599       C  
ATOM   2915  O   GLY A 377     -20.693  13.901 -11.273  1.00 46.00           O  
ANISOU 2915  O   GLY A 377     5435   6407   5638    205      6   -619       O  
ATOM   2916  N   HIS A 378     -22.308  12.741 -12.328  1.00 32.99           N  
ANISOU 2916  N   HIS A 378     3798   4684   4054    207     33   -583       N  
ATOM   2917  CA  HIS A 378     -23.280  13.821 -12.194  1.00 36.43           C  
ANISOU 2917  CA  HIS A 378     4227   5095   4518    171     67   -585       C  
ATOM   2918  C   HIS A 378     -23.606  14.076 -10.731  1.00 34.04           C  
ANISOU 2918  C   HIS A 378     3965   4783   4188    168     94   -582       C  
ATOM   2919  O   HIS A 378     -23.678  15.230 -10.293  1.00 39.79           O  
ANISOU 2919  O   HIS A 378     4690   5517   4913    145    110   -598       O  
ATOM   2920  CB  HIS A 378     -24.560  13.487 -12.958  1.00 35.01           C  
ANISOU 2920  CB  HIS A 378     4040   4870   4392    158     89   -567       C  
ATOM   2921  CG  HIS A 378     -24.402  13.486 -14.444  1.00 30.23           C  
ANISOU 2921  CG  HIS A 378     3398   4271   3815    152     66   -571       C  
ATOM   2922  ND1 HIS A 378     -23.955  14.584 -15.147  1.00 28.91           N  
ANISOU 2922  ND1 HIS A 378     3201   4127   3657    134     56   -588       N  
ATOM   2923  CD2 HIS A 378     -24.645  12.523 -15.364  1.00 36.49           C  
ANISOU 2923  CD2 HIS A 378     4187   5048   4628    159     55   -560       C  
ATOM   2924  CE1 HIS A 378     -23.924  14.295 -16.436  1.00 38.12           C  
ANISOU 2924  CE1 HIS A 378     4346   5292   4844    131     38   -586       C  
ATOM   2925  NE2 HIS A 378     -24.337  13.051 -16.594  1.00 40.30           N  
ANISOU 2925  NE2 HIS A 378     4637   5547   5129    146     36   -571       N  
ATOM   2926  N   ILE A 379     -23.812  13.005  -9.961  1.00 36.78           N  
ANISOU 2926  N   ILE A 379     4353   5110   4510    192    101   -564       N  
ATOM   2927  CA  ILE A 379     -24.100  13.154  -8.538  1.00 35.79           C  
ANISOU 2927  CA  ILE A 379     4274   4974   4350    190    127   -560       C  
ATOM   2928  C   ILE A 379     -22.961  13.890  -7.847  1.00 39.06           C  
ANISOU 2928  C   ILE A 379     4690   5438   4714    192    102   -584       C  
ATOM   2929  O   ILE A 379     -23.180  14.871  -7.129  1.00 40.78           O  
ANISOU 2929  O   ILE A 379     4920   5656   4920    167    125   -597       O  
ATOM   2930  CB  ILE A 379     -24.358  11.778  -7.898  1.00 39.37           C  
ANISOU 2930  CB  ILE A 379     4780   5399   4778    216    135   -535       C  
ATOM   2931  CG1 ILE A 379     -25.630  11.152  -8.471  1.00 38.59           C  
ANISOU 2931  CG1 ILE A 379     4681   5250   4732    201    169   -516       C  
ATOM   2932  CG2 ILE A 379     -24.482  11.906  -6.393  1.00 40.54           C  
ANISOU 2932  CG2 ILE A 379     4984   5542   4879    217    158   -532       C  
ATOM   2933  CD1 ILE A 379     -26.845  12.050  -8.375  1.00 40.24           C  
ANISOU 2933  CD1 ILE A 379     4872   5434   4984    164    216   -519       C  
ATOM   2934  N   GLN A 380     -21.721  13.454  -8.096  1.00 40.90           N  
ANISOU 2934  N   GLN A 380     4908   5717   4917    219     53   -592       N  
ATOM   2935  CA  GLN A 380     -20.565  14.108  -7.488  1.00 39.46           C  
ANISOU 2935  CA  GLN A 380     4716   5590   4685    218     23   -617       C  
ATOM   2936  C   GLN A 380     -20.528  15.592  -7.828  1.00 38.64           C  
ANISOU 2936  C   GLN A 380     4581   5500   4602    172     36   -645       C  
ATOM   2937  O   GLN A 380     -20.192  16.423  -6.976  1.00 41.76           O  
ANISOU 2937  O   GLN A 380     4989   5916   4962    151     38   -665       O  
ATOM   2938  CB  GLN A 380     -19.276  13.424  -7.941  1.00 32.14           C  
ANISOU 2938  CB  GLN A 380     3762   4714   3736    256    -30   -624       C  
ATOM   2939  CG  GLN A 380     -19.093  12.022  -7.388  1.00 36.14           C  
ANISOU 2939  CG  GLN A 380     4312   5213   4209    310    -47   -598       C  
ATOM   2940  CD  GLN A 380     -18.758  12.012  -5.909  1.00 35.01           C  
ANISOU 2940  CD  GLN A 380     4215   5087   4000    325    -58   -597       C  
ATOM   2941  OE1 GLN A 380     -18.539  13.059  -5.300  1.00 40.91           O  
ANISOU 2941  OE1 GLN A 380     4958   5861   4725    293    -56   -620       O  
ATOM   2942  NE2 GLN A 380     -18.714  10.822  -5.323  1.00 40.28           N  
ANISOU 2942  NE2 GLN A 380     4934   5738   4634    372    -68   -570       N  
ATOM   2943  N   TYR A 381     -20.866  15.942  -9.070  1.00 35.76           N  
ANISOU 2943  N   TYR A 381     4177   5120   4288    155     44   -646       N  
ATOM   2944  CA  TYR A 381     -21.034  17.348  -9.416  1.00 34.08           C  
ANISOU 2944  CA  TYR A 381     3946   4905   4098    112     63   -667       C  
ATOM   2945  C   TYR A 381     -22.122  17.984  -8.558  1.00 41.31           C  
ANISOU 2945  C   TYR A 381     4898   5777   5020     93    112   -662       C  
ATOM   2946  O   TYR A 381     -21.904  19.028  -7.932  1.00 43.79           O  
ANISOU 2946  O   TYR A 381     5226   6101   5312     67    125   -684       O  
ATOM   2947  CB  TYR A 381     -21.361  17.478 -10.906  1.00 30.05           C  
ANISOU 2947  CB  TYR A 381     3398   4378   3641    103     64   -662       C  
ATOM   2948  CG  TYR A 381     -20.899  18.765 -11.560  1.00 33.03           C  
ANISOU 2948  CG  TYR A 381     3750   4773   4028     67     64   -688       C  
ATOM   2949  CD1 TYR A 381     -20.404  19.819 -10.805  1.00 37.43           C  
ANISOU 2949  CD1 TYR A 381     4318   5350   4553     38     72   -714       C  
ATOM   2950  CD2 TYR A 381     -20.967  18.927 -12.940  1.00 30.71           C  
ANISOU 2950  CD2 TYR A 381     3426   4472   3771     58     59   -685       C  
ATOM   2951  CE1 TYR A 381     -19.994  20.997 -11.403  1.00 37.64           C  
ANISOU 2951  CE1 TYR A 381     4330   5386   4587      0     77   -737       C  
ATOM   2952  CE2 TYR A 381     -20.553  20.100 -13.546  1.00 28.73           C  
ANISOU 2952  CE2 TYR A 381     3161   4232   3525     23     63   -706       C  
ATOM   2953  CZ  TYR A 381     -20.067  21.131 -12.771  1.00 35.54           C  
ANISOU 2953  CZ  TYR A 381     4036   5110   4357     -7     73   -732       C  
ATOM   2954  OH  TYR A 381     -19.653  22.302 -13.365  1.00 36.31           O  
ANISOU 2954  OH  TYR A 381     4127   5212   4458    -46     82   -754       O  
ATOM   2955  N   ASP A 382     -23.289  17.335  -8.476  1.00 39.93           N  
ANISOU 2955  N   ASP A 382     4741   5556   4875    105    141   -635       N  
ATOM   2956  CA  ASP A 382     -24.413  17.904  -7.736  1.00 36.77           C  
ANISOU 2956  CA  ASP A 382     4368   5114   4488     89    194   -631       C  
ATOM   2957  C   ASP A 382     -24.085  18.085  -6.257  1.00 40.51           C  
ANISOU 2957  C   ASP A 382     4890   5599   4902     87    204   -642       C  
ATOM   2958  O   ASP A 382     -24.387  19.133  -5.674  1.00 46.70           O  
ANISOU 2958  O   ASP A 382     5693   6371   5681     62    237   -658       O  
ATOM   2959  CB  ASP A 382     -25.652  17.024  -7.901  1.00 36.55           C  
ANISOU 2959  CB  ASP A 382     4344   5042   4500    101    222   -602       C  
ATOM   2960  CG  ASP A 382     -26.055  16.849  -9.351  1.00 40.12           C  
ANISOU 2960  CG  ASP A 382     4751   5483   5009    101    210   -593       C  
ATOM   2961  OD1 ASP A 382     -25.749  17.745 -10.165  1.00 34.17           O  
ANISOU 2961  OD1 ASP A 382     3967   4742   4274     87    197   -606       O  
ATOM   2962  OD2 ASP A 382     -26.676  15.816  -9.678  1.00 39.76           O1-
ANISOU 2962  OD2 ASP A 382     4704   5416   4986    111    213   -572       O1-
ATOM   2963  N   MET A 383     -23.470  17.076  -5.631  1.00 37.92           N  
ANISOU 2963  N   MET A 383     4588   5292   4526    113    176   -633       N  
ATOM   2964  CA  MET A 383     -23.115  17.195  -4.220  1.00 41.28           C  
ANISOU 2964  CA  MET A 383     5065   5732   4887    112    180   -642       C  
ATOM   2965  C   MET A 383     -22.042  18.246  -3.976  1.00 43.72           C  
ANISOU 2965  C   MET A 383     5362   6089   5159     89    153   -677       C  
ATOM   2966  O   MET A 383     -21.956  18.779  -2.864  1.00 53.19           O  
ANISOU 2966  O   MET A 383     6603   7293   6312     72    168   -692       O  
ATOM   2967  CB  MET A 383     -22.646  15.847  -3.662  1.00 31.67           C  
ANISOU 2967  CB  MET A 383     3881   4528   3624    152    150   -621       C  
ATOM   2968  CG  MET A 383     -23.426  14.646  -4.165  1.00 33.68           C  
ANISOU 2968  CG  MET A 383     4141   4740   3914    175    164   -588       C  
ATOM   2969  SD  MET A 383     -22.947  13.085  -3.400  1.00 46.56           S  
ANISOU 2969  SD  MET A 383     5831   6374   5487    223    137   -561       S  
ATOM   2970  CE  MET A 383     -22.220  13.652  -1.866  1.00 49.44           C  
ANISOU 2970  CE  MET A 383     6244   6775   5767    222    123   -578       C  
ATOM   2971  N   ALA A 384     -21.225  18.557  -4.984  1.00 39.68           N  
ANISOU 2971  N   ALA A 384     4798   5614   4663     82    118   -693       N  
ATOM   2972  CA  ALA A 384     -20.136  19.506  -4.781  1.00 41.71           C  
ANISOU 2972  CA  ALA A 384     5041   5922   4885     54     93   -730       C  
ATOM   2973  C   ALA A 384     -20.646  20.940  -4.694  1.00 47.94           C  
ANISOU 2973  C   ALA A 384     5843   6682   5691      8    137   -752       C  
ATOM   2974  O   ALA A 384     -20.165  21.722  -3.866  1.00 53.33           O  
ANISOU 2974  O   ALA A 384     6550   7386   6329    -22    139   -780       O  
ATOM   2975  CB  ALA A 384     -19.107  19.367  -5.899  1.00 42.42           C  
ANISOU 2975  CB  ALA A 384     5072   6059   4988     58     48   -742       C  
ATOM   2976  N   TYR A 385     -21.612  21.310  -5.537  1.00 45.70           N  
ANISOU 2976  N   TYR A 385     5545   6350   5470      1    173   -739       N  
ATOM   2977  CA  TYR A 385     -22.165  22.658  -5.513  1.00 46.28           C  
ANISOU 2977  CA  TYR A 385     5633   6388   5563    -34    218   -756       C  
ATOM   2978  C   TYR A 385     -23.491  22.733  -4.766  1.00 46.81           C  
ANISOU 2978  C   TYR A 385     5740   6399   5646    -27    276   -741       C  
ATOM   2979  O   TYR A 385     -24.222  23.716  -4.918  1.00 45.40           O  
ANISOU 2979  O   TYR A 385     5568   6180   5500    -43    319   -746       O  
ATOM   2980  CB  TYR A 385     -22.331  23.218  -6.930  1.00 40.17           C  
ANISOU 2980  CB  TYR A 385     4819   5599   4845    -44    220   -755       C  
ATOM   2981  CG  TYR A 385     -23.132  22.370  -7.901  1.00 44.07           C  
ANISOU 2981  CG  TYR A 385     5284   6068   5394    -13    218   -721       C  
ATOM   2982  CD1 TYR A 385     -24.505  22.209  -7.753  1.00 46.25           C  
ANISOU 2982  CD1 TYR A 385     5571   6293   5710      1    260   -698       C  
ATOM   2983  CD2 TYR A 385     -22.516  21.748  -8.977  1.00 48.03           C  
ANISOU 2983  CD2 TYR A 385     5744   6597   5908     -2    177   -715       C  
ATOM   2984  CE1 TYR A 385     -25.237  21.442  -8.640  1.00 45.01           C  
ANISOU 2984  CE1 TYR A 385     5385   6116   5602     23    256   -670       C  
ATOM   2985  CE2 TYR A 385     -23.243  20.982  -9.872  1.00 43.97           C  
ANISOU 2985  CE2 TYR A 385     5207   6060   5441     21    175   -687       C  
ATOM   2986  CZ  TYR A 385     -24.598  20.830  -9.699  1.00 41.58           C  
ANISOU 2986  CZ  TYR A 385     4915   5708   5175     32    212   -665       C  
ATOM   2987  OH  TYR A 385     -25.313  20.065 -10.591  1.00 43.50           O  
ANISOU 2987  OH  TYR A 385     5133   5932   5463     49    207   -641       O  
ATOM   2988  N   ALA A 386     -23.822  21.712  -3.970  1.00 48.64           N  
ANISOU 2988  N   ALA A 386     5999   6626   5856     -2    280   -721       N  
ATOM   2989  CA  ALA A 386     -25.048  21.763  -3.181  1.00 48.44           C  
ANISOU 2989  CA  ALA A 386     6013   6551   5842      0    340   -709       C  
ATOM   2990  C   ALA A 386     -25.035  22.930  -2.203  1.00 52.25           C  
ANISOU 2990  C   ALA A 386     6540   7024   6289    -30    376   -738       C  
ATOM   2991  O   ALA A 386     -26.089  23.510  -1.913  1.00 55.62           O  
ANISOU 2991  O   ALA A 386     6986   7403   6744    -35    436   -738       O  
ATOM   2992  CB  ALA A 386     -25.251  20.445  -2.435  1.00 47.29           C  
ANISOU 2992  CB  ALA A 386     5897   6403   5666     26    338   -684       C  
ATOM   2993  N   ALA A 387     -23.858  23.290  -1.686  1.00 55.95           N  
ANISOU 2993  N   ALA A 387     7025   7537   6695    -51    341   -766       N  
ATOM   2994  CA  ALA A 387     -23.737  24.433  -0.790  1.00 56.94           C  
ANISOU 2994  CA  ALA A 387     7198   7655   6782    -86    372   -799       C  
ATOM   2995  C   ALA A 387     -23.903  25.767  -1.506  1.00 49.45           C  
ANISOU 2995  C   ALA A 387     6236   6681   5874   -114    398   -820       C  
ATOM   2996  O   ALA A 387     -24.038  26.796  -0.835  1.00 67.78           O  
ANISOU 2996  O   ALA A 387     8601   8979   8173   -143    438   -846       O  
ATOM   2997  CB  ALA A 387     -22.386  24.397  -0.074  1.00 55.30           C  
ANISOU 2997  CB  ALA A 387     7007   7511   6495   -104    320   -825       C  
ATOM   2998  N   GLN A 388     -23.890  25.777  -2.836  1.00 32.41           N  
ANISOU 2998  N   GLN A 388     4023   4521   3768   -106    380   -808       N  
ATOM   2999  CA  GLN A 388     -24.094  27.003  -3.583  1.00 32.76           C  
ANISOU 2999  CA  GLN A 388     4061   4534   3851   -128    405   -822       C  
ATOM   3000  C   GLN A 388     -25.555  27.437  -3.496  1.00 38.98           C  
ANISOU 3000  C   GLN A 388     4866   5255   4688   -110    471   -807       C  
ATOM   3001  O   GLN A 388     -26.430  26.638  -3.155  1.00 39.66           O  
ANISOU 3001  O   GLN A 388     4951   5324   4794    -81    492   -782       O  
ATOM   3002  CB  GLN A 388     -23.690  26.809  -5.044  1.00 34.57           C  
ANISOU 3002  CB  GLN A 388     4232   4782   4119   -122    365   -811       C  
ATOM   3003  CG  GLN A 388     -22.209  26.549  -5.258  1.00 33.25           C  
ANISOU 3003  CG  GLN A 388     4041   4683   3910   -142    305   -832       C  
ATOM   3004  CD  GLN A 388     -21.383  27.819  -5.217  1.00 32.66           C  
ANISOU 3004  CD  GLN A 388     3983   4621   3806   -195    309   -873       C  
ATOM   3005  OE1 GLN A 388     -21.916  28.915  -5.045  1.00 31.12           O  
ANISOU 3005  OE1 GLN A 388     3825   4378   3621   -216    357   -885       O  
ATOM   3006  NE2 GLN A 388     -20.072  27.677  -5.379  1.00 29.27           N  
ANISOU 3006  NE2 GLN A 388     3525   4257   3340   -217    260   -896       N  
ATOM   3007  N   PRO A 389     -25.842  28.708  -3.786  1.00 35.51           N  
ANISOU 3007  N   PRO A 389     4442   4777   4271   -127    507   -823       N  
ATOM   3008  CA  PRO A 389     -27.241  29.139  -3.866  1.00 32.38           C  
ANISOU 3008  CA  PRO A 389     4052   4320   3932   -100    567   -806       C  
ATOM   3009  C   PRO A 389     -27.999  28.338  -4.914  1.00 36.68           C  
ANISOU 3009  C   PRO A 389     4536   4858   4541    -62    551   -768       C  
ATOM   3010  O   PRO A 389     -27.418  27.815  -5.867  1.00 41.07           O  
ANISOU 3010  O   PRO A 389     5052   5446   5106    -61    498   -758       O  
ATOM   3011  CB  PRO A 389     -27.137  30.618  -4.256  1.00 37.10           C  
ANISOU 3011  CB  PRO A 389     4675   4882   4538   -122    592   -829       C  
ATOM   3012  CG  PRO A 389     -25.804  31.042  -3.751  1.00 36.36           C  
ANISOU 3012  CG  PRO A 389     4614   4826   4376   -173    568   -867       C  
ATOM   3013  CD  PRO A 389     -24.907  29.843  -3.888  1.00 34.03           C  
ANISOU 3013  CD  PRO A 389     4278   4598   4053   -172    501   -859       C  
ATOM   3014  N   PHE A 390     -29.316  28.236  -4.711  1.00 51.01           N  
ANISOU 3014  N   PHE A 390     6346   6635   6402    -33    599   -750       N  
ATOM   3015  CA  PHE A 390     -30.142  27.372  -5.552  1.00 50.97           C  
ANISOU 3015  CA  PHE A 390     6284   6628   6455     -1    586   -716       C  
ATOM   3016  C   PHE A 390     -29.996  27.719  -7.029  1.00 46.21           C  
ANISOU 3016  C   PHE A 390     5641   6025   5892      5    550   -706       C  
ATOM   3017  O   PHE A 390     -29.868  26.825  -7.874  1.00 45.72           O  
ANISOU 3017  O   PHE A 390     5535   5987   5847     15    505   -686       O  
ATOM   3018  CB  PHE A 390     -31.607  27.472  -5.121  1.00 47.65           C  
ANISOU 3018  CB  PHE A 390     5858   6166   6081     25    649   -705       C  
ATOM   3019  CG  PHE A 390     -32.553  26.696  -5.995  1.00 46.97           C  
ANISOU 3019  CG  PHE A 390     5708   6078   6059     53    639   -673       C  
ATOM   3020  CD1 PHE A 390     -32.797  25.355  -5.752  1.00 44.69           C  
ANISOU 3020  CD1 PHE A 390     5403   5808   5769     55    630   -657       C  
ATOM   3021  CD2 PHE A 390     -33.205  27.309  -7.054  1.00 37.85           C  
ANISOU 3021  CD2 PHE A 390     4515   4902   4964     75    638   -661       C  
ATOM   3022  CE1 PHE A 390     -33.667  24.637  -6.551  1.00 38.14           C  
ANISOU 3022  CE1 PHE A 390     4516   4977   4997     74    621   -632       C  
ATOM   3023  CE2 PHE A 390     -34.074  26.597  -7.858  1.00 37.82           C  
ANISOU 3023  CE2 PHE A 390     4451   4902   5017     98    624   -635       C  
ATOM   3024  CZ  PHE A 390     -34.306  25.259  -7.605  1.00 43.63           C  
ANISOU 3024  CZ  PHE A 390     5167   5658   5752     94    616   -622       C  
ATOM   3025  N   LEU A 391     -30.014  29.011  -7.361  1.00 55.52           N  
ANISOU 3025  N   LEU A 391     6840   7174   7083      0    570   -718       N  
ATOM   3026  CA  LEU A 391     -29.921  29.422  -8.757  1.00 55.76           C  
ANISOU 3026  CA  LEU A 391     6842   7199   7147      7    540   -706       C  
ATOM   3027  C   LEU A 391     -28.559  29.117  -9.368  1.00 55.29           C  
ANISOU 3027  C   LEU A 391     6774   7184   7050    -23    482   -716       C  
ATOM   3028  O   LEU A 391     -28.442  29.072 -10.597  1.00 55.29           O  
ANISOU 3028  O   LEU A 391     6744   7189   7075    -18    449   -702       O  
ATOM   3029  CB  LEU A 391     -30.231  30.913  -8.880  1.00 59.58           C  
ANISOU 3029  CB  LEU A 391     7362   7632   7645      8    580   -718       C  
ATOM   3030  CG  LEU A 391     -31.704  31.260  -8.658  1.00 56.56           C  
ANISOU 3030  CG  LEU A 391     6970   7203   7316     52    632   -703       C  
ATOM   3031  CD1 LEU A 391     -31.887  32.743  -8.394  1.00 63.51           C  
ANISOU 3031  CD1 LEU A 391     7906   8031   8196     53    682   -720       C  
ATOM   3032  CD2 LEU A 391     -32.542  30.817  -9.845  1.00 51.82           C  
ANISOU 3032  CD2 LEU A 391     6308   6603   6778     89    605   -668       C  
ATOM   3033  N   LEU A 392     -27.532  28.912  -8.547  1.00 41.35           N  
ANISOU 3033  N   LEU A 392     5032   5453   5224    -53    469   -740       N  
ATOM   3034  CA  LEU A 392     -26.203  28.565  -9.029  1.00 35.31           C  
ANISOU 3034  CA  LEU A 392     4252   4739   4424    -79    416   -752       C  
ATOM   3035  C   LEU A 392     -25.914  27.072  -8.948  1.00 38.20           C  
ANISOU 3035  C   LEU A 392     4587   5149   4779    -63    376   -738       C  
ATOM   3036  O   LEU A 392     -24.797  26.653  -9.267  1.00 35.33           O  
ANISOU 3036  O   LEU A 392     4206   4832   4386    -77    332   -748       O  
ATOM   3037  CB  LEU A 392     -25.141  29.343  -8.245  1.00 40.41           C  
ANISOU 3037  CB  LEU A 392     4940   5403   5010   -124    421   -792       C  
ATOM   3038  CG  LEU A 392     -25.313  30.863  -8.236  1.00 41.09           C  
ANISOU 3038  CG  LEU A 392     5071   5441   5099   -147    465   -812       C  
ATOM   3039  CD1 LEU A 392     -24.379  31.510  -7.225  1.00 39.42           C  
ANISOU 3039  CD1 LEU A 392     4906   5248   4824   -196    474   -854       C  
ATOM   3040  CD2 LEU A 392     -25.085  31.437  -9.627  1.00 44.73           C  
ANISOU 3040  CD2 LEU A 392     5519   5891   5588   -155    450   -806       C  
ATOM   3041  N   ARG A 393     -26.890  26.262  -8.534  1.00 45.97           N  
ANISOU 3041  N   ARG A 393     5564   6118   5787    -33    394   -715       N  
ATOM   3042  CA  ARG A 393     -26.703  24.819  -8.388  1.00 44.49           C  
ANISOU 3042  CA  ARG A 393     5357   5961   5586    -17    362   -699       C  
ATOM   3043  C   ARG A 393     -26.878  24.159  -9.753  1.00 46.72           C  
ANISOU 3043  C   ARG A 393     5592   6249   5911      0    329   -676       C  
ATOM   3044  O   ARG A 393     -27.935  23.622 -10.096  1.00 51.80           O  
ANISOU 3044  O   ARG A 393     6213   6870   6600     21    340   -652       O  
ATOM   3045  CB  ARG A 393     -27.676  24.250  -7.364  1.00 39.47           C  
ANISOU 3045  CB  ARG A 393     4740   5302   4954      0    402   -686       C  
ATOM   3046  CG  ARG A 393     -27.142  24.231  -5.945  1.00 46.05           C  
ANISOU 3046  CG  ARG A 393     5623   6151   5723    -14    413   -705       C  
ATOM   3047  CD  ARG A 393     -28.152  23.630  -4.985  1.00 61.00           C  
ANISOU 3047  CD  ARG A 393     7541   8018   7620      1    458   -690       C  
ATOM   3048  NE  ARG A 393     -28.294  24.429  -3.774  1.00 53.97           N  
ANISOU 3048  NE  ARG A 393     6704   7110   6695    -15    504   -711       N  
ATOM   3049  CZ  ARG A 393     -29.344  24.383  -2.966  1.00 60.29           C  
ANISOU 3049  CZ  ARG A 393     7528   7875   7505     -8    563   -705       C  
ATOM   3050  NH1 ARG A 393     -30.370  23.585  -3.211  1.00 59.04           N  
ANISOU 3050  NH1 ARG A 393     7342   7698   7394     12    583   -679       N  
ATOM   3051  NH2 ARG A 393     -29.365  25.159  -1.886  1.00 67.06           N  
ANISOU 3051  NH2 ARG A 393     8438   8717   8325    -24    605   -728       N  
ATOM   3052  N   ASN A 394     -25.807  24.194 -10.540  1.00 44.26           N  
ANISOU 3052  N   ASN A 394     5263   5970   5582    -13    287   -686       N  
ATOM   3053  CA  ASN A 394     -25.820  23.671 -11.900  1.00 46.87           C  
ANISOU 3053  CA  ASN A 394     5555   6308   5946     -2    254   -670       C  
ATOM   3054  C   ASN A 394     -24.384  23.621 -12.399  1.00 48.22           C  
ANISOU 3054  C   ASN A 394     5714   6526   6082    -20    214   -689       C  
ATOM   3055  O   ASN A 394     -23.466  24.132 -11.753  1.00 47.94           O  
ANISOU 3055  O   ASN A 394     5696   6517   6003    -44    212   -716       O  
ATOM   3056  CB  ASN A 394     -26.687  24.534 -12.820  1.00 48.98           C  
ANISOU 3056  CB  ASN A 394     5812   6536   6262      1    272   -658       C  
ATOM   3057  CG  ASN A 394     -27.512  23.715 -13.787  1.00 55.40           C  
ANISOU 3057  CG  ASN A 394     6588   7340   7122     24    254   -630       C  
ATOM   3058  OD1 ASN A 394     -27.127  22.612 -14.173  1.00 45.84           O  
ANISOU 3058  OD1 ASN A 394     5360   6155   5904     30    222   -622       O  
ATOM   3059  ND2 ASN A 394     -28.658  24.254 -14.186  1.00 62.93           N  
ANISOU 3059  ND2 ASN A 394     7531   8256   8122     38    276   -614       N  
ATOM   3060  N   GLY A 395     -24.198  22.999 -13.561  1.00 43.57           N  
ANISOU 3060  N   GLY A 395     5093   5949   5512    -11    183   -677       N  
ATOM   3061  CA  GLY A 395     -22.895  23.013 -14.194  1.00 36.40           C  
ANISOU 3061  CA  GLY A 395     4169   5085   4578    -28    150   -696       C  
ATOM   3062  C   GLY A 395     -22.492  24.411 -14.621  1.00 43.37           C  
ANISOU 3062  C   GLY A 395     5062   5960   5456    -64    164   -716       C  
ATOM   3063  O   GLY A 395     -23.328  25.295 -14.817  1.00 51.37           O  
ANISOU 3063  O   GLY A 395     6094   6929   6496    -67    192   -708       O  
ATOM   3064  N   ALA A 396     -21.177  24.609 -14.761  1.00 38.59           N  
ANISOU 3064  N   ALA A 396     4447   5401   4815    -91    144   -744       N  
ATOM   3065  CA  ALA A 396     -20.654  25.934 -15.087  1.00 31.81           C  
ANISOU 3065  CA  ALA A 396     3604   4538   3945   -135    160   -768       C  
ATOM   3066  C   ALA A 396     -21.287  26.482 -16.359  1.00 32.61           C  
ANISOU 3066  C   ALA A 396     3711   4597   4084   -135    170   -749       C  
ATOM   3067  O   ALA A 396     -21.620  27.670 -16.436  1.00 44.97           O  
ANISOU 3067  O   ALA A 396     5309   6123   5655   -155    200   -753       O  
ATOM   3068  CB  ALA A 396     -19.132  25.882 -15.220  1.00 31.94           C  
ANISOU 3068  CB  ALA A 396     3595   4618   3922   -165    135   -801       C  
ATOM   3069  N   ASN A 397     -21.461  25.632 -17.366  1.00 35.49           N  
ANISOU 3069  N   ASN A 397     4047   4966   4470   -113    145   -728       N  
ATOM   3070  CA  ASN A 397     -22.314  25.938 -18.506  1.00 38.81           C  
ANISOU 3070  CA  ASN A 397     4473   5346   4928   -103    148   -703       C  
ATOM   3071  C   ASN A 397     -23.025  24.650 -18.908  1.00 37.53           C  
ANISOU 3071  C   ASN A 397     4283   5182   4793    -64    125   -675       C  
ATOM   3072  O   ASN A 397     -22.955  23.636 -18.206  1.00 39.26           O  
ANISOU 3072  O   ASN A 397     4489   5424   5004    -46    115   -674       O  
ATOM   3073  CB  ASN A 397     -21.512  26.582 -19.650  1.00 37.84           C  
ANISOU 3073  CB  ASN A 397     4355   5231   4792   -136    143   -716       C  
ATOM   3074  CG  ASN A 397     -20.435  25.670 -20.215  1.00 39.04           C  
ANISOU 3074  CG  ASN A 397     4472   5437   4924   -142    113   -728       C  
ATOM   3075  OD1 ASN A 397     -20.683  24.510 -20.541  1.00 44.73           O  
ANISOU 3075  OD1 ASN A 397     5168   6168   5658   -111     90   -712       O  
ATOM   3076  ND2 ASN A 397     -19.228  26.207 -20.350  1.00 36.62           N  
ANISOU 3076  ND2 ASN A 397     4163   5165   4586   -183    117   -760       N  
ATOM   3077  N   GLU A 398     -23.716  24.689 -20.048  1.00 36.57           N  
ANISOU 3077  N   GLU A 398     4158   5035   4702    -54    116   -653       N  
ATOM   3078  CA  GLU A 398     -24.541  23.555 -20.453  1.00 35.79           C  
ANISOU 3078  CA  GLU A 398     4036   4931   4632    -24     97   -628       C  
ATOM   3079  C   GLU A 398     -23.709  22.311 -20.743  1.00 35.92           C  
ANISOU 3079  C   GLU A 398     4032   4988   4629    -20     68   -635       C  
ATOM   3080  O   GLU A 398     -24.208  21.189 -20.598  1.00 42.92           O  
ANISOU 3080  O   GLU A 398     4905   5874   5530      3     58   -621       O  
ATOM   3081  CB  GLU A 398     -25.380  23.931 -21.673  1.00 37.27           C  
ANISOU 3081  CB  GLU A 398     4224   5087   4850    -17     87   -605       C  
ATOM   3082  CG  GLU A 398     -24.577  24.503 -22.827  1.00 37.97           C  
ANISOU 3082  CG  GLU A 398     4325   5182   4918    -42     76   -613       C  
ATOM   3083  CD  GLU A 398     -25.454  24.952 -23.977  1.00 40.28           C  
ANISOU 3083  CD  GLU A 398     4627   5441   5236    -32     65   -588       C  
ATOM   3084  OE1 GLU A 398     -26.634  25.279 -23.733  1.00 42.19           O  
ANISOU 3084  OE1 GLU A 398     4867   5651   5512     -7     74   -568       O  
ATOM   3085  OE2 GLU A 398     -24.965  24.974 -25.126  1.00 45.15           O1-
ANISOU 3085  OE2 GLU A 398     5251   6066   5839    -46     48   -587       O1-
ATOM   3086  N   GLY A 399     -22.452  22.480 -21.150  1.00 29.78           N  
ANISOU 3086  N   GLY A 399     3250   4244   3820    -42     59   -658       N  
ATOM   3087  CA  GLY A 399     -21.608  21.346 -21.468  1.00 28.05           C  
ANISOU 3087  CA  GLY A 399     3009   4064   3583    -33     35   -666       C  
ATOM   3088  C   GLY A 399     -20.811  20.769 -20.322  1.00 28.37           C  
ANISOU 3088  C   GLY A 399     3041   4142   3595    -22     31   -683       C  
ATOM   3089  O   GLY A 399     -20.229  19.691 -20.470  1.00 26.00           O  
ANISOU 3089  O   GLY A 399     2725   3871   3284     -2     10   -687       O  
ATOM   3090  N   PHE A 400     -20.774  21.451 -19.176  1.00 36.54           N  
ANISOU 3090  N   PHE A 400     4090   5178   4616    -32     49   -694       N  
ATOM   3091  CA  PHE A 400     -19.906  21.022 -18.083  1.00 31.31           C  
ANISOU 3091  CA  PHE A 400     3420   4557   3918    -25     40   -713       C  
ATOM   3092  C   PHE A 400     -20.405  19.735 -17.437  1.00 32.43           C  
ANISOU 3092  C   PHE A 400     3566   4692   4063     16     31   -693       C  
ATOM   3093  O   PHE A 400     -19.623  18.807 -17.198  1.00 30.82           O  
ANISOU 3093  O   PHE A 400     3350   4524   3836     38      8   -699       O  
ATOM   3094  CB  PHE A 400     -19.793  22.132 -17.040  1.00 28.12           C  
ANISOU 3094  CB  PHE A 400     3037   4152   3495    -51     62   -731       C  
ATOM   3095  CG  PHE A 400     -18.563  22.977 -17.184  1.00 35.44           C  
ANISOU 3095  CG  PHE A 400     3954   5119   4392    -92     60   -766       C  
ATOM   3096  CD1 PHE A 400     -18.408  23.822 -18.269  1.00 34.53           C  
ANISOU 3096  CD1 PHE A 400     3841   4991   4287   -124     71   -773       C  
ATOM   3097  CD2 PHE A 400     -17.559  22.924 -16.236  1.00 32.88           C  
ANISOU 3097  CD2 PHE A 400     3619   4846   4028   -100     48   -793       C  
ATOM   3098  CE1 PHE A 400     -17.273  24.602 -18.400  1.00 34.07           C  
ANISOU 3098  CE1 PHE A 400     3775   4969   4201   -169     75   -807       C  
ATOM   3099  CE2 PHE A 400     -16.424  23.700 -16.359  1.00 36.72           C  
ANISOU 3099  CE2 PHE A 400     4090   5374   4488   -144     47   -830       C  
ATOM   3100  CZ  PHE A 400     -16.280  24.540 -17.443  1.00 38.59           C  
ANISOU 3100  CZ  PHE A 400     4330   5597   4737   -181     64   -837       C  
ATOM   3101  N   HIS A 401     -21.705  19.663 -17.140  1.00 31.53           N  
ANISOU 3101  N   HIS A 401     3470   4532   3978     26     50   -669       N  
ATOM   3102  CA  HIS A 401     -22.227  18.545 -16.358  1.00 31.80           C  
ANISOU 3102  CA  HIS A 401     3516   4555   4012     56     50   -651       C  
ATOM   3103  C   HIS A 401     -22.057  17.221 -17.094  1.00 31.77           C  
ANISOU 3103  C   HIS A 401     3500   4557   4013     80     26   -640       C  
ATOM   3104  O   HIS A 401     -21.579  16.236 -16.521  1.00 34.78           O  
ANISOU 3104  O   HIS A 401     3889   4955   4370    107     13   -639       O  
ATOM   3105  CB  HIS A 401     -23.696  18.790 -16.012  1.00 34.56           C  
ANISOU 3105  CB  HIS A 401     3880   4856   4397     56     81   -631       C  
ATOM   3106  CG  HIS A 401     -24.030  18.514 -14.579  1.00 27.58           C  
ANISOU 3106  CG  HIS A 401     3021   3963   3494     66    101   -627       C  
ATOM   3107  ND1 HIS A 401     -23.931  17.258 -14.021  1.00 26.12           N  
ANISOU 3107  ND1 HIS A 401     2850   3783   3291     91     92   -616       N  
ATOM   3108  CD2 HIS A 401     -24.455  19.333 -13.588  1.00 28.24           C  
ANISOU 3108  CD2 HIS A 401     3127   4031   3573     55    133   -632       C  
ATOM   3109  CE1 HIS A 401     -24.285  17.314 -12.750  1.00 31.08           C  
ANISOU 3109  CE1 HIS A 401     3508   4400   3902     93    117   -614       C  
ATOM   3110  NE2 HIS A 401     -24.607  18.562 -12.461  1.00 33.60           N  
ANISOU 3110  NE2 HIS A 401     3831   4707   4228     71    143   -625       N  
ATOM   3111  N   GLU A 402     -22.441  17.179 -18.372  1.00 43.80           N  
ANISOU 3111  N   GLU A 402     5011   6066   5566     73     19   -632       N  
ATOM   3112  CA  GLU A 402     -22.281  15.946 -19.136  1.00 42.77           C  
ANISOU 3112  CA  GLU A 402     4875   5937   5438     92     -1   -624       C  
ATOM   3113  C   GLU A 402     -20.814  15.645 -19.411  1.00 47.65           C  
ANISOU 3113  C   GLU A 402     5478   6603   6024    102    -22   -646       C  
ATOM   3114  O   GLU A 402     -20.446  14.481 -19.608  1.00 47.89           O  
ANISOU 3114  O   GLU A 402     5510   6641   6046    130    -37   -643       O  
ATOM   3115  CB  GLU A 402     -23.069  16.031 -20.442  1.00 33.83           C  
ANISOU 3115  CB  GLU A 402     3734   4778   4340     79     -5   -612       C  
ATOM   3116  CG  GLU A 402     -23.799  14.751 -20.817  1.00 50.87           C  
ANISOU 3116  CG  GLU A 402     5899   6911   6517     93    -11   -594       C  
ATOM   3117  CD  GLU A 402     -24.885  14.376 -19.827  1.00 58.75           C  
ANISOU 3117  CD  GLU A 402     6911   7880   7532     99     10   -577       C  
ATOM   3118  OE1 GLU A 402     -25.553  15.283 -19.287  1.00 58.28           O  
ANISOU 3118  OE1 GLU A 402     6849   7806   7488     88     30   -573       O  
ATOM   3119  OE2 GLU A 402     -25.076  13.166 -19.597  1.00 49.31           O1-
ANISOU 3119  OE2 GLU A 402     5731   6671   6333    114      9   -568       O1-
ATOM   3120  N   ALA A 403     -19.964  16.675 -19.439  1.00 38.97           N  
ANISOU 3120  N   ALA A 403     4363   5536   4906     79    -22   -670       N  
ATOM   3121  CA  ALA A 403     -18.532  16.442 -19.594  1.00 33.66           C  
ANISOU 3121  CA  ALA A 403     3668   4918   4205     87    -40   -694       C  
ATOM   3122  C   ALA A 403     -17.957  15.732 -18.377  1.00 39.38           C  
ANISOU 3122  C   ALA A 403     4394   5670   4897    121    -54   -698       C  
ATOM   3123  O   ALA A 403     -17.090  14.861 -18.510  1.00 39.96           O  
ANISOU 3123  O   ALA A 403     4453   5776   4954    153    -74   -705       O  
ATOM   3124  CB  ALA A 403     -17.804  17.763 -19.840  1.00 28.70           C  
ANISOU 3124  CB  ALA A 403     3022   4318   3564     46    -33   -721       C  
ATOM   3125  N   VAL A 404     -18.431  16.092 -17.182  1.00 36.78           N  
ANISOU 3125  N   VAL A 404     4087   5328   4559    118    -42   -692       N  
ATOM   3126  CA  VAL A 404     -17.971  15.432 -15.964  1.00 30.25           C  
ANISOU 3126  CA  VAL A 404     3272   4524   3697    151    -55   -691       C  
ATOM   3127  C   VAL A 404     -18.344  13.956 -15.986  1.00 34.05           C  
ANISOU 3127  C   VAL A 404     3775   4979   4183    195    -63   -666       C  
ATOM   3128  O   VAL A 404     -17.562  13.094 -15.566  1.00 36.67           O  
ANISOU 3128  O   VAL A 404     4108   5339   4485    236    -85   -668       O  
ATOM   3129  CB  VAL A 404     -18.544  16.148 -14.727  1.00 33.04           C  
ANISOU 3129  CB  VAL A 404     3653   4861   4039    134    -36   -689       C  
ATOM   3130  CG1 VAL A 404     -18.244  15.360 -13.460  1.00 31.77           C  
ANISOU 3130  CG1 VAL A 404     3517   4715   3840    170    -49   -683       C  
ATOM   3131  CG2 VAL A 404     -17.985  17.560 -14.629  1.00 31.11           C  
ANISOU 3131  CG2 VAL A 404     3393   4644   3782     90    -29   -719       C  
ATOM   3132  N   GLY A 405     -19.543  13.639 -16.476  1.00 31.11           N  
ANISOU 3132  N   GLY A 405     3420   4553   3846    188    -44   -644       N  
ATOM   3133  CA  GLY A 405     -19.956  12.248 -16.549  1.00 27.20           C  
ANISOU 3133  CA  GLY A 405     2952   4028   3356    221    -46   -622       C  
ATOM   3134  C   GLY A 405     -19.122  11.430 -17.517  1.00 31.36           C  
ANISOU 3134  C   GLY A 405     3463   4575   3879    247    -68   -630       C  
ATOM   3135  O   GLY A 405     -18.782  10.278 -17.235  1.00 35.37           O  
ANISOU 3135  O   GLY A 405     3991   5079   4368    289    -79   -621       O  
ATOM   3136  N   GLU A 406     -18.787  12.008 -18.674  1.00 44.77           N  
ANISOU 3136  N   GLU A 406     5129   6290   5592    223    -72   -646       N  
ATOM   3137  CA  GLU A 406     -18.068  11.253 -19.697  1.00 46.90           C  
ANISOU 3137  CA  GLU A 406     5386   6575   5860    244    -86   -655       C  
ATOM   3138  C   GLU A 406     -16.673  10.857 -19.228  1.00 44.07           C  
ANISOU 3138  C   GLU A 406     5008   6271   5466    285   -107   -673       C  
ATOM   3139  O   GLU A 406     -16.230   9.729 -19.473  1.00 51.05           O  
ANISOU 3139  O   GLU A 406     5901   7155   6342    329   -117   -670       O  
ATOM   3140  CB  GLU A 406     -17.990  12.059 -20.994  1.00 45.25           C  
ANISOU 3140  CB  GLU A 406     5151   6373   5670    205    -82   -669       C  
ATOM   3141  CG  GLU A 406     -19.335  12.284 -21.670  1.00 47.33           C  
ANISOU 3141  CG  GLU A 406     5431   6586   5968    174    -70   -650       C  
ATOM   3142  CD  GLU A 406     -19.985  10.995 -22.141  1.00 50.58           C  
ANISOU 3142  CD  GLU A 406     5869   6958   6393    192    -71   -633       C  
ATOM   3143  OE1 GLU A 406     -19.260  10.006 -22.380  1.00 54.67           O  
ANISOU 3143  OE1 GLU A 406     6392   7486   6894    225    -80   -640       O  
ATOM   3144  OE2 GLU A 406     -21.227  10.971 -22.272  1.00 49.43           O1-
ANISOU 3144  OE2 GLU A 406     5737   6770   6274    172    -62   -615       O1-
ATOM   3145  N   ILE A 407     -15.965  11.764 -18.549  1.00 41.65           N  
ANISOU 3145  N   ILE A 407     4674   6011   5138    272   -114   -692       N  
ATOM   3146  CA  ILE A 407     -14.613  11.467 -18.088  1.00 40.29           C  
ANISOU 3146  CA  ILE A 407     4474   5903   4933    309   -139   -712       C  
ATOM   3147  C   ILE A 407     -14.578  10.395 -17.012  1.00 43.09           C  
ANISOU 3147  C   ILE A 407     4862   6249   5261    367   -154   -692       C  
ATOM   3148  O   ILE A 407     -13.496   9.895 -16.685  1.00 54.09           O  
ANISOU 3148  O   ILE A 407     6235   7691   6627    413   -180   -703       O  
ATOM   3149  CB  ILE A 407     -13.913  12.740 -17.570  1.00 37.36           C  
ANISOU 3149  CB  ILE A 407     4066   5585   4543    273   -144   -740       C  
ATOM   3150  CG1 ILE A 407     -14.448  13.136 -16.194  1.00 42.62           C  
ANISOU 3150  CG1 ILE A 407     4764   6238   5191    266   -142   -729       C  
ATOM   3151  CG2 ILE A 407     -14.094  13.875 -18.551  1.00 32.57           C  
ANISOU 3151  CG2 ILE A 407     3442   4973   3960    212   -123   -754       C  
ATOM   3152  CD1 ILE A 407     -13.813  14.393 -15.636  1.00 39.66           C  
ANISOU 3152  CD1 ILE A 407     4362   5912   4796    225   -145   -758       C  
ATOM   3153  N   MET A 408     -15.731  10.034 -16.447  1.00 33.62           N  
ANISOU 3153  N   MET A 408     3715   4991   4069    366   -138   -663       N  
ATOM   3154  CA  MET A 408     -15.783   8.920 -15.508  1.00 37.82           C  
ANISOU 3154  CA  MET A 408     4293   5504   4575    419   -147   -641       C  
ATOM   3155  C   MET A 408     -15.816   7.588 -16.245  1.00 39.40           C  
ANISOU 3155  C   MET A 408     4516   5670   4784    460   -147   -627       C  
ATOM   3156  O   MET A 408     -15.094   6.652 -15.886  1.00 42.84           O  
ANISOU 3156  O   MET A 408     4965   6119   5192    521   -166   -623       O  
ATOM   3157  CB  MET A 408     -17.000   9.061 -14.595  1.00 32.84           C  
ANISOU 3157  CB  MET A 408     3710   4823   3946    396   -123   -617       C  
ATOM   3158  CG  MET A 408     -16.897  10.221 -13.628  1.00 34.50           C  
ANISOU 3158  CG  MET A 408     3910   5063   4136    367   -123   -630       C  
ATOM   3159  SD  MET A 408     -15.185  10.686 -13.319  1.00 58.48           S  
ANISOU 3159  SD  MET A 408     6895   8194   7133    386   -164   -664       S  
ATOM   3160  CE  MET A 408     -15.408  12.329 -12.653  1.00 26.18           C  
ANISOU 3160  CE  MET A 408     2793   4119   3036    321   -149   -683       C  
ATOM   3161  N   SER A 409     -16.651   7.488 -17.283  1.00 45.18           N  
ANISOU 3161  N   SER A 409     5256   6358   5553    427   -125   -622       N  
ATOM   3162  CA  SER A 409     -16.664   6.288 -18.109  1.00 43.42           C  
ANISOU 3162  CA  SER A 409     5057   6102   5339    457   -123   -614       C  
ATOM   3163  C   SER A 409     -15.350   6.113 -18.857  1.00 47.37           C  
ANISOU 3163  C   SER A 409     5515   6654   5830    491   -141   -640       C  
ATOM   3164  O   SER A 409     -14.950   4.979 -19.143  1.00 52.71           O  
ANISOU 3164  O   SER A 409     6213   7316   6497    541   -145   -636       O  
ATOM   3165  CB  SER A 409     -17.834   6.334 -19.090  1.00 48.83           C  
ANISOU 3165  CB  SER A 409     5754   6736   6063    408   -100   -607       C  
ATOM   3166  OG  SER A 409     -17.967   7.622 -19.667  1.00 55.70           O  
ANISOU 3166  OG  SER A 409     6581   7630   6954    357    -97   -622       O  
ATOM   3167  N   LEU A 410     -14.673   7.215 -19.189  1.00 44.81           N  
ANISOU 3167  N   LEU A 410     5132   6386   5507    461   -148   -667       N  
ATOM   3168  CA  LEU A 410     -13.366   7.118 -19.832  1.00 45.01           C  
ANISOU 3168  CA  LEU A 410     5109   6469   5524    489   -162   -694       C  
ATOM   3169  C   LEU A 410     -12.373   6.382 -18.942  1.00 45.88           C  
ANISOU 3169  C   LEU A 410     5215   6617   5600    563   -188   -695       C  
ATOM   3170  O   LEU A 410     -11.715   5.431 -19.379  1.00 49.60           O  
ANISOU 3170  O   LEU A 410     5685   7094   6065    619   -194   -699       O  
ATOM   3171  CB  LEU A 410     -12.846   8.515 -20.176  1.00 36.81           C  
ANISOU 3171  CB  LEU A 410     4012   5484   4490    436   -161   -724       C  
ATOM   3172  CG  LEU A 410     -13.598   9.293 -21.258  1.00 38.76           C  
ANISOU 3172  CG  LEU A 410     4260   5702   4768    371   -138   -726       C  
ATOM   3173  CD1 LEU A 410     -12.962  10.654 -21.489  1.00 33.61           C  
ANISOU 3173  CD1 LEU A 410     3556   5100   4112    322   -135   -755       C  
ATOM   3174  CD2 LEU A 410     -13.649   8.499 -22.553  1.00 40.37           C  
ANISOU 3174  CD2 LEU A 410     4475   5878   4985    381   -128   -727       C  
ATOM   3175  N   SER A 411     -12.260   6.804 -17.680  1.00 41.34           N  
ANISOU 3175  N   SER A 411     4640   6068   4999    568   -205   -690       N  
ATOM   3176  CA  SER A 411     -11.336   6.147 -16.762  1.00 43.28           C  
ANISOU 3176  CA  SER A 411     4883   6353   5207    640   -237   -689       C  
ATOM   3177  C   SER A 411     -11.824   4.754 -16.384  1.00 43.76           C  
ANISOU 3177  C   SER A 411     5020   6350   5257    699   -234   -654       C  
ATOM   3178  O   SER A 411     -11.022   3.819 -16.274  1.00 50.17           O  
ANISOU 3178  O   SER A 411     5835   7179   6049    775   -254   -652       O  
ATOM   3179  CB  SER A 411     -11.140   7.004 -15.511  1.00 38.20           C  
ANISOU 3179  CB  SER A 411     4227   5753   4536    623   -256   -694       C  
ATOM   3180  OG  SER A 411     -10.746   8.323 -15.849  1.00 40.72           O  
ANISOU 3180  OG  SER A 411     4484   6123   4864    561   -254   -727       O  
ATOM   3181  N   ALA A 412     -13.135   4.596 -16.184  1.00 40.81           N  
ANISOU 3181  N   ALA A 412     4707   5902   4895    665   -208   -627       N  
ATOM   3182  CA  ALA A 412     -13.670   3.310 -15.749  1.00 36.83           C  
ANISOU 3182  CA  ALA A 412     4283   5332   4378    710   -200   -594       C  
ATOM   3183  C   ALA A 412     -13.517   2.234 -16.817  1.00 40.26           C  
ANISOU 3183  C   ALA A 412     4737   5733   4828    745   -189   -594       C  
ATOM   3184  O   ALA A 412     -13.372   1.053 -16.485  1.00 42.03           O  
ANISOU 3184  O   ALA A 412     5017   5923   5032    809   -192   -574       O  
ATOM   3185  CB  ALA A 412     -15.140   3.458 -15.355  1.00 28.54           C  
ANISOU 3185  CB  ALA A 412     3286   4216   3344    656   -169   -570       C  
ATOM   3186  N   ALA A 413     -13.550   2.615 -18.096  1.00 48.36           N  
ANISOU 3186  N   ALA A 413     5724   6764   5887    705   -176   -616       N  
ATOM   3187  CA  ALA A 413     -13.477   1.646 -19.182  1.00 46.27           C  
ANISOU 3187  CA  ALA A 413     5482   6464   5636    729   -161   -619       C  
ATOM   3188  C   ALA A 413     -12.053   1.252 -19.548  1.00 46.54           C  
ANISOU 3188  C   ALA A 413     5474   6553   5656    797   -180   -641       C  
ATOM   3189  O   ALA A 413     -11.876   0.301 -20.318  1.00 55.35           O  
ANISOU 3189  O   ALA A 413     6617   7637   6777    832   -167   -643       O  
ATOM   3190  CB  ALA A 413     -14.180   2.189 -20.427  1.00 46.63           C  
ANISOU 3190  CB  ALA A 413     5510   6489   5718    655   -139   -632       C  
ATOM   3191  N   THR A 414     -11.046   1.949 -19.032  1.00 42.76           N  
ANISOU 3191  N   THR A 414     4930   6156   5161    815   -207   -660       N  
ATOM   3192  CA  THR A 414      -9.673   1.614 -19.376  1.00 44.13           C  
ANISOU 3192  CA  THR A 414     5051   6392   5325    880   -224   -684       C  
ATOM   3193  C   THR A 414      -9.328   0.220 -18.858  1.00 54.34           C  
ANISOU 3193  C   THR A 414     6400   7655   6592    979   -236   -662       C  
ATOM   3194  O   THR A 414      -9.812  -0.186 -17.797  1.00 50.26           O  
ANISOU 3194  O   THR A 414     5944   7102   6052   1001   -245   -630       O  
ATOM   3195  CB  THR A 414      -8.698   2.635 -18.791  1.00 40.95           C  
ANISOU 3195  CB  THR A 414     4565   6086   4907    875   -254   -709       C  
ATOM   3196  OG1 THR A 414      -8.918   2.758 -17.380  1.00 49.01           O  
ANISOU 3196  OG1 THR A 414     5612   7110   5897    888   -278   -687       O  
ATOM   3197  CG2 THR A 414      -8.884   3.989 -19.453  1.00 33.95           C  
ANISOU 3197  CG2 THR A 414     3626   5228   4045    782   -238   -735       C  
ATOM   3198  N   PRO A 415      -8.508  -0.540 -19.590  1.00 60.36           N  
ANISOU 3198  N   PRO A 415     7148   8429   7358   1041   -232   -677       N  
ATOM   3199  CA  PRO A 415      -8.096  -1.859 -19.085  1.00 56.02           C  
ANISOU 3199  CA  PRO A 415     6653   7850   6782   1145   -244   -656       C  
ATOM   3200  C   PRO A 415      -7.400  -1.791 -17.740  1.00 56.12           C  
ANISOU 3200  C   PRO A 415     6646   7920   6757   1207   -290   -645       C  
ATOM   3201  O   PRO A 415      -7.568  -2.703 -16.922  1.00 59.12           O  
ANISOU 3201  O   PRO A 415     7102   8254   7108   1271   -300   -611       O  
ATOM   3202  CB  PRO A 415      -7.156  -2.376 -20.184  1.00 58.57           C  
ANISOU 3202  CB  PRO A 415     6938   8198   7118   1196   -232   -684       C  
ATOM   3203  CG  PRO A 415      -7.549  -1.621 -21.408  1.00 53.34           C  
ANISOU 3203  CG  PRO A 415     6242   7535   6489   1104   -201   -710       C  
ATOM   3204  CD  PRO A 415      -7.972  -0.265 -20.933  1.00 41.70           C  
ANISOU 3204  CD  PRO A 415     4728   6097   5020   1019   -213   -713       C  
ATOM   3205  N   LYS A 416      -6.639  -0.724 -17.478  1.00 61.77           N  
ANISOU 3205  N   LYS A 416     7268   8733   7470   1186   -317   -672       N  
ATOM   3206  CA  LYS A 416      -5.969  -0.590 -16.189  1.00 67.11           C  
ANISOU 3206  CA  LYS A 416     7921   9471   8107   1238   -366   -665       C  
ATOM   3207  C   LYS A 416      -6.975  -0.553 -15.046  1.00 68.84           C  
ANISOU 3207  C   LYS A 416     8220   9635   8300   1212   -370   -628       C  
ATOM   3208  O   LYS A 416      -6.771  -1.193 -14.008  1.00 74.35           O  
ANISOU 3208  O   LYS A 416     8966  10328   8958   1284   -399   -600       O  
ATOM   3209  CB  LYS A 416      -5.100   0.669 -16.178  1.00 71.12           C  
ANISOU 3209  CB  LYS A 416     8313  10090   8618   1196   -390   -707       C  
ATOM   3210  CG  LYS A 416      -4.423   0.943 -14.844  1.00 71.93           C  
ANISOU 3210  CG  LYS A 416     8385  10266   8678   1236   -445   -705       C  
ATOM   3211  CD  LYS A 416      -4.334   2.435 -14.560  1.00 77.95           C  
ANISOU 3211  CD  LYS A 416     9080  11095   9441   1144   -454   -734       C  
ATOM   3212  CE  LYS A 416      -3.314   3.111 -15.461  1.00 72.26           C  
ANISOU 3212  CE  LYS A 416     8246  10463   8746   1118   -452   -785       C  
ATOM   3213  NZ  LYS A 416      -3.474   4.591 -15.469  1.00 65.38           N  
ANISOU 3213  NZ  LYS A 416     7328   9630   7884   1008   -442   -812       N  
ATOM   3214  N   HIS A 417      -8.070   0.192 -15.218  1.00 57.34           N  
ANISOU 3214  N   HIS A 417     6783   8138   6865   1113   -340   -625       N  
ATOM   3215  CA  HIS A 417      -9.105   0.222 -14.191  1.00 46.67           C  
ANISOU 3215  CA  HIS A 417     5508   6730   5493   1084   -334   -591       C  
ATOM   3216  C   HIS A 417      -9.821  -1.119 -14.087  1.00 46.01           C  
ANISOU 3216  C   HIS A 417     5534   6547   5402   1126   -311   -553       C  
ATOM   3217  O   HIS A 417     -10.098  -1.596 -12.981  1.00 54.49           O  
ANISOU 3217  O   HIS A 417     6677   7589   6437   1160   -321   -521       O  
ATOM   3218  CB  HIS A 417     -10.104   1.339 -14.482  1.00 46.03           C  
ANISOU 3218  CB  HIS A 417     5415   6632   5444    972   -304   -600       C  
ATOM   3219  CG  HIS A 417     -11.092   1.567 -13.381  1.00 46.54           C  
ANISOU 3219  CG  HIS A 417     5541   6653   5488    938   -295   -572       C  
ATOM   3220  ND1 HIS A 417     -10.803   2.325 -12.267  1.00 41.06           N  
ANISOU 3220  ND1 HIS A 417     4828   6011   4761    929   -323   -576       N  
ATOM   3221  CD2 HIS A 417     -12.366   1.136 -13.222  1.00 41.69           C  
ANISOU 3221  CD2 HIS A 417     5008   5951   4883    907   -260   -543       C  
ATOM   3222  CE1 HIS A 417     -11.855   2.351 -11.469  1.00 44.36           C  
ANISOU 3222  CE1 HIS A 417     5315   6372   5167    897   -302   -549       C  
ATOM   3223  NE2 HIS A 417     -12.818   1.638 -12.026  1.00 41.01           N  
ANISOU 3223  NE2 HIS A 417     4949   5864   4770    882   -263   -529       N  
ATOM   3224  N   LEU A 418     -10.132  -1.740 -15.227  1.00 45.47           N  
ANISOU 3224  N   LEU A 418     5486   6425   5364   1121   -278   -556       N  
ATOM   3225  CA  LEU A 418     -10.844  -3.013 -15.201  1.00 48.58           C  
ANISOU 3225  CA  LEU A 418     5988   6718   5751   1151   -251   -524       C  
ATOM   3226  C   LEU A 418      -9.978  -4.121 -14.614  1.00 50.48           C  
ANISOU 3226  C   LEU A 418     6271   6957   5951   1270   -277   -505       C  
ATOM   3227  O   LEU A 418     -10.485  -5.019 -13.932  1.00 55.33           O  
ANISOU 3227  O   LEU A 418     6986   7498   6538   1303   -267   -468       O  
ATOM   3228  CB  LEU A 418     -11.322  -3.380 -16.606  1.00 43.32           C  
ANISOU 3228  CB  LEU A 418     5333   6001   5125   1114   -212   -537       C  
ATOM   3229  CG  LEU A 418     -12.298  -2.389 -17.249  1.00 43.44           C  
ANISOU 3229  CG  LEU A 418     5317   6008   5179   1001   -186   -551       C  
ATOM   3230  CD1 LEU A 418     -12.497  -2.693 -18.728  1.00 45.25           C  
ANISOU 3230  CD1 LEU A 418     5544   6207   5443    973   -158   -570       C  
ATOM   3231  CD2 LEU A 418     -13.630  -2.395 -16.515  1.00 33.22           C  
ANISOU 3231  CD2 LEU A 418     4091   4648   3883    947   -165   -521       C  
ATOM   3232  N   LYS A 419      -8.669  -4.084 -14.878  1.00 59.61           N  
ANISOU 3232  N   LYS A 419     7352   8194   7105   1337   -309   -529       N  
ATOM   3233  CA  LYS A 419      -7.769  -5.058 -14.267  1.00 63.44           C  
ANISOU 3233  CA  LYS A 419     7866   8687   7550   1460   -341   -511       C  
ATOM   3234  C   LYS A 419      -7.683  -4.866 -12.758  1.00 65.33           C  
ANISOU 3234  C   LYS A 419     8131   8953   7740   1488   -382   -485       C  
ATOM   3235  O   LYS A 419      -7.673  -5.844 -12.001  1.00 70.22           O  
ANISOU 3235  O   LYS A 419     8838   9524   8318   1565   -392   -449       O  
ATOM   3236  CB  LYS A 419      -6.379  -4.962 -14.894  1.00 61.21           C  
ANISOU 3236  CB  LYS A 419     7481   8497   7279   1522   -367   -548       C  
ATOM   3237  CG  LYS A 419      -6.322  -5.385 -16.347  1.00 63.67           C  
ANISOU 3237  CG  LYS A 419     7783   8778   7631   1517   -326   -571       C  
ATOM   3238  CD  LYS A 419      -4.919  -5.809 -16.737  1.00 76.64           C  
ANISOU 3238  CD  LYS A 419     9360  10488   9273   1619   -347   -595       C  
ATOM   3239  CE  LYS A 419      -4.895  -6.366 -18.148  1.00 89.27           C  
ANISOU 3239  CE  LYS A 419    10967  12046  10906   1620   -301   -616       C  
ATOM   3240  NZ  LYS A 419      -3.585  -6.147 -18.824  1.00 93.23           N  
ANISOU 3240  NZ  LYS A 419    11356  12642  11423   1667   -311   -659       N  
ATOM   3241  N   SER A 420      -7.627  -3.613 -12.303  1.00 55.15           N  
ANISOU 3241  N   SER A 420     6770   7735   6448   1424   -403   -504       N  
ATOM   3242  CA  SER A 420      -7.439  -3.337 -10.884  1.00 59.40           C  
ANISOU 3242  CA  SER A 420     7325   8310   6935   1448   -445   -485       C  
ATOM   3243  C   SER A 420      -8.649  -3.720 -10.042  1.00 58.94           C  
ANISOU 3243  C   SER A 420     7387   8157   6851   1419   -418   -443       C  
ATOM   3244  O   SER A 420      -8.523  -3.834  -8.818  1.00 69.86           O  
ANISOU 3244  O   SER A 420     8814   9549   8181   1458   -449   -418       O  
ATOM   3245  CB  SER A 420      -7.113  -1.856 -10.676  1.00 60.64           C  
ANISOU 3245  CB  SER A 420     7380   8563   7098   1376   -468   -520       C  
ATOM   3246  OG  SER A 420      -8.256  -1.046 -10.883  1.00 57.44           O  
ANISOU 3246  OG  SER A 420     6986   8117   6721   1263   -426   -524       O  
ATOM   3247  N   ILE A 421      -9.811  -3.924 -10.660  1.00 54.71           N  
ANISOU 3247  N   ILE A 421     6904   7533   6350   1351   -361   -434       N  
ATOM   3248  CA  ILE A 421     -11.033  -4.251  -9.937  1.00 54.64           C  
ANISOU 3248  CA  ILE A 421     7002   7435   6324   1312   -327   -398       C  
ATOM   3249  C   ILE A 421     -11.471  -5.689 -10.182  1.00 52.86           C  
ANISOU 3249  C   ILE A 421     6886   7104   6092   1357   -294   -368       C  
ATOM   3250  O   ILE A 421     -12.602  -6.054  -9.844  1.00 54.79           O  
ANISOU 3250  O   ILE A 421     7220   7265   6334   1310   -252   -342       O  
ATOM   3251  CB  ILE A 421     -12.164  -3.268 -10.278  1.00 56.48           C  
ANISOU 3251  CB  ILE A 421     7211   7650   6598   1188   -286   -413       C  
ATOM   3252  CG1 ILE A 421     -12.550  -3.390 -11.752  1.00 53.37           C  
ANISOU 3252  CG1 ILE A 421     6792   7224   6262   1145   -250   -433       C  
ATOM   3253  CG2 ILE A 421     -11.749  -1.843  -9.945  1.00 46.01           C  
ANISOU 3253  CG2 ILE A 421     5791   6419   5273   1144   -316   -441       C  
ATOM   3254  CD1 ILE A 421     -13.780  -2.600 -12.122  1.00 51.71           C  
ANISOU 3254  CD1 ILE A 421     6571   6985   6093   1032   -211   -440       C  
ATOM   3255  N   GLY A 422     -10.608  -6.516 -10.766  1.00 60.48           N  
ANISOU 3255  N   GLY A 422     7848   8072   7057   1444   -307   -372       N  
ATOM   3256  CA  GLY A 422     -10.905  -7.924 -10.932  1.00 65.08           C  
ANISOU 3256  CA  GLY A 422     8544   8554   7628   1497   -278   -343       C  
ATOM   3257  C   GLY A 422     -11.872  -8.264 -12.043  1.00 63.54           C  
ANISOU 3257  C   GLY A 422     8381   8279   7481   1424   -219   -352       C  
ATOM   3258  O   GLY A 422     -12.338  -9.408 -12.103  1.00 58.86           O  
ANISOU 3258  O   GLY A 422     7896   7590   6877   1447   -186   -327       O  
ATOM   3259  N   LEU A 423     -12.201  -7.312 -12.915  1.00 51.97           N  
ANISOU 3259  N   LEU A 423     6831   6852   6066   1335   -205   -386       N  
ATOM   3260  CA  LEU A 423     -13.062  -7.583 -14.058  1.00 45.79           C  
ANISOU 3260  CA  LEU A 423     6067   6003   5326   1266   -157   -398       C  
ATOM   3261  C   LEU A 423     -12.284  -7.924 -15.319  1.00 52.62           C  
ANISOU 3261  C   LEU A 423     6889   6887   6217   1305   -157   -427       C  
ATOM   3262  O   LEU A 423     -12.893  -8.320 -16.319  1.00 60.12           O  
ANISOU 3262  O   LEU A 423     7866   7779   7196   1259   -119   -437       O  
ATOM   3263  CB  LEU A 423     -13.968  -6.381 -14.336  1.00 48.79           C  
ANISOU 3263  CB  LEU A 423     6387   6405   5744   1147   -141   -415       C  
ATOM   3264  CG  LEU A 423     -15.111  -6.169 -13.346  1.00 48.34           C  
ANISOU 3264  CG  LEU A 423     6387   6304   5675   1086   -119   -389       C  
ATOM   3265  CD1 LEU A 423     -16.089  -5.142 -13.890  1.00 45.74           C  
ANISOU 3265  CD1 LEU A 423     6002   5984   5394    974    -96   -408       C  
ATOM   3266  CD2 LEU A 423     -15.807  -7.487 -13.040  1.00 42.78           C  
ANISOU 3266  CD2 LEU A 423     5812   5492   4951   1101    -82   -356       C  
ATOM   3267  N   LEU A 424     -10.961  -7.781 -15.295  1.00 53.26           N  
ANISOU 3267  N   LEU A 424     6901   7048   6285   1386   -198   -443       N  
ATOM   3268  CA  LEU A 424     -10.112  -8.096 -16.437  1.00 52.28           C  
ANISOU 3268  CA  LEU A 424     6732   6949   6184   1431   -195   -472       C  
ATOM   3269  C   LEU A 424      -8.895  -8.843 -15.918  1.00 63.45           C  
ANISOU 3269  C   LEU A 424     8153   8391   7562   1567   -230   -462       C  
ATOM   3270  O   LEU A 424      -8.190  -8.341 -15.037  1.00 57.46           O  
ANISOU 3270  O   LEU A 424     7342   7711   6778   1609   -277   -459       O  
ATOM   3271  CB  LEU A 424      -9.696  -6.824 -17.183  1.00 48.31           C  
ANISOU 3271  CB  LEU A 424     6100   6541   5716   1373   -207   -515       C  
ATOM   3272  CG  LEU A 424      -9.326  -6.955 -18.661  1.00 54.30           C  
ANISOU 3272  CG  LEU A 424     6819   7305   6508   1366   -183   -550       C  
ATOM   3273  CD1 LEU A 424     -10.291  -7.884 -19.382  1.00 55.65           C  
ANISOU 3273  CD1 LEU A 424     7088   7365   6691   1334   -136   -540       C  
ATOM   3274  CD2 LEU A 424      -9.307  -5.585 -19.318  1.00 49.36           C  
ANISOU 3274  CD2 LEU A 424     6089   6752   5915   1278   -185   -585       C  
ATOM   3275  N   SER A 425      -8.657 -10.035 -16.454  1.00 66.25           N  
ANISOU 3275  N   SER A 425     8574   8683   7914   1637   -207   -457       N  
ATOM   3276  CA  SER A 425      -7.572 -10.866 -15.955  1.00 70.96           C  
ANISOU 3276  CA  SER A 425     9190   9294   8476   1778   -238   -442       C  
ATOM   3277  C   SER A 425      -6.224 -10.199 -16.223  1.00 74.17           C  
ANISOU 3277  C   SER A 425     9458   9828   8894   1828   -278   -479       C  
ATOM   3278  O   SER A 425      -6.043  -9.558 -17.263  1.00 79.27           O  
ANISOU 3278  O   SER A 425    10019  10520   9580   1772   -263   -519       O  
ATOM   3279  CB  SER A 425      -7.608 -12.245 -16.612  1.00 76.90           C  
ANISOU 3279  CB  SER A 425    10043   9947   9228   1838   -198   -434       C  
ATOM   3280  OG  SER A 425      -6.571 -13.074 -16.115  1.00 86.20           O  
ANISOU 3280  OG  SER A 425    11245  11134  10372   1984   -227   -417       O  
ATOM   3281  N   PRO A 426      -5.268 -10.317 -15.300  1.00 73.85           N  
ANISOU 3281  N   PRO A 426     9391   9850   8818   1930   -331   -466       N  
ATOM   3282  CA  PRO A 426      -3.906  -9.843 -15.594  1.00 80.96           C  
ANISOU 3282  CA  PRO A 426    10157  10874   9730   1988   -368   -504       C  
ATOM   3283  C   PRO A 426      -3.262 -10.572 -16.758  1.00 82.81           C  
ANISOU 3283  C   PRO A 426    10377  11095   9991   2052   -338   -529       C  
ATOM   3284  O   PRO A 426      -2.315 -10.043 -17.354  1.00 82.27           O  
ANISOU 3284  O   PRO A 426    10188  11125   9948   2066   -350   -571       O  
ATOM   3285  CB  PRO A 426      -3.153 -10.097 -14.281  1.00 80.48           C  
ANISOU 3285  CB  PRO A 426    10099  10862   9619   2097   -432   -476       C  
ATOM   3286  CG  PRO A 426      -4.222 -10.138 -13.233  1.00 70.02           C  
ANISOU 3286  CG  PRO A 426     8882   9466   8259   2050   -430   -432       C  
ATOM   3287  CD  PRO A 426      -5.410 -10.761 -13.903  1.00 69.05           C  
ANISOU 3287  CD  PRO A 426     8867   9213   8156   1987   -362   -419       C  
ATOM   3288  N   ASP A 427      -3.741 -11.774 -17.096  1.00121.81           N  
ANISOU 3288  N   ASP A 427    15439  15917  14925   2090   -298   -507       N  
ATOM   3289  CA  ASP A 427      -3.266 -12.458 -18.294  1.00127.45           C  
ANISOU 3289  CA  ASP A 427    16153  16608  15666   2138   -259   -534       C  
ATOM   3290  C   ASP A 427      -3.535 -11.635 -19.545  1.00126.84           C  
ANISOU 3290  C   ASP A 427    16002  16558  15635   2022   -223   -579       C  
ATOM   3291  O   ASP A 427      -2.754 -11.685 -20.503  1.00129.57           O  
ANISOU 3291  O   ASP A 427    16282  16944  16004   2054   -206   -617       O  
ATOM   3292  CB  ASP A 427      -3.931 -13.830 -18.416  1.00119.01           C  
ANISOU 3292  CB  ASP A 427    15245  15394  14581   2175   -216   -502       C  
ATOM   3293  CG  ASP A 427      -3.612 -14.741 -17.247  1.00126.22           C  
ANISOU 3293  CG  ASP A 427    16244  16270  15443   2300   -247   -455       C  
ATOM   3294  OD1 ASP A 427      -2.511 -14.612 -16.672  1.00127.66           O  
ANISOU 3294  OD1 ASP A 427    16351  16544  15609   2401   -301   -455       O  
ATOM   3295  OD2 ASP A 427      -4.465 -15.586 -16.903  1.00117.31           O1-
ANISOU 3295  OD2 ASP A 427    15260  15021  14291   2296   -218   -417       O1-
ATOM   3296  N   PHE A 428      -4.636 -10.883 -19.559  1.00113.77           N  
ANISOU 3296  N   PHE A 428    14358  14879  13991   1891   -210   -576       N  
ATOM   3297  CA  PHE A 428      -4.939 -10.004 -20.679  1.00110.38           C  
ANISOU 3297  CA  PHE A 428    13862  14478  13601   1780   -182   -614       C  
ATOM   3298  C   PHE A 428      -3.817  -8.991 -20.866  1.00114.89           C  
ANISOU 3298  C   PHE A 428    14282  15183  14187   1785   -210   -654       C  
ATOM   3299  O   PHE A 428      -3.329  -8.398 -19.900  1.00112.60           O  
ANISOU 3299  O   PHE A 428    13931  14973  13881   1806   -258   -649       O  
ATOM   3300  CB  PHE A 428      -6.274  -9.293 -20.436  1.00106.47           C  
ANISOU 3300  CB  PHE A 428    13397  13944  13112   1651   -173   -599       C  
ATOM   3301  CG  PHE A 428      -6.814  -8.560 -21.638  1.00109.00           C  
ANISOU 3301  CG  PHE A 428    13678  14267  13470   1537   -140   -631       C  
ATOM   3302  CD1 PHE A 428      -6.256  -7.359 -22.051  1.00107.30           C  
ANISOU 3302  CD1 PHE A 428    13341  14152  13274   1490   -153   -666       C  
ATOM   3303  CD2 PHE A 428      -7.889  -9.069 -22.347  1.00105.35           C  
ANISOU 3303  CD2 PHE A 428    13302  13706  13020   1474    -98   -625       C  
ATOM   3304  CE1 PHE A 428      -6.754  -6.688 -23.152  1.00105.48           C  
ANISOU 3304  CE1 PHE A 428    13084  13921  13074   1389   -125   -692       C  
ATOM   3305  CE2 PHE A 428      -8.392  -8.402 -23.448  1.00 98.84           C  
ANISOU 3305  CE2 PHE A 428    12444  12886  12225   1373    -74   -652       C  
ATOM   3306  CZ  PHE A 428      -7.823  -7.211 -23.851  1.00 99.82           C  
ANISOU 3306  CZ  PHE A 428    12452  13107  12366   1334    -87   -684       C  
ATOM   3307  N   GLN A 429      -3.395  -8.810 -22.114  1.00110.40           N  
ANISOU 3307  N   GLN A 429    13658  14642  13648   1764   -179   -695       N  
ATOM   3308  CA  GLN A 429      -2.396  -7.810 -22.468  1.00117.42           C  
ANISOU 3308  CA  GLN A 429    14405  15655  14555   1750   -194   -738       C  
ATOM   3309  C   GLN A 429      -2.898  -7.046 -23.681  1.00112.67           C  
ANISOU 3309  C   GLN A 429    13776  15049  13984   1630   -154   -769       C  
ATOM   3310  O   GLN A 429      -3.186  -7.648 -24.721  1.00102.99           O  
ANISOU 3310  O   GLN A 429    12603  13758  12770   1620   -109   -780       O  
ATOM   3311  CB  GLN A 429      -1.037  -8.455 -22.756  1.00120.95           C  
ANISOU 3311  CB  GLN A 429    14797  16156  15003   1874   -197   -762       C  
ATOM   3312  CG  GLN A 429       0.124  -7.475 -22.739  1.00121.27           C  
ANISOU 3312  CG  GLN A 429    14683  16338  15054   1876   -224   -802       C  
ATOM   3313  CD  GLN A 429       0.479  -7.017 -21.338  1.00122.19           C  
ANISOU 3313  CD  GLN A 429    14754  16527  15146   1906   -290   -784       C  
ATOM   3314  OE1 GLN A 429       0.544  -7.820 -20.407  1.00117.16           O  
ANISOU 3314  OE1 GLN A 429    14177  15860  14478   2001   -322   -747       O  
ATOM   3315  NE2 GLN A 429       0.711  -5.719 -21.180  1.00115.17           N  
ANISOU 3315  NE2 GLN A 429    13765  15730  14264   1824   -310   -809       N  
ATOM   3316  N   GLU A 430      -3.006  -5.728 -23.548  1.00 93.87           N  
ANISOU 3316  N   GLU A 430    11319  12734  11612   1539   -170   -783       N  
ATOM   3317  CA  GLU A 430      -3.491  -4.895 -24.639  1.00 84.62           C  
ANISOU 3317  CA  GLU A 430    10124  11562  10466   1425   -136   -809       C  
ATOM   3318  C   GLU A 430      -2.370  -4.676 -25.648  1.00 82.77           C  
ANISOU 3318  C   GLU A 430     9800  11401  10248   1442   -114   -857       C  
ATOM   3319  O   GLU A 430      -1.281  -4.215 -25.289  1.00 88.93           O  
ANISOU 3319  O   GLU A 430    10478  12282  11027   1479   -139   -880       O  
ATOM   3320  CB  GLU A 430      -4.012  -3.561 -24.105  1.00 86.70           C  
ANISOU 3320  CB  GLU A 430    10346  11863  10732   1326   -159   -805       C  
ATOM   3321  CG  GLU A 430      -3.070  -2.854 -23.140  1.00 86.42           C  
ANISOU 3321  CG  GLU A 430    10216  11936  10685   1355   -204   -815       C  
ATOM   3322  CD  GLU A 430      -3.685  -2.635 -21.773  1.00 86.21           C  
ANISOU 3322  CD  GLU A 430    10227  11893  10634   1346   -241   -779       C  
ATOM   3323  OE1 GLU A 430      -4.272  -3.591 -21.223  1.00 88.47           O  
ANISOU 3323  OE1 GLU A 430    10610  12101  10904   1393   -243   -741       O  
ATOM   3324  OE2 GLU A 430      -3.580  -1.507 -21.247  1.00 83.92           O1-
ANISOU 3324  OE2 GLU A 430     9876  11668  10342   1290   -264   -789       O1-
ATOM   3325  N   ASP A 431      -2.629  -5.022 -26.903  1.00 94.17           N  
ANISOU 3325  N   ASP A 431    11281  12794  11705   1413    -67   -874       N  
ATOM   3326  CA  ASP A 431      -1.709  -4.742 -27.992  1.00 98.27           C  
ANISOU 3326  CA  ASP A 431    11725  13374  12239   1410    -36   -922       C  
ATOM   3327  C   ASP A 431      -2.130  -3.459 -28.700  1.00 90.71           C  
ANISOU 3327  C   ASP A 431    10730  12442  11296   1280    -20   -941       C  
ATOM   3328  O   ASP A 431      -3.190  -2.891 -28.431  1.00 89.28           O  
ANISOU 3328  O   ASP A 431    10586  12221  11113   1200    -32   -917       O  
ATOM   3329  CB  ASP A 431      -1.653  -5.917 -28.975  1.00 99.37           C  
ANISOU 3329  CB  ASP A 431    11932  13443  12379   1461     10   -932       C  
ATOM   3330  CG  ASP A 431      -2.991  -6.193 -29.632  1.00 95.01           C  
ANISOU 3330  CG  ASP A 431    11489  12783  11827   1383     37   -915       C  
ATOM   3331  OD1 ASP A 431      -4.030  -5.826 -29.047  1.00 92.70           O  
ANISOU 3331  OD1 ASP A 431    11238  12452  11532   1320     15   -883       O  
ATOM   3332  OD2 ASP A 431      -3.003  -6.779 -30.735  1.00100.48           O1-
ANISOU 3332  OD2 ASP A 431    12226  13430  12522   1383     80   -934       O1-
ATOM   3333  N   ASN A 432      -1.279  -3.003 -29.621  1.00 83.51           N  
ANISOU 3333  N   ASN A 432     9742  11594  10394   1263      9   -986       N  
ATOM   3334  CA  ASN A 432      -1.554  -1.748 -30.312  1.00 76.99           C  
ANISOU 3334  CA  ASN A 432     8881  10796   9577   1144     26  -1005       C  
ATOM   3335  C   ASN A 432      -2.796  -1.827 -31.190  1.00 75.50           C  
ANISOU 3335  C   ASN A 432     8787  10511   9388   1067     52   -990       C  
ATOM   3336  O   ASN A 432      -3.325  -0.784 -31.589  1.00 75.19           O  
ANISOU 3336  O   ASN A 432     8739  10477   9354    967     56   -993       O  
ATOM   3337  CB  ASN A 432      -0.349  -1.323 -31.156  1.00 84.66           C  
ANISOU 3337  CB  ASN A 432     9758  11852  10557   1142     58  -1056       C  
ATOM   3338  CG  ASN A 432       0.163  -2.431 -32.062  1.00100.47           C  
ANISOU 3338  CG  ASN A 432    11787  13828  12560   1213    101  -1078       C  
ATOM   3339  OD1 ASN A 432      -0.086  -3.613 -31.826  1.00 96.87           O  
ANISOU 3339  OD1 ASN A 432    11404  13304  12098   1292     99  -1055       O  
ATOM   3340  ND2 ASN A 432       0.887  -2.042 -33.109  1.00117.25           N  
ANISOU 3340  ND2 ASN A 432    13856  16001  14691   1184    145  -1122       N  
ATOM   3341  N   GLU A 433      -3.276  -3.033 -31.493  1.00 73.01           N  
ANISOU 3341  N   GLU A 433     8563  10109   9067   1111     68   -975       N  
ATOM   3342  CA  GLU A 433      -4.421  -3.169 -32.385  1.00 68.27           C  
ANISOU 3342  CA  GLU A 433     8050   9423   8466   1037     90   -966       C  
ATOM   3343  C   GLU A 433      -5.742  -2.972 -31.649  1.00 59.24           C  
ANISOU 3343  C   GLU A 433     6963   8222   7322    986     60   -924       C  
ATOM   3344  O   GLU A 433      -6.659  -2.336 -32.181  1.00 57.59           O  
ANISOU 3344  O   GLU A 433     6778   7986   7118    893     64   -918       O  
ATOM   3345  CB  GLU A 433      -4.382  -4.533 -33.073  1.00 65.51           C  
ANISOU 3345  CB  GLU A 433     7777   9004   8108   1096    124   -972       C  
ATOM   3346  CG  GLU A 433      -3.575  -4.532 -34.361  1.00 69.12           C  
ANISOU 3346  CG  GLU A 433     8204   9491   8565   1095    171  -1018       C  
ATOM   3347  CD  GLU A 433      -3.587  -5.872 -35.066  1.00 77.73           C  
ANISOU 3347  CD  GLU A 433     9380  10506   9646   1150    208  -1026       C  
ATOM   3348  OE1 GLU A 433      -4.318  -6.777 -34.613  1.00 76.91           O  
ANISOU 3348  OE1 GLU A 433     9365  10320   9536   1178    198   -996       O  
ATOM   3349  OE2 GLU A 433      -2.863  -6.019 -36.073  1.00 77.88           O1-
ANISOU 3349  OE2 GLU A 433     9382  10547   9663   1162    251  -1064       O1-
ATOM   3350  N   THR A 434      -5.864  -3.507 -30.431  1.00 63.97           N  
ANISOU 3350  N   THR A 434     7585   8804   7916   1046     32   -894       N  
ATOM   3351  CA  THR A 434      -7.092  -3.307 -29.666  1.00 64.44           C  
ANISOU 3351  CA  THR A 434     7695   8814   7976    998      8   -855       C  
ATOM   3352  C   THR A 434      -7.270  -1.850 -29.261  1.00 64.13           C  
ANISOU 3352  C   THR A 434     7589   8832   7944    924    -14   -854       C  
ATOM   3353  O   THR A 434      -8.406  -1.385 -29.114  1.00 61.81           O  
ANISOU 3353  O   THR A 434     7328   8499   7657    854    -22   -833       O  
ATOM   3354  CB  THR A 434      -7.108  -4.205 -28.428  1.00 61.39           C  
ANISOU 3354  CB  THR A 434     7352   8396   7576   1081    -14   -824       C  
ATOM   3355  OG1 THR A 434      -5.913  -3.998 -27.664  1.00 65.51           O  
ANISOU 3355  OG1 THR A 434     7796   9003   8091   1153    -39   -833       O  
ATOM   3356  CG2 THR A 434      -7.213  -5.669 -28.829  1.00 66.40           C  
ANISOU 3356  CG2 THR A 434     8077   8949   8202   1142     12   -818       C  
ATOM   3357  N   GLU A 435      -6.169  -1.120 -29.066  1.00 65.82           N  
ANISOU 3357  N   GLU A 435     7709   9140   8159    939    -24   -880       N  
ATOM   3358  CA  GLU A 435      -6.274   0.312 -28.806  1.00 61.09           C  
ANISOU 3358  CA  GLU A 435     7051   8594   7566    862    -38   -885       C  
ATOM   3359  C   GLU A 435      -6.822   1.050 -30.021  1.00 60.80           C  
ANISOU 3359  C   GLU A 435     7023   8540   7539    768    -13   -898       C  
ATOM   3360  O   GLU A 435      -7.665   1.945 -29.884  1.00 65.13           O  
ANISOU 3360  O   GLU A 435     7578   9074   8093    694    -22   -883       O  
ATOM   3361  CB  GLU A 435      -4.911   0.875 -28.402  1.00 67.44           C  
ANISOU 3361  CB  GLU A 435     7753   9504   8367    894    -51   -914       C  
ATOM   3362  CG  GLU A 435      -4.129  -0.004 -27.436  1.00 77.05           C  
ANISOU 3362  CG  GLU A 435     8955  10748   9571   1005    -77   -908       C  
ATOM   3363  CD  GLU A 435      -4.508   0.224 -25.984  1.00 85.02           C  
ANISOU 3363  CD  GLU A 435     9973  11761  10568   1014   -119   -876       C  
ATOM   3364  OE1 GLU A 435      -5.666   0.609 -25.715  1.00 87.76           O  
ANISOU 3364  OE1 GLU A 435    10371  12054  10918    951   -122   -850       O  
ATOM   3365  OE2 GLU A 435      -3.643   0.015 -25.108  1.00 95.29           O1-
ANISOU 3365  OE2 GLU A 435    11229  13120  11856   1087   -149   -879       O1-
ATOM   3366  N   ILE A 436      -6.351   0.692 -31.218  1.00 55.31           N  
ANISOU 3366  N   ILE A 436     6329   7843   6842    772     21   -925       N  
ATOM   3367  CA  ILE A 436      -6.881   1.292 -32.439  1.00 48.47           C  
ANISOU 3367  CA  ILE A 436     5483   6956   5979    687     45   -936       C  
ATOM   3368  C   ILE A 436      -8.345   0.914 -32.621  1.00 51.56           C  
ANISOU 3368  C   ILE A 436     5962   7256   6372    648     39   -904       C  
ATOM   3369  O   ILE A 436      -9.177   1.751 -32.995  1.00 50.95           O  
ANISOU 3369  O   ILE A 436     5896   7163   6300    569     35   -895       O  
ATOM   3370  CB  ILE A 436      -6.026   0.879 -33.652  1.00 49.46           C  
ANISOU 3370  CB  ILE A 436     5598   7098   6098    706     85   -973       C  
ATOM   3371  CG1 ILE A 436      -4.765   1.740 -33.725  1.00 52.06           C  
ANISOU 3371  CG1 ILE A 436     5828   7524   6428    701     96  -1009       C  
ATOM   3372  CG2 ILE A 436      -6.822   0.998 -34.944  1.00 48.62           C  
ANISOU 3372  CG2 ILE A 436     5551   6937   5986    634    108   -975       C  
ATOM   3373  CD1 ILE A 436      -5.041   3.225 -33.681  1.00 52.11           C  
ANISOU 3373  CD1 ILE A 436     5799   7562   6436    610     88  -1008       C  
ATOM   3374  N   ASN A 437      -8.683  -0.351 -32.356  1.00 54.80           N  
ANISOU 3374  N   ASN A 437     6435   7606   6779    703     39   -888       N  
ATOM   3375  CA  ASN A 437     -10.080  -0.772 -32.401  1.00 54.42           C  
ANISOU 3375  CA  ASN A 437     6468   7476   6735    664     33   -859       C  
ATOM   3376  C   ASN A 437     -10.929   0.044 -31.436  1.00 54.46           C  
ANISOU 3376  C   ASN A 437     6460   7481   6750    620      4   -830       C  
ATOM   3377  O   ASN A 437     -12.034   0.480 -31.781  1.00 51.19           O  
ANISOU 3377  O   ASN A 437     6073   7032   6345    551     -1   -816       O  
ATOM   3378  CB  ASN A 437     -10.188  -2.262 -32.070  1.00 53.29           C  
ANISOU 3378  CB  ASN A 437     6393   7270   6583    733     40   -847       C  
ATOM   3379  CG  ASN A 437     -10.235  -3.135 -33.306  1.00 54.97           C  
ANISOU 3379  CG  ASN A 437     6665   7434   6788    733     72   -866       C  
ATOM   3380  OD1 ASN A 437     -10.097  -2.652 -34.428  1.00 54.63           O  
ANISOU 3380  OD1 ASN A 437     6607   7408   6741    686     88   -890       O  
ATOM   3381  ND2 ASN A 437     -10.434  -4.432 -33.105  1.00 68.03           N  
ANISOU 3381  ND2 ASN A 437     8392   9022   8434    785     82   -856       N  
ATOM   3382  N   PHE A 438     -10.428   0.259 -30.218  1.00 51.09           N  
ANISOU 3382  N   PHE A 438     5994   7096   6322    663    -16   -821       N  
ATOM   3383  CA  PHE A 438     -11.160   1.049 -29.235  1.00 43.40           C  
ANISOU 3383  CA  PHE A 438     5010   6124   5355    625    -39   -796       C  
ATOM   3384  C   PHE A 438     -11.255   2.510 -29.660  1.00 39.17           C  
ANISOU 3384  C   PHE A 438     4425   5629   4828    549    -41   -808       C  
ATOM   3385  O   PHE A 438     -12.334   3.112 -29.611  1.00 38.51           O  
ANISOU 3385  O   PHE A 438     4360   5516   4756    490    -47   -789       O  
ATOM   3386  CB  PHE A 438     -10.486   0.923 -27.868  1.00 43.88           C  
ANISOU 3386  CB  PHE A 438     5043   6224   5406    690    -61   -788       C  
ATOM   3387  CG  PHE A 438     -10.981   1.910 -26.850  1.00 42.67           C  
ANISOU 3387  CG  PHE A 438     4868   6090   5256    651    -82   -771       C  
ATOM   3388  CD1 PHE A 438     -12.147   1.669 -26.144  1.00 39.05           C  
ANISOU 3388  CD1 PHE A 438     4464   5572   4801    635    -88   -738       C  
ATOM   3389  CD2 PHE A 438     -10.275   3.074 -26.590  1.00 41.21           C  
ANISOU 3389  CD2 PHE A 438     4609   5979   5070    629    -92   -790       C  
ATOM   3390  CE1 PHE A 438     -12.604   2.572 -25.204  1.00 32.58           C  
ANISOU 3390  CE1 PHE A 438     3626   4768   3984    601   -102   -724       C  
ATOM   3391  CE2 PHE A 438     -10.727   3.982 -25.653  1.00 42.50           C  
ANISOU 3391  CE2 PHE A 438     4758   6155   5234    593   -109   -776       C  
ATOM   3392  CZ  PHE A 438     -11.893   3.730 -24.958  1.00 33.89           C  
ANISOU 3392  CZ  PHE A 438     3724   5006   4147    582   -113   -743       C  
ATOM   3393  N   LEU A 439     -10.131   3.096 -30.081  1.00 37.20           N  
ANISOU 3393  N   LEU A 439     4114   5447   4574    551    -32   -839       N  
ATOM   3394  CA  LEU A 439     -10.124   4.508 -30.453  1.00 30.39           C  
ANISOU 3394  CA  LEU A 439     3209   4621   3715    479    -29   -851       C  
ATOM   3395  C   LEU A 439     -10.988   4.765 -31.681  1.00 31.03           C  
ANISOU 3395  C   LEU A 439     3332   4657   3801    415    -15   -848       C  
ATOM   3396  O   LEU A 439     -11.643   5.809 -31.776  1.00 32.25           O  
ANISOU 3396  O   LEU A 439     3483   4807   3962    353    -21   -838       O  
ATOM   3397  CB  LEU A 439      -8.690   4.980 -30.691  1.00 30.32           C  
ANISOU 3397  CB  LEU A 439     3127   4694   3699    491    -17   -888       C  
ATOM   3398  CG  LEU A 439      -7.867   5.227 -29.426  1.00 34.49           C  
ANISOU 3398  CG  LEU A 439     3596   5286   4222    531    -39   -894       C  
ATOM   3399  CD1 LEU A 439      -6.398   5.418 -29.765  1.00 40.69           C  
ANISOU 3399  CD1 LEU A 439     4306   6153   5001    552    -25   -936       C  
ATOM   3400  CD2 LEU A 439      -8.408   6.428 -28.665  1.00 32.64           C  
ANISOU 3400  CD2 LEU A 439     3349   5061   3991    474    -56   -881       C  
ATOM   3401  N   LEU A 440     -10.992   3.832 -32.636  1.00 40.57           N  
ANISOU 3401  N   LEU A 440     4580   5831   5003    430      2   -857       N  
ATOM   3402  CA  LEU A 440     -11.872   3.968 -33.792  1.00 36.51           C  
ANISOU 3402  CA  LEU A 440     4112   5272   4489    371      9   -853       C  
ATOM   3403  C   LEU A 440     -13.334   3.975 -33.365  1.00 37.47           C  
ANISOU 3403  C   LEU A 440     4274   5338   4624    339    -13   -818       C  
ATOM   3404  O   LEU A 440     -14.129   4.782 -33.859  1.00 39.40           O  
ANISOU 3404  O   LEU A 440     4526   5570   4874    279    -20   -808       O  
ATOM   3405  CB  LEU A 440     -11.603   2.841 -34.792  1.00 37.39           C  
ANISOU 3405  CB  LEU A 440     4266   5354   4587    397     32   -870       C  
ATOM   3406  CG  LEU A 440     -12.284   2.887 -36.165  1.00 41.21           C  
ANISOU 3406  CG  LEU A 440     4797   5799   5061    338     41   -874       C  
ATOM   3407  CD1 LEU A 440     -13.622   2.150 -36.157  1.00 36.44           C  
ANISOU 3407  CD1 LEU A 440     4259   5123   4464    322     25   -849       C  
ATOM   3408  CD2 LEU A 440     -12.455   4.320 -36.653  1.00 34.08           C  
ANISOU 3408  CD2 LEU A 440     3869   4924   4157    270     38   -875       C  
ATOM   3409  N   LYS A 441     -13.705   3.083 -32.443  1.00 44.91           N  
ANISOU 3409  N   LYS A 441     5243   6248   5572    381    -22   -799       N  
ATOM   3410  CA  LYS A 441     -15.074   3.073 -31.938  1.00 41.11           C  
ANISOU 3410  CA  LYS A 441     4795   5718   5106    350    -38   -768       C  
ATOM   3411  C   LYS A 441     -15.396   4.371 -31.210  1.00 43.95           C  
ANISOU 3411  C   LYS A 441     5114   6108   5478    317    -52   -756       C  
ATOM   3412  O   LYS A 441     -16.514   4.889 -31.310  1.00 51.60           O  
ANISOU 3412  O   LYS A 441     6093   7049   6461    269    -62   -738       O  
ATOM   3413  CB  LYS A 441     -15.285   1.870 -31.018  1.00 39.53           C  
ANISOU 3413  CB  LYS A 441     4634   5479   4905    402    -39   -752       C  
ATOM   3414  CG  LYS A 441     -16.726   1.668 -30.581  1.00 43.78           C  
ANISOU 3414  CG  LYS A 441     5211   5963   5459    367    -47   -724       C  
ATOM   3415  CD  LYS A 441     -16.918   0.309 -29.930  1.00 56.39           C  
ANISOU 3415  CD  LYS A 441     6865   7511   7051    412    -40   -711       C  
ATOM   3416  CE  LYS A 441     -18.392  -0.048 -29.822  1.00 67.70           C  
ANISOU 3416  CE  LYS A 441     8341   8883   8498    365    -40   -690       C  
ATOM   3417  NZ  LYS A 441     -18.593  -1.458 -29.387  1.00 76.52           N  
ANISOU 3417  NZ  LYS A 441     9526   9942   9606    400    -26   -680       N  
ATOM   3418  N   GLN A 442     -14.427   4.908 -30.464  1.00 48.10           N  
ANISOU 3418  N   GLN A 442     5590   6688   5997    343    -54   -766       N  
ATOM   3419  CA  GLN A 442     -14.630   6.190 -29.798  1.00 44.48           C  
ANISOU 3419  CA  GLN A 442     5096   6257   5547    309    -64   -758       C  
ATOM   3420  C   GLN A 442     -14.828   7.314 -30.808  1.00 45.81           C  
ANISOU 3420  C   GLN A 442     5253   6434   5718    247    -59   -766       C  
ATOM   3421  O   GLN A 442     -15.722   8.152 -30.646  1.00 48.93           O  
ANISOU 3421  O   GLN A 442     5651   6814   6127    206    -67   -749       O  
ATOM   3422  CB  GLN A 442     -13.444   6.495 -28.884  1.00 48.56           C  
ANISOU 3422  CB  GLN A 442     5563   6836   6052    346    -68   -774       C  
ATOM   3423  CG  GLN A 442     -13.310   5.560 -27.696  1.00 47.88           C  
ANISOU 3423  CG  GLN A 442     5491   6743   5960    409    -79   -760       C  
ATOM   3424  CD  GLN A 442     -14.319   5.856 -26.608  1.00 48.47           C  
ANISOU 3424  CD  GLN A 442     5585   6789   6043    393    -90   -731       C  
ATOM   3425  OE1 GLN A 442     -15.406   5.278 -26.579  1.00 46.13           O  
ANISOU 3425  OE1 GLN A 442     5337   6434   5758    384    -88   -709       O  
ATOM   3426  NE2 GLN A 442     -13.966   6.763 -25.705  1.00 45.48           N  
ANISOU 3426  NE2 GLN A 442     5169   6452   5658    386    -99   -735       N  
ATOM   3427  N   ALA A 443     -14.007   7.343 -31.862  1.00 33.00           N  
ANISOU 3427  N   ALA A 443     3620   4837   4083    241    -43   -792       N  
ATOM   3428  CA  ALA A 443     -14.082   8.432 -32.833  1.00 35.22           C  
ANISOU 3428  CA  ALA A 443     3896   5126   4360    183    -35   -800       C  
ATOM   3429  C   ALA A 443     -15.403   8.418 -33.589  1.00 38.37           C  
ANISOU 3429  C   ALA A 443     4342   5471   4767    145    -46   -778       C  
ATOM   3430  O   ALA A 443     -15.943   9.478 -33.922  1.00 40.03           O  
ANISOU 3430  O   ALA A 443     4553   5676   4980    100    -52   -768       O  
ATOM   3431  CB  ALA A 443     -12.910   8.352 -33.807  1.00 30.63           C  
ANISOU 3431  CB  ALA A 443     3298   4580   3758    185    -11   -833       C  
ATOM   3432  N   LEU A 444     -15.930   7.228 -33.882  1.00 28.38           N  
ANISOU 3432  N   LEU A 444     3117   4164   3503    163    -50   -771       N  
ATOM   3433  CA  LEU A 444     -17.219   7.138 -34.558  1.00 26.81           C  
ANISOU 3433  CA  LEU A 444     2957   3918   3311    126    -65   -753       C  
ATOM   3434  C   LEU A 444     -18.303   7.858 -33.767  1.00 32.81           C  
ANISOU 3434  C   LEU A 444     3706   4663   4095    104    -83   -725       C  
ATOM   3435  O   LEU A 444     -19.114   8.597 -34.337  1.00 32.78           O  
ANISOU 3435  O   LEU A 444     3709   4646   4098     64    -96   -713       O  
ATOM   3436  CB  LEU A 444     -17.593   5.673 -34.772  1.00 25.37           C  
ANISOU 3436  CB  LEU A 444     2819   3694   3128    147    -65   -753       C  
ATOM   3437  CG  LEU A 444     -16.732   4.871 -35.746  1.00 22.76           C  
ANISOU 3437  CG  LEU A 444     2510   3364   2772    165    -44   -780       C  
ATOM   3438  CD1 LEU A 444     -17.082   3.396 -35.667  1.00 27.21           C  
ANISOU 3438  CD1 LEU A 444     3123   3881   3336    193    -41   -778       C  
ATOM   3439  CD2 LEU A 444     -16.896   5.387 -37.164  1.00 21.90           C  
ANISOU 3439  CD2 LEU A 444     2421   3254   2646    116    -44   -789       C  
ATOM   3440  N   THR A 445     -18.323   7.663 -32.448  1.00 32.10           N  
ANISOU 3440  N   THR A 445     3602   4577   4018    134    -84   -715       N  
ATOM   3441  CA  THR A 445     -19.272   8.365 -31.592  1.00 31.61           C  
ANISOU 3441  CA  THR A 445     3528   4503   3978    118    -95   -692       C  
ATOM   3442  C   THR A 445     -18.812   9.791 -31.316  1.00 30.28           C  
ANISOU 3442  C   THR A 445     3326   4371   3809    100    -91   -696       C  
ATOM   3443  O   THR A 445     -19.538  10.755 -31.582  1.00 29.87           O  
ANISOU 3443  O   THR A 445     3273   4309   3768     66    -98   -684       O  
ATOM   3444  CB  THR A 445     -19.447   7.609 -30.273  1.00 32.12           C  
ANISOU 3444  CB  THR A 445     3598   4556   4052    154    -93   -680       C  
ATOM   3445  OG1 THR A 445     -19.807   6.250 -30.541  1.00 38.24           O  
ANISOU 3445  OG1 THR A 445     4412   5291   4824    168    -91   -678       O  
ATOM   3446  CG2 THR A 445     -20.527   8.260 -29.420  1.00 25.94           C  
ANISOU 3446  CG2 THR A 445     2807   3757   3292    135    -98   -657       C  
ATOM   3447  N   ILE A 446     -17.600   9.937 -30.785  1.00 32.34           N  
ANISOU 3447  N   ILE A 446     3559   4674   4054    123    -80   -716       N  
ATOM   3448  CA  ILE A 446     -17.149  11.225 -30.270  1.00 32.24           C  
ANISOU 3448  CA  ILE A 446     3515   4696   4039    104    -75   -722       C  
ATOM   3449  C   ILE A 446     -16.779  12.169 -31.409  1.00 33.74           C  
ANISOU 3449  C   ILE A 446     3703   4899   4218     64    -66   -735       C  
ATOM   3450  O   ILE A 446     -17.318  13.276 -31.519  1.00 32.87           O  
ANISOU 3450  O   ILE A 446     3597   4777   4114     29    -66   -724       O  
ATOM   3451  CB  ILE A 446     -15.974  11.024 -29.297  1.00 31.38           C  
ANISOU 3451  CB  ILE A 446     3374   4633   3916    140    -70   -740       C  
ATOM   3452  CG1 ILE A 446     -16.419  10.174 -28.104  1.00 28.11           C  
ANISOU 3452  CG1 ILE A 446     2972   4200   3509    180    -80   -723       C  
ATOM   3453  CG2 ILE A 446     -15.435  12.357 -28.840  1.00 30.18           C  
ANISOU 3453  CG2 ILE A 446     3190   4518   3758    112    -64   -753       C  
ATOM   3454  CD1 ILE A 446     -15.283   9.723 -27.214  1.00 32.36           C  
ANISOU 3454  CD1 ILE A 446     3485   4781   4029    227    -83   -738       C  
ATOM   3455  N   VAL A 447     -15.845  11.752 -32.266  1.00 36.28           N  
ANISOU 3455  N   VAL A 447     4021   5243   4520     68    -53   -759       N  
ATOM   3456  CA  VAL A 447     -15.410  12.620 -33.356  1.00 34.51           C  
ANISOU 3456  CA  VAL A 447     3800   5032   4280     26    -39   -773       C  
ATOM   3457  C   VAL A 447     -16.508  12.763 -34.403  1.00 37.76           C  
ANISOU 3457  C   VAL A 447     4255   5399   4694     -3    -51   -752       C  
ATOM   3458  O   VAL A 447     -16.742  13.857 -34.929  1.00 44.45           O  
ANISOU 3458  O   VAL A 447     5115   6240   5535    -41    -49   -746       O  
ATOM   3459  CB  VAL A 447     -14.102  12.093 -33.975  1.00 35.58           C  
ANISOU 3459  CB  VAL A 447     3918   5206   4394     40    -18   -806       C  
ATOM   3460  CG1 VAL A 447     -13.683  12.960 -35.154  1.00 32.12           C  
ANISOU 3460  CG1 VAL A 447     3490   4778   3936     -9      3   -821       C  
ATOM   3461  CG2 VAL A 447     -13.003  12.045 -32.928  1.00 39.52           C  
ANISOU 3461  CG2 VAL A 447     4366   5759   4891     70    -11   -828       C  
ATOM   3462  N   GLY A 448     -17.202  11.666 -34.716  1.00 40.67           N  
ANISOU 3462  N   GLY A 448     4650   5735   5068     14    -65   -742       N  
ATOM   3463  CA  GLY A 448     -18.200  11.702 -35.772  1.00 39.13           C  
ANISOU 3463  CA  GLY A 448     4492   5503   4871    -14    -82   -726       C  
ATOM   3464  C   GLY A 448     -19.338  12.665 -35.499  1.00 41.53           C  
ANISOU 3464  C   GLY A 448     4798   5786   5196    -36   -101   -697       C  
ATOM   3465  O   GLY A 448     -19.913  13.233 -36.432  1.00 42.64           O  
ANISOU 3465  O   GLY A 448     4963   5909   5329    -64   -114   -685       O  
ATOM   3466  N   THR A 449     -19.685  12.861 -34.227  1.00 36.14           N  
ANISOU 3466  N   THR A 449     4092   5103   4537    -19   -103   -686       N  
ATOM   3467  CA  THR A 449     -20.773  13.767 -33.883  1.00 30.42           C  
ANISOU 3467  CA  THR A 449     3367   4357   3835    -33   -116   -660       C  
ATOM   3468  C   THR A 449     -20.385  15.235 -34.003  1.00 33.13           C  
ANISOU 3468  C   THR A 449     3708   4711   4168    -58   -104   -662       C  
ATOM   3469  O   THR A 449     -21.271  16.080 -34.161  1.00 36.43           O  
ANISOU 3469  O   THR A 449     4137   5106   4598    -71   -115   -640       O  
ATOM   3470  CB  THR A 449     -21.276  13.481 -32.463  1.00 30.12           C  
ANISOU 3470  CB  THR A 449     3309   4312   3823     -9   -116   -649       C  
ATOM   3471  OG1 THR A 449     -22.619  13.963 -32.323  1.00 35.81           O  
ANISOU 3471  OG1 THR A 449     4030   5005   4570    -18   -131   -623       O  
ATOM   3472  CG2 THR A 449     -20.395  14.148 -31.417  1.00 33.19           C  
ANISOU 3472  CG2 THR A 449     3673   4731   4206     -1    -97   -662       C  
ATOM   3473  N   LEU A 450     -19.092  15.555 -33.937  1.00 32.42           N  
ANISOU 3473  N   LEU A 450     3606   4656   4057    -64    -80   -687       N  
ATOM   3474  CA  LEU A 450     -18.679  16.957 -33.885  1.00 32.99           C  
ANISOU 3474  CA  LEU A 450     3678   4737   4119    -92    -63   -692       C  
ATOM   3475  C   LEU A 450     -19.042  17.736 -35.144  1.00 30.24           C  
ANISOU 3475  C   LEU A 450     3369   4366   3756   -124    -66   -680       C  
ATOM   3476  O   LEU A 450     -19.641  18.818 -35.018  1.00 31.46           O  
ANISOU 3476  O   LEU A 450     3538   4498   3918   -136    -68   -662       O  
ATOM   3477  CB  LEU A 450     -17.181  17.031 -33.574  1.00 30.49           C  
ANISOU 3477  CB  LEU A 450     3334   4469   3783    -97    -37   -727       C  
ATOM   3478  CG  LEU A 450     -16.823  16.457 -32.205  1.00 28.40           C  
ANISOU 3478  CG  LEU A 450     3033   4230   3530    -64    -38   -735       C  
ATOM   3479  CD1 LEU A 450     -15.324  16.296 -32.062  1.00 37.25           C  
ANISOU 3479  CD1 LEU A 450     4119   5405   4630    -61    -19   -771       C  
ATOM   3480  CD2 LEU A 450     -17.383  17.344 -31.106  1.00 31.09           C  
ANISOU 3480  CD2 LEU A 450     3369   4557   3885    -69    -38   -722       C  
ATOM   3481  N   PRO A 451     -18.717  17.282 -36.363  1.00 21.74           N  
ANISOU 3481  N   PRO A 451     2315   3291   2654   -136    -66   -689       N  
ATOM   3482  CA  PRO A 451     -19.200  18.019 -37.542  1.00 22.87           C  
ANISOU 3482  CA  PRO A 451     2503   3407   2779   -164    -75   -672       C  
ATOM   3483  C   PRO A 451     -20.710  18.006 -37.665  1.00 26.12           C  
ANISOU 3483  C   PRO A 451     2929   3783   3214   -151   -114   -637       C  
ATOM   3484  O   PRO A 451     -21.300  18.998 -38.107  1.00 28.95           O  
ANISOU 3484  O   PRO A 451     3315   4117   3568   -164   -124   -616       O  
ATOM   3485  CB  PRO A 451     -18.520  17.295 -38.713  1.00 25.72           C  
ANISOU 3485  CB  PRO A 451     2884   3780   3107   -176    -66   -692       C  
ATOM   3486  CG  PRO A 451     -17.379  16.573 -38.099  1.00 26.22           C  
ANISOU 3486  CG  PRO A 451     2908   3883   3171   -159    -41   -724       C  
ATOM   3487  CD  PRO A 451     -17.866  16.150 -36.761  1.00 22.10           C  
ANISOU 3487  CD  PRO A 451     2352   3361   2684   -124    -56   -714       C  
ATOM   3488  N   PHE A 452     -21.353  16.902 -37.281  1.00 28.74           N  
ANISOU 3488  N   PHE A 452     3242   4110   3568   -126   -134   -632       N  
ATOM   3489  CA  PHE A 452     -22.810  16.868 -37.243  1.00 27.47           C  
ANISOU 3489  CA  PHE A 452     3081   3922   3435   -116   -169   -603       C  
ATOM   3490  C   PHE A 452     -23.345  17.911 -36.271  1.00 32.63           C  
ANISOU 3490  C   PHE A 452     3718   4564   4116   -107   -164   -585       C  
ATOM   3491  O   PHE A 452     -24.259  18.676 -36.599  1.00 37.60           O  
ANISOU 3491  O   PHE A 452     4361   5172   4755   -107   -184   -560       O  
ATOM   3492  CB  PHE A 452     -23.284  15.464 -36.854  1.00 23.33           C  
ANISOU 3492  CB  PHE A 452     2538   3396   2930    -98   -182   -605       C  
ATOM   3493  CG  PHE A 452     -24.768  15.359 -36.614  1.00 23.37           C  
ANISOU 3493  CG  PHE A 452     2530   3380   2970    -91   -212   -579       C  
ATOM   3494  CD1 PHE A 452     -25.319  15.697 -35.386  1.00 27.18           C  
ANISOU 3494  CD1 PHE A 452     2982   3857   3487    -73   -205   -568       C  
ATOM   3495  CD2 PHE A 452     -25.609  14.901 -37.611  1.00 28.02           C  
ANISOU 3495  CD2 PHE A 452     3135   3956   3555   -102   -247   -569       C  
ATOM   3496  CE1 PHE A 452     -26.680  15.602 -35.170  1.00 28.90           C  
ANISOU 3496  CE1 PHE A 452     3183   4060   3739    -67   -229   -547       C  
ATOM   3497  CE2 PHE A 452     -26.972  14.798 -37.397  1.00 33.10           C  
ANISOU 3497  CE2 PHE A 452     3757   4587   4231    -98   -276   -549       C  
ATOM   3498  CZ  PHE A 452     -27.506  15.148 -36.175  1.00 24.61           C  
ANISOU 3498  CZ  PHE A 452     2648   3508   3195    -80   -264   -538       C  
ATOM   3499  N   THR A 453     -22.779  17.952 -35.064  1.00 29.48           N  
ANISOU 3499  N   THR A 453     3292   4181   3728    -96   -139   -599       N  
ATOM   3500  CA  THR A 453     -23.253  18.879 -34.042  1.00 29.83           C  
ANISOU 3500  CA  THR A 453     3324   4215   3797    -88   -130   -586       C  
ATOM   3501  C   THR A 453     -23.012  20.327 -34.452  1.00 31.07           C  
ANISOU 3501  C   THR A 453     3510   4359   3937   -108   -117   -581       C  
ATOM   3502  O   THR A 453     -23.898  21.178 -34.313  1.00 29.20           O  
ANISOU 3502  O   THR A 453     3282   4095   3718   -100   -124   -558       O  
ATOM   3503  CB  THR A 453     -22.569  18.574 -32.710  1.00 30.71           C  
ANISOU 3503  CB  THR A 453     3406   4348   3914    -76   -107   -605       C  
ATOM   3504  OG1 THR A 453     -22.890  17.238 -32.301  1.00 33.20           O  
ANISOU 3504  OG1 THR A 453     3704   4667   4244    -54   -118   -605       O  
ATOM   3505  CG2 THR A 453     -23.019  19.548 -31.642  1.00 30.68           C  
ANISOU 3505  CG2 THR A 453     3394   4331   3930    -70    -93   -595       C  
ATOM   3506  N   TYR A 454     -21.814  20.624 -34.960  1.00 29.88           N  
ANISOU 3506  N   TYR A 454     3375   4226   3751   -135    -95   -603       N  
ATOM   3507  CA  TYR A 454     -21.502  21.990 -35.367  1.00 30.85           C  
ANISOU 3507  CA  TYR A 454     3535   4334   3854   -161    -76   -601       C  
ATOM   3508  C   TYR A 454     -22.362  22.425 -36.547  1.00 36.94           C  
ANISOU 3508  C   TYR A 454     4348   5072   4616   -163   -102   -571       C  
ATOM   3509  O   TYR A 454     -22.913  23.532 -36.552  1.00 43.38           O  
ANISOU 3509  O   TYR A 454     5190   5856   5436   -161   -102   -550       O  
ATOM   3510  CB  TYR A 454     -20.017  22.106 -35.714  1.00 31.88           C  
ANISOU 3510  CB  TYR A 454     3669   4495   3948   -195    -44   -634       C  
ATOM   3511  CG  TYR A 454     -19.683  23.287 -36.599  1.00 34.60           C  
ANISOU 3511  CG  TYR A 454     4065   4820   4261   -232    -24   -631       C  
ATOM   3512  CD1 TYR A 454     -19.898  24.589 -36.166  1.00 33.03           C  
ANISOU 3512  CD1 TYR A 454     3892   4594   4066   -243     -8   -621       C  
ATOM   3513  CD2 TYR A 454     -19.153  23.100 -37.868  1.00 39.36           C  
ANISOU 3513  CD2 TYR A 454     4698   5428   4829   -256    -19   -639       C  
ATOM   3514  CE1 TYR A 454     -19.592  25.671 -36.970  1.00 39.07           C  
ANISOU 3514  CE1 TYR A 454     4713   5334   4799   -278     13   -617       C  
ATOM   3515  CE2 TYR A 454     -18.845  24.175 -38.681  1.00 37.59           C  
ANISOU 3515  CE2 TYR A 454     4529   5183   4572   -293      2   -635       C  
ATOM   3516  CZ  TYR A 454     -19.067  25.458 -38.227  1.00 38.24           C  
ANISOU 3516  CZ  TYR A 454     4638   5235   4657   -303     17   -623       C  
ATOM   3517  OH  TYR A 454     -18.760  26.531 -39.032  1.00 45.69           O  
ANISOU 3517  OH  TYR A 454     5645   6150   5565   -341     41   -618       O  
ATOM   3518  N   MET A 455     -22.491  21.561 -37.556  1.00 40.10           N  
ANISOU 3518  N   MET A 455     4757   5477   5001   -164   -126   -570       N  
ATOM   3519  CA  MET A 455     -23.235  21.928 -38.756  1.00 35.84           C  
ANISOU 3519  CA  MET A 455     4261   4911   4446   -167   -156   -543       C  
ATOM   3520  C   MET A 455     -24.714  22.137 -38.453  1.00 35.41           C  
ANISOU 3520  C   MET A 455     4193   4833   4428   -134   -192   -510       C  
ATOM   3521  O   MET A 455     -25.335  23.068 -38.981  1.00 37.21           O  
ANISOU 3521  O   MET A 455     4455   5033   4651   -128   -208   -483       O  
ATOM   3522  CB  MET A 455     -23.040  20.859 -39.830  1.00 31.09           C  
ANISOU 3522  CB  MET A 455     3672   4322   3817   -178   -173   -553       C  
ATOM   3523  CG  MET A 455     -23.875  21.045 -41.075  1.00 34.50           C  
ANISOU 3523  CG  MET A 455     4147   4733   4230   -180   -213   -526       C  
ATOM   3524  SD  MET A 455     -25.394  20.082 -41.046  1.00 34.68           S  
ANISOU 3524  SD  MET A 455     4136   4752   4288   -152   -270   -506       S  
ATOM   3525  CE  MET A 455     -26.553  21.326 -41.590  1.00 35.22           C  
ANISOU 3525  CE  MET A 455     4234   4790   4358   -135   -308   -463       C  
ATOM   3526  N   LEU A 456     -25.298  21.281 -37.611  1.00 36.45           N  
ANISOU 3526  N   LEU A 456     4276   4976   4598   -112   -203   -511       N  
ATOM   3527  CA  LEU A 456     -26.706  21.437 -37.258  1.00 34.26           C  
ANISOU 3527  CA  LEU A 456     3975   4680   4360    -83   -232   -484       C  
ATOM   3528  C   LEU A 456     -26.943  22.748 -36.521  1.00 36.63           C  
ANISOU 3528  C   LEU A 456     4282   4959   4678    -69   -211   -470       C  
ATOM   3529  O   LEU A 456     -27.843  23.519 -36.874  1.00 42.78           O  
ANISOU 3529  O   LEU A 456     5075   5713   5467    -49   -233   -442       O  
ATOM   3530  CB  LEU A 456     -27.171  20.252 -36.409  1.00 32.49           C  
ANISOU 3530  CB  LEU A 456     3701   4472   4171    -70   -237   -492       C  
ATOM   3531  CG  LEU A 456     -28.637  20.263 -35.964  1.00 35.77           C  
ANISOU 3531  CG  LEU A 456     4082   4877   4633    -44   -262   -468       C  
ATOM   3532  CD1 LEU A 456     -29.229  18.870 -36.066  1.00 36.22           C  
ANISOU 3532  CD1 LEU A 456     4111   4947   4706    -47   -286   -473       C  
ATOM   3533  CD2 LEU A 456     -28.789  20.800 -34.546  1.00 32.97           C  
ANISOU 3533  CD2 LEU A 456     3702   4515   4310    -25   -230   -468       C  
ATOM   3534  N   GLU A 457     -26.142  23.016 -35.487  1.00 42.54           N  
ANISOU 3534  N   GLU A 457     5021   5715   5429    -76   -170   -491       N  
ATOM   3535  CA  GLU A 457     -26.324  24.242 -34.720  1.00 39.33           C  
ANISOU 3535  CA  GLU A 457     4624   5284   5036    -66   -145   -483       C  
ATOM   3536  C   GLU A 457     -25.987  25.476 -35.544  1.00 40.47           C  
ANISOU 3536  C   GLU A 457     4829   5401   5148    -82   -136   -473       C  
ATOM   3537  O   GLU A 457     -26.613  26.526 -35.365  1.00 46.85           O  
ANISOU 3537  O   GLU A 457     5658   6174   5968    -63   -132   -452       O  
ATOM   3538  CB  GLU A 457     -25.481  24.202 -33.446  1.00 39.00           C  
ANISOU 3538  CB  GLU A 457     4561   5260   4997    -77   -106   -511       C  
ATOM   3539  CG  GLU A 457     -25.917  25.202 -32.382  1.00 37.29           C  
ANISOU 3539  CG  GLU A 457     4346   5019   4803    -62    -81   -505       C  
ATOM   3540  CD  GLU A 457     -27.103  24.727 -31.560  1.00 40.84           C  
ANISOU 3540  CD  GLU A 457     4754   5465   5300    -26    -93   -491       C  
ATOM   3541  OE1 GLU A 457     -28.052  24.151 -32.135  1.00 38.69           O  
ANISOU 3541  OE1 GLU A 457     4462   5191   5046     -8   -128   -471       O  
ATOM   3542  OE2 GLU A 457     -27.088  24.934 -30.328  1.00 43.57           O1-
ANISOU 3542  OE2 GLU A 457     5084   5809   5660    -20    -65   -501       O1-
ATOM   3543  N   LYS A 458     -25.004  25.375 -36.442  1.00 37.07           N  
ANISOU 3543  N   LYS A 458     4430   4982   4674   -116   -128   -488       N  
ATOM   3544  CA  LYS A 458     -24.734  26.485 -37.348  1.00 45.48           C  
ANISOU 3544  CA  LYS A 458     5561   6017   5703   -135   -119   -476       C  
ATOM   3545  C   LYS A 458     -25.945  26.776 -38.223  1.00 45.16           C  
ANISOU 3545  C   LYS A 458     5545   5947   5665   -104   -164   -436       C  
ATOM   3546  O   LYS A 458     -26.321  27.939 -38.404  1.00 49.23           O  
ANISOU 3546  O   LYS A 458     6106   6423   6175    -92   -161   -412       O  
ATOM   3547  CB  LYS A 458     -23.510  26.181 -38.212  1.00 36.09           C  
ANISOU 3547  CB  LYS A 458     4396   4849   4466   -179   -101   -500       C  
ATOM   3548  CG  LYS A 458     -23.215  27.248 -39.255  1.00 40.11           C  
ANISOU 3548  CG  LYS A 458     4983   5326   4932   -205    -89   -487       C  
ATOM   3549  CD  LYS A 458     -21.748  27.632 -39.265  1.00 49.15           C  
ANISOU 3549  CD  LYS A 458     6147   6486   6042   -258    -36   -522       C  
ATOM   3550  CE  LYS A 458     -21.553  29.035 -39.813  1.00 51.15           C  
ANISOU 3550  CE  LYS A 458     6480   6694   6262   -284     -9   -509       C  
ATOM   3551  NZ  LYS A 458     -22.196  30.059 -38.947  1.00 49.67           N  
ANISOU 3551  NZ  LYS A 458     6306   6467   6101   -261     -1   -491       N  
ATOM   3552  N   TRP A 459     -26.584  25.729 -38.752  1.00 33.98           N  
ANISOU 3552  N   TRP A 459     4102   4550   4258    -90   -208   -428       N  
ATOM   3553  CA  TRP A 459     -27.778  25.924 -39.568  1.00 32.84           C  
ANISOU 3553  CA  TRP A 459     3972   4388   4118    -60   -260   -391       C  
ATOM   3554  C   TRP A 459     -28.874  26.627 -38.780  1.00 37.85           C  
ANISOU 3554  C   TRP A 459     4583   5000   4800    -15   -267   -367       C  
ATOM   3555  O   TRP A 459     -29.523  27.549 -39.288  1.00 44.44           O  
ANISOU 3555  O   TRP A 459     5453   5803   5628     12   -287   -336       O  
ATOM   3556  CB  TRP A 459     -28.277  24.580 -40.096  1.00 31.49           C  
ANISOU 3556  CB  TRP A 459     3766   4247   3953    -60   -304   -394       C  
ATOM   3557  CG  TRP A 459     -29.510  24.681 -40.943  1.00 30.07           C  
ANISOU 3557  CG  TRP A 459     3591   4058   3776    -32   -364   -360       C  
ATOM   3558  CD1 TRP A 459     -29.563  24.832 -42.298  1.00 29.66           C  
ANISOU 3558  CD1 TRP A 459     3593   3999   3679    -41   -397   -344       C  
ATOM   3559  CD2 TRP A 459     -30.870  24.629 -40.492  1.00 34.13           C  
ANISOU 3559  CD2 TRP A 459     4053   4574   4341      9   -398   -339       C  
ATOM   3560  NE1 TRP A 459     -30.870  24.881 -42.719  1.00 31.33           N  
ANISOU 3560  NE1 TRP A 459     3786   4210   3908     -7   -457   -314       N  
ATOM   3561  CE2 TRP A 459     -31.692  24.759 -41.629  1.00 34.00           C  
ANISOU 3561  CE2 TRP A 459     4056   4555   4308     24   -457   -311       C  
ATOM   3562  CE3 TRP A 459     -31.472  24.488 -39.238  1.00 35.44           C  
ANISOU 3562  CE3 TRP A 459     4156   4746   4563     33   -384   -342       C  
ATOM   3563  CZ2 TRP A 459     -33.083  24.752 -41.550  1.00 34.34           C  
ANISOU 3563  CZ2 TRP A 459     4050   4606   4392     64   -504   -288       C  
ATOM   3564  CZ3 TRP A 459     -32.853  24.482 -39.161  1.00 34.80           C  
ANISOU 3564  CZ3 TRP A 459     4029   4669   4524     70   -424   -320       C  
ATOM   3565  CH2 TRP A 459     -33.643  24.614 -40.310  1.00 33.15           C  
ANISOU 3565  CH2 TRP A 459     3833   4462   4301     86   -484   -294       C  
ATOM   3566  N   ARG A 460     -29.096  26.204 -37.533  1.00 36.45           N  
ANISOU 3566  N   ARG A 460     4347   4837   4666     -3   -249   -381       N  
ATOM   3567  CA  ARG A 460     -30.083  26.874 -36.693  1.00 33.52           C  
ANISOU 3567  CA  ARG A 460     3952   4444   4338     39   -246   -363       C  
ATOM   3568  C   ARG A 460     -29.664  28.306 -36.385  1.00 38.18           C  
ANISOU 3568  C   ARG A 460     4596   4994   4915     41   -205   -358       C  
ATOM   3569  O   ARG A 460     -30.499  29.218 -36.402  1.00 45.32           O  
ANISOU 3569  O   ARG A 460     5518   5865   5836     80   -213   -330       O  
ATOM   3570  CB  ARG A 460     -30.299  26.078 -35.407  1.00 29.02           C  
ANISOU 3570  CB  ARG A 460     3316   3898   3811     45   -228   -381       C  
ATOM   3571  CG  ARG A 460     -30.890  24.697 -35.645  1.00 32.04           C  
ANISOU 3571  CG  ARG A 460     3649   4314   4213     44   -265   -384       C  
ATOM   3572  CD  ARG A 460     -31.662  24.201 -34.437  1.00 26.88           C  
ANISOU 3572  CD  ARG A 460     2932   3669   3610     64   -254   -388       C  
ATOM   3573  NE  ARG A 460     -30.777  23.816 -33.345  1.00 25.01           N  
ANISOU 3573  NE  ARG A 460     2688   3444   3371     45   -210   -416       N  
ATOM   3574  CZ  ARG A 460     -31.183  23.244 -32.221  1.00 25.53           C  
ANISOU 3574  CZ  ARG A 460     2711   3519   3471     54   -193   -424       C  
ATOM   3575  NH1 ARG A 460     -32.459  22.975 -32.004  1.00 29.67           N  
ANISOU 3575  NH1 ARG A 460     3190   4045   4038     78   -210   -409       N  
ATOM   3576  NH2 ARG A 460     -30.286  22.940 -31.287  1.00 31.20           N  
ANISOU 3576  NH2 ARG A 460     3429   4248   4178     38   -157   -448       N  
ATOM   3577  N   TRP A 461     -28.374  28.524 -36.112  1.00 39.10           N  
ANISOU 3577  N   TRP A 461     4741   5113   5001     -2   -161   -386       N  
ATOM   3578  CA  TRP A 461     -27.889  29.879 -35.867  1.00 38.82           C  
ANISOU 3578  CA  TRP A 461     4764   5037   4947    -13   -118   -386       C  
ATOM   3579  C   TRP A 461     -28.131  30.776 -37.074  1.00 41.46           C  
ANISOU 3579  C   TRP A 461     5172   5332   5250     -4   -136   -355       C  
ATOM   3580  O   TRP A 461     -28.580  31.919 -36.928  1.00 53.83           O  
ANISOU 3580  O   TRP A 461     6780   6852   6822     23   -124   -334       O  
ATOM   3581  CB  TRP A 461     -26.400  29.855 -35.519  1.00 36.62           C  
ANISOU 3581  CB  TRP A 461     4499   4778   4637    -70    -73   -426       C  
ATOM   3582  CG  TRP A 461     -26.087  29.330 -34.151  1.00 36.29           C  
ANISOU 3582  CG  TRP A 461     4401   4765   4621    -74    -48   -455       C  
ATOM   3583  CD1 TRP A 461     -26.956  29.173 -33.110  1.00 35.06           C  
ANISOU 3583  CD1 TRP A 461     4202   4607   4510    -38    -50   -449       C  
ATOM   3584  CD2 TRP A 461     -24.807  28.900 -33.674  1.00 34.77           C  
ANISOU 3584  CD2 TRP A 461     4193   4611   4409   -118    -20   -494       C  
ATOM   3585  NE1 TRP A 461     -26.295  28.668 -32.016  1.00 34.06           N  
ANISOU 3585  NE1 TRP A 461     4041   4512   4388    -57    -24   -480       N  
ATOM   3586  CE2 TRP A 461     -24.975  28.493 -32.336  1.00 36.90           C  
ANISOU 3586  CE2 TRP A 461     4414   4898   4709   -103     -8   -508       C  
ATOM   3587  CE3 TRP A 461     -23.535  28.819 -34.250  1.00 36.08           C  
ANISOU 3587  CE3 TRP A 461     4377   4799   4533   -166     -2   -520       C  
ATOM   3588  CZ2 TRP A 461     -23.919  28.010 -31.565  1.00 32.57           C  
ANISOU 3588  CZ2 TRP A 461     3836   4388   4148   -131     14   -544       C  
ATOM   3589  CZ3 TRP A 461     -22.489  28.340 -33.483  1.00 30.84           C  
ANISOU 3589  CZ3 TRP A 461     3678   4179   3863   -193     22   -557       C  
ATOM   3590  CH2 TRP A 461     -22.687  27.942 -32.156  1.00 28.61           C  
ANISOU 3590  CH2 TRP A 461     3349   3913   3610   -174     27   -568       C  
ATOM   3591  N   MET A 462     -27.839  30.275 -38.277  1.00 37.32           N  
ANISOU 3591  N   MET A 462     4668   4822   4688    -24   -164   -351       N  
ATOM   3592  CA  MET A 462     -28.072  31.065 -39.482  1.00 42.88           C  
ANISOU 3592  CA  MET A 462     5448   5490   5355    -16   -185   -319       C  
ATOM   3593  C   MET A 462     -29.559  31.232 -39.769  1.00 41.92           C  
ANISOU 3593  C   MET A 462     5312   5352   5263     50   -240   -277       C  
ATOM   3594  O   MET A 462     -29.971  32.270 -40.299  1.00 47.69           O  
ANISOU 3594  O   MET A 462     6105   6038   5978     78   -249   -245       O  
ATOM   3595  CB  MET A 462     -27.363  30.425 -40.676  1.00 42.03           C  
ANISOU 3595  CB  MET A 462     5367   5404   5197    -58   -199   -328       C  
ATOM   3596  CG  MET A 462     -25.886  30.144 -40.440  1.00 40.08           C  
ANISOU 3596  CG  MET A 462     5122   5182   4924   -119   -147   -372       C  
ATOM   3597  SD  MET A 462     -25.056  29.377 -41.844  1.00 50.19           S  
ANISOU 3597  SD  MET A 462     6434   6489   6147   -165   -156   -386       S  
ATOM   3598  CE  MET A 462     -25.943  30.121 -43.209  1.00 49.01           C  
ANISOU 3598  CE  MET A 462     6366   6294   5961   -138   -202   -335       C  
ATOM   3599  N   VAL A 463     -30.376  30.230 -39.435  1.00 39.40           N  
ANISOU 3599  N   VAL A 463     4912   5071   4987     75   -276   -278       N  
ATOM   3600  CA  VAL A 463     -31.819  30.357 -39.620  1.00 44.29           C  
ANISOU 3600  CA  VAL A 463     5502   5686   5642    136   -328   -243       C  
ATOM   3601  C   VAL A 463     -32.382  31.424 -38.688  1.00 45.99           C  
ANISOU 3601  C   VAL A 463     5718   5862   5894    182   -300   -229       C  
ATOM   3602  O   VAL A 463     -33.156  32.293 -39.108  1.00 48.70           O  
ANISOU 3602  O   VAL A 463     6093   6172   6240    232   -323   -193       O  
ATOM   3603  CB  VAL A 463     -32.510  28.997 -39.407  1.00 37.86           C  
ANISOU 3603  CB  VAL A 463     4597   4922   4865    141   -366   -253       C  
ATOM   3604  CG1 VAL A 463     -33.968  29.193 -39.014  1.00 39.36           C  
ANISOU 3604  CG1 VAL A 463     4731   5112   5111    203   -398   -228       C  
ATOM   3605  CG2 VAL A 463     -32.407  28.150 -40.664  1.00 31.36           C  
ANISOU 3605  CG2 VAL A 463     3787   4126   4004    115   -414   -252       C  
ATOM   3606  N   PHE A 464     -31.996  31.377 -37.411  1.00 43.44           N  
ANISOU 3606  N   PHE A 464     5364   5543   5598    168   -248   -258       N  
ATOM   3607  CA  PHE A 464     -32.461  32.383 -36.461  1.00 37.88           C  
ANISOU 3607  CA  PHE A 464     4665   4800   4926    206   -213   -250       C  
ATOM   3608  C   PHE A 464     -31.942  33.767 -36.830  1.00 43.97           C  
ANISOU 3608  C   PHE A 464     5538   5511   5658    203   -182   -236       C  
ATOM   3609  O   PHE A 464     -32.660  34.765 -36.696  1.00 48.96           O  
ANISOU 3609  O   PHE A 464     6199   6098   6307    256   -178   -210       O  
ATOM   3610  CB  PHE A 464     -32.037  32.003 -35.042  1.00 42.29           C  
ANISOU 3610  CB  PHE A 464     5180   5377   5513    183   -164   -286       C  
ATOM   3611  CG  PHE A 464     -32.607  30.694 -34.569  1.00 37.63           C  
ANISOU 3611  CG  PHE A 464     4499   4838   4963    188   -188   -297       C  
ATOM   3612  CD1 PHE A 464     -33.896  30.320 -34.913  1.00 43.53           C  
ANISOU 3612  CD1 PHE A 464     5194   5600   5746    233   -237   -272       C  
ATOM   3613  CD2 PHE A 464     -31.857  29.839 -33.778  1.00 34.76           C  
ANISOU 3613  CD2 PHE A 464     4102   4506   4598    148   -160   -332       C  
ATOM   3614  CE1 PHE A 464     -34.423  29.118 -34.480  1.00 50.28           C  
ANISOU 3614  CE1 PHE A 464     5969   6498   6636    230   -254   -285       C  
ATOM   3615  CE2 PHE A 464     -32.378  28.636 -33.343  1.00 38.29           C  
ANISOU 3615  CE2 PHE A 464     4476   4993   5079    151   -178   -341       C  
ATOM   3616  CZ  PHE A 464     -33.663  28.274 -33.694  1.00 38.08           C  
ANISOU 3616  CZ  PHE A 464     4402   4979   5089    189   -222   -318       C  
ATOM   3617  N   LYS A 465     -30.695  33.845 -37.302  1.00 53.48           N  
ANISOU 3617  N   LYS A 465     6798   6713   6810    141   -157   -255       N  
ATOM   3618  CA  LYS A 465     -30.143  35.114 -37.762  1.00 48.53           C  
ANISOU 3618  CA  LYS A 465     6274   6027   6138    127   -125   -244       C  
ATOM   3619  C   LYS A 465     -30.873  35.654 -38.984  1.00 52.78           C  
ANISOU 3619  C   LYS A 465     6868   6531   6654    172   -172   -197       C  
ATOM   3620  O   LYS A 465     -30.782  36.854 -39.267  1.00 61.53           O  
ANISOU 3620  O   LYS A 465     8066   7578   7735    182   -149   -176       O  
ATOM   3621  CB  LYS A 465     -28.658  34.955 -38.093  1.00 47.98           C  
ANISOU 3621  CB  LYS A 465     6243   5972   6017     45    -89   -277       C  
ATOM   3622  CG  LYS A 465     -27.717  35.112 -36.912  1.00 56.83           C  
ANISOU 3622  CG  LYS A 465     7351   7100   7143     -1    -26   -320       C  
ATOM   3623  CD  LYS A 465     -26.271  35.169 -37.381  1.00 65.34           C  
ANISOU 3623  CD  LYS A 465     8472   8188   8167    -80      9   -350       C  
ATOM   3624  CE  LYS A 465     -25.345  34.430 -36.430  1.00 66.32           C  
ANISOU 3624  CE  LYS A 465     8531   8366   8300   -125     38   -399       C  
ATOM   3625  NZ  LYS A 465     -25.054  35.229 -35.208  1.00 61.37           N  
ANISOU 3625  NZ  LYS A 465     7915   7716   7686   -139     89   -421       N  
ATOM   3626  N   GLY A 466     -31.595  34.804 -39.708  1.00 49.30           N  
ANISOU 3626  N   GLY A 466     6382   6130   6222    197   -238   -178       N  
ATOM   3627  CA  GLY A 466     -32.194  35.186 -40.968  1.00 52.30           C  
ANISOU 3627  CA  GLY A 466     6814   6487   6570    234   -292   -135       C  
ATOM   3628  C   GLY A 466     -31.299  35.021 -42.173  1.00 54.56           C  
ANISOU 3628  C   GLY A 466     7169   6775   6786    179   -298   -137       C  
ATOM   3629  O   GLY A 466     -31.690  35.427 -43.275  1.00 62.59           O  
ANISOU 3629  O   GLY A 466     8247   7768   7765    205   -340   -100       O  
ATOM   3630  N   GLU A 467     -30.109  34.440 -42.002  1.00 55.12           N  
ANISOU 3630  N   GLU A 467     7233   6874   6836    106   -257   -179       N  
ATOM   3631  CA  GLU A 467     -29.178  34.247 -43.107  1.00 52.47           C  
ANISOU 3631  CA  GLU A 467     6959   6543   6435     49   -253   -187       C  
ATOM   3632  C   GLU A 467     -29.616  33.146 -44.064  1.00 55.18           C  
ANISOU 3632  C   GLU A 467     7270   6931   6766     54   -320   -179       C  
ATOM   3633  O   GLU A 467     -29.016  33.007 -45.135  1.00 62.45           O  
ANISOU 3633  O   GLU A 467     8249   7853   7628     15   -324   -179       O  
ATOM   3634  CB  GLU A 467     -27.782  33.945 -42.559  1.00 47.94           C  
ANISOU 3634  CB  GLU A 467     6374   5991   5849    -25   -188   -238       C  
ATOM   3635  CG  GLU A 467     -27.180  35.091 -41.759  1.00 54.78           C  
ANISOU 3635  CG  GLU A 467     7287   6813   6714    -46   -120   -250       C  
ATOM   3636  CD  GLU A 467     -25.842  34.736 -41.141  1.00 60.85           C  
ANISOU 3636  CD  GLU A 467     8029   7615   7475   -117    -62   -303       C  
ATOM   3637  OE1 GLU A 467     -25.467  33.546 -41.175  1.00 54.22           O  
ANISOU 3637  OE1 GLU A 467     7126   6835   6641   -139    -76   -329       O  
ATOM   3638  OE2 GLU A 467     -25.166  35.649 -40.619  1.00 69.12           O1-
ANISOU 3638  OE2 GLU A 467     9120   8631   8511   -151     -4   -320       O1-
ATOM   3639  N   ILE A 468     -30.632  32.367 -43.709  1.00 54.76           N  
ANISOU 3639  N   ILE A 468     7128   6915   6764     95   -368   -174       N  
ATOM   3640  CA  ILE A 468     -31.195  31.367 -44.613  1.00 55.04           C  
ANISOU 3640  CA  ILE A 468     7134   6990   6788    100   -437   -165       C  
ATOM   3641  C   ILE A 468     -32.673  31.670 -44.828  1.00 59.61           C  
ANISOU 3641  C   ILE A 468     7689   7565   7397    175   -504   -123       C  
ATOM   3642  O   ILE A 468     -33.461  31.603 -43.871  1.00 56.37           O  
ANISOU 3642  O   ILE A 468     7203   7166   7050    215   -507   -122       O  
ATOM   3643  CB  ILE A 468     -31.010  29.943 -44.068  1.00 50.91           C  
ANISOU 3643  CB  ILE A 468     6521   6525   6298     71   -436   -204       C  
ATOM   3644  CG1 ILE A 468     -29.556  29.697 -43.663  1.00 47.72           C  
ANISOU 3644  CG1 ILE A 468     6128   6129   5873      8   -368   -247       C  
ATOM   3645  CG2 ILE A 468     -31.457  28.917 -45.098  1.00 48.35           C  
ANISOU 3645  CG2 ILE A 468     6181   6237   5952     64   -500   -200       C  
ATOM   3646  CD1 ILE A 468     -29.355  28.398 -42.920  1.00 39.10           C  
ANISOU 3646  CD1 ILE A 468     4952   5087   4818    -11   -360   -283       C  
ATOM   3647  N   PRO A 469     -33.096  32.014 -46.042  1.00 54.16           N  
ANISOU 3647  N   PRO A 469     7059   6860   6661    196   -557    -87       N  
ATOM   3648  CA  PRO A 469     -34.528  32.214 -46.290  1.00 48.85           C  
ANISOU 3648  CA  PRO A 469     6352   6194   6017    270   -630    -48       C  
ATOM   3649  C   PRO A 469     -35.288  30.898 -46.211  1.00 56.24           C  
ANISOU 3649  C   PRO A 469     7181   7195   6992    270   -683    -64       C  
ATOM   3650  O   PRO A 469     -34.725  29.810 -46.344  1.00 56.51           O  
ANISOU 3650  O   PRO A 469     7193   7266   7014    213   -676    -97       O  
ATOM   3651  CB  PRO A 469     -34.590  32.806 -47.703  1.00 58.89           C  
ANISOU 3651  CB  PRO A 469     7725   7436   7215    283   -675     -9       C  
ATOM   3652  CG  PRO A 469     -33.178  32.992 -48.152  1.00 59.63           C  
ANISOU 3652  CG  PRO A 469     7910   7503   7243    212   -615    -28       C  
ATOM   3653  CD  PRO A 469     -32.272  32.233 -47.242  1.00 53.26           C  
ANISOU 3653  CD  PRO A 469     7047   6725   6465    153   -553    -81       C  
ATOM   3654  N   LYS A 470     -36.600  31.019 -45.980  1.00 60.07           N  
ANISOU 3654  N   LYS A 470     7601   7695   7527    336   -734    -39       N  
ATOM   3655  CA  LYS A 470     -37.440  29.834 -45.823  1.00 48.82           C  
ANISOU 3655  CA  LYS A 470     6069   6333   6147    334   -781    -55       C  
ATOM   3656  C   LYS A 470     -37.409  28.960 -47.071  1.00 49.29           C  
ANISOU 3656  C   LYS A 470     6147   6427   6154    296   -841    -58       C  
ATOM   3657  O   LYS A 470     -37.435  27.727 -46.976  1.00 50.55           O  
ANISOU 3657  O   LYS A 470     6246   6631   6328    254   -851    -89       O  
ATOM   3658  CB  LYS A 470     -38.875  30.247 -45.495  1.00 51.33           C  
ANISOU 3658  CB  LYS A 470     6316   6662   6523    414   -828    -26       C  
ATOM   3659  CG  LYS A 470     -39.233  30.142 -44.023  1.00 55.46           C  
ANISOU 3659  CG  LYS A 470     6752   7193   7125    430   -779    -46       C  
ATOM   3660  CD  LYS A 470     -39.978  31.379 -43.551  1.00 66.25           C  
ANISOU 3660  CD  LYS A 470     8119   8525   8530    513   -773    -14       C  
ATOM   3661  CE  LYS A 470     -41.315  31.522 -44.261  1.00 61.10           C  
ANISOU 3661  CE  LYS A 470     7422   7900   7892    580   -862     22       C  
ATOM   3662  NZ  LYS A 470     -42.368  32.062 -43.358  1.00 70.77           N  
ANISOU 3662  NZ  LYS A 470     8572   9126   9192    655   -854     34       N  
ATOM   3663  N   ASP A 471     -37.349  29.579 -48.250  1.00 61.17           N  
ANISOU 3663  N   ASP A 471     7741   7908   7593    308   -880    -26       N  
ATOM   3664  CA  ASP A 471     -37.292  28.830 -49.500  1.00 67.29           C  
ANISOU 3664  CA  ASP A 471     8547   8712   8308    271   -936    -28       C  
ATOM   3665  C   ASP A 471     -35.927  28.206 -49.757  1.00 60.36           C  
ANISOU 3665  C   ASP A 471     7722   7830   7383    191   -881    -66       C  
ATOM   3666  O   ASP A 471     -35.748  27.565 -50.798  1.00 64.66           O  
ANISOU 3666  O   ASP A 471     8301   8393   7872    153   -917    -72       O  
ATOM   3667  CB  ASP A 471     -37.676  29.738 -50.671  1.00 71.38           C  
ANISOU 3667  CB  ASP A 471     9151   9203   8766    313   -995     21       C  
ATOM   3668  CG  ASP A 471     -36.542  30.648 -51.100  1.00 69.95           C  
ANISOU 3668  CG  ASP A 471     9099   8960   8518    290   -939     32       C  
ATOM   3669  OD1 ASP A 471     -36.014  31.387 -50.242  1.00 66.08           O  
ANISOU 3669  OD1 ASP A 471     8627   8429   8052    296   -866     27       O  
ATOM   3670  OD2 ASP A 471     -36.179  30.625 -52.294  1.00 79.41           O1-
ANISOU 3670  OD2 ASP A 471    10382  10151   9638    264   -965     42       O1-
ATOM   3671  N   GLN A 472     -34.966  28.377 -48.846  1.00 45.07           N  
ANISOU 3671  N   GLN A 472     5789   5871   5464    164   -796    -91       N  
ATOM   3672  CA  GLN A 472     -33.638  27.797 -48.995  1.00 51.23           C  
ANISOU 3672  CA  GLN A 472     6607   6653   6206     94   -740   -129       C  
ATOM   3673  C   GLN A 472     -33.208  27.003 -47.767  1.00 46.24           C  
ANISOU 3673  C   GLN A 472     5896   6044   5629     68   -686   -172       C  
ATOM   3674  O   GLN A 472     -32.018  26.692 -47.634  1.00 42.07           O  
ANISOU 3674  O   GLN A 472     5392   5514   5079     19   -628   -204       O  
ATOM   3675  CB  GLN A 472     -32.606  28.891 -49.291  1.00 49.91           C  
ANISOU 3675  CB  GLN A 472     6544   6433   5985     76   -683   -120       C  
ATOM   3676  CG  GLN A 472     -32.206  28.991 -50.752  1.00 41.42           C  
ANISOU 3676  CG  GLN A 472     5569   5345   4823     48   -706   -107       C  
ATOM   3677  CD  GLN A 472     -31.493  30.290 -51.069  1.00 57.63           C  
ANISOU 3677  CD  GLN A 472     7731   7338   6826     43   -659    -86       C  
ATOM   3678  OE1 GLN A 472     -30.283  30.308 -51.296  1.00 62.50           O  
ANISOU 3678  OE1 GLN A 472     8403   7944   7402    -15   -598   -112       O  
ATOM   3679  NE2 GLN A 472     -32.241  31.387 -51.084  1.00 65.91           N  
ANISOU 3679  NE2 GLN A 472     8813   8349   7880    104   -686    -41       N  
ATOM   3680  N   TRP A 473     -34.139  26.673 -46.868  1.00 51.49           N  
ANISOU 3680  N   TRP A 473     6468   6731   6364    101   -704   -172       N  
ATOM   3681  CA  TRP A 473     -33.792  25.954 -45.646  1.00 43.10           C  
ANISOU 3681  CA  TRP A 473     5337   5688   5353     81   -654   -209       C  
ATOM   3682  C   TRP A 473     -33.141  24.613 -45.963  1.00 45.38           C  
ANISOU 3682  C   TRP A 473     5617   6007   5619     25   -647   -246       C  
ATOM   3683  O   TRP A 473     -31.984  24.366 -45.603  1.00 46.08           O  
ANISOU 3683  O   TRP A 473     5722   6092   5694    -11   -588   -275       O  
ATOM   3684  CB  TRP A 473     -35.041  25.751 -44.787  1.00 45.52           C  
ANISOU 3684  CB  TRP A 473     5548   6014   5732    123   -680   -201       C  
ATOM   3685  CG  TRP A 473     -35.304  26.851 -43.806  1.00 42.53           C  
ANISOU 3685  CG  TRP A 473     5159   5606   5396    170   -645   -185       C  
ATOM   3686  CD1 TRP A 473     -34.751  28.098 -43.799  1.00 40.02           C  
ANISOU 3686  CD1 TRP A 473     4914   5240   5052    183   -608   -169       C  
ATOM   3687  CD2 TRP A 473     -36.194  26.801 -42.685  1.00 35.41           C  
ANISOU 3687  CD2 TRP A 473     4172   4716   4565    206   -638   -186       C  
ATOM   3688  NE1 TRP A 473     -35.241  28.827 -42.743  1.00 42.03           N  
ANISOU 3688  NE1 TRP A 473     5136   5475   5358    228   -581   -160       N  
ATOM   3689  CE2 TRP A 473     -36.129  28.053 -42.043  1.00 38.14           C  
ANISOU 3689  CE2 TRP A 473     4545   5019   4926    243   -598   -170       C  
ATOM   3690  CE3 TRP A 473     -37.040  25.817 -42.162  1.00 35.64           C  
ANISOU 3690  CE3 TRP A 473     4108   4787   4648    206   -659   -199       C  
ATOM   3691  CZ2 TRP A 473     -36.877  28.348 -40.905  1.00 39.11           C  
ANISOU 3691  CZ2 TRP A 473     4606   5141   5114    285   -577   -168       C  
ATOM   3692  CZ3 TRP A 473     -37.781  26.112 -41.032  1.00 38.25           C  
ANISOU 3692  CZ3 TRP A 473     4374   5117   5042    245   -638   -196       C  
ATOM   3693  CH2 TRP A 473     -37.695  27.366 -40.416  1.00 41.87           C  
ANISOU 3693  CH2 TRP A 473     4862   5534   5514    286   -597   -181       C  
ATOM   3694  N   MET A 474     -33.877  23.730 -46.642  1.00 49.38           N  
ANISOU 3694  N   MET A 474     6097   6544   6120     18   -708   -246       N  
ATOM   3695  CA  MET A 474     -33.340  22.413 -46.967  1.00 44.09           C  
ANISOU 3695  CA  MET A 474     5424   5898   5429    -33   -703   -281       C  
ATOM   3696  C   MET A 474     -32.207  22.500 -47.979  1.00 44.35           C  
ANISOU 3696  C   MET A 474     5547   5917   5388    -71   -681   -291       C  
ATOM   3697  O   MET A 474     -31.301  21.659 -47.964  1.00 41.99           O  
ANISOU 3697  O   MET A 474     5255   5627   5073   -110   -643   -326       O  
ATOM   3698  CB  MET A 474     -34.453  21.506 -47.489  1.00 49.03           C  
ANISOU 3698  CB  MET A 474     6006   6558   6065    -37   -774   -280       C  
ATOM   3699  CG  MET A 474     -35.336  20.932 -46.395  1.00 44.74           C  
ANISOU 3699  CG  MET A 474     5365   6038   5598    -22   -777   -289       C  
ATOM   3700  SD  MET A 474     -34.428  20.634 -44.866  1.00 44.74           S  
ANISOU 3700  SD  MET A 474     5334   6027   5639    -31   -688   -319       S  
ATOM   3701  CE  MET A 474     -35.121  21.903 -43.809  1.00 44.31           C  
ANISOU 3701  CE  MET A 474     5238   5956   5641     28   -674   -291       C  
ATOM   3702  N   LYS A 475     -32.242  23.497 -48.867  1.00 49.15           N  
ANISOU 3702  N   LYS A 475     6227   6501   5948    -58   -703   -260       N  
ATOM   3703  CA  LYS A 475     -31.141  23.689 -49.804  1.00 45.48           C  
ANISOU 3703  CA  LYS A 475     5853   6018   5410    -97   -674   -268       C  
ATOM   3704  C   LYS A 475     -29.840  23.962 -49.061  1.00 46.78           C  
ANISOU 3704  C   LYS A 475     6027   6169   5579   -121   -587   -295       C  
ATOM   3705  O   LYS A 475     -28.825  23.297 -49.296  1.00 41.13           O  
ANISOU 3705  O   LYS A 475     5329   5464   4835   -163   -547   -329       O  
ATOM   3706  CB  LYS A 475     -31.463  24.832 -50.767  1.00 47.69           C  
ANISOU 3706  CB  LYS A 475     6213   6268   5639    -75   -709   -225       C  
ATOM   3707  CG  LYS A 475     -30.544  24.905 -51.977  1.00 46.46           C  
ANISOU 3707  CG  LYS A 475     6157   6097   5397   -119   -692   -231       C  
ATOM   3708  CD  LYS A 475     -30.164  26.343 -52.296  1.00 59.46           C  
ANISOU 3708  CD  LYS A 475     7892   7696   7004   -108   -666   -200       C  
ATOM   3709  CE  LYS A 475     -28.851  26.414 -53.058  1.00 66.91           C  
ANISOU 3709  CE  LYS A 475     8922   8624   7877   -165   -609   -221       C  
ATOM   3710  NZ  LYS A 475     -29.040  26.910 -54.449  1.00 75.04           N  
ANISOU 3710  NZ  LYS A 475    10054   9631   8825   -168   -648   -188       N  
ATOM   3711  N   LYS A 476     -29.855  24.938 -48.150  1.00 52.19           N  
ANISOU 3711  N   LYS A 476     6699   6831   6299    -93   -556   -281       N  
ATOM   3712  CA  LYS A 476     -28.667  25.212 -47.349  1.00 51.09           C  
ANISOU 3712  CA  LYS A 476     6561   6684   6166   -117   -477   -309       C  
ATOM   3713  C   LYS A 476     -28.345  24.045 -46.423  1.00 46.57           C  
ANISOU 3713  C   LYS A 476     5912   6146   5637   -130   -453   -347       C  
ATOM   3714  O   LYS A 476     -27.180  23.654 -46.298  1.00 49.31           O  
ANISOU 3714  O   LYS A 476     6264   6503   5966   -165   -402   -380       O  
ATOM   3715  CB  LYS A 476     -28.856  26.502 -46.550  1.00 42.26           C  
ANISOU 3715  CB  LYS A 476     5449   5532   5077    -86   -453   -287       C  
ATOM   3716  CG  LYS A 476     -27.728  27.512 -46.729  1.00 55.60           C  
ANISOU 3716  CG  LYS A 476     7214   7189   6722   -117   -392   -292       C  
ATOM   3717  CD  LYS A 476     -26.541  27.181 -45.839  1.00 62.60           C  
ANISOU 3717  CD  LYS A 476     8066   8095   7624   -154   -324   -336       C  
ATOM   3718  CE  LYS A 476     -25.336  28.053 -46.155  1.00 64.44           C  
ANISOU 3718  CE  LYS A 476     8370   8304   7808   -198   -263   -348       C  
ATOM   3719  NZ  LYS A 476     -24.233  27.848 -45.173  1.00 80.93           N  
ANISOU 3719  NZ  LYS A 476    10416  10417   9917   -230   -201   -391       N  
ATOM   3720  N   TRP A 477     -29.369  23.458 -45.792  1.00 47.63           N  
ANISOU 3720  N   TRP A 477     5974   6297   5825   -102   -488   -342       N  
ATOM   3721  CA  TRP A 477     -29.140  22.400 -44.809  1.00 42.75           C  
ANISOU 3721  CA  TRP A 477     5289   5705   5248   -110   -464   -374       C  
ATOM   3722  C   TRP A 477     -28.327  21.256 -45.399  1.00 40.33           C  
ANISOU 3722  C   TRP A 477     4998   5419   4907   -148   -452   -407       C  
ATOM   3723  O   TRP A 477     -27.404  20.744 -44.754  1.00 44.50           O  
ANISOU 3723  O   TRP A 477     5505   5958   5443   -163   -404   -438       O  
ATOM   3724  CB  TRP A 477     -30.474  21.879 -44.271  1.00 37.96           C  
ANISOU 3724  CB  TRP A 477     4613   5114   4697    -80   -507   -362       C  
ATOM   3725  CG  TRP A 477     -30.352  20.604 -43.484  1.00 32.07           C  
ANISOU 3725  CG  TRP A 477     3810   4391   3984    -93   -490   -392       C  
ATOM   3726  CD1 TRP A 477     -30.470  19.330 -43.961  1.00 34.07           C  
ANISOU 3726  CD1 TRP A 477     4054   4662   4228   -116   -512   -411       C  
ATOM   3727  CD2 TRP A 477     -30.092  20.483 -42.080  1.00 38.23           C  
ANISOU 3727  CD2 TRP A 477     4544   5174   4808    -83   -446   -407       C  
ATOM   3728  NE1 TRP A 477     -30.296  18.425 -42.943  1.00 37.11           N  
ANISOU 3728  NE1 TRP A 477     4392   5059   4649   -119   -483   -434       N  
ATOM   3729  CE2 TRP A 477     -30.064  19.107 -41.778  1.00 35.21           C  
ANISOU 3729  CE2 TRP A 477     4128   4812   4441    -98   -444   -432       C  
ATOM   3730  CE3 TRP A 477     -29.885  21.403 -41.049  1.00 36.47           C  
ANISOU 3730  CE3 TRP A 477     4309   4937   4610    -63   -408   -402       C  
ATOM   3731  CZ2 TRP A 477     -29.833  18.631 -40.489  1.00 33.59           C  
ANISOU 3731  CZ2 TRP A 477     3879   4612   4272    -91   -407   -448       C  
ATOM   3732  CZ3 TRP A 477     -29.651  20.928 -39.772  1.00 34.36           C  
ANISOU 3732  CZ3 TRP A 477     3997   4680   4379    -60   -372   -422       C  
ATOM   3733  CH2 TRP A 477     -29.629  19.555 -39.503  1.00 30.80           C  
ANISOU 3733  CH2 TRP A 477     3514   4249   3940    -72   -373   -443       C  
ATOM   3734  N   TRP A 478     -28.650  20.841 -46.621  1.00 39.81           N  
ANISOU 3734  N   TRP A 478     4968   5356   4801   -163   -495   -401       N  
ATOM   3735  CA  TRP A 478     -27.908  19.769 -47.266  1.00 34.55           C  
ANISOU 3735  CA  TRP A 478     4324   4705   4098   -199   -481   -433       C  
ATOM   3736  C   TRP A 478     -26.661  20.260 -47.985  1.00 37.35           C  
ANISOU 3736  C   TRP A 478     4747   5049   4394   -229   -436   -445       C  
ATOM   3737  O   TRP A 478     -25.774  19.449 -48.276  1.00 43.18           O  
ANISOU 3737  O   TRP A 478     5496   5800   5109   -255   -405   -478       O  
ATOM   3738  CB  TRP A 478     -28.822  19.010 -48.230  1.00 32.26           C  
ANISOU 3738  CB  TRP A 478     4043   4424   3789   -207   -546   -426       C  
ATOM   3739  CG  TRP A 478     -29.761  18.132 -47.479  1.00 31.63           C  
ANISOU 3739  CG  TRP A 478     3891   4362   3767   -194   -573   -431       C  
ATOM   3740  CD1 TRP A 478     -31.110  18.288 -47.346  1.00 37.32           C  
ANISOU 3740  CD1 TRP A 478     4570   5090   4522   -171   -629   -406       C  
ATOM   3741  CD2 TRP A 478     -29.412  16.978 -46.709  1.00 33.57           C  
ANISOU 3741  CD2 TRP A 478     4096   4619   4042   -204   -541   -463       C  
ATOM   3742  NE1 TRP A 478     -31.625  17.288 -46.555  1.00 33.12           N  
ANISOU 3742  NE1 TRP A 478     3973   4572   4038   -173   -630   -422       N  
ATOM   3743  CE2 TRP A 478     -30.601  16.472 -46.152  1.00 26.75           C  
ANISOU 3743  CE2 TRP A 478     3171   3765   3228   -192   -578   -456       C  
ATOM   3744  CE3 TRP A 478     -28.209  16.316 -46.447  1.00 32.83           C  
ANISOU 3744  CE3 TRP A 478     4011   4528   3936   -220   -486   -497       C  
ATOM   3745  CZ2 TRP A 478     -30.621  15.338 -45.347  1.00 32.37           C  
ANISOU 3745  CZ2 TRP A 478     3840   4484   3974   -198   -557   -479       C  
ATOM   3746  CZ3 TRP A 478     -28.230  15.192 -45.648  1.00 33.04           C  
ANISOU 3746  CZ3 TRP A 478     3994   4562   3998   -218   -471   -518       C  
ATOM   3747  CH2 TRP A 478     -29.427  14.713 -45.108  1.00 33.94           C  
ANISOU 3747  CH2 TRP A 478     4058   4680   4158   -210   -505   -509       C  
ATOM   3748  N   GLU A 479     -26.570  21.558 -48.278  1.00 37.99           N  
ANISOU 3748  N   GLU A 479     4876   5106   4452   -225   -430   -420       N  
ATOM   3749  CA  GLU A 479     -25.290  22.120 -48.693  1.00 31.06           C  
ANISOU 3749  CA  GLU A 479     4055   4218   3527   -258   -372   -436       C  
ATOM   3750  C   GLU A 479     -24.278  22.060 -47.556  1.00 37.38           C  
ANISOU 3750  C   GLU A 479     4809   5034   4360   -265   -308   -467       C  
ATOM   3751  O   GLU A 479     -23.110  21.720 -47.774  1.00 43.79           O  
ANISOU 3751  O   GLU A 479     5632   5860   5145   -296   -260   -500       O  
ATOM   3752  CB  GLU A 479     -25.471  23.558 -49.178  1.00 39.29           C  
ANISOU 3752  CB  GLU A 479     5165   5226   4539   -253   -376   -400       C  
ATOM   3753  CG  GLU A 479     -25.966  23.673 -50.610  1.00 52.60           C  
ANISOU 3753  CG  GLU A 479     6924   6897   6163   -259   -425   -375       C  
ATOM   3754  CD  GLU A 479     -26.069  25.112 -51.075  1.00 69.57           C  
ANISOU 3754  CD  GLU A 479     9150   9006   8278   -252   -425   -338       C  
ATOM   3755  OE1 GLU A 479     -26.076  26.017 -50.214  1.00 67.60           O  
ANISOU 3755  OE1 GLU A 479     8887   8736   8062   -232   -400   -326       O  
ATOM   3756  OE2 GLU A 479     -26.145  25.338 -52.301  1.00 82.48           O1-
ANISOU 3756  OE2 GLU A 479    10865  10626   9849   -265   -449   -320       O1-
ATOM   3757  N   MET A 480     -24.709  22.385 -46.333  1.00 40.04           N  
ANISOU 3757  N   MET A 480     5091   5369   4752   -236   -306   -459       N  
ATOM   3758  CA  MET A 480     -23.811  22.302 -45.184  1.00 38.17           C  
ANISOU 3758  CA  MET A 480     4809   5150   4545   -241   -253   -488       C  
ATOM   3759  C   MET A 480     -23.502  20.855 -44.823  1.00 34.58           C  
ANISOU 3759  C   MET A 480     4304   4727   4109   -240   -248   -520       C  
ATOM   3760  O   MET A 480     -22.376  20.540 -44.420  1.00 37.57           O  
ANISOU 3760  O   MET A 480     4664   5127   4485   -254   -202   -552       O  
ATOM   3761  CB  MET A 480     -24.415  23.036 -43.988  1.00 39.29           C  
ANISOU 3761  CB  MET A 480     4914   5279   4737   -210   -254   -471       C  
ATOM   3762  CG  MET A 480     -25.045  24.368 -44.332  1.00 35.93           C  
ANISOU 3762  CG  MET A 480     4538   4815   4301   -196   -269   -433       C  
ATOM   3763  SD  MET A 480     -25.766  25.206 -42.912  1.00 35.15           S  
ANISOU 3763  SD  MET A 480     4396   4697   4260   -157   -264   -415       S  
ATOM   3764  CE  MET A 480     -24.418  25.073 -41.747  1.00 37.55           C  
ANISOU 3764  CE  MET A 480     4665   5025   4576   -184   -197   -459       C  
ATOM   3765  N   LYS A 481     -24.487  19.963 -44.951  1.00 44.04           N  
ANISOU 3765  N   LYS A 481     5479   5927   5325   -223   -296   -511       N  
ATOM   3766  CA  LYS A 481     -24.234  18.550 -44.692  1.00 37.97           C  
ANISOU 3766  CA  LYS A 481     4676   5181   4570   -223   -291   -539       C  
ATOM   3767  C   LYS A 481     -23.160  18.009 -45.624  1.00 44.23           C  
ANISOU 3767  C   LYS A 481     5507   5984   5313   -252   -262   -568       C  
ATOM   3768  O   LYS A 481     -22.259  17.280 -45.194  1.00 47.27           O  
ANISOU 3768  O   LYS A 481     5868   6389   5704   -252   -225   -600       O  
ATOM   3769  CB  LYS A 481     -25.525  17.747 -44.847  1.00 43.00           C  
ANISOU 3769  CB  LYS A 481     5294   5815   5228   -210   -347   -524       C  
ATOM   3770  CG  LYS A 481     -26.462  17.816 -43.657  1.00 42.83           C  
ANISOU 3770  CG  LYS A 481     5213   5793   5267   -181   -362   -508       C  
ATOM   3771  CD  LYS A 481     -26.062  16.821 -42.583  1.00 39.52           C  
ANISOU 3771  CD  LYS A 481     4748   5387   4880   -172   -333   -533       C  
ATOM   3772  CE  LYS A 481     -27.182  16.635 -41.578  1.00 33.70           C  
ANISOU 3772  CE  LYS A 481     3958   4648   4197   -149   -353   -518       C  
ATOM   3773  NZ  LYS A 481     -26.685  16.073 -40.299  1.00 32.46           N  
ANISOU 3773  NZ  LYS A 481     3765   4500   4070   -136   -316   -536       N  
ATOM   3774  N   ARG A 482     -23.244  18.353 -46.910  1.00 35.20           N  
ANISOU 3774  N   ARG A 482     4427   4828   4119   -274   -278   -558       N  
ATOM   3775  CA  ARG A 482     -22.208  17.953 -47.855  1.00 35.60           C  
ANISOU 3775  CA  ARG A 482     4522   4887   4119   -305   -244   -586       C  
ATOM   3776  C   ARG A 482     -20.888  18.651 -47.549  1.00 35.80           C  
ANISOU 3776  C   ARG A 482     4546   4923   4133   -321   -179   -607       C  
ATOM   3777  O   ARG A 482     -19.829  18.014 -47.523  1.00 33.54           O  
ANISOU 3777  O   ARG A 482     4246   4661   3839   -331   -136   -643       O  
ATOM   3778  CB  ARG A 482     -22.658  18.261 -49.284  1.00 45.51           C  
ANISOU 3778  CB  ARG A 482     5850   6123   5317   -326   -277   -567       C  
ATOM   3779  CG  ARG A 482     -23.830  17.428 -49.782  1.00 40.71           C  
ANISOU 3779  CG  ARG A 482     5246   5512   4710   -319   -342   -555       C  
ATOM   3780  CD  ARG A 482     -24.458  18.069 -51.012  1.00 43.61           C  
ANISOU 3780  CD  ARG A 482     5682   5861   5025   -332   -387   -526       C  
ATOM   3781  NE  ARG A 482     -25.678  17.391 -51.436  1.00 57.55           N  
ANISOU 3781  NE  ARG A 482     7442   7630   6794   -327   -457   -513       N  
ATOM   3782  CZ  ARG A 482     -25.851  16.838 -52.629  1.00 55.71           C  
ANISOU 3782  CZ  ARG A 482     7263   7396   6508   -352   -486   -519       C  
ATOM   3783  NH1 ARG A 482     -24.895  16.856 -53.544  1.00 48.41           N  
ANISOU 3783  NH1 ARG A 482     6406   6466   5522   -383   -448   -538       N  
ATOM   3784  NH2 ARG A 482     -27.011  16.253 -52.911  1.00 54.09           N  
ANISOU 3784  NH2 ARG A 482     7044   7197   6310   -350   -553   -509       N  
ATOM   3785  N   GLU A 483     -20.933  19.964 -47.311  1.00 48.03           N  
ANISOU 3785  N   GLU A 483     6111   6457   5682   -326   -171   -586       N  
ATOM   3786  CA  GLU A 483     -19.702  20.736 -47.162  1.00 47.67           C  
ANISOU 3786  CA  GLU A 483     6073   6420   5619   -354   -109   -607       C  
ATOM   3787  C   GLU A 483     -19.018  20.458 -45.827  1.00 42.62           C  
ANISOU 3787  C   GLU A 483     5359   5811   5023   -340    -76   -634       C  
ATOM   3788  O   GLU A 483     -17.800  20.254 -45.775  1.00 48.73           O  
ANISOU 3788  O   GLU A 483     6116   6614   5785   -359    -27   -670       O  
ATOM   3789  CB  GLU A 483     -20.000  22.228 -47.312  1.00 48.06           C  
ANISOU 3789  CB  GLU A 483     6170   6436   5653   -365   -108   -576       C  
ATOM   3790  CG  GLU A 483     -18.799  23.130 -47.079  1.00 63.22           C  
ANISOU 3790  CG  GLU A 483     8101   8362   7557   -401    -43   -597       C  
ATOM   3791  CD  GLU A 483     -19.169  24.427 -46.385  1.00 83.81           C  
ANISOU 3791  CD  GLU A 483    10719  10941  10184   -396    -40   -573       C  
ATOM   3792  OE1 GLU A 483     -20.367  24.783 -46.382  1.00 74.86           O  
ANISOU 3792  OE1 GLU A 483     9602   9777   9064   -364    -89   -533       O  
ATOM   3793  OE2 GLU A 483     -18.261  25.091 -45.841  1.00 81.01           O1-
ANISOU 3793  OE2 GLU A 483    10356  10596   9830   -424     12   -594       O1-
ATOM   3794  N   ILE A 484     -19.782  20.441 -44.738  1.00 33.08           N  
ANISOU 3794  N   ILE A 484     4105   4599   3866   -307   -103   -617       N  
ATOM   3795  CA  ILE A 484     -19.194  20.377 -43.401  1.00 29.83           C  
ANISOU 3795  CA  ILE A 484     3630   4212   3490   -294    -75   -638       C  
ATOM   3796  C   ILE A 484     -19.090  18.943 -42.900  1.00 32.38           C  
ANISOU 3796  C   ILE A 484     3904   4560   3838   -267    -82   -658       C  
ATOM   3797  O   ILE A 484     -18.022  18.502 -42.469  1.00 36.60           O  
ANISOU 3797  O   ILE A 484     4404   5127   4374   -267    -47   -691       O  
ATOM   3798  CB  ILE A 484     -20.006  21.255 -42.425  1.00 28.79           C  
ANISOU 3798  CB  ILE A 484     3484   4060   3396   -275    -91   -611       C  
ATOM   3799  CG1 ILE A 484     -20.044  22.705 -42.913  1.00 33.46           C  
ANISOU 3799  CG1 ILE A 484     4133   4621   3961   -299    -79   -591       C  
ATOM   3800  CG2 ILE A 484     -19.422  21.175 -41.023  1.00 29.71           C  
ANISOU 3800  CG2 ILE A 484     3540   4203   3545   -264    -65   -632       C  
ATOM   3801  CD1 ILE A 484     -20.884  23.618 -42.048  1.00 29.63           C  
ANISOU 3801  CD1 ILE A 484     3641   4109   3510   -276    -92   -564       C  
ATOM   3802  N   VAL A 485     -20.194  18.191 -42.946  1.00 36.70           N  
ANISOU 3802  N   VAL A 485     4448   5092   4404   -244   -127   -639       N  
ATOM   3803  CA  VAL A 485     -20.211  16.838 -42.394  1.00 34.46           C  
ANISOU 3803  CA  VAL A 485     4126   4823   4145   -218   -133   -654       C  
ATOM   3804  C   VAL A 485     -19.729  15.786 -43.382  1.00 40.48           C  
ANISOU 3804  C   VAL A 485     4914   5592   4876   -227   -126   -678       C  
ATOM   3805  O   VAL A 485     -19.450  14.649 -42.972  1.00 39.16           O  
ANISOU 3805  O   VAL A 485     4721   5435   4721   -205   -119   -696       O  
ATOM   3806  CB  VAL A 485     -21.627  16.465 -41.908  1.00 35.03           C  
ANISOU 3806  CB  VAL A 485     4181   4876   4255   -195   -179   -627       C  
ATOM   3807  CG1 VAL A 485     -21.563  15.410 -40.810  1.00 37.47           C  
ANISOU 3807  CG1 VAL A 485     4443   5196   4598   -167   -173   -640       C  
ATOM   3808  CG2 VAL A 485     -22.363  17.699 -41.420  1.00 36.59           C  
ANISOU 3808  CG2 VAL A 485     4373   5056   4473   -190   -192   -598       C  
ATOM   3809  N   GLY A 486     -19.606  16.124 -44.661  1.00 40.37           N  
ANISOU 3809  N   GLY A 486     4954   5568   4817   -256   -125   -677       N  
ATOM   3810  CA  GLY A 486     -19.281  15.109 -45.651  1.00 36.92           C  
ANISOU 3810  CA  GLY A 486     4549   5133   4348   -266   -119   -698       C  
ATOM   3811  C   GLY A 486     -20.371  14.071 -45.785  1.00 37.00           C  
ANISOU 3811  C   GLY A 486     4563   5124   4370   -253   -164   -688       C  
ATOM   3812  O   GLY A 486     -20.084  12.888 -46.005  1.00 40.94           O  
ANISOU 3812  O   GLY A 486     5066   5625   4862   -246   -155   -711       O  
ATOM   3813  N   VAL A 487     -21.624  14.494 -45.653  1.00 30.72           N  
ANISOU 3813  N   VAL A 487     3766   4312   3595   -250   -212   -654       N  
ATOM   3814  CA  VAL A 487     -22.778  13.607 -45.674  1.00 27.41           C  
ANISOU 3814  CA  VAL A 487     3341   3878   3194   -243   -258   -644       C  
ATOM   3815  C   VAL A 487     -23.767  14.143 -46.698  1.00 34.29           C  
ANISOU 3815  C   VAL A 487     4253   4736   4041   -262   -308   -617       C  
ATOM   3816  O   VAL A 487     -24.048  15.347 -46.723  1.00 38.77           O  
ANISOU 3816  O   VAL A 487     4826   5296   4606   -261   -319   -591       O  
ATOM   3817  CB  VAL A 487     -23.433  13.499 -44.284  1.00 28.07           C  
ANISOU 3817  CB  VAL A 487     3366   3962   3336   -215   -268   -630       C  
ATOM   3818  CG1 VAL A 487     -24.758  12.771 -44.372  1.00 30.47           C  
ANISOU 3818  CG1 VAL A 487     3663   4253   3660   -216   -316   -617       C  
ATOM   3819  CG2 VAL A 487     -22.492  12.800 -43.312  1.00 17.90           C  
ANISOU 3819  CG2 VAL A 487     2045   2689   2067   -193   -226   -656       C  
ATOM   3820  N   VAL A 488     -24.289  13.257 -47.541  1.00 38.55           N  
ANISOU 3820  N   VAL A 488     4822   5268   4558   -278   -339   -623       N  
ATOM   3821  CA  VAL A 488     -25.170  13.634 -48.639  1.00 35.88           C  
ANISOU 3821  CA  VAL A 488     4526   4921   4187   -298   -392   -601       C  
ATOM   3822  C   VAL A 488     -26.525  12.970 -48.440  1.00 37.03           C  
ANISOU 3822  C   VAL A 488     4640   5064   4364   -296   -447   -590       C  
ATOM   3823  O   VAL A 488     -26.607  11.814 -48.009  1.00 40.52           O  
ANISOU 3823  O   VAL A 488     5062   5506   4828   -296   -439   -610       O  
ATOM   3824  CB  VAL A 488     -24.562  13.253 -50.008  1.00 34.83           C  
ANISOU 3824  CB  VAL A 488     4463   4784   3986   -329   -381   -622       C  
ATOM   3825  CG1 VAL A 488     -24.285  11.756 -50.084  1.00 34.30           C  
ANISOU 3825  CG1 VAL A 488     4401   4716   3917   -336   -365   -657       C  
ATOM   3826  CG2 VAL A 488     -25.472  13.697 -51.144  1.00 40.53           C  
ANISOU 3826  CG2 VAL A 488     5233   5498   4668   -348   -442   -597       C  
ATOM   3827  N   GLU A 489     -27.588  13.716 -48.726  1.00 44.97           N  
ANISOU 3827  N   GLU A 489     5643   6070   5375   -292   -501   -557       N  
ATOM   3828  CA  GLU A 489     -28.923  13.144 -48.681  1.00 39.64           C  
ANISOU 3828  CA  GLU A 489     4935   5400   4727   -296   -558   -548       C  
ATOM   3829  C   GLU A 489     -29.089  12.122 -49.804  1.00 43.44           C  
ANISOU 3829  C   GLU A 489     5463   5881   5163   -333   -584   -569       C  
ATOM   3830  O   GLU A 489     -28.614  12.341 -50.924  1.00 52.49           O  
ANISOU 3830  O   GLU A 489     6674   7023   6248   -352   -586   -573       O  
ATOM   3831  CB  GLU A 489     -29.985  14.243 -48.795  1.00 40.28           C  
ANISOU 3831  CB  GLU A 489     4998   5485   4820   -278   -612   -508       C  
ATOM   3832  CG  GLU A 489     -30.146  14.857 -50.184  1.00 48.34           C  
ANISOU 3832  CG  GLU A 489     6083   6503   5779   -291   -654   -491       C  
ATOM   3833  CD  GLU A 489     -29.124  15.940 -50.485  1.00 51.53           C  
ANISOU 3833  CD  GLU A 489     6540   6893   6145   -287   -613   -482       C  
ATOM   3834  OE1 GLU A 489     -27.983  15.852 -49.985  1.00 48.62           O  
ANISOU 3834  OE1 GLU A 489     6172   6520   5779   -289   -547   -504       O  
ATOM   3835  OE2 GLU A 489     -29.464  16.884 -51.230  1.00 53.12           O1-
ANISOU 3835  OE2 GLU A 489     6783   7087   6313   -281   -647   -452       O1-
ATOM   3836  N   PRO A 490     -29.725  10.980 -49.531  1.00 29.96           N  
ANISOU 3836  N   PRO A 490     3728   4174   3480   -347   -601   -585       N  
ATOM   3837  CA  PRO A 490     -29.951   9.989 -50.592  1.00 33.42           C  
ANISOU 3837  CA  PRO A 490     4214   4609   3874   -387   -627   -608       C  
ATOM   3838  C   PRO A 490     -31.137  10.299 -51.489  1.00 40.64           C  
ANISOU 3838  C   PRO A 490     5136   5539   4768   -406   -708   -588       C  
ATOM   3839  O   PRO A 490     -31.288   9.647 -52.532  1.00 46.41           O  
ANISOU 3839  O   PRO A 490     5916   6269   5449   -444   -735   -605       O  
ATOM   3840  CB  PRO A 490     -30.174   8.690 -49.810  1.00 33.98           C  
ANISOU 3840  CB  PRO A 490     4254   4672   3985   -396   -608   -632       C  
ATOM   3841  CG  PRO A 490     -30.728   9.137 -48.503  1.00 35.24           C  
ANISOU 3841  CG  PRO A 490     4338   4840   4213   -365   -606   -610       C  
ATOM   3842  CD  PRO A 490     -30.110  10.474 -48.202  1.00 31.32           C  
ANISOU 3842  CD  PRO A 490     3836   4347   3719   -331   -584   -588       C  
ATOM   3843  N   VAL A 491     -31.976  11.262 -51.122  1.00 39.93           N  
ANISOU 3843  N   VAL A 491     4997   5462   4711   -380   -747   -552       N  
ATOM   3844  CA  VAL A 491     -33.129  11.659 -51.926  1.00 40.67           C  
ANISOU 3844  CA  VAL A 491     5089   5576   4787   -388   -829   -530       C  
ATOM   3845  C   VAL A 491     -33.190  13.181 -51.934  1.00 45.30           C  
ANISOU 3845  C   VAL A 491     5676   6163   5374   -348   -843   -488       C  
ATOM   3846  O   VAL A 491     -33.069  13.803 -50.868  1.00 46.97           O  
ANISOU 3846  O   VAL A 491     5843   6370   5636   -312   -809   -474       O  
ATOM   3847  CB  VAL A 491     -34.430  11.047 -51.380  1.00 38.99           C  
ANISOU 3847  CB  VAL A 491     4800   5383   4630   -398   -871   -531       C  
ATOM   3848  CG1 VAL A 491     -35.646  11.723 -51.998  1.00 45.23           C  
ANISOU 3848  CG1 VAL A 491     5567   6202   5416   -391   -958   -501       C  
ATOM   3849  CG2 VAL A 491     -34.465   9.546 -51.634  1.00 38.55           C  
ANISOU 3849  CG2 VAL A 491     4764   5323   4562   -448   -866   -571       C  
ATOM   3850  N   PRO A 492     -33.354  13.824 -53.091  1.00 57.56           N  
ANISOU 3850  N   PRO A 492     7285   7719   6868   -351   -889   -468       N  
ATOM   3851  CA  PRO A 492     -33.483  15.287 -53.101  1.00 54.42           C  
ANISOU 3851  CA  PRO A 492     6894   7315   6469   -309   -904   -426       C  
ATOM   3852  C   PRO A 492     -34.677  15.728 -52.268  1.00 49.35           C  
ANISOU 3852  C   PRO A 492     6164   6690   5896   -270   -943   -400       C  
ATOM   3853  O   PRO A 492     -35.737  15.100 -52.286  1.00 54.59           O  
ANISOU 3853  O   PRO A 492     6776   7380   6585   -282   -996   -405       O  
ATOM   3854  CB  PRO A 492     -33.671  15.618 -54.586  1.00 46.73           C  
ANISOU 3854  CB  PRO A 492     5997   6342   5414   -324   -961   -411       C  
ATOM   3855  CG  PRO A 492     -34.162  14.347 -55.203  1.00 61.32           C  
ANISOU 3855  CG  PRO A 492     7847   8210   7240   -370  -1002   -440       C  
ATOM   3856  CD  PRO A 492     -33.481  13.250 -54.441  1.00 55.77           C  
ANISOU 3856  CD  PRO A 492     7122   7497   6570   -393   -933   -482       C  
ATOM   3857  N   HIS A 493     -34.494  16.819 -51.529  1.00 44.49           N  
ANISOU 3857  N   HIS A 493     5532   6060   5312   -227   -912   -375       N  
ATOM   3858  CA  HIS A 493     -35.469  17.257 -50.536  1.00 46.10           C  
ANISOU 3858  CA  HIS A 493     5650   6275   5589   -186   -929   -355       C  
ATOM   3859  C   HIS A 493     -35.846  18.708 -50.800  1.00 47.84           C  
ANISOU 3859  C   HIS A 493     5890   6485   5801   -137   -960   -310       C  
ATOM   3860  O   HIS A 493     -35.009  19.606 -50.662  1.00 43.41           O  
ANISOU 3860  O   HIS A 493     5377   5893   5222   -121   -912   -298       O  
ATOM   3861  CB  HIS A 493     -34.919  17.082 -49.121  1.00 42.65           C  
ANISOU 3861  CB  HIS A 493     5169   5827   5210   -177   -854   -372       C  
ATOM   3862  CG  HIS A 493     -35.134  15.711 -48.559  1.00 38.69           C  
ANISOU 3862  CG  HIS A 493     4618   5340   4742   -208   -842   -405       C  
ATOM   3863  ND1 HIS A 493     -34.989  15.423 -47.219  1.00 39.38           N  
ANISOU 3863  ND1 HIS A 493     4652   5422   4887   -198   -790   -418       N  
ATOM   3864  CD2 HIS A 493     -35.488  14.549 -49.157  1.00 41.10           C  
ANISOU 3864  CD2 HIS A 493     4926   5660   5029   -251   -873   -429       C  
ATOM   3865  CE1 HIS A 493     -35.242  14.142 -47.016  1.00 42.16           C  
ANISOU 3865  CE1 HIS A 493     4980   5785   5256   -231   -788   -445       C  
ATOM   3866  NE2 HIS A 493     -35.547  13.589 -48.176  1.00 41.38           N  
ANISOU 3866  NE2 HIS A 493     4913   5697   5113   -265   -837   -454       N  
ATOM   3867  N   ASP A 494     -37.105  18.934 -51.170  1.00 66.46           N  
ANISOU 3867  N   ASP A 494     8211   8869   8172   -113  -1038   -285       N  
ATOM   3868  CA  ASP A 494     -37.610  20.281 -51.378  1.00 60.44           C  
ANISOU 3868  CA  ASP A 494     7462   8096   7407    -56  -1073   -239       C  
ATOM   3869  C   ASP A 494     -37.852  20.964 -50.033  1.00 57.35           C  
ANISOU 3869  C   ASP A 494     7008   7694   7090     -8  -1032   -227       C  
ATOM   3870  O   ASP A 494     -37.558  20.422 -48.964  1.00 54.95           O  
ANISOU 3870  O   ASP A 494     6656   7390   6835    -22   -975   -254       O  
ATOM   3871  CB  ASP A 494     -38.881  20.249 -52.227  1.00 53.09           C  
ANISOU 3871  CB  ASP A 494     6506   7201   6463    -41  -1175   -218       C  
ATOM   3872  CG  ASP A 494     -39.904  19.245 -51.720  1.00 65.05           C  
ANISOU 3872  CG  ASP A 494     7915   8762   8040    -58  -1207   -241       C  
ATOM   3873  OD1 ASP A 494     -40.116  19.164 -50.492  1.00 62.38           O  
ANISOU 3873  OD1 ASP A 494     7502   8424   7774    -42  -1164   -249       O  
ATOM   3874  OD2 ASP A 494     -40.504  18.538 -52.558  1.00 72.92           O1-
ANISOU 3874  OD2 ASP A 494     8904   9792   9008    -90  -1274   -251       O1-
ATOM   3875  N   GLU A 495     -38.409  22.171 -50.085  1.00 49.50           N  
ANISOU 3875  N   GLU A 495     6017   6686   6103     51  -1060   -186       N  
ATOM   3876  CA  GLU A 495     -38.634  22.949 -48.874  1.00 45.19           C  
ANISOU 3876  CA  GLU A 495     5424   6125   5623    100  -1018   -173       C  
ATOM   3877  C   GLU A 495     -39.876  22.515 -48.107  1.00 46.56           C  
ANISOU 3877  C   GLU A 495     5480   6336   5874    122  -1046   -177       C  
ATOM   3878  O   GLU A 495     -40.155  23.082 -47.046  1.00 53.59           O  
ANISOU 3878  O   GLU A 495     6323   7215   6822    162  -1010   -170       O  
ATOM   3879  CB  GLU A 495     -38.719  24.439 -49.214  1.00 46.92           C  
ANISOU 3879  CB  GLU A 495     5702   6308   5820    158  -1031   -128       C  
ATOM   3880  CG  GLU A 495     -37.502  24.959 -49.965  1.00 55.87           C  
ANISOU 3880  CG  GLU A 495     6954   7399   6874    133   -997   -123       C  
ATOM   3881  CD  GLU A 495     -36.199  24.688 -49.232  1.00 54.67           C  
ANISOU 3881  CD  GLU A 495     6821   7227   6725     89   -904   -159       C  
ATOM   3882  OE1 GLU A 495     -36.165  24.829 -47.991  1.00 54.03           O  
ANISOU 3882  OE1 GLU A 495     6686   7140   6704    104   -854   -169       O  
ATOM   3883  OE2 GLU A 495     -35.206  24.328 -49.900  1.00 49.49           O1-
ANISOU 3883  OE2 GLU A 495     6232   6563   6010     40   -880   -177       O1-
ATOM   3884  N   THR A 496     -40.634  21.540 -48.611  1.00 38.42           N  
ANISOU 3884  N   THR A 496     4402   5351   4845     93  -1106   -191       N  
ATOM   3885  CA  THR A 496     -41.677  20.936 -47.791  1.00 42.46           C  
ANISOU 3885  CA  THR A 496     4799   5900   5432     96  -1117   -205       C  
ATOM   3886  C   THR A 496     -41.092  20.077 -46.678  1.00 41.20           C  
ANISOU 3886  C   THR A 496     4613   5733   5310     56  -1039   -243       C  
ATOM   3887  O   THR A 496     -41.752  19.874 -45.653  1.00 34.66           O  
ANISOU 3887  O   THR A 496     3699   4920   4549     68  -1019   -250       O  
ATOM   3888  CB  THR A 496     -42.622  20.100 -48.656  1.00 40.19           C  
ANISOU 3888  CB  THR A 496     4471   5665   5134     67  -1202   -213       C  
ATOM   3889  OG1 THR A 496     -41.967  18.887 -49.048  1.00 44.33           O  
ANISOU 3889  OG1 THR A 496     5032   6192   5620     -8  -1188   -251       O  
ATOM   3890  CG2 THR A 496     -43.033  20.874 -49.899  1.00 38.25           C  
ANISOU 3890  CG2 THR A 496     4270   5427   4835    103  -1285   -176       C  
ATOM   3891  N   TYR A 497     -39.876  19.569 -46.860  1.00 45.21           N  
ANISOU 3891  N   TYR A 497     5188   6217   5771     11   -994   -266       N  
ATOM   3892  CA  TYR A 497     -39.173  18.838 -45.817  1.00 40.33           C  
ANISOU 3892  CA  TYR A 497     4556   5587   5181    -19   -919   -298       C  
ATOM   3893  C   TYR A 497     -38.641  19.791 -44.754  1.00 42.41           C  
ANISOU 3893  C   TYR A 497     4824   5818   5472     19   -853   -287       C  
ATOM   3894  O   TYR A 497     -38.298  20.944 -45.035  1.00 41.69           O  
ANISOU 3894  O   TYR A 497     4784   5701   5356     52   -849   -262       O  
ATOM   3895  CB  TYR A 497     -37.999  18.052 -46.402  1.00 38.19           C  
ANISOU 3895  CB  TYR A 497     4357   5302   4850    -72   -893   -326       C  
ATOM   3896  CG  TYR A 497     -38.365  16.915 -47.328  1.00 47.05           C  
ANISOU 3896  CG  TYR A 497     5485   6450   5943   -120   -943   -346       C  
ATOM   3897  CD1 TYR A 497     -38.682  15.657 -46.830  1.00 46.85           C  
ANISOU 3897  CD1 TYR A 497     5411   6440   5950   -159   -932   -377       C  
ATOM   3898  CD2 TYR A 497     -38.352  17.090 -48.704  1.00 52.64           C  
ANISOU 3898  CD2 TYR A 497     6252   7162   6584   -132   -998   -335       C  
ATOM   3899  CE1 TYR A 497     -38.999  14.612 -47.680  1.00 46.19           C  
ANISOU 3899  CE1 TYR A 497     5338   6376   5836   -209   -974   -399       C  
ATOM   3900  CE2 TYR A 497     -38.667  16.055 -49.561  1.00 50.50           C  
ANISOU 3900  CE2 TYR A 497     5992   6914   6282   -180  -1044   -356       C  
ATOM   3901  CZ  TYR A 497     -38.990  14.817 -49.045  1.00 47.08           C  
ANISOU 3901  CZ  TYR A 497     5508   6495   5883   -220  -1031   -389       C  
ATOM   3902  OH  TYR A 497     -39.306  13.785 -49.899  1.00 52.90           O  
ANISOU 3902  OH  TYR A 497     6260   7251   6587   -273  -1074   -414       O  
ATOM   3903  N   CYS A 498     -38.579  19.297 -43.518  1.00 50.07           N  
ANISOU 3903  N   CYS A 498     5744   6788   6491     12   -800   -308       N  
ATOM   3904  CA  CYS A 498     -37.823  19.937 -42.440  1.00 47.46           C  
ANISOU 3904  CA  CYS A 498     5427   6428   6179     32   -729   -309       C  
ATOM   3905  C   CYS A 498     -36.997  18.832 -41.788  1.00 52.47           C  
ANISOU 3905  C   CYS A 498     6063   7061   6813    -10   -676   -344       C  
ATOM   3906  O   CYS A 498     -37.414  18.238 -40.790  1.00 53.78           O  
ANISOU 3906  O   CYS A 498     6172   7235   7026    -14   -652   -358       O  
ATOM   3907  CB  CYS A 498     -38.737  20.636 -41.442  1.00 46.17           C  
ANISOU 3907  CB  CYS A 498     5198   6265   6078     80   -718   -292       C  
ATOM   3908  SG  CYS A 498     -37.885  21.819 -40.373  1.00 56.18           S  
ANISOU 3908  SG  CYS A 498     6500   7491   7355    112   -642   -286       S  
ATOM   3909  N   ASP A 499     -35.822  18.565 -42.353  1.00 45.43           N  
ANISOU 3909  N   ASP A 499     5237   6157   5867    -39   -658   -359       N  
ATOM   3910  CA  ASP A 499     -34.997  17.440 -41.929  1.00 42.83           C  
ANISOU 3910  CA  ASP A 499     4915   5827   5530    -74   -616   -392       C  
ATOM   3911  C   ASP A 499     -34.332  17.676 -40.574  1.00 42.33           C  
ANISOU 3911  C   ASP A 499     4840   5751   5495    -60   -550   -402       C  
ATOM   3912  O   ASP A 499     -34.223  16.729 -39.785  1.00 40.36           O  
ANISOU 3912  O   ASP A 499     4563   5505   5266    -74   -521   -422       O  
ATOM   3913  CB  ASP A 499     -33.944  17.122 -42.995  1.00 38.56           C  
ANISOU 3913  CB  ASP A 499     4447   5281   4925   -104   -615   -407       C  
ATOM   3914  CG  ASP A 499     -34.560  16.626 -44.287  1.00 42.25           C  
ANISOU 3914  CG  ASP A 499     4930   5763   5360   -128   -678   -405       C  
ATOM   3915  OD1 ASP A 499     -35.747  16.235 -44.270  1.00 48.88           O  
ANISOU 3915  OD1 ASP A 499     5717   6622   6231   -129   -721   -400       O  
ATOM   3916  OD2 ASP A 499     -33.859  16.624 -45.320  1.00 39.74           O1-
ANISOU 3916  OD2 ASP A 499     4678   5438   4983   -147   -685   -410       O1-
ATOM   3917  N   PRO A 500     -33.850  18.889 -40.263  1.00 50.97           N  
ANISOU 3917  N   PRO A 500     5956   6826   6583    -34   -523   -388       N  
ATOM   3918  CA  PRO A 500     -33.383  19.126 -38.885  1.00 47.00           C  
ANISOU 3918  CA  PRO A 500     5435   6314   6109    -22   -465   -397       C  
ATOM   3919  C   PRO A 500     -34.439  18.822 -37.838  1.00 49.65           C  
ANISOU 3919  C   PRO A 500     5702   6657   6504     -6   -461   -395       C  
ATOM   3920  O   PRO A 500     -34.122  18.219 -36.805  1.00 50.90           O  
ANISOU 3920  O   PRO A 500     5842   6817   6681    -13   -421   -412       O  
ATOM   3921  CB  PRO A 500     -33.002  20.616 -38.886  1.00 46.56           C  
ANISOU 3921  CB  PRO A 500     5415   6236   6040      2   -448   -379       C  
ATOM   3922  CG  PRO A 500     -33.314  21.134 -40.261  1.00 45.09           C  
ANISOU 3922  CG  PRO A 500     5269   6046   5819      5   -497   -357       C  
ATOM   3923  CD  PRO A 500     -33.403  19.962 -41.165  1.00 49.19           C  
ANISOU 3923  CD  PRO A 500     5790   6584   6314    -26   -534   -370       C  
ATOM   3924  N   ALA A 501     -35.698  19.189 -38.093  1.00 39.68           N  
ANISOU 3924  N   ALA A 501     4401   5403   5272     16   -501   -373       N  
ATOM   3925  CA  ALA A 501     -36.761  18.923 -37.130  1.00 39.99           C  
ANISOU 3925  CA  ALA A 501     4370   5453   5370     30   -494   -372       C  
ATOM   3926  C   ALA A 501     -36.996  17.433 -36.930  1.00 39.51           C  
ANISOU 3926  C   ALA A 501     4281   5409   5322     -8   -494   -395       C  
ATOM   3927  O   ALA A 501     -37.630  17.042 -35.944  1.00 36.40           O  
ANISOU 3927  O   ALA A 501     3838   5021   4972     -8   -470   -401       O  
ATOM   3928  CB  ALA A 501     -38.057  19.602 -37.572  1.00 42.17           C  
ANISOU 3928  CB  ALA A 501     4605   5741   5676     63   -542   -346       C  
ATOM   3929  N   SER A 502     -36.497  16.592 -37.839  1.00 39.52           N  
ANISOU 3929  N   SER A 502     4318   5415   5282    -43   -515   -409       N  
ATOM   3930  CA  SER A 502     -36.583  15.150 -37.661  1.00 37.76           C  
ANISOU 3930  CA  SER A 502     4083   5199   5064    -81   -509   -433       C  
ATOM   3931  C   SER A 502     -35.675  14.643 -36.548  1.00 37.00           C  
ANISOU 3931  C   SER A 502     4002   5087   4968    -84   -448   -450       C  
ATOM   3932  O   SER A 502     -35.769  13.465 -36.187  1.00 45.91           O  
ANISOU 3932  O   SER A 502     5124   6215   6104   -110   -434   -468       O  
ATOM   3933  CB  SER A 502     -36.248  14.439 -38.973  1.00 45.29           C  
ANISOU 3933  CB  SER A 502     5080   6158   5970   -115   -546   -444       C  
ATOM   3934  OG  SER A 502     -34.854  14.466 -39.224  1.00 44.26           O  
ANISOU 3934  OG  SER A 502     5011   6012   5792   -118   -518   -455       O  
ATOM   3935  N   LEU A 503     -34.796  15.487 -36.014  1.00 33.68           N  
ANISOU 3935  N   LEU A 503     3606   4655   4537    -60   -412   -447       N  
ATOM   3936  CA  LEU A 503     -33.994  15.152 -34.846  1.00 33.11           C  
ANISOU 3936  CA  LEU A 503     3542   4573   4466    -57   -359   -461       C  
ATOM   3937  C   LEU A 503     -34.665  15.711 -33.598  1.00 35.57           C  
ANISOU 3937  C   LEU A 503     3812   4881   4823    -33   -331   -452       C  
ATOM   3938  O   LEU A 503     -35.280  16.781 -33.638  1.00 36.44           O  
ANISOU 3938  O   LEU A 503     3902   4991   4954     -9   -342   -433       O  
ATOM   3939  CB  LEU A 503     -32.569  15.696 -34.975  1.00 30.65           C  
ANISOU 3939  CB  LEU A 503     3277   4255   4112    -51   -336   -469       C  
ATOM   3940  CG  LEU A 503     -31.625  15.426 -33.798  1.00 33.43           C  
ANISOU 3940  CG  LEU A 503     3636   4604   4460    -45   -287   -484       C  
ATOM   3941  CD1 LEU A 503     -31.427  13.933 -33.595  1.00 24.86           C  
ANISOU 3941  CD1 LEU A 503     2557   3520   3371    -61   -279   -502       C  
ATOM   3942  CD2 LEU A 503     -30.289  16.118 -33.999  1.00 32.70           C  
ANISOU 3942  CD2 LEU A 503     3581   4514   4330    -42   -269   -493       C  
ATOM   3943  N   PHE A 504     -34.543  14.973 -32.491  1.00 33.16           N  
ANISOU 3943  N   PHE A 504     3496   4570   4531    -39   -293   -464       N  
ATOM   3944  CA  PHE A 504     -35.275  15.303 -31.271  1.00 30.59           C  
ANISOU 3944  CA  PHE A 504     3132   4241   4248    -22   -262   -457       C  
ATOM   3945  C   PHE A 504     -34.979  16.722 -30.803  1.00 31.03           C  
ANISOU 3945  C   PHE A 504     3196   4289   4306      9   -241   -447       C  
ATOM   3946  O   PHE A 504     -35.897  17.490 -30.496  1.00 36.14           O  
ANISOU 3946  O   PHE A 504     3808   4934   4989     31   -240   -433       O  
ATOM   3947  CB  PHE A 504     -34.927  14.290 -30.176  1.00 29.99           C  
ANISOU 3947  CB  PHE A 504     3065   4158   4172    -34   -221   -472       C  
ATOM   3948  CG  PHE A 504     -35.427  14.667 -28.810  1.00 28.04           C  
ANISOU 3948  CG  PHE A 504     2792   3904   3958    -18   -180   -467       C  
ATOM   3949  CD1 PHE A 504     -36.712  14.339 -28.413  1.00 29.47           C  
ANISOU 3949  CD1 PHE A 504     2926   4089   4183    -26   -173   -464       C  
ATOM   3950  CD2 PHE A 504     -34.604  15.333 -27.915  1.00 31.55           C  
ANISOU 3950  CD2 PHE A 504     3260   4342   4387      2   -145   -470       C  
ATOM   3951  CE1 PHE A 504     -37.171  14.679 -27.154  1.00 31.55           C  
ANISOU 3951  CE1 PHE A 504     3168   4345   4475    -13   -129   -461       C  
ATOM   3952  CE2 PHE A 504     -35.058  15.677 -26.657  1.00 26.80           C  
ANISOU 3952  CE2 PHE A 504     2640   3732   3810     15   -105   -468       C  
ATOM   3953  CZ  PHE A 504     -36.343  15.350 -26.276  1.00 27.26           C  
ANISOU 3953  CZ  PHE A 504     2655   3791   3912      9    -95   -463       C  
ATOM   3954  N   HIS A 505     -33.698  17.090 -30.753  1.00 32.98           N  
ANISOU 3954  N   HIS A 505     3486   4530   4514     11   -225   -455       N  
ATOM   3955  CA  HIS A 505     -33.313  18.362 -30.149  1.00 33.21           C  
ANISOU 3955  CA  HIS A 505     3527   4549   4541     33   -197   -451       C  
ATOM   3956  C   HIS A 505     -33.866  19.547 -30.932  1.00 33.64           C  
ANISOU 3956  C   HIS A 505     3582   4595   4604     52   -222   -430       C  
ATOM   3957  O   HIS A 505     -34.250  20.564 -30.343  1.00 35.08           O  
ANISOU 3957  O   HIS A 505     3757   4764   4807     77   -202   -421       O  
ATOM   3958  CB  HIS A 505     -31.791  18.444 -30.042  1.00 29.68           C  
ANISOU 3958  CB  HIS A 505     3124   4105   4050     24   -178   -468       C  
ATOM   3959  CG  HIS A 505     -31.177  17.287 -29.317  1.00 27.88           C  
ANISOU 3959  CG  HIS A 505     2899   3885   3811     14   -158   -486       C  
ATOM   3960  ND1 HIS A 505     -31.155  16.009 -29.835  1.00 28.53           N  
ANISOU 3960  ND1 HIS A 505     2982   3972   3883     -2   -175   -492       N  
ATOM   3961  CD2 HIS A 505     -30.569  17.213 -28.109  1.00 30.07           C  
ANISOU 3961  CD2 HIS A 505     3182   4164   4080     20   -122   -497       C  
ATOM   3962  CE1 HIS A 505     -30.558  15.199 -28.979  1.00 31.31           C  
ANISOU 3962  CE1 HIS A 505     3344   4327   4225     -1   -151   -506       C  
ATOM   3963  NE2 HIS A 505     -30.192  15.904 -27.924  1.00 33.39           N  
ANISOU 3963  NE2 HIS A 505     3608   4590   4488     12   -121   -508       N  
ATOM   3964  N   VAL A 506     -33.912  19.436 -32.259  1.00 26.58           N  
ANISOU 3964  N   VAL A 506     2701   3707   3690     43   -266   -424       N  
ATOM   3965  CA  VAL A 506     -34.399  20.543 -33.076  1.00 29.02           C  
ANISOU 3965  CA  VAL A 506     3020   4007   4000     65   -295   -401       C  
ATOM   3966  C   VAL A 506     -35.902  20.729 -32.894  1.00 33.62           C  
ANISOU 3966  C   VAL A 506     3545   4594   4634     91   -313   -384       C  
ATOM   3967  O   VAL A 506     -36.387  21.857 -32.751  1.00 45.23           O  
ANISOU 3967  O   VAL A 506     5013   6050   6123    126   -310   -366       O  
ATOM   3968  CB  VAL A 506     -34.024  20.313 -34.550  1.00 24.80           C  
ANISOU 3968  CB  VAL A 506     2519   3479   3424     46   -338   -398       C  
ATOM   3969  CG1 VAL A 506     -34.582  21.416 -35.424  1.00 26.83           C  
ANISOU 3969  CG1 VAL A 506     2792   3725   3678     71   -372   -371       C  
ATOM   3970  CG2 VAL A 506     -32.512  20.221 -34.702  1.00 25.43           C  
ANISOU 3970  CG2 VAL A 506     2650   3556   3456     22   -313   -418       C  
ATOM   3971  N   SER A 507     -36.662  19.632 -32.895  1.00 37.23           N  
ANISOU 3971  N   SER A 507     3958   5072   5116     74   -331   -389       N  
ATOM   3972  CA  SER A 507     -38.111  19.733 -32.749  1.00 37.71           C  
ANISOU 3972  CA  SER A 507     3954   5145   5229     95   -349   -377       C  
ATOM   3973  C   SER A 507     -38.538  19.956 -31.303  1.00 38.84           C  
ANISOU 3973  C   SER A 507     4064   5281   5414    112   -295   -381       C  
ATOM   3974  O   SER A 507     -39.601  20.538 -31.061  1.00 41.62           O  
ANISOU 3974  O   SER A 507     4368   5636   5809    144   -297   -368       O  
ATOM   3975  CB  SER A 507     -38.788  18.480 -33.306  1.00 38.84           C  
ANISOU 3975  CB  SER A 507     4061   5315   5382     62   -386   -385       C  
ATOM   3976  OG  SER A 507     -38.089  17.308 -32.925  1.00 37.81           O  
ANISOU 3976  OG  SER A 507     3952   5183   5233     24   -360   -408       O  
ATOM   3977  N   ASN A 508     -37.741  19.503 -30.334  1.00 35.80           N  
ANISOU 3977  N   ASN A 508     3701   4886   5015     95   -248   -399       N  
ATOM   3978  CA  ASN A 508     -38.066  19.664 -28.923  1.00 33.45           C  
ANISOU 3978  CA  ASN A 508     3382   4580   4749    107   -194   -404       C  
ATOM   3979  C   ASN A 508     -37.372  20.870 -28.300  1.00 31.50           C  
ANISOU 3979  C   ASN A 508     3174   4308   4486    131   -158   -403       C  
ATOM   3980  O   ASN A 508     -37.307  20.972 -27.070  1.00 27.69           O  
ANISOU 3980  O   ASN A 508     2691   3815   4014    136   -109   -412       O  
ATOM   3981  CB  ASN A 508     -37.726  18.390 -28.149  1.00 25.76           C  
ANISOU 3981  CB  ASN A 508     2410   3609   3768     74   -166   -423       C  
ATOM   3982  CG  ASN A 508     -38.756  17.296 -28.353  1.00 39.26           C  
ANISOU 3982  CG  ASN A 508     4071   5337   5508     49   -183   -426       C  
ATOM   3983  OD1 ASN A 508     -39.588  17.041 -27.482  1.00 45.97           O  
ANISOU 3983  OD1 ASN A 508     4880   6189   6396     48   -152   -429       O  
ATOM   3984  ND2 ASN A 508     -38.709  16.646 -29.511  1.00 38.18           N  
ANISOU 3984  ND2 ASN A 508     3940   5214   5354     26   -231   -428       N  
ATOM   3985  N   ASP A 509     -36.840  21.773 -29.128  1.00 30.83           N  
ANISOU 3985  N   ASP A 509     3130   4212   4374    143   -179   -392       N  
ATOM   3986  CA  ASP A 509     -36.357  23.081 -28.683  1.00 33.52           C  
ANISOU 3986  CA  ASP A 509     3508   4524   4702    166   -147   -390       C  
ATOM   3987  C   ASP A 509     -35.230  22.951 -27.658  1.00 35.00           C  
ANISOU 3987  C   ASP A 509     3730   4707   4862    144   -101   -412       C  
ATOM   3988  O   ASP A 509     -35.253  23.561 -26.587  1.00 42.10           O  
ANISOU 3988  O   ASP A 509     4634   5590   5772    157    -57   -418       O  
ATOM   3989  CB  ASP A 509     -37.511  23.923 -28.133  1.00 34.65           C  
ANISOU 3989  CB  ASP A 509     3617   4654   4895    209   -129   -376       C  
ATOM   3990  CG  ASP A 509     -37.123  25.368 -27.903  1.00 41.51           C  
ANISOU 3990  CG  ASP A 509     4534   5488   5751    235   -101   -370       C  
ATOM   3991  OD1 ASP A 509     -36.527  25.976 -28.817  1.00 37.46           O  
ANISOU 3991  OD1 ASP A 509     4068   4961   5203    234   -124   -361       O  
ATOM   3992  OD2 ASP A 509     -37.413  25.895 -26.809  1.00 46.39           O1-
ANISOU 3992  OD2 ASP A 509     5147   6088   6391    254    -54   -375       O1-
ATOM   3993  N   TYR A 510     -34.233  22.138 -27.994  1.00 31.09           N  
ANISOU 3993  N   TYR A 510     3257   4226   4330    112   -112   -426       N  
ATOM   3994  CA  TYR A 510     -33.034  21.988 -27.182  1.00 33.54           C  
ANISOU 3994  CA  TYR A 510     3597   4539   4607     94    -79   -448       C  
ATOM   3995  C   TYR A 510     -31.835  22.481 -27.977  1.00 32.92           C  
ANISOU 3995  C   TYR A 510     3564   4460   4482     77    -89   -454       C  
ATOM   3996  O   TYR A 510     -31.685  22.140 -29.155  1.00 32.76           O  
ANISOU 3996  O   TYR A 510     3553   4449   4447     67   -125   -449       O  
ATOM   3997  CB  TYR A 510     -32.823  20.532 -26.755  1.00 29.52           C  
ANISOU 3997  CB  TYR A 510     3074   4049   4094     74    -77   -461       C  
ATOM   3998  CG  TYR A 510     -33.747  20.071 -25.650  1.00 33.22           C  
ANISOU 3998  CG  TYR A 510     3509   4516   4599     82    -50   -460       C  
ATOM   3999  CD1 TYR A 510     -33.596  20.539 -24.351  1.00 41.27           C  
ANISOU 3999  CD1 TYR A 510     4538   5525   5619     90     -4   -468       C  
ATOM   4000  CD2 TYR A 510     -34.764  19.161 -25.904  1.00 39.70           C  
ANISOU 4000  CD2 TYR A 510     4290   5344   5450     76    -66   -453       C  
ATOM   4001  CE1 TYR A 510     -34.436  20.118 -23.337  1.00 50.66           C  
ANISOU 4001  CE1 TYR A 510     5702   6711   6838     95     26   -468       C  
ATOM   4002  CE2 TYR A 510     -35.609  18.733 -24.897  1.00 37.80           C  
ANISOU 4002  CE2 TYR A 510     4020   5102   5243     78    -35   -454       C  
ATOM   4003  CZ  TYR A 510     -35.440  19.215 -23.616  1.00 44.64           C  
ANISOU 4003  CZ  TYR A 510     4898   5956   6108     88     12   -460       C  
ATOM   4004  OH  TYR A 510     -36.280  18.792 -22.612  1.00 68.56           O  
ANISOU 4004  OH  TYR A 510     7902   8981   9166     88     48   -461       O  
ATOM   4005  N   SER A 511     -30.990  23.286 -27.336  1.00 46.28           N  
ANISOU 4005  N   SER A 511     5288   6144   6153     71    -56   -467       N  
ATOM   4006  CA  SER A 511     -29.746  23.698 -27.967  1.00 39.75           C  
ANISOU 4006  CA  SER A 511     4501   5322   5282     47    -58   -479       C  
ATOM   4007  C   SER A 511     -28.870  22.478 -28.219  1.00 44.73           C  
ANISOU 4007  C   SER A 511     5125   5982   5886     26    -71   -497       C  
ATOM   4008  O   SER A 511     -28.942  21.477 -27.502  1.00 46.44           O  
ANISOU 4008  O   SER A 511     5320   6214   6113     28    -66   -504       O  
ATOM   4009  CB  SER A 511     -29.009  24.710 -27.089  1.00 38.24           C  
ANISOU 4009  CB  SER A 511     4339   5119   5073     38    -17   -495       C  
ATOM   4010  OG  SER A 511     -28.208  24.057 -26.119  1.00 52.85           O  
ANISOU 4010  OG  SER A 511     6181   6995   6907     23      1   -519       O  
ATOM   4011  N   PHE A 512     -28.048  22.554 -29.266  1.00 35.90           N  
ANISOU 4011  N   PHE A 512     4032   4873   4736      6    -85   -503       N  
ATOM   4012  CA  PHE A 512     -27.254  21.409 -29.684  1.00 32.92           C  
ANISOU 4012  CA  PHE A 512     3651   4524   4335    -10    -98   -518       C  
ATOM   4013  C   PHE A 512     -25.751  21.610 -29.583  1.00 36.59           C  
ANISOU 4013  C   PHE A 512     4132   5009   4760    -32    -77   -545       C  
ATOM   4014  O   PHE A 512     -25.027  20.613 -29.490  1.00 41.19           O  
ANISOU 4014  O   PHE A 512     4704   5618   5328    -36    -79   -562       O  
ATOM   4015  CB  PHE A 512     -27.599  21.014 -31.128  1.00 29.52           C  
ANISOU 4015  CB  PHE A 512     3228   4091   3897    -15   -135   -506       C  
ATOM   4016  CG  PHE A 512     -27.461  19.545 -31.398  1.00 27.92           C  
ANISOU 4016  CG  PHE A 512     3012   3908   3690    -20   -151   -516       C  
ATOM   4017  CD1 PHE A 512     -28.320  18.636 -30.804  1.00 31.48           C  
ANISOU 4017  CD1 PHE A 512     3433   4357   4171     -8   -156   -510       C  
ATOM   4018  CD2 PHE A 512     -26.473  19.072 -32.243  1.00 29.75           C  
ANISOU 4018  CD2 PHE A 512     3263   4156   3886    -37   -156   -531       C  
ATOM   4019  CE1 PHE A 512     -28.197  17.283 -31.048  1.00 33.53           C  
ANISOU 4019  CE1 PHE A 512     3688   4626   4425    -14   -168   -519       C  
ATOM   4020  CE2 PHE A 512     -26.344  17.720 -32.491  1.00 36.48           C  
ANISOU 4020  CE2 PHE A 512     4108   5019   4733    -39   -168   -541       C  
ATOM   4021  CZ  PHE A 512     -27.208  16.824 -31.893  1.00 37.80           C  
ANISOU 4021  CZ  PHE A 512     4251   5180   4930    -27   -174   -534       C  
ATOM   4022  N   ILE A 513     -25.260  22.851 -29.584  1.00 24.23           N  
ANISOU 4022  N   ILE A 513     2594   3434   3178    -47    -57   -550       N  
ATOM   4023  CA  ILE A 513     -23.829  23.096 -29.478  1.00 25.29           C  
ANISOU 4023  CA  ILE A 513     2739   3594   3278    -76    -36   -579       C  
ATOM   4024  C   ILE A 513     -23.251  22.591 -28.165  1.00 25.43           C  
ANISOU 4024  C   ILE A 513     2731   3640   3293    -71    -20   -600       C  
ATOM   4025  O   ILE A 513     -22.028  22.470 -28.042  1.00 26.77           O  
ANISOU 4025  O   ILE A 513     2895   3843   3435    -90    -10   -627       O  
ATOM   4026  CB  ILE A 513     -23.526  24.600 -29.657  1.00 28.86           C  
ANISOU 4026  CB  ILE A 513     3228   4023   3713    -98    -12   -581       C  
ATOM   4027  CG1 ILE A 513     -22.079  24.806 -30.115  1.00 25.24           C  
ANISOU 4027  CG1 ILE A 513     2782   3593   3215   -138      4   -610       C  
ATOM   4028  CG2 ILE A 513     -23.793  25.360 -28.366  1.00 24.14           C  
ANISOU 4028  CG2 ILE A 513     2633   3410   3130    -92     14   -584       C  
ATOM   4029  CD1 ILE A 513     -21.754  24.135 -31.432  1.00 27.61           C  
ANISOU 4029  CD1 ILE A 513     3088   3906   3498   -146    -15   -610       C  
ATOM   4030  N   ARG A 514     -24.103  22.285 -27.181  1.00 36.43           N  
ANISOU 4030  N   ARG A 514     4107   5020   4713    -47    -18   -589       N  
ATOM   4031  CA  ARG A 514     -23.615  21.738 -25.921  1.00 31.57           C  
ANISOU 4031  CA  ARG A 514     3475   4429   4091    -40     -6   -606       C  
ATOM   4032  C   ARG A 514     -22.886  20.418 -26.129  1.00 30.40           C  
ANISOU 4032  C   ARG A 514     3309   4314   3927    -33    -22   -618       C  
ATOM   4033  O   ARG A 514     -21.927  20.124 -25.411  1.00 35.18           O  
ANISOU 4033  O   ARG A 514     3904   4952   4511    -33    -16   -639       O  
ATOM   4034  CB  ARG A 514     -24.775  21.561 -24.935  1.00 37.63           C  
ANISOU 4034  CB  ARG A 514     4233   5174   4890    -16      2   -589       C  
ATOM   4035  CG  ARG A 514     -25.626  20.316 -25.162  1.00 30.40           C  
ANISOU 4035  CG  ARG A 514     3299   4253   3998      4    -18   -572       C  
ATOM   4036  CD  ARG A 514     -27.110  20.633 -25.135  1.00 38.09           C  
ANISOU 4036  CD  ARG A 514     4264   5195   5012     18    -16   -548       C  
ATOM   4037  NE  ARG A 514     -27.578  20.982 -23.799  1.00 46.53           N  
ANISOU 4037  NE  ARG A 514     5332   6253   6096     28     13   -548       N  
ATOM   4038  CZ  ARG A 514     -28.689  21.662 -23.550  1.00 46.52           C  
ANISOU 4038  CZ  ARG A 514     5325   6224   6127     41     27   -533       C  
ATOM   4039  NH1 ARG A 514     -29.468  22.095 -24.528  1.00 44.31           N  
ANISOU 4039  NH1 ARG A 514     5038   5928   5871     49      9   -514       N  
ATOM   4040  NH2 ARG A 514     -29.026  21.915 -22.289  1.00 45.44           N  
ANISOU 4040  NH2 ARG A 514     5190   6078   5999     49     59   -536       N  
ATOM   4041  N   TYR A 515     -23.309  19.620 -27.113  1.00 28.86           N  
ANISOU 4041  N   TYR A 515     3113   4112   3741    -26    -44   -605       N  
ATOM   4042  CA  TYR A 515     -22.656  18.338 -27.351  1.00 28.34           C  
ANISOU 4042  CA  TYR A 515     3036   4070   3660    -16    -56   -617       C  
ATOM   4043  C   TYR A 515     -21.298  18.517 -28.016  1.00 29.02           C  
ANISOU 4043  C   TYR A 515     3123   4189   3714    -34    -52   -642       C  
ATOM   4044  O   TYR A 515     -20.424  17.653 -27.878  1.00 32.07           O  
ANISOU 4044  O   TYR A 515     3496   4606   4084    -21    -54   -659       O  
ATOM   4045  CB  TYR A 515     -23.562  17.440 -28.192  1.00 28.08           C  
ANISOU 4045  CB  TYR A 515     3006   4017   3646     -8    -78   -599       C  
ATOM   4046  CG  TYR A 515     -24.899  17.175 -27.539  1.00 27.18           C  
ANISOU 4046  CG  TYR A 515     2884   3877   3566      6    -79   -578       C  
ATOM   4047  CD1 TYR A 515     -25.020  16.245 -26.515  1.00 29.94           C  
ANISOU 4047  CD1 TYR A 515     3228   4228   3922     23    -72   -578       C  
ATOM   4048  CD2 TYR A 515     -26.037  17.866 -27.934  1.00 34.78           C  
ANISOU 4048  CD2 TYR A 515     3846   4815   4556      2    -87   -557       C  
ATOM   4049  CE1 TYR A 515     -26.238  16.003 -25.909  1.00 29.38           C  
ANISOU 4049  CE1 TYR A 515     3148   4133   3881     30    -66   -561       C  
ATOM   4050  CE2 TYR A 515     -27.260  17.631 -27.333  1.00 39.96           C  
ANISOU 4050  CE2 TYR A 515     4485   5452   5246     14    -85   -541       C  
ATOM   4051  CZ  TYR A 515     -27.354  16.699 -26.322  1.00 33.50           C  
ANISOU 4051  CZ  TYR A 515     3661   4635   4433     24    -72   -544       C  
ATOM   4052  OH  TYR A 515     -28.568  16.460 -25.720  1.00 32.45           O  
ANISOU 4052  OH  TYR A 515     3511   4484   4334     30    -63   -530       O  
ATOM   4053  N   TYR A 516     -21.103  19.619 -28.741  1.00 30.83           N  
ANISOU 4053  N   TYR A 516     3368   4412   3933    -62    -44   -644       N  
ATOM   4054  CA  TYR A 516     -19.779  19.931 -29.269  1.00 33.28           C  
ANISOU 4054  CA  TYR A 516     3678   4755   4212    -87    -32   -671       C  
ATOM   4055  C   TYR A 516     -18.858  20.433 -28.164  1.00 33.21           C  
ANISOU 4055  C   TYR A 516     3652   4779   4189    -97    -14   -696       C  
ATOM   4056  O   TYR A 516     -17.723  19.963 -28.025  1.00 40.97           O  
ANISOU 4056  O   TYR A 516     4609   5806   5152    -96    -11   -722       O  
ATOM   4057  CB  TYR A 516     -19.892  20.965 -30.391  1.00 33.33           C  
ANISOU 4057  CB  TYR A 516     3716   4738   4208   -118    -26   -664       C  
ATOM   4058  CG  TYR A 516     -18.565  21.382 -30.986  1.00 30.73           C  
ANISOU 4058  CG  TYR A 516     3389   4440   3846   -152     -6   -693       C  
ATOM   4059  CD1 TYR A 516     -17.850  22.452 -30.461  1.00 36.72           C  
ANISOU 4059  CD1 TYR A 516     4149   5213   4591   -184     20   -713       C  
ATOM   4060  CD2 TYR A 516     -18.028  20.708 -32.074  1.00 36.07           C  
ANISOU 4060  CD2 TYR A 516     4066   5133   4505   -157    -10   -703       C  
ATOM   4061  CE1 TYR A 516     -16.638  22.834 -30.999  1.00 45.17           C  
ANISOU 4061  CE1 TYR A 516     5216   6314   5632   -222     42   -743       C  
ATOM   4062  CE2 TYR A 516     -16.816  21.084 -32.620  1.00 38.20           C  
ANISOU 4062  CE2 TYR A 516     4334   5434   4746   -191     14   -732       C  
ATOM   4063  CZ  TYR A 516     -16.126  22.148 -32.078  1.00 43.05           C  
ANISOU 4063  CZ  TYR A 516     4944   6063   5348   -225     40   -752       C  
ATOM   4064  OH  TYR A 516     -14.920  22.529 -32.615  1.00 40.17           O  
ANISOU 4064  OH  TYR A 516     4575   5733   4956   -265     67   -783       O  
ATOM   4065  N   THR A 517     -19.334  21.393 -27.366  1.00 27.01           N  
ANISOU 4065  N   THR A 517     2878   3973   3413   -105     -1   -690       N  
ATOM   4066  CA  THR A 517     -18.505  21.953 -26.303  1.00 31.54           C  
ANISOU 4066  CA  THR A 517     3439   4576   3969   -121     16   -715       C  
ATOM   4067  C   THR A 517     -18.220  20.923 -25.218  1.00 33.15           C  
ANISOU 4067  C   THR A 517     3615   4810   4170    -89      4   -722       C  
ATOM   4068  O   THR A 517     -17.097  20.851 -24.704  1.00 34.62           O  
ANISOU 4068  O   THR A 517     3777   5044   4333    -95      5   -750       O  
ATOM   4069  CB  THR A 517     -19.180  23.188 -25.704  1.00 25.85           C  
ANISOU 4069  CB  THR A 517     2746   3818   3258   -136     35   -707       C  
ATOM   4070  OG1 THR A 517     -20.462  22.827 -25.177  1.00 28.35           O  
ANISOU 4070  OG1 THR A 517     3066   4100   3604   -102     27   -678       O  
ATOM   4071  CG2 THR A 517     -19.356  24.265 -26.765  1.00 22.79           C  
ANISOU 4071  CG2 THR A 517     2394   3398   2868   -165     47   -699       C  
ATOM   4072  N   ARG A 518     -19.222  20.116 -24.855  1.00 30.91           N  
ANISOU 4072  N   ARG A 518     3335   4500   3909    -54     -8   -697       N  
ATOM   4073  CA  ARG A 518     -19.019  19.097 -23.829  1.00 34.05           C  
ANISOU 4073  CA  ARG A 518     3718   4919   4301    -22    -17   -699       C  
ATOM   4074  C   ARG A 518     -17.958  18.092 -24.255  1.00 35.05           C  
ANISOU 4074  C   ARG A 518     3821   5087   4409     -4    -32   -716       C  
ATOM   4075  O   ARG A 518     -17.139  17.658 -23.435  1.00 35.21           O  
ANISOU 4075  O   ARG A 518     3822   5146   4409     14    -38   -732       O  
ATOM   4076  CB  ARG A 518     -20.337  18.385 -23.526  1.00 32.78           C  
ANISOU 4076  CB  ARG A 518     3569   4718   4168      5    -22   -669       C  
ATOM   4077  CG  ARG A 518     -20.195  17.136 -22.681  1.00 29.87           C  
ANISOU 4077  CG  ARG A 518     3196   4362   3792     41    -31   -667       C  
ATOM   4078  CD  ARG A 518     -20.926  15.960 -23.302  1.00 42.72           C  
ANISOU 4078  CD  ARG A 518     4831   5962   5438     60    -43   -647       C  
ATOM   4079  NE  ARG A 518     -20.081  15.208 -24.222  1.00 45.54           N  
ANISOU 4079  NE  ARG A 518     5181   6341   5781     69    -56   -659       N  
ATOM   4080  CZ  ARG A 518     -20.517  14.237 -25.012  1.00 49.07           C  
ANISOU 4080  CZ  ARG A 518     5638   6767   6238     80    -65   -649       C  
ATOM   4081  NH1 ARG A 518     -21.789  13.873 -25.023  1.00 40.23           N  
ANISOU 4081  NH1 ARG A 518     4532   5608   5146     79    -66   -626       N  
ATOM   4082  NH2 ARG A 518     -19.655  13.613 -25.810  1.00 47.91           N  
ANISOU 4082  NH2 ARG A 518     5486   6641   6075     89    -73   -664       N  
ATOM   4083  N   THR A 519     -17.964  17.703 -25.531  1.00 37.58           N  
ANISOU 4083  N   THR A 519     4145   5400   4734     -7    -37   -713       N  
ATOM   4084  CA  THR A 519     -16.944  16.789 -26.033  1.00 39.29           C  
ANISOU 4084  CA  THR A 519     4342   5653   4934     10    -45   -731       C  
ATOM   4085  C   THR A 519     -15.550  17.372 -25.841  1.00 40.72           C  
ANISOU 4085  C   THR A 519     4492   5891   5089     -9    -36   -766       C  
ATOM   4086  O   THR A 519     -14.642  16.694 -25.346  1.00 41.43           O  
ANISOU 4086  O   THR A 519     4553   6024   5163     19    -45   -783       O  
ATOM   4087  CB  THR A 519     -17.199  16.482 -27.509  1.00 37.82           C  
ANISOU 4087  CB  THR A 519     4170   5446   4753      1    -47   -725       C  
ATOM   4088  OG1 THR A 519     -18.342  15.625 -27.632  1.00 38.85           O  
ANISOU 4088  OG1 THR A 519     4322   5535   4905     23    -60   -698       O  
ATOM   4089  CG2 THR A 519     -15.989  15.805 -28.130  1.00 40.16           C  
ANISOU 4089  CG2 THR A 519     4447   5784   5030     12    -46   -750       C  
ATOM   4090  N   LEU A 520     -15.366  18.640 -26.212  1.00 31.16           N  
ANISOU 4090  N   LEU A 520     3287   4680   3873    -56    -19   -777       N  
ATOM   4091  CA  LEU A 520     -14.069  19.281 -26.026  1.00 31.84           C  
ANISOU 4091  CA  LEU A 520     3342   4821   3935    -86     -7   -814       C  
ATOM   4092  C   LEU A 520     -13.747  19.459 -24.547  1.00 33.15           C  
ANISOU 4092  C   LEU A 520     3491   5016   4090    -78    -14   -825       C  
ATOM   4093  O   LEU A 520     -12.594  19.292 -24.134  1.00 34.87           O  
ANISOU 4093  O   LEU A 520     3667   5294   4287    -75    -20   -855       O  
ATOM   4094  CB  LEU A 520     -14.035  20.623 -26.758  1.00 29.20           C  
ANISOU 4094  CB  LEU A 520     3030   4470   3596   -144     17   -821       C  
ATOM   4095  CG  LEU A 520     -13.567  20.587 -28.217  1.00 29.98           C  
ANISOU 4095  CG  LEU A 520     3131   4573   3685   -166     29   -830       C  
ATOM   4096  CD1 LEU A 520     -14.547  19.829 -29.103  1.00 27.68           C  
ANISOU 4096  CD1 LEU A 520     2869   4237   3410   -138     16   -799       C  
ATOM   4097  CD2 LEU A 520     -13.342  21.991 -28.752  1.00 23.72           C  
ANISOU 4097  CD2 LEU A 520     2364   3769   2881   -227     58   -842       C  
ATOM   4098  N   TYR A 521     -14.754  19.796 -23.734  1.00 37.91           N  
ANISOU 4098  N   TYR A 521     4121   5577   4704    -74    -13   -803       N  
ATOM   4099  CA  TYR A 521     -14.527  19.962 -22.301  1.00 33.33           C  
ANISOU 4099  CA  TYR A 521     3533   5021   4109    -68    -19   -813       C  
ATOM   4100  C   TYR A 521     -14.053  18.666 -21.658  1.00 36.07           C  
ANISOU 4100  C   TYR A 521     3857   5404   4446    -14    -44   -813       C  
ATOM   4101  O   TYR A 521     -13.131  18.675 -20.832  1.00 39.72           O  
ANISOU 4101  O   TYR A 521     4291   5920   4882    -10    -56   -837       O  
ATOM   4102  CB  TYR A 521     -15.806  20.439 -21.610  1.00 36.62           C  
ANISOU 4102  CB  TYR A 521     3990   5382   4543    -68     -8   -787       C  
ATOM   4103  CG  TYR A 521     -16.265  21.827 -21.988  1.00 34.44           C  
ANISOU 4103  CG  TYR A 521     3742   5069   4275   -114     17   -787       C  
ATOM   4104  CD1 TYR A 521     -15.380  22.760 -22.512  1.00 31.57           C  
ANISOU 4104  CD1 TYR A 521     3373   4729   3894   -162     32   -815       C  
ATOM   4105  CD2 TYR A 521     -17.589  22.206 -21.814  1.00 31.80           C  
ANISOU 4105  CD2 TYR A 521     3442   4676   3966   -107     29   -759       C  
ATOM   4106  CE1 TYR A 521     -15.805  24.030 -22.855  1.00 37.33           C  
ANISOU 4106  CE1 TYR A 521     4138   5417   4628   -202     58   -813       C  
ATOM   4107  CE2 TYR A 521     -18.022  23.471 -22.153  1.00 30.94           C  
ANISOU 4107  CE2 TYR A 521     3362   4528   3864   -140     52   -756       C  
ATOM   4108  CZ  TYR A 521     -17.127  24.379 -22.673  1.00 34.47           C  
ANISOU 4108  CZ  TYR A 521     3813   4994   4291   -187     66   -782       C  
ATOM   4109  OH  TYR A 521     -17.558  25.640 -23.012  1.00 39.68           O  
ANISOU 4109  OH  TYR A 521     4512   5609   4955   -218     92   -777       O  
ATOM   4110  N   GLN A 522     -14.674  17.540 -22.020  1.00 35.09           N  
ANISOU 4110  N   GLN A 522     3746   5249   4338     27    -54   -787       N  
ATOM   4111  CA  GLN A 522     -14.383  16.282 -21.340  1.00 33.97           C  
ANISOU 4111  CA  GLN A 522     3597   5126   4184     83    -75   -782       C  
ATOM   4112  C   GLN A 522     -12.946  15.834 -21.571  1.00 37.17           C  
ANISOU 4112  C   GLN A 522     3955   5598   4568    102    -89   -811       C  
ATOM   4113  O   GLN A 522     -12.330  15.245 -20.676  1.00 41.77           O  
ANISOU 4113  O   GLN A 522     4521   6219   5130    140   -110   -817       O  
ATOM   4114  CB  GLN A 522     -15.376  15.204 -21.786  1.00 33.90           C  
ANISOU 4114  CB  GLN A 522     3618   5065   4198    115    -77   -750       C  
ATOM   4115  CG  GLN A 522     -14.976  14.420 -23.027  1.00 37.87           C  
ANISOU 4115  CG  GLN A 522     4111   5572   4705    130    -81   -755       C  
ATOM   4116  CD  GLN A 522     -16.130  13.639 -23.622  1.00 41.52           C  
ANISOU 4116  CD  GLN A 522     4609   5975   5192    142    -79   -726       C  
ATOM   4117  OE1 GLN A 522     -17.286  14.053 -23.533  1.00 36.87           O  
ANISOU 4117  OE1 GLN A 522     4043   5342   4622    122    -72   -705       O  
ATOM   4118  NE2 GLN A 522     -15.822  12.502 -24.235  1.00 44.54           N  
ANISOU 4118  NE2 GLN A 522     4995   6357   5572    174    -86   -727       N  
ATOM   4119  N   PHE A 523     -12.385  16.111 -22.747  1.00 40.20           N  
ANISOU 4119  N   PHE A 523     4318   6000   4956     76    -77   -830       N  
ATOM   4120  CA  PHE A 523     -10.999  15.734 -22.982  1.00 39.87           C  
ANISOU 4120  CA  PHE A 523     4226   6027   4898     93    -85   -862       C  
ATOM   4121  C   PHE A 523     -10.035  16.764 -22.414  1.00 40.00           C  
ANISOU 4121  C   PHE A 523     4200   6105   4892     52    -84   -897       C  
ATOM   4122  O   PHE A 523      -8.915  16.410 -22.031  1.00 41.21           O  
ANISOU 4122  O   PHE A 523     4304   6327   5028     76   -102   -923       O  
ATOM   4123  CB  PHE A 523     -10.770  15.506 -24.474  1.00 37.51           C  
ANISOU 4123  CB  PHE A 523     3922   5722   4609     83    -69   -869       C  
ATOM   4124  CG  PHE A 523     -11.527  14.327 -25.011  1.00 37.13           C  
ANISOU 4124  CG  PHE A 523     3909   5624   4576    125    -74   -841       C  
ATOM   4125  CD1 PHE A 523     -11.174  13.039 -24.647  1.00 30.83           C  
ANISOU 4125  CD1 PHE A 523     3104   4838   3771    191    -91   -837       C  
ATOM   4126  CD2 PHE A 523     -12.610  14.506 -25.851  1.00 33.79           C  
ANISOU 4126  CD2 PHE A 523     3528   5140   4172    100    -62   -818       C  
ATOM   4127  CE1 PHE A 523     -11.879  11.952 -25.125  1.00 30.52           C  
ANISOU 4127  CE1 PHE A 523     3105   4748   3745    224    -92   -813       C  
ATOM   4128  CE2 PHE A 523     -13.317  13.423 -26.331  1.00 31.61           C  
ANISOU 4128  CE2 PHE A 523     3283   4819   3907    131    -68   -796       C  
ATOM   4129  CZ  PHE A 523     -12.950  12.144 -25.970  1.00 29.07           C  
ANISOU 4129  CZ  PHE A 523     2960   4507   3580    191    -80   -794       C  
ATOM   4130  N   GLN A 524     -10.453  18.030 -22.334  1.00 38.55           N  
ANISOU 4130  N   GLN A 524     4038   5899   4711     -8    -65   -900       N  
ATOM   4131  CA  GLN A 524      -9.720  18.989 -21.516  1.00 40.11           C  
ANISOU 4131  CA  GLN A 524     4210   6146   4886    -49    -66   -932       C  
ATOM   4132  C   GLN A 524      -9.719  18.556 -20.057  1.00 40.49           C  
ANISOU 4132  C   GLN A 524     4256   6213   4915    -10    -94   -926       C  
ATOM   4133  O   GLN A 524      -8.690  18.637 -19.376  1.00 48.01           O  
ANISOU 4133  O   GLN A 524     5164   7236   5842    -10   -114   -956       O  
ATOM   4134  CB  GLN A 524     -10.328  20.385 -21.651  1.00 35.68           C  
ANISOU 4134  CB  GLN A 524     3688   5541   4330   -116    -36   -932       C  
ATOM   4135  CG  GLN A 524     -10.190  21.014 -23.023  1.00 38.68           C  
ANISOU 4135  CG  GLN A 524     4073   5905   4718   -163     -7   -941       C  
ATOM   4136  CD  GLN A 524     -10.803  22.399 -23.083  1.00 40.82           C  
ANISOU 4136  CD  GLN A 524     4391   6128   4992   -222     21   -937       C  
ATOM   4137  OE1 GLN A 524     -11.913  22.577 -23.585  1.00 40.67           O  
ANISOU 4137  OE1 GLN A 524     4420   6041   4993   -218     31   -905       O  
ATOM   4138  NE2 GLN A 524     -10.083  23.390 -22.570  1.00 47.10           N  
ANISOU 4138  NE2 GLN A 524     5173   6957   5765   -276     34   -972       N  
ATOM   4139  N   PHE A 525     -10.868  18.089 -19.563  1.00 41.57           N  
ANISOU 4139  N   PHE A 525     4442   6290   5063     22    -98   -888       N  
ATOM   4140  CA  PHE A 525     -10.957  17.624 -18.182  1.00 41.24           C  
ANISOU 4140  CA  PHE A 525     4410   6258   4999     60   -122   -878       C  
ATOM   4141  C   PHE A 525     -10.050  16.424 -17.948  1.00 44.62           C  
ANISOU 4141  C   PHE A 525     4803   6741   5411    125   -155   -884       C  
ATOM   4142  O   PHE A 525      -9.250  16.411 -17.006  1.00 55.40           O  
ANISOU 4142  O   PHE A 525     6139   8165   6744    138   -181   -902       O  
ATOM   4143  CB  PHE A 525     -12.405  17.269 -17.841  1.00 41.28           C  
ANISOU 4143  CB  PHE A 525     4475   6186   5022     81   -112   -837       C  
ATOM   4144  CG  PHE A 525     -13.309  18.460 -17.698  1.00 38.72           C  
ANISOU 4144  CG  PHE A 525     4186   5814   4710     29    -83   -831       C  
ATOM   4145  CD1 PHE A 525     -12.788  19.739 -17.611  1.00 40.30           C  
ANISOU 4145  CD1 PHE A 525     4375   6038   4897    -29    -70   -862       C  
ATOM   4146  CD2 PHE A 525     -14.683  18.297 -17.650  1.00 43.58           C  
ANISOU 4146  CD2 PHE A 525     4846   6360   5352     40    -67   -797       C  
ATOM   4147  CE1 PHE A 525     -13.621  20.832 -17.478  1.00 42.81           C  
ANISOU 4147  CE1 PHE A 525     4732   6307   5227    -70    -41   -856       C  
ATOM   4148  CE2 PHE A 525     -15.521  19.387 -17.518  1.00 47.44           C  
ANISOU 4148  CE2 PHE A 525     5365   6806   5854      1    -40   -791       C  
ATOM   4149  CZ  PHE A 525     -14.989  20.657 -17.433  1.00 45.17           C  
ANISOU 4149  CZ  PHE A 525     5072   6537   5552    -51    -27   -820       C  
ATOM   4150  N   GLN A 526     -10.156  15.406 -18.805  1.00 41.59           N  
ANISOU 4150  N   GLN A 526     4420   6336   5044    167   -155   -868       N  
ATOM   4151  CA  GLN A 526      -9.384  14.184 -18.604  1.00 43.85           C  
ANISOU 4151  CA  GLN A 526     4681   6662   5317    238   -183   -869       C  
ATOM   4152  C   GLN A 526      -7.889  14.461 -18.676  1.00 44.65           C  
ANISOU 4152  C   GLN A 526     4708   6858   5401    234   -198   -912       C  
ATOM   4153  O   GLN A 526      -7.130  14.059 -17.788  1.00 52.64           O  
ANISOU 4153  O   GLN A 526     5689   7926   6385    276   -232   -922       O  
ATOM   4154  CB  GLN A 526      -9.787  13.132 -19.636  1.00 33.44           C  
ANISOU 4154  CB  GLN A 526     3384   5299   4022    275   -173   -848       C  
ATOM   4155  CG  GLN A 526     -10.721  12.068 -19.094  1.00 40.18           C  
ANISOU 4155  CG  GLN A 526     4296   6092   4878    326   -180   -808       C  
ATOM   4156  CD  GLN A 526      -9.985  10.937 -18.405  1.00 39.88           C  
ANISOU 4156  CD  GLN A 526     4251   6088   4815    404   -210   -804       C  
ATOM   4157  OE1 GLN A 526     -10.009  10.821 -17.180  1.00 45.10           O  
ANISOU 4157  OE1 GLN A 526     4928   6757   5449    427   -230   -794       O  
ATOM   4158  NE2 GLN A 526      -9.329  10.093 -19.192  1.00 52.37           N  
ANISOU 4158  NE2 GLN A 526     5810   7687   6402    448   -213   -812       N  
ATOM   4159  N   GLU A 527      -7.451  15.176 -19.716  1.00 47.81           N  
ANISOU 4159  N   GLU A 527     5075   7277   5814    181   -174   -939       N  
ATOM   4160  CA  GLU A 527      -6.027  15.455 -19.877  1.00 49.33           C  
ANISOU 4160  CA  GLU A 527     5189   7562   5993    169   -181   -984       C  
ATOM   4161  C   GLU A 527      -5.469  16.188 -18.664  1.00 52.12           C  
ANISOU 4161  C   GLU A 527     5513   7973   6316    142   -205  -1009       C  
ATOM   4162  O   GLU A 527      -4.357  15.894 -18.209  1.00 61.04           O  
ANISOU 4162  O   GLU A 527     6579   9186   7425    172   -235  -1035       O  
ATOM   4163  CB  GLU A 527      -5.794  16.267 -21.150  1.00 41.76           C  
ANISOU 4163  CB  GLU A 527     4214   6603   5051    101   -142  -1008       C  
ATOM   4164  CG  GLU A 527      -4.366  16.225 -21.662  1.00 43.41           C  
ANISOU 4164  CG  GLU A 527     4340   6900   5254     99   -141  -1053       C  
ATOM   4165  CD  GLU A 527      -4.098  17.277 -22.721  1.00 52.23           C  
ANISOU 4165  CD  GLU A 527     5445   8020   6379     14    -98  -1080       C  
ATOM   4166  OE1 GLU A 527      -4.163  18.481 -22.394  1.00 47.90           O  
ANISOU 4166  OE1 GLU A 527     4906   7473   5822    -58    -85  -1096       O  
ATOM   4167  OE2 GLU A 527      -3.823  16.900 -23.879  1.00 53.88           O1-
ANISOU 4167  OE2 GLU A 527     5643   8229   6602     20    -74  -1087       O1-
ATOM   4168  N   ALA A 528      -6.228  17.144 -18.127  1.00 30.96           N  
ANISOU 4168  N   ALA A 528     2880   5253   3632     88   -192  -1002       N  
ATOM   4169  CA  ALA A 528      -5.794  17.844 -16.922  1.00 29.85           C  
ANISOU 4169  CA  ALA A 528     2723   5161   3459     60   -213  -1024       C  
ATOM   4170  C   ALA A 528      -5.752  16.909 -15.719  1.00 35.47           C  
ANISOU 4170  C   ALA A 528     3444   5891   4144    134   -257  -1005       C  
ATOM   4171  O   ALA A 528      -4.816  16.970 -14.913  1.00 42.86           O  
ANISOU 4171  O   ALA A 528     4332   6906   5047    142   -293  -1032       O  
ATOM   4172  CB  ALA A 528      -6.716  19.030 -16.650  1.00 29.96           C  
ANISOU 4172  CB  ALA A 528     2795   5114   3474     -9   -183  -1019       C  
ATOM   4173  N   LEU A 529      -6.758  16.041 -15.577  1.00 33.59           N  
ANISOU 4173  N   LEU A 529     3266   5581   3915    187   -256   -959       N  
ATOM   4174  CA  LEU A 529      -6.784  15.122 -14.443  1.00 36.16           C  
ANISOU 4174  CA  LEU A 529     3613   5913   4211    257   -294   -937       C  
ATOM   4175  C   LEU A 529      -5.695  14.064 -14.560  1.00 40.00           C  
ANISOU 4175  C   LEU A 529     4045   6465   4688    333   -330   -945       C  
ATOM   4176  O   LEU A 529      -5.054  13.713 -13.563  1.00 45.11           O  
ANISOU 4176  O   LEU A 529     4674   7169   5299    376   -374   -950       O  
ATOM   4177  CB  LEU A 529      -8.159  14.465 -14.323  1.00 40.29           C  
ANISOU 4177  CB  LEU A 529     4218   6340   4750    287   -277   -887       C  
ATOM   4178  CG  LEU A 529      -9.336  15.399 -14.029  1.00 40.02           C  
ANISOU 4178  CG  LEU A 529     4240   6240   4726    227   -243   -874       C  
ATOM   4179  CD1 LEU A 529     -10.581  14.601 -13.674  1.00 34.64           C  
ANISOU 4179  CD1 LEU A 529     3629   5479   4054    264   -232   -828       C  
ATOM   4180  CD2 LEU A 529      -8.986  16.385 -12.925  1.00 39.20           C  
ANISOU 4180  CD2 LEU A 529     4131   6177   4586    184   -255   -899       C  
ATOM   4181  N   CYS A 530      -5.474  13.538 -15.768  1.00 52.15           N  
ANISOU 4181  N   CYS A 530     5560   7997   6256    353   -313   -947       N  
ATOM   4182  CA  CYS A 530      -4.396  12.575 -15.964  1.00 50.37           C  
ANISOU 4182  CA  CYS A 530     5278   7835   6025    427   -341   -959       C  
ATOM   4183  C   CYS A 530      -3.032  13.220 -15.762  1.00 50.53           C  
ANISOU 4183  C   CYS A 530     5205   7968   6028    403   -364  -1010       C  
ATOM   4184  O   CYS A 530      -2.098  12.559 -15.292  1.00 60.01           O  
ANISOU 4184  O   CYS A 530     6355   9238   7207    470   -406  -1020       O  
ATOM   4185  CB  CYS A 530      -4.498  11.949 -17.353  1.00 49.70           C  
ANISOU 4185  CB  CYS A 530     5194   7715   5976    446   -310   -953       C  
ATOM   4186  SG  CYS A 530      -6.130  11.267 -17.715  1.00 54.63           S  
ANISOU 4186  SG  CYS A 530     5922   8211   6624    459   -282   -899       S  
ATOM   4187  N   GLN A 531      -2.896  14.499 -16.118  1.00 48.63           N  
ANISOU 4187  N   GLN A 531     4939   7745   5794    308   -338  -1043       N  
ATOM   4188  CA  GLN A 531      -1.692  15.239 -15.758  1.00 56.33           C  
ANISOU 4188  CA  GLN A 531     5830   8826   6748    268   -359  -1094       C  
ATOM   4189  C   GLN A 531      -1.542  15.323 -14.246  1.00 61.76           C  
ANISOU 4189  C   GLN A 531     6523   9551   7391    284   -408  -1093       C  
ATOM   4190  O   GLN A 531      -0.442  15.146 -13.710  1.00 66.83           O  
ANISOU 4190  O   GLN A 531     7093  10291   8008    314   -452  -1121       O  
ATOM   4191  CB  GLN A 531      -1.734  16.637 -16.373  1.00 54.39           C  
ANISOU 4191  CB  GLN A 531     5577   8575   6516    155   -314  -1125       C  
ATOM   4192  CG  GLN A 531      -0.402  17.134 -16.904  1.00 61.40           C  
ANISOU 4192  CG  GLN A 531     6364   9561   7404    112   -309  -1182       C  
ATOM   4193  CD  GLN A 531      -0.562  18.289 -17.874  1.00 82.80           C  
ANISOU 4193  CD  GLN A 531     9084  12242  10134      9   -252  -1204       C  
ATOM   4194  OE1 GLN A 531       0.078  19.331 -17.728  1.00 83.59           O  
ANISOU 4194  OE1 GLN A 531     9145  12397  10221    -71   -243  -1248       O  
ATOM   4195  NE2 GLN A 531      -1.421  18.110 -18.871  1.00 72.44           N  
ANISOU 4195  NE2 GLN A 531     7830  10844   8850     10   -213  -1174       N  
ATOM   4196  N   ALA A 532      -2.643  15.591 -13.540  1.00 40.15           N  
ANISOU 4196  N   ALA A 532     3872   6741   4643    266   -400  -1062       N  
ATOM   4197  CA  ALA A 532      -2.618  15.600 -12.083  1.00 39.10           C  
ANISOU 4197  CA  ALA A 532     3761   6633   4463    284   -443  -1057       C  
ATOM   4198  C   ALA A 532      -2.442  14.203 -11.505  1.00 45.02           C  
ANISOU 4198  C   ALA A 532     4521   7392   5192    398   -489  -1024       C  
ATOM   4199  O   ALA A 532      -1.962  14.068 -10.374  1.00 59.98           O  
ANISOU 4199  O   ALA A 532     6407   9342   7041    428   -539  -1029       O  
ATOM   4200  CB  ALA A 532      -3.898  16.233 -11.539  1.00 38.72           C  
ANISOU 4200  CB  ALA A 532     3805   6497   4411    236   -414  -1032       C  
ATOM   4201  N   ALA A 533      -2.811  13.168 -12.254  1.00 40.12           N  
ANISOU 4201  N   ALA A 533     3924   6718   4600    460   -473   -993       N  
ATOM   4202  CA  ALA A 533      -2.682  11.789 -11.807  1.00 43.89           C  
ANISOU 4202  CA  ALA A 533     4424   7192   5060    571   -509   -959       C  
ATOM   4203  C   ALA A 533      -1.332  11.181 -12.162  1.00 50.87           C  
ANISOU 4203  C   ALA A 533     5215   8169   5943    636   -543   -985       C  
ATOM   4204  O   ALA A 533      -1.135   9.981 -11.949  1.00 51.76           O  
ANISOU 4204  O   ALA A 533     5343   8277   6045    737   -571   -959       O  
ATOM   4205  CB  ALA A 533      -3.809  10.936 -12.396  1.00 41.19           C  
ANISOU 4205  CB  ALA A 533     4163   6740   4748    604   -472   -913       C  
ATOM   4206  N   LYS A 534      -0.407  11.982 -12.698  1.00 51.57           N  
ANISOU 4206  N   LYS A 534     5211   8339   6045    581   -538  -1037       N  
ATOM   4207  CA  LYS A 534       0.927  11.512 -13.078  1.00 56.31           C  
ANISOU 4207  CA  LYS A 534     5709   9039   6649    635   -566  -1069       C  
ATOM   4208  C   LYS A 534       0.842  10.331 -14.041  1.00 62.93           C  
ANISOU 4208  C   LYS A 534     6561   9831   7519    715   -544  -1045       C  
ATOM   4209  O   LYS A 534       1.591   9.357 -13.935  1.00 66.94           O  
ANISOU 4209  O   LYS A 534     7031  10384   8019    814   -578  -1043       O  
ATOM   4210  CB  LYS A 534       1.757  11.150 -11.844  1.00 62.98           C  
ANISOU 4210  CB  LYS A 534     6515   9971   7446    701   -640  -1074       C  
ATOM   4211  CG  LYS A 534       1.863  12.258 -10.808  1.00 64.02           C  
ANISOU 4211  CG  LYS A 534     6637  10149   7537    624   -666  -1100       C  
ATOM   4212  CD  LYS A 534       2.552  11.758  -9.546  1.00 70.66           C  
ANISOU 4212  CD  LYS A 534     7456  11068   8324    700   -745  -1096       C  
ATOM   4213  CE  LYS A 534       2.458  12.774  -8.420  1.00 72.59           C  
ANISOU 4213  CE  LYS A 534     7718  11341   8523    625   -770  -1114       C  
ATOM   4214  NZ  LYS A 534       3.305  13.971  -8.679  1.00 64.74           N  
ANISOU 4214  NZ  LYS A 534     6654  10407   7540    520   -746  -1167       N  
ATOM   4215  N   HIS A 535      -0.084  10.418 -14.992  1.00 50.15           N  
ANISOU 4215  N   HIS A 535     4999   8121   5936    672   -487  -1028       N  
ATOM   4216  CA  HIS A 535      -0.331   9.319 -15.916  1.00 50.98           C  
ANISOU 4216  CA  HIS A 535     5133   8167   6068    737   -462  -1005       C  
ATOM   4217  C   HIS A 535       0.707   9.332 -17.032  1.00 59.25           C  
ANISOU 4217  C   HIS A 535     6088   9281   7142    737   -442  -1048       C  
ATOM   4218  O   HIS A 535       0.804  10.306 -17.789  1.00 54.04           O  
ANISOU 4218  O   HIS A 535     5395   8635   6501    646   -404  -1080       O  
ATOM   4219  CB  HIS A 535      -1.740   9.413 -16.497  1.00 49.77           C  
ANISOU 4219  CB  HIS A 535     5074   7896   5939    689   -413   -972       C  
ATOM   4220  CG  HIS A 535      -1.960   8.521 -17.678  1.00 45.22           C  
ANISOU 4220  CG  HIS A 535     4522   7266   5395    727   -379   -959       C  
ATOM   4221  ND1 HIS A 535      -2.171   7.164 -17.555  1.00 51.54           N  
ANISOU 4221  ND1 HIS A 535     5373   8019   6190    823   -390   -925       N  
ATOM   4222  CD2 HIS A 535      -1.993   8.789 -19.004  1.00 45.29           C  
ANISOU 4222  CD2 HIS A 535     4515   7257   5435    681   -334   -978       C  
ATOM   4223  CE1 HIS A 535      -2.325   6.635 -18.756  1.00 48.91           C  
ANISOU 4223  CE1 HIS A 535     5054   7643   5886    833   -353   -925       C  
ATOM   4224  NE2 HIS A 535      -2.225   7.600 -19.652  1.00 44.21           N  
ANISOU 4224  NE2 HIS A 535     4419   7067   5313    748   -319   -956       N  
ATOM   4225  N   GLU A 536       1.474   8.251 -17.136  1.00 74.02           N  
ANISOU 4225  N   GLU A 536     7923  11190   9013    840   -463  -1048       N  
ATOM   4226  CA  GLU A 536       2.450   8.075 -18.201  1.00 71.82           C  
ANISOU 4226  CA  GLU A 536     7560  10970   8760    856   -440  -1087       C  
ATOM   4227  C   GLU A 536       1.830   7.248 -19.319  1.00 66.36           C  
ANISOU 4227  C   GLU A 536     6932  10186   8097    885   -393  -1063       C  
ATOM   4228  O   GLU A 536       1.280   6.170 -19.068  1.00 62.30           O  
ANISOU 4228  O   GLU A 536     6494   9602   7576    963   -403  -1021       O  
ATOM   4229  CB  GLU A 536       3.714   7.390 -17.679  1.00 73.53           C  
ANISOU 4229  CB  GLU A 536     7702  11277   8959    952   -487  -1100       C  
ATOM   4230  CG  GLU A 536       4.567   8.253 -16.765  1.00 79.15           C  
ANISOU 4230  CG  GLU A 536     8359  12073   9642    904   -522  -1126       C  
ATOM   4231  CD  GLU A 536       5.032   7.507 -15.530  1.00 93.53           C  
ANISOU 4231  CD  GLU A 536    10185  13929  11425   1002   -589  -1103       C  
ATOM   4232  OE1 GLU A 536       5.789   6.524 -15.678  1.00 94.55           O  
ANISOU 4232  OE1 GLU A 536    10294  14075  11555   1096   -601  -1096       O  
ATOM   4233  OE2 GLU A 536       4.642   7.903 -14.411  1.00 90.70           O1-
ANISOU 4233  OE2 GLU A 536     9852  13578  11032    986   -629  -1091       O1-
ATOM   4234  N   GLY A 537       1.918   7.752 -20.547  1.00 48.94           N  
ANISOU 4234  N   GLY A 537     4700   7976   5918    819   -341  -1091       N  
ATOM   4235  CA  GLY A 537       1.408   7.041 -21.694  1.00 50.00           C  
ANISOU 4235  CA  GLY A 537     4890   8031   6076    837   -296  -1076       C  
ATOM   4236  C   GLY A 537       0.338   7.810 -22.439  1.00 45.97           C  
ANISOU 4236  C   GLY A 537     4443   7442   5581    734   -251  -1066       C  
ATOM   4237  O   GLY A 537       0.027   8.962 -22.119  1.00 50.35           O  
ANISOU 4237  O   GLY A 537     4997   8004   6131    647   -250  -1073       O  
ATOM   4238  N   PRO A 538      -0.241   7.182 -23.463  1.00 54.77           N  
ANISOU 4238  N   PRO A 538     5616   8480   6713    744   -214  -1050       N  
ATOM   4239  CA  PRO A 538      -1.308   7.840 -24.227  1.00 52.89           C  
ANISOU 4239  CA  PRO A 538     5441   8166   6489    654   -177  -1037       C  
ATOM   4240  C   PRO A 538      -2.504   8.171 -23.346  1.00 51.35           C  
ANISOU 4240  C   PRO A 538     5318   7907   6285    624   -196   -998       C  
ATOM   4241  O   PRO A 538      -2.832   7.446 -22.403  1.00 53.02           O  
ANISOU 4241  O   PRO A 538     5568   8094   6483    686   -227   -967       O  
ATOM   4242  CB  PRO A 538      -1.671   6.804 -25.298  1.00 53.00           C  
ANISOU 4242  CB  PRO A 538     5508   8112   6516    694   -146  -1024       C  
ATOM   4243  CG  PRO A 538      -0.462   5.931 -25.410  1.00 59.16           C  
ANISOU 4243  CG  PRO A 538     6227   8956   7296    784   -151  -1048       C  
ATOM   4244  CD  PRO A 538       0.127   5.875 -24.033  1.00 53.10           C  
ANISOU 4244  CD  PRO A 538     5413   8253   6510    838   -204  -1047       C  
ATOM   4245  N   LEU A 539      -3.158   9.288 -23.673  1.00 46.76           N  
ANISOU 4245  N   LEU A 539     4757   7298   5711    529   -174   -999       N  
ATOM   4246  CA  LEU A 539      -4.232   9.804 -22.829  1.00 41.62           C  
ANISOU 4246  CA  LEU A 539     4162   6596   5054    492   -187   -968       C  
ATOM   4247  C   LEU A 539      -5.413   8.843 -22.751  1.00 44.67           C  
ANISOU 4247  C   LEU A 539     4638   6888   5448    532   -188   -922       C  
ATOM   4248  O   LEU A 539      -6.075   8.760 -21.710  1.00 49.70           O  
ANISOU 4248  O   LEU A 539     5317   7495   6074    543   -208   -894       O  
ATOM   4249  CB  LEU A 539      -4.689  11.168 -23.347  1.00 34.47           C  
ANISOU 4249  CB  LEU A 539     3264   5674   4158    389   -158   -979       C  
ATOM   4250  CG  LEU A 539      -5.907  11.803 -22.673  1.00 32.88           C  
ANISOU 4250  CG  LEU A 539     3123   5412   3956    346   -162   -948       C  
ATOM   4251  CD1 LEU A 539      -5.634  12.040 -21.197  1.00 40.36           C  
ANISOU 4251  CD1 LEU A 539     4054   6401   4879    361   -197   -950       C  
ATOM   4252  CD2 LEU A 539      -6.290  13.102 -23.364  1.00 36.02           C  
ANISOU 4252  CD2 LEU A 539     3530   5792   4366    253   -130   -959       C  
ATOM   4253  N   HIS A 540      -5.691   8.107 -23.828  1.00 49.04           N  
ANISOU 4253  N   HIS A 540     5223   7394   6016    549   -163   -915       N  
ATOM   4254  CA  HIS A 540      -6.861   7.236 -23.851  1.00 44.82           C  
ANISOU 4254  CA  HIS A 540     4774   6768   5489    572   -160   -875       C  
ATOM   4255  C   HIS A 540      -6.737   6.037 -22.919  1.00 40.14           C  
ANISOU 4255  C   HIS A 540     4207   6163   4879    663   -186   -853       C  
ATOM   4256  O   HIS A 540      -7.745   5.368 -22.667  1.00 45.64           O  
ANISOU 4256  O   HIS A 540     4978   6784   5578    678   -184   -818       O  
ATOM   4257  CB  HIS A 540      -7.133   6.762 -25.281  1.00 42.20           C  
ANISOU 4257  CB  HIS A 540     4469   6391   5173    562   -127   -878       C  
ATOM   4258  CG  HIS A 540      -6.287   5.604 -25.710  1.00 41.85           C  
ANISOU 4258  CG  HIS A 540     4413   6362   5125    640   -123   -891       C  
ATOM   4259  ND1 HIS A 540      -5.091   5.763 -26.375  1.00 46.15           N  
ANISOU 4259  ND1 HIS A 540     4888   6976   5670    648   -109   -931       N  
ATOM   4260  CD2 HIS A 540      -6.471   4.269 -25.582  1.00 44.28           C  
ANISOU 4260  CD2 HIS A 540     4772   6624   5429    714   -127   -870       C  
ATOM   4261  CE1 HIS A 540      -4.570   4.576 -26.631  1.00 53.42           C  
ANISOU 4261  CE1 HIS A 540     5815   7893   6588    728   -105   -934       C  
ATOM   4262  NE2 HIS A 540      -5.388   3.652 -26.159  1.00 47.92           N  
ANISOU 4262  NE2 HIS A 540     5194   7125   5888    770   -116   -897       N  
ATOM   4263  N   LYS A 541      -5.544   5.750 -22.404  1.00 38.67           N  
ANISOU 4263  N   LYS A 541     3965   6051   4677    725   -210   -871       N  
ATOM   4264  CA  LYS A 541      -5.337   4.656 -21.465  1.00 44.02           C  
ANISOU 4264  CA  LYS A 541     4670   6723   5334    818   -240   -849       C  
ATOM   4265  C   LYS A 541      -5.430   5.103 -20.012  1.00 40.03           C  
ANISOU 4265  C   LYS A 541     4164   6242   4802    818   -276   -835       C  
ATOM   4266  O   LYS A 541      -5.153   4.306 -19.111  1.00 41.38           O  
ANISOU 4266  O   LYS A 541     4355   6418   4949    896   -306   -816       O  
ATOM   4267  CB  LYS A 541      -3.974   4.002 -21.707  1.00 46.03           C  
ANISOU 4267  CB  LYS A 541     4861   7044   5582    899   -251   -875       C  
ATOM   4268  CG  LYS A 541      -3.720   3.573 -23.140  1.00 45.11           C  
ANISOU 4268  CG  LYS A 541     4739   6913   5488    902   -212   -895       C  
ATOM   4269  CD  LYS A 541      -2.873   2.312 -23.183  1.00 46.44           C  
ANISOU 4269  CD  LYS A 541     4900   7096   5650   1015   -219   -898       C  
ATOM   4270  CE  LYS A 541      -1.697   2.466 -24.133  1.00 70.41           C  
ANISOU 4270  CE  LYS A 541     7848  10206   8698   1024   -198   -945       C  
ATOM   4271  NZ  LYS A 541      -1.504   1.257 -24.980  1.00 73.78           N  
ANISOU 4271  NZ  LYS A 541     8310  10591   9133   1093   -170   -946       N  
ATOM   4272  N   CYS A 542      -5.813   6.352 -19.766  1.00 47.64           N  
ANISOU 4272  N   CYS A 542     5114   7218   5769    734   -272   -843       N  
ATOM   4273  CA  CYS A 542      -5.665   6.944 -18.446  1.00 47.79           C  
ANISOU 4273  CA  CYS A 542     5120   7278   5760    727   -305   -842       C  
ATOM   4274  C   CYS A 542      -6.820   6.587 -17.520  1.00 49.99           C  
ANISOU 4274  C   CYS A 542     5486   7482   6026    734   -309   -798       C  
ATOM   4275  O   CYS A 542      -7.991   6.638 -17.906  1.00 48.50           O  
ANISOU 4275  O   CYS A 542     5354   7216   5858    691   -279   -777       O  
ATOM   4276  CB  CYS A 542      -5.550   8.460 -18.563  1.00 44.10           C  
ANISOU 4276  CB  CYS A 542     4604   6853   5299    632   -294   -872       C  
ATOM   4277  SG  CYS A 542      -6.025   9.347 -17.077  1.00 48.77           S  
ANISOU 4277  SG  CYS A 542     5219   7449   5862    591   -316   -862       S  
ATOM   4278  N   ASP A 543      -6.472   6.239 -16.284  1.00 60.25           N  
ANISOU 4278  N   ASP A 543     6795   8809   7290    788   -346   -786       N  
ATOM   4279  CA  ASP A 543      -7.427   6.025 -15.205  1.00 55.67           C  
ANISOU 4279  CA  ASP A 543     6293   8171   6688    791   -351   -748       C  
ATOM   4280  C   ASP A 543      -7.037   6.944 -14.058  1.00 51.36           C  
ANISOU 4280  C   ASP A 543     5718   7687   6109    766   -381   -762       C  
ATOM   4281  O   ASP A 543      -5.901   6.890 -13.575  1.00 60.04           O  
ANISOU 4281  O   ASP A 543     6763   8869   7181    810   -422   -781       O  
ATOM   4282  CB  ASP A 543      -7.432   4.561 -14.757  1.00 56.49           C  
ANISOU 4282  CB  ASP A 543     6458   8234   6770    887   -366   -714       C  
ATOM   4283  CG  ASP A 543      -8.424   4.291 -13.642  1.00 54.98           C  
ANISOU 4283  CG  ASP A 543     6354   7980   6555    888   -365   -675       C  
ATOM   4284  OD1 ASP A 543      -9.318   5.133 -13.412  1.00 62.51           O  
ANISOU 4284  OD1 ASP A 543     7328   8906   7519    812   -343   -672       O  
ATOM   4285  OD2 ASP A 543      -8.308   3.231 -12.991  1.00 56.39           O1-
ANISOU 4285  OD2 ASP A 543     6586   8137   6704    966   -383   -647       O1-
ATOM   4286  N   ILE A 544      -7.973   7.786 -13.624  1.00 42.03           N  
ANISOU 4286  N   ILE A 544     4572   6469   4930    696   -362   -754       N  
ATOM   4287  CA  ILE A 544      -7.682   8.782 -12.598  1.00 45.45           C  
ANISOU 4287  CA  ILE A 544     4983   6955   5331    658   -384   -772       C  
ATOM   4288  C   ILE A 544      -7.879   8.179 -11.214  1.00 44.76           C  
ANISOU 4288  C   ILE A 544     4956   6854   5197    710   -412   -741       C  
ATOM   4289  O   ILE A 544      -7.800   8.887 -10.205  1.00 42.02           O  
ANISOU 4289  O   ILE A 544     4611   6538   4816    682   -430   -750       O  
ATOM   4290  CB  ILE A 544      -8.551  10.040 -12.777  1.00 33.64           C  
ANISOU 4290  CB  ILE A 544     3498   5426   3858    560   -346   -780       C  
ATOM   4291  CG1 ILE A 544     -10.023   9.721 -12.508  1.00 41.10           C  
ANISOU 4291  CG1 ILE A 544     4529   6272   4814    550   -314   -740       C  
ATOM   4292  CG2 ILE A 544      -8.372  10.618 -14.171  1.00 34.29           C  
ANISOU 4292  CG2 ILE A 544     3530   5516   3981    511   -319   -806       C  
ATOM   4293  CD1 ILE A 544     -10.925  10.936 -12.538  1.00 34.57           C  
ANISOU 4293  CD1 ILE A 544     3715   5412   4007    466   -280   -745       C  
ATOM   4294  N   SER A 545      -8.116   6.870 -11.156  1.00 42.12           N  
ANISOU 4294  N   SER A 545     4678   6471   4856    784   -414   -707       N  
ATOM   4295  CA  SER A 545      -8.379   6.207  -9.886  1.00 38.62           C  
ANISOU 4295  CA  SER A 545     4307   6002   4366    834   -435   -673       C  
ATOM   4296  C   SER A 545      -7.183   6.334  -8.948  1.00 47.53           C  
ANISOU 4296  C   SER A 545     5392   7225   5443    879   -496   -689       C  
ATOM   4297  O   SER A 545      -6.032   6.436  -9.380  1.00 50.95           O  
ANISOU 4297  O   SER A 545     5740   7740   5880    903   -525   -721       O  
ATOM   4298  CB  SER A 545      -8.704   4.731 -10.112  1.00 35.29           C  
ANISOU 4298  CB  SER A 545     3951   5511   3946    909   -426   -635       C  
ATOM   4299  OG  SER A 545      -9.870   4.579 -10.899  1.00 37.75           O  
ANISOU 4299  OG  SER A 545     4306   5737   4302    864   -373   -620       O  
ATOM   4300  N   ASN A 546      -7.476   6.346  -7.648  1.00 50.66           N  
ANISOU 4300  N   ASN A 546     5847   7613   5790    887   -514   -669       N  
ATOM   4301  CA  ASN A 546      -6.492   6.429  -6.571  1.00 43.74           C  
ANISOU 4301  CA  ASN A 546     4946   6820   4854    929   -576   -679       C  
ATOM   4302  C   ASN A 546      -5.688   7.723  -6.600  1.00 47.91           C  
ANISOU 4302  C   ASN A 546     5377   7444   5381    865   -597   -732       C  
ATOM   4303  O   ASN A 546      -4.665   7.825  -5.912  1.00 55.92           O  
ANISOU 4303  O   ASN A 546     6346   8548   6352    897   -655   -750       O  
ATOM   4304  CB  ASN A 546      -5.539   5.227  -6.590  1.00 41.46           C  
ANISOU 4304  CB  ASN A 546     4643   6565   4545   1044   -622   -666       C  
ATOM   4305  CG  ASN A 546      -6.210   3.941  -6.148  1.00 50.71           C  
ANISOU 4305  CG  ASN A 546     5927   7647   5694   1114   -612   -612       C  
ATOM   4306  OD1 ASN A 546      -7.339   3.950  -5.659  1.00 53.57           O  
ANISOU 4306  OD1 ASN A 546     6375   7930   6048   1076   -576   -584       O  
ATOM   4307  ND2 ASN A 546      -5.513   2.825  -6.324  1.00 57.09           N  
ANISOU 4307  ND2 ASN A 546     6735   8464   6492   1218   -641   -597       N  
ATOM   4308  N   SER A 547      -6.122   8.716  -7.369  1.00 41.81           N  
ANISOU 4308  N   SER A 547     4575   6657   4654    774   -553   -757       N  
ATOM   4309  CA  SER A 547      -5.407   9.981  -7.517  1.00 44.27           C  
ANISOU 4309  CA  SER A 547     4803   7050   4969    703   -562   -808       C  
ATOM   4310  C   SER A 547      -6.235  11.079  -6.856  1.00 46.42           C  
ANISOU 4310  C   SER A 547     5121   7289   5229    617   -535   -813       C  
ATOM   4311  O   SER A 547      -7.093  11.697  -7.488  1.00 42.68           O  
ANISOU 4311  O   SER A 547     4665   6756   4797    551   -482   -813       O  
ATOM   4312  CB  SER A 547      -5.142  10.289  -8.988  1.00 36.70           C  
ANISOU 4312  CB  SER A 547     3776   6100   4068    669   -531   -835       C  
ATOM   4313  OG  SER A 547      -4.743  11.638  -9.161  1.00 36.87           O  
ANISOU 4313  OG  SER A 547     3738   6175   4095    580   -523   -881       O  
ATOM   4314  N   THR A 548      -5.968  11.320  -5.570  1.00 57.31           N  
ANISOU 4314  N   THR A 548     6521   8707   6549    620   -572   -816       N  
ATOM   4315  CA  THR A 548      -6.641  12.405  -4.865  1.00 50.47           C  
ANISOU 4315  CA  THR A 548     5696   7816   5665    539   -547   -826       C  
ATOM   4316  C   THR A 548      -6.274  13.769  -5.431  1.00 47.07           C  
ANISOU 4316  C   THR A 548     5198   7426   5258    447   -528   -877       C  
ATOM   4317  O   THR A 548      -7.051  14.719  -5.283  1.00 52.82           O  
ANISOU 4317  O   THR A 548     5964   8110   5996    373   -486   -883       O  
ATOM   4318  CB  THR A 548      -6.308  12.355  -3.373  1.00 45.39           C  
ANISOU 4318  CB  THR A 548     5088   7213   4944    563   -595   -823       C  
ATOM   4319  OG1 THR A 548      -4.924  12.028  -3.200  1.00 63.24           O  
ANISOU 4319  OG1 THR A 548     7274   9580   7174    615   -665   -845       O  
ATOM   4320  CG2 THR A 548      -7.163  11.309  -2.673  1.00 49.54           C  
ANISOU 4320  CG2 THR A 548     5718   7661   5445    623   -587   -768       C  
ATOM   4321  N   GLU A 549      -5.105  13.890  -6.066  1.00 53.54           N  
ANISOU 4321  N   GLU A 549     5922   8331   6088    449   -556   -913       N  
ATOM   4322  CA  GLU A 549      -4.736  15.149  -6.704  1.00 59.63           C  
ANISOU 4322  CA  GLU A 549     6634   9138   6885    357   -533   -961       C  
ATOM   4323  C   GLU A 549      -5.696  15.493  -7.836  1.00 59.05           C  
ANISOU 4323  C   GLU A 549     6585   8978   6872    313   -466   -949       C  
ATOM   4324  O   GLU A 549      -6.113  16.648  -7.979  1.00 56.25           O  
ANISOU 4324  O   GLU A 549     6242   8599   6530    229   -428   -969       O  
ATOM   4325  CB  GLU A 549      -3.300  15.072  -7.223  1.00 61.08           C  
ANISOU 4325  CB  GLU A 549     6708   9430   7071    373   -572  -1001       C  
ATOM   4326  CG  GLU A 549      -2.334  14.369  -6.283  1.00 77.51           C  
ANISOU 4326  CG  GLU A 549     8755  11596   9098    448   -646  -1003       C  
ATOM   4327  CD  GLU A 549      -1.441  15.336  -5.531  1.00 92.75           C  
ANISOU 4327  CD  GLU A 549    10631  13625  10985    390   -685  -1054       C  
ATOM   4328  OE1 GLU A 549      -1.963  16.338  -4.998  1.00 93.04           O  
ANISOU 4328  OE1 GLU A 549    10714  13634  11004    309   -662  -1068       O  
ATOM   4329  OE2 GLU A 549      -0.217  15.095  -5.475  1.00 85.92           O1-
ANISOU 4329  OE2 GLU A 549     9676  12867  10104    424   -739  -1083       O1-
ATOM   4330  N   ALA A 550      -6.053  14.501  -8.656  1.00 51.70           N  
ANISOU 4330  N   ALA A 550     5665   8001   5978    369   -451   -918       N  
ATOM   4331  CA  ALA A 550      -7.016  14.735  -9.727  1.00 39.18           C  
ANISOU 4331  CA  ALA A 550     4105   6334   4447    332   -394   -903       C  
ATOM   4332  C   ALA A 550      -8.394  15.068  -9.169  1.00 45.12           C  
ANISOU 4332  C   ALA A 550     4944   6998   5201    302   -357   -874       C  
ATOM   4333  O   ALA A 550      -9.076  15.964  -9.679  1.00 50.76           O  
ANISOU 4333  O   ALA A 550     5672   7668   5946    238   -313   -880       O  
ATOM   4334  CB  ALA A 550      -7.089  13.516 -10.645  1.00 35.68           C  
ANISOU 4334  CB  ALA A 550     3659   5861   4035    399   -390   -877       C  
ATOM   4335  N   GLY A 551      -8.821  14.354  -8.124  1.00 53.19           N  
ANISOU 4335  N   GLY A 551     6026   7995   6189    350   -373   -843       N  
ATOM   4336  CA  GLY A 551     -10.128  14.619  -7.546  1.00 44.86           C  
ANISOU 4336  CA  GLY A 551     5049   6859   5135    324   -334   -817       C  
ATOM   4337  C   GLY A 551     -10.239  16.014  -6.962  1.00 43.86           C  
ANISOU 4337  C   GLY A 551     4931   6743   4992    247   -317   -847       C  
ATOM   4338  O   GLY A 551     -11.246  16.699  -7.156  1.00 48.07           O  
ANISOU 4338  O   GLY A 551     5498   7212   5554    200   -268   -841       O  
ATOM   4339  N   GLN A 552      -9.206  16.455  -6.240  1.00 59.24           N  
ANISOU 4339  N   GLN A 552     6845   8771   6892    234   -358   -880       N  
ATOM   4340  CA  GLN A 552      -9.198  17.816  -5.714  1.00 60.60           C  
ANISOU 4340  CA  GLN A 552     7025   8956   7044    154   -342   -915       C  
ATOM   4341  C   GLN A 552      -9.199  18.839  -6.843  1.00 56.19           C  
ANISOU 4341  C   GLN A 552     6429   8388   6533     86   -304   -942       C  
ATOM   4342  O   GLN A 552      -9.888  19.863  -6.764  1.00 56.07           O  
ANISOU 4342  O   GLN A 552     6450   8325   6528     26   -261   -950       O  
ATOM   4343  CB  GLN A 552      -7.987  18.020  -4.804  1.00 63.90           C  
ANISOU 4343  CB  GLN A 552     7406   9472   7400    152   -399   -950       C  
ATOM   4344  CG  GLN A 552      -7.887  19.413  -4.200  1.00 55.15           C  
ANISOU 4344  CG  GLN A 552     6309   8381   6265     65   -386   -991       C  
ATOM   4345  CD  GLN A 552      -8.915  19.652  -3.111  1.00 67.51           C  
ANISOU 4345  CD  GLN A 552     7968   9882   7801     53   -358   -972       C  
ATOM   4346  OE1 GLN A 552      -9.256  18.744  -2.352  1.00 58.96           O  
ANISOU 4346  OE1 GLN A 552     6934   8781   6688    113   -375   -937       O  
ATOM   4347  NE2 GLN A 552      -9.415  20.880  -3.029  1.00 66.26           N  
ANISOU 4347  NE2 GLN A 552     7840   9686   7650    -23   -311   -994       N  
ATOM   4348  N   LYS A 553      -8.428  18.579  -7.902  1.00 58.29           N  
ANISOU 4348  N   LYS A 553     6626   8696   6826     96   -317   -956       N  
ATOM   4349  CA  LYS A 553      -8.428  19.468  -9.058  1.00 47.23           C  
ANISOU 4349  CA  LYS A 553     5196   7282   5468     34   -279   -978       C  
ATOM   4350  C   LYS A 553      -9.803  19.519  -9.711  1.00 51.77           C  
ANISOU 4350  C   LYS A 553     5825   7756   6090     29   -228   -942       C  
ATOM   4351  O   LYS A 553     -10.284  20.596 -10.083  1.00 54.38           O  
ANISOU 4351  O   LYS A 553     6173   8047   6441    -32   -188   -953       O  
ATOM   4352  CB  LYS A 553      -7.372  19.012 -10.065  1.00 42.09           C  
ANISOU 4352  CB  LYS A 553     4465   6694   4834     54   -301   -996       C  
ATOM   4353  CG  LYS A 553      -7.204  19.932 -11.260  1.00 45.08           C  
ANISOU 4353  CG  LYS A 553     4813   7068   5248    -14   -263  -1022       C  
ATOM   4354  CD  LYS A 553      -5.869  19.690 -11.946  1.00 56.03           C  
ANISOU 4354  CD  LYS A 553     6111   8542   6637     -8   -287  -1056       C  
ATOM   4355  CE  LYS A 553      -4.968  20.909 -11.852  1.00 58.58           C  
ANISOU 4355  CE  LYS A 553     6388   8929   6940    -94   -284  -1111       C  
ATOM   4356  NZ  LYS A 553      -5.022  21.734 -13.090  1.00 66.30           N  
ANISOU 4356  NZ  LYS A 553     7360   9880   7953   -160   -234  -1127       N  
ATOM   4357  N   LEU A 554     -10.450  18.362  -9.860  1.00 44.38           N  
ANISOU 4357  N   LEU A 554     4916   6776   5172     94   -229   -900       N  
ATOM   4358  CA  LEU A 554     -11.801  18.335 -10.407  1.00 39.27           C  
ANISOU 4358  CA  LEU A 554     4315   6038   4569     90   -185   -867       C  
ATOM   4359  C   LEU A 554     -12.802  18.954  -9.439  1.00 45.77           C  
ANISOU 4359  C   LEU A 554     5200   6808   5380     64   -155   -856       C  
ATOM   4360  O   LEU A 554     -13.687  19.712  -9.854  1.00 43.39           O  
ANISOU 4360  O   LEU A 554     4923   6450   5112     27   -113   -851       O  
ATOM   4361  CB  LEU A 554     -12.198  16.899 -10.745  1.00 40.14           C  
ANISOU 4361  CB  LEU A 554     4438   6118   4696    160   -194   -828       C  
ATOM   4362  CG  LEU A 554     -13.655  16.678 -11.150  1.00 37.52           C  
ANISOU 4362  CG  LEU A 554     4154   5697   4406    161   -154   -792       C  
ATOM   4363  CD1 LEU A 554     -13.938  17.277 -12.521  1.00 28.11           C  
ANISOU 4363  CD1 LEU A 554     2940   4480   3261    123   -128   -798       C  
ATOM   4364  CD2 LEU A 554     -13.989  15.200 -11.123  1.00 22.31           C  
ANISOU 4364  CD2 LEU A 554     2251   3743   2482    227   -166   -757       C  
ATOM   4365  N   PHE A 555     -12.675  18.647  -8.144  1.00 48.38           N  
ANISOU 4365  N   PHE A 555     5561   7158   5664     86   -176   -853       N  
ATOM   4366  CA  PHE A 555     -13.603  19.188  -7.156  1.00 34.55           C  
ANISOU 4366  CA  PHE A 555     3873   5357   3896     63   -144   -845       C  
ATOM   4367  C   PHE A 555     -13.547  20.707  -7.103  1.00 36.30           C  
ANISOU 4367  C   PHE A 555     4096   5579   4116    -11   -117   -881       C  
ATOM   4368  O   PHE A 555     -14.565  21.351  -6.832  1.00 36.84           O  
ANISOU 4368  O   PHE A 555     4212   5586   4200    -37    -72   -873       O  
ATOM   4369  CB  PHE A 555     -13.307  18.601  -5.774  1.00 36.83           C  
ANISOU 4369  CB  PHE A 555     4195   5675   4124     98   -176   -839       C  
ATOM   4370  CG  PHE A 555     -14.294  19.007  -4.716  1.00 45.93           C  
ANISOU 4370  CG  PHE A 555     5419   6774   5257     79   -139   -829       C  
ATOM   4371  CD1 PHE A 555     -15.494  18.330  -4.573  1.00 42.80           C  
ANISOU 4371  CD1 PHE A 555     5072   6307   4883    108   -105   -788       C  
ATOM   4372  CD2 PHE A 555     -14.019  20.061  -3.859  1.00 42.08           C  
ANISOU 4372  CD2 PHE A 555     4950   6309   4729     29   -135   -862       C  
ATOM   4373  CE1 PHE A 555     -16.403  18.699  -3.598  1.00 42.34           C  
ANISOU 4373  CE1 PHE A 555     5076   6202   4808     91    -66   -781       C  
ATOM   4374  CE2 PHE A 555     -14.925  20.435  -2.883  1.00 42.83           C  
ANISOU 4374  CE2 PHE A 555     5115   6354   4806     13    -96   -854       C  
ATOM   4375  CZ  PHE A 555     -16.118  19.753  -2.753  1.00 42.24           C  
ANISOU 4375  CZ  PHE A 555     5084   6210   4754     46    -60   -813       C  
ATOM   4376  N   ASN A 556     -12.373  21.295  -7.361  1.00 45.13           N  
ANISOU 4376  N   ASN A 556     5165   6766   5218    -47   -141   -921       N  
ATOM   4377  CA  ASN A 556     -12.245  22.749  -7.341  1.00 46.73           C  
ANISOU 4377  CA  ASN A 556     5374   6966   5416   -124   -114   -958       C  
ATOM   4378  C   ASN A 556     -13.204  23.411  -8.321  1.00 49.31           C  
ANISOU 4378  C   ASN A 556     5720   7218   5799   -150    -61   -945       C  
ATOM   4379  O   ASN A 556     -13.666  24.532  -8.078  1.00 46.50           O  
ANISOU 4379  O   ASN A 556     5402   6822   5443   -198    -22   -958       O  
ATOM   4380  CB  ASN A 556     -10.804  23.154  -7.654  1.00 46.76           C  
ANISOU 4380  CB  ASN A 556     5311   7057   5399   -161   -146  -1004       C  
ATOM   4381  CG  ASN A 556      -9.890  23.034  -6.451  1.00 54.12           C  
ANISOU 4381  CG  ASN A 556     6231   8065   6266   -160   -194  -1030       C  
ATOM   4382  OD1 ASN A 556     -10.263  22.460  -5.427  1.00 51.48           O  
ANISOU 4382  OD1 ASN A 556     5939   7721   5900   -120   -208  -1009       O  
ATOM   4383  ND2 ASN A 556      -8.683  23.576  -6.569  1.00 48.08           N  
ANISOU 4383  ND2 ASN A 556     5409   7379   5480   -205   -218  -1077       N  
ATOM   4384  N   MET A 557     -13.513  22.739  -9.429  1.00 49.90           N  
ANISOU 4384  N   MET A 557     5772   7271   5918   -117    -60   -918       N  
ATOM   4385  CA  MET A 557     -14.515  23.226 -10.367  1.00 46.92           C  
ANISOU 4385  CA  MET A 557     5413   6822   5592   -131    -17   -899       C  
ATOM   4386  C   MET A 557     -15.917  22.754 -10.009  1.00 46.36           C  
ANISOU 4386  C   MET A 557     5388   6682   5546    -94      8   -858       C  
ATOM   4387  O   MET A 557     -16.883  23.509 -10.167  1.00 43.92           O  
ANISOU 4387  O   MET A 557     5111   6312   5265   -114     50   -850       O  
ATOM   4388  CB  MET A 557     -14.174  22.776 -11.788  1.00 35.38           C  
ANISOU 4388  CB  MET A 557     3906   5372   4164   -119    -28   -893       C  
ATOM   4389  CG  MET A 557     -15.143  23.283 -12.839  1.00 44.54           C  
ANISOU 4389  CG  MET A 557     5085   6464   5374   -133      9   -873       C  
ATOM   4390  SD  MET A 557     -16.475  22.119 -13.184  1.00 47.20           S  
ANISOU 4390  SD  MET A 557     5439   6742   5752    -72     14   -821       S  
ATOM   4391  CE  MET A 557     -15.555  20.596 -13.363  1.00 38.94           C  
ANISOU 4391  CE  MET A 557     4352   5753   4691    -21    -33   -817       C  
ATOM   4392  N   LEU A 558     -16.045  21.511  -9.537  1.00 42.40           N  
ANISOU 4392  N   LEU A 558     4890   6187   5033    -41    -14   -834       N  
ATOM   4393  CA  LEU A 558     -17.364  20.965  -9.238  1.00 38.11           C  
ANISOU 4393  CA  LEU A 558     4386   5579   4513    -10     13   -797       C  
ATOM   4394  C   LEU A 558     -18.066  21.776  -8.156  1.00 43.12           C  
ANISOU 4394  C   LEU A 558     5072   6179   5132    -34     50   -802       C  
ATOM   4395  O   LEU A 558     -19.273  22.030  -8.245  1.00 48.81           O  
ANISOU 4395  O   LEU A 558     5818   6838   5889    -35     91   -782       O  
ATOM   4396  CB  LEU A 558     -17.248  19.499  -8.815  1.00 41.00           C  
ANISOU 4396  CB  LEU A 558     4757   5960   4860     46    -16   -773       C  
ATOM   4397  CG  LEU A 558     -16.622  18.458  -9.746  1.00 36.72           C  
ANISOU 4397  CG  LEU A 558     4175   5447   4331     84    -51   -764       C  
ATOM   4398  CD1 LEU A 558     -16.647  17.092  -9.078  1.00 33.04           C  
ANISOU 4398  CD1 LEU A 558     3733   4981   3841    141    -72   -738       C  
ATOM   4399  CD2 LEU A 558     -17.324  18.404 -11.089  1.00 40.12           C  
ANISOU 4399  CD2 LEU A 558     4590   5834   4819     80    -32   -748       C  
ATOM   4400  N   ARG A 559     -17.325  22.191  -7.125  1.00 48.10           N  
ANISOU 4400  N   ARG A 559     5718   6851   5708    -55     36   -830       N  
ATOM   4401  CA  ARG A 559     -17.922  22.970  -6.044  1.00 47.91           C  
ANISOU 4401  CA  ARG A 559     5748   6794   5662    -80     74   -839       C  
ATOM   4402  C   ARG A 559     -18.407  24.331  -6.523  1.00 42.26           C  
ANISOU 4402  C   ARG A 559     5044   6035   4978   -126    118   -854       C  
ATOM   4403  O   ARG A 559     -19.331  24.900  -5.930  1.00 49.64           O  
ANISOU 4403  O   ARG A 559     6024   6919   5919   -134    164   -850       O  
ATOM   4404  CB  ARG A 559     -16.916  23.146  -4.906  1.00 53.59           C  
ANISOU 4404  CB  ARG A 559     6480   7573   6311    -97     43   -869       C  
ATOM   4405  CG  ARG A 559     -15.612  23.808  -5.330  1.00 55.15           C  
ANISOU 4405  CG  ARG A 559     6632   7834   6489   -139     12   -911       C  
ATOM   4406  CD  ARG A 559     -14.859  24.372  -4.140  1.00 62.18           C  
ANISOU 4406  CD  ARG A 559     7543   8772   7312   -174     -6   -948       C  
ATOM   4407  NE  ARG A 559     -15.702  25.248  -3.336  1.00 65.72           N  
ANISOU 4407  NE  ARG A 559     8057   9163   7749   -205     46   -955       N  
ATOM   4408  CZ  ARG A 559     -15.827  26.552  -3.538  1.00 62.45           C  
ANISOU 4408  CZ  ARG A 559     7661   8720   7345   -262     85   -982       C  
ATOM   4409  NH1 ARG A 559     -15.165  27.169  -4.504  1.00 59.12           N  
ANISOU 4409  NH1 ARG A 559     7200   8320   6944   -300     79  -1005       N  
ATOM   4410  NH2 ARG A 559     -16.634  27.256  -2.750  1.00 59.34           N  
ANISOU 4410  NH2 ARG A 559     7333   8273   6942   -281    134   -987       N  
ATOM   4411  N   LEU A 560     -17.799  24.870  -7.583  1.00 43.45           N  
ANISOU 4411  N   LEU A 560     5158   6204   5148   -153    108   -871       N  
ATOM   4412  CA  LEU A 560     -18.159  26.206  -8.048  1.00 44.91           C  
ANISOU 4412  CA  LEU A 560     5361   6346   5356   -196    150   -885       C  
ATOM   4413  C   LEU A 560     -19.595  26.253  -8.552  1.00 42.45           C  
ANISOU 4413  C   LEU A 560     5067   5960   5102   -170    189   -850       C  
ATOM   4414  O   LEU A 560     -20.320  27.221  -8.294  1.00 44.49           O  
ANISOU 4414  O   LEU A 560     5364   6168   5373   -187    234   -854       O  
ATOM   4415  CB  LEU A 560     -17.191  26.655  -9.142  1.00 36.29           C  
ANISOU 4415  CB  LEU A 560     4229   5289   4271   -230    131   -907       C  
ATOM   4416  CG  LEU A 560     -15.867  27.249  -8.660  1.00 49.19           C  
ANISOU 4416  CG  LEU A 560     5852   6986   5852   -282    111   -955       C  
ATOM   4417  CD1 LEU A 560     -15.149  27.956  -9.797  1.00 47.46           C  
ANISOU 4417  CD1 LEU A 560     5604   6783   5646   -327    113   -978       C  
ATOM   4418  CD2 LEU A 560     -16.104  28.204  -7.500  1.00 56.01           C  
ANISOU 4418  CD2 LEU A 560     6773   7826   6682   -319    142   -979       C  
ATOM   4419  N   GLY A 561     -20.026  25.216  -9.262  1.00 39.28           N  
ANISOU 4419  N   GLY A 561     4636   5553   4736   -128    173   -817       N  
ATOM   4420  CA  GLY A 561     -21.347  25.252  -9.864  1.00 30.83           C  
ANISOU 4420  CA  GLY A 561     3571   4422   3723   -106    204   -786       C  
ATOM   4421  C   GLY A 561     -21.430  26.352 -10.903  1.00 37.86           C  
ANISOU 4421  C   GLY A 561     4460   5285   4642   -133    221   -793       C  
ATOM   4422  O   GLY A 561     -20.551  26.497 -11.760  1.00 43.81           O  
ANISOU 4422  O   GLY A 561     5188   6069   5390   -153    197   -806       O  
ATOM   4423  N   LYS A 562     -22.502  27.141 -10.835  1.00 43.52           N  
ANISOU 4423  N   LYS A 562     5206   5943   5389   -130    264   -783       N  
ATOM   4424  CA  LYS A 562     -22.675  28.306 -11.692  1.00 35.24           C  
ANISOU 4424  CA  LYS A 562     4169   4857   4363   -151    285   -787       C  
ATOM   4425  C   LYS A 562     -22.267  29.603 -11.007  1.00 42.17           C  
ANISOU 4425  C   LYS A 562     5094   5721   5208   -195    317   -821       C  
ATOM   4426  O   LYS A 562     -22.489  30.681 -11.566  1.00 46.03           O  
ANISOU 4426  O   LYS A 562     5609   6168   5714   -212    343   -825       O  
ATOM   4427  CB  LYS A 562     -24.125  28.410 -12.168  1.00 36.70           C  
ANISOU 4427  CB  LYS A 562     4355   4984   4605   -114    311   -754       C  
ATOM   4428  CG  LYS A 562     -24.322  28.059 -13.633  1.00 42.34           C  
ANISOU 4428  CG  LYS A 562     5035   5696   5356    -98    284   -729       C  
ATOM   4429  CD  LYS A 562     -25.767  27.693 -13.922  1.00 52.88           C  
ANISOU 4429  CD  LYS A 562     6355   6993   6745    -55    296   -695       C  
ATOM   4430  CE  LYS A 562     -26.518  28.828 -14.596  1.00 59.09           C  
ANISOU 4430  CE  LYS A 562     7158   7727   7565    -48    320   -684       C  
ATOM   4431  NZ  LYS A 562     -27.675  28.315 -15.383  1.00 62.94           N  
ANISOU 4431  NZ  LYS A 562     7612   8197   8106     -8    309   -649       N  
ATOM   4432  N   SER A 563     -21.678  29.522  -9.812  1.00 36.10           N  
ANISOU 4432  N   SER A 563     4342   4984   4391   -214    315   -847       N  
ATOM   4433  CA  SER A 563     -21.328  30.729  -9.069  1.00 42.76           C  
ANISOU 4433  CA  SER A 563     5236   5814   5199   -261    346   -883       C  
ATOM   4434  C   SER A 563     -20.305  31.567  -9.822  1.00 42.46           C  
ANISOU 4434  C   SER A 563     5197   5792   5146   -314    338   -911       C  
ATOM   4435  O   SER A 563     -20.383  32.802  -9.831  1.00 47.29           O  
ANISOU 4435  O   SER A 563     5854   6360   5753   -348    377   -930       O  
ATOM   4436  CB  SER A 563     -20.793  30.355  -7.688  1.00 41.68           C  
ANISOU 4436  CB  SER A 563     5113   5719   5006   -273    335   -906       C  
ATOM   4437  OG  SER A 563     -19.517  29.744  -7.787  1.00 38.72           O  
ANISOU 4437  OG  SER A 563     4697   5420   4596   -289    282   -923       O  
ATOM   4438  N   GLU A 564     -19.346  30.917 -10.458  1.00 51.28           N  
ANISOU 4438  N   GLU A 564     6263   6969   6253   -322    293   -916       N  
ATOM   4439  CA  GLU A 564     -18.237  31.569 -11.124  1.00 52.73           C  
ANISOU 4439  CA  GLU A 564     6436   7181   6416   -377    284   -947       C  
ATOM   4440  C   GLU A 564     -18.313  31.349 -12.631  1.00 44.61           C  
ANISOU 4440  C   GLU A 564     5379   6144   5427   -363    273   -923       C  
ATOM   4441  O   GLU A 564     -18.948  30.396 -13.096  1.00 44.46           O  
ANISOU 4441  O   GLU A 564     5331   6119   5441   -310    255   -887       O  
ATOM   4442  CB  GLU A 564     -16.915  31.020 -10.573  1.00 49.83           C  
ANISOU 4442  CB  GLU A 564     6030   6902   6001   -402    242   -980       C  
ATOM   4443  CG  GLU A 564     -15.928  32.082 -10.135  1.00 53.27           C  
ANISOU 4443  CG  GLU A 564     6486   7362   6391   -478    252  -1031       C  
ATOM   4444  CD  GLU A 564     -16.390  32.880  -8.934  1.00 61.74           C  
ANISOU 4444  CD  GLU A 564     7625   8396   7438   -499    289  -1049       C  
ATOM   4445  OE1 GLU A 564     -16.550  32.288  -7.848  1.00 66.72           O  
ANISOU 4445  OE1 GLU A 564     8260   9047   8044   -474    276  -1047       O  
ATOM   4446  OE2 GLU A 564     -16.591  34.103  -9.079  1.00 64.46           O1-
ANISOU 4446  OE2 GLU A 564     8021   8686   7784   -540    334  -1065       O1-
ATOM   4447  N   PRO A 565     -17.698  32.225 -13.429  1.00 34.85           N  
ANISOU 4447  N   PRO A 565     4153   4902   4185   -412    285   -942       N  
ATOM   4448  CA  PRO A 565     -17.734  32.042 -14.885  1.00 31.58           C  
ANISOU 4448  CA  PRO A 565     3718   4479   3802   -401    275   -920       C  
ATOM   4449  C   PRO A 565     -17.162  30.694 -15.296  1.00 36.72           C  
ANISOU 4449  C   PRO A 565     4302   5195   4453   -374    227   -912       C  
ATOM   4450  O   PRO A 565     -16.196  30.202 -14.708  1.00 47.48           O  
ANISOU 4450  O   PRO A 565     5630   6626   5784   -388    201   -939       O  
ATOM   4451  CB  PRO A 565     -16.875  33.197 -15.408  1.00 36.00           C  
ANISOU 4451  CB  PRO A 565     4304   5037   4339   -473    298   -953       C  
ATOM   4452  CG  PRO A 565     -16.976  34.242 -14.360  1.00 36.89           C  
ANISOU 4452  CG  PRO A 565     4474   5117   4427   -509    335   -980       C  
ATOM   4453  CD  PRO A 565     -17.095  33.517 -13.052  1.00 40.89           C  
ANISOU 4453  CD  PRO A 565     4963   5657   4916   -482    316   -984       C  
ATOM   4454  N   TRP A 566     -17.780  30.091 -16.315  1.00 36.02           N  
ANISOU 4454  N   TRP A 566     4197   5086   4402   -333    216   -876       N  
ATOM   4455  CA  TRP A 566     -17.299  28.810 -16.819  1.00 37.45           C  
ANISOU 4455  CA  TRP A 566     4322   5320   4586   -305    175   -868       C  
ATOM   4456  C   TRP A 566     -15.880  28.908 -17.358  1.00 39.10           C  
ANISOU 4456  C   TRP A 566     4499   5589   4769   -351    163   -903       C  
ATOM   4457  O   TRP A 566     -15.172  27.895 -17.394  1.00 37.95           O  
ANISOU 4457  O   TRP A 566     4302   5503   4613   -332    130   -910       O  
ATOM   4458  CB  TRP A 566     -18.244  28.277 -17.900  1.00 33.94           C  
ANISOU 4458  CB  TRP A 566     3874   4837   4184   -263    168   -826       C  
ATOM   4459  CG  TRP A 566     -18.173  29.017 -19.203  1.00 33.34           C  
ANISOU 4459  CG  TRP A 566     3816   4734   4118   -289    181   -823       C  
ATOM   4460  CD1 TRP A 566     -18.959  30.062 -19.595  1.00 34.75           C  
ANISOU 4460  CD1 TRP A 566     4044   4847   4314   -295    210   -807       C  
ATOM   4461  CD2 TRP A 566     -17.276  28.761 -20.291  1.00 29.46           C  
ANISOU 4461  CD2 TRP A 566     3299   4279   3617   -311    167   -834       C  
ATOM   4462  NE1 TRP A 566     -18.603  30.476 -20.855  1.00 30.65           N  
ANISOU 4462  NE1 TRP A 566     3535   4319   3793   -320    213   -806       N  
ATOM   4463  CE2 TRP A 566     -17.572  29.694 -21.305  1.00 32.03           C  
ANISOU 4463  CE2 TRP A 566     3664   4556   3951   -333    189   -823       C  
ATOM   4464  CE3 TRP A 566     -16.249  27.836 -20.505  1.00 32.28           C  
ANISOU 4464  CE3 TRP A 566     3603   4703   3958   -310    140   -851       C  
ATOM   4465  CZ2 TRP A 566     -16.878  29.729 -22.513  1.00 33.16           C  
ANISOU 4465  CZ2 TRP A 566     3800   4715   4084   -360    187   -830       C  
ATOM   4466  CZ3 TRP A 566     -15.561  27.873 -21.705  1.00 27.42           C  
ANISOU 4466  CZ3 TRP A 566     2975   4105   3337   -336    140   -860       C  
ATOM   4467  CH2 TRP A 566     -15.879  28.812 -22.693  1.00 34.23           C  
ANISOU 4467  CH2 TRP A 566     3882   4919   4206   -363    164   -850       C  
ATOM   4468  N   THR A 567     -15.454  30.099 -17.786  1.00 37.59           N  
ANISOU 4468  N   THR A 567     4336   5382   4565   -409    191   -925       N  
ATOM   4469  CA  THR A 567     -14.061  30.288 -18.173  1.00 37.41           C  
ANISOU 4469  CA  THR A 567     4280   5421   4515   -463    186   -965       C  
ATOM   4470  C   THR A 567     -13.132  30.059 -16.989  1.00 45.31           C  
ANISOU 4470  C   THR A 567     5245   6492   5478   -481    166  -1003       C  
ATOM   4471  O   THR A 567     -12.091  29.405 -17.123  1.00 43.36           O  
ANISOU 4471  O   THR A 567     4938   6320   5216   -484    138  -1024       O  
ATOM   4472  CB  THR A 567     -13.859  31.690 -18.750  1.00 36.47           C  
ANISOU 4472  CB  THR A 567     4210   5263   4387   -530    228   -983       C  
ATOM   4473  OG1 THR A 567     -14.450  32.659 -17.876  1.00 46.30           O  
ANISOU 4473  OG1 THR A 567     5513   6454   5625   -546    259   -987       O  
ATOM   4474  CG2 THR A 567     -14.504  31.795 -20.123  1.00 36.76           C  
ANISOU 4474  CG2 THR A 567     4272   5245   4452   -512    239   -948       C  
ATOM   4475  N   LEU A 568     -13.496  30.586 -15.817  1.00 44.41           N  
ANISOU 4475  N   LEU A 568     5168   6358   5348   -491    179  -1012       N  
ATOM   4476  CA  LEU A 568     -12.687  30.349 -14.628  1.00 43.66           C  
ANISOU 4476  CA  LEU A 568     5045   6330   5213   -505    154  -1045       C  
ATOM   4477  C   LEU A 568     -12.860  28.916 -14.138  1.00 37.50           C  
ANISOU 4477  C   LEU A 568     4228   5584   4437   -432    112  -1021       C  
ATOM   4478  O   LEU A 568     -11.881  28.266 -13.757  1.00 45.03           O  
ANISOU 4478  O   LEU A 568     5129   6615   5364   -426     75  -1042       O  
ATOM   4479  CB  LEU A 568     -13.043  31.367 -13.539  1.00 52.21           C  
ANISOU 4479  CB  LEU A 568     6188   7376   6273   -540    184  -1063       C  
ATOM   4480  CG  LEU A 568     -12.680  31.187 -12.062  1.00 43.68           C  
ANISOU 4480  CG  LEU A 568     5105   6340   5150   -544    163  -1088       C  
ATOM   4481  CD1 LEU A 568     -11.249  30.758 -11.902  1.00 50.90           C  
ANISOU 4481  CD1 LEU A 568     5951   7358   6031   -569    120  -1126       C  
ATOM   4482  CD2 LEU A 568     -12.849  32.504 -11.364  1.00 55.01           C  
ANISOU 4482  CD2 LEU A 568     6606   7734   6561   -603    204  -1116       C  
ATOM   4483  N   ALA A 569     -14.091  28.395 -14.179  1.00 38.46           N  
ANISOU 4483  N   ALA A 569     4374   5647   4590   -375    118   -976       N  
ATOM   4484  CA  ALA A 569     -14.325  27.016 -13.758  1.00 43.37           C  
ANISOU 4484  CA  ALA A 569     4972   6292   5216   -308     84   -950       C  
ATOM   4485  C   ALA A 569     -13.495  26.042 -14.585  1.00 44.11           C  
ANISOU 4485  C   ALA A 569     5005   6442   5314   -285     49   -951       C  
ATOM   4486  O   ALA A 569     -12.908  25.099 -14.044  1.00 40.69           O  
ANISOU 4486  O   ALA A 569     4537   6064   4860   -252     13   -955       O  
ATOM   4487  CB  ALA A 569     -15.812  26.679 -13.860  1.00 37.04           C  
ANISOU 4487  CB  ALA A 569     4204   5417   4454   -261    102   -904       C  
ATOM   4488  N   LEU A 570     -13.423  26.266 -15.899  1.00 34.82           N  
ANISOU 4488  N   LEU A 570     3818   5250   4160   -302     62   -948       N  
ATOM   4489  CA  LEU A 570     -12.540  25.466 -16.741  1.00 30.38           C  
ANISOU 4489  CA  LEU A 570     3200   4742   3600   -287     37   -955       C  
ATOM   4490  C   LEU A 570     -11.084  25.627 -16.318  1.00 36.08           C  
ANISOU 4490  C   LEU A 570     3873   5552   4285   -322     18  -1003       C  
ATOM   4491  O   LEU A 570     -10.317  24.657 -16.318  1.00 38.06           O  
ANISOU 4491  O   LEU A 570     4071   5864   4527   -287    -16  -1010       O  
ATOM   4492  CB  LEU A 570     -12.722  25.865 -18.206  1.00 31.56           C  
ANISOU 4492  CB  LEU A 570     3358   4857   3776   -309     60   -946       C  
ATOM   4493  CG  LEU A 570     -12.102  24.979 -19.285  1.00 23.10           C  
ANISOU 4493  CG  LEU A 570     2242   3823   2714   -288     42   -946       C  
ATOM   4494  CD1 LEU A 570     -12.779  23.624 -19.324  1.00 22.29           C  
ANISOU 4494  CD1 LEU A 570     2135   3704   2632   -215     18   -909       C  
ATOM   4495  CD2 LEU A 570     -12.199  25.661 -20.638  1.00 29.85           C  
ANISOU 4495  CD2 LEU A 570     3116   4643   3583   -326     71   -944       C  
ATOM   4496  N   GLU A 571     -10.690  26.849 -15.948  1.00 49.95           N  
ANISOU 4496  N   GLU A 571     5646   7313   6019   -391     40  -1037       N  
ATOM   4497  CA  GLU A 571      -9.313  27.101 -15.535  1.00 53.50           C  
ANISOU 4497  CA  GLU A 571     6045   7850   6433   -435     22  -1088       C  
ATOM   4498  C   GLU A 571      -8.958  26.353 -14.256  1.00 54.73           C  
ANISOU 4498  C   GLU A 571     6175   8061   6558   -395    -22  -1093       C  
ATOM   4499  O   GLU A 571      -7.802  25.955 -14.074  1.00 60.63           O  
ANISOU 4499  O   GLU A 571     6858   8896   7283   -395    -55  -1124       O  
ATOM   4500  CB  GLU A 571      -9.091  28.603 -15.353  1.00 54.06           C  
ANISOU 4500  CB  GLU A 571     6150   7904   6485   -524     59  -1123       C  
ATOM   4501  CG  GLU A 571      -7.649  29.049 -15.514  1.00 57.38           C  
ANISOU 4501  CG  GLU A 571     6514   8408   6879   -591     55  -1179       C  
ATOM   4502  CD  GLU A 571      -7.483  30.544 -15.325  1.00 66.27           C  
ANISOU 4502  CD  GLU A 571     7685   9509   7985   -684     96  -1214       C  
ATOM   4503  OE1 GLU A 571      -8.004  31.077 -14.323  1.00 67.12           O  
ANISOU 4503  OE1 GLU A 571     7845   9582   8074   -696    105  -1216       O  
ATOM   4504  OE2 GLU A 571      -6.834  31.185 -16.177  1.00 74.70           O1-
ANISOU 4504  OE2 GLU A 571     8741  10589   9053   -748    124  -1242       O1-
ATOM   4505  N   ASN A 572      -9.929  26.152 -13.361  1.00 41.97           N  
ANISOU 4505  N   ASN A 572     4609   6398   4939   -360    -22  -1065       N  
ATOM   4506  CA  ASN A 572      -9.678  25.417 -12.126  1.00 44.78           C  
ANISOU 4506  CA  ASN A 572     4955   6799   5261   -319    -62  -1065       C  
ATOM   4507  C   ASN A 572      -9.323  23.960 -12.369  1.00 50.37           C  
ANISOU 4507  C   ASN A 572     5615   7547   5976   -243   -103  -1045       C  
ATOM   4508  O   ASN A 572      -8.817  23.303 -11.453  1.00 51.56           O  
ANISOU 4508  O   ASN A 572     5746   7752   6093   -207   -144  -1049       O  
ATOM   4509  CB  ASN A 572     -10.895  25.501 -11.206  1.00 47.24           C  
ANISOU 4509  CB  ASN A 572     5337   7041   5571   -298    -44  -1036       C  
ATOM   4510  CG  ASN A 572     -11.147  26.901 -10.722  1.00 47.86           C  
ANISOU 4510  CG  ASN A 572     5465   7085   5634   -367     -7  -1061       C  
ATOM   4511  OD1 ASN A 572     -10.704  27.859 -11.345  1.00 43.80           O  
ANISOU 4511  OD1 ASN A 572     4946   6572   5123   -430     17  -1089       O  
ATOM   4512  ND2 ASN A 572     -11.860  27.034  -9.611  1.00 54.66           N  
ANISOU 4512  ND2 ASN A 572     6380   7912   6477   -357      4  -1051       N  
ATOM   4513  N   VAL A 573      -9.568  23.444 -13.567  1.00 53.30           N  
ANISOU 4513  N   VAL A 573     5973   7893   6386   -217    -94  -1022       N  
ATOM   4514  CA  VAL A 573      -9.207  22.083 -13.934  1.00 55.05           C  
ANISOU 4514  CA  VAL A 573     6154   8148   6616   -148   -126  -1006       C  
ATOM   4515  C   VAL A 573      -8.009  22.065 -14.874  1.00 58.36           C  
ANISOU 4515  C   VAL A 573     6503   8633   7038   -166   -133  -1038       C  
ATOM   4516  O   VAL A 573      -6.998  21.421 -14.593  1.00 63.33           O  
ANISOU 4516  O   VAL A 573     7074   9340   7647   -135   -170  -1057       O  
ATOM   4517  CB  VAL A 573     -10.409  21.341 -14.562  1.00 51.76           C  
ANISOU 4517  CB  VAL A 573     5776   7652   6238   -100   -110   -956       C  
ATOM   4518  CG1 VAL A 573     -10.409  19.878 -14.147  1.00 53.43           C  
ANISOU 4518  CG1 VAL A 573     5982   7876   6442    -20   -145   -930       C  
ATOM   4519  CG2 VAL A 573     -11.710  22.016 -14.183  1.00 43.83           C  
ANISOU 4519  CG2 VAL A 573     4839   6568   5247   -120    -77   -934       C  
ATOM   4520  N   VAL A 574      -8.101  22.790 -15.990  1.00 44.52           N  
ANISOU 4520  N   VAL A 574     4754   6851   5309   -216    -96  -1046       N  
ATOM   4521  CA  VAL A 574      -7.143  22.644 -17.082  1.00 45.27           C  
ANISOU 4521  CA  VAL A 574     4791   6996   5414   -229    -93  -1070       C  
ATOM   4522  C   VAL A 574      -6.109  23.761 -17.137  1.00 51.45           C  
ANISOU 4522  C   VAL A 574     5537   7836   6177   -313    -78  -1124       C  
ATOM   4523  O   VAL A 574      -5.139  23.648 -17.904  1.00 51.22           O  
ANISOU 4523  O   VAL A 574     5447   7863   6150   -328    -76  -1152       O  
ATOM   4524  CB  VAL A 574      -7.874  22.549 -18.439  1.00 39.92           C  
ANISOU 4524  CB  VAL A 574     4144   6251   4773   -226    -62  -1042       C  
ATOM   4525  CG1 VAL A 574      -9.085  21.640 -18.317  1.00 37.52           C  
ANISOU 4525  CG1 VAL A 574     3885   5881   4490   -160    -70   -991       C  
ATOM   4526  CG2 VAL A 574      -8.292  23.928 -18.917  1.00 44.01           C  
ANISOU 4526  CG2 VAL A 574     4706   6718   5298   -302    -18  -1049       C  
ATOM   4527  N   GLY A 575      -6.274  24.827 -16.359  1.00 59.02           N  
ANISOU 4527  N   GLY A 575     6530   8781   7114   -370    -66  -1141       N  
ATOM   4528  CA  GLY A 575      -5.345  25.936 -16.417  1.00 55.37           C  
ANISOU 4528  CA  GLY A 575     6040   8365   6632   -460    -47  -1193       C  
ATOM   4529  C   GLY A 575      -5.508  26.842 -17.615  1.00 56.67           C  
ANISOU 4529  C   GLY A 575     6234   8480   6816   -523      6  -1198       C  
ATOM   4530  O   GLY A 575      -4.638  27.687 -17.857  1.00 66.68           O  
ANISOU 4530  O   GLY A 575     7477   9789   8068   -602     27  -1243       O  
ATOM   4531  N   ALA A 576      -6.590  26.691 -18.375  1.00 45.49           N  
ANISOU 4531  N   ALA A 576     4874   6980   5431   -494     27  -1153       N  
ATOM   4532  CA  ALA A 576      -6.874  27.525 -19.533  1.00 51.10           C  
ANISOU 4532  CA  ALA A 576     5624   7634   6156   -545     74  -1150       C  
ATOM   4533  C   ALA A 576      -8.287  28.076 -19.414  1.00 52.84           C  
ANISOU 4533  C   ALA A 576     5932   7751   6392   -537     96  -1110       C  
ATOM   4534  O   ALA A 576      -9.201  27.373 -18.973  1.00 40.37           O  
ANISOU 4534  O   ALA A 576     4372   6137   4827   -471     77  -1072       O  
ATOM   4535  CB  ALA A 576      -6.722  26.742 -20.842  1.00 40.17           C  
ANISOU 4535  CB  ALA A 576     4213   6254   4794   -513     76  -1135       C  
ATOM   4536  N   LYS A 577      -8.458  29.339 -19.805  1.00 64.89           N  
ANISOU 4536  N   LYS A 577     7511   9229   7916   -604    139  -1120       N  
ATOM   4537  CA  LYS A 577      -9.746  30.005 -19.659  1.00 59.88           C  
ANISOU 4537  CA  LYS A 577     6957   8498   7294   -598    163  -1086       C  
ATOM   4538  C   LYS A 577     -10.743  29.631 -20.748  1.00 58.29           C  
ANISOU 4538  C   LYS A 577     6788   8232   7128   -552    169  -1037       C  
ATOM   4539  O   LYS A 577     -11.951  29.760 -20.529  1.00 58.88           O  
ANISOU 4539  O   LYS A 577     6911   8238   7222   -517    174  -1001       O  
ATOM   4540  CB  LYS A 577      -9.552  31.524 -19.649  1.00 59.86           C  
ANISOU 4540  CB  LYS A 577     7008   8463   7274   -683    208  -1114       C  
ATOM   4541  CG  LYS A 577      -8.595  32.021 -18.577  1.00 68.78           C  
ANISOU 4541  CG  LYS A 577     8113   9654   8366   -742    205  -1167       C  
ATOM   4542  CD  LYS A 577      -8.132  33.441 -18.863  1.00 69.99           C  
ANISOU 4542  CD  LYS A 577     8309   9784   8499   -840    254  -1203       C  
ATOM   4543  CE  LYS A 577      -7.906  34.220 -17.577  1.00 73.20           C  
ANISOU 4543  CE  LYS A 577     8739  10200   8873   -891    260  -1240       C  
ATOM   4544  NZ  LYS A 577      -6.462  34.347 -17.237  1.00 83.04           N  
ANISOU 4544  NZ  LYS A 577     9918  11547  10086   -960    248  -1302       N  
ATOM   4545  N   ASN A 578     -10.279  29.167 -21.905  1.00 55.27           N  
ANISOU 4545  N   ASN A 578     6376   7872   6753   -550    168  -1037       N  
ATOM   4546  CA  ASN A 578     -11.146  28.961 -23.054  1.00 53.78           C  
ANISOU 4546  CA  ASN A 578     6222   7622   6589   -520    174   -995       C  
ATOM   4547  C   ASN A 578     -11.201  27.487 -23.436  1.00 51.57           C  
ANISOU 4547  C   ASN A 578     5896   7371   6325   -453    139   -975       C  
ATOM   4548  O   ASN A 578     -10.315  26.697 -23.099  1.00 51.72           O  
ANISOU 4548  O   ASN A 578     5855   7463   6335   -437    117   -998       O  
ATOM   4549  CB  ASN A 578     -10.677  29.792 -24.256  1.00 61.95           C  
ANISOU 4549  CB  ASN A 578     7283   8642   7614   -581    210  -1009       C  
ATOM   4550  CG  ASN A 578     -11.755  29.953 -25.310  1.00 66.49           C  
ANISOU 4550  CG  ASN A 578     7916   9138   8208   -558    220   -963       C  
ATOM   4551  OD1 ASN A 578     -12.874  29.461 -25.152  1.00 61.77           O  
ANISOU 4551  OD1 ASN A 578     7334   8500   7635   -498    199   -924       O  
ATOM   4552  ND2 ASN A 578     -11.424  30.642 -26.394  1.00 65.95           N  
ANISOU 4552  ND2 ASN A 578     7882   9050   8128   -607    250   -969       N  
ATOM   4553  N   MET A 579     -12.269  27.132 -24.147  1.00 50.24           N  
ANISOU 4553  N   MET A 579     5762   7146   6183   -412    135   -933       N  
ATOM   4554  CA  MET A 579     -12.438  25.777 -24.654  1.00 51.24           C  
ANISOU 4554  CA  MET A 579     5858   7286   6325   -355    107   -912       C  
ATOM   4555  C   MET A 579     -11.356  25.475 -25.684  1.00 57.82           C  
ANISOU 4555  C   MET A 579     6656   8166   7145   -377    114   -937       C  
ATOM   4556  O   MET A 579     -11.201  26.209 -26.665  1.00 58.53           O  
ANISOU 4556  O   MET A 579     6776   8236   7228   -422    142   -942       O  
ATOM   4557  CB  MET A 579     -13.827  25.619 -25.267  1.00 56.79           C  
ANISOU 4557  CB  MET A 579     6606   7916   7055   -320    103   -865       C  
ATOM   4558  CG  MET A 579     -13.999  24.376 -26.123  1.00 52.96           C  
ANISOU 4558  CG  MET A 579     6102   7436   6582   -277     81   -847       C  
ATOM   4559  SD  MET A 579     -15.558  24.363 -27.034  1.00 58.70           S  
ANISOU 4559  SD  MET A 579     6881   8085   7337   -251     74   -797       S  
ATOM   4560  CE  MET A 579     -15.734  26.099 -27.440  1.00 52.46           C  
ANISOU 4560  CE  MET A 579     6147   7249   6538   -306    108   -797       C  
ATOM   4561  N   ASN A 580     -10.614  24.393 -25.465  1.00 53.20           N  
ANISOU 4561  N   ASN A 580     6013   7645   6557   -342     91   -953       N  
ATOM   4562  CA  ASN A 580      -9.517  24.005 -26.336  1.00 51.65           C  
ANISOU 4562  CA  ASN A 580     5774   7502   6351   -356     99   -980       C  
ATOM   4563  C   ASN A 580      -9.782  22.627 -26.923  1.00 49.03           C  
ANISOU 4563  C   ASN A 580     5430   7166   6033   -291     78   -958       C  
ATOM   4564  O   ASN A 580     -10.376  21.759 -26.277  1.00 55.23           O  
ANISOU 4564  O   ASN A 580     6215   7941   6831   -233     50   -935       O  
ATOM   4565  CB  ASN A 580      -8.180  24.002 -25.584  1.00 51.68           C  
ANISOU 4565  CB  ASN A 580     5708   7592   6334   -374     94  -1028       C  
ATOM   4566  CG  ASN A 580      -6.987  23.945 -26.518  1.00 55.70           C  
ANISOU 4566  CG  ASN A 580     6173   8159   6833   -406    116  -1064       C  
ATOM   4567  OD1 ASN A 580      -7.119  24.140 -27.727  1.00 59.79           O  
ANISOU 4567  OD1 ASN A 580     6721   8646   7352   -428    142  -1057       O  
ATOM   4568  ND2 ASN A 580      -5.811  23.680 -25.961  1.00 67.27           N  
ANISOU 4568  ND2 ASN A 580     7563   9711   8286   -407    104  -1104       N  
ATOM   4569  N   VAL A 581      -9.328  22.434 -28.163  1.00 37.16           N  
ANISOU 4569  N   VAL A 581     3922   5672   4525   -305     95   -968       N  
ATOM   4570  CA  VAL A 581      -9.532  21.177 -28.874  1.00 30.28           C  
ANISOU 4570  CA  VAL A 581     3047   4794   3665   -252     81   -951       C  
ATOM   4571  C   VAL A 581      -8.307  20.275 -28.833  1.00 36.06           C  
ANISOU 4571  C   VAL A 581     3711   5602   4389   -223     76   -984       C  
ATOM   4572  O   VAL A 581      -8.416  19.084 -29.171  1.00 35.10           O  
ANISOU 4572  O   VAL A 581     3584   5477   4276   -167     61   -972       O  
ATOM   4573  CB  VAL A 581      -9.943  21.439 -30.339  1.00 28.42           C  
ANISOU 4573  CB  VAL A 581     2859   4513   3427   -278    102   -937       C  
ATOM   4574  CG1 VAL A 581      -8.724  21.795 -31.180  1.00 31.91           C  
ANISOU 4574  CG1 VAL A 581     3275   5001   3848   -326    137   -976       C  
ATOM   4575  CG2 VAL A 581     -10.671  20.243 -30.911  1.00 22.42           C  
ANISOU 4575  CG2 VAL A 581     2117   3721   2681   -224     81   -908       C  
ATOM   4576  N   ARG A 582      -7.150  20.797 -28.423  1.00 41.30           N  
ANISOU 4576  N   ARG A 582     4322   6334   5038   -258     87  -1026       N  
ATOM   4577  CA  ARG A 582      -5.922  20.003 -28.420  1.00 37.16           C  
ANISOU 4577  CA  ARG A 582     3723   5889   4508   -229     83  -1060       C  
ATOM   4578  C   ARG A 582      -6.027  18.718 -27.607  1.00 39.87           C  
ANISOU 4578  C   ARG A 582     4044   6246   4859   -142     42  -1044       C  
ATOM   4579  O   ARG A 582      -5.566  17.671 -28.095  1.00 46.33           O  
ANISOU 4579  O   ARG A 582     4835   7088   5681    -93     39  -1050       O  
ATOM   4580  CB  ARG A 582      -4.758  20.874 -27.937  1.00 38.94           C  
ANISOU 4580  CB  ARG A 582     3891   6188   4717   -286     97  -1108       C  
ATOM   4581  CG  ARG A 582      -3.397  20.415 -28.428  1.00 50.21           C  
ANISOU 4581  CG  ARG A 582     5240   7698   6138   -282    111  -1151       C  
ATOM   4582  CD  ARG A 582      -2.294  20.770 -27.435  1.00 56.82           C  
ANISOU 4582  CD  ARG A 582     5998   8627   6963   -302     98  -1195       C  
ATOM   4583  NE  ARG A 582      -2.804  21.019 -26.091  1.00 56.81           N  
ANISOU 4583  NE  ARG A 582     6013   8615   6957   -291     63  -1180       N  
ATOM   4584  CZ  ARG A 582      -3.096  20.074 -25.207  1.00 52.63           C  
ANISOU 4584  CZ  ARG A 582     5477   8088   6431   -212     19  -1157       C  
ATOM   4585  NH1 ARG A 582      -2.953  18.790 -25.493  1.00 48.36           N  
ANISOU 4585  NH1 ARG A 582     4916   7559   5901   -133      2  -1146       N  
ATOM   4586  NH2 ARG A 582      -3.553  20.425 -24.008  1.00 44.41           N  
ANISOU 4586  NH2 ARG A 582     4457   7036   5381   -212     -7  -1146       N  
ATOM   4587  N   PRO A 583      -6.575  18.708 -26.383  1.00 37.76           N  
ANISOU 4587  N   PRO A 583     3789   5965   4592   -118     13  -1025       N  
ATOM   4588  CA  PRO A 583      -6.687  17.428 -25.662  1.00 39.32           C  
ANISOU 4588  CA  PRO A 583     3976   6170   4794    -35    -22  -1008       C  
ATOM   4589  C   PRO A 583      -7.518  16.390 -26.395  1.00 43.47           C  
ANISOU 4589  C   PRO A 583     4546   6635   5336     12    -24   -973       C  
ATOM   4590  O   PRO A 583      -7.230  15.191 -26.286  1.00 46.35           O  
ANISOU 4590  O   PRO A 583     4894   7014   5701     79    -41   -970       O  
ATOM   4591  CB  PRO A 583      -7.335  17.831 -24.330  1.00 28.84           C  
ANISOU 4591  CB  PRO A 583     2673   4823   3462    -35    -44   -990       C  
ATOM   4592  CG  PRO A 583      -7.025  19.269 -24.173  1.00 32.32           C  
ANISOU 4592  CG  PRO A 583     3108   5281   3891   -115    -23  -1016       C  
ATOM   4593  CD  PRO A 583      -7.041  19.836 -25.553  1.00 40.18           C  
ANISOU 4593  CD  PRO A 583     4122   6251   4893   -165     14  -1022       C  
ATOM   4594  N   LEU A 584      -8.545  16.813 -27.134  1.00 43.05           N  
ANISOU 4594  N   LEU A 584     4551   6514   5294    -21     -8   -949       N  
ATOM   4595  CA  LEU A 584      -9.326  15.871 -27.930  1.00 37.41           C  
ANISOU 4595  CA  LEU A 584     3876   5744   4592     14    -10   -921       C  
ATOM   4596  C   LEU A 584      -8.471  15.221 -29.011  1.00 45.01           C  
ANISOU 4596  C   LEU A 584     4815   6737   5550     28      6   -944       C  
ATOM   4597  O   LEU A 584      -8.553  14.007 -29.233  1.00 44.47           O  
ANISOU 4597  O   LEU A 584     4756   6656   5487     84     -3   -934       O  
ATOM   4598  CB  LEU A 584     -10.526  16.589 -28.545  1.00 42.88           C  
ANISOU 4598  CB  LEU A 584     4628   6368   5296    -28      0   -893       C  
ATOM   4599  CG  LEU A 584     -11.237  15.931 -29.728  1.00 40.47           C  
ANISOU 4599  CG  LEU A 584     4364   6012   4999    -18      3   -872       C  
ATOM   4600  CD1 LEU A 584     -11.910  14.638 -29.312  1.00 35.28           C  
ANISOU 4600  CD1 LEU A 584     3725   5325   4355     42    -21   -847       C  
ATOM   4601  CD2 LEU A 584     -12.249  16.894 -30.319  1.00 42.14           C  
ANISOU 4601  CD2 LEU A 584     4624   6169   5217    -64     10   -850       C  
ATOM   4602  N   LEU A 585      -7.641  16.013 -29.693  1.00 34.75           N  
ANISOU 4602  N   LEU A 585     3489   5475   4240    -24     35   -976       N  
ATOM   4603  CA  LEU A 585      -6.732  15.452 -30.686  1.00 33.81           C  
ANISOU 4603  CA  LEU A 585     3342   5391   4114    -14     57  -1003       C  
ATOM   4604  C   LEU A 585      -5.631  14.627 -30.032  1.00 43.34           C  
ANISOU 4604  C   LEU A 585     4480   6670   5320     46     43  -1029       C  
ATOM   4605  O   LEU A 585      -5.135  13.669 -30.634  1.00 50.45           O  
ANISOU 4605  O   LEU A 585     5365   7584   6221     90     52  -1040       O  
ATOM   4606  CB  LEU A 585      -6.135  16.570 -31.540  1.00 37.16           C  
ANISOU 4606  CB  LEU A 585     3757   5837   4526    -91     97  -1032       C  
ATOM   4607  CG  LEU A 585      -7.164  17.507 -32.177  1.00 33.81           C  
ANISOU 4607  CG  LEU A 585     3404   5342   4100   -148    109  -1005       C  
ATOM   4608  CD1 LEU A 585      -6.480  18.647 -32.915  1.00 37.16           C  
ANISOU 4608  CD1 LEU A 585     3825   5788   4506   -225    151  -1034       C  
ATOM   4609  CD2 LEU A 585      -8.087  16.736 -33.108  1.00 32.37           C  
ANISOU 4609  CD2 LEU A 585     3280   5098   3923   -122    103   -975       C  
ATOM   4610  N   ASN A 586      -5.234  14.989 -28.809  1.00 42.35           N  
ANISOU 4610  N   ASN A 586     4313   6589   5189     49     21  -1039       N  
ATOM   4611  CA  ASN A 586      -4.299  14.161 -28.054  1.00 42.36           C  
ANISOU 4611  CA  ASN A 586     4251   6656   5186    116     -2  -1056       C  
ATOM   4612  C   ASN A 586      -4.904  12.795 -27.757  1.00 41.36           C  
ANISOU 4612  C   ASN A 586     4162   6485   5066    201    -28  -1022       C  
ATOM   4613  O   ASN A 586      -4.211  11.771 -27.816  1.00 51.31           O  
ANISOU 4613  O   ASN A 586     5391   7777   6326    268    -34  -1033       O  
ATOM   4614  CB  ASN A 586      -3.907  14.875 -26.759  1.00 41.02           C  
ANISOU 4614  CB  ASN A 586     4042   6539   5006     98    -27  -1070       C  
ATOM   4615  CG  ASN A 586      -2.920  14.082 -25.922  1.00 43.11           C  
ANISOU 4615  CG  ASN A 586     4239   6878   5262    170    -59  -1088       C  
ATOM   4616  OD1 ASN A 586      -2.242  13.183 -26.419  1.00 46.61           O  
ANISOU 4616  OD1 ASN A 586     4648   7352   5710    224    -54  -1101       O  
ATOM   4617  ND2 ASN A 586      -2.836  14.415 -24.639  1.00 43.75           N  
ANISOU 4617  ND2 ASN A 586     4304   6990   5330    172    -92  -1088       N  
ATOM   4618  N   TYR A 587      -6.199  12.762 -27.437  1.00 37.63           N  
ANISOU 4618  N   TYR A 587     3757   5938   4601    198    -40   -982       N  
ATOM   4619  CA  TYR A 587      -6.869  11.500 -27.138  1.00 41.48           C  
ANISOU 4619  CA  TYR A 587     4289   6377   5095    268    -60   -949       C  
ATOM   4620  C   TYR A 587      -6.875  10.571 -28.346  1.00 42.75           C  
ANISOU 4620  C   TYR A 587     4473   6508   5262    294    -40   -950       C  
ATOM   4621  O   TYR A 587      -6.639   9.364 -28.211  1.00 45.75           O  
ANISOU 4621  O   TYR A 587     4857   6884   5640    366    -50   -945       O  
ATOM   4622  CB  TYR A 587      -8.296  11.779 -26.665  1.00 33.60           C  
ANISOU 4622  CB  TYR A 587     3354   5307   4106    246    -70   -910       C  
ATOM   4623  CG  TYR A 587      -9.053  10.563 -26.184  1.00 32.58           C  
ANISOU 4623  CG  TYR A 587     3272   5126   3981    307    -88   -876       C  
ATOM   4624  CD1 TYR A 587      -9.020  10.184 -24.849  1.00 33.04           C  
ANISOU 4624  CD1 TYR A 587     3328   5195   4028    351   -114   -864       C  
ATOM   4625  CD2 TYR A 587      -9.817   9.803 -27.062  1.00 35.50           C  
ANISOU 4625  CD2 TYR A 587     3692   5433   4362    315    -77   -857       C  
ATOM   4626  CE1 TYR A 587      -9.720   9.080 -24.403  1.00 34.39           C  
ANISOU 4626  CE1 TYR A 587     3550   5314   4201    402   -126   -832       C  
ATOM   4627  CE2 TYR A 587     -10.516   8.695 -26.625  1.00 32.52           C  
ANISOU 4627  CE2 TYR A 587     3361   5005   3988    363    -89   -829       C  
ATOM   4628  CZ  TYR A 587     -10.464   8.338 -25.295  1.00 33.92           C  
ANISOU 4628  CZ  TYR A 587     3540   5193   4157    406   -111   -816       C  
ATOM   4629  OH  TYR A 587     -11.159   7.236 -24.853  1.00 40.22           O  
ANISOU 4629  OH  TYR A 587     4391   5936   4955    450   -119   -786       O  
ATOM   4630  N   PHE A 588      -7.142  11.111 -29.534  1.00 40.41           N  
ANISOU 4630  N   PHE A 588     4198   6188   4969    237    -12   -955       N  
ATOM   4631  CA  PHE A 588      -7.291  10.316 -30.745  1.00 40.68           C  
ANISOU 4631  CA  PHE A 588     4266   6187   5004    251      8   -955       C  
ATOM   4632  C   PHE A 588      -6.037  10.310 -31.609  1.00 49.44           C  
ANISOU 4632  C   PHE A 588     5326   7353   6105    249     39   -997       C  
ATOM   4633  O   PHE A 588      -6.089   9.853 -32.755  1.00 50.90           O  
ANISOU 4633  O   PHE A 588     5542   7512   6287    247     63  -1002       O  
ATOM   4634  CB  PHE A 588      -8.482  10.823 -31.557  1.00 39.74           C  
ANISOU 4634  CB  PHE A 588     4210   5999   4889    194     16   -931       C  
ATOM   4635  CG  PHE A 588      -9.809  10.499 -30.941  1.00 36.68           C  
ANISOU 4635  CG  PHE A 588     3874   5549   4515    206     -9   -891       C  
ATOM   4636  CD1 PHE A 588     -10.328   9.219 -31.021  1.00 36.49           C  
ANISOU 4636  CD1 PHE A 588     3889   5479   4495    253    -18   -873       C  
ATOM   4637  CD2 PHE A 588     -10.532  11.469 -30.269  1.00 39.74           C  
ANISOU 4637  CD2 PHE A 588     4269   5920   4909    168    -21   -872       C  
ATOM   4638  CE1 PHE A 588     -11.544   8.915 -30.450  1.00 35.51           C  
ANISOU 4638  CE1 PHE A 588     3809   5300   4383    258    -37   -838       C  
ATOM   4639  CE2 PHE A 588     -11.751  11.169 -29.695  1.00 35.24           C  
ANISOU 4639  CE2 PHE A 588     3740   5296   4352    178    -40   -837       C  
ATOM   4640  CZ  PHE A 588     -12.258   9.891 -29.786  1.00 35.33           C  
ANISOU 4640  CZ  PHE A 588     3788   5267   4369    221    -47   -820       C  
ATOM   4641  N   GLU A 589      -4.918  10.811 -31.087  1.00 49.10           N  
ANISOU 4641  N   GLU A 589     5209   7391   6058    246     40  -1029       N  
ATOM   4642  CA  GLU A 589      -3.681  10.853 -31.865  1.00 48.90           C  
ANISOU 4642  CA  GLU A 589     5126   7428   6027    240     74  -1073       C  
ATOM   4643  C   GLU A 589      -3.224   9.483 -32.352  1.00 48.62           C  
ANISOU 4643  C   GLU A 589     5088   7392   5992    318     84  -1081       C  
ATOM   4644  O   GLU A 589      -2.850   9.371 -33.533  1.00 53.58           O  
ANISOU 4644  O   GLU A 589     5720   8022   6616    301    123  -1103       O  
ATOM   4645  CB  GLU A 589      -2.587  11.545 -31.048  1.00 54.18           C  
ANISOU 4645  CB  GLU A 589     5706   8189   6691    228     67  -1106       C  
ATOM   4646  CG  GLU A 589      -1.473  12.116 -31.895  1.00 58.33           C  
ANISOU 4646  CG  GLU A 589     6174   8779   7212    182    111  -1154       C  
ATOM   4647  CD  GLU A 589      -0.229  12.430 -31.093  1.00 68.21           C  
ANISOU 4647  CD  GLU A 589     7322  10133   8461    189    101  -1193       C  
ATOM   4648  OE1 GLU A 589      -0.366  12.920 -29.951  1.00 59.63           O  
ANISOU 4648  OE1 GLU A 589     6221   9064   7371    180     66  -1185       O  
ATOM   4649  OE2 GLU A 589       0.884  12.199 -31.610  1.00 66.70           O1-
ANISOU 4649  OE2 GLU A 589     7064  10008   8272    202    128  -1234       O1-
ATOM   4650  N   PRO A 590      -3.201   8.423 -31.532  1.00 44.09           N  
ANISOU 4650  N   PRO A 590     4515   6816   5423    404     54  -1066       N  
ATOM   4651  CA  PRO A 590      -2.837   7.106 -32.079  1.00 49.69           C  
ANISOU 4651  CA  PRO A 590     5235   7512   6133    479     68  -1073       C  
ATOM   4652  C   PRO A 590      -3.737   6.663 -33.216  1.00 48.61           C  
ANISOU 4652  C   PRO A 590     5183   7291   5994    458     91  -1057       C  
ATOM   4653  O   PRO A 590      -3.267   5.996 -34.146  1.00 49.53           O  
ANISOU 4653  O   PRO A 590     5306   7407   6108    483    123  -1078       O  
ATOM   4654  CB  PRO A 590      -2.957   6.175 -30.865  1.00 42.25           C  
ANISOU 4654  CB  PRO A 590     4301   6561   5192    566     27  -1048       C  
ATOM   4655  CG  PRO A 590      -2.770   7.063 -29.693  1.00 41.02           C  
ANISOU 4655  CG  PRO A 590     4097   6456   5033    544     -5  -1047       C  
ATOM   4656  CD  PRO A 590      -3.404   8.363 -30.072  1.00 41.86           C  
ANISOU 4656  CD  PRO A 590     4222   6543   5140    440      9  -1045       C  
ATOM   4657  N   LEU A 591      -5.025   7.011 -33.169  1.00 48.54           N  
ANISOU 4657  N   LEU A 591     5240   7216   5988    411     75  -1022       N  
ATOM   4658  CA  LEU A 591      -5.905   6.719 -34.294  1.00 44.84           C  
ANISOU 4658  CA  LEU A 591     4847   6675   5514    380     92  -1009       C  
ATOM   4659  C   LEU A 591      -5.620   7.640 -35.473  1.00 45.20           C  
ANISOU 4659  C   LEU A 591     4887   6737   5549    306    128  -1032       C  
ATOM   4660  O   LEU A 591      -5.649   7.203 -36.630  1.00 50.47           O  
ANISOU 4660  O   LEU A 591     5593   7377   6206    298    156  -1043       O  
ATOM   4661  CB  LEU A 591      -7.365   6.838 -33.864  1.00 35.83           C  
ANISOU 4661  CB  LEU A 591     3768   5464   4381    354     63   -965       C  
ATOM   4662  CG  LEU A 591      -8.386   6.513 -34.954  1.00 35.48           C  
ANISOU 4662  CG  LEU A 591     3800   5348   4332    321     71   -950       C  
ATOM   4663  CD1 LEU A 591      -8.496   5.010 -35.160  1.00 38.81           C  
ANISOU 4663  CD1 LEU A 591     4266   5727   4752    383     75   -947       C  
ATOM   4664  CD2 LEU A 591      -9.732   7.109 -34.611  1.00 28.62           C  
ANISOU 4664  CD2 LEU A 591     2970   4432   3474    275     45   -914       C  
ATOM   4665  N   PHE A 592      -5.341   8.918 -35.200  1.00 39.89           N  
ANISOU 4665  N   PHE A 592     4173   6107   4876    249    130  -1042       N  
ATOM   4666  CA  PHE A 592      -5.098   9.876 -36.275  1.00 34.69           C  
ANISOU 4666  CA  PHE A 592     3518   5459   4203    173    166  -1062       C  
ATOM   4667  C   PHE A 592      -3.888   9.473 -37.108  1.00 41.70           C  
ANISOU 4667  C   PHE A 592     4366   6395   5081    189    210  -1105       C  
ATOM   4668  O   PHE A 592      -3.937   9.488 -38.344  1.00 40.44           O  
ANISOU 4668  O   PHE A 592     4247   6212   4906    155    244  -1115       O  
ATOM   4669  CB  PHE A 592      -4.910  11.277 -35.693  1.00 30.78           C  
ANISOU 4669  CB  PHE A 592     2986   5002   3709    112    163  -1067       C  
ATOM   4670  CG  PHE A 592      -4.806  12.356 -36.732  1.00 33.44           C  
ANISOU 4670  CG  PHE A 592     3340   5337   4029     29    200  -1081       C  
ATOM   4671  CD1 PHE A 592      -5.728  12.436 -37.763  1.00 33.84           C  
ANISOU 4671  CD1 PHE A 592     3470   5320   4066     -5    206  -1058       C  
ATOM   4672  CD2 PHE A 592      -3.787  13.292 -36.678  1.00 35.70           C  
ANISOU 4672  CD2 PHE A 592     3567   5688   4308    -18    228  -1116       C  
ATOM   4673  CE1 PHE A 592      -5.634  13.429 -38.720  1.00 37.98           C  
ANISOU 4673  CE1 PHE A 592     4020   5840   4571    -79    238  -1068       C  
ATOM   4674  CE2 PHE A 592      -3.688  14.287 -37.632  1.00 36.28           C  
ANISOU 4674  CE2 PHE A 592     3667   5755   4363    -98    266  -1127       C  
ATOM   4675  CZ  PHE A 592      -4.613  14.355 -38.653  1.00 36.27           C  
ANISOU 4675  CZ  PHE A 592     3751   5683   4347   -126    271  -1101       C  
ATOM   4676  N   THR A 593      -2.788   9.104 -36.446  1.00 46.95           N  
ANISOU 4676  N   THR A 593     4952   7130   5755    243    211  -1132       N  
ATOM   4677  CA  THR A 593      -1.619   8.623 -37.174  1.00 51.11           C  
ANISOU 4677  CA  THR A 593     5434   7708   6278    270    254  -1175       C  
ATOM   4678  C   THR A 593      -1.911   7.309 -37.887  1.00 47.67           C  
ANISOU 4678  C   THR A 593     5058   7217   5838    326    267  -1169       C  
ATOM   4679  O   THR A 593      -1.343   7.042 -38.952  1.00 53.09           O  
ANISOU 4679  O   THR A 593     5746   7913   6514    322    314  -1199       O  
ATOM   4680  CB  THR A 593      -0.434   8.456 -36.222  1.00 45.84           C  
ANISOU 4680  CB  THR A 593     4664   7131   5624    325    244  -1203       C  
ATOM   4681  OG1 THR A 593      -0.815   7.620 -35.122  1.00 50.96           O  
ANISOU 4681  OG1 THR A 593     5322   7759   6282    405    195  -1174       O  
ATOM   4682  CG2 THR A 593       0.020   9.810 -35.687  1.00 41.27           C  
ANISOU 4682  CG2 THR A 593     4023   6614   5044    255    242  -1221       C  
ATOM   4683  N   TRP A 594      -2.788   6.481 -37.316  1.00 37.79           N  
ANISOU 4683  N   TRP A 594     3858   5906   4594    376    229  -1133       N  
ATOM   4684  CA  TRP A 594      -3.163   5.229 -37.964  1.00 38.64           C  
ANISOU 4684  CA  TRP A 594     4033   5952   4696    423    240  -1126       C  
ATOM   4685  C   TRP A 594      -4.055   5.478 -39.175  1.00 40.81           C  
ANISOU 4685  C   TRP A 594     4390   6163   4953    353    256  -1116       C  
ATOM   4686  O   TRP A 594      -3.887   4.836 -40.218  1.00 41.85           O  
ANISOU 4686  O   TRP A 594     4559   6271   5069    361    291  -1134       O  
ATOM   4687  CB  TRP A 594      -3.861   4.315 -36.957  1.00 35.71           C  
ANISOU 4687  CB  TRP A 594     3697   5534   4336    488    197  -1090       C  
ATOM   4688  CG  TRP A 594      -4.285   3.001 -37.525  1.00 42.32           C  
ANISOU 4688  CG  TRP A 594     4609   6302   5167    533    208  -1084       C  
ATOM   4689  CD1 TRP A 594      -3.548   1.855 -37.576  1.00 41.33           C  
ANISOU 4689  CD1 TRP A 594     4479   6182   5043    620    227  -1102       C  
ATOM   4690  CD2 TRP A 594      -5.549   2.691 -38.120  1.00 47.95           C  
ANISOU 4690  CD2 TRP A 594     5417   6930   5873    495    201  -1058       C  
ATOM   4691  NE1 TRP A 594      -4.274   0.850 -38.167  1.00 39.42           N  
ANISOU 4691  NE1 TRP A 594     4328   5857   4791    634    235  -1090       N  
ATOM   4692  CE2 TRP A 594      -5.507   1.338 -38.510  1.00 41.84           C  
ANISOU 4692  CE2 TRP A 594     4694   6111   5093    555    218  -1064       C  
ATOM   4693  CE3 TRP A 594      -6.713   3.426 -38.361  1.00 45.18           C  
ANISOU 4693  CE3 TRP A 594     5109   6537   5518    417    181  -1032       C  
ATOM   4694  CZ2 TRP A 594      -6.582   0.706 -39.128  1.00 40.36           C  
ANISOU 4694  CZ2 TRP A 594     4600   5840   4895    531    216  -1047       C  
ATOM   4695  CZ3 TRP A 594      -7.779   2.797 -38.975  1.00 38.57           C  
ANISOU 4695  CZ3 TRP A 594     4358   5624   4673    398    176  -1014       C  
ATOM   4696  CH2 TRP A 594      -7.705   1.453 -39.355  1.00 34.63           C  
ANISOU 4696  CH2 TRP A 594     3909   5083   4167    451    193  -1023       C  
ATOM   4697  N   LEU A 595      -5.015   6.400 -39.052  1.00 40.33           N  
ANISOU 4697  N   LEU A 595     4359   6072   4891    286    231  -1087       N  
ATOM   4698  CA  LEU A 595      -5.910   6.697 -40.167  1.00 30.72           C  
ANISOU 4698  CA  LEU A 595     3218   4798   3655    222    238  -1074       C  
ATOM   4699  C   LEU A 595      -5.147   7.267 -41.355  1.00 35.05           C  
ANISOU 4699  C   LEU A 595     3760   5378   4180    173    289  -1109       C  
ATOM   4700  O   LEU A 595      -5.404   6.891 -42.505  1.00 42.56           O  
ANISOU 4700  O   LEU A 595     4772   6290   5109    154    312  -1114       O  
ATOM   4701  CB  LEU A 595      -7.002   7.670 -39.721  1.00 29.66           C  
ANISOU 4701  CB  LEU A 595     3107   4636   3528    168    201  -1037       C  
ATOM   4702  CG  LEU A 595      -8.060   7.168 -38.738  1.00 31.89           C  
ANISOU 4702  CG  LEU A 595     3415   4872   3829    199    154   -999       C  
ATOM   4703  CD1 LEU A 595      -8.943   8.316 -38.279  1.00 24.74           C  
ANISOU 4703  CD1 LEU A 595     2515   3952   2931    145    126   -969       C  
ATOM   4704  CD2 LEU A 595      -8.899   6.072 -39.365  1.00 31.93           C  
ANISOU 4704  CD2 LEU A 595     3495   4810   3828    214    148   -985       C  
ATOM   4705  N   LYS A 596      -4.205   8.178 -41.098  1.00 39.01           N  
ANISOU 4705  N   LYS A 596     4189   5948   4684    147    310  -1133       N  
ATOM   4706  CA  LYS A 596      -3.467   8.808 -42.188  1.00 40.95           C  
ANISOU 4706  CA  LYS A 596     4428   6224   4906     91    364  -1167       C  
ATOM   4707  C   LYS A 596      -2.661   7.781 -42.974  1.00 47.95           C  
ANISOU 4707  C   LYS A 596     5312   7125   5784    136    410  -1203       C  
ATOM   4708  O   LYS A 596      -2.577   7.858 -44.205  1.00 51.89           O  
ANISOU 4708  O   LYS A 596     5855   7605   6254     95    451  -1219       O  
ATOM   4709  CB  LYS A 596      -2.560   9.909 -41.639  1.00 34.19           C  
ANISOU 4709  CB  LYS A 596     3489   5444   4058     55    379  -1190       C  
ATOM   4710  CG  LYS A 596      -3.321  11.093 -41.059  1.00 33.97           C  
ANISOU 4710  CG  LYS A 596     3476   5397   4033     -3    346  -1160       C  
ATOM   4711  CD  LYS A 596      -2.403  12.272 -40.782  1.00 41.21           C  
ANISOU 4711  CD  LYS A 596     4327   6383   4950    -58    372  -1189       C  
ATOM   4712  CE  LYS A 596      -1.495  12.003 -39.594  1.00 39.84           C  
ANISOU 4712  CE  LYS A 596     4054   6285   4800     -6    358  -1211       C  
ATOM   4713  NZ  LYS A 596      -0.531  13.116 -39.375  1.00 43.38           N  
ANISOU 4713  NZ  LYS A 596     4431   6805   5245    -66    386  -1246       N  
ATOM   4714  N   ASP A 597      -2.056   6.816 -42.279  1.00 49.48           N  
ANISOU 4714  N   ASP A 597     5455   7347   5998    223    404  -1216       N  
ATOM   4715  CA  ASP A 597      -1.401   5.713 -42.974  1.00 53.38           C  
ANISOU 4715  CA  ASP A 597     5954   7842   6486    279    446  -1246       C  
ATOM   4716  C   ASP A 597      -2.417   4.838 -43.700  1.00 50.44           C  
ANISOU 4716  C   ASP A 597     5690   7380   6096    285    439  -1225       C  
ATOM   4717  O   ASP A 597      -2.161   4.374 -44.816  1.00 62.31           O  
ANISOU 4717  O   ASP A 597     7234   8865   7576    281    484  -1249       O  
ATOM   4718  CB  ASP A 597      -0.584   4.878 -41.990  1.00 52.82           C  
ANISOU 4718  CB  ASP A 597     5809   7818   6441    379    435  -1260       C  
ATOM   4719  CG  ASP A 597       0.003   3.634 -42.630  1.00 64.17           C  
ANISOU 4719  CG  ASP A 597     7260   9247   7874    451    476  -1288       C  
ATOM   4720  OD1 ASP A 597       0.713   3.767 -43.649  1.00 64.81           O  
ANISOU 4720  OD1 ASP A 597     7331   9355   7940    426    536  -1326       O  
ATOM   4721  OD2 ASP A 597      -0.248   2.524 -42.116  1.00 74.03           O1-
ANISOU 4721  OD2 ASP A 597     8536  10459   9134    532    452  -1271       O1-
ATOM   4722  N   GLN A 598      -3.576   4.601 -43.081  1.00 44.93           N  
ANISOU 4722  N   GLN A 598     5040   6624   5407    292    384  -1182       N  
ATOM   4723  CA  GLN A 598      -4.587   3.749 -43.696  1.00 39.29           C  
ANISOU 4723  CA  GLN A 598     4424   5827   4678    293    374  -1163       C  
ATOM   4724  C   GLN A 598      -5.280   4.420 -44.872  1.00 40.79           C  
ANISOU 4724  C   GLN A 598     4682   5981   4836    206    381  -1156       C  
ATOM   4725  O   GLN A 598      -5.931   3.732 -45.666  1.00 48.91           O  
ANISOU 4725  O   GLN A 598     5791   6950   5844    198    382  -1152       O  
ATOM   4726  CB  GLN A 598      -5.621   3.328 -42.654  1.00 37.49           C  
ANISOU 4726  CB  GLN A 598     4220   5553   4470    321    316  -1120       C  
ATOM   4727  CG  GLN A 598      -5.242   2.067 -41.910  1.00 47.92           C  
ANISOU 4727  CG  GLN A 598     5532   6868   5809    419    313  -1123       C  
ATOM   4728  CD  GLN A 598      -5.493   0.814 -42.723  1.00 47.78           C  
ANISOU 4728  CD  GLN A 598     5594   6787   5774    447    335  -1133       C  
ATOM   4729  OE1 GLN A 598      -6.490   0.714 -43.439  1.00 51.18           O  
ANISOU 4729  OE1 GLN A 598     6102   7157   6187    396    326  -1119       O  
ATOM   4730  NE2 GLN A 598      -4.588  -0.152 -42.618  1.00 44.55           N  
ANISOU 4730  NE2 GLN A 598     5167   6391   5370    531    364  -1157       N  
ATOM   4731  N   ASN A 599      -5.163   5.741 -45.000  1.00 38.31           N  
ANISOU 4731  N   ASN A 599     4341   5700   4515    139    386  -1155       N  
ATOM   4732  CA  ASN A 599      -5.706   6.470 -46.137  1.00 40.88           C  
ANISOU 4732  CA  ASN A 599     4731   5996   4806     59    395  -1148       C  
ATOM   4733  C   ASN A 599      -4.617   6.905 -47.112  1.00 51.56           C  
ANISOU 4733  C   ASN A 599     6069   7391   6131     24    461  -1190       C  
ATOM   4734  O   ASN A 599      -4.825   7.842 -47.889  1.00 54.94           O  
ANISOU 4734  O   ASN A 599     6535   7812   6530    -49    474  -1186       O  
ATOM   4735  CB  ASN A 599      -6.508   7.683 -45.661  1.00 40.41           C  
ANISOU 4735  CB  ASN A 599     4672   5928   4753      5    353  -1112       C  
ATOM   4736  CG  ASN A 599      -7.518   7.331 -44.585  1.00 35.18           C  
ANISOU 4736  CG  ASN A 599     4012   5232   4120     37    293  -1073       C  
ATOM   4737  OD1 ASN A 599      -8.152   6.277 -44.632  1.00 33.90           O  
ANISOU 4737  OD1 ASN A 599     3896   5024   3962     70    274  -1062       O  
ATOM   4738  ND2 ASN A 599      -7.672   8.216 -43.608  1.00 33.45           N  
ANISOU 4738  ND2 ASN A 599     3750   5036   3924     25    267  -1054       N  
ATOM   4739  N   LYS A 600      -3.454   6.246 -47.080  1.00 76.13           N  
ANISOU 4739  N   LYS A 600     9126  10548   9251     78    506  -1230       N  
ATOM   4740  CA  LYS A 600      -2.358   6.644 -47.958  1.00 77.44           C  
ANISOU 4740  CA  LYS A 600     9269  10761   9395     46    576  -1274       C  
ATOM   4741  C   LYS A 600      -2.684   6.385 -49.424  1.00 88.49           C  
ANISOU 4741  C   LYS A 600    10764  12110  10746      5    608  -1283       C  
ATOM   4742  O   LYS A 600      -2.232   7.134 -50.297  1.00 96.99           O  
ANISOU 4742  O   LYS A 600    11854  13206  11792    -58    655  -1303       O  
ATOM   4743  CB  LYS A 600      -1.065   5.929 -47.554  1.00 76.83           C  
ANISOU 4743  CB  LYS A 600     9103  10746   9342    121    614  -1316       C  
ATOM   4744  CG  LYS A 600      -1.060   4.423 -47.767  1.00 88.69           C  
ANISOU 4744  CG  LYS A 600    10642  12212  10846    202    623  -1326       C  
ATOM   4745  CD  LYS A 600       0.273   3.821 -47.344  1.00 96.92           C  
ANISOU 4745  CD  LYS A 600    11590  13322  11913    283    660  -1367       C  
ATOM   4746  CE  LYS A 600       0.269   2.305 -47.465  1.00 99.15           C  
ANISOU 4746  CE  LYS A 600    11914  13560  12198    372    669  -1374       C  
ATOM   4747  NZ  LYS A 600      -0.507   1.660 -46.370  1.00 73.83           N  
ANISOU 4747  NZ  LYS A 600     8724  10312   9016    429    603  -1334       N  
ATOM   4748  N   ASN A 601      -3.460   5.344 -49.716  1.00 87.32           N  
ANISOU 4748  N   ASN A 601    10689  11898  10589     36    585  -1269       N  
ATOM   4749  CA  ASN A 601      -3.959   5.089 -51.061  1.00 89.67           C  
ANISOU 4749  CA  ASN A 601    11090  12143  10839     -7    604  -1272       C  
ATOM   4750  C   ASN A 601      -5.480   5.182 -51.092  1.00 83.99           C  
ANISOU 4750  C   ASN A 601    10446  11358  10109    -40    535  -1225       C  
ATOM   4751  O   ASN A 601      -6.163   4.387 -51.742  1.00 78.62           O  
ANISOU 4751  O   ASN A 601     9847  10621   9404    -41    523  -1221       O  
ATOM   4752  CB  ASN A 601      -3.477   3.737 -51.586  1.00 92.79           C  
ANISOU 4752  CB  ASN A 601    11512  12520  11223     51    647  -1307       C  
ATOM   4753  CG  ASN A 601      -3.640   2.623 -50.574  1.00 96.79           C  
ANISOU 4753  CG  ASN A 601    11997  13010  11770    139    614  -1298       C  
ATOM   4754  OD1 ASN A 601      -2.686   2.242 -49.895  1.00 96.29           O  
ANISOU 4754  OD1 ASN A 601    11855  12993  11738    208    636  -1319       O  
ATOM   4755  ND2 ASN A 601      -4.850   2.086 -50.474  1.00 95.30           N  
ANISOU 4755  ND2 ASN A 601    11878  12752  11578    138    562  -1265       N  
ATOM   4756  N   SER A 602      -6.023   6.159 -50.369  1.00 76.36           N  
ANISOU 4756  N   SER A 602     9452  10400   9162    -68    488  -1190       N  
ATOM   4757  CA  SER A 602      -7.440   6.485 -50.411  1.00 66.32           C  
ANISOU 4757  CA  SER A 602     8240   9075   7883   -106    425  -1144       C  
ATOM   4758  C   SER A 602      -7.582   7.997 -50.483  1.00 62.77           C  
ANISOU 4758  C   SER A 602     7784   8642   7423   -170    417  -1125       C  
ATOM   4759  O   SER A 602      -6.710   8.738 -50.021  1.00 68.66           O  
ANISOU 4759  O   SER A 602     8464   9442   8184   -177    446  -1140       O  
ATOM   4760  CB  SER A 602      -8.193   5.943 -49.188  1.00 68.01           C  
ANISOU 4760  CB  SER A 602     8429   9269   8142    -57    368  -1115       C  
ATOM   4761  OG  SER A 602      -7.616   4.736 -48.721  1.00 81.99           O  
ANISOU 4761  OG  SER A 602    10174  11045   9934     17    387  -1137       O  
ATOM   4762  N   PHE A 603      -8.686   8.453 -51.068  1.00 54.28           N  
ANISOU 4762  N   PHE A 603     6779   7522   6320   -218    377  -1092       N  
ATOM   4763  CA  PHE A 603      -8.933   9.884 -51.175  1.00 55.52           C  
ANISOU 4763  CA  PHE A 603     6946   7685   6466   -275    366  -1068       C  
ATOM   4764  C   PHE A 603      -9.477  10.415 -49.855  1.00 55.74           C  
ANISOU 4764  C   PHE A 603     6919   7718   6541   -258    318  -1036       C  
ATOM   4765  O   PHE A 603     -10.468   9.899 -49.328  1.00 57.59           O  
ANISOU 4765  O   PHE A 603     7160   7921   6799   -231    265  -1009       O  
ATOM   4766  CB  PHE A 603      -9.909  10.183 -52.313  1.00 53.85           C  
ANISOU 4766  CB  PHE A 603     6831   7425   6204   -325    338  -1044       C  
ATOM   4767  CG  PHE A 603     -10.172  11.650 -52.515  1.00 54.91           C  
ANISOU 4767  CG  PHE A 603     6986   7556   6319   -379    329  -1017       C  
ATOM   4768  CD1 PHE A 603      -9.323  12.418 -53.295  1.00 55.44           C  
ANISOU 4768  CD1 PHE A 603     7077   7643   6347   -427    388  -1037       C  
ATOM   4769  CD2 PHE A 603     -11.262  12.263 -51.917  1.00 55.76           C  
ANISOU 4769  CD2 PHE A 603     7095   7642   6450   -381    266   -972       C  
ATOM   4770  CE1 PHE A 603      -9.558  13.768 -53.480  1.00 59.66           C  
ANISOU 4770  CE1 PHE A 603     7639   8167   6860   -477    382  -1011       C  
ATOM   4771  CE2 PHE A 603     -11.502  13.613 -52.098  1.00 57.24           C  
ANISOU 4771  CE2 PHE A 603     7308   7822   6620   -425    260   -946       C  
ATOM   4772  CZ  PHE A 603     -10.648  14.366 -52.880  1.00 54.61           C  
ANISOU 4772  CZ  PHE A 603     7003   7501   6243   -473    317   -965       C  
ATOM   4773  N   VAL A 604      -8.826  11.446 -49.323  1.00 44.06           N  
ANISOU 4773  N   VAL A 604     5387   6278   5074   -277    340  -1041       N  
ATOM   4774  CA  VAL A 604      -9.241  12.092 -48.083  1.00 35.66           C  
ANISOU 4774  CA  VAL A 604     4275   5222   4051   -268    301  -1014       C  
ATOM   4775  C   VAL A 604      -9.958  13.385 -48.438  1.00 40.43           C  
ANISOU 4775  C   VAL A 604     4928   5800   4636   -323    281   -981       C  
ATOM   4776  O   VAL A 604      -9.438  14.203 -49.208  1.00 44.08           O  
ANISOU 4776  O   VAL A 604     5419   6269   5062   -374    320   -992       O  
ATOM   4777  CB  VAL A 604      -8.040  12.356 -47.159  1.00 36.60           C  
ANISOU 4777  CB  VAL A 604     4303   5405   4198   -251    336  -1043       C  
ATOM   4778  CG1 VAL A 604      -8.494  13.064 -45.893  1.00 41.17           C  
ANISOU 4778  CG1 VAL A 604     4840   5988   4813   -246    296  -1016       C  
ATOM   4779  CG2 VAL A 604      -7.337  11.052 -46.822  1.00 39.43           C  
ANISOU 4779  CG2 VAL A 604     4616   5790   4576   -185    352  -1074       C  
ATOM   4780  N   GLY A 605     -11.144  13.571 -47.879  1.00 41.33           N  
ANISOU 4780  N   GLY A 605     5051   5880   4771   -313    222   -940       N  
ATOM   4781  CA  GLY A 605     -12.039  14.641 -48.271  1.00 42.74           C  
ANISOU 4781  CA  GLY A 605     5284   6024   4932   -352    192   -903       C  
ATOM   4782  C   GLY A 605     -13.251  14.087 -48.999  1.00 40.75           C  
ANISOU 4782  C   GLY A 605     5095   5725   4662   -350    143   -877       C  
ATOM   4783  O   GLY A 605     -13.438  12.877 -49.128  1.00 44.07           O  
ANISOU 4783  O   GLY A 605     5520   6138   5087   -321    132   -888       O  
ATOM   4784  N   TRP A 606     -14.083  15.004 -49.484  1.00 35.00           N  
ANISOU 4784  N   TRP A 606     4420   4967   3913   -380    113   -842       N  
ATOM   4785  CA  TRP A 606     -15.303  14.595 -50.160  1.00 39.44           C  
ANISOU 4785  CA  TRP A 606     5036   5490   4458   -380     58   -815       C  
ATOM   4786  C   TRP A 606     -15.720  15.653 -51.169  1.00 40.32           C  
ANISOU 4786  C   TRP A 606     5221   5576   4521   -422     45   -790       C  
ATOM   4787  O   TRP A 606     -15.375  16.831 -51.042  1.00 31.53           O  
ANISOU 4787  O   TRP A 606     4113   4465   3402   -445     68   -781       O  
ATOM   4788  CB  TRP A 606     -16.438  14.348 -49.162  1.00 40.66           C  
ANISOU 4788  CB  TRP A 606     5154   5631   4664   -346      0   -786       C  
ATOM   4789  CG  TRP A 606     -16.617  15.472 -48.200  1.00 31.12           C  
ANISOU 4789  CG  TRP A 606     3909   4426   3488   -343     -7   -764       C  
ATOM   4790  CD1 TRP A 606     -17.338  16.611 -48.399  1.00 30.26           C  
ANISOU 4790  CD1 TRP A 606     3834   4294   3371   -360    -34   -728       C  
ATOM   4791  CD2 TRP A 606     -16.055  15.575 -46.888  1.00 31.47           C  
ANISOU 4791  CD2 TRP A 606     3884   4498   3576   -319     14   -775       C  
ATOM   4792  NE1 TRP A 606     -17.266  17.417 -47.288  1.00 30.70           N  
ANISOU 4792  NE1 TRP A 606     3844   4357   3462   -350    -27   -719       N  
ATOM   4793  CE2 TRP A 606     -16.482  16.804 -46.347  1.00 32.83           C  
ANISOU 4793  CE2 TRP A 606     4050   4660   3763   -328      1   -748       C  
ATOM   4794  CE3 TRP A 606     -15.234  14.747 -46.117  1.00 31.08           C  
ANISOU 4794  CE3 TRP A 606     3777   4481   3552   -289     41   -806       C  
ATOM   4795  CZ2 TRP A 606     -16.119  17.222 -45.069  1.00 27.59           C  
ANISOU 4795  CZ2 TRP A 606     3329   4017   3138   -314     15   -753       C  
ATOM   4796  CZ3 TRP A 606     -14.873  15.165 -44.850  1.00 27.07           C  
ANISOU 4796  CZ3 TRP A 606     3209   3997   3081   -272     50   -808       C  
ATOM   4797  CH2 TRP A 606     -15.315  16.391 -44.338  1.00 29.36           C  
ANISOU 4797  CH2 TRP A 606     3496   4276   3383   -288     38   -783       C  
ATOM   4798  N   SER A 607     -16.470  15.211 -52.172  1.00 48.74           N  
ANISOU 4798  N   SER A 607     6350   6617   5551   -433      9   -778       N  
ATOM   4799  CA  SER A 607     -17.056  16.090 -53.172  1.00 50.74           C  
ANISOU 4799  CA  SER A 607     6681   6843   5754   -465    -18   -747       C  
ATOM   4800  C   SER A 607     -18.535  16.276 -52.869  1.00 51.87           C  
ANISOU 4800  C   SER A 607     6820   6964   5923   -443    -97   -704       C  
ATOM   4801  O   SER A 607     -19.259  15.297 -52.662  1.00 52.51           O  
ANISOU 4801  O   SER A 607     6880   7044   6029   -422   -137   -703       O  
ATOM   4802  CB  SER A 607     -16.872  15.513 -54.575  1.00 49.90           C  
ANISOU 4802  CB  SER A 607     6651   6727   5583   -493     -7   -765       C  
ATOM   4803  OG  SER A 607     -17.561  16.294 -55.534  1.00 65.51           O  
ANISOU 4803  OG  SER A 607     8707   8676   7508   -519    -44   -731       O  
ATOM   4804  N   THR A 608     -18.978  17.533 -52.837  1.00 43.93           N  
ANISOU 4804  N   THR A 608     5837   5942   4914   -449   -116   -668       N  
ATOM   4805  CA  THR A 608     -20.382  17.821 -52.579  1.00 47.62           C  
ANISOU 4805  CA  THR A 608     6297   6391   5406   -425   -190   -626       C  
ATOM   4806  C   THR A 608     -21.259  17.618 -53.807  1.00 48.15           C  
ANISOU 4806  C   THR A 608     6433   6440   5423   -438   -246   -606       C  
ATOM   4807  O   THR A 608     -22.479  17.486 -53.664  1.00 50.35           O  
ANISOU 4807  O   THR A 608     6694   6713   5724   -416   -314   -579       O  
ATOM   4808  CB  THR A 608     -20.544  19.255 -52.070  1.00 50.72           C  
ANISOU 4808  CB  THR A 608     6690   6768   5812   -420   -188   -594       C  
ATOM   4809  OG1 THR A 608     -20.465  20.168 -53.171  1.00 52.54           O  
ANISOU 4809  OG1 THR A 608     7009   6975   5979   -449   -185   -575       O  
ATOM   4810  CG2 THR A 608     -19.452  19.588 -51.063  1.00 45.47           C  
ANISOU 4810  CG2 THR A 608     5973   6123   5180   -422   -123   -620       C  
ATOM   4811  N   ASP A 609     -20.670  17.582 -55.005  1.00 54.57           N  
ANISOU 4811  N   ASP A 609     7320   7248   6167   -473   -221   -620       N  
ATOM   4812  CA  ASP A 609     -21.464  17.468 -56.222  1.00 60.31           C  
ANISOU 4812  CA  ASP A 609     8121   7958   6836   -488   -277   -600       C  
ATOM   4813  C   ASP A 609     -22.014  16.063 -56.432  1.00 61.79           C  
ANISOU 4813  C   ASP A 609     8293   8154   7028   -486   -314   -620       C  
ATOM   4814  O   ASP A 609     -22.933  15.888 -57.239  1.00 64.86           O  
ANISOU 4814  O   ASP A 609     8726   8536   7383   -494   -378   -602       O  
ATOM   4815  CB  ASP A 609     -20.634  17.887 -57.436  1.00 62.94           C  
ANISOU 4815  CB  ASP A 609     8547   8281   7088   -531   -232   -610       C  
ATOM   4816  CG  ASP A 609     -19.762  16.766 -57.964  1.00 67.27           C  
ANISOU 4816  CG  ASP A 609     9109   8842   7608   -554   -182   -660       C  
ATOM   4817  OD1 ASP A 609     -19.017  16.162 -57.165  1.00 70.00           O  
ANISOU 4817  OD1 ASP A 609     9389   9209   7999   -541   -134   -694       O  
ATOM   4818  OD2 ASP A 609     -19.818  16.489 -59.181  1.00 71.13           O1-
ANISOU 4818  OD2 ASP A 609     9678   9321   8027   -582   -192   -665       O1-
ATOM   4819  N   TRP A 610     -21.479  15.065 -55.735  1.00 48.29           N  
ANISOU 4819  N   TRP A 610     6528   6461   5360   -475   -277   -656       N  
ATOM   4820  CA  TRP A 610     -21.937  13.691 -55.887  1.00 43.30           C  
ANISOU 4820  CA  TRP A 610     5888   5831   4733   -474   -304   -678       C  
ATOM   4821  C   TRP A 610     -23.083  13.411 -54.925  1.00 44.65           C  
ANISOU 4821  C   TRP A 610     5990   6004   4969   -445   -360   -657       C  
ATOM   4822  O   TRP A 610     -23.013  13.762 -53.743  1.00 44.38           O  
ANISOU 4822  O   TRP A 610     5890   5978   4995   -417   -346   -649       O  
ATOM   4823  CB  TRP A 610     -20.796  12.703 -55.642  1.00 38.42           C  
ANISOU 4823  CB  TRP A 610     5252   5223   4124   -472   -233   -726       C  
ATOM   4824  CG  TRP A 610     -21.213  11.267 -55.792  1.00 40.05           C  
ANISOU 4824  CG  TRP A 610     5461   5423   4333   -472   -253   -750       C  
ATOM   4825  CD1 TRP A 610     -21.105  10.497 -56.913  1.00 47.88           C  
ANISOU 4825  CD1 TRP A 610     6522   6404   5267   -501   -250   -775       C  
ATOM   4826  CD2 TRP A 610     -21.807  10.432 -54.788  1.00 40.20           C  
ANISOU 4826  CD2 TRP A 610     5417   5442   4414   -446   -277   -752       C  
ATOM   4827  NE1 TRP A 610     -21.594   9.236 -56.671  1.00 44.85           N  
ANISOU 4827  NE1 TRP A 610     6123   6012   4906   -495   -269   -794       N  
ATOM   4828  CE2 TRP A 610     -22.032   9.171 -55.374  1.00 39.62           C  
ANISOU 4828  CE2 TRP A 610     5381   5356   4317   -462   -285   -779       C  
ATOM   4829  CE3 TRP A 610     -22.170  10.629 -53.452  1.00 40.06           C  
ANISOU 4829  CE3 TRP A 610     5321   5432   4466   -413   -288   -734       C  
ATOM   4830  CZ2 TRP A 610     -22.601   8.111 -54.671  1.00 46.64           C  
ANISOU 4830  CZ2 TRP A 610     6233   6238   5251   -448   -303   -788       C  
ATOM   4831  CZ3 TRP A 610     -22.737   9.577 -52.756  1.00 38.93           C  
ANISOU 4831  CZ3 TRP A 610     5142   5285   4367   -398   -306   -742       C  
ATOM   4832  CH2 TRP A 610     -22.947   8.334 -53.366  1.00 42.56           C  
ANISOU 4832  CH2 TRP A 610     5640   5728   4801   -416   -313   -768       C  
ATOM   4833  N   SER A 611     -24.132  12.778 -55.438  1.00 60.08           N  
ANISOU 4833  N   SER A 611     7962   7955   6912   -456   -424   -651       N  
ATOM   4834  CA  SER A 611     -25.243  12.286 -54.642  1.00 52.77           C  
ANISOU 4834  CA  SER A 611     6971   7034   6045   -438   -474   -639       C  
ATOM   4835  C   SER A 611     -25.642  10.917 -55.170  1.00 55.85           C  
ANISOU 4835  C   SER A 611     7384   7420   6417   -463   -496   -667       C  
ATOM   4836  O   SER A 611     -25.475  10.639 -56.364  1.00 61.73           O  
ANISOU 4836  O   SER A 611     8201   8158   7094   -495   -502   -681       O  
ATOM   4837  CB  SER A 611     -26.447  13.241 -54.690  1.00 55.46           C  
ANISOU 4837  CB  SER A 611     7300   7377   6395   -426   -546   -593       C  
ATOM   4838  OG  SER A 611     -26.529  13.900 -55.941  1.00 68.46           O  
ANISOU 4838  OG  SER A 611     9025   9017   7971   -447   -574   -576       O  
ATOM   4839  N   PRO A 612     -26.166  10.039 -54.308  1.00 44.62           N  
ANISOU 4839  N   PRO A 612     5906   5999   5050   -452   -506   -676       N  
ATOM   4840  CA  PRO A 612     -26.518   8.682 -54.760  1.00 48.04           C  
ANISOU 4840  CA  PRO A 612     6365   6423   5466   -480   -521   -706       C  
ATOM   4841  C   PRO A 612     -27.637   8.636 -55.790  1.00 51.60           C  
ANISOU 4841  C   PRO A 612     6852   6878   5876   -515   -600   -695       C  
ATOM   4842  O   PRO A 612     -27.806   7.593 -56.435  1.00 63.10           O  
ANISOU 4842  O   PRO A 612     8350   8325   7300   -549   -610   -724       O  
ATOM   4843  CB  PRO A 612     -26.923   7.966 -53.464  1.00 49.29           C  
ANISOU 4843  CB  PRO A 612     6452   6580   5698   -459   -516   -711       C  
ATOM   4844  CG  PRO A 612     -27.210   9.045 -52.494  1.00 36.33           C  
ANISOU 4844  CG  PRO A 612     4745   4950   4107   -425   -524   -676       C  
ATOM   4845  CD  PRO A 612     -26.340  10.201 -52.856  1.00 36.89           C  
ANISOU 4845  CD  PRO A 612     4844   5026   4147   -416   -495   -664       C  
ATOM   4846  N   TYR A 613     -28.411   9.706 -55.963  1.00 45.51           N  
ANISOU 4846  N   TYR A 613     6067   6120   5104   -507   -657   -655       N  
ATOM   4847  CA  TYR A 613     -29.363   9.791 -57.066  1.00 62.51           C  
ANISOU 4847  CA  TYR A 613     8260   8283   7208   -536   -735   -642       C  
ATOM   4848  C   TYR A 613     -28.643  10.422 -58.253  1.00 73.30           C  
ANISOU 4848  C   TYR A 613     9717   9640   8491   -551   -722   -639       C  
ATOM   4849  O   TYR A 613     -28.300  11.608 -58.222  1.00 59.38           O  
ANISOU 4849  O   TYR A 613     7964   7877   6722   -528   -710   -610       O  
ATOM   4850  CB  TYR A 613     -30.616  10.575 -56.673  1.00 56.35           C  
ANISOU 4850  CB  TYR A 613     7419   7524   6469   -513   -808   -600       C  
ATOM   4851  CG  TYR A 613     -30.387  11.917 -56.006  1.00 59.30           C  
ANISOU 4851  CG  TYR A 613     7762   7897   6875   -468   -790   -564       C  
ATOM   4852  CD1 TYR A 613     -30.091  12.003 -54.651  1.00 55.03           C  
ANISOU 4852  CD1 TYR A 613     7152   7353   6405   -436   -742   -564       C  
ATOM   4853  CD2 TYR A 613     -30.508  13.100 -56.725  1.00 58.34           C  
ANISOU 4853  CD2 TYR A 613     7683   7774   6708   -457   -822   -529       C  
ATOM   4854  CE1 TYR A 613     -29.896  13.228 -54.038  1.00 54.08           C  
ANISOU 4854  CE1 TYR A 613     7008   7230   6311   -399   -724   -534       C  
ATOM   4855  CE2 TYR A 613     -30.314  14.328 -56.121  1.00 55.22           C  
ANISOU 4855  CE2 TYR A 613     7268   7372   6341   -417   -803   -497       C  
ATOM   4856  CZ  TYR A 613     -30.009  14.387 -54.778  1.00 58.03           C  
ANISOU 4856  CZ  TYR A 613     7555   7726   6769   -390   -753   -501       C  
ATOM   4857  OH  TYR A 613     -29.818  15.609 -54.175  1.00 48.27           O  
ANISOU 4857  OH  TYR A 613     6302   6481   5557   -356   -732   -472       O  
ATOM   4858  N   ALA A 614     -28.402   9.617 -59.288  1.00109.84           N  
ANISOU 4858  N   ALA A 614    14419  14261  13055   -592   -720   -670       N  
ATOM   4859  CA  ALA A 614     -27.563   9.988 -60.430  1.00106.31           C  
ANISOU 4859  CA  ALA A 614    14067  13802  12524   -613   -690   -677       C  
ATOM   4860  C   ALA A 614     -27.872  11.373 -60.992  1.00103.55           C  
ANISOU 4860  C   ALA A 614    13752  13458  12136   -603   -733   -631       C  
ATOM   4861  O   ALA A 614     -27.111  12.317 -60.780  1.00 99.87           O  
ANISOU 4861  O   ALA A 614    13293  12982  11670   -583   -685   -615       O  
ATOM   4862  CB  ALA A 614     -27.698   8.941 -61.529  1.00 92.30           C  
ANISOU 4862  CB  ALA A 614    12366  12021  10683   -661   -708   -712       C  
TER    4863      ALA A 614                                                      
ATOM   4864  N   THR B 333     -34.268  12.437  47.083  1.00151.60           N  
ANISOU 4864  N   THR B 333    18548  20554  18500   2089    537    -42       N  
ATOM   4865  CA  THR B 333     -33.889  12.304  45.681  1.00160.72           C  
ANISOU 4865  CA  THR B 333    19666  21699  19700   2018    526    -64       C  
ATOM   4866  C   THR B 333     -35.022  12.760  44.763  1.00152.79           C  
ANISOU 4866  C   THR B 333    18692  20601  18759   1970    552    -32       C  
ATOM   4867  O   THR B 333     -35.801  11.945  44.264  1.00145.30           O  
ANISOU 4867  O   THR B 333    17736  19600  17870   1994    575     24       O  
ATOM   4868  CB  THR B 333     -33.501  10.853  45.337  1.00162.69           C  
ANISOU 4868  CB  THR B 333    19863  21973  19978   2060    523    -38       C  
ATOM   4869  OG1 THR B 333     -34.568   9.969  45.705  1.00165.41           O  
ANISOU 4869  OG1 THR B 333    20222  22266  20361   2134    558     40       O  
ATOM   4870  CG2 THR B 333     -32.239  10.450  46.087  1.00155.97           C  
ANISOU 4870  CG2 THR B 333    18975  21222  19064   2098    493    -76       C  
ATOM   4871  N   ASN B 334     -35.097  14.071  44.544  1.00125.92           N  
ANISOU 4871  N   ASN B 334    15323  17179  15341   1903    549    -70       N  
ATOM   4872  CA  ASN B 334     -36.130  14.694  43.716  1.00121.51           C  
ANISOU 4872  CA  ASN B 334    14799  16537  14834   1854    574    -46       C  
ATOM   4873  C   ASN B 334     -35.557  14.898  42.317  1.00115.54           C  
ANISOU 4873  C   ASN B 334    14012  15781  14108   1769    557    -87       C  
ATOM   4874  O   ASN B 334     -34.768  15.815  42.090  1.00110.23           O  
ANISOU 4874  O   ASN B 334    13339  15139  13402   1706    536   -151       O  
ATOM   4875  CB  ASN B 334     -36.575  16.013  44.341  1.00120.69           C  
ANISOU 4875  CB  ASN B 334    14754  16409  14694   1836    585    -61       C  
ATOM   4876  CG  ASN B 334     -37.836  16.558  43.715  1.00117.47           C  
ANISOU 4876  CG  ASN B 334    14385  15911  14336   1808    617    -21       C  
ATOM   4877  OD1 ASN B 334     -38.775  15.814  43.442  1.00115.39           O  
ANISOU 4877  OD1 ASN B 334    14120  15595  14126   1843    641     43       O  
ATOM   4878  ND2 ASN B 334     -37.867  17.866  43.486  1.00111.21           N  
ANISOU 4878  ND2 ASN B 334    13629  15099  13527   1743    619    -58       N  
ATOM   4879  N   LEU B 335     -35.972  14.058  41.372  1.00104.71           N  
ANISOU 4879  N   LEU B 335    12615  14371  12799   1768    567    -49       N  
ATOM   4880  CA  LEU B 335     -35.303  13.978  40.080  1.00 98.48           C  
ANISOU 4880  CA  LEU B 335    11788  13592  12037   1700    548    -84       C  
ATOM   4881  C   LEU B 335     -35.769  15.073  39.124  1.00 93.44           C  
ANISOU 4881  C   LEU B 335    11180  12899  11425   1621    558   -100       C  
ATOM   4882  O   LEU B 335     -36.966  15.356  39.002  1.00 91.29           O  
ANISOU 4882  O   LEU B 335    10944  12556  11185   1626    586    -54       O  
ATOM   4883  CB  LEU B 335     -35.524  12.597  39.463  1.00 88.11           C  
ANISOU 4883  CB  LEU B 335    10437  12263  10779   1733    555    -39       C  
ATOM   4884  CG  LEU B 335     -35.057  11.434  40.353  1.00 93.34           C  
ANISOU 4884  CG  LEU B 335    11068  12978  11418   1814    549    -20       C  
ATOM   4885  CD1 LEU B 335     -36.227  10.780  41.083  1.00 93.77           C  
ANISOU 4885  CD1 LEU B 335    11146  12985  11496   1894    583     54       C  
ATOM   4886  CD2 LEU B 335     -34.268  10.394  39.564  1.00 93.00           C  
ANISOU 4886  CD2 LEU B 335    10969  12968  11398   1809    533    -30       C  
ATOM   4887  N   CYS B 336     -34.798  15.684  38.442  1.00 94.18           N  
ANISOU 4887  N   CYS B 336    11256  13026  11503   1549    535   -163       N  
ATOM   4888  CA  CYS B 336     -35.074  16.783  37.525  1.00 85.91           C  
ANISOU 4888  CA  CYS B 336    10235  11934  10473   1470    543   -186       C  
ATOM   4889  C   CYS B 336     -35.857  16.290  36.308  1.00 84.84           C  
ANISOU 4889  C   CYS B 336    10091  11736  10409   1454    559   -143       C  
ATOM   4890  O   CYS B 336     -35.743  15.128  35.921  1.00 90.99           O  
ANISOU 4890  O   CYS B 336    10830  12523  11219   1480    553   -120       O  
ATOM   4891  CB  CYS B 336     -33.770  17.449  37.079  1.00 83.51           C  
ANISOU 4891  CB  CYS B 336     9909  11684  10138   1400    515   -265       C  
ATOM   4892  SG  CYS B 336     -32.942  18.438  38.358  1.00 95.26           S  
ANISOU 4892  SG  CYS B 336    11418  13235  11542   1395    499   -326       S  
ATOM   4893  N   PRO B 337     -36.656  17.166  35.680  1.00 68.70           N  
ANISOU 4893  N   PRO B 337     8084   9629   8390   1409    579   -134       N  
ATOM   4894  CA  PRO B 337     -37.551  16.738  34.604  1.00 67.37           C  
ANISOU 4894  CA  PRO B 337     7912   9399   8287   1399    595    -89       C  
ATOM   4895  C   PRO B 337     -36.903  16.839  33.225  1.00 71.93           C  
ANISOU 4895  C   PRO B 337     8460   9981   8887   1328    580   -127       C  
ATOM   4896  O   PRO B 337     -37.419  17.492  32.312  1.00 69.92           O  
ANISOU 4896  O   PRO B 337     8227   9679   8662   1279    593   -125       O  
ATOM   4897  CB  PRO B 337     -38.720  17.708  34.773  1.00 71.14           C  
ANISOU 4897  CB  PRO B 337     8446   9812   8771   1393    625    -60       C  
ATOM   4898  CG  PRO B 337     -38.049  18.997  35.204  1.00 66.46           C  
ANISOU 4898  CG  PRO B 337     7882   9248   8122   1349    618   -120       C  
ATOM   4899  CD  PRO B 337     -36.744  18.614  35.905  1.00 65.28           C  
ANISOU 4899  CD  PRO B 337     7699   9182   7924   1365    588   -166       C  
ATOM   4900  N   PHE B 338     -35.767  16.165  33.054  1.00 80.23           N  
ANISOU 4900  N   PHE B 338     9464  11093   9928   1325    553   -160       N  
ATOM   4901  CA  PHE B 338     -35.159  16.072  31.729  1.00 76.35           C  
ANISOU 4901  CA  PHE B 338     8940  10606   9462   1267    540   -190       C  
ATOM   4902  C   PHE B 338     -35.979  15.196  30.793  1.00 79.62           C  
ANISOU 4902  C   PHE B 338     9340  10969   9941   1278    551   -140       C  
ATOM   4903  O   PHE B 338     -35.834  15.305  29.572  1.00 77.52           O  
ANISOU 4903  O   PHE B 338     9063  10687   9705   1225    547   -155       O  
ATOM   4904  CB  PHE B 338     -33.732  15.541  31.846  1.00 75.00           C  
ANISOU 4904  CB  PHE B 338     8721  10514   9260   1265    509   -237       C  
ATOM   4905  CG  PHE B 338     -32.789  16.490  32.531  1.00 77.77           C  
ANISOU 4905  CG  PHE B 338     9079  10919   9550   1238    493   -298       C  
ATOM   4906  CD1 PHE B 338     -32.416  17.677  31.925  1.00 74.31           C  
ANISOU 4906  CD1 PHE B 338     8659  10475   9101   1161    492   -348       C  
ATOM   4907  CD2 PHE B 338     -32.279  16.194  33.786  1.00 86.67           C  
ANISOU 4907  CD2 PHE B 338    10197  12103  10629   1289    480   -308       C  
ATOM   4908  CE1 PHE B 338     -31.545  18.548  32.553  1.00 70.51           C  
ANISOU 4908  CE1 PHE B 338     8183  10042   8564   1133    478   -407       C  
ATOM   4909  CE2 PHE B 338     -31.406  17.060  34.416  1.00 89.32           C  
ANISOU 4909  CE2 PHE B 338    10539  12491  10908   1262    464   -367       C  
ATOM   4910  CZ  PHE B 338     -31.041  18.239  33.800  1.00 80.18           C  
ANISOU 4910  CZ  PHE B 338     9397  11325   9742   1183    463   -418       C  
ATOM   4911  N   ASP B 339     -36.837  14.335  31.348  1.00 90.48           N  
ANISOU 4911  N   ASP B 339    10718  12320  11340   1344    566    -80       N  
ATOM   4912  CA  ASP B 339     -37.731  13.526  30.528  1.00 87.00           C  
ANISOU 4912  CA  ASP B 339    10267  11826  10963   1356    580    -30       C  
ATOM   4913  C   ASP B 339     -38.670  14.410  29.714  1.00 82.43           C  
ANISOU 4913  C   ASP B 339     9723  11184  10414   1310    598    -17       C  
ATOM   4914  O   ASP B 339     -38.863  14.190  28.513  1.00 78.79           O  
ANISOU 4914  O   ASP B 339     9248  10695   9995   1276    597    -13       O  
ATOM   4915  CB  ASP B 339     -38.520  12.574  31.430  1.00 93.64           C  
ANISOU 4915  CB  ASP B 339    11108  12650  11819   1437    597     31       C  
ATOM   4916  CG  ASP B 339     -39.322  11.546  30.652  1.00 94.76           C  
ANISOU 4916  CG  ASP B 339    11231  12745  12027   1454    609     80       C  
ATOM   4917  OD1 ASP B 339     -39.384  11.636  29.409  1.00 90.36           O  
ANISOU 4917  OD1 ASP B 339    10665  12165  11504   1402    605     70       O  
ATOM   4918  OD2 ASP B 339     -39.893  10.638  31.292  1.00101.06           O1-
ANISOU 4918  OD2 ASP B 339    12025  13531  12843   1518    624    128       O1-
ATOM   4919  N   GLU B 340     -39.253  15.427  30.353  1.00 84.05           N  
ANISOU 4919  N   GLU B 340     9975  11365  10596   1311    615    -11       N  
ATOM   4920  CA  GLU B 340     -40.195  16.295  29.654  1.00 78.33           C  
ANISOU 4920  CA  GLU B 340     9287  10580   9897   1273    635      5       C  
ATOM   4921  C   GLU B 340     -39.514  17.116  28.566  1.00 79.03           C  
ANISOU 4921  C   GLU B 340     9374  10675   9981   1194    624    -48       C  
ATOM   4922  O   GLU B 340     -40.148  17.450  27.560  1.00 74.61           O  
ANISOU 4922  O   GLU B 340     8825  10069   9456   1160    636    -34       O  
ATOM   4923  CB  GLU B 340     -40.899  17.218  30.650  1.00 81.50           C  
ANISOU 4923  CB  GLU B 340     9739  10956  10270   1293    657     22       C  
ATOM   4924  CG  GLU B 340     -41.101  16.613  32.030  1.00 92.99           C  
ANISOU 4924  CG  GLU B 340    11198  12429  11705   1369    662     53       C  
ATOM   4925  CD  GLU B 340     -41.595  17.627  33.044  1.00101.31           C  
ANISOU 4925  CD  GLU B 340    12305  13468  12722   1384    681     59       C  
ATOM   4926  OE1 GLU B 340     -41.590  18.836  32.730  1.00 98.43           O  
ANISOU 4926  OE1 GLU B 340    11972  13087  12340   1331    688     31       O  
ATOM   4927  OE2 GLU B 340     -41.983  17.215  34.158  1.00 97.87           O1-
ANISOU 4927  OE2 GLU B 340    11879  13034  12273   1448    691     93       O1-
ATOM   4928  N   VAL B 341     -38.237  17.448  28.744  1.00 67.01           N  
ANISOU 4928  N   VAL B 341     7836   9210   8415   1166    603   -108       N  
ATOM   4929  CA  VAL B 341     -37.547  18.301  27.780  1.00 54.84           C  
ANISOU 4929  CA  VAL B 341     6295   7675   6866   1090    596   -160       C  
ATOM   4930  C   VAL B 341     -37.068  17.487  26.583  1.00 59.46           C  
ANISOU 4930  C   VAL B 341     6835   8269   7487   1067    579   -168       C  
ATOM   4931  O   VAL B 341     -37.390  17.798  25.430  1.00 55.17           O  
ANISOU 4931  O   VAL B 341     6298   7690   6975   1025    586   -167       O  
ATOM   4932  CB  VAL B 341     -36.381  19.045  28.459  1.00 55.00           C  
ANISOU 4932  CB  VAL B 341     6317   7752   6826   1065    581   -223       C  
ATOM   4933  CG1 VAL B 341     -35.294  19.386  27.451  1.00 56.95           C  
ANISOU 4933  CG1 VAL B 341     6540   8027   7070    997    564   -281       C  
ATOM   4934  CG2 VAL B 341     -36.883  20.302  29.137  1.00 63.95           C  
ANISOU 4934  CG2 VAL B 341     7508   8862   7930   1055    602   -228       C  
ATOM   4935  N   PHE B 342     -36.298  16.427  26.838  1.00 51.48           N  
ANISOU 4935  N   PHE B 342     5781   7308   6472   1097    559   -176       N  
ATOM   4936  CA  PHE B 342     -35.660  15.691  25.751  1.00 46.49           C  
ANISOU 4936  CA  PHE B 342     5105   6691   5866   1073    542   -191       C  
ATOM   4937  C   PHE B 342     -36.646  14.774  25.036  1.00 42.09           C  
ANISOU 4937  C   PHE B 342     4538   6085   5369   1096    552   -136       C  
ATOM   4938  O   PHE B 342     -36.782  14.830  23.809  1.00 42.00           O  
ANISOU 4938  O   PHE B 342     4522   6047   5390   1056    552   -139       O  
ATOM   4939  CB  PHE B 342     -34.486  14.873  26.288  1.00 51.77           C  
ANISOU 4939  CB  PHE B 342     5730   7431   6508   1099    518   -217       C  
ATOM   4940  CG  PHE B 342     -33.252  15.681  26.585  1.00 49.14           C  
ANISOU 4940  CG  PHE B 342     5393   7155   6124   1060    501   -283       C  
ATOM   4941  CD1 PHE B 342     -33.137  16.393  27.769  1.00 56.86           C  
ANISOU 4941  CD1 PHE B 342     6395   8155   7053   1073    502   -300       C  
ATOM   4942  CD2 PHE B 342     -32.193  15.702  25.692  1.00 49.02           C  
ANISOU 4942  CD2 PHE B 342     5345   7171   6107   1010    483   -329       C  
ATOM   4943  CE1 PHE B 342     -31.996  17.126  28.047  1.00 56.50           C  
ANISOU 4943  CE1 PHE B 342     6344   8164   6961   1034    486   -364       C  
ATOM   4944  CE2 PHE B 342     -31.050  16.432  25.965  1.00 54.08           C  
ANISOU 4944  CE2 PHE B 342     5978   7866   6702    972    468   -392       C  
ATOM   4945  CZ  PHE B 342     -30.951  17.143  27.144  1.00 53.79           C  
ANISOU 4945  CZ  PHE B 342     5966   7851   6619    983    468   -410       C  
ATOM   4946  N   ASN B 343     -37.339  13.920  25.791  1.00 73.25           N  
ANISOU 4946  N   ASN B 343     8483  10019   9330   1162    561    -86       N  
ATOM   4947  CA  ASN B 343     -38.201  12.890  25.221  1.00 76.41           C  
ANISOU 4947  CA  ASN B 343     8868  10378   9787   1188    570    -35       C  
ATOM   4948  C   ASN B 343     -39.439  13.454  24.537  1.00 70.95           C  
ANISOU 4948  C   ASN B 343     8208   9619   9132   1167    590     -4       C  
ATOM   4949  O   ASN B 343     -40.136  12.697  23.853  1.00 77.56           O  
ANISOU 4949  O   ASN B 343     9031  10420  10019   1177    596     32       O  
ATOM   4950  CB  ASN B 343     -38.638  11.909  26.314  1.00 83.40           C  
ANISOU 4950  CB  ASN B 343     9746  11266  10676   1265    579     10       C  
ATOM   4951  CG  ASN B 343     -37.892  10.589  26.256  1.00101.39           C  
ANISOU 4951  CG  ASN B 343    11977  13583  12964   1295    564      8       C  
ATOM   4952  OD1 ASN B 343     -38.382   9.621  25.676  1.00110.93           O  
ANISOU 4952  OD1 ASN B 343    13166  14763  14220   1311    570     42       O  
ATOM   4953  ND2 ASN B 343     -36.712  10.536  26.880  1.00106.17           N  
ANISOU 4953  ND2 ASN B 343    12563  14254  13522   1303    546    -30       N  
ATOM   4954  N   ALA B 344     -39.712  14.752  24.697  1.00 51.66           N  
ANISOU 4954  N   ALA B 344     5806   7158   6665   1138    602    -17       N  
ATOM   4955  CA  ALA B 344     -41.012  15.333  24.379  1.00 39.33           C  
ANISOU 4955  CA  ALA B 344     4280   5534   5131   1132    625     21       C  
ATOM   4956  C   ALA B 344     -41.480  14.967  22.975  1.00 41.67           C  
ANISOU 4956  C   ALA B 344     4561   5795   5478   1104    625     36       C  
ATOM   4957  O   ALA B 344     -40.680  14.781  22.053  1.00 53.26           O  
ANISOU 4957  O   ALA B 344     6003   7284   6951   1066    608      1       O  
ATOM   4958  CB  ALA B 344     -40.959  16.855  24.525  1.00 40.64           C  
ANISOU 4958  CB  ALA B 344     4490   5693   5260   1092    636     -8       C  
ATOM   4959  N   THR B 345     -42.805  14.874  22.827  1.00 49.42           N  
ANISOU 4959  N   THR B 345     5559   6722   6498   1124    644     88       N  
ATOM   4960  CA  THR B 345     -43.401  14.453  21.563  1.00 44.05           C  
ANISOU 4960  CA  THR B 345     4863   6006   5867   1105    644    108       C  
ATOM   4961  C   THR B 345     -43.063  15.420  20.437  1.00 49.20           C  
ANISOU 4961  C   THR B 345     5528   6652   6513   1039    640     70       C  
ATOM   4962  O   THR B 345     -42.563  15.013  19.382  1.00 47.93           O  
ANISOU 4962  O   THR B 345     5340   6501   6370   1009    625     49       O  
ATOM   4963  CB  THR B 345     -44.918  14.334  21.720  1.00 38.72           C  
ANISOU 4963  CB  THR B 345     4206   5276   5230   1138    667    170       C  
ATOM   4964  OG1 THR B 345     -45.233  13.227  22.574  1.00 48.34           O  
ANISOU 4964  OG1 THR B 345     5406   6496   6464   1199    670    207       O  
ATOM   4965  CG2 THR B 345     -45.583  14.139  20.366  1.00 37.84           C  
ANISOU 4965  CG2 THR B 345     4084   5128   5166   1111    666    185       C  
ATOM   4966  N   ARG B 346     -43.324  16.709  20.643  1.00 43.68           N  
ANISOU 4966  N   ARG B 346     4872   5938   5788   1017    656     62       N  
ATOM   4967  CA  ARG B 346     -43.097  17.727  19.626  1.00 38.10           C  
ANISOU 4967  CA  ARG B 346     4182   5220   5073    957    659     30       C  
ATOM   4968  C   ARG B 346     -42.232  18.826  20.218  1.00 37.88           C  
ANISOU 4968  C   ARG B 346     4180   5221   4990    929    661    -18       C  
ATOM   4969  O   ARG B 346     -42.578  19.401  21.256  1.00 43.80           O  
ANISOU 4969  O   ARG B 346     4962   5966   5715    951    676     -7       O  
ATOM   4970  CB  ARG B 346     -44.420  18.304  19.112  1.00 38.74           C  
ANISOU 4970  CB  ARG B 346     4294   5244   5180    953    682     70       C  
ATOM   4971  CG  ARG B 346     -44.275  19.656  18.429  1.00 35.63           C  
ANISOU 4971  CG  ARG B 346     3934   4838   4766    899    693     40       C  
ATOM   4972  CD  ARG B 346     -45.621  20.216  17.998  1.00 32.93           C  
ANISOU 4972  CD  ARG B 346     3623   4440   4447    902    717     84       C  
ATOM   4973  NE  ARG B 346     -46.136  19.532  16.819  1.00 34.38           N  
ANISOU 4973  NE  ARG B 346     3781   4604   4678    897    709    105       N  
ATOM   4974  CZ  ARG B 346     -47.015  18.541  16.851  1.00 31.35           C  
ANISOU 4974  CZ  ARG B 346     3376   4200   4335    936    707    152       C  
ATOM   4975  NH1 ARG B 346     -47.522  18.103  17.991  1.00 31.94           N  
ANISOU 4975  NH1 ARG B 346     3453   4271   4413    986    715    186       N  
ATOM   4976  NH2 ARG B 346     -47.395  17.973  15.712  1.00 31.11           N  
ANISOU 4976  NH2 ARG B 346     3322   4154   4346    925    698    164       N  
ATOM   4977  N   PHE B 347     -41.115  19.118  19.561  1.00 40.91           N  
ANISOU 4977  N   PHE B 347     4550   5636   5358    881    647    -72       N  
ATOM   4978  CA  PHE B 347     -40.257  20.205  19.992  1.00 40.56           C  
ANISOU 4978  CA  PHE B 347     4528   5618   5264    846    649   -122       C  
ATOM   4979  C   PHE B 347     -40.777  21.533  19.448  1.00 34.98           C  
ANISOU 4979  C   PHE B 347     3867   4872   4553    807    674   -126       C  
ATOM   4980  O   PHE B 347     -41.639  21.584  18.567  1.00 34.63           O  
ANISOU 4980  O   PHE B 347     3831   4785   4542    801    685    -95       O  
ATOM   4981  CB  PHE B 347     -38.819  19.965  19.538  1.00 38.20           C  
ANISOU 4981  CB  PHE B 347     4193   5371   4951    811    625   -178       C  
ATOM   4982  CG  PHE B 347     -38.001  19.166  20.512  1.00 41.71           C  
ANISOU 4982  CG  PHE B 347     4606   5869   5373    845    604   -192       C  
ATOM   4983  CD1 PHE B 347     -38.505  18.002  21.068  1.00 45.03           C  
ANISOU 4983  CD1 PHE B 347     5005   6288   5814    904    600   -148       C  
ATOM   4984  CD2 PHE B 347     -36.726  19.575  20.866  1.00 44.04           C  
ANISOU 4984  CD2 PHE B 347     4891   6217   5627    817    591   -250       C  
ATOM   4985  CE1 PHE B 347     -37.755  17.264  21.962  1.00 43.22           C  
ANISOU 4985  CE1 PHE B 347     4748   6111   5564    939    583   -160       C  
ATOM   4986  CE2 PHE B 347     -35.970  18.840  21.759  1.00 43.56           C  
ANISOU 4986  CE2 PHE B 347     4798   6208   5543    850    571   -262       C  
ATOM   4987  CZ  PHE B 347     -36.486  17.683  22.308  1.00 43.36           C  
ANISOU 4987  CZ  PHE B 347     4755   6183   5538    913    568   -216       C  
ATOM   4988  N   ALA B 348     -40.249  22.620  19.996  1.00 33.25           N  
ANISOU 4988  N   ALA B 348     3677   4665   4290    780    684   -163       N  
ATOM   4989  CA  ALA B 348     -40.635  23.947  19.547  1.00 31.78           C  
ANISOU 4989  CA  ALA B 348     3538   4443   4094    741    711   -171       C  
ATOM   4990  C   ALA B 348     -39.932  24.301  18.243  1.00 41.21           C  
ANISOU 4990  C   ALA B 348     4721   5641   5295    683    707   -210       C  
ATOM   4991  O   ALA B 348     -38.850  23.791  17.935  1.00 47.06           O  
ANISOU 4991  O   ALA B 348     5424   6424   6033    665    683   -248       O  
ATOM   4992  CB  ALA B 348     -40.309  24.992  20.613  1.00 34.23           C  
ANISOU 4992  CB  ALA B 348     3886   4764   4355    732    724   -199       C  
ATOM   4993  N   SER B 349     -40.569  25.172  17.464  1.00 36.08           N  
ANISOU 4993  N   SER B 349     4106   4947   4655    657    732   -200       N  
ATOM   4994  CA  SER B 349     -39.880  25.790  16.342  1.00 34.43           C  
ANISOU 4994  CA  SER B 349     3899   4740   4444    599    735   -241       C  
ATOM   4995  C   SER B 349     -38.738  26.648  16.869  1.00 40.83           C  
ANISOU 4995  C   SER B 349     4721   5583   5210    560    737   -303       C  
ATOM   4996  O   SER B 349     -38.839  27.249  17.942  1.00 44.05           O  
ANISOU 4996  O   SER B 349     5158   5992   5586    570    750   -307       O  
ATOM   4997  CB  SER B 349     -40.850  26.633  15.514  1.00 39.29           C  
ANISOU 4997  CB  SER B 349     4554   5301   5074    584    765   -215       C  
ATOM   4998  OG  SER B 349     -41.963  25.863  15.092  1.00 41.06           O  
ANISOU 4998  OG  SER B 349     4766   5496   5339    621    763   -158       O  
ATOM   4999  N   VAL B 350     -37.636  26.691  16.117  1.00 51.26           N  
ANISOU 4999  N   VAL B 350     6018   6932   6528    516    725   -351       N  
ATOM   5000  CA  VAL B 350     -36.432  27.347  16.620  1.00 43.29           C  
ANISOU 5000  CA  VAL B 350     5009   5961   5478    478    723   -413       C  
ATOM   5001  C   VAL B 350     -36.646  28.843  16.813  1.00 41.19           C  
ANISOU 5001  C   VAL B 350     4800   5664   5185    445    758   -430       C  
ATOM   5002  O   VAL B 350     -36.028  29.453  17.695  1.00 41.71           O  
ANISOU 5002  O   VAL B 350     4880   5755   5214    430    761   -469       O  
ATOM   5003  CB  VAL B 350     -35.231  27.045  15.702  1.00 47.39           C  
ANISOU 5003  CB  VAL B 350     5488   6515   6004    437    704   -459       C  
ATOM   5004  CG1 VAL B 350     -35.286  27.877  14.436  1.00 45.07           C  
ANISOU 5004  CG1 VAL B 350     5217   6185   5721    390    728   -471       C  
ATOM   5005  CG2 VAL B 350     -33.935  27.313  16.446  1.00 43.89           C  
ANISOU 5005  CG2 VAL B 350     5029   6126   5522    412    690   -519       C  
ATOM   5006  N   TYR B 351     -37.515  29.462  16.011  1.00 42.52           N  
ANISOU 5006  N   TYR B 351     5003   5780   5371    435    787   -402       N  
ATOM   5007  CA  TYR B 351     -37.820  30.875  16.223  1.00 51.95           C  
ANISOU 5007  CA  TYR B 351     6256   6941   6541    409    825   -412       C  
ATOM   5008  C   TYR B 351     -38.573  31.081  17.533  1.00 50.30           C  
ANISOU 5008  C   TYR B 351     6080   6721   6313    450    836   -383       C  
ATOM   5009  O   TYR B 351     -38.369  32.087  18.223  1.00 50.52           O  
ANISOU 5009  O   TYR B 351     6146   6745   6306    431    857   -410       O  
ATOM   5010  CB  TYR B 351     -38.617  31.426  15.038  1.00 41.89           C  
ANISOU 5010  CB  TYR B 351     5011   5614   5290    395    854   -385       C  
ATOM   5011  CG  TYR B 351     -40.117  31.285  15.173  1.00 44.90           C  
ANISOU 5011  CG  TYR B 351     5417   5952   5692    443    868   -316       C  
ATOM   5012  CD1 TYR B 351     -40.757  30.108  14.809  1.00 46.69           C  
ANISOU 5012  CD1 TYR B 351     5609   6176   5956    483    846   -270       C  
ATOM   5013  CD2 TYR B 351     -40.894  32.330  15.658  1.00 48.36           C  
ANISOU 5013  CD2 TYR B 351     5911   6351   6111    448    905   -296       C  
ATOM   5014  CE1 TYR B 351     -42.126  29.973  14.929  1.00 44.83           C  
ANISOU 5014  CE1 TYR B 351     5391   5902   5739    526    860   -208       C  
ATOM   5015  CE2 TYR B 351     -42.264  32.203  15.784  1.00 52.38           C  
ANISOU 5015  CE2 TYR B 351     6440   6822   6639    493    919   -232       C  
ATOM   5016  CZ  TYR B 351     -42.875  31.023  15.417  1.00 42.40           C  
ANISOU 5016  CZ  TYR B 351     5138   5557   5413    531    895   -188       C  
ATOM   5017  OH  TYR B 351     -44.239  30.894  15.538  1.00 52.28           O  
ANISOU 5017  OH  TYR B 351     6407   6772   6684    574    909   -125       O  
ATOM   5018  N   ALA B 352     -39.441  30.137  17.889  1.00 41.36           N  
ANISOU 5018  N   ALA B 352     4932   5580   5203    507    824   -328       N  
ATOM   5019  CA  ALA B 352     -40.202  30.155  19.136  1.00 35.00           C  
ANISOU 5019  CA  ALA B 352     4151   4763   4382    554    832   -294       C  
ATOM   5020  C   ALA B 352     -39.635  29.165  20.142  1.00 35.60           C  
ANISOU 5020  C   ALA B 352     4189   4891   4448    588    799   -302       C  
ATOM   5021  O   ALA B 352     -40.386  28.454  20.815  1.00 35.05           O  
ANISOU 5021  O   ALA B 352     4114   4815   4390    644    794   -255       O  
ATOM   5022  CB  ALA B 352     -41.674  29.865  18.865  1.00 29.10           C  
ANISOU 5022  CB  ALA B 352     3418   3968   3669    596    847   -222       C  
ATOM   5023  N   TRP B 353     -38.306  29.093  20.235  1.00 46.21           N  
ANISOU 5023  N   TRP B 353     5504   6285   5770    557    777   -361       N  
ATOM   5024  CA  TRP B 353     -37.639  28.027  20.974  1.00 44.78           C  
ANISOU 5024  CA  TRP B 353     5276   6158   5580    588    742   -371       C  
ATOM   5025  C   TRP B 353     -38.132  27.946  22.413  1.00 42.45           C  
ANISOU 5025  C   TRP B 353     5001   5867   5262    638    745   -346       C  
ATOM   5026  O   TRP B 353     -38.270  28.963  23.099  1.00 45.26           O  
ANISOU 5026  O   TRP B 353     5401   6210   5585    629    767   -359       O  
ATOM   5027  CB  TRP B 353     -36.124  28.239  20.951  1.00 44.99           C  
ANISOU 5027  CB  TRP B 353     5276   6238   5579    541    724   -443       C  
ATOM   5028  CG  TRP B 353     -35.688  29.645  21.257  1.00 48.95           C  
ANISOU 5028  CG  TRP B 353     5820   6737   6043    493    746   -491       C  
ATOM   5029  CD1 TRP B 353     -35.589  30.683  20.377  1.00 52.58           C  
ANISOU 5029  CD1 TRP B 353     6308   7166   6504    438    773   -515       C  
ATOM   5030  CD2 TRP B 353     -35.284  30.163  22.532  1.00 53.01           C  
ANISOU 5030  CD2 TRP B 353     6352   7278   6512    496    746   -521       C  
ATOM   5031  NE1 TRP B 353     -35.151  31.813  21.022  1.00 54.63           N  
ANISOU 5031  NE1 TRP B 353     6603   7430   6724    405    790   -558       N  
ATOM   5032  CE2 TRP B 353     -34.956  31.521  22.346  1.00 57.62           C  
ANISOU 5032  CE2 TRP B 353     6976   7845   7073    439    773   -564       C  
ATOM   5033  CE3 TRP B 353     -35.167  29.610  23.811  1.00 54.58           C  
ANISOU 5033  CE3 TRP B 353     6539   7514   6686    542    727   -517       C  
ATOM   5034  CZ2 TRP B 353     -34.522  32.333  23.391  1.00 64.54           C  
ANISOU 5034  CZ2 TRP B 353     7879   8739   7904    424    780   -605       C  
ATOM   5035  CZ3 TRP B 353     -34.736  30.419  24.847  1.00 52.30           C  
ANISOU 5035  CZ3 TRP B 353     6277   7245   6350    530    732   -556       C  
ATOM   5036  CH2 TRP B 353     -34.419  31.766  24.631  1.00 56.39           C  
ANISOU 5036  CH2 TRP B 353     6833   7745   6847    470    758   -600       C  
ATOM   5037  N   ASN B 354     -38.400  26.723  22.860  1.00 49.04           N  
ANISOU 5037  N   ASN B 354     5802   6718   6113    694    725   -310       N  
ATOM   5038  CA  ASN B 354     -38.877  26.480  24.209  1.00 47.90           C  
ANISOU 5038  CA  ASN B 354     5671   6578   5949    749    726   -282       C  
ATOM   5039  C   ASN B 354     -37.770  26.734  25.228  1.00 54.80           C  
ANISOU 5039  C   ASN B 354     6540   7508   6773    741    710   -336       C  
ATOM   5040  O   ASN B 354     -36.578  26.666  24.923  1.00 61.23           O  
ANISOU 5040  O   ASN B 354     7321   8368   7574    705    689   -390       O  
ATOM   5041  CB  ASN B 354     -39.381  25.042  24.342  1.00 53.59           C  
ANISOU 5041  CB  ASN B 354     6355   7302   6704    809    710   -231       C  
ATOM   5042  CG  ASN B 354     -40.702  24.951  25.072  1.00 63.85           C  
ANISOU 5042  CG  ASN B 354     7685   8561   8014    864    730   -168       C  
ATOM   5043  OD1 ASN B 354     -41.729  25.421  24.582  1.00 52.61           O  
ANISOU 5043  OD1 ASN B 354     6292   7084   6613    862    755   -132       O  
ATOM   5044  ND2 ASN B 354     -40.685  24.338  26.250  1.00 71.46           N  
ANISOU 5044  ND2 ASN B 354     8640   9550   8961    917    721   -154       N  
ATOM   5045  N   ARG B 355     -38.185  27.042  26.454  1.00 55.69           N  
ANISOU 5045  N   ARG B 355     6684   7619   6857    777    720   -322       N  
ATOM   5046  CA  ARG B 355     -37.268  27.155  27.583  1.00 55.89           C  
ANISOU 5046  CA  ARG B 355     6704   7699   6833    782    703   -367       C  
ATOM   5047  C   ARG B 355     -37.941  26.547  28.802  1.00 54.73           C  
ANISOU 5047  C   ARG B 355     6564   7553   6677    857    703   -321       C  
ATOM   5048  O   ARG B 355     -39.051  26.949  29.163  1.00 56.01           O  
ANISOU 5048  O   ARG B 355     6770   7668   6844    883    731   -276       O  
ATOM   5049  CB  ARG B 355     -36.878  28.611  27.856  1.00 50.05           C  
ANISOU 5049  CB  ARG B 355     6009   6956   6053    731    722   -417       C  
ATOM   5050  CG  ARG B 355     -36.111  28.799  29.157  1.00 49.43           C  
ANISOU 5050  CG  ARG B 355     5930   6930   5920    742    706   -458       C  
ATOM   5051  CD  ARG B 355     -35.275  30.066  29.141  1.00 59.97           C  
ANISOU 5051  CD  ARG B 355     7289   8278   7218    674    714   -529       C  
ATOM   5052  NE  ARG B 355     -33.958  29.845  28.555  1.00 60.58           N  
ANISOU 5052  NE  ARG B 355     7317   8408   7293    628    687   -586       N  
ATOM   5053  CZ  ARG B 355     -32.930  30.670  28.694  1.00 62.60           C  
ANISOU 5053  CZ  ARG B 355     7575   8696   7514    574    683   -656       C  
ATOM   5054  NH1 ARG B 355     -33.026  31.781  29.406  1.00 61.03           N  
ANISOU 5054  NH1 ARG B 355     7426   8484   7279    555    704   -681       N  
ATOM   5055  NH2 ARG B 355     -31.775  30.373  28.104  1.00 64.28           N  
ANISOU 5055  NH2 ARG B 355     7738   8956   7730    536    659   -704       N  
ATOM   5056  N   LYS B 356     -37.276  25.581  29.429  1.00 48.48           N  
ANISOU 5056  N   LYS B 356     5730   6817   5872    892    674   -329       N  
ATOM   5057  CA  LYS B 356     -37.788  24.917  30.623  1.00 50.99           C  
ANISOU 5057  CA  LYS B 356     6051   7143   6179    966    673   -288       C  
ATOM   5058  C   LYS B 356     -36.806  25.155  31.760  1.00 57.46           C  
ANISOU 5058  C   LYS B 356     6867   8024   6940    972    654   -338       C  
ATOM   5059  O   LYS B 356     -35.725  24.557  31.789  1.00 64.24           O  
ANISOU 5059  O   LYS B 356     7679   8944   7786    968    624   -374       O  
ATOM   5060  CB  LYS B 356     -37.997  23.424  30.376  1.00 40.66           C  
ANISOU 5060  CB  LYS B 356     4696   5843   4911   1014    657   -245       C  
ATOM   5061  CG  LYS B 356     -38.403  22.639  31.613  1.00 51.70           C  
ANISOU 5061  CG  LYS B 356     6091   7254   6297   1093    656   -205       C  
ATOM   5062  CD  LYS B 356     -39.648  23.224  32.259  1.00 59.55           C  
ANISOU 5062  CD  LYS B 356     7141   8194   7290   1124    688   -158       C  
ATOM   5063  CE  LYS B 356     -40.399  22.173  33.057  1.00 60.08           C  
ANISOU 5063  CE  LYS B 356     7201   8254   7374   1206    693    -97       C  
ATOM   5064  NZ  LYS B 356     -40.351  20.838  32.399  1.00 74.08           N  
ANISOU 5064  NZ  LYS B 356     8921  10033   9192   1226    678    -72       N  
ATOM   5065  N   ARG B 357     -37.178  26.033  32.688  1.00 51.75           N  
ANISOU 5065  N   ARG B 357     6195   7288   6182    980    672   -340       N  
ATOM   5066  CA  ARG B 357     -36.360  26.258  33.869  1.00 53.14           C  
ANISOU 5066  CA  ARG B 357     6371   7520   6299    992    656   -384       C  
ATOM   5067  C   ARG B 357     -36.346  25.011  34.743  1.00 54.09           C  
ANISOU 5067  C   ARG B 357     6459   7678   6414   1069    637   -353       C  
ATOM   5068  O   ARG B 357     -37.379  24.373  34.962  1.00 49.61           O  
ANISOU 5068  O   ARG B 357     5900   7073   5875   1126    651   -286       O  
ATOM   5069  CB  ARG B 357     -36.885  27.454  34.662  1.00 58.44           C  
ANISOU 5069  CB  ARG B 357     7108   8161   6936    988    682   -388       C  
ATOM   5070  CG  ARG B 357     -35.930  27.948  35.733  1.00 56.77           C  
ANISOU 5070  CG  ARG B 357     6901   8008   6660    981    665   -448       C  
ATOM   5071  CD  ARG B 357     -36.647  28.226  37.040  1.00 63.41           C  
ANISOU 5071  CD  ARG B 357     7790   8834   7469   1036    682   -420       C  
ATOM   5072  NE  ARG B 357     -35.786  28.929  37.984  1.00 71.07           N  
ANISOU 5072  NE  ARG B 357     8773   9853   8376   1019    669   -483       N  
ATOM   5073  CZ  ARG B 357     -35.953  30.193  38.349  1.00 69.48           C  
ANISOU 5073  CZ  ARG B 357     8628   9627   8144    986    692   -509       C  
ATOM   5074  NH1 ARG B 357     -36.941  30.926  37.868  1.00 59.76           N  
ANISOU 5074  NH1 ARG B 357     7446   8322   6937    968    730   -476       N  
ATOM   5075  NH2 ARG B 357     -35.103  30.735  39.217  1.00 77.01           N  
ANISOU 5075  NH2 ARG B 357     9589  10632   9041    971    676   -570       N  
ATOM   5076  N   ILE B 358     -35.163  24.663  35.242  1.00 62.86           N  
ANISOU 5076  N   ILE B 358     7533   8863   7489   1071    605   -400       N  
ATOM   5077  CA  ILE B 358     -34.966  23.472  36.060  1.00 69.50           C  
ANISOU 5077  CA  ILE B 358     8338   9748   8319   1143    586   -377       C  
ATOM   5078  C   ILE B 358     -34.374  23.911  37.391  1.00 69.76           C  
ANISOU 5078  C   ILE B 358     8386   9834   8287   1162    573   -415       C  
ATOM   5079  O   ILE B 358     -33.278  24.486  37.428  1.00 71.74           O  
ANISOU 5079  O   ILE B 358     8623  10133   8500   1113    554   -485       O  
ATOM   5080  CB  ILE B 358     -34.058  22.449  35.359  1.00 62.77           C  
ANISOU 5080  CB  ILE B 358     7420   8942   7486   1136    557   -393       C  
ATOM   5081  CG1 ILE B 358     -34.750  21.898  34.107  1.00 59.56           C  
ANISOU 5081  CG1 ILE B 358     7000   8482   7146   1127    569   -349       C  
ATOM   5082  CG2 ILE B 358     -33.666  21.338  36.317  1.00 69.57           C  
ANISOU 5082  CG2 ILE B 358     8247   9861   8327   1209    536   -380       C  
ATOM   5083  CD1 ILE B 358     -34.314  20.501  33.716  1.00 68.67           C  
ANISOU 5083  CD1 ILE B 358     8095   9668   8327   1157    548   -333       C  
ATOM   5084  N   SER B 359     -35.094  23.643  38.480  1.00 67.70           N  
ANISOU 5084  N   SER B 359     8151   9562   8010   1232    585   -372       N  
ATOM   5085  CA  SER B 359     -34.664  24.083  39.799  1.00 77.45           C  
ANISOU 5085  CA  SER B 359     9405  10841   9180   1256    576   -404       C  
ATOM   5086  C   SER B 359     -35.154  23.105  40.856  1.00 86.43           C  
ANISOU 5086  C   SER B 359    10540  11991  10310   1352    577   -350       C  
ATOM   5087  O   SER B 359     -36.189  22.454  40.690  1.00 81.17           O  
ANISOU 5087  O   SER B 359     9880  11274   9688   1396    598   -280       O  
ATOM   5088  CB  SER B 359     -35.178  25.493  40.116  1.00 77.25           C  
ANISOU 5088  CB  SER B 359     9447  10773   9132   1223    602   -418       C  
ATOM   5089  OG  SER B 359     -34.841  26.408  39.087  1.00 75.92           O  
ANISOU 5089  OG  SER B 359     9285  10584   8975   1136    607   -461       O  
ATOM   5090  N   ASN B 360     -34.393  23.017  41.949  1.00 90.04           N  
ANISOU 5090  N   ASN B 360    10987  12515  10709   1383    554   -383       N  
ATOM   5091  CA  ASN B 360     -34.768  22.254  43.141  1.00 87.52           C  
ANISOU 5091  CA  ASN B 360    10672  12213  10370   1475    556   -340       C  
ATOM   5092  C   ASN B 360     -35.010  20.778  42.810  1.00 90.65           C  
ANISOU 5092  C   ASN B 360    11024  12608  10811   1530    555   -284       C  
ATOM   5093  O   ASN B 360     -36.081  20.223  43.063  1.00 89.10           O  
ANISOU 5093  O   ASN B 360    10844  12363  10645   1588    580   -215       O  
ATOM   5094  CB  ASN B 360     -35.993  22.876  43.821  1.00 86.31           C  
ANISOU 5094  CB  ASN B 360    10585  11996  10211   1507    592   -296       C  
ATOM   5095  CG  ASN B 360     -35.824  24.360  44.084  1.00 92.35           C  
ANISOU 5095  CG  ASN B 360    11399  12755  10935   1450    598   -348       C  
ATOM   5096  OD1 ASN B 360     -36.550  25.186  43.532  1.00 78.72           O  
ANISOU 5096  OD1 ASN B 360     9714  10963   9232   1410    626   -336       O  
ATOM   5097  ND2 ASN B 360     -34.862  24.705  44.932  1.00 92.74           N  
ANISOU 5097  ND2 ASN B 360    11444  12873  10921   1448    573   -407       N  
ATOM   5098  N   CYS B 361     -33.985  20.145  42.245  1.00 97.91           N  
ANISOU 5098  N   CYS B 361    11885  13581  11735   1510    526   -317       N  
ATOM   5099  CA  CYS B 361     -34.081  18.734  41.895  1.00 99.30           C  
ANISOU 5099  CA  CYS B 361    12017  13760  11952   1558    524   -271       C  
ATOM   5100  C   CYS B 361     -32.685  18.161  41.693  1.00 98.08           C  
ANISOU 5100  C   CYS B 361    11801  13687  11777   1545    487   -320       C  
ATOM   5101  O   CYS B 361     -31.722  18.899  41.472  1.00101.18           O  
ANISOU 5101  O   CYS B 361    12184  14122  12140   1483    465   -388       O  
ATOM   5102  CB  CYS B 361     -34.937  18.531  40.640  1.00 97.97           C  
ANISOU 5102  CB  CYS B 361    11850  13518  11856   1529    545   -229       C  
ATOM   5103  SG  CYS B 361     -34.437  19.516  39.213  1.00 92.72           S  
ANISOU 5103  SG  CYS B 361    11181  12838  11211   1417    538   -285       S  
ATOM   5104  N   VAL B 362     -32.583  16.833  41.764  1.00 82.06           N  
ANISOU 5104  N   VAL B 362     9732  11681   9766   1605    482   -284       N  
ATOM   5105  CA  VAL B 362     -31.318  16.172  41.457  1.00 85.83           C  
ANISOU 5105  CA  VAL B 362    10149  12231  10230   1596    450   -322       C  
ATOM   5106  C   VAL B 362     -31.234  15.967  39.951  1.00 79.01           C  
ANISOU 5106  C   VAL B 362     9259  11338   9424   1537    450   -325       C  
ATOM   5107  O   VAL B 362     -32.172  15.460  39.324  1.00 76.22           O  
ANISOU 5107  O   VAL B 362     8912  10921   9128   1549    472   -270       O  
ATOM   5108  CB  VAL B 362     -31.165  14.843  42.224  1.00 85.53           C  
ANISOU 5108  CB  VAL B 362    10080  12235  10182   1689    446   -285       C  
ATOM   5109  CG1 VAL B 362     -30.943  15.105  43.717  1.00 76.43           C  
ANISOU 5109  CG1 VAL B 362     8947  11131   8961   1743    438   -298       C  
ATOM   5110  CG2 VAL B 362     -32.323  13.869  41.967  1.00 80.15           C  
ANISOU 5110  CG2 VAL B 362     9405  11487   9561   1741    476   -204       C  
ATOM   5111  N   ALA B 363     -30.120  16.393  39.362  1.00 76.64           N  
ANISOU 5111  N   ALA B 363     8930  11084   9108   1471    424   -390       N  
ATOM   5112  CA  ALA B 363     -29.931  16.379  37.913  1.00 79.92           C  
ANISOU 5112  CA  ALA B 363     9322  11473   9570   1406    423   -402       C  
ATOM   5113  C   ALA B 363     -29.012  15.214  37.562  1.00 85.76           C  
ANISOU 5113  C   ALA B 363     9999  12268  10316   1426    401   -408       C  
ATOM   5114  O   ALA B 363     -27.788  15.343  37.550  1.00 92.46           O  
ANISOU 5114  O   ALA B 363    10812  13187  11131   1398    373   -465       O  
ATOM   5115  CB  ALA B 363     -29.369  17.710  37.430  1.00 77.76           C  
ANISOU 5115  CB  ALA B 363     9062  11204   9278   1317    415   -468       C  
ATOM   5116  N   ASP B 364     -29.617  14.063  37.273  1.00 90.83           N  
ANISOU 5116  N   ASP B 364    10627  12880  11004   1475    415   -348       N  
ATOM   5117  CA  ASP B 364     -28.875  12.883  36.832  1.00 94.59           C  
ANISOU 5117  CA  ASP B 364    11048  13398  11495   1495    400   -345       C  
ATOM   5118  C   ASP B 364     -28.590  13.043  35.345  1.00 98.20           C  
ANISOU 5118  C   ASP B 364    11486  13832  11993   1420    395   -367       C  
ATOM   5119  O   ASP B 364     -29.374  12.633  34.488  1.00 93.23           O  
ANISOU 5119  O   ASP B 364    10863  13141  11421   1415    414   -326       O  
ATOM   5120  CB  ASP B 364     -29.661  11.610  37.121  1.00102.11           C  
ANISOU 5120  CB  ASP B 364    11996  14322  12480   1576    420   -272       C  
ATOM   5121  CG  ASP B 364     -28.820  10.357  36.966  1.00108.27           C  
ANISOU 5121  CG  ASP B 364    12720  15155  13262   1612    405   -270       C  
ATOM   5122  OD1 ASP B 364     -27.609  10.479  36.693  1.00100.49           O  
ANISOU 5122  OD1 ASP B 364    11698  14233  12249   1577    378   -324       O  
ATOM   5123  OD2 ASP B 364     -29.373   9.247  37.115  1.00106.65           O1-
ANISOU 5123  OD2 ASP B 364    12508  14928  13086   1675    423   -213       O1-
ATOM   5124  N   TYR B 365     -27.445  13.655  35.035  1.00 99.56           N  
ANISOU 5124  N   TYR B 365    11636  14057  12136   1362    371   -434       N  
ATOM   5125  CA  TYR B 365     -27.079  13.906  33.647  1.00 89.34           C  
ANISOU 5125  CA  TYR B 365    10324  12744  10875   1288    367   -461       C  
ATOM   5126  C   TYR B 365     -26.668  12.641  32.905  1.00 98.96           C  
ANISOU 5126  C   TYR B 365    11494  13978  12128   1306    360   -442       C  
ATOM   5127  O   TYR B 365     -26.527  12.685  31.678  1.00 96.40           O  
ANISOU 5127  O   TYR B 365    11159  13630  11840   1253    360   -453       O  
ATOM   5128  CB  TYR B 365     -25.955  14.942  33.581  1.00 88.50           C  
ANISOU 5128  CB  TYR B 365    10207  12690  10728   1220    345   -539       C  
ATOM   5129  CG  TYR B 365     -26.364  16.316  34.068  1.00 89.24           C  
ANISOU 5129  CG  TYR B 365    10353  12759  10796   1186    355   -563       C  
ATOM   5130  CD1 TYR B 365     -27.152  17.149  33.284  1.00 83.23           C  
ANISOU 5130  CD1 TYR B 365     9632  11923  10068   1133    378   -556       C  
ATOM   5131  CD2 TYR B 365     -25.964  16.778  35.312  1.00 87.74           C  
ANISOU 5131  CD2 TYR B 365    10172  12620  10546   1207    343   -593       C  
ATOM   5132  CE1 TYR B 365     -27.525  18.405  33.730  1.00 78.06           C  
ANISOU 5132  CE1 TYR B 365     9026  11244   9389   1103    390   -576       C  
ATOM   5133  CE2 TYR B 365     -26.327  18.029  35.764  1.00 83.36           C  
ANISOU 5133  CE2 TYR B 365     9666  12040   9966   1175    353   -616       C  
ATOM   5134  CZ  TYR B 365     -27.109  18.838  34.971  1.00 75.90           C  
ANISOU 5134  CZ  TYR B 365     8762  11019   9056   1123    378   -606       C  
ATOM   5135  OH  TYR B 365     -27.474  20.085  35.425  1.00 77.56           O  
ANISOU 5135  OH  TYR B 365     9023  11204   9242   1093    391   -628       O  
ATOM   5136  N   SER B 366     -26.469  11.524  33.609  1.00127.01           N  
ANISOU 5136  N   SER B 366    15020  17569  15667   1381    355   -414       N  
ATOM   5137  CA  SER B 366     -26.211  10.257  32.936  1.00123.35           C  
ANISOU 5137  CA  SER B 366    14515  17112  15239   1405    354   -389       C  
ATOM   5138  C   SER B 366     -27.469   9.679  32.301  1.00123.60           C  
ANISOU 5138  C   SER B 366    14567  17059  15334   1421    382   -326       C  
ATOM   5139  O   SER B 366     -27.366   8.874  31.370  1.00123.01           O  
ANISOU 5139  O   SER B 366    14467  16972  15301   1415    383   -311       O  
ATOM   5140  CB  SER B 366     -25.606   9.251  33.914  1.00121.35           C  
ANISOU 5140  CB  SER B 366    14230  16927  14952   1482    343   -378       C  
ATOM   5141  OG  SER B 366     -24.288   9.627  34.273  1.00115.01           O  
ANISOU 5141  OG  SER B 366    13396  16209  14094   1462    314   -439       O  
ATOM   5142  N   VAL B 367     -28.651  10.064  32.788  1.00142.35           N  
ANISOU 5142  N   VAL B 367    16988  19378  17720   1441    404   -289       N  
ATOM   5143  CA  VAL B 367     -29.888   9.690  32.110  1.00141.05           C  
ANISOU 5143  CA  VAL B 367    16844  19130  17617   1446    430   -234       C  
ATOM   5144  C   VAL B 367     -30.006  10.424  30.779  1.00141.48           C  
ANISOU 5144  C   VAL B 367    16908  19143  17704   1364    431   -257       C  
ATOM   5145  O   VAL B 367     -30.637   9.924  29.838  1.00147.15           O  
ANISOU 5145  O   VAL B 367    17624  19808  18476   1355    443   -225       O  
ATOM   5146  CB  VAL B 367     -31.100   9.966  33.021  1.00144.37           C  
ANISOU 5146  CB  VAL B 367    17312  19505  18038   1490    454   -189       C  
ATOM   5147  CG1 VAL B 367     -32.386   9.452  32.384  1.00148.13           C  
ANISOU 5147  CG1 VAL B 367    17804  19900  18580   1501    481   -129       C  
ATOM   5148  CG2 VAL B 367     -30.895   9.326  34.384  1.00138.69           C  
ANISOU 5148  CG2 VAL B 367    16584  18831  17280   1572    454   -171       C  
ATOM   5149  N   LEU B 368     -29.385  11.603  30.666  1.00150.70           N  
ANISOU 5149  N   LEU B 368    18085  20334  18840   1302    417   -314       N  
ATOM   5150  CA  LEU B 368     -29.506  12.457  29.488  1.00147.90           C  
ANISOU 5150  CA  LEU B 368    17745  19939  18510   1224    421   -338       C  
ATOM   5151  C   LEU B 368     -28.886  11.803  28.262  1.00151.77           C  
ANISOU 5151  C   LEU B 368    18195  20438  19033   1194    410   -350       C  
ATOM   5152  O   LEU B 368     -28.875  12.386  27.175  1.00148.90           O  
ANISOU 5152  O   LEU B 368    17838  20046  18692   1131    412   -370       O  
ATOM   5153  CB  LEU B 368     -28.867  13.825  29.734  1.00142.31           C  
ANISOU 5153  CB  LEU B 368    17055  19260  17758   1168    411   -399       C  
ATOM   5154  CG  LEU B 368     -29.778  14.880  30.362  1.00139.58           C  
ANISOU 5154  CG  LEU B 368    16765  18871  17398   1165    430   -389       C  
ATOM   5155  CD1 LEU B 368     -30.121  14.514  31.793  1.00148.83           C  
ANISOU 5155  CD1 LEU B 368    17949  20061  18539   1240    434   -360       C  
ATOM   5156  CD2 LEU B 368     -29.122  16.246  30.305  1.00123.52           C  
ANISOU 5156  CD2 LEU B 368    14747  16856  15328   1096    422   -453       C  
ATOM   5157  N   TYR B 369     -28.345  10.604  28.435  1.00156.29           N  
ANISOU 5157  N   TYR B 369    18727  21051  19605   1241    400   -337       N  
ATOM   5158  CA  TYR B 369     -27.898   9.795  27.309  1.00158.25           C  
ANISOU 5158  CA  TYR B 369    18939  21302  19889   1224    394   -338       C  
ATOM   5159  C   TYR B 369     -29.034   8.860  26.920  1.00156.92           C  
ANISOU 5159  C   TYR B 369    18778  21069  19775   1261    415   -274       C  
ATOM   5160  O   TYR B 369     -29.255   7.833  27.565  1.00159.54           O  
ANISOU 5160  O   TYR B 369    19097  21408  20111   1328    422   -235       O  
ATOM   5161  CB  TYR B 369     -26.644   9.007  27.665  1.00155.87           C  
ANISOU 5161  CB  TYR B 369    18589  21080  19557   1252    373   -360       C  
ATOM   5162  CG  TYR B 369     -25.463   9.838  28.103  1.00157.70           C  
ANISOU 5162  CG  TYR B 369    18805  21381  19731   1219    349   -425       C  
ATOM   5163  CD1 TYR B 369     -25.366  10.319  29.403  1.00159.83           C  
ANISOU 5163  CD1 TYR B 369    19090  21687  19952   1248    344   -437       C  
ATOM   5164  CD2 TYR B 369     -24.433  10.124  27.220  1.00155.58           C  
ANISOU 5164  CD2 TYR B 369    18508  21144  19460   1159    333   -474       C  
ATOM   5165  CE1 TYR B 369     -24.281  11.062  29.807  1.00158.05           C  
ANISOU 5165  CE1 TYR B 369    18849  21527  19676   1216    322   -498       C  
ATOM   5166  CE2 TYR B 369     -23.342  10.870  27.615  1.00157.59           C  
ANISOU 5166  CE2 TYR B 369    18747  21463  19666   1127    312   -534       C  
ATOM   5167  CZ  TYR B 369     -23.272  11.337  28.912  1.00158.81           C  
ANISOU 5167  CZ  TYR B 369    18915  21654  19772   1154    306   -547       C  
ATOM   5168  OH  TYR B 369     -22.196  12.083  29.333  1.00154.85           O  
ANISOU 5168  OH  TYR B 369    18397  21218  19221   1121    284   -609       O  
ATOM   5169  N   ASN B 370     -29.777   9.219  25.873  1.00136.83           N  
ANISOU 5169  N   ASN B 370    16254  18461  17274   1218    427   -262       N  
ATOM   5170  CA  ASN B 370     -30.615   8.211  25.240  1.00141.18           C  
ANISOU 5170  CA  ASN B 370    16801  18961  17882   1242    442   -211       C  
ATOM   5171  C   ASN B 370     -29.784   7.220  24.434  1.00151.90           C  
ANISOU 5171  C   ASN B 370    18114  20346  19256   1239    429   -221       C  
ATOM   5172  O   ASN B 370     -30.326   6.210  23.973  1.00153.78           O  
ANISOU 5172  O   ASN B 370    18342  20550  19538   1265    440   -182       O  
ATOM   5173  CB  ASN B 370     -31.690   8.882  24.369  1.00134.62           C  
ANISOU 5173  CB  ASN B 370    16004  18056  17090   1199    457   -195       C  
ATOM   5174  CG  ASN B 370     -31.164   9.366  23.022  1.00133.06           C  
ANISOU 5174  CG  ASN B 370    15797  17854  16905   1127    447   -234       C  
ATOM   5175  OD1 ASN B 370     -29.961   9.537  22.822  1.00135.86           O  
ANISOU 5175  OD1 ASN B 370    16126  18261  17232   1098    428   -281       O  
ATOM   5176  ND2 ASN B 370     -32.082   9.602  22.091  1.00125.79           N  
ANISOU 5176  ND2 ASN B 370    14898  16870  16027   1099    459   -213       N  
ATOM   5177  N   PHE B 371     -28.498   7.521  24.232  1.00155.58           N  
ANISOU 5177  N   PHE B 371    18553  20871  19689   1205    408   -274       N  
ATOM   5178  CA  PHE B 371     -27.490   6.671  23.602  1.00153.36           C  
ANISOU 5178  CA  PHE B 371    18227  20629  19412   1202    394   -291       C  
ATOM   5179  C   PHE B 371     -27.727   6.541  22.103  1.00150.84           C  
ANISOU 5179  C   PHE B 371    17907  20265  19142   1155    398   -290       C  
ATOM   5180  O   PHE B 371     -26.852   6.064  21.373  1.00151.20           O  
ANISOU 5180  O   PHE B 371    17920  20339  19191   1138    386   -311       O  
ATOM   5181  CB  PHE B 371     -27.445   5.279  24.242  1.00156.36           C  
ANISOU 5181  CB  PHE B 371    18583  21031  19796   1279    399   -253       C  
ATOM   5182  CG  PHE B 371     -27.290   5.293  25.739  1.00158.89           C  
ANISOU 5182  CG  PHE B 371    18906  21395  20069   1334    398   -249       C  
ATOM   5183  CD1 PHE B 371     -26.064   5.567  26.325  1.00154.52           C  
ANISOU 5183  CD1 PHE B 371    18328  20921  19462   1333    376   -294       C  
ATOM   5184  CD2 PHE B 371     -28.365   4.994  26.558  1.00159.44           C  
ANISOU 5184  CD2 PHE B 371    19001  21428  20150   1390    418   -199       C  
ATOM   5185  CE1 PHE B 371     -25.922   5.566  27.704  1.00152.73           C  
ANISOU 5185  CE1 PHE B 371    18103  20736  19190   1387    374   -290       C  
ATOM   5186  CE2 PHE B 371     -28.230   4.989  27.935  1.00157.65           C  
ANISOU 5186  CE2 PHE B 371    18779  21242  19880   1444    418   -194       C  
ATOM   5187  CZ  PHE B 371     -27.008   5.278  28.508  1.00154.24           C  
ANISOU 5187  CZ  PHE B 371    18323  20889  19392   1443    395   -240       C  
ATOM   5188  N   ALA B 372     -28.877   6.998  21.630  1.00152.69           N  
ANISOU 5188  N   ALA B 372    18175  20430  19409   1135    413   -265       N  
ATOM   5189  CA  ALA B 372     -29.107   7.078  20.198  1.00146.60           C  
ANISOU 5189  CA  ALA B 372    17406  19616  18678   1085    415   -269       C  
ATOM   5190  C   ALA B 372     -28.236   8.213  19.691  1.00148.62           C  
ANISOU 5190  C   ALA B 372    17663  19899  18907   1018    402   -327       C  
ATOM   5191  O   ALA B 372     -28.385   9.345  20.170  1.00143.35           O  
ANISOU 5191  O   ALA B 372    17023  19229  18213    995    405   -346       O  
ATOM   5192  CB  ALA B 372     -30.578   7.328  19.887  1.00135.43           C  
ANISOU 5192  CB  ALA B 372    16029  18126  17304   1083    435   -228       C  
ATOM   5193  N   PRO B 373     -27.333   7.971  18.724  1.00175.17           N  
ANISOU 5193  N   PRO B 373    20997  23284  22276    984    390   -356       N  
ATOM   5194  CA  PRO B 373     -26.135   8.816  18.614  1.00170.88           C  
ANISOU 5194  CA  PRO B 373    20440  22790  21694    935    375   -416       C  
ATOM   5195  C   PRO B 373     -26.456  10.298  18.620  1.00160.18           C  
ANISOU 5195  C   PRO B 373    19124  21412  20325    886    382   -440       C  
ATOM   5196  O   PRO B 373     -26.999  10.845  17.657  1.00156.14           O  
ANISOU 5196  O   PRO B 373    18635  20850  19840    844    392   -439       O  
ATOM   5197  CB  PRO B 373     -25.515   8.382  17.278  1.00164.73           C  
ANISOU 5197  CB  PRO B 373    19636  22013  20940    901    369   -432       C  
ATOM   5198  CG  PRO B 373     -26.082   7.033  17.002  1.00164.90           C  
ANISOU 5198  CG  PRO B 373    19645  22007  21001    948    375   -384       C  
ATOM   5199  CD  PRO B 373     -27.444   7.004  17.620  1.00168.95           C  
ANISOU 5199  CD  PRO B 373    20191  22470  21531    984    392   -337       C  
ATOM   5200  N   PHE B 374     -26.110  10.950  19.724  1.00 98.11           N  
ANISOU 5200  N   PHE B 374    11270  13589  12420    891    377   -463       N  
ATOM   5201  CA  PHE B 374     -26.301  12.386  19.843  1.00 91.07           C  
ANISOU 5201  CA  PHE B 374    10415  12680  11508    845    384   -491       C  
ATOM   5202  C   PHE B 374     -25.308  13.060  18.912  1.00 90.89           C  
ANISOU 5202  C   PHE B 374    10378  12677  11478    776    377   -545       C  
ATOM   5203  O   PHE B 374     -24.099  13.007  19.153  1.00 99.15           O  
ANISOU 5203  O   PHE B 374    11391  13788  12495    767    359   -585       O  
ATOM   5204  CB  PHE B 374     -26.093  12.835  21.288  1.00 89.47           C  
ANISOU 5204  CB  PHE B 374    10220  12517  11257    870    380   -505       C  
ATOM   5205  CG  PHE B 374     -27.306  12.668  22.165  1.00 96.53           C  
ANISOU 5205  CG  PHE B 374    11146  13374  12158    923    395   -454       C  
ATOM   5206  CD1 PHE B 374     -28.578  12.889  21.668  1.00 95.14           C  
ANISOU 5206  CD1 PHE B 374    11006  13123  12019    919    416   -415       C  
ATOM   5207  CD2 PHE B 374     -27.171  12.302  23.494  1.00 97.18           C  
ANISOU 5207  CD2 PHE B 374    11222  13497  12206    979    389   -446       C  
ATOM   5208  CE1 PHE B 374     -29.692  12.739  22.474  1.00 92.05           C  
ANISOU 5208  CE1 PHE B 374    10643  12699  11635    968    431   -368       C  
ATOM   5209  CE2 PHE B 374     -28.280  12.152  24.301  1.00103.87           C  
ANISOU 5209  CE2 PHE B 374    12098  14308  13059   1029    405   -398       C  
ATOM   5210  CZ  PHE B 374     -29.543  12.375  23.792  1.00101.31           C  
ANISOU 5210  CZ  PHE B 374    11810  13910  12776   1022    426   -359       C  
ATOM   5211  N   PHE B 375     -25.811  13.662  17.831  1.00 95.52           N  
ANISOU 5211  N   PHE B 375    10990  13209  12093    730    390   -544       N  
ATOM   5212  CA  PHE B 375     -24.937  14.370  16.900  1.00 96.47           C  
ANISOU 5212  CA  PHE B 375    11102  13342  12209    664    387   -594       C  
ATOM   5213  C   PHE B 375     -23.989  15.286  17.668  1.00 99.06           C  
ANISOU 5213  C   PHE B 375    11426  13723  12490    636    379   -648       C  
ATOM   5214  O   PHE B 375     -22.771  15.264  17.458  1.00 95.50           O  
ANISOU 5214  O   PHE B 375    10940  13325  12022    610    364   -691       O  
ATOM   5215  CB  PHE B 375     -25.788  15.164  15.899  1.00 88.91           C  
ANISOU 5215  CB  PHE B 375    10185  12316  11282    623    408   -584       C  
ATOM   5216  CG  PHE B 375     -25.005  15.855  14.798  1.00 92.74           C  
ANISOU 5216  CG  PHE B 375    10665  12804  11769    557    410   -629       C  
ATOM   5217  CD1 PHE B 375     -23.617  15.817  14.726  1.00 95.84           C  
ANISOU 5217  CD1 PHE B 375    11020  13257  12139    532    394   -676       C  
ATOM   5218  CD2 PHE B 375     -25.688  16.562  13.831  1.00 92.70           C  
ANISOU 5218  CD2 PHE B 375    10695  12740  11788    520    429   -622       C  
ATOM   5219  CE1 PHE B 375     -22.942  16.466  13.714  1.00 88.70           C  
ANISOU 5219  CE1 PHE B 375    10113  12352  11239    472    398   -715       C  
ATOM   5220  CE2 PHE B 375     -25.022  17.208  12.812  1.00 91.17           C  
ANISOU 5220  CE2 PHE B 375    10500  12545  11596    462    434   -660       C  
ATOM   5221  CZ  PHE B 375     -23.646  17.162  12.753  1.00 95.77           C  
ANISOU 5221  CZ  PHE B 375    11044  13185  12158    438    419   -707       C  
ATOM   5222  N   ALA B 376     -24.527  16.061  18.605  1.00 91.34           N  
ANISOU 5222  N   ALA B 376    10483  12734  11488    642    388   -647       N  
ATOM   5223  CA  ALA B 376     -23.723  16.959  19.419  1.00 89.95           C  
ANISOU 5223  CA  ALA B 376    10307  12605  11265    617    381   -698       C  
ATOM   5224  C   ALA B 376     -23.972  16.678  20.892  1.00 88.14           C  
ANISOU 5224  C   ALA B 376    10082  12404  11005    674    374   -681       C  
ATOM   5225  O   ALA B 376     -25.123  16.602  21.330  1.00 95.79           O  
ANISOU 5225  O   ALA B 376    11082  13328  11984    711    388   -636       O  
ATOM   5226  CB  ALA B 376     -24.034  18.425  19.101  1.00 73.07           C  
ANISOU 5226  CB  ALA B 376     8214  10426   9122    557    401   -724       C  
ATOM   5227  N   PHE B 377     -22.890  16.499  21.642  1.00 76.35           N  
ANISOU 5227  N   PHE B 377     8552  10984   9472    684    352   -717       N  
ATOM   5228  CA  PHE B 377     -22.908  16.561  23.100  1.00 77.63           C  
ANISOU 5228  CA  PHE B 377     8721  11184   9593    726    345   -718       C  
ATOM   5229  C   PHE B 377     -21.720  17.401  23.556  1.00 82.44           C  
ANISOU 5229  C   PHE B 377     9313  11855  10156    683    330   -787       C  
ATOM   5230  O   PHE B 377     -20.968  17.034  24.460  1.00 97.39           O  
ANISOU 5230  O   PHE B 377    11176  13817  12012    713    308   -806       O  
ATOM   5231  CB  PHE B 377     -22.898  15.171  23.735  1.00 88.00           C  
ANISOU 5231  CB  PHE B 377    10001  12529  10904    803    332   -680       C  
ATOM   5232  CG  PHE B 377     -23.660  15.092  25.033  1.00 95.29           C  
ANISOU 5232  CG  PHE B 377    10952  13449  11807    862    338   -648       C  
ATOM   5233  CD1 PHE B 377     -23.659  16.161  25.915  1.00 94.85           C  
ANISOU 5233  CD1 PHE B 377    10924  13403  11710    847    339   -677       C  
ATOM   5234  CD2 PHE B 377     -24.382  13.957  25.367  1.00105.98           C  
ANISOU 5234  CD2 PHE B 377    12301  14784  13181    932    343   -588       C  
ATOM   5235  CE1 PHE B 377     -24.354  16.099  27.106  1.00 94.02           C  
ANISOU 5235  CE1 PHE B 377    10844  13293  11584    902    345   -647       C  
ATOM   5236  CE2 PHE B 377     -25.083  13.891  26.560  1.00110.38           C  
ANISOU 5236  CE2 PHE B 377    12884  15337  13720    988    351   -557       C  
ATOM   5237  CZ  PHE B 377     -25.068  14.964  27.429  1.00103.01           C  
ANISOU 5237  CZ  PHE B 377    11980  14415  12745    974    351   -586       C  
ATOM   5238  N   LYS B 378     -21.544  18.546  22.905  1.00 68.32           N  
ANISOU 5238  N   LYS B 378     7546  10043   8370    612    341   -826       N  
ATOM   5239  CA  LYS B 378     -20.403  19.421  23.137  1.00 74.92           C  
ANISOU 5239  CA  LYS B 378     8367  10931   9169    559    330   -896       C  
ATOM   5240  C   LYS B 378     -20.792  20.478  24.164  1.00 78.69           C  
ANISOU 5240  C   LYS B 378     8887  11400   9611    552    339   -913       C  
ATOM   5241  O   LYS B 378     -21.699  21.281  23.924  1.00 80.69           O  
ANISOU 5241  O   LYS B 378     9192  11588   9879    530    365   -898       O  
ATOM   5242  CB  LYS B 378     -19.967  20.059  21.816  1.00 72.90           C  
ANISOU 5242  CB  LYS B 378     8110  10651   8938    486    341   -928       C  
ATOM   5243  CG  LYS B 378     -18.510  20.516  21.722  1.00 84.13           C  
ANISOU 5243  CG  LYS B 378     9494  12139  10334    433    325   -998       C  
ATOM   5244  CD  LYS B 378     -18.253  21.805  22.490  1.00 84.49           C  
ANISOU 5244  CD  LYS B 378     9564  12197  10340    392    329  -1049       C  
ATOM   5245  CE  LYS B 378     -16.775  22.157  22.503  1.00 79.49           C  
ANISOU 5245  CE  LYS B 378     8887  11637   9681    345    310  -1119       C  
ATOM   5246  NZ  LYS B 378     -16.070  21.507  23.635  1.00 76.46           N  
ANISOU 5246  NZ  LYS B 378     8460  11336   9256    390    278  -1133       N  
ATOM   5247  N   CYS B 379     -20.105  20.476  25.300  1.00 72.94           N  
ANISOU 5247  N   CYS B 379     8138  10740   8836    572    318   -944       N  
ATOM   5248  CA  CYS B 379     -20.352  21.432  26.367  1.00 67.89           C  
ANISOU 5248  CA  CYS B 379     7536  10102   8157    567    323   -965       C  
ATOM   5249  C   CYS B 379     -19.267  22.501  26.384  1.00 71.52           C  
ANISOU 5249  C   CYS B 379     7985  10602   8586    496    316  -1043       C  
ATOM   5250  O   CYS B 379     -18.128  22.265  25.970  1.00 75.83           O  
ANISOU 5250  O   CYS B 379     8482  11202   9128    469    297  -1082       O  
ATOM   5251  CB  CYS B 379     -20.416  20.732  27.725  1.00 72.94           C  
ANISOU 5251  CB  CYS B 379     8164  10789   8761    643    305   -945       C  
ATOM   5252  SG  CYS B 379     -21.606  19.378  27.820  1.00 97.81           S  
ANISOU 5252  SG  CYS B 379    11320  13897  11945    731    314   -854       S  
ATOM   5253  N   TYR B 380     -19.632  23.684  26.872  1.00 74.41           N  
ANISOU 5253  N   TYR B 380     8400  10943   8931    465    333  -1066       N  
ATOM   5254  CA  TYR B 380     -18.758  24.848  26.852  1.00 76.92           C  
ANISOU 5254  CA  TYR B 380     8718  11284   9224    391    333  -1140       C  
ATOM   5255  C   TYR B 380     -18.540  25.349  28.273  1.00 87.10           C  
ANISOU 5255  C   TYR B 380    10018  12618  10458    404    321  -1173       C  
ATOM   5256  O   TYR B 380     -19.504  25.602  29.002  1.00 80.40           O  
ANISOU 5256  O   TYR B 380     9217  11734   9598    438    335  -1142       O  
ATOM   5257  CB  TYR B 380     -19.347  25.959  25.972  1.00 73.94           C  
ANISOU 5257  CB  TYR B 380     8392  10828   8875    330    370  -1144       C  
ATOM   5258  CG  TYR B 380     -19.717  25.493  24.578  1.00 75.53           C  
ANISOU 5258  CG  TYR B 380     8590  10980   9130    321    384  -1107       C  
ATOM   5259  CD1 TYR B 380     -20.900  24.799  24.344  1.00 67.82           C  
ANISOU 5259  CD1 TYR B 380     7634   9948   8185    374    396  -1034       C  
ATOM   5260  CD2 TYR B 380     -18.876  25.730  23.499  1.00 69.61           C  
ANISOU 5260  CD2 TYR B 380     7813  10237   8399    261    386  -1144       C  
ATOM   5261  CE1 TYR B 380     -21.236  24.361  23.077  1.00 65.25           C  
ANISOU 5261  CE1 TYR B 380     7304   9580   7908    366    407  -1002       C  
ATOM   5262  CE2 TYR B 380     -19.203  25.295  22.227  1.00 69.99           C  
ANISOU 5262  CE2 TYR B 380     7857  10241   8493    255    398  -1111       C  
ATOM   5263  CZ  TYR B 380     -20.385  24.613  22.022  1.00 67.59           C  
ANISOU 5263  CZ  TYR B 380     7577   9886   8220    308    407  -1041       C  
ATOM   5264  OH  TYR B 380     -20.715  24.180  20.759  1.00 64.19           O  
ANISOU 5264  OH  TYR B 380     7143   9413   7835    301    418  -1009       O  
ATOM   5265  N   GLY B 381     -17.273  25.495  28.657  1.00108.08           N  
ANISOU 5265  N   GLY B 381    12631  15354  13080    378    294  -1236       N  
ATOM   5266  CA  GLY B 381     -16.928  25.997  29.973  1.00107.22           C  
ANISOU 5266  CA  GLY B 381    12528  15296  12916    385    279  -1276       C  
ATOM   5267  C   GLY B 381     -16.906  24.933  31.051  1.00105.01           C  
ANISOU 5267  C   GLY B 381    12221  15074  12605    471    251  -1248       C  
ATOM   5268  O   GLY B 381     -16.172  25.055  32.036  1.00107.77           O  
ANISOU 5268  O   GLY B 381    12547  15495  12905    479    226  -1291       O  
ATOM   5269  N   VAL B 382     -17.701  23.881  30.874  1.00 85.92           N  
ANISOU 5269  N   VAL B 382     9804  12624  10216    536    256  -1176       N  
ATOM   5270  CA  VAL B 382     -17.845  22.821  31.864  1.00 98.02           C  
ANISOU 5270  CA  VAL B 382    11318  14201  11726    624    237  -1138       C  
ATOM   5271  C   VAL B 382     -17.674  21.475  31.172  1.00101.82           C  
ANISOU 5271  C   VAL B 382    11752  14694  12242    662    227  -1097       C  
ATOM   5272  O   VAL B 382     -18.232  21.244  30.094  1.00 97.53           O  
ANISOU 5272  O   VAL B 382    11220  14088  11749    649    247  -1061       O  
ATOM   5273  CB  VAL B 382     -19.206  22.910  32.588  1.00 94.33           C  
ANISOU 5273  CB  VAL B 382    10910  13674  11257    676    258  -1084       C  
ATOM   5274  CG1 VAL B 382     -20.330  23.168  31.591  1.00 87.94           C  
ANISOU 5274  CG1 VAL B 382    10145  12765  10502    655    294  -1038       C  
ATOM   5275  CG2 VAL B 382     -19.475  21.652  33.397  1.00 98.73           C  
ANISOU 5275  CG2 VAL B 382    11447  14263  11802    771    244  -1033       C  
ATOM   5276  N   SER B 383     -16.893  20.595  31.788  1.00118.74           N  
ANISOU 5276  N   SER B 383    13843  16917  14355    710    198  -1103       N  
ATOM   5277  CA  SER B 383     -16.604  19.298  31.184  1.00122.72           C  
ANISOU 5277  CA  SER B 383    14300  17440  14887    748    188  -1069       C  
ATOM   5278  C   SER B 383     -17.815  18.377  31.287  1.00118.69           C  
ANISOU 5278  C   SER B 383    13815  16875  14406    821    206   -987       C  
ATOM   5279  O   SER B 383     -18.408  18.257  32.365  1.00119.37           O  
ANISOU 5279  O   SER B 383    13926  16962  14467    878    208   -961       O  
ATOM   5280  CB  SER B 383     -15.399  18.654  31.864  1.00136.61           C  
ANISOU 5280  CB  SER B 383    15998  19304  16602    780    153  -1099       C  
ATOM   5281  OG  SER B 383     -14.203  19.343  31.545  1.00137.04           O  
ANISOU 5281  OG  SER B 383    16019  19410  16640    709    137  -1173       O  
ATOM   5282  N   PRO B 384     -18.219  17.717  30.197  1.00112.16           N  
ANISOU 5282  N   PRO B 384    12983  16000  13632    822    220   -946       N  
ATOM   5283  CA  PRO B 384     -19.290  16.714  30.305  1.00109.49           C  
ANISOU 5283  CA  PRO B 384    12661  15617  13324    894    234   -870       C  
ATOM   5284  C   PRO B 384     -18.865  15.443  31.020  1.00119.53           C  
ANISOU 5284  C   PRO B 384    13890  16952  14575    973    216   -846       C  
ATOM   5285  O   PRO B 384     -19.730  14.726  31.539  1.00117.79           O  
ANISOU 5285  O   PRO B 384    13687  16704  14363   1042    228   -788       O  
ATOM   5286  CB  PRO B 384     -19.648  16.427  28.842  1.00109.73           C  
ANISOU 5286  CB  PRO B 384    12691  15586  13414    862    251   -844       C  
ATOM   5287  CG  PRO B 384     -18.388  16.711  28.095  1.00111.99           C  
ANISOU 5287  CG  PRO B 384    12936  15918  13696    800    235   -902       C  
ATOM   5288  CD  PRO B 384     -17.736  17.865  28.813  1.00113.94           C  
ANISOU 5288  CD  PRO B 384    13189  16208  13894    758    223   -967       C  
ATOM   5289  N   THR B 385     -17.569  15.146  31.072  1.00159.91           N  
ANISOU 5289  N   THR B 385    18949  22148  19661    967    189   -888       N  
ATOM   5290  CA  THR B 385     -17.080  13.858  31.563  1.00159.99           C  
ANISOU 5290  CA  THR B 385    18914  22219  19655   1040    173   -864       C  
ATOM   5291  C   THR B 385     -17.245  13.778  33.075  1.00155.97           C  
ANISOU 5291  C   THR B 385    18415  21750  19095   1106    165   -856       C  
ATOM   5292  O   THR B 385     -16.399  14.259  33.832  1.00156.67           O  
ANISOU 5292  O   THR B 385    18485  21911  19131   1097    142   -908       O  
ATOM   5293  CB  THR B 385     -15.621  13.664  31.166  1.00161.59           C  
ANISOU 5293  CB  THR B 385    19055  22501  19842   1011    147   -914       C  
ATOM   5294  OG1 THR B 385     -14.883  14.858  31.453  1.00154.79           O  
ANISOU 5294  OG1 THR B 385    18191  21680  18943    948    132   -985       O  
ATOM   5295  CG2 THR B 385     -15.508  13.354  29.680  1.00145.83           C  
ANISOU 5295  CG2 THR B 385    17044  20466  17899    968    157   -906       C  
ATOM   5296  N   LYS B 386     -18.341  13.151  33.511  1.00132.89           N  
ANISOU 5296  N   LYS B 386    15522  18780  16189   1173    185   -791       N  
ATOM   5297  CA  LYS B 386     -18.583  12.818  34.920  1.00140.70           C  
ANISOU 5297  CA  LYS B 386    16521  19804  17136   1251    181   -769       C  
ATOM   5298  C   LYS B 386     -18.336  14.008  35.847  1.00142.62           C  
ANISOU 5298  C   LYS B 386    16786  20079  17324   1225    168   -822       C  
ATOM   5299  O   LYS B 386     -17.827  13.863  36.960  1.00144.93           O  
ANISOU 5299  O   LYS B 386    17062  20443  17563   1270    149   -838       O  
ATOM   5300  CB  LYS B 386     -17.747  11.610  35.348  1.00139.86           C  
ANISOU 5300  CB  LYS B 386    16360  19777  17005   1317    162   -760       C  
ATOM   5301  CG  LYS B 386     -18.383  10.269  35.008  1.00134.79           C  
ANISOU 5301  CG  LYS B 386    15713  19096  16407   1380    182   -688       C  
ATOM   5302  CD  LYS B 386     -17.953   9.186  35.987  1.00137.82           C  
ANISOU 5302  CD  LYS B 386    16064  19548  16754   1471    173   -665       C  
ATOM   5303  CE  LYS B 386     -18.466   7.820  35.569  1.00121.67           C  
ANISOU 5303  CE  LYS B 386    14010  17466  14754   1529    194   -598       C  
ATOM   5304  NZ  LYS B 386     -17.769   7.332  34.349  1.00120.23           N  
ANISOU 5304  NZ  LYS B 386    13786  17291  14604   1491    189   -609       N  
ATOM   5305  N   LEU B 387     -18.706  15.198  35.384  1.00127.05           N  
ANISOU 5305  N   LEU B 387    14853  18054  15366   1152    180   -848       N  
ATOM   5306  CA  LEU B 387     -18.597  16.419  36.172  1.00132.22           C  
ANISOU 5306  CA  LEU B 387    15536  18725  15975   1120    173   -896       C  
ATOM   5307  C   LEU B 387     -19.984  16.929  36.560  1.00129.15           C  
ANISOU 5307  C   LEU B 387    15217  18256  15599   1136    203   -856       C  
ATOM   5308  O   LEU B 387     -20.253  18.133  36.559  1.00123.41           O  
ANISOU 5308  O   LEU B 387    14530  17496  14865   1081    213   -886       O  
ATOM   5309  CB  LEU B 387     -17.797  17.480  35.415  1.00128.82           C  
ANISOU 5309  CB  LEU B 387    15096  18306  15545   1020    165   -967       C  
ATOM   5310  CG  LEU B 387     -17.328  18.743  36.153  1.00132.26           C  
ANISOU 5310  CG  LEU B 387    15547  18776  15928    975    153  -1034       C  
ATOM   5311  CD1 LEU B 387     -16.227  18.429  37.155  1.00130.24           C  
ANISOU 5311  CD1 LEU B 387    15245  18629  15612   1009    117  -1074       C  
ATOM   5312  CD2 LEU B 387     -16.870  19.798  35.163  1.00117.33           C  
ANISOU 5312  CD2 LEU B 387    13660  16864  14057    873    158  -1089       C  
ATOM   5313  N   ASN B 388     -20.894  16.010  36.884  1.00118.54           N  
ANISOU 5313  N   ASN B 388    13887  16878  14275   1212    219   -785       N  
ATOM   5314  CA  ASN B 388     -22.220  16.385  37.361  1.00115.12           C  
ANISOU 5314  CA  ASN B 388    13515  16373  13851   1238    247   -741       C  
ATOM   5315  C   ASN B 388     -22.296  16.464  38.879  1.00116.86           C  
ANISOU 5315  C   ASN B 388    13754  16634  14015   1300    240   -740       C  
ATOM   5316  O   ASN B 388     -23.367  16.755  39.420  1.00118.42           O  
ANISOU 5316  O   ASN B 388    14002  16777  14214   1329    263   -703       O  
ATOM   5317  CB  ASN B 388     -23.288  15.432  36.781  1.00110.43           C  
ANISOU 5317  CB  ASN B 388    12932  15708  13318   1280    273   -663       C  
ATOM   5318  CG  ASN B 388     -23.405  14.090  37.515  1.00105.09           C  
ANISOU 5318  CG  ASN B 388    12233  15061  12634   1378    272   -612       C  
ATOM   5319  OD1 ASN B 388     -23.441  14.009  38.742  1.00104.95           O  
ANISOU 5319  OD1 ASN B 388    12225  15078  12572   1436    268   -606       O  
ATOM   5320  ND2 ASN B 388     -23.488  13.020  36.732  1.00 96.80           N  
ANISOU 5320  ND2 ASN B 388    11155  13994  11630   1397    279   -574       N  
ATOM   5321  N   ASP B 389     -21.187  16.228  39.574  1.00140.11           N  
ANISOU 5321  N   ASP B 389    16657  19673  16907   1321    209   -781       N  
ATOM   5322  CA  ASP B 389     -21.111  16.483  41.005  1.00151.58           C  
ANISOU 5322  CA  ASP B 389    18124  21172  18296   1369    198   -794       C  
ATOM   5323  C   ASP B 389     -20.932  17.963  41.317  1.00153.78           C  
ANISOU 5323  C   ASP B 389    18437  21453  18541   1302    193   -856       C  
ATOM   5324  O   ASP B 389     -20.594  18.311  42.454  1.00151.53           O  
ANISOU 5324  O   ASP B 389    18158  21221  18196   1327    177   -886       O  
ATOM   5325  CB  ASP B 389     -19.978  15.665  41.632  1.00151.03           C  
ANISOU 5325  CB  ASP B 389    17996  21207  18182   1418    165   -815       C  
ATOM   5326  CG  ASP B 389     -18.704  15.704  40.813  1.00154.96           C  
ANISOU 5326  CG  ASP B 389    18436  21761  18680   1356    140   -872       C  
ATOM   5327  OD1 ASP B 389     -17.963  16.704  40.909  1.00159.88           O  
ANISOU 5327  OD1 ASP B 389    19054  22423  19270   1293    121   -942       O  
ATOM   5328  OD2 ASP B 389     -18.440  14.729  40.079  1.00153.96           O1-
ANISOU 5328  OD2 ASP B 389    18270  21640  18587   1371    139   -846       O1-
ATOM   5329  N   LEU B 390     -21.140  18.825  40.327  1.00133.23           N  
ANISOU 5329  N   LEU B 390    15855  18792  15973   1219    208   -877       N  
ATOM   5330  CA  LEU B 390     -21.122  20.270  40.486  1.00135.88           C  
ANISOU 5330  CA  LEU B 390    16230  19112  16285   1151    212   -930       C  
ATOM   5331  C   LEU B 390     -22.550  20.784  40.629  1.00131.52           C  
ANISOU 5331  C   LEU B 390    15749  18466  15755   1162    248   -882       C  
ATOM   5332  O   LEU B 390     -23.501  20.170  40.138  1.00120.61           O  
ANISOU 5332  O   LEU B 390    14383  17020  14423   1193    272   -815       O  
ATOM   5333  CB  LEU B 390     -20.437  20.934  39.289  1.00127.62           C  
ANISOU 5333  CB  LEU B 390    15165  18060  15264   1053    208   -982       C  
ATOM   5334  CG  LEU B 390     -19.990  22.390  39.421  1.00125.40           C  
ANISOU 5334  CG  LEU B 390    14907  17786  14952    973    206  -1056       C  
ATOM   5335  CD1 LEU B 390     -19.092  22.569  40.634  1.00111.49           C  
ANISOU 5335  CD1 LEU B 390    13124  16117  13119    992    173  -1110       C  
ATOM   5336  CD2 LEU B 390     -19.280  22.837  38.152  1.00118.97           C  
ANISOU 5336  CD2 LEU B 390    14067  16967  14168    884    204  -1101       C  
ATOM   5337  N   CYS B 391     -22.693  21.920  41.305  1.00141.24           N  
ANISOU 5337  N   CYS B 391    17026  19691  16949   1136    253   -917       N  
ATOM   5338  CA  CYS B 391     -23.998  22.479  41.624  1.00134.85           C  
ANISOU 5338  CA  CYS B 391    16286  18801  16151   1151    287   -875       C  
ATOM   5339  C   CYS B 391     -24.169  23.839  40.960  1.00132.37           C  
ANISOU 5339  C   CYS B 391    16012  18432  15849   1060    307   -912       C  
ATOM   5340  O   CYS B 391     -23.211  24.605  40.820  1.00131.94           O  
ANISOU 5340  O   CYS B 391    15942  18418  15770    993    291   -985       O  
ATOM   5341  CB  CYS B 391     -24.186  22.609  43.139  1.00134.00           C  
ANISOU 5341  CB  CYS B 391    16206  18724  15984   1213    282   -874       C  
ATOM   5342  SG  CYS B 391     -24.048  21.045  44.036  1.00150.39           S  
ANISOU 5342  SG  CYS B 391    18241  20862  18039   1328    264   -826       S  
ATOM   5343  N   PHE B 392     -25.404  24.132  40.553  1.00105.13           N  
ANISOU 5343  N   PHE B 392    12614  14892  12440   1059    343   -861       N  
ATOM   5344  CA  PHE B 392     -25.732  25.364  39.852  1.00103.17           C  
ANISOU 5344  CA  PHE B 392    12408  14581  12210    980    369   -884       C  
ATOM   5345  C   PHE B 392     -26.994  25.976  40.444  1.00104.37           C  
ANISOU 5345  C   PHE B 392    12632  14664  12358   1006    402   -844       C  
ATOM   5346  O   PHE B 392     -27.848  25.273  40.992  1.00101.06           O  
ANISOU 5346  O   PHE B 392    12228  14223  11947   1083    412   -779       O  
ATOM   5347  CB  PHE B 392     -25.933  25.125  38.347  1.00 97.67           C  
ANISOU 5347  CB  PHE B 392    11696  13836  11579    939    382   -863       C  
ATOM   5348  CG  PHE B 392     -24.818  24.353  37.699  1.00 99.67           C  
ANISOU 5348  CG  PHE B 392    11879  14149  11842    924    353   -890       C  
ATOM   5349  CD1 PHE B 392     -24.805  22.967  37.725  1.00101.07           C  
ANISOU 5349  CD1 PHE B 392    12014  14352  12036    990    339   -845       C  
ATOM   5350  CD2 PHE B 392     -23.780  25.015  37.066  1.00 92.11           C  
ANISOU 5350  CD2 PHE B 392    10897  13222  10879    843    340   -959       C  
ATOM   5351  CE1 PHE B 392     -23.778  22.258  37.130  1.00 96.31           C  
ANISOU 5351  CE1 PHE B 392    11347  13804  11441    977    314   -868       C  
ATOM   5352  CE2 PHE B 392     -22.752  24.312  36.469  1.00 97.20           C  
ANISOU 5352  CE2 PHE B 392    11476  13922  11533    830    314   -983       C  
ATOM   5353  CZ  PHE B 392     -22.750  22.932  36.501  1.00100.42           C  
ANISOU 5353  CZ  PHE B 392    11844  14356  11956    897    301   -937       C  
ATOM   5354  N   THR B 393     -27.100  27.302  40.326  1.00100.26           N  
ANISOU 5354  N   THR B 393    12158  14109  11827    942    421   -882       N  
ATOM   5355  CA  THR B 393     -28.276  28.001  40.835  1.00 99.52           C  
ANISOU 5355  CA  THR B 393    12136  13947  11729    960    456   -846       C  
ATOM   5356  C   THR B 393     -29.525  27.623  40.051  1.00 98.62           C  
ANISOU 5356  C   THR B 393    12044  13749  11677    981    487   -768       C  
ATOM   5357  O   THR B 393     -30.553  27.258  40.635  1.00 96.83           O  
ANISOU 5357  O   THR B 393    11847  13486  11456   1047    505   -706       O  
ATOM   5358  CB  THR B 393     -28.051  29.512  40.784  1.00102.13           C  
ANISOU 5358  CB  THR B 393    12510  14258  12037    882    471   -907       C  
ATOM   5359  OG1 THR B 393     -26.775  29.830  41.355  1.00100.81           O  
ANISOU 5359  OG1 THR B 393    12313  14172  11816    852    439   -986       O  
ATOM   5360  CG2 THR B 393     -29.144  30.235  41.551  1.00102.94           C  
ANISOU 5360  CG2 THR B 393    12687  14303  12121    908    504   -876       C  
ATOM   5361  N   ASN B 394     -29.455  27.702  38.725  1.00 99.79           N  
ANISOU 5361  N   ASN B 394    12177  13867  11872    926    495   -771       N  
ATOM   5362  CA  ASN B 394     -30.564  27.336  37.860  1.00 93.39           C  
ANISOU 5362  CA  ASN B 394    11381  12982  11122    940    522   -702       C  
ATOM   5363  C   ASN B 394     -30.017  26.661  36.613  1.00 87.51           C  
ANISOU 5363  C   ASN B 394    10581  12248  10420    910    508   -707       C  
ATOM   5364  O   ASN B 394     -28.876  26.900  36.209  1.00 91.22           O  
ANISOU 5364  O   ASN B 394    11017  12765  10877    855    487   -769       O  
ATOM   5365  CB  ASN B 394     -31.412  28.555  37.466  1.00 94.56           C  
ANISOU 5365  CB  ASN B 394    11594  13051  11283    896    562   -695       C  
ATOM   5366  CG  ASN B 394     -32.110  29.190  38.651  1.00 91.87           C  
ANISOU 5366  CG  ASN B 394    11313  12689  10905    930    581   -680       C  
ATOM   5367  OD1 ASN B 394     -33.196  28.767  39.046  1.00 84.00           O  
ANISOU 5367  OD1 ASN B 394    10341  11652   9925    993    599   -613       O  
ATOM   5368  ND2 ASN B 394     -31.492  30.217  39.222  1.00 93.11           N  
ANISOU 5368  ND2 ASN B 394    11494  12871  11013    889    579   -744       N  
ATOM   5369  N   VAL B 395     -30.841  25.809  36.010  1.00 79.24           N  
ANISOU 5369  N   VAL B 395     9525  11157   9424    945    519   -641       N  
ATOM   5370  CA  VAL B 395     -30.502  25.125  34.769  1.00 75.30           C  
ANISOU 5370  CA  VAL B 395     8981  10660   8971    921    509   -636       C  
ATOM   5371  C   VAL B 395     -31.616  25.397  33.770  1.00 77.26           C  
ANISOU 5371  C   VAL B 395     9261  10822   9271    903    542   -590       C  
ATOM   5372  O   VAL B 395     -32.782  25.079  34.036  1.00 78.44           O  
ANISOU 5372  O   VAL B 395     9438  10924   9442    954    562   -526       O  
ATOM   5373  CB  VAL B 395     -30.310  23.613  34.974  1.00 68.29           C  
ANISOU 5373  CB  VAL B 395     8040   9811   8094    987    487   -602       C  
ATOM   5374  CG1 VAL B 395     -30.135  22.913  33.634  1.00 61.05           C  
ANISOU 5374  CG1 VAL B 395     7083   8883   7229    964    482   -590       C  
ATOM   5375  CG2 VAL B 395     -29.116  23.349  35.880  1.00 83.25           C  
ANISOU 5375  CG2 VAL B 395     9898  11797   9936   1004    453   -651       C  
ATOM   5376  N   TYR B 396     -31.265  25.986  32.632  1.00 69.57           N  
ANISOU 5376  N   TYR B 396     8285   9831   8318    831    548   -622       N  
ATOM   5377  CA  TYR B 396     -32.223  26.317  31.585  1.00 61.84           C  
ANISOU 5377  CA  TYR B 396     7335   8776   7386    808    577   -584       C  
ATOM   5378  C   TYR B 396     -31.994  25.393  30.398  1.00 60.15           C  
ANISOU 5378  C   TYR B 396     7073   8563   7219    799    565   -570       C  
ATOM   5379  O   TYR B 396     -30.919  25.416  29.788  1.00 64.48           O  
ANISOU 5379  O   TYR B 396     7585   9151   7765    753    547   -620       O  
ATOM   5380  CB  TYR B 396     -32.090  27.779  31.160  1.00 61.45           C  
ANISOU 5380  CB  TYR B 396     7326   8697   7324    734    600   -629       C  
ATOM   5381  CG  TYR B 396     -32.352  28.768  32.270  1.00 64.50           C  
ANISOU 5381  CG  TYR B 396     7766   9076   7665    737    616   -644       C  
ATOM   5382  CD1 TYR B 396     -33.630  28.945  32.782  1.00 69.46           C  
ANISOU 5382  CD1 TYR B 396     8443   9649   8298    782    643   -586       C  
ATOM   5383  CD2 TYR B 396     -31.321  29.524  32.809  1.00 77.51           C  
ANISOU 5383  CD2 TYR B 396     9414  10771   9265    696    604   -716       C  
ATOM   5384  CE1 TYR B 396     -33.874  29.851  33.796  1.00 79.41           C  
ANISOU 5384  CE1 TYR B 396     9755  10902   9517    786    659   -600       C  
ATOM   5385  CE2 TYR B 396     -31.555  30.430  33.824  1.00 85.13           C  
ANISOU 5385  CE2 TYR B 396    10430  11729  10188    698    619   -732       C  
ATOM   5386  CZ  TYR B 396     -32.833  30.589  34.315  1.00 89.45           C  
ANISOU 5386  CZ  TYR B 396    11028  12220  10740    744    647   -673       C  
ATOM   5387  OH  TYR B 396     -33.071  31.490  35.327  1.00 96.67           O  
ANISOU 5387  OH  TYR B 396    11994  13125  11611    748    663   -688       O  
ATOM   5388  N   ALA B 397     -33.001  24.589  30.073  1.00 52.94           N  
ANISOU 5388  N   ALA B 397     6159   7608   6348    844    575   -503       N  
ATOM   5389  CA  ALA B 397     -32.954  23.692  28.924  1.00 50.10           C  
ANISOU 5389  CA  ALA B 397     5759   7241   6037    840    566   -483       C  
ATOM   5390  C   ALA B 397     -33.780  24.311  27.803  1.00 52.25           C  
ANISOU 5390  C   ALA B 397     6062   7443   6347    801    593   -462       C  
ATOM   5391  O   ALA B 397     -35.011  24.358  27.882  1.00 53.37           O  
ANISOU 5391  O   ALA B 397     6237   7529   6510    831    616   -407       O  
ATOM   5392  CB  ALA B 397     -33.474  22.304  29.292  1.00 53.87           C  
ANISOU 5392  CB  ALA B 397     6209   7721   6537    915    558   -425       C  
ATOM   5393  N   ASP B 398     -33.101  24.790  26.764  1.00 53.87           N  
ANISOU 5393  N   ASP B 398     6257   7652   6561    736    591   -504       N  
ATOM   5394  CA  ASP B 398     -33.752  25.404  25.613  1.00 49.00           C  
ANISOU 5394  CA  ASP B 398     5667   6973   5977    697    617   -490       C  
ATOM   5395  C   ASP B 398     -33.843  24.365  24.502  1.00 44.49           C  
ANISOU 5395  C   ASP B 398     5056   6394   5454    703    605   -462       C  
ATOM   5396  O   ASP B 398     -32.825  23.984  23.914  1.00 47.82           O  
ANISOU 5396  O   ASP B 398     5436   6855   5879    676    584   -499       O  
ATOM   5397  CB  ASP B 398     -32.991  26.645  25.152  1.00 48.98           C  
ANISOU 5397  CB  ASP B 398     5682   6975   5953    621    626   -552       C  
ATOM   5398  CG  ASP B 398     -32.812  27.664  26.261  1.00 55.39           C  
ANISOU 5398  CG  ASP B 398     6532   7798   6716    612    636   -585       C  
ATOM   5399  OD1 ASP B 398     -33.742  27.825  27.078  1.00 60.78           O  
ANISOU 5399  OD1 ASP B 398     7252   8452   7389    653    652   -547       O  
ATOM   5400  OD2 ASP B 398     -31.741  28.304  26.316  1.00 61.62           O1-
ANISOU 5400  OD2 ASP B 398     7314   8624   7475    562    628   -650       O1-
ATOM   5401  N   SER B 399     -35.060  23.914  24.213  1.00 48.37           N  
ANISOU 5401  N   SER B 399     5561   6835   5984    738    620   -400       N  
ATOM   5402  CA  SER B 399     -35.301  22.865  23.235  1.00 49.45           C  
ANISOU 5402  CA  SER B 399     5662   6959   6168    751    610   -368       C  
ATOM   5403  C   SER B 399     -35.937  23.447  21.980  1.00 51.95           C  
ANISOU 5403  C   SER B 399     6002   7220   6517    712    631   -356       C  
ATOM   5404  O   SER B 399     -36.846  24.280  22.062  1.00 51.27           O  
ANISOU 5404  O   SER B 399     5963   7087   6431    709    658   -333       O  
ATOM   5405  CB  SER B 399     -36.199  21.769  23.815  1.00 53.63           C  
ANISOU 5405  CB  SER B 399     6182   7474   6720    823    609   -306       C  
ATOM   5406  OG  SER B 399     -37.559  22.168  23.811  1.00 65.89           O  
ANISOU 5406  OG  SER B 399     7777   8966   8294    840    636   -256       O  
ATOM   5407  N   PHE B 400     -35.454  23.003  20.824  1.00 42.73           N  
ANISOU 5407  N   PHE B 400     4801   6059   5375    684    619   -369       N  
ATOM   5408  CA  PHE B 400     -35.991  23.428  19.537  1.00 39.16           C  
ANISOU 5408  CA  PHE B 400     4366   5559   4955    649    636   -357       C  
ATOM   5409  C   PHE B 400     -35.565  22.414  18.483  1.00 43.05           C  
ANISOU 5409  C   PHE B 400     4812   6066   5481    644    615   -358       C  
ATOM   5410  O   PHE B 400     -34.892  21.424  18.781  1.00 45.75           O  
ANISOU 5410  O   PHE B 400     5110   6451   5820    666    590   -366       O  
ATOM   5411  CB  PHE B 400     -35.528  24.843  19.180  1.00 41.55           C  
ANISOU 5411  CB  PHE B 400     4702   5854   5232    587    654   -404       C  
ATOM   5412  CG  PHE B 400     -34.051  25.059  19.341  1.00 45.19           C  
ANISOU 5412  CG  PHE B 400     5137   6371   5661    549    637   -471       C  
ATOM   5413  CD1 PHE B 400     -33.159  24.601  18.385  1.00 39.55           C  
ANISOU 5413  CD1 PHE B 400     4383   5684   4962    520    619   -500       C  
ATOM   5414  CD2 PHE B 400     -33.555  25.724  20.448  1.00 50.88           C  
ANISOU 5414  CD2 PHE B 400     5874   7120   6337    543    638   -505       C  
ATOM   5415  CE1 PHE B 400     -31.804  24.805  18.530  1.00 43.11           C  
ANISOU 5415  CE1 PHE B 400     4809   6188   5384    484    604   -560       C  
ATOM   5416  CE2 PHE B 400     -32.199  25.927  20.600  1.00 48.52           C  
ANISOU 5416  CE2 PHE B 400     5549   6876   6009    507    621   -568       C  
ATOM   5417  CZ  PHE B 400     -31.323  25.467  19.642  1.00 49.68           C  
ANISOU 5417  CZ  PHE B 400     5654   7049   6172    478    604   -595       C  
ATOM   5418  N   VAL B 401     -35.964  22.672  17.239  1.00 51.95           N  
ANISOU 5418  N   VAL B 401     5948   7155   6637    614    626   -349       N  
ATOM   5419  CA  VAL B 401     -35.637  21.809  16.110  1.00 45.48           C  
ANISOU 5419  CA  VAL B 401     5089   6341   5849    605    610   -350       C  
ATOM   5420  C   VAL B 401     -35.086  22.665  14.979  1.00 48.55           C  
ANISOU 5420  C   VAL B 401     5489   6722   6237    543    619   -389       C  
ATOM   5421  O   VAL B 401     -35.692  23.675  14.605  1.00 50.83           O  
ANISOU 5421  O   VAL B 401     5819   6969   6525    520    645   -383       O  
ATOM   5422  CB  VAL B 401     -36.859  21.002  15.632  1.00 43.10           C  
ANISOU 5422  CB  VAL B 401     4785   5997   5593    642    612   -289       C  
ATOM   5423  CG1 VAL B 401     -36.716  20.626  14.167  1.00 36.40           C  
ANISOU 5423  CG1 VAL B 401     3915   5137   4776    615    605   -293       C  
ATOM   5424  CG2 VAL B 401     -37.030  19.760  16.475  1.00 44.15           C  
ANISOU 5424  CG2 VAL B 401     4889   6151   5736    700    596   -258       C  
ATOM   5425  N   ILE B 402     -33.937  22.259  14.443  1.00 48.18           N  
ANISOU 5425  N   ILE B 402     5403   6714   6188    517    599   -428       N  
ATOM   5426  CA  ILE B 402     -33.349  22.838  13.247  1.00 47.52           C  
ANISOU 5426  CA  ILE B 402     5322   6626   6109    462    606   -463       C  
ATOM   5427  C   ILE B 402     -32.970  21.695  12.311  1.00 47.38           C  
ANISOU 5427  C   ILE B 402     5260   6622   6122    467    584   -458       C  
ATOM   5428  O   ILE B 402     -33.217  20.526  12.600  1.00 48.96           O  
ANISOU 5428  O   ILE B 402     5431   6832   6339    511    567   -428       O  
ATOM   5429  CB  ILE B 402     -32.124  23.719  13.564  1.00 47.04           C  
ANISOU 5429  CB  ILE B 402     5262   6602   6010    416    607   -526       C  
ATOM   5430  CG1 ILE B 402     -31.280  23.079  14.667  1.00 47.33           C  
ANISOU 5430  CG1 ILE B 402     5264   6700   6022    439    582   -547       C  
ATOM   5431  CG2 ILE B 402     -32.561  25.109  13.975  1.00 47.72           C  
ANISOU 5431  CG2 ILE B 402     5402   6657   6072    393    638   -534       C  
ATOM   5432  CD1 ILE B 402     -30.086  23.908  15.070  1.00 44.93           C  
ANISOU 5432  CD1 ILE B 402     4957   6437   5679    395    581   -611       C  
ATOM   5433  N   ARG B 403     -32.365  22.043  11.180  1.00 57.33           N  
ANISOU 5433  N   ARG B 403     6515   7881   7388    421    587   -489       N  
ATOM   5434  CA  ARG B 403     -31.844  21.038  10.267  1.00 55.37           C  
ANISOU 5434  CA  ARG B 403     6225   7649   7163    421    567   -492       C  
ATOM   5435  C   ARG B 403     -30.355  20.823  10.522  1.00 54.55           C  
ANISOU 5435  C   ARG B 403     6084   7606   7037    401    549   -543       C  
ATOM   5436  O   ARG B 403     -29.706  21.574  11.254  1.00 58.21           O  
ANISOU 5436  O   ARG B 403     6555   8097   7466    380    552   -580       O  
ATOM   5437  CB  ARG B 403     -32.113  21.426   8.808  1.00 51.85           C  
ANISOU 5437  CB  ARG B 403     5795   7166   6742    388    581   -491       C  
ATOM   5438  CG  ARG B 403     -31.552  22.763   8.379  1.00 51.68           C  
ANISOU 5438  CG  ARG B 403     5800   7138   6698    332    602   -534       C  
ATOM   5439  CD  ARG B 403     -30.950  22.679   6.986  1.00 55.82           C  
ANISOU 5439  CD  ARG B 403     6309   7662   7239    298    601   -555       C  
ATOM   5440  NE  ARG B 403     -30.948  23.969   6.307  1.00 59.96           N  
ANISOU 5440  NE  ARG B 403     6871   8156   7754    253    631   -575       N  
ATOM   5441  CZ  ARG B 403     -29.965  24.404   5.532  1.00 74.11           C  
ANISOU 5441  CZ  ARG B 403     8656   9961   9541    208    637   -618       C  
ATOM   5442  NH1 ARG B 403     -28.883  23.675   5.313  1.00 69.82           N  
ANISOU 5442  NH1 ARG B 403     8068   9460   8999    200    614   -645       N  
ATOM   5443  NH2 ARG B 403     -30.070  25.600   4.959  1.00 76.18           N  
ANISOU 5443  NH2 ARG B 403     8958  10192   9797    170    668   -632       N  
ATOM   5444  N   GLY B 404     -29.820  19.768   9.901  1.00 50.69           N  
ANISOU 5444  N   GLY B 404     5553   7139   6566    409    528   -544       N  
ATOM   5445  CA  GLY B 404     -28.500  19.281  10.277  1.00 46.17           C  
ANISOU 5445  CA  GLY B 404     4938   6629   5974    405    507   -581       C  
ATOM   5446  C   GLY B 404     -27.394  20.300  10.082  1.00 51.56           C  
ANISOU 5446  C   GLY B 404     5622   7337   6630    348    514   -640       C  
ATOM   5447  O   GLY B 404     -26.515  20.444  10.935  1.00 57.09           O  
ANISOU 5447  O   GLY B 404     6306   8087   7300    343    503   -675       O  
ATOM   5448  N   ASN B 405     -27.418  21.018   8.959  1.00 55.08           N  
ANISOU 5448  N   ASN B 405     6090   7751   7088    305    532   -653       N  
ATOM   5449  CA  ASN B 405     -26.357  21.976   8.671  1.00 57.85           C  
ANISOU 5449  CA  ASN B 405     6441   8122   7418    248    541   -709       C  
ATOM   5450  C   ASN B 405     -26.343  23.144   9.649  1.00 60.59           C  
ANISOU 5450  C   ASN B 405     6820   8471   7731    229    557   -734       C  
ATOM   5451  O   ASN B 405     -25.324  23.836   9.751  1.00 69.50           O  
ANISOU 5451  O   ASN B 405     7942   9630   8837    186    560   -785       O  
ATOM   5452  CB  ASN B 405     -26.496  22.497   7.241  1.00 70.16           C  
ANISOU 5452  CB  ASN B 405     8020   9640   8998    211    561   -712       C  
ATOM   5453  CG  ASN B 405     -25.944  21.529   6.211  1.00 82.65           C  
ANISOU 5453  CG  ASN B 405     9564  11236  10603    212    544   -713       C  
ATOM   5454  OD1 ASN B 405     -26.264  21.618   5.025  1.00 74.52           O  
ANISOU 5454  OD1 ASN B 405     8546  10170   9595    198    555   -702       O  
ATOM   5455  ND2 ASN B 405     -25.107  20.599   6.659  1.00 73.07           N  
ANISOU 5455  ND2 ASN B 405     8304  10076   9383    231    518   -725       N  
ATOM   5456  N   GLU B 406     -27.440  23.381  10.365  1.00 52.50           N  
ANISOU 5456  N   GLU B 406     5828   7415   6703    259    568   -698       N  
ATOM   5457  CA  GLU B 406     -27.550  24.513  11.274  1.00 53.76           C  
ANISOU 5457  CA  GLU B 406     6024   7570   6832    242    585   -718       C  
ATOM   5458  C   GLU B 406     -27.208  24.166  12.718  1.00 47.61           C  
ANISOU 5458  C   GLU B 406     5227   6838   6023    273    566   -726       C  
ATOM   5459  O   GLU B 406     -27.214  25.061  13.570  1.00 50.50           O  
ANISOU 5459  O   GLU B 406     5620   7206   6360    260    578   -746       O  
ATOM   5460  CB  GLU B 406     -28.963  25.098  11.204  1.00 45.31           C  
ANISOU 5460  CB  GLU B 406     5006   6436   5773    256    612   -674       C  
ATOM   5461  CG  GLU B 406     -29.513  25.163   9.793  1.00 51.13           C  
ANISOU 5461  CG  GLU B 406     5758   7127   6543    242    627   -652       C  
ATOM   5462  CD  GLU B 406     -30.632  26.170   9.640  1.00 52.55           C  
ANISOU 5462  CD  GLU B 406     5995   7248   6725    237    661   -626       C  
ATOM   5463  OE1 GLU B 406     -31.782  25.837   9.996  1.00 55.09           O  
ANISOU 5463  OE1 GLU B 406     6331   7541   7058    280    662   -576       O  
ATOM   5464  OE2 GLU B 406     -30.364  27.294   9.167  1.00 57.59           O1-
ANISOU 5464  OE2 GLU B 406     6662   7867   7352    191    687   -656       O1-
ATOM   5465  N   VAL B 407     -26.914  22.898  13.016  1.00 38.43           N  
ANISOU 5465  N   VAL B 407     4020   5714   4867    314    537   -712       N  
ATOM   5466  CA  VAL B 407     -26.496  22.532  14.367  1.00 40.88           C  
ANISOU 5466  CA  VAL B 407     4310   6075   5147    345    518   -722       C  
ATOM   5467  C   VAL B 407     -25.169  23.198  14.709  1.00 42.08           C  
ANISOU 5467  C   VAL B 407     4445   6279   5264    300    512   -788       C  
ATOM   5468  O   VAL B 407     -24.903  23.516  15.875  1.00 45.68           O  
ANISOU 5468  O   VAL B 407     4903   6767   5685    308    506   -808       O  
ATOM   5469  CB  VAL B 407     -26.432  20.996  14.501  1.00 42.35           C  
ANISOU 5469  CB  VAL B 407     4452   6289   5349    399    492   -691       C  
ATOM   5470  CG1 VAL B 407     -25.555  20.578  15.673  1.00 42.01           C  
ANISOU 5470  CG1 VAL B 407     4375   6315   5271    422    468   -716       C  
ATOM   5471  CG2 VAL B 407     -27.833  20.425  14.657  1.00 47.28           C  
ANISOU 5471  CG2 VAL B 407     5098   6868   6000    450    499   -626       C  
ATOM   5472  N   SER B 408     -24.331  23.448  13.698  1.00 47.60           N  
ANISOU 5472  N   SER B 408     5127   6986   5971    251    514   -824       N  
ATOM   5473  CA  SER B 408     -23.080  24.164  13.923  1.00 46.66           C  
ANISOU 5473  CA  SER B 408     4992   6914   5823    202    511   -889       C  
ATOM   5474  C   SER B 408     -23.319  25.550  14.509  1.00 52.44           C  
ANISOU 5474  C   SER B 408     5772   7624   6529    169    535   -914       C  
ATOM   5475  O   SER B 408     -22.451  26.086  15.207  1.00 50.74           O  
ANISOU 5475  O   SER B 408     5546   7452   6281    142    529   -965       O  
ATOM   5476  CB  SER B 408     -22.297  24.276  12.614  1.00 48.80           C  
ANISOU 5476  CB  SER B 408     5244   7186   6113    154    516   -918       C  
ATOM   5477  OG  SER B 408     -22.881  25.240  11.753  1.00 55.16           O  
ANISOU 5477  OG  SER B 408     6096   7929   6935    117    548   -914       O  
ATOM   5478  N   GLN B 409     -24.487  26.140  14.245  1.00 47.70           N  
ANISOU 5478  N   GLN B 409     5224   6958   5943    171    563   -880       N  
ATOM   5479  CA  GLN B 409     -24.790  27.484  14.719  1.00 44.91           C  
ANISOU 5479  CA  GLN B 409     4920   6577   5567    140    591   -900       C  
ATOM   5480  C   GLN B 409     -25.178  27.530  16.190  1.00 43.00           C  
ANISOU 5480  C   GLN B 409     4693   6351   5294    177    584   -891       C  
ATOM   5481  O   GLN B 409     -25.241  28.625  16.759  1.00 45.84           O  
ANISOU 5481  O   GLN B 409     5090   6698   5628    151    604   -916       O  
ATOM   5482  CB  GLN B 409     -25.908  28.101  13.878  1.00 40.99           C  
ANISOU 5482  CB  GLN B 409     4475   6005   5095    132    626   -865       C  
ATOM   5483  CG  GLN B 409     -25.612  28.130  12.391  1.00 42.65           C  
ANISOU 5483  CG  GLN B 409     4676   6194   5334     97    636   -872       C  
ATOM   5484  CD  GLN B 409     -26.701  28.819  11.599  1.00 46.42           C  
ANISOU 5484  CD  GLN B 409     5206   6601   5832     89    671   -838       C  
ATOM   5485  OE1 GLN B 409     -27.206  29.866  12.002  1.00 47.88           O  
ANISOU 5485  OE1 GLN B 409     5439   6753   6001     75    699   -840       O  
ATOM   5486  NE2 GLN B 409     -27.069  28.235  10.465  1.00 45.80           N  
ANISOU 5486  NE2 GLN B 409     5118   6496   5786     99    669   -808       N  
ATOM   5487  N   ILE B 410     -25.433  26.387  16.821  1.00 36.60           N  
ANISOU 5487  N   ILE B 410     3856   5565   4485    238    559   -856       N  
ATOM   5488  CA  ILE B 410     -25.730  26.360  18.262  1.00 40.88           C  
ANISOU 5488  CA  ILE B 410     4410   6128   4997    278    550   -848       C  
ATOM   5489  C   ILE B 410     -24.381  26.248  18.959  1.00 46.76           C  
ANISOU 5489  C   ILE B 410     5111   6950   5706    264    524   -904       C  
ATOM   5490  O   ILE B 410     -23.936  25.180  19.388  1.00 45.00           O  
ANISOU 5490  O   ILE B 410     4843   6777   5478    304    494   -898       O  
ATOM   5491  CB  ILE B 410     -26.696  25.233  18.633  1.00 41.21           C  
ANISOU 5491  CB  ILE B 410     4446   6156   5057    350    540   -782       C  
ATOM   5492  CG1 ILE B 410     -27.780  25.110  17.564  1.00 38.68           C  
ANISOU 5492  CG1 ILE B 410     4149   5768   4780    356    560   -732       C  
ATOM   5493  CG2 ILE B 410     -27.319  25.489  19.993  1.00 46.70           C  
ANISOU 5493  CG2 ILE B 410     5171   6849   5723    388    544   -766       C  
ATOM   5494  CD1 ILE B 410     -28.724  26.293  17.525  1.00 34.74           C  
ANISOU 5494  CD1 ILE B 410     3712   5209   4280    338    595   -719       C  
ATOM   5495  N   ALA B 411     -23.722  27.392  19.092  1.00 55.88           N  
ANISOU 5495  N   ALA B 411     6281   8115   6835    207    536   -961       N  
ATOM   5496  CA  ALA B 411     -22.383  27.494  19.656  1.00 63.08           C  
ANISOU 5496  CA  ALA B 411     7153   9100   7713    182    513  -1024       C  
ATOM   5497  C   ALA B 411     -22.058  28.974  19.835  1.00 67.06           C  
ANISOU 5497  C   ALA B 411     7694   9593   8194    118    537  -1077       C  
ATOM   5498  O   ALA B 411     -22.646  29.823  19.157  1.00 64.90           O  
ANISOU 5498  O   ALA B 411     7466   9257   7937     86    572  -1070       O  
ATOM   5499  CB  ALA B 411     -21.339  26.818  18.750  1.00 59.80           C  
ANISOU 5499  CB  ALA B 411     6681   8723   7316    162    494  -1045       C  
ATOM   5500  N   PRO B 412     -21.145  29.305  20.749  1.00 62.87           N  
ANISOU 5500  N   PRO B 412     7144   9121   7623    101    520  -1132       N  
ATOM   5501  CA  PRO B 412     -20.741  30.708  20.905  1.00 64.05           C  
ANISOU 5501  CA  PRO B 412     7324   9262   7750     35    543  -1189       C  
ATOM   5502  C   PRO B 412     -20.092  31.247  19.639  1.00 67.26           C  
ANISOU 5502  C   PRO B 412     7723   9652   8180    -32    562  -1224       C  
ATOM   5503  O   PRO B 412     -19.417  30.525  18.900  1.00 60.08           O  
ANISOU 5503  O   PRO B 412     6766   8772   7291    -36    544  -1228       O  
ATOM   5504  CB  PRO B 412     -19.743  30.680  22.070  1.00 62.49           C  
ANISOU 5504  CB  PRO B 412     7092   9144   7507     34    513  -1241       C  
ATOM   5505  CG  PRO B 412     -19.601  29.269  22.494  1.00 71.28           C  
ANISOU 5505  CG  PRO B 412     8156  10309   8619    101    475  -1210       C  
ATOM   5506  CD  PRO B 412     -20.603  28.424  21.796  1.00 62.87           C  
ANISOU 5506  CD  PRO B 412     7099   9194   7594    147    482  -1137       C  
ATOM   5507  N   GLY B 413     -20.314  32.537  19.392  1.00 70.69           N  
ANISOU 5507  N   GLY B 413     8208  10038   8612    -84    600  -1247       N  
ATOM   5508  CA  GLY B 413     -19.664  33.219  18.287  1.00 72.24           C  
ANISOU 5508  CA  GLY B 413     8402  10218   8827   -152    623  -1285       C  
ATOM   5509  C   GLY B 413     -19.991  32.660  16.922  1.00 68.37           C  
ANISOU 5509  C   GLY B 413     7904   9691   8381   -144    631  -1245       C  
ATOM   5510  O   GLY B 413     -19.159  32.738  16.011  1.00 67.71           O  
ANISOU 5510  O   GLY B 413     7794   9620   8314   -188    634  -1276       O  
ATOM   5511  N   GLN B 414     -21.182  32.099  16.749  1.00 63.45           N  
ANISOU 5511  N   GLN B 414     7304   9026   7779    -91    634  -1176       N  
ATOM   5512  CA  GLN B 414     -21.589  31.532  15.474  1.00 58.87           C  
ANISOU 5512  CA  GLN B 414     6718   8410   7240    -80    640  -1135       C  
ATOM   5513  C   GLN B 414     -22.579  32.456  14.776  1.00 55.94           C  
ANISOU 5513  C   GLN B 414     6410   7958   6887    -98    685  -1110       C  
ATOM   5514  O   GLN B 414     -23.285  33.240  15.415  1.00 61.84           O  
ANISOU 5514  O   GLN B 414     7208   8673   7617    -96    708  -1102       O  
ATOM   5515  CB  GLN B 414     -22.207  30.147  15.660  1.00 51.84           C  
ANISOU 5515  CB  GLN B 414     5803   7529   6364     -7    611  -1076       C  
ATOM   5516  CG  GLN B 414     -21.643  29.104  14.713  1.00 55.91           C  
ANISOU 5516  CG  GLN B 414     6266   8068   6908     -1    590  -1068       C  
ATOM   5517  CD  GLN B 414     -20.217  28.721  15.048  1.00 60.37           C  
ANISOU 5517  CD  GLN B 414     6772   8711   7453    -17    560  -1120       C  
ATOM   5518  OE1 GLN B 414     -19.829  28.688  16.216  1.00 64.66           O  
ANISOU 5518  OE1 GLN B 414     7302   9303   7963     -4    541  -1143       O  
ATOM   5519  NE2 GLN B 414     -19.426  28.428  14.022  1.00 64.66           N  
ANISOU 5519  NE2 GLN B 414     7281   9269   8016    -45    556  -1138       N  
ATOM   5520  N   THR B 415     -22.620  32.352  13.451  1.00 66.08           N  
ANISOU 5520  N   THR B 415     7691   9211   8203   -115    699  -1096       N  
ATOM   5521  CA  THR B 415     -23.441  33.215  12.618  1.00 67.15           C  
ANISOU 5521  CA  THR B 415     7883   9276   8357   -134    742  -1075       C  
ATOM   5522  C   THR B 415     -24.253  32.364  11.651  1.00 67.28           C  
ANISOU 5522  C   THR B 415     7895   9259   8409    -95    738  -1015       C  
ATOM   5523  O   THR B 415     -24.003  31.169  11.473  1.00 59.40           O  
ANISOU 5523  O   THR B 415     6850   8294   7426    -64    704   -998       O  
ATOM   5524  CB  THR B 415     -22.584  34.228  11.850  1.00 67.75           C  
ANISOU 5524  CB  THR B 415     7966   9342   8433   -206    771  -1129       C  
ATOM   5525  OG1 THR B 415     -23.364  34.831  10.810  1.00 73.22           O  
ANISOU 5525  OG1 THR B 415     8705   9966   9148   -217    811  -1100       O  
ATOM   5526  CG2 THR B 415     -21.381  33.537  11.240  1.00 77.45           C  
ANISOU 5526  CG2 THR B 415     9133  10621   9674   -225    746  -1160       C  
ATOM   5527  N   GLY B 416     -25.231  33.000  11.024  1.00 69.21           N  
ANISOU 5527  N   GLY B 416     8189   9438   8668    -97    773   -983       N  
ATOM   5528  CA  GLY B 416     -26.181  32.324  10.166  1.00 61.28           C  
ANISOU 5528  CA  GLY B 416     7189   8397   7696    -59    772   -924       C  
ATOM   5529  C   GLY B 416     -27.611  32.553  10.624  1.00 63.78           C  
ANISOU 5529  C   GLY B 416     7554   8667   8014    -19    788   -870       C  
ATOM   5530  O   GLY B 416     -27.877  33.127  11.677  1.00 66.27           O  
ANISOU 5530  O   GLY B 416     7896   8979   8302    -15    798   -876       O  
ATOM   5531  N   ASN B 417     -28.536  32.055   9.798  1.00 78.81           N  
ANISOU 5531  N   ASN B 417     9464  10534   9947     11    791   -818       N  
ATOM   5532  CA  ASN B 417     -29.958  32.317  10.010  1.00 68.30           C  
ANISOU 5532  CA  ASN B 417     8178   9152   8621     47    810   -763       C  
ATOM   5533  C   ASN B 417     -30.400  31.959  11.424  1.00 67.62           C  
ANISOU 5533  C   ASN B 417     8092   9083   8516     90    794   -744       C  
ATOM   5534  O   ASN B 417     -31.140  32.715  12.063  1.00 74.37           O  
ANISOU 5534  O   ASN B 417     8994   9907   9356     98    818   -728       O  
ATOM   5535  CB  ASN B 417     -30.784  31.538   8.988  1.00 67.57           C  
ANISOU 5535  CB  ASN B 417     8077   9031   8564     79    804   -711       C  
ATOM   5536  CG  ASN B 417     -31.036  32.324   7.721  1.00 83.97           C  
ANISOU 5536  CG  ASN B 417    10187  11064  10655     48    838   -709       C  
ATOM   5537  OD1 ASN B 417     -30.790  33.529   7.662  1.00 78.19           O  
ANISOU 5537  OD1 ASN B 417     9491  10312   9906      8    873   -739       O  
ATOM   5538  ND2 ASN B 417     -31.519  31.641   6.692  1.00 88.96           N  
ANISOU 5538  ND2 ASN B 417    10805  11679  11317     69    830   -674       N  
ATOM   5539  N   ILE B 418     -29.950  30.811  11.932  1.00 38.95           N  
ANISOU 5539  N   ILE B 418     4411   5501   4887    119    754   -744       N  
ATOM   5540  CA  ILE B 418     -30.395  30.361  13.247  1.00 41.23           C  
ANISOU 5540  CA  ILE B 418     4698   5806   5160    166    737   -721       C  
ATOM   5541  C   ILE B 418     -29.782  31.222  14.344  1.00 42.42           C  
ANISOU 5541  C   ILE B 418     4866   5982   5270    141    744   -768       C  
ATOM   5542  O   ILE B 418     -30.494  31.778  15.189  1.00 41.44           O  
ANISOU 5542  O   ILE B 418     4783   5835   5128    158    761   -751       O  
ATOM   5543  CB  ILE B 418     -30.057  28.872  13.446  1.00 37.06           C  
ANISOU 5543  CB  ILE B 418     4113   5324   4645    207    695   -707       C  
ATOM   5544  CG1 ILE B 418     -30.864  27.996  12.483  1.00 29.60           C  
ANISOU 5544  CG1 ILE B 418     3157   4349   3742    237    689   -655       C  
ATOM   5545  CG2 ILE B 418     -30.312  28.458  14.885  1.00 39.15           C  
ANISOU 5545  CG2 ILE B 418     4373   5613   4888    253    679   -692       C  
ATOM   5546  CD1 ILE B 418     -32.246  28.527  12.146  1.00 30.18           C  
ANISOU 5546  CD1 ILE B 418     3279   4359   3830    252    719   -607       C  
ATOM   5547  N   ALA B 419     -28.453  31.345  14.350  1.00 55.16           N  
ANISOU 5547  N   ALA B 419     6448   7642   6867    100    732   -828       N  
ATOM   5548  CA  ALA B 419     -27.785  32.099  15.406  1.00 55.76           C  
ANISOU 5548  CA  ALA B 419     6535   7749   6904     74    734   -878       C  
ATOM   5549  C   ALA B 419     -28.145  33.578  15.348  1.00 63.03           C  
ANISOU 5549  C   ALA B 419     7517   8620   7810     34    780   -893       C  
ATOM   5550  O   ALA B 419     -28.300  34.226  16.390  1.00 59.37           O  
ANISOU 5550  O   ALA B 419     7085   8157   7317     35    790   -906       O  
ATOM   5551  CB  ALA B 419     -26.272  31.909  15.311  1.00 56.47           C  
ANISOU 5551  CB  ALA B 419     6573   7900   6982     36    711   -940       C  
ATOM   5552  N   ASP B 420     -28.272  34.134  14.141  1.00 66.67           N  
ANISOU 5552  N   ASP B 420     7999   9040   8293      0    809   -892       N  
ATOM   5553  CA  ASP B 420     -28.597  35.551  14.020  1.00 62.77           C  
ANISOU 5553  CA  ASP B 420     7566   8497   7787    -37    856   -906       C  
ATOM   5554  C   ASP B 420     -30.058  35.823  14.362  1.00 61.44           C  
ANISOU 5554  C   ASP B 420     7449   8276   7620      4    879   -847       C  
ATOM   5555  O   ASP B 420     -30.362  36.780  15.084  1.00 66.78           O  
ANISOU 5555  O   ASP B 420     8172   8930   8271     -6    906   -856       O  
ATOM   5556  CB  ASP B 420     -28.283  36.049  12.608  1.00 66.49           C  
ANISOU 5556  CB  ASP B 420     8044   8940   8280    -83    882   -921       C  
ATOM   5557  CG  ASP B 420     -26.835  35.823  12.215  1.00 66.93           C  
ANISOU 5557  CG  ASP B 420     8049   9046   8335   -126    863   -979       C  
ATOM   5558  OD1 ASP B 420     -25.995  35.622  13.118  1.00 62.59           O  
ANISOU 5558  OD1 ASP B 420     7468   8550   7762   -133    837  -1019       O  
ATOM   5559  OD2 ASP B 420     -26.539  35.839  11.002  1.00 65.57           O1-
ANISOU 5559  OD2 ASP B 420     7867   8860   8186   -151    874   -984       O1-
ATOM   5560  N   TYR B 421     -30.979  34.997  13.858  1.00 57.18           N  
ANISOU 5560  N   TYR B 421     6901   7714   7110     51    870   -786       N  
ATOM   5561  CA  TYR B 421     -32.396  35.333  13.885  1.00 51.60           C  
ANISOU 5561  CA  TYR B 421     6243   6951   6411     85    897   -728       C  
ATOM   5562  C   TYR B 421     -33.266  34.407  14.725  1.00 52.77           C  
ANISOU 5562  C   TYR B 421     6382   7105   6565    151    873   -676       C  
ATOM   5563  O   TYR B 421     -34.429  34.748  14.967  1.00 55.48           O  
ANISOU 5563  O   TYR B 421     6767   7404   6910    180    896   -630       O  
ATOM   5564  CB  TYR B 421     -32.971  35.359  12.458  1.00 53.95           C  
ANISOU 5564  CB  TYR B 421     6551   7206   6742     81    915   -696       C  
ATOM   5565  CG  TYR B 421     -32.344  36.374  11.523  1.00 58.72           C  
ANISOU 5565  CG  TYR B 421     7176   7792   7345     21    948   -738       C  
ATOM   5566  CD1 TYR B 421     -31.598  37.442  12.009  1.00 58.77           C  
ANISOU 5566  CD1 TYR B 421     7206   7804   7321    -28    971   -793       C  
ATOM   5567  CD2 TYR B 421     -32.508  36.265  10.148  1.00 50.19           C  
ANISOU 5567  CD2 TYR B 421     6092   6687   6292     12    958   -721       C  
ATOM   5568  CE1 TYR B 421     -31.028  38.366  11.153  1.00 63.64           C  
ANISOU 5568  CE1 TYR B 421     7842   8400   7938    -83   1005   -830       C  
ATOM   5569  CE2 TYR B 421     -31.943  37.186   9.284  1.00 47.44           C  
ANISOU 5569  CE2 TYR B 421     5763   6320   5942    -40    990   -757       C  
ATOM   5570  CZ  TYR B 421     -31.204  38.234   9.792  1.00 55.61           C  
ANISOU 5570  CZ  TYR B 421     6821   7358   6948    -88   1015   -811       C  
ATOM   5571  OH  TYR B 421     -30.640  39.152   8.938  1.00 54.28           O  
ANISOU 5571  OH  TYR B 421     6673   7170   6781   -141   1051   -847       O  
ATOM   5572  N   ASN B 422     -32.761  33.258  15.173  1.00 60.81           N  
ANISOU 5572  N   ASN B 422     7347   8173   7585    178    830   -679       N  
ATOM   5573  CA  ASN B 422     -33.611  32.287  15.854  1.00 56.26           C  
ANISOU 5573  CA  ASN B 422     6759   7599   7019    243    810   -625       C  
ATOM   5574  C   ASN B 422     -33.164  31.970  17.273  1.00 54.31           C  
ANISOU 5574  C   ASN B 422     6496   7398   6740    266    787   -643       C  
ATOM   5575  O   ASN B 422     -33.979  32.037  18.200  1.00 56.49           O  
ANISOU 5575  O   ASN B 422     6800   7659   7006    306    794   -610       O  
ATOM   5576  CB  ASN B 422     -33.689  30.998  15.024  1.00 50.90           C  
ANISOU 5576  CB  ASN B 422     6032   6931   6378    269    782   -596       C  
ATOM   5577  CG  ASN B 422     -34.385  31.208  13.692  1.00 51.14           C  
ANISOU 5577  CG  ASN B 422     6080   6912   6440    259    803   -566       C  
ATOM   5578  OD1 ASN B 422     -35.596  31.020  13.579  1.00 50.51           O  
ANISOU 5578  OD1 ASN B 422     6019   6793   6379    296    812   -510       O  
ATOM   5579  ND2 ASN B 422     -33.623  31.599  12.676  1.00 51.82           N  
ANISOU 5579  ND2 ASN B 422     6158   7000   6530    210    810   -603       N  
ATOM   5580  N   TYR B 423     -31.891  31.638  17.480  1.00 46.00           N  
ANISOU 5580  N   TYR B 423     5401   6404   5673    244    760   -694       N  
ATOM   5581  CA  TYR B 423     -31.413  31.259  18.809  1.00 46.61           C  
ANISOU 5581  CA  TYR B 423     5458   6532   5719    270    734   -713       C  
ATOM   5582  C   TYR B 423     -29.923  31.555  18.881  1.00 52.36           C  
ANISOU 5582  C   TYR B 423     6157   7315   6423    219    720   -786       C  
ATOM   5583  O   TYR B 423     -29.129  30.914  18.185  1.00 54.09           O  
ANISOU 5583  O   TYR B 423     6329   7566   6658    204    698   -805       O  
ATOM   5584  CB  TYR B 423     -31.698  29.787  19.098  1.00 39.62           C  
ANISOU 5584  CB  TYR B 423     4530   5671   4852    332    701   -670       C  
ATOM   5585  CG  TYR B 423     -31.308  29.345  20.491  1.00 38.84           C  
ANISOU 5585  CG  TYR B 423     4414   5623   4721    367    677   -681       C  
ATOM   5586  CD1 TYR B 423     -32.171  29.525  21.563  1.00 48.53           C  
ANISOU 5586  CD1 TYR B 423     5676   6831   5931    409    688   -649       C  
ATOM   5587  CD2 TYR B 423     -30.081  28.743  20.732  1.00 43.19           C  
ANISOU 5587  CD2 TYR B 423     4912   6241   5257    360    644   -723       C  
ATOM   5588  CE1 TYR B 423     -31.821  29.123  22.837  1.00 49.82           C  
ANISOU 5588  CE1 TYR B 423     5824   7041   6063    444    666   -659       C  
ATOM   5589  CE2 TYR B 423     -29.722  28.337  22.002  1.00 48.13           C  
ANISOU 5589  CE2 TYR B 423     5522   6916   5851    395    622   -733       C  
ATOM   5590  CZ  TYR B 423     -30.596  28.529  23.051  1.00 50.52           C  
ANISOU 5590  CZ  TYR B 423     5860   7198   6136    437    633   -701       C  
ATOM   5591  OH  TYR B 423     -30.243  28.127  24.317  1.00 53.82           O  
ANISOU 5591  OH  TYR B 423     6264   7666   6521    475    611   -710       O  
ATOM   5592  N   LYS B 424     -29.546  32.513  19.722  1.00 57.69           N  
ANISOU 5592  N   LYS B 424     6859   8000   7059    192    732   -828       N  
ATOM   5593  CA  LYS B 424     -28.164  32.951  19.854  1.00 58.59           C  
ANISOU 5593  CA  LYS B 424     6949   8164   7148    139    721   -903       C  
ATOM   5594  C   LYS B 424     -27.635  32.597  21.236  1.00 64.41           C  
ANISOU 5594  C   LYS B 424     7665   8962   7848    165    692   -926       C  
ATOM   5595  O   LYS B 424     -28.311  32.830  22.244  1.00 68.74           O  
ANISOU 5595  O   LYS B 424     8246   9496   8374    198    699   -906       O  
ATOM   5596  CB  LYS B 424     -28.040  34.457  19.618  1.00 61.61           C  
ANISOU 5596  CB  LYS B 424     7382   8512   7517     77    762   -942       C  
ATOM   5597  CG  LYS B 424     -26.619  34.985  19.743  1.00 63.43           C  
ANISOU 5597  CG  LYS B 424     7588   8790   7722     17    754  -1022       C  
ATOM   5598  CD  LYS B 424     -25.781  34.588  18.539  1.00 68.36           C  
ANISOU 5598  CD  LYS B 424     8166   9432   8373    -17    744  -1043       C  
ATOM   5599  CE  LYS B 424     -24.295  34.675  18.844  1.00 68.48           C  
ANISOU 5599  CE  LYS B 424     8139   9516   8366    -60    722  -1116       C  
ATOM   5600  NZ  LYS B 424     -23.467  34.516  17.617  1.00 62.92           N  
ANISOU 5600  NZ  LYS B 424     7398   8821   7687   -101    720  -1141       N  
ATOM   5601  N   LEU B 425     -26.428  32.032  21.276  1.00 61.04           N  
ANISOU 5601  N   LEU B 425     7180   8600   7412    152    658   -968       N  
ATOM   5602  CA  LEU B 425     -25.723  31.763  22.515  1.00 59.19           C  
ANISOU 5602  CA  LEU B 425     6920   8433   7139    170    629  -1001       C  
ATOM   5603  C   LEU B 425     -24.659  32.826  22.761  1.00 63.15           C  
ANISOU 5603  C   LEU B 425     7424   8963   7608    103    634  -1080       C  
ATOM   5604  O   LEU B 425     -24.046  33.330  21.814  1.00 71.48           O  
ANISOU 5604  O   LEU B 425     8472  10011   8677     44    648  -1115       O  
ATOM   5605  CB  LEU B 425     -25.061  30.382  22.476  1.00 49.97           C  
ANISOU 5605  CB  LEU B 425     5683   7325   5979    204    587   -995       C  
ATOM   5606  CG  LEU B 425     -26.021  29.194  22.487  1.00 51.15           C  
ANISOU 5606  CG  LEU B 425     5823   7456   6155    277    577   -922       C  
ATOM   5607  CD1 LEU B 425     -25.397  27.994  21.808  1.00 51.23           C  
ANISOU 5607  CD1 LEU B 425     5772   7504   6190    290    548   -916       C  
ATOM   5608  CD2 LEU B 425     -26.425  28.856  23.906  1.00 54.82           C  
ANISOU 5608  CD2 LEU B 425     6296   7942   6590    336    564   -901       C  
ATOM   5609  N   PRO B 426     -24.418  33.192  24.017  1.00 59.69           N  
ANISOU 5609  N   PRO B 426     6995   8557   7126    109    626  -1109       N  
ATOM   5610  CA  PRO B 426     -23.401  34.208  24.304  1.00 65.30           C  
ANISOU 5610  CA  PRO B 426     7708   9298   7806     44    630  -1187       C  
ATOM   5611  C   PRO B 426     -22.003  33.694  24.001  1.00 68.96           C  
ANISOU 5611  C   PRO B 426     8101   9832   8267     16    597  -1237       C  
ATOM   5612  O   PRO B 426     -21.754  32.490  23.915  1.00 65.04           O  
ANISOU 5612  O   PRO B 426     7554   9376   7782     57    565  -1214       O  
ATOM   5613  CB  PRO B 426     -23.581  34.481  25.801  1.00 66.47           C  
ANISOU 5613  CB  PRO B 426     7879   9468   7907     72    622  -1198       C  
ATOM   5614  CG  PRO B 426     -24.194  33.233  26.337  1.00 60.52           C  
ANISOU 5614  CG  PRO B 426     7106   8730   7158    156    597  -1137       C  
ATOM   5615  CD  PRO B 426     -25.075  32.701  25.241  1.00 61.22           C  
ANISOU 5615  CD  PRO B 426     7201   8763   7298    177    612  -1072       C  
ATOM   5616  N   ASP B 427     -21.082  34.643  23.816  1.00 74.00           N  
ANISOU 5616  N   ASP B 427     8738  10486   8892    -57    608  -1307       N  
ATOM   5617  CA  ASP B 427     -19.690  34.277  23.581  1.00 66.05           C  
ANISOU 5617  CA  ASP B 427     7666   9550   7881    -89    578  -1360       C  
ATOM   5618  C   ASP B 427     -19.120  33.510  24.768  1.00 78.97           C  
ANISOU 5618  C   ASP B 427     9257  11268   9480    -46    533  -1375       C  
ATOM   5619  O   ASP B 427     -18.413  32.510  24.590  1.00 79.16           O  
ANISOU 5619  O   ASP B 427     9219  11348   9510    -26    499  -1376       O  
ATOM   5620  CB  ASP B 427     -18.859  35.527  23.294  1.00 64.21           C  
ANISOU 5620  CB  ASP B 427     7444   9316   7638   -175    601  -1434       C  
ATOM   5621  CG  ASP B 427     -19.226  36.179  21.975  1.00 82.08           C  
ANISOU 5621  CG  ASP B 427     9741  11507   9940   -219    644  -1422       C  
ATOM   5622  OD1 ASP B 427     -20.098  35.635  21.264  1.00 85.52           O  
ANISOU 5622  OD1 ASP B 427    10188  11896  10408   -182    653  -1359       O  
ATOM   5623  OD2 ASP B 427     -18.643  37.234  21.648  1.00 87.34           O1-
ANISOU 5623  OD2 ASP B 427    10422  12161  10603   -289    670  -1477       O1-
ATOM   5624  N   ASP B 428     -19.415  33.960  25.983  1.00 86.66           N  
ANISOU 5624  N   ASP B 428    10262  12250  10415    -28    532  -1385       N  
ATOM   5625  CA  ASP B 428     -19.035  33.233  27.194  1.00 89.35           C  
ANISOU 5625  CA  ASP B 428    10568  12664  10718     23    491  -1392       C  
ATOM   5626  C   ASP B 428     -20.158  32.312  27.665  1.00 83.05           C  
ANISOU 5626  C   ASP B 428     9785  11845   9926    110    485  -1313       C  
ATOM   5627  O   ASP B 428     -20.575  32.344  28.822  1.00 84.79           O  
ANISOU 5627  O   ASP B 428    10027  12075  10112    151    479  -1303       O  
ATOM   5628  CB  ASP B 428     -18.632  34.216  28.288  1.00 98.19           C  
ANISOU 5628  CB  ASP B 428    11710  13812  11788     -7    491  -1452       C  
ATOM   5629  CG  ASP B 428     -19.733  35.208  28.623  1.00 96.09           C  
ANISOU 5629  CG  ASP B 428    11525  13471  11515    -11    531  -1433       C  
ATOM   5630  OD1 ASP B 428     -20.754  35.241  27.902  1.00 80.74           O  
ANISOU 5630  OD1 ASP B 428     9618  11453   9606      2    562  -1376       O  
ATOM   5631  OD2 ASP B 428     -19.577  35.954  29.612  1.00 95.95           O1-
ANISOU 5631  OD2 ASP B 428    11533  13470  11455    -26    532  -1474       O1-
ATOM   5632  N   PHE B 429     -20.655  31.473  26.761  1.00 64.56           N  
ANISOU 5632  N   PHE B 429     7430   9473   7628    139    487  -1257       N  
ATOM   5633  CA  PHE B 429     -21.738  30.556  27.090  1.00 64.69           C  
ANISOU 5633  CA  PHE B 429     7458   9465   7658    219    484  -1181       C  
ATOM   5634  C   PHE B 429     -21.187  29.392  27.902  1.00 68.38           C  
ANISOU 5634  C   PHE B 429     7870  10008   8101    277    442  -1177       C  
ATOM   5635  O   PHE B 429     -20.255  28.708  27.466  1.00 75.83           O  
ANISOU 5635  O   PHE B 429     8755  11004   9052    271    417  -1196       O  
ATOM   5636  CB  PHE B 429     -22.423  30.053  25.822  1.00 61.68           C  
ANISOU 5636  CB  PHE B 429     7079   9026   7331    227    501  -1126       C  
ATOM   5637  CG  PHE B 429     -23.274  28.832  26.034  1.00 57.57           C  
ANISOU 5637  CG  PHE B 429     6550   8496   6829    307    489  -1053       C  
ATOM   5638  CD1 PHE B 429     -24.413  28.893  26.819  1.00 61.33           C  
ANISOU 5638  CD1 PHE B 429     7072   8934   7298    357    503  -1007       C  
ATOM   5639  CD2 PHE B 429     -22.937  27.625  25.443  1.00 58.49           C  
ANISOU 5639  CD2 PHE B 429     6614   8639   6972    334    467  -1031       C  
ATOM   5640  CE1 PHE B 429     -25.199  27.772  27.015  1.00 57.74           C  
ANISOU 5640  CE1 PHE B 429     6608   8468   6862    430    495   -940       C  
ATOM   5641  CE2 PHE B 429     -23.719  26.501  25.635  1.00 53.18           C  
ANISOU 5641  CE2 PHE B 429     5933   7954   6318    406    459   -965       C  
ATOM   5642  CZ  PHE B 429     -24.852  26.575  26.420  1.00 51.37           C  
ANISOU 5642  CZ  PHE B 429     5748   7687   6082    454    474   -920       C  
ATOM   5643  N   THR B 430     -21.760  29.169  29.079  1.00 77.54           N  
ANISOU 5643  N   THR B 430     9051  11178   9234    336    436  -1150       N  
ATOM   5644  CA  THR B 430     -21.379  28.062  29.951  1.00 79.33           C  
ANISOU 5644  CA  THR B 430     9232  11473   9436    402    399  -1139       C  
ATOM   5645  C   THR B 430     -22.544  27.078  29.971  1.00 81.80           C  
ANISOU 5645  C   THR B 430     9558  11744   9778    477    406  -1055       C  
ATOM   5646  O   THR B 430     -23.556  27.312  30.638  1.00 73.86           O  
ANISOU 5646  O   THR B 430     8599  10698   8764    514    424  -1018       O  
ATOM   5647  CB  THR B 430     -21.034  28.556  31.353  1.00 75.08           C  
ANISOU 5647  CB  THR B 430     8704  10983   8839    412    385  -1179       C  
ATOM   5648  OG1 THR B 430     -19.849  29.360  31.299  1.00 84.89           O  
ANISOU 5648  OG1 THR B 430     9926  12271  10057    340    375  -1261       O  
ATOM   5649  CG2 THR B 430     -20.793  27.379  32.289  1.00 77.71           C  
ANISOU 5649  CG2 THR B 430     8997  11383   9148    490    351  -1158       C  
ATOM   5650  N   GLY B 431     -22.401  25.986  29.233  1.00 79.07           N  
ANISOU 5650  N   GLY B 431     9168  11407   9466    500    394  -1024       N  
ATOM   5651  CA  GLY B 431     -23.452  24.993  29.176  1.00 69.96           C  
ANISOU 5651  CA  GLY B 431     8022  10215   8344    568    400   -947       C  
ATOM   5652  C   GLY B 431     -23.197  23.987  28.077  1.00 70.93           C  
ANISOU 5652  C   GLY B 431     8100  10341   8510    572    391   -925       C  
ATOM   5653  O   GLY B 431     -22.184  24.035  27.372  1.00 83.35           O  
ANISOU 5653  O   GLY B 431     9636  11947  10087    524    379   -968       O  
ATOM   5654  N   CYS B 432     -24.152  23.070  27.942  1.00 64.29           N  
ANISOU 5654  N   CYS B 432     7263   9462   7701    630    398   -856       N  
ATOM   5655  CA  CYS B 432     -24.077  21.978  26.985  1.00 67.41           C  
ANISOU 5655  CA  CYS B 432     7620   9854   8138    644    391   -826       C  
ATOM   5656  C   CYS B 432     -25.075  22.188  25.853  1.00 70.22           C  
ANISOU 5656  C   CYS B 432     8009  10126   8544    623    419   -787       C  
ATOM   5657  O   CYS B 432     -26.145  22.772  26.043  1.00 64.22           O  
ANISOU 5657  O   CYS B 432     7300   9309   7791    629    443   -758       O  
ATOM   5658  CB  CYS B 432     -24.352  20.632  27.663  1.00 67.18           C  
ANISOU 5658  CB  CYS B 432     7566   9849   8110    729    377   -777       C  
ATOM   5659  SG  CYS B 432     -23.138  20.150  28.907  1.00 88.89           S  
ANISOU 5659  SG  CYS B 432    10269  12704  10802    765    341   -815       S  
ATOM   5660  N   VAL B 433     -24.709  21.702  24.670  1.00 55.77           N  
ANISOU 5660  N   VAL B 433     6148   8293   6749    600    414   -787       N  
ATOM   5661  CA  VAL B 433     -25.580  21.705  23.501  1.00 41.04           C  
ANISOU 5661  CA  VAL B 433     4305   6356   4933    585    436   -750       C  
ATOM   5662  C   VAL B 433     -25.737  20.257  23.062  1.00 47.02           C  
ANISOU 5662  C   VAL B 433     5025   7116   5724    632    424   -705       C  
ATOM   5663  O   VAL B 433     -24.764  19.619  22.639  1.00 57.86           O  
ANISOU 5663  O   VAL B 433     6350   8535   7099    625    404   -727       O  
ATOM   5664  CB  VAL B 433     -25.021  22.571  22.365  1.00 41.45           C  
ANISOU 5664  CB  VAL B 433     4359   6393   4995    506    446   -794       C  
ATOM   5665  CG1 VAL B 433     -25.806  22.333  21.084  1.00 42.49           C  
ANISOU 5665  CG1 VAL B 433     4504   6462   5179    498    464   -753       C  
ATOM   5666  CG2 VAL B 433     -25.055  24.041  22.754  1.00 48.30           C  
ANISOU 5666  CG2 VAL B 433     5272   7244   5834    460    466   -831       C  
ATOM   5667  N   ILE B 434     -26.957  19.735  23.156  1.00 55.25           N  
ANISOU 5667  N   ILE B 434     6089   8109   6794    680    437   -643       N  
ATOM   5668  CA  ILE B 434     -27.246  18.339  22.848  1.00 57.77           C  
ANISOU 5668  CA  ILE B 434     6378   8426   7147    730    429   -596       C  
ATOM   5669  C   ILE B 434     -28.197  18.303  21.661  1.00 56.14           C  
ANISOU 5669  C   ILE B 434     6192   8149   6991    714    448   -559       C  
ATOM   5670  O   ILE B 434     -29.298  18.863  21.723  1.00 59.16           O  
ANISOU 5670  O   ILE B 434     6618   8475   7385    717    470   -529       O  
ATOM   5671  CB  ILE B 434     -27.844  17.597  24.054  1.00 63.05           C  
ANISOU 5671  CB  ILE B 434     7049   9103   7805    806    427   -552       C  
ATOM   5672  CG1 ILE B 434     -26.900  17.684  25.257  1.00 65.09           C  
ANISOU 5672  CG1 ILE B 434     7289   9434   8008    823    408   -591       C  
ATOM   5673  CG2 ILE B 434     -28.122  16.144  23.696  1.00 67.02           C  
ANISOU 5673  CG2 ILE B 434     7520   9599   8344    855    422   -506       C  
ATOM   5674  CD1 ILE B 434     -27.263  18.766  26.252  1.00 61.61           C  
ANISOU 5674  CD1 ILE B 434     6893   8986   7531    820    419   -604       C  
ATOM   5675  N   ALA B 435     -27.774  17.640  20.586  1.00 44.53           N  
ANISOU 5675  N   ALA B 435     4689   6682   5550    699    439   -561       N  
ATOM   5676  CA  ALA B 435     -28.565  17.543  19.370  1.00 40.45           C  
ANISOU 5676  CA  ALA B 435     4186   6104   5080    683    454   -531       C  
ATOM   5677  C   ALA B 435     -28.523  16.115  18.849  1.00 45.18           C  
ANISOU 5677  C   ALA B 435     4745   6709   5712    718    442   -501       C  
ATOM   5678  O   ALA B 435     -27.516  15.416  18.991  1.00 58.57           O  
ANISOU 5678  O   ALA B 435     6399   8461   7395    729    422   -522       O  
ATOM   5679  CB  ALA B 435     -28.062  18.508  18.290  1.00 44.11           C  
ANISOU 5679  CB  ALA B 435     4658   6556   5546    610    461   -573       C  
ATOM   5680  N   TRP B 436     -29.629  15.687  18.243  1.00 49.75           N  
ANISOU 5680  N   TRP B 436     5339   7231   6334    735    454   -452       N  
ATOM   5681  CA  TRP B 436     -29.710  14.357  17.658  1.00 52.44           C  
ANISOU 5681  CA  TRP B 436     5646   7568   6709    764    446   -423       C  
ATOM   5682  C   TRP B 436     -30.695  14.376  16.500  1.00 51.80           C  
ANISOU 5682  C   TRP B 436     5585   7422   6674    747    460   -392       C  
ATOM   5683  O   TRP B 436     -31.563  15.247  16.409  1.00 46.70           O  
ANISOU 5683  O   TRP B 436     4979   6731   6034    731    478   -379       O  
ATOM   5684  CB  TRP B 436     -30.126  13.305  18.689  1.00 48.57           C  
ANISOU 5684  CB  TRP B 436     5144   7089   6221    836    443   -381       C  
ATOM   5685  CG  TRP B 436     -31.503  13.502  19.244  1.00 47.60           C  
ANISOU 5685  CG  TRP B 436     5059   6915   6112    868    462   -334       C  
ATOM   5686  CD1 TRP B 436     -32.640  12.853  18.861  1.00 43.53           C  
ANISOU 5686  CD1 TRP B 436     4551   6347   5641    895    474   -281       C  
ATOM   5687  CD2 TRP B 436     -31.887  14.403  20.290  1.00 45.31           C  
ANISOU 5687  CD2 TRP B 436     4804   6621   5790    876    473   -334       C  
ATOM   5688  NE1 TRP B 436     -33.709  13.296  19.601  1.00 41.35           N  
ANISOU 5688  NE1 TRP B 436     4311   6036   5364    920    492   -248       N  
ATOM   5689  CE2 TRP B 436     -33.274  14.247  20.485  1.00 44.87           C  
ANISOU 5689  CE2 TRP B 436     4776   6509   5763    910    492   -279       C  
ATOM   5690  CE3 TRP B 436     -31.195  15.328  21.077  1.00 46.13           C  
ANISOU 5690  CE3 TRP B 436     4919   6763   5845    857    469   -377       C  
ATOM   5691  CZ2 TRP B 436     -33.980  14.981  21.436  1.00 47.63           C  
ANISOU 5691  CZ2 TRP B 436     5165   6839   6093    927    507   -263       C  
ATOM   5692  CZ3 TRP B 436     -31.897  16.054  22.021  1.00 49.99           C  
ANISOU 5692  CZ3 TRP B 436     5448   7232   6313    873    484   -363       C  
ATOM   5693  CH2 TRP B 436     -33.276  15.877  22.192  1.00 46.22           C  
ANISOU 5693  CH2 TRP B 436     4998   6698   5864    909    503   -305       C  
ATOM   5694  N   ASN B 437     -30.549  13.392  15.616  1.00 57.81           N  
ANISOU 5694  N   ASN B 437     6317   8180   7467    752    451   -381       N  
ATOM   5695  CA  ASN B 437     -31.400  13.308  14.438  1.00 50.82           C  
ANISOU 5695  CA  ASN B 437     5445   7239   6625    736    461   -356       C  
ATOM   5696  C   ASN B 437     -32.801  12.854  14.825  1.00 47.80           C  
ANISOU 5696  C   ASN B 437     5081   6810   6271    782    474   -297       C  
ATOM   5697  O   ASN B 437     -32.970  11.867  15.547  1.00 45.14           O  
ANISOU 5697  O   ASN B 437     4726   6485   5941    834    470   -269       O  
ATOM   5698  CB  ASN B 437     -30.790  12.350  13.416  1.00 52.10           C  
ANISOU 5698  CB  ASN B 437     5571   7414   6811    729    448   -363       C  
ATOM   5699  CG  ASN B 437     -31.616  12.242  12.152  1.00 54.33           C  
ANISOU 5699  CG  ASN B 437     5866   7642   7137    711    456   -340       C  
ATOM   5700  OD1 ASN B 437     -32.594  11.498  12.099  1.00 48.20           O  
ANISOU 5700  OD1 ASN B 437     5090   6830   6393    746    460   -295       O  
ATOM   5701  ND2 ASN B 437     -31.226  12.987  11.124  1.00 50.91           N  
ANISOU 5701  ND2 ASN B 437     5441   7202   6702    658    457   -371       N  
ATOM   5702  N   SER B 438     -33.805  13.578  14.341  1.00 49.86           N  
ANISOU 5702  N   SER B 438     5377   7018   6550    763    490   -278       N  
ATOM   5703  CA  SER B 438     -35.207  13.263  14.580  1.00 53.18           C  
ANISOU 5703  CA  SER B 438     5816   7390   7000    800    504   -223       C  
ATOM   5704  C   SER B 438     -35.955  13.100  13.263  1.00 54.25           C  
ANISOU 5704  C   SER B 438     5956   7479   7179    781    508   -203       C  
ATOM   5705  O   SER B 438     -37.109  13.512  13.125  1.00 53.22           O  
ANISOU 5705  O   SER B 438     5853   7301   7066    784    523   -171       O  
ATOM   5706  CB  SER B 438     -35.868  14.333  15.445  1.00 49.30           C  
ANISOU 5706  CB  SER B 438     5366   6879   6486    804    521   -213       C  
ATOM   5707  OG  SER B 438     -35.775  15.609  14.837  1.00 53.40           O  
ANISOU 5707  OG  SER B 438     5915   7384   6992    751    531   -242       O  
ATOM   5708  N   ASN B 439     -35.292  12.498  12.272  1.00 50.78           N  
ANISOU 5708  N   ASN B 439     5487   7052   6754    761    494   -222       N  
ATOM   5709  CA  ASN B 439     -35.937  12.263  10.984  1.00 43.05           C  
ANISOU 5709  CA  ASN B 439     4509   6032   5814    744    496   -206       C  
ATOM   5710  C   ASN B 439     -37.127  11.325  11.129  1.00 48.63           C  
ANISOU 5710  C   ASN B 439     5212   6703   6561    789    501   -152       C  
ATOM   5711  O   ASN B 439     -38.143  11.487  10.444  1.00 50.89           O  
ANISOU 5711  O   ASN B 439     5514   6945   6876    782    509   -127       O  
ATOM   5712  CB  ASN B 439     -34.928  11.697   9.986  1.00 44.55           C  
ANISOU 5712  CB  ASN B 439     4669   6247   6011    720    480   -236       C  
ATOM   5713  CG  ASN B 439     -35.338  11.930   8.548  1.00 42.26           C  
ANISOU 5713  CG  ASN B 439     4389   5922   5747    686    482   -236       C  
ATOM   5714  OD1 ASN B 439     -35.895  12.974   8.211  1.00 46.93           O  
ANISOU 5714  OD1 ASN B 439     5013   6484   6335    660    495   -236       O  
ATOM   5715  ND2 ASN B 439     -35.055  10.959   7.688  1.00 42.52           N  
ANISOU 5715  ND2 ASN B 439     4394   5957   5805    686    470   -237       N  
ATOM   5716  N   LYS B 440     -37.018  10.331  12.012  1.00 65.56           N  
ANISOU 5716  N   LYS B 440     7334   8867   8708    835    496   -134       N  
ATOM   5717  CA  LYS B 440     -38.127   9.408  12.219  1.00 64.45           C  
ANISOU 5717  CA  LYS B 440     7189   8692   8608    878    504    -83       C  
ATOM   5718  C   LYS B 440     -39.341  10.109  12.817  1.00 65.11           C  
ANISOU 5718  C   LYS B 440     7307   8738   8694    893    522    -48       C  
ATOM   5719  O   LYS B 440     -40.480   9.730  12.521  1.00 68.35           O  
ANISOU 5719  O   LYS B 440     7721   9106   9144    909    530     -9       O  
ATOM   5720  CB  LYS B 440     -37.686   8.253  13.116  1.00 67.46           C  
ANISOU 5720  CB  LYS B 440     7541   9104   8987    927    499    -71       C  
ATOM   5721  CG  LYS B 440     -38.530   7.000  12.969  1.00 83.67           C  
ANISOU 5721  CG  LYS B 440     9578  11125  11088    964    504    -28       C  
ATOM   5722  CD  LYS B 440     -38.029   6.130  11.828  1.00 95.08           C  
ANISOU 5722  CD  LYS B 440    10994  12574  12558    947    491    -42       C  
ATOM   5723  CE  LYS B 440     -38.998   4.996  11.535  1.00 96.00           C  
ANISOU 5723  CE  LYS B 440    11098  12651  12726    976    498      0       C  
ATOM   5724  NZ  LYS B 440     -39.127   4.064  12.689  1.00 75.10           N  
ANISOU 5724  NZ  LYS B 440     8438  10012  10084   1034    507     30       N  
ATOM   5725  N   LEU B 441     -39.122  11.127  13.647  1.00 46.96           N  
ANISOU 5725  N   LEU B 441     5033   6453   6355    888    529    -63       N  
ATOM   5726  CA  LEU B 441     -40.202  11.812  14.348  1.00 45.93           C  
ANISOU 5726  CA  LEU B 441     4937   6290   6223    906    548    -30       C  
ATOM   5727  C   LEU B 441     -40.677  13.071  13.633  1.00 52.28           C  
ANISOU 5727  C   LEU B 441     5776   7064   7024    864    559    -38       C  
ATOM   5728  O   LEU B 441     -41.881  13.251  13.431  1.00 53.74           O  
ANISOU 5728  O   LEU B 441     5979   7205   7235    872    573      0       O  
ATOM   5729  CB  LEU B 441     -39.759  12.171  15.772  1.00 42.66           C  
ANISOU 5729  CB  LEU B 441     4534   5909   5767    931    552    -39       C  
ATOM   5730  CG  LEU B 441     -39.434  11.017  16.721  1.00 50.92           C  
ANISOU 5730  CG  LEU B 441     5552   6984   6812    984    546    -24       C  
ATOM   5731  CD1 LEU B 441     -38.245  11.372  17.601  1.00 40.24           C  
ANISOU 5731  CD1 LEU B 441     4195   5687   5407    984    537    -64       C  
ATOM   5732  CD2 LEU B 441     -40.646  10.666  17.567  1.00 47.20           C  
ANISOU 5732  CD2 LEU B 441     5094   6478   6361   1036    564     31       C  
ATOM   5733  N   ASP B 442     -39.755  13.949  13.245  1.00 55.95           N  
ANISOU 5733  N   ASP B 442     6249   7552   7457    818    555    -85       N  
ATOM   5734  CA  ASP B 442     -40.105  15.282  12.776  1.00 47.20           C  
ANISOU 5734  CA  ASP B 442     5180   6419   6337    780    570    -95       C  
ATOM   5735  C   ASP B 442     -40.144  15.409  11.259  1.00 45.90           C  
ANISOU 5735  C   ASP B 442     5011   6234   6193    741    567   -106       C  
ATOM   5736  O   ASP B 442     -40.356  16.515  10.752  1.00 47.14           O  
ANISOU 5736  O   ASP B 442     5199   6371   6339    708    581   -116       O  
ATOM   5737  CB  ASP B 442     -39.131  16.309  13.360  1.00 48.22           C  
ANISOU 5737  CB  ASP B 442     5326   6581   6416    753    573   -141       C  
ATOM   5738  CG  ASP B 442     -39.246  16.420  14.868  1.00 58.57           C  
ANISOU 5738  CG  ASP B 442     6649   7906   7701    790    580   -129       C  
ATOM   5739  OD1 ASP B 442     -40.385  16.385  15.380  1.00 59.81           O  
ANISOU 5739  OD1 ASP B 442     6824   8029   7872    824    594    -83       O  
ATOM   5740  OD2 ASP B 442     -38.201  16.541  15.541  1.00 58.65           O1-
ANISOU 5740  OD2 ASP B 442     6649   7961   7674    786    570   -165       O1-
ATOM   5741  N   SER B 443     -39.944  14.322  10.523  1.00 47.42           N  
ANISOU 5741  N   SER B 443     5170   6432   6415    745    551   -104       N  
ATOM   5742  CA  SER B 443     -40.128  14.328   9.080  1.00 45.41           C  
ANISOU 5742  CA  SER B 443     4912   6156   6185    714    547   -109       C  
ATOM   5743  C   SER B 443     -41.460  13.690   8.712  1.00 48.58           C  
ANISOU 5743  C   SER B 443     5312   6516   6632    740    550    -60       C  
ATOM   5744  O   SER B 443     -42.050  12.928   9.482  1.00 52.74           O  
ANISOU 5744  O   SER B 443     5827   7035   7176    783    551    -25       O  
ATOM   5745  CB  SER B 443     -38.989  13.594   8.368  1.00 45.74           C  
ANISOU 5745  CB  SER B 443     4919   6230   6229    696    527   -143       C  
ATOM   5746  OG  SER B 443     -37.802  14.363   8.368  1.00 58.34           O  
ANISOU 5746  OG  SER B 443     6520   7860   7788    661    526   -192       O  
ATOM   5747  N   LYS B 444     -41.929  14.018   7.512  1.00 46.74           N  
ANISOU 5747  N   LYS B 444     5087   6256   6415    714    551    -58       N  
ATOM   5748  CA  LYS B 444     -43.184  13.491   7.000  1.00 43.44           C  
ANISOU 5748  CA  LYS B 444     4665   5800   6040    733    552    -15       C  
ATOM   5749  C   LYS B 444     -43.073  13.388   5.487  1.00 47.99           C  
ANISOU 5749  C   LYS B 444     5234   6369   6633    701    542    -32       C  
ATOM   5750  O   LYS B 444     -42.446  14.239   4.849  1.00 47.91           O  
ANISOU 5750  O   LYS B 444     5239   6367   6599    663    545    -65       O  
ATOM   5751  CB  LYS B 444     -44.362  14.381   7.407  1.00 49.56           C  
ANISOU 5751  CB  LYS B 444     5476   6541   6814    744    574     19       C  
ATOM   5752  CG  LYS B 444     -45.724  13.856   6.994  1.00 56.54           C  
ANISOU 5752  CG  LYS B 444     6353   7388   7742    765    575     65       C  
ATOM   5753  CD  LYS B 444     -46.763  14.957   7.045  1.00 57.58           C  
ANISOU 5753  CD  LYS B 444     6522   7487   7867    765    597     91       C  
ATOM   5754  CE  LYS B 444     -46.614  15.786   8.307  1.00 49.63           C  
ANISOU 5754  CE  LYS B 444     5545   6488   6825    775    615     91       C  
ATOM   5755  NZ  LYS B 444     -47.684  16.807   8.398  1.00 49.30           N  
ANISOU 5755  NZ  LYS B 444     5540   6413   6779    779    638    121       N  
ATOM   5756  N   VAL B 445     -43.679  12.340   4.922  1.00 64.76           N  
ANISOU 5756  N   VAL B 445     7333   8475   8798    716    531     -8       N  
ATOM   5757  CA  VAL B 445     -43.540  12.079   3.490  1.00 66.46           C  
ANISOU 5757  CA  VAL B 445     7537   8685   9029    690    518    -24       C  
ATOM   5758  C   VAL B 445     -44.049  13.263   2.679  1.00 66.52           C  
ANISOU 5758  C   VAL B 445     7577   8671   9028    663    530    -26       C  
ATOM   5759  O   VAL B 445     -43.402  13.703   1.719  1.00 68.38           O  
ANISOU 5759  O   VAL B 445     7818   8914   9249    629    526    -57       O  
ATOM   5760  CB  VAL B 445     -44.267  10.774   3.113  1.00 64.55           C  
ANISOU 5760  CB  VAL B 445     7266   8425   8834    713    506      4       C  
ATOM   5761  CG1 VAL B 445     -44.575  10.744   1.623  1.00 55.64           C  
ANISOU 5761  CG1 VAL B 445     6136   7281   7725    688    497     -3       C  
ATOM   5762  CG2 VAL B 445     -43.428   9.569   3.512  1.00 62.83           C  
ANISOU 5762  CG2 VAL B 445     7016   8234   8624    730    494     -8       C  
ATOM   5763  N   GLY B 446     -45.201  13.810   3.057  1.00 40.66           N  
ANISOU 5763  N   GLY B 446     4324   5367   5758    679    545     10       N  
ATOM   5764  CA  GLY B 446     -45.709  15.000   2.412  1.00 45.96           C  
ANISOU 5764  CA  GLY B 446     5028   6018   6416    657    560     13       C  
ATOM   5765  C   GLY B 446     -45.047  16.288   2.838  1.00 44.28           C  
ANISOU 5765  C   GLY B 446     4848   5816   6159    635    578    -14       C  
ATOM   5766  O   GLY B 446     -45.372  17.351   2.302  1.00 49.76           O  
ANISOU 5766  O   GLY B 446     5573   6493   6839    616    594    -14       O  
ATOM   5767  N   GLY B 447     -44.121  16.224   3.791  1.00 44.09           N  
ANISOU 5767  N   GLY B 447     4820   5821   6113    637    577    -36       N  
ATOM   5768  CA  GLY B 447     -43.447  17.408   4.281  1.00 42.07           C  
ANISOU 5768  CA  GLY B 447     4593   5578   5814    614    594    -64       C  
ATOM   5769  C   GLY B 447     -44.029  17.906   5.587  1.00 41.61           C  
ANISOU 5769  C   GLY B 447     4559   5510   5743    640    611    -39       C  
ATOM   5770  O   GLY B 447     -45.215  18.243   5.656  1.00 44.84           O  
ANISOU 5770  O   GLY B 447     4988   5887   6164    657    625      0       O  
ATOM   5771  N   ASN B 448     -43.207  17.953   6.632  1.00 41.85           N  
ANISOU 5771  N   ASN B 448     4587   5570   5746    644    611    -60       N  
ATOM   5772  CA  ASN B 448     -43.644  18.424   7.945  1.00 39.31           C  
ANISOU 5772  CA  ASN B 448     4288   5242   5406    668    627    -40       C  
ATOM   5773  C   ASN B 448     -43.364  19.917   8.030  1.00 38.34           C  
ANISOU 5773  C   ASN B 448     4207   5115   5246    637    649    -64       C  
ATOM   5774  O   ASN B 448     -42.219  20.339   8.212  1.00 36.70           O  
ANISOU 5774  O   ASN B 448     4000   4936   5007    609    648   -110       O  
ATOM   5775  CB  ASN B 448     -42.941  17.660   9.060  1.00 38.42           C  
ANISOU 5775  CB  ASN B 448     4151   5164   5284    693    614    -50       C  
ATOM   5776  CG  ASN B 448     -43.382  18.111  10.439  1.00 37.19           C  
ANISOU 5776  CG  ASN B 448     4020   5004   5108    721    630    -29       C  
ATOM   5777  OD1 ASN B 448     -44.512  18.564  10.624  1.00 39.66           O  
ANISOU 5777  OD1 ASN B 448     4358   5281   5430    738    648      9       O  
ATOM   5778  ND2 ASN B 448     -42.490  17.993  11.415  1.00 37.03           N  
ANISOU 5778  ND2 ASN B 448     3990   5019   5059    729    623    -54       N  
ATOM   5779  N   TYR B 449     -44.416  20.723   7.901  1.00 44.63           N  
ANISOU 5779  N   TYR B 449     5038   5874   6044    640    672    -34       N  
ATOM   5780  CA  TYR B 449     -44.303  22.170   7.977  1.00 39.44           C  
ANISOU 5780  CA  TYR B 449     4426   5206   5352    613    699    -52       C  
ATOM   5781  C   TYR B 449     -44.591  22.705   9.374  1.00 40.29           C  
ANISOU 5781  C   TYR B 449     4562   5311   5437    635    716    -39       C  
ATOM   5782  O   TYR B 449     -44.846  23.905   9.531  1.00 41.88           O  
ANISOU 5782  O   TYR B 449     4806   5492   5613    621    744    -40       O  
ATOM   5783  CB  TYR B 449     -45.227  22.823   6.947  1.00 42.00           C  
ANISOU 5783  CB  TYR B 449     4776   5493   5689    604    717    -29       C  
ATOM   5784  CG  TYR B 449     -44.819  22.535   5.518  1.00 44.24           C  
ANISOU 5784  CG  TYR B 449     5041   5782   5988    576    703    -49       C  
ATOM   5785  CD1 TYR B 449     -43.868  23.318   4.876  1.00 45.66           C  
ANISOU 5785  CD1 TYR B 449     5234   5972   6144    533    711    -94       C  
ATOM   5786  CD2 TYR B 449     -45.375  21.473   4.817  1.00 46.87           C  
ANISOU 5786  CD2 TYR B 449     5341   6107   6360    594    682    -25       C  
ATOM   5787  CE1 TYR B 449     -43.487  23.057   3.574  1.00 39.25           C  
ANISOU 5787  CE1 TYR B 449     4405   5162   5344    510    700   -113       C  
ATOM   5788  CE2 TYR B 449     -44.999  21.204   3.512  1.00 49.70           C  
ANISOU 5788  CE2 TYR B 449     5683   6470   6730    570    670    -44       C  
ATOM   5789  CZ  TYR B 449     -44.055  21.999   2.897  1.00 46.12           C  
ANISOU 5789  CZ  TYR B 449     5245   6027   6251    529    679    -88       C  
ATOM   5790  OH  TYR B 449     -43.678  21.737   1.600  1.00 53.76           O  
ANISOU 5790  OH  TYR B 449     6199   6999   7230    508    667   -106       O  
ATOM   5791  N   ASN B 450     -44.562  21.838  10.389  1.00 38.55           N  
ANISOU 5791  N   ASN B 450     4319   5108   5221    670    703    -25       N  
ATOM   5792  CA  ASN B 450     -44.779  22.287  11.760  1.00 38.12           C  
ANISOU 5792  CA  ASN B 450     4289   5052   5142    694    718    -14       C  
ATOM   5793  C   ASN B 450     -43.641  23.177  12.242  1.00 38.11           C  
ANISOU 5793  C   ASN B 450     4307   5078   5094    661    724    -66       C  
ATOM   5794  O   ASN B 450     -43.881  24.209  12.879  1.00 49.90           O  
ANISOU 5794  O   ASN B 450     5841   6557   6560    658    748    -66       O  
ATOM   5795  CB  ASN B 450     -44.939  21.080  12.684  1.00 42.34           C  
ANISOU 5795  CB  ASN B 450     4793   5602   5693    741    701     11       C  
ATOM   5796  CG  ASN B 450     -44.766  21.437  14.147  1.00 41.50           C  
ANISOU 5796  CG  ASN B 450     4706   5509   5553    763    710      9       C  
ATOM   5797  OD1 ASN B 450     -45.378  22.381  14.645  1.00 48.19           O  
ANISOU 5797  OD1 ASN B 450     5596   6332   6383    768    735     25       O  
ATOM   5798  ND2 ASN B 450     -43.923  20.683  14.844  1.00 39.98           N  
ANISOU 5798  ND2 ASN B 450     4485   5356   5350    778    691    -10       N  
ATOM   5799  N   TYR B 451     -42.401  22.802  11.946  1.00 42.55           N  
ANISOU 5799  N   TYR B 451     4840   5680   5649    635    703   -112       N  
ATOM   5800  CA  TYR B 451     -41.236  23.495  12.478  1.00 39.47           C  
ANISOU 5800  CA  TYR B 451     4459   5322   5217    605    705   -165       C  
ATOM   5801  C   TYR B 451     -40.865  24.659  11.568  1.00 42.15           C  
ANISOU 5801  C   TYR B 451     4826   5648   5541    552    724   -198       C  
ATOM   5802  O   TYR B 451     -40.628  24.469  10.370  1.00 45.51           O  
ANISOU 5802  O   TYR B 451     5235   6070   5984    529    717   -208       O  
ATOM   5803  CB  TYR B 451     -40.066  22.527  12.634  1.00 39.85           C  
ANISOU 5803  CB  TYR B 451     4459   5420   5261    605    674   -197       C  
ATOM   5804  CG  TYR B 451     -40.350  21.427  13.626  1.00 41.98           C  
ANISOU 5804  CG  TYR B 451     4704   5705   5542    658    659   -167       C  
ATOM   5805  CD1 TYR B 451     -40.204  21.643  14.988  1.00 37.25           C  
ANISOU 5805  CD1 TYR B 451     4118   5124   4913    681    662   -170       C  
ATOM   5806  CD2 TYR B 451     -40.780  20.177  13.203  1.00 42.20           C  
ANISOU 5806  CD2 TYR B 451     4698   5727   5609    687    643   -135       C  
ATOM   5807  CE1 TYR B 451     -40.466  20.644  15.901  1.00 39.50           C  
ANISOU 5807  CE1 TYR B 451     4382   5422   5206    733    651   -140       C  
ATOM   5808  CE2 TYR B 451     -41.048  19.172  14.108  1.00 43.66           C  
ANISOU 5808  CE2 TYR B 451     4862   5923   5805    737    633   -106       C  
ATOM   5809  CZ  TYR B 451     -40.889  19.410  15.456  1.00 43.84           C  
ANISOU 5809  CZ  TYR B 451     4897   5964   5797    761    638   -108       C  
ATOM   5810  OH  TYR B 451     -41.153  18.411  16.364  1.00 51.50           O  
ANISOU 5810  OH  TYR B 451     5847   6944   6776    814    630    -78       O  
ATOM   5811  N   LEU B 452     -40.811  25.855  12.141  1.00 42.42           N  
ANISOU 5811  N   LEU B 452     4902   5673   5542    535    749   -214       N  
ATOM   5812  CA  LEU B 452     -40.489  27.074  11.419  1.00 40.76           C  
ANISOU 5812  CA  LEU B 452     4725   5447   5315    486    773   -245       C  
ATOM   5813  C   LEU B 452     -39.131  27.604  11.861  1.00 41.08           C  
ANISOU 5813  C   LEU B 452     4764   5526   5320    447    771   -307       C  
ATOM   5814  O   LEU B 452     -38.534  27.136  12.835  1.00 41.34           O  
ANISOU 5814  O   LEU B 452     4775   5595   5336    461    752   -324       O  
ATOM   5815  CB  LEU B 452     -41.566  28.143  11.643  1.00 44.73           C  
ANISOU 5815  CB  LEU B 452     5282   5903   5808    493    810   -213       C  
ATOM   5816  CG  LEU B 452     -43.005  27.819  11.236  1.00 45.63           C  
ANISOU 5816  CG  LEU B 452     5403   5978   5955    530    817   -150       C  
ATOM   5817  CD1 LEU B 452     -43.865  29.071  11.275  1.00 44.04           C  
ANISOU 5817  CD1 LEU B 452     5260   5734   5740    527    858   -128       C  
ATOM   5818  CD2 LEU B 452     -43.049  27.188   9.862  1.00 39.08           C  
ANISOU 5818  CD2 LEU B 452     4545   5145   5159    521    802   -145       C  
ATOM   5819  N   TYR B 453     -38.650  28.599  11.121  1.00 37.15           N  
ANISOU 5819  N   TYR B 453     4289   5017   4809    399    792   -342       N  
ATOM   5820  CA  TYR B 453     -37.439  29.320  11.478  1.00 37.14           C  
ANISOU 5820  CA  TYR B 453     4292   5044   4774    355    797   -402       C  
ATOM   5821  C   TYR B 453     -37.574  30.749  10.978  1.00 35.26           C  
ANISOU 5821  C   TYR B 453     4106   4770   4521    316    838   -417       C  
ATOM   5822  O   TYR B 453     -38.316  31.027  10.032  1.00 38.28           O  
ANISOU 5822  O   TYR B 453     4508   5114   4923    315    856   -389       O  
ATOM   5823  CB  TYR B 453     -36.183  28.659  10.894  1.00 37.65           C  
ANISOU 5823  CB  TYR B 453     4308   5152   4844    329    769   -445       C  
ATOM   5824  CG  TYR B 453     -36.196  28.540   9.386  1.00 40.49           C  
ANISOU 5824  CG  TYR B 453     4660   5495   5231    309    771   -442       C  
ATOM   5825  CD1 TYR B 453     -35.687  29.554   8.585  1.00 40.83           C  
ANISOU 5825  CD1 TYR B 453     4726   5525   5264    259    796   -477       C  
ATOM   5826  CD2 TYR B 453     -36.716  27.413   8.764  1.00 39.21           C  
ANISOU 5826  CD2 TYR B 453     4467   5328   5104    340    750   -405       C  
ATOM   5827  CE1 TYR B 453     -35.699  29.450   7.207  1.00 44.83           C  
ANISOU 5827  CE1 TYR B 453     5226   6015   5793    243    799   -474       C  
ATOM   5828  CE2 TYR B 453     -36.732  27.300   7.387  1.00 40.06           C  
ANISOU 5828  CE2 TYR B 453     4568   5420   5234    323    751   -403       C  
ATOM   5829  CZ  TYR B 453     -36.222  28.321   6.614  1.00 47.78           C  
ANISOU 5829  CZ  TYR B 453     5569   6386   6200    276    775   -437       C  
ATOM   5830  OH  TYR B 453     -36.236  28.210   5.242  1.00 45.61           O  
ANISOU 5830  OH  TYR B 453     5288   6096   5945    261    777   -435       O  
ATOM   5831  N   ARG B 454     -36.849  31.658  11.623  1.00 36.18           N  
ANISOU 5831  N   ARG B 454     4244   4899   4603    283    853   -462       N  
ATOM   5832  CA  ARG B 454     -36.855  33.059  11.227  1.00 41.52           C  
ANISOU 5832  CA  ARG B 454     4970   5542   5262    242    895   -482       C  
ATOM   5833  C   ARG B 454     -35.835  33.265  10.114  1.00 44.73           C  
ANISOU 5833  C   ARG B 454     5360   5960   5674    192    896   -527       C  
ATOM   5834  O   ARG B 454     -34.649  32.964  10.286  1.00 48.98           O  
ANISOU 5834  O   ARG B 454     5864   6544   6204    167    874   -574       O  
ATOM   5835  CB  ARG B 454     -36.550  33.968  12.416  1.00 47.26           C  
ANISOU 5835  CB  ARG B 454     5731   6275   5951    227    913   -512       C  
ATOM   5836  CG  ARG B 454     -36.775  35.442  12.125  1.00 46.55           C  
ANISOU 5836  CG  ARG B 454     5701   6141   5844    191    962   -524       C  
ATOM   5837  CD  ARG B 454     -36.934  36.243  13.404  1.00 52.66           C  
ANISOU 5837  CD  ARG B 454     6516   6909   6584    193    982   -533       C  
ATOM   5838  NE  ARG B 454     -38.074  35.799  14.197  1.00 52.90           N  
ANISOU 5838  NE  ARG B 454     6557   6924   6618    252    978   -476       N  
ATOM   5839  CZ  ARG B 454     -39.322  36.204  14.008  1.00 50.49           C  
ANISOU 5839  CZ  ARG B 454     6292   6570   6323    278   1007   -424       C  
ATOM   5840  NH1 ARG B 454     -39.632  37.063  13.051  1.00 49.58           N  
ANISOU 5840  NH1 ARG B 454     6211   6414   6212    253   1043   -419       N  
ATOM   5841  NH2 ARG B 454     -40.283  35.737  14.800  1.00 48.89           N  
ANISOU 5841  NH2 ARG B 454     6095   6358   6125    332   1000   -374       N  
ATOM   5842  N   LEU B 455     -36.302  33.771   8.975  1.00 31.52           N  
ANISOU 5842  N   LEU B 455     3711   4248   4016    178    922   -511       N  
ATOM   5843  CA  LEU B 455     -35.450  34.007   7.818  1.00 38.14           C  
ANISOU 5843  CA  LEU B 455     4539   5092   4861    134    928   -548       C  
ATOM   5844  C   LEU B 455     -35.009  35.457   7.689  1.00 46.54           C  
ANISOU 5844  C   LEU B 455     5648   6134   5901     84    973   -587       C  
ATOM   5845  O   LEU B 455     -33.929  35.719   7.151  1.00 56.14           O  
ANISOU 5845  O   LEU B 455     6851   7368   7114     39    976   -636       O  
ATOM   5846  CB  LEU B 455     -36.176  33.577   6.536  1.00 42.06           C  
ANISOU 5846  CB  LEU B 455     5030   5561   5389    152    928   -508       C  
ATOM   5847  CG  LEU B 455     -35.429  33.646   5.203  1.00 43.80           C  
ANISOU 5847  CG  LEU B 455     5237   5785   5622    115    932   -536       C  
ATOM   5848  CD1 LEU B 455     -34.066  32.997   5.310  1.00 46.56           C  
ANISOU 5848  CD1 LEU B 455     5536   6186   5968     92    900   -585       C  
ATOM   5849  CD2 LEU B 455     -36.242  32.985   4.104  1.00 44.32           C  
ANISOU 5849  CD2 LEU B 455     5292   5830   5718    143    922   -492       C  
ATOM   5850  N   PHE B 456     -35.810  36.401   8.178  1.00 45.73           N  
ANISOU 5850  N   PHE B 456     5599   5993   5782     91   1008   -567       N  
ATOM   5851  CA  PHE B 456     -35.490  37.819   8.103  1.00 47.44           C  
ANISOU 5851  CA  PHE B 456     5865   6183   5976     45   1056   -601       C  
ATOM   5852  C   PHE B 456     -35.730  38.477   9.453  1.00 54.53           C  
ANISOU 5852  C   PHE B 456     6799   7076   6844     50   1072   -606       C  
ATOM   5853  O   PHE B 456     -36.701  38.159  10.146  1.00 53.17           O  
ANISOU 5853  O   PHE B 456     6637   6893   6672     97   1065   -560       O  
ATOM   5854  CB  PHE B 456     -36.325  38.522   7.028  1.00 44.74           C  
ANISOU 5854  CB  PHE B 456     5566   5789   5645     46   1096   -568       C  
ATOM   5855  CG  PHE B 456     -36.398  37.773   5.731  1.00 46.71           C  
ANISOU 5855  CG  PHE B 456     5783   6039   5925     56   1078   -549       C  
ATOM   5856  CD1 PHE B 456     -35.286  37.670   4.913  1.00 49.95           C  
ANISOU 5856  CD1 PHE B 456     6166   6470   6341     16   1072   -593       C  
ATOM   5857  CD2 PHE B 456     -37.579  37.172   5.329  1.00 51.32           C  
ANISOU 5857  CD2 PHE B 456     6364   6603   6531    103   1068   -488       C  
ATOM   5858  CE1 PHE B 456     -35.350  36.981   3.718  1.00 48.08           C  
ANISOU 5858  CE1 PHE B 456     5902   6235   6131     26   1056   -576       C  
ATOM   5859  CE2 PHE B 456     -37.648  36.483   4.135  1.00 53.63           C  
ANISOU 5859  CE2 PHE B 456     6629   6898   6851    111   1051   -473       C  
ATOM   5860  CZ  PHE B 456     -36.533  36.390   3.327  1.00 51.16           C  
ANISOU 5860  CZ  PHE B 456     6292   6606   6543     73   1045   -517       C  
ATOM   5861  N   ARG B 457     -34.839  39.396   9.818  1.00 50.66           N  
ANISOU 5861  N   ARG B 457     6328   6592   6328      1   1093   -663       N  
ATOM   5862  CA  ARG B 457     -34.988  40.179  11.036  1.00 48.33           C  
ANISOU 5862  CA  ARG B 457     6073   6289   6002     -2   1114   -675       C  
ATOM   5863  C   ARG B 457     -34.179  41.457  10.888  1.00 57.94           C  
ANISOU 5863  C   ARG B 457     7323   7493   7197    -66   1155   -733       C  
ATOM   5864  O   ARG B 457     -33.118  41.466  10.257  1.00 63.10           O  
ANISOU 5864  O   ARG B 457     7950   8169   7857   -109   1150   -780       O  
ATOM   5865  CB  ARG B 457     -34.541  39.397  12.276  1.00 47.13           C  
ANISOU 5865  CB  ARG B 457     5883   6189   5835     17   1070   -691       C  
ATOM   5866  CG  ARG B 457     -35.457  39.575  13.476  1.00 57.15           C  
ANISOU 5866  CG  ARG B 457     7187   7442   7086     57   1077   -657       C  
ATOM   5867  CD  ARG B 457     -34.905  38.875  14.707  1.00 51.82           C  
ANISOU 5867  CD  ARG B 457     6476   6821   6394     74   1036   -678       C  
ATOM   5868  NE  ARG B 457     -35.237  39.590  15.933  1.00 61.44           N  
ANISOU 5868  NE  ARG B 457     7739   8028   7579     82   1056   -682       N  
ATOM   5869  CZ  ARG B 457     -34.357  40.241  16.681  1.00 63.17           C  
ANISOU 5869  CZ  ARG B 457     7967   8270   7765     44   1060   -741       C  
ATOM   5870  NH1 ARG B 457     -33.075  40.283  16.360  1.00 63.69           N  
ANISOU 5870  NH1 ARG B 457     7999   8373   7826     -6   1047   -803       N  
ATOM   5871  NH2 ARG B 457     -34.775  40.867  17.777  1.00 59.40           N  
ANISOU 5871  NH2 ARG B 457     7533   7778   7257     55   1078   -739       N  
ATOM   5872  N   LYS B 458     -34.694  42.538  11.482  1.00 59.26           N  
ANISOU 5872  N   LYS B 458     7551   7623   7341    -71   1197   -730       N  
ATOM   5873  CA  LYS B 458     -34.040  43.837  11.355  1.00 52.76           C  
ANISOU 5873  CA  LYS B 458     6768   6780   6500   -131   1243   -782       C  
ATOM   5874  C   LYS B 458     -32.645  43.832  11.968  1.00 49.89           C  
ANISOU 5874  C   LYS B 458     6370   6467   6118   -176   1220   -856       C  
ATOM   5875  O   LYS B 458     -31.779  44.606  11.544  1.00 62.00           O  
ANISOU 5875  O   LYS B 458     7913   7997   7646   -234   1247   -908       O  
ATOM   5876  CB  LYS B 458     -34.898  44.925  12.003  1.00 54.74           C  
ANISOU 5876  CB  LYS B 458     7090   6982   6726   -123   1291   -762       C  
ATOM   5877  CG  LYS B 458     -36.235  45.160  11.318  1.00 50.36           C  
ANISOU 5877  CG  LYS B 458     6575   6373   6187    -85   1323   -694       C  
ATOM   5878  CD  LYS B 458     -36.725  46.581  11.549  1.00 52.01           C  
ANISOU 5878  CD  LYS B 458     6861   6528   6372   -100   1387   -692       C  
ATOM   5879  CE  LYS B 458     -38.191  46.605  11.952  1.00 55.29           C  
ANISOU 5879  CE  LYS B 458     7314   6908   6787    -42   1401   -620       C  
ATOM   5880  NZ  LYS B 458     -39.033  47.330  10.959  1.00 42.98           N  
ANISOU 5880  NZ  LYS B 458     5801   5294   5236    -33   1452   -580       N  
ATOM   5881  N   SER B 459     -32.407  42.973  12.956  1.00 40.04           N  
ANISOU 5881  N   SER B 459     5084   5268   4862   -151   1173   -860       N  
ATOM   5882  CA  SER B 459     -31.109  42.906  13.609  1.00 54.61           C  
ANISOU 5882  CA  SER B 459     6893   7168   6687   -189   1147   -929       C  
ATOM   5883  C   SER B 459     -30.914  41.518  14.198  1.00 53.35           C  
ANISOU 5883  C   SER B 459     6672   7066   6532   -147   1086   -917       C  
ATOM   5884  O   SER B 459     -31.864  40.744  14.348  1.00 50.76           O  
ANISOU 5884  O   SER B 459     6340   6731   6218    -88   1068   -857       O  
ATOM   5885  CB  SER B 459     -30.973  43.977  14.700  1.00 58.91           C  
ANISOU 5885  CB  SER B 459     7484   7704   7195   -215   1175   -966       C  
ATOM   5886  OG  SER B 459     -31.885  43.746  15.760  1.00 52.97           O  
ANISOU 5886  OG  SER B 459     6752   6946   6427   -163   1166   -925       O  
ATOM   5887  N   ASN B 460     -29.663  41.210  14.525  1.00 64.68           N  
ANISOU 5887  N   ASN B 460     8060   8558   7956   -177   1055   -974       N  
ATOM   5888  CA  ASN B 460     -29.345  39.948  15.176  1.00 61.64           C  
ANISOU 5888  CA  ASN B 460     7618   8233   7570   -139    998   -969       C  
ATOM   5889  C   ASN B 460     -29.936  39.914  16.581  1.00 63.30           C  
ANISOU 5889  C   ASN B 460     7849   8449   7753    -99    990   -951       C  
ATOM   5890  O   ASN B 460     -30.132  40.950  17.223  1.00 70.03           O  
ANISOU 5890  O   ASN B 460     8752   9277   8580   -117   1022   -968       O  
ATOM   5891  CB  ASN B 460     -27.831  39.749  15.247  1.00 59.39           C  
ANISOU 5891  CB  ASN B 460     7280   8010   7276   -183    971  -1038       C  
ATOM   5892  CG  ASN B 460     -27.207  39.522  13.885  1.00 71.85           C  
ANISOU 5892  CG  ASN B 460     8826   9590   8883   -214    972  -1052       C  
ATOM   5893  OD1 ASN B 460     -27.864  39.671  12.855  1.00 73.35           O  
ANISOU 5893  OD1 ASN B 460     9040   9732   9098   -209    997  -1015       O  
ATOM   5894  ND2 ASN B 460     -25.927  39.164  13.873  1.00 80.68           N  
ANISOU 5894  ND2 ASN B 460     9891  10765   9998   -245    944  -1104       N  
ATOM   5895  N   LEU B 461     -30.228  38.705  17.055  1.00 49.38           N  
ANISOU 5895  N   LEU B 461     6048   6718   5998    -42    948   -915       N  
ATOM   5896  CA  LEU B 461     -30.726  38.541  18.411  1.00 53.90           C  
ANISOU 5896  CA  LEU B 461     6634   7301   6544      1    936   -897       C  
ATOM   5897  C   LEU B 461     -29.605  38.715  19.424  1.00 56.97           C  
ANISOU 5897  C   LEU B 461     7002   7747   6896    -26    914   -963       C  
ATOM   5898  O   LEU B 461     -28.456  38.331  19.190  1.00 57.60           O  
ANISOU 5898  O   LEU B 461     7031   7877   6976    -54    888  -1008       O  
ATOM   5899  CB  LEU B 461     -31.351  37.161  18.624  1.00 46.87           C  
ANISOU 5899  CB  LEU B 461     5709   6427   5673     70    899   -839       C  
ATOM   5900  CG  LEU B 461     -32.473  36.616  17.750  1.00 48.34           C  
ANISOU 5900  CG  LEU B 461     5900   6570   5899    109    906   -769       C  
ATOM   5901  CD1 LEU B 461     -32.372  35.118  17.770  1.00 48.09           C  
ANISOU 5901  CD1 LEU B 461     5808   6579   5887    154    859   -744       C  
ATOM   5902  CD2 LEU B 461     -33.830  37.053  18.256  1.00 46.02           C  
ANISOU 5902  CD2 LEU B 461     5661   6224   5600    147    934   -715       C  
ATOM   5903  N   LYS B 462     -29.960  39.289  20.567  1.00 58.22           N  
ANISOU 5903  N   LYS B 462     7201   7899   7022    -14    926   -966       N  
ATOM   5904  CA  LYS B 462     -29.095  39.232  21.724  1.00 58.86           C  
ANISOU 5904  CA  LYS B 462     7259   8039   7065    -20    898  -1017       C  
ATOM   5905  C   LYS B 462     -29.035  37.791  22.227  1.00 59.84           C  
ANISOU 5905  C   LYS B 462     7327   8215   7193     39    847   -990       C  
ATOM   5906  O   LYS B 462     -29.914  36.983  21.920  1.00 54.21           O  
ANISOU 5906  O   LYS B 462     6608   7481   6508     91    841   -925       O  
ATOM   5907  CB  LYS B 462     -29.613  40.169  22.811  1.00 53.89           C  
ANISOU 5907  CB  LYS B 462     6691   7385   6401    -16    925  -1021       C  
ATOM   5908  CG  LYS B 462     -29.581  41.636  22.409  1.00 59.43           C  
ANISOU 5908  CG  LYS B 462     7450   8037   7094    -78    978  -1054       C  
ATOM   5909  CD  LYS B 462     -30.557  42.460  23.232  1.00 73.35           C  
ANISOU 5909  CD  LYS B 462     9283   9752   8832    -58   1013  -1030       C  
ATOM   5910  CE  LYS B 462     -31.519  43.232  22.341  1.00 75.19           C  
ANISOU 5910  CE  LYS B 462     9573   9907   9087    -65   1067   -989       C  
ATOM   5911  NZ  LYS B 462     -30.856  43.736  21.106  1.00 67.69           N  
ANISOU 5911  NZ  LYS B 462     8617   8945   8159   -127   1089  -1025       N  
ATOM   5912  N   PRO B 463     -27.985  37.430  22.963  1.00 66.45           N  
ANISOU 5912  N   PRO B 463     8122   9123   8005     33    811  -1038       N  
ATOM   5913  CA  PRO B 463     -27.895  36.058  23.483  1.00 63.82           C  
ANISOU 5913  CA  PRO B 463     7736   8840   7672     92    765  -1012       C  
ATOM   5914  C   PRO B 463     -29.119  35.699  24.314  1.00 61.85           C  
ANISOU 5914  C   PRO B 463     7517   8565   7419    162    768   -948       C  
ATOM   5915  O   PRO B 463     -29.561  36.471  25.169  1.00 67.24           O  
ANISOU 5915  O   PRO B 463     8249   9227   8072    167    788   -951       O  
ATOM   5916  CB  PRO B 463     -26.617  36.084  24.329  1.00 66.84           C  
ANISOU 5916  CB  PRO B 463     8083   9298   8016     69    735  -1082       C  
ATOM   5917  CG  PRO B 463     -25.799  37.179  23.732  1.00 73.55           C  
ANISOU 5917  CG  PRO B 463     8942  10140   8861    -13    758  -1146       C  
ATOM   5918  CD  PRO B 463     -26.774  38.216  23.260  1.00 69.88           C  
ANISOU 5918  CD  PRO B 463     8549   9594   8409    -31    811  -1120       C  
ATOM   5919  N   PHE B 464     -29.671  34.518  24.041  1.00 53.90           N  
ANISOU 5919  N   PHE B 464     6481   7557   6441    217    748   -891       N  
ATOM   5920  CA  PHE B 464     -30.866  33.976  24.683  1.00 52.87           C  
ANISOU 5920  CA  PHE B 464     6371   7402   6316    288    750   -823       C  
ATOM   5921  C   PHE B 464     -32.116  34.814  24.427  1.00 54.08           C  
ANISOU 5921  C   PHE B 464     6591   7477   6481    291    795   -780       C  
ATOM   5922  O   PHE B 464     -33.123  34.641  25.124  1.00 49.21           O  
ANISOU 5922  O   PHE B 464     6002   6836   5862    344    803   -730       O  
ATOM   5923  CB  PHE B 464     -30.661  33.793  26.193  1.00 46.54           C  
ANISOU 5923  CB  PHE B 464     5567   6644   5472    325    729   -836       C  
ATOM   5924  CG  PHE B 464     -29.642  32.747  26.540  1.00 54.98           C  
ANISOU 5924  CG  PHE B 464     6569   7790   6530    343    683   -861       C  
ATOM   5925  CD1 PHE B 464     -29.652  31.516  25.906  1.00 52.23           C  
ANISOU 5925  CD1 PHE B 464     6172   7456   6218    374    660   -826       C  
ATOM   5926  CD2 PHE B 464     -28.674  32.995  27.498  1.00 56.78           C  
ANISOU 5926  CD2 PHE B 464     6782   8078   6712    329    662   -919       C  
ATOM   5927  CE1 PHE B 464     -28.715  30.550  26.222  1.00 57.59           C  
ANISOU 5927  CE1 PHE B 464     6790   8204   6886    392    620   -848       C  
ATOM   5928  CE2 PHE B 464     -27.734  32.033  27.819  1.00 63.10           C  
ANISOU 5928  CE2 PHE B 464     7520   8952   7502    348    620   -941       C  
ATOM   5929  CZ  PHE B 464     -27.755  30.809  27.180  1.00 66.41           C  
ANISOU 5929  CZ  PHE B 464     7892   9382   7956    380    600   -904       C  
ATOM   5930  N   GLU B 465     -32.084  35.716  23.449  1.00 56.20           N  
ANISOU 5930  N   GLU B 465     6885   7706   6762    236    827   -798       N  
ATOM   5931  CA  GLU B 465     -33.281  36.450  23.067  1.00 54.19           C  
ANISOU 5931  CA  GLU B 465     6691   7379   6522    241    870   -753       C  
ATOM   5932  C   GLU B 465     -34.166  35.586  22.177  1.00 56.87           C  
ANISOU 5932  C   GLU B 465     7013   7688   6908    279    867   -687       C  
ATOM   5933  O   GLU B 465     -33.687  34.720  21.439  1.00 62.65           O  
ANISOU 5933  O   GLU B 465     7693   8446   7664    277    840   -689       O  
ATOM   5934  CB  GLU B 465     -32.916  37.747  22.340  1.00 56.93           C  
ANISOU 5934  CB  GLU B 465     7074   7694   6865    171    908   -796       C  
ATOM   5935  CG  GLU B 465     -34.079  38.712  22.151  1.00 56.66           C  
ANISOU 5935  CG  GLU B 465     7109   7586   6833    174    959   -757       C  
ATOM   5936  CD  GLU B 465     -33.810  39.752  21.080  1.00 62.28           C  
ANISOU 5936  CD  GLU B 465     7848   8262   7553    111    997   -786       C  
ATOM   5937  OE1 GLU B 465     -32.633  40.119  20.885  1.00 67.50           O  
ANISOU 5937  OE1 GLU B 465     8490   8954   8202     55    992   -852       O  
ATOM   5938  OE2 GLU B 465     -34.778  40.200  20.429  1.00 70.55           O1-
ANISOU 5938  OE2 GLU B 465     8936   9251   8620    118   1033   -742       O1-
ATOM   5939  N   ARG B 466     -35.472  35.827  22.257  1.00 57.72           N  
ANISOU 5939  N   ARG B 466     7165   7741   7025    314    894   -628       N  
ATOM   5940  CA  ARG B 466     -36.453  35.095  21.468  1.00 53.57           C  
ANISOU 5940  CA  ARG B 466     6629   7183   6544    351    894   -563       C  
ATOM   5941  C   ARG B 466     -37.349  36.086  20.743  1.00 55.34           C  
ANISOU 5941  C   ARG B 466     6908   7340   6779    335    941   -536       C  
ATOM   5942  O   ARG B 466     -37.819  37.058  21.343  1.00 65.93           O  
ANISOU 5942  O   ARG B 466     8304   8651   8096    333    974   -533       O  
ATOM   5943  CB  ARG B 466     -37.293  34.168  22.352  1.00 47.22           C  
ANISOU 5943  CB  ARG B 466     5815   6381   5744    424    878   -506       C  
ATOM   5944  CG  ARG B 466     -38.229  33.246  21.589  1.00 56.44           C  
ANISOU 5944  CG  ARG B 466     6962   7522   6959    464    872   -442       C  
ATOM   5945  CD  ARG B 466     -39.319  32.708  22.500  1.00 55.02           C  
ANISOU 5945  CD  ARG B 466     6794   7326   6784    532    872   -381       C  
ATOM   5946  NE  ARG B 466     -38.766  31.941  23.610  1.00 57.73           N  
ANISOU 5946  NE  ARG B 466     7106   7722   7106    565    840   -394       N  
ATOM   5947  CZ  ARG B 466     -38.891  32.277  24.887  1.00 63.63           C  
ANISOU 5947  CZ  ARG B 466     7882   8477   7819    589    846   -396       C  
ATOM   5948  NH1 ARG B 466     -39.548  33.365  25.255  1.00 59.77           N  
ANISOU 5948  NH1 ARG B 466     7454   7946   7312    584    883   -385       N  
ATOM   5949  NH2 ARG B 466     -38.343  31.501  25.819  1.00 63.43           N  
ANISOU 5949  NH2 ARG B 466     7824   8502   7775    621    815   -407       N  
ATOM   5950  N   ASP B 467     -37.585  35.836  19.458  1.00 52.87           N  
ANISOU 5950  N   ASP B 467     6580   7006   6502    325    944   -516       N  
ATOM   5951  CA  ASP B 467     -38.475  36.660  18.647  1.00 57.24           C  
ANISOU 5951  CA  ASP B 467     7180   7498   7069    315    986   -484       C  
ATOM   5952  C   ASP B 467     -39.533  35.759  18.027  1.00 58.29           C  
ANISOU 5952  C   ASP B 467     7295   7610   7244    362    977   -416       C  
ATOM   5953  O   ASP B 467     -39.232  34.972  17.125  1.00 57.82           O  
ANISOU 5953  O   ASP B 467     7191   7566   7213    357    954   -416       O  
ATOM   5954  CB  ASP B 467     -37.702  37.412  17.566  1.00 53.32           C  
ANISOU 5954  CB  ASP B 467     6688   6995   6574    250   1005   -531       C  
ATOM   5955  CG  ASP B 467     -38.548  38.452  16.866  1.00 63.63           C  
ANISOU 5955  CG  ASP B 467     8052   8240   7886    238   1055   -505       C  
ATOM   5956  OD1 ASP B 467     -39.791  38.329  16.889  1.00 62.23           O  
ANISOU 5956  OD1 ASP B 467     7896   8027   7723    283   1068   -442       O  
ATOM   5957  OD2 ASP B 467     -37.964  39.393  16.291  1.00 61.97           O1-
ANISOU 5957  OD2 ASP B 467     7864   8017   7666    185   1082   -547       O1-
ATOM   5958  N   ILE B 468     -40.770  35.875  18.512  1.00 50.34           N  
ANISOU 5958  N   ILE B 468     6322   6565   6239    406    996   -360       N  
ATOM   5959  CA  ILE B 468     -41.897  35.139  17.955  1.00 41.02           C  
ANISOU 5959  CA  ILE B 468     5129   5359   5098    450    992   -293       C  
ATOM   5960  C   ILE B 468     -42.785  36.032  17.099  1.00 47.96           C  
ANISOU 5960  C   ILE B 468     6052   6181   5987    440   1034   -262       C  
ATOM   5961  O   ILE B 468     -43.849  35.595  16.648  1.00 50.33           O  
ANISOU 5961  O   ILE B 468     6350   6456   6318    476   1036   -205       O  
ATOM   5962  CB  ILE B 468     -42.718  34.458  19.062  1.00 44.56           C  
ANISOU 5962  CB  ILE B 468     5575   5807   5549    513    981   -244       C  
ATOM   5963  CG1 ILE B 468     -43.486  35.502  19.878  1.00 47.30           C  
ANISOU 5963  CG1 ILE B 468     5986   6116   5870    527   1021   -223       C  
ATOM   5964  CG2 ILE B 468     -41.816  33.622  19.956  1.00 40.87           C  
ANISOU 5964  CG2 ILE B 468     5066   5396   5067    525    942   -275       C  
ATOM   5965  CD1 ILE B 468     -44.608  34.917  20.710  1.00 44.10           C  
ANISOU 5965  CD1 ILE B 468     5585   5696   5475    593   1020   -160       C  
ATOM   5966  N   SER B 469     -42.376  37.278  16.873  1.00 48.99           N  
ANISOU 5966  N   SER B 469     6226   6295   6093    394   1069   -300       N  
ATOM   5967  CA  SER B 469     -43.182  38.206  16.095  1.00 44.33           C  
ANISOU 5967  CA  SER B 469     5682   5652   5509    385   1113   -272       C  
ATOM   5968  C   SER B 469     -43.323  37.722  14.659  1.00 45.04           C  
ANISOU 5968  C   SER B 469     5743   5736   5635    380   1103   -256       C  
ATOM   5969  O   SER B 469     -42.360  37.259  14.041  1.00 50.14           O  
ANISOU 5969  O   SER B 469     6348   6413   6290    350   1078   -295       O  
ATOM   5970  CB  SER B 469     -42.553  39.599  16.120  1.00 46.44           C  
ANISOU 5970  CB  SER B 469     5998   5904   5742    332   1152   -322       C  
ATOM   5971  OG  SER B 469     -42.110  39.979  14.829  1.00 60.85           O  
ANISOU 5971  OG  SER B 469     7821   7720   7580    290   1165   -346       O  
ATOM   5972  N   THR B 470     -44.541  37.825  14.130  1.00 55.89           N  
ANISOU 5972  N   THR B 470     7137   7070   7029    409   1123   -198       N  
ATOM   5973  CA  THR B 470     -44.829  37.473  12.746  1.00 51.00           C  
ANISOU 5973  CA  THR B 470     6496   6441   6441    407   1118   -178       C  
ATOM   5974  C   THR B 470     -45.065  38.706  11.881  1.00 58.78           C  
ANISOU 5974  C   THR B 470     7531   7386   7417    379   1166   -179       C  
ATOM   5975  O   THR B 470     -45.719  38.612  10.838  1.00 62.67           O  
ANISOU 5975  O   THR B 470     8021   7859   7933    390   1172   -146       O  
ATOM   5976  CB  THR B 470     -46.035  36.536  12.671  1.00 56.79           C  
ANISOU 5976  CB  THR B 470     7207   7164   7208    463   1101   -111       C  
ATOM   5977  OG1 THR B 470     -47.236  37.309  12.565  1.00 68.74           O  
ANISOU 5977  OG1 THR B 470     8769   8630   8720    485   1140    -62       O  
ATOM   5978  CG2 THR B 470     -46.108  35.658  13.912  1.00 53.78           C  
ANISOU 5978  CG2 THR B 470     6800   6807   6826    501   1071    -98       C  
ATOM   5979  N   GLU B 471     -44.555  39.861  12.303  1.00 54.52           N  
ANISOU 5979  N   GLU B 471     7036   6834   6843    344   1201   -218       N  
ATOM   5980  CA  GLU B 471     -44.701  41.078  11.517  1.00 56.21           C  
ANISOU 5980  CA  GLU B 471     7301   7010   7047    315   1251   -222       C  
ATOM   5981  C   GLU B 471     -43.945  40.942  10.202  1.00 61.90           C  
ANISOU 5981  C   GLU B 471     7994   7742   7783    279   1243   -254       C  
ATOM   5982  O   GLU B 471     -42.803  40.473  10.176  1.00 64.28           O  
ANISOU 5982  O   GLU B 471     8256   8082   8085    248   1213   -303       O  
ATOM   5983  CB  GLU B 471     -44.189  42.284  12.304  1.00 61.17           C  
ANISOU 5983  CB  GLU B 471     7981   7626   7637    281   1289   -263       C  
ATOM   5984  CG  GLU B 471     -44.886  43.590  11.956  1.00 81.04           C  
ANISOU 5984  CG  GLU B 471    10566  10088  10138    276   1351   -242       C  
ATOM   5985  CD  GLU B 471     -43.939  44.774  11.942  1.00 93.62           C  
ANISOU 5985  CD  GLU B 471    12198  11672  11703    218   1389   -303       C  
ATOM   5986  OE1 GLU B 471     -42.709  44.555  11.948  1.00 79.82           O  
ANISOU 5986  OE1 GLU B 471    10417   9959   9951    176   1366   -363       O  
ATOM   5987  OE2 GLU B 471     -44.425  45.925  11.926  1.00 96.97           O1-
ANISOU 5987  OE2 GLU B 471    12684  12052  12109    212   1444   -291       O1-
ATOM   5988  N   ILE B 472     -44.587  41.358   9.108  1.00 46.53           N  
ANISOU 5988  N   ILE B 472     6068   5763   5848    283   1270   -224       N  
ATOM   5989  CA  ILE B 472     -43.989  41.210   7.787  1.00 40.71           C  
ANISOU 5989  CA  ILE B 472     5307   5034   5127    254   1264   -247       C  
ATOM   5990  C   ILE B 472     -42.713  42.033   7.710  1.00 46.11           C  
ANISOU 5990  C   ILE B 472     6007   5724   5788    194   1286   -316       C  
ATOM   5991  O   ILE B 472     -42.713  43.241   7.980  1.00 46.38           O  
ANISOU 5991  O   ILE B 472     6096   5728   5796    172   1334   -329       O  
ATOM   5992  CB  ILE B 472     -44.991  41.624   6.700  1.00 43.88           C  
ANISOU 5992  CB  ILE B 472     5736   5398   5540    274   1294   -200       C  
ATOM   5993  CG1 ILE B 472     -46.300  40.847   6.857  1.00 45.52           C  
ANISOU 5993  CG1 ILE B 472     5927   5599   5770    333   1273   -132       C  
ATOM   5994  CG2 ILE B 472     -44.398  41.405   5.318  1.00 59.44           C  
ANISOU 5994  CG2 ILE B 472     7681   7378   7527    248   1285   -222       C  
ATOM   5995  CD1 ILE B 472     -46.157  39.358   6.638  1.00 47.97           C  
ANISOU 5995  CD1 ILE B 472     6168   5946   6111    350   1214   -126       C  
ATOM   5996  N   TYR B 473     -41.615  41.378   7.342  1.00 60.24           N  
ANISOU 5996  N   TYR B 473     7748   7553   7588    165   1251   -359       N  
ATOM   5997  CA  TYR B 473     -40.331  42.059   7.245  1.00 59.31           C  
ANISOU 5997  CA  TYR B 473     7637   7446   7452    106   1268   -427       C  
ATOM   5998  C   TYR B 473     -40.352  43.051   6.090  1.00 55.92           C  
ANISOU 5998  C   TYR B 473     7247   6979   7021     80   1316   -431       C  
ATOM   5999  O   TYR B 473     -40.738  42.708   4.968  1.00 57.78           O  
ANISOU 5999  O   TYR B 473     7470   7206   7279     95   1312   -404       O  
ATOM   6000  CB  TYR B 473     -39.205  41.042   7.056  1.00 53.86           C  
ANISOU 6000  CB  TYR B 473     6882   6807   6776     87   1218   -468       C  
ATOM   6001  CG  TYR B 473     -37.843  41.659   6.817  1.00 55.93           C  
ANISOU 6001  CG  TYR B 473     7143   7083   7024     25   1232   -538       C  
ATOM   6002  CD1 TYR B 473     -37.030  42.026   7.881  1.00 51.99           C  
ANISOU 6002  CD1 TYR B 473     6647   6607   6500     -5   1232   -587       C  
ATOM   6003  CD2 TYR B 473     -37.365  41.862   5.527  1.00 64.50           C  
ANISOU 6003  CD2 TYR B 473     8224   8161   8122     -4   1246   -555       C  
ATOM   6004  CE1 TYR B 473     -35.784  42.586   7.669  1.00 60.42           C  
ANISOU 6004  CE1 TYR B 473     7711   7688   7557    -64   1244   -652       C  
ATOM   6005  CE2 TYR B 473     -36.120  42.422   5.306  1.00 62.48           C  
ANISOU 6005  CE2 TYR B 473     7967   7918   7856    -61   1261   -618       C  
ATOM   6006  CZ  TYR B 473     -35.334  42.781   6.380  1.00 63.76           C  
ANISOU 6006  CZ  TYR B 473     8129   8101   7994    -92   1260   -667       C  
ATOM   6007  OH  TYR B 473     -34.094  43.338   6.162  1.00 70.83           O  
ANISOU 6007  OH  TYR B 473     9020   9010   8881   -151   1275   -731       O  
ATOM   6008  N   GLN B 474     -39.933  44.282   6.366  1.00 65.93           N  
ANISOU 6008  N   GLN B 474     8563   8224   8263     41   1364   -466       N  
ATOM   6009  CA  GLN B 474     -39.887  45.335   5.355  1.00 65.04           C  
ANISOU 6009  CA  GLN B 474     8493   8073   8146     14   1417   -474       C  
ATOM   6010  C   GLN B 474     -38.480  45.369   4.772  1.00 70.14           C  
ANISOU 6010  C   GLN B 474     9112   8743   8796    -41   1412   -538       C  
ATOM   6011  O   GLN B 474     -37.548  45.886   5.393  1.00 70.79           O  
ANISOU 6011  O   GLN B 474     9200   8836   8859    -85   1423   -594       O  
ATOM   6012  CB  GLN B 474     -40.272  46.681   5.960  1.00 64.64           C  
ANISOU 6012  CB  GLN B 474     8514   7980   8067      4   1477   -473       C  
ATOM   6013  CG  GLN B 474     -40.114  47.860   5.013  1.00 74.52           C  
ANISOU 6013  CG  GLN B 474     9813   9190   9310    -28   1539   -487       C  
ATOM   6014  CD  GLN B 474     -40.596  49.164   5.625  1.00 82.53           C  
ANISOU 6014  CD  GLN B 474    10901  10159  10297    -34   1600   -481       C  
ATOM   6015  OE1 GLN B 474     -41.414  49.878   5.048  1.00 89.36           O  
ANISOU 6015  OE1 GLN B 474    11814  10981  11159    -15   1647   -442       O  
ATOM   6016  NE2 GLN B 474     -40.085  49.479   6.809  1.00 78.77           N  
ANISOU 6016  NE2 GLN B 474    10436   9693   9800    -58   1600   -520       N  
ATOM   6017  N   ALA B 475     -38.322  44.803   3.576  1.00 65.93           N  
ANISOU 6017  N   ALA B 475     8547   8219   8285    -39   1396   -531       N  
ATOM   6018  CA  ALA B 475     -37.052  44.879   2.865  1.00 69.55           C  
ANISOU 6018  CA  ALA B 475     8982   8694   8748    -89   1396   -587       C  
ATOM   6019  C   ALA B 475     -36.943  46.156   2.044  1.00 70.06           C  
ANISOU 6019  C   ALA B 475     9100   8715   8804   -120   1462   -600       C  
ATOM   6020  O   ALA B 475     -35.859  46.744   1.952  1.00 68.77           O  
ANISOU 6020  O   ALA B 475     8941   8555   8632   -173   1484   -657       O  
ATOM   6021  CB  ALA B 475     -36.877  43.657   1.960  1.00 74.08           C  
ANISOU 6021  CB  ALA B 475     9498   9299   9351    -72   1349   -575       C  
ATOM   6022  N   GLY B 476     -38.049  46.602   1.458  1.00 63.63           N  
ANISOU 6022  N   GLY B 476     8326   7859   7989    -87   1496   -547       N  
ATOM   6023  CA  GLY B 476     -38.075  47.830   0.697  1.00 64.73           C  
ANISOU 6023  CA  GLY B 476     8522   7954   8118   -109   1562   -552       C  
ATOM   6024  C   GLY B 476     -38.202  49.048   1.592  1.00 70.91           C  
ANISOU 6024  C   GLY B 476     9365   8703   8874   -128   1615   -565       C  
ATOM   6025  O   GLY B 476     -38.154  48.972   2.820  1.00 63.86           O  
ANISOU 6025  O   GLY B 476     8470   7824   7968   -129   1598   -577       O  
ATOM   6026  N   ASN B 477     -38.357  50.200   0.947  1.00 85.94           N  
ANISOU 6026  N   ASN B 477    11326  10561  10768   -142   1681   -563       N  
ATOM   6027  CA  ASN B 477     -38.512  51.466   1.647  1.00 81.85           C  
ANISOU 6027  CA  ASN B 477    10873  10003  10222   -161   1740   -574       C  
ATOM   6028  C   ASN B 477     -39.961  51.931   1.723  1.00 78.11           C  
ANISOU 6028  C   ASN B 477    10450   9489   9738   -110   1774   -506       C  
ATOM   6029  O   ASN B 477     -40.221  53.023   2.239  1.00 81.44           O  
ANISOU 6029  O   ASN B 477    10933   9872  10137   -120   1829   -508       O  
ATOM   6030  CB  ASN B 477     -37.649  52.542   0.980  1.00 85.75           C  
ANISOU 6030  CB  ASN B 477    11401  10470  10710   -216   1799   -621       C  
ATOM   6031  CG  ASN B 477     -36.246  52.051   0.671  1.00 81.98           C  
ANISOU 6031  CG  ASN B 477    10870  10032  10246   -264   1768   -683       C  
ATOM   6032  OD1 ASN B 477     -35.683  51.240   1.408  1.00 72.95           O  
ANISOU 6032  OD1 ASN B 477     9676   8935   9107   -273   1713   -710       O  
ATOM   6033  ND2 ASN B 477     -35.674  52.540  -0.424  1.00 79.77           N  
ANISOU 6033  ND2 ASN B 477    10600   9735   9974   -293   1804   -705       N  
ATOM   6034  N   LYS B 478     -40.925  51.115   1.219  1.00 68.02           N  
ANISOU 6034  N   LYS B 478     9149   8219   8478    -54   1742   -446       N  
ATOM   6035  CA  LYS B 478     -42.366  51.320   1.223  1.00 77.78           C  
ANISOU 6035  CA  LYS B 478    10420   9425   9709      2   1762   -376       C  
ATOM   6036  C   LYS B 478     -43.022  50.546   2.362  1.00 84.43           C  
ANISOU 6036  C   LYS B 478    11239  10289  10553     39   1716   -346       C  
ATOM   6037  O   LYS B 478     -42.607  49.427   2.677  1.00 79.92           O  
ANISOU 6037  O   LYS B 478    10607   9762   9997     40   1654   -360       O  
ATOM   6038  CB  LYS B 478     -42.980  50.855  -0.098  1.00 66.91           C  
ANISOU 6038  CB  LYS B 478     9026   8048   8351     38   1752   -331       C  
ATOM   6039  CG  LYS B 478     -42.973  51.884  -1.205  1.00 70.77           C  
ANISOU 6039  CG  LYS B 478     9562   8498   8831     27   1816   -329       C  
ATOM   6040  CD  LYS B 478     -43.835  51.412  -2.362  1.00 67.78           C  
ANISOU 6040  CD  LYS B 478     9168   8118   8466     75   1805   -275       C  
ATOM   6041  CE  LYS B 478     -43.003  51.189  -3.612  1.00 66.99           C  
ANISOU 6041  CE  LYS B 478     9043   8030   8380     50   1799   -304       C  
ATOM   6042  NZ  LYS B 478     -42.260  52.418  -4.007  1.00 60.02           N  
ANISOU 6042  NZ  LYS B 478     8210   7114   7481      6   1868   -344       N  
ATOM   6043  N   PRO B 479     -44.082  51.088   2.964  1.00101.28           N  
ANISOU 6043  N   PRO B 479    13419  12392  12672     73   1747   -300       N  
ATOM   6044  CA  PRO B 479     -44.724  50.390   4.086  1.00 94.80           C  
ANISOU 6044  CA  PRO B 479    12579  11588  11852    110   1707   -271       C  
ATOM   6045  C   PRO B 479     -45.392  49.097   3.640  1.00 95.50           C  
ANISOU 6045  C   PRO B 479    12612  11705  11970    157   1650   -224       C  
ATOM   6046  O   PRO B 479     -46.055  49.040   2.601  1.00 95.83           O  
ANISOU 6046  O   PRO B 479    12654  11734  12024    184   1659   -185       O  
ATOM   6047  CB  PRO B 479     -45.755  51.406   4.593  1.00101.08           C  
ANISOU 6047  CB  PRO B 479    13444  12337  12625    137   1764   -228       C  
ATOM   6048  CG  PRO B 479     -46.060  52.256   3.410  1.00104.34           C  
ANISOU 6048  CG  PRO B 479    13898  12713  13034    137   1819   -210       C  
ATOM   6049  CD  PRO B 479     -44.782  52.337   2.613  1.00103.20           C  
ANISOU 6049  CD  PRO B 479    13734  12581  12895     84   1820   -271       C  
ATOM   6050  N   CYS B 480     -45.220  48.053   4.455  1.00 87.15           N  
ANISOU 6050  N   CYS B 480    11504  10685  10923    167   1593   -230       N  
ATOM   6051  CA  CYS B 480     -45.709  46.724   4.104  1.00 83.79           C  
ANISOU 6051  CA  CYS B 480    11020  10288  10527    206   1535   -195       C  
ATOM   6052  C   CYS B 480     -47.203  46.555   4.352  1.00 85.12           C  
ANISOU 6052  C   CYS B 480    11202  10439  10702    266   1538   -121       C  
ATOM   6053  O   CYS B 480     -47.858  45.790   3.635  1.00 80.85           O  
ANISOU 6053  O   CYS B 480    10628   9907  10185    300   1510    -81       O  
ATOM   6054  CB  CYS B 480     -44.928  45.662   4.878  1.00 88.24           C  
ANISOU 6054  CB  CYS B 480    11526  10899  11100    195   1476   -229       C  
ATOM   6055  SG  CYS B 480     -43.342  45.262   4.127  1.00101.75           S  
ANISOU 6055  SG  CYS B 480    13192  12647  12822    140   1450   -299       S  
ATOM   6056  N   ASN B 481     -47.748  47.241   5.359  1.00 98.47           N  
ANISOU 6056  N   ASN B 481    12939  12104  12371    280   1570   -103       N  
ATOM   6057  CA  ASN B 481     -49.170  47.160   5.706  1.00 97.86           C  
ANISOU 6057  CA  ASN B 481    12877  12007  12298    337   1576    -32       C  
ATOM   6058  C   ASN B 481     -49.580  45.739   6.094  1.00 97.79           C  
ANISOU 6058  C   ASN B 481    12807  12032  12317    374   1513     -4       C  
ATOM   6059  O   ASN B 481     -50.680  45.280   5.776  1.00 95.79           O  
ANISOU 6059  O   ASN B 481    12541  11773  12082    419   1502     54       O  
ATOM   6060  CB  ASN B 481     -50.052  47.692   4.573  1.00 98.48           C  
ANISOU 6060  CB  ASN B 481    12984  12056  12379    361   1613     14       C  
ATOM   6061  CG  ASN B 481     -49.649  49.084   4.129  1.00100.17           C  
ANISOU 6061  CG  ASN B 481    13260  12235  12567    327   1680    -12       C  
ATOM   6062  OD1 ASN B 481     -49.234  49.911   4.941  1.00 94.49           O  
ANISOU 6062  OD1 ASN B 481    12583  11498  11822    301   1714    -41       O  
ATOM   6063  ND2 ASN B 481     -49.769  49.350   2.833  1.00 95.40           N  
ANISOU 6063  ND2 ASN B 481    12662  11620  11968    328   1699     -1       N  
ATOM   6064  N   GLY B 482     -48.682  45.033   6.781  1.00 67.70           N  
ANISOU 6064  N   GLY B 482     8957   8257   8508    353   1471    -47       N  
ATOM   6065  CA  GLY B 482     -49.024  43.775   7.418  1.00 62.14           C  
ANISOU 6065  CA  GLY B 482     8202   7581   7826    388   1417    -23       C  
ATOM   6066  C   GLY B 482     -49.375  42.630   6.496  1.00 62.61           C  
ANISOU 6066  C   GLY B 482     8206   7662   7922    411   1374      3       C  
ATOM   6067  O   GLY B 482     -49.947  41.638   6.954  1.00 63.13           O  
ANISOU 6067  O   GLY B 482     8235   7743   8009    448   1337     36       O  
ATOM   6068  N   VAL B 483     -49.050  42.728   5.207  1.00 77.39           N  
ANISOU 6068  N   VAL B 483    10070   9534   9802    390   1378    -11       N  
ATOM   6069  CA  VAL B 483     -49.341  41.669   4.251  1.00 77.72           C  
ANISOU 6069  CA  VAL B 483    10059   9594   9876    410   1337     11       C  
ATOM   6070  C   VAL B 483     -48.106  41.432   3.391  1.00 81.14           C  
ANISOU 6070  C   VAL B 483    10464  10050  10314    366   1320    -45       C  
ATOM   6071  O   VAL B 483     -47.241  42.298   3.247  1.00 79.38           O  
ANISOU 6071  O   VAL B 483    10270   9820  10070    323   1351    -90       O  
ATOM   6072  CB  VAL B 483     -50.571  41.998   3.373  1.00 79.30           C  
ANISOU 6072  CB  VAL B 483    10280   9767  10084    444   1361     68       C  
ATOM   6073  CG1 VAL B 483     -50.201  42.974   2.264  1.00 84.15           C  
ANISOU 6073  CG1 VAL B 483    10929  10361  10683    416   1403     48       C  
ATOM   6074  CG2 VAL B 483     -51.192  40.726   2.804  1.00 65.17           C  
ANISOU 6074  CG2 VAL B 483     8433   7997   8330    477   1313    102       C  
ATOM   6075  N   ALA B 484     -48.029  40.230   2.826  1.00 68.02           N  
ANISOU 6075  N   ALA B 484     8745   8417   8681    376   1271    -41       N  
ATOM   6076  CA  ALA B 484     -46.900  39.851   1.991  1.00 63.38           C  
ANISOU 6076  CA  ALA B 484     8126   7855   8102    340   1250    -89       C  
ATOM   6077  C   ALA B 484     -47.032  40.444   0.594  1.00 70.05           C  
ANISOU 6077  C   ALA B 484     8992   8680   8946    331   1278    -84       C  
ATOM   6078  O   ALA B 484     -48.136  40.629   0.072  1.00 72.75           O  
ANISOU 6078  O   ALA B 484     9349   9000   9292    365   1293    -35       O  
ATOM   6079  CB  ALA B 484     -46.785  38.329   1.901  1.00 52.64           C  
ANISOU 6079  CB  ALA B 484     6698   6530   6772    356   1189    -86       C  
ATOM   6080  N   GLY B 485     -45.889  40.736  -0.009  1.00 63.36           N  
ANISOU 6080  N   GLY B 485     8142   7840   8090    287   1286   -135       N  
ATOM   6081  CA  GLY B 485     -45.879  41.323  -1.333  1.00 57.91           C  
ANISOU 6081  CA  GLY B 485     7474   7132   7398    277   1316   -136       C  
ATOM   6082  C   GLY B 485     -44.465  41.606  -1.779  1.00 55.68           C  
ANISOU 6082  C   GLY B 485     7186   6861   7107    225   1323   -198       C  
ATOM   6083  O   GLY B 485     -43.512  40.987  -1.301  1.00 60.58           O  
ANISOU 6083  O   GLY B 485     7770   7514   7733    201   1290   -239       O  
ATOM   6084  N   PHE B 486     -44.337  42.548  -2.710  1.00 56.63           N  
ANISOU 6084  N   PHE B 486     7345   6957   7216    209   1368   -206       N  
ATOM   6085  CA  PHE B 486     -43.024  42.956  -3.188  1.00 68.61           C  
ANISOU 6085  CA  PHE B 486     8864   8479   8725    158   1384   -264       C  
ATOM   6086  C   PHE B 486     -42.242  43.618  -2.060  1.00 73.11           C  
ANISOU 6086  C   PHE B 486     9456   9049   9276    120   1405   -308       C  
ATOM   6087  O   PHE B 486     -42.728  44.557  -1.421  1.00 81.39           O  
ANISOU 6087  O   PHE B 486    10554  10068  10304    123   1447   -295       O  
ATOM   6088  CB  PHE B 486     -43.173  43.905  -4.377  1.00 68.90           C  
ANISOU 6088  CB  PHE B 486     8943   8484   8752    153   1435   -257       C  
ATOM   6089  CG  PHE B 486     -41.872  44.444  -4.898  1.00 70.30           C  
ANISOU 6089  CG  PHE B 486     9128   8662   8922    101   1460   -315       C  
ATOM   6090  CD1 PHE B 486     -40.854  43.587  -5.277  1.00 74.09           C  
ANISOU 6090  CD1 PHE B 486     9556   9176   9418     77   1419   -353       C  
ATOM   6091  CD2 PHE B 486     -41.677  45.810  -5.034  1.00 78.47           C  
ANISOU 6091  CD2 PHE B 486    10222   9660   9935     76   1527   -330       C  
ATOM   6092  CE1 PHE B 486     -39.660  44.080  -5.763  1.00 74.53           C  
ANISOU 6092  CE1 PHE B 486     9616   9232   9468     30   1443   -405       C  
ATOM   6093  CE2 PHE B 486     -40.485  46.309  -5.524  1.00 85.80           C  
ANISOU 6093  CE2 PHE B 486    11156  10586  10858     27   1552   -383       C  
ATOM   6094  CZ  PHE B 486     -39.474  45.442  -5.887  1.00 76.22           C  
ANISOU 6094  CZ  PHE B 486     9888   9410   9662      4   1509   -420       C  
ATOM   6095  N   ASN B 487     -41.033  43.112  -1.809  1.00 61.11           N  
ANISOU 6095  N   ASN B 487     7896   7563   7760     84   1375   -360       N  
ATOM   6096  CA  ASN B 487     -40.149  43.542  -0.726  1.00 58.52           C  
ANISOU 6096  CA  ASN B 487     7575   7245   7414     45   1383   -409       C  
ATOM   6097  C   ASN B 487     -40.764  43.365   0.658  1.00 59.81           C  
ANISOU 6097  C   ASN B 487     7743   7412   7570     71   1369   -387       C  
ATOM   6098  O   ASN B 487     -40.202  43.853   1.646  1.00 57.85           O  
ANISOU 6098  O   ASN B 487     7510   7168   7303     44   1381   -422       O  
ATOM   6099  CB  ASN B 487     -39.701  45.001  -0.893  1.00 57.34           C  
ANISOU 6099  CB  ASN B 487     7483   7061   7242      5   1449   -440       C  
ATOM   6100  CG  ASN B 487     -38.709  45.181  -2.020  1.00 67.14           C  
ANISOU 6100  CG  ASN B 487     8715   8306   8490    -33   1462   -479       C  
ATOM   6101  OD1 ASN B 487     -37.715  44.458  -2.108  1.00 70.60           O  
ANISOU 6101  OD1 ASN B 487     9104   8781   8939    -57   1425   -517       O  
ATOM   6102  ND2 ASN B 487     -38.949  46.173  -2.864  1.00 74.66           N  
ANISOU 6102  ND2 ASN B 487     9715   9218   9433    -39   1518   -470       N  
ATOM   6103  N   CYS B 488     -41.899  42.681   0.763  1.00 62.79           N  
ANISOU 6103  N   CYS B 488     8107   7788   7961    123   1345   -330       N  
ATOM   6104  CA  CYS B 488     -42.597  42.490   2.032  1.00 61.45           C  
ANISOU 6104  CA  CYS B 488     7943   7619   7785    153   1334   -302       C  
ATOM   6105  C   CYS B 488     -42.739  40.991   2.262  1.00 56.27           C  
ANISOU 6105  C   CYS B 488     7224   7000   7154    183   1270   -285       C  
ATOM   6106  O   CYS B 488     -43.613  40.343   1.678  1.00 54.25           O  
ANISOU 6106  O   CYS B 488     6951   6742   6921    221   1251   -239       O  
ATOM   6107  CB  CYS B 488     -43.948  43.195   2.018  1.00 64.25           C  
ANISOU 6107  CB  CYS B 488     8349   7932   8133    190   1373   -245       C  
ATOM   6108  SG  CYS B 488     -43.812  44.985   2.172  1.00 72.36           S  
ANISOU 6108  SG  CYS B 488     9456   8913   9125    158   1452   -265       S  
ATOM   6109  N   TYR B 489     -41.881  40.444   3.118  1.00 58.05           N  
ANISOU 6109  N   TYR B 489     7417   7261   7377    167   1238   -322       N  
ATOM   6110  CA  TYR B 489     -41.766  39.006   3.308  1.00 58.92           C  
ANISOU 6110  CA  TYR B 489     7465   7410   7511    189   1178   -316       C  
ATOM   6111  C   TYR B 489     -42.209  38.626   4.712  1.00 54.11           C  
ANISOU 6111  C   TYR B 489     6851   6810   6896    219   1161   -296       C  
ATOM   6112  O   TYR B 489     -41.819  39.275   5.689  1.00 49.38           O  
ANISOU 6112  O   TYR B 489     6279   6212   6272    201   1178   -323       O  
ATOM   6113  CB  TYR B 489     -40.327  38.544   3.069  1.00 51.96           C  
ANISOU 6113  CB  TYR B 489     6543   6568   6633    149   1152   -374       C  
ATOM   6114  CG  TYR B 489     -39.710  39.113   1.813  1.00 53.41           C  
ANISOU 6114  CG  TYR B 489     6736   6740   6816    112   1177   -402       C  
ATOM   6115  CD1 TYR B 489     -40.414  39.126   0.617  1.00 58.66           C  
ANISOU 6115  CD1 TYR B 489     7411   7382   7496    131   1188   -368       C  
ATOM   6116  CD2 TYR B 489     -38.427  39.642   1.824  1.00 50.95           C  
ANISOU 6116  CD2 TYR B 489     6426   6442   6490     60   1190   -464       C  
ATOM   6117  CE1 TYR B 489     -39.858  39.643  -0.534  1.00 58.13           C  
ANISOU 6117  CE1 TYR B 489     7355   7304   7427    101   1212   -392       C  
ATOM   6118  CE2 TYR B 489     -37.862  40.164   0.676  1.00 56.26           C  
ANISOU 6118  CE2 TYR B 489     7109   7104   7164     28   1216   -488       C  
ATOM   6119  CZ  TYR B 489     -38.582  40.161  -0.499  1.00 60.62           C  
ANISOU 6119  CZ  TYR B 489     7672   7631   7730     49   1227   -451       C  
ATOM   6120  OH  TYR B 489     -38.028  40.680  -1.645  1.00 70.50           O  
ANISOU 6120  OH  TYR B 489     8936   8871   8982     20   1254   -474       O  
ATOM   6121  N   PHE B 490     -43.023  37.584   4.804  1.00 52.86           N  
ANISOU 6121  N   PHE B 490     6662   6660   6762    264   1128   -251       N  
ATOM   6122  CA  PHE B 490     -43.337  36.982   6.088  1.00 45.88           C  
ANISOU 6122  CA  PHE B 490     5764   5791   5878    295   1104   -234       C  
ATOM   6123  C   PHE B 490     -42.045  36.448   6.697  1.00 47.91           C  
ANISOU 6123  C   PHE B 490     5983   6094   6127    270   1072   -287       C  
ATOM   6124  O   PHE B 490     -41.350  35.650   6.050  1.00 48.88           O  
ANISOU 6124  O   PHE B 490     6060   6244   6266    258   1041   -308       O  
ATOM   6125  CB  PHE B 490     -44.364  35.866   5.906  1.00 42.68           C  
ANISOU 6125  CB  PHE B 490     5325   5386   5504    345   1073   -178       C  
ATOM   6126  CG  PHE B 490     -44.824  35.241   7.190  1.00 47.95           C  
ANISOU 6126  CG  PHE B 490     5981   6065   6175    382   1053   -152       C  
ATOM   6127  CD1 PHE B 490     -45.633  35.941   8.069  1.00 49.11           C  
ANISOU 6127  CD1 PHE B 490     6171   6184   6304    404   1083   -123       C  
ATOM   6128  CD2 PHE B 490     -44.466  33.942   7.509  1.00 49.18           C  
ANISOU 6128  CD2 PHE B 490     6081   6256   6348    398   1007   -156       C  
ATOM   6129  CE1 PHE B 490     -46.065  35.363   9.247  1.00 45.39           C  
ANISOU 6129  CE1 PHE B 490     5689   5722   5835    441   1066    -98       C  
ATOM   6130  CE2 PHE B 490     -44.895  33.358   8.685  1.00 41.58           C  
ANISOU 6130  CE2 PHE B 490     5108   5302   5388    435    991   -132       C  
ATOM   6131  CZ  PHE B 490     -45.694  34.070   9.556  1.00 43.05           C  
ANISOU 6131  CZ  PHE B 490     5338   5462   5558    457   1020   -102       C  
ATOM   6132  N   PRO B 491     -41.685  36.855   7.918  1.00 44.37           N  
ANISOU 6132  N   PRO B 491     5551   5655   5653    262   1079   -309       N  
ATOM   6133  CA  PRO B 491     -40.327  36.574   8.415  1.00 40.43           C  
ANISOU 6133  CA  PRO B 491     5021   5200   5140    231   1055   -368       C  
ATOM   6134  C   PRO B 491     -40.026  35.100   8.610  1.00 40.15           C  
ANISOU 6134  C   PRO B 491     4922   5206   5125    255   1002   -365       C  
ATOM   6135  O   PRO B 491     -38.847  34.737   8.695  1.00 42.17           O  
ANISOU 6135  O   PRO B 491     5144   5502   5376    228    978   -412       O  
ATOM   6136  CB  PRO B 491     -40.281  37.330   9.749  1.00 43.34           C  
ANISOU 6136  CB  PRO B 491     5425   5565   5475    227   1075   -383       C  
ATOM   6137  CG  PRO B 491     -41.704  37.385  10.190  1.00 39.50           C  
ANISOU 6137  CG  PRO B 491     4969   5046   4995    276   1089   -319       C  
ATOM   6138  CD  PRO B 491     -42.520  37.520   8.932  1.00 43.23           C  
ANISOU 6138  CD  PRO B 491     5453   5484   5490    286   1107   -281       C  
ATOM   6139  N   LEU B 492     -41.038  34.242   8.678  1.00 45.74           N  
ANISOU 6139  N   LEU B 492     5614   5907   5858    304    983   -310       N  
ATOM   6140  CA  LEU B 492     -40.849  32.834   8.991  1.00 35.83           C  
ANISOU 6140  CA  LEU B 492     4304   4688   4623    332    936   -302       C  
ATOM   6141  C   LEU B 492     -41.032  31.977   7.748  1.00 38.02           C  
ANISOU 6141  C   LEU B 492     4545   4965   4934    340    915   -284       C  
ATOM   6142  O   LEU B 492     -41.954  32.197   6.956  1.00 42.59           O  
ANISOU 6142  O   LEU B 492     5143   5511   5530    352    931   -248       O  
ATOM   6143  CB  LEU B 492     -41.826  32.379  10.076  1.00 36.76           C  
ANISOU 6143  CB  LEU B 492     4424   4798   4744    384    930   -255       C  
ATOM   6144  CG  LEU B 492     -41.861  33.218  11.352  1.00 35.99           C  
ANISOU 6144  CG  LEU B 492     4367   4695   4612    386    952   -264       C  
ATOM   6145  CD1 LEU B 492     -42.849  32.626  12.340  1.00 37.71           C  
ANISOU 6145  CD1 LEU B 492     4583   4906   4837    442    943   -212       C  
ATOM   6146  CD2 LEU B 492     -40.474  33.318  11.968  1.00 35.82           C  
ANISOU 6146  CD2 LEU B 492     4330   4717   4564    352    938   -327       C  
ATOM   6147  N   ARG B 493     -40.140  30.987   7.625  1.00 36.46           N  
ANISOU 6147  N   ARG B 493     4297   4808   4747    334    878   -311       N  
ATOM   6148  CA  ARG B 493     -40.125  29.984   6.527  1.00 38.47           C  
ANISOU 6148  CA  ARG B 493     4512   5071   5035    340    852   -300       C  
ATOM   6149  C   ARG B 493     -40.053  28.595   7.174  1.00 35.59           C  
ANISOU 6149  C   ARG B 493     4098   4738   4687    375    812   -287       C  
ATOM   6150  O   ARG B 493     -39.358  28.462   8.201  1.00 39.87           O  
ANISOU 6150  O   ARG B 493     4628   5311   5209    375    801   -313       O  
ATOM   6151  CB  ARG B 493     -38.928  30.224   5.602  1.00 39.67           C  
ANISOU 6151  CB  ARG B 493     4651   5240   5181    292    852   -352       C  
ATOM   6152  CG  ARG B 493     -39.304  30.723   4.214  1.00 36.90           C  
ANISOU 6152  CG  ARG B 493     4321   4858   4842    277    873   -342       C  
ATOM   6153  CD  ARG B 493     -40.793  30.979   4.077  1.00 39.08           C  
ANISOU 6153  CD  ARG B 493     4626   5092   5129    311    891   -284       C  
ATOM   6154  NE  ARG B 493     -41.147  32.358   4.382  1.00 48.29           N  
ANISOU 6154  NE  ARG B 493     5850   6227   6270    298    935   -283       N  
ATOM   6155  CZ  ARG B 493     -41.331  33.306   3.470  1.00 47.14           C  
ANISOU 6155  CZ  ARG B 493     5740   6053   6119    278    970   -284       C  
ATOM   6156  NH1 ARG B 493     -41.195  33.026   2.187  1.00 51.49           N  
ANISOU 6156  NH1 ARG B 493     6276   6603   6687    268    963   -286       N  
ATOM   6157  NH2 ARG B 493     -41.651  34.533   3.846  1.00 46.82           N  
ANISOU 6157  NH2 ARG B 493     5752   5983   6053    268   1012   -282       N  
ATOM   6158  N   SER B 494     -40.743  27.608   6.596  1.00 35.88           N  
ANISOU 6158  N   SER B 494     4108   4766   4757    405    792   -250       N  
ATOM   6159  CA  SER B 494     -40.775  26.265   7.148  1.00 35.16           C  
ANISOU 6159  CA  SER B 494     3974   4700   4686    441    759   -233       C  
ATOM   6160  C   SER B 494     -39.640  25.419   6.589  1.00 40.16           C  
ANISOU 6160  C   SER B 494     4562   5371   5328    423    730   -268       C  
ATOM   6161  O   SER B 494     -39.118  25.668   5.499  1.00 46.75           O  
ANISOU 6161  O   SER B 494     5394   6205   6165    389    733   -294       O  
ATOM   6162  CB  SER B 494     -42.113  25.588   6.855  1.00 40.91           C  
ANISOU 6162  CB  SER B 494     4695   5400   5449    482    753   -174       C  
ATOM   6163  OG  SER B 494     -42.134  24.285   7.405  1.00 40.54           O  
ANISOU 6163  OG  SER B 494     4607   5373   5421    516    724   -158       O  
ATOM   6164  N   TYR B 495     -39.261  24.404   7.364  1.00 37.05           N  
ANISOU 6164  N   TYR B 495     4132   5010   4938    447    703   -269       N  
ATOM   6165  CA  TYR B 495     -38.272  23.444   6.897  1.00 39.45           C  
ANISOU 6165  CA  TYR B 495     4389   5349   5252    438    675   -296       C  
ATOM   6166  C   TYR B 495     -38.861  22.465   5.892  1.00 38.48           C  
ANISOU 6166  C   TYR B 495     4242   5211   5169    456    659   -266       C  
ATOM   6167  O   TYR B 495     -38.165  22.048   4.960  1.00 54.58           O  
ANISOU 6167  O   TYR B 495     6257   7265   7217    435    645   -290       O  
ATOM   6168  CB  TYR B 495     -37.683  22.679   8.080  1.00 40.21           C  
ANISOU 6168  CB  TYR B 495     4456   5486   5337    462    654   -305       C  
ATOM   6169  CG  TYR B 495     -36.734  23.491   8.929  1.00 36.50           C  
ANISOU 6169  CG  TYR B 495     3997   5044   4826    437    661   -350       C  
ATOM   6170  CD1 TYR B 495     -35.430  23.727   8.515  1.00 34.41           C  
ANISOU 6170  CD1 TYR B 495     3716   4812   4546    395    655   -403       C  
ATOM   6171  CD2 TYR B 495     -37.137  24.012  10.152  1.00 38.38           C  
ANISOU 6171  CD2 TYR B 495     4262   5278   5042    455    674   -339       C  
ATOM   6172  CE1 TYR B 495     -34.558  24.465   9.290  1.00 42.03           C  
ANISOU 6172  CE1 TYR B 495     4690   5805   5474    370    661   -447       C  
ATOM   6173  CE2 TYR B 495     -36.271  24.751  10.935  1.00 38.62           C  
ANISOU 6173  CE2 TYR B 495     4304   5337   5035    431    680   -382       C  
ATOM   6174  CZ  TYR B 495     -34.983  24.974  10.498  1.00 40.34           C  
ANISOU 6174  CZ  TYR B 495     4503   5587   5238    388    672   -437       C  
ATOM   6175  OH  TYR B 495     -34.116  25.710  11.271  1.00 37.76           O  
ANISOU 6175  OH  TYR B 495     4185   5289   4874    362    677   -482       O  
ATOM   6176  N   GLY B 496     -40.129  22.093   6.056  1.00 27.42           N  
ANISOU 6176  N   GLY B 496     2847   3781   3791    493    661   -215       N  
ATOM   6177  CA  GLY B 496     -40.732  21.090   5.200  1.00 35.61           C  
ANISOU 6177  CA  GLY B 496     3858   4805   4866    512    644   -186       C  
ATOM   6178  C   GLY B 496     -40.019  19.759   5.308  1.00 34.25           C  
ANISOU 6178  C   GLY B 496     3638   4666   4708    525    614   -197       C  
ATOM   6179  O   GLY B 496     -39.708  19.132   4.291  1.00 39.32           O  
ANISOU 6179  O   GLY B 496     4256   5313   5370    514    599   -207       O  
ATOM   6180  N   PHE B 497     -39.750  19.328   6.540  1.00 39.88           N  
ANISOU 6180  N   PHE B 497     4338   5403   5410    550    607   -196       N  
ATOM   6181  CA  PHE B 497     -38.957  18.128   6.779  1.00 37.02           C  
ANISOU 6181  CA  PHE B 497     3933   5078   5057    565    582   -209       C  
ATOM   6182  C   PHE B 497     -39.586  16.911   6.115  1.00 44.06           C  
ANISOU 6182  C   PHE B 497     4796   5954   5990    589    566   -177       C  
ATOM   6183  O   PHE B 497     -40.726  16.543   6.418  1.00 42.09           O  
ANISOU 6183  O   PHE B 497     4551   5677   5765    622    570   -132       O  
ATOM   6184  CB  PHE B 497     -38.812  17.888   8.281  1.00 44.65           C  
ANISOU 6184  CB  PHE B 497     4894   6067   6005    596    580   -203       C  
ATOM   6185  CG  PHE B 497     -37.868  18.835   8.962  1.00 41.67           C  
ANISOU 6185  CG  PHE B 497     4532   5718   5584    571    587   -245       C  
ATOM   6186  CD1 PHE B 497     -36.591  19.043   8.465  1.00 39.96           C  
ANISOU 6186  CD1 PHE B 497     4301   5534   5350    532    579   -295       C  
ATOM   6187  CD2 PHE B 497     -38.252  19.507  10.110  1.00 36.88           C  
ANISOU 6187  CD2 PHE B 497     3954   5107   4954    586    602   -235       C  
ATOM   6188  CE1 PHE B 497     -35.720  19.911   9.096  1.00 39.54           C  
ANISOU 6188  CE1 PHE B 497     4259   5508   5257    506    586   -336       C  
ATOM   6189  CE2 PHE B 497     -37.386  20.374  10.746  1.00 40.97           C  
ANISOU 6189  CE2 PHE B 497     4486   5651   5431    561    608   -276       C  
ATOM   6190  CZ  PHE B 497     -36.115  20.572  10.242  1.00 42.74           C  
ANISOU 6190  CZ  PHE B 497     4693   5909   5639    520    600   -328       C  
ATOM   6191  N