CNRS Nantes University UFIP UFIP
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***  AHW1  ***

elNémo ID: 21022301195911200

Job options:

ID        	=	 21022301195911200
JOBID     	=	 AHW1
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 AHW1

HEADER    SIGNALING PROTEIN                       07-JUN-17   5XR8              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN CB1 IN COMPLEX WITH AGONIST AM841      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CANNABINOID RECEPTOR 1,FLAVODOXIN,CANNABINOID RECEPTOR 1;  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 99-306,UNP RESIDUES 3-148,UNP RESIDUES 332-   
COMPND   5 414,UNP RESIDUES 99-306,UNP RESIDUES 3-148,UNP RESIDUES 332-414,UNP  
COMPND   6 RESIDUES 99-306,UNP RESIDUES 3-148,UNP RESIDUES 332-414;             
COMPND   7 SYNONYM: CB1,CANN6,CB1,CANN6;                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, DESULFOVIBRIO VULGARIS (STRAIN    
SOURCE   3 HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303);                  
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606, 882;                                           
SOURCE   6 STRAIN: HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303;           
SOURCE   7 GENE: CNR1, CNR, DVU_2680;                                           
SOURCE   8 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: HEK293F                                 
KEYWDS    MEMBRANE PROTEIN, HUMAN G PROTEIN-COUPLED RECEPTOR, STABILIZING       
KEYWDS   2 AGONISTS, LIPIDIC CUBIC PHASE, SIGNALING PROTEIN                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HUA,K.VEMURI,P.S.NIKAS,R.B.LAPRAIRIE,Y.WU,L.QU,M.PU,A.KORDE,J.SHAN, 
AUTHOR   2 J.H.HO,G.W.HAN,K.DING,X.LI,H.LIU,M.A.HANSON,S.ZHAO,L.M.BOHN,         
AUTHOR   3 A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU                                    
REVDAT   7   22-JAN-20 5XR8    1       COMPND SOURCE JRNL   REMARK              
REVDAT   7 2                   1       DBREF  SEQADV HETNAM FORMUL              
REVDAT   7 3                   1       HELIX  SHEET  ATOM                       
REVDAT   6   08-NOV-17 5XR8    1       SOURCE                                   
REVDAT   5   18-OCT-17 5XR8    1       REMARK                                   
REVDAT   4   16-AUG-17 5XR8    1       REMARK                                   
REVDAT   3   09-AUG-17 5XR8    1       JRNL                                     
REVDAT   2   19-JUL-17 5XR8    1       JRNL                                     
REVDAT   1   12-JUL-17 5XR8    0                                                
JRNL        AUTH   T.HUA,K.VEMURI,S.P.NIKAS,R.B.LAPRAIRIE,Y.WU,L.QU,M.PU,       
JRNL        AUTH 2 A.KORDE,S.JIANG,J.H.HO,G.W.HAN,K.DING,X.LI,H.LIU,M.A.HANSON, 
JRNL        AUTH 3 S.ZHAO,L.M.BOHN,A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU            
JRNL        TITL   CRYSTAL STRUCTURES OF AGONIST-BOUND HUMAN CANNABINOID        
JRNL        TITL 2 RECEPTOR CB1.                                                
JRNL        REF    NATURE                        V. 547   468 2017              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   28678776                                                     
JRNL        DOI    10.1038/NATURE23272                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 13329                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.256                           
REMARK   3   R VALUE            (WORKING SET) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.640                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 618                             
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 49.4866 -  4.6819    0.96     3613   177  0.2249 0.2420        
REMARK   3     2  4.6819 -  3.7165    0.92     3282   155  0.2665 0.2671        
REMARK   3     3  3.7165 -  3.2468    0.86     3046   159  0.3197 0.3998        
REMARK   3     4  3.2468 -  2.9500    0.78     2770   127  0.3858 0.4094        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.260           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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      :  0.002           3491                                  
REMARK   3   ANGLE     :  0.484           4764                                  
REMARK   3   CHIRALITY :  0.036            561                                  
REMARK   3   PLANARITY :  0.003            600                                  
REMARK   3   DIHEDRAL  : 15.503           2016                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 306 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.5828-149.0927 305.7149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4816 T22:   0.3626                                     
REMARK   3      T33:   0.7640 T12:   0.0670                                     
REMARK   3      T13:  -0.0421 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2421 L22:   1.1492                                     
REMARK   3      L33:   2.9624 L12:   1.0127                                     
REMARK   3      L13:   0.3310 L23:   0.3575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2469 S12:   0.3485 S13:   0.0282                       
REMARK   3      S21:   0.0083 S22:   0.1019 S23:   0.3089                       
REMARK   3      S31:   0.1342 S32:  -0.2645 S33:  -0.3070                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 307 THROUGH 335 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -35.983 -118.941  259.680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8387 T22:   0.6905                                     
REMARK   3      T33:   1.5988 T12:  -0.0400                                     
REMARK   3      T13:   0.0550 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3074 L22:   7.2240                                     
REMARK   3      L33:   5.4565 L12:  -4.1474                                     
REMARK   3      L13:   2.7337 L23:  -4.6072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4097 S12:  -0.1339 S13:   0.3508                       
REMARK   3      S21:   1.0589 S22:   0.0256 S23:  -0.4847                       
REMARK   3      S31:  -0.4268 S32:  -0.1613 S33:   0.4333                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 336 THROUGH 536 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -41.886 -126.754  276.328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7203 T22:   0.6250                                     
REMARK   3      T33:   0.8890 T12:  -0.0255                                     
REMARK   3      T13:   0.1857 T23:  -0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7720 L22:   2.1089                                     
REMARK   3      L33:   4.3409 L12:   0.5375                                     
REMARK   3      L13:   1.3216 L23:   2.9628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2097 S12:   0.0659 S13:   0.2704                       
REMARK   3      S21:   0.3455 S22:  -0.1191 S23:   1.0514                       
REMARK   3      S31:  -0.6220 S32:   0.1866 S33:   0.3059                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THERE ARE SOME UNKNOWN DENSITIES LOCATED                            
REMARK   3  AT THE END OF THE SIDE CHAIN OF SER152, WHICH MIGHT BE              
REMARK   3  PHOSPHORYLATION                                                     
REMARK   3  BUT NOT CHEMICALLY CONFIRMED YET. THEY HAVE NOT BEEN MODELLED; DUE  
REMARK   3  TO LACK OF DENSITIES, LAST TWO C AND S ATOMS IN THE TAIL OF THE     
REMARK   3  LIGAND 8D0 HAS BEEN DELETED DURING THE FINAL REFINEMENT.            
REMARK   4                                                                      
REMARK   4 5XR8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004013.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13367                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.0600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.970                              
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: 5TGZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE TRIHYDRATE PH    
REMARK 280  6.2, 120 MM C6H5NA3O7, 30% PEG400 AND 100 MM GLYCINE, LIPIDIC       
REMARK 280  CUBIC PHASE, TEMPERATURE 293.0K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       33.41500            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.82000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       33.41500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.82000            
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 21960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    99                                                      
REMARK 465     GLU A   100                                                      
REMARK 465     ASN A   101                                                      
REMARK 465     PRO A   454                                                      
REMARK 465     ASP A   455                                                      
REMARK 465     GLN A   456                                                      
REMARK 465     ALA A   457                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A 102    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 148    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 183    CG   CD   CE   NZ                                   
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
REMARK 470     LEU A 379    CG   CD1  CD2                                       
REMARK 470     GLU A 385    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 392    CG   CD   CE   NZ                                   
REMARK 470     ARG A 450    CZ   NH1  NH2                                       
REMARK 470     ILE A 453    CG1  CG2  CD1                                       
REMARK 470     ARG A 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 459    CG   SD   CE                                        
REMARK 470     ARG A 522    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 524    CD   CE   NZ                                        
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   SG   CYS A   257     SG   CYS A   264              1.34            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 261       97.33    -64.29                                   
REMARK 500    SER A 315       80.52     56.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     8D0 A 1202                                                       
DBREF  5XR8 A   99   306  UNP    P21554   CNR1_HUMAN      99    306             
DBREF  5XR8 A  308   453  UNP    P00323   FLAV_DESVH       3    148             
DBREF  5XR8 A  356   536  UNP    P21554   CNR1_HUMAN     332    414             
SEQADV 5XR8 ALA A  210  UNP  P21554    THR   210 ENGINEERED MUTATION            
SEQADV 5XR8 LYS A  273  UNP  P21554    GLU   273 ENGINEERED MUTATION            
SEQADV 5XR8 VAL A  283  UNP  P21554    THR   283 ENGINEERED MUTATION            
SEQADV 5XR8 ALA A  307  UNP  P21554              LINKER                         
SEQADV 5XR8 TRP A  403  UNP  P00323    TYR    98 ENGINEERED MUTATION            
SEQADV 5XR8 GLU A  462  UNP  P21554    ARG   340 ENGINEERED MUTATION            
SEQRES   1 A  438  GLY GLU ASN PHE MET ASP ILE GLU CYS PHE MET VAL LEU          
SEQRES   2 A  438  ASN PRO SER GLN GLN LEU ALA ILE ALA VAL LEU SER LEU          
SEQRES   3 A  438  THR LEU GLY THR PHE THR VAL LEU GLU ASN LEU LEU VAL          
SEQRES   4 A  438  LEU CYS VAL ILE LEU HIS SER ARG SER LEU ARG CYS ARG          
SEQRES   5 A  438  PRO SER TYR HIS PHE ILE GLY SER LEU ALA VAL ALA ASP          
SEQRES   6 A  438  LEU LEU GLY SER VAL ILE PHE VAL TYR SER PHE ILE ASP          
SEQRES   7 A  438  PHE HIS VAL PHE HIS ARG LYS ASP SER ARG ASN VAL PHE          
SEQRES   8 A  438  LEU PHE LYS LEU GLY GLY VAL THR ALA SER PHE THR ALA          
SEQRES   9 A  438  SER VAL GLY SER LEU PHE LEU ALA ALA ILE ASP ARG TYR          
SEQRES  10 A  438  ILE SER ILE HIS ARG PRO LEU ALA TYR LYS ARG ILE VAL          
SEQRES  11 A  438  THR ARG PRO LYS ALA VAL VAL ALA PHE CYS LEU MET TRP          
SEQRES  12 A  438  THR ILE ALA ILE VAL ILE ALA VAL LEU PRO LEU LEU GLY          
SEQRES  13 A  438  TRP ASN CYS GLU LYS LEU GLN SER VAL CYS SER ASP ILE          
SEQRES  14 A  438  PHE PRO HIS ILE ASP LYS THR TYR LEU MET PHE TRP ILE          
SEQRES  15 A  438  GLY VAL VAL SER VAL LEU LEU LEU PHE ILE VAL TYR ALA          
SEQRES  16 A  438  TYR MET TYR ILE LEU TRP LYS ALA HIS SER HIS ALA VAL          
SEQRES  17 A  438  ALA LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY ASN          
SEQRES  18 A  438  THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU ALA          
SEQRES  19 A  438  ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA SER          
SEQRES  20 A  438  VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL          
SEQRES  21 A  438  LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE GLU          
SEQRES  22 A  438  LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU GLU          
SEQRES  23 A  438  GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY          
SEQRES  24 A  438  CYS GLY ASP SER SER TRP GLU TYR PHE CYS GLY ALA VAL          
SEQRES  25 A  438  ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU          
SEQRES  26 A  438  ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG          
SEQRES  27 A  438  ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL          
SEQRES  28 A  438  ARG GLY ALA ILE PRO ASP GLN ALA ARG MET ASP ILE GLU          
SEQRES  29 A  438  LEU ALA LYS THR LEU VAL LEU ILE LEU VAL VAL LEU ILE          
SEQRES  30 A  438  ILE CYS TRP GLY PRO LEU LEU ALA ILE MET VAL TYR ASP          
SEQRES  31 A  438  VAL PHE GLY LYS MET ASN LYS LEU ILE LYS THR VAL PHE          
SEQRES  32 A  438  ALA PHE CYS SER MET LEU CYS LEU LEU ASN SER THR VAL          
SEQRES  33 A  438  ASN PRO ILE ILE TYR ALA LEU ARG SER LYS ASP LEU ARG          
SEQRES  34 A  438  HIS ALA PHE ARG SER MET PHE PRO SER                          
HET    FMN  A1201      31                                                       
HET    8D0  A1202      29                                                       
HET    CLR  A1203      28                                                       
HET    PEG  A1204       7                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     8D0 (6~{A}~{R},9~{R},10~{A}~{R})-9-(HYDROXYMETHYL)-3-(8-             
HETNAM   2 8D0  ISOTHIOCYANATO-2-METHYL-OCTAN-2-YL)-6,6-DIMETHYL-               
HETNAM   3 8D0  6~{A},7,8,9,10,10~{A}-HEXAHYDROBENZO[C]CHROMEN-1-OL             
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   2  FMN    C17 H21 N4 O9 P                                              
FORMUL   3  8D0    C26 H39 N O3 S                                               
FORMUL   4  CLR    C27 H46 O                                                    
FORMUL   5  PEG    C4 H10 O3                                                    
FORMUL   6  HOH   *(H2 O)                                                       
HELIX    1 AA1 ILE A  105  MET A  109  5                                   5    
HELIX    2 AA2 ASN A  112  SER A  146  1                                  35    
HELIX    3 AA3 TYR A  153  VAL A  179  1                                  27    
HELIX    4 AA4 SER A  185  ARG A  220  1                                  36    
HELIX    5 AA5 ALA A  223  VAL A  228  1                                   6    
HELIX    6 AA6 THR A  229  GLY A  254  1                                  26    
HELIX    7 AA7 ASP A  272  VAL A  306  1                                  35    
HELIX    8 AA8 GLY A  318  GLY A  335  1                                  18    
HELIX    9 AA9 ASP A  375  SER A  382  1                                   8    
HELIX   10 AB1 LEU A  383  THR A  386  5                                   4    
HELIX   11 AB2 CYS A  407  GLY A  421  1                                  15    
HELIX   12 AB3 ALA A  438  ALA A  452  1                                  15    
HELIX   13 AB4 ASP A  460  PHE A  490  1                                  31    
HELIX   14 AB5 ASN A  494  TYR A  519  1                                  26    
HELIX   15 AB6 SER A  523  MET A  533  1                                  11    
SHEET    1 AA1 5 TYR A 336  ASP A 342  0                                        
SHEET    2 AA1 5 ALA A 307  TYR A 313  1  N  ALA A 309   O  GLU A 337           
SHEET    3 AA1 5 LEU A 357  GLY A 361  1  O  LEU A 359   N  LEU A 310           
SHEET    4 AA1 5 VAL A 393  GLY A 399  1  O  ALA A 394   N  LEU A 360           
SHEET    5 AA1 5 LEU A 429  ASP A 432  1  O  ILE A 431   N  GLY A 399           
CRYST1   66.830   73.610  139.640  90.00  90.00  90.00 P 21 2 21     4          
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      0.014963  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013585  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007161        0.00000                         
ATOM      1  N   PHE A 102     -50.192-176.431 309.191  1.00178.23           N  
ANISOU    1  N   PHE A 102    23409  15777  28535  -1484  -3374    -23       N  
ATOM      2  CA  PHE A 102     -49.299-176.942 310.225  1.00178.03           C  
ANISOU    2  CA  PHE A 102    23472  15546  28628  -1364  -3467    280       C  
ATOM      3  C   PHE A 102     -47.847-176.901 309.761  1.00175.25           C  
ANISOU    3  C   PHE A 102    23106  15157  28325   -987  -3490      6       C  
ATOM      4  O   PHE A 102     -47.346-177.856 309.166  1.00174.37           O  
ANISOU    4  O   PHE A 102    23010  14771  28473   -863  -3575   -244       O  
ATOM      5  CB  PHE A 102     -49.690-178.368 310.616  1.00184.96           C  
ANISOU    5  CB  PHE A 102    24437  16023  29817  -1546  -3600    463       C  
ATOM      6  N   MET A 103     -47.177-175.786 310.039  1.00171.05           N  
ANISOU    6  N   MET A 103    22536  14911  27546   -814  -3409     46       N  
ATOM      7  CA  MET A 103     -45.788-175.573 309.660  1.00174.03           C  
ANISOU    7  CA  MET A 103    22880  15329  27916   -473  -3410   -195       C  
ATOM      8  C   MET A 103     -44.954-175.342 310.912  1.00171.97           C  
ANISOU    8  C   MET A 103    22660  15089  27593   -371  -3450    168       C  
ATOM      9  O   MET A 103     -45.419-174.718 311.871  1.00170.90           O  
ANISOU    9  O   MET A 103    22545  15114  27274   -529  -3407    523       O  
ATOM     10  CB  MET A 103     -45.650-174.373 308.713  1.00173.09           C  
ANISOU   10  CB  MET A 103    22661  15566  27540   -350  -3270   -529       C  
ATOM     11  CG  MET A 103     -46.721-174.294 307.630  1.00175.71           C  
ANISOU   11  CG  MET A 103    22934  15983  27845   -514  -3218   -807       C  
ATOM     12  SD  MET A 103     -46.321-175.206 306.126  1.00182.82           S  
ANISOU   12  SD  MET A 103    23776  16737  28949   -377  -3269  -1363       S  
ATOM     13  CE  MET A 103     -44.978-174.217 305.474  1.00178.10           C  
ANISOU   13  CE  MET A 103    23079  16454  28138    -36  -3181  -1662       C  
ATOM     14  N   ASP A 104     -43.723-175.847 310.902  1.00168.99           N  
ANISOU   14  N   ASP A 104    22281  14562  27365   -116  -3534     73       N  
ATOM     15  CA  ASP A 104     -42.828-175.639 312.032  1.00166.66           C  
ANISOU   15  CA  ASP A 104    22010  14302  27012     -2  -3586    391       C  
ATOM     16  C   ASP A 104     -42.342-174.195 312.060  1.00161.22           C  
ANISOU   16  C   ASP A 104    21260  14004  25992    119  -3448    325       C  
ATOM     17  O   ASP A 104     -42.032-173.607 311.020  1.00160.39           O  
ANISOU   17  O   ASP A 104    21080  14077  25783    263  -3350    -62       O  
ATOM     18  CB  ASP A 104     -41.638-176.596 311.953  1.00170.36           C  
ANISOU   18  CB  ASP A 104    22475  14501  27753    246  -3720    287       C  
ATOM     19  CG  ASP A 104     -40.809-176.600 313.222  1.00171.78           C  
ANISOU   19  CG  ASP A 104    22682  14669  27917    329  -3812    675       C  
ATOM     20  OD1 ASP A 104     -41.402-176.594 314.321  1.00174.72           O  
ANISOU   20  OD1 ASP A 104    23116  15049  28223    112  -3849   1124       O  
ATOM     21  OD2 ASP A 104     -39.564-176.608 313.121  1.00170.27           O  
ANISOU   21  OD2 ASP A 104    22440  14486  27769    602  -3850    533       O  
ATOM     22  N   ILE A 105     -42.281-173.620 313.263  1.00156.77           N  
ANISOU   22  N   ILE A 105    20725  13581  25260     47  -3441    710       N  
ATOM     23  CA  ILE A 105     -41.838-172.234 313.395  1.00148.86           C  
ANISOU   23  CA  ILE A 105    19673  12925  23961    146  -3311    668       C  
ATOM     24  C   ILE A 105     -40.358-172.111 313.053  1.00149.05           C  
ANISOU   24  C   ILE A 105    19641  12997  23994    467  -3327    428       C  
ATOM     25  O   ILE A 105     -39.940-171.162 312.380  1.00151.09           O  
ANISOU   25  O   ILE A 105    19831  13503  24073    602  -3203    145       O  
ATOM     26  CB  ILE A 105     -42.144-171.704 314.809  1.00140.88           C  
ANISOU   26  CB  ILE A 105    18701  12052  22776    -27  -3307   1138       C  
ATOM     27  CG1 ILE A 105     -43.655-171.659 315.049  1.00135.76           C  
ANISOU   27  CG1 ILE A 105    18077  11431  22076   -359  -3258   1337       C  
ATOM     28  CG2 ILE A 105     -41.535-170.323 315.010  1.00134.21           C  
ANISOU   28  CG2 ILE A 105    17810  11526  21660     98  -3187   1086       C  
ATOM     29  CD1 ILE A 105     -44.044-171.099 316.402  1.00132.30           C  
ANISOU   29  CD1 ILE A 105    17655  11179  21436   -565  -3236   1788       C  
ATOM     30  N   GLU A 106     -39.544-173.073 313.497  1.00146.61           N  
ANISOU   30  N   GLU A 106    19350  12455  23899    588  -3480    540       N  
ATOM     31  CA  GLU A 106     -38.116-173.029 313.206  1.00142.87           C  
ANISOU   31  CA  GLU A 106    18805  12026  23451    891  -3505    318       C  
ATOM     32  C   GLU A 106     -37.818-173.267 311.731  1.00139.69           C  
ANISOU   32  C   GLU A 106    18328  11608  23141   1043  -3459   -195       C  
ATOM     33  O   GLU A 106     -36.705-172.972 311.282  1.00136.64           O  
ANISOU   33  O   GLU A 106    17854  11356  22708   1278  -3433   -449       O  
ATOM     34  CB  GLU A 106     -37.371-174.051 314.067  1.00150.08           C  
ANISOU   34  CB  GLU A 106    19747  12679  24596    981  -3694    587       C  
ATOM     35  CG  GLU A 106     -37.611-173.874 315.557  1.00155.76           C  
ANISOU   35  CG  GLU A 106    20528  13449  25207    819  -3758   1124       C  
ATOM     36  CD  GLU A 106     -36.491-174.440 316.408  1.00164.75           C  
ANISOU   36  CD  GLU A 106    21652  14476  26467    986  -3922   1366       C  
ATOM     37  OE1 GLU A 106     -35.672-175.222 315.880  1.00168.93           O  
ANISOU   37  OE1 GLU A 106    22144  14799  27244   1206  -4007   1147       O  
ATOM     38  OE2 GLU A 106     -36.425-174.094 317.606  1.00167.25           O  
ANISOU   38  OE2 GLU A 106    21988  14931  26629    895  -3969   1778       O  
ATOM     39  N   CYS A 107     -38.784-173.791 310.971  1.00142.64           N  
ANISOU   39  N   CYS A 107    18720  11843  23632    905  -3450   -353       N  
ATOM     40  CA  CYS A 107     -38.604-173.918 309.529  1.00144.14           C  
ANISOU   40  CA  CYS A 107    18825  12075  23867   1020  -3398   -847       C  
ATOM     41  C   CYS A 107     -38.508-172.553 308.858  1.00130.85           C  
ANISOU   41  C   CYS A 107    17062  10796  21861   1068  -3226  -1076       C  
ATOM     42  O   CYS A 107     -37.878-172.423 307.803  1.00125.52           O  
ANISOU   42  O   CYS A 107    16284  10256  21152   1230  -3178  -1467       O  
ATOM     43  CB  CYS A 107     -39.752-174.732 308.928  1.00154.49           C  
ANISOU   43  CB  CYS A 107    20173  13164  25360    832  -3431   -947       C  
ATOM     44  SG  CYS A 107     -39.647-174.993 307.142  1.00160.84           S  
ANISOU   44  SG  CYS A 107    20864  14025  26223    940  -3383  -1561       S  
ATOM     45  N   PHE A 108     -39.122-171.531 309.452  1.00127.19           N  
ANISOU   45  N   PHE A 108    16634  10530  21162    926  -3131   -837       N  
ATOM     46  CA  PHE A 108     -39.026-170.166 308.950  1.00120.61           C  
ANISOU   46  CA  PHE A 108    15734  10057  20035    970  -2969  -1002       C  
ATOM     47  C   PHE A 108     -37.778-169.443 309.437  1.00118.06           C  
ANISOU   47  C   PHE A 108    15369   9921  19566   1159  -2935   -971       C  
ATOM     48  O   PHE A 108     -37.580-168.276 309.082  1.00111.71           O  
ANISOU   48  O   PHE A 108    14509   9409  18525   1203  -2799  -1096       O  
ATOM     49  CB  PHE A 108     -40.265-169.365 309.361  1.00110.86           C  
ANISOU   49  CB  PHE A 108    14548   8933  18642    739  -2880   -776       C  
ATOM     50  CG  PHE A 108     -41.536-169.841 308.725  1.00107.39           C  
ANISOU   50  CG  PHE A 108    14121   8385  18298    544  -2890   -854       C  
ATOM     51  CD1 PHE A 108     -42.321-170.801 309.342  1.00110.03           C  
ANISOU   51  CD1 PHE A 108    14536   8449  18822    353  -2994   -601       C  
ATOM     52  CD2 PHE A 108     -41.951-169.324 307.511  1.00107.37           C  
ANISOU   52  CD2 PHE A 108    14041   8562  18191    539  -2801  -1172       C  
ATOM     53  CE1 PHE A 108     -43.495-171.238 308.757  1.00113.39           C  
ANISOU   53  CE1 PHE A 108    14965   8784  19336    157  -3003   -683       C  
ATOM     54  CE2 PHE A 108     -43.122-169.755 306.923  1.00110.83           C  
ANISOU   54  CE2 PHE A 108    14479   8917  18716    352  -2821  -1254       C  
ATOM     55  CZ  PHE A 108     -43.896-170.714 307.545  1.00113.79           C  
ANISOU   55  CZ  PHE A 108    14933   9019  19283    158  -2919  -1018       C  
ATOM     56  N   MET A 109     -36.939-170.101 310.232  1.00123.59           N  
ANISOU   56  N   MET A 109    16089  10461  20410   1267  -3059   -805       N  
ATOM     57  CA  MET A 109     -35.772-169.484 310.857  1.00118.55           C  
ANISOU   57  CA  MET A 109    15410   9988  19648   1432  -3052   -733       C  
ATOM     58  C   MET A 109     -34.512-170.015 310.175  1.00126.98           C  
ANISOU   58  C   MET A 109    16374  11039  20832   1682  -3104  -1047       C  
ATOM     59  O   MET A 109     -33.933-171.018 310.598  1.00136.47           O  
ANISOU   59  O   MET A 109    17583  12004  22266   1783  -3253   -958       O  
ATOM     60  CB  MET A 109     -35.754-169.766 312.357  1.00114.59           C  
ANISOU   60  CB  MET A 109    14988   9352  19200   1363  -3168   -274       C  
ATOM     61  CG  MET A 109     -36.867-169.093 313.145  1.00108.91           C  
ANISOU   61  CG  MET A 109    14345   8710  18324   1118  -3107     44       C  
ATOM     62  SD  MET A 109     -36.738-169.445 314.911  1.00111.11           S  
ANISOU   62  SD  MET A 109    14695   8891  18632   1028  -3260    601       S  
ATOM     63  CE  MET A 109     -38.188-168.600 315.537  1.00112.34           C  
ANISOU   63  CE  MET A 109    14913   9182  18588    713  -3153    881       C  
ATOM     64  N   VAL A 110     -34.090-169.334 309.114  1.00125.16           N  
ANISOU   64  N   VAL A 110    16039  11071  20444   1779  -2983  -1407       N  
ATOM     65  CA  VAL A 110     -32.837-169.630 308.427  1.00131.82           C  
ANISOU   65  CA  VAL A 110    16756  11987  21344   2010  -3006  -1731       C  
ATOM     66  C   VAL A 110     -31.800-168.670 308.999  1.00134.52           C  
ANISOU   66  C   VAL A 110    17039  12584  21488   2131  -2956  -1667       C  
ATOM     67  O   VAL A 110     -31.740-167.498 308.615  1.00141.91           O  
ANISOU   67  O   VAL A 110    17926  13826  22168   2114  -2807  -1784       O  
ATOM     68  CB  VAL A 110     -32.972-169.488 306.910  1.00131.84           C  
ANISOU   68  CB  VAL A 110    16659  12157  21278   2026  -2913  -2160       C  
ATOM     69  CG1 VAL A 110     -31.631-169.729 306.240  1.00133.63           C  
ANISOU   69  CG1 VAL A 110    16733  12503  21537   2257  -2929  -2497       C  
ATOM     70  CG2 VAL A 110     -34.021-170.456 306.379  1.00135.25           C  
ANISOU   70  CG2 VAL A 110    17142  12334  21914   1901  -2973  -2233       C  
ATOM     71  N   LEU A 111     -30.982-169.161 309.930  1.00130.13           N  
ANISOU   71  N   LEU A 111    16483  11903  21059   2253  -3085  -1474       N  
ATOM     72  CA  LEU A 111     -30.198-168.285 310.802  1.00123.90           C  
ANISOU   72  CA  LEU A 111    15659  11323  20094   2328  -3066  -1312       C  
ATOM     73  C   LEU A 111     -28.781-168.825 310.957  1.00126.35           C  
ANISOU   73  C   LEU A 111    15857  11621  20528   2575  -3178  -1399       C  
ATOM     74  O   LEU A 111     -28.552-169.772 311.713  1.00137.08           O  
ANISOU   74  O   LEU A 111    17252  12722  22109   2634  -3344  -1166       O  
ATOM     75  CB  LEU A 111     -30.877-168.148 312.158  1.00119.88           C  
ANISOU   75  CB  LEU A 111    15273  10710  19564   2174  -3126   -848       C  
ATOM     76  CG  LEU A 111     -32.330-167.680 312.109  1.00112.19           C  
ANISOU   76  CG  LEU A 111    14404   9733  18490   1924  -3026   -736       C  
ATOM     77  CD1 LEU A 111     -33.007-167.927 313.432  1.00113.36           C  
ANISOU   77  CD1 LEU A 111    14665   9726  18680   1762  -3125   -270       C  
ATOM     78  CD2 LEU A 111     -32.386-166.215 311.734  1.00101.31           C  
ANISOU   78  CD2 LEU A 111    12983   8683  16829   1896  -2838   -885       C  
ATOM     79  N   ASN A 112     -27.840-168.210 310.261  1.00116.72           N  
ANISOU   79  N   ASN A 112    14493  10690  19164   2714  -3087  -1717       N  
ATOM     80  CA  ASN A 112     -26.416-168.437 310.486  1.00113.11           C  
ANISOU   80  CA  ASN A 112    13901  10313  18763   2949  -3168  -1799       C  
ATOM     81  C   ASN A 112     -25.908-167.431 311.512  1.00112.27           C  
ANISOU   81  C   ASN A 112    13766  10440  18450   2969  -3153  -1577       C  
ATOM     82  O   ASN A 112     -26.189-166.236 311.379  1.00111.33           O  
ANISOU   82  O   ASN A 112    13646  10574  18080   2867  -3003  -1625       O  
ATOM     83  CB  ASN A 112     -25.645-168.296 309.178  1.00109.58           C  
ANISOU   83  CB  ASN A 112    13289  10095  18253   3075  -3077  -2273       C  
ATOM     84  CG  ASN A 112     -24.139-168.336 309.365  1.00112.35           C  
ANISOU   84  CG  ASN A 112    13471  10604  18613   3311  -3134  -2388       C  
ATOM     85  OD1 ASN A 112     -23.623-168.984 310.273  1.00112.21           O  
ANISOU   85  OD1 ASN A 112    13453  10410  18770   3433  -3289  -2162       O  
ATOM     86  ND2 ASN A 112     -23.423-167.643 308.487  1.00113.38           N  
ANISOU   86  ND2 ASN A 112    13444  11086  18551   3374  -3009  -2734       N  
ATOM     87  N   PRO A 113     -25.199-167.874 312.560  1.00112.92           N  
ANISOU   87  N   PRO A 113    13820  10446  18637   3094  -3313  -1322       N  
ATOM     88  CA  PRO A 113     -24.703-166.920 313.572  1.00110.09           C  
ANISOU   88  CA  PRO A 113    13410  10346  18073   3113  -3321  -1113       C  
ATOM     89  C   PRO A 113     -24.038-165.679 312.996  1.00103.01           C  
ANISOU   89  C   PRO A 113    12372   9853  16914   3160  -3156  -1424       C  
ATOM     90  O   PRO A 113     -24.201-164.587 313.555  1.00109.98           O  
ANISOU   90  O   PRO A 113    13255  10946  17586   3076  -3091  -1310       O  
ATOM     91  CB  PRO A 113     -23.719-167.773 314.379  1.00112.98           C  
ANISOU   91  CB  PRO A 113    13698  10620  18611   3308  -3524   -915       C  
ATOM     92  CG  PRO A 113     -24.315-169.140 314.331  1.00113.32           C  
ANISOU   92  CG  PRO A 113    13859  10234  18963   3280  -3641   -787       C  
ATOM     93  CD  PRO A 113     -24.994-169.272 312.981  1.00112.10           C  
ANISOU   93  CD  PRO A 113    13744   9998  18850   3195  -3507  -1151       C  
ATOM     94  N   SER A 114     -23.300-165.809 311.892  1.00 96.08           N  
ANISOU   94  N   SER A 114    11362   9099  16044   3283  -3088  -1817       N  
ATOM     95  CA  SER A 114     -22.787-164.623 311.213  1.00 90.73           C  
ANISOU   95  CA  SER A 114    10554   8816  15104   3283  -2910  -2113       C  
ATOM     96  C   SER A 114     -23.915-163.864 310.523  1.00 99.03           C  
ANISOU   96  C   SER A 114    11709   9910  16008   3074  -2734  -2190       C  
ATOM     97  O   SER A 114     -24.000-162.634 310.621  1.00 99.47           O  
ANISOU   97  O   SER A 114    11744  10209  15842   2992  -2600  -2199       O  
ATOM     98  CB  SER A 114     -21.698-165.015 310.214  1.00 82.27           C  
ANISOU   98  CB  SER A 114     9300   7893  14067   3454  -2894  -2497       C  
ATOM     99  OG  SER A 114     -20.567-165.545 310.887  1.00 82.41           O  
ANISOU   99  OG  SER A 114     9195   7923  14195   3661  -3042  -2427       O  
ATOM    100  N   GLN A 115     -24.800-164.583 309.826  1.00100.71           N  
ANISOU  100  N   GLN A 115    12022   9890  16352   2989  -2734  -2247       N  
ATOM    101  CA  GLN A 115     -25.983-163.942 309.259  1.00 96.89           C  
ANISOU  101  CA  GLN A 115    11637   9432  15743   2788  -2588  -2266       C  
ATOM    102  C   GLN A 115     -26.886-163.381 310.350  1.00 84.49           C  
ANISOU  102  C   GLN A 115    10213   7771  14120   2637  -2583  -1908       C  
ATOM    103  O   GLN A 115     -27.635-162.429 310.106  1.00 74.36           O  
ANISOU  103  O   GLN A 115     8980   6597  12678   2493  -2436  -1909       O  
ATOM    104  CB  GLN A 115     -26.760-164.934 308.391  1.00110.42           C  
ANISOU  104  CB  GLN A 115    13410  10920  17624   2733  -2622  -2385       C  
ATOM    105  CG  GLN A 115     -26.032-165.375 307.130  1.00125.50           C  
ANISOU  105  CG  GLN A 115    15164  12960  19561   2856  -2606  -2793       C  
ATOM    106  CD  GLN A 115     -26.750-166.499 306.403  1.00141.11           C  
ANISOU  106  CD  GLN A 115    17185  14681  21748   2821  -2674  -2915       C  
ATOM    107  OE1 GLN A 115     -27.624-167.161 306.965  1.00146.11           O  
ANISOU  107  OE1 GLN A 115    17962  14996  22556   2731  -2763  -2674       O  
ATOM    108  NE2 GLN A 115     -26.384-166.719 305.145  1.00147.33           N  
ANISOU  108  NE2 GLN A 115    17835  15626  22516   2885  -2633  -3301       N  
ATOM    109  N   GLN A 116     -26.838-163.959 311.553  1.00 92.69           N  
ANISOU  109  N   GLN A 116    11311   8616  15292   2667  -2747  -1592       N  
ATOM    110  CA  GLN A 116     -27.606-163.406 312.664  1.00 95.88           C  
ANISOU  110  CA  GLN A 116    11827   8976  15628   2526  -2759  -1248       C  
ATOM    111  C   GLN A 116     -27.001-162.095 313.146  1.00 92.93           C  
ANISOU  111  C   GLN A 116    11362   8949  15000   2529  -2656  -1260       C  
ATOM    112  O   GLN A 116     -27.730-161.147 313.463  1.00 90.12           O  
ANISOU  112  O   GLN A 116    11076   8762  14403   2290  -2478  -1138       O  
ATOM    113  CB  GLN A 116     -27.679-164.411 313.813  1.00103.95           C  
ANISOU  113  CB  GLN A 116    12920   9744  16831   2534  -2974   -874       C  
ATOM    114  CG  GLN A 116     -28.474-165.667 313.503  1.00108.77           C  
ANISOU  114  CG  GLN A 116    13640  10014  17674   2455  -3048   -806       C  
ATOM    115  CD  GLN A 116     -28.540-166.612 314.686  1.00115.59           C  
ANISOU  115  CD  GLN A 116    14572  10637  18707   2442  -3255   -394       C  
ATOM    116  OE1 GLN A 116     -28.600-166.180 315.838  1.00113.69           O  
ANISOU  116  OE1 GLN A 116    14354  10479  18362   2381  -3321    -63       O  
ATOM    117  NE2 GLN A 116     -28.522-167.909 314.410  1.00124.53           N  
ANISOU  117  NE2 GLN A 116    15729  11484  20102   2494  -3365   -405       N  
ATOM    118  N   LEU A 117     -25.671-162.023 313.211  1.00 97.12           N  
ANISOU  118  N   LEU A 117    11727   9678  15494   2713  -2702  -1396       N  
ATOM    119  CA  LEU A 117     -25.017-160.790 313.634  1.00101.97           C  
ANISOU  119  CA  LEU A 117    12245  10728  15771   2611  -2538  -1411       C  
ATOM    120  C   LEU A 117     -25.255-159.672 312.626  1.00101.54           C  
ANISOU  120  C   LEU A 117    12174  10893  15514   2482  -2280  -1665       C  
ATOM    121  O   LEU A 117     -25.600-158.546 313.003  1.00103.25           O  
ANISOU  121  O   LEU A 117    12428  11321  15482   2264  -2096  -1578       O  
ATOM    122  CB  LEU A 117     -23.521-161.032 313.832  1.00101.88           C  
ANISOU  122  CB  LEU A 117    12036  10892  15782   2842  -2656  -1521       C  
ATOM    123  CG  LEU A 117     -22.701-159.824 314.286  1.00 95.03           C  
ANISOU  123  CG  LEU A 117    11041  10487  14577   2734  -2505  -1562       C  
ATOM    124  CD1 LEU A 117     -23.287-159.221 315.552  1.00 85.44           C  
ANISOU  124  CD1 LEU A 117     9927   9386  13149   2479  -2448  -1237       C  
ATOM    125  CD2 LEU A 117     -21.250-160.220 314.506  1.00101.67           C  
ANISOU  125  CD2 LEU A 117    11666  11497  15465   2977  -2654  -1656       C  
ATOM    126  N   ALA A 118     -25.082-159.969 311.335  1.00101.15           N  
ANISOU  126  N   ALA A 118    12061  10798  15573   2613  -2266  -1981       N  
ATOM    127  CA  ALA A 118     -25.318-158.962 310.305  1.00 97.17           C  
ANISOU  127  CA  ALA A 118    11533  10515  14873   2486  -2039  -2185       C  
ATOM    128  C   ALA A 118     -26.752-158.453 310.349  1.00 99.48           C  
ANISOU  128  C   ALA A 118    11996  10706  15098   2251  -1919  -2001       C  
ATOM    129  O   ALA A 118     -26.997-157.252 310.185  1.00105.22           O  
ANISOU  129  O   ALA A 118    12728  11645  15606   2078  -1717  -1995       O  
ATOM    130  CB  ALA A 118     -24.996-159.532 308.924  1.00 97.72           C  
ANISOU  130  CB  ALA A 118    11500  10566  15065   2656  -2066  -2544       C  
ATOM    131  N   ILE A 119     -27.713-159.351 310.570  1.00101.14           N  
ANISOU  131  N   ILE A 119    12335  10583  15510   2240  -2045  -1847       N  
ATOM    132  CA  ILE A 119     -29.101-158.929 310.741  1.00100.61           C  
ANISOU  132  CA  ILE A 119    12409  10434  15383   2018  -1943  -1653       C  
ATOM    133  C   ILE A 119     -29.225-158.010 311.951  1.00 94.44           C  
ANISOU  133  C   ILE A 119    11663   9823  14397   1846  -1837  -1410       C  
ATOM    134  O   ILE A 119     -29.854-156.948 311.885  1.00 93.28           O  
ANISOU  134  O   ILE A 119    11548   9807  14086   1675  -1646  -1379       O  
ATOM    135  CB  ILE A 119     -30.025-160.155 310.862  1.00104.39           C  
ANISOU  135  CB  ILE A 119    13005  10532  16125   2024  -2115  -1521       C  
ATOM    136  CG1 ILE A 119     -30.248-160.794 309.490  1.00105.70           C  
ANISOU  136  CG1 ILE A 119    13145  10597  16418   2092  -2138  -1794       C  
ATOM    137  CG2 ILE A 119     -31.354-159.769 311.494  1.00106.08           C  
ANISOU  137  CG2 ILE A 119    13346  10699  16261   1786  -2032  -1245       C  
ATOM    138  CD1 ILE A 119     -30.954-159.889 308.507  1.00105.21           C  
ANISOU  138  CD1 ILE A 119    13078  10690  16207   1982  -1962  -1928       C  
ATOM    139  N   ALA A 120     -28.611-158.401 313.070  1.00 96.08           N  
ANISOU  139  N   ALA A 120    11850  10041  14613   1893  -1962  -1245       N  
ATOM    140  CA  ALA A 120     -28.701-157.597 314.284  1.00 99.09           C  
ANISOU  140  CA  ALA A 120    12247  10621  14780   1719  -1869  -1041       C  
ATOM    141  C   ALA A 120     -28.010-156.250 314.112  1.00103.52           C  
ANISOU  141  C   ALA A 120    12712  11511  15110   1654  -1667  -1216       C  
ATOM    142  O   ALA A 120     -28.520-155.222 314.575  1.00100.85           O  
ANISOU  142  O   ALA A 120    12410  11304  14606   1463  -1493  -1153       O  
ATOM    143  CB  ALA A 120     -28.104-158.361 315.465  1.00103.74           C  
ANISOU  143  CB  ALA A 120    12811  11198  15408   1786  -2069   -821       C  
ATOM    144  N   VAL A 121     -26.852-156.233 313.448  1.00106.32           N  
ANISOU  144  N   VAL A 121    12936  11997  15462   1805  -1685  -1448       N  
ATOM    145  CA  VAL A 121     -26.119-154.983 313.257  1.00104.28           C  
ANISOU  145  CA  VAL A 121    12577  12050  14994   1722  -1500  -1607       C  
ATOM    146  C   VAL A 121     -26.928-154.017 312.399  1.00 97.15           C  
ANISOU  146  C   VAL A 121    11733  11153  14029   1580  -1293  -1675       C  
ATOM    147  O   VAL A 121     -27.147-152.859 312.774  1.00108.42           O  
ANISOU  147  O   VAL A 121    13178  12706  15313   1403  -1117  -1640       O  
ATOM    148  CB  VAL A 121     -24.734-155.259 312.645  1.00101.76           C  
ANISOU  148  CB  VAL A 121    12084  11890  14688   1912  -1567  -1844       C  
ATOM    149  CG1 VAL A 121     -24.089-153.960 312.187  1.00103.84           C  
ANISOU  149  CG1 VAL A 121    12247  12459  14747   1794  -1361  -2016       C  
ATOM    150  CG2 VAL A 121     -23.839-155.964 313.653  1.00102.41           C  
ANISOU  150  CG2 VAL A 121    12081  12026  14804   2042  -1759  -1748       C  
ATOM    151  N   LEU A 122     -27.390-154.481 311.236  1.00 83.67           N  
ANISOU  151  N   LEU A 122    10046   9308  12436   1656  -1316  -1778       N  
ATOM    152  CA  LEU A 122     -28.137-153.604 310.341  1.00 84.02           C  
ANISOU  152  CA  LEU A 122    10126   9382  12417   1534  -1142  -1816       C  
ATOM    153  C   LEU A 122     -29.462-153.165 310.949  1.00 97.95           C  
ANISOU  153  C   LEU A 122    12020  11017  14181   1372  -1059  -1602       C  
ATOM    154  O   LEU A 122     -29.925-152.050 310.683  1.00104.32           O  
ANISOU  154  O   LEU A 122    12841  11890  14904   1242   -883  -1586       O  
ATOM    155  CB  LEU A 122     -28.376-154.300 309.004  1.00 89.05           C  
ANISOU  155  CB  LEU A 122    10740   9939  13155   1643  -1205  -1973       C  
ATOM    156  CG  LEU A 122     -27.127-154.658 308.203  1.00100.89           C  
ANISOU  156  CG  LEU A 122    12082  11611  14642   1803  -1255  -2242       C  
ATOM    157  CD1 LEU A 122     -27.506-155.433 306.951  1.00108.45           C  
ANISOU  157  CD1 LEU A 122    13017  12491  15698   1898  -1320  -2422       C  
ATOM    158  CD2 LEU A 122     -26.348-153.402 307.847  1.00104.86           C  
ANISOU  158  CD2 LEU A 122    12478  12430  14934   1702  -1077  -2328       C  
ATOM    159  N   SER A 123     -30.085-154.014 311.766  1.00103.24           N  
ANISOU  159  N   SER A 123    12773  11504  14951   1375  -1185  -1431       N  
ATOM    160  CA  SER A 123     -31.385-153.666 312.328  1.00105.10           C  
ANISOU  160  CA  SER A 123    13107  11649  15178   1219  -1104  -1245       C  
ATOM    161  C   SER A 123     -31.265-152.792 313.569  1.00102.70           C  
ANISOU  161  C   SER A 123    12798  11500  14725   1082   -991  -1156       C  
ATOM    162  O   SER A 123     -32.150-151.968 313.821  1.00 96.86           O  
ANISOU  162  O   SER A 123    12096  10767  13939    946   -839  -1095       O  
ATOM    163  CB  SER A 123     -32.179-154.933 312.647  1.00105.57           C  
ANISOU  163  CB  SER A 123    13250  11467  15396   1241  -1276  -1088       C  
ATOM    164  OG  SER A 123     -31.387-155.867 313.358  1.00108.53           O  
ANISOU  164  OG  SER A 123    13607  11797  15832   1343  -1460  -1025       O  
ATOM    165  N   LEU A 124     -30.197-152.950 314.354  1.00104.74           N  
ANISOU  165  N   LEU A 124    12993  11895  14906   1118  -1062  -1163       N  
ATOM    166  CA  LEU A 124     -30.044-152.112 315.537  1.00105.09           C  
ANISOU  166  CA  LEU A 124    13016  12131  14784    970   -953  -1116       C  
ATOM    167  C   LEU A 124     -29.450-150.751 315.205  1.00104.76           C  
ANISOU  167  C   LEU A 124    12908  12262  14636    895   -758  -1300       C  
ATOM    168  O   LEU A 124     -29.687-149.785 315.939  1.00104.70           O  
ANISOU  168  O   LEU A 124    12900  12356  14527    739   -606  -1308       O  
ATOM    169  CB  LEU A 124     -29.191-152.820 316.591  1.00107.81           C  
ANISOU  169  CB  LEU A 124    13307  12592  15066   1016  -1119  -1022       C  
ATOM    170  CG  LEU A 124     -30.005-153.751 317.492  1.00110.09           C  
ANISOU  170  CG  LEU A 124    13671  12766  15394    972  -1253   -754       C  
ATOM    171  CD1 LEU A 124     -29.176-154.305 318.637  1.00113.35           C  
ANISOU  171  CD1 LEU A 124    14018  13339  15711    991  -1413   -611       C  
ATOM    172  CD2 LEU A 124     -31.236-153.029 318.021  1.00108.68           C  
ANISOU  172  CD2 LEU A 124    13550  12614  15130    771  -1081   -678       C  
ATOM    173  N   THR A 125     -28.684-150.648 314.121  1.00103.30           N  
ANISOU  173  N   THR A 125    12658  12115  14474    989   -756  -1457       N  
ATOM    174  CA  THR A 125     -28.208-149.343 313.684  1.00100.44           C  
ANISOU  174  CA  THR A 125    12241  11889  14031    890   -568  -1598       C  
ATOM    175  C   THR A 125     -29.348-148.580 313.025  1.00102.53           C  
ANISOU  175  C   THR A 125    12581  12012  14363    809   -419  -1556       C  
ATOM    176  O   THR A 125     -29.791-147.549 313.541  1.00105.02           O  
ANISOU  176  O   THR A 125    12921  12327  14655    669   -260  -1543       O  
ATOM    177  CB  THR A 125     -27.025-149.471 312.720  1.00 90.79           C  
ANISOU  177  CB  THR A 125    10907  10802  12789    996   -607  -1765       C  
ATOM    178  OG1 THR A 125     -27.376-150.341 311.634  1.00 89.68           O  
ANISOU  178  OG1 THR A 125    10783  10531  12760   1137   -708  -1783       O  
ATOM    179  CG2 THR A 125     -25.798-150.016 313.444  1.00 83.83           C  
ANISOU  179  CG2 THR A 125     9916  10098  11837   1076   -737  -1819       C  
ATOM    180  N   LEU A 126     -29.834-149.092 311.890  1.00 99.08           N  
ANISOU  180  N   LEU A 126    12168  11461  14017    901   -475  -1544       N  
ATOM    181  CA  LEU A 126     -30.920-148.425 311.177  1.00 99.30           C  
ANISOU  181  CA  LEU A 126    12247  11379  14105    840   -357  -1479       C  
ATOM    182  C   LEU A 126     -32.139-148.240 312.070  1.00101.66           C  
ANISOU  182  C   LEU A 126    12623  11554  14449    757   -303  -1343       C  
ATOM    183  O   LEU A 126     -32.793-147.192 312.027  1.00105.10           O  
ANISOU  183  O   LEU A 126    13073  11944  14916    669   -146  -1313       O  
ATOM    184  CB  LEU A 126     -31.295-149.215 309.924  1.00100.92           C  
ANISOU  184  CB  LEU A 126    12451  11519  14375    948   -458  -1490       C  
ATOM    185  CG  LEU A 126     -30.551-148.900 308.623  1.00102.73           C  
ANISOU  185  CG  LEU A 126    12592  11901  14542    979   -426  -1615       C  
ATOM    186  CD1 LEU A 126     -29.054-149.134 308.762  1.00105.13           C  
ANISOU  186  CD1 LEU A 126    12794  12386  14765   1038   -475  -1775       C  
ATOM    187  CD2 LEU A 126     -31.120-149.726 307.477  1.00101.27           C  
ANISOU  187  CD2 LEU A 126    12402  11671  14404   1066   -524  -1642       C  
ATOM    188  N   GLY A 127     -32.458-149.243 312.886  1.00103.54           N  
ANISOU  188  N   GLY A 127    12899  11740  14701    782   -431  -1255       N  
ATOM    189  CA  GLY A 127     -33.579-149.150 313.799  1.00101.84           C  
ANISOU  189  CA  GLY A 127    12735  11463  14497    687   -380  -1129       C  
ATOM    190  C   GLY A 127     -33.444-147.998 314.773  1.00 99.70           C  
ANISOU  190  C   GLY A 127    12437  11308  14138    556   -210  -1186       C  
ATOM    191  O   GLY A 127     -34.322-147.133 314.840  1.00 99.26           O  
ANISOU  191  O   GLY A 127    12390  11197  14129    483    -58  -1180       O  
ATOM    192  N   THR A 128     -32.344-147.972 315.528  1.00 98.72           N  
ANISOU  192  N   THR A 128    12264  11351  13895    529   -236  -1259       N  
ATOM    193  CA  THR A 128     -32.103-146.851 316.431  1.00104.40           C  
ANISOU  193  CA  THR A 128    12943  12205  14521    388    -70  -1365       C  
ATOM    194  C   THR A 128     -31.984-145.544 315.658  1.00104.41           C  
ANISOU  194  C   THR A 128    12929  12146  14596    346    107  -1487       C  
ATOM    195  O   THR A 128     -32.429-144.491 316.128  1.00105.47           O  
ANISOU  195  O   THR A 128    13059  12257  14758    237    279  -1557       O  
ATOM    196  CB  THR A 128     -30.842-147.102 317.261  1.00109.24           C  
ANISOU  196  CB  THR A 128    13486  13044  14977    366   -150  -1428       C  
ATOM    197  OG1 THR A 128     -30.971-148.345 317.964  1.00111.75           O  
ANISOU  197  OG1 THR A 128    13819  13397  15246    410   -335  -1262       O  
ATOM    198  CG2 THR A 128     -30.631-145.981 318.268  1.00107.85           C  
ANISOU  198  CG2 THR A 128    13258  13033  14687    193     20  -1570       C  
ATOM    199  N   PHE A 129     -31.400-145.595 314.460  1.00107.15           N  
ANISOU  199  N   PHE A 129    13261  12467  14984    426     67  -1511       N  
ATOM    200  CA  PHE A 129     -31.275-144.389 313.650  1.00111.46           C  
ANISOU  200  CA  PHE A 129    13792  12958  15600    371    219  -1571       C  
ATOM    201  C   PHE A 129     -32.636-143.921 313.147  1.00106.67           C  
ANISOU  201  C   PHE A 129    13237  12153  15141    378    304  -1462       C  
ATOM    202  O   PHE A 129     -32.926-142.719 313.157  1.00110.93           O  
ANISOU  202  O   PHE A 129    13774  12601  15773    298    467  -1492       O  
ATOM    203  CB  PHE A 129     -30.323-144.645 312.481  1.00122.05           C  
ANISOU  203  CB  PHE A 129    15084  14380  16909    442    149  -1608       C  
ATOM    204  CG  PHE A 129     -29.741-143.397 311.885  1.00135.76           C  
ANISOU  204  CG  PHE A 129    16779  16141  18661    337    295  -1671       C  
ATOM    205  CD1 PHE A 129     -28.816-142.644 312.590  1.00143.91           C  
ANISOU  205  CD1 PHE A 129    17759  17288  19631    208    386  -1808       C  
ATOM    206  CD2 PHE A 129     -30.101-142.987 310.612  1.00141.58           C  
ANISOU  206  CD2 PHE A 129    17522  16803  19471    350    335  -1582       C  
ATOM    207  CE1 PHE A 129     -28.271-141.496 312.043  1.00148.63           C  
ANISOU  207  CE1 PHE A 129    18322  17885  20265     86    519  -1854       C  
ATOM    208  CE2 PHE A 129     -29.558-141.841 310.058  1.00146.48           C  
ANISOU  208  CE2 PHE A 129    18104  17438  20112    234    462  -1595       C  
ATOM    209  CZ  PHE A 129     -28.643-141.094 310.774  1.00148.74           C  
ANISOU  209  CZ  PHE A 129    18351  17800  20363     98    556  -1731       C  
ATOM    210  N   THR A 130     -33.486-144.855 312.714  1.00100.78           N  
ANISOU  210  N   THR A 130    12527  11331  14434    473    191  -1338       N  
ATOM    211  CA  THR A 130     -34.801-144.478 312.202  1.00101.36           C  
ANISOU  211  CA  THR A 130    12624  11251  14637    488    254  -1226       C  
ATOM    212  C   THR A 130     -35.690-143.925 313.308  1.00102.73           C  
ANISOU  212  C   THR A 130    12802  11370  14860    416    375  -1233       C  
ATOM    213  O   THR A 130     -36.405-142.937 313.101  1.00107.15           O  
ANISOU  213  O   THR A 130    13350  11809  15551    400    509  -1216       O  
ATOM    214  CB  THR A 130     -35.473-145.678 311.534  1.00101.72           C  
ANISOU  214  CB  THR A 130    12693  11256  14699    585     96  -1119       C  
ATOM    215  OG1 THR A 130     -34.583-146.248 310.567  1.00100.06           O  
ANISOU  215  OG1 THR A 130    12460  11124  14434    657    -14  -1168       O  
ATOM    216  CG2 THR A 130     -36.757-145.252 310.842  1.00101.94           C  
ANISOU  216  CG2 THR A 130    12718  11170  14844    601    151  -1000       C  
ATOM    217  N   VAL A 131     -35.665-144.550 314.487  1.00102.20           N  
ANISOU  217  N   VAL A 131    12739  11404  14690    373    329  -1256       N  
ATOM    218  CA  VAL A 131     -36.501-144.084 315.588  1.00104.47           C  
ANISOU  218  CA  VAL A 131    13006  11704  14984    290    451  -1289       C  
ATOM    219  C   VAL A 131     -36.095-142.679 316.008  1.00108.97           C  
ANISOU  219  C   VAL A 131    13540  12269  15596    202    643  -1468       C  
ATOM    220  O   VAL A 131     -36.949-141.810 316.221  1.00118.59           O  
ANISOU  220  O   VAL A 131    14733  13384  16942    180    793  -1516       O  
ATOM    221  CB  VAL A 131     -36.434-145.069 316.769  1.00104.76           C  
ANISOU  221  CB  VAL A 131    13042  11904  14858    236    351  -1253       C  
ATOM    222  CG1 VAL A 131     -37.236-144.539 317.948  1.00 99.48           C  
ANISOU  222  CG1 VAL A 131    12327  11321  14150    125    495  -1317       C  
ATOM    223  CG2 VAL A 131     -36.949-146.428 316.346  1.00109.57           C  
ANISOU  223  CG2 VAL A 131    13695  12454  15482    310    164  -1069       C  
ATOM    224  N   LEU A 132     -34.788-142.428 316.120  1.00104.97           N  
ANISOU  224  N   LEU A 132    13019  11864  15001    151    641  -1584       N  
ATOM    225  CA  LEU A 132     -34.325-141.112 316.550  1.00100.48           C  
ANISOU  225  CA  LEU A 132    12415  11284  14481     38    819  -1778       C  
ATOM    226  C   LEU A 132     -34.678-140.036 315.531  1.00 95.93           C  
ANISOU  226  C   LEU A 132    11852  10463  14134     65    932  -1748       C  
ATOM    227  O   LEU A 132     -34.992-138.900 315.904  1.00 90.34           O  
ANISOU  227  O   LEU A 132    11123   9629  13572      1   1102  -1873       O  
ATOM    228  CB  LEU A 132     -32.818-141.140 316.803  1.00 96.79           C  
ANISOU  228  CB  LEU A 132    11914  11002  13862    -33    776  -1896       C  
ATOM    229  CG  LEU A 132     -32.371-141.904 318.051  1.00 94.98           C  
ANISOU  229  CG  LEU A 132    11645  11037  13405    -88    689  -1943       C  
ATOM    230  CD1 LEU A 132     -30.862-141.820 318.221  1.00 96.47           C  
ANISOU  230  CD1 LEU A 132    11775  11422  13458   -151    650  -2065       C  
ATOM    231  CD2 LEU A 132     -33.086-141.377 319.286  1.00 95.10           C  
ANISOU  231  CD2 LEU A 132    11627  11123  13385   -204    828  -2069       C  
ATOM    232  N   GLU A 133     -34.629-140.373 314.240  1.00 99.49           N  
ANISOU  232  N   GLU A 133    12328  10847  14625    158    837  -1585       N  
ATOM    233  CA  GLU A 133     -35.022-139.423 313.204  1.00106.41           C  
ANISOU  233  CA  GLU A 133    13210  11518  15703    183    919  -1490       C  
ATOM    234  C   GLU A 133     -36.476-139.000 313.373  1.00107.23           C  
ANISOU  234  C   GLU A 133    13306  11448  15989    240   1002  -1432       C  
ATOM    235  O   GLU A 133     -36.782-137.809 313.504  1.00110.21           O  
ANISOU  235  O   GLU A 133    13666  11642  16568    210   1153  -1494       O  
ATOM    236  CB  GLU A 133     -34.801-140.036 311.822  1.00110.09           C  
ANISOU  236  CB  GLU A 133    13685  12024  16122    266    785  -1320       C  
ATOM    237  CG  GLU A 133     -33.356-140.079 311.376  1.00118.35           C  
ANISOU  237  CG  GLU A 133    14707  13219  17040    211    745  -1384       C  
ATOM    238  CD  GLU A 133     -33.193-140.782 310.046  1.00127.71           C  
ANISOU  238  CD  GLU A 133    15879  14493  18151    295    616  -1258       C  
ATOM    239  OE1 GLU A 133     -34.019-141.668 309.745  1.00131.09           O  
ANISOU  239  OE1 GLU A 133    16324  14913  18571    399    511  -1166       O  
ATOM    240  OE2 GLU A 133     -32.251-140.443 309.299  1.00131.35           O  
ANISOU  240  OE2 GLU A 133    16302  15050  18557    243    626  -1264       O  
ATOM    241  N   ASN A 134     -37.391-139.971 313.378  1.00102.90           N  
ANISOU  241  N   ASN A 134    12760  10948  15390    322    903  -1322       N  
ATOM    242  CA  ASN A 134     -38.812-139.644 313.430  1.00 99.38           C  
ANISOU  242  CA  ASN A 134    12279  10373  15107    386    971  -1255       C  
ATOM    243  C   ASN A 134     -39.209-139.088 314.793  1.00 97.44           C  
ANISOU  243  C   ASN A 134    11989  10134  14898    320   1123  -1454       C  
ATOM    244  O   ASN A 134     -40.068-138.202 314.878  1.00 93.08           O  
ANISOU  244  O   ASN A 134    11387   9421  14557    360   1252  -1489       O  
ATOM    245  CB  ASN A 134     -39.641-140.876 313.077  1.00 91.92           C  
ANISOU  245  CB  ASN A 134    11336   9504  14084    461    822  -1096       C  
ATOM    246  CG  ASN A 134     -39.376-141.361 311.667  1.00 88.16           C  
ANISOU  246  CG  ASN A 134    10883   9034  13581    526    685   -939       C  
ATOM    247  OD1 ASN A 134     -40.026-140.925 310.714  1.00 79.42           O  
ANISOU  247  OD1 ASN A 134     9747   7832  12597    591    690   -797       O  
ATOM    248  ND2 ASN A 134     -38.406-142.257 311.523  1.00 96.35           N  
ANISOU  248  ND2 ASN A 134    11956  10201  14451    514    561   -970       N  
ATOM    249  N   LEU A 135     -38.596-139.590 315.869  1.00 98.49           N  
ANISOU  249  N   LEU A 135    12124  10470  14827    222   1108  -1594       N  
ATOM    250  CA  LEU A 135     -38.851-139.012 317.185  1.00 99.02           C  
ANISOU  250  CA  LEU A 135    12131  10606  14884    130   1262  -1820       C  
ATOM    251  C   LEU A 135     -38.440-137.546 317.227  1.00101.82           C  
ANISOU  251  C   LEU A 135    12468  10781  15438     81   1438  -2015       C  
ATOM    252  O   LEU A 135     -39.035-136.753 317.965  1.00102.94           O  
ANISOU  252  O   LEU A 135    12545  10864  15705     56   1602  -2210       O  
ATOM    253  CB  LEU A 135     -38.118-139.809 318.266  1.00 96.72           C  
ANISOU  253  CB  LEU A 135    11837  10609  14305     18   1194  -1904       C  
ATOM    254  CG  LEU A 135     -38.615-139.660 319.707  1.00 97.56           C  
ANISOU  254  CG  LEU A 135    11861  10908  14298    -89   1311  -2088       C  
ATOM    255  CD1 LEU A 135     -40.070-140.085 319.822  1.00 94.88           C  
ANISOU  255  CD1 LEU A 135    11478  10575  13999    -34   1319  -1976       C  
ATOM    256  CD2 LEU A 135     -37.747-140.467 320.660  1.00 97.71           C  
ANISOU  256  CD2 LEU A 135    11874  11243  14009   -206   1212  -2113       C  
ATOM    257  N   LEU A 136     -37.431-137.169 316.437  1.00101.65           N  
ANISOU  257  N   LEU A 136    12494  10669  15459     60   1409  -1977       N  
ATOM    258  CA  LEU A 136     -37.087-135.759 316.296  1.00102.59           C  
ANISOU  258  CA  LEU A 136    12606  10556  15816      4   1564  -2111       C  
ATOM    259  C   LEU A 136     -38.102-135.031 315.425  1.00108.80           C  
ANISOU  259  C   LEU A 136    13385  11033  16920    133   1615  -1954       C  
ATOM    260  O   LEU A 136     -38.493-133.899 315.733  1.00119.19           O  
ANISOU  260  O   LEU A 136    14665  12119  18503    130   1773  -2099       O  
ATOM    261  CB  LEU A 136     -35.681-135.618 315.712  1.00 99.81           C  
ANISOU  261  CB  LEU A 136    12294  10238  15391    -85   1514  -2093       C  
ATOM    262  CG  LEU A 136     -35.246-134.221 315.259  1.00101.21           C  
ANISOU  262  CG  LEU A 136    12480  10142  15833   -161   1643  -2147       C  
ATOM    263  CD1 LEU A 136     -35.183-133.257 316.436  1.00100.29           C  
ANISOU  263  CD1 LEU A 136    12321   9952  15833   -282   1826  -2489       C  
ATOM    264  CD2 LEU A 136     -33.906-134.282 314.538  1.00101.00           C  
ANISOU  264  CD2 LEU A 136    12476  10211  15687   -253   1570  -2077       C  
ATOM    265  N   VAL A 137     -38.545-135.667 314.337  1.00107.39           N  
ANISOU  265  N   VAL A 137    13230  10849  16727    249   1478  -1664       N  
ATOM    266  CA  VAL A 137     -39.508-135.034 313.438  1.00108.62           C  
ANISOU  266  CA  VAL A 137    13361  10753  17158    377   1499  -1469       C  
ATOM    267  C   VAL A 137     -40.816-134.757 314.169  1.00106.48           C  
ANISOU  267  C   VAL A 137    13007  10406  17044    462   1602  -1571       C  
ATOM    268  O   VAL A 137     -41.375-133.657 314.082  1.00107.88           O  
ANISOU  268  O   VAL A 137    13138  10339  17512    522   1708  -1584       O  
ATOM    269  CB  VAL A 137     -39.733-135.906 312.189  1.00107.67           C  
ANISOU  269  CB  VAL A 137    13260  10722  16928    465   1320  -1165       C  
ATOM    270  CG1 VAL A 137     -40.829-135.311 311.318  1.00105.82           C  
ANISOU  270  CG1 VAL A 137    12976  10282  16948    600   1325   -941       C  
ATOM    271  CG2 VAL A 137     -38.442-136.046 311.401  1.00107.93           C  
ANISOU  271  CG2 VAL A 137    13346  10841  16822    386   1241  -1091       C  
ATOM    272  N   LEU A 138     -41.322-135.753 314.901  1.00103.22           N  
ANISOU  272  N   LEU A 138    12564  10234  16421    459   1559  -1624       N  
ATOM    273  CA  LEU A 138     -42.549-135.554 315.665  1.00105.44           C  
ANISOU  273  CA  LEU A 138    12741  10514  16809    519   1667  -1743       C  
ATOM    274  C   LEU A 138     -42.374-134.461 316.712  1.00109.04           C  
ANISOU  274  C   LEU A 138    13146  10876  17409    450   1872  -2089       C  
ATOM    275  O   LEU A 138     -43.291-133.665 316.950  1.00114.21           O  
ANISOU  275  O   LEU A 138    13706  11400  18288    530   1983  -2173       O  
ATOM    276  CB  LEU A 138     -42.979-136.865 316.324  1.00108.34           C  
ANISOU  276  CB  LEU A 138    13087  11193  16885    478   1580  -1725       C  
ATOM    277  CG  LEU A 138     -43.452-137.977 315.384  1.00112.37           C  
ANISOU  277  CG  LEU A 138    13624  11774  17297    551   1390  -1426       C  
ATOM    278  CD1 LEU A 138     -43.876-139.203 316.175  1.00117.34           C  
ANISOU  278  CD1 LEU A 138    14234  12671  17678    481   1317  -1418       C  
ATOM    279  CD2 LEU A 138     -44.590-137.486 314.503  1.00112.08           C  
ANISOU  279  CD2 LEU A 138    13513  11559  17513    705   1399  -1259       C  
ATOM    280  N   CYS A 139     -41.201-134.401 317.346  1.00108.28           N  
ANISOU  280  N   CYS A 139    13096  10896  17150    290   1902  -2284       N  
ATOM    281  CA  CYS A 139     -40.952-133.351 318.328  1.00112.97           C  
ANISOU  281  CA  CYS A 139    13636  11435  17851    192   2087  -2638       C  
ATOM    282  C   CYS A 139     -40.930-131.978 317.669  1.00114.10           C  
ANISOU  282  C   CYS A 139    13785  11289  18281    222   2116  -2546       C  
ATOM    283  O   CYS A 139     -41.395-130.994 318.257  1.00118.84           O  
ANISOU  283  O   CYS A 139    14304  11803  19045    219   2234  -2729       O  
ATOM    284  CB  CYS A 139     -39.638-133.614 319.061  1.00116.23           C  
ANISOU  284  CB  CYS A 139    14087  12076  17997     -1   2086  -2837       C  
ATOM    285  SG  CYS A 139     -39.164-132.294 320.204  1.00127.79           S  
ANISOU  285  SG  CYS A 139    15479  13542  19533   -167   2277  -3254       S  
ATOM    286  N   VAL A 140     -40.400-131.896 316.448  1.00108.08           N  
ANISOU  286  N   VAL A 140    13106  10371  17587    249   2013  -2271       N  
ATOM    287  CA  VAL A 140     -40.350-130.619 315.742  1.00107.71           C  
ANISOU  287  CA  VAL A 140    13069  10036  17821    269   2038  -2148       C  
ATOM    288  C   VAL A 140     -41.754-130.149 315.382  1.00112.44           C  
ANISOU  288  C   VAL A 140    13589  10482  18651    450   2038  -1998       C  
ATOM    289  O   VAL A 140     -42.084-128.968 315.536  1.00124.73           O  
ANISOU  289  O   VAL A 140    15097  11833  20461    474   2119  -2069       O  
ATOM    290  CB  VAL A 140     -39.451-130.734 314.497  1.00101.00           C  
ANISOU  290  CB  VAL A 140    12314   9096  16966    239   1936  -1884       C  
ATOM    291  CG1 VAL A 140     -39.629-129.526 313.595  1.00100.54           C  
ANISOU  291  CG1 VAL A 140    12258   8729  17212    284   1943  -1669       C  
ATOM    292  CG2 VAL A 140     -37.993-130.877 314.906  1.00 98.44           C  
ANISOU  292  CG2 VAL A 140    12043   8887  16472     46   1963  -2081       C  
ATOM    293  N   ILE A 141     -42.604-131.065 314.911  1.00105.28           N  
ANISOU  293  N   ILE A 141    12659   9670  17673    581   1944  -1799       N  
ATOM    294  CA  ILE A 141     -43.952-130.687 314.491  1.00101.54           C  
ANISOU  294  CA  ILE A 141    12094   9081  17407    757   1931  -1640       C  
ATOM    295  C   ILE A 141     -44.747-130.142 315.671  1.00105.12           C  
ANISOU  295  C   ILE A 141    12429   9549  17964    780   2074  -1945       C  
ATOM    296  O   ILE A 141     -45.375-129.080 315.581  1.00 95.30           O  
ANISOU  296  O   ILE A 141    11116   8100  16993    870   2122  -1944       O  
ATOM    297  CB  ILE A 141     -44.667-131.884 313.839  1.00103.69           C  
ANISOU  297  CB  ILE A 141    12348   9494  17554    868   1805  -1402       C  
ATOM    298  CG1 ILE A 141     -43.897-132.359 312.605  1.00102.73           C  
ANISOU  298  CG1 ILE A 141    12326   9362  17343    850   1666  -1119       C  
ATOM    299  CG2 ILE A 141     -46.092-131.513 313.468  1.00104.57           C  
ANISOU  299  CG2 ILE A 141    12340   9524  17869   1046   1793  -1257       C  
ATOM    300  CD1 ILE A 141     -44.419-133.659 312.024  1.00 98.40           C  
ANISOU  300  CD1 ILE A 141    11766   8975  16646    930   1535   -931       C  
ATOM    301  N   LEU A 142     -44.734-130.863 316.795  1.00114.19           N  
ANISOU  301  N   LEU A 142    13541  10947  18900    699   2146  -2216       N  
ATOM    302  CA  LEU A 142     -45.461-130.402 317.975  1.00118.71           C  
ANISOU  302  CA  LEU A 142    13980  11590  19535    701   2297  -2542       C  
ATOM    303  C   LEU A 142     -44.889-129.089 318.492  1.00117.69           C  
ANISOU  303  C   LEU A 142    13846  11300  19571    609   2405  -2784       C  
ATOM    304  O   LEU A 142     -45.636-128.210 318.938  1.00123.16           O  
ANISOU  304  O   LEU A 142    14428  11886  20479    676   2502  -2952       O  
ATOM    305  CB  LEU A 142     -45.432-131.470 319.068  1.00120.33           C  
ANISOU  305  CB  LEU A 142    14144  12135  19441    600   2357  -2779       C  
ATOM    306  CG  LEU A 142     -46.610-132.447 319.102  1.00121.09           C  
ANISOU  306  CG  LEU A 142    14140  12397  19472    711   2343  -2697       C  
ATOM    307  CD1 LEU A 142     -46.710-133.242 317.807  1.00121.15           C  
ANISOU  307  CD1 LEU A 142    14225  12329  19477    813   2167  -2299       C  
ATOM    308  CD2 LEU A 142     -46.492-133.377 320.299  1.00123.36           C  
ANISOU  308  CD2 LEU A 142    14374  13032  19467    581   2435  -2963       C  
ATOM    309  N   HIS A 143     -43.564-128.940 318.444  1.00115.67           N  
ANISOU  309  N   HIS A 143    13696  11023  19228    454   2393  -2819       N  
ATOM    310  CA  HIS A 143     -42.962-127.645 318.741  1.00120.95           C  
ANISOU  310  CA  HIS A 143    14364  11496  20094    362   2484  -3006       C  
ATOM    311  C   HIS A 143     -43.381-126.607 317.708  1.00122.34           C  
ANISOU  311  C   HIS A 143    14551  11302  20632    498   2444  -2754       C  
ATOM    312  O   HIS A 143     -43.648-125.448 318.050  1.00122.58           O  
ANISOU  312  O   HIS A 143    14519  11123  20934    518   2536  -2919       O  
ATOM    313  CB  HIS A 143     -41.439-127.776 318.793  1.00122.50           C  
ANISOU  313  CB  HIS A 143    14664  11765  20116    164   2469  -3067       C  
ATOM    314  CG  HIS A 143     -40.725-126.477 318.995  1.00128.70           C  
ANISOU  314  CG  HIS A 143    15453  12339  21109     50   2557  -3238       C  
ATOM    315  ND1 HIS A 143     -40.569-125.896 320.236  1.00133.02           N  
ANISOU  315  ND1 HIS A 143    15911  12976  21654    -73   2696  -3649       N  
ATOM    316  CD2 HIS A 143     -40.121-125.645 318.113  1.00130.15           C  
ANISOU  316  CD2 HIS A 143    15712  12229  21512     28   2527  -3057       C  
ATOM    317  CE1 HIS A 143     -39.901-124.763 320.109  1.00134.38           C  
ANISOU  317  CE1 HIS A 143    16107  12901  22051   -160   2747  -3722       C  
ATOM    318  NE2 HIS A 143     -39.618-124.588 318.831  1.00132.16           N  
ANISOU  318  NE2 HIS A 143    15928  12376  21911   -103   2648  -3360       N  
ATOM    319  N   SER A 144     -43.455-127.010 316.435  1.00118.45           N  
ANISOU  319  N   SER A 144    14129  10730  20148    592   2305  -2354       N  
ATOM    320  CA  SER A 144     -43.921-126.102 315.391  1.00115.18           C  
ANISOU  320  CA  SER A 144    13714   9998  20053    725   2251  -2070       C  
ATOM    321  C   SER A 144     -45.424-125.860 315.485  1.00118.70           C  
ANISOU  321  C   SER A 144    14027  10389  20684    926   2266  -2057       C  
ATOM    322  O   SER A 144     -45.894-124.767 315.148  1.00114.23           O  
ANISOU  322  O   SER A 144    13419   9536  20446   1029   2279  -1987       O  
ATOM    323  CB  SER A 144     -43.549-126.653 314.013  1.00102.35           C  
ANISOU  323  CB  SER A 144    12182   8361  18346    748   2098  -1654       C  
ATOM    324  OG  SER A 144     -44.051-125.828 312.977  1.00101.68           O  
ANISOU  324  OG  SER A 144    12083   8003  18546    873   2036  -1345       O  
ATOM    325  N   ARG A 145     -46.188-126.861 315.938  1.00124.74           N  
ANISOU  325  N   ARG A 145    14719  11420  21255    983   2265  -2125       N  
ATOM    326  CA  ARG A 145     -47.618-126.669 316.159  1.00129.05           C  
ANISOU  326  CA  ARG A 145    15116  11956  21962   1162   2299  -2165       C  
ATOM    327  C   ARG A 145     -47.878-125.596 317.210  1.00131.51           C  
ANISOU  327  C   ARG A 145    15329  12156  22484   1155   2457  -2545       C  
ATOM    328  O   ARG A 145     -48.856-124.847 317.106  1.00137.67           O  
ANISOU  328  O   ARG A 145    16002  12759  23546   1322   2479  -2540       O  
ATOM    329  CB  ARG A 145     -48.271-127.988 316.576  1.00131.70           C  
ANISOU  329  CB  ARG A 145    15384  12622  22033   1186   2290  -2207       C  
ATOM    330  CG  ARG A 145     -49.774-127.889 316.788  1.00138.30           C  
ANISOU  330  CG  ARG A 145    16044  13492  23014   1367   2329  -2248       C  
ATOM    331  CD  ARG A 145     -50.327-129.028 317.634  1.00136.13           C  
ANISOU  331  CD  ARG A 145    15672  13568  22485   1337   2387  -2427       C  
ATOM    332  NE  ARG A 145     -49.950-128.902 319.039  1.00133.50           N  
ANISOU  332  NE  ARG A 145    15297  13402  22026   1186   2547  -2862       N  
ATOM    333  CZ  ARG A 145     -50.432-129.667 320.013  1.00127.76           C  
ANISOU  333  CZ  ARG A 145    14454  13003  21087   1134   2641  -3094       C  
ATOM    334  NH1 ARG A 145     -50.031-129.482 321.263  1.00124.96           N  
ANISOU  334  NH1 ARG A 145    14056  12832  20593    976   2782  -3485       N  
ATOM    335  NH2 ARG A 145     -51.318-130.615 319.739  1.00125.81           N  
ANISOU  335  NH2 ARG A 145    14120  12926  20757   1226   2598  -2934       N  
ATOM    336  N   SER A 146     -47.005-125.491 318.216  1.00129.66           N  
ANISOU  336  N   SER A 146    15118  12026  22119    965   2564  -2886       N  
ATOM    337  CA  SER A 146     -47.192-124.480 319.254  1.00135.24           C  
ANISOU  337  CA  SER A 146    15722  12653  23012    936   2718  -3285       C  
ATOM    338  C   SER A 146     -46.902-123.075 318.741  1.00141.99           C  
ANISOU  338  C   SER A 146    16612  13087  24252    972   2723  -3225       C  
ATOM    339  O   SER A 146     -47.317-122.091 319.367  1.00149.57           O  
ANISOU  339  O   SER A 146    17470  13889  25470   1013   2832  -3504       O  
ATOM    340  CB  SER A 146     -46.296-124.782 320.453  1.00133.01           C  
ANISOU  340  CB  SER A 146    15442  12640  22455    703   2822  -3661       C  
ATOM    341  OG  SER A 146     -44.966-125.039 320.043  1.00130.53           O  
ANISOU  341  OG  SER A 146    15280  12327  21991    548   2757  -3533       O  
ATOM    342  N   LEU A 147     -46.184-122.951 317.626  1.00138.00           N  
ANISOU  342  N   LEU A 147    16241  12394  23796    950   2610  -2877       N  
ATOM    343  CA  LEU A 147     -45.750-121.634 317.178  1.00136.43           C  
ANISOU  343  CA  LEU A 147    16088  11799  23951    944   2620  -2818       C  
ATOM    344  C   LEU A 147     -46.472-121.167 315.920  1.00139.75           C  
ANISOU  344  C   LEU A 147    16511  11938  24652   1147   2502  -2396       C  
ATOM    345  O   LEU A 147     -46.872-119.999 315.835  1.00148.98           O  
ANISOU  345  O   LEU A 147    17632  12771  26202   1247   2534  -2418       O  
ATOM    346  CB  LEU A 147     -44.233-121.638 316.945  1.00132.76           C  
ANISOU  346  CB  LEU A 147    15765  11323  23355    724   2604  -2777       C  
ATOM    347  CG  LEU A 147     -43.299-121.267 318.117  1.00133.62           C  
ANISOU  347  CG  LEU A 147    15866  11512  23391    505   2742  -3221       C  
ATOM    348  CD1 LEU A 147     -43.489-122.155 319.345  1.00131.40           C  
ANISOU  348  CD1 LEU A 147    15499  11646  22780    433   2821  -3564       C  
ATOM    349  CD2 LEU A 147     -41.836-121.280 317.668  1.00134.21           C  
ANISOU  349  CD2 LEU A 147    16078  11563  23355    307   2706  -3115       C  
ATOM    350  N   ARG A 148     -46.661-122.062 314.949  1.00135.13           N  
ANISOU  350  N   ARG A 148    15969  11488  23886   1211   2363  -2017       N  
ATOM    351  CA  ARG A 148     -47.296-121.740 313.677  1.00136.93           C  
ANISOU  351  CA  ARG A 148    16190  11514  24321   1385   2233  -1580       C  
ATOM    352  C   ARG A 148     -48.386-122.765 313.397  1.00138.17           C  
ANISOU  352  C   ARG A 148    16262  11928  24308   1538   2155  -1424       C  
ATOM    353  O   ARG A 148     -48.133-123.974 313.440  1.00138.02           O  
ANISOU  353  O   ARG A 148    16281  12216  23945   1463   2118  -1406       O  
ATOM    354  CB  ARG A 148     -46.276-121.720 312.537  1.00134.39           C  
ANISOU  354  CB  ARG A 148    16009  11095  23957   1279   2126  -1218       C  
ATOM    355  N   CYS A 149     -49.593-122.278 313.109  1.00140.30           N  
ANISOU  355  N   CYS A 149    16411  12065  24833   1755   2127  -1314       N  
ATOM    356  CA  CYS A 149     -50.750-123.110 312.802  1.00137.36           C  
ANISOU  356  CA  CYS A 149    15928  11912  24349   1916   2053  -1160       C  
ATOM    357  C   CYS A 149     -51.053-123.160 311.309  1.00141.53           C  
ANISOU  357  C   CYS A 149    16467  12373  24933   2027   1876   -645       C  
ATOM    358  O   CYS A 149     -52.113-123.656 310.917  1.00142.47           O  
ANISOU  358  O   CYS A 149    16474  12637  25022   2183   1801   -481       O  
ATOM    359  CB  CYS A 149     -51.980-122.605 313.565  1.00136.54           C  
ANISOU  359  CB  CYS A 149    15647  11765  24468   2092   2146  -1418       C  
ATOM    360  SG  CYS A 149     -52.519-120.920 313.137  1.00134.38           S  
ANISOU  360  SG  CYS A 149    15308  11011  24737   2284   2140  -1318       S  
ATOM    361  N   ARG A 150     -50.150-122.653 310.470  1.00149.31           N  
ANISOU  361  N   ARG A 150    17572  13165  25993   1940   1810   -386       N  
ATOM    362  CA  ARG A 150     -50.373-122.617 309.028  1.00159.37           C  
ANISOU  362  CA  ARG A 150    18847  14390  27316   2024   1644    119       C  
ATOM    363  C   ARG A 150     -49.960-123.919 308.343  1.00157.74           C  
ANISOU  363  C   ARG A 150    18700  14502  26734   1935   1538    335       C  
ATOM    364  O   ARG A 150     -50.744-124.451 307.547  1.00160.13           O  
ANISOU  364  O   ARG A 150    18920  14956  26966   2055   1416    621       O  
ATOM    365  CB  ARG A 150     -49.642-121.426 308.401  1.00170.00           C  
ANISOU  365  CB  ARG A 150    20278  15381  28933   1968   1621    327       C  
ATOM    366  CG  ARG A 150     -49.831-121.307 306.896  1.00175.34           C  
ANISOU  366  CG  ARG A 150    20945  16017  29658   2036   1448    878       C  
ATOM    367  CD  ARG A 150     -51.307-121.255 306.527  1.00180.74           C  
ANISOU  367  CD  ARG A 150    21461  16730  30480   2287   1366   1054       C  
ATOM    368  NE  ARG A 150     -51.510-121.114 305.088  1.00185.60           N  
ANISOU  368  NE  ARG A 150    22049  17341  31130   2347   1193   1596       N  
ATOM    369  CZ  ARG A 150     -52.697-121.159 304.492  1.00189.41           C  
ANISOU  369  CZ  ARG A 150    22383  17902  31684   2547   1083   1849       C  
ATOM    370  NH1 ARG A 150     -52.786-121.020 303.176  1.00191.08           N  
ANISOU  370  NH1 ARG A 150    22565  18140  31898   2575    921   2354       N  
ATOM    371  NH2 ARG A 150     -53.797-121.345 305.210  1.00190.40           N  
ANISOU  371  NH2 ARG A 150    22375  18103  31867   2714   1134   1601       N  
ATOM    372  N   PRO A 151     -48.765-124.466 308.592  1.00157.41           N  
ANISOU  372  N   PRO A 151    18787  14571  26450   1735   1573    209       N  
ATOM    373  CA  PRO A 151     -48.402-125.730 307.932  1.00153.52           C  
ANISOU  373  CA  PRO A 151    18342  14366  25622   1669   1469    398       C  
ATOM    374  C   PRO A 151     -49.282-126.874 308.416  1.00149.24           C  
ANISOU  374  C   PRO A 151    17712  14116  24877   1746   1462    261       C  
ATOM    375  O   PRO A 151     -49.427-127.099 309.620  1.00147.49           O  
ANISOU  375  O   PRO A 151    17467  13972  24601   1718   1579   -107       O  
ATOM    376  CB  PRO A 151     -46.935-125.935 308.331  1.00151.95           C  
ANISOU  376  CB  PRO A 151    18288  14190  25256   1449   1535    212       C  
ATOM    377  CG  PRO A 151     -46.787-125.178 309.596  1.00153.96           C  
ANISOU  377  CG  PRO A 151    18540  14298  25660   1402   1693   -191       C  
ATOM    378  CD  PRO A 151     -47.654-123.970 309.428  1.00157.55           C  
ANISOU  378  CD  PRO A 151    18905  14464  26491   1558   1700   -103       C  
ATOM    379  N   SER A 152     -49.870-127.599 307.461  1.00148.25           N  
ANISOU  379  N   SER A 152    17526  14164  24638   1832   1323    569       N  
ATOM    380  CA  SER A 152     -50.776-128.689 307.810  1.00146.11           C  
ANISOU  380  CA  SER A 152    17155  14160  24199   1905   1303    479       C  
ATOM    381  C   SER A 152     -50.038-129.806 308.537  1.00141.70           C  
ANISOU  381  C   SER A 152    16688  13804  23347   1754   1349    225       C  
ATOM    382  O   SER A 152     -50.483-130.275 309.591  1.00141.34           O  
ANISOU  382  O   SER A 152    16588  13879  23234   1754   1437    -60       O  
ATOM    383  CB  SER A 152     -51.462-129.226 306.551  1.00144.27           C  
ANISOU  383  CB  SER A 152    16834  14080  23901   2009   1131    872       C  
ATOM    384  OG  SER A 152     -50.539-129.893 305.707  1.00139.70           O  
ANISOU  384  OG  SER A 152    16354  13617  23110   1896   1033   1070       O  
ATOM    385  N   TYR A 153     -48.906-130.245 307.984  1.00136.73           N  
ANISOU  385  N   TYR A 153    16186  13217  22547   1627   1290    333       N  
ATOM    386  CA  TYR A 153     -48.104-131.342 308.527  1.00130.31           C  
ANISOU  386  CA  TYR A 153    15466  12587  21459   1493   1307    132       C  
ATOM    387  C   TYR A 153     -48.902-132.635 308.665  1.00122.52           C  
ANISOU  387  C   TYR A 153    14403  11847  20303   1547   1248    117       C  
ATOM    388  O   TYR A 153     -48.548-133.502 309.472  1.00117.44           O  
ANISOU  388  O   TYR A 153    13804  11339  19478   1459   1287   -111       O  
ATOM    389  CB  TYR A 153     -47.479-130.968 309.877  1.00132.65           C  
ANISOU  389  CB  TYR A 153    15819  12827  21753   1377   1465   -257       C  
ATOM    390  CG  TYR A 153     -46.364-129.951 309.789  1.00137.48           C  
ANISOU  390  CG  TYR A 153    16530  13229  22477   1267   1519   -281       C  
ATOM    391  CD1 TYR A 153     -45.553-129.874 308.663  1.00137.70           C  
ANISOU  391  CD1 TYR A 153    16635  13198  22487   1213   1431     -5       C  
ATOM    392  CD2 TYR A 153     -46.121-129.067 310.833  1.00139.83           C  
ANISOU  392  CD2 TYR A 153    16829  13393  22907   1207   1662   -584       C  
ATOM    393  CE1 TYR A 153     -44.532-128.945 308.582  1.00138.74           C  
ANISOU  393  CE1 TYR A 153    16846  13132  22737   1095   1488    -17       C  
ATOM    394  CE2 TYR A 153     -45.104-128.136 310.760  1.00138.55           C  
ANISOU  394  CE2 TYR A 153    16747  13031  22864   1093   1712   -612       C  
ATOM    395  CZ  TYR A 153     -44.313-128.078 309.633  1.00137.49           C  
ANISOU  395  CZ  TYR A 153    16693  12830  22718   1034   1625   -322       C  
ATOM    396  OH  TYR A 153     -43.299-127.152 309.560  1.00136.86           O  
ANISOU  396  OH  TYR A 153    16685  12547  22769    903   1681   -343       O  
ATOM    397  N   HIS A 154     -49.980-132.786 307.892  1.00119.75           N  
ANISOU  397  N   HIS A 154    13925  11559  20015   1685   1148    365       N  
ATOM    398  CA  HIS A 154     -50.770-134.010 307.964  1.00118.63           C  
ANISOU  398  CA  HIS A 154    13690  11647  19738   1728   1086    364       C  
ATOM    399  C   HIS A 154     -50.029-135.182 307.334  1.00114.62           C  
ANISOU  399  C   HIS A 154    13273  11306  18973   1632    959    461       C  
ATOM    400  O   HIS A 154     -50.098-136.310 307.836  1.00109.75           O  
ANISOU  400  O   HIS A 154    12681  10918  18101   1535    923    319       O  
ATOM    401  CB  HIS A 154     -52.124-133.803 307.288  1.00120.39           C  
ANISOU  401  CB  HIS A 154    13728  11917  20096   1895   1007    600       C  
ATOM    402  CG  HIS A 154     -53.059-132.932 308.066  1.00122.45           C  
ANISOU  402  CG  HIS A 154    13868  12079  20577   2002   1126    444       C  
ATOM    403  ND1 HIS A 154     -53.835-131.958 307.476  1.00128.44           N  
ANISOU  403  ND1 HIS A 154    14518  12723  21560   2151   1089    642       N  
ATOM    404  CD2 HIS A 154     -53.347-132.891 309.389  1.00122.85           C  
ANISOU  404  CD2 HIS A 154    13877  12141  20661   1986   1281    102       C  
ATOM    405  CE1 HIS A 154     -54.557-131.351 308.401  1.00131.56           C  
ANISOU  405  CE1 HIS A 154    14813  13045  22130   2233   1215    411       C  
ATOM    406  NE2 HIS A 154     -54.280-131.899 309.571  1.00128.56           N  
ANISOU  406  NE2 HIS A 154    14465  12753  21630   2131   1339     76       N  
ATOM    407  N   PHE A 155     -49.313-134.937 306.237  1.00115.24           N  
ANISOU  407  N   PHE A 155    13418  11359  19008   1600    866    694       N  
ATOM    408  CA  PHE A 155     -48.587-136.012 305.570  1.00113.34           C  
ANISOU  408  CA  PHE A 155    13270  11384  18411   1466    726    744       C  
ATOM    409  C   PHE A 155     -47.313-136.379 306.323  1.00114.19           C  
ANISOU  409  C   PHE A 155    13534  11500  18352   1315    787    483       C  
ATOM    410  O   PHE A 155     -47.027-137.564 306.530  1.00113.01           O  
ANISOU  410  O   PHE A 155    13441  11562  17937   1225    713    366       O  
ATOM    411  CB  PHE A 155     -48.259-135.612 304.131  1.00115.25           C  
ANISOU  411  CB  PHE A 155    13501  11660  18630   1471    614   1073       C  
ATOM    412  CG  PHE A 155     -47.073-136.336 303.558  1.00117.95           C  
ANISOU  412  CG  PHE A 155    13955  12206  18654   1318    530   1051       C  
ATOM    413  CD1 PHE A 155     -45.879-135.671 303.339  1.00120.28           C  
ANISOU  413  CD1 PHE A 155    14342  12396  18963   1230    581   1076       C  
ATOM    414  CD2 PHE A 155     -47.149-137.685 303.252  1.00123.11           C  
ANISOU  414  CD2 PHE A 155    14610  13154  19011   1259    403    987       C  
ATOM    415  CE1 PHE A 155     -44.784-136.335 302.816  1.00123.57           C  
ANISOU  415  CE1 PHE A 155    14834  13032  19086   1099    511   1033       C  
ATOM    416  CE2 PHE A 155     -46.056-138.356 302.732  1.00124.79           C  
ANISOU  416  CE2 PHE A 155    14908  13550  18958   1141    330    928       C  
ATOM    417  CZ  PHE A 155     -44.873-137.679 302.512  1.00125.24           C  
ANISOU  417  CZ  PHE A 155    15038  13535  19013   1068    386    949       C  
ATOM    418  N   ILE A 156     -46.534-135.377 306.736  1.00116.04           N  
ANISOU  418  N   ILE A 156    13833  11501  18756   1284    914    393       N  
ATOM    419  CA  ILE A 156     -45.249-135.660 307.366  1.00114.58           C  
ANISOU  419  CA  ILE A 156    13778  11355  18402   1134    961    163       C  
ATOM    420  C   ILE A 156     -45.445-136.265 308.753  1.00103.88           C  
ANISOU  420  C   ILE A 156    12431  10078  16960   1095   1033   -132       C  
ATOM    421  O   ILE A 156     -44.638-137.093 309.196  1.00 92.90           O  
ANISOU  421  O   ILE A 156    11124   8846  15326    983    996   -277       O  
ATOM    422  CB  ILE A 156     -44.386-134.385 307.410  1.00127.49           C  
ANISOU  422  CB  ILE A 156    15467  12726  20246   1086   1077    144       C  
ATOM    423  CG1 ILE A 156     -42.961-134.715 307.857  1.00133.44           C  
ANISOU  423  CG1 ILE A 156    16335  13579  20788    920   1100    -60       C  
ATOM    424  CG2 ILE A 156     -45.007-133.336 308.318  1.00135.86           C  
ANISOU  424  CG2 ILE A 156    16473  13547  21599   1150   1230     -7       C  
ATOM    425  CD1 ILE A 156     -42.249-135.677 306.932  1.00139.64           C  
ANISOU  425  CD1 ILE A 156    17160  14635  21260    853    947     53       C  
ATOM    426  N   GLY A 157     -46.515-135.883 309.453  1.00102.54           N  
ANISOU  426  N   GLY A 157    12160   9824  16979   1186   1130   -217       N  
ATOM    427  CA  GLY A 157     -46.778-136.476 310.752  1.00 99.06           C  
ANISOU  427  CA  GLY A 157    11704   9517  16420   1128   1199   -472       C  
ATOM    428  C   GLY A 157     -47.214-137.924 310.648  1.00 95.04           C  
ANISOU  428  C   GLY A 157    11190   9275  15647   1087   1054   -402       C  
ATOM    429  O   GLY A 157     -46.766-138.773 311.424  1.00 91.65           O  
ANISOU  429  O   GLY A 157    10823   8998  15000    973   1036   -542       O  
ATOM    430  N   SER A 158     -48.089-138.227 309.686  1.00 98.15           N  
ANISOU  430  N   SER A 158    11505   9726  16063   1172    942   -177       N  
ATOM    431  CA  SER A 158     -48.525-139.605 309.489  1.00102.93           C  
ANISOU  431  CA  SER A 158    12104  10561  16445   1118    797   -116       C  
ATOM    432  C   SER A 158     -47.362-140.496 309.073  1.00 99.17           C  
ANISOU  432  C   SER A 158    11767  10181  15733   1016    671   -119       C  
ATOM    433  O   SER A 158     -47.217-141.617 309.576  1.00101.24           O  
ANISOU  433  O   SER A 158    12080  10572  15815    926    601   -198       O  
ATOM    434  CB  SER A 158     -49.640-139.657 308.444  1.00109.63           C  
ANISOU  434  CB  SER A 158    12825  11466  17364   1219    699    115       C  
ATOM    435  OG  SER A 158     -49.976-140.996 308.121  1.00113.38           O  
ANISOU  435  OG  SER A 158    13301  12148  17630   1144    548    161       O  
ATOM    436  N   LEU A 159     -46.520-140.012 308.157  1.00 94.91           N  
ANISOU  436  N   LEU A 159    11279   9583  15201   1028    640    -28       N  
ATOM    437  CA  LEU A 159     -45.377-140.802 307.712  1.00 91.09           C  
ANISOU  437  CA  LEU A 159    10899   9211  14499    947    531    -59       C  
ATOM    438  C   LEU A 159     -44.397-141.046 308.853  1.00 93.07           C  
ANISOU  438  C   LEU A 159    11244   9462  14658    857    589   -277       C  
ATOM    439  O   LEU A 159     -43.835-142.141 308.976  1.00 99.90           O  
ANISOU  439  O   LEU A 159    12172  10444  15341    800    484   -342       O  
ATOM    440  CB  LEU A 159     -44.682-140.100 306.546  1.00 93.82           C  
ANISOU  440  CB  LEU A 159    11254   9531  14862    962    510     82       C  
ATOM    441  CG  LEU A 159     -43.538-140.859 305.872  1.00 96.70           C  
ANISOU  441  CG  LEU A 159    11686  10055  14999    893    400     47       C  
ATOM    442  CD1 LEU A 159     -44.045-142.149 305.247  1.00 98.54           C  
ANISOU  442  CD1 LEU A 159    11891  10472  15077    898    236     74       C  
ATOM    443  CD2 LEU A 159     -42.859-139.985 304.830  1.00 99.05           C  
ANISOU  443  CD2 LEU A 159    11973  10352  15309    880    413    193       C  
ATOM    444  N   ALA A 160     -44.185-140.041 309.705  1.00 93.48           N  
ANISOU  444  N   ALA A 160    11296   9382  14841    845    750   -399       N  
ATOM    445  CA  ALA A 160     -43.263-140.201 310.825  1.00 89.85           C  
ANISOU  445  CA  ALA A 160    10904   8964  14272    747    807   -611       C  
ATOM    446  C   ALA A 160     -43.821-141.162 311.867  1.00 86.13           C  
ANISOU  446  C   ALA A 160    10420   8626  13680    699    782   -688       C  
ATOM    447  O   ALA A 160     -43.099-142.030 312.371  1.00 87.32           O  
ANISOU  447  O   ALA A 160    10635   8893  13649    623    707   -755       O  
ATOM    448  CB  ALA A 160     -42.958-138.841 311.453  1.00 96.58           C  
ANISOU  448  CB  ALA A 160    11744   9652  15301    728    992   -752       C  
ATOM    449  N   VAL A 161     -45.106-141.017 312.208  1.00 88.48           N  
ANISOU  449  N   VAL A 161    10622   8918  14080    739    842   -665       N  
ATOM    450  CA  VAL A 161     -45.719-141.906 313.193  1.00 92.94           C  
ANISOU  450  CA  VAL A 161    11158   9636  14519    666    826   -710       C  
ATOM    451  C   VAL A 161     -45.663-143.351 312.715  1.00 92.37           C  
ANISOU  451  C   VAL A 161    11144   9662  14289    628    626   -585       C  
ATOM    452  O   VAL A 161     -45.342-144.265 313.485  1.00 88.20           O  
ANISOU  452  O   VAL A 161    10666   9239  13608    534    563   -617       O  
ATOM    453  CB  VAL A 161     -47.166-141.465 313.487  1.00 96.27           C  
ANISOU  453  CB  VAL A 161    11436  10059  15083    721    927   -704       C  
ATOM    454  CG1 VAL A 161     -47.909-142.556 314.241  1.00 95.94           C  
ANISOU  454  CG1 VAL A 161    11353  10211  14889    623    879   -685       C  
ATOM    455  CG2 VAL A 161     -47.177-140.172 314.282  1.00101.67           C  
ANISOU  455  CG2 VAL A 161    12058  10650  15922    744   1136   -904       C  
ATOM    456  N   ALA A 162     -45.970-143.579 311.436  1.00 93.04           N  
ANISOU  456  N   ALA A 162    11218   9716  14417    699    518   -441       N  
ATOM    457  CA  ALA A 162     -45.919-144.932 310.896  1.00 91.27           C  
ANISOU  457  CA  ALA A 162    11042   9563  14073    664    330   -366       C  
ATOM    458  C   ALA A 162     -44.498-145.480 310.918  1.00 88.21           C  
ANISOU  458  C   ALA A 162    10768   9185  13563    633    247   -444       C  
ATOM    459  O   ALA A 162     -44.277-146.640 311.284  1.00 83.51           O  
ANISOU  459  O   ALA A 162    10228   8631  12872    578    128   -448       O  
ATOM    460  CB  ALA A 162     -46.483-144.950 309.476  1.00 92.72           C  
ANISOU  460  CB  ALA A 162    11170   9752  14308    737    242   -232       C  
ATOM    461  N   ASP A 163     -43.519-144.655 310.538  1.00 90.66           N  
ANISOU  461  N   ASP A 163    11105   9454  13887    668    305   -497       N  
ATOM    462  CA  ASP A 163     -42.136-145.120 310.509  1.00 93.05           C  
ANISOU  462  CA  ASP A 163    11486   9796  14072    649    231   -584       C  
ATOM    463  C   ASP A 163     -41.604-145.368 311.915  1.00 87.36           C  
ANISOU  463  C   ASP A 163    10803   9121  13267    573    262   -687       C  
ATOM    464  O   ASP A 163     -40.847-146.319 312.139  1.00 83.37           O  
ANISOU  464  O   ASP A 163    10350   8667  12659    557    141   -715       O  
ATOM    465  CB  ASP A 163     -41.257-144.113 309.767  1.00102.70           C  
ANISOU  465  CB  ASP A 163    12707  10992  15322    676    298   -606       C  
ATOM    466  CG  ASP A 163     -41.524-144.095 308.272  1.00111.73           C  
ANISOU  466  CG  ASP A 163    13813  12160  16479    733    225   -483       C  
ATOM    467  OD1 ASP A 163     -42.620-144.529 307.854  1.00112.72           O  
ANISOU  467  OD1 ASP A 163    13893  12300  16636    761    162   -383       O  
ATOM    468  OD2 ASP A 163     -40.639-143.645 307.514  1.00116.27           O  
ANISOU  468  OD2 ASP A 163    14389  12773  17015    735    232   -484       O  
ATOM    469  N   LEU A 164     -41.990-144.528 312.876  1.00 91.47           N  
ANISOU  469  N   LEU A 164    11283   9638  13831    529    420   -751       N  
ATOM    470  CA  LEU A 164     -41.560-144.740 314.254  1.00 97.03           C  
ANISOU  470  CA  LEU A 164    12002  10449  14417    435    453   -849       C  
ATOM    471  C   LEU A 164     -42.187-146.006 314.825  1.00 95.82           C  
ANISOU  471  C   LEU A 164    11856  10374  14176    379    336   -746       C  
ATOM    472  O   LEU A 164     -41.480-146.908 315.290  1.00 94.27           O  
ANISOU  472  O   LEU A 164    11712  10243  13862    339    215   -726       O  
ATOM    473  CB  LEU A 164     -41.913-143.521 315.110  1.00102.59           C  
ANISOU  473  CB  LEU A 164    12640  11153  15185    393    663   -982       C  
ATOM    474  CG  LEU A 164     -41.066-143.261 316.361  1.00104.74           C  
ANISOU  474  CG  LEU A 164    12913  11559  15325    286    738  -1152       C  
ATOM    475  CD1 LEU A 164     -41.281-141.839 316.844  1.00109.18           C  
ANISOU  475  CD1 LEU A 164    13410  12064  16010    264    956  -1339       C  
ATOM    476  CD2 LEU A 164     -41.369-144.247 317.483  1.00102.93           C  
ANISOU  476  CD2 LEU A 164    12671  11522  14915    187    674  -1108       C  
ATOM    477  N   LEU A 165     -43.520-146.089 314.798  1.00 98.00           N  
ANISOU  477  N   LEU A 165    12072  10644  14519    371    364   -664       N  
ATOM    478  CA  LEU A 165     -44.201-147.273 315.312  1.00 95.38           C  
ANISOU  478  CA  LEU A 165    11741  10383  14115    286    257   -544       C  
ATOM    479  C   LEU A 165     -43.787-148.523 314.549  1.00 87.72           C  
ANISOU  479  C   LEU A 165    10854   9334  13141    315     41   -450       C  
ATOM    480  O   LEU A 165     -43.531-149.571 315.153  1.00 84.01           O  
ANISOU  480  O   LEU A 165    10435   8890  12597    246    -83   -376       O  
ATOM    481  CB  LEU A 165     -45.717-147.087 315.240  1.00 94.12           C  
ANISOU  481  CB  LEU A 165    11479  10244  14040    275    327   -482       C  
ATOM    482  CG  LEU A 165     -46.335-145.983 316.098  1.00 91.82           C  
ANISOU  482  CG  LEU A 165    11075  10037  13774    253    543   -598       C  
ATOM    483  CD1 LEU A 165     -47.854-146.005 315.975  1.00 88.97           C  
ANISOU  483  CD1 LEU A 165    10591   9721  13493    252    584   -524       C  
ATOM    484  CD2 LEU A 165     -45.905-146.120 317.552  1.00 90.28           C  
ANISOU  484  CD2 LEU A 165    10878  10023  13400    118    599   -676       C  
ATOM    485  N   GLY A 166     -43.713-148.429 313.220  1.00 85.37           N  
ANISOU  485  N   GLY A 166    10563   8945  12927    416    -10   -452       N  
ATOM    486  CA  GLY A 166     -43.337-149.589 312.429  1.00 89.97           C  
ANISOU  486  CA  GLY A 166    11206   9461  13516    449   -204   -421       C  
ATOM    487  C   GLY A 166     -41.952-150.102 312.772  1.00 92.48           C  
ANISOU  487  C   GLY A 166    11597   9777  13765    471   -295   -484       C  
ATOM    488  O   GLY A 166     -41.768-151.288 313.057  1.00 96.19           O  
ANISOU  488  O   GLY A 166    12117  10197  14232    447   -450   -428       O  
ATOM    489  N   SER A 167     -40.961-149.207 312.769  1.00 91.47           N  
ANISOU  489  N   SER A 167    11465   9696  13594    513   -203   -594       N  
ATOM    490  CA  SER A 167     -39.582-149.624 313.003  1.00 93.27           C  
ANISOU  490  CA  SER A 167    11733   9955  13753    547   -289   -667       C  
ATOM    491  C   SER A 167     -39.399-150.209 314.399  1.00 90.50           C  
ANISOU  491  C   SER A 167    11404   9665  13318    465   -338   -602       C  
ATOM    492  O   SER A 167     -38.715-151.226 314.565  1.00 88.84           O  
ANISOU  492  O   SER A 167    11231   9426  13097    499   -502   -570       O  
ATOM    493  CB  SER A 167     -38.634-148.445 312.790  1.00102.19           C  
ANISOU  493  CB  SER A 167    12835  11147  14845    572   -162   -794       C  
ATOM    494  OG  SER A 167     -37.292-148.818 313.046  1.00110.53           O  
ANISOU  494  OG  SER A 167    13903  12270  15822    602   -240   -873       O  
ATOM    495  N   VAL A 168     -40.000-149.583 315.415  1.00 92.10           N  
ANISOU  495  N   VAL A 168    11569   9963  13461    360   -201   -583       N  
ATOM    496  CA  VAL A 168     -39.833-150.064 316.787  1.00 96.47           C  
ANISOU  496  CA  VAL A 168    12124  10644  13887    255   -238   -508       C  
ATOM    497  C   VAL A 168     -40.334-151.496 316.913  1.00100.71           C  
ANISOU  497  C   VAL A 168    12708  11098  14461    220   -427   -315       C  
ATOM    498  O   VAL A 168     -39.633-152.376 317.425  1.00107.74           O  
ANISOU  498  O   VAL A 168    13634  11991  15310    218   -581   -224       O  
ATOM    499  CB  VAL A 168     -40.549-149.133 317.782  1.00 96.36           C  
ANISOU  499  CB  VAL A 168    12038  10783  13793    136    -40   -554       C  
ATOM    500  CG1 VAL A 168     -40.588-149.773 319.160  1.00 94.23           C  
ANISOU  500  CG1 VAL A 168    11753  10694  13354     -3    -91   -437       C  
ATOM    501  CG2 VAL A 168     -39.851-147.792 317.852  1.00 98.53           C  
ANISOU  501  CG2 VAL A 168    12276  11114  14048    152    129   -760       C  
ATOM    502  N   ILE A 169     -41.555-151.752 316.441  1.00 99.11           N  
ANISOU  502  N   ILE A 169    12497  10810  14352    190   -425   -239       N  
ATOM    503  CA  ILE A 169     -42.111-153.097 316.539  1.00 97.53           C  
ANISOU  503  CA  ILE A 169    12340  10506  14211    125   -599    -57       C  
ATOM    504  C   ILE A 169     -41.375-154.051 315.605  1.00 97.50           C  
ANISOU  504  C   ILE A 169    12407  10304  14335    251   -796    -83       C  
ATOM    505  O   ILE A 169     -41.149-155.219 315.945  1.00102.97           O  
ANISOU  505  O   ILE A 169    13155  10887  15083    231   -976     46       O  
ATOM    506  CB  ILE A 169     -43.623-153.073 316.252  1.00 96.67           C  
ANISOU  506  CB  ILE A 169    12181  10386  14163     45   -539      8       C  
ATOM    507  CG1 ILE A 169     -44.303-151.979 317.075  1.00103.11           C  
ANISOU  507  CG1 ILE A 169    12898  11405  14873    -41   -320    -29       C  
ATOM    508  CG2 ILE A 169     -44.246-154.420 316.574  1.00 93.44           C  
ANISOU  508  CG2 ILE A 169    11811   9889  13804    -78   -702    212       C  
ATOM    509  CD1 ILE A 169     -45.780-151.821 316.778  1.00105.33           C  
ANISOU  509  CD1 ILE A 169    13096  11707  15220    -95   -244     13       C  
ATOM    510  N   PHE A 170     -40.978-153.571 314.423  1.00 93.16           N  
ANISOU  510  N   PHE A 170    11846   9709  13841    381   -764   -252       N  
ATOM    511  CA  PHE A 170     -40.303-154.436 313.458  1.00 89.33           C  
ANISOU  511  CA  PHE A 170    11401   9074  13465    504   -932   -333       C  
ATOM    512  C   PHE A 170     -38.956-154.907 313.990  1.00 83.34           C  
ANISOU  512  C   PHE A 170    10668   8313  12683    580  -1042   -349       C  
ATOM    513  O   PHE A 170     -38.722-156.110 314.146  1.00 84.36           O  
ANISOU  513  O   PHE A 170    10845   8287  12920    608  -1232   -270       O  
ATOM    514  CB  PHE A 170     -40.124-153.707 312.124  1.00 87.02           C  
ANISOU  514  CB  PHE A 170    11066   8814  13183    604   -855   -506       C  
ATOM    515  CG  PHE A 170     -39.339-154.489 311.107  1.00 88.94           C  
ANISOU  515  CG  PHE A 170    11321   8969  13504    731  -1001   -646       C  
ATOM    516  CD1 PHE A 170     -39.968-155.416 310.289  1.00 86.32           C  
ANISOU  516  CD1 PHE A 170    11000   8504  13292    734  -1123   -672       C  
ATOM    517  CD2 PHE A 170     -37.972-154.297 310.965  1.00 87.95           C  
ANISOU  517  CD2 PHE A 170    11176   8911  13329    840  -1010   -780       C  
ATOM    518  CE1 PHE A 170     -39.251-156.137 309.349  1.00 78.80           C  
ANISOU  518  CE1 PHE A 170    10041   7484  12414    853  -1247   -853       C  
ATOM    519  CE2 PHE A 170     -37.247-155.017 310.030  1.00 83.71           C  
ANISOU  519  CE2 PHE A 170    10623   8322  12862    966  -1134   -944       C  
ATOM    520  CZ  PHE A 170     -37.888-155.937 309.220  1.00 81.41           C  
ANISOU  520  CZ  PHE A 170    10345   7894  12695    977  -1249   -993       C  
ATOM    521  N   VAL A 171     -38.054-153.961 314.266  1.00 80.26           N  
ANISOU  521  N   VAL A 171    10239   8085  12171    615   -932   -450       N  
ATOM    522  CA  VAL A 171     -36.700-154.306 314.693  1.00 79.05           C  
ANISOU  522  CA  VAL A 171    10079   7975  11980    700  -1032   -486       C  
ATOM    523  C   VAL A 171     -36.733-155.206 315.921  1.00 77.49           C  
ANISOU  523  C   VAL A 171     9916   7757  11772    629  -1169   -266       C  
ATOM    524  O   VAL A 171     -35.991-156.194 316.003  1.00 73.35           O  
ANISOU  524  O   VAL A 171     9409   7126  11336    727  -1360   -221       O  
ATOM    525  CB  VAL A 171     -35.881-153.026 314.949  1.00 86.84           C  
ANISOU  525  CB  VAL A 171    11006   9172  12817    694   -867   -619       C  
ATOM    526  CG1 VAL A 171     -34.519-153.367 315.536  1.00 88.96           C  
ANISOU  526  CG1 VAL A 171    11243   9537  13021    762   -973   -642       C  
ATOM    527  CG2 VAL A 171     -35.727-152.230 313.663  1.00 86.19           C  
ANISOU  527  CG2 VAL A 171    10891   9096  12760    760   -761   -792       C  
ATOM    528  N   TYR A 172     -37.599-154.891 316.889  1.00 81.56           N  
ANISOU  528  N   TYR A 172    10427   8383  12181    459  -1077   -120       N  
ATOM    529  CA  TYR A 172     -37.694-155.718 318.088  1.00 93.97           C  
ANISOU  529  CA  TYR A 172    12018   9982  13703    356  -1202    130       C  
ATOM    530  C   TYR A 172     -38.163-157.127 317.747  1.00102.15           C  
ANISOU  530  C   TYR A 172    13129  10734  14951    369  -1412    291       C  
ATOM    531  O   TYR A 172     -37.538-158.116 318.146  1.00100.98           O  
ANISOU  531  O   TYR A 172    13011  10474  14882    420  -1613    435       O  
ATOM    532  CB  TYR A 172     -38.631-155.067 319.107  1.00 92.60           C  
ANISOU  532  CB  TYR A 172    11803  10027  13353    153  -1039    225       C  
ATOM    533  CG  TYR A 172     -38.736-155.830 320.412  1.00 97.28           C  
ANISOU  533  CG  TYR A 172    12398  10729  13837      8  -1153    507       C  
ATOM    534  CD1 TYR A 172     -37.773-155.685 321.403  1.00 99.78           C  
ANISOU  534  CD1 TYR A 172    12668  11275  13968    -14  -1184    554       C  
ATOM    535  CD2 TYR A 172     -39.797-156.694 320.652  1.00101.83           C  
ANISOU  535  CD2 TYR A 172    13010  11201  14480   -127  -1236    744       C  
ATOM    536  CE1 TYR A 172     -37.864-156.380 322.598  1.00105.46           C  
ANISOU  536  CE1 TYR A 172    13377  12134  14560   -159  -1299    850       C  
ATOM    537  CE2 TYR A 172     -39.897-157.393 321.843  1.00106.73           C  
ANISOU  537  CE2 TYR A 172    13627  11938  14988   -284  -1345   1046       C  
ATOM    538  CZ  TYR A 172     -38.928-157.232 322.812  1.00109.27           C  
ANISOU  538  CZ  TYR A 172    13902  12504  15113   -296  -1379   1108       C  
ATOM    539  OH  TYR A 172     -39.022-157.926 323.999  1.00114.34           O  
ANISOU  539  OH  TYR A 172    14529  13300  15616   -464  -1498   1444       O  
ATOM    540  N   SER A 173     -39.264-157.238 317.001  1.00104.29           N  
ANISOU  540  N   SER A 173    13421  10874  15331    322  -1375    268       N  
ATOM    541  CA  SER A 173     -39.770-158.557 316.634  1.00103.86           C  
ANISOU  541  CA  SER A 173    13433  10533  15495    308  -1566    389       C  
ATOM    542  C   SER A 173     -38.811-159.277 315.695  1.00108.75           C  
ANISOU  542  C   SER A 173    14082  10928  16312    519  -1729    227       C  
ATOM    543  O   SER A 173     -38.622-160.493 315.809  1.00119.72           O  
ANISOU  543  O   SER A 173    15526  12067  17894    551  -1940    346       O  
ATOM    544  CB  SER A 173     -41.153-158.433 315.995  1.00 94.18           C  
ANISOU  544  CB  SER A 173    12199   9265  14321    202  -1481    366       C  
ATOM    545  OG  SER A 173     -42.099-157.932 316.923  1.00 88.06           O  
ANISOU  545  OG  SER A 173    11380   8692  13389      9  -1346    520       O  
ATOM    546  N   PHE A 174     -38.192-158.543 314.768  1.00101.90           N  
ANISOU  546  N   PHE A 174    13166  10143  15406    661  -1634    -45       N  
ATOM    547  CA  PHE A 174     -37.278-159.168 313.818  1.00 97.13           C  
ANISOU  547  CA  PHE A 174    12559   9383  14964    861  -1766   -247       C  
ATOM    548  C   PHE A 174     -36.061-159.752 314.526  1.00 99.68           C  
ANISOU  548  C   PHE A 174    12877   9669  15329    981  -1921   -177       C  
ATOM    549  O   PHE A 174     -35.640-160.876 314.231  1.00103.81           O  
ANISOU  549  O   PHE A 174    13424   9937  16082   1107  -2119   -200       O  
ATOM    550  CB  PHE A 174     -36.849-158.149 312.763  1.00 87.71           C  
ANISOU  550  CB  PHE A 174    11296   8362  13669    955  -1613   -522       C  
ATOM    551  CG  PHE A 174     -36.448-158.761 311.455  1.00 92.22           C  
ANISOU  551  CG  PHE A 174    11844   8807  14388   1106  -1707   -768       C  
ATOM    552  CD1 PHE A 174     -37.410-159.195 310.557  1.00 99.45           C  
ANISOU  552  CD1 PHE A 174    12776   9598  15411   1059  -1734   -837       C  
ATOM    553  CD2 PHE A 174     -35.110-158.890 311.116  1.00 93.05           C  
ANISOU  553  CD2 PHE A 174    11890   8954  14509   1289  -1765   -955       C  
ATOM    554  CE1 PHE A 174     -37.047-159.755 309.347  1.00102.45           C  
ANISOU  554  CE1 PHE A 174    13119   9902  15904   1185  -1814  -1103       C  
ATOM    555  CE2 PHE A 174     -34.737-159.449 309.906  1.00 95.03           C  
ANISOU  555  CE2 PHE A 174    12097   9129  14881   1427  -1839  -1222       C  
ATOM    556  CZ  PHE A 174     -35.708-159.882 309.020  1.00101.75           C  
ANISOU  556  CZ  PHE A 174    12970   9862  15831   1372  -1862  -1305       C  
ATOM    557  N   ILE A 175     -35.488-159.005 315.470  1.00100.34           N  
ANISOU  557  N   ILE A 175    12916  10005  15202    945  -1838   -100       N  
ATOM    558  CA  ILE A 175     -34.325-159.500 316.198  1.00108.82           C  
ANISOU  558  CA  ILE A 175    13961  11098  16286   1054  -1990    -12       C  
ATOM    559  C   ILE A 175     -34.735-160.582 317.188  1.00114.43           C  
ANISOU  559  C   ILE A 175    14737  11642  17099    964  -2178    337       C  
ATOM    560  O   ILE A 175     -34.022-161.576 317.372  1.00120.37           O  
ANISOU  560  O   ILE A 175    15495  12208  18032   1102  -2398    431       O  
ATOM    561  CB  ILE A 175     -33.599-158.334 316.891  1.00111.00           C  
ANISOU  561  CB  ILE A 175    14156  11733  16285   1016  -1842    -56       C  
ATOM    562  CG1 ILE A 175     -33.037-157.375 315.845  1.00108.80           C  
ANISOU  562  CG1 ILE A 175    13813  11580  15947   1110  -1686   -379       C  
ATOM    563  CG2 ILE A 175     -32.484-158.845 317.789  1.00114.39           C  
ANISOU  563  CG2 ILE A 175    14536  12237  16690   1103  -2009     79       C  
ATOM    564  CD1 ILE A 175     -32.331-156.196 316.439  1.00108.77           C  
ANISOU  564  CD1 ILE A 175    13731  11894  15702   1053  -1533   -451       C  
ATOM    565  N   ASP A 176     -35.890-160.414 317.838  1.00114.27           N  
ANISOU  565  N   ASP A 176    14756  11686  16974    733  -2098    546       N  
ATOM    566  CA  ASP A 176     -36.361-161.435 318.768  1.00115.38           C  
ANISOU  566  CA  ASP A 176    14955  11690  17194    606  -2271    914       C  
ATOM    567  C   ASP A 176     -36.694-162.729 318.036  1.00114.64           C  
ANISOU  567  C   ASP A 176    14943  11153  17461    672  -2468    939       C  
ATOM    568  O   ASP A 176     -36.426-163.824 318.544  1.00120.04           O  
ANISOU  568  O   ASP A 176    15672  11606  18332    697  -2697   1189       O  
ATOM    569  CB  ASP A 176     -37.577-160.923 319.539  1.00116.80           C  
ANISOU  569  CB  ASP A 176    15134  12081  17164    328  -2116   1094       C  
ATOM    570  CG  ASP A 176     -37.777-161.639 320.862  1.00120.38           C  
ANISOU  570  CG  ASP A 176    15604  12584  17553    157  -2254   1510       C  
ATOM    571  OD1 ASP A 176     -37.218-162.741 321.040  1.00128.09           O  
ANISOU  571  OD1 ASP A 176    16623  13314  18730    246  -2502   1706       O  
ATOM    572  OD2 ASP A 176     -38.497-161.098 321.727  1.00116.39           O  
ANISOU  572  OD2 ASP A 176    15058  12371  16795    -68  -2115   1645       O  
ATOM    573  N   PHE A 177     -37.269-162.625 316.835  1.00109.96           N  
ANISOU  573  N   PHE A 177    14367  10434  16980    699  -2391    681       N  
ATOM    574  CA  PHE A 177     -37.601-163.825 316.074  1.00112.86           C  
ANISOU  574  CA  PHE A 177    14802  10390  17690    749  -2567    639       C  
ATOM    575  C   PHE A 177     -36.350-164.483 315.501  1.00117.84           C  
ANISOU  575  C   PHE A 177    15412  10809  18552   1035  -2734    442       C  
ATOM    576  O   PHE A 177     -36.232-165.714 315.508  1.00121.41           O  
ANISOU  576  O   PHE A 177    15905  10966  19259   1077  -2918    527       O  
ATOM    577  CB  PHE A 177     -38.586-163.481 314.956  1.00109.33           C  
ANISOU  577  CB  PHE A 177    14353   9934  17255    681  -2433    406       C  
ATOM    578  CG  PHE A 177     -38.969-164.656 314.101  1.00114.04           C  
ANISOU  578  CG  PHE A 177    15004  10139  18186    708  -2597    302       C  
ATOM    579  CD1 PHE A 177     -40.029-165.473 314.457  1.00117.06           C  
ANISOU  579  CD1 PHE A 177    15453  10325  18700    494  -2680    540       C  
ATOM    580  CD2 PHE A 177     -38.272-164.940 312.938  1.00113.27           C  
ANISOU  580  CD2 PHE A 177    14850  10034  18153    899  -2596    -59       C  
ATOM    581  CE1 PHE A 177     -40.384-166.551 313.670  1.00117.77           C  
ANISOU  581  CE1 PHE A 177    15552  10223  18973    477  -2748    400       C  
ATOM    582  CE2 PHE A 177     -38.619-166.018 312.150  1.00113.13           C  
ANISOU  582  CE2 PHE A 177    14837   9835  18312    883  -2666   -199       C  
ATOM    583  CZ  PHE A 177     -39.677-166.824 312.515  1.00116.66           C  
ANISOU  583  CZ  PHE A 177    15355  10078  18895    677  -2744     22       C  
ATOM    584  N   HIS A 178     -35.409-163.684 314.999  1.00114.19           N  
ANISOU  584  N   HIS A 178    14861  10576  17951   1205  -2627    161       N  
ATOM    585  CA  HIS A 178     -34.224-164.227 314.341  1.00111.71           C  
ANISOU  585  CA  HIS A 178    14489  10137  17819   1477  -2747    -87       C  
ATOM    586  C   HIS A 178     -33.102-164.523 315.333  1.00111.76           C  
ANISOU  586  C   HIS A 178    14455  10160  17849   1614  -2905    106       C  
ATOM    587  O   HIS A 178     -32.652-165.665 315.445  1.00124.84           O  
ANISOU  587  O   HIS A 178    16110  11630  19693   1698  -3058    175       O  
ATOM    588  CB  HIS A 178     -33.740-163.265 313.250  1.00110.01           C  
ANISOU  588  CB  HIS A 178    14180  10161  17456   1590  -2575   -478       C  
ATOM    589  CG  HIS A 178     -34.539-163.338 311.984  1.00113.27           C  
ANISOU  589  CG  HIS A 178    14594  10568  17875   1516  -2469   -714       C  
ATOM    590  ND1 HIS A 178     -35.899-163.117 311.949  1.00116.38           N  
ANISOU  590  ND1 HIS A 178    15056  10911  18252   1316  -2403   -603       N  
ATOM    591  CD2 HIS A 178     -34.169-163.608 310.710  1.00114.86           C  
ANISOU  591  CD2 HIS A 178    14720  10828  18094   1615  -2434  -1051       C  
ATOM    592  CE1 HIS A 178     -36.333-163.250 310.708  1.00116.94           C  
ANISOU  592  CE1 HIS A 178    15094  11006  18331   1304  -2342   -855       C  
ATOM    593  NE2 HIS A 178     -35.303-163.548 309.936  1.00115.55           N  
ANISOU  593  NE2 HIS A 178    14833  10899  18172   1479  -2361  -1128       N  
ATOM    594  N   VAL A 179     -32.643-163.507 316.061  1.00104.68           N  
ANISOU  594  N   VAL A 179    13493   9650  16630   1559  -2775    178       N  
ATOM    595  CA  VAL A 179     -31.473-163.695 316.913  1.00106.02           C  
ANISOU  595  CA  VAL A 179    13587   9926  16768   1690  -2910    320       C  
ATOM    596  C   VAL A 179     -31.832-164.499 318.158  1.00104.49           C  
ANISOU  596  C   VAL A 179    13461   9602  16637   1570  -3094    793       C  
ATOM    597  O   VAL A 179     -31.037-165.321 318.632  1.00108.26           O  
ANISOU  597  O   VAL A 179    13908   9937  17289   1728  -3324    966       O  
ATOM    598  CB  VAL A 179     -30.851-162.334 317.271  1.00106.93           C  
ANISOU  598  CB  VAL A 179    13600  10515  16512   1647  -2710    215       C  
ATOM    599  CG1 VAL A 179     -29.538-162.526 318.012  1.00106.33           C  
ANISOU  599  CG1 VAL A 179    13416  10588  16399   1800  -2854    309       C  
ATOM    600  CG2 VAL A 179     -30.640-161.505 316.012  1.00104.48           C  
ANISOU  600  CG2 VAL A 179    13235  10325  16138   1719  -2519   -198       C  
ATOM    601  N   PHE A 180     -33.030-164.286 318.705  1.00101.79           N  
ANISOU  601  N   PHE A 180    13197   9320  16157   1288  -3002   1023       N  
ATOM    602  CA  PHE A 180     -33.444-164.961 319.929  1.00108.37           C  
ANISOU  602  CA  PHE A 180    14083  10103  16991   1120  -3154   1501       C  
ATOM    603  C   PHE A 180     -34.303-166.194 319.683  1.00114.96           C  
ANISOU  603  C   PHE A 180    15038  10461  18179   1054  -3325   1683       C  
ATOM    604  O   PHE A 180     -34.503-166.981 320.615  1.00116.24           O  
ANISOU  604  O   PHE A 180    15246  10500  18418    943  -3505   2113       O  
ATOM    605  CB  PHE A 180     -34.201-163.990 320.844  1.00105.68           C  
ANISOU  605  CB  PHE A 180    13727  10177  16251    825  -2948   1660       C  
ATOM    606  CG  PHE A 180     -33.334-162.913 321.429  1.00102.58           C  
ANISOU  606  CG  PHE A 180    13216  10245  15516    843  -2821   1565       C  
ATOM    607  CD1 PHE A 180     -33.159-161.709 320.767  1.00101.63           C  
ANISOU  607  CD1 PHE A 180    13041  10340  15234    879  -2579   1182       C  
ATOM    608  CD2 PHE A 180     -32.690-163.108 322.640  1.00 99.44           C  
ANISOU  608  CD2 PHE A 180    12755  10068  14959    811  -2951   1869       C  
ATOM    609  CE1 PHE A 180     -32.358-160.719 321.304  1.00100.54           C  
ANISOU  609  CE1 PHE A 180    12796  10601  14804    874  -2462   1079       C  
ATOM    610  CE2 PHE A 180     -31.889-162.122 323.182  1.00 98.89           C  
ANISOU  610  CE2 PHE A 180    12566  10440  14568    807  -2836   1754       C  
ATOM    611  CZ  PHE A 180     -31.722-160.926 322.514  1.00 99.67           C  
ANISOU  611  CZ  PHE A 180    12619  10722  14531    835  -2587   1346       C  
ATOM    612  N   HIS A 181     -34.807-166.381 318.460  1.00122.63           N  
ANISOU  612  N   HIS A 181    16055  11177  19360   1103  -3277   1375       N  
ATOM    613  CA  HIS A 181     -35.577-167.569 318.083  1.00130.53           C  
ANISOU  613  CA  HIS A 181    17131  11856  20607    999  -3345   1420       C  
ATOM    614  C   HIS A 181     -36.807-167.744 318.975  1.00132.45           C  
ANISOU  614  C   HIS A 181    17456  12071  20798    677  -3369   1843       C  
ATOM    615  O   HIS A 181     -37.019-168.795 319.583  1.00135.25           O  
ANISOU  615  O   HIS A 181    17853  12254  21282    570  -3511   2155       O  
ATOM    616  CB  HIS A 181     -34.703-168.828 318.111  1.00139.97           C  
ANISOU  616  CB  HIS A 181    18307  12832  22042   1169  -3519   1447       C  
ATOM    617  CG  HIS A 181     -33.250-168.567 317.862  1.00141.41           C  
ANISOU  617  CG  HIS A 181    18382  13137  22210   1467  -3542   1214       C  
ATOM    618  ND1 HIS A 181     -32.743-168.308 316.607  1.00137.70           N  
ANISOU  618  ND1 HIS A 181    17841  12716  21760   1646  -3430    728       N  
ATOM    619  CD2 HIS A 181     -32.193-168.530 318.708  1.00145.22           C  
ANISOU  619  CD2 HIS A 181    18796  13738  22641   1605  -3667   1409       C  
ATOM    620  CE1 HIS A 181     -31.437-168.121 316.691  1.00139.76           C  
ANISOU  620  CE1 HIS A 181    17997  13112  21993   1878  -3476    623       C  
ATOM    621  NE2 HIS A 181     -31.079-168.250 317.956  1.00144.04           N  
ANISOU  621  NE2 HIS A 181    18536  13693  22499   1868  -3623   1025       N  
ATOM    622  N   ARG A 182     -37.629-166.700 319.048  1.00132.82           N  
ANISOU  622  N   ARG A 182    17495  12383  20589    497  -3172   1820       N  
ATOM    623  CA  ARG A 182     -38.820-166.743 319.887  1.00133.69           C  
ANISOU  623  CA  ARG A 182    17636  12607  20554    163  -3124   2166       C  
ATOM    624  C   ARG A 182     -39.970-167.398 319.132  1.00132.87           C  
ANISOU  624  C   ARG A 182    17606  12178  20702     27  -3148   2116       C  
ATOM    625  O   ARG A 182     -40.278-167.018 317.997  1.00132.91           O  
ANISOU  625  O   ARG A 182    17595  12158  20748     96  -3029   1741       O  
ATOM    626  CB  ARG A 182     -39.217-165.338 320.340  1.00132.44           C  
ANISOU  626  CB  ARG A 182    17390  12978  19952     21  -2839   2097       C  
ATOM    627  CG  ARG A 182     -39.624-165.268 321.806  1.00137.02           C  
ANISOU  627  CG  ARG A 182    17942  13860  20260   -244  -2827   2515       C  
ATOM    628  CD  ARG A 182     -40.427-164.016 322.122  1.00136.41           C  
ANISOU  628  CD  ARG A 182    17780  14231  19817   -428  -2531   2405       C  
ATOM    629  NE  ARG A 182     -40.574-163.821 323.562  1.00140.45           N  
ANISOU  629  NE  ARG A 182    18230  15123  20011   -653  -2500   2733       N  
ATOM    630  CZ  ARG A 182     -41.429-162.971 324.121  1.00141.91           C  
ANISOU  630  CZ  ARG A 182    18331  15701  19889   -869  -2271   2721       C  
ATOM    631  NH1 ARG A 182     -42.231-162.236 323.362  1.00140.41           N  
ANISOU  631  NH1 ARG A 182    18113  15542  19695   -876  -2063   2424       N  
ATOM    632  NH2 ARG A 182     -41.488-162.860 325.442  1.00142.78           N  
ANISOU  632  NH2 ARG A 182    18369  16188  19692  -1077  -2254   3003       N  
ATOM    633  N   LYS A 183     -40.605-168.381 319.766  1.00132.35           N  
ANISOU  633  N   LYS A 183    17594  11947  20748   -187  -3275   2477       N  
ATOM    634  CA  LYS A 183     -41.747-169.089 319.199  1.00134.35           C  
ANISOU  634  CA  LYS A 183    17879  12016  21153   -366  -3255   2422       C  
ATOM    635  C   LYS A 183     -43.007-168.604 319.907  1.00130.21           C  
ANISOU  635  C   LYS A 183    17352  11685  20437   -718  -3163   2726       C  
ATOM    636  O   LYS A 183     -43.255-168.966 321.062  1.00133.68           O  
ANISOU  636  O   LYS A 183    17801  12208  20782   -935  -3238   3173       O  
ATOM    637  CB  LYS A 183     -41.581-170.600 319.341  1.00142.74           C  
ANISOU  637  CB  LYS A 183    18983  12771  22480   -365  -3439   2570       C  
ATOM    638  N   ASP A 184     -43.794-167.789 319.218  1.00126.27           N  
ANISOU  638  N   ASP A 184    16802  11361  19815   -775  -2961   2453       N  
ATOM    639  CA  ASP A 184     -45.032-167.254 319.761  1.00131.38           C  
ANISOU  639  CA  ASP A 184    17378  12351  20191  -1075  -2781   2604       C  
ATOM    640  C   ASP A 184     -46.230-168.035 319.232  1.00132.52           C  
ANISOU  640  C   ASP A 184    17554  12235  20563  -1294  -2838   2640       C  
ATOM    641  O   ASP A 184     -46.170-168.681 318.183  1.00133.17           O  
ANISOU  641  O   ASP A 184    17681  11991  20925  -1175  -2928   2386       O  
ATOM    642  CB  ASP A 184     -45.179-165.770 319.414  1.00132.82           C  
ANISOU  642  CB  ASP A 184    17449  12953  20064   -991  -2496   2280       C  
ATOM    643  CG  ASP A 184     -44.088-164.914 320.031  1.00135.67           C  
ANISOU  643  CG  ASP A 184    17765  13608  20174   -829  -2417   2242       C  
ATOM    644  OD1 ASP A 184     -43.716-165.169 321.196  1.00139.18           O  
ANISOU  644  OD1 ASP A 184    18211  14173  20496   -923  -2496   2566       O  
ATOM    645  OD2 ASP A 184     -43.601-163.986 319.350  1.00132.23           O  
ANISOU  645  OD2 ASP A 184    17287  13298  19658   -626  -2280   1896       O  
ATOM    646  N   SER A 185     -47.327-167.970 319.984  1.00130.29           N  
ANISOU  646  N   SER A 185    17214  12193  20097  -1618  -2751   2912       N  
ATOM    647  CA  SER A 185     -48.577-168.557 319.530  1.00128.00           C  
ANISOU  647  CA  SER A 185    16919  11748  19967  -1865  -2770   2939       C  
ATOM    648  C   SER A 185     -49.062-167.844 318.271  1.00118.58           C  
ANISOU  648  C   SER A 185    15652  10647  18756  -1748  -2611   2487       C  
ATOM    649  O   SER A 185     -48.595-166.757 317.921  1.00116.87           O  
ANISOU  649  O   SER A 185    15375  10681  18350  -1526  -2452   2212       O  
ATOM    650  CB  SER A 185     -49.637-168.476 320.628  1.00132.79           C  
ANISOU  650  CB  SER A 185    17440  12695  20319  -2235  -2675   3303       C  
ATOM    651  OG  SER A 185     -49.196-169.122 321.809  1.00142.04           O  
ANISOU  651  OG  SER A 185    18668  13830  21470  -2365  -2827   3761       O  
ATOM    652  N   ARG A 186     -50.016-168.475 317.583  1.00117.88           N  
ANISOU  652  N   ARG A 186    15562  10357  18869  -1916  -2665   2425       N  
ATOM    653  CA  ARG A 186     -50.503-167.923 316.322  1.00118.00           C  
ANISOU  653  CA  ARG A 186    15498  10458  18879  -1819  -2549   2020       C  
ATOM    654  C   ARG A 186     -51.090-166.530 316.517  1.00116.67           C  
ANISOU  654  C   ARG A 186    15171  10817  18341  -1826  -2277   1946       C  
ATOM    655  O   ARG A 186     -50.721-165.584 315.812  1.00116.10           O  
ANISOU  655  O   ARG A 186    15048  10903  18162  -1587  -2153   1643       O  
ATOM    656  CB  ARG A 186     -51.540-168.855 315.698  1.00121.37           C  
ANISOU  656  CB  ARG A 186    15927  10636  19552  -2055  -2653   1999       C  
ATOM    657  CG  ARG A 186     -52.422-168.162 314.673  1.00118.96           C  
ANISOU  657  CG  ARG A 186    15482  10583  19134  -2055  -2501   1687       C  
ATOM    658  CD  ARG A 186     -53.080-169.153 313.739  1.00124.30           C  
ANISOU  658  CD  ARG A 186    16173  10963  20092  -2200  -2638   1533       C  
ATOM    659  NE  ARG A 186     -53.813-170.190 314.459  1.00132.19           N  
ANISOU  659  NE  ARG A 186    17198  11874  21155  -2496  -2706   1838       N  
ATOM    660  CZ  ARG A 186     -55.092-170.097 314.805  1.00136.54           C  
ANISOU  660  CZ  ARG A 186    17633  12635  21612  -2829  -2637   2020       C  
ATOM    661  NH1 ARG A 186     -55.786-169.009 314.501  1.00134.34           N  
ANISOU  661  NH1 ARG A 186    17184  12745  21114  -2844  -2462   1897       N  
ATOM    662  NH2 ARG A 186     -55.679-171.093 315.456  1.00143.45           N  
ANISOU  662  NH2 ARG A 186    18537  13428  22539  -3092  -2700   2296       N  
ATOM    663  N   ASN A 187     -52.008-166.386 317.475  1.00113.46           N  
ANISOU  663  N   ASN A 187    14676  10689  17745  -2101  -2180   2220       N  
ATOM    664  CA  ASN A 187     -52.653-165.094 317.683  1.00104.69           C  
ANISOU  664  CA  ASN A 187    13394  10062  16320  -2104  -1920   2127       C  
ATOM    665  C   ASN A 187     -51.666-164.057 318.205  1.00100.46           C  
ANISOU  665  C   ASN A 187    12852   9753  15563  -1881  -1793   2056       C  
ATOM    666  O   ASN A 187     -51.738-162.881 317.828  1.00100.39           O  
ANISOU  666  O   ASN A 187    12745   9992  15406  -1724  -1605   1814       O  
ATOM    667  CB  ASN A 187     -53.835-165.247 318.639  1.00102.32           C  
ANISOU  667  CB  ASN A 187    12980  10029  15867  -2457  -1845   2420       C  
ATOM    668  CG  ASN A 187     -54.942-166.114 318.066  1.00 98.01           C  
ANISOU  668  CG  ASN A 187    12405   9319  15516  -2703  -1937   2457       C  
ATOM    669  OD1 ASN A 187     -55.179-166.120 316.857  1.00 93.68           O  
ANISOU  669  OD1 ASN A 187    11841   8638  15116  -2599  -1961   2177       O  
ATOM    670  ND2 ASN A 187     -55.626-166.850 318.932  1.00 98.92           N  
ANISOU  670  ND2 ASN A 187    12501   9468  15618  -3051  -1990   2808       N  
ATOM    671  N   VAL A 188     -50.734-164.472 319.068  1.00 97.54           N  
ANISOU  671  N   VAL A 188    12582   9300  15180  -1868  -1903   2269       N  
ATOM    672  CA  VAL A 188     -49.739-163.537 319.584  1.00 93.67           C  
ANISOU  672  CA  VAL A 188    12079   9033  14477  -1676  -1796   2191       C  
ATOM    673  C   VAL A 188     -48.779-163.106 318.482  1.00 90.69           C  
ANISOU  673  C   VAL A 188    11754   8491  14214  -1343  -1805   1844       C  
ATOM    674  O   VAL A 188     -48.312-161.960 318.469  1.00 82.96           O  
ANISOU  674  O   VAL A 188    10718   7745  13059  -1179  -1641   1652       O  
ATOM    675  CB  VAL A 188     -48.987-164.159 320.775  1.00 96.65           C  
ANISOU  675  CB  VAL A 188    12530   9391  14800  -1757  -1935   2530       C  
ATOM    676  CG1 VAL A 188     -47.982-163.168 321.350  1.00 98.75           C  
ANISOU  676  CG1 VAL A 188    12762   9937  14820  -1585  -1820   2432       C  
ATOM    677  CG2 VAL A 188     -49.972-164.605 321.841  1.00 94.31           C  
ANISOU  677  CG2 VAL A 188    12170   9297  14365  -2122  -1925   2900       C  
ATOM    678  N   PHE A 189     -48.467-164.002 317.544  1.00 96.80           N  
ANISOU  678  N   PHE A 189    12627   8871  15284  -1249  -1990   1745       N  
ATOM    679  CA  PHE A 189     -47.624-163.617 316.417  1.00 97.16           C  
ANISOU  679  CA  PHE A 189    12695   8806  15413   -954  -1989   1398       C  
ATOM    680  C   PHE A 189     -48.404-162.776 315.415  1.00 93.87           C  
ANISOU  680  C   PHE A 189    12173   8563  14930   -918  -1827   1140       C  
ATOM    681  O   PHE A 189     -47.928-161.725 314.970  1.00 89.34           O  
ANISOU  681  O   PHE A 189    11553   8158  14234   -728  -1693    926       O  
ATOM    682  CB  PHE A 189     -47.043-164.858 315.742  1.00 99.90           C  
ANISOU  682  CB  PHE A 189    13159   8702  16096   -862  -2233   1335       C  
ATOM    683  CG  PHE A 189     -46.249-164.554 314.505  1.00 95.13           C  
ANISOU  683  CG  PHE A 189    12556   8021  15568   -584  -2231    954       C  
ATOM    684  CD1 PHE A 189     -44.933-164.128 314.596  1.00 91.51           C  
ANISOU  684  CD1 PHE A 189    12114   7609  15047   -348  -2226    852       C  
ATOM    685  CD2 PHE A 189     -46.820-164.689 313.249  1.00 91.26           C  
ANISOU  685  CD2 PHE A 189    12032   7456  15187   -575  -2233    697       C  
ATOM    686  CE1 PHE A 189     -44.201-163.844 313.457  1.00 86.96           C  
ANISOU  686  CE1 PHE A 189    11519   7003  14517   -114  -2215    507       C  
ATOM    687  CE2 PHE A 189     -46.097-164.407 312.108  1.00 85.59           C  
ANISOU  687  CE2 PHE A 189    11296   6723  14500   -341  -2227    354       C  
ATOM    688  CZ  PHE A 189     -44.785-163.984 312.210  1.00 83.60           C  
ANISOU  688  CZ  PHE A 189    11060   6517  14185   -113  -2214    261       C  
ATOM    689  N   LEU A 190     -49.612-163.224 315.048  1.00 94.84           N  
ANISOU  689  N   LEU A 190    12249   8651  15134  -1108  -1845   1175       N  
ATOM    690  CA  LEU A 190     -50.445-162.441 314.139  1.00 97.40           C  
ANISOU  690  CA  LEU A 190    12449   9173  15386  -1082  -1706    972       C  
ATOM    691  C   LEU A 190     -50.800-161.085 314.734  1.00101.17           C  
ANISOU  691  C   LEU A 190    12803  10035  15604  -1068  -1466    989       C  
ATOM    692  O   LEU A 190     -51.083-160.138 313.992  1.00 95.13           O  
ANISOU  692  O   LEU A 190    11942   9431  14774   -947  -1337    804       O  
ATOM    693  CB  LEU A 190     -51.709-163.220 313.781  1.00 98.22           C  
ANISOU  693  CB  LEU A 190    12504   9203  15611  -1320  -1777   1031       C  
ATOM    694  CG  LEU A 190     -51.513-164.397 312.825  1.00 98.12           C  
ANISOU  694  CG  LEU A 190    12583   8815  15883  -1316  -1989    891       C  
ATOM    695  CD1 LEU A 190     -52.830-165.116 312.600  1.00102.99           C  
ANISOU  695  CD1 LEU A 190    13138   9390  16603  -1597  -2046    960       C  
ATOM    696  CD2 LEU A 190     -50.924-163.924 311.503  1.00 91.35           C  
ANISOU  696  CD2 LEU A 190    11707   7969  15034  -1061  -1973    539       C  
ATOM    697  N   PHE A 191     -50.796-160.972 316.064  1.00108.37           N  
ANISOU  697  N   PHE A 191    13704  11100  16370  -1192  -1407   1208       N  
ATOM    698  CA  PHE A 191     -50.913-159.662 316.693  1.00110.45           C  
ANISOU  698  CA  PHE A 191    13856  11711  16401  -1150  -1176   1166       C  
ATOM    699  C   PHE A 191     -49.700-158.801 316.362  1.00104.27           C  
ANISOU  699  C   PHE A 191    13117  10926  15575   -884  -1117    961       C  
ATOM    700  O   PHE A 191     -49.837-157.645 315.944  1.00106.83           O  
ANISOU  700  O   PHE A 191    13353  11406  15830   -758   -951    786       O  
ATOM    701  CB  PHE A 191     -51.069-159.819 318.206  1.00118.74           C  
ANISOU  701  CB  PHE A 191    14881  12957  17279  -1358  -1137   1422       C  
ATOM    702  CG  PHE A 191     -51.455-158.551 318.915  1.00125.46           C  
ANISOU  702  CG  PHE A 191    15582  14192  17895  -1364   -886   1349       C  
ATOM    703  CD1 PHE A 191     -50.489-157.647 319.330  1.00127.52           C  
ANISOU  703  CD1 PHE A 191    15854  14570  18028  -1209   -781   1223       C  
ATOM    704  CD2 PHE A 191     -52.787-158.267 319.173  1.00127.33           C  
ANISOU  704  CD2 PHE A 191    15653  14676  18052  -1527   -752   1383       C  
ATOM    705  CE1 PHE A 191     -50.844-156.481 319.982  1.00127.05           C  
ANISOU  705  CE1 PHE A 191    15654  14836  17783  -1216   -547   1113       C  
ATOM    706  CE2 PHE A 191     -53.148-157.104 319.827  1.00128.52           C  
ANISOU  706  CE2 PHE A 191    15650  15166  18015  -1514   -516   1275       C  
ATOM    707  CZ  PHE A 191     -52.175-156.209 320.232  1.00128.98           C  
ANISOU  707  CZ  PHE A 191    15732  15308  17966  -1358   -413   1131       C  
ATOM    708  N   LYS A 192     -48.499-159.356 316.540  1.00 92.78           N  
ANISOU  708  N   LYS A 192    11787   9289  14176   -796  -1257    989       N  
ATOM    709  CA  LYS A 192     -47.283-158.612 316.229  1.00 83.84           C  
ANISOU  709  CA  LYS A 192    10687   8168  13001   -562  -1210    796       C  
ATOM    710  C   LYS A 192     -47.161-158.365 314.730  1.00 83.21           C  
ANISOU  710  C   LYS A 192    10602   7977  13035   -389  -1219    551       C  
ATOM    711  O   LYS A 192     -46.881-157.240 314.297  1.00 81.13           O  
ANISOU  711  O   LYS A 192    10287   7847  12693   -252  -1076    387       O  
ATOM    712  CB  LYS A 192     -46.060-159.360 316.758  1.00 78.14           C  
ANISOU  712  CB  LYS A 192    10075   7293  12320   -507  -1376    893       C  
ATOM    713  CG  LYS A 192     -46.066-159.550 318.265  1.00 85.75           C  
ANISOU  713  CG  LYS A 192    11032   8422  13128   -680  -1376   1162       C  
ATOM    714  CD  LYS A 192     -44.841-160.316 318.738  1.00 91.82           C  
ANISOU  714  CD  LYS A 192    11897   9039  13953   -606  -1567   1287       C  
ATOM    715  CE  LYS A 192     -44.896-160.560 320.239  1.00 96.33           C  
ANISOU  715  CE  LYS A 192    12448   9813  14339   -804  -1586   1601       C  
ATOM    716  NZ  LYS A 192     -43.731-161.351 320.720  1.00102.59           N  
ANISOU  716  NZ  LYS A 192    13320  10461  15197   -726  -1798   1772       N  
ATOM    717  N   LEU A 193     -47.374-159.409 313.921  1.00 82.29           N  
ANISOU  717  N   LEU A 193    10534   7626  13106   -406  -1387    524       N  
ATOM    718  CA  LEU A 193     -47.301-159.245 312.473  1.00 82.29           C  
ANISOU  718  CA  LEU A 193    10512   7575  13181   -267  -1402    283       C  
ATOM    719  C   LEU A 193     -48.350-158.258 311.981  1.00 81.88           C  
ANISOU  719  C   LEU A 193    10327   7747  13035   -290  -1239    237       C  
ATOM    720  O   LEU A 193     -48.091-157.474 311.060  1.00 72.92           O  
ANISOU  720  O   LEU A 193     9146   6699  11863   -143  -1169     73       O  
ATOM    721  CB  LEU A 193     -47.465-160.599 311.778  1.00 85.28           C  
ANISOU  721  CB  LEU A 193    10949   7676  13777   -316  -1608    237       C  
ATOM    722  CG  LEU A 193     -47.094-160.683 310.291  1.00 81.69           C  
ANISOU  722  CG  LEU A 193    10478   7163  13396   -167  -1663    -52       C  
ATOM    723  CD1 LEU A 193     -48.239-160.241 309.382  1.00 75.84           C  
ANISOU  723  CD1 LEU A 193     9619   6597  12601   -232  -1590   -126       C  
ATOM    724  CD2 LEU A 193     -45.842-159.861 310.009  1.00 78.88           C  
ANISOU  724  CD2 LEU A 193    10125   6909  12937     54  -1590   -205       C  
ATOM    725  N   GLY A 194     -49.542-158.283 312.578  1.00 89.24           N  
ANISOU  725  N   GLY A 194    11184   8790  13933   -473  -1181    393       N  
ATOM    726  CA  GLY A 194     -50.551-157.301 312.220  1.00 95.15           C  
ANISOU  726  CA  GLY A 194    11783   9762  14608   -473  -1025    360       C  
ATOM    727  C   GLY A 194     -50.127-155.886 312.563  1.00 96.48           C  
ANISOU  727  C   GLY A 194    11904  10099  14655   -335   -832    301       C  
ATOM    728  O   GLY A 194     -50.434-154.941 311.833  1.00 97.53           O  
ANISOU  728  O   GLY A 194    11945  10337  14777   -225   -732    212       O  
ATOM    729  N   GLY A 195     -49.403-155.724 313.672  1.00 94.44           N  
ANISOU  729  N   GLY A 195    11703   9867  14313   -345   -786    353       N  
ATOM    730  CA  GLY A 195     -48.974-154.393 314.073  1.00 94.21           C  
ANISOU  730  CA  GLY A 195    11629   9983  14182   -238   -599    267       C  
ATOM    731  C   GLY A 195     -48.002-153.773 313.089  1.00 95.09           C  
ANISOU  731  C   GLY A 195    11780  10028  14323    -39   -593    104       C  
ATOM    732  O   GLY A 195     -48.164-152.621 312.677  1.00 98.92           O  
ANISOU  732  O   GLY A 195    12189  10596  14801     58   -454     27       O  
ATOM    733  N   VAL A 196     -46.979-154.531 312.692  1.00 96.73           N  
ANISOU  733  N   VAL A 196    12096  10083  14574     22   -745     56       N  
ATOM    734  CA  VAL A 196     -45.994-154.002 311.755  1.00 99.47           C  
ANISOU  734  CA  VAL A 196    12464  10406  14923    192   -738   -103       C  
ATOM    735  C   VAL A 196     -46.611-153.815 310.373  1.00 97.62           C  
ANISOU  735  C   VAL A 196    12161  10194  14737    243   -751   -167       C  
ATOM    736  O   VAL A 196     -46.345-152.817 309.692  1.00 99.43           O  
ANISOU  736  O   VAL A 196    12344  10501  14934    349   -658   -236       O  
ATOM    737  CB  VAL A 196     -44.752-154.913 311.707  1.00104.11           C  
ANISOU  737  CB  VAL A 196    13157  10853  15547    255   -898   -161       C  
ATOM    738  CG1 VAL A 196     -43.946-154.772 312.985  1.00109.50           C  
ANISOU  738  CG1 VAL A 196    13881  11578  16144    237   -867   -103       C  
ATOM    739  CG2 VAL A 196     -45.154-156.362 311.498  1.00102.33           C  
ANISOU  739  CG2 VAL A 196    12981  10448  15451    179  -1090   -109       C  
ATOM    740  N   THR A 197     -47.453-154.758 309.942  1.00 96.66           N  
ANISOU  740  N   THR A 197    12023  10016  14687    154   -869   -132       N  
ATOM    741  CA  THR A 197     -48.048-154.674 308.611  1.00 89.91           C  
ANISOU  741  CA  THR A 197    11086   9225  13852    184   -901   -197       C  
ATOM    742  C   THR A 197     -48.904-153.421 308.469  1.00 95.86           C  
ANISOU  742  C   THR A 197    11710  10150  14565    213   -742   -129       C  
ATOM    743  O   THR A 197     -48.808-152.699 307.470  1.00 94.02           O  
ANISOU  743  O   THR A 197    11416  10004  14304    315   -709   -171       O  
ATOM    744  CB  THR A 197     -48.877-155.927 308.327  1.00 81.46           C  
ANISOU  744  CB  THR A 197    10010   8071  12870     48  -1052   -181       C  
ATOM    745  OG1 THR A 197     -48.031-157.084 308.382  1.00 82.86           O  
ANISOU  745  OG1 THR A 197    10308   8039  13136     48  -1210   -257       O  
ATOM    746  CG2 THR A 197     -49.518-155.842 306.953  1.00 47.25           C  
ANISOU  746  CG2 THR A 197     5571   3856   8526     63  -1089   -263       C  
ATOM    747  N   ALA A 198     -49.747-153.143 309.468  1.00 95.70           N  
ANISOU  747  N   ALA A 198    11631  10185  14543    127   -643    -18       N  
ATOM    748  CA  ALA A 198     -50.584-151.948 309.421  1.00 94.82           C  
ANISOU  748  CA  ALA A 198    11380  10213  14433    179   -489     30       C  
ATOM    749  C   ALA A 198     -49.737-150.683 309.376  1.00 91.83           C  
ANISOU  749  C   ALA A 198    11016   9832  14041    325   -359    -25       C  
ATOM    750  O   ALA A 198     -50.026-149.760 308.603  1.00 83.44           O  
ANISOU  750  O   ALA A 198     9866   8826  13012    427   -299     -4       O  
ATOM    751  CB  ALA A 198     -51.524-151.917 310.626  1.00 95.94           C  
ANISOU  751  CB  ALA A 198    11446  10436  14569     59   -394    117       C  
ATOM    752  N   SER A 199     -48.682-150.625 310.195  1.00 89.46           N  
ANISOU  752  N   SER A 199    10822   9469  13699    329   -323    -81       N  
ATOM    753  CA  SER A 199     -47.827-149.442 310.229  1.00 85.41           C  
ANISOU  753  CA  SER A 199    10326   8947  13180    436   -197   -149       C  
ATOM    754  C   SER A 199     -47.168-149.201 308.878  1.00 87.62           C  
ANISOU  754  C   SER A 199    10620   9216  13457    538   -256   -187       C  
ATOM    755  O   SER A 199     -47.186-148.080 308.356  1.00 91.68           O  
ANISOU  755  O   SER A 199    11076   9750  14008    621   -161   -163       O  
ATOM    756  CB  SER A 199     -46.773-149.592 311.325  1.00 82.24           C  
ANISOU  756  CB  SER A 199    10023   8515  12708    399   -175   -211       C  
ATOM    757  OG  SER A 199     -47.378-149.706 312.601  1.00 87.30           O  
ANISOU  757  OG  SER A 199    10632   9224  13313    288   -106   -168       O  
ATOM    758  N   PHE A 200     -46.580-150.247 308.293  1.00 87.44           N  
ANISOU  758  N   PHE A 200    10665   9164  13395    528   -413   -245       N  
ATOM    759  CA  PHE A 200     -45.964-150.097 306.980  1.00 94.33           C  
ANISOU  759  CA  PHE A 200    11528  10086  14228    607   -467   -304       C  
ATOM    760  C   PHE A 200     -47.008-149.867 305.895  1.00 94.11           C  
ANISOU  760  C   PHE A 200    11380  10168  14208    617   -492   -222       C  
ATOM    761  O   PHE A 200     -46.741-149.147 304.925  1.00 87.83           O  
ANISOU  761  O   PHE A 200    10535   9463  13373    682   -470   -197       O  
ATOM    762  CB  PHE A 200     -45.108-151.322 306.656  1.00 99.95           C  
ANISOU  762  CB  PHE A 200    12318  10749  14909    604   -624   -434       C  
ATOM    763  CG  PHE A 200     -43.785-151.344 307.374  1.00108.37           C  
ANISOU  763  CG  PHE A 200    13473  11755  15947    640   -610   -516       C  
ATOM    764  CD1 PHE A 200     -43.719-151.616 308.732  1.00110.68           C  
ANISOU  764  CD1 PHE A 200    13824  11972  16257    583   -593   -471       C  
ATOM    765  CD2 PHE A 200     -42.606-151.096 306.689  1.00112.23           C  
ANISOU  765  CD2 PHE A 200    13968  12302  16371    718   -615   -632       C  
ATOM    766  CE1 PHE A 200     -42.506-151.638 309.395  1.00110.72           C  
ANISOU  766  CE1 PHE A 200    13891  11957  16220    614   -593   -536       C  
ATOM    767  CE2 PHE A 200     -41.388-151.117 307.346  1.00114.02           C  
ANISOU  767  CE2 PHE A 200    14252  12500  16568    750   -607   -711       C  
ATOM    768  CZ  PHE A 200     -41.338-151.389 308.701  1.00113.54           C  
ANISOU  768  CZ  PHE A 200    14249  12361  16530    703   -601   -661       C  
ATOM    769  N   THR A 201     -48.196-150.457 306.040  1.00 97.22           N  
ANISOU  769  N   THR A 201    11716  10579  14643    540   -542   -163       N  
ATOM    770  CA  THR A 201     -49.270-150.186 305.090  1.00102.83           C  
ANISOU  770  CA  THR A 201    12286  11428  15355    547   -566    -73       C  
ATOM    771  C   THR A 201     -49.740-148.742 305.204  1.00104.89           C  
ANISOU  771  C   THR A 201    12452  11722  15679    636   -415     58       C  
ATOM    772  O   THR A 201     -49.915-148.054 304.191  1.00111.33           O  
ANISOU  772  O   THR A 201    13179  12641  16482    707   -418    148       O  
ATOM    773  CB  THR A 201     -50.434-151.152 305.314  1.00102.34           C  
ANISOU  773  CB  THR A 201    12171  11386  15328    426   -650    -47       C  
ATOM    774  OG1 THR A 201     -49.963-152.501 305.205  1.00 99.15           O  
ANISOU  774  OG1 THR A 201    11865  10893  14914    346   -798   -172       O  
ATOM    775  CG2 THR A 201     -51.528-150.918 304.283  1.00100.91           C  
ANISOU  775  CG2 THR A 201    11821  11388  15130    429   -691     38       C  
ATOM    776  N   ALA A 202     -49.947-148.263 306.433  1.00 99.49           N  
ANISOU  776  N   ALA A 202    11777  10955  15069    633   -285     69       N  
ATOM    777  CA  ALA A 202     -50.323-146.866 306.621  1.00 95.93           C  
ANISOU  777  CA  ALA A 202    11238  10488  14725    733   -131    149       C  
ATOM    778  C   ALA A 202     -49.223-145.927 306.147  1.00 93.25           C  
ANISOU  778  C   ALA A 202    10956  10085  14391    819    -76    147       C  
ATOM    779  O   ALA A 202     -49.513-144.831 305.652  1.00 96.01           O  
ANISOU  779  O   ALA A 202    11222  10423  14836    913    -11    263       O  
ATOM    780  CB  ALA A 202     -50.655-146.599 308.089  1.00 93.56           C  
ANISOU  780  CB  ALA A 202    10931  10134  14485    700      7     98       C  
ATOM    781  N   SER A 203     -47.960-146.338 306.288  1.00 87.15           N  
ANISOU  781  N   SER A 203    10316   9269  13528    785   -106     30       N  
ATOM    782  CA  SER A 203     -46.851-145.534 305.785  1.00 83.91           C  
ANISOU  782  CA  SER A 203     9951   8831  13099    835    -60     22       C  
ATOM    783  C   SER A 203     -46.944-145.359 304.276  1.00 92.73           C  
ANISOU  783  C   SER A 203    10994  10081  14160    872   -144    139       C  
ATOM    784  O   SER A 203     -46.864-144.238 303.761  1.00102.60           O  
ANISOU  784  O   SER A 203    12196  11317  15469    929    -78    269       O  
ATOM    785  CB  SER A 203     -45.520-146.181 306.168  1.00 76.12           C  
ANISOU  785  CB  SER A 203     9091   7821  12010    791    -98   -136       C  
ATOM    786  OG  SER A 203     -44.451-145.612 305.431  1.00 74.15           O  
ANISOU  786  OG  SER A 203     8862   7606  11706    819    -83   -148       O  
ATOM    787  N   VAL A 204     -47.113-146.463 303.545  1.00 97.19           N  
ANISOU  787  N   VAL A 204    11542  10779  14607    828   -294     95       N  
ATOM    788  CA  VAL A 204     -47.244-146.366 302.099  1.00 99.52           C  
ANISOU  788  CA  VAL A 204    11744  11267  14801    841   -380    188       C  
ATOM    789  C   VAL A 204     -48.603-145.797 301.709  1.00 99.51           C  
ANISOU  789  C   VAL A 204    11593  11337  14879    883   -379    394       C  
ATOM    790  O   VAL A 204     -48.756-145.259 300.605  1.00 86.65           O  
ANISOU  790  O   VAL A 204     9867   9864  13193    913   -418    553       O  
ATOM    791  CB  VAL A 204     -46.989-147.741 301.451  1.00102.86           C  
ANISOU  791  CB  VAL A 204    12182  11820  15080    776   -536     22       C  
ATOM    792  CG1 VAL A 204     -48.225-148.625 301.539  1.00106.95           C  
ANISOU  792  CG1 VAL A 204    12640  12365  15630    718   -626     17       C  
ATOM    793  CG2 VAL A 204     -46.524-147.573 300.017  1.00102.68           C  
ANISOU  793  CG2 VAL A 204    12087  12038  14890    776   -598     43       C  
ATOM    794  N   GLY A 205     -49.597-145.893 302.596  1.00109.95           N  
ANISOU  794  N   GLY A 205    12877  12575  16323    884   -337    406       N  
ATOM    795  CA  GLY A 205     -50.842-145.181 302.374  1.00112.73           C  
ANISOU  795  CA  GLY A 205    13068  12978  16787    954   -312    595       C  
ATOM    796  C   GLY A 205     -50.682-143.682 302.513  1.00113.87           C  
ANISOU  796  C   GLY A 205    13189  12981  17096   1070   -178    734       C  
ATOM    797  O   GLY A 205     -51.370-142.914 301.834  1.00118.54           O  
ANISOU  797  O   GLY A 205    13643  13628  17767   1158   -191    947       O  
ATOM    798  N   SER A 206     -49.778-143.244 303.393  1.00104.23           N  
ANISOU  798  N   SER A 206    12093  11568  15940   1071    -56    618       N  
ATOM    799  CA  SER A 206     -49.446-141.826 303.470  1.00 99.34           C  
ANISOU  799  CA  SER A 206    11473  10779  15494   1158     69    719       C  
ATOM    800  C   SER A 206     -48.776-141.358 302.186  1.00 96.90           C  
ANISOU  800  C   SER A 206    11159  10557  15102   1161      6    888       C  
ATOM    801  O   SER A 206     -49.112-140.294 301.652  1.00103.49           O  
ANISOU  801  O   SER A 206    11908  11337  16077   1245     30   1117       O  
ATOM    802  CB  SER A 206     -48.550-141.561 304.681  1.00 94.37           C  
ANISOU  802  CB  SER A 206    10975   9964  14919   1123    204    520       C  
ATOM    803  OG  SER A 206     -49.178-141.961 305.886  1.00 92.06           O  
ANISOU  803  OG  SER A 206    10670   9639  14671   1102    267    380       O  
ATOM    804  N   LEU A 207     -47.830-142.146 301.668  1.00 84.95           N  
ANISOU  804  N   LEU A 207     9724   9190  13364   1069    -78    785       N  
ATOM    805  CA  LEU A 207     -47.223-141.811 300.385  1.00 85.00           C  
ANISOU  805  CA  LEU A 207     9700   9362  13236   1045   -141    935       C  
ATOM    806  C   LEU A 207     -48.254-141.830 299.266  1.00 89.35           C  
ANISOU  806  C   LEU A 207    10086  10138  13724   1075   -260   1161       C  
ATOM    807  O   LEU A 207     -48.124-141.087 298.285  1.00 84.03           O  
ANISOU  807  O   LEU A 207     9341   9573  13014   1085   -289   1405       O  
ATOM    808  CB  LEU A 207     -46.081-142.775 300.070  1.00 86.93           C  
ANISOU  808  CB  LEU A 207    10029   9759  13242    951   -206    726       C  
ATOM    809  CG  LEU A 207     -44.978-142.895 301.123  1.00 92.66           C  
ANISOU  809  CG  LEU A 207    10899  10316  13993    919   -117    502       C  
ATOM    810  CD1 LEU A 207     -43.922-143.901 300.684  1.00 94.68           C  
ANISOU  810  CD1 LEU A 207    11202  10743  14029    856   -202    303       C  
ATOM    811  CD2 LEU A 207     -44.349-141.540 301.402  1.00 97.89           C  
ANISOU  811  CD2 LEU A 207    11597  10802  14794    927     22    597       C  
ATOM    812  N   PHE A 208     -49.284-142.670 299.393  1.00 99.24           N  
ANISOU  812  N   PHE A 208    11267  11484  14955   1074   -336   1100       N  
ATOM    813  CA  PHE A 208     -50.363-142.663 298.412  1.00101.52           C  
ANISOU  813  CA  PHE A 208    11374  12007  15190   1101   -451   1309       C  
ATOM    814  C   PHE A 208     -51.168-141.374 298.493  1.00103.67           C  
ANISOU  814  C   PHE A 208    11534  12143  15712   1240   -388   1589       C  
ATOM    815  O   PHE A 208     -51.537-140.801 297.462  1.00107.15           O  
ANISOU  815  O   PHE A 208    11843  12746  16125   1282   -465   1875       O  
ATOM    816  CB  PHE A 208     -51.266-143.879 298.615  1.00 97.60           C  
ANISOU  816  CB  PHE A 208    10825  11630  14630   1045   -540   1156       C  
ATOM    817  CG  PHE A 208     -52.492-143.873 297.748  1.00 94.05           C  
ANISOU  817  CG  PHE A 208    10165  11433  14135   1066   -654   1352       C  
ATOM    818  CD1 PHE A 208     -52.383-143.955 296.369  1.00 92.49           C  
ANISOU  818  CD1 PHE A 208     9870  11561  13712   1018   -779   1472       C  
ATOM    819  CD2 PHE A 208     -53.755-143.789 298.312  1.00 91.34           C  
ANISOU  819  CD2 PHE A 208     9703  11047  13955   1127   -635   1409       C  
ATOM    820  CE1 PHE A 208     -53.510-143.953 295.567  1.00 91.87           C  
ANISOU  820  CE1 PHE A 208     9580  11758  13569   1030   -896   1659       C  
ATOM    821  CE2 PHE A 208     -54.887-143.784 297.515  1.00 91.36           C  
ANISOU  821  CE2 PHE A 208     9489  11311  13912   1149   -748   1592       C  
ATOM    822  CZ  PHE A 208     -54.764-143.867 296.140  1.00 91.77           C  
ANISOU  822  CZ  PHE A 208     9448  11684  13736   1100   -885   1723       C  
ATOM    823  N   LEU A 209     -51.446-140.900 299.711  1.00105.88           N  
ANISOU  823  N   LEU A 209    11852  12134  16243   1317   -251   1510       N  
ATOM    824  CA  LEU A 209     -52.154-139.633 299.865  1.00108.83           C  
ANISOU  824  CA  LEU A 209    12116  12325  16909   1474   -177   1730       C  
ATOM    825  C   LEU A 209     -51.277-138.448 299.473  1.00110.00           C  
ANISOU  825  C   LEU A 209    12325  12304  17168   1505   -121   1914       C  
ATOM    826  O   LEU A 209     -51.791-137.424 299.012  1.00111.23           O  
ANISOU  826  O   LEU A 209    12366  12375  17521   1626   -129   2208       O  
ATOM    827  CB  LEU A 209     -52.656-139.481 301.302  1.00101.57           C  
ANISOU  827  CB  LEU A 209    11206  11173  16213   1536    -32   1535       C  
ATOM    828  CG  LEU A 209     -53.795-140.418 301.716  1.00 95.44           C  
ANISOU  828  CG  LEU A 209    10320  10557  15384   1515    -77   1428       C  
ATOM    829  CD1 LEU A 209     -54.133-140.244 303.189  1.00 95.89           C  
ANISOU  829  CD1 LEU A 209    10389  10425  15620   1547     86   1221       C  
ATOM    830  CD2 LEU A 209     -55.025-140.178 300.852  1.00 89.40           C  
ANISOU  830  CD2 LEU A 209     9324   9980  14666   1614   -184   1686       C  
ATOM    831  N   ALA A 210     -49.960-138.565 299.649  1.00106.57           N  
ANISOU  831  N   ALA A 210    12058  11810  16621   1396    -68   1761       N  
ATOM    832  CA  ALA A 210     -49.058-137.532 299.151  1.00105.31           C  
ANISOU  832  CA  ALA A 210    11951  11538  16526   1379    -27   1946       C  
ATOM    833  C   ALA A 210     -49.041-137.506 297.630  1.00110.22           C  
ANISOU  833  C   ALA A 210    12471  12472  16936   1335   -174   2250       C  
ATOM    834  O   ALA A 210     -48.915-136.435 297.024  1.00110.92           O  
ANISOU  834  O   ALA A 210    12517  12482  17145   1364   -174   2570       O  
ATOM    835  CB  ALA A 210     -47.652-137.757 299.699  1.00106.19           C  
ANISOU  835  CB  ALA A 210    12241  11571  16536   1257     59   1689       C  
ATOM    836  N   ALA A 211     -49.180-138.670 296.997  1.00115.54           N  
ANISOU  836  N   ALA A 211    13096  13505  17298   1254   -302   2157       N  
ATOM    837  CA  ALA A 211     -49.222-138.716 295.541  1.00120.12           C  
ANISOU  837  CA  ALA A 211    13553  14458  17628   1196   -445   2412       C  
ATOM    838  C   ALA A 211     -50.473-138.029 295.011  1.00123.19           C  
ANISOU  838  C   ALA A 211    13751  14891  18163   1322   -524   2781       C  
ATOM    839  O   ALA A 211     -50.400-137.216 294.082  1.00128.95           O  
ANISOU  839  O   ALA A 211    14398  15721  18876   1324   -581   3151       O  
ATOM    840  CB  ALA A 211     -49.155-140.163 295.056  1.00122.17           C  
ANISOU  840  CB  ALA A 211    13793  15081  17545   1083   -559   2162       C  
ATOM    841  N   ILE A 212     -51.633-138.330 295.603  1.00119.94           N  
ANISOU  841  N   ILE A 212    13257  14417  17899   1426   -531   2704       N  
ATOM    842  CA  ILE A 212     -52.871-137.708 295.142  1.00127.28           C  
ANISOU  842  CA  ILE A 212    13977  15403  18981   1568   -611   3041       C  
ATOM    843  C   ILE A 212     -52.884-136.220 295.473  1.00130.23           C  
ANISOU  843  C   ILE A 212    14352  15377  19751   1722   -514   3298       C  
ATOM    844  O   ILE A 212     -53.524-135.428 294.771  1.00130.41           O  
ANISOU  844  O   ILE A 212    14216  15435  19900   1834   -599   3695       O  
ATOM    845  CB  ILE A 212     -54.100-138.432 295.730  1.00132.51           C  
ANISOU  845  CB  ILE A 212    14529  16120  19697   1629   -633   2868       C  
ATOM    846  CG1 ILE A 212     -54.226-138.187 297.236  1.00133.69           C  
ANISOU  846  CG1 ILE A 212    14771  15872  20153   1717   -456   2625       C  
ATOM    847  CG2 ILE A 212     -54.024-139.923 295.457  1.00131.13           C  
ANISOU  847  CG2 ILE A 212    14375  16274  19177   1458   -727   2592       C  
ATOM    848  CD1 ILE A 212     -55.288-137.167 297.618  1.00138.06           C  
ANISOU  848  CD1 ILE A 212    15164  16211  21080   1936   -406   2812       C  
ATOM    849  N   ASP A 213     -52.187-135.814 296.538  1.00128.38           N  
ANISOU  849  N   ASP A 213    14290  14756  19731   1729   -342   3079       N  
ATOM    850  CA  ASP A 213     -52.120-134.397 296.879  1.00127.26           C  
ANISOU  850  CA  ASP A 213    14163  14194  19996   1858   -240   3272       C  
ATOM    851  C   ASP A 213     -51.372-133.614 295.809  1.00126.04           C  
ANISOU  851  C   ASP A 213    14023  14073  19793   1787   -300   3652       C  
ATOM    852  O   ASP A 213     -51.801-132.523 295.413  1.00131.75           O  
ANISOU  852  O   ASP A 213    14649  14612  20797   1913   -332   4034       O  
ATOM    853  CB  ASP A 213     -51.453-134.219 298.244  1.00126.34           C  
ANISOU  853  CB  ASP A 213    14225  13710  20067   1841    -43   2902       C  
ATOM    854  CG  ASP A 213     -51.749-132.867 298.875  1.00130.74           C  
ANISOU  854  CG  ASP A 213    14762  13797  21115   2010     81   2985       C  
ATOM    855  OD1 ASP A 213     -52.272-131.975 298.174  1.00133.03           O  
ANISOU  855  OD1 ASP A 213    14942  14025  21576   2110     13   3341       O  
ATOM    856  OD2 ASP A 213     -51.454-132.697 300.077  1.00130.62           O  
ANISOU  856  OD2 ASP A 213    14849  13508  21274   2015    247   2653       O  
ATOM    857  N   ARG A 214     -50.260-134.159 295.320  1.00119.99           N  
ANISOU  857  N   ARG A 214    13363  13549  18678   1584   -321   3565       N  
ATOM    858  CA  ARG A 214     -49.462-133.481 294.310  1.00124.30           C  
ANISOU  858  CA  ARG A 214    13916  14188  19125   1473   -368   3912       C  
ATOM    859  C   ARG A 214     -49.871-133.839 292.887  1.00128.11           C  
ANISOU  859  C   ARG A 214    14223  15188  19264   1416   -563   4232       C  
ATOM    860  O   ARG A 214     -49.509-133.113 291.954  1.00131.26           O  
ANISOU  860  O   ARG A 214    14574  15691  19609   1348   -625   4639       O  
ATOM    861  CB  ARG A 214     -47.979-133.789 294.529  1.00122.85           C  
ANISOU  861  CB  ARG A 214    13914  14023  18742   1278   -273   3644       C  
ATOM    862  CG  ARG A 214     -47.500-133.391 295.918  1.00126.18           C  
ANISOU  862  CG  ARG A 214    14496  13974  19471   1310    -86   3334       C  
ATOM    863  CD  ARG A 214     -46.098-133.885 296.218  1.00128.54           C  
ANISOU  863  CD  ARG A 214    14951  14346  19543   1129     -7   3023       C  
ATOM    864  NE  ARG A 214     -45.753-133.669 297.621  1.00128.69           N  
ANISOU  864  NE  ARG A 214    15103  13985  19809   1156    157   2688       N  
ATOM    865  CZ  ARG A 214     -44.583-133.987 298.164  1.00124.31           C  
ANISOU  865  CZ  ARG A 214    14679  13423  19130   1026    243   2389       C  
ATOM    866  NH1 ARG A 214     -43.632-134.539 297.423  1.00119.19           N  
ANISOU  866  NH1 ARG A 214    14046  13109  18134    873    187   2369       N  
ATOM    867  NH2 ARG A 214     -44.364-133.752 299.451  1.00123.94           N  
ANISOU  867  NH2 ARG A 214    14731  13064  19298   1049    385   2100       N  
ATOM    868  N   TYR A 215     -50.619-134.930 292.696  1.00126.71           N  
ANISOU  868  N   TYR A 215    13942  15352  18849   1423   -662   4064       N  
ATOM    869  CA  TYR A 215     -51.153-135.228 291.370  1.00127.41           C  
ANISOU  869  CA  TYR A 215    13832  15955  18622   1374   -852   4355       C  
ATOM    870  C   TYR A 215     -52.316-134.307 291.028  1.00128.07           C  
ANISOU  870  C   TYR A 215    13726  15958  18977   1562   -945   4819       C  
ATOM    871  O   TYR A 215     -52.420-133.825 289.893  1.00127.66           O  
ANISOU  871  O   TYR A 215    13536  16184  18786   1528  -1079   5271       O  
ATOM    872  CB  TYR A 215     -51.587-136.694 291.288  1.00126.27           C  
ANISOU  872  CB  TYR A 215    13634  16182  18162   1307   -930   3998       C  
ATOM    873  CG  TYR A 215     -52.404-137.035 290.058  1.00127.12           C  
ANISOU  873  CG  TYR A 215    13503  16821  17976   1273  -1128   4246       C  
ATOM    874  CD1 TYR A 215     -51.789-137.289 288.839  1.00124.47           C  
ANISOU  874  CD1 TYR A 215    13101  16975  17215   1091  -1226   4361       C  
ATOM    875  CD2 TYR A 215     -53.791-137.111 290.121  1.00128.75           C  
ANISOU  875  CD2 TYR A 215    13530  17081  18308   1412  -1214   4349       C  
ATOM    876  CE1 TYR A 215     -52.533-137.602 287.714  1.00125.96           C  
ANISOU  876  CE1 TYR A 215    13056  17698  17103   1042  -1409   4571       C  
ATOM    877  CE2 TYR A 215     -54.542-137.422 289.001  1.00129.19           C  
ANISOU  877  CE2 TYR A 215    13350  17656  18080   1370  -1403   4570       C  
ATOM    878  CZ  TYR A 215     -53.908-137.667 287.801  1.00127.89           C  
ANISOU  878  CZ  TYR A 215    13130  17980  17485   1181  -1502   4680       C  
ATOM    879  OH  TYR A 215     -54.654-137.978 286.686  1.00128.79           O  
ANISOU  879  OH  TYR A 215    12993  18657  17284   1122  -1692   4884       O  
ATOM    880  N   ILE A 216     -53.202-134.053 291.994  1.00127.99           N  
ANISOU  880  N   ILE A 216    13689  15593  19349   1765   -879   4720       N  
ATOM    881  CA  ILE A 216     -54.331-133.161 291.750  1.00133.97           C  
ANISOU  881  CA  ILE A 216    14247  16239  20417   1983   -962   5134       C  
ATOM    882  C   ILE A 216     -53.849-131.734 291.515  1.00139.28           C  
ANISOU  882  C   ILE A 216    14973  16559  21387   2024   -926   5525       C  
ATOM    883  O   ILE A 216     -54.432-130.998 290.709  1.00142.96           O  
ANISOU  883  O   ILE A 216    15318  17126  21874   2054  -1022   5892       O  
ATOM    884  CB  ILE A 216     -55.334-133.245 292.917  1.00133.59           C  
ANISOU  884  CB  ILE A 216    14149  15903  20705   2184   -873   4866       C  
ATOM    885  CG1 ILE A 216     -56.031-134.608 292.922  1.00127.81           C  
ANISOU  885  CG1 ILE A 216    13322  15582  19660   2116   -947   4574       C  
ATOM    886  CG2 ILE A 216     -56.365-132.129 292.838  1.00139.66           C  
ANISOU  886  CG2 ILE A 216    14809  16487  21768   2347   -876   5088       C  
ATOM    887  CD1 ILE A 216     -57.124-134.732 293.963  1.00123.69           C  
ANISOU  887  CD1 ILE A 216    12706  14873  19419   2288   -874   4354       C  
ATOM    888  N   SER A 217     -52.770-131.325 292.189  1.00139.12           N  
ANISOU  888  N   SER A 217    15166  16151  21544   1964   -766   5366       N  
ATOM    889  CA  SER A 217     -52.245-129.977 291.997  1.00140.01           C  
ANISOU  889  CA  SER A 217    15371  15937  21888   1918   -703   5612       C  
ATOM    890  C   SER A 217     -51.756-129.759 290.570  1.00146.89           C  
ANISOU  890  C   SER A 217    16166  17189  22457   1759   -855   6113       C  
ATOM    891  O   SER A 217     -51.807-128.632 290.063  1.00155.71           O  
ANISOU  891  O   SER A 217    17264  18163  23736   1744   -875   6447       O  
ATOM    892  CB  SER A 217     -51.117-129.706 292.993  1.00131.18           C  
ANISOU  892  CB  SER A 217    14487  14392  20965   1845   -506   5302       C  
ATOM    893  OG  SER A 217     -50.067-130.646 292.847  1.00121.99           O  
ANISOU  893  OG  SER A 217    13422  13518  19410   1644   -494   5100       O  
ATOM    894  N   ILE A 218     -51.287-130.813 289.907  1.00147.23           N  
ANISOU  894  N   ILE A 218    16171  17762  22009   1599   -948   6082       N  
ATOM    895  CA  ILE A 218     -50.802-130.694 288.535  1.00151.73           C  
ANISOU  895  CA  ILE A 218    16652  18805  22194   1406  -1083   6499       C  
ATOM    896  C   ILE A 218     -51.922-130.921 287.527  1.00156.73           C  
ANISOU  896  C   ILE A 218    17016  19922  22613   1472  -1303   6853       C  
ATOM    897  O   ILE A 218     -52.049-130.175 286.554  1.00161.89           O  
ANISOU  897  O   ILE A 218    17571  20750  23188   1398  -1391   7284       O  
ATOM    898  CB  ILE A 218     -49.633-131.672 288.303  1.00149.22           C  
ANISOU  898  CB  ILE A 218    16442  18876  21379   1140  -1030   6119       C  
ATOM    899  CG1 ILE A 218     -48.508-131.412 289.307  1.00147.25           C  
ANISOU  899  CG1 ILE A 218    16438  18172  21339   1075   -823   5789       C  
ATOM    900  CG2 ILE A 218     -49.116-131.557 286.875  1.00151.37           C  
ANISOU  900  CG2 ILE A 218    16597  19703  21213    922  -1155   6519       C  
ATOM    901  CD1 ILE A 218     -47.900-130.030 289.204  1.00150.17           C  
ANISOU  901  CD1 ILE A 218    16877  18165  22016   1029   -768   6200       C  
ATOM    902  N   HIS A 219     -52.748-131.947 287.744  1.00158.94           N  
ANISOU  902  N   HIS A 219    17203  20447  22741   1540  -1348   6520       N  
ATOM    903  CA  HIS A 219     -53.806-132.260 286.789  1.00164.91           C  
ANISOU  903  CA  HIS A 219    17691  21719  23248   1572  -1556   6791       C  
ATOM    904  C   HIS A 219     -54.915-131.215 286.830  1.00169.94           C  
ANISOU  904  C   HIS A 219    18251  22060  24257   1743  -1549   7003       C  
ATOM    905  O   HIS A 219     -55.460-130.839 285.785  1.00172.17           O  
ANISOU  905  O   HIS A 219    18364  22672  24380   1707  -1684   7376       O  
ATOM    906  CB  HIS A 219     -54.367-133.655 287.073  1.00162.06           C  
ANISOU  906  CB  HIS A 219    17278  21662  22636   1553  -1577   6289       C  
ATOM    907  CG  HIS A 219     -54.980-134.319 285.879  1.00162.38           C  
ANISOU  907  CG  HIS A 219    17072  22419  22208   1449  -1785   6438       C  
ATOM    908  ND1 HIS A 219     -54.250-134.659 284.760  1.00162.27           N  
ANISOU  908  ND1 HIS A 219    17013  22960  21682   1201  -1865   6524       N  
ATOM    909  CD2 HIS A 219     -56.251-134.716 285.633  1.00163.21           C  
ANISOU  909  CD2 HIS A 219    16943  22807  22262   1546  -1925   6491       C  
ATOM    910  CE1 HIS A 219     -55.046-135.231 283.874  1.00164.37           C  
ANISOU  910  CE1 HIS A 219    17033  23822  21598   1148  -2048   6614       C  
ATOM    911  NE2 HIS A 219     -56.265-135.279 284.380  1.00164.99           N  
ANISOU  911  NE2 HIS A 219    16994  23744  21950   1352  -2092   6603       N  
ATOM    912  N   ARG A 220     -55.263-130.733 288.024  1.00172.44           N  
ANISOU  912  N   ARG A 220    18679  21783  25056   1927  -1396   6756       N  
ATOM    913  CA  ARG A 220     -56.344-129.766 288.217  1.00178.01           C  
ANISOU  913  CA  ARG A 220    19306  22189  26141   2119  -1384   6882       C  
ATOM    914  C   ARG A 220     -55.851-128.656 289.137  1.00175.98           C  
ANISOU  914  C   ARG A 220    19245  21250  26368   2194  -1200   6778       C  
ATOM    915  O   ARG A 220     -56.183-128.629 290.330  1.00174.96           O  
ANISOU  915  O   ARG A 220    19193  20744  26541   2333  -1060   6394       O  
ATOM    916  CB  ARG A 220     -57.589-130.441 288.796  1.00178.10           C  
ANISOU  916  CB  ARG A 220    19191  22274  26205   2281  -1396   6594       C  
ATOM    917  CG  ARG A 220     -57.921-131.791 288.172  1.00178.41           C  
ANISOU  917  CG  ARG A 220    19070  22954  25765   2176  -1548   6528       C  
ATOM    918  CD  ARG A 220     -58.963-131.670 287.075  1.00185.66           C  
ANISOU  918  CD  ARG A 220    19738  24313  26490   2188  -1731   6867       C  
ATOM    919  NE  ARG A 220     -60.297-131.442 287.622  1.00189.88           N  
ANISOU  919  NE  ARG A 220    20152  24679  27313   2403  -1717   6773       N  
ATOM    920  CZ  ARG A 220     -61.102-132.410 288.050  1.00190.18           C  
ANISOU  920  CZ  ARG A 220    20080  24918  27263   2444  -1738   6469       C  
ATOM    921  NH1 ARG A 220     -62.300-132.113 288.535  1.00194.19           N  
ANISOU  921  NH1 ARG A 220    20464  25285  28033   2638  -1721   6406       N  
ATOM    922  NH2 ARG A 220     -60.709-133.676 287.995  1.00186.11           N  
ANISOU  922  NH2 ARG A 220    19563  24751  26398   2286  -1781   6221       N  
ATOM    923  N   PRO A 221     -55.053-127.718 288.616  1.00170.81           N  
ANISOU  923  N   PRO A 221    18668  20450  25784   2084  -1196   7098       N  
ATOM    924  CA  PRO A 221     -54.544-126.645 289.489  1.00165.91           C  
ANISOU  924  CA  PRO A 221    18230  19185  25621   2131  -1026   6966       C  
ATOM    925  C   PRO A 221     -55.625-125.680 289.940  1.00163.82           C  
ANISOU  925  C   PRO A 221    17900  18543  25801   2364  -1001   6966       C  
ATOM    926  O   PRO A 221     -55.618-125.247 291.099  1.00161.98           O  
ANISOU  926  O   PRO A 221    17787  17836  25923   2468   -838   6609       O  
ATOM    927  CB  PRO A 221     -53.488-125.949 288.615  1.00168.84           C  
ANISOU  927  CB  PRO A 221    18659  19588  25902   1927  -1064   7369       C  
ATOM    928  CG  PRO A 221     -53.204-126.905 287.490  1.00168.39           C  
ANISOU  928  CG  PRO A 221    18487  20220  25276   1747  -1217   7595       C  
ATOM    929  CD  PRO A 221     -54.485-127.640 287.261  1.00170.46           C  
ANISOU  929  CD  PRO A 221    18548  20842  25377   1880  -1336   7553       C  
ATOM    930  N   LEU A 222     -56.559-125.327 289.053  1.00160.75           N  
ANISOU  930  N   LEU A 222    17311  18375  25390   2448  -1161   7350       N  
ATOM    931  CA  LEU A 222     -57.607-124.382 289.420  1.00160.19           C  
ANISOU  931  CA  LEU A 222    17160  17956  25750   2689  -1153   7380       C  
ATOM    932  C   LEU A 222     -58.601-124.992 290.400  1.00157.86           C  
ANISOU  932  C   LEU A 222    16803  17632  25546   2877  -1085   6945       C  
ATOM    933  O   LEU A 222     -59.201-124.268 291.202  1.00157.58           O  
ANISOU  933  O   LEU A 222    16767  17192  25913   3072   -997   6764       O  
ATOM    934  CB  LEU A 222     -58.334-123.888 288.168  1.00163.39           C  
ANISOU  934  CB  LEU A 222    17355  18637  26088   2728  -1355   7930       C  
ATOM    935  CG  LEU A 222     -57.746-122.690 287.413  1.00166.73           C  
ANISOU  935  CG  LEU A 222    17811  18871  26668   2640  -1410   8404       C  
ATOM    936  CD1 LEU A 222     -56.347-122.979 286.886  1.00163.00           C  
ANISOU  936  CD1 LEU A 222    17460  18604  25869   2342  -1401   8528       C  
ATOM    937  CD2 LEU A 222     -58.671-122.275 286.278  1.00173.76           C  
ANISOU  937  CD2 LEU A 222    18465  20053  27502   2711  -1614   8921       C  
ATOM    938  N   ALA A 223     -58.785-126.310 290.356  1.00155.94           N  
ANISOU  938  N   ALA A 223    16496  17823  24931   2815  -1126   6768       N  
ATOM    939  CA  ALA A 223     -59.728-126.999 291.225  1.00153.44           C  
ANISOU  939  CA  ALA A 223    16101  17544  24656   2960  -1073   6378       C  
ATOM    940  C   ALA A 223     -59.052-127.694 292.400  1.00151.50           C  
ANISOU  940  C   ALA A 223    16035  17127  24402   2894   -896   5869       C  
ATOM    941  O   ALA A 223     -59.719-128.422 293.141  1.00153.35           O  
ANISOU  941  O   ALA A 223    16209  17440  24619   2971   -847   5534       O  
ATOM    942  CB  ALA A 223     -60.543-128.013 290.420  1.00150.26           C  
ANISOU  942  CB  ALA A 223    15478  17747  23867   2938  -1250   6512       C  
ATOM    943  N   TYR A 224     -57.746-127.487 292.586  1.00151.65           N  
ANISOU  943  N   TYR A 224    16263  16928  24428   2745   -800   5812       N  
ATOM    944  CA  TYR A 224     -57.041-128.135 293.690  1.00148.49           C  
ANISOU  944  CA  TYR A 224    16034  16374  24011   2674   -636   5340       C  
ATOM    945  C   TYR A 224     -57.533-127.626 295.039  1.00149.87           C  
ANISOU  945  C   TYR A 224    16253  16140  24550   2826   -462   4942       C  
ATOM    946  O   TYR A 224     -57.670-128.405 295.990  1.00145.73           O  
ANISOU  946  O   TYR A 224    15757  15638  23976   2832   -362   4537       O  
ATOM    947  CB  TYR A 224     -55.534-127.916 293.549  1.00150.11           C  
ANISOU  947  CB  TYR A 224    16439  16440  24155   2483   -576   5389       C  
ATOM    948  CG  TYR A 224     -54.730-128.325 294.766  1.00148.91           C  
ANISOU  948  CG  TYR A 224    16479  16049  24050   2418   -390   4905       C  
ATOM    949  CD1 TYR A 224     -54.364-129.649 294.967  1.00147.53           C  
ANISOU  949  CD1 TYR A 224    16334  16140  23579   2332   -394   4682       C  
ATOM    950  CD2 TYR A 224     -54.330-127.384 295.708  1.00151.15           C  
ANISOU  950  CD2 TYR A 224    16905  15855  24669   2437   -219   4668       C  
ATOM    951  CE1 TYR A 224     -53.627-130.026 296.076  1.00145.09           C  
ANISOU  951  CE1 TYR A 224    16196  15623  23309   2270   -230   4254       C  
ATOM    952  CE2 TYR A 224     -53.595-127.752 296.819  1.00148.33           C  
ANISOU  952  CE2 TYR A 224    16711  15326  24321   2360    -53   4224       C  
ATOM    953  CZ  TYR A 224     -53.246-129.073 296.998  1.00144.08           C  
ANISOU  953  CZ  TYR A 224    16203  15056  23484   2278    -59   4027       C  
ATOM    954  OH  TYR A 224     -52.512-129.443 298.103  1.00139.14           O  
ANISOU  954  OH  TYR A 224    15736  14273  22860   2199     99   3599       O  
ATOM    955  N   LYS A 225     -57.799-126.322 295.145  1.00154.76           N  
ANISOU  955  N   LYS A 225    16870  16398  25533   2943   -427   5051       N  
ATOM    956  CA  LYS A 225     -58.255-125.757 296.409  1.00153.45           C  
ANISOU  956  CA  LYS A 225    16730  15866  25710   3088   -264   4665       C  
ATOM    957  C   LYS A 225     -59.669-126.193 296.766  1.00147.05           C  
ANISOU  957  C   LYS A 225    15716  15239  24918   3273   -289   4524       C  
ATOM    958  O   LYS A 225     -60.042-126.134 297.942  1.00140.24           O  
ANISOU  958  O   LYS A 225    14858  14200  24226   3362   -142   4121       O  
ATOM    959  CB  LYS A 225     -58.175-124.230 296.361  1.00163.55           C  
ANISOU  959  CB  LYS A 225    18045  16708  27389   3172   -238   4828       C  
ATOM    960  CG  LYS A 225     -56.765-123.686 296.524  1.00167.33           C  
ANISOU  960  CG  LYS A 225    18745  16894  27940   2992   -141   4789       C  
ATOM    961  CD  LYS A 225     -56.151-124.164 297.833  1.00165.06           C  
ANISOU  961  CD  LYS A 225    18608  16488  27619   2907     53   4243       C  
ATOM    962  CE  LYS A 225     -54.744-123.622 298.024  1.00165.25           C  
ANISOU  962  CE  LYS A 225    18840  16240  27709   2722    149   4184       C  
ATOM    963  NZ  LYS A 225     -54.139-124.101 299.299  1.00160.89           N  
ANISOU  963  NZ  LYS A 225    18422  15610  27098   2631    329   3654       N  
ATOM    964  N   ARG A 226     -60.459-126.633 295.785  1.00150.21           N  
ANISOU  964  N   ARG A 226    15924  16021  25128   3320   -471   4843       N  
ATOM    965  CA  ARG A 226     -61.818-127.081 296.068  1.00154.37           C  
ANISOU  965  CA  ARG A 226    16235  16762  25656   3484   -505   4723       C  
ATOM    966  C   ARG A 226     -61.856-128.526 296.550  1.00148.30           C  
ANISOU  966  C   ARG A 226    15453  16309  24586   3380   -474   4420       C  
ATOM    967  O   ARG A 226     -62.722-128.882 297.356  1.00148.48           O  
ANISOU  967  O   ARG A 226    15358  16386  24671   3483   -407   4135       O  
ATOM    968  CB  ARG A 226     -62.693-126.920 294.823  1.00163.45           C  
ANISOU  968  CB  ARG A 226    17166  18210  26728   3572   -721   5184       C  
ATOM    969  CG  ARG A 226     -64.174-127.191 295.057  1.00168.53           C  
ANISOU  969  CG  ARG A 226    17557  19058  27417   3764   -766   5093       C  
ATOM    970  CD  ARG A 226     -64.982-127.008 293.780  1.00174.17           C  
ANISOU  970  CD  ARG A 226    18053  20090  28035   3837   -989   5562       C  
ATOM    971  NE  ARG A 226     -64.644-128.004 292.768  1.00173.73           N  
ANISOU  971  NE  ARG A 226    17964  20526  27521   3630  -1137   5778       N  
ATOM    972  CZ  ARG A 226     -65.317-129.134 292.576  1.00173.22           C  
ANISOU  972  CZ  ARG A 226    17731  20929  27156   3584  -1225   5698       C  
ATOM    973  NH1 ARG A 226     -66.373-129.415 293.327  1.00174.80           N  
ANISOU  973  NH1 ARG A 226    17776  21173  27467   3727  -1178   5429       N  
ATOM    974  NH2 ARG A 226     -64.936-129.983 291.631  1.00170.97           N  
ANISOU  974  NH2 ARG A 226    17420  21088  26453   3385  -1362   5875       N  
ATOM    975  N   ILE A 227     -60.931-129.363 296.083  1.00143.67           N  
ANISOU  975  N   ILE A 227    14970  15934  23682   3177   -523   4475       N  
ATOM    976  CA  ILE A 227     -60.934-130.783 296.422  1.00136.83           C  
ANISOU  976  CA  ILE A 227    14083  15371  22534   3072   -522   4225       C  
ATOM    977  C   ILE A 227     -60.184-131.013 297.727  1.00131.90           C  
ANISOU  977  C   ILE A 227    13655  14472  21990   3003   -316   3782       C  
ATOM    978  O   ILE A 227     -60.783-131.385 298.743  1.00132.07           O  
ANISOU  978  O   ILE A 227    13619  14482  22082   3059   -211   3452       O  
ATOM    979  CB  ILE A 227     -60.328-131.625 295.284  1.00132.67           C  
ANISOU  979  CB  ILE A 227    13554  15233  21623   2899   -687   4475       C  
ATOM    980  CG1 ILE A 227     -61.154-131.464 294.005  1.00136.05           C  
ANISOU  980  CG1 ILE A 227    13762  16014  21916   2946   -896   4897       C  
ATOM    981  CG2 ILE A 227     -60.242-133.091 295.690  1.00126.89           C  
ANISOU  981  CG2 ILE A 227    12810  14764  20638   2787   -688   4190       C  
ATOM    982  CD1 ILE A 227     -60.654-132.295 292.842  1.00134.96           C  
ANISOU  982  CD1 ILE A 227    13584  16344  21352   2764  -1069   5126       C  
ATOM    983  N   VAL A 228     -58.872-130.796 297.710  1.00125.15           N  
ANISOU  983  N   VAL A 228    13017  13425  21110   2870   -258   3775       N  
ATOM    984  CA  VAL A 228     -58.028-131.057 298.873  1.00117.69           C  
ANISOU  984  CA  VAL A 228    12263  12258  20193   2776    -77   3368       C  
ATOM    985  C   VAL A 228     -58.223-129.922 299.873  1.00123.52           C  
ANISOU  985  C   VAL A 228    13049  12603  21280   2882     91   3142       C  
ATOM    986  O   VAL A 228     -57.854-128.776 299.608  1.00130.87           O  
ANISOU  986  O   VAL A 228    14047  13258  22420   2907    106   3299       O  
ATOM    987  CB  VAL A 228     -56.554-131.198 298.478  1.00111.08           C  
ANISOU  987  CB  VAL A 228    11624  11377  19206   2600    -80   3439       C  
ATOM    988  CG1 VAL A 228     -55.749-131.795 299.627  1.00101.13           C  
ANISOU  988  CG1 VAL A 228    10533   9995  17896   2491     77   3011       C  
ATOM    989  CG2 VAL A 228     -56.420-132.042 297.218  1.00111.76           C  
ANISOU  989  CG2 VAL A 228    11623  11872  18967   2520   -278   3751       C  
ATOM    990  N   THR A 229     -58.808-130.240 301.026  1.00119.71           N  
ANISOU  990  N   THR A 229    12517  12108  20861   2936    215   2774       N  
ATOM    991  CA  THR A 229     -59.018-129.278 302.096  1.00120.71           C  
ANISOU  991  CA  THR A 229    12665  11915  21284   3030    383   2493       C  
ATOM    992  C   THR A 229     -58.431-129.830 303.388  1.00114.46           C  
ANISOU  992  C   THR A 229    11997  11082  20410   2908    556   2046       C  
ATOM    993  O   THR A 229     -57.963-130.971 303.450  1.00108.98           O  
ANISOU  993  O   THR A 229    11362  10590  19456   2772    539   1970       O  
ATOM    994  CB  THR A 229     -60.507-128.962 302.295  1.00131.11           C  
ANISOU  994  CB  THR A 229    13742  13293  22780   3247    372   2479       C  
ATOM    995  OG1 THR A 229     -61.163-130.100 302.867  1.00134.39           O  
ANISOU  995  OG1 THR A 229    14031  14006  23023   3233    398   2264       O  
ATOM    996  CG2 THR A 229     -61.168-128.616 300.969  1.00132.91           C  
ANISOU  996  CG2 THR A 229    13821  13645  23033   3361    174   2940       C  
ATOM    997  N   ARG A 230     -58.460-128.999 304.433  1.00117.42           N  
ANISOU  997  N   ARG A 230    12402  11198  21015   2958    720   1748       N  
ATOM    998  CA  ARG A 230     -58.011-129.467 305.744  1.00119.79           C  
ANISOU  998  CA  ARG A 230    12787  11498  21229   2844    889   1315       C  
ATOM    999  C   ARG A 230     -58.952-130.516 306.325  1.00120.05           C  
ANISOU  999  C   ARG A 230    12651  11831  21131   2875    914   1144       C  
ATOM   1000  O   ARG A 230     -58.464-131.573 306.761  1.00118.38           O  
ANISOU 1000  O   ARG A 230    12509  11778  20693   2727    945    992       O  
ATOM   1001  CB  ARG A 230     -57.819-128.272 306.686  1.00126.27           C  
ANISOU 1001  CB  ARG A 230    13658  12000  22318   2881   1052   1035       C  
ATOM   1002  CG  ARG A 230     -57.202-128.612 308.040  1.00126.70           C  
ANISOU 1002  CG  ARG A 230    13808  12062  22271   2739   1229    593       C  
ATOM   1003  CD  ARG A 230     -58.266-128.796 309.113  1.00130.86           C  
ANISOU 1003  CD  ARG A 230    14150  12724  22846   2835   1349    280       C  
ATOM   1004  NE  ARG A 230     -59.151-127.639 309.207  1.00138.52           N  
ANISOU 1004  NE  ARG A 230    14979  13510  24141   3042   1383    253       N  
ATOM   1005  CZ  ARG A 230     -60.205-127.567 310.014  1.00142.83           C  
ANISOU 1005  CZ  ARG A 230    15328  14160  24781   3170   1483      2       C  
ATOM   1006  NH1 ARG A 230     -60.508-128.590 310.801  1.00142.89           N  
ANISOU 1006  NH1 ARG A 230    15249  14467  24574   3093   1565   -227       N  
ATOM   1007  NH2 ARG A 230     -60.956-126.475 310.034  1.00146.88           N  
ANISOU 1007  NH2 ARG A 230    15717  14483  25608   3375   1504    -17       N  
ATOM   1008  N   PRO A 231     -60.278-130.315 306.366  1.00121.83           N  
ANISOU 1008  N   PRO A 231    12645  12154  21490   3055    901   1163       N  
ATOM   1009  CA  PRO A 231     -61.135-131.380 306.917  1.00120.18           C  
ANISOU 1009  CA  PRO A 231    12254  12266  21145   3055    930   1006       C  
ATOM   1010  C   PRO A 231     -61.136-132.645 306.078  1.00119.22           C  
ANISOU 1010  C   PRO A 231    12097  12439  20763   2960    768   1243       C  
ATOM   1011  O   PRO A 231     -61.176-133.748 306.637  1.00121.37           O  
ANISOU 1011  O   PRO A 231    12328  12918  20869   2849    808   1079       O  
ATOM   1012  CB  PRO A 231     -62.523-130.725 306.963  1.00124.41           C  
ANISOU 1012  CB  PRO A 231    12535  12836  21899   3285    933   1016       C  
ATOM   1013  CG  PRO A 231     -62.469-129.658 305.936  1.00125.77           C  
ANISOU 1013  CG  PRO A 231    12744  12784  22257   3405    814   1340       C  
ATOM   1014  CD  PRO A 231     -61.070-129.127 305.999  1.00126.41           C  
ANISOU 1014  CD  PRO A 231    13101  12565  22364   3268    868   1305       C  
ATOM   1015  N   LYS A 232     -61.096-132.522 304.748  1.00116.86           N  
ANISOU 1015  N   LYS A 232    11797  12179  20425   2991    584   1625       N  
ATOM   1016  CA  LYS A 232     -61.054-133.712 303.903  1.00111.25           C  
ANISOU 1016  CA  LYS A 232    11044  11772  19455   2891    420   1834       C  
ATOM   1017  C   LYS A 232     -59.766-134.496 304.121  1.00100.87           C  
ANISOU 1017  C   LYS A 232     9950  10426  17949   2694    446   1714       C  
ATOM   1018  O   LYS A 232     -59.793-135.728 304.221  1.00 98.50           O  
ANISOU 1018  O   LYS A 232     9604  10351  17472   2591    403   1654       O  
ATOM   1019  CB  LYS A 232     -61.206-133.325 302.432  1.00118.78           C  
ANISOU 1019  CB  LYS A 232    11945  12801  20383   2954    222   2263       C  
ATOM   1020  CG  LYS A 232     -62.592-132.821 302.056  1.00132.50           C  
ANISOU 1020  CG  LYS A 232    13427  14660  22259   3147    148   2425       C  
ATOM   1021  CD  LYS A 232     -63.652-133.890 302.273  1.00140.62           C  
ANISOU 1021  CD  LYS A 232    14211  16059  23159   3141    109   2341       C  
ATOM   1022  CE  LYS A 232     -65.026-133.407 301.832  1.00148.39           C  
ANISOU 1022  CE  LYS A 232    14923  17202  24257   3332     22   2508       C  
ATOM   1023  NZ  LYS A 232     -65.053-133.044 300.388  1.00151.51           N  
ANISOU 1023  NZ  LYS A 232    15288  17692  24586   3370   -184   2937       N  
ATOM   1024  N   ALA A 233     -58.629-133.801 304.200  1.00 99.31           N  
ANISOU 1024  N   ALA A 233     9981   9953  17800   2636    512   1677       N  
ATOM   1025  CA  ALA A 233     -57.369-134.486 304.470  1.00 94.75           C  
ANISOU 1025  CA  ALA A 233     9610   9343  17045   2459    544   1539       C  
ATOM   1026  C   ALA A 233     -57.323-135.034 305.891  1.00 91.45           C  
ANISOU 1026  C   ALA A 233     9216   8927  16604   2387    707   1150       C  
ATOM   1027  O   ALA A 233     -56.700-136.076 306.131  1.00 83.80           O  
ANISOU 1027  O   ALA A 233     8370   8090  15380   2212    686   1032       O  
ATOM   1028  CB  ALA A 233     -56.188-133.547 304.224  1.00 93.83           C  
ANISOU 1028  CB  ALA A 233     9704   8958  16991   2405    580   1592       C  
ATOM   1029  N   VAL A 234     -57.968-134.353 306.842  1.00 99.53           N  
ANISOU 1029  N   VAL A 234    10152   9862  17804   2471    856    932       N  
ATOM   1030  CA  VAL A 234     -58.053-134.874 308.204  1.00101.40           C  
ANISOU 1030  CA  VAL A 234    10360  10164  18004   2400   1017    574       C  
ATOM   1031  C   VAL A 234     -58.850-136.173 308.220  1.00 99.15           C  
ANISOU 1031  C   VAL A 234     9930  10228  17514   2326    941    593       C  
ATOM   1032  O   VAL A 234     -58.436-137.171 308.822  1.00 97.49           O  
ANISOU 1032  O   VAL A 234     9846  10183  17012   2107    949    432       O  
ATOM   1033  CB  VAL A 234     -58.664-133.821 309.147  1.00109.83           C  
ANISOU 1033  CB  VAL A 234    11333  11114  19284   2507   1186    330       C  
ATOM   1034  CG1 VAL A 234     -59.267-134.486 310.376  1.00112.40           C  
ANISOU 1034  CG1 VAL A 234    11502  11647  19557   2465   1333     23       C  
ATOM   1035  CG2 VAL A 234     -57.609-132.807 309.562  1.00113.06           C  
ANISOU 1035  CG2 VAL A 234    11950  11230  19778   2452   1285    177       C  
ATOM   1036  N   VAL A 235     -59.999-136.181 307.542  1.00 99.69           N  
ANISOU 1036  N   VAL A 235     9765  10453  17658   2456    841    799       N  
ATOM   1037  CA  VAL A 235     -60.825-137.384 307.487  1.00104.88           C  
ANISOU 1037  CA  VAL A 235    10308  11489  18051   2321    745    815       C  
ATOM   1038  C   VAL A 235     -60.124-138.484 306.698  1.00107.26           C  
ANISOU 1038  C   VAL A 235    10802  11938  18014   2107    563    943       C  
ATOM   1039  O   VAL A 235     -60.132-139.654 307.099  1.00109.06           O  
ANISOU 1039  O   VAL A 235    11092  12366  17979   1894    531    828       O  
ATOM   1040  CB  VAL A 235     -62.205-137.050 306.892  1.00107.28           C  
ANISOU 1040  CB  VAL A 235    10293  11942  18528   2518    674   1007       C  
ATOM   1041  CG1 VAL A 235     -62.960-138.323 306.541  1.00105.47           C  
ANISOU 1041  CG1 VAL A 235     9957  12110  18004   2346    532   1075       C  
ATOM   1042  CG2 VAL A 235     -63.012-136.201 307.865  1.00108.40           C  
ANISOU 1042  CG2 VAL A 235    10210  11999  18980   2712    870    797       C  
ATOM   1043  N   ALA A 236     -59.500-138.127 305.571  1.00104.95           N  
ANISOU 1043  N   ALA A 236    10600  11548  17728   2156    443   1180       N  
ATOM   1044  CA  ALA A 236     -58.887-139.134 304.709  1.00 99.47           C  
ANISOU 1044  CA  ALA A 236    10050  11025  16718   1973    270   1278       C  
ATOM   1045  C   ALA A 236     -57.789-139.896 305.439  1.00 97.38           C  
ANISOU 1045  C   ALA A 236    10040  10709  16251   1770    320   1041       C  
ATOM   1046  O   ALA A 236     -57.715-141.128 305.359  1.00 97.84           O  
ANISOU 1046  O   ALA A 236    10165  10954  16056   1587    221    985       O  
ATOM   1047  CB  ALA A 236     -58.338-138.476 303.443  1.00 96.56           C  
ANISOU 1047  CB  ALA A 236     9720  10584  16386   2057    160   1563       C  
ATOM   1048  N   PHE A 237     -56.922-139.178 306.159  1.00 95.01           N  
ANISOU 1048  N   PHE A 237     9877  10150  16074   1798    467    900       N  
ATOM   1049  CA  PHE A 237     -55.846-139.845 306.886  1.00 98.78           C  
ANISOU 1049  CA  PHE A 237    10577  10595  16362   1618    509    689       C  
ATOM   1050  C   PHE A 237     -56.395-140.740 307.990  1.00100.44           C  
ANISOU 1050  C   PHE A 237    10749  10963  16448   1487    561    499       C  
ATOM   1051  O   PHE A 237     -55.888-141.847 308.209  1.00 99.82           O  
ANISOU 1051  O   PHE A 237    10808  10978  16140   1306    491    428       O  
ATOM   1052  CB  PHE A 237     -54.875-138.815 307.462  1.00104.67           C  
ANISOU 1052  CB  PHE A 237    11444  11058  17269   1668    660    567       C  
ATOM   1053  CG  PHE A 237     -53.769-138.431 306.521  1.00106.24           C  
ANISOU 1053  CG  PHE A 237    11785  11137  17445   1665    590    711       C  
ATOM   1054  CD1 PHE A 237     -52.670-139.258 306.352  1.00105.03           C  
ANISOU 1054  CD1 PHE A 237    11815  11057  17034   1507    515    651       C  
ATOM   1055  CD2 PHE A 237     -53.825-137.243 305.811  1.00107.13           C  
ANISOU 1055  CD2 PHE A 237    11835  11067  17802   1820    597    916       C  
ATOM   1056  CE1 PHE A 237     -51.648-138.909 305.487  1.00106.85           C  
ANISOU 1056  CE1 PHE A 237    12151  11224  17222   1492    461    770       C  
ATOM   1057  CE2 PHE A 237     -52.807-136.887 304.945  1.00108.06           C  
ANISOU 1057  CE2 PHE A 237    12073  11108  17878   1787    537   1072       C  
ATOM   1058  CZ  PHE A 237     -51.717-137.721 304.783  1.00109.22           C  
ANISOU 1058  CZ  PHE A 237    12390  11372  17739   1617    475    986       C  
ATOM   1059  N   CYS A 238     -57.431-140.279 308.697  1.00101.08           N  
ANISOU 1059  N   CYS A 238    10636  11083  16688   1574    683    421       N  
ATOM   1060  CA  CYS A 238     -58.050-141.109 309.725  1.00100.90           C  
ANISOU 1060  CA  CYS A 238    10546  11264  16529   1427    737    269       C  
ATOM   1061  C   CYS A 238     -58.597-142.399 309.127  1.00101.29           C  
ANISOU 1061  C   CYS A 238    10564  11548  16374   1280    557    396       C  
ATOM   1062  O   CYS A 238     -58.351-143.492 309.650  1.00101.06           O  
ANISOU 1062  O   CYS A 238    10642  11613  16144   1072    517    325       O  
ATOM   1063  CB  CYS A 238     -59.160-140.332 310.434  1.00107.14           C  
ANISOU 1063  CB  CYS A 238    11084  12100  17525   1563    900    162       C  
ATOM   1064  SG  CYS A 238     -58.610-138.943 311.450  1.00113.05           S  
ANISOU 1064  SG  CYS A 238    11851  12585  18517   1696   1145    -98       S  
ATOM   1065  N   LEU A 239     -59.338-142.291 308.020  1.00102.01           N  
ANISOU 1065  N   LEU A 239    10503  11733  16523   1377    439    590       N  
ATOM   1066  CA  LEU A 239     -59.863-143.487 307.370  1.00 98.74           C  
ANISOU 1066  CA  LEU A 239    10048  11548  15922   1225    263    684       C  
ATOM   1067  C   LEU A 239     -58.741-144.336 306.786  1.00101.17           C  
ANISOU 1067  C   LEU A 239    10599  11802  16039   1087    124    690       C  
ATOM   1068  O   LEU A 239     -58.825-145.570 306.787  1.00106.71           O  
ANISOU 1068  O   LEU A 239    11354  12615  16575    894     19    654       O  
ATOM   1069  CB  LEU A 239     -60.871-143.100 306.288  1.00 89.60           C  
ANISOU 1069  CB  LEU A 239     8653  10538  14854   1364    163    887       C  
ATOM   1070  CG  LEU A 239     -62.191-142.523 306.807  1.00 85.51           C  
ANISOU 1070  CG  LEU A 239     7840  10137  14512   1491    270    876       C  
ATOM   1071  CD1 LEU A 239     -63.186-142.304 305.673  1.00 89.81           C  
ANISOU 1071  CD1 LEU A 239     8136  10872  15114   1613    134   1102       C  
ATOM   1072  CD2 LEU A 239     -62.782-143.429 307.876  1.00 76.01           C  
ANISOU 1072  CD2 LEU A 239     6581   9117  13184   1285    336    716       C  
ATOM   1073  N   MET A 240     -57.680-143.696 306.290  1.00 97.45           N  
ANISOU 1073  N   MET A 240    10269  11157  15601   1180    124    724       N  
ATOM   1074  CA  MET A 240     -56.532-144.452 305.800  1.00 93.62           C  
ANISOU 1074  CA  MET A 240     9997  10634  14938   1065     13    691       C  
ATOM   1075  C   MET A 240     -55.901-145.272 306.920  1.00 93.62           C  
ANISOU 1075  C   MET A 240    10166  10568  14838    907     55    511       C  
ATOM   1076  O   MET A 240     -55.458-146.405 306.697  1.00 87.75           O  
ANISOU 1076  O   MET A 240     9541   9855  13946    767    -71    468       O  
ATOM   1077  CB  MET A 240     -55.512-143.499 305.174  1.00 90.62           C  
ANISOU 1077  CB  MET A 240     9713  10102  14616   1185     32    761       C  
ATOM   1078  CG  MET A 240     -54.357-144.174 304.447  1.00 89.49           C  
ANISOU 1078  CG  MET A 240     9744   9974  14285   1092    -87    733       C  
ATOM   1079  SD  MET A 240     -52.999-144.652 305.534  1.00 94.12           S  
ANISOU 1079  SD  MET A 240    10572  10395  14795    987    -17    509       S  
ATOM   1080  CE  MET A 240     -52.592-143.078 306.282  1.00 93.64           C  
ANISOU 1080  CE  MET A 240    10523  10117  14941   1118    190    485       C  
ATOM   1081  N   TRP A 241     -55.864-144.721 308.136  1.00 99.70           N  
ANISOU 1081  N   TRP A 241    10938  11254  15690    928    225    401       N  
ATOM   1082  CA  TRP A 241     -55.292-145.453 309.261  1.00100.06           C  
ANISOU 1082  CA  TRP A 241    11122  11277  15618    771    261    263       C  
ATOM   1083  C   TRP A 241     -56.204-146.589 309.710  1.00 93.92           C  
ANISOU 1083  C   TRP A 241    10272  10668  14746    596    201    276       C  
ATOM   1084  O   TRP A 241     -55.729-147.696 309.988  1.00 86.57           O  
ANISOU 1084  O   TRP A 241     9479   9723  13690    435    107    253       O  
ATOM   1085  CB  TRP A 241     -55.011-144.501 310.424  1.00107.74           C  
ANISOU 1085  CB  TRP A 241    12094  12165  16677    825    464    125       C  
ATOM   1086  CG  TRP A 241     -53.674-143.838 310.332  1.00110.32           C  
ANISOU 1086  CG  TRP A 241    12581  12306  17030    889    505     64       C  
ATOM   1087  CD1 TRP A 241     -53.375-142.680 309.676  1.00111.38           C  
ANISOU 1087  CD1 TRP A 241    12700  12294  17324   1048    552    112       C  
ATOM   1088  CD2 TRP A 241     -52.447-144.296 310.915  1.00109.15           C  
ANISOU 1088  CD2 TRP A 241    12620  12104  16746    785    496    -41       C  
ATOM   1089  NE1 TRP A 241     -52.040-142.388 309.814  1.00111.00           N  
ANISOU 1089  NE1 TRP A 241    12819  12114  17243   1030    583     30       N  
ATOM   1090  CE2 TRP A 241     -51.448-143.365 310.570  1.00109.89           C  
ANISOU 1090  CE2 TRP A 241    12797  12039  16916    879    548    -74       C  
ATOM   1091  CE3 TRP A 241     -52.098-145.403 311.695  1.00108.15           C  
ANISOU 1091  CE3 TRP A 241    12591  12050  16451    620    440    -89       C  
ATOM   1092  CZ2 TRP A 241     -50.123-143.506 310.979  1.00109.40           C  
ANISOU 1092  CZ2 TRP A 241    12897  11918  16753    814    551   -178       C  
ATOM   1093  CZ3 TRP A 241     -50.782-145.542 312.100  1.00107.96           C  
ANISOU 1093  CZ3 TRP A 241    12729  11955  16336    577    433   -174       C  
ATOM   1094  CH2 TRP A 241     -49.811-144.598 311.741  1.00107.76           C  
ANISOU 1094  CH2 TRP A 241    12768  11799  16375    675    491   -231       C  
ATOM   1095  N   THR A 242     -57.513-146.336 309.792  1.00 99.72           N  
ANISOU 1095  N   THR A 242    10783  11555  15553    622    251    320       N  
ATOM   1096  CA  THR A 242     -58.439-147.380 310.222  1.00102.90           C  
ANISOU 1096  CA  THR A 242    11095  12139  15865    428    203    343       C  
ATOM   1097  C   THR A 242     -58.447-148.543 309.238  1.00106.17           C  
ANISOU 1097  C   THR A 242    11573  12576  16192    306    -12    419       C  
ATOM   1098  O   THR A 242     -58.386-149.711 309.640  1.00110.97           O  
ANISOU 1098  O   THR A 242    12270  13186  16706    100    -94    413       O  
ATOM   1099  CB  THR A 242     -59.848-146.807 310.387  1.00100.14           C  
ANISOU 1099  CB  THR A 242    10457  11978  15613    496    299    365       C  
ATOM   1100  OG1 THR A 242     -60.285-146.241 309.145  1.00101.62           O  
ANISOU 1100  OG1 THR A 242    10519  12184  15907    669    224    479       O  
ATOM   1101  CG2 THR A 242     -59.866-145.733 311.464  1.00100.35           C  
ANISOU 1101  CG2 THR A 242    10408  11984  15735    606    524    230       C  
ATOM   1102  N   ILE A 243     -58.516-148.240 307.939  1.00 98.73           N  
ANISOU 1102  N   ILE A 243    10579  11651  15284    423   -108    492       N  
ATOM   1103  CA  ILE A 243     -58.473-149.294 306.929  1.00 89.58           C  
ANISOU 1103  CA  ILE A 243     9467  10537  14033    310   -307    515       C  
ATOM   1104  C   ILE A 243     -57.159-150.059 307.015  1.00 90.43           C  
ANISOU 1104  C   ILE A 243     9834  10460  14066    231   -382    423       C  
ATOM   1105  O   ILE A 243     -57.132-151.292 306.907  1.00 93.63           O  
ANISOU 1105  O   ILE A 243    10314  10845  14417     61   -514    385       O  
ATOM   1106  CB  ILE A 243     -58.694-148.701 305.526  1.00 87.31           C  
ANISOU 1106  CB  ILE A 243     9063  10352  13759    455   -387    611       C  
ATOM   1107  CG1 ILE A 243     -60.119-148.159 305.394  1.00 86.61           C  
ANISOU 1107  CG1 ILE A 243     8688  10469  13749    523   -353    719       C  
ATOM   1108  CG2 ILE A 243     -58.420-149.743 304.451  1.00 84.60           C  
ANISOU 1108  CG2 ILE A 243     8784  10066  13293    338   -582    576       C  
ATOM   1109  CD1 ILE A 243     -60.392-147.490 304.064  1.00 89.61           C  
ANISOU 1109  CD1 ILE A 243     8929  10975  14144    676   -438    864       C  
ATOM   1110  N   ALA A 244     -56.049-149.345 307.220  1.00 92.61           N  
ANISOU 1110  N   ALA A 244    10241  10590  14358    354   -301    379       N  
ATOM   1111  CA  ALA A 244     -54.765-150.017 307.386  1.00 95.59           C  
ANISOU 1111  CA  ALA A 244    10840  10810  14669    300   -365    286       C  
ATOM   1112  C   ALA A 244     -54.783-150.946 308.594  1.00 99.99           C  
ANISOU 1112  C   ALA A 244    11478  11315  15197    126   -368    263       C  
ATOM   1113  O   ALA A 244     -54.247-152.059 308.539  1.00104.90           O  
ANISOU 1113  O   ALA A 244    12234  11836  15788     21   -500    224       O  
ATOM   1114  CB  ALA A 244     -53.641-148.989 307.514  1.00 91.61           C  
ANISOU 1114  CB  ALA A 244    10432  10190  14185    447   -259    245       C  
ATOM   1115  N   ILE A 245     -55.404-150.512 309.692  1.00 98.52           N  
ANISOU 1115  N   ILE A 245    11202  11204  15026     92   -225    288       N  
ATOM   1116  CA  ILE A 245     -55.512-151.378 310.861  1.00100.09           C  
ANISOU 1116  CA  ILE A 245    11453  11409  15166   -102   -227    308       C  
ATOM   1117  C   ILE A 245     -56.477-152.525 310.586  1.00102.41           C  
ANISOU 1117  C   ILE A 245    11681  11771  15458   -292   -359    381       C  
ATOM   1118  O   ILE A 245     -56.195-153.681 310.921  1.00102.41           O  
ANISOU 1118  O   ILE A 245    11803  11668  15439   -459   -475    412       O  
ATOM   1119  CB  ILE A 245     -55.936-150.565 312.098  1.00100.08           C  
ANISOU 1119  CB  ILE A 245    11345  11533  15149   -103    -24    289       C  
ATOM   1120  CG1 ILE A 245     -54.856-149.544 312.460  1.00 98.98           C  
ANISOU 1120  CG1 ILE A 245    11295  11297  15018     47     97    186       C  
ATOM   1121  CG2 ILE A 245     -56.213-151.491 313.275  1.00 99.00           C  
ANISOU 1121  CG2 ILE A 245    11227  11477  14914   -340    -31    352       C  
ATOM   1122  CD1 ILE A 245     -55.209-148.682 313.651  1.00 98.50           C  
ANISOU 1122  CD1 ILE A 245    11121  11358  14945     53    308    107       C  
ATOM   1123  N   VAL A 246     -57.618-152.228 309.959  1.00101.74           N  
ANISOU 1123  N   VAL A 246    11397  11851  15410   -273   -352    417       N  
ATOM   1124  CA  VAL A 246     -58.636-153.251 309.726  1.00 97.15           C  
ANISOU 1124  CA  VAL A 246    10722  11367  14825   -477   -465    475       C  
ATOM   1125  C   VAL A 246     -58.069-154.394 308.892  1.00 93.02           C  
ANISOU 1125  C   VAL A 246    10352  10678  14314   -561   -671    429       C  
ATOM   1126  O   VAL A 246     -58.247-155.572 309.221  1.00 95.30           O  
ANISOU 1126  O   VAL A 246    10705  10887  14618   -778   -776    461       O  
ATOM   1127  CB  VAL A 246     -59.880-152.629 309.065  1.00 99.87           C  
ANISOU 1127  CB  VAL A 246    10802  11943  15200   -409   -431    511       C  
ATOM   1128  CG1 VAL A 246     -60.727-153.703 308.404  1.00102.77           C  
ANISOU 1128  CG1 VAL A 246    11086  12404  15559   -607   -591    537       C  
ATOM   1129  CG2 VAL A 246     -60.700-151.873 310.097  1.00101.05           C  
ANISOU 1129  CG2 VAL A 246    10766  12270  15357   -393   -240    536       C  
ATOM   1130  N   ILE A 247     -57.365-154.062 307.807  1.00 92.13           N  
ANISOU 1130  N   ILE A 247    10294  10509  14202   -397   -729    349       N  
ATOM   1131  CA  ILE A 247     -56.827-155.099 306.928  1.00100.12           C  
ANISOU 1131  CA  ILE A 247    11423  11395  15224   -458   -914    250       C  
ATOM   1132  C   ILE A 247     -55.800-155.951 307.665  1.00104.74           C  
ANISOU 1132  C   ILE A 247    12229  11723  15844   -527   -973    218       C  
ATOM   1133  O   ILE A 247     -55.785-157.182 307.536  1.00109.88           O  
ANISOU 1133  O   ILE A 247    12959  12230  16559   -680  -1122    179       O  
ATOM   1134  CB  ILE A 247     -56.230-154.468 305.657  1.00100.24           C  
ANISOU 1134  CB  ILE A 247    11428  11463  15195   -269   -943    170       C  
ATOM   1135  CG1 ILE A 247     -57.309-153.720 304.875  1.00 99.96           C  
ANISOU 1135  CG1 ILE A 247    11158  11691  15130   -210   -919    247       C  
ATOM   1136  CG2 ILE A 247     -55.591-155.533 304.779  1.00103.69           C  
ANISOU 1136  CG2 ILE A 247    11973  11794  15630   -325  -1118     11       C  
ATOM   1137  CD1 ILE A 247     -56.794-153.069 303.613  1.00100.38           C  
ANISOU 1137  CD1 ILE A 247    11183  11840  15116    -47   -954    222       C  
ATOM   1138  N   ALA A 248     -54.932-155.315 308.454  1.00100.85           N  
ANISOU 1138  N   ALA A 248    11832  11162  15324   -416   -863    233       N  
ATOM   1139  CA  ALA A 248     -53.874-156.045 309.140  1.00 98.78           C  
ANISOU 1139  CA  ALA A 248    11764  10683  15086   -453   -928    220       C  
ATOM   1140  C   ALA A 248     -54.371-156.818 310.355  1.00100.92           C  
ANISOU 1140  C   ALA A 248    12056  10918  15370   -671   -941    365       C  
ATOM   1141  O   ALA A 248     -53.674-157.725 310.820  1.00109.63           O  
ANISOU 1141  O   ALA A 248    13311  11819  16524   -740  -1051    397       O  
ATOM   1142  CB  ALA A 248     -52.761-155.087 309.562  1.00 98.97           C  
ANISOU 1142  CB  ALA A 248    11862  10686  15054   -278   -812    183       C  
ATOM   1143  N   VAL A 249     -55.547-156.479 310.886  1.00 98.35           N  
ANISOU 1143  N   VAL A 249    11571  10795  15003   -780   -836    467       N  
ATOM   1144  CA  VAL A 249     -56.112-157.239 311.997  1.00102.14           C  
ANISOU 1144  CA  VAL A 249    12046  11294  15467  -1027   -846    625       C  
ATOM   1145  C   VAL A 249     -56.895-158.456 311.509  1.00103.76           C  
ANISOU 1145  C   VAL A 249    12231  11422  15769  -1245  -1009    667       C  
ATOM   1146  O   VAL A 249     -57.072-159.416 312.274  1.00110.66           O  
ANISOU 1146  O   VAL A 249    13166  12202  16676  -1471  -1083    813       O  
ATOM   1147  CB  VAL A 249     -56.975-156.312 312.879  1.00108.04           C  
ANISOU 1147  CB  VAL A 249    12610  12331  16109  -1056   -640    687       C  
ATOM   1148  CG1 VAL A 249     -57.729-157.087 313.949  1.00109.97           C  
ANISOU 1148  CG1 VAL A 249    12806  12676  16303  -1348   -641    862       C  
ATOM   1149  CG2 VAL A 249     -56.099-155.262 313.547  1.00113.01           C  
ANISOU 1149  CG2 VAL A 249    13285  12992  16661   -885   -489    627       C  
ATOM   1150  N   LEU A 250     -57.325-158.463 310.246  1.00 98.12           N  
ANISOU 1150  N   LEU A 250    11436  10745  15102  -1196  -1075    546       N  
ATOM   1151  CA  LEU A 250     -58.045-159.605 309.682  1.00 98.19           C  
ANISOU 1151  CA  LEU A 250    11417  10684  15207  -1411  -1233    537       C  
ATOM   1152  C   LEU A 250     -57.383-160.953 309.952  1.00103.90           C  
ANISOU 1152  C   LEU A 250    12346  11060  16072  -1549  -1407    561       C  
ATOM   1153  O   LEU A 250     -58.098-161.890 310.340  1.00105.79           O  
ANISOU 1153  O   LEU A 250    12572  11234  16388  -1821  -1486    680       O  
ATOM   1154  CB  LEU A 250     -58.241-159.393 308.174  1.00 92.61           C  
ANISOU 1154  CB  LEU A 250    10620  10064  14505  -1300  -1297    357       C  
ATOM   1155  CG  LEU A 250     -59.196-158.275 307.760  1.00 89.44           C  
ANISOU 1155  CG  LEU A 250     9975  10003  14005  -1206  -1174    377       C  
ATOM   1156  CD1 LEU A 250     -59.367-158.240 306.249  1.00 91.24           C  
ANISOU 1156  CD1 LEU A 250    10114  10336  14217  -1133  -1273    233       C  
ATOM   1157  CD2 LEU A 250     -60.539-158.442 308.452  1.00 92.77           C  
ANISOU 1157  CD2 LEU A 250    10217  10621  14410  -1425  -1117    516       C  
ATOM   1158  N   PRO A 251     -56.063-161.132 309.776  1.00103.11           N  
ANISOU 1158  N   PRO A 251    12426  10721  16031  -1382  -1478    463       N  
ATOM   1159  CA  PRO A 251     -55.473-162.445 310.102  1.00105.02           C  
ANISOU 1159  CA  PRO A 251    12849  10604  16450  -1497  -1654    504       C  
ATOM   1160  C   PRO A 251     -55.681-162.857 311.548  1.00106.03           C  
ANISOU 1160  C   PRO A 251    13022  10695  16569  -1700  -1641    794       C  
ATOM   1161  O   PRO A 251     -55.876-164.046 311.828  1.00114.67           O  
ANISOU 1161  O   PRO A 251    14198  11547  17826  -1916  -1790    912       O  
ATOM   1162  CB  PRO A 251     -53.987-162.252 309.773  1.00102.17           C  
ANISOU 1162  CB  PRO A 251    12627  10080  16111  -1230  -1688    351       C  
ATOM   1163  CG  PRO A 251     -53.961-161.165 308.777  1.00 99.96           C  
ANISOU 1163  CG  PRO A 251    12237  10039  15703  -1032  -1585    172       C  
ATOM   1164  CD  PRO A 251     -55.061-160.231 309.175  1.00100.45           C  
ANISOU 1164  CD  PRO A 251    12123  10417  15625  -1090  -1419    304       C  
ATOM   1165  N   LEU A 252     -55.647-161.904 312.479  1.00102.07           N  
ANISOU 1165  N   LEU A 252    12465  10435  15882  -1648  -1467    913       N  
ATOM   1166  CA  LEU A 252     -55.880-162.234 313.880  1.00103.29           C  
ANISOU 1166  CA  LEU A 252    12633  10641  15972  -1860  -1440   1190       C  
ATOM   1167  C   LEU A 252     -57.334-162.620 314.120  1.00107.69           C  
ANISOU 1167  C   LEU A 252    13037  11366  16512  -2162  -1419   1329       C  
ATOM   1168  O   LEU A 252     -57.621-163.515 314.924  1.00 94.15           O  
ANISOU 1168  O   LEU A 252    11366   9568  14838  -2430  -1498   1571       O  
ATOM   1169  CB  LEU A 252     -55.477-161.053 314.763  1.00110.89           C  
ANISOU 1169  CB  LEU A 252    13549  11864  16720  -1729  -1244   1219       C  
ATOM   1170  CG  LEU A 252     -55.690-161.198 316.270  1.00117.52           C  
ANISOU 1170  CG  LEU A 252    14368  12868  17417  -1941  -1183   1483       C  
ATOM   1171  CD1 LEU A 252     -54.991-162.436 316.786  1.00125.32           C  
ANISOU 1171  CD1 LEU A 252    15542  13549  18525  -2064  -1387   1693       C  
ATOM   1172  CD2 LEU A 252     -55.195-159.960 317.000  1.00114.31           C  
ANISOU 1172  CD2 LEU A 252    13909  12720  16802  -1786   -985   1423       C  
ATOM   1173  N   LEU A 253     -58.265-161.959 313.430  1.00131.19           N  
ANISOU 1173  N   LEU A 253    15823  14594  19431  -2131  -1320   1198       N  
ATOM   1174  CA  LEU A 253     -59.678-162.293 313.573  1.00145.45           C  
ANISOU 1174  CA  LEU A 253    17449  16598  21216  -2412  -1298   1305       C  
ATOM   1175  C   LEU A 253     -59.994-163.629 312.911  1.00147.33           C  
ANISOU 1175  C   LEU A 253    17756  16556  21666  -2627  -1511   1299       C  
ATOM   1176  O   LEU A 253     -60.591-164.516 313.533  1.00151.17           O  
ANISOU 1176  O   LEU A 253    18240  16992  22207  -2947  -1576   1507       O  
ATOM   1177  CB  LEU A 253     -60.536-161.175 312.977  1.00153.28           C  
ANISOU 1177  CB  LEU A 253    18200  17938  22102  -2281  -1145   1163       C  
ATOM   1178  CG  LEU A 253     -62.008-161.482 312.696  1.00162.78           C  
ANISOU 1178  CG  LEU A 253    19181  19363  23306  -2519  -1147   1198       C  
ATOM   1179  CD1 LEU A 253     -62.760-161.778 313.985  1.00167.56           C  
ANISOU 1179  CD1 LEU A 253    19685  20168  23810  -2818  -1065   1435       C  
ATOM   1180  CD2 LEU A 253     -62.658-160.333 311.938  1.00163.31           C  
ANISOU 1180  CD2 LEU A 253    19018  19734  23299  -2312  -1027   1049       C  
ATOM   1181  N   GLY A 254     -59.607-163.783 311.657  1.00139.69           N  
ANISOU 1181  N   GLY A 254    16842  15415  20818  -2471  -1617   1055       N  
ATOM   1182  CA  GLY A 254     -59.795-165.022 310.925  1.00136.65           C  
ANISOU 1182  CA  GLY A 254    16525  14742  20654  -2648  -1819    970       C  
ATOM   1183  C   GLY A 254     -58.880-164.996 309.726  1.00133.50           C  
ANISOU 1183  C   GLY A 254    16220  14164  20341  -2386  -1907    669       C  
ATOM   1184  O   GLY A 254     -57.772-164.465 309.798  1.00134.99           O  
ANISOU 1184  O   GLY A 254    16515  14290  20485  -2121  -1868    613       O  
ATOM   1185  N   TRP A 255     -59.342-165.582 308.618  1.00130.88           N  
ANISOU 1185  N   TRP A 255    15834  13779  20117  -2476  -2023    461       N  
ATOM   1186  CA  TRP A 255     -58.668-165.460 307.318  1.00126.35           C  
ANISOU 1186  CA  TRP A 255    15285  13159  19564  -2249  -2087    137       C  
ATOM   1187  C   TRP A 255     -57.161-165.698 307.426  1.00131.56           C  
ANISOU 1187  C   TRP A 255    16163  13491  20332  -2030  -2151     57       C  
ATOM   1188  O   TRP A 255     -56.351-164.969 306.849  1.00128.84           O  
ANISOU 1188  O   TRP A 255    15828  13240  19886  -1754  -2098   -107       O  
ATOM   1189  CB  TRP A 255     -58.956-164.098 306.686  1.00116.01           C  
ANISOU 1189  CB  TRP A 255    13791  12273  18015  -2043  -1939     62       C  
ATOM   1190  CG  TRP A 255     -58.664-164.034 305.219  1.00118.37           C  
ANISOU 1190  CG  TRP A 255    14045  12642  18289  -1905  -2010   -243       C  
ATOM   1191  CD1 TRP A 255     -58.165-165.032 304.433  1.00125.14           C  
ANISOU 1191  CD1 TRP A 255    14999  13244  19306  -1939  -2175   -503       C  
ATOM   1192  CD2 TRP A 255     -58.859-162.908 304.357  1.00119.40           C  
ANISOU 1192  CD2 TRP A 255    14008  13141  18217  -1720  -1921   -319       C  
ATOM   1193  NE1 TRP A 255     -58.035-164.597 303.137  1.00127.15           N  
ANISOU 1193  NE1 TRP A 255    15147  13734  19431  -1799  -2184   -751       N  
ATOM   1194  CE2 TRP A 255     -58.456-163.296 303.064  1.00123.88           C  
ANISOU 1194  CE2 TRP A 255    14573  13702  18792  -1668  -2037   -615       C  
ATOM   1195  CE3 TRP A 255     -59.337-161.608 304.552  1.00118.12           C  
ANISOU 1195  CE3 TRP A 255    13689  13309  17882  -1591  -1758   -165       C  
ATOM   1196  CZ2 TRP A 255     -58.517-162.433 301.972  1.00124.56           C  
ANISOU 1196  CZ2 TRP A 255    14508  14134  18685  -1511  -2001   -719       C  
ATOM   1197  CZ3 TRP A 255     -59.395-160.753 303.469  1.00119.21           C  
ANISOU 1197  CZ3 TRP A 255    13688  13731  17875  -1417  -1730   -258       C  
ATOM   1198  CH2 TRP A 255     -58.987-161.168 302.195  1.00123.05           C  
ANISOU 1198  CH2 TRP A 255    14177  14237  18340  -1388  -1854   -512       C  
ATOM   1199  N   ASN A 256     -56.782-166.715 308.191  1.00141.38           N  
ANISOU 1199  N   ASN A 256    17574  14360  21786  -2157  -2268    195       N  
ATOM   1200  CA  ASN A 256     -55.390-167.122 308.328  1.00142.47           C  
ANISOU 1200  CA  ASN A 256    17906  14154  22072  -1961  -2361    130       C  
ATOM   1201  C   ASN A 256     -55.247-168.571 307.875  1.00148.34           C  
ANISOU 1201  C   ASN A 256    18760  14447  23156  -2087  -2580    -21       C  
ATOM   1202  O   ASN A 256     -56.231-169.246 307.563  1.00145.84           O  
ANISOU 1202  O   ASN A 256    18382  14080  22952  -2355  -2653    -52       O  
ATOM   1203  CB  ASN A 256     -54.895-166.926 309.766  1.00139.06           C  
ANISOU 1203  CB  ASN A 256    17571  13677  21590  -1948  -2309    463       C  
ATOM   1204  CG  ASN A 256     -55.704-167.714 310.777  1.00136.94           C  
ANISOU 1204  CG  ASN A 256    17320  13298  21414  -2288  -2365    793       C  
ATOM   1205  OD1 ASN A 256     -55.486-168.909 310.968  1.00145.55           O  
ANISOU 1205  OD1 ASN A 256    18544  13977  22782  -2419  -2546    868       O  
ATOM   1206  ND2 ASN A 256     -56.633-167.040 311.446  1.00131.20           N  
ANISOU 1206  ND2 ASN A 256    16450  12940  20462  -2434  -2207    997       N  
ATOM   1207  N   CYS A 257     -54.003-169.048 307.835  1.00156.48           N  
ANISOU 1207  N   CYS A 257    19945  15140  24368  -1888  -2686   -134       N  
ATOM   1208  CA  CYS A 257     -53.743-170.374 307.293  1.00163.75           C  
ANISOU 1208  CA  CYS A 257    20955  15727  25536  -1897  -2828   -339       C  
ATOM   1209  C   CYS A 257     -54.126-171.496 308.249  1.00165.07           C  
ANISOU 1209  C   CYS A 257    21222  15650  25848  -2109  -2891    -30       C  
ATOM   1210  O   CYS A 257     -54.334-172.627 307.797  1.00170.11           O  
ANISOU 1210  O   CYS A 257    21901  16062  26673  -2196  -2978   -172       O  
ATOM   1211  CB  CYS A 257     -52.269-170.525 306.904  1.00171.31           C  
ANISOU 1211  CB  CYS A 257    22000  16555  26534  -1545  -2852   -570       C  
ATOM   1212  SG  CYS A 257     -51.995-171.927 305.790  1.00182.23           S  
ANISOU 1212  SG  CYS A 257    23413  17681  28144  -1497  -2965   -972       S  
ATOM   1213  N   GLU A 258     -54.224-171.220 309.549  1.00155.81           N  
ANISOU 1213  N   GLU A 258    20083  14525  24591  -2205  -2849    384       N  
ATOM   1214  CA  GLU A 258     -54.589-172.260 310.503  1.00152.91           C  
ANISOU 1214  CA  GLU A 258    19800  13961  24339  -2424  -2915    713       C  
ATOM   1215  C   GLU A 258     -56.077-172.275 310.822  1.00151.50           C  
ANISOU 1215  C   GLU A 258    19510  13958  24095  -2810  -2871    914       C  
ATOM   1216  O   GLU A 258     -56.638-173.350 311.062  1.00158.47           O  
ANISOU 1216  O   GLU A 258    20436  14658  25118  -3036  -2940   1037       O  
ATOM   1217  CB  GLU A 258     -53.794-172.096 311.802  1.00153.58           C  
ANISOU 1217  CB  GLU A 258    19976  14024  24354  -2331  -2912   1068       C  
ATOM   1218  CG  GLU A 258     -52.294-172.282 311.648  1.00154.14           C  
ANISOU 1218  CG  GLU A 258    20146  13911  24508  -1973  -2973    917       C  
ATOM   1219  CD  GLU A 258     -51.581-172.400 312.983  1.00154.32           C  
ANISOU 1219  CD  GLU A 258    20254  13887  24496  -1931  -3011   1297       C  
ATOM   1220  OE1 GLU A 258     -52.243-172.241 314.031  1.00153.60           O  
ANISOU 1220  OE1 GLU A 258    20143  13935  24283  -2181  -2977   1676       O  
ATOM   1221  OE2 GLU A 258     -50.359-172.658 312.983  1.00154.31           O  
ANISOU 1221  OE2 GLU A 258    20318  13736  24576  -1659  -3077   1217       O  
ATOM   1222  N   LYS A 259     -56.728-171.109 310.831  1.00145.76           N  
ANISOU 1222  N   LYS A 259    18625  13590  23166  -2895  -2756    950       N  
ATOM   1223  CA  LYS A 259     -58.160-171.068 311.106  1.00140.81           C  
ANISOU 1223  CA  LYS A 259    17845  13199  22457  -3258  -2702   1125       C  
ATOM   1224  C   LYS A 259     -58.947-171.774 310.010  1.00136.38           C  
ANISOU 1224  C   LYS A 259    17216  12577  22024  -3412  -2770    843       C  
ATOM   1225  O   LYS A 259     -59.953-172.439 310.283  1.00142.00           O  
ANISOU 1225  O   LYS A 259    17879  13307  22767  -3729  -2779    987       O  
ATOM   1226  CB  LYS A 259     -58.626-169.620 311.250  1.00138.23           C  
ANISOU 1226  CB  LYS A 259    17326  13372  21823  -3212  -2512   1161       C  
ATOM   1227  CG  LYS A 259     -59.826-169.436 312.162  1.00140.13           C  
ANISOU 1227  CG  LYS A 259    17414  13943  21888  -3527  -2399   1474       C  
ATOM   1228  CD  LYS A 259     -59.470-169.778 313.599  1.00141.25           C  
ANISOU 1228  CD  LYS A 259    17668  13979  22022  -3658  -2416   1885       C  
ATOM   1229  CE  LYS A 259     -60.615-169.462 314.544  1.00144.04           C  
ANISOU 1229  CE  LYS A 259    17838  14753  22137  -3958  -2271   2175       C  
ATOM   1230  NZ  LYS A 259     -60.265-169.776 315.956  1.00147.44           N  
ANISOU 1230  NZ  LYS A 259    18362  15148  22511  -4107  -2286   2589       N  
ATOM   1231  N   LEU A 260     -58.501-171.642 308.766  1.00130.44           N  
ANISOU 1231  N   LEU A 260    16451  11781  21330  -3205  -2813    431       N  
ATOM   1232  CA  LEU A 260     -59.110-172.299 307.623  1.00138.42           C  
ANISOU 1232  CA  LEU A 260    17394  12755  22445  -3330  -2882    103       C  
ATOM   1233  C   LEU A 260     -58.150-173.346 307.077  1.00145.61           C  
ANISOU 1233  C   LEU A 260    18480  13274  23570  -3140  -2981   -159       C  
ATOM   1234  O   LEU A 260     -56.929-173.204 307.188  1.00145.11           O  
ANISOU 1234  O   LEU A 260    18533  13073  23531  -2832  -2990   -201       O  
ATOM   1235  CB  LEU A 260     -59.448-171.295 306.515  1.00140.77           C  
ANISOU 1235  CB  LEU A 260    17483  13397  22606  -3269  -2857   -192       C  
ATOM   1236  CG  LEU A 260     -60.605-170.297 306.614  1.00147.40           C  
ANISOU 1236  CG  LEU A 260    18077  14787  23141  -3378  -2701    -50       C  
ATOM   1237  CD1 LEU A 260     -60.566-169.467 307.888  1.00149.21           C  
ANISOU 1237  CD1 LEU A 260    18302  15220  23169  -3316  -2540    327       C  
ATOM   1238  CD2 LEU A 260     -60.565-169.386 305.397  1.00146.18           C  
ANISOU 1238  CD2 LEU A 260    17770  15014  22759  -3136  -2630   -359       C  
ATOM   1239  N   GLN A 261     -58.703-174.406 306.493  1.00150.53           N  
ANISOU 1239  N   GLN A 261    19109  13734  24353  -3329  -3051   -345       N  
ATOM   1240  CA  GLN A 261     -57.862-175.331 305.746  1.00151.92           C  
ANISOU 1240  CA  GLN A 261    19404  13585  24734  -3146  -3134   -682       C  
ATOM   1241  C   GLN A 261     -57.286-174.571 304.558  1.00149.36           C  
ANISOU 1241  C   GLN A 261    18988  13477  24285  -2889  -3117  -1097       C  
ATOM   1242  O   GLN A 261     -57.958-174.410 303.534  1.00149.52           O  
ANISOU 1242  O   GLN A 261    18855  13729  24226  -3007  -3123  -1392       O  
ATOM   1243  CB  GLN A 261     -58.656-176.562 305.299  1.00155.33           C  
ANISOU 1243  CB  GLN A 261    19843  13818  25356  -3429  -3201   -831       C  
ATOM   1244  CG  GLN A 261     -57.820-177.637 304.614  1.00158.45           C  
ANISOU 1244  CG  GLN A 261    20362  13841  26002  -3261  -3284  -1170       C  
ATOM   1245  CD  GLN A 261     -58.615-178.897 304.306  1.00163.64           C  
ANISOU 1245  CD  GLN A 261    21045  14254  26876  -3567  -3346  -1289       C  
ATOM   1246  OE1 GLN A 261     -59.561-179.241 305.015  1.00166.29           O  
ANISOU 1246  OE1 GLN A 261    21378  14563  27243  -3887  -3341   -984       O  
ATOM   1247  NE2 GLN A 261     -58.232-179.590 303.239  1.00165.15           N  
ANISOU 1247  NE2 GLN A 261    21255  14282  27212  -3479  -3397  -1744       N  
ATOM   1248  N   SER A 262     -56.056-174.076 304.691  1.00148.81           N  
ANISOU 1248  N   SER A 262    18991  13374  24176  -2550  -3096  -1116       N  
ATOM   1249  CA  SER A 262     -55.524-173.104 303.747  1.00148.23           C  
ANISOU 1249  CA  SER A 262    18814  13575  23931  -2316  -3057  -1428       C  
ATOM   1250  C   SER A 262     -54.100-173.462 303.350  1.00147.70           C  
ANISOU 1250  C   SER A 262    18846  13324  23950  -1978  -3080  -1677       C  
ATOM   1251  O   SER A 262     -53.406-174.205 304.045  1.00145.77           O  
ANISOU 1251  O   SER A 262    18745  12762  23878  -1878  -3121  -1523       O  
ATOM   1252  CB  SER A 262     -55.551-171.687 304.339  1.00148.11           C  
ANISOU 1252  CB  SER A 262    18729  13842  23706  -2255  -2968  -1171       C  
ATOM   1253  OG  SER A 262     -56.847-171.346 304.798  1.00150.73           O  
ANISOU 1253  OG  SER A 262    18940  14367  23963  -2562  -2938   -917       O  
ATOM   1254  N   VAL A 263     -53.649-172.855 302.268  1.00151.56           N  
ANISOU 1254  N   VAL A 263    19230  14051  24305  -1808  -3059  -2058       N  
ATOM   1255  CA  VAL A 263     -52.297-173.054 301.815  1.00153.78           C  
ANISOU 1255  CA  VAL A 263    19556  14272  24601  -1471  -3054  -2302       C  
ATOM   1256  C   VAL A 263     -51.514-171.910 302.425  1.00149.75           C  
ANISOU 1256  C   VAL A 263    19077  13880  23943  -1259  -2981  -2063       C  
ATOM   1257  O   VAL A 263     -51.821-170.753 302.199  1.00146.68           O  
ANISOU 1257  O   VAL A 263    18601  13767  23365  -1307  -2919  -1955       O  
ATOM   1258  CB  VAL A 263     -52.223-172.952 300.299  1.00155.69           C  
ANISOU 1258  CB  VAL A 263    19655  14779  24722  -1405  -3051  -2811       C  
ATOM   1259  CG1 VAL A 263     -50.809-173.217 299.828  1.00157.32           C  
ANISOU 1259  CG1 VAL A 263    19904  14831  25039  -1138  -3068  -3117       C  
ATOM   1260  CG2 VAL A 263     -53.201-173.926 299.671  1.00157.89           C  
ANISOU 1260  CG2 VAL A 263    19838  15128  25024  -1716  -3099  -2990       C  
ATOM   1261  N   CYS A 264     -50.511-172.244 303.217  1.00149.71           N  
ANISOU 1261  N   CYS A 264    19180  13671  24030  -1031  -2991  -1984       N  
ATOM   1262  CA  CYS A 264     -49.695-171.255 303.907  1.00146.95           C  
ANISOU 1262  CA  CYS A 264    18874  13410  23550   -858  -2924  -1723       C  
ATOM   1263  C   CYS A 264     -48.520-170.589 303.168  1.00141.16           C  
ANISOU 1263  C   CYS A 264    18077  12893  22666   -569  -2867  -2017       C  
ATOM   1264  O   CYS A 264     -48.125-171.012 302.088  1.00140.92           O  
ANISOU 1264  O   CYS A 264    17977  12914  22652   -474  -2888  -2414       O  
ATOM   1265  CB  CYS A 264     -49.294-171.810 305.265  1.00153.12           C  
ANISOU 1265  CB  CYS A 264    19793  13894  24491   -803  -2977  -1408       C  
ATOM   1266  SG  CYS A 264     -50.761-172.206 306.236  1.00160.62           S  
ANISOU 1266  SG  CYS A 264    20824  14640  25565  -1149  -3028   -948       S  
ATOM   1267  N   SER A 265     -47.992-169.524 303.772  1.00133.17           N  
ANISOU 1267  N   SER A 265    17078  12024  21494   -443  -2787  -1819       N  
ATOM   1268  CA  SER A 265     -46.879-168.760 303.232  1.00126.86           C  
ANISOU 1268  CA  SER A 265    16227  11436  20539   -179  -2720  -2034       C  
ATOM   1269  C   SER A 265     -45.565-169.287 303.790  1.00124.51           C  
ANISOU 1269  C   SER A 265    15999  10980  20328     39  -2746  -1985       C  
ATOM   1270  O   SER A 265     -45.466-169.601 304.979  1.00116.51           O  
ANISOU 1270  O   SER A 265    15085   9784  19401      6  -2778  -1645       O  
ATOM   1271  CB  SER A 265     -47.030-167.279 303.578  1.00121.37           C  
ANISOU 1271  CB  SER A 265    15502  10980  19633   -168  -2613  -1860       C  
ATOM   1272  OG  SER A 265     -45.867-166.554 303.223  1.00116.63           O  
ANISOU 1272  OG  SER A 265    14867  10562  18884     81  -2541  -2018       O  
ATOM   1273  N   ASP A 266     -44.554-169.376 302.930  1.00131.99           N  
ANISOU 1273  N   ASP A 266    16877  12029  21246    250  -2738  -2324       N  
ATOM   1274  CA  ASP A 266     -43.236-169.840 303.345  1.00140.35           C  
ANISOU 1274  CA  ASP A 266    17963  12974  22389    467  -2769  -2319       C  
ATOM   1275  C   ASP A 266     -42.355-168.718 303.862  1.00137.46           C  
ANISOU 1275  C   ASP A 266    17590  12818  21819    623  -2677  -2187       C  
ATOM   1276  O   ASP A 266     -41.218-168.977 304.271  1.00138.64           O  
ANISOU 1276  O   ASP A 266    17748  12916  22013    798  -2703  -2167       O  
ATOM   1277  CB  ASP A 266     -42.534-170.537 302.184  1.00150.87           C  
ANISOU 1277  CB  ASP A 266    19200  14325  23801    612  -2804  -2764       C  
ATOM   1278  CG  ASP A 266     -43.462-171.435 301.417  1.00161.26           C  
ANISOU 1278  CG  ASP A 266    20494  15512  25266    448  -2867  -2984       C  
ATOM   1279  OD1 ASP A 266     -43.720-172.557 301.896  1.00166.29           O  
ANISOU 1279  OD1 ASP A 266    21214  15804  26166    370  -2965  -2872       O  
ATOM   1280  OD2 ASP A 266     -43.944-171.017 300.345  1.00163.84           O  
ANISOU 1280  OD2 ASP A 266    20717  16092  25443    384  -2822  -3265       O  
ATOM   1281  N   ILE A 267     -42.839-167.482 303.832  1.00127.46           N  
ANISOU 1281  N   ILE A 267    16301  11785  20343    563  -2574  -2109       N  
ATOM   1282  CA  ILE A 267     -42.112-166.366 304.412  1.00112.76           C  
ANISOU 1282  CA  ILE A 267    14443  10104  18297    683  -2474  -1961       C  
ATOM   1283  C   ILE A 267     -42.838-165.741 305.592  1.00111.57           C  
ANISOU 1283  C   ILE A 267    14371   9921  18099    538  -2430  -1566       C  
ATOM   1284  O   ILE A 267     -42.183-165.102 306.432  1.00115.27           O  
ANISOU 1284  O   ILE A 267    14869  10462  18468    621  -2371  -1384       O  
ATOM   1285  CB  ILE A 267     -41.807-165.296 303.346  1.00105.92           C  
ANISOU 1285  CB  ILE A 267    13466   9562  17216    779  -2371  -2233       C  
ATOM   1286  CG1 ILE A 267     -43.059-165.003 302.520  1.00105.94           C  
ANISOU 1286  CG1 ILE A 267    13416   9651  17184    612  -2369  -2351       C  
ATOM   1287  CG2 ILE A 267     -40.674-165.760 302.448  1.00105.10           C  
ANISOU 1287  CG2 ILE A 267    13269   9554  17108    963  -2391  -2588       C  
ATOM   1288  CD1 ILE A 267     -42.862-163.950 301.458  1.00104.67           C  
ANISOU 1288  CD1 ILE A 267    13117   9947  16707    669  -2233  -2515       C  
ATOM   1289  N   PHE A 268     -44.152-165.904 305.707  1.00110.10           N  
ANISOU 1289  N   PHE A 268    14205   9648  17978    315  -2454  -1437       N  
ATOM   1290  CA  PHE A 268     -44.920-165.371 306.833  1.00107.96           C  
ANISOU 1290  CA  PHE A 268    13987   9362  17671    154  -2410  -1067       C  
ATOM   1291  C   PHE A 268     -45.724-166.502 307.458  1.00100.97           C  
ANISOU 1291  C   PHE A 268    13168   8227  16969    -57  -2518   -853       C  
ATOM   1292  O   PHE A 268     -46.634-167.050 306.800  1.00102.60           O  
ANISOU 1292  O   PHE A 268    13344   8368  17274   -211  -2570   -970       O  
ATOM   1293  CB  PHE A 268     -45.839-164.234 306.394  1.00105.86           C  
ANISOU 1293  CB  PHE A 268    13611   9477  17134     62  -2237  -1039       C  
ATOM   1294  CG  PHE A 268     -45.107-163.001 305.952  1.00103.81           C  
ANISOU 1294  CG  PHE A 268    13279   9539  16625    239  -2085  -1143       C  
ATOM   1295  CD1 PHE A 268     -44.645-162.082 306.881  1.00105.36           C  
ANISOU 1295  CD1 PHE A 268    13496   9864  16673    297  -1964   -939       C  
ATOM   1296  CD2 PHE A 268     -44.885-162.758 304.606  1.00102.50           C  
ANISOU 1296  CD2 PHE A 268    13017   9562  16366    326  -2064  -1444       C  
ATOM   1297  CE1 PHE A 268     -43.970-160.949 306.476  1.00108.52           C  
ANISOU 1297  CE1 PHE A 268    13833  10529  16871    436  -1827  -1029       C  
ATOM   1298  CE2 PHE A 268     -44.212-161.628 304.197  1.00105.88           C  
ANISOU 1298  CE2 PHE A 268    13379  10282  16568    462  -1929  -1502       C  
ATOM   1299  CZ  PHE A 268     -43.755-160.722 305.134  1.00109.63           C  
ANISOU 1299  CZ  PHE A 268    13886  10836  16931    515  -1811  -1292       C  
ATOM   1300  N   PRO A 269     -45.439-166.883 308.699  1.00 93.02           N  
ANISOU 1300  N   PRO A 269    12245   7090  16010    -87  -2560   -541       N  
ATOM   1301  CA  PRO A 269     -46.181-167.986 309.318  1.00 93.43           C  
ANISOU 1301  CA  PRO A 269    12360   6905  16235   -302  -2667   -307       C  
ATOM   1302  C   PRO A 269     -47.607-167.584 309.661  1.00 95.13           C  
ANISOU 1302  C   PRO A 269    12548   7196  16401   -588  -2617    -99       C  
ATOM   1303  O   PRO A 269     -47.893-166.429 309.989  1.00 87.68           O  
ANISOU 1303  O   PRO A 269    11550   6517  15248   -611  -2478      5       O  
ATOM   1304  CB  PRO A 269     -45.373-168.297 310.586  1.00 89.34           C  
ANISOU 1304  CB  PRO A 269    11920   6287  15739   -244  -2724     -8       C  
ATOM   1305  CG  PRO A 269     -44.044-167.592 310.395  1.00 83.10           C  
ANISOU 1305  CG  PRO A 269    11100   5648  14827     38  -2668   -182       C  
ATOM   1306  CD  PRO A 269     -44.354-166.394 309.563  1.00 79.24           C  
ANISOU 1306  CD  PRO A 269    10533   5411  14166     70  -2528   -398       C  
ATOM   1307  N   HIS A 270     -48.506-168.567 309.570  1.00103.23           N  
ANISOU 1307  N   HIS A 270    13586   8057  17581   -804  -2700    -48       N  
ATOM   1308  CA  HIS A 270     -49.908-168.424 309.957  1.00103.07           C  
ANISOU 1308  CA  HIS A 270    13521   8105  17535  -1120  -2671    172       C  
ATOM   1309  C   HIS A 270     -50.657-167.422 309.080  1.00 99.57           C  
ANISOU 1309  C   HIS A 270    12933   7994  16904  -1142  -2539    -21       C  
ATOM   1310  O   HIS A 270     -51.584-166.758 309.548  1.00 99.53           O  
ANISOU 1310  O   HIS A 270    12834   8285  16696  -1291  -2404    174       O  
ATOM   1311  CB  HIS A 270     -50.043-168.028 311.433  1.00104.81           C  
ANISOU 1311  CB  HIS A 270    13773   8401  17650  -1249  -2626    602       C  
ATOM   1312  CG  HIS A 270     -49.155-168.804 312.355  1.00110.55           C  
ANISOU 1312  CG  HIS A 270    14609   8946  18448  -1174  -2723    820       C  
ATOM   1313  ND1 HIS A 270     -48.477-168.218 313.402  1.00109.73           N  
ANISOU 1313  ND1 HIS A 270    14537   8946  18212  -1106  -2689   1057       N  
ATOM   1314  CD2 HIS A 270     -48.839-170.120 312.392  1.00119.45           C  
ANISOU 1314  CD2 HIS A 270    15811   9792  19780  -1162  -2862    843       C  
ATOM   1315  CE1 HIS A 270     -47.779-169.139 314.043  1.00110.49           C  
ANISOU 1315  CE1 HIS A 270    14714   8852  18416  -1055  -2815   1231       C  
ATOM   1316  NE2 HIS A 270     -47.982-170.302 313.451  1.00119.62           N  
ANISOU 1316  NE2 HIS A 270    15899   9759  19790  -1082  -2920   1109       N  
ATOM   1317  N   ILE A 271     -50.284-167.300 307.808  1.00100.18           N  
ANISOU 1317  N   ILE A 271    12961   8119  16982   -978  -2547   -399       N  
ATOM   1318  CA  ILE A 271     -50.927-166.357 306.898  1.00105.23           C  
ANISOU 1318  CA  ILE A 271    13443   9162  17377   -966  -2410   -559       C  
ATOM   1319  C   ILE A 271     -51.397-167.100 305.655  1.00118.19           C  
ANISOU 1319  C   ILE A 271    15027  10730  19150  -1053  -2520   -881       C  
ATOM   1320  O   ILE A 271     -50.639-167.876 305.063  1.00119.48           O  
ANISOU 1320  O   ILE A 271    15253  10630  19514   -949  -2647  -1159       O  
ATOM   1321  CB  ILE A 271     -49.991-165.192 306.519  1.00 91.25           C  
ANISOU 1321  CB  ILE A 271    11634   7656  15382   -686  -2278   -684       C  
ATOM   1322  CG1 ILE A 271     -49.996-164.131 307.623  1.00 80.99           C  
ANISOU 1322  CG1 ILE A 271    10326   6569  13879   -662  -2115   -388       C  
ATOM   1323  CG2 ILE A 271     -50.401-164.570 305.189  1.00 81.72           C  
ANISOU 1323  CG2 ILE A 271    10277   6768  14004   -644  -2212   -929       C  
ATOM   1324  CD1 ILE A 271     -49.311-162.843 307.231  1.00 70.50           C  
ANISOU 1324  CD1 ILE A 271     8939   5520  12327   -438  -1965   -489       C  
ATOM   1325  N   ASP A 272     -52.649-166.863 305.268  1.00127.81           N  
ANISOU 1325  N   ASP A 272    16109  12199  20254  -1243  -2470   -861       N  
ATOM   1326  CA  ASP A 272     -53.202-167.428 304.046  1.00133.73           C  
ANISOU 1326  CA  ASP A 272    16767  12978  21067  -1350  -2559  -1176       C  
ATOM   1327  C   ASP A 272     -52.699-166.656 302.833  1.00132.37           C  
ANISOU 1327  C   ASP A 272    16488  13132  20676  -1135  -2493  -1469       C  
ATOM   1328  O   ASP A 272     -52.629-165.423 302.850  1.00130.67           O  
ANISOU 1328  O   ASP A 272    16198  13251  20201  -1003  -2342  -1348       O  
ATOM   1329  CB  ASP A 272     -54.731-167.397 304.100  1.00137.66           C  
ANISOU 1329  CB  ASP A 272    17130  13681  21493  -1634  -2530  -1028       C  
ATOM   1330  CG  ASP A 272     -55.376-167.832 302.798  1.00140.62           C  
ANISOU 1330  CG  ASP A 272    17374  14183  21874  -1757  -2610  -1356       C  
ATOM   1331  OD1 ASP A 272     -54.790-168.674 302.085  1.00144.85           O  
ANISOU 1331  OD1 ASP A 272    17967  14476  22592  -1721  -2737  -1692       O  
ATOM   1332  OD2 ASP A 272     -56.479-167.332 302.492  1.00138.57           O  
ANISOU 1332  OD2 ASP A 272    16936  14281  21433  -1889  -2546  -1290       O  
ATOM   1333  N   LYS A 273     -52.345-167.392 301.774  1.00136.95           N  
ANISOU 1333  N   LYS A 273    17055  13613  21368  -1112  -2607  -1862       N  
ATOM   1334  CA  LYS A 273     -51.823-166.748 300.572  1.00139.12           C  
ANISOU 1334  CA  LYS A 273    17216  14231  21414   -933  -2554  -2150       C  
ATOM   1335  C   LYS A 273     -52.871-165.869 299.903  1.00139.79           C  
ANISOU 1335  C   LYS A 273    17102  14807  21206  -1022  -2465  -2088       C  
ATOM   1336  O   LYS A 273     -52.526-164.851 299.291  1.00145.03           O  
ANISOU 1336  O   LYS A 273    17670  15826  21607   -862  -2367  -2112       O  
ATOM   1337  CB  LYS A 273     -51.309-167.797 299.586  1.00146.86           C  
ANISOU 1337  CB  LYS A 273    18197  15034  22568   -915  -2693  -2622       C  
ATOM   1338  CG  LYS A 273     -50.153-168.636 300.108  1.00154.60           C  
ANISOU 1338  CG  LYS A 273    19349  15531  23862   -768  -2791  -2722       C  
ATOM   1339  CD  LYS A 273     -49.516-169.453 298.992  1.00163.74           C  
ANISOU 1339  CD  LYS A 273    20463  16680  25069   -665  -2841  -3189       C  
ATOM   1340  CE  LYS A 273     -50.561-170.235 298.211  1.00173.56           C  
ANISOU 1340  CE  LYS A 273    21620  17964  26362   -911  -2909  -3414       C  
ATOM   1341  NZ  LYS A 273     -49.948-171.102 297.167  1.00179.22           N  
ANISOU 1341  NZ  LYS A 273    22293  18690  27112   -811  -2928  -3860       N  
ATOM   1342  N   THR A 274     -54.149-166.243 300.003  1.00135.45           N  
ANISOU 1342  N   THR A 274    16476  14288  20702  -1280  -2505  -1992       N  
ATOM   1343  CA  THR A 274     -55.205-165.404 299.443  1.00129.00           C  
ANISOU 1343  CA  THR A 274    15448  13946  19621  -1354  -2431  -1899       C  
ATOM   1344  C   THR A 274     -55.243-164.044 300.130  1.00119.37           C  
ANISOU 1344  C   THR A 274    14201  12939  18217  -1209  -2260  -1546       C  
ATOM   1345  O   THR A 274     -55.414-163.012 299.470  1.00115.20           O  
ANISOU 1345  O   THR A 274    13527  12798  17445  -1103  -2178  -1510       O  
ATOM   1346  CB  THR A 274     -56.557-166.109 299.562  1.00131.31           C  
ANISOU 1346  CB  THR A 274    15657  14219  20017  -1669  -2506  -1850       C  
ATOM   1347  OG1 THR A 274     -56.524-167.338 298.824  1.00133.73           O  
ANISOU 1347  OG1 THR A 274    15979  14326  20507  -1812  -2665  -2225       O  
ATOM   1348  CG2 THR A 274     -57.671-165.228 299.017  1.00131.01           C  
ANISOU 1348  CG2 THR A 274    15374  14692  19711  -1728  -2438  -1737       C  
ATOM   1349  N   TYR A 275     -55.075-164.021 301.454  1.00116.05           N  
ANISOU 1349  N   TYR A 275    13912  12269  17911  -1206  -2208  -1284       N  
ATOM   1350  CA  TYR A 275     -54.987-162.746 302.157  1.00113.93           C  
ANISOU 1350  CA  TYR A 275    13626  12174  17487  -1060  -2038  -1007       C  
ATOM   1351  C   TYR A 275     -53.768-161.956 301.702  1.00117.94           C  
ANISOU 1351  C   TYR A 275    14172  12771  17869   -790  -1972  -1106       C  
ATOM   1352  O   TYR A 275     -53.839-160.732 301.537  1.00121.29           O  
ANISOU 1352  O   TYR A 275    14502  13472  18109   -665  -1847   -982       O  
ATOM   1353  CB  TYR A 275     -54.941-162.971 303.668  1.00113.72           C  
ANISOU 1353  CB  TYR A 275    13730  11889  17588  -1127  -2002   -747       C  
ATOM   1354  CG  TYR A 275     -54.574-161.723 304.440  1.00114.64           C  
ANISOU 1354  CG  TYR A 275    13854  12140  17565   -956  -1828   -537       C  
ATOM   1355  CD1 TYR A 275     -55.533-160.768 304.750  1.00118.97           C  
ANISOU 1355  CD1 TYR A 275    14250  12971  17984   -979  -1693   -347       C  
ATOM   1356  CD2 TYR A 275     -53.266-161.493 304.847  1.00112.37           C  
ANISOU 1356  CD2 TYR A 275    13709  11700  17287   -770  -1799   -553       C  
ATOM   1357  CE1 TYR A 275     -55.201-159.621 305.448  1.00116.69           C  
ANISOU 1357  CE1 TYR A 275    13962  12780  17595   -825  -1530   -198       C  
ATOM   1358  CE2 TYR A 275     -52.925-160.351 305.542  1.00113.20           C  
ANISOU 1358  CE2 TYR A 275    13815  11926  17270   -635  -1640   -395       C  
ATOM   1359  CZ  TYR A 275     -53.895-159.418 305.841  1.00112.04           C  
ANISOU 1359  CZ  TYR A 275    13526  12031  17011   -664  -1503   -228       C  
ATOM   1360  OH  TYR A 275     -53.555-158.281 306.539  1.00104.41           O  
ANISOU 1360  OH  TYR A 275    12558  11159  15953   -532  -1340   -110       O  
ATOM   1361  N   LEU A 276     -52.640-162.638 301.499  1.00118.39           N  
ANISOU 1361  N   LEU A 276    14358  12588  18038   -700  -2057  -1327       N  
ATOM   1362  CA  LEU A 276     -51.431-161.955 301.051  1.00117.04           C  
ANISOU 1362  CA  LEU A 276    14209  12520  17741   -464  -1996  -1439       C  
ATOM   1363  C   LEU A 276     -51.622-161.363 299.660  1.00119.50           C  
ANISOU 1363  C   LEU A 276    14348  13231  17824   -424  -1978  -1588       C  
ATOM   1364  O   LEU A 276     -51.252-160.212 299.408  1.00117.26           O  
ANISOU 1364  O   LEU A 276    14012  13188  17355   -281  -1865  -1489       O  
ATOM   1365  CB  LEU A 276     -50.244-162.918 301.075  1.00118.32           C  
ANISOU 1365  CB  LEU A 276    14511  12360  18086   -376  -2102  -1676       C  
ATOM   1366  CG  LEU A 276     -48.881-162.319 300.724  1.00117.93           C  
ANISOU 1366  CG  LEU A 276    14481  12406  17920   -140  -2042  -1803       C  
ATOM   1367  CD1 LEU A 276     -48.584-161.116 301.605  1.00116.68           C  
ANISOU 1367  CD1 LEU A 276    14356  12333  17644    -38  -1886  -1508       C  
ATOM   1368  CD2 LEU A 276     -47.783-163.364 300.854  1.00117.34           C  
ANISOU 1368  CD2 LEU A 276    14526  11993  18067    -45  -2158  -2034       C  
ATOM   1369  N   MET A 277     -52.207-162.141 298.744  1.00126.57           N  
ANISOU 1369  N   MET A 277    15150  14210  18729   -565  -2094  -1819       N  
ATOM   1370  CA  MET A 277     -52.502-161.621 297.412  1.00129.70           C  
ANISOU 1370  CA  MET A 277    15357  15048  18874   -560  -2091  -1939       C  
ATOM   1371  C   MET A 277     -53.410-160.400 297.486  1.00125.35           C  
ANISOU 1371  C   MET A 277    14670  14806  18153   -554  -1985  -1606       C  
ATOM   1372  O   MET A 277     -53.221-159.431 296.742  1.00125.76           O  
ANISOU 1372  O   MET A 277    14611  15186  17984   -445  -1925  -1549       O  
ATOM   1373  CB  MET A 277     -53.142-162.710 296.552  1.00141.30           C  
ANISOU 1373  CB  MET A 277    16735  16567  20386   -754  -2236  -2241       C  
ATOM   1374  CG  MET A 277     -53.598-162.224 295.187  1.00154.85           C  
ANISOU 1374  CG  MET A 277    18226  18802  21808   -787  -2249  -2346       C  
ATOM   1375  SD  MET A 277     -54.588-163.441 294.298  1.00172.52           S  
ANISOU 1375  SD  MET A 277    20326  21143  24079  -1064  -2414  -2685       S  
ATOM   1376  CE  MET A 277     -53.382-164.738 294.037  1.00177.93           C  
ANISOU 1376  CE  MET A 277    21157  21463  24987  -1025  -2513  -3185       C  
ATOM   1377  N   PHE A 278     -54.402-160.428 298.380  1.00121.64           N  
ANISOU 1377  N   PHE A 278    14192  14235  17790   -670  -1961  -1376       N  
ATOM   1378  CA  PHE A 278     -55.233-159.248 298.587  1.00118.83           C  
ANISOU 1378  CA  PHE A 278    13701  14133  17318   -630  -1849  -1071       C  
ATOM   1379  C   PHE A 278     -54.423-158.105 299.183  1.00115.83           C  
ANISOU 1379  C   PHE A 278    13402  13706  16902   -418  -1701   -887       C  
ATOM   1380  O   PHE A 278     -54.564-156.951 298.763  1.00119.77           O  
ANISOU 1380  O   PHE A 278    13787  14459  17261   -303  -1621   -733       O  
ATOM   1381  CB  PHE A 278     -56.421-159.587 299.487  1.00118.69           C  
ANISOU 1381  CB  PHE A 278    13643  14028  17425   -806  -1845   -900       C  
ATOM   1382  CG  PHE A 278     -57.121-158.379 300.048  1.00112.70           C  
ANISOU 1382  CG  PHE A 278    12771  13443  16607   -726  -1704   -597       C  
ATOM   1383  CD1 PHE A 278     -57.958-157.613 299.252  1.00110.85           C  
ANISOU 1383  CD1 PHE A 278    12310  13581  16229   -694  -1694   -498       C  
ATOM   1384  CD2 PHE A 278     -56.942-158.011 301.372  1.00109.92           C  
ANISOU 1384  CD2 PHE A 278    12524  12893  16348   -678  -1585   -420       C  
ATOM   1385  CE1 PHE A 278     -58.601-156.502 299.766  1.00110.82           C  
ANISOU 1385  CE1 PHE A 278    12188  13703  16215   -593  -1567   -237       C  
ATOM   1386  CE2 PHE A 278     -57.582-156.901 301.892  1.00108.88           C  
ANISOU 1386  CE2 PHE A 278    12273  12913  16182   -595  -1446   -193       C  
ATOM   1387  CZ  PHE A 278     -58.413-156.146 301.088  1.00109.69           C  
ANISOU 1387  CZ  PHE A 278    12152  13342  16182   -542  -1437   -106       C  
ATOM   1388  N   TRP A 279     -53.568-158.406 300.162  1.00109.30           N  
ANISOU 1388  N   TRP A 279    12767  12554  16209   -370  -1671   -893       N  
ATOM   1389  CA  TRP A 279     -52.726-157.367 300.744  1.00104.67           C  
ANISOU 1389  CA  TRP A 279    12258  11926  15587   -190  -1534   -758       C  
ATOM   1390  C   TRP A 279     -51.712-156.851 299.732  1.00104.85           C  
ANISOU 1390  C   TRP A 279    12267  12112  15462    -46  -1524   -884       C  
ATOM   1391  O   TRP A 279     -51.462-155.643 299.658  1.00109.36           O  
ANISOU 1391  O   TRP A 279    12797  12817  15936     78  -1411   -731       O  
ATOM   1392  CB  TRP A 279     -52.017-157.896 301.988  1.00103.01           C  
ANISOU 1392  CB  TRP A 279    12237  11372  15528   -188  -1525   -745       C  
ATOM   1393  CG  TRP A 279     -51.091-156.897 302.596  1.00 99.26           C  
ANISOU 1393  CG  TRP A 279    11838  10867  15011    -24  -1391   -647       C  
ATOM   1394  CD1 TRP A 279     -51.381-156.013 303.590  1.00 93.40           C  
ANISOU 1394  CD1 TRP A 279    11091  10128  14271      5  -1251   -438       C  
ATOM   1395  CD2 TRP A 279     -49.720-156.668 302.240  1.00105.69           C  
ANISOU 1395  CD2 TRP A 279    12727  11661  15771    122  -1380   -780       C  
ATOM   1396  NE1 TRP A 279     -50.277-155.249 303.881  1.00 96.55           N  
ANISOU 1396  NE1 TRP A 279    11566  10491  14628    149  -1157   -436       N  
ATOM   1397  CE2 TRP A 279     -49.244-155.632 303.067  1.00102.57           C  
ANISOU 1397  CE2 TRP A 279    12376  11245  15352    220  -1235   -630       C  
ATOM   1398  CE3 TRP A 279     -48.850-157.240 301.306  1.00115.10           C  
ANISOU 1398  CE3 TRP A 279    13935  12869  16929    173  -1474  -1035       C  
ATOM   1399  CZ2 TRP A 279     -47.936-155.154 302.988  1.00107.35           C  
ANISOU 1399  CZ2 TRP A 279    13045  11842  15900    352  -1186   -705       C  
ATOM   1400  CZ3 TRP A 279     -47.552-156.765 301.229  1.00117.34           C  
ANISOU 1400  CZ3 TRP A 279    14271  13164  17148    317  -1420  -1108       C  
ATOM   1401  CH2 TRP A 279     -47.107-155.733 302.065  1.00113.53           C  
ANISOU 1401  CH2 TRP A 279    13836  12658  16642    398  -1280   -933       C  
ATOM   1402  N   ILE A 280     -51.104-157.752 298.958  1.00102.68           N  
ANISOU 1402  N   ILE A 280    12016  11823  15175    -66  -1638  -1171       N  
ATOM   1403  CA  ILE A 280     -50.193-157.322 297.901  1.00101.17           C  
ANISOU 1403  CA  ILE A 280    11777  11859  14805     43  -1629  -1312       C  
ATOM   1404  C   ILE A 280     -50.933-156.465 296.882  1.00 99.53           C  
ANISOU 1404  C   ILE A 280    11373  12057  14388     29  -1611  -1182       C  
ATOM   1405  O   ILE A 280     -50.407-155.456 296.397  1.00 94.34           O  
ANISOU 1405  O   ILE A 280    10668  11600  13578    134  -1536  -1079       O  
ATOM   1406  CB  ILE A 280     -49.526-158.542 297.238  1.00104.31           C  
ANISOU 1406  CB  ILE A 280    12205  12193  15237     15  -1756  -1695       C  
ATOM   1407  CG1 ILE A 280     -48.518-159.187 298.190  1.00110.09           C  
ANISOU 1407  CG1 ILE A 280    13123  12533  16173     91  -1771  -1787       C  
ATOM   1408  CG2 ILE A 280     -48.851-158.148 295.933  1.00100.79           C  
ANISOU 1408  CG2 ILE A 280    11644  12105  14546     80  -1751  -1865       C  
ATOM   1409  CD1 ILE A 280     -47.885-160.445 297.635  1.00116.97           C  
ANISOU 1409  CD1 ILE A 280    14023  13273  17149     89  -1903  -2177       C  
ATOM   1410  N   GLY A 281     -52.172-156.842 296.559  1.00105.40           N  
ANISOU 1410  N   GLY A 281    11992  12932  15126   -109  -1686  -1162       N  
ATOM   1411  CA  GLY A 281     -52.922-156.105 295.555  1.00108.04           C  
ANISOU 1411  CA  GLY A 281    12115  13678  15256   -122  -1696  -1026       C  
ATOM   1412  C   GLY A 281     -53.148-154.656 295.938  1.00103.82           C  
ANISOU 1412  C   GLY A 281    11538  13202  14708      7  -1565   -665       C  
ATOM   1413  O   GLY A 281     -52.826-153.742 295.175  1.00101.68           O  
ANISOU 1413  O   GLY A 281    11183  13180  14272     93  -1533   -543       O  
ATOM   1414  N   VAL A 282     -53.695-154.427 297.134  1.00102.57           N  
ANISOU 1414  N   VAL A 282    11432  12812  14728     18  -1488   -492       N  
ATOM   1415  CA  VAL A 282     -53.985-153.061 297.566  1.00104.34           C  
ANISOU 1415  CA  VAL A 282    11605  13056  14983    148  -1358   -190       C  
ATOM   1416  C   VAL A 282     -52.694-152.264 297.722  1.00103.15           C  
ANISOU 1416  C   VAL A 282    11577  12798  14816    290  -1255   -158       C  
ATOM   1417  O   VAL A 282     -52.642-151.071 297.399  1.00106.60           O  
ANISOU 1417  O   VAL A 282    11945  13350  15210    398  -1183     52       O  
ATOM   1418  CB  VAL A 282     -54.817-153.075 298.864  1.00104.39           C  
ANISOU 1418  CB  VAL A 282    11627  12864  15173    115  -1286    -73       C  
ATOM   1419  CG1 VAL A 282     -54.143-153.919 299.935  1.00106.60           C  
ANISOU 1419  CG1 VAL A 282    12115  12812  15578     60  -1274   -217       C  
ATOM   1420  CG2 VAL A 282     -55.058-151.658 299.365  1.00103.82           C  
ANISOU 1420  CG2 VAL A 282    11500  12781  15168    268  -1139    181       C  
ATOM   1421  N   VAL A 283     -51.629-152.912 298.196  1.00101.14           N  
ANISOU 1421  N   VAL A 283    11499  12322  14609    288  -1254   -358       N  
ATOM   1422  CA  VAL A 283     -50.344-152.232 298.327  1.00100.05           C  
ANISOU 1422  CA  VAL A 283    11464  12109  14442    403  -1163   -357       C  
ATOM   1423  C   VAL A 283     -49.744-151.949 296.954  1.00106.23           C  
ANISOU 1423  C   VAL A 283    12160  13191  15010    423  -1204   -408       C  
ATOM   1424  O   VAL A 283     -49.157-150.885 296.726  1.00109.58           O  
ANISOU 1424  O   VAL A 283    12577  13688  15372    505  -1118   -261       O  
ATOM   1425  CB  VAL A 283     -49.391-153.061 299.209  1.00 98.93           C  
ANISOU 1425  CB  VAL A 283    11507  11677  14404    401  -1168   -552       C  
ATOM   1426  CG1 VAL A 283     -47.971-152.524 299.120  1.00 97.26           C  
ANISOU 1426  CG1 VAL A 283    11372  11455  14127    502  -1100   -607       C  
ATOM   1427  CG2 VAL A 283     -49.870-153.054 300.652  1.00 98.92           C  
ANISOU 1427  CG2 VAL A 283    11584  11428  14573    380  -1099   -435       C  
ATOM   1428  N   SER A 284     -49.891-152.886 296.015  1.00111.08           N  
ANISOU 1428  N   SER A 284    12699  14002  15504    332  -1333   -621       N  
ATOM   1429  CA  SER A 284     -49.326-152.682 294.685  1.00112.78           C  
ANISOU 1429  CA  SER A 284    12808  14571  15472    328  -1371   -695       C  
ATOM   1430  C   SER A 284     -50.078-151.599 293.922  1.00112.57           C  
ANISOU 1430  C   SER A 284    12605  14859  15308    338  -1362   -379       C  
ATOM   1431  O   SER A 284     -49.468-150.826 293.174  1.00115.98           O  
ANISOU 1431  O   SER A 284    12979  15519  15568    371  -1330   -266       O  
ATOM   1432  CB  SER A 284     -49.337-153.992 293.898  1.00116.22           C  
ANISOU 1432  CB  SER A 284    13192  15152  15817    220  -1508  -1052       C  
ATOM   1433  OG  SER A 284     -48.814-153.809 292.595  1.00117.57           O  
ANISOU 1433  OG  SER A 284    13234  15730  15709    201  -1538  -1150       O  
ATOM   1434  N   VAL A 285     -51.400-151.525 294.098  1.00109.97           N  
ANISOU 1434  N   VAL A 285    12176  14552  15055    307  -1395   -214       N  
ATOM   1435  CA  VAL A 285     -52.198-150.548 293.357  1.00109.81           C  
ANISOU 1435  CA  VAL A 285    11964  14833  14926    333  -1411    105       C  
ATOM   1436  C   VAL A 285     -51.755-149.129 293.694  1.00111.93           C  
ANISOU 1436  C   VAL A 285    12275  14977  15277    472  -1282    410       C  
ATOM   1437  O   VAL A 285     -51.451-148.326 292.804  1.00114.26           O  
ANISOU 1437  O   VAL A 285    12479  15522  15414    496  -1286    605       O  
ATOM   1438  CB  VAL A 285     -53.699-150.753 293.634  1.00102.05           C  
ANISOU 1438  CB  VAL A 285    10857  13873  14046    290  -1464    210       C  
ATOM   1439  CG1 VAL A 285     -54.488-149.532 293.192  1.00 99.03           C  
ANISOU 1439  CG1 VAL A 285    10289  13698  13639    380  -1456    600       C  
ATOM   1440  CG2 VAL A 285     -54.205-151.993 292.910  1.00103.58           C  
ANISOU 1440  CG2 VAL A 285    10952  14301  14103    120  -1613    -57       C  
ATOM   1441  N   LEU A 286     -51.709-148.799 294.987  1.00107.00           N  
ANISOU 1441  N   LEU A 286    11784  13971  14900    551  -1166    454       N  
ATOM   1442  CA  LEU A 286     -51.295-147.457 295.377  1.00107.63           C  
ANISOU 1442  CA  LEU A 286    11908  13891  15096    673  -1035    699       C  
ATOM   1443  C   LEU A 286     -49.835-147.201 295.024  1.00108.97           C  
ANISOU 1443  C   LEU A 286    12177  14082  15146    672   -990    626       C  
ATOM   1444  O   LEU A 286     -49.473-146.079 294.652  1.00112.78           O  
ANISOU 1444  O   LEU A 286    12630  14608  15613    724   -933    868       O  
ATOM   1445  CB  LEU A 286     -51.555-147.239 296.867  1.00104.79           C  
ANISOU 1445  CB  LEU A 286    11655  13157  15004    736   -916    699       C  
ATOM   1446  CG  LEU A 286     -51.055-148.238 297.908  1.00 97.11           C  
ANISOU 1446  CG  LEU A 286    10855  11939  14103    680   -894    421       C  
ATOM   1447  CD1 LEU A 286     -49.597-147.989 298.264  1.00 94.81           C  
ANISOU 1447  CD1 LEU A 286    10724  11492  13806    714   -813    318       C  
ATOM   1448  CD2 LEU A 286     -51.926-148.162 299.153  1.00 89.55           C  
ANISOU 1448  CD2 LEU A 286     9904  10771  13348    698   -818    469       C  
ATOM   1449  N   LEU A 287     -48.990-148.227 295.108  1.00105.80           N  
ANISOU 1449  N   LEU A 287    11881  13652  14668    613  -1020    301       N  
ATOM   1450  CA  LEU A 287     -47.599-148.060 294.703  1.00105.49           C  
ANISOU 1450  CA  LEU A 287    11900  13688  14492    609   -982    201       C  
ATOM   1451  C   LEU A 287     -47.492-147.789 293.209  1.00110.20           C  
ANISOU 1451  C   LEU A 287    12335  14732  14806    550  -1052    296       C  
ATOM   1452  O   LEU A 287     -46.730-146.913 292.781  1.00112.54           O  
ANISOU 1452  O   LEU A 287    12618  15133  15008    555   -990    453       O  
ATOM   1453  CB  LEU A 287     -46.783-149.296 295.076  1.00105.40           C  
ANISOU 1453  CB  LEU A 287    12006  13562  14480    581  -1016   -182       C  
ATOM   1454  CG  LEU A 287     -46.264-149.347 296.512  1.00103.85           C  
ANISOU 1454  CG  LEU A 287    11988  12971  14500    638   -927   -252       C  
ATOM   1455  CD1 LEU A 287     -45.675-150.714 296.824  1.00106.39           C  
ANISOU 1455  CD1 LEU A 287    12402  13177  14846    617  -1002   -594       C  
ATOM   1456  CD2 LEU A 287     -45.230-148.256 296.728  1.00100.40           C  
ANISOU 1456  CD2 LEU A 287    11607  12477  14064    688   -801   -139       C  
ATOM   1457  N   LEU A 288     -48.247-148.533 292.398  1.00111.50           N  
ANISOU 1457  N   LEU A 288    12363  15184  14817    472  -1180    204       N  
ATOM   1458  CA  LEU A 288     -48.254-148.273 290.963  1.00114.90           C  
ANISOU 1458  CA  LEU A 288    12611  16108  14939    398  -1255    309       C  
ATOM   1459  C   LEU A 288     -48.826-146.895 290.662  1.00118.41           C  
ANISOU 1459  C   LEU A 288    12953  16635  15404    449  -1231    796       C  
ATOM   1460  O   LEU A 288     -48.346-146.199 289.760  1.00120.19           O  
ANISOU 1460  O   LEU A 288    13090  17155  15423    411  -1233    998       O  
ATOM   1461  CB  LEU A 288     -49.042-149.359 290.230  1.00117.49           C  
ANISOU 1461  CB  LEU A 288    12802  16731  15108    292  -1400     89       C  
ATOM   1462  CG  LEU A 288     -48.381-150.737 290.168  1.00117.41           C  
ANISOU 1462  CG  LEU A 288    12856  16709  15047    230  -1446   -415       C  
ATOM   1463  CD1 LEU A 288     -49.230-151.701 289.355  1.00122.65           C  
ANISOU 1463  CD1 LEU A 288    13364  17679  15559    104  -1590   -629       C  
ATOM   1464  CD2 LEU A 288     -46.973-150.638 289.599  1.00115.14           C  
ANISOU 1464  CD2 LEU A 288    12574  16615  14558    223  -1397   -572       C  
ATOM   1465  N   PHE A 289     -49.849-146.478 291.412  1.00120.58           N  
ANISOU 1465  N   PHE A 289    13228  16654  15934    536  -1211    997       N  
ATOM   1466  CA  PHE A 289     -50.378-145.130 291.238  1.00125.19           C  
ANISOU 1466  CA  PHE A 289    13720  17235  16613    622  -1186   1455       C  
ATOM   1467  C   PHE A 289     -49.342-144.084 291.627  1.00124.96           C  
ANISOU 1467  C   PHE A 289    13818  16957  16702    677  -1050   1606       C  
ATOM   1468  O   PHE A 289     -49.193-143.064 290.943  1.00128.28           O  
ANISOU 1468  O   PHE A 289    14160  17516  17066    682  -1050   1952       O  
ATOM   1469  CB  PHE A 289     -51.655-144.946 292.055  1.00125.19           C  
ANISOU 1469  CB  PHE A 289    13682  16996  16890    721  -1177   1577       C  
ATOM   1470  CG  PHE A 289     -52.251-143.573 291.934  1.00129.14           C  
ANISOU 1470  CG  PHE A 289    14075  17443  17549    846  -1155   2028       C  
ATOM   1471  CD1 PHE A 289     -53.136-143.276 290.910  1.00132.74           C  
ANISOU 1471  CD1 PHE A 289    14300  18264  17869    847  -1286   2321       C  
ATOM   1472  CD2 PHE A 289     -51.918-142.575 292.835  1.00128.69           C  
ANISOU 1472  CD2 PHE A 289    14137  16970  17789    964  -1010   2156       C  
ATOM   1473  CE1 PHE A 289     -53.682-142.012 290.792  1.00134.20           C  
ANISOU 1473  CE1 PHE A 289    14380  18371  18239    984  -1281   2761       C  
ATOM   1474  CE2 PHE A 289     -52.456-141.311 292.719  1.00131.65           C  
ANISOU 1474  CE2 PHE A 289    14413  17246  18361   1093   -994   2556       C  
ATOM   1475  CZ  PHE A 289     -53.342-141.028 291.698  1.00134.19           C  
ANISOU 1475  CZ  PHE A 289    14509  17904  18573   1114  -1134   2874       C  
ATOM   1476  N   ILE A 290     -48.629-144.313 292.731  1.00116.96           N  
ANISOU 1476  N   ILE A 290    12997  15582  15859    706   -939   1364       N  
ATOM   1477  CA  ILE A 290     -47.533-143.425 293.113  1.00109.11           C  
ANISOU 1477  CA  ILE A 290    12124  14376  14957    728   -811   1443       C  
ATOM   1478  C   ILE A 290     -46.507-143.346 291.991  1.00110.18           C  
ANISOU 1478  C   ILE A 290    12208  14871  14785    619   -836   1458       C  
ATOM   1479  O   ILE A 290     -46.078-142.258 291.590  1.00110.89           O  
ANISOU 1479  O   ILE A 290    12274  14990  14867    603   -789   1758       O  
ATOM   1480  CB  ILE A 290     -46.891-143.899 294.429  1.00100.74           C  
ANISOU 1480  CB  ILE A 290    11257  12955  14065    755   -711   1131       C  
ATOM   1481  CG1 ILE A 290     -47.827-143.637 295.610  1.00 94.53           C  
ANISOU 1481  CG1 ILE A 290    10511  11823  13584    853   -648   1180       C  
ATOM   1482  CG2 ILE A 290     -45.550-143.215 294.645  1.00 97.99           C  
ANISOU 1482  CG2 ILE A 290    11014  12490  13727    735   -597   1130       C  
ATOM   1483  CD1 ILE A 290     -47.326-144.215 296.911  1.00 87.07           C  
ANISOU 1483  CD1 ILE A 290     9733  10587  12764    858   -571    890       C  
ATOM   1484  N   VAL A 291     -46.104-144.504 291.463  1.00114.14           N  
ANISOU 1484  N   VAL A 291    12681  15653  15034    534   -910   1127       N  
ATOM   1485  CA  VAL A 291     -45.140-144.523 290.369  1.00117.82           C  
ANISOU 1485  CA  VAL A 291    13067  16528  15173    423   -928   1086       C  
ATOM   1486  C   VAL A 291     -45.734-143.885 289.120  1.00123.20           C  
ANISOU 1486  C   VAL A 291    13549  17627  15636    359  -1015   1462       C  
ATOM   1487  O   VAL A 291     -45.064-143.111 288.427  1.00127.32           O  
ANISOU 1487  O   VAL A 291    14014  18370  15993    283   -987   1696       O  
ATOM   1488  CB  VAL A 291     -44.662-145.963 290.102  1.00115.23           C  
ANISOU 1488  CB  VAL A 291    12732  16395  14656    367   -989    596       C  
ATOM   1489  CG1 VAL A 291     -43.794-146.012 288.855  1.00118.57           C  
ANISOU 1489  CG1 VAL A 291    13022  17329  14701    247  -1010    526       C  
ATOM   1490  CG2 VAL A 291     -43.898-146.496 291.305  1.00106.35           C  
ANISOU 1490  CG2 VAL A 291    11798  14867  13743    435   -911    285       C  
ATOM   1491  N   TYR A 292     -46.999-144.186 288.818  1.00123.95           N  
ANISOU 1491  N   TYR A 292    13522  17854  15719    377  -1128   1548       N  
ATOM   1492  CA  TYR A 292     -47.641-143.590 287.650  1.00127.28           C  
ANISOU 1492  CA  TYR A 292    13733  18699  15927    323  -1232   1936       C  
ATOM   1493  C   TYR A 292     -47.736-142.076 287.786  1.00129.61           C  
ANISOU 1493  C   TYR A 292    14038  18776  16433    398  -1175   2459       C  
ATOM   1494  O   TYR A 292     -47.415-141.336 286.849  1.00133.52           O  
ANISOU 1494  O   TYR A 292    14425  19577  16729    316  -1205   2798       O  
ATOM   1495  CB  TYR A 292     -49.031-144.192 287.442  1.00126.83           C  
ANISOU 1495  CB  TYR A 292    13539  18796  15855    338  -1363   1920       C  
ATOM   1496  CG  TYR A 292     -49.970-143.291 286.669  1.00128.43           C  
ANISOU 1496  CG  TYR A 292    13540  19259  15998    358  -1462   2434       C  
ATOM   1497  CD1 TYR A 292     -49.856-143.154 285.291  1.00130.42           C  
ANISOU 1497  CD1 TYR A 292    13597  20111  15847    224  -1565   2621       C  
ATOM   1498  CD2 TYR A 292     -50.969-142.575 287.317  1.00127.07           C  
ANISOU 1498  CD2 TYR A 292    13357  18756  16169    515  -1455   2736       C  
ATOM   1499  CE1 TYR A 292     -50.709-142.330 284.581  1.00132.46           C  
ANISOU 1499  CE1 TYR A 292    13659  20622  16047    246  -1674   3134       C  
ATOM   1500  CE2 TYR A 292     -51.827-141.749 286.616  1.00129.13           C  
ANISOU 1500  CE2 TYR A 292    13419  19239  16406    560  -1559   3223       C  
ATOM   1501  CZ  TYR A 292     -51.693-141.631 285.248  1.00131.95           C  
ANISOU 1501  CZ  TYR A 292    13590  20183  16362    425  -1676   3441       C  
ATOM   1502  OH  TYR A 292     -52.546-140.810 284.546  1.00134.74           O  
ANISOU 1502  OH  TYR A 292    13735  20773  16688    473  -1798   3968       O  
ATOM   1503  N   ALA A 293     -48.181-141.597 288.951  1.00124.37           N  
ANISOU 1503  N   ALA A 293    13493  17582  16178    547  -1094   2528       N  
ATOM   1504  CA  ALA A 293     -48.383-140.164 289.139  1.00120.57           C  
ANISOU 1504  CA  ALA A 293    13015  16827  15967    641  -1043   2992       C  
ATOM   1505  C   ALA A 293     -47.079-139.396 288.968  1.00120.27           C  
ANISOU 1505  C   ALA A 293    13065  16742  15889    554   -945   3115       C  
ATOM   1506  O   ALA A 293     -47.011-138.433 288.196  1.00123.58           O  
ANISOU 1506  O   ALA A 293    13394  17306  16256    510   -979   3559       O  
ATOM   1507  CB  ALA A 293     -48.992-139.896 290.516  1.00114.44           C  
ANISOU 1507  CB  ALA A 293    12351  15499  15632    809   -950   2930       C  
ATOM   1508  N   TYR A 294     -46.027-139.818 289.672  1.00115.68           N  
ANISOU 1508  N   TYR A 294    12652  15973  15330    517   -832   2743       N  
ATOM   1509  CA  TYR A 294     -44.757-139.102 289.595  1.00116.44           C  
ANISOU 1509  CA  TYR A 294    12825  16021  15397    422   -729   2829       C  
ATOM   1510  C   TYR A 294     -44.139-139.212 288.205  1.00121.32           C  
ANISOU 1510  C   TYR A 294    13298  17231  15569    242   -798   2933       C  
ATOM   1511  O   TYR A 294     -43.542-138.249 287.710  1.00118.60           O  
ANISOU 1511  O   TYR A 294    12928  16958  15177    144   -762   3271       O  
ATOM   1512  CB  TYR A 294     -43.798-139.616 290.668  1.00110.93           C  
ANISOU 1512  CB  TYR A 294    12310  15038  14800    428   -606   2387       C  
ATOM   1513  CG  TYR A 294     -44.212-139.238 292.075  1.00112.39           C  
ANISOU 1513  CG  TYR A 294    12637  14656  15410    570   -509   2334       C  
ATOM   1514  CD1 TYR A 294     -45.163-138.249 292.296  1.00113.00           C  
ANISOU 1514  CD1 TYR A 294    12683  14465  15789    682   -503   2682       C  
ATOM   1515  CD2 TYR A 294     -43.652-139.867 293.181  1.00116.34           C  
ANISOU 1515  CD2 TYR A 294    13287  14911  16007    597   -427   1934       C  
ATOM   1516  CE1 TYR A 294     -45.547-137.897 293.577  1.00114.50           C  
ANISOU 1516  CE1 TYR A 294    12979  14175  16352    809   -402   2591       C  
ATOM   1517  CE2 TYR A 294     -44.030-139.521 294.469  1.00115.88           C  
ANISOU 1517  CE2 TYR A 294    13339  14395  16294    706   -333   1875       C  
ATOM   1518  CZ  TYR A 294     -44.978-138.535 294.660  1.00114.78           C  
ANISOU 1518  CZ  TYR A 294    13159  14016  16437    808   -314   2184       C  
ATOM   1519  OH  TYR A 294     -45.361-138.185 295.936  1.00110.17           O  
ANISOU 1519  OH  TYR A 294    12662  13013  16183    914   -209   2084       O  
ATOM   1520  N   MET A 295     -44.273-140.373 287.557  1.00127.23           N  
ANISOU 1520  N   MET A 295    13939  18419  15984    182   -893   2641       N  
ATOM   1521  CA  MET A 295     -43.861-140.476 286.161  1.00131.74           C  
ANISOU 1521  CA  MET A 295    14328  19631  16095      8   -966   2738       C  
ATOM   1522  C   MET A 295     -44.713-139.585 285.269  1.00130.70           C  
ANISOU 1522  C   MET A 295    14028  19739  15892    -17  -1075   3322       C  
ATOM   1523  O   MET A 295     -44.213-139.032 284.282  1.00131.32           O  
ANISOU 1523  O   MET A 295    13989  20219  15687   -172  -1098   3625       O  
ATOM   1524  CB  MET A 295     -43.937-141.928 285.686  1.00137.07           C  
ANISOU 1524  CB  MET A 295    14913  20706  16463    -41  -1048   2256       C  
ATOM   1525  CG  MET A 295     -42.827-142.825 286.215  1.00137.93           C  
ANISOU 1525  CG  MET A 295    15138  20720  16549    -47   -961   1706       C  
ATOM   1526  SD  MET A 295     -41.207-142.425 285.533  1.00141.01           S  
ANISOU 1526  SD  MET A 295    15475  21479  16626   -219   -865   1691       S  
ATOM   1527  CE  MET A 295     -41.474-142.773 283.797  1.00145.71           C  
ANISOU 1527  CE  MET A 295    15776  22930  16657   -398   -994   1751       C  
ATOM   1528  N   TYR A 296     -45.998-139.434 285.598  1.00131.55           N  
ANISOU 1528  N   TYR A 296    14107  19629  16248    131  -1148   3502       N  
ATOM   1529  CA  TYR A 296     -46.857-138.529 284.844  1.00138.56           C  
ANISOU 1529  CA  TYR A 296    14828  20691  17129    146  -1264   4092       C  
ATOM   1530  C   TYR A 296     -46.477-137.073 285.076  1.00135.95           C  
ANISOU 1530  C   TYR A 296    14577  19983  17095    172  -1186   4570       C  
ATOM   1531  O   TYR A 296     -46.687-136.230 284.196  1.00135.74           O  
ANISOU 1531  O   TYR A 296    14413  20189  16973    113  -1274   5112       O  
ATOM   1532  CB  TYR A 296     -48.320-138.771 285.217  1.00143.00           C  
ANISOU 1532  CB  TYR A 296    15323  21102  17908    316  -1355   4122       C  
ATOM   1533  CG  TYR A 296     -49.268-137.686 284.762  1.00150.51           C  
ANISOU 1533  CG  TYR A 296    16125  22058  19006    407  -1460   4749       C  
ATOM   1534  CD1 TYR A 296     -49.649-137.583 283.431  1.00157.82           C  
ANISOU 1534  CD1 TYR A 296    16809  23602  19555    296  -1624   5101       C  
ATOM   1535  CD2 TYR A 296     -49.788-136.771 285.667  1.00152.06           C  
ANISOU 1535  CD2 TYR A 296    16405  21652  19720    609  -1399   4982       C  
ATOM   1536  CE1 TYR A 296     -50.519-136.593 283.013  1.00164.43           C  
ANISOU 1536  CE1 TYR A 296    17496  24440  20539    395  -1739   5712       C  
ATOM   1537  CE2 TYR A 296     -50.658-135.779 285.259  1.00158.90           C  
ANISOU 1537  CE2 TYR A 296    17122  22486  20765    722  -1504   5554       C  
ATOM   1538  CZ  TYR A 296     -51.020-135.694 283.931  1.00164.90           C  
ANISOU 1538  CZ  TYR A 296    17646  23851  21157    620  -1681   5938       C  
ATOM   1539  OH  TYR A 296     -51.887-134.707 283.521  1.00169.21           O  
ANISOU 1539  OH  TYR A 296    18033  24366  21895    747  -1803   6545       O  
ATOM   1540  N   ILE A 297     -45.917-136.759 286.245  1.00131.34           N  
ANISOU 1540  N   ILE A 297    14209  18821  16874    248  -1029   4386       N  
ATOM   1541  CA  ILE A 297     -45.474-135.395 286.517  1.00130.06           C  
ANISOU 1541  CA  ILE A 297    14136  18260  17023    252   -943   4778       C  
ATOM   1542  C   ILE A 297     -44.247-135.059 285.680  1.00135.35           C  
ANISOU 1542  C   ILE A 297    14775  19282  17368     11   -912   4931       C  
ATOM   1543  O   ILE A 297     -44.168-133.990 285.064  1.00143.39           O  
ANISOU 1543  O   ILE A 297    15731  20332  18418    -67   -946   5477       O  
ATOM   1544  CB  ILE A 297     -45.195-135.211 288.019  1.00123.32           C  
ANISOU 1544  CB  ILE A 297    13505  16739  16613    377   -779   4476       C  
ATOM   1545  CG1 ILE A 297     -46.478-135.393 288.832  1.00117.73           C  
ANISOU 1545  CG1 ILE A 297    12799  15704  16230    605   -802   4388       C  
ATOM   1546  CG2 ILE A 297     -44.583-133.845 288.284  1.00124.20           C  
ANISOU 1546  CG2 ILE A 297    13713  16442  17034    344   -678   4809       C  
ATOM   1547  CD1 ILE A 297     -46.257-135.373 290.328  1.00111.60           C  
ANISOU 1547  CD1 ILE A 297    12219  14364  15821    712   -644   4034       C  
ATOM   1548  N   LEU A 298     -43.272-135.971 285.644  1.00134.39           N  
ANISOU 1548  N   LEU A 298    14687  19435  16938   -111   -850   4459       N  
ATOM   1549  CA  LEU A 298     -42.028-135.699 284.931  1.00138.86           C  
ANISOU 1549  CA  LEU A 298    15214  20359  17190   -346   -798   4541       C  
ATOM   1550  C   LEU A 298     -42.258-135.594 283.429  1.00147.26           C  
ANISOU 1550  C   LEU A 298    16037  22113  17801   -508   -936   4925       C  
ATOM   1551  O   LEU A 298     -41.656-134.744 282.763  1.00152.58           O  
ANISOU 1551  O   LEU A 298    16652  22979  18343   -689   -925   5343       O  
ATOM   1552  CB  LEU A 298     -41.001-136.785 285.244  1.00136.30           C  
ANISOU 1552  CB  LEU A 298    14949  20191  16649   -404   -709   3906       C  
ATOM   1553  CG  LEU A 298     -40.716-136.990 286.732  1.00135.65           C  
ANISOU 1553  CG  LEU A 298    15089  19494  16959   -258   -584   3517       C  
ATOM   1554  CD1 LEU A 298     -39.723-138.120 286.939  1.00137.47           C  
ANISOU 1554  CD1 LEU A 298    15348  19922  16962   -302   -527   2928       C  
ATOM   1555  CD2 LEU A 298     -40.213-135.701 287.366  1.00135.20           C  
ANISOU 1555  CD2 LEU A 298    15164  18945  17261   -281   -464   3799       C  
ATOM   1556  N   TRP A 299     -43.121-136.450 282.875  1.00151.68           N  
ANISOU 1556  N   TRP A 299    16448  23076  18108   -468  -1071   4797       N  
ATOM   1557  CA  TRP A 299     -43.423-136.360 281.451  1.00161.17           C  
ANISOU 1557  CA  TRP A 299    17398  24985  18853   -628  -1214   5162       C  
ATOM   1558  C   TRP A 299     -44.210-135.098 281.125  1.00168.83           C  
ANISOU 1558  C   TRP A 299    18302  25802  20043   -581  -1314   5918       C  
ATOM   1559  O   TRP A 299     -44.030-134.518 280.048  1.00174.74           O  
ANISOU 1559  O   TRP A 299    18890  27017  20487   -764  -1392   6404       O  
ATOM   1560  CB  TRP A 299     -44.193-137.599 280.994  1.00163.20           C  
ANISOU 1560  CB  TRP A 299    17508  25695  18807   -601  -1336   4799       C  
ATOM   1561  CG  TRP A 299     -44.479-137.611 279.523  1.00170.29           C  
ANISOU 1561  CG  TRP A 299    18125  27402  19175   -785  -1484   5103       C  
ATOM   1562  CD1 TRP A 299     -43.665-138.082 278.534  1.00173.26           C  
ANISOU 1562  CD1 TRP A 299    18346  28490  18994  -1022  -1479   4921       C  
ATOM   1563  CD2 TRP A 299     -45.661-137.127 278.873  1.00176.34           C  
ANISOU 1563  CD2 TRP A 299    18711  28390  19900   -749  -1662   5640       C  
ATOM   1564  NE1 TRP A 299     -44.267-137.922 277.309  1.00179.81           N  
ANISOU 1564  NE1 TRP A 299    18912  29994  19412  -1155  -1641   5311       N  
ATOM   1565  CE2 TRP A 299     -45.493-137.338 277.490  1.00181.20           C  
ANISOU 1565  CE2 TRP A 299    19070  29882  19898   -988  -1764   5773       C  
ATOM   1566  CE3 TRP A 299     -46.845-136.537 279.327  1.00177.38           C  
ANISOU 1566  CE3 TRP A 299    18855  28089  20452   -533  -1747   6013       C  
ATOM   1567  CZ2 TRP A 299     -46.464-136.980 276.556  1.00185.45           C  
ANISOU 1567  CZ2 TRP A 299    19368  30881  20215  -1025  -1958   6291       C  
ATOM   1568  CZ3 TRP A 299     -47.808-136.181 278.398  1.00182.18           C  
ANISOU 1568  CZ3 TRP A 299    19222  29130  20869   -549  -1940   6524       C  
ATOM   1569  CH2 TRP A 299     -47.611-136.404 277.029  1.00186.19           C  
ANISOU 1569  CH2 TRP A 299    19481  30517  20747   -798  -2050   6673       C  
ATOM   1570  N   LYS A 300     -45.080-134.658 282.038  1.00169.71           N  
ANISOU 1570  N   LYS A 300    18522  25276  20685   -337  -1315   6034       N  
ATOM   1571  CA  LYS A 300     -45.823-133.422 281.813  1.00171.77           C  
ANISOU 1571  CA  LYS A 300    18721  25306  21239   -251  -1408   6737       C  
ATOM   1572  C   LYS A 300     -44.911-132.207 281.916  1.00170.85           C  
ANISOU 1572  C   LYS A 300    18719  24849  21347   -359  -1308   7122       C  
ATOM   1573  O   LYS A 300     -45.021-131.270 281.116  1.00177.48           O  
ANISOU 1573  O   LYS A 300    19446  25834  22153   -450  -1405   7780       O  
ATOM   1574  CB  LYS A 300     -46.976-133.316 282.811  1.00169.88           C  
ANISOU 1574  CB  LYS A 300    18549  24478  21520     52  -1419   6685       C  
ATOM   1575  CG  LYS A 300     -47.888-132.117 282.595  1.00173.66           C  
ANISOU 1575  CG  LYS A 300    18934  24704  22346    197  -1532   7375       C  
ATOM   1576  CD  LYS A 300     -48.647-132.225 281.282  1.00175.62           C  
ANISOU 1576  CD  LYS A 300    18895  25644  22187    131  -1754   7795       C  
ATOM   1577  CE  LYS A 300     -49.600-131.054 281.099  1.00177.58           C  
ANISOU 1577  CE  LYS A 300    19048  25597  22827    295  -1855   8412       C  
ATOM   1578  NZ  LYS A 300     -50.381-131.163 279.836  1.00181.37           N  
ANISOU 1578  NZ  LYS A 300    19261  26721  22930    202  -2016   8656       N  
ATOM   1579  N   ALA A 301     -44.000-132.205 282.893  1.00165.65           N  
ANISOU 1579  N   ALA A 301    18278  23743  20919   -365  -1122   6736       N  
ATOM   1580  CA  ALA A 301     -43.069-131.094 283.043  1.00168.81           C  
ANISOU 1580  CA  ALA A 301    18790  23812  21536   -497  -1015   7041       C  
ATOM   1581  C   ALA A 301     -41.992-131.090 281.968  1.00171.46           C  
ANISOU 1581  C   ALA A 301    19015  24788  21343   -825  -1010   7191       C  
ATOM   1582  O   ALA A 301     -41.384-130.043 281.723  1.00175.35           O  
ANISOU 1582  O   ALA A 301    19535  25148  21941   -988   -973   7642       O  
ATOM   1583  CB  ALA A 301     -42.422-131.133 284.428  1.00167.37           C  
ANISOU 1583  CB  ALA A 301    18853  23013  21729   -419   -821   6548       C  
ATOM   1584  N   HIS A 302     -41.741-132.232 281.323  1.00169.62           N  
ANISOU 1584  N   HIS A 302    18649  25247  20552   -936  -1043   6814       N  
ATOM   1585  CA  HIS A 302     -40.734-132.280 280.269  1.00171.35           C  
ANISOU 1585  CA  HIS A 302    18727  26154  20225  -1251  -1030   6912       C  
ATOM   1586  C   HIS A 302     -41.183-131.522 279.027  1.00175.90           C  
ANISOU 1586  C   HIS A 302    19095  27181  20557  -1400  -1191   7673       C  
ATOM   1587  O   HIS A 302     -40.353-130.919 278.337  1.00179.55           O  
ANISOU 1587  O   HIS A 302    19488  27960  20773  -1673  -1164   8031       O  
ATOM   1588  CB  HIS A 302     -40.411-133.733 279.918  1.00168.86           C  
ANISOU 1588  CB  HIS A 302    18306  26450  19404  -1304  -1024   6256       C  
ATOM   1589  CG  HIS A 302     -39.383-133.881 278.841  1.00175.12           C  
ANISOU 1589  CG  HIS A 302    18921  28011  19604  -1618   -997   6266       C  
ATOM   1590  ND1 HIS A 302     -39.708-133.930 277.502  1.00181.24           N  
ANISOU 1590  ND1 HIS A 302    19434  29570  19859  -1793  -1135   6597       N  
ATOM   1591  CD2 HIS A 302     -38.034-133.991 278.904  1.00174.97           C  
ANISOU 1591  CD2 HIS A 302    18930  28142  19411  -1794   -845   5977       C  
ATOM   1592  CE1 HIS A 302     -38.605-134.063 276.787  1.00184.00           C  
ANISOU 1592  CE1 HIS A 302    19655  30524  19731  -2070  -1060   6501       C  
ATOM   1593  NE2 HIS A 302     -37.575-134.102 277.614  1.00180.32           N  
ANISOU 1593  NE2 HIS A 302    19358  29683  19472  -2070   -884   6125       N  
ATOM   1594  N   SER A 303     -42.483-131.534 278.728  1.00176.09           N  
ANISOU 1594  N   SER A 303    19007  27264  20637  -1235  -1364   7948       N  
ATOM   1595  CA  SER A 303     -42.971-130.835 277.544  1.00184.26           C  
ANISOU 1595  CA  SER A 303    19824  28754  21431  -1362  -1542   8706       C  
ATOM   1596  C   SER A 303     -42.978-129.325 277.743  1.00188.22           C  
ANISOU 1596  C   SER A 303    20422  28602  22491  -1341  -1522   9262       C  
ATOM   1597  O   SER A 303     -42.871-128.573 276.768  1.00192.61           O  
ANISOU 1597  O   SER A 303    20831  29419  22934  -1523  -1583   9668       O  
ATOM   1598  CB  SER A 303     -44.371-131.330 277.183  1.00188.12           C  
ANISOU 1598  CB  SER A 303    20143  29499  21835  -1181  -1731   8756       C  
ATOM   1599  OG  SER A 303     -44.385-132.737 277.012  1.00187.64           O  
ANISOU 1599  OG  SER A 303    19999  29954  21342  -1205  -1729   8086       O  
ATOM   1600  N   HIS A 304     -43.100-128.863 278.989  1.00188.42           N  
ANISOU 1600  N   HIS A 304    20682  27759  23149  -1120  -1429   9199       N  
ATOM   1601  CA  HIS A 304     -43.129-127.431 279.264  1.00191.05           C  
ANISOU 1601  CA  HIS A 304    21117  27395  24079  -1076  -1393   9558       C  
ATOM   1602  C   HIS A 304     -41.740-126.823 279.390  1.00190.71           C  
ANISOU 1602  C   HIS A 304    21201  27195  24064  -1334  -1245   9604       C  
ATOM   1603  O   HIS A 304     -41.602-125.601 279.256  1.00195.89           O  
ANISOU 1603  O   HIS A 304    21894  27466  25071  -1387  -1245   9953       O  
ATOM   1604  CB  HIS A 304     -43.917-127.150 280.546  1.00187.93           C  
ANISOU 1604  CB  HIS A 304    20896  26142  24368   -726  -1346   9391       C  
ATOM   1605  CG  HIS A 304     -45.390-127.386 280.420  1.00188.61           C  
ANISOU 1605  CG  HIS A 304    20843  26264  24554   -468  -1489   9427       C  
ATOM   1606  ND1 HIS A 304     -46.318-126.705 281.177  1.00189.21           N  
ANISOU 1606  ND1 HIS A 304    20989  25644  25258   -178  -1480   9442       N  
ATOM   1607  CD2 HIS A 304     -46.095-128.230 279.629  1.00189.36           C  
ANISOU 1607  CD2 HIS A 304    20723  27032  24193   -469  -1635   9413       C  
ATOM   1608  CE1 HIS A 304     -47.532-127.116 280.857  1.00190.49           C  
ANISOU 1608  CE1 HIS A 304    20983  26051  25345    -13  -1612   9463       C  
ATOM   1609  NE2 HIS A 304     -47.425-128.042 279.920  1.00190.67           N  
ANISOU 1609  NE2 HIS A 304    20834  26891  24721   -188  -1711   9450       N  
ATOM   1610  N   ALA A 305     -40.715-127.639 279.648  1.00184.12           N  
ANISOU 1610  N   ALA A 305    20428  26658  22869  -1498  -1117   9249       N  
ATOM   1611  CA  ALA A 305     -39.372-127.105 279.855  1.00181.46           C  
ANISOU 1611  CA  ALA A 305    20206  26174  22567  -1752   -954   9238       C  
ATOM   1612  C   ALA A 305     -38.852-126.413 278.602  1.00185.91           C  
ANISOU 1612  C   ALA A 305    20599  27214  22824  -2051  -1019   9636       C  
ATOM   1613  O   ALA A 305     -38.395-125.265 278.656  1.00190.48           O  
ANISOU 1613  O   ALA A 305    21261  27368  23744  -2155   -981   9909       O  
ATOM   1614  CB  ALA A 305     -38.424-128.224 280.287  1.00176.93           C  
ANISOU 1614  CB  ALA A 305    19679  25877  21668  -1824   -799   8476       C  
ATOM   1615  N   VAL A 306     -38.913-127.095 277.462  1.00182.55           N  
ANISOU 1615  N   VAL A 306    19927  27678  21754  -2198  -1120   9651       N  
ATOM   1616  CA  VAL A 306     -38.471-126.543 276.188  1.00184.40           C  
ANISOU 1616  CA  VAL A 306    19958  28463  21641  -2491  -1195  10015       C  
ATOM   1617  C   VAL A 306     -39.679-125.963 275.469  1.00184.51           C  
ANISOU 1617  C   VAL A 306    19818  28483  21804  -2369  -1396  10480       C  
ATOM   1618  O   VAL A 306     -40.722-126.621 275.358  1.00183.95           O  
ANISOU 1618  O   VAL A 306    19649  28601  21641  -2175  -1500  10385       O  
ATOM   1619  CB  VAL A 306     -37.777-127.610 275.325  1.00181.19           C  
ANISOU 1619  CB  VAL A 306    19338  29071  20433  -2742  -1171   9700       C  
ATOM   1620  CG1 VAL A 306     -37.274-126.995 274.026  1.00187.13           C  
ANISOU 1620  CG1 VAL A 306    19865  30393  20844  -3059  -1243  10072       C  
ATOM   1621  CG2 VAL A 306     -36.634-128.253 276.095  1.00176.02           C  
ANISOU 1621  CG2 VAL A 306    18821  28419  19640  -2833   -960   9191       C  
ATOM   1622  N   ALA A 307     -39.545-124.734 274.983  1.00186.61           N  
ANISOU 1622  N   ALA A 307    20057  28547  22301  -2488  -1452  10980       N  
ATOM   1623  CA  ALA A 307     -40.626-124.080 274.265  1.00188.67           C  
ANISOU 1623  CA  ALA A 307    20158  28813  22714  -2392  -1638  11467       C  
ATOM   1624  C   ALA A 307     -40.566-124.430 272.784  1.00189.41           C  
ANISOU 1624  C   ALA A 307    19924  29911  22132  -2657  -1757  11658       C  
ATOM   1625  O   ALA A 307     -39.495-124.688 272.226  1.00187.40           O  
ANISOU 1625  O   ALA A 307    19577  30226  21400  -2966  -1695  11556       O  
ATOM   1626  CB  ALA A 307     -40.564-122.566 274.454  1.00196.98           C  
ANISOU 1626  CB  ALA A 307    21334  29147  24361  -2380  -1650  11922       C  
ATOM   1627  N   LYS A 308     -41.735-124.442 272.150  1.00151.51           N  
ANISOU 1627  N   LYS A 308    18587  16564  22414   1203   1136   2415       N  
ATOM   1628  CA  LYS A 308     -41.875-124.826 270.752  1.00145.14           C  
ANISOU 1628  CA  LYS A 308    17405  15441  22302    782   1218   2307       C  
ATOM   1629  C   LYS A 308     -42.216-123.600 269.917  1.00139.91           C  
ANISOU 1629  C   LYS A 308    16806  14740  21612    712   1144   1844       C  
ATOM   1630  O   LYS A 308     -43.150-122.860 270.247  1.00141.93           O  
ANISOU 1630  O   LYS A 308    17210  15223  21495    957   1327   1800       O  
ATOM   1631  CB  LYS A 308     -42.955-125.897 270.586  1.00144.03           C  
ANISOU 1631  CB  LYS A 308    16908  15287  22528    679   1640   2763       C  
ATOM   1632  N   ALA A 309     -41.465-123.394 268.837  1.00138.66           N  
ANISOU 1632  N   ALA A 309    16519  14319  21847    424    906   1550       N  
ATOM   1633  CA  ALA A 309     -41.650-122.257 267.946  1.00136.81           C  
ANISOU 1633  CA  ALA A 309    16297  14028  21657    331    813   1173       C  
ATOM   1634  C   ALA A 309     -41.927-122.755 266.534  1.00135.06           C  
ANISOU 1634  C   ALA A 309    15722  13640  21953     42    966   1121       C  
ATOM   1635  O   ALA A 309     -41.191-123.602 266.015  1.00136.11           O  
ANISOU 1635  O   ALA A 309    15684  13593  22441   -110    902   1170       O  
ATOM   1636  CB  ALA A 309     -40.421-121.343 267.954  1.00135.61           C  
ANISOU 1636  CB  ALA A 309    16316  13754  21457    300    332    909       C  
ATOM   1637  N   LEU A 310     -42.982-122.227 265.920  1.00131.20           N  
ANISOU 1637  N   LEU A 310    15152  13221  21478     14   1150   1010       N  
ATOM   1638  CA  LEU A 310     -43.384-122.595 264.569  1.00126.40           C  
ANISOU 1638  CA  LEU A 310    14260  12491  21276   -221   1244    917       C  
ATOM   1639  C   LEU A 310     -43.078-121.448 263.618  1.00121.28           C  
ANISOU 1639  C   LEU A 310    13611  11834  20634   -278   1092    604       C  
ATOM   1640  O   LEU A 310     -43.500-120.310 263.853  1.00117.41           O  
ANISOU 1640  O   LEU A 310    13267  11451  19893   -158   1073    492       O  
ATOM   1641  CB  LEU A 310     -44.874-122.943 264.514  1.00127.58           C  
ANISOU 1641  CB  LEU A 310    14235  12732  21508   -244   1537   1112       C  
ATOM   1642  CG  LEU A 310     -45.472-123.187 263.126  1.00125.33           C  
ANISOU 1642  CG  LEU A 310    13695  12332  21592   -476   1551    970       C  
ATOM   1643  CD1 LEU A 310     -44.758-124.322 262.414  1.00121.86           C  
ANISOU 1643  CD1 LEU A 310    13165  11611  21527   -635   1407    896       C  
ATOM   1644  CD2 LEU A 310     -46.959-123.477 263.228  1.00126.81           C  
ANISOU 1644  CD2 LEU A 310    13659  12613  21909   -520   1779   1248       C  
ATOM   1645  N   ILE A 311     -42.351-121.750 262.546  1.00120.78           N  
ANISOU 1645  N   ILE A 311    13384  11652  20855   -414    999    496       N  
ATOM   1646  CA  ILE A 311     -41.961-120.765 261.544  1.00116.90           C  
ANISOU 1646  CA  ILE A 311    12815  11186  20413   -457    887    313       C  
ATOM   1647  C   ILE A 311     -42.522-121.198 260.197  1.00120.21           C  
ANISOU 1647  C   ILE A 311    13034  11617  21024   -540   1021    205       C  
ATOM   1648  O   ILE A 311     -42.290-122.330 259.758  1.00122.62           O  
ANISOU 1648  O   ILE A 311    13263  11808  21519   -564   1047    199       O  
ATOM   1649  CB  ILE A 311     -40.432-120.605 261.469  1.00108.55           C  
ANISOU 1649  CB  ILE A 311    11716  10060  19470   -463    651    358       C  
ATOM   1650  CG1 ILE A 311     -39.872-120.146 262.817  1.00105.01           C  
ANISOU 1650  CG1 ILE A 311    11498   9573  18830   -395    397    428       C  
ATOM   1651  CG2 ILE A 311     -40.054-119.631 260.365  1.00107.83           C  
ANISOU 1651  CG2 ILE A 311    11457  10022  19490   -505    579    297       C  
ATOM   1652  CD1 ILE A 311     -38.372-119.925 262.816  1.00102.20           C  
ANISOU 1652  CD1 ILE A 311    11039   9133  18660   -445     85    541       C  
ATOM   1653  N   VAL A 312     -43.262-120.301 259.547  1.00115.98           N  
ANISOU 1653  N   VAL A 312    12442  11199  20425   -554   1070    100       N  
ATOM   1654  CA  VAL A 312     -43.724-120.517 258.184  1.00110.16           C  
ANISOU 1654  CA  VAL A 312    11538  10517  19800   -603   1126    -29       C  
ATOM   1655  C   VAL A 312     -43.269-119.341 257.333  1.00 98.45           C  
ANISOU 1655  C   VAL A 312     9971   9167  18267   -560   1070    -72       C  
ATOM   1656  O   VAL A 312     -43.111-118.220 257.826  1.00102.43           O  
ANISOU 1656  O   VAL A 312    10542   9677  18700   -543    988    -20       O  
ATOM   1657  CB  VAL A 312     -45.257-120.695 258.099  1.00110.32           C  
ANISOU 1657  CB  VAL A 312    11486  10582  19847   -677   1240    -22       C  
ATOM   1658  CG1 VAL A 312     -45.719-121.817 259.018  1.00 99.59           C  
ANISOU 1658  CG1 VAL A 312    10137   9090  18613   -735   1304    158       C  
ATOM   1659  CG2 VAL A 312     -45.961-119.396 258.434  1.00116.19           C  
ANISOU 1659  CG2 VAL A 312    12260  11478  20411   -611   1312     16       C  
ATOM   1660  N   TYR A 313     -43.047-119.602 256.047  1.00 94.34           N  
ANISOU 1660  N   TYR A 313     9316   8743  17785   -511   1093   -155       N  
ATOM   1661  CA  TYR A 313     -42.547-118.565 255.157  1.00105.96           C  
ANISOU 1661  CA  TYR A 313    10644  10390  19226   -441   1082    -85       C  
ATOM   1662  C   TYR A 313     -42.977-118.855 253.729  1.00111.98           C  
ANISOU 1662  C   TYR A 313    11306  11344  19897   -338   1155   -217       C  
ATOM   1663  O   TYR A 313     -43.145-120.014 253.339  1.00113.17           O  
ANISOU 1663  O   TYR A 313    11524  11436  20040   -283   1148   -399       O  
ATOM   1664  CB  TYR A 313     -41.018-118.448 255.229  1.00113.71           C  
ANISOU 1664  CB  TYR A 313    11529  11362  20314   -374   1013    112       C  
ATOM   1665  CG  TYR A 313     -40.268-119.722 254.895  1.00117.57           C  
ANISOU 1665  CG  TYR A 313    11999  11838  20833   -229   1078     86       C  
ATOM   1666  CD1 TYR A 313     -40.024-120.088 253.575  1.00119.30           C  
ANISOU 1666  CD1 TYR A 313    12117  12259  20954     -1   1200     29       C  
ATOM   1667  CD2 TYR A 313     -39.786-120.549 255.901  1.00119.45           C  
ANISOU 1667  CD2 TYR A 313    12344  11874  21166   -260   1017    121       C  
ATOM   1668  CE1 TYR A 313     -39.337-121.247 253.269  1.00120.97           C  
ANISOU 1668  CE1 TYR A 313    12364  12435  21164    221   1260    -37       C  
ATOM   1669  CE2 TYR A 313     -39.093-121.708 255.603  1.00120.09           C  
ANISOU 1669  CE2 TYR A 313    12418  11904  21307    -90   1075    102       C  
ATOM   1670  CZ  TYR A 313     -38.871-122.051 254.285  1.00121.99           C  
ANISOU 1670  CZ  TYR A 313    12586  12313  21453    165   1197      3       C  
ATOM   1671  OH  TYR A 313     -38.183-123.202 253.979  1.00124.31           O  
ANISOU 1671  OH  TYR A 313    12923  12534  21776    421   1257    -58       O  
ATOM   1672  N   GLY A 314     -43.143-117.784 252.953  1.00114.63           N  
ANISOU 1672  N   GLY A 314    11504  11887  20164   -293   1183   -127       N  
ATOM   1673  CA  GLY A 314     -43.375-117.910 251.529  1.00118.04           C  
ANISOU 1673  CA  GLY A 314    11844  12581  20424   -124   1238   -212       C  
ATOM   1674  C   GLY A 314     -42.065-117.924 250.768  1.00121.73           C  
ANISOU 1674  C   GLY A 314    12173  13252  20826    128   1333    -33       C  
ATOM   1675  O   GLY A 314     -41.566-118.990 250.395  1.00132.86           O  
ANISOU 1675  O   GLY A 314    13662  14675  22142    330   1370   -172       O  
ATOM   1676  N   SER A 315     -41.502-116.739 250.537  1.00115.49           N  
ANISOU 1676  N   SER A 315    11155  12608  20116    143   1372    318       N  
ATOM   1677  CA  SER A 315     -40.166-116.575 249.972  1.00119.88           C  
ANISOU 1677  CA  SER A 315    11462  13379  20708    362   1489    675       C  
ATOM   1678  C   SER A 315     -40.007-117.277 248.629  1.00122.59           C  
ANISOU 1678  C   SER A 315    11793  14093  20694    776   1677    589       C  
ATOM   1679  O   SER A 315     -39.448-118.378 248.557  1.00129.81           O  
ANISOU 1679  O   SER A 315    12821  14991  21511   1000   1737    438       O  
ATOM   1680  CB  SER A 315     -39.100-117.081 250.947  1.00123.41           C  
ANISOU 1680  CB  SER A 315    11908  13596  21386    299   1421    788       C  
ATOM   1681  OG  SER A 315     -38.920-118.482 250.839  1.00131.15           O  
ANISOU 1681  OG  SER A 315    13060  14553  22220    497   1497    527       O  
ATOM   1682  N   THR A 316     -40.482-116.643 247.556  1.00119.29           N  
ANISOU 1682  N   THR A 316    11264  14013  20049    932   1760    678       N  
ATOM   1683  CA  THR A 316     -40.235-117.181 246.222  1.00121.73           C  
ANISOU 1683  CA  THR A 316    11584  14753  19916   1429   1938    626       C  
ATOM   1684  C   THR A 316     -38.744-117.182 245.908  1.00124.98           C  
ANISOU 1684  C   THR A 316    11708  15431  20347   1766   2193   1102       C  
ATOM   1685  O   THR A 316     -38.173-118.214 245.537  1.00130.00           O  
ANISOU 1685  O   THR A 316    12474  16184  20737   2166   2319    943       O  
ATOM   1686  CB  THR A 316     -40.998-116.375 245.169  1.00122.05           C  
ANISOU 1686  CB  THR A 316    11528  15160  19686   1547   1974    716       C  
ATOM   1687  OG1 THR A 316     -42.400-116.636 245.280  1.00119.67           O  
ANISOU 1687  OG1 THR A 316    11482  14669  19317   1322   1737    251       O  
ATOM   1688  CG2 THR A 316     -40.522-116.745 243.770  1.00127.10           C  
ANISOU 1688  CG2 THR A 316    12151  16350  19790   2166   2195    777       C  
ATOM   1689  N   THR A 317     -38.094-116.027 246.061  1.00124.47           N  
ANISOU 1689  N   THR A 317    11231  15441  20620   1621   2252   1724       N  
ATOM   1690  CA  THR A 317     -36.672-115.928 245.752  1.00122.97           C  
ANISOU 1690  CA  THR A 317    10639  15534  20549   1909   2494   2334       C  
ATOM   1691  C   THR A 317     -35.823-116.707 246.749  1.00114.43           C  
ANISOU 1691  C   THR A 317     9595  14137  19747   1816   2419   2296       C  
ATOM   1692  O   THR A 317     -34.751-117.209 246.391  1.00113.81           O  
ANISOU 1692  O   THR A 317     9308  14322  19615   2212   2664   2605       O  
ATOM   1693  CB  THR A 317     -36.242-114.461 245.732  1.00126.80           C  
ANISOU 1693  CB  THR A 317    10628  16077  21473   1682   2475   3064       C  
ATOM   1694  OG1 THR A 317     -37.177-113.698 244.959  1.00127.39           O  
ANISOU 1694  OG1 THR A 317    10699  16366  21337   1706   2501   3076       O  
ATOM   1695  CG2 THR A 317     -34.858-114.317 245.121  1.00133.30           C  
ANISOU 1695  CG2 THR A 317    10917  17327  22405   2047   2783   3845       C  
ATOM   1696  N   GLY A 318     -36.283-116.825 247.991  1.00112.53           N  
ANISOU 1696  N   GLY A 318     9604  13375  19776   1351   2110   1960       N  
ATOM   1697  CA  GLY A 318     -35.524-117.472 249.038  1.00114.01           C  
ANISOU 1697  CA  GLY A 318     9824  13258  20238   1227   1994   1962       C  
ATOM   1698  C   GLY A 318     -34.979-116.549 250.106  1.00114.69           C  
ANISOU 1698  C   GLY A 318     9685  13036  20854    790   1705   2335       C  
ATOM   1699  O   GLY A 318     -34.169-116.996 250.928  1.00111.35           O  
ANISOU 1699  O   GLY A 318     9216  12419  20672    710   1584   2445       O  
ATOM   1700  N   ASN A 319     -35.393-115.279 250.126  1.00113.01           N  
ANISOU 1700  N   ASN A 319     9355  12744  20839    521   1542   2517       N  
ATOM   1701  CA  ASN A 319     -34.896-114.346 251.131  1.00112.02           C  
ANISOU 1701  CA  ASN A 319     9087  12245  21231    121   1158   2803       C  
ATOM   1702  C   ASN A 319     -35.598-114.545 252.469  1.00104.49           C  
ANISOU 1702  C   ASN A 319     8607  10845  20251   -166    855   2274       C  
ATOM   1703  O   ASN A 319     -34.940-114.688 253.506  1.00104.09           O  
ANISOU 1703  O   ASN A 319     8594  10524  20433   -335    581   2322       O  
ATOM   1704  CB  ASN A 319     -35.068-112.905 250.646  1.00114.16           C  
ANISOU 1704  CB  ASN A 319     9085  12526  21766    -24   1059   3192       C  
ATOM   1705  CG  ASN A 319     -34.264-112.611 249.395  1.00115.46           C  
ANISOU 1705  CG  ASN A 319     8692  13174  22003    270   1373   3887       C  
ATOM   1706  OD1 ASN A 319     -33.070-112.317 249.465  1.00116.32           O  
ANISOU 1706  OD1 ASN A 319     8333  13300  22564    224   1300   4524       O  
ATOM   1707  ND2 ASN A 319     -34.918-112.680 248.242  1.00114.82           N  
ANISOU 1707  ND2 ASN A 319     8633  13518  21475    595   1716   3818       N  
ATOM   1708  N   THR A 320     -36.935-114.549 252.467  1.00 97.73           N  
ANISOU 1708  N   THR A 320     8091   9943  19099   -195    903   1814       N  
ATOM   1709  CA  THR A 320     -37.667-114.788 253.706  1.00102.00           C  
ANISOU 1709  CA  THR A 320     9048  10149  19557   -381    707   1386       C  
ATOM   1710  C   THR A 320     -37.371-116.174 254.261  1.00114.46           C  
ANISOU 1710  C   THR A 320    10793  11680  21017   -303    769   1194       C  
ATOM   1711  O   THR A 320     -37.422-116.379 255.479  1.00115.96           O  
ANISOU 1711  O   THR A 320    11222  11608  21229   -442    568   1045       O  
ATOM   1712  CB  THR A 320     -39.170-114.612 253.481  1.00 95.82           C  
ANISOU 1712  CB  THR A 320     8497   9400  18511   -381    813   1038       C  
ATOM   1713  OG1 THR A 320     -39.403-113.421 252.719  1.00 87.92           O  
ANISOU 1713  OG1 THR A 320     7294   8501  17611   -389    813   1266       O  
ATOM   1714  CG2 THR A 320     -39.902-114.502 254.813  1.00 96.03           C  
ANISOU 1714  CG2 THR A 320     8882   9121  18485   -529    632    745       C  
ATOM   1715  N   GLU A 321     -37.054-117.135 253.389  1.00123.18           N  
ANISOU 1715  N   GLU A 321    11797  13030  21974    -35   1038   1197       N  
ATOM   1716  CA  GLU A 321     -36.552-118.420 253.861  1.00127.43           C  
ANISOU 1716  CA  GLU A 321    12447  13477  22494     70   1075   1094       C  
ATOM   1717  C   GLU A 321     -35.191-118.254 254.520  1.00130.62           C  
ANISOU 1717  C   GLU A 321    12617  13796  23215      7    899   1495       C  
ATOM   1718  O   GLU A 321     -34.977-118.715 255.647  1.00133.50           O  
ANISOU 1718  O   GLU A 321    13149  13924  23652   -115    712   1424       O  
ATOM   1719  CB  GLU A 321     -36.470-119.420 252.708  1.00129.15           C  
ANISOU 1719  CB  GLU A 321    12654  13939  22479    448   1364    973       C  
ATOM   1720  CG  GLU A 321     -35.789-120.730 253.090  1.00131.06           C  
ANISOU 1720  CG  GLU A 321    12982  14056  22760    622   1407    916       C  
ATOM   1721  CD  GLU A 321     -35.869-121.781 251.999  1.00129.39           C  
ANISOU 1721  CD  GLU A 321    12893  13989  22280   1047   1627    655       C  
ATOM   1722  OE1 GLU A 321     -35.898-122.984 252.335  1.00121.07           O  
ANISOU 1722  OE1 GLU A 321    12071  12691  21240   1135   1600    403       O  
ATOM   1723  OE2 GLU A 321     -35.904-121.406 250.808  1.00134.28           O  
ANISOU 1723  OE2 GLU A 321    13401  14954  22664   1320   1801    699       O  
ATOM   1724  N   TYR A 322     -34.258-117.594 253.829  1.00132.01           N  
ANISOU 1724  N   TYR A 322    12366  14185  23605     94    943   1980       N  
ATOM   1725  CA  TYR A 322     -32.970-117.284 254.441  1.00137.05           C  
ANISOU 1725  CA  TYR A 322    12692  14726  24655    -30    695   2452       C  
ATOM   1726  C   TYR A 322     -33.154-116.461 255.709  1.00140.69           C  
ANISOU 1726  C   TYR A 322    13354  14791  25313   -423    197   2356       C  
ATOM   1727  O   TYR A 322     -32.413-116.634 256.684  1.00144.72           O  
ANISOU 1727  O   TYR A 322    13860  15105  26024   -552   -113   2476       O  
ATOM   1728  CB  TYR A 322     -32.072-116.546 253.449  1.00140.45           C  
ANISOU 1728  CB  TYR A 322    12550  15456  25358     90    818   3100       C  
ATOM   1729  CG  TYR A 322     -30.796-116.024 254.069  1.00141.62           C  
ANISOU 1729  CG  TYR A 322    12283  15457  26069   -131    461   3681       C  
ATOM   1730  CD1 TYR A 322     -29.706-116.860 254.267  1.00142.50           C  
ANISOU 1730  CD1 TYR A 322    12145  15670  26327     45    530   3988       C  
ATOM   1731  CD2 TYR A 322     -30.685-114.696 254.462  1.00142.31           C  
ANISOU 1731  CD2 TYR A 322    12223  15264  26584   -515      3   3929       C  
ATOM   1732  CE1 TYR A 322     -28.540-116.388 254.838  1.00145.12           C  
ANISOU 1732  CE1 TYR A 322    12044  15869  27225   -187    146   4566       C  
ATOM   1733  CE2 TYR A 322     -29.524-114.217 255.034  1.00145.23           C  
ANISOU 1733  CE2 TYR A 322    12203  15437  27540   -764   -439   4462       C  
ATOM   1734  CZ  TYR A 322     -28.455-115.066 255.219  1.00146.47           C  
ANISOU 1734  CZ  TYR A 322    12070  15740  27843   -614   -369   4799       C  
ATOM   1735  OH  TYR A 322     -27.295-114.593 255.786  1.00152.40           O  
ANISOU 1735  OH  TYR A 322    12379  16299  29229   -889   -863   5378       O  
ATOM   1736  N   THR A 323     -34.135-115.556 255.712  1.00139.85           N  
ANISOU 1736  N   THR A 323    13446  14568  25122   -571     97   2130       N  
ATOM   1737  CA  THR A 323     -34.494-114.859 256.941  1.00139.02           C  
ANISOU 1737  CA  THR A 323    13671  14084  25065   -822   -348   1903       C  
ATOM   1738  C   THR A 323     -34.976-115.849 257.993  1.00138.60           C  
ANISOU 1738  C   THR A 323    14045  13929  24687   -779   -339   1508       C  
ATOM   1739  O   THR A 323     -34.438-115.906 259.105  1.00141.33           O  
ANISOU 1739  O   THR A 323    14528  14070  25100   -875   -690   1518       O  
ATOM   1740  CB  THR A 323     -35.569-113.807 256.658  1.00133.45           C  
ANISOU 1740  CB  THR A 323    13122  13304  24279   -885   -366   1712       C  
ATOM   1741  OG1 THR A 323     -35.101-112.898 255.655  1.00136.66           O  
ANISOU 1741  OG1 THR A 323    13091  13810  25022   -922   -363   2165       O  
ATOM   1742  CG2 THR A 323     -35.898-113.029 257.925  1.00130.07           C  
ANISOU 1742  CG2 THR A 323    13088  12477  23857  -1040   -833   1449       C  
ATOM   1743  N   ALA A 324     -35.985-116.653 257.646  1.00136.32           N  
ANISOU 1743  N   ALA A 324    13946  13784  24065   -635     33   1200       N  
ATOM   1744  CA  ALA A 324     -36.489-117.662 258.573  1.00131.17           C  
ANISOU 1744  CA  ALA A 324    13622  13045  23172   -597     84    936       C  
ATOM   1745  C   ALA A 324     -35.389-118.627 258.994  1.00133.21           C  
ANISOU 1745  C   ALA A 324    13775  13281  23558   -538     33   1132       C  
ATOM   1746  O   ALA A 324     -35.329-119.039 260.158  1.00133.79           O  
ANISOU 1746  O   ALA A 324    14075  13217  23541   -570   -137   1076       O  
ATOM   1747  CB  ALA A 324     -37.656-118.419 257.942  1.00124.90           C  
ANISOU 1747  CB  ALA A 324    12935  12375  22148   -491    444    672       C  
ATOM   1748  N   GLU A 325     -34.508-118.999 258.061  1.00134.77           N  
ANISOU 1748  N   GLU A 325    13623  13647  23936   -400    200   1396       N  
ATOM   1749  CA  GLU A 325     -33.376-119.850 258.415  1.00137.51           C  
ANISOU 1749  CA  GLU A 325    13814  13985  24448   -302    162   1645       C  
ATOM   1750  C   GLU A 325     -32.426-119.131 259.365  1.00140.70           C  
ANISOU 1750  C   GLU A 325    14103  14237  25119   -508   -317   1935       C  
ATOM   1751  O   GLU A 325     -31.831-119.755 260.251  1.00143.98           O  
ANISOU 1751  O   GLU A 325    14567  14559  25579   -508   -492   2030       O  
ATOM   1752  CB  GLU A 325     -32.637-120.301 257.154  1.00137.72           C  
ANISOU 1752  CB  GLU A 325    13479  14275  24575    -13    486   1898       C  
ATOM   1753  CG  GLU A 325     -33.396-121.325 256.322  1.00139.97           C  
ANISOU 1753  CG  GLU A 325    13958  14645  24579    256    857   1546       C  
ATOM   1754  CD  GLU A 325     -32.730-121.605 254.989  1.00145.95           C  
ANISOU 1754  CD  GLU A 325    14430  15717  25308    653   1179   1743       C  
ATOM   1755  OE1 GLU A 325     -31.708-120.954 254.684  1.00146.30           O  
ANISOU 1755  OE1 GLU A 325    14046  15962  25580    706   1179   2246       O  
ATOM   1756  OE2 GLU A 325     -33.230-122.475 254.245  1.00150.60           O  
ANISOU 1756  OE2 GLU A 325    15220  16353  25649    937   1413   1413       O  
ATOM   1757  N   THR A 326     -32.270-117.816 259.197  1.00140.05           N  
ANISOU 1757  N   THR A 326    13871  14096  25247   -692   -588   2089       N  
ATOM   1758  CA  THR A 326     -31.499-117.034 260.156  1.00142.86           C  
ANISOU 1758  CA  THR A 326    14192  14204  25886   -932  -1190   2283       C  
ATOM   1759  C   THR A 326     -32.303-116.752 261.420  1.00143.08           C  
ANISOU 1759  C   THR A 326    14793  13991  25579  -1010  -1504   1838       C  
ATOM   1760  O   THR A 326     -31.731-116.702 262.516  1.00141.83           O  
ANISOU 1760  O   THR A 326    14780  13658  25452  -1094  -1972   1865       O  
ATOM   1761  CB  THR A 326     -31.035-115.721 259.518  1.00142.75           C  
ANISOU 1761  CB  THR A 326    13800  14129  26308  -1115  -1434   2640       C  
ATOM   1762  OG1 THR A 326     -30.504-115.983 258.212  1.00141.77           O  
ANISOU 1762  OG1 THR A 326    13155  14345  26366   -935   -996   3071       O  
ATOM   1763  CG2 THR A 326     -29.953-115.070 260.365  1.00145.93           C  
ANISOU 1763  CG2 THR A 326    14041  14240  27164  -1384  -2139   2951       C  
ATOM   1764  N   ILE A 327     -33.621-116.573 261.289  1.00143.40           N  
ANISOU 1764  N   ILE A 327    15158  14055  25274   -940  -1251   1453       N  
ATOM   1765  CA  ILE A 327     -34.475-116.391 262.461  1.00142.01           C  
ANISOU 1765  CA  ILE A 327    15517  13741  24699   -896  -1422   1073       C  
ATOM   1766  C   ILE A 327     -34.467-117.646 263.323  1.00143.47           C  
ANISOU 1766  C   ILE A 327    15889  14002  24620   -766  -1303   1038       C  
ATOM   1767  O   ILE A 327     -34.416-117.573 264.557  1.00143.74           O  
ANISOU 1767  O   ILE A 327    16262  13939  24415   -720  -1630    931       O  
ATOM   1768  CB  ILE A 327     -35.907-116.020 262.027  1.00136.74           C  
ANISOU 1768  CB  ILE A 327    15049  13143  23763   -812  -1090    773       C  
ATOM   1769  CG1 ILE A 327     -35.960-114.606 261.444  1.00140.14           C  
ANISOU 1769  CG1 ILE A 327    15379  13431  24435   -927  -1307    799       C  
ATOM   1770  CG2 ILE A 327     -36.864-116.133 263.197  1.00135.15           C  
ANISOU 1770  CG2 ILE A 327    15344  12918  23089   -654  -1087    464       C  
ATOM   1771  CD1 ILE A 327     -35.943-113.514 262.485  1.00147.08           C  
ANISOU 1771  CD1 ILE A 327    16635  13976  25272   -958  -1881    598       C  
ATOM   1772  N   ALA A 328     -34.503-118.819 262.684  1.00146.20           N  
ANISOU 1772  N   ALA A 328    16038  14511  25002   -673   -859   1133       N  
ATOM   1773  CA  ALA A 328     -34.645-120.070 263.422  1.00147.24           C  
ANISOU 1773  CA  ALA A 328    16332  14670  24944   -554   -705   1131       C  
ATOM   1774  C   ALA A 328     -33.417-120.367 264.273  1.00153.02           C  
ANISOU 1774  C   ALA A 328    17002  15339  25800   -568  -1072   1388       C  
ATOM   1775  O   ALA A 328     -33.541-120.912 265.376  1.00157.04           O  
ANISOU 1775  O   ALA A 328    17773  15841  26052   -482  -1157   1378       O  
ATOM   1776  CB  ALA A 328     -34.909-121.222 262.454  1.00143.43           C  
ANISOU 1776  CB  ALA A 328    15668  14273  24556   -452   -238   1143       C  
ATOM   1777  N   ARG A 329     -32.225-120.021 263.783  1.00152.80           N  
ANISOU 1777  N   ARG A 329    16590  15295  26170   -661  -1291   1685       N  
ATOM   1778  CA  ARG A 329     -31.008-120.422 264.481  1.00154.48           C  
ANISOU 1778  CA  ARG A 329    16648  15471  26574   -676  -1628   2003       C  
ATOM   1779  C   ARG A 329     -30.854-119.696 265.812  1.00155.27           C  
ANISOU 1779  C   ARG A 329    17090  15419  26488   -771  -2257   1897       C  
ATOM   1780  O   ARG A 329     -30.459-120.310 266.809  1.00157.42           O  
ANISOU 1780  O   ARG A 329    17502  15700  26610   -696  -2460   1990       O  
ATOM   1781  CB  ARG A 329     -29.790-120.205 263.586  1.00159.27           C  
ANISOU 1781  CB  ARG A 329    16675  16137  27702   -733  -1681   2443       C  
ATOM   1782  CG  ARG A 329     -29.448-121.445 262.780  1.00162.66           C  
ANISOU 1782  CG  ARG A 329    16826  16738  28238   -481  -1158   2632       C  
ATOM   1783  CD  ARG A 329     -28.609-121.138 261.558  1.00168.04           C  
ANISOU 1783  CD  ARG A 329    16951  17594  29302   -409   -987   3028       C  
ATOM   1784  NE  ARG A 329     -28.610-122.271 260.637  1.00168.87           N  
ANISOU 1784  NE  ARG A 329    16949  17869  29343    -51   -416   3027       N  
ATOM   1785  CZ  ARG A 329     -28.038-122.265 259.438  1.00170.43           C  
ANISOU 1785  CZ  ARG A 329    16733  18312  29712    186    -94   3321       C  
ATOM   1786  NH1 ARG A 329     -27.411-121.181 259.004  1.00172.70           N  
ANISOU 1786  NH1 ARG A 329    16585  18718  30314     54   -256   3742       N  
ATOM   1787  NH2 ARG A 329     -28.096-123.346 258.672  1.00169.99           N  
ANISOU 1787  NH2 ARG A 329    16704  18373  29512    588    378   3213       N  
ATOM   1788  N   GLU A 330     -31.160-118.395 265.857  1.00155.46           N  
ANISOU 1788  N   GLU A 330    17283  15287  26497   -899  -2603   1689       N  
ATOM   1789  CA  GLU A 330     -31.174-117.700 267.142  1.00154.68           C  
ANISOU 1789  CA  GLU A 330    17652  15011  26108   -898  -3227   1453       C  
ATOM   1790  C   GLU A 330     -32.140-118.371 268.110  1.00151.16           C  
ANISOU 1790  C   GLU A 330    17713  14718  25003   -613  -2970   1192       C  
ATOM   1791  O   GLU A 330     -31.805-118.592 269.279  1.00153.94           O  
ANISOU 1791  O   GLU A 330    18350  15081  25059   -498  -3336   1187       O  
ATOM   1792  CB  GLU A 330     -31.537-116.226 266.951  1.00152.78           C  
ANISOU 1792  CB  GLU A 330    17582  14521  25947  -1017  -3585   1200       C  
ATOM   1793  CG  GLU A 330     -32.190-115.561 268.166  1.00154.28           C  
ANISOU 1793  CG  GLU A 330    18475  14566  25579   -830  -3996    729       C  
ATOM   1794  CD  GLU A 330     -31.330-115.589 269.419  1.00158.74           C  
ANISOU 1794  CD  GLU A 330    19294  15016  26005   -806  -4716    732       C  
ATOM   1795  OE1 GLU A 330     -31.824-116.056 270.468  1.00157.47           O  
ANISOU 1795  OE1 GLU A 330    19617  15024  25191   -491  -4664    523       O  
ATOM   1796  OE2 GLU A 330     -30.164-115.146 269.357  1.00163.67           O  
ANISOU 1796  OE2 GLU A 330    19610  15403  27176  -1093  -5345    989       O  
ATOM   1797  N   LEU A 331     -33.337-118.718 267.636  1.00144.20           N  
ANISOU 1797  N   LEU A 331    16912  13980  23896   -488  -2351   1031       N  
ATOM   1798  CA  LEU A 331     -34.259-119.489 268.462  1.00143.82           C  
ANISOU 1798  CA  LEU A 331    17203  14115  23328   -229  -2019    946       C  
ATOM   1799  C   LEU A 331     -33.673-120.854 268.802  1.00148.82           C  
ANISOU 1799  C   LEU A 331    17660  14845  24040   -182  -1876   1279       C  
ATOM   1800  O   LEU A 331     -33.716-121.290 269.959  1.00153.10           O  
ANISOU 1800  O   LEU A 331    18483  15494  24196      9  -1980   1345       O  
ATOM   1801  CB  LEU A 331     -35.603-119.639 267.749  1.00140.97           C  
ANISOU 1801  CB  LEU A 331    16829  13861  22871   -171  -1417    809       C  
ATOM   1802  CG  LEU A 331     -36.340-118.339 267.427  1.00145.11           C  
ANISOU 1802  CG  LEU A 331    17533  14312  23290   -163  -1484    502       C  
ATOM   1803  CD1 LEU A 331     -37.561-118.615 266.562  1.00144.01           C  
ANISOU 1803  CD1 LEU A 331    17260  14300  23157   -148   -897    449       C  
ATOM   1804  CD2 LEU A 331     -36.736-117.621 268.708  1.00151.00           C  
ANISOU 1804  CD2 LEU A 331    18838  15055  23480    110  -1799    249       C  
ATOM   1805  N   ALA A 332     -33.109-121.540 267.805  1.00147.95           N  
ANISOU 1805  N   ALA A 332    17098  14711  24405   -301  -1632   1507       N  
ATOM   1806  CA  ALA A 332     -32.553-122.867 268.044  1.00149.57           C  
ANISOU 1806  CA  ALA A 332    17134  14953  24743   -221  -1480   1817       C  
ATOM   1807  C   ALA A 332     -31.321-122.794 268.942  1.00157.11           C  
ANISOU 1807  C   ALA A 332    18066  15889  25739   -234  -2039   2052       C  
ATOM   1808  O   ALA A 332     -31.179-123.591 269.877  1.00160.39           O  
ANISOU 1808  O   ALA A 332    18613  16380  25948    -89  -2071   2234       O  
ATOM   1809  CB  ALA A 332     -32.226-123.548 266.714  1.00143.79           C  
ANISOU 1809  CB  ALA A 332    15983  14187  24466   -253  -1106   1943       C  
ATOM   1810  N   ASP A 333     -30.429-121.827 268.689  1.00160.12           N  
ANISOU 1810  N   ASP A 333    18256  16165  26417   -419  -2521   2097       N  
ATOM   1811  CA  ASP A 333     -29.261-121.651 269.550  1.00163.58           C  
ANISOU 1811  CA  ASP A 333    18650  16553  26950   -479  -3178   2325       C  
ATOM   1812  C   ASP A 333     -29.677-121.256 270.962  1.00167.12           C  
ANISOU 1812  C   ASP A 333    19699  17024  26775   -330  -3605   2065       C  
ATOM   1813  O   ASP A 333     -29.051-121.677 271.940  1.00171.53           O  
ANISOU 1813  O   ASP A 333    20354  17646  27172   -240  -3966   2250       O  
ATOM   1814  CB  ASP A 333     -28.312-120.617 268.936  1.00167.79           C  
ANISOU 1814  CB  ASP A 333    18801  16924  28027   -755  -3648   2480       C  
ATOM   1815  CG  ASP A 333     -27.014-120.448 269.725  1.00178.82           C  
ANISOU 1815  CG  ASP A 333    20042  18237  29666   -880  -4408   2791       C  
ATOM   1816  OD1 ASP A 333     -26.642-121.353 270.508  1.00180.87           O  
ANISOU 1816  OD1 ASP A 333    20354  18614  29755   -732  -4456   2981       O  
ATOM   1817  OD2 ASP A 333     -26.352-119.403 269.541  1.00185.13           O  
ANISOU 1817  OD2 ASP A 333    20626  18834  30883  -1145  -4991   2891       O  
ATOM   1818  N   ALA A 334     -30.744-120.466 271.094  1.00166.58           N  
ANISOU 1818  N   ALA A 334    20053  16936  26303   -242  -3552   1646       N  
ATOM   1819  CA  ALA A 334     -31.215-120.109 272.428  1.00171.74           C  
ANISOU 1819  CA  ALA A 334    21335  17670  26248     34  -3882   1376       C  
ATOM   1820  C   ALA A 334     -31.748-121.328 273.171  1.00171.78           C  
ANISOU 1820  C   ALA A 334    21493  17972  25804    336  -3415   1577       C  
ATOM   1821  O   ALA A 334     -31.567-121.447 274.388  1.00175.93           O  
ANISOU 1821  O   ALA A 334    22381  18642  25821    584  -3752   1601       O  
ATOM   1822  CB  ALA A 334     -32.291-119.031 272.347  1.00172.57           C  
ANISOU 1822  CB  ALA A 334    21840  17707  26020    147  -3837    911       C  
ATOM   1823  N   GLY A 335     -32.408-122.239 272.460  1.00167.94           N  
ANISOU 1823  N   GLY A 335    20735  17567  25506    328  -2680   1745       N  
ATOM   1824  CA  GLY A 335     -32.991-123.406 273.091  1.00169.94           C  
ANISOU 1824  CA  GLY A 335    21065  18040  25463    569  -2228   2013       C  
ATOM   1825  C   GLY A 335     -34.473-123.548 272.815  1.00169.84           C  
ANISOU 1825  C   GLY A 335    21143  18140  25251    685  -1602   1921       C  
ATOM   1826  O   GLY A 335     -35.245-123.949 273.694  1.00173.80           O  
ANISOU 1826  O   GLY A 335    21882  18886  25267    979  -1343   2072       O  
ATOM   1827  N   TYR A 336     -34.879-123.218 271.592  1.00166.66           N  
ANISOU 1827  N   TYR A 336    20511  17588  25224    471  -1356   1731       N  
ATOM   1828  CA  TYR A 336     -36.260-123.334 271.146  1.00166.15           C  
ANISOU 1828  CA  TYR A 336    20441  17598  25092    516   -809   1662       C  
ATOM   1829  C   TYR A 336     -36.392-124.499 270.175  1.00167.74           C  
ANISOU 1829  C   TYR A 336    20233  17666  25837    333   -395   1866       C  
ATOM   1830  O   TYR A 336     -35.605-124.617 269.230  1.00167.28           O  
ANISOU 1830  O   TYR A 336    19893  17432  26236    146   -476   1834       O  
ATOM   1831  CB  TYR A 336     -36.729-122.044 270.467  1.00163.26           C  
ANISOU 1831  CB  TYR A 336    20162  17159  24712    438   -882   1265       C  
ATOM   1832  CG  TYR A 336     -37.414-121.053 271.380  1.00167.59           C  
ANISOU 1832  CG  TYR A 336    21200  17854  24624    749  -1020   1016       C  
ATOM   1833  CD1 TYR A 336     -38.798-121.008 271.467  1.00167.75           C  
ANISOU 1833  CD1 TYR A 336    21320  18071  24347    962   -542   1009       C  
ATOM   1834  CD2 TYR A 336     -36.681-120.149 272.139  1.00173.07           C  
ANISOU 1834  CD2 TYR A 336    22258  18474  25027    860  -1658    787       C  
ATOM   1835  CE1 TYR A 336     -39.437-120.098 272.286  1.00171.75           C  
ANISOU 1835  CE1 TYR A 336    22292  18740  24224   1352   -613    781       C  
ATOM   1836  CE2 TYR A 336     -37.311-119.233 272.967  1.00176.94           C  
ANISOU 1836  CE2 TYR A 336    23284  19066  24878   1235  -1815    481       C  
ATOM   1837  CZ  TYR A 336     -38.691-119.213 273.036  1.00175.65           C  
ANISOU 1837  CZ  TYR A 336    23227  19142  24370   1517  -1249    479       C  
ATOM   1838  OH  TYR A 336     -39.327-118.309 273.855  1.00178.47           O  
ANISOU 1838  OH  TYR A 336    24133  19633  24045   1992  -1350    182       O  
ATOM   1839  N   GLU A 337     -37.382-125.360 270.406  1.00171.32           N  
ANISOU 1839  N   GLU A 337    20651  18192  26251    417     28   2097       N  
ATOM   1840  CA  GLU A 337     -37.746-126.330 269.385  1.00170.26           C  
ANISOU 1840  CA  GLU A 337    20195  17847  26648    234    350   2180       C  
ATOM   1841  C   GLU A 337     -38.309-125.586 268.187  1.00167.20           C  
ANISOU 1841  C   GLU A 337    19724  17401  26406     81    441   1821       C  
ATOM   1842  O   GLU A 337     -39.264-124.813 268.320  1.00170.25           O  
ANISOU 1842  O   GLU A 337    20247  17939  26501    144    552   1690       O  
ATOM   1843  CB  GLU A 337     -38.777-127.325 269.910  1.00174.76           C  
ANISOU 1843  CB  GLU A 337    20706  18458  27235    305    711   2558       C  
ATOM   1844  CG  GLU A 337     -39.164-128.386 268.887  1.00176.77           C  
ANISOU 1844  CG  GLU A 337    20669  18389  28106     93    917   2611       C  
ATOM   1845  CD  GLU A 337     -40.650-128.684 268.886  1.00181.74           C  
ANISOU 1845  CD  GLU A 337    21186  19048  28818     41   1236   2805       C  
ATOM   1846  OE1 GLU A 337     -41.267-128.659 269.973  1.00186.93           O  
ANISOU 1846  OE1 GLU A 337    21912  19983  29130    231   1412   3167       O  
ATOM   1847  OE2 GLU A 337     -41.203-128.936 267.796  1.00180.74           O  
ANISOU 1847  OE2 GLU A 337    20889  18692  29092   -163   1301   2625       O  
ATOM   1848  N   VAL A 338     -37.714-125.810 267.018  1.00161.55           N  
ANISOU 1848  N   VAL A 338    18784  16494  26102    -65    413   1685       N  
ATOM   1849  CA  VAL A 338     -38.092-125.109 265.799  1.00156.67           C  
ANISOU 1849  CA  VAL A 338    18070  15857  25600   -180    476   1377       C  
ATOM   1850  C   VAL A 338     -38.678-126.106 264.809  1.00155.80           C  
ANISOU 1850  C   VAL A 338    17785  15566  25845   -260    720   1337       C  
ATOM   1851  O   VAL A 338     -38.205-127.242 264.692  1.00157.40           O  
ANISOU 1851  O   VAL A 338    17899  15571  26335   -235    743   1469       O  
ATOM   1852  CB  VAL A 338     -36.897-124.356 265.175  1.00154.19           C  
ANISOU 1852  CB  VAL A 338    17641  15533  25410   -224    218   1267       C  
ATOM   1853  CG1 VAL A 338     -36.332-123.349 266.169  1.00153.62           C  
ANISOU 1853  CG1 VAL A 338    17761  15545  25065   -190   -161   1278       C  
ATOM   1854  CG2 VAL A 338     -35.806-125.322 264.717  1.00155.97           C  
ANISOU 1854  CG2 VAL A 338    17644  15636  25983   -183    216   1428       C  
ATOM   1855  N   ASP A 339     -39.728-125.677 264.106  1.00152.63           N  
ANISOU 1855  N   ASP A 339    17355  15205  25433   -343    857   1143       N  
ATOM   1856  CA  ASP A 339     -40.374-126.463 263.058  1.00149.13           C  
ANISOU 1856  CA  ASP A 339    16781  14575  25308   -435    977   1025       C  
ATOM   1857  C   ASP A 339     -40.674-125.521 261.890  1.00144.52           C  
ANISOU 1857  C   ASP A 339    16146  14106  24659   -476    980    715       C  
ATOM   1858  O   ASP A 339     -41.830-125.219 261.593  1.00146.44           O  
ANISOU 1858  O   ASP A 339    16359  14408  24873   -561   1073    641       O  
ATOM   1859  CB  ASP A 339     -41.640-127.142 263.571  1.00149.11           C  
ANISOU 1859  CB  ASP A 339    16737  14500  25419   -522   1128   1251       C  
ATOM   1860  CG  ASP A 339     -42.273-128.055 262.536  1.00148.82           C  
ANISOU 1860  CG  ASP A 339    16576  14169  25802   -661   1115   1123       C  
ATOM   1861  OD1 ASP A 339     -41.566-128.944 262.016  1.00150.61           O  
ANISOU 1861  OD1 ASP A 339    16813  14118  26294   -615   1009   1020       O  
ATOM   1862  OD2 ASP A 339     -43.475-127.877 262.240  1.00146.21           O  
ANISOU 1862  OD2 ASP A 339    16146  13870  25536   -791   1177   1119       O  
ATOM   1863  N   SER A 340     -39.618-125.036 261.244  1.00140.89           N  
ANISOU 1863  N   SER A 340    15633  13708  24191   -402    886    606       N  
ATOM   1864  CA  SER A 340     -39.789-124.196 260.068  1.00142.29           C  
ANISOU 1864  CA  SER A 340    15727  14022  24317   -405    908    391       C  
ATOM   1865  C   SER A 340     -40.433-125.000 258.946  1.00140.55           C  
ANISOU 1865  C   SER A 340    15471  13690  24244   -394    982    179       C  
ATOM   1866  O   SER A 340     -40.051-126.145 258.680  1.00141.04           O  
ANISOU 1866  O   SER A 340    15552  13540  24496   -302    967    140       O  
ATOM   1867  CB  SER A 340     -38.444-123.635 259.602  1.00147.16           C  
ANISOU 1867  CB  SER A 340    16213  14744  24956   -303    820    453       C  
ATOM   1868  OG  SER A 340     -37.750-124.573 258.800  1.00152.26           O  
ANISOU 1868  OG  SER A 340    16768  15328  25757   -127    894    428       O  
ATOM   1869  N   ARG A 341     -41.423-124.398 258.292  1.00139.19           N  
ANISOU 1869  N   ARG A 341    15268  13632  23986   -470   1018     24       N  
ATOM   1870  CA  ARG A 341     -42.174-125.064 257.235  1.00136.65           C  
ANISOU 1870  CA  ARG A 341    14938  13204  23780   -482    991   -211       C  
ATOM   1871  C   ARG A 341     -42.471-124.080 256.115  1.00124.22           C  
ANISOU 1871  C   ARG A 341    13295  11889  22014   -433   1010   -381       C  
ATOM   1872  O   ARG A 341     -42.965-122.978 256.370  1.00118.05           O  
ANISOU 1872  O   ARG A 341    12462  11287  21105   -519   1057   -298       O  
ATOM   1873  CB  ARG A 341     -43.484-125.655 257.773  1.00142.95           C  
ANISOU 1873  CB  ARG A 341    15716  13825  24772   -692    972   -119       C  
ATOM   1874  CG  ARG A 341     -43.295-126.879 258.653  1.00151.18           C  
ANISOU 1874  CG  ARG A 341    16793  14564  26083   -733    943     88       C  
ATOM   1875  CD  ARG A 341     -44.623-127.432 259.144  1.00158.69           C  
ANISOU 1875  CD  ARG A 341    17629  15363  27304   -955    939    310       C  
ATOM   1876  NE  ARG A 341     -44.449-128.679 259.884  1.00168.56           N  
ANISOU 1876  NE  ARG A 341    18874  16284  28888  -1003    897    569       N  
ATOM   1877  CZ  ARG A 341     -45.443-129.359 260.444  1.00177.60           C  
ANISOU 1877  CZ  ARG A 341    19855  17249  30377  -1199    896    914       C  
ATOM   1878  NH1 ARG A 341     -46.687-128.909 260.353  1.00176.84           N  
ANISOU 1878  NH1 ARG A 341    19569  17298  30322  -1354    945   1038       N  
ATOM   1879  NH2 ARG A 341     -45.195-130.487 261.099  1.00185.22           N  
ANISOU 1879  NH2 ARG A 341    20799  17895  31683  -1233    853   1203       N  
ATOM   1880  N   ASP A 342     -42.166-124.480 254.882  1.00120.47           N  
ANISOU 1880  N   ASP A 342    12842  11440  21492   -243    974   -614       N  
ATOM   1881  CA  ASP A 342     -42.553-123.689 253.724  1.00112.83           C  
ANISOU 1881  CA  ASP A 342    11811  10747  20311   -162    988   -755       C  
ATOM   1882  C   ASP A 342     -44.070-123.570 253.669  1.00108.09           C  
ANISOU 1882  C   ASP A 342    11185  10111  19772   -393    897   -833       C  
ATOM   1883  O   ASP A 342     -44.794-124.534 253.930  1.00112.29           O  
ANISOU 1883  O   ASP A 342    11761  10360  20544   -544    761   -894       O  
ATOM   1884  CB  ASP A 342     -42.019-124.337 252.443  1.00119.62           C  
ANISOU 1884  CB  ASP A 342    12763  11659  21029    176    959  -1015       C  
ATOM   1885  CG  ASP A 342     -42.012-123.387 251.261  1.00123.63           C  
ANISOU 1885  CG  ASP A 342    13174  12574  21227    369   1041  -1042       C  
ATOM   1886  OD1 ASP A 342     -42.859-122.468 251.218  1.00131.54           O  
ANISOU 1886  OD1 ASP A 342    14072  13719  22187    179   1032   -977       O  
ATOM   1887  OD2 ASP A 342     -41.154-123.565 250.370  1.00118.27           O  
ANISOU 1887  OD2 ASP A 342    12509  12095  20332    757   1140  -1089       O  
ATOM   1888  N   ALA A 343     -44.554-122.372 253.333  1.00107.13           N  
ANISOU 1888  N   ALA A 343    10950  10263  19491   -425    960   -773       N  
ATOM   1889  CA  ALA A 343     -45.994-122.149 253.280  1.00108.33           C  
ANISOU 1889  CA  ALA A 343    11018  10433  19710   -616    899   -780       C  
ATOM   1890  C   ALA A 343     -46.668-122.974 252.192  1.00106.69           C  
ANISOU 1890  C   ALA A 343    10847  10138  19552   -617    658  -1068       C  
ATOM   1891  O   ALA A 343     -47.891-123.150 252.233  1.00107.12           O  
ANISOU 1891  O   ALA A 343    10794  10113  19795   -833    526  -1040       O  
ATOM   1892  CB  ALA A 343     -46.292-120.664 253.065  1.00108.01           C  
ANISOU 1892  CB  ALA A 343    10858  10688  19493   -596   1011   -657       C  
ATOM   1893  N   ALA A 344     -45.904-123.482 251.223  1.00103.86           N  
ANISOU 1893  N   ALA A 344    10640   9799  19025   -350    574  -1334       N  
ATOM   1894  CA  ALA A 344     -46.475-124.277 250.144  1.00109.31           C  
ANISOU 1894  CA  ALA A 344    11465  10378  19692   -279    257  -1705       C  
ATOM   1895  C   ALA A 344     -46.885-125.675 250.589  1.00124.44           C  
ANISOU 1895  C   ALA A 344    13489  11769  22025   -470    -28  -1830       C  
ATOM   1896  O   ALA A 344     -47.575-126.368 249.833  1.00125.46           O  
ANISOU 1896  O   ALA A 344    13727  11686  22255   -506   -417  -2140       O  
ATOM   1897  CB  ALA A 344     -45.480-124.370 248.985  1.00105.17           C  
ANISOU 1897  CB  ALA A 344    11120  10078  18762    192    289  -1957       C  
ATOM   1898  N   SER A 345     -46.484-126.106 251.796  1.00129.74           N  
ANISOU 1898  N   SER A 345    14130  12203  22963   -596    109  -1577       N  
ATOM   1899  CA  SER A 345     -46.783-127.447 252.308  1.00135.71           C  
ANISOU 1899  CA  SER A 345    14947  12431  24186   -780   -134  -1586       C  
ATOM   1900  C   SER A 345     -47.194-127.314 253.776  1.00137.94           C  
ANISOU 1900  C   SER A 345    15002  12670  24738  -1067     75  -1082       C  
ATOM   1901  O   SER A 345     -46.434-127.641 254.690  1.00139.20           O  
ANISOU 1901  O   SER A 345    15202  12726  24962  -1019    239   -881       O  
ATOM   1902  CB  SER A 345     -45.588-128.385 252.143  1.00134.61           C  
ANISOU 1902  CB  SER A 345    15074  12039  24033   -472   -172  -1810       C  
ATOM   1903  OG  SER A 345     -44.416-127.825 252.711  1.00129.05           O  
ANISOU 1903  OG  SER A 345    14329  11599  23104   -286    194  -1578       O  
ATOM   1904  N   VAL A 346     -48.414-126.827 254.002  1.00141.88           N  
ANISOU 1904  N   VAL A 346    15256  13290  25365  -1317     80   -849       N  
ATOM   1905  CA  VAL A 346     -48.944-126.652 255.348  1.00145.72           C  
ANISOU 1905  CA  VAL A 346    15522  13822  26024  -1494    324   -340       C  
ATOM   1906  C   VAL A 346     -50.389-127.128 255.390  1.00157.23           C  
ANISOU 1906  C   VAL A 346    16683  15105  27950  -1814    126    -87       C  
ATOM   1907  O   VAL A 346     -51.112-127.083 254.389  1.00157.37           O  
ANISOU 1907  O   VAL A 346    16631  15109  28055  -1917   -167   -298       O  
ATOM   1908  CB  VAL A 346     -48.850-125.185 255.830  1.00141.24           C  
ANISOU 1908  CB  VAL A 346    14909  13717  25038  -1360    678   -178       C  
ATOM   1909  CG1 VAL A 346     -47.398-124.772 256.014  1.00137.79           C  
ANISOU 1909  CG1 VAL A 346    14688  13387  24279  -1117    818   -296       C  
ATOM   1910  CG2 VAL A 346     -49.562-124.256 254.857  1.00141.52           C  
ANISOU 1910  CG2 VAL A 346    14841  14025  24903  -1356    628   -323       C  
ATOM   1911  N   GLU A 347     -50.803-127.592 256.566  1.00166.14           N  
ANISOU 1911  N   GLU A 347    17608  16126  29393  -1960    278    424       N  
ATOM   1912  CA  GLU A 347     -52.181-127.983 256.828  1.00175.72           C  
ANISOU 1912  CA  GLU A 347    18417  17233  31117  -2264    178    876       C  
ATOM   1913  C   GLU A 347     -52.851-126.888 257.648  1.00175.62           C  
ANISOU 1913  C   GLU A 347    18165  17724  30839  -2158    637   1324       C  
ATOM   1914  O   GLU A 347     -52.309-126.451 258.668  1.00173.29           O  
ANISOU 1914  O   GLU A 347    17991  17660  30193  -1924   1014   1510       O  
ATOM   1915  CB  GLU A 347     -52.234-129.322 257.565  1.00185.50           C  
ANISOU 1915  CB  GLU A 347    19530  18010  32943  -2464     56   1258       C  
ATOM   1916  CG  GLU A 347     -51.502-130.446 256.843  1.00192.86           C  
ANISOU 1916  CG  GLU A 347    20765  18370  34142  -2496   -402    785       C  
ATOM   1917  CD  GLU A 347     -51.138-131.598 257.762  1.00198.97           C  
ANISOU 1917  CD  GLU A 347    21508  18725  35367  -2578   -408   1157       C  
ATOM   1918  OE1 GLU A 347     -51.693-131.672 258.878  1.00202.18           O  
ANISOU 1918  OE1 GLU A 347    21576  19257  35988  -2687   -123   1861       O  
ATOM   1919  OE2 GLU A 347     -50.289-132.427 257.369  1.00201.08           O  
ANISOU 1919  OE2 GLU A 347    22088  18560  35752  -2485   -675    775       O  
ATOM   1920  N   ALA A 348     -54.027-126.447 257.196  1.00179.28           N  
ANISOU 1920  N   ALA A 348    18311  18353  31454  -2291    575   1480       N  
ATOM   1921  CA  ALA A 348     -54.673-125.282 257.795  1.00178.96           C  
ANISOU 1921  CA  ALA A 348    18084  18811  31103  -2095   1015   1824       C  
ATOM   1922  C   ALA A 348     -55.133-125.567 259.220  1.00182.26           C  
ANISOU 1922  C   ALA A 348    18247  19355  31648  -2026   1402   2533       C  
ATOM   1923  O   ALA A 348     -54.679-124.924 260.174  1.00180.80           O  
ANISOU 1923  O   ALA A 348    18265  19466  30966  -1682   1804   2627       O  
ATOM   1924  CB  ALA A 348     -55.851-124.839 256.928  1.00182.20           C  
ANISOU 1924  CB  ALA A 348    18162  19360  31706  -2247    840   1878       C  
ATOM   1925  N   GLY A 349     -56.042-126.526 259.381  1.00187.36           N  
ANISOU 1925  N   GLY A 349    18442  19783  32963  -2332   1261   3065       N  
ATOM   1926  CA  GLY A 349     -56.647-126.809 260.668  1.00191.57           C  
ANISOU 1926  CA  GLY A 349    18617  20512  33658  -2245   1672   3894       C  
ATOM   1927  C   GLY A 349     -55.667-127.220 261.747  1.00191.07           C  
ANISOU 1927  C   GLY A 349    18846  20424  33329  -2027   1914   4002       C  
ATOM   1928  O   GLY A 349     -54.910-128.180 261.578  1.00191.11           O  
ANISOU 1928  O   GLY A 349    19030  19973  33611  -2214   1604   3793       O  
ATOM   1929  N   GLY A 350     -55.678-126.496 262.864  1.00186.27           N  
ANISOU 1929  N   GLY A 350    18310  20306  32159  -1589   2448   4317       N  
ATOM   1930  CA  GLY A 350     -54.789-126.810 263.970  1.00180.19           C  
ANISOU 1930  CA  GLY A 350    17824  19586  31054  -1334   2665   4450       C  
ATOM   1931  C   GLY A 350     -53.323-126.647 263.645  1.00169.44           C  
ANISOU 1931  C   GLY A 350    17032  18019  29328  -1277   2425   3700       C  
ATOM   1932  O   GLY A 350     -52.488-127.377 264.191  1.00168.67           O  
ANISOU 1932  O   GLY A 350    17103  17732  29253  -1262   2380   3760       O  
ATOM   1933  N   LEU A 351     -52.983-125.703 262.765  1.00159.87           N  
ANISOU 1933  N   LEU A 351    16076  16858  27811  -1233   2277   3063       N  
ATOM   1934  CA  LEU A 351     -51.591-125.531 262.366  1.00154.42           C  
ANISOU 1934  CA  LEU A 351    15831  15996  26844  -1186   2057   2443       C  
ATOM   1935  C   LEU A 351     -50.730-125.024 263.515  1.00154.17           C  
ANISOU 1935  C   LEU A 351    16144  16195  26240   -824   2271   2455       C  
ATOM   1936  O   LEU A 351     -49.548-125.374 263.602  1.00152.03           O  
ANISOU 1936  O   LEU A 351    16127  15737  25901   -818   2107   2223       O  
ATOM   1937  CB  LEU A 351     -51.504-124.578 261.173  1.00151.63           C  
ANISOU 1937  CB  LEU A 351    15595  15698  26318  -1203   1889   1894       C  
ATOM   1938  CG  LEU A 351     -50.114-124.317 260.586  1.00149.88           C  
ANISOU 1938  CG  LEU A 351    15735  15353  25861  -1146   1683   1339       C  
ATOM   1939  CD1 LEU A 351     -49.467-125.616 260.131  1.00150.86           C  
ANISOU 1939  CD1 LEU A 351    15896  15064  26360  -1330   1408   1203       C  
ATOM   1940  CD2 LEU A 351     -50.193-123.323 259.437  1.00148.18           C  
ANISOU 1940  CD2 LEU A 351    15552  15263  25485  -1135   1579    952       C  
ATOM   1941  N   PHE A 352     -51.297-124.215 264.408  1.00159.69           N  
ANISOU 1941  N   PHE A 352    16866  17297  26512   -485   2610   2720       N  
ATOM   1942  CA  PHE A 352     -50.540-123.602 265.491  1.00164.71           C  
ANISOU 1942  CA  PHE A 352    17907  18152  26524    -88   2728   2646       C  
ATOM   1943  C   PHE A 352     -50.662-124.356 266.808  1.00172.82           C  
ANISOU 1943  C   PHE A 352    18879  19344  27440    119   2986   3241       C  
ATOM   1944  O   PHE A 352     -50.130-123.891 267.820  1.00172.77           O  
ANISOU 1944  O   PHE A 352    19231  19568  26845    508   3071   3214       O  
ATOM   1945  CB  PHE A 352     -50.987-122.151 265.704  1.00167.32           C  
ANISOU 1945  CB  PHE A 352    18429  18808  26338    279   2899   2472       C  
ATOM   1946  CG  PHE A 352     -50.711-121.239 264.538  1.00162.99           C  
ANISOU 1946  CG  PHE A 352    17980  18125  25823    138   2650   1922       C  
ATOM   1947  CD1 PHE A 352     -50.006-121.682 263.430  1.00158.96           C  
ANISOU 1947  CD1 PHE A 352    17425  17303  25672   -225   2330   1603       C  
ATOM   1948  CD2 PHE A 352     -51.156-119.927 264.561  1.00164.06           C  
ANISOU 1948  CD2 PHE A 352    18262  18461  25612    427   2755   1755       C  
ATOM   1949  CE1 PHE A 352     -49.762-120.839 262.365  1.00156.26           C  
ANISOU 1949  CE1 PHE A 352    17138  16908  25324   -304   2150   1194       C  
ATOM   1950  CE2 PHE A 352     -50.912-119.079 263.500  1.00161.80           C  
ANISOU 1950  CE2 PHE A 352    18029  18054  25393    299   2537   1337       C  
ATOM   1951  CZ  PHE A 352     -50.215-119.536 262.401  1.00157.77           C  
ANISOU 1951  CZ  PHE A 352    17431  17290  25225    -70   2248   1088       C  
ATOM   1952  N   GLU A 353     -51.343-125.501 266.818  1.00183.17           N  
ANISOU 1952  N   GLU A 353    19751  20533  29314   -126   3072   3795       N  
ATOM   1953  CA  GLU A 353     -51.619-126.214 268.060  1.00189.95           C  
ANISOU 1953  CA  GLU A 353    20457  21602  30114     86   3382   4524       C  
ATOM   1954  C   GLU A 353     -50.332-126.592 268.785  1.00186.52           C  
ANISOU 1954  C   GLU A 353    20393  21091  29385    222   3251   4416       C  
ATOM   1955  O   GLU A 353     -49.405-127.146 268.188  1.00182.91           O  
ANISOU 1955  O   GLU A 353    20035  20213  29251    -74   2898   4070       O  
ATOM   1956  CB  GLU A 353     -52.440-127.470 267.769  1.00199.21           C  
ANISOU 1956  CB  GLU A 353    21044  22502  32144   -323   3370   5142       C  
ATOM   1957  CG  GLU A 353     -52.370-128.518 268.869  1.00209.74           C  
ANISOU 1957  CG  GLU A 353    22201  23872  33617   -235   3568   5897       C  
ATOM   1958  CD  GLU A 353     -52.800-129.892 268.397  1.00216.18           C  
ANISOU 1958  CD  GLU A 353    22521  24164  35454   -763   3339   6350       C  
ATOM   1959  OE1 GLU A 353     -53.898-130.343 268.787  1.00223.23           O  
ANISOU 1959  OE1 GLU A 353    22861  25191  36765   -820   3592   7202       O  
ATOM   1960  OE2 GLU A 353     -52.040-130.520 267.629  1.00213.88           O  
ANISOU 1960  OE2 GLU A 353    22387  23309  35570  -1100   2888   5872       O  
ATOM   1961  N   GLY A 354     -50.282-126.286 270.080  1.00185.52           N  
ANISOU 1961  N   GLY A 354    20479  21401  28609    723   3536   4723       N  
ATOM   1962  CA  GLY A 354     -49.184-126.722 270.919  1.00183.10           C  
ANISOU 1962  CA  GLY A 354    20472  21086  28011    883   3418   4759       C  
ATOM   1963  C   GLY A 354     -47.900-125.940 270.783  1.00176.84           C  
ANISOU 1963  C   GLY A 354    20202  20184  26806    951   3030   4007       C  
ATOM   1964  O   GLY A 354     -46.852-126.415 271.230  1.00178.68           O  
ANISOU 1964  O   GLY A 354    20620  20305  26967    961   2822   3992       O  
ATOM   1965  N   PHE A 355     -47.942-124.753 270.185  1.00169.95           N  
ANISOU 1965  N   PHE A 355    19533  19328  25712    989   2908   3443       N  
ATOM   1966  CA  PHE A 355     -46.759-123.921 270.005  1.00161.28           C  
ANISOU 1966  CA  PHE A 355    18860  18093  24328   1011   2502   2800       C  
ATOM   1967  C   PHE A 355     -46.828-122.735 270.955  1.00161.10           C  
ANISOU 1967  C   PHE A 355    19299  18414  23498   1551   2525   2615       C  
ATOM   1968  O   PHE A 355     -47.785-121.953 270.910  1.00164.20           O  
ANISOU 1968  O   PHE A 355    19704  19018  23667   1788   2760   2582       O  
ATOM   1969  CB  PHE A 355     -46.635-123.443 268.559  1.00154.67           C  
ANISOU 1969  CB  PHE A 355    17917  16960  23892    648   2282   2310       C  
ATOM   1970  CG  PHE A 355     -46.065-124.472 267.629  1.00152.17           C  
ANISOU 1970  CG  PHE A 355    17355  16256  24206    222   2096   2266       C  
ATOM   1971  CD1 PHE A 355     -44.700-124.705 267.591  1.00152.11           C  
ANISOU 1971  CD1 PHE A 355    17503  16050  24241    150   1793   2061       C  
ATOM   1972  CD2 PHE A 355     -46.890-125.205 266.794  1.00152.16           C  
ANISOU 1972  CD2 PHE A 355    16977  16078  24758    -73   2191   2426       C  
ATOM   1973  CE1 PHE A 355     -44.168-125.651 266.737  1.00152.30           C  
ANISOU 1973  CE1 PHE A 355    17339  15735  24794   -135   1657   2005       C  
ATOM   1974  CE2 PHE A 355     -46.364-126.153 265.937  1.00152.20           C  
ANISOU 1974  CE2 PHE A 355    16848  15692  25289   -383   1976   2305       C  
ATOM   1975  CZ  PHE A 355     -45.001-126.376 265.908  1.00152.42           C  
ANISOU 1975  CZ  PHE A 355    17061  15552  25298   -377   1744   2088       C  
ATOM   1976  N   ASP A 356     -45.813-122.604 271.812  1.00157.12           N  
ANISOU 1976  N   ASP A 356    19192  17948  22561   1771   2242   2479       N  
ATOM   1977  CA  ASP A 356     -45.750-121.460 272.714  1.00156.02           C  
ANISOU 1977  CA  ASP A 356    19601  18052  21629   2308   2117   2182       C  
ATOM   1978  C   ASP A 356     -45.521-120.163 271.951  1.00147.91           C  
ANISOU 1978  C   ASP A 356    18785  16773  20642   2206   1778   1544       C  
ATOM   1979  O   ASP A 356     -45.957-119.096 272.397  1.00149.50           O  
ANISOU 1979  O   ASP A 356    19364  17122  20317   2645   1774   1285       O  
ATOM   1980  CB  ASP A 356     -44.647-121.671 273.751  1.00159.04           C  
ANISOU 1980  CB  ASP A 356    20357  18485  21588   2515   1768   2164       C  
ATOM   1981  CG  ASP A 356     -44.794-122.982 274.497  1.00162.60           C  
ANISOU 1981  CG  ASP A 356    20576  19172  22033   2611   2092   2857       C  
ATOM   1982  OD1 ASP A 356     -45.942-123.438 274.681  1.00165.20           O  
ANISOU 1982  OD1 ASP A 356    20604  19781  22382   2766   2636   3391       O  
ATOM   1983  OD2 ASP A 356     -43.761-123.559 274.899  1.00163.76           O  
ANISOU 1983  OD2 ASP A 356    20799  19222  22202   2525   1797   2930       O  
ATOM   1984  N   LEU A 357     -44.846-120.235 270.805  1.00138.29           N  
ANISOU 1984  N   LEU A 357    17330  15177  20036   1679   1505   1313       N  
ATOM   1985  CA  LEU A 357     -44.592-119.077 269.963  1.00130.12           C  
ANISOU 1985  CA  LEU A 357    16393  13897  19151   1528   1203    827       C  
ATOM   1986  C   LEU A 357     -44.741-119.490 268.507  1.00122.64           C  
ANISOU 1986  C   LEU A 357    14961  12756  18881   1043   1310    851       C  
ATOM   1987  O   LEU A 357     -44.349-120.596 268.126  1.00118.23           O  
ANISOU 1987  O   LEU A 357    14118  12088  18718    756   1342   1054       O  
ATOM   1988  CB  LEU A 357     -43.194-118.498 270.212  1.00129.08           C  
ANISOU 1988  CB  LEU A 357    16577  13512  18954   1467    578    485       C  
ATOM   1989  CG  LEU A 357     -42.840-117.225 269.445  1.00126.59           C  
ANISOU 1989  CG  LEU A 357    16349  12905  18846   1311    204     65       C  
ATOM   1990  CD1 LEU A 357     -43.818-116.110 269.777  1.00130.46           C  
ANISOU 1990  CD1 LEU A 357    17175  13486  18908   1726    301   -170       C  
ATOM   1991  CD2 LEU A 357     -41.413-116.799 269.744  1.00129.49           C  
ANISOU 1991  CD2 LEU A 357    16927  12999  19275   1189   -461   -139       C  
ATOM   1992  N   VAL A 358     -45.317-118.603 267.699  1.00122.76           N  
ANISOU 1992  N   VAL A 358    14914  12728  19003    998   1350    633       N  
ATOM   1993  CA  VAL A 358     -45.577-118.870 266.289  1.00119.14           C  
ANISOU 1993  CA  VAL A 358    14045  12145  19077    615   1438    625       C  
ATOM   1994  C   VAL A 358     -45.092-117.674 265.483  1.00117.97           C  
ANISOU 1994  C   VAL A 358    13968  11815  19041    511   1140    269       C  
ATOM   1995  O   VAL A 358     -45.578-116.554 265.674  1.00121.49           O  
ANISOU 1995  O   VAL A 358    14628  12288  19244    744   1116     96       O  
ATOM   1996  CB  VAL A 358     -47.067-119.136 266.021  1.00120.20           C  
ANISOU 1996  CB  VAL A 358    13895  12480  19295    653   1864    881       C  
ATOM   1997  CG1 VAL A 358     -47.306-119.336 264.541  1.00117.70           C  
ANISOU 1997  CG1 VAL A 358    13223  12028  19471    282   1848    799       C  
ATOM   1998  CG2 VAL A 358     -47.535-120.353 266.798  1.00123.13           C  
ANISOU 1998  CG2 VAL A 358    14108  13004  19672    715   2148   1357       C  
ATOM   1999  N   LEU A 359     -44.140-117.908 264.585  1.00116.41           N  
ANISOU 1999  N   LEU A 359    13578  11433  19219    200    931    201       N  
ATOM   2000  CA  LEU A 359     -43.546-116.854 263.773  1.00111.97           C  
ANISOU 2000  CA  LEU A 359    12992  10713  18839     76    656     -4       C  
ATOM   2001  C   LEU A 359     -44.027-116.997 262.337  1.00107.64           C  
ANISOU 2001  C   LEU A 359    12088  10213  18596   -121    849     12       C  
ATOM   2002  O   LEU A 359     -43.742-118.005 261.679  1.00102.99           O  
ANISOU 2002  O   LEU A 359    11269   9621  18240   -286    928     92       O  
ATOM   2003  CB  LEU A 359     -42.020-116.903 263.846  1.00115.12           C  
ANISOU 2003  CB  LEU A 359    13396  10932  19413    -64    275     -1       C  
ATOM   2004  CG  LEU A 359     -41.375-115.923 264.831  1.00123.36           C  
ANISOU 2004  CG  LEU A 359    14808  11811  20252     71   -180   -152       C  
ATOM   2005  CD1 LEU A 359     -42.094-115.932 266.167  1.00125.00           C  
ANISOU 2005  CD1 LEU A 359    15423  12154  19918    438    -94   -216       C  
ATOM   2006  CD2 LEU A 359     -39.910-116.253 265.023  1.00128.13           C  
ANISOU 2006  CD2 LEU A 359    15335  12273  21074    -93   -552    -40       C  
ATOM   2007  N   LEU A 360     -44.750-115.989 261.854  1.00113.03           N  
ANISOU 2007  N   LEU A 360    12758  10932  19255    -63    898    -82       N  
ATOM   2008  CA  LEU A 360     -45.340-115.996 260.520  1.00113.09           C  
ANISOU 2008  CA  LEU A 360    12458  11034  19477   -203   1056    -69       C  
ATOM   2009  C   LEU A 360     -44.581-115.010 259.643  1.00108.41           C  
ANISOU 2009  C   LEU A 360    11777  10348  19068   -291    835   -121       C  
ATOM   2010  O   LEU A 360     -44.751-113.794 259.776  1.00110.17           O  
ANISOU 2010  O   LEU A 360    12127  10479  19255   -196    708   -188       O  
ATOM   2011  CB  LEU A 360     -46.821-115.635 260.578  1.00117.09           C  
ANISOU 2011  CB  LEU A 360    12933  11700  19856    -60   1311    -31       C  
ATOM   2012  CG  LEU A 360     -47.666-116.479 261.527  1.00118.03           C  
ANISOU 2012  CG  LEU A 360    13069  11956  19821     66   1571    158       C  
ATOM   2013  CD1 LEU A 360     -49.143-116.183 261.332  1.00119.93           C  
ANISOU 2013  CD1 LEU A 360    13130  12396  20043    177   1848    297       C  
ATOM   2014  CD2 LEU A 360     -47.373-117.944 261.304  1.00114.22           C  
ANISOU 2014  CD2 LEU A 360    12399  11426  19572   -160   1593    281       C  
ATOM   2015  N   GLY A 361     -43.757-115.532 258.744  1.00107.88           N  
ANISOU 2015  N   GLY A 361    11482  10301  19207   -436    800    -54       N  
ATOM   2016  CA  GLY A 361     -43.006-114.718 257.800  1.00112.64           C  
ANISOU 2016  CA  GLY A 361    11897  10891  20011   -501    661     33       C  
ATOM   2017  C   GLY A 361     -43.572-114.873 256.400  1.00114.82           C  
ANISOU 2017  C   GLY A 361    11920  11394  20313   -509    864     52       C  
ATOM   2018  O   GLY A 361     -43.959-115.971 255.999  1.00114.59           O  
ANISOU 2018  O   GLY A 361    11833  11472  20233   -515   1014    -20       O  
ATOM   2019  N   CYS A 362     -43.624-113.767 255.664  1.00119.39           N  
ANISOU 2019  N   CYS A 362    12364  12019  20982   -501    822    150       N  
ATOM   2020  CA  CYS A 362     -44.134-113.804 254.303  1.00115.46           C  
ANISOU 2020  CA  CYS A 362    11638  11785  20446   -465    985    188       C  
ATOM   2021  C   CYS A 362     -43.515-112.678 253.496  1.00115.18           C  
ANISOU 2021  C   CYS A 362    11382  11801  20580   -452    909    451       C  
ATOM   2022  O   CYS A 362     -43.389-111.550 253.981  1.00117.26           O  
ANISOU 2022  O   CYS A 362    11701  11839  21015   -493    725    540       O  
ATOM   2023  CB  CYS A 362     -45.660-113.689 254.263  1.00108.26           C  
ANISOU 2023  CB  CYS A 362    10762  10961  19411   -437   1112     70       C  
ATOM   2024  SG  CYS A 362     -46.333-113.708 252.586  1.00101.95           S  
ANISOU 2024  SG  CYS A 362     9704  10500  18534   -391   1215     99       S  
ATOM   2025  N   SER A 363     -43.137-112.993 252.262  1.00115.52           N  
ANISOU 2025  N   SER A 363    11185  12133  20574   -363   1038    590       N  
ATOM   2026  CA  SER A 363     -42.612-111.988 251.354  1.00119.09           C  
ANISOU 2026  CA  SER A 363    11348  12725  21175   -314   1036    958       C  
ATOM   2027  C   SER A 363     -43.755-111.243 250.678  1.00118.74           C  
ANISOU 2027  C   SER A 363    11246  12828  21043   -264   1107    965       C  
ATOM   2028  O   SER A 363     -44.810-111.819 250.392  1.00119.10           O  
ANISOU 2028  O   SER A 363    11377  13028  20846   -218   1208    715       O  
ATOM   2029  CB  SER A 363     -41.715-112.635 250.301  1.00117.27           C  
ANISOU 2029  CB  SER A 363    10881  12835  20840   -127   1206   1160       C  
ATOM   2030  OG  SER A 363     -41.419-111.717 249.265  1.00118.19           O  
ANISOU 2030  OG  SER A 363    10672  13203  21032    -20   1285   1588       O  
ATOM   2031  N   THR A 364     -43.542-109.954 250.429  1.00113.68           N  
ANISOU 2031  N   THR A 364    10431  12106  20657   -290   1015   1292       N  
ATOM   2032  CA  THR A 364     -44.539-109.118 249.779  1.00108.38           C  
ANISOU 2032  CA  THR A 364     9670  11558  19952   -225   1073   1377       C  
ATOM   2033  C   THR A 364     -44.246-109.057 248.286  1.00103.19           C  
ANISOU 2033  C   THR A 364     8680  11364  19163    -53   1248   1721       C  
ATOM   2034  O   THR A 364     -43.111-108.789 247.879  1.00 96.42           O  
ANISOU 2034  O   THR A 364     7559  10590  18486    -17   1264   2138       O  
ATOM   2035  CB  THR A 364     -44.548-107.712 250.378  1.00108.59           C  
ANISOU 2035  CB  THR A 364     9733  11173  20354   -315    846   1533       C  
ATOM   2036  OG1 THR A 364     -44.485-107.805 251.805  1.00110.23           O  
ANISOU 2036  OG1 THR A 364    10292  10973  20618   -397    649   1224       O  
ATOM   2037  CG2 THR A 364     -45.823-106.981 249.984  1.00 98.78           C  
ANISOU 2037  CG2 THR A 364     8480  10001  19051   -217    922   1524       C  
ATOM   2038  N   TRP A 365     -45.271-109.322 247.475  1.00108.95           N  
ANISOU 2038  N   TRP A 365     9403  12424  19569     78   1370   1583       N  
ATOM   2039  CA  TRP A 365     -45.137-109.371 246.021  1.00124.87           C  
ANISOU 2039  CA  TRP A 365    11180  14959  21304    329   1529   1837       C  
ATOM   2040  C   TRP A 365     -46.225-108.511 245.377  1.00135.83           C  
ANISOU 2040  C   TRP A 365    12452  16514  22643    384   1533   1972       C  
ATOM   2041  O   TRP A 365     -47.067-108.987 244.617  1.00134.69           O  
ANISOU 2041  O   TRP A 365    12336  16706  22133    517   1558   1785       O  
ATOM   2042  CB  TRP A 365     -45.194-110.813 245.520  1.00129.47           C  
ANISOU 2042  CB  TRP A 365    11924  15827  21443    503   1596   1465       C  
ATOM   2043  CG  TRP A 365     -44.011-111.623 245.945  1.00133.88           C  
ANISOU 2043  CG  TRP A 365    12540  16287  22041    533   1636   1427       C  
ATOM   2044  CD1 TRP A 365     -43.880-112.346 247.095  1.00136.22           C  
ANISOU 2044  CD1 TRP A 365    13069  16210  22478    342   1535   1115       C  
ATOM   2045  CD2 TRP A 365     -42.783-111.781 245.228  1.00135.25           C  
ANISOU 2045  CD2 TRP A 365    12500  16777  22113    808   1815   1780       C  
ATOM   2046  NE1 TRP A 365     -42.646-112.950 247.135  1.00137.32           N  
ANISOU 2046  NE1 TRP A 365    13160  16383  22632    459   1610   1225       N  
ATOM   2047  CE2 TRP A 365     -41.953-112.618 246.000  1.00137.66           C  
ANISOU 2047  CE2 TRP A 365    12919  16852  22533    756   1796   1638       C  
ATOM   2048  CE3 TRP A 365     -42.305-111.299 244.006  1.00136.63           C  
ANISOU 2048  CE3 TRP A 365    12367  17450  22096   1137   2023   2264       C  
ATOM   2049  CZ2 TRP A 365     -40.673-112.980 245.591  1.00139.31           C  
ANISOU 2049  CZ2 TRP A 365    12932  17300  22700   1023   1977   1955       C  
ATOM   2050  CZ3 TRP A 365     -41.034-111.663 243.602  1.00140.89           C  
ANISOU 2050  CZ3 TRP A 365    12707  18261  22563   1428   2235   2604       C  
ATOM   2051  CH2 TRP A 365     -40.233-112.495 244.391  1.00141.72           C  
ANISOU 2051  CH2 TRP A 365    12919  18114  22814   1369   2211   2443       C  
ATOM   2052  N   GLY A 366     -46.191-107.216 245.681  1.00148.61           N  
ANISOU 2052  N   GLY A 366    13940  17861  24666    283   1459   2307       N  
ATOM   2053  CA  GLY A 366     -47.189-106.297 245.177  1.00158.38           C  
ANISOU 2053  CA  GLY A 366    15055  19189  25931    345   1461   2482       C  
ATOM   2054  C   GLY A 366     -46.769-105.538 243.936  1.00169.96           C  
ANISOU 2054  C   GLY A 366    16145  21030  27402    529   1573   3097       C  
ATOM   2055  O   GLY A 366     -46.153-104.472 244.031  1.00172.86           O  
ANISOU 2055  O   GLY A 366    16298  21142  28238    452   1509   3579       O  
ATOM   2056  N   ASP A 367     -47.097-106.079 242.761  1.00177.52           N  
ANISOU 2056  N   ASP A 367    17020  22585  27844    787   1708   3106       N  
ATOM   2057  CA  ASP A 367     -46.805-105.384 241.511  1.00184.85           C  
ANISOU 2057  CA  ASP A 367    17589  23985  28662   1045   1859   3733       C  
ATOM   2058  C   ASP A 367     -47.674-104.140 241.368  1.00186.58           C  
ANISOU 2058  C   ASP A 367    17649  24079  29165    999   1791   4035       C  
ATOM   2059  O   ASP A 367     -47.166-103.016 241.274  1.00190.10           O  
ANISOU 2059  O   ASP A 367    17808  24347  30074    960   1792   4638       O  
ATOM   2060  CB  ASP A 367     -47.010-106.330 240.326  1.00187.39           C  
ANISOU 2060  CB  ASP A 367    17961  24993  28244   1410   1972   3567       C  
ATOM   2061  CG  ASP A 367     -46.815-105.642 238.989  1.00192.84           C  
ANISOU 2061  CG  ASP A 367    18301  26284  28685   1767   2159   4229       C  
ATOM   2062  OD1 ASP A 367     -45.948-104.748 238.898  1.00194.53           O  
ANISOU 2062  OD1 ASP A 367    18155  26455  29303   1765   2291   4934       O  
ATOM   2063  OD2 ASP A 367     -47.531-105.997 238.029  1.00196.56           O  
ANISOU 2063  OD2 ASP A 367    18842  27269  28571   2050   2143   4078       O  
ATOM   2064  N   ASP A 368     -48.994-104.325 241.347  1.00178.84           N  
ANISOU 2064  N   ASP A 368    16820  23165  27967   1002   1710   3664       N  
ATOM   2065  CA  ASP A 368     -49.944-103.218 241.310  1.00174.56           C  
ANISOU 2065  CA  ASP A 368    16150  22483  27692    990   1653   3898       C  
ATOM   2066  C   ASP A 368     -50.460-102.890 242.708  1.00169.65           C  
ANISOU 2066  C   ASP A 368    15773  21198  27487    768   1525   3556       C  
ATOM   2067  O   ASP A 368     -50.314-101.760 243.180  1.00169.98           O  
ANISOU 2067  O   ASP A 368    15771  20779  28032    710   1448   3821       O  
ATOM   2068  CB  ASP A 368     -51.104-103.558 240.363  1.00176.73           C  
ANISOU 2068  CB  ASP A 368    16376  23298  27477   1175   1636   3791       C  
ATOM   2069  CG  ASP A 368     -51.932-102.341 239.980  1.00178.61           C  
ANISOU 2069  CG  ASP A 368    16371  23551  27942   1256   1626   4221       C  
ATOM   2070  OD1 ASP A 368     -52.238-101.511 240.861  1.00178.11           O  
ANISOU 2070  OD1 ASP A 368    16347  22935  28392   1126   1578   4253       O  
ATOM   2071  OD2 ASP A 368     -52.279-102.217 238.787  1.00181.72           O  
ANISOU 2071  OD2 ASP A 368    16557  24517  27970   1495   1654   4519       O  
ATOM   2072  N   SER A 369     -51.064-103.866 243.377  1.00166.33           N  
ANISOU 2072  N   SER A 369    15618  20715  26864    679   1489   2987       N  
ATOM   2073  CA  SER A 369     -51.536-103.727 244.746  1.00161.49           C  
ANISOU 2073  CA  SER A 369    15263  19579  26518    558   1429   2660       C  
ATOM   2074  C   SER A 369     -50.835-104.758 245.621  1.00157.24           C  
ANISOU 2074  C   SER A 369    14989  18844  25912    409   1402   2268       C  
ATOM   2075  O   SER A 369     -50.165-105.667 245.129  1.00155.51           O  
ANISOU 2075  O   SER A 369    14753  18897  25435    404   1431   2200       O  
ATOM   2076  CB  SER A 369     -53.059-103.894 244.826  1.00159.07           C  
ANISOU 2076  CB  SER A 369    14947  19411  26083    616   1454   2477       C  
ATOM   2077  OG  SER A 369     -53.463-105.141 244.290  1.00155.57           O  
ANISOU 2077  OG  SER A 369    14484  19373  25251    578   1423   2227       O  
ATOM   2078  N   ILE A 370     -50.999-104.606 246.937  1.00155.91           N  
ANISOU 2078  N   ILE A 370    15085  18210  25944    343   1352   2012       N  
ATOM   2079  CA  ILE A 370     -50.316-105.478 247.889  1.00150.12           C  
ANISOU 2079  CA  ILE A 370    14608  17261  25170    215   1311   1687       C  
ATOM   2080  C   ILE A 370     -50.724-106.922 247.640  1.00147.17           C  
ANISOU 2080  C   ILE A 370    14251  17219  24447    170   1380   1405       C  
ATOM   2081  O   ILE A 370     -51.914-107.261 247.659  1.00147.22           O  
ANISOU 2081  O   ILE A 370    14227  17364  24346    187   1421   1282       O  
ATOM   2082  CB  ILE A 370     -50.626-105.055 249.328  1.00147.29           C  
ANISOU 2082  CB  ILE A 370    14564  16425  24973    244   1251   1453       C  
ATOM   2083  CG1 ILE A 370     -50.136-103.629 249.588  1.00150.20           C  
ANISOU 2083  CG1 ILE A 370    14988  16343  25739    288   1062   1662       C  
ATOM   2084  CG2 ILE A 370     -49.998-106.025 250.315  1.00143.51           C  
ANISOU 2084  CG2 ILE A 370    14343  15787  24396    134   1212   1145       C  
ATOM   2085  CD1 ILE A 370     -50.362-103.161 251.010  1.00151.02           C  
ANISOU 2085  CD1 ILE A 370    15504  15950  25926    409    942   1355       C  
ATOM   2086  N   GLU A 371     -49.737-107.782 247.401  1.00145.14           N  
ANISOU 2086  N   GLU A 371    14023  17062  24060    117   1368   1331       N  
ATOM   2087  CA  GLU A 371     -49.980-109.201 247.191  1.00144.60           C  
ANISOU 2087  CA  GLU A 371    14028  17199  23715     82   1365   1023       C  
ATOM   2088  C   GLU A 371     -48.914-110.004 247.922  1.00142.25           C  
ANISOU 2088  C   GLU A 371    13916  16685  23448     -2   1350    852       C  
ATOM   2089  O   GLU A 371     -47.741-109.618 247.944  1.00139.79           O  
ANISOU 2089  O   GLU A 371    13564  16286  23263     11   1347   1053       O  
ATOM   2090  CB  GLU A 371     -49.984-109.558 245.700  1.00149.12           C  
ANISOU 2090  CB  GLU A 371    14443  18250  23967    234   1355   1090       C  
ATOM   2091  CG  GLU A 371     -51.132-108.945 244.911  1.00154.31           C  
ANISOU 2091  CG  GLU A 371    14909  19179  24544    317   1324   1244       C  
ATOM   2092  CD  GLU A 371     -51.036-109.230 243.423  1.00161.57           C  
ANISOU 2092  CD  GLU A 371    15719  20613  25057    536   1281   1313       C  
ATOM   2093  OE1 GLU A 371     -51.600-108.447 242.629  1.00165.77           O  
ANISOU 2093  OE1 GLU A 371    16047  21423  25513    660   1278   1592       O  
ATOM   2094  OE2 GLU A 371     -50.394-110.232 243.043  1.00162.95           O  
ANISOU 2094  OE2 GLU A 371    16034  20925  24955    633   1248   1087       O  
ATOM   2095  N   LEU A 372     -49.329-111.117 248.522  1.00146.37           N  
ANISOU 2095  N   LEU A 372    14596  17115  23903    -99   1326    544       N  
ATOM   2096  CA  LEU A 372     -48.431-111.955 249.298  1.00148.72           C  
ANISOU 2096  CA  LEU A 372    15073  17199  24236   -171   1311    389       C  
ATOM   2097  C   LEU A 372     -47.884-113.084 248.427  1.00145.52           C  
ANISOU 2097  C   LEU A 372    14675  17002  23616    -88   1288    247       C  
ATOM   2098  O   LEU A 372     -48.109-113.143 247.214  1.00142.80           O  
ANISOU 2098  O   LEU A 372    14229  16984  23045     60   1271    256       O  
ATOM   2099  CB  LEU A 372     -49.146-112.512 250.533  1.00153.68           C  
ANISOU 2099  CB  LEU A 372    15863  17590  24936   -287   1319    209       C  
ATOM   2100  CG  LEU A 372     -49.267-111.612 251.776  1.00159.12           C  
ANISOU 2100  CG  LEU A 372    16696  18010  25752   -264   1350    267       C  
ATOM   2101  CD1 LEU A 372     -50.172-110.415 251.520  1.00164.96           C  
ANISOU 2101  CD1 LEU A 372    17329  18807  26542   -156   1395    415       C  
ATOM   2102  CD2 LEU A 372     -49.746-112.410 252.980  1.00157.87           C  
ANISOU 2102  CD2 LEU A 372    16698  17715  25571   -301   1413    141       C  
ATOM   2103  N   GLN A 373     -47.131-113.983 249.052  1.00145.50           N  
ANISOU 2103  N   GLN A 373    14822  16812  23651   -131   1277    106       N  
ATOM   2104  CA  GLN A 373     -46.592-115.123 248.328  1.00147.40           C  
ANISOU 2104  CA  GLN A 373    15128  17184  23693     11   1253    -76       C  
ATOM   2105  C   GLN A 373     -47.707-116.099 247.980  1.00150.01           C  
ANISOU 2105  C   GLN A 373    15549  17513  23935    -46   1090   -394       C  
ATOM   2106  O   GLN A 373     -48.552-116.418 248.822  1.00149.53           O  
ANISOU 2106  O   GLN A 373    15518  17224  24074   -264   1031   -461       O  
ATOM   2107  CB  GLN A 373     -45.514-115.815 249.155  1.00144.34           C  
ANISOU 2107  CB  GLN A 373    14861  16559  23423    -13   1274   -110       C  
ATOM   2108  CG  GLN A 373     -45.046-117.135 248.569  1.00143.97           C  
ANISOU 2108  CG  GLN A 373    14940  16560  23200    171   1245   -355       C  
ATOM   2109  CD  GLN A 373     -44.554-117.005 247.139  1.00148.38           C  
ANISOU 2109  CD  GLN A 373    15416  17535  23428    531   1329   -290       C  
ATOM   2110  OE1 GLN A 373     -44.079-115.945 246.722  1.00152.58           O  
ANISOU 2110  OE1 GLN A 373    15721  18311  23942    632   1467     84       O  
ATOM   2111  NE2 GLN A 373     -44.659-118.090 246.379  1.00150.12           N  
ANISOU 2111  NE2 GLN A 373    15828  17829  23381    760   1230   -637       N  
ATOM   2112  N   ASP A 374     -47.701-116.571 246.729  1.00155.41           N  
ANISOU 2112  N   ASP A 374    16268  18457  24322    175    995   -561       N  
ATOM   2113  CA  ASP A 374     -48.745-117.476 246.257  1.00159.99           C  
ANISOU 2113  CA  ASP A 374    16946  18995  24850    111    710   -891       C  
ATOM   2114  C   ASP A 374     -48.836-118.733 247.110  1.00155.23           C  
ANISOU 2114  C   ASP A 374    16502  17967  24513    -89    569  -1117       C  
ATOM   2115  O   ASP A 374     -49.907-119.342 247.204  1.00156.53           O  
ANISOU 2115  O   ASP A 374    16650  17952  24872   -307    316  -1251       O  
ATOM   2116  CB  ASP A 374     -48.490-117.848 244.794  1.00170.17           C  
ANISOU 2116  CB  ASP A 374    18355  20615  25688    477    582  -1109       C  
ATOM   2117  CG  ASP A 374     -48.483-116.638 243.877  1.00176.34           C  
ANISOU 2117  CG  ASP A 374    18939  21871  26191    697    728   -805       C  
ATOM   2118  OD1 ASP A 374     -49.245-115.685 244.143  1.00178.54           O  
ANISOU 2118  OD1 ASP A 374    19005  22174  26659    498    765   -554       O  
ATOM   2119  OD2 ASP A 374     -47.718-116.640 242.891  1.00178.80           O  
ANISOU 2119  OD2 ASP A 374    19298  22546  26091   1109    828   -778       O  
ATOM   2120  N   ASP A 375     -47.729-119.138 247.731  1.00146.45           N  
ANISOU 2120  N   ASP A 375    15500  16684  23459    -27    709  -1102       N  
ATOM   2121  CA  ASP A 375     -47.765-120.270 248.646  1.00137.51           C  
ANISOU 2121  CA  ASP A 375    14495  15141  22613   -213    607  -1231       C  
ATOM   2122  C   ASP A 375     -48.381-119.896 249.987  1.00139.84           C  
ANISOU 2122  C   ASP A 375    14665  15261  23208   -507    717   -973       C  
ATOM   2123  O   ASP A 375     -49.005-120.742 250.637  1.00144.43           O  
ANISOU 2123  O   ASP A 375    15247  15566  24063   -716    604   -986       O  
ATOM   2124  CB  ASP A 375     -46.354-120.818 248.854  1.00126.79           C  
ANISOU 2124  CB  ASP A 375    13280  13691  21203     -8    726  -1263       C  
ATOM   2125  CG  ASP A 375     -45.638-121.081 247.544  1.00121.79           C  
ANISOU 2125  CG  ASP A 375    12764  13321  20189    417    719  -1455       C  
ATOM   2126  OD1 ASP A 375     -46.314-121.447 246.560  1.00120.07           O  
ANISOU 2126  OD1 ASP A 375    12662  13189  19771    532    477  -1752       O  
ATOM   2127  OD2 ASP A 375     -44.400-120.915 247.498  1.00120.84           O  
ANISOU 2127  OD2 ASP A 375    12613  13345  19956    668    944  -1287       O  
ATOM   2128  N   PHE A 376     -48.219-118.641 250.413  1.00139.12           N  
ANISOU 2128  N   PHE A 376    14469  15317  23072   -492    926   -717       N  
ATOM   2129  CA  PHE A 376     -48.740-118.196 251.701  1.00135.40           C  
ANISOU 2129  CA  PHE A 376    13955  14719  22771   -642   1049   -511       C  
ATOM   2130  C   PHE A 376     -50.224-117.874 251.657  1.00136.50           C  
ANISOU 2130  C   PHE A 376    13913  14947  23005   -753   1032   -410       C  
ATOM   2131  O   PHE A 376     -50.858-117.787 252.716  1.00138.78           O  
ANISOU 2131  O   PHE A 376    14153  15154  23424   -826   1155   -226       O  
ATOM   2132  CB  PHE A 376     -47.958-116.970 252.182  1.00129.62           C  
ANISOU 2132  CB  PHE A 376    13248  14032  21970   -546   1191   -338       C  
ATOM   2133  CG  PHE A 376     -47.879-116.848 253.675  1.00126.66           C  
ANISOU 2133  CG  PHE A 376    12994  13460  21671   -592   1268   -236       C  
ATOM   2134  CD1 PHE A 376     -48.887-116.223 254.391  1.00123.25           C  
ANISOU 2134  CD1 PHE A 376    12544  13042  21242   -583   1370   -121       C  
ATOM   2135  CD2 PHE A 376     -46.790-117.354 254.360  1.00126.77           C  
ANISOU 2135  CD2 PHE A 376    13146  13309  21710   -586   1244   -242       C  
ATOM   2136  CE1 PHE A 376     -48.811-116.115 255.766  1.00121.50           C  
ANISOU 2136  CE1 PHE A 376    12492  12694  20980   -523   1450    -48       C  
ATOM   2137  CE2 PHE A 376     -46.709-117.247 255.734  1.00124.45           C  
ANISOU 2137  CE2 PHE A 376    13002  12874  21410   -583   1280   -160       C  
ATOM   2138  CZ  PHE A 376     -47.720-116.625 256.438  1.00122.66           C  
ANISOU 2138  CZ  PHE A 376    12806  12683  21117   -530   1384    -79       C  
ATOM   2139  N   ILE A 377     -50.783-117.699 250.465  1.00136.65           N  
ANISOU 2139  N   ILE A 377    13819  15167  22935   -726    891   -490       N  
ATOM   2140  CA  ILE A 377     -52.182-117.303 250.312  1.00139.14           C  
ANISOU 2140  CA  ILE A 377    13899  15606  23361   -822    852   -342       C  
ATOM   2141  C   ILE A 377     -53.153-118.377 250.808  1.00140.87           C  
ANISOU 2141  C   ILE A 377    13987  15626  23910  -1062    711   -279       C  
ATOM   2142  O   ILE A 377     -54.101-118.041 251.536  1.00143.72           O  
ANISOU 2142  O   ILE A 377    14137  16027  24444  -1123    865     23       O  
ATOM   2143  CB  ILE A 377     -52.494-116.924 248.852  1.00143.45           C  
ANISOU 2143  CB  ILE A 377    14357  16437  23710   -726    673   -436       C  
ATOM   2144  CG1 ILE A 377     -51.627-115.751 248.385  1.00143.30           C  
ANISOU 2144  CG1 ILE A 377    14369  16640  23440   -494    853   -339       C  
ATOM   2145  CG2 ILE A 377     -53.964-116.590 248.678  1.00145.85           C  
ANISOU 2145  CG2 ILE A 377    14374  16869  24173   -842    588   -252       C  
ATOM   2146  CD1 ILE A 377     -51.847-114.497 249.169  1.00145.12           C  
ANISOU 2146  CD1 ILE A 377    14516  16852  23770   -469   1082    -66       C  
ATOM   2147  N   PRO A 378     -52.998-119.661 250.436  1.00139.81           N  
ANISOU 2147  N   PRO A 378    13948  15268  23907  -1181    416   -511       N  
ATOM   2148  CA  PRO A 378     -53.945-120.670 250.948  1.00139.99           C  
ANISOU 2148  CA  PRO A 378    13782  15033  24375  -1465    236   -354       C  
ATOM   2149  C   PRO A 378     -53.998-120.725 252.464  1.00139.56           C  
ANISOU 2149  C   PRO A 378    13656  14881  24491  -1503    570      6       C  
ATOM   2150  O   PRO A 378     -55.091-120.823 253.036  1.00144.41           O  
ANISOU 2150  O   PRO A 378    13957  15512  25400  -1642    638    386       O  
ATOM   2151  CB  PRO A 378     -53.417-121.976 250.341  1.00141.89           C  
ANISOU 2151  CB  PRO A 378    14253  14955  24702  -1518   -152   -735       C  
ATOM   2152  CG  PRO A 378     -52.721-121.543 249.109  1.00141.98           C  
ANISOU 2152  CG  PRO A 378    14485  15207  24252  -1236   -235  -1091       C  
ATOM   2153  CD  PRO A 378     -52.060-120.253 249.460  1.00140.05           C  
ANISOU 2153  CD  PRO A 378    14239  15259  23714  -1033    203   -900       C  
ATOM   2154  N   LEU A 379     -52.848-120.637 253.138  1.00136.06           N  
ANISOU 2154  N   LEU A 379    13473  14376  23847  -1350    783    -60       N  
ATOM   2155  CA  LEU A 379     -52.856-120.612 254.596  1.00136.36           C  
ANISOU 2155  CA  LEU A 379    13502  14378  23931  -1312   1085    259       C  
ATOM   2156  C   LEU A 379     -53.462-119.321 255.125  1.00141.43           C  
ANISOU 2156  C   LEU A 379    14049  15302  24387  -1127   1390    497       C  
ATOM   2157  O   LEU A 379     -54.095-119.322 256.187  1.00147.00           O  
ANISOU 2157  O   LEU A 379    14632  16068  25153  -1065   1635    850       O  
ATOM   2158  CB  LEU A 379     -51.438-120.790 255.136  1.00131.47           C  
ANISOU 2158  CB  LEU A 379    13195  13629  23127  -1187   1160    110       C  
ATOM   2159  N   PHE A 380     -53.287-118.217 254.395  1.00141.73           N  
ANISOU 2159  N   PHE A 380    14142  15516  24193   -992   1390    338       N  
ATOM   2160  CA  PHE A 380     -53.858-116.941 254.810  1.00145.23           C  
ANISOU 2160  CA  PHE A 380    14533  16162  24486   -779   1636    520       C  
ATOM   2161  C   PHE A 380     -55.381-116.990 254.800  1.00147.66           C  
ANISOU 2161  C   PHE A 380    14454  16629  25020   -834   1709    856       C  
ATOM   2162  O   PHE A 380     -56.034-116.519 255.738  1.00148.68           O  
ANISOU 2162  O   PHE A 380    14501  16887  25102   -628   2015   1156       O  
ATOM   2163  CB  PHE A 380     -53.339-115.830 253.895  1.00148.42           C  
ANISOU 2163  CB  PHE A 380    15030  16668  24696   -663   1568    330       C  
ATOM   2164  CG  PHE A 380     -54.130-114.554 253.965  1.00151.72           C  
ANISOU 2164  CG  PHE A 380    15345  17254  25048   -466   1737    500       C  
ATOM   2165  CD1 PHE A 380     -53.884-113.623 254.962  1.00150.59           C  
ANISOU 2165  CD1 PHE A 380    15428  17047  24741   -204   1924    530       C  
ATOM   2166  CD2 PHE A 380     -55.099-114.271 253.018  1.00155.87           C  
ANISOU 2166  CD2 PHE A 380    15576  17978  25668   -510   1665    607       C  
ATOM   2167  CE1 PHE A 380     -54.603-112.439 255.020  1.00153.14           C  
ANISOU 2167  CE1 PHE A 380    15704  17472  25012     39   2066    652       C  
ATOM   2168  CE2 PHE A 380     -55.824-113.092 253.072  1.00158.05           C  
ANISOU 2168  CE2 PHE A 380    15746  18398  25908   -293   1833    789       C  
ATOM   2169  CZ  PHE A 380     -55.574-112.174 254.075  1.00156.50           C  
ANISOU 2169  CZ  PHE A 380    15796  18104  25562     -3   2048    804       C  
ATOM   2170  N   ASP A 381     -55.937-117.523 253.731  1.00151.50           N  
ANISOU 2170  N   ASP A 381    14696  17123  25746  -1075   1411    824       N  
ATOM   2171  CA  ASP A 381     -57.375-117.600 253.593  1.00157.49           C  
ANISOU 2171  CA  ASP A 381    15008  18035  26795  -1169   1412   1200       C  
ATOM   2172  C   ASP A 381     -58.060-118.477 254.621  1.00164.45           C  
ANISOU 2172  C   ASP A 381    15642  18834  28008  -1279   1553   1634       C  
ATOM   2173  O   ASP A 381     -59.155-118.179 255.075  1.00167.12           O  
ANISOU 2173  O   ASP A 381    15626  19386  28484  -1173   1816   2115       O  
ATOM   2174  CB  ASP A 381     -57.740-118.037 252.184  1.00156.81           C  
ANISOU 2174  CB  ASP A 381    14748  17937  26896  -1425    939   1031       C  
ATOM   2175  CG  ASP A 381     -57.535-116.942 251.174  1.00152.32           C  
ANISOU 2175  CG  ASP A 381    14298  17581  25994  -1258    869    781       C  
ATOM   2176  OD1 ASP A 381     -57.138-115.830 251.570  1.00148.89           O  
ANISOU 2176  OD1 ASP A 381    13990  17276  25305   -988   1184    825       O  
ATOM   2177  OD2 ASP A 381     -57.776-117.188 249.980  1.00153.47           O  
ANISOU 2177  OD2 ASP A 381    14427  17754  26132  -1377    474    550       O  
ATOM   2178  N   SER A 382     -57.409-119.567 254.978  1.00170.53           N  
ANISOU 2178  N   SER A 382    16559  19312  28922  -1456   1409   1534       N  
ATOM   2179  CA  SER A 382     -57.972-120.532 255.901  1.00176.05           C  
ANISOU 2179  CA  SER A 382    16994  19899  29997  -1592   1514   2012       C  
ATOM   2180  C   SER A 382     -57.492-120.370 257.326  1.00174.02           C  
ANISOU 2180  C   SER A 382    16958  19746  29416  -1266   1976   2197       C  
ATOM   2181  O   SER A 382     -57.427-121.330 258.080  1.00179.25           O  
ANISOU 2181  O   SER A 382    17619  20238  30251  -1352   2013   2407       O  
ATOM   2182  CB  SER A 382     -57.693-121.943 255.397  1.00179.83           C  
ANISOU 2182  CB  SER A 382    17510  19948  30870  -1956   1054   1826       C  
ATOM   2183  OG  SER A 382     -56.302-122.190 255.382  1.00178.06           O  
ANISOU 2183  OG  SER A 382    17783  19561  30312  -1854    972   1299       O  
ATOM   2184  N   LEU A 383     -57.142-119.154 257.698  1.00164.72           N  
ANISOU 2184  N   LEU A 383    15993  18823  27768   -872   2290   2118       N  
ATOM   2185  CA  LEU A 383     -56.625-118.929 259.032  1.00157.69           C  
ANISOU 2185  CA  LEU A 383    15426  18012  26478   -511   2630   2174       C  
ATOM   2186  C   LEU A 383     -57.544-119.288 260.198  1.00157.06           C  
ANISOU 2186  C   LEU A 383    15032  18177  26466   -306   3036   2839       C  
ATOM   2187  O   LEU A 383     -57.092-119.863 261.180  1.00153.58           O  
ANISOU 2187  O   LEU A 383    14798  17782  25774    -73   3265   2988       O  
ATOM   2188  CB  LEU A 383     -56.174-117.480 259.154  1.00154.91           C  
ANISOU 2188  CB  LEU A 383    15439  17771  25649   -149   2737   1842       C  
ATOM   2189  CG  LEU A 383     -55.002-117.023 258.291  1.00151.47           C  
ANISOU 2189  CG  LEU A 383    15520  17239  24793    107   2786   1585       C  
ATOM   2190  CD1 LEU A 383     -54.728-115.528 258.383  1.00149.27           C  
ANISOU 2190  CD1 LEU A 383    15386  16681  24651   -200   2503   1359       C  
ATOM   2191  CD2 LEU A 383     -53.763-117.838 258.623  1.00146.52           C  
ANISOU 2191  CD2 LEU A 383    15227  16585  23858    351   2722   1219       C  
ATOM   2192  N   GLU A 384     -58.823-118.966 260.103  1.00161.40           N  
ANISOU 2192  N   GLU A 384    15052  18924  27348   -362   3136   3299       N  
ATOM   2193  CA  GLU A 384     -59.733-119.284 261.178  1.00170.02           C  
ANISOU 2193  CA  GLU A 384    15722  20294  28585   -170   3555   4077       C  
ATOM   2194  C   GLU A 384     -59.497-120.726 261.529  1.00175.83           C  
ANISOU 2194  C   GLU A 384    16231  20787  29790   -535   3415   4431       C  
ATOM   2195  O   GLU A 384     -59.532-121.113 262.691  1.00177.94           O  
ANISOU 2195  O   GLU A 384    16344  21258  30007   -296   3805   5017       O  
ATOM   2196  CB  GLU A 384     -61.172-119.095 260.721  1.00175.43           C  
ANISOU 2196  CB  GLU A 384    15792  21237  29624   -191   3654   4566       C  
ATOM   2197  CG  GLU A 384     -61.559-117.655 260.432  1.00174.35           C  
ANISOU 2197  CG  GLU A 384    15830  21367  29050    258   3874   4345       C  
ATOM   2198  CD  GLU A 384     -62.972-117.538 259.914  1.00170.28           C  
ANISOU 2198  CD  GLU A 384    15597  20613  28487     14   3419   3648       C  
ATOM   2199  OE1 GLU A 384     -63.560-118.598 259.609  1.00167.95           O  
ANISOU 2199  OE1 GLU A 384    15316  20005  28490   -477   2945   3358       O  
ATOM   2200  OE2 GLU A 384     -63.482-116.410 259.806  1.00170.24           O  
ANISOU 2200  OE2 GLU A 384    15807  20734  28142    354   3540   3410       O  
ATOM   2201  N   GLU A 385     -59.243-121.521 260.506  1.00179.63           N  
ANISOU 2201  N   GLU A 385    16708  20831  30712  -1067   2862   4096       N  
ATOM   2202  CA  GLU A 385     -58.974-122.932 260.686  1.00187.37           C  
ANISOU 2202  CA  GLU A 385    17583  21461  32149  -1401   2657   4319       C  
ATOM   2203  C   GLU A 385     -57.735-123.037 261.558  1.00188.32           C  
ANISOU 2203  C   GLU A 385    18231  21527  31796  -1151   2821   4079       C  
ATOM   2204  O   GLU A 385     -57.615-123.923 262.390  1.00192.81           O  
ANISOU 2204  O   GLU A 385    18679  22022  32559  -1179   2944   4537       O  
ATOM   2205  CB  GLU A 385     -58.739-123.605 259.341  1.00187.88           C  
ANISOU 2205  CB  GLU A 385    17626  21036  32723  -1934   1981   3894       C  
ATOM   2206  N   THR A 386     -56.810-122.112 261.366  1.00184.85           N  
ANISOU 2206  N   THR A 386    18338  21121  30776   -915   2799   3425       N  
ATOM   2207  CA  THR A 386     -55.588-122.084 262.141  1.00182.02           C  
ANISOU 2207  CA  THR A 386    18463  20759  29938   -642   2931   3226       C  
ATOM   2208  C   THR A 386     -56.082-121.811 263.530  1.00189.26           C  
ANISOU 2208  C   THR A 386    19366  22098  30448   -141   3460   3742       C  
ATOM   2209  O   THR A 386     -57.183-121.289 263.671  1.00194.22           O  
ANISOU 2209  O   THR A 386    19737  23069  30988    120   3775   4081       O  
ATOM   2210  CB  THR A 386     -54.736-120.900 261.719  1.00172.40           C  
ANISOU 2210  CB  THR A 386    17746  19494  28266   -508   2763   2508       C  
ATOM   2211  OG1 THR A 386     -54.403-121.044 260.337  1.00167.68           O  
ANISOU 2211  OG1 THR A 386    17090  18657  27963   -857   2368   2114       O  
ATOM   2212  CG2 THR A 386     -53.477-120.832 262.550  1.00169.81           C  
ANISOU 2212  CG2 THR A 386    17856  19030  27632   -393   2702   2265       C  
ATOM   2213  N   GLY A 387     -55.316-122.159 264.560  1.00190.34           N  
ANISOU 2213  N   GLY A 387    19781  22235  30304     46   3565   3823       N  
ATOM   2214  CA  GLY A 387     -55.821-121.946 265.903  1.00200.05           C  
ANISOU 2214  CA  GLY A 387    21095  23902  31011    615   4052   4270       C  
ATOM   2215  C   GLY A 387     -56.145-120.478 266.047  1.00205.64           C  
ANISOU 2215  C   GLY A 387    22102  24933  31099   1148   4277   4005       C  
ATOM   2216  O   GLY A 387     -57.235-120.120 266.481  1.00213.16           O  
ANISOU 2216  O   GLY A 387    22720  26224  32046   1410   4636   4436       O  
ATOM   2217  N   ALA A 388     -55.231-119.614 265.646  1.00203.99           N  
ANISOU 2217  N   ALA A 388    22499  24593  30416   1318   4046   3329       N  
ATOM   2218  CA  ALA A 388     -55.526-118.193 265.658  1.00203.77           C  
ANISOU 2218  CA  ALA A 388    22818  24679  29924   1724   4082   2921       C  
ATOM   2219  C   ALA A 388     -56.118-117.642 266.962  1.00209.61           C  
ANISOU 2219  C   ALA A 388    23572  25910  30161   2433   4617   3341       C  
ATOM   2220  O   ALA A 388     -57.096-116.884 266.909  1.00211.25           O  
ANISOU 2220  O   ALA A 388    23583  26315  30368   2662   4847   3462       O  
ATOM   2221  CB  ALA A 388     -56.435-117.859 264.480  1.00200.78           C  
ANISOU 2221  CB  ALA A 388    22182  24140  29966   1372   3881   2686       C  
ATOM   2222  N   GLN A 389     -55.663-118.101 268.119  1.00206.35           N  
ANISOU 2222  N   GLN A 389    23398  25726  29278   2839   4833   3588       N  
ATOM   2223  CA  GLN A 389     -56.285-117.585 269.331  1.00206.06           C  
ANISOU 2223  CA  GLN A 389    23457  26226  28610   3657   5380   3986       C  
ATOM   2224  C   GLN A 389     -55.437-117.553 270.576  1.00202.71           C  
ANISOU 2224  C   GLN A 389    23727  25895  27397   4170   5313   3716       C  
ATOM   2225  O   GLN A 389     -55.015-118.587 271.080  1.00204.17           O  
ANISOU 2225  O   GLN A 389    23862  26115  27599   4044   5311   4025       O  
ATOM   2226  CB  GLN A 389     -57.593-118.319 269.599  1.00209.75           C  
ANISOU 2226  CB  GLN A 389    23179  27082  29433   3664   5899   5007       C  
ATOM   2227  CG  GLN A 389     -58.644-118.020 268.550  1.00208.60           C  
ANISOU 2227  CG  GLN A 389    22382  27018  29859   3454   6065   5362       C  
ATOM   2228  CD  GLN A 389     -59.909-118.808 268.785  1.00209.01           C  
ANISOU 2228  CD  GLN A 389    22699  27314  29400   4105   6305   5105       C  
ATOM   2229  OE1 GLN A 389     -59.877-119.867 269.402  1.00212.64           O  
ANISOU 2229  OE1 GLN A 389    23627  28119  29049   4935   6632   5068       O  
ATOM   2230  NE2 GLN A 389     -61.033-118.295 268.301  1.00206.21           N  
ANISOU 2230  NE2 GLN A 389    22082  26775  29494   3774   6120   4905       N  
ATOM   2231  N   GLY A 390     -55.197-116.354 271.079  1.00198.48           N  
ANISOU 2231  N   GLY A 390    23846  25373  26196   4751   5212   3144       N  
ATOM   2232  CA  GLY A 390     -54.426-116.200 272.291  1.00196.46           C  
ANISOU 2232  CA  GLY A 390    24323  25201  25122   5308   5059   2822       C  
ATOM   2233  C   GLY A 390     -53.120-116.925 272.116  1.00186.90           C  
ANISOU 2233  C   GLY A 390    23299  23604  24112   4765   4513   2525       C  
ATOM   2234  O   GLY A 390     -52.599-117.515 273.052  1.00190.49           O  
ANISOU 2234  O   GLY A 390    24014  24252  24110   5045   4524   2684       O  
ATOM   2235  N   ARG A 391     -52.587-116.875 270.908  1.00173.96           N  
ANISOU 2235  N   ARG A 391    21513  21457  23126   4034   4054   2137       N  
ATOM   2236  CA  ARG A 391     -51.344-117.550 270.623  1.00167.08           C  
ANISOU 2236  CA  ARG A 391    20677  20228  22576   3479   3595   1949       C  
ATOM   2237  C   ARG A 391     -50.306-116.483 270.501  1.00158.91           C  
ANISOU 2237  C   ARG A 391    20164  18769  21445   3385   2967   1188       C  
ATOM   2238  O   ARG A 391     -50.496-115.531 269.757  1.00157.52           O  
ANISOU 2238  O   ARG A 391    20015  18382  21453   3300   2821    844       O  
ATOM   2239  CB  ARG A 391     -51.433-118.304 269.293  1.00165.58           C  
ANISOU 2239  CB  ARG A 391    19831  19818  23262   2728   3592   2209       C  
ATOM   2240  CG  ARG A 391     -52.410-119.478 269.240  1.00166.08           C  
ANISOU 2240  CG  ARG A 391    19891  19547  23666   2233   3204   2088       C  
ATOM   2241  CD  ARG A 391     -52.374-120.209 267.901  1.00165.12           C  
ANISOU 2241  CD  ARG A 391    19182  19224  24334   1623   3229   2347       C  
ATOM   2242  NE  ARG A 391     -53.307-121.338 267.771  1.00170.60           N  
ANISOU 2242  NE  ARG A 391    19406  20187  25227   1676   3678   3068       N  
ATOM   2243  CZ  ARG A 391     -53.106-122.583 268.202  1.00175.41           C  
ANISOU 2243  CZ  ARG A 391    19850  20865  25930   1658   3817   3585       C  
ATOM   2244  NH1 ARG A 391     -51.975-122.923 268.800  1.00181.25           N  
ANISOU 2244  NH1 ARG A 391    20084  21834  26948   1678   4216   4334       N  
ATOM   2245  NH2 ARG A 391     -54.047-123.505 268.021  1.00174.67           N  
ANISOU 2245  NH2 ARG A 391    20054  20607  25706   1612   3548   3417       N  
ATOM   2246  N   LYS A 392     -49.200-116.625 271.220  1.00155.06           N  
ANISOU 2246  N   LYS A 392    20046  18152  20718   3386   2575    989       N  
ATOM   2247  CA  LYS A 392     -48.161-115.627 271.115  1.00149.46           C  
ANISOU 2247  CA  LYS A 392    19743  17002  20041   3214   1903    371       C  
ATOM   2248  C   LYS A 392     -47.659-115.800 269.709  1.00140.50           C  
ANISOU 2248  C   LYS A 392    18173  15504  19704   2493   1692    276       C  
ATOM   2249  O   LYS A 392     -47.293-116.891 269.308  1.00133.15           O  
ANISOU 2249  O   LYS A 392    16896  14504  19190   2057   1686    504       O  
ATOM   2250  CB  LYS A 392     -47.043-115.905 272.109  1.00152.36           C  
ANISOU 2250  CB  LYS A 392    20487  17336  20066   3310   1513    286       C  
ATOM   2251  N   VAL A 393     -47.645-114.717 268.958  1.00139.37           N  
ANISOU 2251  N   VAL A 393    18060  15139  19755   2418   1529    -43       N  
ATOM   2252  CA  VAL A 393     -47.220-114.783 267.584  1.00130.79           C  
ANISOU 2252  CA  VAL A 393    16557  13802  19334   1840   1401    -89       C  
ATOM   2253  C   VAL A 393     -46.465-113.534 267.206  1.00129.81           C  
ANISOU 2253  C   VAL A 393    16705  13286  19333   1749    853   -517       C  
ATOM   2254  O   VAL A 393     -46.618-112.491 267.815  1.00133.28           O  
ANISOU 2254  O   VAL A 393    17615  13614  19413   2148    639   -816       O  
ATOM   2255  CB  VAL A 393     -48.422-114.968 266.653  1.00123.37           C  
ANISOU 2255  CB  VAL A 393    15187  13046  18642   1777   1846    138       C  
ATOM   2256  CG1 VAL A 393     -49.494-113.961 266.987  1.00130.13           C  
ANISOU 2256  CG1 VAL A 393    16293  13930  19223   2207   1916    -57       C  
ATOM   2257  CG2 VAL A 393     -48.012-114.840 265.200  1.00115.74           C  
ANISOU 2257  CG2 VAL A 393    13789  11902  18286   1213   1737    135       C  
ATOM   2258  N   ALA A 394     -45.645-113.670 266.184  1.00128.26           N  
ANISOU 2258  N   ALA A 394    16207  12864  19662   1248    608   -521       N  
ATOM   2259  CA  ALA A 394     -44.830-112.583 265.664  1.00126.92           C  
ANISOU 2259  CA  ALA A 394    16124  12324  19774   1072    115   -768       C  
ATOM   2260  C   ALA A 394     -44.676-112.767 264.163  1.00122.59           C  
ANISOU 2260  C   ALA A 394    15055  11755  19770    642    215   -611       C  
ATOM   2261  O   ALA A 394     -44.810-113.875 263.636  1.00122.83           O  
ANISOU 2261  O   ALA A 394    14741  11974  19955    444    508   -398       O  
ATOM   2262  CB  ALA A 394     -43.456-112.521 266.344  1.00129.43           C  
ANISOU 2262  CB  ALA A 394    16699  12387  20091    990   -456   -890       C  
ATOM   2263  N   CYS A 395     -44.394-111.668 263.474  1.00117.38           N  
ANISOU 2263  N   CYS A 395    14357  10851  19392    531    -53   -711       N  
ATOM   2264  CA  CYS A 395     -44.315-111.674 262.024  1.00114.22           C  
ANISOU 2264  CA  CYS A 395    13490  10493  19415    222     63   -540       C  
ATOM   2265  C   CYS A 395     -42.943-111.214 261.553  1.00123.46           C  
ANISOU 2265  C   CYS A 395    14515  11399  20996    -53   -371   -459       C  
ATOM   2266  O   CYS A 395     -42.202-110.543 262.274  1.00129.62           O  
ANISOU 2266  O   CYS A 395    15566  11863  21821    -36   -856   -575       O  
ATOM   2267  CB  CYS A 395     -45.397-110.781 261.405  1.00110.00           C  
ANISOU 2267  CB  CYS A 395    12895   9998  18904    348    248   -569       C  
ATOM   2268  SG  CYS A 395     -47.066-111.442 261.557  1.00111.88           S  
ANISOU 2268  SG  CYS A 395    13045  10629  18835    585    828   -479       S  
ATOM   2269  N   PHE A 396     -42.614-111.601 260.324  1.00125.92           N  
ANISOU 2269  N   PHE A 396    14381  11854  21607   -285   -210   -232       N  
ATOM   2270  CA  PHE A 396     -41.431-111.103 259.640  1.00127.62           C  
ANISOU 2270  CA  PHE A 396    14320  11915  22256   -511   -505     -9       C  
ATOM   2271  C   PHE A 396     -41.689-111.181 258.141  1.00120.22           C  
ANISOU 2271  C   PHE A 396    12960  11240  21477   -585   -185    202       C  
ATOM   2272  O   PHE A 396     -42.748-111.633 257.697  1.00116.12           O  
ANISOU 2272  O   PHE A 396    12402  10969  20747   -496    176    120       O  
ATOM   2273  CB  PHE A 396     -40.167-111.869 260.060  1.00132.40           C  
ANISOU 2273  CB  PHE A 396    14849  12480  22977   -637   -706    124       C  
ATOM   2274  CG  PHE A 396     -40.244-113.358 259.854  1.00135.25           C  
ANISOU 2274  CG  PHE A 396    15075  13133  23180   -617   -323    168       C  
ATOM   2275  CD1 PHE A 396     -40.898-114.167 260.770  1.00136.96           C  
ANISOU 2275  CD1 PHE A 396    15563  13427  23050   -479   -157      4       C  
ATOM   2276  CD2 PHE A 396     -39.628-113.952 258.763  1.00135.02           C  
ANISOU 2276  CD2 PHE A 396    14657  13287  23360   -698   -143    400       C  
ATOM   2277  CE1 PHE A 396     -40.959-115.537 260.589  1.00134.90           C  
ANISOU 2277  CE1 PHE A 396    15173  13340  22744   -490    131     69       C  
ATOM   2278  CE2 PHE A 396     -39.682-115.321 258.577  1.00132.46           C  
ANISOU 2278  CE2 PHE A 396    14271  13142  22917   -646    141    382       C  
ATOM   2279  CZ  PHE A 396     -40.349-116.115 259.492  1.00133.43           C  
ANISOU 2279  CZ  PHE A 396    14655  13257  22786   -576    249    216       C  
ATOM   2280  N   GLY A 397     -40.724-110.712 257.358  1.00118.58           N  
ANISOU 2280  N   GLY A 397    12417  10991  21646   -732   -340    516       N  
ATOM   2281  CA  GLY A 397     -40.883-110.728 255.918  1.00117.61           C  
ANISOU 2281  CA  GLY A 397    11913  11176  21599   -727    -41    751       C  
ATOM   2282  C   GLY A 397     -39.883-109.863 255.183  1.00122.00           C  
ANISOU 2282  C   GLY A 397    12085  11666  22602   -845   -231   1203       C  
ATOM   2283  O   GLY A 397     -39.267-108.969 255.772  1.00128.02           O  
ANISOU 2283  O   GLY A 397    12889  12038  23715   -985   -675   1313       O  
ATOM   2284  N   CYS A 398     -39.714-110.121 253.892  1.00119.67           N  
ANISOU 2284  N   CYS A 398    11413  11750  22307   -772     78   1495       N  
ATOM   2285  CA  CYS A 398     -38.788-109.375 253.058  1.00122.40           C  
ANISOU 2285  CA  CYS A 398    11294  12150  23062   -831      6   2067       C  
ATOM   2286  C   CYS A 398     -39.550-108.481 252.091  1.00127.10           C  
ANISOU 2286  C   CYS A 398    11733  12884  23673   -761    149   2236       C  
ATOM   2287  O   CYS A 398     -40.706-108.746 251.750  1.00122.03           O  
ANISOU 2287  O   CYS A 398    11261  12451  22653   -624    399   1934       O  
ATOM   2288  CB  CYS A 398     -37.864-110.318 252.284  1.00118.63           C  
ANISOU 2288  CB  CYS A 398    10468  12082  22524   -690    294   2378       C  
ATOM   2289  SG  CYS A 398     -36.653-111.157 253.325  1.00119.09           S  
ANISOU 2289  SG  CYS A 398    10554  11957  22740   -785     74   2396       S  
ATOM   2290  N   GLY A 399     -38.893-107.421 251.660  1.00139.86           N  
ANISOU 2290  N   GLY A 399    12990  14371  25781   -872    -39   2773       N  
ATOM   2291  CA  GLY A 399     -39.484-106.485 250.725  1.00146.08           C  
ANISOU 2291  CA  GLY A 399    13570  15274  26658   -807     74   3053       C  
ATOM   2292  C   GLY A 399     -38.424-105.681 250.012  1.00156.19           C  
ANISOU 2292  C   GLY A 399    14272  16572  28500   -897    -19   3862       C  
ATOM   2293  O   GLY A 399     -37.309-106.157 249.783  1.00161.96           O  
ANISOU 2293  O   GLY A 399    14653  17508  29375   -888     55   4268       O  
ATOM   2294  N   ASP A 400     -38.777-104.449 249.653  1.00158.15           N  
ANISOU 2294  N   ASP A 400    14378  16606  29105   -966   -168   4163       N  
ATOM   2295  CA  ASP A 400     -37.850-103.553 248.979  1.00157.74           C  
ANISOU 2295  CA  ASP A 400    13716  16516  29700  -1084   -284   5047       C  
ATOM   2296  C   ASP A 400     -38.350-102.126 249.144  1.00150.43           C  
ANISOU 2296  C   ASP A 400    12849  15020  29287  -1251   -673   5155       C  
ATOM   2297  O   ASP A 400     -39.557-101.877 249.088  1.00141.47           O  
ANISOU 2297  O   ASP A 400    12043  13881  27829  -1107   -558   4745       O  
ATOM   2298  CB  ASP A 400     -37.706-103.910 247.495  1.00160.57           C  
ANISOU 2298  CB  ASP A 400    13595  17677  29738   -762    299   5599       C  
ATOM   2299  CG  ASP A 400     -36.674-103.056 246.784  1.00168.48           C  
ANISOU 2299  CG  ASP A 400    13959  18730  31324   -810    248   6627       C  
ATOM   2300  OD1 ASP A 400     -35.849-102.414 247.469  1.00171.34           O  
ANISOU 2300  OD1 ASP A 400    14292  18519  32291  -1082   -283   6874       O  
ATOM   2301  OD2 ASP A 400     -36.682-103.033 245.535  1.00172.08           O  
ANISOU 2301  OD2 ASP A 400    14164  19801  31416   -473    683   7104       O  
ATOM   2302  N   SER A 401     -37.413-101.197 249.348  1.00151.71           N  
ANISOU 2302  N   SER A 401    12672  14671  30301  -1552  -1163   5735       N  
ATOM   2303  CA  SER A 401     -37.786 -99.803 249.560  1.00149.56           C  
ANISOU 2303  CA  SER A 401    12523  13762  30539  -1669  -1640   5793       C  
ATOM   2304  C   SER A 401     -38.421 -99.190 248.318  1.00145.12           C  
ANISOU 2304  C   SER A 401    11603  13541  29994  -1502  -1256   6312       C  
ATOM   2305  O   SER A 401     -39.222 -98.256 248.433  1.00141.77           O  
ANISOU 2305  O   SER A 401    11385  12666  29814  -1522  -1468   6178       O  
ATOM   2306  CB  SER A 401     -36.562 -98.990 249.983  1.00154.94           C  
ANISOU 2306  CB  SER A 401    13022  14033  31816  -1826  -2318   6169       C  
ATOM   2307  OG  SER A 401     -35.975 -99.521 251.159  1.00153.49           O  
ANISOU 2307  OG  SER A 401    13169  13570  31580  -1969  -2718   5693       O  
ATOM   2308  N   SER A 402     -38.095 -99.710 247.131  1.00148.63           N  
ANISOU 2308  N   SER A 402    11581  14798  30093  -1256   -693   6874       N  
ATOM   2309  CA  SER A 402     -38.577 -99.133 245.880  1.00155.78           C  
ANISOU 2309  CA  SER A 402    12161  16128  30901  -1022   -340   7435       C  
ATOM   2310  C   SER A 402     -40.086 -99.251 245.702  1.00146.39           C  
ANISOU 2310  C   SER A 402    11294  15133  29194   -843    -64   6860       C  
ATOM   2311  O   SER A 402     -40.632 -98.617 244.792  1.00146.60           O  
ANISOU 2311  O   SER A 402    11074  15409  29219   -684    136   7283       O  
ATOM   2312  CB  SER A 402     -37.870 -99.790 244.692  1.00163.63           C  
ANISOU 2312  CB  SER A 402    12811  17992  31369   -674    199   8033       C  
ATOM   2313  OG  SER A 402     -38.269 -99.194 243.469  1.00174.25           O  
ANISOU 2313  OG  SER A 402    13905  19762  32540   -416    508   8616       O  
ATOM   2314  N   TRP A 403     -40.767-100.030 246.533  1.00139.31           N  
ANISOU 2314  N   TRP A 403    11010  14163  27760   -793    -68   5917       N  
ATOM   2315  CA  TRP A 403     -42.203-100.223 246.414  1.00137.75           C  
ANISOU 2315  CA  TRP A 403    11189  14183  26969   -563    166   5345       C  
ATOM   2316  C   TRP A 403     -42.940 -99.378 247.447  1.00138.13           C  
ANISOU 2316  C   TRP A 403    11701  13471  27310   -654   -240   4874       C  
ATOM   2317  O   TRP A 403     -42.431 -99.112 248.539  1.00136.62           O  
ANISOU 2317  O   TRP A 403    11779  12627  27503   -858   -702   4627       O  
ATOM   2318  CB  TRP A 403     -42.564-101.701 246.576  1.00135.32           C  
ANISOU 2318  CB  TRP A 403    11192  14344  25878   -406    473   4697       C  
ATOM   2319  CG  TRP A 403     -41.835-102.581 245.603  1.00138.91           C  
ANISOU 2319  CG  TRP A 403    11291  15504  25983   -224    849   5056       C  
ATOM   2320  CD1 TRP A 403     -40.596-103.129 245.764  1.00143.44           C  
ANISOU 2320  CD1 TRP A 403    11668  16137  26697   -286    847   5291       C  
ATOM   2321  CD2 TRP A 403     -42.295-103.001 244.312  1.00138.85           C  
ANISOU 2321  CD2 TRP A 403    11104  16258  25394    117   1270   5217       C  
ATOM   2322  NE1 TRP A 403     -40.257-103.868 244.656  1.00144.95           N  
ANISOU 2322  NE1 TRP A 403    11583  17083  26408     45   1289   5582       N  
ATOM   2323  CE2 TRP A 403     -41.283-103.806 243.750  1.00142.87           C  
ANISOU 2323  CE2 TRP A 403    11358  17257  25668    304   1530   5511       C  
ATOM   2324  CE3 TRP A 403     -43.464-102.777 243.578  1.00137.03           C  
ANISOU 2324  CE3 TRP A 403    10914  16351  24798    315   1426   5137       C  
ATOM   2325  CZ2 TRP A 403     -41.406-104.388 242.489  1.00143.89           C  
ANISOU 2325  CZ2 TRP A 403    11344  18178  25151    729   1930   5665       C  
ATOM   2326  CZ3 TRP A 403     -43.584-103.356 242.326  1.00138.06           C  
ANISOU 2326  CZ3 TRP A 403    10878  17261  24317    675   1772   5303       C  
ATOM   2327  CH2 TRP A 403     -42.561-104.151 241.795  1.00141.60           C  
ANISOU 2327  CH2 TRP A 403    11143  18178  24483    901   2016   5536       C  
ATOM   2328  N   GLU A 404     -44.152 -98.953 247.081  1.00140.59           N  
ANISOU 2328  N   GLU A 404    12117  13891  27409   -454    -76   4750       N  
ATOM   2329  CA  GLU A 404     -44.923 -98.062 247.942  1.00147.26           C  
ANISOU 2329  CA  GLU A 404    13385  14062  28505   -422   -394   4360       C  
ATOM   2330  C   GLU A 404     -45.339 -98.744 249.240  1.00144.29           C  
ANISOU 2330  C   GLU A 404    13615  13477  27730   -364   -473   3514       C  
ATOM   2331  O   GLU A 404     -45.542 -98.069 250.256  1.00146.96           O  
ANISOU 2331  O   GLU A 404    14384  13149  28304   -331   -848   3150       O  
ATOM   2332  CB  GLU A 404     -46.155 -97.551 247.193  1.00150.56           C  
ANISOU 2332  CB  GLU A 404    13716  14744  28746   -171   -132   4477       C  
ATOM   2333  CG  GLU A 404     -46.929 -96.458 247.916  1.00155.45           C  
ANISOU 2333  CG  GLU A 404    14704  14669  29692    -52   -424   4207       C  
ATOM   2334  CD  GLU A 404     -46.741 -95.094 247.282  1.00162.85           C  
ANISOU 2334  CD  GLU A 404    15306  15218  31353    -99   -652   4894       C  
ATOM   2335  OE1 GLU A 404     -45.997 -95.001 246.283  1.00165.49           O  
ANISOU 2335  OE1 GLU A 404    15073  15875  31930   -234   -551   5649       O  
ATOM   2336  OE2 GLU A 404     -47.340 -94.116 247.779  1.00166.98           O  
ANISOU 2336  OE2 GLU A 404    16125  15116  32202     38   -916   4712       O  
ATOM   2337  N   TYR A 405     -45.464-100.068 249.232  1.00140.34           N  
ANISOU 2337  N   TYR A 405    13173  13524  26626   -315   -141   3207       N  
ATOM   2338  CA  TYR A 405     -45.945-100.829 250.384  1.00138.87           C  
ANISOU 2338  CA  TYR A 405    13491  13249  26024   -236   -130   2507       C  
ATOM   2339  C   TYR A 405     -44.815-101.728 250.867  1.00136.87           C  
ANISOU 2339  C   TYR A 405    13263  13007  25735   -424   -236   2422       C  
ATOM   2340  O   TYR A 405     -44.753-102.912 250.530  1.00135.39           O  
ANISOU 2340  O   TYR A 405    12979  13328  25134   -407     74   2342       O  
ATOM   2341  CB  TYR A 405     -47.180-101.615 250.014  1.00137.12           C  
ANISOU 2341  CB  TYR A 405    13292  13591  25217    -37    305   2259       C  
ATOM   2342  CG  TYR A 405     -48.178-100.782 249.251  1.00142.66           C  
ANISOU 2342  CG  TYR A 405    13816  14413  25976    136    436   2500       C  
ATOM   2343  CD1 TYR A 405     -48.930 -99.807 249.893  1.00147.18           C  
ANISOU 2343  CD1 TYR A 405    14664  14529  26729    317    296   2330       C  
ATOM   2344  CD2 TYR A 405     -48.354-100.955 247.887  1.00144.87           C  
ANISOU 2344  CD2 TYR A 405    13672  15270  26100    172    688   2899       C  
ATOM   2345  CE1 TYR A 405     -49.836 -99.032 249.199  1.00151.12           C  
ANISOU 2345  CE1 TYR A 405    14977  15129  27314    496    419   2588       C  
ATOM   2346  CE2 TYR A 405     -49.258-100.187 247.184  1.00150.37           C  
ANISOU 2346  CE2 TYR A 405    14188  16100  26847    334    785   3159       C  
ATOM   2347  CZ  TYR A 405     -49.997 -99.227 247.844  1.00153.11           C  
ANISOU 2347  CZ  TYR A 405    14768  15970  27437    479    657   3022       C  
ATOM   2348  OH  TYR A 405     -50.901 -98.459 247.147  1.00156.25           O  
ANISOU 2348  OH  TYR A 405    14963  16495  27911    662    760   3313       O  
ATOM   2349  N   PHE A 406     -43.916-101.152 251.662  1.00136.40           N  
ANISOU 2349  N   PHE A 406    13343  12344  26139   -597   -725   2436       N  
ATOM   2350  CA  PHE A 406     -42.783-101.894 252.202  1.00131.32           C  
ANISOU 2350  CA  PHE A 406    12703  11657  25537   -785   -898   2404       C  
ATOM   2351  C   PHE A 406     -43.294-102.958 253.164  1.00126.77           C  
ANISOU 2351  C   PHE A 406    12581  11214  24372   -652   -747   1770       C  
ATOM   2352  O   PHE A 406     -43.822-102.633 254.231  1.00128.85           O  
ANISOU 2352  O   PHE A 406    13339  11107  24511   -516   -952   1315       O  
ATOM   2353  CB  PHE A 406     -41.817-100.947 252.904  1.00136.40           C  
ANISOU 2353  CB  PHE A 406    13417  11558  26852  -1015  -1571   2539       C  
ATOM   2354  CG  PHE A 406     -40.524-101.593 253.297  1.00137.44           C  
ANISOU 2354  CG  PHE A 406    13407  11664  27151  -1245  -1792   2677       C  
ATOM   2355  CD1 PHE A 406     -39.431-101.538 252.452  1.00140.94           C  
ANISOU 2355  CD1 PHE A 406    13212  12279  28062  -1447  -1786   3421       C  
ATOM   2356  CD2 PHE A 406     -40.402-102.266 254.502  1.00134.38           C  
ANISOU 2356  CD2 PHE A 406    13487  11129  26443  -1220  -1974   2128       C  
ATOM   2357  CE1 PHE A 406     -38.242-102.131 252.802  1.00139.66           C  
ANISOU 2357  CE1 PHE A 406    12862  12118  28083  -1632  -1969   3609       C  
ATOM   2358  CE2 PHE A 406     -39.211-102.866 254.856  1.00134.14           C  
ANISOU 2358  CE2 PHE A 406    13299  11088  26580  -1423  -2187   2289       C  
ATOM   2359  CZ  PHE A 406     -38.128-102.798 254.004  1.00136.65           C  
ANISOU 2359  CZ  PHE A 406    12961  11557  27404  -1634  -2189   3027       C  
ATOM   2360  N   CYS A 407     -43.136-104.227 252.787  1.00117.82           N  
ANISOU 2360  N   CYS A 407    11289  10605  22873   -650   -388   1763       N  
ATOM   2361  CA  CYS A 407     -43.582-105.356 253.604  1.00105.33           C  
ANISOU 2361  CA  CYS A 407    10051   9171  20799   -555   -221   1275       C  
ATOM   2362  C   CYS A 407     -45.053-105.218 253.980  1.00103.43           C  
ANISOU 2362  C   CYS A 407    10109   8964  20225   -323    -31    923       C  
ATOM   2363  O   CYS A 407     -45.449-105.426 255.130  1.00104.31           O  
ANISOU 2363  O   CYS A 407    10631   8909  20095   -192    -85    544       O  
ATOM   2364  CB  CYS A 407     -42.715-105.516 254.855  1.00101.40           C  
ANISOU 2364  CB  CYS A 407     9848   8283  20397   -657   -611   1072       C  
ATOM   2365  SG  CYS A 407     -41.002-106.004 254.539  1.00105.51           S  
ANISOU 2365  SG  CYS A 407     9960   8855  21273   -911   -775   1513       S  
ATOM   2366  N   GLY A 408     -45.876-104.853 252.997  1.00103.95           N  
ANISOU 2366  N   GLY A 408     9941   9291  20265   -233    209   1101       N  
ATOM   2367  CA  GLY A 408     -47.309-104.799 253.227  1.00110.44           C  
ANISOU 2367  CA  GLY A 408    10932  10227  20803     -7    434    866       C  
ATOM   2368  C   GLY A 408     -47.907-106.138 253.604  1.00115.54           C  
ANISOU 2368  C   GLY A 408    11667  11200  21034     33    712    609       C  
ATOM   2369  O   GLY A 408     -48.990-106.179 254.201  1.00118.60           O  
ANISOU 2369  O   GLY A 408    12230  11625  21208    228    872    427       O  
ATOM   2370  N   ALA A 409     -47.226-107.236 253.254  1.00115.20           N  
ANISOU 2370  N   ALA A 409    11478  11387  20905   -126    777    639       N  
ATOM   2371  CA  ALA A 409     -47.647-108.569 253.675  1.00105.63           C  
ANISOU 2371  CA  ALA A 409    10355  10377  19402   -130    963    420       C  
ATOM   2372  C   ALA A 409     -47.682-108.676 255.193  1.00105.08           C  
ANISOU 2372  C   ALA A 409    10669  10045  19212    -34    888    181       C  
ATOM   2373  O   ALA A 409     -48.629-109.230 255.766  1.00101.42           O  
ANISOU 2373  O   ALA A 409    10302   9711  18524     85   1095     69       O  
ATOM   2374  CB  ALA A 409     -46.701-109.618 253.092  1.00 98.38           C  
ANISOU 2374  CB  ALA A 409     9274   9642  18464   -270    981    477       C  
ATOM   2375  N   VAL A 410     -46.657-108.139 255.860  1.00109.71           N  
ANISOU 2375  N   VAL A 410    11460  10276  19949    -67    571    143       N  
ATOM   2376  CA  VAL A 410     -46.591-108.204 257.317  1.00110.93           C  
ANISOU 2376  CA  VAL A 410    12040  10198  19910     78    436   -112       C  
ATOM   2377  C   VAL A 410     -47.760-107.450 257.939  1.00117.31           C  
ANISOU 2377  C   VAL A 410    13117  10936  20517    418    538   -268       C  
ATOM   2378  O   VAL A 410     -48.306-107.857 258.972  1.00120.05           O  
ANISOU 2378  O   VAL A 410    13735  11355  20523    660    685   -425       O  
ATOM   2379  CB  VAL A 410     -45.234-107.664 257.804  1.00107.12           C  
ANISOU 2379  CB  VAL A 410    11713   9311  19679    -45    -45   -121       C  
ATOM   2380  CG1 VAL A 410     -45.121-107.748 259.318  1.00108.69           C  
ANISOU 2380  CG1 VAL A 410    12409   9293  19596    146   -250   -424       C  
ATOM   2381  CG2 VAL A 410     -44.097-108.423 257.130  1.00105.27           C  
ANISOU 2381  CG2 VAL A 410    11133   9215  19650   -321    -68    122       C  
ATOM   2382  N   ASP A 411     -48.177-106.350 257.308  1.00118.58           N  
ANISOU 2382  N   ASP A 411    13187  10988  20879    490    496   -178       N  
ATOM   2383  CA  ASP A 411     -49.312-105.589 257.818  1.00122.75           C  
ANISOU 2383  CA  ASP A 411    13953  11455  21230    881    625   -304       C  
ATOM   2384  C   ASP A 411     -50.616-106.358 257.651  1.00120.91           C  
ANISOU 2384  C   ASP A 411    13491  11699  20749   1003   1115   -193       C  
ATOM   2385  O   ASP A 411     -51.448-106.385 258.567  1.00120.95           O  
ANISOU 2385  O   ASP A 411    13716  11791  20449   1364   1332   -282       O  
ATOM   2386  CB  ASP A 411     -49.392-104.237 257.111  1.00129.22           C  
ANISOU 2386  CB  ASP A 411    14693  12005  22401    913    441   -186       C  
ATOM   2387  CG  ASP A 411     -48.108-103.440 257.232  1.00133.94           C  
ANISOU 2387  CG  ASP A 411    15437  12068  23386    733   -111   -203       C  
ATOM   2388  OD1 ASP A 411     -47.394-103.609 258.244  1.00138.46           O  
ANISOU 2388  OD1 ASP A 411    16368  12379  23860    745   -414   -449       O  
ATOM   2389  OD2 ASP A 411     -47.812-102.645 256.315  1.00133.32           O  
ANISOU 2389  OD2 ASP A 411    15086  11832  23739    572   -266     78       O  
ATOM   2390  N   ALA A 412     -50.813-106.991 256.491  1.00121.74           N  
ANISOU 2390  N   ALA A 412    13146  12125  20984    730   1272     27       N  
ATOM   2391  CA  ALA A 412     -52.052-107.725 256.251  1.00120.88           C  
ANISOU 2391  CA  ALA A 412    12767  12413  20748    773   1623    163       C  
ATOM   2392  C   ALA A 412     -52.174-108.923 257.183  1.00120.47           C  
ANISOU 2392  C   ALA A 412    12805  12488  20480    781   1781    121       C  
ATOM   2393  O   ALA A 412     -53.274-109.251 257.644  1.00118.23           O  
ANISOU 2393  O   ALA A 412    12429  12426  20065    973   2073    254       O  
ATOM   2394  CB  ALA A 412     -52.124-108.173 254.791  1.00115.29           C  
ANISOU 2394  CB  ALA A 412    11632  11972  20201    483   1631    337       C  
ATOM   2395  N   ILE A 413     -51.055-109.588 257.473  1.00121.06           N  
ANISOU 2395  N   ILE A 413    13012  12436  20550    585   1605      9       N  
ATOM   2396  CA  ILE A 413     -51.084-110.745 258.363  1.00120.64           C  
ANISOU 2396  CA  ILE A 413    13036  12478  20324    587   1738     15       C  
ATOM   2397  C   ILE A 413     -51.357-110.307 259.797  1.00126.91           C  
ANISOU 2397  C   ILE A 413    14226  13204  20788   1005   1821    -73       C  
ATOM   2398  O   ILE A 413     -52.216-110.873 260.483  1.00128.76           O  
ANISOU 2398  O   ILE A 413    14417  13677  20830   1207   2135     94       O  
ATOM   2399  CB  ILE A 413     -49.769-111.536 258.253  1.00113.99           C  
ANISOU 2399  CB  ILE A 413    12222  11514  19574    304   1521    -61       C  
ATOM   2400  CG1 ILE A 413     -49.599-112.090 256.838  1.00105.72           C  
ANISOU 2400  CG1 ILE A 413    10823  10603  18744     14   1496     10       C  
ATOM   2401  CG2 ILE A 413     -49.734-112.661 259.277  1.00113.57           C  
ANISOU 2401  CG2 ILE A 413    12280  11514  19359    331   1634    -28       C  
ATOM   2402  CD1 ILE A 413     -48.254-112.733 256.598  1.00101.66           C  
ANISOU 2402  CD1 ILE A 413    10318   9991  18319   -175   1319    -39       C  
ATOM   2403  N   GLU A 414     -50.632-109.287 260.269  1.00131.39           N  
ANISOU 2403  N   GLU A 414    15187  13446  21289   1168   1519   -313       N  
ATOM   2404  CA  GLU A 414     -50.829-108.797 261.630  1.00139.56           C  
ANISOU 2404  CA  GLU A 414    16712  14393  21920   1654   1522   -492       C  
ATOM   2405  C   GLU A 414     -52.252-108.301 261.851  1.00150.37           C  
ANISOU 2405  C   GLU A 414    18057  15990  23087   2109   1912   -376       C  
ATOM   2406  O   GLU A 414     -52.765-108.368 262.974  1.00156.13           O  
ANISOU 2406  O   GLU A 414    19060  16879  23383   2587   2143   -379       O  
ATOM   2407  CB  GLU A 414     -49.828-107.683 261.939  1.00139.38           C  
ANISOU 2407  CB  GLU A 414    17122  13882  21953   1717    996   -813       C  
ATOM   2408  CG  GLU A 414     -48.402-108.164 262.142  1.00138.93           C  
ANISOU 2408  CG  GLU A 414    17148  13619  22018   1386    602   -893       C  
ATOM   2409  CD  GLU A 414     -47.405-107.023 262.206  1.00144.51           C  
ANISOU 2409  CD  GLU A 414    18136  13798  22975   1322     -4  -1109       C  
ATOM   2410  OE1 GLU A 414     -47.726-105.922 261.708  1.00148.16           O  
ANISOU 2410  OE1 GLU A 414    18604  14032  23659   1400   -115  -1139       O  
ATOM   2411  OE2 GLU A 414     -46.302-107.227 262.756  1.00144.63           O  
ANISOU 2411  OE2 GLU A 414    18337  13600  23015   1181   -404  -1211       O  
ATOM   2412  N   GLU A 415     -52.904-107.802 260.798  1.00152.43           N  
ANISOU 2412  N   GLU A 415    17977  16311  23628   2016   2009   -231       N  
ATOM   2413  CA  GLU A 415     -54.286-107.357 260.936  1.00156.08           C  
ANISOU 2413  CA  GLU A 415    18330  17020  23952   2448   2398    -49       C  
ATOM   2414  C   GLU A 415     -55.220-108.535 261.185  1.00154.43           C  
ANISOU 2414  C   GLU A 415    17735  17277  23663   2450   2844    341       C  
ATOM   2415  O   GLU A 415     -56.185-108.417 261.947  1.00157.77           O  
ANISOU 2415  O   GLU A 415    18180  17961  23803   2953   3229    535       O  
ATOM   2416  CB  GLU A 415     -54.715-106.579 259.693  1.00158.18           C  
ANISOU 2416  CB  GLU A 415    18279  17246  24575   2311   2356     59       C  
ATOM   2417  CG  GLU A 415     -56.014-105.804 259.863  1.00165.45           C  
ANISOU 2417  CG  GLU A 415    19152  18328  25383   2833   2688    211       C  
ATOM   2418  CD  GLU A 415     -55.888-104.654 260.847  1.00171.80           C  
ANISOU 2418  CD  GLU A 415    20596  18795  25887   3441   2574   -131       C  
ATOM   2419  OE1 GLU A 415     -54.754-104.179 261.071  1.00171.98           O  
ANISOU 2419  OE1 GLU A 415    21043  18351  25950   3339   2098   -491       O  
ATOM   2420  OE2 GLU A 415     -56.924-104.225 261.397  1.00176.44           O  
ANISOU 2420  OE2 GLU A 415    21262  19570  26207   4047   2935    -35       O  
ATOM   2421  N   LYS A 416     -54.947-109.680 260.555  1.00152.33           N  
ANISOU 2421  N   LYS A 416    17103  17108  23666   1920   2790    491       N  
ATOM   2422  CA  LYS A 416     -55.758-110.867 260.806  1.00155.19           C  
ANISOU 2422  CA  LYS A 416    17082  17809  24073   1846   3113    891       C  
ATOM   2423  C   LYS A 416     -55.428-111.505 262.149  1.00164.07           C  
ANISOU 2423  C   LYS A 416    18490  18996  24853   2081   3247    932       C  
ATOM   2424  O   LYS A 416     -56.308-112.097 262.784  1.00168.56           O  
ANISOU 2424  O   LYS A 416    18828  19889  25330   2295   3634   1351       O  
ATOM   2425  CB  LYS A 416     -55.568-111.888 259.685  1.00145.82           C  
ANISOU 2425  CB  LYS A 416    15482  16620  23302   1234   2927    975       C  
ATOM   2426  CG  LYS A 416     -56.628-111.831 258.601  1.00142.53           C  
ANISOU 2426  CG  LYS A 416    14565  16397  23194   1072   2981   1220       C  
ATOM   2427  CD  LYS A 416     -56.602-113.089 257.750  1.00137.67           C  
ANISOU 2427  CD  LYS A 416    13600  15788  22920    551   2783   1300       C  
ATOM   2428  CE  LYS A 416     -57.722-113.086 256.723  1.00137.33           C  
ANISOU 2428  CE  LYS A 416    13066  15943  23172    389   2753   1543       C  
ATOM   2429  NZ  LYS A 416     -57.655-114.271 255.823  1.00133.84           N  
ANISOU 2429  NZ  LYS A 416    12375  15438  23039    -91   2439   1513       N  
ATOM   2430  N   LEU A 417     -54.175-111.400 262.595  1.00169.65           N  
ANISOU 2430  N   LEU A 417    19652  19421  25384   2049   2927    569       N  
ATOM   2431  CA  LEU A 417     -53.781-112.030 263.851  1.00175.13           C  
ANISOU 2431  CA  LEU A 417    20632  20191  25719   2269   3004    607       C  
ATOM   2432  C   LEU A 417     -54.405-111.316 265.045  1.00180.67           C  
ANISOU 2432  C   LEU A 417    21710  21086  25849   3027   3286    616       C  
ATOM   2433  O   LEU A 417     -55.014-111.954 265.911  1.00185.30           O  
ANISOU 2433  O   LEU A 417    22208  22034  26164   3344   3687    997       O  
ATOM   2434  CB  LEU A 417     -52.257-112.057 263.966  1.00174.91           C  
ANISOU 2434  CB  LEU A 417    20964  19812  25683   2029   2528    232       C  
ATOM   2435  CG  LEU A 417     -51.546-112.899 262.905  1.00171.15           C  
ANISOU 2435  CG  LEU A 417    20149  19200  25679   1397   2312    250       C  
ATOM   2436  CD1 LEU A 417     -50.041-112.761 263.032  1.00172.01           C  
ANISOU 2436  CD1 LEU A 417    20565  18992  25799   1228   1868    -51       C  
ATOM   2437  CD2 LEU A 417     -51.965-114.358 263.005  1.00169.42           C  
ANISOU 2437  CD2 LEU A 417    19574  19185  25612   1193   2555    619       C  
ATOM   2438  N   LYS A 418     -54.262-109.990 265.110  1.00176.72           N  
ANISOU 2438  N   LYS A 418    21639  20345  25161   3368   3081    223       N  
ATOM   2439  CA  LYS A 418     -54.910-109.233 266.175  1.00176.07           C  
ANISOU 2439  CA  LYS A 418    21983  20428  24489   4196   3340    160       C  
ATOM   2440  C   LYS A 418     -56.423-109.199 266.016  1.00174.04           C  
ANISOU 2440  C   LYS A 418    21264  20607  24255   4522   3936    653       C  
ATOM   2441  O   LYS A 418     -57.128-108.897 266.985  1.00179.10           O  
ANISOU 2441  O   LYS A 418    22129  21559  24363   5283   4333    787       O  
ATOM   2442  CB  LYS A 418     -54.356-107.808 266.232  1.00175.20           C  
ANISOU 2442  CB  LYS A 418    22479  19833  24255   4465   2875   -429       C  
ATOM   2443  CG  LYS A 418     -53.038-107.693 266.979  1.00173.94           C  
ANISOU 2443  CG  LYS A 418    22932  19312  23845   4461   2315   -889       C  
ATOM   2444  CD  LYS A 418     -52.556-106.253 267.049  1.00174.39           C  
ANISOU 2444  CD  LYS A 418    23575  18805  23879   4707   1767  -1448       C  
ATOM   2445  CE  LYS A 418     -51.263-106.145 267.842  1.00173.77           C  
ANISOU 2445  CE  LYS A 418    24089  18346  23589   4687   1117  -1886       C  
ATOM   2446  NZ  LYS A 418     -50.755-104.747 267.900  1.00176.36           N  
ANISOU 2446  NZ  LYS A 418    24979  18015  24015   4859    457  -2423       N  
ATOM   2447  N   ASN A 419     -56.935-109.496 264.819  1.00166.39           N  
ANISOU 2447  N   ASN A 419    19656  19694  23871   4003   3996    943       N  
ATOM   2448  CA  ASN A 419     -58.377-109.632 264.645  1.00167.78           C  
ANISOU 2448  CA  ASN A 419    19271  20307  24170   4217   4518   1516       C  
ATOM   2449  C   ASN A 419     -58.912-110.799 265.462  1.00169.24           C  
ANISOU 2449  C   ASN A 419    19135  20936  24231   4338   4960   2106       C  
ATOM   2450  O   ASN A 419     -59.954-110.684 266.119  1.00175.08           O  
ANISOU 2450  O   ASN A 419    19705  22112  24704   4944   5498   2564       O  
ATOM   2451  CB  ASN A 419     -58.708-109.813 263.162  1.00164.68           C  
ANISOU 2451  CB  ASN A 419    18277  19855  24438   3566   4362   1673       C  
ATOM   2452  CG  ASN A 419     -60.198-109.749 262.877  1.00171.55           C  
ANISOU 2452  CG  ASN A 419    18550  21126  25506   3768   4797   2247       C  
ATOM   2453  OD1 ASN A 419     -60.994-110.480 263.467  1.00176.19           O  
ANISOU 2453  OD1 ASN A 419    18759  22111  26075   3941   5218   2821       O  
ATOM   2454  ND2 ASN A 419     -60.582-108.867 261.962  1.00173.39           N  
ANISOU 2454  ND2 ASN A 419    18645  21267  25968   3743   4694   2164       N  
ATOM   2455  N   LEU A 420     -58.209-111.927 265.439  1.00166.23           N  
ANISOU 2455  N   LEU A 420    18642  20456  24060   3800   4759   2158       N  
ATOM   2456  CA  LEU A 420     -58.633-113.129 266.140  1.00168.48           C  
ANISOU 2456  CA  LEU A 420    18571  21090  24355   3812   5117   2779       C  
ATOM   2457  C   LEU A 420     -58.146-113.180 267.582  1.00172.62           C  
ANISOU 2457  C   LEU A 420    19648  21773  24166   4406   5272   2720       C  
ATOM   2458  O   LEU A 420     -58.505-114.112 268.309  1.00179.08           O  
ANISOU 2458  O   LEU A 420    20193  22936  24913   4528   5631   3312       O  
ATOM   2459  CB  LEU A 420     -58.150-114.369 265.381  1.00161.25           C  
ANISOU 2459  CB  LEU A 420    17269  19941  24057   2964   4797   2873       C  
ATOM   2460  CG  LEU A 420     -58.516-114.387 263.895  1.00154.14           C  
ANISOU 2460  CG  LEU A 420    15904  18873  23790   2381   4543   2844       C  
ATOM   2461  CD1 LEU A 420     -58.031-115.664 263.227  1.00147.63           C  
ANISOU 2461  CD1 LEU A 420    14799  17801  23491   1659   4207   2875       C  
ATOM   2462  CD2 LEU A 420     -60.017-114.215 263.705  1.00157.63           C  
ANISOU 2462  CD2 LEU A 420    15759  19680  24454   2571   4929   3436       C  
ATOM   2463  N   GLY A 421     -57.344-112.210 268.013  1.00170.02           N  
ANISOU 2463  N   GLY A 421    20079  21194  23329   4776   4973   2052       N  
ATOM   2464  CA  GLY A 421     -56.895-112.137 269.386  1.00171.28           C  
ANISOU 2464  CA  GLY A 421    20854  21504  22719   5417   5038   1911       C  
ATOM   2465  C   GLY A 421     -55.526-112.714 269.668  1.00163.96           C  
ANISOU 2465  C   GLY A 421    20264  20278  21754   5033   4554   1586       C  
ATOM   2466  O   GLY A 421     -55.137-112.785 270.839  1.00167.41           O  
ANISOU 2466  O   GLY A 421    21189  20878  21540   5540   4575   1516       O  
ATOM   2467  N   ALA A 422     -54.787-113.129 268.642  1.00154.59           N  
ANISOU 2467  N   ALA A 422    18837  18696  21206   4208   4129   1404       N  
ATOM   2468  CA  ALA A 422     -53.449-113.668 268.848  1.00152.33           C  
ANISOU 2468  CA  ALA A 422    18816  18127  20937   3850   3677   1133       C  
ATOM   2469  C   ALA A 422     -52.520-112.568 269.348  1.00155.87           C  
ANISOU 2469  C   ALA A 422    20030  18253  20941   4167   3178    456       C  
ATOM   2470  O   ALA A 422     -52.382-111.522 268.704  1.00157.24           O  
ANISOU 2470  O   ALA A 422    20359  18094  21289   4103   2881     53       O  
ATOM   2471  CB  ALA A 422     -52.919-114.277 267.553  1.00144.69           C  
ANISOU 2471  CB  ALA A 422    17414  16837  20726   2999   3379   1095       C  
ATOM   2472  N   GLU A 423     -51.884-112.802 270.494  1.00158.05           N  
ANISOU 2472  N   GLU A 423    20775  18605  20673   4502   3040    355       N  
ATOM   2473  CA  GLU A 423     -51.028-111.794 271.112  1.00161.83           C  
ANISOU 2473  CA  GLU A 423    22029  18759  20702   4841   2472   -293       C  
ATOM   2474  C   GLU A 423     -49.772-111.600 270.273  1.00159.86           C  
ANISOU 2474  C   GLU A 423    21757  17942  21042   4125   1799   -659       C  
ATOM   2475  O   GLU A 423     -48.900-112.474 270.234  1.00154.63           O  
ANISOU 2475  O   GLU A 423    20931  17209  20611   3680   1599   -546       O  
ATOM   2476  CB  GLU A 423     -50.667-112.203 272.536  1.00165.48           C  
ANISOU 2476  CB  GLU A 423    22971  19496  20409   5373   2461   -269       C  
ATOM   2477  CG  GLU A 423     -49.865-111.150 273.288  1.00169.24           C  
ANISOU 2477  CG  GLU A 423    24324  19631  20348   5803   1792   -980       C  
ATOM   2478  CD  GLU A 423     -49.414-111.619 274.656  1.00173.03           C  
ANISOU 2478  CD  GLU A 423    25293  20402  20048   6304   1701   -972       C  
ATOM   2479  OE1 GLU A 423     -48.209-111.495 274.961  1.00171.48           O  
ANISOU 2479  OE1 GLU A 423    25487  19845  19824   6099    978  -1370       O  
ATOM   2480  OE2 GLU A 423     -50.263-112.117 275.425  1.00178.00           O  
ANISOU 2480  OE2 GLU A 423    25882  21646  20103   6912   2349   -511       O  
ATOM   2481  N   ILE A 424     -49.677-110.455 269.600  1.00165.79           N  
ANISOU 2481  N   ILE A 424    22638  18297  22056   4042   1469  -1036       N  
ATOM   2482  CA  ILE A 424     -48.475-110.089 268.854  1.00168.38           C  
ANISOU 2482  CA  ILE A 424    22943  18099  22934   3444    826  -1318       C  
ATOM   2483  C   ILE A 424     -47.492-109.497 269.860  1.00183.00           C  
ANISOU 2483  C   ILE A 424    25500  19624  24409   3709    156  -1783       C  
ATOM   2484  O   ILE A 424     -47.649-108.359 270.305  1.00187.99           O  
ANISOU 2484  O   ILE A 424    26688  20000  24739   4178   -141  -2205       O  
ATOM   2485  CB  ILE A 424     -48.779-109.118 267.713  1.00161.95           C  
ANISOU 2485  CB  ILE A 424    21924  17002  22607   3237    744  -1427       C  
ATOM   2486  CG1 ILE A 424     -49.760-109.754 266.726  1.00156.09           C  
ANISOU 2486  CG1 ILE A 424    20498  16607  22204   2979   1335   -979       C  
ATOM   2487  CG2 ILE A 424     -47.498-108.712 267.002  1.00156.85           C  
ANISOU 2487  CG2 ILE A 424    21212  15853  22529   2668    104  -1606       C  
ATOM   2488  CD1 ILE A 424     -49.993-108.934 265.476  1.00153.40           C  
ANISOU 2488  CD1 ILE A 424    19881  16047  22359   2717   1256  -1016       C  
ATOM   2489  N   VAL A 425     -46.470-110.274 270.225  1.00191.46           N  
ANISOU 2489  N   VAL A 425    26563  20674  25510   3421   -131  -1718       N  
ATOM   2490  CA  VAL A 425     -45.572-109.865 271.300  1.00197.58           C  
ANISOU 2490  CA  VAL A 425    27998  21205  25870   3689   -796  -2115       C  
ATOM   2491  C   VAL A 425     -44.659-108.734 270.842  1.00195.10           C  
ANISOU 2491  C   VAL A 425    27866  20212  26052   3366  -1613  -2510       C  
ATOM   2492  O   VAL A 425     -44.365-107.808 271.608  1.00202.61           O  
ANISOU 2492  O   VAL A 425    29496  20813  26673   3745  -2222  -2998       O  
ATOM   2493  CB  VAL A 425     -44.768-111.073 271.812  1.00200.95           C  
ANISOU 2493  CB  VAL A 425    28296  21835  26219   3470   -852  -1851       C  
ATOM   2494  CG1 VAL A 425     -44.031-110.710 273.087  1.00208.21           C  
ANISOU 2494  CG1 VAL A 425    29944  22618  26547   3874  -1500  -2236       C  
ATOM   2495  CG2 VAL A 425     -45.688-112.262 272.042  1.00202.74           C  
ANISOU 2495  CG2 VAL A 425    28177  22668  26187   3650    -29  -1325       C  
ATOM   2496  N   GLN A 426     -44.194-108.787 269.596  1.00184.93           N  
ANISOU 2496  N   GLN A 426    25982  18717  25566   2688  -1666  -2286       N  
ATOM   2497  CA  GLN A 426     -43.337-107.744 269.052  1.00182.49           C  
ANISOU 2497  CA  GLN A 426    25696  17789  25852   2328  -2385  -2492       C  
ATOM   2498  C   GLN A 426     -43.724-107.481 267.604  1.00177.27           C  
ANISOU 2498  C   GLN A 426    24438  17099  25816   1947  -2055  -2225       C  
ATOM   2499  O   GLN A 426     -44.309-108.334 266.930  1.00169.70           O  
ANISOU 2499  O   GLN A 426    22982  16568  24930   1797  -1400  -1877       O  
ATOM   2500  CB  GLN A 426     -41.851-108.120 269.155  1.00181.55           C  
ANISOU 2500  CB  GLN A 426    25442  17435  26102   1852  -2995  -2399       C  
ATOM   2501  CG  GLN A 426     -40.898-106.955 268.916  1.00182.44           C  
ANISOU 2501  CG  GLN A 426    25657  16856  26805   1546  -3889  -2589       C  
ATOM   2502  CD  GLN A 426     -39.445-107.352 269.049  1.00179.63           C  
ANISOU 2502  CD  GLN A 426    25086  16313  26850   1086  -4482  -2404       C  
ATOM   2503  OE1 GLN A 426     -39.129-108.402 269.601  1.00177.03           O  
ANISOU 2503  OE1 GLN A 426    24729  16330  26204   1117  -4327  -2265       O  
ATOM   2504  NE2 GLN A 426     -38.551-106.513 268.538  1.00179.83           N  
ANISOU 2504  NE2 GLN A 426    24912  15788  27627    655  -5163  -2331       N  
ATOM   2505  N   ASP A 427     -43.389-106.281 267.133  1.00179.14           N  
ANISOU 2505  N   ASP A 427    24741  16804  26519   1799  -2568  -2383       N  
ATOM   2506  CA  ASP A 427     -43.720-105.865 265.779  1.00175.21           C  
ANISOU 2506  CA  ASP A 427    23719  16265  26587   1491  -2317  -2118       C  
ATOM   2507  C   ASP A 427     -43.075-106.791 264.750  1.00164.38           C  
ANISOU 2507  C   ASP A 427    21634  15141  25683    920  -2084  -1649       C  
ATOM   2508  O   ASP A 427     -42.132-107.533 265.038  1.00163.46           O  
ANISOU 2508  O   ASP A 427    21417  15067  25622    691  -2275  -1535       O  
ATOM   2509  CB  ASP A 427     -43.268-104.425 265.536  1.00181.99           C  
ANISOU 2509  CB  ASP A 427    24759  16438  27951   1392  -3011  -2295       C  
ATOM   2510  CG  ASP A 427     -43.891-103.445 266.512  1.00191.34           C  
ANISOU 2510  CG  ASP A 427    26730  17294  28676   2026  -3304  -2839       C  
ATOM   2511  OD1 ASP A 427     -45.010-103.714 266.996  1.00193.43           O  
ANISOU 2511  OD1 ASP A 427    27239  17974  28280   2581  -2728  -2961       O  
ATOM   2512  OD2 ASP A 427     -43.260-102.404 266.792  1.00196.99           O  
ANISOU 2512  OD2 ASP A 427    27815  17322  29709   1994  -4126  -3125       O  
ATOM   2513  N   GLY A 428     -43.598-106.733 263.528  1.00154.25           N  
ANISOU 2513  N   GLY A 428    19868  14032  24707    741  -1673  -1380       N  
ATOM   2514  CA  GLY A 428     -43.087-107.585 262.471  1.00145.72           C  
ANISOU 2514  CA  GLY A 428    18168  13221  23977    316  -1416   -982       C  
ATOM   2515  C   GLY A 428     -41.734-107.110 261.970  1.00146.35           C  
ANISOU 2515  C   GLY A 428    17974  12958  24673    -82  -1939   -755       C  
ATOM   2516  O   GLY A 428     -41.468-105.911 261.868  1.00154.65           O  
ANISOU 2516  O   GLY A 428    19111  13556  26092   -139  -2405   -783       O  
ATOM   2517  N   LEU A 429     -40.868-108.071 261.657  1.00139.33           N  
ANISOU 2517  N   LEU A 429    16723  12276  23941   -347  -1864   -481       N  
ATOM   2518  CA  LEU A 429     -39.556-107.757 261.106  1.00137.39           C  
ANISOU 2518  CA  LEU A 429    16084  11814  24305   -706  -2260   -122       C  
ATOM   2519  C   LEU A 429     -39.681-107.484 259.613  1.00130.99           C  
ANISOU 2519  C   LEU A 429    14733  11192  23846   -852  -1934    263       C  
ATOM   2520  O   LEU A 429     -40.342-108.231 258.886  1.00127.73           O  
ANISOU 2520  O   LEU A 429    14116  11223  23191   -774  -1356    318       O  
ATOM   2521  CB  LEU A 429     -38.577-108.902 261.363  1.00136.98           C  
ANISOU 2521  CB  LEU A 429    15844  11949  24255   -847  -2262     57       C  
ATOM   2522  CG  LEU A 429     -37.138-108.685 260.889  1.00137.11           C  
ANISOU 2522  CG  LEU A 429    15384  11801  24910  -1182  -2645    521       C  
ATOM   2523  CD1 LEU A 429     -36.571-107.398 261.463  1.00138.68           C  
ANISOU 2523  CD1 LEU A 429    15775  11386  25529  -1329  -3464    474       C  
ATOM   2524  CD2 LEU A 429     -36.270-109.871 261.274  1.00140.46           C  
ANISOU 2524  CD2 LEU A 429    15671  12427  25270  -1238  -2613    666       C  
ATOM   2525  N   ARG A 430     -39.052-106.405 259.156  1.00132.27           N  
ANISOU 2525  N   ARG A 430    14663  11005  24590  -1057  -2343    550       N  
ATOM   2526  CA  ARG A 430     -39.200-105.940 257.783  1.00130.57           C  
ANISOU 2526  CA  ARG A 430    13957  10959  24694  -1143  -2068    967       C  
ATOM   2527  C   ARG A 430     -37.818-105.729 257.185  1.00132.84           C  
ANISOU 2527  C   ARG A 430    13679  11171  25622  -1445  -2328   1582       C  
ATOM   2528  O   ARG A 430     -37.034-104.925 257.700  1.00134.49           O  
ANISOU 2528  O   ARG A 430    13904  10852  26343  -1657  -2993   1705       O  
ATOM   2529  CB  ARG A 430     -40.023-104.651 257.743  1.00131.81           C  
ANISOU 2529  CB  ARG A 430    14340  10763  24979  -1034  -2242    823       C  
ATOM   2530  CG  ARG A 430     -41.333-104.764 258.509  1.00133.45           C  
ANISOU 2530  CG  ARG A 430    15109  11025  24572   -670  -2019    258       C  
ATOM   2531  CD  ARG A 430     -41.900-103.407 258.873  1.00140.97           C  
ANISOU 2531  CD  ARG A 430    16435  11464  25664   -495  -2374     23       C  
ATOM   2532  NE  ARG A 430     -42.909-102.958 257.920  1.00140.66           N  
ANISOU 2532  NE  ARG A 430    16184  11629  25631   -370  -1959    171       N  
ATOM   2533  CZ  ARG A 430     -44.206-103.223 258.031  1.00136.67           C  
ANISOU 2533  CZ  ARG A 430    15873  11434  24622    -42  -1491    -82       C  
ATOM   2534  NH1 ARG A 430     -44.653-103.940 259.054  1.00132.75           N  
ANISOU 2534  NH1 ARG A 430    15769  11094  23575    208  -1336   -455       N  
ATOM   2535  NH2 ARG A 430     -45.057-102.772 257.120  1.00136.56           N  
ANISOU 2535  NH2 ARG A 430    15616  11598  24673     45  -1177    105       N  
ATOM   2536  N   ILE A 431     -37.522-106.446 256.102  1.00134.95           N  
ANISOU 2536  N   ILE A 431    13444  11963  25867  -1438  -1829   1985       N  
ATOM   2537  CA  ILE A 431     -36.204-106.431 255.478  1.00142.54           C  
ANISOU 2537  CA  ILE A 431    13791  13010  27358  -1628  -1923   2666       C  
ATOM   2538  C   ILE A 431     -36.349-106.073 254.003  1.00147.12           C  
ANISOU 2538  C   ILE A 431    13861  13967  28072  -1553  -1502   3188       C  
ATOM   2539  O   ILE A 431     -37.317-106.476 253.349  1.00138.03           O  
ANISOU 2539  O   ILE A 431    12796  13220  26428  -1319   -996   2979       O  
ATOM   2540  CB  ILE A 431     -35.490-107.792 255.647  1.00139.88           C  
ANISOU 2540  CB  ILE A 431    13339  13016  26791  -1571  -1695   2701       C  
ATOM   2541  CG1 ILE A 431     -35.368-108.153 257.129  1.00142.64           C  
ANISOU 2541  CG1 ILE A 431    14193  13038  26965  -1619  -2107   2227       C  
ATOM   2542  CG2 ILE A 431     -34.118-107.774 255.001  1.00137.74           C  
ANISOU 2542  CG2 ILE A 431    12381  12889  27065  -1697  -1735   3476       C  
ATOM   2543  CD1 ILE A 431     -34.561-107.157 257.938  1.00149.57           C  
ANISOU 2543  CD1 ILE A 431    15118  13301  28411  -1895  -2934   2343       C  
ATOM   2544  N   ASP A 432     -35.390-105.305 253.485  1.00161.67           N  
ANISOU 2544  N   ASP A 432    15150  15681  30598  -1750  -1742   3912       N  
ATOM   2545  CA  ASP A 432     -35.311-104.963 252.072  1.00169.98           C  
ANISOU 2545  CA  ASP A 432    15625  17157  31801  -1645  -1334   4577       C  
ATOM   2546  C   ASP A 432     -34.031-105.530 251.475  1.00175.13           C  
ANISOU 2546  C   ASP A 432    15639  18224  32677  -1609  -1113   5290       C  
ATOM   2547  O   ASP A 432     -33.010-105.644 252.158  1.00174.05           O  
ANISOU 2547  O   ASP A 432    15453  17863  32817  -1745  -1504   5441       O  
ATOM   2548  CB  ASP A 432     -35.342-103.449 251.844  1.00177.88           C  
ANISOU 2548  CB  ASP A 432    16429  17697  33460  -1845  -1737   4991       C  
ATOM   2549  CG  ASP A 432     -34.494-102.686 252.846  1.00185.95           C  
ANISOU 2549  CG  ASP A 432    17600  18113  34940  -2052  -2560   4992       C  
ATOM   2550  OD1 ASP A 432     -34.027-103.307 253.824  1.00185.14           O  
ANISOU 2550  OD1 ASP A 432    17748  17853  34743  -2141  -2833   4654       O  
ATOM   2551  OD2 ASP A 432     -34.311-101.463 252.664  1.00191.94           O  
ANISOU 2551  OD2 ASP A 432    18212  18564  36153  -2118  -2962   5321       O  
ATOM   2552  N   GLY A 433     -34.091-105.866 250.191  1.00183.38           N  
ANISOU 2552  N   GLY A 433    16314  19940  33421  -1290   -491   5683       N  
ATOM   2553  CA  GLY A 433     -32.921-106.406 249.519  1.00189.50           C  
ANISOU 2553  CA  GLY A 433    16676  21202  34122  -1040   -190   6311       C  
ATOM   2554  C   GLY A 433     -32.564-107.772 250.061  1.00189.09           C  
ANISOU 2554  C   GLY A 433    16710  21320  33814   -952    -31   5957       C  
ATOM   2555  O   GLY A 433     -33.404-108.673 250.141  1.00185.08           O  
ANISOU 2555  O   GLY A 433    16673  20991  32657   -747    247   5249       O  
ATOM   2556  N   ASP A 434     -31.305-107.925 250.461  1.00190.02           N  
ANISOU 2556  N   ASP A 434    16634  21336  34229  -1019   -268   6366       N  
ATOM   2557  CA  ASP A 434     -30.841-109.197 250.995  1.00188.34           C  
ANISOU 2557  CA  ASP A 434    16455  21264  33841   -923   -141   6122       C  
ATOM   2558  C   ASP A 434     -30.696-109.122 252.507  1.00182.05           C  
ANISOU 2558  C   ASP A 434    15964  19824  33382  -1338   -815   5723       C  
ATOM   2559  O   ASP A 434     -30.105-108.160 253.030  1.00184.53           O  
ANISOU 2559  O   ASP A 434    16263  19678  34171  -1605  -1435   5993       O  
ATOM   2560  CB  ASP A 434     -29.507-109.597 250.369  1.00197.56           C  
ANISOU 2560  CB  ASP A 434    17203  22843  35017   -636    133   6868       C  
ATOM   2561  CG  ASP A 434     -29.641-109.982 248.902  1.00202.90           C  
ANISOU 2561  CG  ASP A 434    17708  24253  35130    -96    871   7136       C  
ATOM   2562  OD1 ASP A 434     -30.772-110.282 248.458  1.00200.77           O  
ANISOU 2562  OD1 ASP A 434    17655  24215  34411     97   1183   6617       O  
ATOM   2563  OD2 ASP A 434     -28.611-109.993 248.198  1.00209.46           O  
ANISOU 2563  OD2 ASP A 434    18204  25436  35944    160   1120   7869       O  
ATOM   2564  N   PRO A 435     -31.201-110.119 253.234  1.00173.92           N  
ANISOU 2564  N   PRO A 435    15485  18759  31836  -1248   -750   4984       N  
ATOM   2565  CA  PRO A 435     -31.036-110.145 254.691  1.00170.64           C  
ANISOU 2565  CA  PRO A 435    15461  17820  31554  -1533  -1355   4592       C  
ATOM   2566  C   PRO A 435     -29.654-110.580 255.141  1.00170.46           C  
ANISOU 2566  C   PRO A 435    15038  17779  31949  -1630  -1604   5071       C  
ATOM   2567  O   PRO A 435     -29.410-110.649 256.350  1.00170.82           O  
ANISOU 2567  O   PRO A 435    15389  17430  32085  -1844  -2145   4787       O  
ATOM   2568  CB  PRO A 435     -32.103-111.161 255.142  1.00168.39           C  
ANISOU 2568  CB  PRO A 435    15840  17630  30510  -1320  -1062   3761       C  
ATOM   2569  CG  PRO A 435     -32.784-111.666 253.873  1.00167.11           C  
ANISOU 2569  CG  PRO A 435    15614  17988  29890   -968   -377   3708       C  
ATOM   2570  CD  PRO A 435     -31.896-111.313 252.735  1.00170.47           C  
ANISOU 2570  CD  PRO A 435    15350  18767  30653   -846   -144   4511       C  
ATOM   2571  N   ARG A 436     -28.755-110.882 254.202  1.00171.11           N  
ANISOU 2571  N   ARG A 436    14462  18317  32235  -1422  -1210   5804       N  
ATOM   2572  CA  ARG A 436     -27.401-111.278 254.565  1.00173.70           C  
ANISOU 2572  CA  ARG A 436    14490  18671  32836  -1409  -1402   6301       C  
ATOM   2573  C   ARG A 436     -26.620-110.111 255.150  1.00175.41           C  
ANISOU 2573  C   ARG A 436    14642  18387  33617  -1749  -2197   6687       C  
ATOM   2574  O   ARG A 436     -25.762-110.311 256.016  1.00176.67           O  
ANISOU 2574  O   ARG A 436    14758  18322  34047  -1905  -2672   6817       O  
ATOM   2575  CB  ARG A 436     -26.687-111.851 253.340  1.00179.08           C  
ANISOU 2575  CB  ARG A 436    14723  19990  33327   -941   -705   6932       C  
ATOM   2576  CG  ARG A 436     -27.594-112.716 252.478  1.00178.57           C  
ANISOU 2576  CG  ARG A 436    14764  20429  32654   -499     39   6525       C  
ATOM   2577  CD  ARG A 436     -26.860-113.345 251.308  1.00185.31           C  
ANISOU 2577  CD  ARG A 436    15310  21922  33178     65    700   7049       C  
ATOM   2578  NE  ARG A 436     -27.790-114.027 250.412  1.00185.06           N  
ANISOU 2578  NE  ARG A 436    15462  22331  32522    542   1308   6597       N  
ATOM   2579  CZ  ARG A 436     -28.244-115.262 250.605  1.00184.12           C  
ANISOU 2579  CZ  ARG A 436    15759  22263  31935    822   1536   5929       C  
ATOM   2580  NH1 ARG A 436     -29.094-115.800 249.740  1.00181.45           N  
ANISOU 2580  NH1 ARG A 436    15781  22229  30930   1235   1964   5450       N  
ATOM   2581  NH2 ARG A 436     -27.851-115.959 251.661  1.00185.50           N  
ANISOU 2581  NH2 ARG A 436    16112  22134  32233    678   1273   5708       N  
ATOM   2582  N   ALA A 437     -26.897-108.892 254.688  1.00177.49           N  
ANISOU 2582  N   ALA A 437    14884  18465  34091  -1843  -2385   6883       N  
ATOM   2583  CA  ALA A 437     -26.340-107.707 255.322  1.00182.91           C  
ANISOU 2583  CA  ALA A 437    15569  18587  35339  -2147  -3243   7106       C  
ATOM   2584  C   ALA A 437     -27.106-107.316 256.576  1.00184.38           C  
ANISOU 2584  C   ALA A 437    16395  18216  35446  -2413  -3902   6242       C  
ATOM   2585  O   ALA A 437     -26.550-106.625 257.437  1.00190.84           O  
ANISOU 2585  O   ALA A 437    17322  18552  36635  -2641  -4726   6246       O  
ATOM   2586  CB  ALA A 437     -26.327-106.536 254.338  1.00184.38           C  
ANISOU 2586  CB  ALA A 437    15458  18766  35831  -2108  -3211   7685       C  
ATOM   2587  N   ALA A 438     -28.362-107.747 256.698  1.00180.03           N  
ANISOU 2587  N   ALA A 438    16300  17712  34393  -2358  -3563   5513       N  
ATOM   2588  CA  ALA A 438     -29.197-107.447 257.853  1.00181.58           C  
ANISOU 2588  CA  ALA A 438    17209  17408  34376  -2515  -4064   4683       C  
ATOM   2589  C   ALA A 438     -29.253-108.603 258.845  1.00179.48           C  
ANISOU 2589  C   ALA A 438    17288  17124  33783  -2528  -4082   4210       C  
ATOM   2590  O   ALA A 438     -30.250-108.757 259.560  1.00176.52           O  
ANISOU 2590  O   ALA A 438    17585  16564  32919  -2457  -4108   3474       O  
ATOM   2591  CB  ALA A 438     -30.607-107.066 257.402  1.00179.54           C  
ANISOU 2591  CB  ALA A 438    17281  17130  33807  -2426  -3704   4240       C  
ATOM   2592  N   ARG A 439     -28.201-109.426 258.899  1.00182.45           N  
ANISOU 2592  N   ARG A 439    17258  17749  34313  -2509  -4018   4642       N  
ATOM   2593  CA  ARG A 439     -28.175-110.528 259.856  1.00182.66           C  
ANISOU 2593  CA  ARG A 439    17621  17802  33981  -2454  -4042   4243       C  
ATOM   2594  C   ARG A 439     -28.209-110.024 261.292  1.00184.47           C  
ANISOU 2594  C   ARG A 439    18442  17468  34181  -2650  -4926   3748       C  
ATOM   2595  O   ARG A 439     -28.780-110.685 262.168  1.00182.68           O  
ANISOU 2595  O   ARG A 439    18831  17284  33294  -2449  -4866   3145       O  
ATOM   2596  CB  ARG A 439     -26.935-111.397 259.636  1.00187.43           C  
ANISOU 2596  CB  ARG A 439    17596  18737  34881  -2406  -3874   4891       C  
ATOM   2597  CG  ARG A 439     -26.939-112.196 258.344  1.00189.20           C  
ANISOU 2597  CG  ARG A 439    17403  19590  34895  -2032  -2929   5225       C  
ATOM   2598  CD  ARG A 439     -25.795-113.202 258.321  1.00195.86           C  
ANISOU 2598  CD  ARG A 439    17765  20746  35905  -1871  -2740   5737       C  
ATOM   2599  NE  ARG A 439     -24.493-112.560 258.484  1.00209.45           N  
ANISOU 2599  NE  ARG A 439    19058  22306  38218  -2054  -3275   6453       N  
ATOM   2600  CZ  ARG A 439     -23.723-112.162 257.476  1.00217.61           C  
ANISOU 2600  CZ  ARG A 439    19611  23584  39486  -1897  -3001   7226       C  
ATOM   2601  NH1 ARG A 439     -22.553-111.586 257.718  1.00222.07           N  
ANISOU 2601  NH1 ARG A 439    19883  23932  40561  -2065  -3515   7874       N  
ATOM   2602  NH2 ARG A 439     -24.124-112.339 256.225  1.00218.95           N  
ANISOU 2602  NH2 ARG A 439    19613  24212  39367  -1563  -2223   7372       N  
ATOM   2603  N   ASP A 440     -27.609-108.861 261.552  1.00189.19           N  
ANISOU 2603  N   ASP A 440    18964  17668  35252  -2864  -5691   3962       N  
ATOM   2604  CA  ASP A 440     -27.599-108.316 262.906  1.00193.18           C  
ANISOU 2604  CA  ASP A 440    20090  17632  35676  -2983  -6614   3442       C  
ATOM   2605  C   ASP A 440     -29.007-107.945 263.357  1.00190.59           C  
ANISOU 2605  C   ASP A 440    20565  17021  34828  -2847  -6601   2606       C  
ATOM   2606  O   ASP A 440     -29.408-108.251 264.486  1.00190.97           O  
ANISOU 2606  O   ASP A 440    21301  16939  34320  -2684  -6863   1991       O  
ATOM   2607  CB  ASP A 440     -26.671-107.104 262.975  1.00201.99           C  
ANISOU 2607  CB  ASP A 440    20973  18410  37363  -3149  -7407   3853       C  
ATOM   2608  CG  ASP A 440     -25.262-107.422 262.512  1.00207.79           C  
ANISOU 2608  CG  ASP A 440    20919  19388  38645  -3229  -7393   4775       C  
ATOM   2609  OD1 ASP A 440     -24.853-108.597 262.616  1.00206.37           O  
ANISOU 2609  OD1 ASP A 440    20520  19538  38353  -3178  -7054   4944       O  
ATOM   2610  OD2 ASP A 440     -24.563-106.497 262.044  1.00214.44           O  
ANISOU 2610  OD2 ASP A 440    21358  20071  40050  -3318  -7714   5367       O  
ATOM   2611  N   ASP A 441     -29.773-107.285 262.485  1.00189.27           N  
ANISOU 2611  N   ASP A 441    20354  16901  34660  -2764  -6207   2597       N  
ATOM   2612  CA  ASP A 441     -31.145-106.932 262.834  1.00186.26           C  
ANISOU 2612  CA  ASP A 441    20697  16307  33768  -2552  -6098   1867       C  
ATOM   2613  C   ASP A 441     -32.030-108.167 262.941  1.00179.07           C  
ANISOU 2613  C   ASP A 441    20088  15978  31972  -2165  -5250   1495       C  
ATOM   2614  O   ASP A 441     -33.015-108.159 263.689  1.00181.05           O  
ANISOU 2614  O   ASP A 441    21022  16193  31576  -1873  -5196    870       O  
ATOM   2615  CB  ASP A 441     -31.717-105.957 261.805  1.00187.42           C  
ANISOU 2615  CB  ASP A 441    20640  16441  34130  -2537  -5843   2033       C  
ATOM   2616  CG  ASP A 441     -30.878-104.702 261.663  1.00196.74           C  
ANISOU 2616  CG  ASP A 441    21527  17344  35882  -2708  -6518   2436       C  
ATOM   2617  OD1 ASP A 441     -30.153-104.357 262.621  1.00204.14           O  
ANISOU 2617  OD1 ASP A 441    22677  17922  36966  -2810  -7343   2329       O  
ATOM   2618  OD2 ASP A 441     -30.944-104.060 260.594  1.00198.23           O  
ANISOU 2618  OD2 ASP A 441    21270  17654  36393  -2729  -6254   2881       O  
ATOM   2619  N   ILE A 442     -31.699-109.231 262.209  1.00170.74           N  
ANISOU 2619  N   ILE A 442    18529  15446  30898  -2131  -4599   1895       N  
ATOM   2620  CA  ILE A 442     -32.487-110.459 262.273  1.00161.94           C  
ANISOU 2620  CA  ILE A 442    17659  14801  29069  -1814  -3871   1588       C  
ATOM   2621  C   ILE A 442     -32.334-111.116 263.639  1.00163.16           C  
ANISOU 2621  C   ILE A 442    18281  14913  28798  -1696  -4163   1263       C  
ATOM   2622  O   ILE A 442     -33.322-111.370 264.339  1.00162.65           O  
ANISOU 2622  O   ILE A 442    18785  14920  28093  -1423  -3979    769       O  
ATOM   2623  CB  ILE A 442     -32.083-111.418 261.141  1.00157.34           C  
ANISOU 2623  CB  ILE A 442    16472  14707  28604  -1769  -3202   2058       C  
ATOM   2624  CG1 ILE A 442     -32.592-110.899 259.797  1.00151.03           C  
ANISOU 2624  CG1 ILE A 442    15355  14082  27949  -1744  -2765   2260       C  
ATOM   2625  CG2 ILE A 442     -32.612-112.816 261.411  1.00156.93           C  
ANISOU 2625  CG2 ILE A 442    16666  15003  27958  -1505  -2660   1776       C  
ATOM   2626  CD1 ILE A 442     -32.246-111.796 258.638  1.00149.01           C  
ANISOU 2626  CD1 ILE A 442    14590  14331  27696  -1593  -2117   2657       C  
ATOM   2627  N   VAL A 443     -31.092-111.401 264.037  1.00163.84           N  
ANISOU 2627  N   VAL A 443    18095  14921  29236  -1876  -4608   1603       N  
ATOM   2628  CA  VAL A 443     -30.854-111.975 265.356  1.00162.74           C  
ANISOU 2628  CA  VAL A 443    18384  14750  28702  -1762  -4960   1348       C  
ATOM   2629  C   VAL A 443     -31.214-110.991 266.458  1.00166.09           C  
ANISOU 2629  C   VAL A 443    19507  14737  28862  -1693  -5694    813       C  
ATOM   2630  O   VAL A 443     -31.491-111.407 267.589  1.00168.14           O  
ANISOU 2630  O   VAL A 443    20321  15058  28505  -1433  -5830    443       O  
ATOM   2631  CB  VAL A 443     -29.391-112.439 265.494  1.00163.12           C  
ANISOU 2631  CB  VAL A 443    17927  14805  29245  -1979  -5328   1885       C  
ATOM   2632  CG1 VAL A 443     -29.049-113.440 264.402  1.00159.08           C  
ANISOU 2632  CG1 VAL A 443    16784  14741  28917  -1922  -4557   2375       C  
ATOM   2633  CG2 VAL A 443     -28.443-111.250 265.453  1.00168.23           C  
ANISOU 2633  CG2 VAL A 443    18265  14980  30677  -2364  -6200   2210       C  
ATOM   2634  N   GLY A 444     -31.219-109.691 266.158  1.00165.47           N  
ANISOU 2634  N   GLY A 444    19438  14215  29220  -1875  -6176    772       N  
ATOM   2635  CA  GLY A 444     -31.688-108.723 267.135  1.00169.19           C  
ANISOU 2635  CA  GLY A 444    20667  14228  29389  -1716  -6850    167       C  
ATOM   2636  C   GLY A 444     -33.184-108.820 267.359  1.00164.04           C  
ANISOU 2636  C   GLY A 444    20591  13815  27922  -1248  -6231   -364       C  
ATOM   2637  O   GLY A 444     -33.650-108.903 268.499  1.00165.52           O  
ANISOU 2637  O   GLY A 444    21467  14014  27408   -875  -6402   -850       O  
ATOM   2638  N   TRP A 445     -33.959-108.819 266.271  1.00160.31           N  
ANISOU 2638  N   TRP A 445    19818  13576  27515  -1230  -5495   -231       N  
ATOM   2639  CA  TRP A 445     -35.403-108.980 266.396  1.00157.07           C  
ANISOU 2639  CA  TRP A 445    19827  13438  26413   -814  -4862   -624       C  
ATOM   2640  C   TRP A 445     -35.767-110.353 266.943  1.00153.16           C  
ANISOU 2640  C   TRP A 445    19449  13450  25297   -561  -4305   -653       C  
ATOM   2641  O   TRP A 445     -36.778-110.496 267.640  1.00152.71           O  
ANISOU 2641  O   TRP A 445    19887  13571  24566   -150  -4025   -995       O  
ATOM   2642  CB  TRP A 445     -36.080-108.754 265.043  1.00153.27           C  
ANISOU 2642  CB  TRP A 445    18923  13119  26192   -894  -4247   -412       C  
ATOM   2643  CG  TRP A 445     -37.566-108.935 265.089  1.00153.29           C  
ANISOU 2643  CG  TRP A 445    19245  13416  25583   -510  -3606   -725       C  
ATOM   2644  CD1 TRP A 445     -38.500-107.978 265.354  1.00157.29           C  
ANISOU 2644  CD1 TRP A 445    20199  13716  25847   -223  -3676  -1097       C  
ATOM   2645  CD2 TRP A 445     -38.290-110.153 264.871  1.00151.52           C  
ANISOU 2645  CD2 TRP A 445    18883  13722  24967   -364  -2825   -648       C  
ATOM   2646  NE1 TRP A 445     -39.761-108.522 265.312  1.00155.17           N  
ANISOU 2646  NE1 TRP A 445    20024  13874  25059     93  -2948  -1200       N  
ATOM   2647  CE2 TRP A 445     -39.659-109.856 265.018  1.00151.58           C  
ANISOU 2647  CE2 TRP A 445    19207  13852  24536    -21  -2451   -923       C  
ATOM   2648  CE3 TRP A 445     -37.913-111.464 264.566  1.00151.00           C  
ANISOU 2648  CE3 TRP A 445    18452  14000  24923   -481  -2438   -360       C  
ATOM   2649  CZ2 TRP A 445     -40.652-110.821 264.871  1.00149.27           C  
ANISOU 2649  CZ2 TRP A 445    18820  14009  23888    146  -1743   -865       C  
ATOM   2650  CZ3 TRP A 445     -38.901-112.421 264.419  1.00149.34           C  
ANISOU 2650  CZ3 TRP A 445    18216  14174  24354   -309  -1771   -372       C  
ATOM   2651  CH2 TRP A 445     -40.254-112.095 264.570  1.00148.91           C  
ANISOU 2651  CH2 TRP A 445    18425  14229  23924    -29  -1448   -597       C  
ATOM   2652  N   ALA A 446     -34.959-111.370 266.643  1.00150.25           N  
ANISOU 2652  N   ALA A 446    18608  13314  25166   -770  -4127   -248       N  
ATOM   2653  CA  ALA A 446     -35.246-112.713 267.131  1.00147.34           C  
ANISOU 2653  CA  ALA A 446    18312  13356  24316   -561  -3636   -218       C  
ATOM   2654  C   ALA A 446     -34.906-112.855 268.611  1.00148.88           C  
ANISOU 2654  C   ALA A 446    19024  13494  24048   -346  -4139   -430       C  
ATOM   2655  O   ALA A 446     -35.613-113.551 269.348  1.00147.69           O  
ANISOU 2655  O   ALA A 446    19199  13645  23271     -3  -3773   -553       O  
ATOM   2656  CB  ALA A 446     -34.487-113.744 266.297  1.00145.74           C  
ANISOU 2656  CB  ALA A 446    17472  13375  24526   -794  -3293    257       C  
ATOM   2657  N   HIS A 447     -33.831-112.206 269.064  1.00153.99           N  
ANISOU 2657  N   HIS A 447    19736  13771  25005   -535  -5002   -434       N  
ATOM   2658  CA  HIS A 447     -33.535-112.197 270.492  1.00161.90           C  
ANISOU 2658  CA  HIS A 447    21319  14698  25498   -288  -5602   -711       C  
ATOM   2659  C   HIS A 447     -34.504-111.304 271.256  1.00166.05           C  
ANISOU 2659  C   HIS A 447    22627  15083  25382    161  -5795  -1306       C  
ATOM   2660  O   HIS A 447     -34.785-111.562 272.432  1.00168.61           O  
ANISOU 2660  O   HIS A 447    23529  15586  24949    600  -5899  -1573       O  
ATOM   2661  CB  HIS A 447     -32.093-111.748 270.732  1.00169.90           C  
ANISOU 2661  CB  HIS A 447    22154  15314  27086   -651  -6574   -539       C  
ATOM   2662  CG  HIS A 447     -31.757-111.541 272.177  1.00178.38           C  
ANISOU 2662  CG  HIS A 447    23895  16240  27642   -401  -7377   -901       C  
ATOM   2663  ND1 HIS A 447     -31.796-110.303 272.780  1.00184.31           N  
ANISOU 2663  ND1 HIS A 447    25258  16492  28279   -285  -8239  -1415       N  
ATOM   2664  CD2 HIS A 447     -31.379-112.416 273.139  1.00181.45           C  
ANISOU 2664  CD2 HIS A 447    24469  16909  27565   -206  -7482   -836       C  
ATOM   2665  CE1 HIS A 447     -31.455-110.423 274.051  1.00190.83           C  
ANISOU 2665  CE1 HIS A 447    26650  17318  28538     -8  -8861  -1692       C  
ATOM   2666  NE2 HIS A 447     -31.197-111.695 274.294  1.00189.35           N  
ANISOU 2666  NE2 HIS A 447    26196  17627  28122     40  -8399  -1317       N  
ATOM   2667  N   ASP A 448     -35.025-110.259 270.610  1.00166.75           N  
ANISOU 2667  N   ASP A 448    22749  14878  25730    118  -5820  -1495       N  
ATOM   2668  CA  ASP A 448     -35.981-109.379 271.276  1.00170.35           C  
ANISOU 2668  CA  ASP A 448    23953  15185  25587    617  -5960  -2067       C  
ATOM   2669  C   ASP A 448     -37.338-110.055 271.426  1.00164.12           C  
ANISOU 2669  C   ASP A 448    23313  14961  24084   1092  -4986  -2102       C  
ATOM   2670  O   ASP A 448     -37.963-109.984 272.491  1.00166.68           O  
ANISOU 2670  O   ASP A 448    24286  15453  23592   1678  -4970  -2442       O  
ATOM   2671  CB  ASP A 448     -36.114-108.064 270.507  1.00174.96           C  
ANISOU 2671  CB  ASP A 448    24487  15247  26742    424  -6282  -2203       C  
ATOM   2672  CG  ASP A 448     -34.886-107.185 270.638  1.00185.82           C  
ANISOU 2672  CG  ASP A 448    25861  15954  28788     33  -7422  -2225       C  
ATOM   2673  OD1 ASP A 448     -34.166-107.311 271.650  1.00193.09           O  
ANISOU 2673  OD1 ASP A 448    27134  16747  29483     94  -8122  -2394       O  
ATOM   2674  OD2 ASP A 448     -34.642-106.365 269.727  1.00187.19           O  
ANISOU 2674  OD2 ASP A 448    25653  15726  29743   -343  -7646  -2029       O  
ATOM   2675  N   VAL A 449     -37.817-110.713 270.366  1.00155.50           N  
ANISOU 2675  N   VAL A 449    21617  14177  23289    874  -4185  -1726       N  
ATOM   2676  CA  VAL A 449     -39.077-111.441 270.464  1.00149.76           C  
ANISOU 2676  CA  VAL A 449    20917  13958  22026   1237  -3311  -1657       C  
ATOM   2677  C   VAL A 449     -38.950-112.621 271.416  1.00150.58           C  
ANISOU 2677  C   VAL A 449    21132  14451  21630   1454  -3114  -1481       C  
ATOM   2678  O   VAL A 449     -39.954-113.077 271.975  1.00149.25           O  
ANISOU 2678  O   VAL A 449    21166  14681  20863   1896  -2564  -1448       O  
ATOM   2679  CB  VAL A 449     -39.553-111.891 269.067  1.00139.91           C  
ANISOU 2679  CB  VAL A 449    19004  12886  21269    909  -2637  -1319       C  
ATOM   2680  CG1 VAL A 449     -38.699-113.035 268.541  1.00137.64           C  
ANISOU 2680  CG1 VAL A 449    18164  12734  21398    512  -2492   -905       C  
ATOM   2681  CG2 VAL A 449     -41.026-112.276 269.100  1.00135.06           C  
ANISOU 2681  CG2 VAL A 449    18431  12674  20210   1266  -1869  -1289       C  
ATOM   2682  N   ARG A 450     -37.731-113.119 271.629  1.00155.10           N  
ANISOU 2682  N   ARG A 450    21537  14932  22461   1167  -3548  -1297       N  
ATOM   2683  CA  ARG A 450     -37.506-114.129 272.654  1.00163.66           C  
ANISOU 2683  CA  ARG A 450    22784  16343  23058   1403  -3482  -1131       C  
ATOM   2684  C   ARG A 450     -37.498-113.509 274.046  1.00180.88           C  
ANISOU 2684  C   ARG A 450    25764  18494  24469   1929  -4045  -1545       C  
ATOM   2685  O   ARG A 450     -37.986-114.119 275.004  1.00184.30           O  
ANISOU 2685  O   ARG A 450    26505  19347  24172   2411  -3735  -1477       O  
ATOM   2686  CB  ARG A 450     -36.191-114.860 272.385  1.00160.08           C  
ANISOU 2686  CB  ARG A 450    21859  15805  23157    951  -3759   -772       C  
ATOM   2687  CG  ARG A 450     -35.774-115.811 273.488  1.00160.55           C  
ANISOU 2687  CG  ARG A 450    22092  16138  22771   1171  -3835   -583       C  
ATOM   2688  CD  ARG A 450     -34.402-116.389 273.213  1.00157.71           C  
ANISOU 2688  CD  ARG A 450    21261  15651  23011    746  -4183   -232       C  
ATOM   2689  NE  ARG A 450     -33.390-115.349 273.055  1.00159.73           N  
ANISOU 2689  NE  ARG A 450    21498  15456  23735    440  -5056   -380       N  
ATOM   2690  N   GLY A 451     -36.957-112.296 274.172  1.00192.41           N  
ANISOU 2690  N   GLY A 451    27574  19454  26079   1873  -4894  -1962       N  
ATOM   2691  CA  GLY A 451     -36.911-111.649 275.474  1.00203.32           C  
ANISOU 2691  CA  GLY A 451    29810  20740  26702   2415  -5554  -2460       C  
ATOM   2692  C   GLY A 451     -38.287-111.266 275.984  1.00208.43           C  
ANISOU 2692  C   GLY A 451    31014  21669  26510   3155  -5050  -2769       C  
ATOM   2693  O   GLY A 451     -38.619-111.501 277.149  1.00217.96           O  
ANISOU 2693  O   GLY A 451    32785  23240  26788   3806  -5003  -2902       O  
ATOM   2694  N   ALA A 452     -39.106-110.671 275.121  1.00200.35           N  
ANISOU 2694  N   ALA A 452    29821  20523  25780   3112  -4645  -2841       N  
ATOM   2695  CA  ALA A 452     -40.464-110.286 275.490  1.00199.41           C  
ANISOU 2695  CA  ALA A 452    30128  20690  24950   3821  -4091  -3057       C  
ATOM   2696  C   ALA A 452     -41.338-111.534 275.522  1.00193.25           C  
ANISOU 2696  C   ALA A 452    28945  20615  23866   3997  -3034  -2502       C  
ATOM   2697  O   ALA A 452     -41.559-112.171 274.487  1.00187.51           O  
ANISOU 2697  O   ALA A 452    27494  19985  23766   3503  -2486  -2073       O  
ATOM   2698  CB  ALA A 452     -41.011-109.251 274.512  1.00193.88           C  
ANISOU 2698  CB  ALA A 452    29310  19610  24747   3679  -4036  -3253       C  
ATOM   2699  N   ILE A 453     -41.828-111.887 276.707  1.00200.09           N  
ANISOU 2699  N   ILE A 453    30278  21965  23782   4717  -2778  -2486       N  
ATOM   2700  CA  ILE A 453     -42.663-113.070 276.873  1.00199.73           C  
ANISOU 2700  CA  ILE A 453    29840  22580  23470   4913  -1818  -1866       C  
ATOM   2701  C   ILE A 453     -43.476-112.961 278.157  1.00207.62           C  
ANISOU 2701  C   ILE A 453    31470  24108  23310   5924  -1504  -1923       C  
ATOM   2702  O   ILE A 453     -43.677-113.951 278.862  1.00153.35           O  
ANISOU 2702  O   ILE A 453    24504  17781  15982   6211  -1052  -1434       O  
ATOM   2703  CB  ILE A 453     -41.818-114.357 276.873  1.00198.56           C  
ANISOU 2703  CB  ILE A 453    29220  22552  23671   4427  -1811  -1377       C  
ATOM   2704  N   ARG A 458     -38.135-124.395 282.018  1.00177.35           N  
ANISOU 2704  N   ARG A 458    31146  15366  20872  -3078  -6384   4226       N  
ATOM   2705  CA  ARG A 458     -37.471-125.481 282.728  1.00172.80           C  
ANISOU 2705  CA  ARG A 458    29913  15420  20325  -3245  -5786   4040       C  
ATOM   2706  C   ARG A 458     -38.311-125.959 283.909  1.00173.57           C  
ANISOU 2706  C   ARG A 458    29421  15460  21066  -2568  -5586   3587       C  
ATOM   2707  O   ARG A 458     -39.506-125.675 283.986  1.00177.01           O  
ANISOU 2707  O   ARG A 458    29885  15439  21931  -1946  -5932   3423       O  
ATOM   2708  CB  ARG A 458     -36.088-125.039 283.209  1.00172.25           C  
ANISOU 2708  CB  ARG A 458    30090  15500  19857  -3972  -5472   4175       C  
ATOM   2709  N   MET A 459     -37.680-126.687 284.828  1.00168.45           N  
ANISOU 2709  N   MET A 459    28242  15292  20470  -2697  -5035   3369       N  
ATOM   2710  CA  MET A 459     -38.377-127.221 285.988  1.00167.54           C  
ANISOU 2710  CA  MET A 459    27563  15192  20902  -2139  -4780   2953       C  
ATOM   2711  C   MET A 459     -37.400-127.346 287.147  1.00165.83           C  
ANISOU 2711  C   MET A 459    27158  15236  20612  -2449  -4296   2833       C  
ATOM   2712  O   MET A 459     -36.180-127.352 286.961  1.00164.81           O  
ANISOU 2712  O   MET A 459    27151  15447  20022  -3064  -4092   3016       O  
ATOM   2713  CB  MET A 459     -39.019-128.580 285.681  1.00163.70           C  
ANISOU 2713  CB  MET A 459    26372  15183  20644  -1761  -4602   2735       C  
ATOM   2714  N   ASP A 460     -37.953-127.440 288.354  1.00168.18           N  
ANISOU 2714  N   ASP A 460    27148  15394  21359  -2019  -4118   2498       N  
ATOM   2715  CA  ASP A 460     -37.149-127.647 289.556  1.00172.06           C  
ANISOU 2715  CA  ASP A 460    27408  16143  21825  -2220  -3657   2339       C  
ATOM   2716  C   ASP A 460     -36.562-129.050 289.507  1.00174.37           C  
ANISOU 2716  C   ASP A 460    27103  17187  21963  -2368  -3214   2263       C  
ATOM   2717  O   ASP A 460     -37.242-130.032 289.813  1.00170.06           O  
ANISOU 2717  O   ASP A 460    26016  16861  21737  -1954  -3024   2019       O  
ATOM   2718  CB  ASP A 460     -37.994-127.447 290.809  1.00175.66           C  
ANISOU 2718  CB  ASP A 460    27669  16283  22793  -1698  -3589   1989       C  
ATOM   2719  CG  ASP A 460     -38.447-126.011 290.985  1.00186.34           C  
ANISOU 2719  CG  ASP A 460    29613  16890  24298  -1560  -4024   2017       C  
ATOM   2720  OD1 ASP A 460     -37.829-125.113 290.376  1.00194.37           O  
ANISOU 2720  OD1 ASP A 460    31245  17637  24970  -1987  -4295   2336       O  
ATOM   2721  OD2 ASP A 460     -39.417-125.780 291.739  1.00187.67           O  
ANISOU 2721  OD2 ASP A 460    29637  16745  24925  -1037  -4098   1706       O  
ATOM   2722  N   ILE A 461     -35.289-129.152 289.116  1.00180.68           N  
ANISOU 2722  N   ILE A 461    27999  18386  22265  -2969  -3054   2453       N  
ATOM   2723  CA  ILE A 461     -34.681-130.467 288.949  1.00180.75           C  
ANISOU 2723  CA  ILE A 461    27464  19112  22102  -3107  -2695   2369       C  
ATOM   2724  C   ILE A 461     -34.529-131.170 290.291  1.00180.70           C  
ANISOU 2724  C   ILE A 461    26995  19342  22320  -2901  -2268   2066       C  
ATOM   2725  O   ILE A 461     -34.638-132.400 290.369  1.00180.90           O  
ANISOU 2725  O   ILE A 461    26494  19789  22451  -2708  -2022   1906       O  
ATOM   2726  CB  ILE A 461     -33.332-130.351 288.216  1.00181.78           C  
ANISOU 2726  CB  ILE A 461    27795  19644  21631  -3810  -2639   2592       C  
ATOM   2727  CG1 ILE A 461     -32.339-129.520 289.029  1.00184.77           C  
ANISOU 2727  CG1 ILE A 461    28476  19937  21793  -4227  -2496   2601       C  
ATOM   2728  CG2 ILE A 461     -33.530-129.749 286.832  1.00184.24           C  
ANISOU 2728  CG2 ILE A 461    28569  19750  21683  -4028  -3053   2911       C  
ATOM   2729  CD1 ILE A 461     -30.919-129.608 288.524  1.00185.26           C  
ANISOU 2729  CD1 ILE A 461    28577  20536  21278  -4923  -2329   2707       C  
ATOM   2730  N   GLU A 462     -34.286-130.415 291.366  1.00177.91           N  
ANISOU 2730  N   GLU A 462    26847  18711  22038  -2936  -2186   1983       N  
ATOM   2731  CA  GLU A 462     -34.204-131.031 292.686  1.00170.09           C  
ANISOU 2731  CA  GLU A 462    25458  17917  21251  -2721  -1801   1700       C  
ATOM   2732  C   GLU A 462     -35.532-131.667 293.072  1.00164.59           C  
ANISOU 2732  C   GLU A 462    24390  17091  21055  -2110  -1764   1474       C  
ATOM   2733  O   GLU A 462     -35.561-132.751 293.665  1.00162.98           O  
ANISOU 2733  O   GLU A 462    23722  17237  20968  -1937  -1434   1284       O  
ATOM   2734  CB  GLU A 462     -33.774-130.002 293.730  1.00173.20           C  
ANISOU 2734  CB  GLU A 462    26167  18008  21633  -2859  -1756   1643       C  
ATOM   2735  CG  GLU A 462     -32.270-129.781 293.802  1.00175.02           C  
ANISOU 2735  CG  GLU A 462    26539  18575  21384  -3459  -1587   1729       C  
ATOM   2736  CD  GLU A 462     -31.721-129.086 292.571  1.00180.15           C  
ANISOU 2736  CD  GLU A 462    27640  19172  21639  -3966  -1860   2037       C  
ATOM   2737  OE1 GLU A 462     -32.435-128.237 291.999  1.00183.36           O  
ANISOU 2737  OE1 GLU A 462    28471  19043  22153  -3878  -2241   2208       O  
ATOM   2738  OE2 GLU A 462     -30.576-129.392 292.175  1.00180.42           O  
ANISOU 2738  OE2 GLU A 462    27608  19705  21240  -4455  -1702   2096       O  
ATOM   2739  N   LEU A 463     -36.645-131.008 292.742  1.00162.65           N  
ANISOU 2739  N   LEU A 463    24351  16345  21102  -1782  -2110   1475       N  
ATOM   2740  CA  LEU A 463     -37.946-131.643 292.909  1.00159.13           C  
ANISOU 2740  CA  LEU A 463    23518  15833  21113  -1231  -2096   1235       C  
ATOM   2741  C   LEU A 463     -38.178-132.708 291.846  1.00159.10           C  
ANISOU 2741  C   LEU A 463    23195  16190  21068  -1182  -2107   1292       C  
ATOM   2742  O   LEU A 463     -38.856-133.707 292.109  1.00162.13           O  
ANISOU 2742  O   LEU A 463    23106  16763  21732   -860  -1907   1075       O  
ATOM   2743  CB  LEU A 463     -39.059-130.596 292.865  1.00163.13           C  
ANISOU 2743  CB  LEU A 463    24317  15717  21949   -866  -2495   1162       C  
ATOM   2744  CG  LEU A 463     -38.946-129.444 293.866  1.00167.92           C  
ANISOU 2744  CG  LEU A 463    25262  15900  22640   -868  -2548   1076       C  
ATOM   2745  CD1 LEU A 463     -40.169-128.543 293.792  1.00172.47           C  
ANISOU 2745  CD1 LEU A 463    26056  15881  23594   -415  -2973    936       C  
ATOM   2746  CD2 LEU A 463     -38.745-129.971 295.280  1.00164.84           C  
ANISOU 2746  CD2 LEU A 463    24507  15757  22368   -797  -2080    812       C  
ATOM   2747  N   ALA A 464     -37.618-132.517 290.649  1.00157.18           N  
ANISOU 2747  N   ALA A 464    23203  16054  20463  -1522  -2330   1573       N  
ATOM   2748  CA  ALA A 464     -37.735-133.531 289.607  1.00154.05           C  
ANISOU 2748  CA  ALA A 464    22495  16048  19988  -1509  -2338   1618       C  
ATOM   2749  C   ALA A 464     -36.872-134.747 289.921  1.00149.05           C  
ANISOU 2749  C   ALA A 464    21427  16020  19183  -1698  -1919   1532       C  
ATOM   2750  O   ALA A 464     -37.304-135.888 289.721  1.00149.55           O  
ANISOU 2750  O   ALA A 464    21040  16365  19416  -1472  -1782   1394       O  
ATOM   2751  CB  ALA A 464     -37.356-132.938 288.250  1.00156.72           C  
ANISOU 2751  CB  ALA A 464    23249  16349  19949  -1846  -2696   1939       C  
ATOM   2752  N   LYS A 465     -35.650-134.524 290.411  1.00145.49           N  
ANISOU 2752  N   LYS A 465    21108  15770  18402  -2103  -1728   1592       N  
ATOM   2753  CA  LYS A 465     -34.806-135.648 290.805  1.00141.73           C  
ANISOU 2753  CA  LYS A 465    20233  15849  17771  -2236  -1363   1471       C  
ATOM   2754  C   LYS A 465     -35.358-136.341 292.043  1.00134.99           C  
ANISOU 2754  C   LYS A 465    19035  14968  17285  -1849  -1067   1208       C  
ATOM   2755  O   LYS A 465     -35.246-137.566 292.175  1.00136.14           O  
ANISOU 2755  O   LYS A 465    18775  15484  17468  -1752   -835   1081       O  
ATOM   2756  CB  LYS A 465     -33.372-135.180 291.055  1.00147.57           C  
ANISOU 2756  CB  LYS A 465    21189  16817  18066  -2749  -1251   1554       C  
ATOM   2757  CG  LYS A 465     -32.429-136.305 291.453  1.00152.34           C  
ANISOU 2757  CG  LYS A 465    21391  18004  18487  -2864   -921   1398       C  
ATOM   2758  CD  LYS A 465     -31.265-135.799 292.285  1.00158.77           C  
ANISOU 2758  CD  LYS A 465    22362  18943  19020  -3200   -751   1356       C  
ATOM   2759  CE  LYS A 465     -30.462-136.959 292.854  1.00156.88           C  
ANISOU 2759  CE  LYS A 465    21712  19233  18663  -3193   -449   1150       C  
ATOM   2760  NZ  LYS A 465     -29.392-136.495 293.780  1.00158.74           N  
ANISOU 2760  NZ  LYS A 465    22065  19592  18655  -3456   -284   1060       N  
ATOM   2761  N   THR A 466     -35.949-135.573 292.964  1.00128.61           N  
ANISOU 2761  N   THR A 466    18400  13726  16739  -1637  -1077   1116       N  
ATOM   2762  CA  THR A 466     -36.553-136.175 294.150  1.00124.08           C  
ANISOU 2762  CA  THR A 466    17521  13126  16499  -1294   -790    860       C  
ATOM   2763  C   THR A 466     -37.613-137.195 293.763  1.00122.98           C  
ANISOU 2763  C   THR A 466    16988  13062  16678   -943   -759    730       C  
ATOM   2764  O   THR A 466     -37.660-138.295 294.326  1.00121.69           O  
ANISOU 2764  O   THR A 466    16474  13151  16613   -827   -458    581       O  
ATOM   2765  CB  THR A 466     -37.155-135.094 295.048  1.00124.70           C  
ANISOU 2765  CB  THR A 466    17840  12718  16821  -1106   -857    754       C  
ATOM   2766  OG1 THR A 466     -36.141-134.148 295.406  1.00120.63           O  
ANISOU 2766  OG1 THR A 466    17695  12128  16011  -1454   -883    867       O  
ATOM   2767  CG2 THR A 466     -37.729-135.713 296.314  1.00127.89           C  
ANISOU 2767  CG2 THR A 466    17927  13146  17517   -806   -526    481       C  
ATOM   2768  N   LEU A 467     -38.469-136.852 292.798  1.00123.83           N  
ANISOU 2768  N   LEU A 467    17162  12944  16942   -776  -1079    778       N  
ATOM   2769  CA  LEU A 467     -39.417-137.829 292.274  1.00121.04           C  
ANISOU 2769  CA  LEU A 467    16420  12706  16864   -479  -1069    646       C  
ATOM   2770  C   LEU A 467     -38.685-139.026 291.683  1.00118.89           C  
ANISOU 2770  C   LEU A 467    15871  12942  16359   -672   -921    706       C  
ATOM   2771  O   LEU A 467     -39.045-140.179 291.944  1.00118.90           O  
ANISOU 2771  O   LEU A 467    15484  13145  16549   -499   -688    540       O  
ATOM   2772  CB  LEU A 467     -40.324-137.178 291.230  1.00119.75           C  
ANISOU 2772  CB  LEU A 467    16412  12241  16845   -288  -1492    699       C  
ATOM   2773  CG  LEU A 467     -41.170-136.005 291.726  1.00119.77           C  
ANISOU 2773  CG  LEU A 467    16672  11711  17123    -21  -1709    590       C  
ATOM   2774  CD1 LEU A 467     -42.161-135.574 290.658  1.00126.14           C  
ANISOU 2774  CD1 LEU A 467    17572  12254  18104    248  -2147    595       C  
ATOM   2775  CD2 LEU A 467     -41.885-136.365 293.021  1.00114.88           C  
ANISOU 2775  CD2 LEU A 467    15745  11034  16869    271  -1396    261       C  
ATOM   2776  N   VAL A 468     -37.644-138.768 290.888  1.00119.75           N  
ANISOU 2776  N   VAL A 468    16180  13269  16050  -1047  -1055    925       N  
ATOM   2777  CA  VAL A 468     -36.814-139.855 290.373  1.00119.77           C  
ANISOU 2777  CA  VAL A 468    15912  13797  15800  -1246   -921    939       C  
ATOM   2778  C   VAL A 468     -36.204-140.641 291.526  1.00116.56           C  
ANISOU 2778  C   VAL A 468    15295  13618  15374  -1256   -553    793       C  
ATOM   2779  O   VAL A 468     -36.230-141.877 291.541  1.00119.36           O  
ANISOU 2779  O   VAL A 468    15293  14248  15810  -1140   -381    670       O  
ATOM   2780  CB  VAL A 468     -35.729-139.307 289.428  1.00119.62           C  
ANISOU 2780  CB  VAL A 468    16158  13998  15295  -1701  -1106   1165       C  
ATOM   2781  CG1 VAL A 468     -34.799-140.425 288.985  1.00120.94           C  
ANISOU 2781  CG1 VAL A 468    16004  14755  15194  -1900   -958   1114       C  
ATOM   2782  CG2 VAL A 468     -36.363-138.631 288.225  1.00119.59           C  
ANISOU 2782  CG2 VAL A 468    16387  13770  15281  -1686  -1490   1333       C  
ATOM   2783  N   LEU A 469     -35.656-139.931 292.515  1.00110.14           N  
ANISOU 2783  N   LEU A 469    14721  12675  14451  -1384   -445    800       N  
ATOM   2784  CA  LEU A 469     -35.084-140.597 293.681  1.00111.75           C  
ANISOU 2784  CA  LEU A 469    14772  13070  14616  -1372   -120    664       C  
ATOM   2785  C   LEU A 469     -36.134-141.424 294.410  1.00116.65           C  
ANISOU 2785  C   LEU A 469    15120  13564  15638   -997     87    479       C  
ATOM   2786  O   LEU A 469     -35.918-142.608 294.695  1.00120.18           O  
ANISOU 2786  O   LEU A 469    15302  14271  16089   -935    290    383       O  
ATOM   2787  CB  LEU A 469     -34.462-139.567 294.623  1.00117.99           C  
ANISOU 2787  CB  LEU A 469    15880  13700  15253  -1545    -64    687       C  
ATOM   2788  CG  LEU A 469     -33.950-140.115 295.957  1.00119.20           C  
ANISOU 2788  CG  LEU A 469    15922  14000  15368  -1497    253    539       C  
ATOM   2789  CD1 LEU A 469     -32.842-141.133 295.730  1.00120.71           C  
ANISOU 2789  CD1 LEU A 469    15903  14704  15258  -1661    351    507       C  
ATOM   2790  CD2 LEU A 469     -33.475-138.988 296.862  1.00117.94           C  
ANISOU 2790  CD2 LEU A 469    16074  13646  15092  -1641    284    542       C  
ATOM   2791  N   ILE A 470     -37.283-140.815 294.718  1.00116.80           N  
ANISOU 2791  N   ILE A 470    15204  13182  15992   -752     31    408       N  
ATOM   2792  CA  ILE A 470     -38.354-141.536 295.404  1.00115.27           C  
ANISOU 2792  CA  ILE A 470    14740  12882  16174   -436    245    201       C  
ATOM   2793  C   ILE A 470     -38.775-142.756 294.595  1.00116.24           C  
ANISOU 2793  C   ILE A 470    14519  13224  16422   -328    258    152       C  
ATOM   2794  O   ILE A 470     -38.941-143.856 295.137  1.00122.05           O  
ANISOU 2794  O   ILE A 470    15014  14089  17270   -234    517     31       O  
ATOM   2795  CB  ILE A 470     -39.548-140.601 295.671  1.00117.24           C  
ANISOU 2795  CB  ILE A 470    15082  12705  16759   -190    128     86       C  
ATOM   2796  CG1 ILE A 470     -39.186-139.559 296.730  1.00121.19           C  
ANISOU 2796  CG1 ILE A 470    15874  12991  17183   -260    181     73       C  
ATOM   2797  CG2 ILE A 470     -40.767-141.400 296.106  1.00115.65           C  
ANISOU 2797  CG2 ILE A 470    14539  12453  16948    107    331   -161       C  
ATOM   2798  CD1 ILE A 470     -40.235-138.482 296.902  1.00124.02           C  
ANISOU 2798  CD1 ILE A 470    16361  12918  17841    -23     -7    -52       C  
ATOM   2799  N   LEU A 471     -38.950-142.581 293.283  1.00110.59           N  
ANISOU 2799  N   LEU A 471    13797  12542  15678   -349    -31    247       N  
ATOM   2800  CA  LEU A 471     -39.293-143.717 292.435  1.00107.16           C  
ANISOU 2800  CA  LEU A 471    13027  12340  15347   -257    -40    188       C  
ATOM   2801  C   LEU A 471     -38.178-144.753 292.432  1.00107.35           C  
ANISOU 2801  C   LEU A 471    12913  12773  15101   -440    112    212       C  
ATOM   2802  O   LEU A 471     -38.442-145.956 292.537  1.00110.70           O  
ANISOU 2802  O   LEU A 471    13050  13335  15678   -318    278     87       O  
ATOM   2803  CB  LEU A 471     -39.602-143.246 291.015  1.00107.36           C  
ANISOU 2803  CB  LEU A 471    13106  12348  15339   -261   -402    295       C  
ATOM   2804  CG  LEU A 471     -40.897-142.442 290.878  1.00112.14           C  
ANISOU 2804  CG  LEU A 471    13780  12554  16276     19   -605    212       C  
ATOM   2805  CD1 LEU A 471     -41.229-142.180 289.418  1.00115.55           C  
ANISOU 2805  CD1 LEU A 471    14243  12997  16663     48   -976    312       C  
ATOM   2806  CD2 LEU A 471     -42.042-143.150 291.582  1.00112.50           C  
ANISOU 2806  CD2 LEU A 471    13492  12499  16752    324   -368    -71       C  
ATOM   2807  N   VAL A 472     -36.925-144.308 292.321  1.00105.10           N  
ANISOU 2807  N   VAL A 472    12831  12688  14417   -735     48    348       N  
ATOM   2808  CA  VAL A 472     -35.805-145.234 292.454  1.00104.49           C  
ANISOU 2808  CA  VAL A 472    12616  13011  14077   -880    181    314       C  
ATOM   2809  C   VAL A 472     -35.794-145.850 293.847  1.00104.96           C  
ANISOU 2809  C   VAL A 472    12630  13006  14244   -748    483    194       C  
ATOM   2810  O   VAL A 472     -35.534-147.048 294.009  1.00107.22           O  
ANISOU 2810  O   VAL A 472    12708  13499  14532   -682    610    101       O  
ATOM   2811  CB  VAL A 472     -34.475-144.526 292.132  1.00106.74           C  
ANISOU 2811  CB  VAL A 472    13114  13539  13904  -1242     66    435       C  
ATOM   2812  CG1 VAL A 472     -33.294-145.377 292.573  1.00105.29           C  
ANISOU 2812  CG1 VAL A 472    12795  13749  13462  -1348    217    334       C  
ATOM   2813  CG2 VAL A 472     -34.380-144.236 290.644  1.00109.16           C  
ANISOU 2813  CG2 VAL A 472    13426  14009  14039  -1415   -209    551       C  
ATOM   2814  N   VAL A 473     -36.100-145.050 294.871  1.00106.35           N  
ANISOU 2814  N   VAL A 473    13015  12883  14509   -702    589    190       N  
ATOM   2815  CA  VAL A 473     -36.148-145.574 296.235  1.00105.68           C  
ANISOU 2815  CA  VAL A 473    12918  12732  14502   -591    881     85       C  
ATOM   2816  C   VAL A 473     -37.266-146.601 296.374  1.00104.29           C  
ANISOU 2816  C   VAL A 473    12489  12454  14682   -354   1037    -43       C  
ATOM   2817  O   VAL A 473     -37.054-147.709 296.882  1.00102.89           O  
ANISOU 2817  O   VAL A 473    12204  12395  14493   -309   1220   -104       O  
ATOM   2818  CB  VAL A 473     -36.307-144.426 297.250  1.00104.42           C  
ANISOU 2818  CB  VAL A 473    13020  12288  14367   -595    952     82       C  
ATOM   2819  CG1 VAL A 473     -36.877-144.948 298.558  1.00104.12           C  
ANISOU 2819  CG1 VAL A 473    12932  12115  14514   -426   1257    -50       C  
ATOM   2820  CG2 VAL A 473     -34.968-143.750 297.494  1.00103.43           C  
ANISOU 2820  CG2 VAL A 473    13126  12323  13849   -855    902    166       C  
ATOM   2821  N   LEU A 474     -38.473-146.251 295.919  1.00105.48           N  
ANISOU 2821  N   LEU A 474    12551  12376  15149   -203    955    -97       N  
ATOM   2822  CA  LEU A 474     -39.605-147.160 296.068  1.00108.53           C  
ANISOU 2822  CA  LEU A 474    12677  12671  15887     -7   1124   -257       C  
ATOM   2823  C   LEU A 474     -39.399-148.440 295.268  1.00107.15           C  
ANISOU 2823  C   LEU A 474    12256  12750  15705     -7   1097   -271       C  
ATOM   2824  O   LEU A 474     -39.712-149.536 295.747  1.00104.28           O  
ANISOU 2824  O   LEU A 474    11751  12394  15478     61   1314   -369       O  
ATOM   2825  CB  LEU A 474     -40.902-146.468 295.650  1.00108.11           C  
ANISOU 2825  CB  LEU A 474    12546  12364  16166    169    999   -361       C  
ATOM   2826  CG  LEU A 474     -41.430-145.403 296.612  1.00105.11           C  
ANISOU 2826  CG  LEU A 474    12336  11694  15908    246   1068   -445       C  
ATOM   2827  CD1 LEU A 474     -42.813-144.946 296.188  1.00106.19           C  
ANISOU 2827  CD1 LEU A 474    12322  11608  16416    479    938   -624       C  
ATOM   2828  CD2 LEU A 474     -41.448-145.924 298.042  1.00100.70           C  
ANISOU 2828  CD2 LEU A 474    11780  11120  15360    236   1441   -543       C  
ATOM   2829  N   ILE A 475     -38.874-148.321 294.047  1.00106.59           N  
ANISOU 2829  N   ILE A 475    12146  12888  15467    -97    831   -180       N  
ATOM   2830  CA  ILE A 475     -38.582-149.510 293.251  1.00105.53           C  
ANISOU 2830  CA  ILE A 475    11763  13030  15305    -97    784   -220       C  
ATOM   2831  C   ILE A 475     -37.513-150.353 293.934  1.00107.58           C  
ANISOU 2831  C   ILE A 475    12057  13486  15331   -172    925   -226       C  
ATOM   2832  O   ILE A 475     -37.581-151.589 293.936  1.00113.79           O  
ANISOU 2832  O   ILE A 475    12665  14353  16216    -91   1013   -317       O  
ATOM   2833  CB  ILE A 475     -38.173-149.110 291.821  1.00107.06           C  
ANISOU 2833  CB  ILE A 475    11920  13445  15312   -208    470   -130       C  
ATOM   2834  CG1 ILE A 475     -39.378-148.549 291.063  1.00113.12           C  
ANISOU 2834  CG1 ILE A 475    12621  14009  16353    -64    300   -153       C  
ATOM   2835  CG2 ILE A 475     -37.578-150.295 291.074  1.00104.08           C  
ANISOU 2835  CG2 ILE A 475    11292  13427  14826   -239    416   -192       C  
ATOM   2836  CD1 ILE A 475     -39.045-148.019 289.685  1.00115.19           C  
ANISOU 2836  CD1 ILE A 475    12918  14448  16401   -185    -26    -32       C  
ATOM   2837  N   ILE A 476     -36.521-149.702 294.544  1.00107.31           N  
ANISOU 2837  N   ILE A 476    12264  13519  14991   -315    935   -143       N  
ATOM   2838  CA  ILE A 476     -35.469-150.439 295.237  1.00109.34           C  
ANISOU 2838  CA  ILE A 476    12566  13969  15010   -354   1035   -174       C  
ATOM   2839  C   ILE A 476     -36.016-151.108 296.493  1.00110.91           C  
ANISOU 2839  C   ILE A 476    12819  13933  15388   -216   1313   -233       C  
ATOM   2840  O   ILE A 476     -35.734-152.283 296.757  1.00107.65           O  
ANISOU 2840  O   ILE A 476    12345  13600  14959   -148   1382   -292       O  
ATOM   2841  CB  ILE A 476     -34.286-149.506 295.558  1.00110.08           C  
ANISOU 2841  CB  ILE A 476    12885  14214  14726   -551    971   -103       C  
ATOM   2842  CG1 ILE A 476     -33.402-149.320 294.322  1.00108.03           C  
ANISOU 2842  CG1 ILE A 476    12534  14323  14188   -743    725    -81       C  
ATOM   2843  CG2 ILE A 476     -33.472-150.041 296.728  1.00108.56           C  
ANISOU 2843  CG2 ILE A 476    12802  14099  14346   -526   1123   -158       C  
ATOM   2844  CD1 ILE A 476     -32.236-148.384 294.543  1.00107.01           C  
ANISOU 2844  CD1 ILE A 476    12608  14374  13678   -994    670    -35       C  
ATOM   2845  N   CYS A 477     -36.814-150.386 297.279  1.00114.71           N  
ANISOU 2845  N   CYS A 477    13428  14121  16035   -179   1468   -228       N  
ATOM   2846  CA  CYS A 477     -37.240-150.887 298.581  1.00117.29           C  
ANISOU 2846  CA  CYS A 477    13849  14258  16460   -107   1758   -278       C  
ATOM   2847  C   CYS A 477     -38.464-151.791 298.517  1.00123.33           C  
ANISOU 2847  C   CYS A 477    14417  14863  17580      2   1913   -381       C  
ATOM   2848  O   CYS A 477     -38.571-152.724 299.321  1.00127.18           O  
ANISOU 2848  O   CYS A 477    14957  15278  18087     22   2122   -409       O  
ATOM   2849  CB  CYS A 477     -37.520-149.717 299.527  1.00115.04           C  
ANISOU 2849  CB  CYS A 477    13766  13771  16175   -130   1875   -270       C  
ATOM   2850  SG  CYS A 477     -36.044-148.790 300.002  1.00113.04           S  
ANISOU 2850  SG  CYS A 477    13782  13677  15489   -282   1779   -179       S  
ATOM   2851  N   TRP A 478     -39.393-151.542 297.593  1.00123.28           N  
ANISOU 2851  N   TRP A 478    14199  14797  17845     63   1811   -444       N  
ATOM   2852  CA  TRP A 478     -40.611-152.337 297.512  1.00126.67           C  
ANISOU 2852  CA  TRP A 478    14407  15093  18628    151   1966   -585       C  
ATOM   2853  C   TRP A 478     -40.655-153.285 296.324  1.00129.32           C  
ANISOU 2853  C   TRP A 478    14486  15584  19066    192   1812   -628       C  
ATOM   2854  O   TRP A 478     -41.503-154.183 296.307  1.00131.56           O  
ANISOU 2854  O   TRP A 478    14592  15779  19616    237   1959   -751       O  
ATOM   2855  CB  TRP A 478     -41.845-151.424 297.461  1.00129.38           C  
ANISOU 2855  CB  TRP A 478    14653  15243  19264    234   1987   -706       C  
ATOM   2856  CG  TRP A 478     -42.022-150.619 298.703  1.00134.01           C  
ANISOU 2856  CG  TRP A 478    15440  15662  19817    215   2176   -730       C  
ATOM   2857  CD1 TRP A 478     -41.724-149.300 298.873  1.00140.13           C  
ANISOU 2857  CD1 TRP A 478    16396  16371  20475    209   2047   -674       C  
ATOM   2858  CD2 TRP A 478     -42.525-151.083 299.961  1.00135.16           C  
ANISOU 2858  CD2 TRP A 478    15635  15688  20031    181   2530   -823       C  
ATOM   2859  NE1 TRP A 478     -42.018-148.909 300.157  1.00142.78           N  
ANISOU 2859  NE1 TRP A 478    16862  16567  20821    200   2292   -750       N  
ATOM   2860  CE2 TRP A 478     -42.510-149.986 300.846  1.00140.62           C  
ANISOU 2860  CE2 TRP A 478    16509  16274  20645    175   2599   -840       C  
ATOM   2861  CE3 TRP A 478     -42.990-152.317 300.425  1.00135.76           C  
ANISOU 2861  CE3 TRP A 478    15638  15731  20214    134   2797   -894       C  
ATOM   2862  CZ2 TRP A 478     -42.942-150.087 302.167  1.00142.41           C  
ANISOU 2862  CZ2 TRP A 478    16822  16405  20885    128   2931   -936       C  
ATOM   2863  CZ3 TRP A 478     -43.418-152.415 301.736  1.00139.10           C  
ANISOU 2863  CZ3 TRP A 478    16181  16039  20634     59   3133   -965       C  
ATOM   2864  CH2 TRP A 478     -43.391-151.307 302.592  1.00141.80           C  
ANISOU 2864  CH2 TRP A 478    16678  16316  20883     59   3201   -990       C  
ATOM   2865  N   GLY A 479     -39.778-153.110 295.340  1.00128.24           N  
ANISOU 2865  N   GLY A 479    14317  15691  18719    156   1533   -548       N  
ATOM   2866  CA  GLY A 479     -39.717-154.003 294.209  1.00129.60           C  
ANISOU 2866  CA  GLY A 479    14235  16054  18953    193   1375   -607       C  
ATOM   2867  C   GLY A 479     -39.362-155.418 294.619  1.00131.54           C  
ANISOU 2867  C   GLY A 479    14461  16329  19188    211   1493   -657       C  
ATOM   2868  O   GLY A 479     -40.179-156.339 294.524  1.00134.06           O  
ANISOU 2868  O   GLY A 479    14613  16535  19787    269   1607   -771       O  
ATOM   2869  N   PRO A 480     -38.125-155.617 295.085  1.00132.39           N  
ANISOU 2869  N   PRO A 480    14751  16580  18971    163   1453   -588       N  
ATOM   2870  CA  PRO A 480     -37.721-156.967 295.514  1.00133.41           C  
ANISOU 2870  CA  PRO A 480    14916  16702  19072    214   1513   -635       C  
ATOM   2871  C   PRO A 480     -38.552-157.516 296.660  1.00132.49           C  
ANISOU 2871  C   PRO A 480    14945  16253  19144    220   1826   -642       C  
ATOM   2872  O   PRO A 480     -38.799-158.727 296.709  1.00140.07           O  
ANISOU 2872  O   PRO A 480    15868  17114  20239    256   1888   -704       O  
ATOM   2873  CB  PRO A 480     -36.251-156.777 295.919  1.00134.13           C  
ANISOU 2873  CB  PRO A 480    15200  17009  18754    180   1396   -579       C  
ATOM   2874  CG  PRO A 480     -35.800-155.578 295.154  1.00133.09           C  
ANISOU 2874  CG  PRO A 480    15015  17106  18446     77   1212   -531       C  
ATOM   2875  CD  PRO A 480     -36.995-154.673 295.088  1.00133.55           C  
ANISOU 2875  CD  PRO A 480    15057  16928  18757     64   1306   -490       C  
ATOM   2876  N   LEU A 481     -38.993-156.662 297.586  1.00124.14           N  
ANISOU 2876  N   LEU A 481    14059  15020  18090    167   2026   -590       N  
ATOM   2877  CA  LEU A 481     -39.768-157.146 298.725  1.00123.80           C  
ANISOU 2877  CA  LEU A 481    14158  14700  18181    128   2351   -607       C  
ATOM   2878  C   LEU A 481     -41.078-157.774 298.268  1.00123.16           C  
ANISOU 2878  C   LEU A 481    13820  14484  18491    128   2481   -749       C  
ATOM   2879  O   LEU A 481     -41.402-158.907 298.643  1.00123.95           O  
ANISOU 2879  O   LEU A 481    13967  14437  18690     87   2640   -782       O  
ATOM   2880  CB  LEU A 481     -40.033-156.005 299.706  1.00128.60           C  
ANISOU 2880  CB  LEU A 481    14942  15195  18724     74   2529   -571       C  
ATOM   2881  CG  LEU A 481     -40.664-156.439 301.032  1.00134.18           C  
ANISOU 2881  CG  LEU A 481    15836  15670  19475     -5   2886   -584       C  
ATOM   2882  CD1 LEU A 481     -39.633-157.120 301.919  1.00135.42           C  
ANISOU 2882  CD1 LEU A 481    16327  15821  19307    -18   2905   -460       C  
ATOM   2883  CD2 LEU A 481     -41.303-155.261 301.748  1.00137.48           C  
ANISOU 2883  CD2 LEU A 481    16295  15996  19946    -43   3063   -635       C  
ATOM   2884  N   LEU A 482     -41.848-157.050 297.451  1.00120.35           N  
ANISOU 2884  N   LEU A 482    13203  14167  18358    170   2402   -845       N  
ATOM   2885  CA  LEU A 482     -43.093-157.607 296.936  1.00117.37           C  
ANISOU 2885  CA  LEU A 482    12533  13704  18359    185   2502  -1026       C  
ATOM   2886  C   LEU A 482     -42.835-158.723 295.932  1.00116.40           C  
ANISOU 2886  C   LEU A 482    12222  13698  18308    231   2326  -1073       C  
ATOM   2887  O   LEU A 482     -43.675-159.616 295.774  1.00121.34           O  
ANISOU 2887  O   LEU A 482    12678  14218  19210    206   2461  -1213       O  
ATOM   2888  CB  LEU A 482     -43.943-156.508 296.300  1.00113.41           C  
ANISOU 2888  CB  LEU A 482    11808  13221  18062    265   2408  -1138       C  
ATOM   2889  CG  LEU A 482     -44.426-155.401 297.239  1.00111.23           C  
ANISOU 2889  CG  LEU A 482    11660  12807  17796    250   2574  -1165       C  
ATOM   2890  CD1 LEU A 482     -45.339-154.434 296.502  1.00111.27           C  
ANISOU 2890  CD1 LEU A 482    11431  12804  18043    378   2424  -1315       C  
ATOM   2891  CD2 LEU A 482     -45.131-155.993 298.450  1.00113.76           C  
ANISOU 2891  CD2 LEU A 482    12050  12953  18221    130   2976  -1261       C  
ATOM   2892  N   ALA A 483     -41.688-158.692 295.249  1.00110.05           N  
ANISOU 2892  N   ALA A 483    11429  13127  17257    283   2032   -986       N  
ATOM   2893  CA  ALA A 483     -41.364-159.755 294.303  1.00110.41           C  
ANISOU 2893  CA  ALA A 483    11281  13317  17353    341   1846  -1063       C  
ATOM   2894  C   ALA A 483     -41.259-161.099 295.009  1.00113.81           C  
ANISOU 2894  C   ALA A 483    11870  13562  17813    312   1994  -1074       C  
ATOM   2895  O   ALA A 483     -41.866-162.088 294.580  1.00115.94           O  
ANISOU 2895  O   ALA A 483    11962  13750  18340    318   2028  -1204       O  
ATOM   2896  CB  ALA A 483     -40.065-159.429 293.567  1.00108.35           C  
ANISOU 2896  CB  ALA A 483    11010  13383  16773    376   1526   -996       C  
ATOM   2897  N   ILE A 484     -40.496-161.151 296.105  1.00114.82           N  
ANISOU 2897  N   ILE A 484    12352  13603  17669    280   2070   -940       N  
ATOM   2898  CA  ILE A 484     -40.355-162.393 296.860  1.00116.25           C  
ANISOU 2898  CA  ILE A 484    12771  13563  17835    257   2182   -918       C  
ATOM   2899  C   ILE A 484     -41.711-162.866 297.365  1.00120.08           C  
ANISOU 2899  C   ILE A 484    13249  13751  18626    120   2523   -984       C  
ATOM   2900  O   ILE A 484     -41.995-164.070 297.393  1.00123.47           O  
ANISOU 2900  O   ILE A 484    13716  13999  19197     79   2583  -1035       O  
ATOM   2901  CB  ILE A 484     -39.355-162.205 298.016  1.00116.86           C  
ANISOU 2901  CB  ILE A 484    13254  13603  17543    259   2200   -761       C  
ATOM   2902  CG1 ILE A 484     -38.013-161.689 297.491  1.00112.73           C  
ANISOU 2902  CG1 ILE A 484    12694  13423  16716    365   1877   -745       C  
ATOM   2903  CG2 ILE A 484     -39.170-163.508 298.776  1.00121.82           C  
ANISOU 2903  CG2 ILE A 484    14188  13973  18126    254   2265   -719       C  
ATOM   2904  CD1 ILE A 484     -37.396-162.557 296.417  1.00112.86           C  
ANISOU 2904  CD1 ILE A 484    12494  13645  16741    487   1573   -872       C  
ATOM   2905  N   MET A 485     -42.574-161.929 297.760  1.00122.22           N  
ANISOU 2905  N   MET A 485    13463  13971  19002     37   2747  -1010       N  
ATOM   2906  CA  MET A 485     -43.902-162.306 298.228  1.00127.54           C  
ANISOU 2906  CA  MET A 485    14075  14423  19960   -119   3092  -1129       C  
ATOM   2907  C   MET A 485     -44.757-162.870 297.100  1.00128.30           C  
ANISOU 2907  C   MET A 485    13768  14557  20423    -97   3042  -1340       C  
ATOM   2908  O   MET A 485     -45.600-163.741 297.341  1.00127.94           O  
ANISOU 2908  O   MET A 485    13689  14324  20600   -243   3281  -1451       O  
ATOM   2909  CB  MET A 485     -44.588-161.105 298.877  1.00131.05           C  
ANISOU 2909  CB  MET A 485    14507  14854  20432   -179   3310  -1167       C  
ATOM   2910  CG  MET A 485     -43.834-160.536 300.066  1.00131.22           C  
ANISOU 2910  CG  MET A 485    14916  14837  20105   -214   3391   -984       C  
ATOM   2911  SD  MET A 485     -44.701-159.158 300.838  1.00131.82           S  
ANISOU 2911  SD  MET A 485    14949  14892  20242   -273   3643  -1079       S  
ATOM   2912  CE  MET A 485     -43.530-158.690 302.110  1.00131.36           C  
ANISOU 2912  CE  MET A 485    15360  14820  19729   -295   3672   -850       C  
ATOM   2913  N   VAL A 486     -44.556-162.395 295.868  1.00130.87           N  
ANISOU 2913  N   VAL A 486    13794  15128  20800     64   2740  -1403       N  
ATOM   2914  CA  VAL A 486     -45.279-162.961 294.733  1.00133.65           C  
ANISOU 2914  CA  VAL A 486    13756  15548  21476    110   2654  -1612       C  
ATOM   2915  C   VAL A 486     -44.796-164.379 294.450  1.00132.91           C  
ANISOU 2915  C   VAL A 486    13708  15394  21399    111   2556  -1623       C  
ATOM   2916  O   VAL A 486     -45.595-165.268 294.128  1.00136.18           O  
ANISOU 2916  O   VAL A 486    13937  15697  22108     45   2661  -1794       O  
ATOM   2917  CB  VAL A 486     -45.138-162.051 293.498  1.00133.39           C  
ANISOU 2917  CB  VAL A 486    13436  15803  21442    276   2337  -1654       C  
ATOM   2918  CG1 VAL A 486     -45.704-162.733 292.262  1.00132.85           C  
ANISOU 2918  CG1 VAL A 486    13040  15843  21592    335   2164  -1841       C  
ATOM   2919  CG2 VAL A 486     -45.845-160.726 293.737  1.00134.61           C  
ANISOU 2919  CG2 VAL A 486    13539  15948  21659    293   2420  -1688       C  
ATOM   2920  N   TYR A 487     -43.485-164.615 294.568  1.00128.63           N  
ANISOU 2920  N   TYR A 487    13405  14923  20547    192   2341  -1471       N  
ATOM   2921  CA  TYR A 487     -42.964-165.976 294.472  1.00128.48           C  
ANISOU 2921  CA  TYR A 487    13492  14800  20526    222   2226  -1491       C  
ATOM   2922  C   TYR A 487     -43.605-166.883 295.513  1.00130.85           C  
ANISOU 2922  C   TYR A 487    14073  14706  20938     31   2546  -1466       C  
ATOM   2923  O   TYR A 487     -43.822-168.074 295.264  1.00138.18           O  
ANISOU 2923  O   TYR A 487    14990  15466  22045     -2   2532  -1559       O  
ATOM   2924  CB  TYR A 487     -41.445-165.980 294.643  1.00130.33           C  
ANISOU 2924  CB  TYR A 487    13966  15175  20380    353   1956  -1360       C  
ATOM   2925  CG  TYR A 487     -40.660-165.576 293.416  1.00135.78           C  
ANISOU 2925  CG  TYR A 487    14360  16274  20954    508   1598  -1435       C  
ATOM   2926  CD1 TYR A 487     -40.211-164.273 293.254  1.00137.38           C  
ANISOU 2926  CD1 TYR A 487    14531  16732  20934    519   1513  -1347       C  
ATOM   2927  CD2 TYR A 487     -40.353-166.502 292.428  1.00140.59           C  
ANISOU 2927  CD2 TYR A 487    14736  17020  21661    621   1348  -1601       C  
ATOM   2928  CE1 TYR A 487     -39.488-163.898 292.140  1.00138.29           C  
ANISOU 2928  CE1 TYR A 487    14405  17235  20904    603   1207  -1407       C  
ATOM   2929  CE2 TYR A 487     -39.629-166.138 291.308  1.00142.13           C  
ANISOU 2929  CE2 TYR A 487    14654  17634  21717    729   1039  -1686       C  
ATOM   2930  CZ  TYR A 487     -39.199-164.834 291.170  1.00141.12           C  
ANISOU 2930  CZ  TYR A 487    14515  17762  21343    702    979  -1580       C  
ATOM   2931  OH  TYR A 487     -38.478-164.465 290.058  1.00141.31           O  
ANISOU 2931  OH  TYR A 487    14287  18214  21190    755    692  -1656       O  
ATOM   2932  N   ASP A 488     -43.909-166.338 296.691  1.00126.63           N  
ANISOU 2932  N   ASP A 488    13807  14018  20287   -115   2839  -1345       N  
ATOM   2933  CA  ASP A 488     -44.559-167.137 297.721  1.00127.09           C  
ANISOU 2933  CA  ASP A 488    14157  13722  20409   -353   3179  -1311       C  
ATOM   2934  C   ASP A 488     -46.019-167.408 297.382  1.00132.83           C  
ANISOU 2934  C   ASP A 488    14558  14376  21536   -530   3447  -1543       C  
ATOM   2935  O   ASP A 488     -46.542-168.478 297.715  1.00139.11           O  
ANISOU 2935  O   ASP A 488    15487  14900  22469   -730   3641  -1584       O  
ATOM   2936  CB  ASP A 488     -44.438-166.436 299.074  1.00124.34           C  
ANISOU 2936  CB  ASP A 488    14172  13283  19789   -467   3419  -1135       C  
ATOM   2937  CG  ASP A 488     -45.255-167.109 300.150  1.00123.60           C  
ANISOU 2937  CG  ASP A 488    14360  12864  19738   -772   3824  -1110       C  
ATOM   2938  OD1 ASP A 488     -45.071-168.325 300.370  1.00125.07           O  
ANISOU 2938  OD1 ASP A 488    14826  12787  19907   -852   3810  -1043       O  
ATOM   2939  OD2 ASP A 488     -46.096-166.422 300.764  1.00123.41           O  
ANISOU 2939  OD2 ASP A 488    14279  12849  19761   -941   4151  -1171       O  
ATOM   2940  N   VAL A 489     -46.688-166.466 296.714  1.00134.70           N  
ANISOU 2940  N   VAL A 489    14376  14845  21960   -461   3445  -1710       N  
ATOM   2941  CA  VAL A 489     -48.094-166.660 296.367  1.00139.20           C  
ANISOU 2941  CA  VAL A 489    14583  15392  22915   -599   3680  -1987       C  
ATOM   2942  C   VAL A 489     -48.225-167.680 295.241  1.00140.82           C  
ANISOU 2942  C   VAL A 489    14516  15614  23374   -537   3493  -2152       C  
ATOM   2943  O   VAL A 489     -48.954-168.672 295.359  1.00140.94           O  
ANISOU 2943  O   VAL A 489    14510  15425  23615   -743   3707  -2286       O  
ATOM   2944  CB  VAL A 489     -48.746-165.316 295.993  1.00138.19           C  
ANISOU 2944  CB  VAL A 489    14106  15497  22903   -490   3678  -2137       C  
ATOM   2945  CG1 VAL A 489     -50.152-165.537 295.472  1.00142.11           C  
ANISOU 2945  CG1 VAL A 489    14251  16017  23729   -575   3783  -2452       C  
ATOM   2946  CG2 VAL A 489     -48.768-164.379 297.197  1.00136.13           C  
ANISOU 2946  CG2 VAL A 489    14100  15188  22435   -577   3905  -2025       C  
ATOM   2947  N   PHE A 490     -47.516-167.457 294.138  1.00141.17           N  
ANISOU 2947  N   PHE A 490    14351  15912  23375   -276   3098  -2156       N  
ATOM   2948  CA  PHE A 490     -47.526-168.373 292.999  1.00145.54           C  
ANISOU 2948  CA  PHE A 490    14623  16534  24143   -184   2878  -2327       C  
ATOM   2949  C   PHE A 490     -46.373-169.352 293.156  1.00148.03           C  
ANISOU 2949  C   PHE A 490    15266  16719  24259   -126   2672  -2179       C  
ATOM   2950  O   PHE A 490     -45.207-168.967 293.030  1.00149.26           O  
ANISOU 2950  O   PHE A 490    15543  17051  24118     54   2394  -2035       O  
ATOM   2951  CB  PHE A 490     -47.404-167.611 291.681  1.00146.33           C  
ANISOU 2951  CB  PHE A 490    14466  17006  24126     30   2470  -2376       C  
ATOM   2952  CG  PHE A 490     -48.567-166.708 291.385  1.00149.22           C  
ANISOU 2952  CG  PHE A 490    14760  17472  24464     -2   2454  -2461       C  
ATOM   2953  CD1 PHE A 490     -49.734-166.801 292.121  1.00150.85           C  
ANISOU 2953  CD1 PHE A 490    14950  17484  24881   -197   2810  -2604       C  
ATOM   2954  CD2 PHE A 490     -48.500-165.774 290.362  1.00150.80           C  
ANISOU 2954  CD2 PHE A 490    14905  17964  24430    162   2094  -2419       C  
ATOM   2955  CE1 PHE A 490     -50.812-165.977 291.858  1.00154.01           C  
ANISOU 2955  CE1 PHE A 490    15255  17988  25275   -186   2765  -2732       C  
ATOM   2956  CE2 PHE A 490     -49.581-164.942 290.088  1.00153.50           C  
ANISOU 2956  CE2 PHE A 490    15166  18368  24788    175   2071  -2519       C  
ATOM   2957  CZ  PHE A 490     -50.740-165.045 290.840  1.00155.04           C  
ANISOU 2957  CZ  PHE A 490    15320  18378  25209     19   2386  -2690       C  
ATOM   2958  N   GLY A 491     -46.695-170.619 293.406  1.00147.48           N  
ANISOU 2958  N   GLY A 491    15337  16344  24354   -277   2791  -2239       N  
ATOM   2959  CA  GLY A 491     -45.631-171.567 293.662  1.00151.62           C  
ANISOU 2959  CA  GLY A 491    16228  16687  24692   -198   2573  -2108       C  
ATOM   2960  C   GLY A 491     -45.007-171.353 295.033  1.00153.89           C  
ANISOU 2960  C   GLY A 491    17073  16771  24627   -271   2690  -1821       C  
ATOM   2961  O   GLY A 491     -45.589-170.733 295.931  1.00155.19           O  
ANISOU 2961  O   GLY A 491    17381  16850  24735   -464   3026  -1732       O  
ATOM   2962  N   LYS A 492     -43.796-171.889 295.187  1.00156.07           N  
ANISOU 2962  N   LYS A 492    17654  16988  24658    -97   2391  -1703       N  
ATOM   2963  CA  LYS A 492     -43.056-171.786 296.436  1.00155.68           C  
ANISOU 2963  CA  LYS A 492    18149  16756  24245   -114   2430  -1444       C  
ATOM   2964  C   LYS A 492     -41.594-171.500 296.119  1.00153.44           C  
ANISOU 2964  C   LYS A 492    17891  16751  23659    199   2011  -1404       C  
ATOM   2965  O   LYS A 492     -41.171-171.500 294.958  1.00151.53           O  
ANISOU 2965  O   LYS A 492    17268  16820  23485    396   1709  -1575       O  
ATOM   2966  CB  LYS A 492     -43.198-173.059 297.289  1.00157.92           C  
ANISOU 2966  CB  LYS A 492    18938  16533  24530   -285   2543  -1343       C  
ATOM   2967  CG  LYS A 492     -44.640-173.388 297.681  1.00157.56           C  
ANISOU 2967  CG  LYS A 492    18891  16220  24753   -669   3002  -1397       C  
ATOM   2968  CD  LYS A 492     -44.760-173.851 299.128  1.00156.56           C  
ANISOU 2968  CD  LYS A 492    19404  15672  24411   -942   3278  -1159       C  
ATOM   2969  CE  LYS A 492     -46.096-173.412 299.732  1.00154.93           C  
ANISOU 2969  CE  LYS A 492    19116  15421  24330  -1333   3815  -1203       C  
ATOM   2970  NZ  LYS A 492     -46.091-173.382 301.224  1.00155.89           N  
ANISOU 2970  NZ  LYS A 492    19817  15285  24129  -1584   4105   -950       N  
ATOM   2971  N   MET A 493     -40.819-171.254 297.168  1.00153.05           N  
ANISOU 2971  N   MET A 493    18280  16614  23256    232   2001  -1197       N  
ATOM   2972  CA  MET A 493     -39.439-170.813 297.043  1.00150.16           C  
ANISOU 2972  CA  MET A 493    17942  16548  22565    495   1655  -1174       C  
ATOM   2973  C   MET A 493     -38.513-171.764 297.787  1.00146.45           C  
ANISOU 2973  C   MET A 493    17969  15812  21862    633   1439  -1088       C  
ATOM   2974  O   MET A 493     -38.945-172.603 298.581  1.00151.00           O  
ANISOU 2974  O   MET A 493    18961  15936  22476    491   1594   -974       O  
ATOM   2975  CB  MET A 493     -39.270-169.389 297.581  1.00156.45           C  
ANISOU 2975  CB  MET A 493    18760  17563  23122    447   1805  -1039       C  
ATOM   2976  CG  MET A 493     -39.616-169.245 299.054  1.00165.38           C  
ANISOU 2976  CG  MET A 493    20362  18380  24097    256   2136   -826       C  
ATOM   2977  SD  MET A 493     -39.836-167.519 299.509  1.00169.60           S  
ANISOU 2977  SD  MET A 493    20797  19155  24488    162   2372   -738       S  
ATOM   2978  CE  MET A 493     -40.957-166.995 298.217  1.00170.11           C  
ANISOU 2978  CE  MET A 493    20250  19425  24957    106   2445   -941       C  
ATOM   2979  N   ASN A 494     -37.221-171.612 297.522  1.00139.28           N  
ANISOU 2979  N   ASN A 494    17026  15196  20697    906   1068  -1156       N  
ATOM   2980  CA  ASN A 494     -36.197-172.419 298.164  1.00138.56           C  
ANISOU 2980  CA  ASN A 494    17371  14917  20360   1114    781  -1123       C  
ATOM   2981  C   ASN A 494     -35.720-171.721 299.437  1.00133.02           C  
ANISOU 2981  C   ASN A 494    17081  14176  19285   1087    902   -901       C  
ATOM   2982  O   ASN A 494     -36.280-170.709 299.869  1.00130.72           O  
ANISOU 2982  O   ASN A 494    16758  13952  18959    882   1236   -771       O  
ATOM   2983  CB  ASN A 494     -35.055-172.685 297.187  1.00138.64           C  
ANISOU 2983  CB  ASN A 494    17076  15305  20297   1437    304  -1387       C  
ATOM   2984  CG  ASN A 494     -34.358-171.414 296.748  1.00134.31           C  
ANISOU 2984  CG  ASN A 494    16186  15322  19523   1489    232  -1449       C  
ATOM   2985  OD1 ASN A 494     -33.591-170.825 297.506  1.00132.08           O  
ANISOU 2985  OD1 ASN A 494    16131  15146  18907   1546    201  -1355       O  
ATOM   2986  ND2 ASN A 494     -34.621-170.983 295.519  1.00133.49           N  
ANISOU 2986  ND2 ASN A 494    15549  15581  19588   1456    202  -1608       N  
ATOM   2987  N   LYS A 495     -34.661-172.259 300.048  1.00131.27           N  
ANISOU 2987  N   LYS A 495    17243  13853  18779   1320    606   -884       N  
ATOM   2988  CA  LYS A 495     -34.137-171.714 301.296  1.00125.93           C  
ANISOU 2988  CA  LYS A 495    16989  13130  17727   1325    682   -690       C  
ATOM   2989  C   LYS A 495     -33.360-170.421 301.082  1.00117.71           C  
ANISOU 2989  C   LYS A 495    15644  12622  16457   1406    615   -762       C  
ATOM   2990  O   LYS A 495     -33.394-169.534 301.942  1.00116.26           O  
ANISOU 2990  O   LYS A 495    15639  12465  16069   1284    847   -598       O  
ATOM   2991  CB  LYS A 495     -33.257-172.763 301.979  1.00126.69           C  
ANISOU 2991  CB  LYS A 495    17605  12936  17596   1582    339   -672       C  
ATOM   2992  CG  LYS A 495     -32.440-172.267 303.162  1.00123.88           C  
ANISOU 2992  CG  LYS A 495    17654  12609  16805   1683    298   -534       C  
ATOM   2993  CD  LYS A 495     -30.962-172.180 302.806  1.00116.40           C  
ANISOU 2993  CD  LYS A 495    16542  12070  15616   2066   -180   -786       C  
ATOM   2994  CE  LYS A 495     -30.094-172.094 304.051  1.00109.66           C  
ANISOU 2994  CE  LYS A 495    16191  11138  14337   2237   -314   -682       C  
ATOM   2995  NZ  LYS A 495     -28.644-172.039 303.717  1.00103.62           N  
ANISOU 2995  NZ  LYS A 495    15233  10802  13337   2616   -787   -985       N  
ATOM   2996  N   LEU A 496     -32.665-170.291 299.950  1.00115.28           N  
ANISOU 2996  N   LEU A 496    14883  12747  16171   1584    311  -1014       N  
ATOM   2997  CA  LEU A 496     -31.899-169.075 299.690  1.00116.61           C  
ANISOU 2997  CA  LEU A 496    14774  13428  16106   1611    250  -1089       C  
ATOM   2998  C   LEU A 496     -32.809-167.857 299.598  1.00118.86           C  
ANISOU 2998  C   LEU A 496    14858  13802  16503   1326    628   -953       C  
ATOM   2999  O   LEU A 496     -32.456-166.772 300.077  1.00115.56           O  
ANISOU 2999  O   LEU A 496    14481  13572  15854   1263    727   -874       O  
ATOM   3000  CB  LEU A 496     -31.087-169.227 298.404  1.00111.63           C  
ANISOU 3000  CB  LEU A 496    13673  13260  15481   1796   -118  -1401       C  
ATOM   3001  CG  LEU A 496     -30.339-167.994 297.895  1.00104.93           C  
ANISOU 3001  CG  LEU A 496    12481  12984  14406   1757   -178  -1505       C  
ATOM   3002  CD1 LEU A 496     -29.001-167.835 298.606  1.00106.91           C  
ANISOU 3002  CD1 LEU A 496    12930  13438  14253   1946   -405  -1594       C  
ATOM   3003  CD2 LEU A 496     -30.151-168.063 296.385  1.00102.52           C  
ANISOU 3003  CD2 LEU A 496    11633  13098  14224   1788   -385  -1765       C  
ATOM   3004  N   ILE A 497     -33.983-168.017 298.984  1.00119.77           N  
ANISOU 3004  N   ILE A 497    14750  13778  16978   1166    823   -949       N  
ATOM   3005  CA  ILE A 497     -34.908-166.897 298.841  1.00115.25           C  
ANISOU 3005  CA  ILE A 497    13970  13277  16542    938   1141   -861       C  
ATOM   3006  C   ILE A 497     -35.392-166.431 300.208  1.00115.95           C  
ANISOU 3006  C   ILE A 497    14447  13088  16522    776   1482   -643       C  
ATOM   3007  O   ILE A 497     -35.562-165.229 300.445  1.00117.43           O  
ANISOU 3007  O   ILE A 497    14567  13416  16634    667   1652   -576       O  
ATOM   3008  CB  ILE A 497     -36.082-167.289 297.925  1.00118.00           C  
ANISOU 3008  CB  ILE A 497    13996  13533  17307    834   1254   -947       C  
ATOM   3009  CG1 ILE A 497     -35.566-168.003 296.673  1.00121.06           C  
ANISOU 3009  CG1 ILE A 497    14050  14158  17791   1012    899  -1178       C  
ATOM   3010  CG2 ILE A 497     -36.881-166.062 297.533  1.00118.15           C  
ANISOU 3010  CG2 ILE A 497    13727  13710  17457    674   1469   -922       C  
ATOM   3011  CD1 ILE A 497     -34.629-167.163 295.829  1.00121.90           C  
ANISOU 3011  CD1 ILE A 497    13830  14797  17688   1096    655  -1298       C  
ATOM   3012  N   LYS A 498     -35.625-167.373 301.127  1.00118.56           N  
ANISOU 3012  N   LYS A 498    15202  13014  16831    748   1580   -534       N  
ATOM   3013  CA  LYS A 498     -35.947-167.002 302.501  1.00122.87           C  
ANISOU 3013  CA  LYS A 498    16154  13328  17201    593   1887   -334       C  
ATOM   3014  C   LYS A 498     -34.838-166.154 303.109  1.00130.85           C  
ANISOU 3014  C   LYS A 498    17309  14583  17823    714   1764   -292       C  
ATOM   3015  O   LYS A 498     -35.108-165.152 303.782  1.00129.46           O  
ANISOU 3015  O   LYS A 498    17199  14446  17545    579   2013   -197       O  
ATOM   3016  CB  LYS A 498     -36.178-168.253 303.349  1.00128.04           C  
ANISOU 3016  CB  LYS A 498    17306  13521  17825    547   1948   -212       C  
ATOM   3017  CG  LYS A 498     -37.338-169.126 302.906  1.00129.43           C  
ANISOU 3017  CG  LYS A 498    17392  13409  18375    367   2122   -250       C  
ATOM   3018  CD  LYS A 498     -37.489-170.315 303.840  1.00134.42           C  
ANISOU 3018  CD  LYS A 498    18603  13551  18919    279   2182    -96       C  
ATOM   3019  CE  LYS A 498     -38.670-171.187 303.457  1.00136.58           C  
ANISOU 3019  CE  LYS A 498    18808  13525  19562     43   2389   -141       C  
ATOM   3020  NZ  LYS A 498     -38.812-172.347 304.381  1.00140.38           N  
ANISOU 3020  NZ  LYS A 498    19914  13492  19930    -90   2449     34       N  
ATOM   3021  N   THR A 499     -33.582-166.543 302.880  1.00138.35           N  
ANISOU 3021  N   THR A 499    18291  15717  18559    972   1373   -398       N  
ATOM   3022  CA  THR A 499     -32.459-165.748 303.362  1.00139.51           C  
ANISOU 3022  CA  THR A 499    18519  16151  18339   1089   1234   -414       C  
ATOM   3023  C   THR A 499     -32.413-164.393 302.668  1.00131.44           C  
ANISOU 3023  C   THR A 499    17084  15521  17336    989   1285   -481       C  
ATOM   3024  O   THR A 499     -32.202-163.362 303.319  1.00130.50           O  
ANISOU 3024  O   THR A 499    17057  15505  17021    914   1416   -409       O  
ATOM   3025  CB  THR A 499     -31.148-166.505 303.144  1.00145.76           C  
ANISOU 3025  CB  THR A 499    19360  17100  18923   1399    782   -586       C  
ATOM   3026  OG1 THR A 499     -31.284-167.849 303.625  1.00151.76           O  
ANISOU 3026  OG1 THR A 499    20512  17436  19714   1504    688   -526       O  
ATOM   3027  CG2 THR A 499     -30.009-165.824 303.885  1.00146.62           C  
ANISOU 3027  CG2 THR A 499    19626  17458  18625   1518    659   -613       C  
ATOM   3028  N   VAL A 500     -32.612-164.375 301.348  1.00116.46           N  
ANISOU 3028  N   VAL A 500    14752  13831  15666    981   1171   -617       N  
ATOM   3029  CA  VAL A 500     -32.638-163.109 300.619  1.00101.83           C  
ANISOU 3029  CA  VAL A 500    12553  12308  13829    865   1203   -655       C  
ATOM   3030  C   VAL A 500     -33.788-162.240 301.109  1.00102.31           C  
ANISOU 3030  C   VAL A 500    12661  12168  14046    656   1574   -505       C  
ATOM   3031  O   VAL A 500     -33.626-161.032 301.324  1.00105.51           O  
ANISOU 3031  O   VAL A 500    13048  12721  14321    571   1649   -463       O  
ATOM   3032  CB  VAL A 500     -32.724-163.363 299.102  1.00 90.90           C  
ANISOU 3032  CB  VAL A 500    10724  11163  12651    892   1009   -820       C  
ATOM   3033  CG1 VAL A 500     -32.922-162.054 298.351  1.00 76.83           C  
ANISOU 3033  CG1 VAL A 500     8649   9653  10891    741   1054   -815       C  
ATOM   3034  CG2 VAL A 500     -31.471-164.071 298.614  1.00 96.74           C  
ANISOU 3034  CG2 VAL A 500    11367  12188  13200   1103    627  -1027       C  
ATOM   3035  N   PHE A 501     -34.964-162.840 301.307  1.00 94.96           N  
ANISOU 3035  N   PHE A 501    11787  10898  13394    564   1808   -449       N  
ATOM   3036  CA  PHE A 501     -36.095-162.076 301.823  1.00 97.85           C  
ANISOU 3036  CA  PHE A 501    12170  11095  13914    377   2164   -365       C  
ATOM   3037  C   PHE A 501     -35.809-161.544 303.221  1.00104.63           C  
ANISOU 3037  C   PHE A 501    13399  11863  14492    329   2337   -241       C  
ATOM   3038  O   PHE A 501     -36.226-160.431 303.565  1.00110.13           O  
ANISOU 3038  O   PHE A 501    14059  12589  15196    224   2524   -214       O  
ATOM   3039  CB  PHE A 501     -37.359-162.932 301.828  1.00 98.77           C  
ANISOU 3039  CB  PHE A 501    12271  10898  14359    263   2396   -373       C  
ATOM   3040  CG  PHE A 501     -38.545-162.240 302.424  1.00 98.45           C  
ANISOU 3040  CG  PHE A 501    12225  10709  14474     71   2773   -345       C  
ATOM   3041  CD1 PHE A 501     -39.221-161.261 301.713  1.00 97.32           C  
ANISOU 3041  CD1 PHE A 501    11728  10703  14547     35   2815   -436       C  
ATOM   3042  CD2 PHE A 501     -38.981-162.559 303.700  1.00104.03           C  
ANISOU 3042  CD2 PHE A 501    13286  11147  15093    -69   3071   -246       C  
ATOM   3043  CE1 PHE A 501     -40.312-160.615 302.262  1.00103.14           C  
ANISOU 3043  CE1 PHE A 501    12430  11321  15438   -107   3133   -467       C  
ATOM   3044  CE2 PHE A 501     -40.074-161.918 304.254  1.00108.13           C  
ANISOU 3044  CE2 PHE A 501    13759  11579  15747   -252   3425   -273       C  
ATOM   3045  CZ  PHE A 501     -40.739-160.943 303.535  1.00107.93           C  
ANISOU 3045  CZ  PHE A 501    13344  11700  15963   -255   3450   -403       C  
ATOM   3046  N   ALA A 502     -35.105-162.327 304.043  1.00107.05           N  
ANISOU 3046  N   ALA A 502    14075  12052  14548    422   2258   -177       N  
ATOM   3047  CA  ALA A 502     -34.695-161.834 305.355  1.00108.04           C  
ANISOU 3047  CA  ALA A 502    14558  12135  14360    403   2381    -70       C  
ATOM   3048  C   ALA A 502     -33.834-160.585 305.220  1.00107.37           C  
ANISOU 3048  C   ALA A 502    14336  12393  14068    448   2248   -124       C  
ATOM   3049  O   ALA A 502     -34.030-159.603 305.946  1.00 98.50           O  
ANISOU 3049  O   ALA A 502    13301  11270  12853    348   2448    -73       O  
ATOM   3050  CB  ALA A 502     -33.947-162.926 306.119  1.00108.39           C  
ANISOU 3050  CB  ALA A 502    15024  12016  14141    546   2228     -7       C  
ATOM   3051  N   PHE A 503     -32.878-160.602 304.288  1.00112.59           N  
ANISOU 3051  N   PHE A 503    14773  13358  14650    578   1917   -246       N  
ATOM   3052  CA  PHE A 503     -32.116-159.395 303.992  1.00110.08           C  
ANISOU 3052  CA  PHE A 503    14292  13382  14153    556   1803   -309       C  
ATOM   3053  C   PHE A 503     -32.983-158.342 303.316  1.00106.62           C  
ANISOU 3053  C   PHE A 503    13579  12970  13960    392   1942   -297       C  
ATOM   3054  O   PHE A 503     -32.768-157.142 303.518  1.00108.64           O  
ANISOU 3054  O   PHE A 503    13834  13344  14102    307   1984   -282       O  
ATOM   3055  CB  PHE A 503     -30.908-159.735 303.118  1.00110.38           C  
ANISOU 3055  CB  PHE A 503    14133  13776  14032    696   1431   -476       C  
ATOM   3056  CG  PHE A 503     -29.821-160.477 303.846  1.00115.65           C  
ANISOU 3056  CG  PHE A 503    15063  14487  14393    901   1231   -541       C  
ATOM   3057  CD1 PHE A 503     -29.613-160.274 305.201  1.00117.23           C  
ANISOU 3057  CD1 PHE A 503    15638  14546  14358    921   1356   -444       C  
ATOM   3058  CD2 PHE A 503     -29.008-161.377 303.176  1.00118.04           C  
ANISOU 3058  CD2 PHE A 503    15233  14980  14635   1092    896   -722       C  
ATOM   3059  CE1 PHE A 503     -28.613-160.955 305.876  1.00117.11           C  
ANISOU 3059  CE1 PHE A 503    15885  14564  14048   1142   1136   -511       C  
ATOM   3060  CE2 PHE A 503     -28.007-162.060 303.845  1.00119.75           C  
ANISOU 3060  CE2 PHE A 503    15693  15230  14575   1326    666   -816       C  
ATOM   3061  CZ  PHE A 503     -27.810-161.848 305.196  1.00118.27           C  
ANISOU 3061  CZ  PHE A 503    15902  14885  14149   1356    779   -702       C  
ATOM   3062  N   CYS A 504     -33.965-158.766 302.517  1.00104.01           N  
ANISOU 3062  N   CYS A 504    13029  12522  13969    357   1994   -314       N  
ATOM   3063  CA  CYS A 504     -34.885-157.821 301.896  1.00102.52           C  
ANISOU 3063  CA  CYS A 504    12599  12326  14029    241   2100   -318       C  
ATOM   3064  C   CYS A 504     -35.929-157.294 302.870  1.00 97.48           C  
ANISOU 3064  C   CYS A 504    12102  11422  13516    139   2438   -259       C  
ATOM   3065  O   CYS A 504     -36.491-156.220 302.632  1.00 96.72           O  
ANISOU 3065  O   CYS A 504    11871  11329  13548     72   2501   -276       O  
ATOM   3066  CB  CYS A 504     -35.575-158.463 300.691  1.00105.93           C  
ANISOU 3066  CB  CYS A 504    12720  12753  14776    260   2022   -394       C  
ATOM   3067  SG  CYS A 504     -34.478-158.735 299.279  1.00104.90           S  
ANISOU 3067  SG  CYS A 504    12311  13025  14522    345   1624   -510       S  
ATOM   3068  N   SER A 505     -36.211-158.025 303.953  1.00 93.76           N  
ANISOU 3068  N   SER A 505    11905  10721  12998    121   2646   -202       N  
ATOM   3069  CA  SER A 505     -37.030-157.454 305.016  1.00 93.63           C  
ANISOU 3069  CA  SER A 505    12036  10522  13018      4   2977   -172       C  
ATOM   3070  C   SER A 505     -36.335-156.261 305.655  1.00 99.48           C  
ANISOU 3070  C   SER A 505    12908  11393  13495      2   2959   -148       C  
ATOM   3071  O   SER A 505     -36.999-155.321 306.107  1.00101.87           O  
ANISOU 3071  O   SER A 505    13193  11628  13884    -77   3151   -178       O  
ATOM   3072  CB  SER A 505     -37.352-158.515 306.069  1.00 83.81           C  
ANISOU 3072  CB  SER A 505    11108   9031  11706    -54   3199   -100       C  
ATOM   3073  OG  SER A 505     -38.224-159.505 305.548  1.00 76.74           O  
ANISOU 3073  OG  SER A 505    10086   7970  11101   -109   3280   -138       O  
ATOM   3074  N   MET A 506     -35.000-156.281 305.698  1.00102.62           N  
ANISOU 3074  N   MET A 506    13423  11990  13577     93   2723   -129       N  
ATOM   3075  CA  MET A 506     -34.239-155.119 306.134  1.00103.80           C  
ANISOU 3075  CA  MET A 506    13655  12303  13480     76   2672   -134       C  
ATOM   3076  C   MET A 506     -34.330-153.972 305.139  1.00 98.37           C  
ANISOU 3076  C   MET A 506    12705  11749  12922     14   2549   -180       C  
ATOM   3077  O   MET A 506     -34.120-152.815 305.520  1.00 93.03           O  
ANISOU 3077  O   MET A 506    12091  11113  12143    -47   2576   -185       O  
ATOM   3078  CB  MET A 506     -32.771-155.500 306.337  1.00110.13           C  
ANISOU 3078  CB  MET A 506    14602  13325  13917    188   2432   -151       C  
ATOM   3079  CG  MET A 506     -32.527-156.536 307.419  1.00118.93           C  
ANISOU 3079  CG  MET A 506    16057  14292  14837    281   2493    -94       C  
ATOM   3080  SD  MET A 506     -32.807-155.859 309.063  1.00127.04           S  
ANISOU 3080  SD  MET A 506    17413  15179  15678    201   2802    -27       S  
ATOM   3081  CE  MET A 506     -32.003-154.270 308.887  1.00130.22           C  
ANISOU 3081  CE  MET A 506    17678  15867  15932    161   2682   -117       C  
ATOM   3082  N   LEU A 507     -34.642-154.272 303.876  1.00 98.29           N  
ANISOU 3082  N   LEU A 507    12424  11794  13126     24   2405   -211       N  
ATOM   3083  CA  LEU A 507     -34.611-153.253 302.832  1.00 97.93           C  
ANISOU 3083  CA  LEU A 507    12174  11886  13150    -39   2238   -230       C  
ATOM   3084  C   LEU A 507     -35.741-152.246 303.003  1.00103.81           C  
ANISOU 3084  C   LEU A 507    12884  12418  14139    -90   2398   -239       C  
ATOM   3085  O   LEU A 507     -35.559-151.052 302.742  1.00109.53           O  
ANISOU 3085  O   LEU A 507    13611  13185  14819   -152   2297   -230       O  
ATOM   3086  CB  LEU A 507     -34.682-153.923 301.461  1.00 98.50           C  
ANISOU 3086  CB  LEU A 507    11973  12084  13370     -5   2042   -269       C  
ATOM   3087  CG  LEU A 507     -34.222-153.137 300.235  1.00 96.11           C  
ANISOU 3087  CG  LEU A 507    11490  12022  13004    -83   1791   -277       C  
ATOM   3088  CD1 LEU A 507     -32.785-152.678 300.404  1.00 91.69           C  
ANISOU 3088  CD1 LEU A 507    11039  11747  12052   -155   1645   -289       C  
ATOM   3089  CD2 LEU A 507     -34.365-154.001 298.995  1.00 96.20           C  
ANISOU 3089  CD2 LEU A 507    11230  12164  13159    -34   1627   -334       C  
ATOM   3090  N   CYS A 508     -36.918-152.706 303.435  1.00108.58           N  
ANISOU 3090  N   CYS A 508    13458  12794  15003    -71   2639   -277       N  
ATOM   3091  CA  CYS A 508     -38.014-151.776 303.682  1.00114.22           C  
ANISOU 3091  CA  CYS A 508    14112  13331  15954    -90   2789   -348       C  
ATOM   3092  C   CYS A 508     -37.753-150.923 304.916  1.00108.10           C  
ANISOU 3092  C   CYS A 508    13573  12507  14993   -130   2932   -348       C  
ATOM   3093  O   CYS A 508     -38.203-149.773 304.980  1.00109.14           O  
ANISOU 3093  O   CYS A 508    13680  12555  15235   -134   2932   -410       O  
ATOM   3094  CB  CYS A 508     -39.328-152.536 303.839  1.00128.67           C  
ANISOU 3094  CB  CYS A 508    15808  14983  18096    -87   3031   -442       C  
ATOM   3095  SG  CYS A 508     -39.480-153.378 305.424  1.00146.27           S  
ANISOU 3095  SG  CYS A 508    18310  17084  20182   -162   3389   -421       S  
ATOM   3096  N   LEU A 509     -37.042-151.469 305.906  1.00104.11           N  
ANISOU 3096  N   LEU A 509    13305  12045  14208   -141   3034   -292       N  
ATOM   3097  CA  LEU A 509     -36.664-150.674 307.070  1.00103.52           C  
ANISOU 3097  CA  LEU A 509    13453  11964  13915   -173   3149   -300       C  
ATOM   3098  C   LEU A 509     -35.751-149.522 306.672  1.00 99.18           C  
ANISOU 3098  C   LEU A 509    12925  11556  13204   -201   2912   -287       C  
ATOM   3099  O   LEU A 509     -35.828-148.429 307.246  1.00 96.23           O  
ANISOU 3099  O   LEU A 509    12638  11121  12805   -233   2968   -336       O  
ATOM   3100  CB  LEU A 509     -35.982-151.564 308.109  1.00101.63           C  
ANISOU 3100  CB  LEU A 509    13480  11762  13371   -160   3252   -234       C  
ATOM   3101  CG  LEU A 509     -35.467-150.866 309.367  1.00 95.06           C  
ANISOU 3101  CG  LEU A 509    12893  10963  12263   -181   3362   -247       C  
ATOM   3102  CD1 LEU A 509     -36.628-150.350 310.201  1.00 93.72           C  
ANISOU 3102  CD1 LEU A 509    12726  10622  12260   -240   3668   -338       C  
ATOM   3103  CD2 LEU A 509     -34.586-151.805 310.178  1.00 95.06           C  
ANISOU 3103  CD2 LEU A 509    13168  11032  11919   -129   3361   -172       C  
ATOM   3104  N   LEU A 510     -34.878-149.752 305.688  1.00 96.80           N  
ANISOU 3104  N   LEU A 510    12544  11454  12783   -209   2650   -239       N  
ATOM   3105  CA  LEU A 510     -34.033-148.680 305.176  1.00 94.91           C  
ANISOU 3105  CA  LEU A 510    12316  11365  12380   -297   2432   -229       C  
ATOM   3106  C   LEU A 510     -34.871-147.558 304.578  1.00 95.00           C  
ANISOU 3106  C   LEU A 510    12242  11205  12649   -334   2373   -242       C  
ATOM   3107  O   LEU A 510     -34.523-146.378 304.704  1.00103.62           O  
ANISOU 3107  O   LEU A 510    13448  12276  13648   -417   2295   -244       O  
ATOM   3108  CB  LEU A 510     -33.063-149.235 304.134  1.00 98.35           C  
ANISOU 3108  CB  LEU A 510    12635  12082  12653   -324   2182   -208       C  
ATOM   3109  CG  LEU A 510     -32.198-148.210 303.400  1.00102.11           C  
ANISOU 3109  CG  LEU A 510    13099  12754  12942   -482   1960   -199       C  
ATOM   3110  CD1 LEU A 510     -30.992-147.823 304.244  1.00107.86           C  
ANISOU 3110  CD1 LEU A 510    14003  13669  13311   -547   1957   -248       C  
ATOM   3111  CD2 LEU A 510     -31.773-148.736 302.037  1.00101.34           C  
ANISOU 3111  CD2 LEU A 510    12791  12902  12811   -524   1735   -197       C  
ATOM   3112  N   ASN A 511     -35.978-147.909 303.918  1.00 93.71           N  
ANISOU 3112  N   ASN A 511    11887  10906  12813   -265   2388   -266       N  
ATOM   3113  CA  ASN A 511     -36.876-146.889 303.385  1.00103.33           C  
ANISOU 3113  CA  ASN A 511    13029  11936  14296   -246   2303   -307       C  
ATOM   3114  C   ASN A 511     -37.413-145.996 304.497  1.00105.22           C  
ANISOU 3114  C   ASN A 511    13393  11977  14610   -218   2474   -406       C  
ATOM   3115  O   ASN A 511     -37.479-144.771 304.341  1.00108.09           O  
ANISOU 3115  O   ASN A 511    13834  12220  15014   -236   2335   -424       O  
ATOM   3116  CB  ASN A 511     -38.025-147.548 302.622  1.00111.49           C  
ANISOU 3116  CB  ASN A 511    13809  12881  15672   -146   2314   -365       C  
ATOM   3117  CG  ASN A 511     -38.821-146.558 301.794  1.00119.90           C  
ANISOU 3117  CG  ASN A 511    14784  13787  16984    -92   2127   -408       C  
ATOM   3118  OD1 ASN A 511     -38.321-145.496 301.423  1.00122.75           O  
ANISOU 3118  OD1 ASN A 511    15284  14131  17224   -161   1914   -337       O  
ATOM   3119  ND2 ASN A 511     -40.069-146.903 301.498  1.00122.91           N  
ANISOU 3119  ND2 ASN A 511    14945  14046  17709     29   2193   -536       N  
ATOM   3120  N   SER A 512     -37.794-146.590 305.632  1.00105.64           N  
ANISOU 3120  N   SER A 512    13482  11989  14668   -184   2769   -477       N  
ATOM   3121  CA  SER A 512     -38.241-145.789 306.767  1.00112.23           C  
ANISOU 3121  CA  SER A 512    14418  12687  15536   -168   2952   -601       C  
ATOM   3122  C   SER A 512     -37.123-144.907 307.303  1.00114.13           C  
ANISOU 3122  C   SER A 512    14891  13001  15473   -246   2867   -557       C  
ATOM   3123  O   SER A 512     -37.391-143.875 307.928  1.00110.47           O  
ANISOU 3123  O   SER A 512    14507  12410  15058   -234   2908   -664       O  
ATOM   3124  CB  SER A 512     -38.778-146.693 307.877  1.00121.57           C  
ANISOU 3124  CB  SER A 512    15617  13858  16717   -165   3301   -670       C  
ATOM   3125  OG  SER A 512     -39.895-147.446 307.434  1.00125.46           O  
ANISOU 3125  OG  SER A 512    15885  14276  17509   -128   3409   -747       O  
ATOM   3126  N   THR A 513     -35.867-145.295 307.074  1.00116.64           N  
ANISOU 3126  N   THR A 513    15299  13536  15482   -323   2744   -436       N  
ATOM   3127  CA  THR A 513     -34.745-144.465 307.497  1.00116.28           C  
ANISOU 3127  CA  THR A 513    15443  13598  15141   -420   2655   -423       C  
ATOM   3128  C   THR A 513     -34.543-143.280 306.559  1.00107.44           C  
ANISOU 3128  C   THR A 513    14342  12414  14065   -519   2389   -389       C  
ATOM   3129  O   THR A 513     -34.294-142.159 307.015  1.00109.46           O  
ANISOU 3129  O   THR A 513    14750  12581  14258   -582   2355   -436       O  
ATOM   3130  CB  THR A 513     -33.467-145.303 307.574  1.00118.60           C  
ANISOU 3130  CB  THR A 513    15797  14181  15085   -460   2604   -359       C  
ATOM   3131  OG1 THR A 513     -33.680-146.429 308.436  1.00120.13           O  
ANISOU 3131  OG1 THR A 513    16036  14381  15228   -363   2818   -365       O  
ATOM   3132  CG2 THR A 513     -32.314-144.469 308.112  1.00120.87           C  
ANISOU 3132  CG2 THR A 513    16254  14612  15058   -566   2537   -394       C  
ATOM   3133  N   VAL A 514     -34.659-143.505 305.247  1.00 96.88           N  
ANISOU 3133  N   VAL A 514    12873  11109  12828   -543   2192   -305       N  
ATOM   3134  CA  VAL A 514     -34.383-142.449 304.276  1.00 99.24           C  
ANISOU 3134  CA  VAL A 514    13240  11356  13109   -675   1920   -235       C  
ATOM   3135  C   VAL A 514     -35.578-141.543 304.013  1.00106.00           C  
ANISOU 3135  C   VAL A 514    14101  11869  14306   -573   1836   -285       C  
ATOM   3136  O   VAL A 514     -35.415-140.502 303.358  1.00101.57           O  
ANISOU 3136  O   VAL A 514    13677  11184  13730   -676   1596   -220       O  
ATOM   3137  CB  VAL A 514     -33.904-143.040 302.935  1.00 97.07           C  
ANISOU 3137  CB  VAL A 514    12837  11305  12742   -765   1724   -126       C  
ATOM   3138  CG1 VAL A 514     -32.746-144.000 303.165  1.00 95.88           C  
ANISOU 3138  CG1 VAL A 514    12648  11508  12276   -821   1774   -131       C  
ATOM   3139  CG2 VAL A 514     -35.052-143.730 302.217  1.00 92.41           C  
ANISOU 3139  CG2 VAL A 514    12028  10607  12477   -605   1715   -132       C  
ATOM   3140  N   ASN A 515     -36.773-141.899 304.497  1.00111.02           N  
ANISOU 3140  N   ASN A 515    14597  12346  15238   -380   2014   -415       N  
ATOM   3141  CA  ASN A 515     -37.936-141.046 304.248  1.00114.62           C  
ANISOU 3141  CA  ASN A 515    15020  12497  16033   -241   1907   -525       C  
ATOM   3142  C   ASN A 515     -37.849-139.712 304.979  1.00116.60           C  
ANISOU 3142  C   ASN A 515    15488  12545  16271   -253   1863   -611       C  
ATOM   3143  O   ASN A 515     -38.082-138.670 304.339  1.00120.78           O  
ANISOU 3143  O   ASN A 515    16137  12842  16912   -242   1587   -593       O  
ATOM   3144  CB  ASN A 515     -39.225-141.801 304.586  1.00116.67           C  
ANISOU 3144  CB  ASN A 515    15029  12694  16605    -54   2128   -698       C  
ATOM   3145  CG  ASN A 515     -39.631-142.774 303.498  1.00117.29           C  
ANISOU 3145  CG  ASN A 515    14883  12862  16819     -9   2060   -643       C  
ATOM   3146  OD1 ASN A 515     -39.175-142.673 302.357  1.00113.46           O  
ANISOU 3146  OD1 ASN A 515    14417  12437  16254    -77   1797   -495       O  
ATOM   3147  ND2 ASN A 515     -40.497-143.719 303.842  1.00121.99           N  
ANISOU 3147  ND2 ASN A 515    15264  13476  17610     82   2304   -772       N  
ATOM   3148  N   PRO A 516     -37.533-139.648 306.280  1.00115.77           N  
ANISOU 3148  N   PRO A 516    15461  12494  16031   -271   2099   -708       N  
ATOM   3149  CA  PRO A 516     -37.398-138.328 306.922  1.00119.05           C  
ANISOU 3149  CA  PRO A 516    16080  12718  16436   -288   2032   -806       C  
ATOM   3150  C   PRO A 516     -36.296-137.473 306.321  1.00117.81           C  
ANISOU 3150  C   PRO A 516    16171  12551  16040   -507   1767   -644       C  
ATOM   3151  O   PRO A 516     -36.290-136.254 306.535  1.00128.64           O  
ANISOU 3151  O   PRO A 516    17738  13683  17455   -530   1626   -705       O  
ATOM   3152  CB  PRO A 516     -37.108-138.672 308.390  1.00117.51           C  
ANISOU 3152  CB  PRO A 516    15904  12674  16072   -290   2357   -920       C  
ATOM   3153  CG  PRO A 516     -36.604-140.068 308.367  1.00112.47           C  
ANISOU 3153  CG  PRO A 516    15177  12323  15234   -342   2512   -797       C  
ATOM   3154  CD  PRO A 516     -37.350-140.736 307.257  1.00111.92           C  
ANISOU 3154  CD  PRO A 516    14905  12219  15401   -266   2423   -742       C  
ATOM   3155  N   ILE A 517     -35.364-138.068 305.578  1.00105.84           N  
ANISOU 3155  N   ILE A 517    14652  11293  14268   -684   1695   -461       N  
ATOM   3156  CA  ILE A 517     -34.379-137.277 304.853  1.00103.78           C  
ANISOU 3156  CA  ILE A 517    14606  11054  13773   -945   1448   -317       C  
ATOM   3157  C   ILE A 517     -34.955-136.782 303.528  1.00105.18           C  
ANISOU 3157  C   ILE A 517    14832  11006  14125   -946   1140   -202       C  
ATOM   3158  O   ILE A 517     -34.556-135.725 303.027  1.00110.68           O  
ANISOU 3158  O   ILE A 517    15789  11538  14725  -1131    901   -105       O  
ATOM   3159  CB  ILE A 517     -33.095-138.102 304.650  1.00111.83           C  
ANISOU 3159  CB  ILE A 517    15572  12499  14420  -1144   1503   -224       C  
ATOM   3160  CG1 ILE A 517     -32.515-138.517 306.004  1.00118.12           C  
ANISOU 3160  CG1 ILE A 517    16364  13489  15026  -1111   1763   -344       C  
ATOM   3161  CG2 ILE A 517     -32.061-137.326 303.846  1.00115.42           C  
ANISOU 3161  CG2 ILE A 517    16216  13036  14603  -1471   1276   -102       C  
ATOM   3162  CD1 ILE A 517     -31.230-139.314 305.905  1.00119.02           C  
ANISOU 3162  CD1 ILE A 517    16421  14025  14776  -1255   1786   -310       C  
ATOM   3163  N   ILE A 518     -35.912-137.513 302.956  1.00107.02           N  
ANISOU 3163  N   ILE A 518    14839  11215  14608   -747   1134   -213       N  
ATOM   3164  CA  ILE A 518     -36.471-137.136 301.661  1.00112.50           C  
ANISOU 3164  CA  ILE A 518    15569  11725  15452   -720    825   -110       C  
ATOM   3165  C   ILE A 518     -37.522-136.045 301.818  1.00116.66           C  
ANISOU 3165  C   ILE A 518    16218  11807  16299   -510    653   -236       C  
ATOM   3166  O   ILE A 518     -37.509-135.041 301.097  1.00122.06           O  
ANISOU 3166  O   ILE A 518    17167  12232  16978   -583    329   -128       O  
ATOM   3167  CB  ILE A 518     -37.048-138.375 300.950  1.00117.67           C  
ANISOU 3167  CB  ILE A 518    15910  12554  16245   -584    871   -101       C  
ATOM   3168  CG1 ILE A 518     -35.924-139.301 300.484  1.00114.29           C  
ANISOU 3168  CG1 ILE A 518    15398  12540  15488   -799    925     33       C  
ATOM   3169  CG2 ILE A 518     -37.915-137.960 299.774  1.00125.50           C  
ANISOU 3169  CG2 ILE A 518    16908  13315  17461   -466    560    -55       C  
ATOM   3170  CD1 ILE A 518     -36.417-140.581 299.847  1.00111.75           C  
ANISOU 3170  CD1 ILE A 518    14768  12395  15299   -669    977     24       C  
ATOM   3171  N   TYR A 519     -38.450-136.220 302.758  1.00116.57           N  
ANISOU 3171  N   TYR A 519    16029  11702  16561   -251    856   -481       N  
ATOM   3172  CA  TYR A 519     -39.581-135.311 302.907  1.00118.35           C  
ANISOU 3172  CA  TYR A 519    16288  11544  17135      9    692   -681       C  
ATOM   3173  C   TYR A 519     -39.383-134.294 304.026  1.00117.05           C  
ANISOU 3173  C   TYR A 519    16323  11193  16959      6    735   -828       C  
ATOM   3174  O   TYR A 519     -39.514-133.089 303.794  1.00116.06           O  
ANISOU 3174  O   TYR A 519    16463  10716  16919     36    431   -839       O  
ATOM   3175  CB  TYR A 519     -40.865-136.113 303.151  1.00119.93           C  
ANISOU 3175  CB  TYR A 519    16112  11784  17674    298    879   -926       C  
ATOM   3176  CG  TYR A 519     -41.120-137.183 302.112  1.00121.94           C  
ANISOU 3176  CG  TYR A 519    16138  12226  17968    314    858   -819       C  
ATOM   3177  CD1 TYR A 519     -41.761-136.881 300.918  1.00123.36           C  
ANISOU 3177  CD1 TYR A 519    16312  12231  18329    448    517   -787       C  
ATOM   3178  CD2 TYR A 519     -40.716-138.495 302.326  1.00123.68           C  
ANISOU 3178  CD2 TYR A 519    16163  12787  18041    210   1156   -758       C  
ATOM   3179  CE1 TYR A 519     -41.993-137.856 299.965  1.00126.30           C  
ANISOU 3179  CE1 TYR A 519    16459  12792  18737    466    497   -709       C  
ATOM   3180  CE2 TYR A 519     -40.945-139.477 301.380  1.00124.39           C  
ANISOU 3180  CE2 TYR A 519    16039  13040  18182    228   1129   -682       C  
ATOM   3181  CZ  TYR A 519     -41.583-139.152 300.202  1.00127.57           C  
ANISOU 3181  CZ  TYR A 519    16409  13294  18768    351    809   -664       C  
ATOM   3182  OH  TYR A 519     -41.812-140.128 299.258  1.00129.48           O  
ANISOU 3182  OH  TYR A 519    16421  13715  19060    373    781   -609       O  
ATOM   3183  N   ALA A 520     -39.073-134.758 305.239  1.00116.87           N  
ANISOU 3183  N   ALA A 520    16194  11386  16824    -27   1093   -944       N  
ATOM   3184  CA  ALA A 520     -38.960-133.846 306.374  1.00117.03           C  
ANISOU 3184  CA  ALA A 520    16360  11260  16845     -7   1159  -1126       C  
ATOM   3185  C   ALA A 520     -37.779-132.899 306.214  1.00120.73           C  
ANISOU 3185  C   ALA A 520    17195  11640  17036   -283    963   -952       C  
ATOM   3186  O   ALA A 520     -37.891-131.704 306.511  1.00130.99           O  
ANISOU 3186  O   ALA A 520    18717  12619  18434   -248    783  -1059       O  
ATOM   3187  CB  ALA A 520     -38.840-134.636 307.676  1.00116.84           C  
ANISOU 3187  CB  ALA A 520    16158  11525  16711     -2   1588  -1266       C  
ATOM   3188  N   LEU A 521     -36.638-133.411 305.751  1.00114.22           N  
ANISOU 3188  N   LEU A 521    16430  11102  15866   -568    994   -712       N  
ATOM   3189  CA  LEU A 521     -35.479-132.548 305.545  1.00115.51           C  
ANISOU 3189  CA  LEU A 521    16919  11229  15741   -887    831   -566       C  
ATOM   3190  C   LEU A 521     -35.729-131.549 304.423  1.00121.49           C  
ANISOU 3190  C   LEU A 521    17958  11609  16594   -948    418   -425       C  
ATOM   3191  O   LEU A 521     -35.265-130.405 304.489  1.00124.52           O  
ANISOU 3191  O   LEU A 521    18677  11743  16894  -1122    236   -395       O  
ATOM   3192  CB  LEU A 521     -34.240-133.390 305.250  1.00109.48           C  
ANISOU 3192  CB  LEU A 521    16099  10913  14586  -1169    955   -395       C  
ATOM   3193  CG  LEU A 521     -32.924-132.626 305.099  1.00110.01           C  
ANISOU 3193  CG  LEU A 521    16445  11050  14306  -1555    848   -288       C  
ATOM   3194  CD1 LEU A 521     -32.526-131.978 306.418  1.00115.47           C  
ANISOU 3194  CD1 LEU A 521    17243  11698  14933  -1573    994   -475       C  
ATOM   3195  CD2 LEU A 521     -31.825-133.546 304.592  1.00105.31           C  
ANISOU 3195  CD2 LEU A 521    15725  10934  13354  -1799    932   -163       C  
ATOM   3196  N   ARG A 522     -36.462-131.962 303.387  1.00123.02           N  
ANISOU 3196  N   ARG A 522    18044  11744  16953   -811    255   -336       N  
ATOM   3197  CA  ARG A 522     -36.797-131.062 302.290  1.00124.47           C  
ANISOU 3197  CA  ARG A 522    18518  11552  17223   -831   -168   -194       C  
ATOM   3198  C   ARG A 522     -37.872-130.051 302.662  1.00124.30           C  
ANISOU 3198  C   ARG A 522    18619  11036  17575   -508   -384   -412       C  
ATOM   3199  O   ARG A 522     -38.098-129.106 301.898  1.00129.96           O  
ANISOU 3199  O   ARG A 522    19669  11356  18355   -511   -783   -305       O  
ATOM   3200  CB  ARG A 522     -37.248-131.866 301.070  1.00126.13           C  
ANISOU 3200  CB  ARG A 522    18554  11887  17482   -761   -282    -53       C  
ATOM   3201  N   SER A 523     -38.535-130.223 303.803  1.00118.39           N  
ANISOU 3201  N   SER A 523    17620  10302  17060   -232   -147   -725       N  
ATOM   3202  CA  SER A 523     -39.558-129.280 304.244  1.00120.88           C  
ANISOU 3202  CA  SER A 523    17994  10195  17738     98   -340  -1008       C  
ATOM   3203  C   SER A 523     -38.895-127.988 304.702  1.00121.80           C  
ANISOU 3203  C   SER A 523    18521  10009  17749    -73   -505  -1005       C  
ATOM   3204  O   SER A 523     -38.204-127.963 305.726  1.00120.87           O  
ANISOU 3204  O   SER A 523    18388  10074  17462   -221   -232  -1089       O  
ATOM   3205  CB  SER A 523     -40.395-129.888 305.365  1.00120.38           C  
ANISOU 3205  CB  SER A 523    17517  10312  17909    385      8  -1368       C  
ATOM   3206  OG  SER A 523     -41.271-128.922 305.923  1.00123.15           O  
ANISOU 3206  OG  SER A 523    17899  10306  18584    688   -158  -1703       O  
ATOM   3207  N   LYS A 524     -39.103-126.911 303.942  1.00122.83           N  
ANISOU 3207  N   LYS A 524    19038   9661  17971    -53   -965   -911       N  
ATOM   3208  CA  LYS A 524     -38.532-125.624 304.321  1.00124.24           C  
ANISOU 3208  CA  LYS A 524    19649   9482  18076   -223  -1160   -910       C  
ATOM   3209  C   LYS A 524     -39.085-125.141 305.655  1.00125.83           C  
ANISOU 3209  C   LYS A 524    19714   9555  18542     67  -1042  -1329       C  
ATOM   3210  O   LYS A 524     -38.373-124.478 306.417  1.00130.33           O  
ANISOU 3210  O   LYS A 524    20478  10061  18981   -120   -977  -1387       O  
ATOM   3211  CB  LYS A 524     -38.798-124.591 303.225  1.00125.08           C  
ANISOU 3211  CB  LYS A 524    20233   9038  18256   -220  -1715   -730       C  
ATOM   3212  CG  LYS A 524     -38.040-123.288 303.399  1.00127.04           C  
ANISOU 3212  CG  LYS A 524    21016   8892  18360   -507  -1942   -642       C  
ATOM   3213  N   ASP A 525     -40.343-125.470 305.959  1.00124.70           N  
ANISOU 3213  N   ASP A 525    19215   9405  18762    508  -1003  -1651       N  
ATOM   3214  CA  ASP A 525     -40.938-125.025 307.216  1.00129.20           C  
ANISOU 3214  CA  ASP A 525    19614   9896  19581    787   -883  -2095       C  
ATOM   3215  C   ASP A 525     -40.368-125.790 308.404  1.00120.54           C  
ANISOU 3215  C   ASP A 525    18232   9297  18269    632   -340  -2188       C  
ATOM   3216  O   ASP A 525     -40.140-125.207 309.471  1.00115.56           O  
ANISOU 3216  O   ASP A 525    17643   8630  17633    633   -231  -2415       O  
ATOM   3217  CB  ASP A 525     -42.459-125.176 307.162  1.00137.84           C  
ANISOU 3217  CB  ASP A 525    20375  10889  21109   1280   -989  -2454       C  
ATOM   3218  CG  ASP A 525     -43.108-124.213 306.188  1.00150.99           C  
ANISOU 3218  CG  ASP A 525    22352  11992  23026   1526  -1592  -2455       C  
ATOM   3219  OD1 ASP A 525     -42.566-123.105 305.992  1.00162.32           O  
ANISOU 3219  OD1 ASP A 525    24287  13001  24387   1389  -1932  -2316       O  
ATOM   3220  OD2 ASP A 525     -44.165-124.565 305.622  1.00150.69           O  
ANISOU 3220  OD2 ASP A 525    22073  11927  23254   1855  -1737  -2602       O  
ATOM   3221  N   LEU A 526     -40.134-127.096 308.244  1.00115.37           N  
ANISOU 3221  N   LEU A 526    17304   9101  17432    509    -14  -2022       N  
ATOM   3222  CA  LEU A 526     -39.603-127.888 309.350  1.00108.85           C  
ANISOU 3222  CA  LEU A 526    16248   8729  16380    381    471  -2090       C  
ATOM   3223  C   LEU A 526     -38.209-127.421 309.747  1.00108.09           C  
ANISOU 3223  C   LEU A 526    16443   8700  15927     26    518  -1933       C  
ATOM   3224  O   LEU A 526     -37.913-127.277 310.940  1.00106.38           O  
ANISOU 3224  O   LEU A 526    16172   8624  15625     13    759  -2135       O  
ATOM   3225  CB  LEU A 526     -39.586-129.371 308.979  1.00100.64           C  
ANISOU 3225  CB  LEU A 526    14919   8106  15213    319    745  -1917       C  
ATOM   3226  CG  LEU A 526     -40.927-130.104 309.047  1.00 97.30           C  
ANISOU 3226  CG  LEU A 526    14098   7769  15103    633    886  -2160       C  
ATOM   3227  CD1 LEU A 526     -40.760-131.542 308.599  1.00100.35           C  
ANISOU 3227  CD1 LEU A 526    14265   8527  15338    520   1125  -1947       C  
ATOM   3228  CD2 LEU A 526     -41.507-130.049 310.452  1.00 91.23           C  
ANISOU 3228  CD2 LEU A 526    13105   7105  14454    800   1186  -2560       C  
ATOM   3229  N   ARG A 527     -37.340-127.174 308.762  1.00108.88           N  
ANISOU 3229  N   ARG A 527    16843   8724  15801   -278    296  -1594       N  
ATOM   3230  CA  ARG A 527     -36.000-126.685 309.067  1.00107.30           C  
ANISOU 3230  CA  ARG A 527    16908   8603  15259   -651    331  -1474       C  
ATOM   3231  C   ARG A 527     -36.046-125.349 309.796  1.00111.09           C  
ANISOU 3231  C   ARG A 527    17631   8703  15874   -601    173  -1708       C  
ATOM   3232  O   ARG A 527     -35.177-125.066 310.629  1.00112.65           O  
ANISOU 3232  O   ARG A 527    17900   9048  15854   -797    340  -1782       O  
ATOM   3233  CB  ARG A 527     -35.177-126.571 307.784  1.00109.76           C  
ANISOU 3233  CB  ARG A 527    17498   8885  15319  -1010    100  -1101       C  
ATOM   3234  CG  ARG A 527     -34.830-127.914 307.159  1.00111.28           C  
ANISOU 3234  CG  ARG A 527    17442   9535  15303  -1120    286   -889       C  
ATOM   3235  CD  ARG A 527     -34.002-127.750 305.894  1.00113.64           C  
ANISOU 3235  CD  ARG A 527    18000   9847  15330  -1501     64   -557       C  
ATOM   3236  NE  ARG A 527     -34.776-127.157 304.807  1.00119.48           N  
ANISOU 3236  NE  ARG A 527    18964  10150  16282  -1402   -333   -430       N  
ATOM   3237  CZ  ARG A 527     -34.287-126.898 303.600  1.00127.27           C  
ANISOU 3237  CZ  ARG A 527    20224  11068  17063  -1710   -582   -132       C  
ATOM   3238  NH1 ARG A 527     -35.064-126.357 302.670  1.00133.03           N  
ANISOU 3238  NH1 ARG A 527    21181  11377  17986  -1577   -965    -24       N  
ATOM   3239  NH2 ARG A 527     -33.020-127.177 303.321  1.00128.93           N  
ANISOU 3239  NH2 ARG A 527    20480  11646  16859  -2151   -455     37       N  
ATOM   3240  N   HIS A 528     -37.048-124.518 309.499  1.00112.44           N  
ANISOU 3240  N   HIS A 528    17927   8386  16408   -321   -166  -1851       N  
ATOM   3241  CA  HIS A 528     -37.240-123.292 310.266  1.00116.08           C  
ANISOU 3241  CA  HIS A 528    18579   8470  17054   -200   -328  -2139       C  
ATOM   3242  C   HIS A 528     -37.613-123.605 311.709  1.00110.25           C  
ANISOU 3242  C   HIS A 528    17478   8012  16399     23     42  -2529       C  
ATOM   3243  O   HIS A 528     -37.141-122.940 312.639  1.00109.69           O  
ANISOU 3243  O   HIS A 528    17507   7907  16263    -49    110  -2717       O  
ATOM   3244  CB  HIS A 528     -38.317-122.425 309.614  1.00129.62           C  
ANISOU 3244  CB  HIS A 528    20484   9606  19161    118   -807  -2244       C  
ATOM   3245  CG  HIS A 528     -38.012-122.035 308.200  1.00137.62           C  
ANISOU 3245  CG  HIS A 528    21913  10298  20076    -98  -1206  -1853       C  
ATOM   3246  ND1 HIS A 528     -36.787-122.263 307.611  1.00139.99           N  
ANISOU 3246  ND1 HIS A 528    22424  10802  19962   -594  -1138  -1468       N  
ATOM   3247  CD2 HIS A 528     -38.776-121.434 307.257  1.00142.52           C  
ANISOU 3247  CD2 HIS A 528    22785  10425  20939    111  -1684  -1799       C  
ATOM   3248  CE1 HIS A 528     -36.809-121.818 306.367  1.00143.87           C  
ANISOU 3248  CE1 HIS A 528    23287  10949  20430   -716  -1534  -1179       C  
ATOM   3249  NE2 HIS A 528     -38.004-121.310 306.128  1.00144.99           N  
ANISOU 3249  NE2 HIS A 528    23480  10646  20962   -284  -1883  -1356       N  
ATOM   3250  N   ALA A 529     -38.458-124.618 311.915  1.00110.08           N  
ANISOU 3250  N   ALA A 529    17041   8280  16506    272    291  -2660       N  
ATOM   3251  CA  ALA A 529     -38.851-124.995 313.267  1.00107.64           C  
ANISOU 3251  CA  ALA A 529    16392   8270  16235    443    672  -3015       C  
ATOM   3252  C   ALA A 529     -37.701-125.641 314.027  1.00106.70           C  
ANISOU 3252  C   ALA A 529    16235   8611  15693    153   1055  -2894       C  
ATOM   3253  O   ALA A 529     -37.626-125.518 315.255  1.00105.28           O  
ANISOU 3253  O   ALA A 529    15946   8601  15454    200   1297  -3163       O  
ATOM   3254  CB  ALA A 529     -40.054-125.936 313.222  1.00103.53           C  
ANISOU 3254  CB  ALA A 529    15459   7938  15939    727    848  -3174       C  
ATOM   3255  N   PHE A 530     -36.802-126.331 313.320  1.00107.76           N  
ANISOU 3255  N   PHE A 530    16451   8968  15526   -132   1100  -2518       N  
ATOM   3256  CA  PHE A 530     -35.642-126.919 313.981  1.00110.90           C  
ANISOU 3256  CA  PHE A 530    16825   9797  15515   -384   1405  -2423       C  
ATOM   3257  C   PHE A 530     -34.677-125.842 314.463  1.00116.12           C  
ANISOU 3257  C   PHE A 530    17769  10338  16014   -601   1307  -2487       C  
ATOM   3258  O   PHE A 530     -34.129-125.941 315.567  1.00116.00           O  
ANISOU 3258  O   PHE A 530    17685  10599  15791   -649   1563  -2642       O  
ATOM   3259  CB  PHE A 530     -34.934-127.890 313.039  1.00111.00           C  
ANISOU 3259  CB  PHE A 530    16832  10078  15266   -611   1435  -2056       C  
ATOM   3260  CG  PHE A 530     -33.665-128.462 313.604  1.00115.59           C  
ANISOU 3260  CG  PHE A 530    17404  11095  15422   -852   1681  -1974       C  
ATOM   3261  CD1 PHE A 530     -33.678-129.161 314.800  1.00111.24           C  
ANISOU 3261  CD1 PHE A 530    16650  10872  14743   -738   2030  -2140       C  
ATOM   3262  CD2 PHE A 530     -32.461-128.310 312.934  1.00121.47           C  
ANISOU 3262  CD2 PHE A 530    18343  11935  15875  -1195   1556  -1750       C  
ATOM   3263  CE1 PHE A 530     -32.513-129.692 315.324  1.00109.59           C  
ANISOU 3263  CE1 PHE A 530    16448  11054  14138   -916   2213  -2082       C  
ATOM   3264  CE2 PHE A 530     -31.291-128.840 313.451  1.00120.89           C  
ANISOU 3264  CE2 PHE A 530    18228  12288  15415  -1384   1757  -1729       C  
ATOM   3265  CZ  PHE A 530     -31.318-129.532 314.648  1.00114.87           C  
ANISOU 3265  CZ  PHE A 530    17277  11826  14542  -1221   2069  -1895       C  
ATOM   3266  N   ARG A 531     -34.455-124.806 313.651  1.00116.34           N  
ANISOU 3266  N   ARG A 531    18133   9950  16119   -745    933  -2371       N  
ATOM   3267  CA  ARG A 531     -33.573-123.727 314.075  1.00112.64           C  
ANISOU 3267  CA  ARG A 531    17955   9326  15517   -982    830  -2444       C  
ATOM   3268  C   ARG A 531     -34.204-122.898 315.185  1.00117.88           C  
ANISOU 3268  C   ARG A 531    18583   9772  16435   -716    829  -2857       C  
ATOM   3269  O   ARG A 531     -33.487-122.324 316.013  1.00119.75           O  
ANISOU 3269  O   ARG A 531    18916  10061  16523   -856    905  -3016       O  
ATOM   3270  CB  ARG A 531     -33.209-122.844 312.881  1.00114.97           C  
ANISOU 3270  CB  ARG A 531    18667   9199  15816  -1245    426  -2192       C  
ATOM   3271  CG  ARG A 531     -32.090-121.854 313.165  1.00118.92           C  
ANISOU 3271  CG  ARG A 531    19490   9590  16106  -1610    347  -2208       C  
ATOM   3272  CD  ARG A 531     -31.470-121.338 311.880  1.00117.28           C  
ANISOU 3272  CD  ARG A 531    19678   9131  15750  -2009     46  -1869       C  
ATOM   3273  NE  ARG A 531     -30.108-120.860 312.094  1.00103.60           N  
ANISOU 3273  NE  ARG A 531    18146   7545  13674  -2479    110  -1842       N  
ATOM   3274  CZ  ARG A 531     -29.234-120.637 311.117  1.00104.20           C  
ANISOU 3274  CZ  ARG A 531    18497   7617  13478  -2953    -21  -1559       C  
ATOM   3275  NH1 ARG A 531     -28.014-120.205 311.404  1.00105.08           N  
ANISOU 3275  NH1 ARG A 531    18744   7902  13281  -3386     68  -1599       N  
ATOM   3276  NH2 ARG A 531     -29.578-120.851 309.853  1.00104.13           N  
ANISOU 3276  NH2 ARG A 531    18616   7458  13492  -3009   -232  -1257       N  
ATOM   3277  N   SER A 532     -35.538-122.831 315.226  1.00121.01           N  
ANISOU 3277  N   SER A 532    18814   9953  17212   -330    744  -3072       N  
ATOM   3278  CA  SER A 532     -36.219-122.110 316.295  1.00127.31           C  
ANISOU 3278  CA  SER A 532    19514  10597  18261    -47    754  -3524       C  
ATOM   3279  C   SER A 532     -36.035-122.782 317.649  1.00127.79           C  
ANISOU 3279  C   SER A 532    19266  11171  18116    -13   1218  -3744       C  
ATOM   3280  O   SER A 532     -36.262-122.141 318.681  1.00129.60           O  
ANISOU 3280  O   SER A 532    19436  11360  18444    128   1273  -4118       O  
ATOM   3281  CB  SER A 532     -37.709-121.980 315.979  1.00129.95           C  
ANISOU 3281  CB  SER A 532    19685  10650  19040    367    562  -3746       C  
ATOM   3282  OG  SER A 532     -38.338-123.250 315.966  1.00128.13           O  
ANISOU 3282  OG  SER A 532    19074  10801  18809    499    859  -3726       O  
ATOM   3283  N   MET A 533     -35.633-124.057 317.666  1.00125.00           N  
ANISOU 3283  N   MET A 533    18732  11290  17472   -133   1536  -3525       N  
ATOM   3284  CA  MET A 533     -35.344-124.740 318.922  1.00123.27           C  
ANISOU 3284  CA  MET A 533    18293  11549  16994   -130   1955  -3678       C  
ATOM   3285  C   MET A 533     -34.169-124.115 319.666  1.00119.15           C  
ANISOU 3285  C   MET A 533    17950  11127  16196   -346   1993  -3754       C  
ATOM   3286  O   MET A 533     -34.081-124.258 320.890  1.00114.76           O  
ANISOU 3286  O   MET A 533    17250  10860  15494   -280   2266  -3999       O  
ATOM   3287  CB  MET A 533     -35.056-126.220 318.660  1.00128.52           C  
ANISOU 3287  CB  MET A 533    18804  12634  17392   -223   2217  -3387       C  
ATOM   3288  CG  MET A 533     -36.154-126.969 317.914  1.00134.34           C  
ANISOU 3288  CG  MET A 533    19344  13322  18376    -42   2214  -3304       C  
ATOM   3289  SD  MET A 533     -37.444-127.615 318.996  1.00138.37           S  
ANISOU 3289  SD  MET A 533    19473  14066  19036    240   2581  -3661       S  
ATOM   3290  CE  MET A 533     -36.486-128.677 320.074  1.00135.43           C  
ANISOU 3290  CE  MET A 533    19066  14240  18151     64   3008  -3558       C  
ATOM   3291  N   PHE A 534     -33.260-123.415 318.954  1.00122.58           N  
ANISOU 3291  N   PHE A 534    18697  11339  16539   -625   1727  -3561       N  
ATOM   3292  CA  PHE A 534     -32.038-122.803 319.454  1.00126.76           C  
ANISOU 3292  CA  PHE A 534    19410  11956  16798   -897   1733  -3612       C  
ATOM   3293  C   PHE A 534     -32.294-121.378 319.947  1.00134.84           C  
ANISOU 3293  C   PHE A 534    20601  12558  18073   -821   1519  -3936       C  
ATOM   3294  O   PHE A 534     -33.202-120.697 319.457  1.00138.51           O  
ANISOU 3294  O   PHE A 534    21164  12547  18916   -635   1231  -4014       O  
ATOM   3295  CB  PHE A 534     -30.975-122.782 318.359  1.00126.10           C  
ANISOU 3295  CB  PHE A 534    19567  11856  16487  -1283   1565  -3258       C  
ATOM   3296  CG  PHE A 534     -30.674-124.137 317.782  1.00127.96           C  
ANISOU 3296  CG  PHE A 534    19643  12489  16488  -1354   1728  -2962       C  
ATOM   3297  CD1 PHE A 534     -30.294-124.271 316.456  1.00130.57           C  
ANISOU 3297  CD1 PHE A 534    20121  12737  16753  -1592   1534  -2631       C  
ATOM   3298  CD2 PHE A 534     -30.763-125.275 318.567  1.00124.98           C  
ANISOU 3298  CD2 PHE A 534    18984  12561  15942  -1190   2066  -3018       C  
ATOM   3299  CE1 PHE A 534     -30.014-125.515 315.925  1.00125.66           C  
ANISOU 3299  CE1 PHE A 534    19332  12485  15927  -1641   1668  -2394       C  
ATOM   3300  CE2 PHE A 534     -30.485-126.519 318.042  1.00118.46           C  
ANISOU 3300  CE2 PHE A 534    18032  12061  14916  -1239   2186  -2759       C  
ATOM   3301  CZ  PHE A 534     -30.109-126.640 316.720  1.00119.38           C  
ANISOU 3301  CZ  PHE A 534    18262  12105  14995  -1452   1985  -2463       C  
ATOM   3302  N   PRO A 535     -31.498-120.910 320.923  1.00136.33           N  
ANISOU 3302  N   PRO A 535    20826  12912  18062   -943   1636  -4151       N  
ATOM   3303  CA  PRO A 535     -31.685-119.548 321.444  1.00141.59           C  
ANISOU 3303  CA  PRO A 535    21651  13179  18967   -877   1431  -4488       C  
ATOM   3304  C   PRO A 535     -31.381-118.471 320.416  1.00143.26           C  
ANISOU 3304  C   PRO A 535    22284  12825  19323  -1112   1009  -4322       C  
ATOM   3305  O   PRO A 535     -30.942-118.762 319.297  1.00139.53           O  
ANISOU 3305  O   PRO A 535    21981  12311  18725  -1368    894  -3940       O  
ATOM   3306  CB  PRO A 535     -30.703-119.483 322.624  1.00139.23           C  
ANISOU 3306  CB  PRO A 535    21287  13275  18340  -1014   1682  -4699       C  
ATOM   3307  CG  PRO A 535     -30.428-120.926 322.981  1.00131.87           C  
ANISOU 3307  CG  PRO A 535    20086  12954  17063   -993   2051  -4556       C  
ATOM   3308  CD  PRO A 535     -30.491-121.667 321.688  1.00131.12           C  
ANISOU 3308  CD  PRO A 535    20031  12826  16961  -1089   1963  -4142       C  
ATOM   3309  N   SER A 536     -31.641-117.220 320.775  1.00146.93           N  
ANISOU 3309  N   SER A 536    22937  12841  20051  -1030    765  -4613       N  
ATOM   3310  CA  SER A 536     -31.365-116.095 319.888  1.00149.82           C  
ANISOU 3310  CA  SER A 536    23775  12600  20552  -1267    339  -4469       C  
ATOM   3311  C   SER A 536     -30.889-114.857 320.640  1.00151.93           C  
ANISOU 3311  C   SER A 536    24253  12600  20874  -1376    217  -4789       C  
ATOM   3312  O   SER A 536     -29.927-114.911 321.401  1.00150.59           O  
ANISOU 3312  O   SER A 536    24003  12809  20405  -1596    464  -4903       O  
ATOM   3313  CB  SER A 536     -32.608-115.742 319.075  1.00151.29           C  
ANISOU 3313  CB  SER A 536    24080  12239  21163   -956    -29  -4438       C  
ATOM   3314  OG  SER A 536     -33.694-115.354 319.904  1.00153.18           O  
ANISOU 3314  OG  SER A 536    24106  12336  21760   -489    -68  -4902       O  
TER    3315      SER A 536                                                      
HETATM 3316  N1  FMN A1201     -41.524-105.577 248.200  1.00103.11           N  
HETATM 3317  C2  FMN A1201     -42.286-104.876 249.091  1.00 99.93           C  
HETATM 3318  O2  FMN A1201     -41.831-104.493 250.175  1.00102.21           O  
HETATM 3319  N3  FMN A1201     -43.601-104.572 248.786  1.00 98.24           N  
HETATM 3320  C4  FMN A1201     -44.264-104.913 247.623  1.00100.58           C  
HETATM 3321  O4  FMN A1201     -45.442-104.589 247.464  1.00 99.33           O  
HETATM 3322  C4A FMN A1201     -43.449-105.654 246.677  1.00103.17           C  
HETATM 3323  N5  FMN A1201     -43.985-106.006 245.544  1.00104.85           N  
HETATM 3324  C5A FMN A1201     -43.197-106.696 244.634  1.00102.47           C  
HETATM 3325  C6  FMN A1201     -43.747-107.046 243.401  1.00 99.98           C  
HETATM 3326  C7  FMN A1201     -42.987-107.703 242.439  1.00102.62           C  
HETATM 3327  C7M FMN A1201     -43.612-108.058 241.115  1.00 99.45           C  
HETATM 3328  C8  FMN A1201     -41.646-108.023 242.714  1.00106.12           C  
HETATM 3329  C8M FMN A1201     -40.785-108.703 241.683  1.00109.73           C  
HETATM 3330  C9  FMN A1201     -41.100-107.688 243.950  1.00104.42           C  
HETATM 3331  C9A FMN A1201     -41.861-107.026 244.907  1.00104.23           C  
HETATM 3332  N10 FMN A1201     -41.323-106.637 246.150  1.00106.27           N  
HETATM 3333  C10 FMN A1201     -42.084-105.942 247.059  1.00103.91           C  
HETATM 3334  C1' FMN A1201     -39.934-106.982 246.482  1.00111.98           C  
HETATM 3335  C2' FMN A1201     -39.803-108.332 247.178  1.00116.67           C  
HETATM 3336  O2' FMN A1201     -40.592-108.352 248.368  1.00118.84           O  
HETATM 3337  C3' FMN A1201     -38.342-108.608 247.537  1.00117.59           C  
HETATM 3338  O3' FMN A1201     -37.653-109.021 246.362  1.00110.63           O  
HETATM 3339  C4' FMN A1201     -38.192-109.700 248.597  1.00122.32           C  
HETATM 3340  O4' FMN A1201     -36.855-109.703 249.099  1.00123.68           O  
HETATM 3341  C5' FMN A1201     -38.569-111.076 248.092  1.00125.45           C  
HETATM 3342  O5' FMN A1201     -38.536-111.992 249.206  1.00126.52           O  
HETATM 3343  P   FMN A1201     -38.423-113.582 249.070  1.00118.69           P  
HETATM 3344  O1P FMN A1201     -39.471-114.088 248.141  1.00111.49           O  
HETATM 3345  O2P FMN A1201     -38.558-114.135 250.494  1.00114.43           O1-
HETATM 3346  O3P FMN A1201     -37.006-113.878 248.581  1.00117.28           O1-
HETATM 3347  C1  8D0 A1202     -42.678-157.964 308.565  1.00 90.95           C  
HETATM 3348  C2  8D0 A1202     -42.185-157.808 307.250  1.00 98.68           C  
HETATM 3349  C3  8D0 A1202     -41.225-158.728 306.787  1.00 94.79           C  
HETATM 3350  C4  8D0 A1202     -40.767-159.781 307.599  1.00 89.59           C  
HETATM 3351  C5  8D0 A1202     -41.266-159.937 308.922  1.00 85.94           C  
HETATM 3352  N1  8D0 A1202     -49.883-159.610 305.995  1.00 81.39           N  
HETATM 3353  C10 8D0 A1202     -40.860-162.472 309.213  1.00 96.19           C  
HETATM 3354  C11 8D0 A1202     -40.386-163.598 310.154  1.00 97.07           C  
HETATM 3355  C12 8D0 A1202     -41.153-163.564 311.492  1.00 93.82           C  
HETATM 3356  C13 8D0 A1202     -41.128-162.161 312.122  1.00 89.63           C  
HETATM 3357  C14 8D0 A1202     -40.513-164.953 309.434  1.00 96.61           C  
HETATM 3358  C15 8D0 A1202     -40.887-158.894 312.040  1.00 84.60           C  
HETATM 3359  C16 8D0 A1202     -43.037-159.836 312.927  1.00 79.15           C  
HETATM 3360  C17 8D0 A1202     -42.646-156.676 306.315  1.00101.71           C  
HETATM 3361  C18 8D0 A1202     -43.870-157.135 305.473  1.00100.83           C  
HETATM 3362  C19 8D0 A1202     -41.528-156.222 305.351  1.00 99.49           C  
HETATM 3363  C20 8D0 A1202     -43.035-155.439 307.155  1.00101.39           C  
HETATM 3364  C21 8D0 A1202     -45.148-157.478 306.270  1.00102.24           C  
HETATM 3365  C22 8D0 A1202     -46.437-157.247 305.470  1.00105.85           C  
HETATM 3366  C23 8D0 A1202     -46.680-158.341 304.420  1.00104.32           C  
HETATM 3367  C24 8D0 A1202     -48.121-158.874 304.455  1.00 98.97           C  
HETATM 3368  C25 8D0 A1202     -48.463-159.601 305.766  1.00 92.44           C  
HETATM 3369  C6  8D0 A1202     -42.235-159.011 309.392  1.00 83.40           C  
HETATM 3370  C7  8D0 A1202     -40.823-161.065 309.859  1.00 92.80           C  
HETATM 3371  C8  8D0 A1202     -41.720-161.149 311.119  1.00 92.27           C  
HETATM 3372  C9  8D0 A1202     -42.113-159.763 311.692  1.00 84.95           C  
HETATM 3373  O1  8D0 A1202     -42.791-159.059 310.652  1.00 79.91           O  
HETATM 3374  O2  8D0 A1202     -40.569-164.744 308.038  1.00 92.58           O  
HETATM 3375  O3  8D0 A1202     -39.835-160.613 307.049  1.00 93.50           O  
HETATM 3376  C1  CLR A1203     -51.283-139.354 312.194  1.00104.94           C  
HETATM 3377  C2  CLR A1203     -51.296-137.964 311.555  1.00106.12           C  
HETATM 3378  C3  CLR A1203     -52.374-137.926 310.475  1.00111.00           C  
HETATM 3379  C4  CLR A1203     -53.740-138.044 311.153  1.00109.48           C  
HETATM 3380  C5  CLR A1203     -53.772-139.350 311.932  1.00108.48           C  
HETATM 3381  C6  CLR A1203     -54.886-140.019 311.945  1.00105.75           C  
HETATM 3382  C7  CLR A1203     -55.015-141.395 312.535  1.00103.28           C  
HETATM 3383  C8  CLR A1203     -54.037-141.599 313.700  1.00102.53           C  
HETATM 3384  C9  CLR A1203     -52.637-141.114 313.309  1.00103.50           C  
HETATM 3385  C10 CLR A1203     -52.633-139.664 312.854  1.00104.07           C  
HETATM 3386  C11 CLR A1203     -51.651-141.330 314.453  1.00103.39           C  
HETATM 3387  C12 CLR A1203     -51.567-142.817 314.829  1.00102.10           C  
HETATM 3388  C13 CLR A1203     -52.957-143.374 315.166  1.00102.64           C  
HETATM 3389  C14 CLR A1203     -53.901-143.093 313.957  1.00103.60           C  
HETATM 3390  C15 CLR A1203     -55.176-143.824 314.389  1.00102.58           C  
HETATM 3391  C16 CLR A1203     -54.604-145.156 314.943  1.00102.20           C  
HETATM 3392  C17 CLR A1203     -53.114-144.895 315.301  1.00102.97           C  
HETATM 3393  C18 CLR A1203     -53.538-142.665 316.395  1.00102.22           C  
HETATM 3394  C19 CLR A1203     -52.773-138.782 314.098  1.00 97.24           C  
HETATM 3395  C20 CLR A1203     -52.820-145.459 316.703  1.00102.51           C  
HETATM 3396  C21 CLR A1203     -51.333-145.391 317.065  1.00100.76           C  
HETATM 3397  C22 CLR A1203     -53.230-146.935 316.743  1.00106.68           C  
HETATM 3398  C23 CLR A1203     -52.374-147.741 315.760  1.00110.60           C  
HETATM 3399  C24 CLR A1203     -51.804-148.987 316.443  1.00109.92           C  
HETATM 3400  C25 CLR A1203     -51.618-150.104 315.414  1.00102.80           C  
HETATM 3401  C26 CLR A1203     -50.863-151.267 316.062  1.00107.03           C  
HETATM 3402  C27 CLR A1203     -50.833-149.589 314.204  1.00 91.03           C  
HETATM 3403  O1  CLR A1203     -52.289-136.690 309.760  1.00116.69           O  
HETATM 3404  C1  PEG A1204     -53.380-130.083 313.708  1.00114.37           C  
HETATM 3405  O1  PEG A1204     -54.683-129.570 313.667  1.00116.00           O  
HETATM 3406  C2  PEG A1204     -52.901-130.379 312.288  1.00113.60           C  
HETATM 3407  O2  PEG A1204     -51.600-130.895 312.321  1.00112.27           O  
HETATM 3408  C3  PEG A1204     -51.483-132.092 313.040  1.00109.17           C  
HETATM 3409  C4  PEG A1204     -50.276-132.887 312.543  1.00 98.00           C  
HETATM 3410  O4  PEG A1204     -50.124-134.037 313.329  1.00 84.96           O  
HETATM 3411  O   HOH A1301     -52.768-134.689 301.305  1.00 61.12           O  
CONECT 3316 3317 3333                                                           
CONECT 3317 3316 3318 3319                                                      
CONECT 3318 3317                                                                
CONECT 3319 3317 3320                                                           
CONECT 3320 3319 3321 3322                                                      
CONECT 3321 3320                                                                
CONECT 3322 3320 3323 3333                                                      
CONECT 3323 3322 3324                                                           
CONECT 3324 3323 3325 3331                                                      
CONECT 3325 3324 3326                                                           
CONECT 3326 3325 3327 3328                                                      
CONECT 3327 3326                                                                
CONECT 3328 3326 3329 3330                                                      
CONECT 3329 3328                                                                
CONECT 3330 3328 3331                                                           
CONECT 3331 3324 3330 3332                                                      
CONECT 3332 3331 3333 3334                                                      
CONECT 3333 3316 3322 3332                                                      
CONECT 3334 3332 3335                                                           
CONECT 3335 3334 3336 3337                                                      
CONECT 3336 3335                                                                
CONECT 3337 3335 3338 3339                                                      
CONECT 3338 3337                                                                
CONECT 3339 3337 3340 3341                                                      
CONECT 3340 3339                                                                
CONECT 3341 3339 3342                                                           
CONECT 3342 3341 3343                                                           
CONECT 3343 3342 3344 3345 3346                                                 
CONECT 3344 3343                                                                
CONECT 3345 3343                                                                
CONECT 3346 3343                                                                
CONECT 3347 3348 3369                                                           
CONECT 3348 3347 3349 3360                                                      
CONECT 3349 3348 3350                                                           
CONECT 3350 3349 3351 3375                                                      
CONECT 3351 3350 3369 3370                                                      
CONECT 3352 3368                                                                
CONECT 3353 3354 3370                                                           
CONECT 3354 3353 3355 3357                                                      
CONECT 3355 3354 3356                                                           
CONECT 3356 3355 3371                                                           
CONECT 3357 3354 3374                                                           
CONECT 3358 3372                                                                
CONECT 3359 3372                                                                
CONECT 3360 3348 3361 3362 3363                                                 
CONECT 3361 3360 3364                                                           
CONECT 3362 3360                                                                
CONECT 3363 3360                                                                
CONECT 3364 3361 3365                                                           
CONECT 3365 3364 3366                                                           
CONECT 3366 3365 3367                                                           
CONECT 3367 3366 3368                                                           
CONECT 3368 3352 3367                                                           
CONECT 3369 3347 3351 3373                                                      
CONECT 3370 3351 3353 3371                                                      
CONECT 3371 3356 3370 3372                                                      
CONECT 3372 3358 3359 3371 3373                                                 
CONECT 3373 3369 3372                                                           
CONECT 3374 3357                                                                
CONECT 3375 3350                                                                
CONECT 3376 3377 3385                                                           
CONECT 3377 3376 3378                                                           
CONECT 3378 3377 3379 3403                                                      
CONECT 3379 3378 3380                                                           
CONECT 3380 3379 3381 3385                                                      
CONECT 3381 3380 3382                                                           
CONECT 3382 3381 3383                                                           
CONECT 3383 3382 3384 3389                                                      
CONECT 3384 3383 3385 3386                                                      
CONECT 3385 3376 3380 3384 3394                                                 
CONECT 3386 3384 3387                                                           
CONECT 3387 3386 3388                                                           
CONECT 3388 3387 3389 3392 3393                                                 
CONECT 3389 3383 3388 3390                                                      
CONECT 3390 3389 3391                                                           
CONECT 3391 3390 3392                                                           
CONECT 3392 3388 3391 3395                                                      
CONECT 3393 3388                                                                
CONECT 3394 3385                                                                
CONECT 3395 3392 3396 3397                                                      
CONECT 3396 3395                                                                
CONECT 3397 3395 3398                                                           
CONECT 3398 3397 3399                                                           
CONECT 3399 3398 3400                                                           
CONECT 3400 3399 3401 3402                                                      
CONECT 3401 3400                                                                
CONECT 3402 3400                                                                
CONECT 3403 3378                                                                
CONECT 3404 3405 3406                                                           
CONECT 3405 3404                                                                
CONECT 3406 3404 3407                                                           
CONECT 3407 3406 3408                                                           
CONECT 3408 3407 3409                                                           
CONECT 3409 3408 3410                                                           
CONECT 3410 3409                                                                
MASTER      316    0    4   15    5    0    0    6 3410    1   95   34          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.