CNRS Nantes University UFIP UFIP
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***  ika  ***

elNémo ID: 2007282237328536

Job options:

ID        	=	 2007282237328536
JOBID     	=	 ika
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER ika

HEADER    TRANSPORT PROTEIN                       27-MAR-14   4PYP              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN GLUCOSE TRANSPORTER GLUT1              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER   
COMPND   3 MEMBER 1;                                                            
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: GLUCOSE TRANSPORTER TYPE 1, ERYTHROCYTE/BRAIN, GLUT-1, HEPG2
COMPND   6 GLUCOSE TRANSPORTER;                                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SLC2A1, GLUT1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    MEMBRANE TRANSPORTER, HELIX, GLYCOSYLATION, TRANSPORT PROTEIN         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.DENG,C.Y.YAN,C.XU,J.P.WU,P.C.SUN,M.X.HU,N.YAN                       
REVDAT   2   11-JUN-14 4PYP    1       JRNL                                     
REVDAT   1   21-MAY-14 4PYP    0                                                
JRNL        AUTH   D.DENG,C.XU,P.C.SUN,J.P.WU,C.Y.YAN,M.X.HU,N.YAN              
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN GLUCOSE TRANSPORTER GLUT1     
JRNL        REF    NATURE                        V. 510   121 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   24847886                                                     
JRNL        DOI    10.1038/NATURE13306                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12780                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 635                             
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 32.6753 -  5.4065    0.96     2502   114  0.2236 0.2666        
REMARK   3     2  5.4065 -  4.2944    0.98     2491   131  0.2213 0.2363        
REMARK   3     3  4.2944 -  3.7525    0.99     2483   137  0.2222 0.2906        
REMARK   3     4  3.7525 -  3.4098    0.99     2511   131  0.2475 0.3055        
REMARK   3     5  3.4098 -  3.1656    0.86     2158   122  0.3112 0.3897        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.380           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 88.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 99.25                          
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      :  0.009           3573                                  
REMARK   3   ANGLE     :  1.252           4850                                  
REMARK   3   CHIRALITY :  0.044            571                                  
REMARK   3   PLANARITY :  0.008            598                                  
REMARK   3   DIHEDRAL  : 18.167           1277                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): 583.8383 -31.0884 202.8414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5424 T22:   0.5349                                     
REMARK   3      T33:   0.6599 T12:  -0.0227                                     
REMARK   3      T13:   0.1025 T23:   0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3068 L22:   3.2016                                     
REMARK   3      L33:   2.3704 L12:   0.0108                                     
REMARK   3      L13:   0.0876 L23:   0.9075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0379 S12:  -0.2773 S13:   0.3084                       
REMARK   3      S21:   0.3977 S22:  -0.0473 S23:   0.1932                       
REMARK   3      S31:  -0.1064 S32:  -0.1333 S33:  -0.0141                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4PYP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085385.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97906                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12780                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.160                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4GC0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M MGCL2, 0.1M MES, PH     
REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       60.25450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.99800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.25450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.99800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     LYS A   456                                                      
REMARK 465     GLY A   457                                                      
REMARK 465     ARG A   458                                                      
REMARK 465     THR A   459                                                      
REMARK 465     PHE A   460                                                      
REMARK 465     ASP A   461                                                      
REMARK 465     GLU A   462                                                      
REMARK 465     ILE A   463                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     SER A   465                                                      
REMARK 465     GLY A   466                                                      
REMARK 465     PHE A   467                                                      
REMARK 465     ARG A   468                                                      
REMARK 465     GLN A   469                                                      
REMARK 465     GLY A   470                                                      
REMARK 465     GLY A   471                                                      
REMARK 465     ALA A   472                                                      
REMARK 465     SER A   473                                                      
REMARK 465     GLN A   474                                                      
REMARK 465     SER A   475                                                      
REMARK 465     ASP A   476                                                      
REMARK 465     LYS A   477                                                      
REMARK 465     THR A   478                                                      
REMARK 465     PRO A   479                                                      
REMARK 465     GLU A   480                                                      
REMARK 465     GLU A   481                                                      
REMARK 465     LEU A   482                                                      
REMARK 465     PHE A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     PRO A   485                                                      
REMARK 465     LEU A   486                                                      
REMARK 465     GLY A   487                                                      
REMARK 465     ALA A   488                                                      
REMARK 465     ASP A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     GLN A   491                                                      
REMARK 465     VAL A   492                                                      
REMARK 465     LEU A   493                                                      
REMARK 465     GLU A   494                                                      
REMARK 465     HIS A   495                                                      
REMARK 465     HIS A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     HIS A   498                                                      
REMARK 465     HIS A   499                                                      
REMARK 465     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     HIS A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN A    25     ND2  ASN A    29              1.99            
REMARK 500   O    MET A   110     OG   SER A   113              2.03            
REMARK 500   OG   SER A   118     OE1  GLU A   120              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 187   C   -  N   -  CA  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  28      -99.34    -59.08                                   
REMARK 500    ASN A  29      -27.39    -25.12                                   
REMARK 500    ILE A  33       12.51    -65.69                                   
REMARK 500    LEU A  61      -34.72    -34.89                                   
REMARK 500    ILE A  71      -17.09    -44.12                                   
REMARK 500    LYS A 114      -89.49    -52.97                                   
REMARK 500    MET A 142      -70.08    -53.76                                   
REMARK 500    ASP A 177      -39.83    -37.75                                   
REMARK 500    ILE A 179      -85.82   -107.51                                   
REMARK 500    ILE A 192       -2.51    -55.89                                   
REMARK 500    CYS A 201        2.24    -65.19                                   
REMARK 500    THR A 234       69.30   -118.55                                   
REMARK 500    ALA A 235      -59.99   -124.25                                   
REMARK 500    ASP A 236       77.29     48.55                                   
REMARK 500    ARG A 249      -78.23    -85.96                                   
REMARK 500    LYS A 256       98.67    -66.81                                   
REMARK 500    TYR A 293       10.18   -143.58                                   
REMARK 500    GLU A 299      -70.34    -49.80                                   
REMARK 500    ALA A 301     -105.45    -61.43                                   
REMARK 500    GLN A 305       75.30     56.79                                   
REMARK 500    TRP A 363       10.38    -69.64                                   
REMARK 500    PRO A 383       -7.46    -54.09                                   
REMARK 500    PHE A 389      -38.82    -37.48                                   
REMARK 500    PRO A 431       21.05    -68.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNG A 601                 
DBREF  4PYP A    1   492  UNP    P11166   GTR1_HUMAN       1    492             
SEQADV 4PYP THR A   45  UNP  P11166    ASN    45 ENGINEERED MUTATION            
SEQADV 4PYP GLN A  329  UNP  P11166    GLU   329 ENGINEERED MUTATION            
SEQADV 4PYP LEU A  493  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP GLU A  494  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  495  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  496  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  497  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  498  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  499  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  500  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  501  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  502  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  503  UNP  P11166              EXPRESSION TAG                 
SEQADV 4PYP HIS A  504  UNP  P11166              EXPRESSION TAG                 
SEQRES   1 A  504  MET GLU PRO SER SER LYS LYS LEU THR GLY ARG LEU MET          
SEQRES   2 A  504  LEU ALA VAL GLY GLY ALA VAL LEU GLY SER LEU GLN PHE          
SEQRES   3 A  504  GLY TYR ASN THR GLY VAL ILE ASN ALA PRO GLN LYS VAL          
SEQRES   4 A  504  ILE GLU GLU PHE TYR THR GLN THR TRP VAL HIS ARG TYR          
SEQRES   5 A  504  GLY GLU SER ILE LEU PRO THR THR LEU THR THR LEU TRP          
SEQRES   6 A  504  SER LEU SER VAL ALA ILE PHE SER VAL GLY GLY MET ILE          
SEQRES   7 A  504  GLY SER PHE SER VAL GLY LEU PHE VAL ASN ARG PHE GLY          
SEQRES   8 A  504  ARG ARG ASN SER MET LEU MET MET ASN LEU LEU ALA PHE          
SEQRES   9 A  504  VAL SER ALA VAL LEU MET GLY PHE SER LYS LEU GLY LYS          
SEQRES  10 A  504  SER PHE GLU MET LEU ILE LEU GLY ARG PHE ILE ILE GLY          
SEQRES  11 A  504  VAL TYR CYS GLY LEU THR THR GLY PHE VAL PRO MET TYR          
SEQRES  12 A  504  VAL GLY GLU VAL SER PRO THR ALA LEU ARG GLY ALA LEU          
SEQRES  13 A  504  GLY THR LEU HIS GLN LEU GLY ILE VAL VAL GLY ILE LEU          
SEQRES  14 A  504  ILE ALA GLN VAL PHE GLY LEU ASP SER ILE MET GLY ASN          
SEQRES  15 A  504  LYS ASP LEU TRP PRO LEU LEU LEU SER ILE ILE PHE ILE          
SEQRES  16 A  504  PRO ALA LEU LEU GLN CYS ILE VAL LEU PRO PHE CYS PRO          
SEQRES  17 A  504  GLU SER PRO ARG PHE LEU LEU ILE ASN ARG ASN GLU GLU          
SEQRES  18 A  504  ASN ARG ALA LYS SER VAL LEU LYS LYS LEU ARG GLY THR          
SEQRES  19 A  504  ALA ASP VAL THR HIS ASP LEU GLN GLU MET LYS GLU GLU          
SEQRES  20 A  504  SER ARG GLN MET MET ARG GLU LYS LYS VAL THR ILE LEU          
SEQRES  21 A  504  GLU LEU PHE ARG SER PRO ALA TYR ARG GLN PRO ILE LEU          
SEQRES  22 A  504  ILE ALA VAL VAL LEU GLN LEU SER GLN GLN LEU SER GLY          
SEQRES  23 A  504  ILE ASN ALA VAL PHE TYR TYR SER THR SER ILE PHE GLU          
SEQRES  24 A  504  LYS ALA GLY VAL GLN GLN PRO VAL TYR ALA THR ILE GLY          
SEQRES  25 A  504  SER GLY ILE VAL ASN THR ALA PHE THR VAL VAL SER LEU          
SEQRES  26 A  504  PHE VAL VAL GLN ARG ALA GLY ARG ARG THR LEU HIS LEU          
SEQRES  27 A  504  ILE GLY LEU ALA GLY MET ALA GLY CYS ALA ILE LEU MET          
SEQRES  28 A  504  THR ILE ALA LEU ALA LEU LEU GLU GLN LEU PRO TRP MET          
SEQRES  29 A  504  SER TYR LEU SER ILE VAL ALA ILE PHE GLY PHE VAL ALA          
SEQRES  30 A  504  PHE PHE GLU VAL GLY PRO GLY PRO ILE PRO TRP PHE ILE          
SEQRES  31 A  504  VAL ALA GLU LEU PHE SER GLN GLY PRO ARG PRO ALA ALA          
SEQRES  32 A  504  ILE ALA VAL ALA GLY PHE SER ASN TRP THR SER ASN PHE          
SEQRES  33 A  504  ILE VAL GLY MET CYS PHE GLN TYR VAL GLU GLN LEU CYS          
SEQRES  34 A  504  GLY PRO TYR VAL PHE ILE ILE PHE THR VAL LEU LEU VAL          
SEQRES  35 A  504  LEU PHE PHE ILE PHE THR TYR PHE LYS VAL PRO GLU THR          
SEQRES  36 A  504  LYS GLY ARG THR PHE ASP GLU ILE ALA SER GLY PHE ARG          
SEQRES  37 A  504  GLN GLY GLY ALA SER GLN SER ASP LYS THR PRO GLU GLU          
SEQRES  38 A  504  LEU PHE HIS PRO LEU GLY ALA ASP SER GLN VAL LEU GLU          
SEQRES  39 A  504  HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS                      
HET    BNG  A 601      21                                                       
HETNAM     BNG B-NONYLGLUCOSIDE                                                 
FORMUL   2  BNG    C15 H30 O6                                                   
HELIX    1   1 ARG A   11  GLY A   31  1                                  21    
HELIX    2   2 PRO A   36  GLY A   53  1                                  18    
HELIX    3   3 LEU A   57  GLY A   91  1                                  35    
HELIX    4   4 ARG A   92  PHE A  112  1                                  21    
HELIX    5   5 PHE A  112  LYS A  117  1                                   6    
HELIX    6   6 PHE A  119  SER A  148  1                                  30    
HELIX    7   7 LEU A  152  PHE A  174  1                                  23    
HELIX    8   8 LEU A  185  ILE A  192  1                                   8    
HELIX    9   9 ILE A  193  LEU A  204  1                                  12    
HELIX   10  10 PRO A  205  CYS A  207  5                                   3    
HELIX   11  11 SER A  210  ILE A  216  1                                   7    
HELIX   12  12 GLU A  220  ARG A  232  1                                  13    
HELIX   13  13 VAL A  237  GLU A  254  1                                  18    
HELIX   14  14 THR A  258  SER A  265  1                                   8    
HELIX   15  15 SER A  265  GLN A  270  1                                   6    
HELIX   16  16 GLN A  270  LEU A  284  1                                  15    
HELIX   17  17 GLY A  286  TYR A  293  1                                   8    
HELIX   18  18 TYR A  293  GLY A  302  1                                  10    
HELIX   19  19 GLN A  305  ALA A  331  1                                  27    
HELIX   20  20 GLY A  332  LEU A  358  1                                  27    
HELIX   21  21 GLU A  359  GLN A  360  5                                   2    
HELIX   22  22 LEU A  361  PRO A  362  5                                   2    
HELIX   23  23 TRP A  363  GLY A  382  1                                  20    
HELIX   24  24 PRO A  385  PHE A  395  1                                  11    
HELIX   25  25 PRO A  399  PHE A  422  1                                  24    
HELIX   26  26 GLN A  423  LEU A  428  1                                   6    
HELIX   27  27 CYS A  429  PRO A  431  5                                   3    
HELIX   28  28 TYR A  432  LYS A  451  1                                  20    
SITE     1 AC1  7 GLN A 282  GLN A 283  ASN A 288  PHE A 291                    
SITE     2 AC1  7 ASN A 317  GLU A 380  PHE A 389                               
CRYST1  120.509  101.996   65.604  90.00 101.27  90.00 C 1 2 1       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      0.008298  0.000000  0.001654        0.00000                         
SCALE2      0.000000  0.009804  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015543        0.00000                         
ATOM      1  N   THR A   9     564.692 -21.021 222.563  1.00160.43           N  
ANISOU    1  N   THR A   9    18795  21747  20415    457   6198  -4444       N  
ATOM      2  CA  THR A   9     565.438 -22.166 222.064  1.00158.62           C  
ANISOU    2  CA  THR A   9    18746  21513  20008    277   5975  -3996       C  
ATOM      3  C   THR A   9     564.548 -23.405 221.969  1.00157.72           C  
ANISOU    3  C   THR A   9    18464  21585  19879    102   6225  -3782       C  
ATOM      4  O   THR A   9     564.969 -24.508 222.314  1.00157.21           O  
ANISOU    4  O   THR A   9    18628  21652  19451   -111   6257  -3502       O  
ATOM      5  CB  THR A   9     566.661 -22.478 222.959  1.00159.35           C  
ANISOU    5  CB  THR A   9    19288  21713  19546    138   5886  -3909       C  
ATOM      6  OG1 THR A   9     566.232 -23.119 224.166  1.00160.54           O  
ANISOU    6  OG1 THR A   9    19566  22183  19249    -27   6268  -3955       O  
ATOM      7  CG2 THR A   9     567.415 -21.198 223.305  1.00161.12           C  
ANISOU    7  CG2 THR A   9    19663  21798  19758    287   5714  -4210       C  
ATOM      8  N   GLY A  10     563.315 -23.213 221.504  1.00136.16           N  
ANISOU    8  N   GLY A  10    15325  18849  17560    195   6395  -3918       N  
ATOM      9  CA  GLY A  10     562.368 -24.308 221.355  1.00136.21           C  
ANISOU    9  CA  GLY A  10    15128  19003  17622     33   6578  -3719       C  
ATOM     10  C   GLY A  10     562.103 -24.695 219.907  1.00133.59           C  
ANISOU   10  C   GLY A  10    14515  18507  17734     69   6367  -3526       C  
ATOM     11  O   GLY A  10     562.526 -25.753 219.437  1.00131.84           O  
ANISOU   11  O   GLY A  10    14408  18270  17415    -97   6221  -3180       O  
ATOM     12  N   ARG A  11     561.402 -23.825 219.189  1.00184.10           N  
ANISOU   12  N   ARG A  11    20579  24763  24609    301   6254  -3705       N  
ATOM     13  CA  ARG A  11     561.121 -24.056 217.778  1.00182.29           C  
ANISOU   13  CA  ARG A  11    20082  24378  24802    372   5998  -3536       C  
ATOM     14  C   ARG A  11     562.405 -23.942 216.951  1.00180.90           C  
ANISOU   14  C   ARG A  11    20174  23968  24592    417   5540  -3282       C  
ATOM     15  O   ARG A  11     562.437 -24.323 215.781  1.00179.49           O  
ANISOU   15  O   ARG A  11    19885  23672  24642    432   5272  -3060       O  
ATOM     16  CB  ARG A  11     560.066 -23.065 217.280  1.00183.82           C  
ANISOU   16  CB  ARG A  11    19895  24473  25476    634   5932  -3769       C  
ATOM     17  CG  ARG A  11     559.448 -23.422 215.942  1.00182.35           C  
ANISOU   17  CG  ARG A  11    19377  24200  25706    692   5718  -3618       C  
ATOM     18  CD  ARG A  11     559.566 -22.265 214.970  1.00182.30           C  
ANISOU   18  CD  ARG A  11    19238  23926  26103   1002   5405  -3708       C  
ATOM     19  NE  ARG A  11     558.259 -21.780 214.541  1.00184.51           N  
ANISOU   19  NE  ARG A  11    19135  24194  26777   1183   5345  -3838       N  
ATOM     20  CZ  ARG A  11     557.593 -22.265 213.500  1.00183.68           C  
ANISOU   20  CZ  ARG A  11    18744  24087  26959   1199   5173  -3700       C  
ATOM     21  NH1 ARG A  11     558.118 -23.251 212.784  1.00180.56           N  
ANISOU   21  NH1 ARG A  11    18404  23695  26504   1042   5053  -3434       N  
ATOM     22  NH2 ARG A  11     556.406 -21.769 213.176  1.00186.14           N  
ANISOU   22  NH2 ARG A  11    18716  24396  27613   1374   5112  -3838       N  
ATOM     23  N   LEU A  12     563.462 -23.428 217.578  1.00149.61           N  
ANISOU   23  N   LEU A  12    16556  19953  20334    430   5459  -3330       N  
ATOM     24  CA  LEU A  12     564.738 -23.182 216.909  1.00148.62           C  
ANISOU   24  CA  LEU A  12    16679  19612  20179    473   5054  -3135       C  
ATOM     25  C   LEU A  12     565.384 -24.476 216.420  1.00146.68           C  
ANISOU   25  C   LEU A  12    16593  19392  19746    273   4895  -2749       C  
ATOM     26  O   LEU A  12     565.804 -24.558 215.268  1.00145.38           O  
ANISOU   26  O   LEU A  12    16403  19060  19774    322   4580  -2547       O  
ATOM     27  CB  LEU A  12     565.697 -22.433 217.847  1.00149.92           C  
ANISOU   27  CB  LEU A  12    17165  19752  20047    496   5038  -3303       C  
ATOM     28  CG  LEU A  12     566.767 -21.506 217.251  1.00149.50           C  
ANISOU   28  CG  LEU A  12    17263  19422  20118    629   4670  -3285       C  
ATOM     29  CD1 LEU A  12     566.903 -20.246 218.091  1.00151.19           C  
ANISOU   29  CD1 LEU A  12    17558  19575  20314    761   4754  -3657       C  
ATOM     30  CD2 LEU A  12     568.102 -22.193 217.162  1.00148.77           C  
ANISOU   30  CD2 LEU A  12    17488  19320  19719    474   4438  -2998       C  
ATOM     31  N   MET A  13     565.455 -25.483 217.292  1.00118.85           N  
ANISOU   31  N   MET A  13    13239  16073  15847     54   5116  -2646       N  
ATOM     32  CA  MET A  13     566.088 -26.764 216.962  1.00117.20           C  
ANISOU   32  CA  MET A  13    13206  15877  15447   -136   4984  -2288       C  
ATOM     33  C   MET A  13     565.521 -27.399 215.692  1.00115.58           C  
ANISOU   33  C   MET A  13    12732  15596  15586   -148   4855  -2111       C  
ATOM     34  O   MET A  13     566.228 -28.103 214.978  1.00114.14           O  
ANISOU   34  O   MET A  13    12667  15327  15373   -218   4609  -1844       O  
ATOM     35  CB  MET A  13     565.947 -27.750 218.124  1.00117.75           C  
ANISOU   35  CB  MET A  13    13452  16176  15110   -364   5299  -2213       C  
ATOM     36  CG  MET A  13     566.805 -27.439 219.338  1.00119.19           C  
ANISOU   36  CG  MET A  13    13996  16453  14838   -393   5349  -2296       C  
ATOM     37  SD  MET A  13     566.213 -28.263 220.844  1.00120.89           S  
ANISOU   37  SD  MET A  13    14356  16979  14596   -617   5826  -2303       S  
ATOM     38  CE  MET A  13     566.433 -29.992 220.428  1.00119.47           C  
ANISOU   38  CE  MET A  13    14286  16788  14320   -854   5765  -1847       C  
ATOM     39  N   LEU A  14     564.245 -27.158 215.414  1.00114.85           N  
ANISOU   39  N   LEU A  14    12269  15546  15822    -76   5015  -2277       N  
ATOM     40  CA  LEU A  14     563.625 -27.681 214.200  1.00113.70           C  
ANISOU   40  CA  LEU A  14    11839  15344  16019    -73   4875  -2150       C  
ATOM     41  C   LEU A  14     564.319 -27.121 212.967  1.00112.78           C  
ANISOU   41  C   LEU A  14    11747  15005  16101     97   4452  -2044       C  
ATOM     42  O   LEU A  14     564.689 -27.866 212.064  1.00111.44           O  
ANISOU   42  O   LEU A  14    11605  14772  15964     28   4231  -1806       O  
ATOM     43  CB  LEU A  14     562.128 -27.348 214.160  1.00114.75           C  
ANISOU   43  CB  LEU A  14    11537  15566  16496      8   5102  -2393       C  
ATOM     44  CG  LEU A  14     561.395 -27.708 212.862  1.00113.73           C  
ANISOU   44  CG  LEU A  14    11067  15383  16761     51   4919  -2315       C  
ATOM     45  CD1 LEU A  14     561.077 -29.190 212.815  1.00112.68           C  
ANISOU   45  CD1 LEU A  14    10895  15361  16555   -223   5045  -2124       C  
ATOM     46  CD2 LEU A  14     560.136 -26.859 212.682  1.00115.16           C  
ANISOU   46  CD2 LEU A  14    10820  15589  17348    251   5017  -2604       C  
ATOM     47  N   ALA A  15     564.495 -25.805 212.943  1.00200.79           N  
ANISOU   47  N   ALA A  15    22890  26026  27375    313   4352  -2225       N  
ATOM     48  CA  ALA A  15     565.129 -25.134 211.815  1.00200.22           C  
ANISOU   48  CA  ALA A  15    22851  25730  27495    477   3978  -2126       C  
ATOM     49  C   ALA A  15     566.600 -25.538 211.660  1.00199.21           C  
ANISOU   49  C   ALA A  15    23077  25527  27086    372   3758  -1887       C  
ATOM     50  O   ALA A  15     567.035 -25.919 210.573  1.00197.90           O  
ANISOU   50  O   ALA A  15    22925  25269  26998    366   3499  -1672       O  
ATOM     51  CB  ALA A  15     565.004 -23.627 211.969  1.00201.63           C  
ANISOU   51  CB  ALA A  15    22973  25767  27869    715   3953  -2377       C  
ATOM     52  N   VAL A  16     567.358 -25.451 212.749  1.00101.05           N  
ANISOU   52  N   VAL A  16    10922  13146  14327    293   3860  -1941       N  
ATOM     53  CA  VAL A  16     568.775 -25.823 212.753  1.00100.41           C  
ANISOU   53  CA  VAL A  16    11162  13013  13977    198   3662  -1745       C  
ATOM     54  C   VAL A  16     569.017 -27.244 212.261  1.00 98.64           C  
ANISOU   54  C   VAL A  16    10986  12845  13648     29   3592  -1460       C  
ATOM     55  O   VAL A  16     569.846 -27.474 211.371  1.00 97.45           O  
ANISOU   55  O   VAL A  16    10922  12581  13522     31   3324  -1270       O  
ATOM     56  CB  VAL A  16     569.382 -25.704 214.169  1.00101.89           C  
ANISOU   56  CB  VAL A  16    11619  13306  13789    119   3813  -1860       C  
ATOM     57  CG1 VAL A  16     570.794 -26.264 214.191  1.00101.43           C  
ANISOU   57  CG1 VAL A  16    11861  13220  13457     14   3603  -1645       C  
ATOM     58  CG2 VAL A  16     569.359 -24.266 214.639  1.00103.55           C  
ANISOU   58  CG2 VAL A  16    11823  13431  14090    283   3845  -2159       C  
ATOM     59  N   GLY A  17     568.291 -28.187 212.864  1.00111.83           N  
ANISOU   59  N   GLY A  17    12603  14682  15206   -121   3850  -1440       N  
ATOM     60  CA  GLY A  17     568.448 -29.601 212.584  1.00110.32           C  
ANISOU   60  CA  GLY A  17    12473  14534  14911   -301   3828  -1189       C  
ATOM     61  C   GLY A  17     568.181 -29.932 211.133  1.00108.76           C  
ANISOU   61  C   GLY A  17    12072  14239  15012   -261   3613  -1069       C  
ATOM     62  O   GLY A  17     568.979 -30.621 210.491  1.00107.31           O  
ANISOU   62  O   GLY A  17    12017  13986  14769   -319   3406   -862       O  
ATOM     63  N   GLY A  18     567.063 -29.431 210.616  1.00 84.88           N  
ANISOU   63  N   GLY A  18     8727  11216  12307   -151   3655  -1212       N  
ATOM     64  CA  GLY A  18     566.697 -29.658 209.230  1.00 83.89           C  
ANISOU   64  CA  GLY A  18     8391  11020  12462    -96   3437  -1125       C  
ATOM     65  C   GLY A  18     567.723 -29.110 208.251  1.00 83.20           C  
ANISOU   65  C   GLY A  18     8436  10771  12407     28   3097  -1012       C  
ATOM     66  O   GLY A  18     567.900 -29.651 207.155  1.00 82.12           O  
ANISOU   66  O   GLY A  18     8261  10589  12352     14   2891   -861       O  
ATOM     67  N   ALA A  19     568.398 -28.035 208.647  1.00 86.61           N  
ANISOU   67  N   ALA A  19     9020  11116  12770    140   3050  -1095       N  
ATOM     68  CA  ALA A  19     569.439 -27.428 207.827  1.00 86.28           C  
ANISOU   68  CA  ALA A  19     9117  10913  12751    237   2762   -990       C  
ATOM     69  C   ALA A  19     570.674 -28.310 207.751  1.00 85.05           C  
ANISOU   69  C   ALA A  19     9214  10755  12347     97   2646   -786       C  
ATOM     70  O   ALA A  19     571.169 -28.604 206.661  1.00 84.01           O  
ANISOU   70  O   ALA A  19     9097  10555  12267    104   2429   -629       O  
ATOM     71  CB  ALA A  19     569.808 -26.053 208.373  1.00 87.77           C  
ANISOU   71  CB  ALA A  19     9396  10997  12957    370   2766  -1155       C  
ATOM     72  N   VAL A  20     571.152 -28.725 208.923  1.00 92.22           N  
ANISOU   72  N   VAL A  20    10318  11744  12978    -22   2791   -796       N  
ATOM     73  CA  VAL A  20     572.342 -29.566 209.064  1.00 91.47           C  
ANISOU   73  CA  VAL A  20    10469  11651  12635   -141   2689   -618       C  
ATOM     74  C   VAL A  20     572.232 -30.881 208.284  1.00 89.78           C  
ANISOU   74  C   VAL A  20    10205  11455  12454   -246   2625   -433       C  
ATOM     75  O   VAL A  20     573.229 -31.429 207.823  1.00 88.82           O  
ANISOU   75  O   VAL A  20    10222  11282  12244   -286   2453   -280       O  
ATOM     76  CB  VAL A  20     572.618 -29.857 210.556  1.00 92.60           C  
ANISOU   76  CB  VAL A  20    10813  11906  12466   -244   2876   -664       C  
ATOM     77  CG1 VAL A  20     573.443 -31.131 210.750  1.00 91.64           C  
ANISOU   77  CG1 VAL A  20    10895  11814  12112   -386   2816   -453       C  
ATOM     78  CG2 VAL A  20     573.311 -28.664 211.196  1.00 94.38           C  
ANISOU   78  CG2 VAL A  20    11174  12086  12601   -156   2836   -820       C  
ATOM     79  N   LEU A  21     571.011 -31.363 208.114  1.00 79.65           N  
ANISOU   79  N   LEU A  21     8705  10239  11319   -288   2761   -467       N  
ATOM     80  CA  LEU A  21     570.728 -32.521 207.274  1.00 78.37           C  
ANISOU   80  CA  LEU A  21     8451  10080  11248   -382   2695   -335       C  
ATOM     81  C   LEU A  21     571.492 -32.467 205.957  1.00 77.27           C  
ANISOU   81  C   LEU A  21     8335   9841  11186   -307   2402   -226       C  
ATOM     82  O   LEU A  21     571.903 -33.490 205.414  1.00 76.10           O  
ANISOU   82  O   LEU A  21     8240   9673  11000   -394   2305    -94       O  
ATOM     83  CB  LEU A  21     569.227 -32.594 207.013  1.00 78.92           C  
ANISOU   83  CB  LEU A  21     8205  10219  11564   -383   2827   -448       C  
ATOM     84  CG  LEU A  21     568.561 -33.958 207.105  1.00 78.58           C  
ANISOU   84  CG  LEU A  21     8077  10239  11541   -574   2969   -382       C  
ATOM     85  CD1 LEU A  21     567.059 -33.795 207.272  1.00 79.67           C  
ANISOU   85  CD1 LEU A  21     7894  10474  11901   -582   3174   -550       C  
ATOM     86  CD2 LEU A  21     568.875 -34.737 205.851  1.00 77.36           C  
ANISOU   86  CD2 LEU A  21     7900  10016  11478   -601   2733   -257       C  
ATOM     87  N   GLY A  22     571.691 -31.253 205.462  1.00 59.87           N  
ANISOU   87  N   GLY A  22     6097   7565   9086   -148   2272   -286       N  
ATOM     88  CA  GLY A  22     572.458 -31.028 204.256  1.00 59.19           C  
ANISOU   88  CA  GLY A  22     6053   7390   9048    -75   2018   -180       C  
ATOM     89  C   GLY A  22     573.961 -31.000 204.479  1.00 58.56           C  
ANISOU   89  C   GLY A  22     6225   7252   8772   -105   1922    -90       C  
ATOM     90  O   GLY A  22     574.723 -31.041 203.519  1.00 57.56           O  
ANISOU   90  O   GLY A  22     6148   7069   8653    -81   1740     12       O  
ATOM     91  N   SER A  23     574.391 -30.914 205.737  1.00 73.82           N  
ANISOU   91  N   SER A  23     8312   9212  10526   -155   2041   -139       N  
ATOM     92  CA  SER A  23     575.812 -31.035 206.069  1.00 73.56           C  
ANISOU   92  CA  SER A  23     8502   9145  10302   -194   1943    -65       C  
ATOM     93  C   SER A  23     576.155 -32.520 206.255  1.00 72.14           C  
ANISOU   93  C   SER A  23     8419   9013   9978   -323   1952     69       C  
ATOM     94  O   SER A  23     577.294 -32.951 206.003  1.00 71.30           O  
ANISOU   94  O   SER A  23     8438   8870   9782   -343   1811    170       O  
ATOM     95  CB  SER A  23     576.150 -30.218 207.326  1.00 75.61           C  
ANISOU   95  CB  SER A  23     8888   9417  10425   -178   2032   -194       C  
ATOM     96  OG  SER A  23     575.924 -30.972 208.508  1.00 76.02           O  
ANISOU   96  OG  SER A  23     9037   9577  10269   -280   2201   -199       O  
ATOM     97  N   LEU A  24     575.144 -33.280 206.699  1.00 65.84           N  
ANISOU   97  N   LEU A  24     7551   8286   9180   -407   2126     64       N  
ATOM     98  CA  LEU A  24     575.149 -34.739 206.674  1.00 64.76           C  
ANISOU   98  CA  LEU A  24     7461   8158   8985   -533   2148    196       C  
ATOM     99  C   LEU A  24     575.380 -35.240 205.260  1.00 63.21           C  
ANISOU   99  C   LEU A  24     7182   7902   8932   -516   1965    271       C  
ATOM    100  O   LEU A  24     576.297 -36.030 205.017  1.00 62.33           O  
ANISOU  100  O   LEU A  24     7193   7746   8743   -552   1853    380       O  
ATOM    101  CB  LEU A  24     573.838 -35.295 207.201  1.00 65.29           C  
ANISOU  101  CB  LEU A  24     7412   8297   9097   -634   2381    160       C  
ATOM    102  CG  LEU A  24     573.645 -34.990 208.674  1.00 66.78           C  
ANISOU  102  CG  LEU A  24     7714   8570   9089   -674   2595     96       C  
ATOM    103  CD1 LEU A  24     572.294 -35.475 209.166  1.00 67.39           C  
ANISOU  103  CD1 LEU A  24     7651   8731   9225   -786   2864     52       C  
ATOM    104  CD2 LEU A  24     574.754 -35.633 209.455  1.00 67.02           C  
ANISOU  104  CD2 LEU A  24     8028   8592   8845   -737   2549    229       C  
ATOM    105  N   GLN A  25     574.545 -34.782 204.332  1.00139.19           N  
ANISOU  105  N   GLN A  25    16596  17530  18758   -451   1928    204       N  
ATOM    106  CA  GLN A  25     574.706 -35.121 202.923  1.00138.27           C  
ANISOU  106  CA  GLN A  25    16402  17381  18753   -421   1746    255       C  
ATOM    107  C   GLN A  25     576.106 -34.796 202.449  1.00137.48           C  
ANISOU  107  C   GLN A  25    16447  17225  18564   -363   1576    324       C  
ATOM    108  O   GLN A  25     576.696 -35.540 201.675  1.00136.36           O  
ANISOU  108  O   GLN A  25    16339  17060  18411   -386   1461    395       O  
ATOM    109  CB  GLN A  25     573.695 -34.381 202.064  1.00139.17           C  
ANISOU  109  CB  GLN A  25    16292  17518  19067   -323   1699    172       C  
ATOM    110  CG  GLN A  25     572.421 -35.142 201.840  1.00139.66           C  
ANISOU  110  CG  GLN A  25    16151  17638  19277   -396   1776    120       C  
ATOM    111  CD  GLN A  25     571.229 -34.220 201.781  1.00141.09           C  
ANISOU  111  CD  GLN A  25    16104  17865  19640   -298   1825     -6       C  
ATOM    112  OE1 GLN A  25     571.377 -33.006 201.615  1.00140.35           O  
ANISOU  112  OE1 GLN A  25    16009  17736  19581   -152   1755    -39       O  
ATOM    113  NE2 GLN A  25     570.036 -34.783 201.933  1.00143.36           N  
ANISOU  113  NE2 GLN A  25    16187  18218  20063   -376   1949    -84       N  
ATOM    114  N   PHE A  26     576.640 -33.677 202.912  1.00 78.23           N  
ANISOU  114  N   PHE A  26     9018   9696  11009   -291   1569    286       N  
ATOM    115  CA  PHE A  26     578.011 -33.330 202.599  1.00 77.76           C  
ANISOU  115  CA  PHE A  26     9085   9585  10876   -258   1431    340       C  
ATOM    116  C   PHE A  26     578.909 -34.411 203.197  1.00 77.04           C  
ANISOU  116  C   PHE A  26     9145   9497  10629   -342   1422    414       C  
ATOM    117  O   PHE A  26     579.829 -34.898 202.546  1.00 75.92           O  
ANISOU  117  O   PHE A  26     9048   9329  10468   -344   1301    481       O  
ATOM    118  CB  PHE A  26     578.350 -31.939 203.144  1.00 79.32           C  
ANISOU  118  CB  PHE A  26     9330   9741  11067   -188   1441    263       C  
ATOM    119  CG  PHE A  26     579.677 -31.376 202.650  1.00 79.31           C  
ANISOU  119  CG  PHE A  26     9414   9675  11045   -161   1301    307       C  
ATOM    120  CD1 PHE A  26     580.857 -31.626 203.340  1.00 79.28           C  
ANISOU  120  CD1 PHE A  26     9549   9673  10902   -208   1265    320       C  
ATOM    121  CD2 PHE A  26     579.745 -30.585 201.505  1.00 79.79           C  
ANISOU  121  CD2 PHE A  26     9411   9677  11227    -90   1207    339       C  
ATOM    122  CE1 PHE A  26     582.065 -31.114 202.902  1.00 79.44           C  
ANISOU  122  CE1 PHE A  26     9613   9641  10928   -197   1151    343       C  
ATOM    123  CE2 PHE A  26     580.969 -30.070 201.067  1.00 79.90           C  
ANISOU  123  CE2 PHE A  26     9498   9633  11228    -90   1111    384       C  
ATOM    124  CZ  PHE A  26     582.119 -30.340 201.768  1.00 79.53           C  
ANISOU  124  CZ  PHE A  26     9559   9593  11067   -148   1090    376       C  
ATOM    125  N   GLY A  27     578.603 -34.826 204.423  1.00 93.80           N  
ANISOU  125  N   GLY A  27    11345  11655  12639   -407   1554    404       N  
ATOM    126  CA  GLY A  27     579.404 -35.833 205.094  1.00 93.83           C  
ANISOU  126  CA  GLY A  27    11513  11653  12486   -472   1534    495       C  
ATOM    127  C   GLY A  27     579.420 -37.178 204.397  1.00 92.62           C  
ANISOU  127  C   GLY A  27    11343  11459  12390   -526   1485    587       C  
ATOM    128  O   GLY A  27     580.474 -37.795 204.265  1.00 92.39           O  
ANISOU  128  O   GLY A  27    11411  11388  12307   -521   1370    657       O  
ATOM    129  N   TYR A  28     578.238 -37.632 203.988  1.00 66.36           N  
ANISOU  129  N   TYR A  28     7884   8143   9188   -577   1572    570       N  
ATOM    130  CA  TYR A  28     578.064 -38.838 203.185  1.00 65.79           C  
ANISOU  130  CA  TYR A  28     7763   8023   9211   -635   1526    618       C  
ATOM    131  C   TYR A  28     578.853 -38.647 201.881  1.00 64.93           C  
ANISOU  131  C   TYR A  28     7614   7896   9160   -553   1343    608       C  
ATOM    132  O   TYR A  28     580.058 -38.779 201.896  1.00 64.67           O  
ANISOU  132  O   TYR A  28     7691   7831   9048   -520   1247    653       O  
ATOM    133  CB  TYR A  28     576.561 -39.093 202.940  1.00 66.16           C  
ANISOU  133  CB  TYR A  28     7630   8101   9409   -703   1644    559       C  
ATOM    134  CG  TYR A  28     576.098 -40.542 202.702  1.00 66.56           C  
ANISOU  134  CG  TYR A  28     7655   8090   9546   -827   1678    601       C  
ATOM    135  CD1 TYR A  28     575.939 -41.443 203.762  1.00 67.28           C  
ANISOU  135  CD1 TYR A  28     7867   8132   9565   -949   1821    690       C  
ATOM    136  CD2 TYR A  28     575.752 -40.979 201.419  1.00 66.71           C  
ANISOU  136  CD2 TYR A  28     7530   8096   9720   -828   1572    546       C  
ATOM    137  CE1 TYR A  28     575.496 -42.747 203.536  1.00 67.98           C  
ANISOU  137  CE1 TYR A  28     7935   8131   9765  -1075   1858    731       C  
ATOM    138  CE2 TYR A  28     575.312 -42.274 201.182  1.00 67.58           C  
ANISOU  138  CE2 TYR A  28     7609   8132   9936   -949   1598    556       C  
ATOM    139  CZ  TYR A  28     575.185 -43.159 202.238  1.00 68.14           C  
ANISOU  139  CZ  TYR A  28     7799   8125   9966  -1077   1744    650       C  
ATOM    140  OH  TYR A  28     574.749 -44.457 201.993  1.00 69.22           O  
ANISOU  140  OH  TYR A  28     7909   8154  10236  -1210   1774    664       O  
ATOM    141  N   ASN A  29     578.187 -38.274 200.785  1.00 67.47           N  
ANISOU  141  N   ASN A  29     7776   8251   9608   -516   1298    548       N  
ATOM    142  CA  ASN A  29     578.770 -38.207 199.416  1.00 67.12           C  
ANISOU  142  CA  ASN A  29     7693   8211   9597   -454   1144    544       C  
ATOM    143  C   ASN A  29     580.274 -38.009 199.261  1.00 66.42           C  
ANISOU  143  C   ASN A  29     7722   8099   9417   -406   1049    586       C  
ATOM    144  O   ASN A  29     580.858 -38.356 198.227  1.00 66.38           O  
ANISOU  144  O   ASN A  29     7703   8097   9421   -383    953    586       O  
ATOM    145  CB  ASN A  29     578.132 -37.081 198.618  1.00 67.65           C  
ANISOU  145  CB  ASN A  29     7633   8331   9740   -372   1099    498       C  
ATOM    146  CG  ASN A  29     576.679 -36.934 198.892  1.00 68.59           C  
ANISOU  146  CG  ASN A  29     7605   8487   9970   -390   1191    434       C  
ATOM    147  OD1 ASN A  29     575.854 -37.618 198.328  1.00 69.23           O  
ANISOU  147  OD1 ASN A  29     7563   8594  10147   -434   1177    394       O  
ATOM    148  ND2 ASN A  29     576.354 -36.023 199.771  1.00 69.05           N  
ANISOU  148  ND2 ASN A  29     7661   8549  10024   -357   1288    405       N  
ATOM    149  N   THR A  30     580.869 -37.367 200.257  1.00 68.85           N  
ANISOU  149  N   THR A  30     8125   8396   9638   -389   1079    603       N  
ATOM    150  CA  THR A  30     582.302 -37.209 200.324  1.00 68.66           C  
ANISOU  150  CA  THR A  30     8193   8354   9543   -357    995    629       C  
ATOM    151  C   THR A  30     582.950 -38.556 200.643  1.00 69.13           C  
ANISOU  151  C   THR A  30     8338   8368   9562   -390    960    677       C  
ATOM    152  O   THR A  30     583.643 -39.117 199.798  1.00 69.19           O  
ANISOU  152  O   THR A  30     8327   8359   9601   -369    878    676       O  
ATOM    153  CB  THR A  30     582.682 -36.140 201.375  1.00 69.42           C  
ANISOU  153  CB  THR A  30     8359   8453   9565   -337   1024    607       C  
ATOM    154  OG1 THR A  30     581.778 -35.034 201.268  1.00 69.81           O  
ANISOU  154  OG1 THR A  30     8330   8514   9679   -306   1082    555       O  
ATOM    155  CG2 THR A  30     584.087 -35.611 201.142  1.00 69.59           C  
ANISOU  155  CG2 THR A  30     8414   8463   9563   -303    924    607       C  
ATOM    156  N   GLY A  31     582.703 -39.077 201.845  1.00123.58           N  
ANISOU  156  N   GLY A  31    15330  15238  16385   -438   1028    720       N  
ATOM    157  CA  GLY A  31     583.358 -40.290 202.321  1.00124.64           C  
ANISOU  157  CA  GLY A  31    15577  15304  16476   -455    982    793       C  
ATOM    158  C   GLY A  31     582.696 -41.615 201.982  1.00125.11           C  
ANISOU  158  C   GLY A  31    15624  15287  16624   -520   1017    825       C  
ATOM    159  O   GLY A  31     582.845 -42.604 202.712  1.00126.56           O  
ANISOU  159  O   GLY A  31    15927  15389  16770   -557   1027    912       O  
ATOM    160  N   VAL A  32     581.975 -41.632 200.865  1.00 72.04           N  
ANISOU  160  N   VAL A  32     8764   8587  10023   -535   1025    756       N  
ATOM    161  CA  VAL A  32     581.240 -42.808 200.415  1.00 72.96           C  
ANISOU  161  CA  VAL A  32     8837   8632  10254   -611   1052    747       C  
ATOM    162  C   VAL A  32     582.103 -43.725 199.556  1.00 74.08           C  
ANISOU  162  C   VAL A  32     8991   8702  10456   -572    935    723       C  
ATOM    163  O   VAL A  32     582.325 -44.904 199.885  1.00 75.44           O  
ANISOU  163  O   VAL A  32     9249   8746  10669   -605    926    772       O  
ATOM    164  CB  VAL A  32     579.997 -42.421 199.595  1.00 72.76           C  
ANISOU  164  CB  VAL A  32     8638   8678  10332   -642   1091    658       C  
ATOM    165  CG1 VAL A  32     579.489 -43.592 198.819  1.00 74.16           C  
ANISOU  165  CG1 VAL A  32     8748   8790  10640   -709   1069    607       C  
ATOM    166  CG2 VAL A  32     578.925 -41.945 200.491  1.00 72.47           C  
ANISOU  166  CG2 VAL A  32     8566   8681  10288   -700   1237    666       C  
ATOM    167  N   ILE A  33     582.596 -43.165 198.459  1.00 59.57           N  
ANISOU  167  N   ILE A  33     7072   6940   8623   -500    854    647       N  
ATOM    168  CA  ILE A  33     583.225 -43.941 197.404  1.00 61.13           C  
ANISOU  168  CA  ILE A  33     7242   7105   8880   -464    768    578       C  
ATOM    169  C   ILE A  33     584.546 -44.637 197.819  1.00 62.50           C  
ANISOU  169  C   ILE A  33     7516   7186   9045   -404    700    615       C  
ATOM    170  O   ILE A  33     585.277 -45.145 196.958  1.00 64.22           O  
ANISOU  170  O   ILE A  33     7702   7390   9310   -350    633    538       O  
ATOM    171  CB  ILE A  33     583.477 -43.031 196.182  1.00 60.69           C  
ANISOU  171  CB  ILE A  33     7092   7180   8789   -404    719    504       C  
ATOM    172  CG1 ILE A  33     583.717 -41.590 196.625  1.00 58.57           C  
ANISOU  172  CG1 ILE A  33     6830   6988   8435   -368    740    556       C  
ATOM    173  CG2 ILE A  33     582.283 -43.024 195.251  1.00 61.58           C  
ANISOU  173  CG2 ILE A  33     7092   7353   8952   -443    719    429       C  
ATOM    174  CD1 ILE A  33     585.015 -41.384 197.341  1.00 58.42           C  
ANISOU  174  CD1 ILE A  33     6891   6945   8360   -323    710    600       C  
ATOM    175  N   ASN A  34     584.843 -44.682 199.119  1.00110.27           N  
ANISOU  175  N   ASN A  34    13684  13182  15033   -406    713    724       N  
ATOM    176  CA  ASN A  34     586.138 -45.172 199.569  1.00111.83           C  
ANISOU  176  CA  ASN A  34    13965  13311  15216   -324    617    765       C  
ATOM    177  C   ASN A  34     586.089 -46.627 200.041  1.00113.26           C  
ANISOU  177  C   ASN A  34    14253  13307  15474   -343    599    835       C  
ATOM    178  O   ASN A  34     587.092 -47.333 199.986  1.00114.85           O  
ANISOU  178  O   ASN A  34    14488  13419  15731   -255    497    833       O  
ATOM    179  CB  ASN A  34     586.688 -44.237 200.662  1.00111.44           C  
ANISOU  179  CB  ASN A  34    13984  13329  15029   -293    600    832       C  
ATOM    180  CG  ASN A  34     586.401 -44.711 202.065  1.00112.39           C  
ANISOU  180  CG  ASN A  34    14264  13375  15062   -331    627    964       C  
ATOM    181  OD1 ASN A  34     587.243 -45.356 202.694  1.00113.80           O  
ANISOU  181  OD1 ASN A  34    14547  13475  15215   -271    529   1038       O  
ATOM    182  ND2 ASN A  34     585.225 -44.356 202.587  1.00111.89           N  
ANISOU  182  ND2 ASN A  34    14222  13347  14944   -425    760    997       N  
ATOM    183  N   ALA A  35     584.909 -47.069 200.474  1.00 75.36           N  
ANISOU  183  N   ALA A  35     9496   8440  10696   -457    702    894       N  
ATOM    184  CA  ALA A  35     584.708 -48.445 200.954  1.00 76.69           C  
ANISOU  184  CA  ALA A  35     9783   8404  10952   -506    709    986       C  
ATOM    185  C   ALA A  35     584.260 -49.402 199.855  1.00 78.15           C  
ANISOU  185  C   ALA A  35     9885   8481  11329   -550    707    869       C  
ATOM    186  O   ALA A  35     584.603 -50.569 199.909  1.00 79.87           O  
ANISOU  186  O   ALA A  35    10183   8502  11661   -535    657    899       O  
ATOM    187  CB  ALA A  35     583.715 -48.488 202.096  1.00 76.15           C  
ANISOU  187  CB  ALA A  35     9817   8311  10807   -631    846   1123       C  
ATOM    188  N   PRO A  36     583.481 -48.935 198.873  1.00 70.45           N  
ANISOU  188  N   PRO A  36     8754   7622  10393   -601    748    734       N  
ATOM    189  CA  PRO A  36     583.097 -49.935 197.887  1.00 72.20           C  
ANISOU  189  CA  PRO A  36     8908   7737  10787   -645    727    605       C  
ATOM    190  C   PRO A  36     583.678 -49.679 196.509  1.00 73.17           C  
ANISOU  190  C   PRO A  36     8915   7971  10914   -551    640    426       C  
ATOM    191  O   PRO A  36     582.960 -49.826 195.518  1.00 73.81           O  
ANISOU  191  O   PRO A  36     8886   8098  11060   -604    639    284       O  
ATOM    192  CB  PRO A  36     581.607 -49.758 197.818  1.00 72.22           C  
ANISOU  192  CB  PRO A  36     8816   7788  10835   -791    833    577       C  
ATOM    193  CG  PRO A  36     581.463 -48.292 197.868  1.00 69.32           C  
ANISOU  193  CG  PRO A  36     8379   7640  10320   -750    858    582       C  
ATOM    194  CD  PRO A  36     582.524 -47.817 198.855  1.00 68.18           C  
ANISOU  194  CD  PRO A  36     8368   7505  10033   -660    836    712       C  
ATOM    195  N   GLN A  37     584.948 -49.312 196.434  1.00 76.22           N  
ANISOU  195  N   GLN A  37     9319   8411  11229   -421    570    424       N  
ATOM    196  CA  GLN A  37     585.588 -48.988 195.163  1.00 77.49           C  
ANISOU  196  CA  GLN A  37     9375   8700  11367   -338    519    267       C  
ATOM    197  C   GLN A  37     585.723 -50.175 194.189  1.00 79.71           C  
ANISOU  197  C   GLN A  37     9624   8874  11786   -322    475     96       C  
ATOM    198  O   GLN A  37     585.344 -50.057 193.024  1.00 80.84           O  
ANISOU  198  O   GLN A  37     9672   9130  11911   -339    470    -57       O  
ATOM    199  CB  GLN A  37     586.946 -48.355 195.478  1.00 77.35           C  
ANISOU  199  CB  GLN A  37     9372   8752  11265   -221    474    312       C  
ATOM    200  CG  GLN A  37     588.150 -48.720 194.621  1.00 78.27           C  
ANISOU  200  CG  GLN A  37     9429   8884  11427   -108    418    177       C  
ATOM    201  CD  GLN A  37     589.374 -47.916 195.046  1.00 77.68           C  
ANISOU  201  CD  GLN A  37     9336   8900  11279    -20    386    228       C  
ATOM    202  OE1 GLN A  37     589.574 -47.650 196.238  1.00 76.49           O  
ANISOU  202  OE1 GLN A  37     9263   8709  11089    -12    359    366       O  
ATOM    203  NE2 GLN A  37     590.182 -47.509 194.075  1.00 78.49           N  
ANISOU  203  NE2 GLN A  37     9333   9134  11355     37    394    110       N  
ATOM    204  N   LYS A  38     586.221 -51.322 194.637  1.00 93.24           N  
ANISOU  204  N   LYS A  38    11422  10367  13637   -284    436    115       N  
ATOM    205  CA  LYS A  38     586.512 -52.376 193.667  1.00 95.01           C  
ANISOU  205  CA  LYS A  38    11611  10486  14003   -243    391    -81       C  
ATOM    206  C   LYS A  38     585.241 -53.050 193.217  1.00 95.90           C  
ANISOU  206  C   LYS A  38    11697  10513  14227   -383    418   -177       C  
ATOM    207  O   LYS A  38     585.240 -53.784 192.233  1.00 97.85           O  
ANISOU  207  O   LYS A  38    11894  10712  14571   -375    384   -385       O  
ATOM    208  CB  LYS A  38     587.510 -53.402 194.234  1.00 95.40           C  
ANISOU  208  CB  LYS A  38    11751  10300  14197   -134    324    -44       C  
ATOM    209  CG  LYS A  38     586.915 -54.490 195.115  1.00 95.48           C  
ANISOU  209  CG  LYS A  38    11897  10018  14364   -214    327     83       C  
ATOM    210  CD  LYS A  38     588.008 -55.333 195.782  1.00 96.05           C  
ANISOU  210  CD  LYS A  38    12077   9863  14554    -71    233    166       C  
ATOM    211  CE  LYS A  38     589.103 -55.713 194.798  1.00 97.00           C  
ANISOU  211  CE  LYS A  38    12097   9989  14770     91    165    -59       C  
ATOM    212  NZ  LYS A  38     590.243 -54.742 194.803  1.00 96.84           N  
ANISOU  212  NZ  LYS A  38    11993  10192  14612    223    132    -58       N  
ATOM    213  N   VAL A  39     584.159 -52.786 193.939  1.00 72.35           N  
ANISOU  213  N   VAL A  39     8735   7521  11234   -514    484    -44       N  
ATOM    214  CA  VAL A  39     582.849 -53.344 193.597  1.00 73.01           C  
ANISOU  214  CA  VAL A  39     8761   7536  11442   -671    517   -132       C  
ATOM    215  C   VAL A  39     582.289 -52.635 192.361  1.00 73.85           C  
ANISOU  215  C   VAL A  39     8714   7892  11453   -684    489   -309       C  
ATOM    216  O   VAL A  39     581.795 -53.262 191.420  1.00 75.67           O  
ANISOU  216  O   VAL A  39     8871   8104  11775   -735    446   -510       O  
ATOM    217  CB  VAL A  39     581.868 -53.220 194.778  1.00 71.52           C  
ANISOU  217  CB  VAL A  39     8618   7285  11270   -811    620     61       C  
ATOM    218  CG1 VAL A  39     580.543 -53.824 194.435  1.00 72.18           C  
ANISOU  218  CG1 VAL A  39     8611   7297  11516   -986    662    -42       C  
ATOM    219  CG2 VAL A  39     582.465 -53.896 196.030  1.00 71.26           C  
ANISOU  219  CG2 VAL A  39     8771   7019  11283   -792    639    267       C  
ATOM    220  N   ILE A  40     582.406 -51.316 192.361  1.00 66.38           N  
ANISOU  220  N   ILE A  40     7730   7173  10317   -630    502   -232       N  
ATOM    221  CA  ILE A  40     581.992 -50.508 191.228  1.00 67.39           C  
ANISOU  221  CA  ILE A  40     7742   7542  10323   -616    462   -352       C  
ATOM    222  C   ILE A  40     582.973 -50.659 190.088  1.00 69.41           C  
ANISOU  222  C   ILE A  40     7987   7881  10504   -508    403   -515       C  
ATOM    223  O   ILE A  40     582.592 -50.633 188.918  1.00 71.19           O  
ANISOU  223  O   ILE A  40     8138   8242  10669   -514    350   -684       O  
ATOM    224  CB  ILE A  40     581.891 -49.034 191.619  1.00 65.64           C  
ANISOU  224  CB  ILE A  40     7502   7499   9940   -584    496   -204       C  
ATOM    225  CG1 ILE A  40     581.166 -48.929 192.964  1.00 63.11           C  
ANISOU  225  CG1 ILE A  40     7214   7085   9680   -673    584    -41       C  
ATOM    226  CG2 ILE A  40     581.242 -48.211 190.499  1.00 66.77           C  
ANISOU  226  CG2 ILE A  40     7533   7865   9971   -575    443   -295       C  
ATOM    227  CD1 ILE A  40     580.682 -47.555 193.318  1.00 60.97           C  
ANISOU  227  CD1 ILE A  40     6897   6974   9295   -664    624     58       C  
ATOM    228  N   GLU A  41     584.247 -50.803 190.427  1.00 76.90           N  
ANISOU  228  N   GLU A  41     9005   8765  11447   -405    411   -470       N  
ATOM    229  CA  GLU A  41     585.240 -50.968 189.394  1.00 78.31           C  
ANISOU  229  CA  GLU A  41     9159   9028  11567   -302    385   -635       C  
ATOM    230  C   GLU A  41     584.941 -52.247 188.629  1.00 79.71           C  
ANISOU  230  C   GLU A  41     9317   9085  11882   -330    343   -868       C  
ATOM    231  O   GLU A  41     585.070 -52.285 187.410  1.00 80.88           O  
ANISOU  231  O   GLU A  41     9413   9378  11938   -299    318  -1066       O  
ATOM    232  CB  GLU A  41     586.637 -50.979 189.991  1.00 77.41           C  
ANISOU  232  CB  GLU A  41     9091   8849  11470   -186    398   -559       C  
ATOM    233  CG  GLU A  41     587.116 -49.604 190.426  1.00 76.06           C  
ANISOU  233  CG  GLU A  41     8916   8842  11143   -152    432   -394       C  
ATOM    234  CD  GLU A  41     588.561 -49.584 190.902  1.00 75.17           C  
ANISOU  234  CD  GLU A  41     8813   8694  11053    -39    427   -355       C  
ATOM    235  OE1 GLU A  41     589.190 -50.670 190.992  1.00 75.68           O  
ANISOU  235  OE1 GLU A  41     8894   8595  11266     33    390   -436       O  
ATOM    236  OE2 GLU A  41     589.066 -48.472 191.190  1.00 73.94           O  
ANISOU  236  OE2 GLU A  41     8640   8668  10785    -18    451   -250       O  
ATOM    237  N   GLU A  42     584.497 -53.279 189.339  1.00111.81           N  
ANISOU  237  N   GLU A  42    13433  12886  16162   -400    338   -845       N  
ATOM    238  CA  GLU A  42     584.046 -54.497 188.677  1.00113.16           C  
ANISOU  238  CA  GLU A  42    13585  12907  16502   -456    296  -1072       C  
ATOM    239  C   GLU A  42     582.886 -54.186 187.757  1.00114.21           C  
ANISOU  239  C   GLU A  42    13616  13223  16558   -556    257  -1214       C  
ATOM    240  O   GLU A  42     582.741 -54.796 186.694  1.00115.75           O  
ANISOU  240  O   GLU A  42    13766  13441  16772   -564    200  -1474       O  
ATOM    241  CB  GLU A  42     583.636 -55.561 189.687  1.00112.67           C  
ANISOU  241  CB  GLU A  42    13604  12509  16694   -546    312   -979       C  
ATOM    242  CG  GLU A  42     584.808 -56.213 190.377  1.00112.24           C  
ANISOU  242  CG  GLU A  42    13658  12231  16755   -424    305   -896       C  
ATOM    243  CD  GLU A  42     584.369 -57.131 191.485  1.00112.00           C  
ANISOU  243  CD  GLU A  42    13743  11872  16938   -516    325   -735       C  
ATOM    244  OE1 GLU A  42     583.216 -57.613 191.426  1.00112.44           O  
ANISOU  244  OE1 GLU A  42    13775  11828  17120   -686    350   -783       O  
ATOM    245  OE2 GLU A  42     585.172 -57.366 192.412  1.00111.50           O  
ANISOU  245  OE2 GLU A  42    13794  11655  16918   -424    313   -557       O  
ATOM    246  N   PHE A  43     582.060 -53.230 188.174  1.00 69.53           N  
ANISOU  246  N   PHE A  43     7914   7694  10809   -624    278  -1053       N  
ATOM    247  CA  PHE A  43     580.983 -52.746 187.318  1.00 70.60           C  
ANISOU  247  CA  PHE A  43     7936   8035  10854   -690    216  -1164       C  
ATOM    248  C   PHE A  43     581.575 -51.964 186.156  1.00 71.75           C  
ANISOU  248  C   PHE A  43     8066   8458  10739   -576    173  -1251       C  
ATOM    249  O   PHE A  43     581.132 -52.099 185.015  1.00 73.23           O  
ANISOU  249  O   PHE A  43     8195   8787  10844   -589     88  -1455       O  
ATOM    250  CB  PHE A  43     579.986 -51.885 188.106  1.00 69.34           C  
ANISOU  250  CB  PHE A  43     7722   7935  10686   -768    254   -971       C  
ATOM    251  CG  PHE A  43     579.097 -51.031 187.238  1.00 70.24           C  
ANISOU  251  CG  PHE A  43     7716   8307  10665   -775    173  -1039       C  
ATOM    252  CD1 PHE A  43     578.232 -51.607 186.326  1.00 71.61           C  
ANISOU  252  CD1 PHE A  43     7786   8526  10898   -848     69  -1268       C  
ATOM    253  CD2 PHE A  43     579.130 -49.647 187.335  1.00 69.77           C  
ANISOU  253  CD2 PHE A  43     7649   8436  10425   -701    183   -876       C  
ATOM    254  CE1 PHE A  43     577.415 -50.820 185.528  1.00 72.50           C  
ANISOU  254  CE1 PHE A  43     7787   8883  10878   -836    -38  -1323       C  
ATOM    255  CE2 PHE A  43     578.316 -48.856 186.541  1.00 70.70           C  
ANISOU  255  CE2 PHE A  43     7666   8772  10425   -687     89   -918       C  
ATOM    256  CZ  PHE A  43     577.462 -49.444 185.635  1.00 72.09           C  
ANISOU  256  CZ  PHE A  43     7738   9008  10647   -748    -30  -1136       C  
ATOM    257  N   TYR A  44     582.594 -51.165 186.446  1.00 72.63           N  
ANISOU  257  N   TYR A  44     8234   8647  10715   -473    232  -1099       N  
ATOM    258  CA  TYR A  44     583.274 -50.439 185.395  1.00 73.49           C  
ANISOU  258  CA  TYR A  44     8342   9002  10581   -379    225  -1157       C  
ATOM    259  C   TYR A  44     583.839 -51.391 184.356  1.00 74.40           C  
ANISOU  259  C   TYR A  44     8459   9123  10688   -336    203  -1431       C  
ATOM    260  O   TYR A  44     583.536 -51.279 183.168  1.00 75.64           O  
ANISOU  260  O   TYR A  44     8588   9477  10676   -333    145  -1595       O  
ATOM    261  CB  TYR A  44     584.381 -49.555 185.976  1.00 72.24           C  
ANISOU  261  CB  TYR A  44     8232   8883  10334   -296    307   -962       C  
ATOM    262  CG  TYR A  44     583.889 -48.183 186.411  1.00 71.89           C  
ANISOU  262  CG  TYR A  44     8178   8956  10179   -312    319   -745       C  
ATOM    263  CD1 TYR A  44     582.543 -47.957 186.639  1.00 71.96           C  
ANISOU  263  CD1 TYR A  44     8136   8969  10236   -390    273   -704       C  
ATOM    264  CD2 TYR A  44     584.771 -47.117 186.570  1.00 70.30           C  
ANISOU  264  CD2 TYR A  44     8007   8853   9850   -249    378   -601       C  
ATOM    265  CE1 TYR A  44     582.089 -46.725 187.035  1.00 70.65           C  
ANISOU  265  CE1 TYR A  44     7954   8894   9995   -387    284   -528       C  
ATOM    266  CE2 TYR A  44     584.330 -45.883 186.961  1.00 68.61           C  
ANISOU  266  CE2 TYR A  44     7792   8716   9562   -259    387   -422       C  
ATOM    267  CZ  TYR A  44     582.980 -45.685 187.196  1.00 68.99           C  
ANISOU  267  CZ  TYR A  44     7795   8760   9660   -319    339   -387       C  
ATOM    268  OH  TYR A  44     582.503 -44.447 187.585  1.00 66.20           O  
ANISOU  268  OH  TYR A  44     7430   8469   9254   -312    346   -226       O  
ATOM    269  N   THR A  45     584.629 -52.354 184.814  1.00 90.39           N  
ANISOU  269  N   THR A  45    10522  10927  12894   -295    241  -1489       N  
ATOM    270  CA  THR A  45     585.380 -53.195 183.894  1.00 91.09           C  
ANISOU  270  CA  THR A  45    10610  11015  12987   -223    243  -1759       C  
ATOM    271  C   THR A  45     584.473 -54.127 183.112  1.00 92.62           C  
ANISOU  271  C   THR A  45    10771  11166  13254   -302    156  -2029       C  
ATOM    272  O   THR A  45     584.783 -54.490 181.981  1.00 93.70           O  
ANISOU  272  O   THR A  45    10897  11424  13282   -258    140  -2290       O  
ATOM    273  CB  THR A  45     586.442 -54.027 184.613  1.00 90.28           C  
ANISOU  273  CB  THR A  45    10544  10659  13099   -138    286  -1759       C  
ATOM    274  OG1 THR A  45     587.112 -54.856 183.654  1.00 91.13           O  
ANISOU  274  OG1 THR A  45    10633  10766  13227    -58    294  -2059       O  
ATOM    275  CG2 THR A  45     585.812 -54.889 185.673  1.00 89.99           C  
ANISOU  275  CG2 THR A  45    10552  10300  13341   -218    253  -1673       C  
ATOM    276  N   GLN A  46     583.350 -54.508 183.702  1.00112.64           N  
ANISOU  276  N   GLN A  46    13286  13540  15972   -428    106  -1982       N  
ATOM    277  CA  GLN A  46     582.448 -55.396 183.004  1.00114.01           C  
ANISOU  277  CA  GLN A  46    13409  13660  16249   -524     14  -2250       C  
ATOM    278  C   GLN A  46     581.669 -54.603 181.977  1.00115.08           C  
ANISOU  278  C   GLN A  46    13478  14123  16125   -551    -77  -2328       C  
ATOM    279  O   GLN A  46     581.461 -55.058 180.853  1.00116.41           O  
ANISOU  279  O   GLN A  46    13620  14403  16207   -556   -159  -2616       O  
ATOM    280  CB  GLN A  46     581.513 -56.093 183.977  1.00113.64           C  
ANISOU  280  CB  GLN A  46    13348  13325  16506   -670      7  -2175       C  
ATOM    281  CG  GLN A  46     580.994 -57.408 183.432  1.00114.97           C  
ANISOU  281  CG  GLN A  46    13485  13307  16891   -762    -63  -2484       C  
ATOM    282  CD  GLN A  46     580.424 -58.294 184.512  1.00114.45           C  
ANISOU  282  CD  GLN A  46    13440  12875  17171   -900    -26  -2387       C  
ATOM    283  OE1 GLN A  46     580.449 -59.521 184.400  1.00115.44           O  
ANISOU  283  OE1 GLN A  46    13592  12726  17545   -946    -45  -2579       O  
ATOM    284  NE2 GLN A  46     579.904 -57.677 185.571  1.00112.90           N  
ANISOU  284  NE2 GLN A  46    13240  12666  16993   -971     36  -2089       N  
ATOM    285  N   THR A  47     581.254 -53.405 182.376  1.00 98.05           N  
ANISOU  285  N   THR A  47    11300  12117  13839   -556    -71  -2074       N  
ATOM    286  CA  THR A  47     580.545 -52.496 181.484  1.00 99.01           C  
ANISOU  286  CA  THR A  47    11367  12543  13708   -554   -172  -2090       C  
ATOM    287  C   THR A  47     581.365 -52.235 180.238  1.00 99.74           C  
ANISOU  287  C   THR A  47    11516  12883  13497   -450   -175  -2228       C  
ATOM    288  O   THR A  47     580.839 -52.241 179.123  1.00100.91           O  
ANISOU  288  O   THR A  47    11640  13237  13466   -457   -293  -2417       O  
ATOM    289  CB  THR A  47     580.234 -51.153 182.165  1.00 98.23           C  
ANISOU  289  CB  THR A  47    11256  12541  13525   -539   -143  -1773       C  
ATOM    290  OG1 THR A  47     579.437 -51.386 183.329  1.00 97.18           O  
ANISOU  290  OG1 THR A  47    11069  12203  13653   -642   -116  -1656       O  
ATOM    291  CG2 THR A  47     579.487 -50.216 181.219  1.00 99.41           C  
ANISOU  291  CG2 THR A  47    11358  12985  13430   -516   -269  -1775       C  
ATOM    292  N   TRP A  48     582.660 -52.008 180.439  1.00 93.37           N  
ANISOU  292  N   TRP A  48    10782  12067  12628   -356    -44  -2139       N  
ATOM    293  CA  TRP A  48     583.561 -51.724 179.334  1.00 93.65           C  
ANISOU  293  CA  TRP A  48    10867  12340  12377   -265      3  -2252       C  
ATOM    294  C   TRP A  48     583.569 -52.868 178.318  1.00 94.88           C  
ANISOU  294  C   TRP A  48    11017  12511  12521   -266    -49  -2635       C  
ATOM    295  O   TRP A  48     583.462 -52.649 177.108  1.00 95.85           O  
ANISOU  295  O   TRP A  48    11162  12905  12351   -245   -102  -2790       O  
ATOM    296  CB  TRP A  48     584.976 -51.474 179.851  1.00 92.25           C  
ANISOU  296  CB  TRP A  48    10728  12106  12217   -178    165  -2124       C  
ATOM    297  CG  TRP A  48     585.899 -50.891 178.810  1.00 92.17           C  
ANISOU  297  CG  TRP A  48    10755  12371  11893   -103    254  -2174       C  
ATOM    298  CD1 TRP A  48     586.452 -51.543 177.737  1.00 93.00           C  
ANISOU  298  CD1 TRP A  48    10872  12594  11870    -58    292  -2469       C  
ATOM    299  CD2 TRP A  48     586.375 -49.540 178.740  1.00 91.13           C  
ANISOU  299  CD2 TRP A  48    10658  12428  11538    -77    335  -1925       C  
ATOM    300  NE1 TRP A  48     587.237 -50.682 177.007  1.00 92.59           N  
ANISOU  300  NE1 TRP A  48    10859  12809  11512    -11    407  -2407       N  
ATOM    301  CE2 TRP A  48     587.206 -49.442 177.603  1.00 91.32           C  
ANISOU  301  CE2 TRP A  48    10715  12685  11297    -28    432  -2065       C  
ATOM    302  CE3 TRP A  48     586.174 -48.392 179.531  1.00 89.97           C  
ANISOU  302  CE3 TRP A  48    10521  12270  11395    -96    343  -1604       C  
ATOM    303  CZ2 TRP A  48     587.841 -48.247 177.236  1.00 90.37           C  
ANISOU  303  CZ2 TRP A  48    10638  12774  10924    -12    544  -1872       C  
ATOM    304  CZ3 TRP A  48     586.803 -47.206 179.164  1.00 88.88           C  
ANISOU  304  CZ3 TRP A  48    10426  12321  11024    -71    436  -1428       C  
ATOM    305  CH2 TRP A  48     587.625 -47.144 178.029  1.00 89.05           C  
ANISOU  305  CH2 TRP A  48    10482  12562  10792    -37    538  -1550       C  
ATOM    306  N   VAL A  49     583.679 -54.090 178.827  1.00 84.66           N  
ANISOU  306  N   VAL A  49     9706  10919  11543   -290    -39  -2787       N  
ATOM    307  CA  VAL A  49     583.833 -55.262 177.980  1.00 85.84           C  
ANISOU  307  CA  VAL A  49     9854  11022  11738   -281    -71  -3174       C  
ATOM    308  C   VAL A  49     582.608 -55.502 177.122  1.00 87.48           C  
ANISOU  308  C   VAL A  49    10018  11361  11859   -374   -243  -3395       C  
ATOM    309  O   VAL A  49     582.716 -55.740 175.913  1.00 88.64           O  
ANISOU  309  O   VAL A  49    10184  11716  11778   -343   -287  -3679       O  
ATOM    310  CB  VAL A  49     584.118 -56.488 178.816  1.00 85.41           C  
ANISOU  310  CB  VAL A  49     9798  10568  12085   -290    -37  -3252       C  
ATOM    311  CG1 VAL A  49     584.150 -57.721 177.940  1.00 86.78           C  
ANISOU  311  CG1 VAL A  49     9967  10661  12345   -287    -84  -3679       C  
ATOM    312  CG2 VAL A  49     585.432 -56.298 179.548  1.00 84.24           C  
ANISOU  312  CG2 VAL A  49     9684  10319  12004   -171    104  -3073       C  
ATOM    313  N   HIS A  50     581.447 -55.433 177.758  1.00134.33           N  
ANISOU  313  N   HIS A  50    15884  17185  17968   -489   -338  -3273       N  
ATOM    314  CA  HIS A  50     580.197 -55.636 177.067  1.00135.39           C  
ANISOU  314  CA  HIS A  50    15939  17434  18069   -587   -522  -3472       C  
ATOM    315  C   HIS A  50     580.061 -54.631 175.941  1.00136.17           C  
ANISOU  315  C   HIS A  50    16063  17948  17726   -521   -609  -3470       C  
ATOM    316  O   HIS A  50     579.735 -54.991 174.810  1.00137.55           O  
ANISOU  316  O   HIS A  50    16234  18306  17721   -528   -736  -3769       O  
ATOM    317  CB  HIS A  50     579.031 -55.503 178.037  1.00134.85           C  
ANISOU  317  CB  HIS A  50    15769  17211  18256   -714   -577  -3288       C  
ATOM    318  CG  HIS A  50     578.921 -56.639 179.016  1.00134.46           C  
ANISOU  318  CG  HIS A  50    15703  16752  18635   -816   -514  -3319       C  
ATOM    319  ND1 HIS A  50     579.898 -57.593 179.167  1.00134.54           N  
ANISOU  319  ND1 HIS A  50    15795  16521  18805   -766   -420  -3443       N  
ATOM    320  CD2 HIS A  50     577.930 -56.965 179.880  1.00134.01           C  
ANISOU  320  CD2 HIS A  50    15557  16481  18877   -966   -528  -3235       C  
ATOM    321  CE1 HIS A  50     579.520 -58.467 180.092  1.00134.20           C  
ANISOU  321  CE1 HIS A  50    15737  16114  19140   -879   -390  -3412       C  
ATOM    322  NE2 HIS A  50     578.335 -58.108 180.537  1.00133.85           N  
ANISOU  322  NE2 HIS A  50    15592  16086  19177  -1012   -441  -3285       N  
ATOM    323  N   ARG A  51     580.342 -53.372 176.265  1.00105.79           N  
ANISOU  323  N   ARG A  51    12254  14240  13700   -457   -543  -3129       N  
ATOM    324  CA  ARG A  51     580.118 -52.257 175.347  1.00106.33           C  
ANISOU  324  CA  ARG A  51    12362  14672  13366   -397   -630  -3037       C  
ATOM    325  C   ARG A  51     581.091 -52.284 174.168  1.00106.90           C  
ANISOU  325  C   ARG A  51    12547  14984  13087   -311   -564  -3211       C  
ATOM    326  O   ARG A  51     580.682 -52.326 173.003  1.00108.05           O  
ANISOU  326  O   ARG A  51    12718  15386  12951   -303   -701  -3415       O  
ATOM    327  CB  ARG A  51     580.224 -50.917 176.109  1.00105.08           C  
ANISOU  327  CB  ARG A  51    12224  14540  13162   -357   -556  -2619       C  
ATOM    328  CG  ARG A  51     579.544 -49.717 175.438  1.00106.01           C  
ANISOU  328  CG  ARG A  51    12355  14951  12974   -314   -696  -2462       C  
ATOM    329  CD  ARG A  51     579.782 -48.395 176.187  1.00104.64           C  
ANISOU  329  CD  ARG A  51    12215  14767  12775   -267   -604  -2066       C  
ATOM    330  NE  ARG A  51     578.961 -48.234 177.392  1.00103.50           N  
ANISOU  330  NE  ARG A  51    11959  14420  12948   -323   -624  -1912       N  
ATOM    331  CZ  ARG A  51     579.008 -47.174 178.201  1.00102.46           C  
ANISOU  331  CZ  ARG A  51    11836  14241  12854   -292   -553  -1603       C  
ATOM    332  NH1 ARG A  51     579.836 -46.168 177.946  1.00102.45           N  
ANISOU  332  NH1 ARG A  51    11948  14360  12618   -214   -465  -1404       N  
ATOM    333  NH2 ARG A  51     578.226 -47.116 179.273  1.00101.25           N  
ANISOU  333  NH2 ARG A  51    11577  13917  12977   -347   -558  -1503       N  
ATOM    334  N   TYR A  52     582.382 -52.283 174.476  1.00125.21           N  
ANISOU  334  N   TYR A  52    14926  17229  15420   -246   -354  -3142       N  
ATOM    335  CA  TYR A  52     583.387 -52.008 173.460  1.00125.40           C  
ANISOU  335  CA  TYR A  52    15048  17514  15086   -165   -239  -3228       C  
ATOM    336  C   TYR A  52     584.030 -53.270 172.893  1.00126.34           C  
ANISOU  336  C   TYR A  52    15169  17578  15255   -139   -174  -3634       C  
ATOM    337  O   TYR A  52     584.976 -53.175 172.113  1.00126.95           O  
ANISOU  337  O   TYR A  52    15311  17855  15068    -71    -37  -3742       O  
ATOM    338  CB  TYR A  52     584.449 -51.054 174.038  1.00123.72           C  
ANISOU  338  CB  TYR A  52    14876  17303  14831   -109    -38  -2903       C  
ATOM    339  CG  TYR A  52     583.885 -49.677 174.339  1.00122.98           C  
ANISOU  339  CG  TYR A  52    14804  17310  14614   -120    -96  -2531       C  
ATOM    340  CD1 TYR A  52     583.042 -49.047 173.434  1.00124.14           C  
ANISOU  340  CD1 TYR A  52    14996  17720  14452   -119   -258  -2501       C  
ATOM    341  CD2 TYR A  52     584.166 -49.023 175.530  1.00121.23           C  
ANISOU  341  CD2 TYR A  52    14558  16912  14591   -121     -7  -2223       C  
ATOM    342  CE1 TYR A  52     582.505 -47.800 173.697  1.00123.57           C  
ANISOU  342  CE1 TYR A  52    14941  17714  14296   -110   -324  -2168       C  
ATOM    343  CE2 TYR A  52     583.631 -47.771 175.802  1.00120.66           C  
ANISOU  343  CE2 TYR A  52    14504  16911  14429   -123    -60  -1910       C  
ATOM    344  CZ  TYR A  52     582.800 -47.166 174.881  1.00121.83           C  
ANISOU  344  CZ  TYR A  52    14694  17301  14295   -112   -217  -1881       C  
ATOM    345  OH  TYR A  52     582.261 -45.920 175.137  1.00121.32           O  
ANISOU  345  OH  TYR A  52    14646  17283  14165    -95   -280  -1573       O  
ATOM    346  N   GLY A  53     583.499 -54.438 173.260  1.00132.43           N  
ANISOU  346  N   GLY A  53    15870  18079  16369   -198   -264  -3865       N  
ATOM    347  CA  GLY A  53     584.019 -55.711 172.787  1.00133.20           C  
ANISOU  347  CA  GLY A  53    15966  18066  16578   -172   -220  -4273       C  
ATOM    348  C   GLY A  53     585.516 -55.831 173.004  1.00132.21           C  
ANISOU  348  C   GLY A  53    15862  17876  16498    -61     13  -4265       C  
ATOM    349  O   GLY A  53     586.239 -56.355 172.159  1.00133.14           O  
ANISOU  349  O   GLY A  53    16004  18104  16481      7    104  -4574       O  
ATOM    350  N   GLU A  54     585.970 -55.332 174.148  1.00136.32           N  
ANISOU  350  N   GLU A  54    16361  18225  17208    -42    108  -3925       N  
ATOM    351  CA  GLU A  54     587.387 -55.210 174.486  1.00135.04           C  
ANISOU  351  CA  GLU A  54    16194  18023  17094     63    314  -3850       C  
ATOM    352  C   GLU A  54     587.439 -55.081 176.006  1.00133.47           C  
ANISOU  352  C   GLU A  54    15960  17515  17237     51    322  -3535       C  
ATOM    353  O   GLU A  54     586.472 -54.631 176.599  1.00133.12           O  
ANISOU  353  O   GLU A  54    15915  17416  17248    -35    215  -3311       O  
ATOM    354  CB  GLU A  54     588.024 -53.989 173.796  1.00135.06           C  
ANISOU  354  CB  GLU A  54    16243  18396  16676    100    443  -3693       C  
ATOM    355  CG  GLU A  54     589.524 -53.775 174.076  1.00132.88           C  
ANISOU  355  CG  GLU A  54    15928  18118  16444    193    670  -3628       C  
ATOM    356  CD  GLU A  54     590.041 -52.359 173.740  1.00132.18           C  
ANISOU  356  CD  GLU A  54    15880  18330  16014    186    802  -3354       C  
ATOM    357  OE1 GLU A  54     589.980 -51.464 174.622  1.00130.61           O  
ANISOU  357  OE1 GLU A  54    15675  18058  15891    156    798  -2998       O  
ATOM    358  OE2 GLU A  54     590.522 -52.149 172.599  1.00133.26           O  
ANISOU  358  OE2 GLU A  54    16058  18767  15808    206    921  -3499       O  
ATOM    359  N   SER A  55     588.531 -55.468 176.655  1.00125.79           N  
ANISOU  359  N   SER A  55    14955  16349  16490    142    439  -3519       N  
ATOM    360  CA  SER A  55     588.570 -55.349 178.115  1.00124.68           C  
ANISOU  360  CA  SER A  55    14801  15932  16638    133    428  -3216       C  
ATOM    361  C   SER A  55     589.306 -54.095 178.587  1.00123.02           C  
ANISOU  361  C   SER A  55    14584  15866  16293    168    536  -2897       C  
ATOM    362  O   SER A  55     590.107 -53.514 177.858  1.00122.70           O  
ANISOU  362  O   SER A  55    14532  16081  16009    217    659  -2931       O  
ATOM    363  CB  SER A  55     589.200 -56.588 178.749  1.00124.92           C  
ANISOU  363  CB  SER A  55    14809  15608  17049    213    442  -3353       C  
ATOM    364  OG  SER A  55     588.907 -56.636 180.143  1.00124.14           O  
ANISOU  364  OG  SER A  55    14729  15226  17214    176    389  -3071       O  
ATOM    365  N   ILE A  56     589.031 -53.684 179.820  1.00120.70           N  
ANISOU  365  N   ILE A  56    14296  15404  16159    131    498  -2594       N  
ATOM    366  CA  ILE A  56     589.522 -52.404 180.303  1.00119.18           C  
ANISOU  366  CA  ILE A  56    14102  15341  15841    138    573  -2292       C  
ATOM    367  C   ILE A  56     590.994 -52.492 180.697  1.00118.11           C  
ANISOU  367  C   ILE A  56    13908  15149  15820    249    690  -2292       C  
ATOM    368  O   ILE A  56     591.450 -53.490 181.268  1.00118.30           O  
ANISOU  368  O   ILE A  56    13905  14918  16123    322    670  -2387       O  
ATOM    369  CB  ILE A  56     588.668 -51.881 181.495  1.00118.51           C  
ANISOU  369  CB  ILE A  56    14045  15115  15869     60    493  -1991       C  
ATOM    370  CG1 ILE A  56     588.673 -50.355 181.531  1.00117.40           C  
ANISOU  370  CG1 ILE A  56    13918  15188  15501     34    536  -1730       C  
ATOM    371  CG2 ILE A  56     589.143 -52.444 182.828  1.00117.70           C  
ANISOU  371  CG2 ILE A  56    13941  14711  16070    100    490  -1882       C  
ATOM    372  CD1 ILE A  56     587.744 -49.775 182.576  1.00116.93           C  
ANISOU  372  CD1 ILE A  56    13879  15024  15525    -38    467  -1473       C  
ATOM    373  N   LEU A  57     591.736 -51.446 180.343  1.00 86.83           N  
ANISOU  373  N   LEU A  57     9919  11425  11646    262    810  -2189       N  
ATOM    374  CA  LEU A  57     593.140 -51.316 180.710  1.00 85.78           C  
ANISOU  374  CA  LEU A  57     9697  11282  11612    351    925  -2172       C  
ATOM    375  C   LEU A  57     593.252 -50.812 182.154  1.00 84.33           C  
ANISOU  375  C   LEU A  57     9511  10928  11601    344    871  -1878       C  
ATOM    376  O   LEU A  57     592.495 -49.930 182.555  1.00 83.81           O  
ANISOU  376  O   LEU A  57     9507  10897  11440    256    826  -1646       O  
ATOM    377  CB  LEU A  57     593.848 -50.359 179.751  1.00 85.44           C  
ANISOU  377  CB  LEU A  57     9622  11564  11279    337   1092  -2172       C  
ATOM    378  CG  LEU A  57     595.037 -50.883 178.951  1.00 86.00           C  
ANISOU  378  CG  LEU A  57     9591  11751  11336    428   1251  -2452       C  
ATOM    379  CD1 LEU A  57     594.603 -51.339 177.566  1.00 87.92           C  
ANISOU  379  CD1 LEU A  57     9890  12183  11334    415   1283  -2725       C  
ATOM    380  CD2 LEU A  57     596.118 -49.810 178.877  1.00 84.71           C  
ANISOU  380  CD2 LEU A  57     9344  11779  11063    413   1427  -2318       C  
ATOM    381  N   PRO A  58     594.195 -51.364 182.937  1.00 87.45           N  
ANISOU  381  N   PRO A  58     9836  11143  12247    446    867  -1898       N  
ATOM    382  CA  PRO A  58     594.295 -51.024 184.364  1.00 86.18           C  
ANISOU  382  CA  PRO A  58     9691  10814  12241    448    791  -1640       C  
ATOM    383  C   PRO A  58     594.368 -49.518 184.646  1.00 84.67           C  
ANISOU  383  C   PRO A  58     9499  10793  11879    369    841  -1395       C  
ATOM    384  O   PRO A  58     593.656 -49.037 185.526  1.00 84.02           O  
ANISOU  384  O   PRO A  58     9491  10628  11807    306    765  -1180       O  
ATOM    385  CB  PRO A  58     595.583 -51.730 184.797  1.00 86.08           C  
ANISOU  385  CB  PRO A  58     9571  10670  12464    596    794  -1747       C  
ATOM    386  CG  PRO A  58     596.334 -51.990 183.526  1.00 86.85           C  
ANISOU  386  CG  PRO A  58     9565  10950  12485    656    931  -2029       C  
ATOM    387  CD  PRO A  58     595.293 -52.240 182.497  1.00 88.04           C  
ANISOU  387  CD  PRO A  58     9805  11190  12455    577    936  -2166       C  
ATOM    388  N   THR A  59     595.209 -48.796 183.911  1.00136.30           N  
ANISOU  388  N   THR A  59    15957  17558  18272    367    979  -1435       N  
ATOM    389  CA  THR A  59     595.345 -47.357 184.099  1.00134.70           C  
ANISOU  389  CA  THR A  59    15756  17496  17929    284   1038  -1213       C  
ATOM    390  C   THR A  59     594.077 -46.631 183.677  1.00134.56           C  
ANISOU  390  C   THR A  59    15859  17571  17695    180   1010  -1082       C  
ATOM    391  O   THR A  59     593.676 -45.660 184.320  1.00133.10           O  
ANISOU  391  O   THR A  59    15720  17371  17481    118    978   -859       O  
ATOM    392  CB  THR A  59     596.539 -46.790 183.313  1.00134.36           C  
ANISOU  392  CB  THR A  59    15597  17669  17785    285   1218  -1287       C  
ATOM    393  OG1 THR A  59     597.746 -47.376 183.804  1.00134.55           O  
ANISOU  393  OG1 THR A  59    15473  17608  18043    393   1232  -1405       O  
ATOM    394  CG2 THR A  59     596.628 -45.282 183.486  1.00132.76           C  
ANISOU  394  CG2 THR A  59    15409  17577  17455    180   1281  -1049       C  
ATOM    395  N   THR A  60     593.449 -47.096 182.598  1.00 68.63           N  
ANISOU  395  N   THR A  60     7555   9321   9201    169   1010  -1236       N  
ATOM    396  CA  THR A  60     592.168 -46.526 182.166  1.00 69.08           C  
ANISOU  396  CA  THR A  60     7713   9466   9069     90    944  -1133       C  
ATOM    397  C   THR A  60     591.198 -46.513 183.341  1.00 68.78           C  
ANISOU  397  C   THR A  60     7719   9228   9186     58    812   -974       C  
ATOM    398  O   THR A  60     590.880 -45.454 183.880  1.00 67.66           O  
ANISOU  398  O   THR A  60     7608   9096   9006     12    802   -755       O  
ATOM    399  CB  THR A  60     591.542 -47.312 181.005  1.00 71.13           C  
ANISOU  399  CB  THR A  60     8006   9822   9196     93    910  -1363       C  
ATOM    400  OG1 THR A  60     592.359 -47.185 179.837  1.00 71.48           O  
ANISOU  400  OG1 THR A  60     8030  10098   9032    112   1053  -1500       O  
ATOM    401  CG2 THR A  60     590.158 -46.781 180.702  1.00 71.85           C  
ANISOU  401  CG2 THR A  60     8179   9986   9135     25    798  -1256       C  
ATOM    402  N   LEU A  61     590.771 -47.713 183.735  1.00 70.30           N  
ANISOU  402  N   LEU A  61     7915   9233   9564     80    727  -1094       N  
ATOM    403  CA  LEU A  61     590.052 -47.979 184.979  1.00 70.21           C  
ANISOU  403  CA  LEU A  61     7939   9001   9738     51    633   -965       C  
ATOM    404  C   LEU A  61     590.503 -47.099 186.141  1.00 68.04           C  
ANISOU  404  C   LEU A  61     7667   8675   9512     50    650   -737       C  
ATOM    405  O   LEU A  61     589.709 -46.725 186.999  1.00 67.45           O  
ANISOU  405  O   LEU A  61     7637   8518   9474     -1    601   -579       O  
ATOM    406  CB  LEU A  61     590.237 -49.447 185.377  1.00 71.35           C  
ANISOU  406  CB  LEU A  61     8079   8913  10119    101    586  -1114       C  
ATOM    407  CG  LEU A  61     589.123 -50.243 186.069  1.00 72.28           C  
ANISOU  407  CG  LEU A  61     8249   8809  10404     41    494  -1089       C  
ATOM    408  CD1 LEU A  61     589.719 -51.468 186.771  1.00 72.42           C  
ANISOU  408  CD1 LEU A  61     8281   8559  10675    111    464  -1148       C  
ATOM    409  CD2 LEU A  61     588.268 -49.416 187.026  1.00 71.05           C  
ANISOU  409  CD2 LEU A  61     8133   8633  10231    -39    472   -844       C  
ATOM    410  N   THR A  62     591.780 -46.776 186.190  1.00 79.34           N  
ANISOU  410  N   THR A  62     9038  10158  10949    102    722   -737       N  
ATOM    411  CA  THR A  62     592.249 -45.975 187.287  1.00 77.33           C  
ANISOU  411  CA  THR A  62     8778   9856  10747     98    721   -553       C  
ATOM    412  C   THR A  62     591.828 -44.503 187.095  1.00 75.65           C  
ANISOU  412  C   THR A  62     8595   9784  10364     21    762   -389       C  
ATOM    413  O   THR A  62     591.163 -43.935 187.966  1.00 74.21           O  
ANISOU  413  O   THR A  62     8464   9531  10203    -19    716   -235       O  
ATOM    414  CB  THR A  62     593.767 -46.137 187.445  1.00 76.87           C  
ANISOU  414  CB  THR A  62     8618   9802  10786    177    767   -624       C  
ATOM    415  OG1 THR A  62     594.017 -47.356 188.148  1.00 77.94           O  
ANISOU  415  OG1 THR A  62     8753   9733  11126    262    680   -693       O  
ATOM    416  CG2 THR A  62     594.380 -44.979 188.232  1.00 74.80           C  
ANISOU  416  CG2 THR A  62     8327   9572  10524    150    784   -461       C  
ATOM    417  N   THR A  63     592.176 -43.893 185.960  1.00 83.46           N  
ANISOU  417  N   THR A  63     9563  10964  11185      1    854   -420       N  
ATOM    418  CA  THR A  63     591.823 -42.490 185.721  1.00 82.05           C  
ANISOU  418  CA  THR A  63     9428  10892  10857    -64    890   -247       C  
ATOM    419  C   THR A  63     590.314 -42.348 185.592  1.00 82.75           C  
ANISOU  419  C   THR A  63     9590  10973  10877    -93    798   -186       C  
ATOM    420  O   THR A  63     589.739 -41.336 185.973  1.00 81.18           O  
ANISOU  420  O   THR A  63     9431  10764  10651   -126    777    -23       O  
ATOM    421  CB  THR A  63     592.491 -41.916 184.451  1.00 82.59           C  
ANISOU  421  CB  THR A  63     9480  11165  10734    -88   1018   -272       C  
ATOM    422  OG1 THR A  63     591.649 -42.150 183.321  1.00 84.54           O  
ANISOU  422  OG1 THR A  63     9790  11537  10796    -92    992   -337       O  
ATOM    423  CG2 THR A  63     593.858 -42.549 184.213  1.00 82.99           C  
ANISOU  423  CG2 THR A  63     9421  11256  10856    -44   1119   -437       C  
ATOM    424  N   LEU A  64     589.677 -43.379 185.054  1.00 60.31           N  
ANISOU  424  N   LEU A  64     6754   8132   8030    -78    740   -337       N  
ATOM    425  CA  LEU A  64     588.222 -43.412 184.932  1.00 61.68           C  
ANISOU  425  CA  LEU A  64     6961   8299   8174   -108    638   -318       C  
ATOM    426  C   LEU A  64     587.537 -43.396 186.301  1.00 60.39           C  
ANISOU  426  C   LEU A  64     6804   7959   8184   -132    586   -208       C  
ATOM    427  O   LEU A  64     586.713 -42.521 186.573  1.00 59.22           O  
ANISOU  427  O   LEU A  64     6670   7823   8007   -156    556    -77       O  
ATOM    428  CB  LEU A  64     587.777 -44.647 184.147  1.00 64.72           C  
ANISOU  428  CB  LEU A  64     7334   8701   8555   -100    583   -540       C  
ATOM    429  CG  LEU A  64     586.272 -44.824 183.924  1.00 66.81           C  
ANISOU  429  CG  LEU A  64     7599   8972   8812   -139    464   -565       C  
ATOM    430  CD1 LEU A  64     585.717 -43.650 183.162  1.00 66.82           C  
ANISOU  430  CD1 LEU A  64     7631   9158   8601   -140    430   -450       C  
ATOM    431  CD2 LEU A  64     585.968 -46.099 183.171  1.00 69.25           C  
ANISOU  431  CD2 LEU A  64     7889   9283   9141   -143    409   -819       C  
ATOM    432  N   TRP A  65     587.864 -44.369 187.150  1.00 62.12           N  
ANISOU  432  N   TRP A  65     7014   8013   8576   -119    578   -261       N  
ATOM    433  CA  TRP A  65     587.381 -44.333 188.518  1.00 60.77           C  
ANISOU  433  CA  TRP A  65     6869   7688   8534   -146    555   -141       C  
ATOM    434  C   TRP A  65     587.936 -43.135 189.277  1.00 57.30           C  
ANISOU  434  C   TRP A  65     6444   7261   8066   -142    595     18       C  
ATOM    435  O   TRP A  65     587.284 -42.657 190.203  1.00 55.46           O  
ANISOU  435  O   TRP A  65     6237   6964   7870   -171    586    128       O  
ATOM    436  CB  TRP A  65     587.728 -45.603 189.292  1.00 62.20           C  
ANISOU  436  CB  TRP A  65     7067   7681   8886   -127    534   -198       C  
ATOM    437  CG  TRP A  65     587.402 -45.435 190.759  1.00 60.87           C  
ANISOU  437  CG  TRP A  65     6949   7382   8799   -156    528    -45       C  
ATOM    438  CD1 TRP A  65     588.272 -45.140 191.765  1.00 59.44           C  
ANISOU  438  CD1 TRP A  65     6797   7145   8643   -120    533     52       C  
ATOM    439  CD2 TRP A  65     586.102 -45.485 191.358  1.00 60.54           C  
ANISOU  439  CD2 TRP A  65     6927   7274   8800   -230    522     20       C  
ATOM    440  NE1 TRP A  65     587.605 -45.038 192.962  1.00 58.47           N  
ANISOU  440  NE1 TRP A  65     6735   6928   8551   -165    531    173       N  
ATOM    441  CE2 TRP A  65     586.271 -45.243 192.741  1.00 58.31           C  
ANISOU  441  CE2 TRP A  65     6706   6899   8548   -236    541    158       C  
ATOM    442  CE3 TRP A  65     584.806 -45.721 190.863  1.00 61.51           C  
ANISOU  442  CE3 TRP A  65     7010   7418   8942   -295    503    -38       C  
ATOM    443  CZ2 TRP A  65     585.193 -45.233 193.639  1.00 56.45           C  
ANISOU  443  CZ2 TRP A  65     6501   6597   8349   -309    570    243       C  
ATOM    444  CZ3 TRP A  65     583.733 -45.703 191.756  1.00 59.66           C  
ANISOU  444  CZ3 TRP A  65     6780   7110   8777   -369    527     43       C  
ATOM    445  CH2 TRP A  65     583.937 -45.459 193.132  1.00 56.98           C  
ANISOU  445  CH2 TRP A  65     6511   6683   8455   -378    574    185       C  
ATOM    446  N   SER A  66     589.136 -42.664 188.924  1.00 61.40           N  
ANISOU  446  N   SER A  66     6938   7858   8533   -113    649     14       N  
ATOM    447  CA  SER A  66     589.683 -41.460 189.568  1.00 58.60           C  
ANISOU  447  CA  SER A  66     6587   7511   8166   -126    685    146       C  
ATOM    448  C   SER A  66     588.742 -40.265 189.312  1.00 57.31           C  
ANISOU  448  C   SER A  66     6456   7408   7911   -162    687    261       C  
ATOM    449  O   SER A  66     588.398 -39.516 190.221  1.00 55.26           O  
ANISOU  449  O   SER A  66     6222   7085   7690   -179    680    363       O  
ATOM    450  CB  SER A  66     591.118 -41.144 189.074  1.00 58.45           C  
ANISOU  450  CB  SER A  66     6508   7578   8122   -110    758    108       C  
ATOM    451  OG  SER A  66     592.139 -41.688 189.915  1.00 58.32           O  
ANISOU  451  OG  SER A  66     6447   7476   8235    -66    738     65       O  
ATOM    452  N   LEU A  67     588.316 -40.108 188.066  1.00 64.98           N  
ANISOU  452  N   LEU A  67     7430   8501   8756   -164    687    237       N  
ATOM    453  CA  LEU A  67     587.414 -39.030 187.699  1.00 64.59           C  
ANISOU  453  CA  LEU A  67     7412   8506   8624   -174    663    350       C  
ATOM    454  C   LEU A  67     586.048 -39.145 188.403  1.00 64.51           C  
ANISOU  454  C   LEU A  67     7395   8416   8701   -177    593    370       C  
ATOM    455  O   LEU A  67     585.381 -38.150 188.646  1.00 63.35           O  
ANISOU  455  O   LEU A  67     7257   8256   8556   -171    577    473       O  
ATOM    456  CB  LEU A  67     587.227 -39.013 186.185  1.00 67.22           C  
ANISOU  456  CB  LEU A  67     7761   9001   8779   -163    652    315       C  
ATOM    457  CG  LEU A  67     586.330 -37.902 185.660  1.00 67.44           C  
ANISOU  457  CG  LEU A  67     7831   9089   8706   -151    601    449       C  
ATOM    458  CD1 LEU A  67     586.915 -36.543 186.035  1.00 64.97           C  
ANISOU  458  CD1 LEU A  67     7557   8726   8404   -168    670    615       C  
ATOM    459  CD2 LEU A  67     586.180 -38.043 184.164  1.00 70.09           C  
ANISOU  459  CD2 LEU A  67     8200   9603   8829   -135    571    407       C  
ATOM    460  N   SER A  68     585.629 -40.359 188.732  1.00 63.32           N  
ANISOU  460  N   SER A  68     7219   8201   8638   -188    561    266       N  
ATOM    461  CA  SER A  68     584.330 -40.559 189.365  1.00 63.35           C  
ANISOU  461  CA  SER A  68     7197   8138   8735   -213    521    273       C  
ATOM    462  C   SER A  68     584.356 -40.004 190.770  1.00 60.06           C  
ANISOU  462  C   SER A  68     6806   7618   8397   -225    568    372       C  
ATOM    463  O   SER A  68     583.347 -39.520 191.285  1.00 59.14           O  
ANISOU  463  O   SER A  68     6666   7479   8326   -235    568    416       O  
ATOM    464  CB  SER A  68     583.954 -42.036 189.408  1.00 65.78           C  
ANISOU  464  CB  SER A  68     7481   8377   9136   -246    494    144       C  
ATOM    465  OG  SER A  68     583.851 -42.572 188.106  1.00 69.41           O  
ANISOU  465  OG  SER A  68     7916   8938   9520   -237    442     16       O  
ATOM    466  N   VAL A  69     585.515 -40.091 191.405  1.00 55.31           N  
ANISOU  466  N   VAL A  69     6243   6961   7812   -219    605    390       N  
ATOM    467  CA  VAL A  69     585.633 -39.566 192.753  1.00 52.89           C  
ANISOU  467  CA  VAL A  69     5974   6574   7549   -229    636    468       C  
ATOM    468  C   VAL A  69     586.045 -38.106 192.666  1.00 51.27           C  
ANISOU  468  C   VAL A  69     5777   6407   7296   -215    659    543       C  
ATOM    469  O   VAL A  69     585.565 -37.292 193.455  1.00 50.02           O  
ANISOU  469  O   VAL A  69     5636   6208   7163   -219    678    596       O  
ATOM    470  CB  VAL A  69     586.632 -40.387 193.614  1.00 53.15           C  
ANISOU  470  CB  VAL A  69     6046   6521   7627   -222    633    452       C  
ATOM    471  CG1 VAL A  69     587.833 -40.773 192.803  1.00 54.23           C  
ANISOU  471  CG1 VAL A  69     6153   6702   7750   -187    623    385       C  
ATOM    472  CG2 VAL A  69     587.063 -39.621 194.857  1.00 51.44           C  
ANISOU  472  CG2 VAL A  69     5876   6263   7407   -224    647    523       C  
ATOM    473  N   ALA A  70     586.889 -37.783 191.674  1.00 83.84           N  
ANISOU  473  N   ALA A  70     9891  10607  11356   -205    670    542       N  
ATOM    474  CA  ALA A  70     587.423 -36.422 191.475  1.00 82.77           C  
ANISOU  474  CA  ALA A  70     9770  10490  11189   -212    705    625       C  
ATOM    475  C   ALA A  70     586.352 -35.437 191.034  1.00 83.08           C  
ANISOU  475  C   ALA A  70     9823  10542  11202   -194    686    704       C  
ATOM    476  O   ALA A  70     586.065 -34.488 191.759  1.00 82.15           O  
ANISOU  476  O   ALA A  70     9724  10350  11140   -191    698    759       O  
ATOM    477  CB  ALA A  70     588.565 -36.422 190.459  1.00 83.55           C  
ANISOU  477  CB  ALA A  70     9851  10675  11221   -222    748    607       C  
ATOM    478  N   ILE A  71     585.744 -35.684 189.871  1.00 64.95           N  
ANISOU  478  N   ILE A  71     7516   8338   8825   -172    646    698       N  
ATOM    479  CA  ILE A  71     584.750 -34.784 189.281  1.00 66.44           C  
ANISOU  479  CA  ILE A  71     7712   8551   8979   -131    595    781       C  
ATOM    480  C   ILE A  71     583.741 -34.270 190.294  1.00 65.89           C  
ANISOU  480  C   ILE A  71     7616   8388   9030   -106    580    798       C  
ATOM    481  O   ILE A  71     583.049 -33.285 190.037  1.00 67.36           O  
ANISOU  481  O   ILE A  71     7805   8558   9232    -56    543    875       O  
ATOM    482  CB  ILE A  71     583.965 -35.448 188.131  1.00 69.56           C  
ANISOU  482  CB  ILE A  71     8081   9068   9282   -104    512    730       C  
ATOM    483  CG1 ILE A  71     583.451 -34.370 187.173  1.00 71.76           C  
ANISOU  483  CG1 ILE A  71     8397   9403   9465    -50    450    852       C  
ATOM    484  CG2 ILE A  71     582.829 -36.299 188.689  1.00 70.34           C  
ANISOU  484  CG2 ILE A  71     8102   9138   9484   -105    462    632       C  
ATOM    485  CD1 ILE A  71     583.370 -34.812 185.754  1.00 74.49           C  
ANISOU  485  CD1 ILE A  71     8765   9910   9627    -34    388    826       C  
ATOM    486  N   PHE A  72     583.658 -34.937 191.438  1.00 73.22           N  
ANISOU  486  N   PHE A  72     8524   9256  10041   -136    613    728       N  
ATOM    487  CA  PHE A  72     582.928 -34.403 192.567  1.00 72.47           C  
ANISOU  487  CA  PHE A  72     8414   9079  10041   -125    640    732       C  
ATOM    488  C   PHE A  72     583.320 -32.958 192.853  1.00 72.24           C  
ANISOU  488  C   PHE A  72     8431   8978  10039   -104    667    806       C  
ATOM    489  O   PHE A  72     582.446 -32.096 192.959  1.00 73.69           O  
ANISOU  489  O   PHE A  72     8592   9119  10286    -51    653    834       O  
ATOM    490  CB  PHE A  72     583.168 -35.252 193.803  1.00 70.81           C  
ANISOU  490  CB  PHE A  72     8219   8819   9866   -174    691    674       C  
ATOM    491  CG  PHE A  72     582.356 -34.835 194.996  1.00 70.57           C  
ANISOU  491  CG  PHE A  72     8178   8731   9902   -173    744    660       C  
ATOM    492  CD1 PHE A  72     580.987 -35.041 195.031  1.00 71.75           C  
ANISOU  492  CD1 PHE A  72     8245   8901  10117   -164    751    626       C  
ATOM    493  CD2 PHE A  72     582.965 -34.267 196.096  1.00 69.69           C  
ANISOU  493  CD2 PHE A  72     8131   8560   9788   -184    790    663       C  
ATOM    494  CE1 PHE A  72     580.241 -34.672 196.143  1.00 71.72           C  
ANISOU  494  CE1 PHE A  72     8219   8861  10172   -166    829    597       C  
ATOM    495  CE2 PHE A  72     582.231 -33.903 197.207  1.00 70.00           C  
ANISOU  495  CE2 PHE A  72     8170   8565   9863   -184    855    630       C  
ATOM    496  CZ  PHE A  72     580.866 -34.108 197.231  1.00 70.86           C  
ANISOU  496  CZ  PHE A  72     8193   8697  10034   -174    887    598       C  
ATOM    497  N   SER A  73     584.629 -32.692 192.950  1.00 64.21           N  
ANISOU  497  N   SER A  73     7465   7937   8994   -144    701    828       N  
ATOM    498  CA  SER A  73     585.140 -31.347 193.322  1.00 64.16           C  
ANISOU  498  CA  SER A  73     7502   7837   9040   -150    732    880       C  
ATOM    499  C   SER A  73     585.084 -30.265 192.257  1.00 65.60           C  
ANISOU  499  C   SER A  73     7716   7997   9211   -124    717    997       C  
ATOM    500  O   SER A  73     584.895 -29.105 192.598  1.00 66.26           O  
ANISOU  500  O   SER A  73     7828   7967   9381   -103    726   1039       O  
ATOM    501  CB  SER A  73     586.577 -31.430 193.802  1.00 63.00           C  
ANISOU  501  CB  SER A  73     7374   7673   8889   -215    767    849       C  
ATOM    502  OG  SER A  73     586.578 -31.538 195.206  1.00 62.61           O  
ANISOU  502  OG  SER A  73     7337   7573   8880   -225    776    775       O  
ATOM    503  N   VAL A  74     585.287 -30.621 190.990  1.00 65.49           N  
ANISOU  503  N   VAL A  74     7710   8085   9087   -126    696   1051       N  
ATOM    504  CA  VAL A  74     584.981 -29.698 189.910  1.00 67.34           C  
ANISOU  504  CA  VAL A  74     7995   8316   9275    -87    664   1189       C  
ATOM    505  C   VAL A  74     583.590 -29.154 190.187  1.00 69.19           C  
ANISOU  505  C   VAL A  74     8202   8485   9601     11    591   1203       C  
ATOM    506  O   VAL A  74     583.365 -27.937 190.127  1.00 70.21           O  
ANISOU  506  O   VAL A  74     8376   8497   9803     55    578   1302       O  
ATOM    507  CB  VAL A  74     584.999 -30.357 188.528  1.00 68.62           C  
ANISOU  507  CB  VAL A  74     8170   8638   9265    -81    629   1220       C  
ATOM    508  CG1 VAL A  74     584.613 -29.344 187.465  1.00 70.44           C  
ANISOU  508  CG1 VAL A  74     8478   8864   9420    -30    579   1391       C  
ATOM    509  CG2 VAL A  74     586.355 -30.955 188.226  1.00 67.45           C  
ANISOU  509  CG2 VAL A  74     8025   8565   9037   -165    718   1178       C  
ATOM    510  N   GLY A  75     582.676 -30.069 190.526  1.00 58.21           N  
ANISOU  510  N   GLY A  75     6728   7160   8231     41    552   1097       N  
ATOM    511  CA  GLY A  75     581.321 -29.728 190.911  1.00 60.37           C  
ANISOU  511  CA  GLY A  75     6929   7394   8616    127    501   1069       C  
ATOM    512  C   GLY A  75     581.261 -28.789 192.108  1.00 59.92           C  
ANISOU  512  C   GLY A  75     6880   7186   8702    142    565   1042       C  
ATOM    513  O   GLY A  75     580.647 -27.732 192.022  1.00 61.65           O  
ANISOU  513  O   GLY A  75     7097   7311   9016    230    528   1096       O  
ATOM    514  N   GLY A  76     581.913 -29.149 193.213  1.00 62.88           N  
ANISOU  514  N   GLY A  76     7270   7532   9088     67    651    955       N  
ATOM    515  CA  GLY A  76     581.805 -28.389 194.456  1.00 63.06           C  
ANISOU  515  CA  GLY A  76     7302   7439   9219     76    713    888       C  
ATOM    516  C   GLY A  76     582.366 -26.972 194.419  1.00 63.81           C  
ANISOU  516  C   GLY A  76     7471   7383   9392     87    720    953       C  
ATOM    517  O   GLY A  76     581.917 -26.066 195.128  1.00 65.42           O  
ANISOU  517  O   GLY A  76     7673   7466   9717    138    744    903       O  
ATOM    518  N   MET A  77     583.380 -26.786 193.593  1.00 84.12           N  
ANISOU  518  N   MET A  77    10106   9954  11901     31    713   1057       N  
ATOM    519  CA  MET A  77     583.927 -25.473 193.364  1.00 84.67           C  
ANISOU  519  CA  MET A  77    10251   9868  12051     19    727   1147       C  
ATOM    520  C   MET A  77     582.837 -24.557 192.824  1.00 86.86           C  
ANISOU  520  C   MET A  77    10535  10049  12421    146    660   1240       C  
ATOM    521  O   MET A  77     582.491 -23.548 193.441  1.00 87.90           O  
ANISOU  521  O   MET A  77    10678  10012  12708    199    670   1206       O  
ATOM    522  CB  MET A  77     585.075 -25.580 192.396  1.00 83.44           C  
ANISOU  522  CB  MET A  77    10146   9763  11796    -71    749   1256       C  
ATOM    523  CG  MET A  77     585.587 -24.290 191.912  1.00 84.37           C  
ANISOU  523  CG  MET A  77    10348   9724  11987   -102    773   1391       C  
ATOM    524  SD  MET A  77     586.365 -24.595 190.330  1.00 83.83           S  
ANISOU  524  SD  MET A  77    10331   9783  11737   -170    800   1560       S  
ATOM    525  CE  MET A  77     586.894 -26.291 190.584  1.00 82.26           C  
ANISOU  525  CE  MET A  77    10039   9803  11414   -220    821   1399       C  
ATOM    526  N   ILE A  78     582.290 -24.938 191.674  1.00 53.87           N  
ANISOU  526  N   ILE A  78     6346   5978   8145    205    579   1343       N  
ATOM    527  CA  ILE A  78     581.175 -24.230 191.059  1.00 55.86           C  
ANISOU  527  CA  ILE A  78     6588   6170   8466    349    475   1438       C  
ATOM    528  C   ILE A  78     580.027 -24.048 192.034  1.00 56.92           C  
ANISOU  528  C   ILE A  78     6612   6249   8767    451    468   1296       C  
ATOM    529  O   ILE A  78     579.391 -22.993 192.070  1.00 58.02           O  
ANISOU  529  O   ILE A  78     6751   6233   9061    569    424   1331       O  
ATOM    530  CB  ILE A  78     580.672 -24.978 189.836  1.00 56.74           C  
ANISOU  530  CB  ILE A  78     6676   6463   8418    394    369   1514       C  
ATOM    531  CG1 ILE A  78     581.756 -24.988 188.773  1.00 55.96           C  
ANISOU  531  CG1 ILE A  78     6698   6420   8142    306    392   1663       C  
ATOM    532  CG2 ILE A  78     579.417 -24.346 189.299  1.00 58.75           C  
ANISOU  532  CG2 ILE A  78     6893   6677   8751    563    227   1590       C  
ATOM    533  CD1 ILE A  78     581.674 -26.189 187.893  1.00 56.26           C  
ANISOU  533  CD1 ILE A  78     6707   6689   7980    288    342   1641       C  
ATOM    534  N   GLY A  79     579.771 -25.080 192.831  1.00 61.75           N  
ANISOU  534  N   GLY A  79     7131   6979   9351    406    523   1135       N  
ATOM    535  CA  GLY A  79     578.736 -25.025 193.843  1.00 62.51           C  
ANISOU  535  CA  GLY A  79     7116   7053   9581    475    561    983       C  
ATOM    536  C   GLY A  79     579.037 -23.887 194.791  1.00 62.67           C  
ANISOU  536  C   GLY A  79     7191   6882   9738    488    634    921       C  
ATOM    537  O   GLY A  79     578.185 -23.033 195.037  1.00 63.75           O  
ANISOU  537  O   GLY A  79     7276   6903  10042    613    619    880       O  
ATOM    538  N   SER A  80     580.275 -23.840 195.287  1.00 54.49           N  
ANISOU  538  N   SER A  80     6253   5805   8645    364    704    903       N  
ATOM    539  CA  SER A  80     580.673 -22.817 196.261  1.00 54.87           C  
ANISOU  539  CA  SER A  80     6357   5678   8814    352    768    809       C  
ATOM    540  C   SER A  80     580.846 -21.448 195.591  1.00 55.44           C  
ANISOU  540  C   SER A  80     6508   5531   9027    408    718    938       C  
ATOM    541  O   SER A  80     580.873 -20.404 196.246  1.00 56.30           O  
ANISOU  541  O   SER A  80     6650   5446   9295    437    750    858       O  
ATOM    542  CB  SER A  80     581.958 -23.244 196.990  1.00 53.74           C  
ANISOU  542  CB  SER A  80     6277   5576   8568    200    831    738       C  
ATOM    543  OG  SER A  80     581.668 -24.129 198.065  1.00 54.19           O  
ANISOU  543  OG  SER A  80     6289   5759   8543    174    892    589       O  
ATOM    544  N   PHE A  81     580.964 -21.454 194.274  1.00 82.76           N  
ANISOU  544  N   PHE A  81    10010   9014  12423    421    639   1140       N  
ATOM    545  CA  PHE A  81     581.055 -20.200 193.571  1.00 83.55           C  
ANISOU  545  CA  PHE A  81    10204   8899  12641    476    589   1304       C  
ATOM    546  C   PHE A  81     579.690 -19.613 193.448  1.00 85.11           C  
ANISOU  546  C   PHE A  81    10336   9007  12994    676    503   1308       C  
ATOM    547  O   PHE A  81     579.523 -18.406 193.490  1.00 86.16           O  
ANISOU  547  O   PHE A  81    10524   8895  13318    759    481   1348       O  
ATOM    548  CB  PHE A  81     581.687 -20.375 192.202  1.00 83.00           C  
ANISOU  548  CB  PHE A  81    10224   8896  12417    415    547   1535       C  
ATOM    549  CG  PHE A  81     583.169 -20.174 192.214  1.00 81.85           C  
ANISOU  549  CG  PHE A  81    10167   8698  12234    235    642   1574       C  
ATOM    550  CD1 PHE A  81     583.707 -18.935 192.569  1.00 82.53           C  
ANISOU  550  CD1 PHE A  81    10333   8520  12503    189    687   1592       C  
ATOM    551  CD2 PHE A  81     584.033 -21.218 191.900  1.00 80.19           C  
ANISOU  551  CD2 PHE A  81     9943   8691  11834    109    688   1573       C  
ATOM    552  CE1 PHE A  81     585.077 -18.736 192.596  1.00 81.72           C  
ANISOU  552  CE1 PHE A  81    10283   8372  12394      7    776   1612       C  
ATOM    553  CE2 PHE A  81     585.397 -21.024 191.917  1.00 79.22           C  
ANISOU  553  CE2 PHE A  81     9867   8530  11703    -53    777   1593       C  
ATOM    554  CZ  PHE A  81     585.923 -19.789 192.270  1.00 80.05           C  
ANISOU  554  CZ  PHE A  81    10037   8386  11991   -113    822   1611       C  
ATOM    555  N   SER A  82     578.701 -20.481 193.317  1.00 74.81           N  
ANISOU  555  N   SER A  82     8900   7893  11631    755    452   1252       N  
ATOM    556  CA  SER A  82     577.352 -20.023 193.048  1.00 76.27           C  
ANISOU  556  CA  SER A  82     8984   8028  11967    958    346   1257       C  
ATOM    557  C   SER A  82     576.591 -19.740 194.333  1.00 76.78           C  
ANISOU  557  C   SER A  82     8926   8030  12217   1034    431   1016       C  
ATOM    558  O   SER A  82     575.447 -19.279 194.285  1.00 77.90           O  
ANISOU  558  O   SER A  82     8951   8115  12531   1215    363    977       O  
ATOM    559  CB  SER A  82     576.597 -21.053 192.215  1.00 76.53           C  
ANISOU  559  CB  SER A  82     8909   8301  11868   1004    237   1299       C  
ATOM    560  OG  SER A  82     577.359 -21.452 191.091  1.00 76.25           O  
ANISOU  560  OG  SER A  82     8990   8362  11619    918    183   1484       O  
ATOM    561  N   VAL A  83     577.230 -19.997 195.476  1.00 80.87           N  
ANISOU  561  N   VAL A  83     9468   8564  12695    903    578    850       N  
ATOM    562  CA  VAL A  83     576.545 -19.881 196.762  1.00 81.37           C  
ANISOU  562  CA  VAL A  83     9426   8618  12873    953    688    603       C  
ATOM    563  C   VAL A  83     576.015 -18.470 197.020  1.00 82.65           C  
ANISOU  563  C   VAL A  83     9582   8519  13304   1116    673    543       C  
ATOM    564  O   VAL A  83     574.868 -18.308 197.446  1.00 83.39           O  
ANISOU  564  O   VAL A  83     9521   8619  13545   1259    694    398       O  
ATOM    565  CB  VAL A  83     577.440 -20.302 197.955  1.00 80.70           C  
ANISOU  565  CB  VAL A  83     9408   8590  12665    785    829    450       C  
ATOM    566  CG1 VAL A  83     578.710 -19.475 198.033  1.00 80.67           C  
ANISOU  566  CG1 VAL A  83     9566   8401  12685    692    834    493       C  
ATOM    567  CG2 VAL A  83     576.675 -20.137 199.241  1.00 81.34           C  
ANISOU  567  CG2 VAL A  83     9398   8677  12832    841    953    200       C  
ATOM    568  N   GLY A  84     576.825 -17.455 196.733  1.00111.90           N  
ANISOU  568  N   GLY A  84    13442  11985  17091   1096    639    650       N  
ATOM    569  CA  GLY A  84     576.429 -16.084 196.995  1.00113.18           C  
ANISOU  569  CA  GLY A  84    13620  11851  17531   1244    624    591       C  
ATOM    570  C   GLY A  84     575.182 -15.706 196.222  1.00114.24           C  
ANISOU  570  C   GLY A  84    13644  11931  17831   1481    486    683       C  
ATOM    571  O   GLY A  84     574.335 -14.960 196.716  1.00115.32           O  
ANISOU  571  O   GLY A  84    13686  11920  18211   1655    494    533       O  
ATOM    572  N   LEU A  85     575.075 -16.257 195.013  1.00 80.10           N  
ANISOU  572  N   LEU A  85     9324   7741  13368   1492    352    914       N  
ATOM    573  CA  LEU A  85     574.020 -15.929 194.043  1.00 81.30           C  
ANISOU  573  CA  LEU A  85     9394   7860  13635   1714    165   1055       C  
ATOM    574  C   LEU A  85     572.630 -16.332 194.540  1.00 81.88           C  
ANISOU  574  C   LEU A  85     9200   8077  13833   1864    170    839       C  
ATOM    575  O   LEU A  85     571.681 -15.561 194.467  1.00 83.23           O  
ANISOU  575  O   LEU A  85     9264   8105  14255   2091     80    805       O  
ATOM    576  CB  LEU A  85     574.310 -16.624 192.701  1.00 80.90           C  
ANISOU  576  CB  LEU A  85     9415   7987  13338   1656     32   1316       C  
ATOM    577  CG  LEU A  85     573.600 -16.291 191.383  1.00 82.38           C  
ANISOU  577  CG  LEU A  85     9603   8154  13543   1846   -204   1553       C  
ATOM    578  CD1 LEU A  85     574.338 -16.967 190.238  1.00 81.93           C  
ANISOU  578  CD1 LEU A  85     9686   8272  13172   1712   -268   1784       C  
ATOM    579  CD2 LEU A  85     572.125 -16.682 191.358  1.00 83.33           C  
ANISOU  579  CD2 LEU A  85     9461   8426  13777   2038   -317   1423       C  
ATOM    580  N   PHE A  86     572.507 -17.552 195.037  1.00109.06           N  
ANISOU  580  N   PHE A  86    12527  11797  17112   1736    277    696       N  
ATOM    581  CA  PHE A  86     571.200 -18.055 195.401  1.00109.53           C  
ANISOU  581  CA  PHE A  86    12320  12020  17277   1843    295    511       C  
ATOM    582  C   PHE A  86     570.765 -17.477 196.751  1.00109.96           C  
ANISOU  582  C   PHE A  86    12280  11971  17530   1904    474    229       C  
ATOM    583  O   PHE A  86     569.646 -17.007 196.890  1.00111.07           O  
ANISOU  583  O   PHE A  86    12226  12064  17912   2105    448    107       O  
ATOM    584  CB  PHE A  86     571.223 -19.588 195.402  1.00108.43           C  
ANISOU  584  CB  PHE A  86    12105  12191  16902   1667    352    477       C  
ATOM    585  CG  PHE A  86     571.351 -20.198 194.012  1.00108.33           C  
ANISOU  585  CG  PHE A  86    12132  12309  16720   1648    162    701       C  
ATOM    586  CD1 PHE A  86     570.529 -19.782 192.974  1.00109.62           C  
ANISOU  586  CD1 PHE A  86    12211  12450  16987   1846    -62    822       C  
ATOM    587  CD2 PHE A  86     572.298 -21.170 193.741  1.00107.14           C  
ANISOU  587  CD2 PHE A  86    12104  12303  16301   1443    199    781       C  
ATOM    588  CE1 PHE A  86     570.640 -20.329 191.700  1.00109.81           C  
ANISOU  588  CE1 PHE A  86    12286  12614  16823   1829   -243   1013       C  
ATOM    589  CE2 PHE A  86     572.411 -21.716 192.469  1.00107.27           C  
ANISOU  589  CE2 PHE A  86    12160  12447  16152   1429     36    957       C  
ATOM    590  CZ  PHE A  86     571.579 -21.292 191.452  1.00108.66           C  
ANISOU  590  CZ  PHE A  86    12265  12617  16405   1617   -182   1070       C  
ATOM    591  N   VAL A  87     571.671 -17.482 197.723  1.00 80.94           N  
ANISOU  591  N   VAL A  87     8741   8264  13749   1739    648    118       N  
ATOM    592  CA  VAL A  87     571.417 -16.961 199.067  1.00 81.41           C  
ANISOU  592  CA  VAL A  87     8751   8246  13937   1770    833   -166       C  
ATOM    593  C   VAL A  87     570.751 -15.595 199.135  1.00 82.93           C  
ANISOU  593  C   VAL A  87     8884   8162  14466   2013    786   -256       C  
ATOM    594  O   VAL A  87     569.744 -15.421 199.810  1.00 83.63           O  
ANISOU  594  O   VAL A  87     8772   8278  14724   2143    885   -491       O  
ATOM    595  CB  VAL A  87     572.731 -16.856 199.844  1.00 80.78           C  
ANISOU  595  CB  VAL A  87     8888   8104  13700   1576    948   -218       C  
ATOM    596  CG1 VAL A  87     572.585 -15.915 201.004  1.00 81.74           C  
ANISOU  596  CG1 VAL A  87     9011   8061  13986   1644   1084   -489       C  
ATOM    597  CG2 VAL A  87     573.170 -18.202 200.307  1.00 79.64           C  
ANISOU  597  CG2 VAL A  87     8758   8237  13264   1367   1055   -243       C  
ATOM    598  N   ASN A  88     571.354 -14.619 198.465  1.00102.79           N  
ANISOU  598  N   ASN A  88    11575  10398  17084   2068    650    -71       N  
ATOM    599  CA  ASN A  88     570.916 -13.234 198.545  1.00104.30           C  
ANISOU  599  CA  ASN A  88    11760  10259  17612   2290    599   -138       C  
ATOM    600  C   ASN A  88     569.618 -13.021 197.799  1.00105.32           C  
ANISOU  600  C   ASN A  88    11681  10378  17959   2560    432    -79       C  
ATOM    601  O   ASN A  88     568.726 -12.311 198.252  1.00106.51           O  
ANISOU  601  O   ASN A  88    11674  10394  18400   2775    455   -276       O  
ATOM    602  CB  ASN A  88     572.000 -12.313 197.989  1.00104.58           C  
ANISOU  602  CB  ASN A  88    12062   9984  17688   2240    505     80       C  
ATOM    603  CG  ASN A  88     573.154 -12.152 198.939  1.00104.16           C  
ANISOU  603  CG  ASN A  88    12173   9864  17539   2025    665    -64       C  
ATOM    604  OD1 ASN A  88     572.960 -11.814 200.112  1.00104.64           O  
ANISOU  604  OD1 ASN A  88    12183   9881  17695   2045    814   -374       O  
ATOM    605  ND2 ASN A  88     574.367 -12.413 198.453  1.00103.33           N  
ANISOU  605  ND2 ASN A  88    12255   9771  17236   1818    637    142       N  
ATOM    606  N   ARG A  89     569.535 -13.663 196.644  1.00116.98           N  
ANISOU  606  N   ARG A  89    13152  12008  19288   2550    257    179       N  
ATOM    607  CA  ARG A  89     568.406 -13.557 195.737  1.00118.06           C  
ANISOU  607  CA  ARG A  89    13108  12167  19583   2794     41    280       C  
ATOM    608  C   ARG A  89     567.160 -14.330 196.219  1.00118.00           C  
ANISOU  608  C   ARG A  89    12755  12433  19647   2863    114     30       C  
ATOM    609  O   ARG A  89     566.036 -13.919 195.942  1.00119.14           O  
ANISOU  609  O   ARG A  89    12677  12537  20055   3118    -12    -24       O  
ATOM    610  CB  ARG A  89     568.863 -14.054 194.363  1.00117.76           C  
ANISOU  610  CB  ARG A  89    13207  12233  19303   2725   -162    626       C  
ATOM    611  CG  ARG A  89     568.024 -13.707 193.147  1.00119.19           C  
ANISOU  611  CG  ARG A  89    13313  12376  19597   2975   -459    834       C  
ATOM    612  CD  ARG A  89     568.770 -14.223 191.905  1.00118.93           C  
ANISOU  612  CD  ARG A  89    13485  12460  19241   2845   -606   1163       C  
ATOM    613  NE  ARG A  89     568.001 -14.191 190.657  1.00120.42           N  
ANISOU  613  NE  ARG A  89    13611  12713  19429   3047   -907   1368       N  
ATOM    614  CZ  ARG A  89     568.368 -14.813 189.532  1.00120.37           C  
ANISOU  614  CZ  ARG A  89    13725  12889  19121   2960  -1051   1607       C  
ATOM    615  NH1 ARG A  89     569.493 -15.531 189.490  1.00118.82           N  
ANISOU  615  NH1 ARG A  89    13702  12822  18621   2679   -909   1666       N  
ATOM    616  NH2 ARG A  89     567.605 -14.723 188.444  1.00121.98           N  
ANISOU  616  NH2 ARG A  89    13870  13155  19320   3163  -1345   1776       N  
ATOM    617  N   PHE A  90     567.357 -15.434 196.944  1.00 94.54           N  
ANISOU  617  N   PHE A  90     9733   9731  16458   2636    318   -118       N  
ATOM    618  CA  PHE A  90     566.262 -16.350 197.296  1.00 94.29           C  
ANISOU  618  CA  PHE A  90     9388   9984  16456   2641    404   -314       C  
ATOM    619  C   PHE A  90     566.106 -16.646 198.789  1.00 93.76           C  
ANISOU  619  C   PHE A  90     9228  10019  16375   2530    725   -630       C  
ATOM    620  O   PHE A  90     565.245 -17.416 199.189  1.00 93.21           O  
ANISOU  620  O   PHE A  90     8909  10182  16325   2500    844   -796       O  
ATOM    621  CB  PHE A  90     566.446 -17.681 196.562  1.00 93.24           C  
ANISOU  621  CB  PHE A  90     9253  10128  16047   2463    327   -158       C  
ATOM    622  CG  PHE A  90     566.475 -17.552 195.063  1.00 94.00           C  
ANISOU  622  CG  PHE A  90     9417  10193  16104   2566     16    132       C  
ATOM    623  CD1 PHE A  90     565.740 -16.565 194.420  1.00 95.74           C  
ANISOU  623  CD1 PHE A  90     9551  10239  16585   2856   -204    204       C  
ATOM    624  CD2 PHE A  90     567.235 -18.415 194.292  1.00 93.10           C  
ANISOU  624  CD2 PHE A  90     9461  10226  15686   2383    -60    332       C  
ATOM    625  CE1 PHE A  90     565.769 -16.443 193.038  1.00 96.59           C  
ANISOU  625  CE1 PHE A  90     9748  10333  16619   2954   -500    491       C  
ATOM    626  CE2 PHE A  90     567.264 -18.295 192.910  1.00 93.99           C  
ANISOU  626  CE2 PHE A  90     9654  10335  15724   2475   -335    592       C  
ATOM    627  CZ  PHE A  90     566.530 -17.313 192.284  1.00 95.76           C  
ANISOU  627  CZ  PHE A  90     9809  10398  16176   2756   -558    681       C  
ATOM    628  N   GLY A  91     566.933 -16.049 199.626  1.00 98.26           N  
ANISOU  628  N   GLY A  91    10002  10427  16906   2457    870   -719       N  
ATOM    629  CA  GLY A  91     566.922 -16.426 201.022  1.00 97.73           C  
ANISOU  629  CA  GLY A  91     9898  10492  16741   2324   1167   -995       C  
ATOM    630  C   GLY A  91     567.702 -17.707 201.166  1.00 96.01           C  
ANISOU  630  C   GLY A  91     9810  10508  16163   2036   1246   -896       C  
ATOM    631  O   GLY A  91     568.064 -18.342 200.176  1.00 95.23           O  
ANISOU  631  O   GLY A  91     9772  10485  15926   1960   1083   -656       O  
ATOM    632  N   ARG A  92     567.958 -18.086 202.407  1.00 98.45           N  
ANISOU  632  N   ARG A  92    10166  10930  16312   1885   1494  -1086       N  
ATOM    633  CA  ARG A  92     568.760 -19.257 202.684  1.00 96.94           C  
ANISOU  633  CA  ARG A  92    10118  10931  15784   1624   1571   -999       C  
ATOM    634  C   ARG A  92     567.910 -20.509 202.594  1.00 96.14           C  
ANISOU  634  C   ARG A  92     9807  11097  15627   1545   1641  -1004       C  
ATOM    635  O   ARG A  92     568.264 -21.434 201.872  1.00 95.10           O  
ANISOU  635  O   ARG A  92     9721  11071  15343   1426   1533   -813       O  
ATOM    636  CB  ARG A  92     569.406 -19.143 204.059  1.00 96.88           C  
ANISOU  636  CB  ARG A  92    10269  10935  15608   1500   1784  -1184       C  
ATOM    637  CG  ARG A  92     569.683 -17.702 204.483  1.00 98.30           C  
ANISOU  637  CG  ARG A  92    10541  10846  15961   1632   1785  -1331       C  
ATOM    638  CD  ARG A  92     570.658 -17.012 203.542  1.00 98.56           C  
ANISOU  638  CD  ARG A  92    10766  10635  16047   1651   1558  -1107       C  
ATOM    639  NE  ARG A  92     571.279 -15.818 204.124  1.00 99.54           N  
ANISOU  639  NE  ARG A  92    11043  10504  16273   1687   1581  -1246       N  
ATOM    640  CZ  ARG A  92     571.025 -14.571 203.747  1.00100.61           C  
ANISOU  640  CZ  ARG A  92    11169  10343  16716   1881   1483  -1265       C  
ATOM    641  NH1 ARG A  92     570.155 -14.328 202.777  1.00100.99           N  
ANISOU  641  NH1 ARG A  92    11062  10321  16988   2076   1338  -1139       N  
ATOM    642  NH2 ARG A  92     571.655 -13.569 204.337  1.00101.43           N  
ANISOU  642  NH2 ARG A  92    11422  10211  16907   1882   1515  -1409       N  
ATOM    643  N   ARG A  93     566.777 -20.525 203.299  1.00 85.94           N  
ANISOU  643  N   ARG A  93     8272   9906  14474   1609   1826  -1235       N  
ATOM    644  CA  ARG A  93     565.945 -21.722 203.345  1.00 85.25           C  
ANISOU  644  CA  ARG A  93     7971  10069  14352   1502   1932  -1263       C  
ATOM    645  C   ARG A  93     565.333 -22.013 201.979  1.00 85.29           C  
ANISOU  645  C   ARG A  93     7793  10104  14511   1595   1683  -1116       C  
ATOM    646  O   ARG A  93     565.370 -23.158 201.542  1.00 84.20           O  
ANISOU  646  O   ARG A  93     7635  10118  14238   1440   1647  -1002       O  
ATOM    647  CB  ARG A  93     564.860 -21.623 204.426  1.00 86.11           C  
ANISOU  647  CB  ARG A  93     7844  10287  14586   1539   2216  -1555       C  
ATOM    648  CG  ARG A  93     563.514 -21.112 203.976  1.00 87.30           C  
ANISOU  648  CG  ARG A  93     7637  10428  15105   1768   2162  -1684       C  
ATOM    649  CD  ARG A  93     562.374 -22.040 204.388  1.00 87.16           C  
ANISOU  649  CD  ARG A  93     7307  10661  15148   1673   2378  -1830       C  
ATOM    650  NE  ARG A  93     561.093 -21.332 204.463  1.00 88.71           N  
ANISOU  650  NE  ARG A  93     7144  10853  15710   1902   2428  -2063       N  
ATOM    651  CZ  ARG A  93     560.372 -20.972 203.406  1.00 89.53           C  
ANISOU  651  CZ  ARG A  93     7008  10901  16108   2114   2169  -2024       C  
ATOM    652  NH1 ARG A  93     560.797 -21.249 202.182  1.00 89.02           N  
ANISOU  652  NH1 ARG A  93     7043  10793  15987   2116   1850  -1759       N  
ATOM    653  NH2 ARG A  93     559.222 -20.329 203.570  1.00 91.00           N  
ANISOU  653  NH2 ARG A  93     6852  11084  16641   2334   2224  -2257       N  
ATOM    654  N   ASN A  94     564.836 -21.003 201.268  1.00 98.37           N  
ANISOU  654  N   ASN A  94     9336  11606  16435   1845   1492  -1108       N  
ATOM    655  CA  ASN A  94     564.256 -21.262 199.956  1.00 98.67           C  
ANISOU  655  CA  ASN A  94     9211  11690  16590   1945   1226   -966       C  
ATOM    656  C   ASN A  94     565.299 -21.769 198.958  1.00 97.81           C  
ANISOU  656  C   ASN A  94     9351  11576  16237   1828   1023   -683       C  
ATOM    657  O   ASN A  94     564.958 -22.174 197.849  1.00 98.14           O  
ANISOU  657  O   ASN A  94     9300  11694  16296   1868    804   -557       O  
ATOM    658  CB  ASN A  94     563.580 -20.016 199.405  1.00100.40           C  
ANISOU  658  CB  ASN A  94     9291  11725  17132   2259   1037   -988       C  
ATOM    659  CG  ASN A  94     562.441 -19.524 200.283  1.00101.41           C  
ANISOU  659  CG  ASN A  94     9120  11868  17545   2407   1227  -1294       C  
ATOM    660  OD1 ASN A  94     562.663 -19.045 201.393  1.00101.40           O  
ANISOU  660  OD1 ASN A  94     9194  11796  17535   2389   1463  -1474       O  
ATOM    661  ND2 ASN A  94     561.216 -19.609 199.775  1.00102.47           N  
ANISOU  661  ND2 ASN A  94     8902  12097  17936   2562   1118  -1370       N  
ATOM    662  N   SER A  95     566.569 -21.753 199.360  1.00 94.88           N  
ANISOU  662  N   SER A  95     9285  11129  15637   1683   1096   -602       N  
ATOM    663  CA  SER A  95     567.661 -22.279 198.545  1.00 94.04           C  
ANISOU  663  CA  SER A  95     9411  11031  15289   1552    953   -361       C  
ATOM    664  C   SER A  95     567.990 -23.722 198.932  1.00 92.48           C  
ANISOU  664  C   SER A  95     9247  11034  14857   1302   1087   -365       C  
ATOM    665  O   SER A  95     568.070 -24.601 198.070  1.00 92.00           O  
ANISOU  665  O   SER A  95     9178  11084  14696   1225    962   -242       O  
ATOM    666  CB  SER A  95     568.896 -21.396 198.686  1.00 94.11           C  
ANISOU  666  CB  SER A  95     9710  10828  15218   1543    938   -270       C  
ATOM    667  OG  SER A  95     568.578 -20.061 198.360  1.00 96.50           O  
ANISOU  667  OG  SER A  95     9996  10910  15761   1769    822   -260       O  
ATOM    668  N   MET A  96     568.178 -23.948 200.231  1.00 78.71           N  
ANISOU  668  N   MET A  96     7552   9330  13025   1183   1338   -507       N  
ATOM    669  CA  MET A  96     568.370 -25.280 200.775  1.00 77.37           C  
ANISOU  669  CA  MET A  96     7412   9330  12655    959   1488   -515       C  
ATOM    670  C   MET A  96     567.296 -26.181 200.213  1.00 77.32           C  
ANISOU  670  C   MET A  96     7147   9479  12753    936   1454   -535       C  
ATOM    671  O   MET A  96     567.582 -27.262 199.666  1.00 76.35           O  
ANISOU  671  O   MET A  96     7062   9445  12502    799   1386   -426       O  
ATOM    672  CB  MET A  96     568.297 -25.263 202.292  1.00 77.33           C  
ANISOU  672  CB  MET A  96     7434   9365  12582    881   1771   -694       C  
ATOM    673  CG  MET A  96     569.201 -24.228 202.927  1.00 78.09           C  
ANISOU  673  CG  MET A  96     7749   9307  12617    924   1800   -735       C  
ATOM    674  SD  MET A  96     569.468 -24.480 204.694  1.00 77.46           S  
ANISOU  674  SD  MET A  96     7790   9319  12323    781   2104   -910       S  
ATOM    675  CE  MET A  96     570.305 -26.083 204.631  1.00 75.98           C  
ANISOU  675  CE  MET A  96     7766   9264  11839    538   2092   -716       C  
ATOM    676  N   LEU A  97     566.058 -25.698 200.323  1.00 78.99           N  
ANISOU  676  N   LEU A  97     7080   9713  13219   1077   1491   -691       N  
ATOM    677  CA  LEU A  97     564.882 -26.406 199.834  1.00 79.34           C  
ANISOU  677  CA  LEU A  97     6815   9905  13424   1073   1455   -754       C  
ATOM    678  C   LEU A  97     564.964 -26.712 198.347  1.00 79.68           C  
ANISOU  678  C   LEU A  97     6850   9966  13460   1117   1144   -591       C  
ATOM    679  O   LEU A  97     564.872 -27.864 197.947  1.00 79.26           O  
ANISOU  679  O   LEU A  97     6749  10035  13332    966   1115   -557       O  
ATOM    680  CB  LEU A  97     563.621 -25.590 200.115  1.00 80.76           C  
ANISOU  680  CB  LEU A  97     6686  10085  13916   1267   1510   -955       C  
ATOM    681  CG  LEU A  97     562.397 -26.337 200.654  1.00 80.99           C  
ANISOU  681  CG  LEU A  97     6383  10296  14094   1176   1718  -1145       C  
ATOM    682  CD1 LEU A  97     561.164 -25.444 200.605  1.00 82.69           C  
ANISOU  682  CD1 LEU A  97     6253  10504  14661   1419   1694  -1332       C  
ATOM    683  CD2 LEU A  97     562.170 -27.671 199.915  1.00 80.48           C  
ANISOU  683  CD2 LEU A  97     6223  10371  13985   1005   1621  -1066       C  
ATOM    684  N   MET A  98     565.119 -25.685 197.523  1.00 99.16           N  
ANISOU  684  N   MET A  98     9371  12305  16001   1322    913   -492       N  
ATOM    685  CA  MET A  98     565.045 -25.896 196.087  1.00 99.87           C  
ANISOU  685  CA  MET A  98     9438  12436  16074   1387    611   -347       C  
ATOM    686  C   MET A  98     566.241 -26.669 195.551  1.00 98.89           C  
ANISOU  686  C   MET A  98     9584  12335  15655   1216    550   -172       C  
ATOM    687  O   MET A  98     566.161 -27.244 194.466  1.00 99.33           O  
ANISOU  687  O   MET A  98     9612  12484  15646   1204    352    -91       O  
ATOM    688  CB  MET A  98     564.937 -24.569 195.350  1.00101.36           C  
ANISOU  688  CB  MET A  98     9648  12470  16394   1653    382   -251       C  
ATOM    689  CG  MET A  98     566.262 -23.863 195.179  1.00101.03           C  
ANISOU  689  CG  MET A  98     9956  12247  16182   1653    342    -65       C  
ATOM    690  SD  MET A  98     566.210 -22.627 193.867  1.00102.54           S  
ANISOU  690  SD  MET A  98    10219  12275  16465   1922     11    142       S  
ATOM    691  CE  MET A  98     565.110 -21.390 194.587  1.00103.69           C  
ANISOU  691  CE  MET A  98    10135  12267  16997   2184     57    -45       C  
ATOM    692  N   MET A  99     567.347 -26.685 196.297  1.00 77.46           N  
ANISOU  692  N   MET A  99     7121   9545  12764   1092    711   -130       N  
ATOM    693  CA  MET A  99     568.558 -27.329 195.799  1.00 76.55           C  
ANISOU  693  CA  MET A  99     7252   9440  12392    952    654     27       C  
ATOM    694  C   MET A  99     568.535 -28.809 196.045  1.00 75.27           C  
ANISOU  694  C   MET A  99     7053   9418  12130    745    757    -21       C  
ATOM    695  O   MET A  99     569.382 -29.538 195.542  1.00 74.52           O  
ANISOU  695  O   MET A  99     7113   9350  11851    634    698     80       O  
ATOM    696  CB  MET A  99     569.805 -26.703 196.404  1.00 75.80           C  
ANISOU  696  CB  MET A  99     7426   9204  12170    916    747     94       C  
ATOM    697  CG  MET A  99     570.220 -25.408 195.695  1.00 77.00           C  
ANISOU  697  CG  MET A  99     7697   9191  12367   1079    585    226       C  
ATOM    698  SD  MET A  99     570.462 -25.525 193.892  1.00 78.06           S  
ANISOU  698  SD  MET A  99     7897   9369  12392   1136    296    443       S  
ATOM    699  CE  MET A  99     568.810 -25.311 193.190  1.00 79.83           C  
ANISOU  699  CE  MET A  99     7820   9669  12843   1339    106    382       C  
ATOM    700  N   ASN A 100     567.530 -29.253 196.786  1.00 70.16           N  
ANISOU  700  N   ASN A 100     6188   8851  11620    693    915   -181       N  
ATOM    701  CA  ASN A 100     567.247 -30.674 196.887  1.00 69.31           C  
ANISOU  701  CA  ASN A 100     5999   8862  11475    500    995   -227       C  
ATOM    702  C   ASN A 100     566.942 -31.278 195.531  1.00 70.31           C  
ANISOU  702  C   ASN A 100     6027   9072  11614    508    754   -191       C  
ATOM    703  O   ASN A 100     567.109 -32.473 195.341  1.00 69.71           O  
ANISOU  703  O   ASN A 100     5970   9055  11460    343    767   -191       O  
ATOM    704  CB  ASN A 100     566.107 -30.924 197.855  1.00 69.37           C  
ANISOU  704  CB  ASN A 100     5762   8941  11656    444   1218   -402       C  
ATOM    705  CG  ASN A 100     566.568 -30.866 199.283  1.00 68.22           C  
ANISOU  705  CG  ASN A 100     5767   8756  11398    348   1495   -434       C  
ATOM    706  OD1 ASN A 100     566.266 -29.916 200.010  1.00 68.84           O  
ANISOU  706  OD1 ASN A 100     5801   8796  11558    453   1612   -531       O  
ATOM    707  ND2 ASN A 100     567.347 -31.878 199.695  1.00 66.70           N  
ANISOU  707  ND2 ASN A 100     5767   8569  11006    157   1590   -356       N  
ATOM    708  N   LEU A 101     566.529 -30.450 194.576  1.00 62.88           N  
ANISOU  708  N   LEU A 101     4999   8129  10762    703    525   -159       N  
ATOM    709  CA  LEU A 101     566.461 -30.902 193.195  1.00 63.16           C  
ANISOU  709  CA  LEU A 101     5009   8252  10737    726    263   -102       C  
ATOM    710  C   LEU A 101     567.804 -31.470 192.732  1.00 60.66           C  
ANISOU  710  C   LEU A 101     4983   7915  10148    613    231     33       C  
ATOM    711  O   LEU A 101     567.853 -32.443 191.989  1.00 60.45           O  
ANISOU  711  O   LEU A 101     4948   7981  10041    522    130     20       O  
ATOM    712  CB  LEU A 101     566.056 -29.777 192.262  1.00 64.98           C  
ANISOU  712  CB  LEU A 101     5185   8462  11043    972      9    -33       C  
ATOM    713  CG  LEU A 101     565.879 -30.344 190.855  1.00 65.72           C  
ANISOU  713  CG  LEU A 101     5242   8685  11043    986   -266      5       C  
ATOM    714  CD1 LEU A 101     564.608 -29.890 190.277  1.00 68.86           C  
ANISOU  714  CD1 LEU A 101     5357   9159  11648   1169   -479    -69       C  
ATOM    715  CD2 LEU A 101     566.969 -29.892 189.964  1.00 64.60           C  
ANISOU  715  CD2 LEU A 101     5394   8496  10657   1042   -408    210       C  
ATOM    716  N   LEU A 102     568.905 -30.850 193.139  1.00 78.51           N  
ANISOU  716  N   LEU A 102     7491  10059  12281    622    313    145       N  
ATOM    717  CA  LEU A 102     570.191 -31.376 192.716  1.00 77.64           C  
ANISOU  717  CA  LEU A 102     7624   9939  11938    521    293    257       C  
ATOM    718  C   LEU A 102     570.404 -32.729 193.364  1.00 75.94           C  
ANISOU  718  C   LEU A 102     7419   9759  11677    319    449    183       C  
ATOM    719  O   LEU A 102     570.799 -33.680 192.689  1.00 76.07           O  
ANISOU  719  O   LEU A 102     7488   9829  11585    231    376    193       O  
ATOM    720  CB  LEU A 102     571.330 -30.423 193.054  1.00 76.85           C  
ANISOU  720  CB  LEU A 102     7756   9705  11739    559    349    377       C  
ATOM    721  CG  LEU A 102     571.293 -29.123 192.255  1.00 78.55           C  
ANISOU  721  CG  LEU A 102     8013   9851  11982    745    183    495       C  
ATOM    722  CD1 LEU A 102     572.693 -28.554 192.180  1.00 77.94           C  
ANISOU  722  CD1 LEU A 102     8195   9666  11755    718    212    638       C  
ATOM    723  CD2 LEU A 102     570.666 -29.301 190.855  1.00 80.36           C  
ANISOU  723  CD2 LEU A 102     8150  10198  12187    833    -63    535       C  
ATOM    724  N   ALA A 103     570.118 -32.818 194.662  1.00 57.51           N  
ANISOU  724  N   ALA A 103     5040   7389   9423    249    664    107       N  
ATOM    725  CA  ALA A 103     570.261 -34.079 195.385  1.00 55.96           C  
ANISOU  725  CA  ALA A 103     4870   7205   9188     57    824     63       C  
ATOM    726  C   ALA A 103     569.470 -35.172 194.693  1.00 57.00           C  
ANISOU  726  C   ALA A 103     4825   7425   9406    -28    744    -21       C  
ATOM    727  O   ALA A 103     569.972 -36.260 194.487  1.00 56.57           O  
ANISOU  727  O   ALA A 103     4859   7366   9269   -154    743     -9       O  
ATOM    728  CB  ALA A 103     569.818 -33.945 196.835  1.00 55.77           C  
ANISOU  728  CB  ALA A 103     4800   7157   9234      3   1069     -8       C  
ATOM    729  N   PHE A 104     568.238 -34.889 194.300  1.00 71.46           N  
ANISOU  729  N   PHE A 104     6397   9332  11421     47    662   -118       N  
ATOM    730  CA  PHE A 104     567.447 -35.945 193.682  1.00 72.57           C  
ANISOU  730  CA  PHE A 104     6346   9561  11666    -51    581   -227       C  
ATOM    731  C   PHE A 104     567.951 -36.300 192.277  1.00 74.01           C  
ANISOU  731  C   PHE A 104     6615   9793  11711    -19    332   -189       C  
ATOM    732  O   PHE A 104     568.032 -37.475 191.953  1.00 74.26           O  
ANISOU  732  O   PHE A 104     6648   9842  11725   -159    315   -248       O  
ATOM    733  CB  PHE A 104     565.956 -35.575 193.657  1.00 73.96           C  
ANISOU  733  CB  PHE A 104     6182   9822  12098     20    550   -366       C  
ATOM    734  CG  PHE A 104     565.280 -35.712 195.000  1.00 72.98           C  
ANISOU  734  CG  PHE A 104     5921   9685  12125    -83    839   -456       C  
ATOM    735  CD1 PHE A 104     565.452 -34.764 195.981  1.00 72.11           C  
ANISOU  735  CD1 PHE A 104     5881   9517  12001     -4   1005   -429       C  
ATOM    736  CD2 PHE A 104     564.508 -36.799 195.294  1.00 73.17           C  
ANISOU  736  CD2 PHE A 104     5757   9751  12294   -273    959   -570       C  
ATOM    737  CE1 PHE A 104     564.845 -34.886 197.225  1.00 71.57           C  
ANISOU  737  CE1 PHE A 104     5701   9458  12034   -101   1291   -519       C  
ATOM    738  CE2 PHE A 104     563.906 -36.919 196.540  1.00 72.54           C  
ANISOU  738  CE2 PHE A 104     5565   9670  12328   -383   1255   -637       C  
ATOM    739  CZ  PHE A 104     564.078 -35.953 197.500  1.00 71.78           C  
ANISOU  739  CZ  PHE A 104     5546   9540  12188   -291   1423   -613       C  
ATOM    740  N   VAL A 105     568.333 -35.333 191.449  1.00 86.66           N  
ANISOU  740  N   VAL A 105     8310  11413  13206    153    152    -91       N  
ATOM    741  CA  VAL A 105     568.704 -35.709 190.087  1.00 88.51           C  
ANISOU  741  CA  VAL A 105     8616  11727  13287    175    -71    -70       C  
ATOM    742  C   VAL A 105     570.049 -36.453 190.066  1.00 87.39           C  
ANISOU  742  C   VAL A 105     8727  11532  12947     60      6     -8       C  
ATOM    743  O   VAL A 105     570.356 -37.171 189.118  1.00 88.55           O  
ANISOU  743  O   VAL A 105     8921  11744  12980     21   -117    -44       O  
ATOM    744  CB  VAL A 105     568.754 -34.495 189.129  1.00 90.33           C  
ANISOU  744  CB  VAL A 105     8899  11996  13428    384   -284     46       C  
ATOM    745  CG1 VAL A 105     568.793 -34.966 187.686  1.00 92.90           C  
ANISOU  745  CG1 VAL A 105     9246  12454  13598    404   -526     32       C  
ATOM    746  CG2 VAL A 105     567.540 -33.652 189.293  1.00 91.17           C  
ANISOU  746  CG2 VAL A 105     8768  12120  13752    529   -352     -2       C  
ATOM    747  N   SER A 106     570.852 -36.315 191.110  1.00101.02           N  
ANISOU  747  N   SER A 106    10607  13145  14633      9    201     67       N  
ATOM    748  CA  SER A 106     572.097 -37.073 191.134  1.00 99.80           C  
ANISOU  748  CA  SER A 106    10659  12939  14322    -88    262    112       C  
ATOM    749  C   SER A 106     571.863 -38.462 191.725  1.00 99.00           C  
ANISOU  749  C   SER A 106    10508  12796  14311   -263    379     14       C  
ATOM    750  O   SER A 106     572.454 -39.445 191.267  1.00 99.56           O  
ANISOU  750  O   SER A 106    10665  12855  14311   -340    346    -16       O  
ATOM    751  CB  SER A 106     573.181 -36.330 191.915  1.00 97.49           C  
ANISOU  751  CB  SER A 106    10559  12547  13935    -59    383    236       C  
ATOM    752  OG  SER A 106     572.832 -36.220 193.279  1.00 95.70           O  
ANISOU  752  OG  SER A 106    10296  12254  13811   -107    565    215       O  
ATOM    753  N   ALA A 107     570.992 -38.533 192.733  1.00 70.74           N  
ANISOU  753  N   ALA A 107     6794   9188  10895   -327    524    -35       N  
ATOM    754  CA  ALA A 107     570.619 -39.802 193.371  1.00 70.20           C  
ANISOU  754  CA  ALA A 107     6673   9066  10935   -510    660   -107       C  
ATOM    755  C   ALA A 107     570.085 -40.763 192.337  1.00 72.35           C  
ANISOU  755  C   ALA A 107     6816   9391  11284   -579    514   -237       C  
ATOM    756  O   ALA A 107     570.392 -41.948 192.353  1.00 72.41           O  
ANISOU  756  O   ALA A 107     6885   9323  11304   -712    551   -275       O  
ATOM    757  CB  ALA A 107     569.581 -39.581 194.465  1.00 69.51           C  
ANISOU  757  CB  ALA A 107     6422   8977  11012   -563    843   -150       C  
ATOM    758  N   VAL A 108     569.285 -40.232 191.426  1.00 70.89           N  
ANISOU  758  N   VAL A 108     6453   9330  11152   -478    333   -311       N  
ATOM    759  CA  VAL A 108     568.707 -41.031 190.354  1.00 73.21           C  
ANISOU  759  CA  VAL A 108     6607   9704  11506   -528    156   -462       C  
ATOM    760  C   VAL A 108     569.784 -41.437 189.338  1.00 74.48           C  
ANISOU  760  C   VAL A 108     6968   9881  11452   -501     21   -448       C  
ATOM    761  O   VAL A 108     569.847 -42.595 188.930  1.00 75.44           O  
ANISOU  761  O   VAL A 108     7087   9975  11600   -617    -13   -565       O  
ATOM    762  CB  VAL A 108     567.545 -40.268 189.653  1.00 75.01           C  
ANISOU  762  CB  VAL A 108     6584  10081  11835   -402    -35   -542       C  
ATOM    763  CG1 VAL A 108     566.930 -41.100 188.564  1.00 77.22           C  
ANISOU  763  CG1 VAL A 108     6711  10462  12168   -458   -241   -720       C  
ATOM    764  CG2 VAL A 108     566.480 -39.908 190.662  1.00 74.06           C  
ANISOU  764  CG2 VAL A 108     6238   9952  11951   -426    119   -585       C  
ATOM    765  N   LEU A 109     570.647 -40.498 188.955  1.00 62.15           N  
ANISOU  765  N   LEU A 109     5576   8351   9688   -356    -37   -314       N  
ATOM    766  CA  LEU A 109     571.667 -40.768 187.941  1.00 63.67           C  
ANISOU  766  CA  LEU A 109     5944   8585   9662   -323   -144   -303       C  
ATOM    767  C   LEU A 109     572.693 -41.810 188.395  1.00 62.47           C  
ANISOU  767  C   LEU A 109     5951   8304   9480   -438     -7   -308       C  
ATOM    768  O   LEU A 109     573.209 -42.571 187.573  1.00 63.93           O  
ANISOU  768  O   LEU A 109     6205   8513   9573   -464    -84   -396       O  
ATOM    769  CB  LEU A 109     572.386 -39.475 187.539  1.00 63.99           C  
ANISOU  769  CB  LEU A 109     6130   8672   9510   -165   -196   -136       C  
ATOM    770  CG  LEU A 109     571.722 -38.606 186.475  1.00 66.09           C  
ANISOU  770  CG  LEU A 109     6318   9086   9708    -20   -417   -118       C  
ATOM    771  CD1 LEU A 109     572.479 -37.306 186.332  1.00 65.70           C  
ANISOU  771  CD1 LEU A 109     6437   9022   9505    111   -415     83       C  
ATOM    772  CD2 LEU A 109     571.669 -39.347 185.157  1.00 68.77           C  
ANISOU  772  CD2 LEU A 109     6654   9564   9912    -33   -602   -244       C  
ATOM    773  N   MET A 110     572.991 -41.858 189.692  1.00 79.11           N  
ANISOU  773  N   MET A 110     8120  10276  11660   -498    186   -222       N  
ATOM    774  CA  MET A 110     573.915 -42.872 190.212  1.00 77.86           C  
ANISOU  774  CA  MET A 110     8110   9980  11493   -593    298   -212       C  
ATOM    775  C   MET A 110     573.196 -44.207 190.471  1.00 78.33           C  
ANISOU  775  C   MET A 110     8069   9947  11746   -757    343   -339       C  
ATOM    776  O   MET A 110     573.641 -45.248 189.994  1.00 79.55           O  
ANISOU  776  O   MET A 110     8282  10039  11903   -814    303   -429       O  
ATOM    777  CB  MET A 110     574.606 -42.376 191.489  1.00 74.69           C  
ANISOU  777  CB  MET A 110     7841   9481  11058   -583    463    -57       C  
ATOM    778  CG  MET A 110     575.388 -41.090 191.287  1.00 73.88           C  
ANISOU  778  CG  MET A 110     7839   9437  10796   -445    431     58       C  
ATOM    779  SD  MET A 110     576.400 -40.624 192.699  1.00 70.59           S  
ANISOU  779  SD  MET A 110     7587   8908  10325   -442    591    200       S  
ATOM    780  CE  MET A 110     575.216 -40.506 194.034  1.00 69.03           C  
ANISOU  780  CE  MET A 110     7284   8669  10274   -512    742    199       C  
ATOM    781  N   GLY A 111     572.076 -44.172 191.195  1.00 67.65           N  
ANISOU  781  N   GLY A 111     6557   8580  10567   -837    432   -356       N  
ATOM    782  CA  GLY A 111     571.373 -45.381 191.585  1.00 68.04           C  
ANISOU  782  CA  GLY A 111     6510   8520  10821  -1021    514   -452       C  
ATOM    783  C   GLY A 111     570.638 -46.109 190.485  1.00 70.92           C  
ANISOU  783  C   GLY A 111     6708   8941  11296  -1084    353   -660       C  
ATOM    784  O   GLY A 111     570.051 -47.159 190.729  1.00 71.69           O  
ANISOU  784  O   GLY A 111     6717   8930  11591  -1256    415   -757       O  
ATOM    785  N   PHE A 112     570.641 -45.551 189.282  1.00 69.47           N  
ANISOU  785  N   PHE A 112     6485   8925  10986   -954    145   -729       N  
ATOM    786  CA  PHE A 112     570.090 -46.248 188.129  1.00 72.02           C  
ANISOU  786  CA  PHE A 112     6678   9323  11361   -999    -43   -946       C  
ATOM    787  C   PHE A 112     571.150 -46.283 187.045  1.00 73.56           C  
ANISOU  787  C   PHE A 112     7050   9588  11312   -893   -178   -973       C  
ATOM    788  O   PHE A 112     570.847 -46.468 185.865  1.00 75.57           O  
ANISOU  788  O   PHE A 112     7235   9978  11499   -864   -375  -1135       O  
ATOM    789  CB  PHE A 112     568.798 -45.588 187.614  1.00 73.07           C  
ANISOU  789  CB  PHE A 112     6546   9637  11579   -949   -196  -1039       C  
ATOM    790  CG  PHE A 112     567.567 -45.913 188.438  1.00 72.38           C  
ANISOU  790  CG  PHE A 112     6213   9498  11791  -1100    -75  -1107       C  
ATOM    791  CD1 PHE A 112     566.989 -47.172 188.385  1.00 73.25           C  
ANISOU  791  CD1 PHE A 112     6198   9515  12118  -1302    -61  -1285       C  
ATOM    792  CD2 PHE A 112     566.996 -44.956 189.268  1.00 71.00           C  
ANISOU  792  CD2 PHE A 112     5928   9359  11689  -1046     38  -1003       C  
ATOM    793  CE1 PHE A 112     565.871 -47.470 189.152  1.00 72.78           C  
ANISOU  793  CE1 PHE A 112     5902   9408  12341  -1463     80  -1341       C  
ATOM    794  CE2 PHE A 112     565.886 -45.245 190.040  1.00 70.54           C  
ANISOU  794  CE2 PHE A 112     5633   9268  11900  -1190    183  -1073       C  
ATOM    795  CZ  PHE A 112     565.316 -46.495 189.980  1.00 71.45           C  
ANISOU  795  CZ  PHE A 112     5618   9302  12228  -1405    209  -1234       C  
ATOM    796  N   SER A 113     572.403 -46.103 187.460  1.00 72.99           N  
ANISOU  796  N   SER A 113     7199   9435  11099   -835    -68   -823       N  
ATOM    797  CA  SER A 113     573.553 -46.403 186.605  1.00 74.39           C  
ANISOU  797  CA  SER A 113     7545   9639  11082   -769   -133   -864       C  
ATOM    798  C   SER A 113     573.725 -47.902 186.534  1.00 75.06           C  
ANISOU  798  C   SER A 113     7651   9566  11301   -896   -111  -1031       C  
ATOM    799  O   SER A 113     574.504 -48.402 185.724  1.00 76.52           O  
ANISOU  799  O   SER A 113     7935   9769  11371   -858   -172  -1139       O  
ATOM    800  CB  SER A 113     574.819 -45.758 187.134  1.00 72.91           C  
ANISOU  800  CB  SER A 113     7549   9409  10745   -678    -17   -668       C  
ATOM    801  OG  SER A 113     574.872 -45.916 188.530  1.00 70.14           O  
ANISOU  801  OG  SER A 113     7232   8889  10531   -749    155   -549       O  
ATOM    802  N   LYS A 114     572.994 -48.599 187.414  1.00100.84           N  
ANISOU  802  N   LYS A 114    10826  12669  14821  -1048     -9  -1048       N  
ATOM    803  CA  LYS A 114     572.813 -50.048 187.356  1.00101.66           C  
ANISOU  803  CA  LYS A 114    10910  12593  15123  -1200      0  -1218       C  
ATOM    804  C   LYS A 114     572.318 -50.454 185.972  1.00104.07           C  
ANISOU  804  C   LYS A 114    11100  13033  15409  -1209   -209  -1489       C  
ATOM    805  O   LYS A 114     573.145 -50.713 185.093  1.00105.32           O  
ANISOU  805  O   LYS A 114    11373  13240  15403  -1130   -291  -1591       O  
ATOM    806  CB  LYS A 114     571.844 -50.560 188.461  1.00100.39           C  
ANISOU  806  CB  LYS A 114    10634  12267  15242  -1386    147  -1181       C  
ATOM    807  CG  LYS A 114     570.482 -49.850 188.635  1.00100.05           C  
ANISOU  807  CG  LYS A 114    10344  12367  15302  -1425    137  -1193       C  
ATOM    808  CD  LYS A 114     569.379 -50.813 189.107  1.00100.22           C  
ANISOU  808  CD  LYS A 114    10188  12248  15643  -1658    224  -1302       C  
ATOM    809  CE  LYS A 114     569.567 -51.289 190.551  1.00 98.57           C  
ANISOU  809  CE  LYS A 114    10098  11805  15549  -1785    486  -1111       C  
ATOM    810  NZ  LYS A 114     568.439 -52.184 190.988  1.00 99.21           N  
ANISOU  810  NZ  LYS A 114    10000  11751  15945  -2035    596  -1203       N  
ATOM    811  N   LEU A 115     570.994 -50.487 185.759  1.00 80.74           N  
ANISOU  811  N   LEU A 115     7912  10155  12609  -1300   -297  -1617       N  
ATOM    812  CA  LEU A 115     570.465 -51.013 184.499  1.00 82.92           C  
ANISOU  812  CA  LEU A 115     8069  10549  12886  -1329   -514  -1906       C  
ATOM    813  C   LEU A 115     570.694 -49.976 183.419  1.00 83.94           C  
ANISOU  813  C   LEU A 115     8231  10969  12693  -1135   -698  -1897       C  
ATOM    814  O   LEU A 115     570.446 -50.216 182.240  1.00 85.67           O  
ANISOU  814  O   LEU A 115     8400  11345  12806  -1113   -903  -2114       O  
ATOM    815  CB  LEU A 115     568.975 -51.420 184.592  1.00 83.36           C  
ANISOU  815  CB  LEU A 115     7839  10600  13233  -1497   -568  -2068       C  
ATOM    816  CG  LEU A 115     568.679 -52.732 183.785  1.00 85.23           C  
ANISOU  816  CG  LEU A 115     8006  10760  13618  -1639   -695  -2398       C  
ATOM    817  CD1 LEU A 115     569.353 -53.988 184.407  1.00 85.15           C  
ANISOU  817  CD1 LEU A 115     8154  10407  13791  -1773   -518  -2406       C  
ATOM    818  CD2 LEU A 115     567.182 -53.028 183.451  1.00 86.23           C  
ANISOU  818  CD2 LEU A 115     7807  10964  13991  -1785   -836  -2632       C  
ATOM    819  N   GLY A 116     571.207 -48.827 183.834  1.00 84.79           N  
ANISOU  819  N   GLY A 116     8440  11141  12635   -999   -622  -1641       N  
ATOM    820  CA  GLY A 116     571.664 -47.832 182.895  1.00 85.82           C  
ANISOU  820  CA  GLY A 116     8661  11502  12444   -819   -755  -1576       C  
ATOM    821  C   GLY A 116     572.796 -48.375 182.040  1.00 86.95           C  
ANISOU  821  C   GLY A 116     8990  11672  12376   -777   -777  -1682       C  
ATOM    822  O   GLY A 116     572.850 -48.076 180.839  1.00 88.43           O  
ANISOU  822  O   GLY A 116     9207  12079  12313   -687   -945  -1772       O  
ATOM    823  N   LYS A 117     573.689 -49.160 182.655  1.00117.91           N  
ANISOU  823  N   LYS A 117    13035  15375  16390   -833   -607  -1671       N  
ATOM    824  CA  LYS A 117     574.855 -49.720 181.970  1.00118.82           C  
ANISOU  824  CA  LYS A 117    13312  15489  16345   -785   -594  -1781       C  
ATOM    825  C   LYS A 117     575.804 -48.569 181.623  1.00118.91           C  
ANISOU  825  C   LYS A 117    13465  15668  16047   -628   -564  -1591       C  
ATOM    826  O   LYS A 117     576.619 -48.656 180.704  1.00119.88           O  
ANISOU  826  O   LYS A 117    13696  15909  15944   -559   -585  -1680       O  
ATOM    827  CB  LYS A 117     574.407 -50.512 180.725  1.00120.58           C  
ANISOU  827  CB  LYS A 117    13472  15825  16520   -823   -777  -2108       C  
ATOM    828  CG  LYS A 117     575.474 -51.192 179.877  1.00121.47           C  
ANISOU  828  CG  LYS A 117    13726  15958  16470   -776   -770  -2295       C  
ATOM    829  CD  LYS A 117     574.904 -51.614 178.513  1.00123.29           C  
ANISOU  829  CD  LYS A 117    13896  16389  16560   -787   -986  -2608       C  
ATOM    830  CE  LYS A 117     574.233 -50.452 177.751  1.00124.17           C  
ANISOU  830  CE  LYS A 117    13957  16820  16401   -694  -1171  -2527       C  
ATOM    831  NZ  LYS A 117     575.188 -49.412 177.249  1.00124.37           N  
ANISOU  831  NZ  LYS A 117    14156  17040  16058   -541  -1124  -2330       N  
ATOM    832  N   SER A 118     575.698 -47.484 182.386  1.00101.52           N  
ANISOU  832  N   SER A 118    11259  13468  13845   -581   -497  -1335       N  
ATOM    833  CA  SER A 118     576.430 -46.259 182.076  1.00101.63           C  
ANISOU  833  CA  SER A 118    11390  13628  13599   -450   -477  -1140       C  
ATOM    834  C   SER A 118     577.163 -45.716 183.285  1.00 99.86           C  
ANISOU  834  C   SER A 118    11244  13256  13443   -433   -295   -908       C  
ATOM    835  O   SER A 118     576.552 -45.416 184.308  1.00 98.17           O  
ANISOU  835  O   SER A 118    10958  12940  13402   -471   -240   -799       O  
ATOM    836  CB  SER A 118     575.478 -45.194 181.534  1.00102.15           C  
ANISOU  836  CB  SER A 118    11373  13886  13551   -377   -638  -1065       C  
ATOM    837  OG  SER A 118     576.166 -43.987 181.262  1.00102.19           O  
ANISOU  837  OG  SER A 118    11506  13997  13324   -262   -611   -853       O  
ATOM    838  N   PHE A 119     578.478 -45.598 183.162  1.00 92.22           N  
ANISOU  838  N   PHE A 119    10414  12288  12338   -379   -199   -851       N  
ATOM    839  CA  PHE A 119     579.293 -45.045 184.227  1.00 90.49           C  
ANISOU  839  CA  PHE A 119    10269  11951  12162   -357    -50   -650       C  
ATOM    840  C   PHE A 119     579.407 -43.551 184.030  1.00 90.08           C  
ANISOU  840  C   PHE A 119    10258  12028  11941   -273    -58   -455       C  
ATOM    841  O   PHE A 119     580.003 -42.843 184.845  1.00 88.06           O  
ANISOU  841  O   PHE A 119    10057  11697  11706   -251     47   -286       O  
ATOM    842  CB  PHE A 119     580.671 -45.677 184.228  1.00 90.81           C  
ANISOU  842  CB  PHE A 119    10407  11920  12176   -341     49   -700       C  
ATOM    843  CG  PHE A 119     581.305 -45.717 182.875  1.00 92.38           C  
ANISOU  843  CG  PHE A 119    10658  12300  12142   -287     16   -819       C  
ATOM    844  CD1 PHE A 119     581.950 -44.604 182.364  1.00 91.87           C  
ANISOU  844  CD1 PHE A 119    10664  12390  11851   -220     52   -680       C  
ATOM    845  CD2 PHE A 119     581.237 -46.863 182.103  1.00 93.17           C  
ANISOU  845  CD2 PHE A 119    10741  12413  12246   -312    -41  -1076       C  
ATOM    846  CE1 PHE A 119     582.521 -44.639 181.110  1.00 91.95           C  
ANISOU  846  CE1 PHE A 119    10732  12586  11620   -182     47   -781       C  
ATOM    847  CE2 PHE A 119     581.807 -46.905 180.852  1.00 93.72           C  
ANISOU  847  CE2 PHE A 119    10864  12672  12073   -262    -57  -1204       C  
ATOM    848  CZ  PHE A 119     582.450 -45.792 180.352  1.00 93.11           C  
ANISOU  848  CZ  PHE A 119    10862  12769  11746   -199     -5  -1050       C  
ATOM    849  N   GLU A 120     578.869 -43.087 182.905  1.00 78.90           N  
ANISOU  849  N   GLU A 120     8825  10800  10351   -224   -194   -482       N  
ATOM    850  CA  GLU A 120     578.748 -41.666 182.642  1.00 78.51           C  
ANISOU  850  CA  GLU A 120     8815  10854  10162   -140   -232   -285       C  
ATOM    851  C   GLU A 120     577.801 -41.116 183.691  1.00 76.67           C  
ANISOU  851  C   GLU A 120     8478  10516  10136   -142   -232   -187       C  
ATOM    852  O   GLU A 120     578.181 -40.251 184.482  1.00 74.61           O  
ANISOU  852  O   GLU A 120     8264  10171   9915   -116   -134    -18       O  
ATOM    853  CB  GLU A 120     578.240 -41.404 181.224  1.00 80.15           C  
ANISOU  853  CB  GLU A 120     9031  11283  10138    -80   -408   -334       C  
ATOM    854  CG  GLU A 120     579.110 -42.003 180.123  1.00 81.12           C  
ANISOU  854  CG  GLU A 120     9256  11541  10026    -82   -396   -466       C  
ATOM    855  CD  GLU A 120     578.813 -43.483 179.830  1.00 82.26           C  
ANISOU  855  CD  GLU A 120     9328  11672  10256   -152   -451   -762       C  
ATOM    856  OE1 GLU A 120     577.631 -43.861 179.669  1.00 82.74           O  
ANISOU  856  OE1 GLU A 120     9266  11759  10411   -178   -607   -886       O  
ATOM    857  OE2 GLU A 120     579.766 -44.283 179.749  1.00 82.55           O  
ANISOU  857  OE2 GLU A 120     9420  11662  10284   -180   -342   -885       O  
ATOM    858  N   MET A 121     576.588 -41.677 183.715  1.00 69.28           N  
ANISOU  858  N   MET A 121     7393   9585   9345   -184   -333   -318       N  
ATOM    859  CA  MET A 121     575.560 -41.394 184.726  1.00 67.61           C  
ANISOU  859  CA  MET A 121     7043   9282   9363   -207   -312   -279       C  
ATOM    860  C   MET A 121     576.125 -41.366 186.146  1.00 64.74           C  
ANISOU  860  C   MET A 121     6734   8737   9129   -255   -113   -176       C  
ATOM    861  O   MET A 121     575.675 -40.607 187.012  1.00 62.48           O  
ANISOU  861  O   MET A 121     6400   8395   8945   -234    -54    -73       O  
ATOM    862  CB  MET A 121     574.449 -42.445 184.674  1.00 68.20           C  
ANISOU  862  CB  MET A 121     6945   9352   9617   -301   -389   -481       C  
ATOM    863  CG  MET A 121     573.741 -42.608 183.337  1.00 70.51           C  
ANISOU  863  CG  MET A 121     7155   9833   9804   -266   -616   -628       C  
ATOM    864  SD  MET A 121     572.498 -43.949 183.328  1.00 71.10           S  
ANISOU  864  SD  MET A 121     7002   9877  10135   -413   -701   -905       S  
ATOM    865  CE  MET A 121     571.596 -43.615 184.839  1.00 68.74           C  
ANISOU  865  CE  MET A 121     6539   9437  10141   -472   -555   -812       C  
ATOM    866  N   LEU A 122     577.114 -42.210 186.388  1.00 72.86           N  
ANISOU  866  N   LEU A 122     7860   9674  10149   -311    -18   -216       N  
ATOM    867  CA  LEU A 122     577.722 -42.262 187.706  1.00 69.58           C  
ANISOU  867  CA  LEU A 122     7510   9098   9829   -349    142   -119       C  
ATOM    868  C   LEU A 122     578.625 -41.051 187.946  1.00 67.55           C  
ANISOU  868  C   LEU A 122     7360   8853   9454   -269    199     51       C  
ATOM    869  O   LEU A 122     578.605 -40.458 189.022  1.00 64.34           O  
ANISOU  869  O   LEU A 122     6965   8364   9119   -269    287    153       O  
ATOM    870  CB  LEU A 122     578.511 -43.566 187.875  1.00 69.95           C  
ANISOU  870  CB  LEU A 122     7625   9032   9922   -413    199   -211       C  
ATOM    871  CG  LEU A 122     578.974 -43.879 189.292  1.00 66.69           C  
ANISOU  871  CG  LEU A 122     7276   8442   9619   -460    333   -120       C  
ATOM    872  CD1 LEU A 122     577.821 -44.382 190.071  1.00 65.62           C  
ANISOU  872  CD1 LEU A 122     7048   8218   9665   -560    376   -143       C  
ATOM    873  CD2 LEU A 122     579.999 -44.935 189.220  1.00 67.72           C  
ANISOU  873  CD2 LEU A 122     7492   8478   9761   -471    355   -188       C  
ATOM    874  N   ILE A 123     579.413 -40.701 186.935  1.00 80.38           N  
ANISOU  874  N   ILE A 123     9062  10581  10896   -212    159     69       N  
ATOM    875  CA  ILE A 123     580.306 -39.562 187.006  1.00 78.22           C  
ANISOU  875  CA  ILE A 123     8884  10318  10520   -157    216    223       C  
ATOM    876  C   ILE A 123     579.519 -38.265 187.024  1.00 78.18           C  
ANISOU  876  C   ILE A 123     8848  10339  10519    -92    165    343       C  
ATOM    877  O   ILE A 123     579.769 -37.381 187.834  1.00 75.48           O  
ANISOU  877  O   ILE A 123     8540   9913  10227    -73    238    456       O  
ATOM    878  CB  ILE A 123     581.270 -39.560 185.818  1.00 79.94           C  
ANISOU  878  CB  ILE A 123     9183  10654  10537   -131    206    209       C  
ATOM    879  CG1 ILE A 123     582.436 -40.523 186.078  1.00 79.04           C  
ANISOU  879  CG1 ILE A 123     9109  10477  10447   -169    299    123       C  
ATOM    880  CG2 ILE A 123     581.762 -38.136 185.524  1.00 78.35           C  
ANISOU  880  CG2 ILE A 123     9059  10494  10215    -79    231    388       C  
ATOM    881  CD1 ILE A 123     583.003 -41.137 184.817  1.00 81.15           C  
ANISOU  881  CD1 ILE A 123     9405  10872  10557   -159    280     -4       C  
ATOM    882  N   LEU A 124     578.556 -38.174 186.115  1.00 55.39           N  
ANISOU  882  N   LEU A 124     5893   7567   7587    -49     25    305       N  
ATOM    883  CA  LEU A 124     577.623 -37.055 186.062  1.00 55.63           C  
ANISOU  883  CA  LEU A 124     5867   7617   7654     37    -60    400       C  
ATOM    884  C   LEU A 124     576.930 -36.804 187.389  1.00 52.92           C  
ANISOU  884  C   LEU A 124     5428   7152   7527     23     17    404       C  
ATOM    885  O   LEU A 124     576.945 -35.705 187.906  1.00 51.55           O  
ANISOU  885  O   LEU A 124     5279   6911   7396     81     57    517       O  
ATOM    886  CB  LEU A 124     576.571 -37.299 184.995  1.00 58.30           C  
ANISOU  886  CB  LEU A 124     6108   8100   7942     80   -250    315       C  
ATOM    887  CG  LEU A 124     575.586 -36.149 184.843  1.00 58.49           C  
ANISOU  887  CG  LEU A 124     6062   8149   8014    198   -371    414       C  
ATOM    888  CD1 LEU A 124     576.336 -34.846 184.756  1.00 57.80           C  
ANISOU  888  CD1 LEU A 124     6125   8011   7825    272   -330    625       C  
ATOM    889  CD2 LEU A 124     574.756 -36.363 183.592  1.00 61.01           C  
ANISOU  889  CD2 LEU A 124     6311   8644   8227    257   -597    341       C  
ATOM    890  N   GLY A 125     576.314 -37.828 187.944  1.00 50.72           N  
ANISOU  890  N   GLY A 125     5043   6841   7388    -60     49    275       N  
ATOM    891  CA  GLY A 125     575.633 -37.662 189.211  1.00 50.42           C  
ANISOU  891  CA  GLY A 125     4916   6709   7534    -88    152    272       C  
ATOM    892  C   GLY A 125     576.619 -37.278 190.288  1.00 48.77           C  
ANISOU  892  C   GLY A 125     4835   6385   7311   -107    304    364       C  
ATOM    893  O   GLY A 125     576.279 -36.663 191.286  1.00 48.57           O  
ANISOU  893  O   GLY A 125     4783   6293   7377    -95    391    396       O  
ATOM    894  N   ARG A 126     577.865 -37.669 190.080  1.00 72.24           N  
ANISOU  894  N   ARG A 126     7937   9341  10168   -136    333    386       N  
ATOM    895  CA  ARG A 126     578.913 -37.327 191.026  1.00 69.11           C  
ANISOU  895  CA  ARG A 126     7653   8851   9753   -151    447    462       C  
ATOM    896  C   ARG A 126     579.215 -35.845 190.888  1.00 68.95           C  
ANISOU  896  C   ARG A 126     7685   8825   9689    -70    437    576       C  
ATOM    897  O   ARG A 126     579.393 -35.140 191.881  1.00 67.04           O  
ANISOU  897  O   ARG A 126     7475   8499   9498    -64    515    618       O  
ATOM    898  CB  ARG A 126     580.163 -38.187 190.803  1.00 68.69           C  
ANISOU  898  CB  ARG A 126     7692   8786   9619   -193    469    437       C  
ATOM    899  CG  ARG A 126     580.061 -39.539 191.462  1.00 68.27           C  
ANISOU  899  CG  ARG A 126     7628   8658   9652   -275    514    358       C  
ATOM    900  CD  ARG A 126     580.130 -39.398 192.964  1.00 65.51           C  
ANISOU  900  CD  ARG A 126     7321   8208   9363   -308    620    414       C  
ATOM    901  NE  ARG A 126     581.496 -39.101 193.392  1.00 63.46           N  
ANISOU  901  NE  ARG A 126     7170   7909   9033   -287    650    473       N  
ATOM    902  CZ  ARG A 126     581.850 -38.857 194.649  1.00 61.60           C  
ANISOU  902  CZ  ARG A 126     6997   7604   8803   -301    718    522       C  
ATOM    903  NH1 ARG A 126     580.920 -38.869 195.606  1.00 61.34           N  
ANISOU  903  NH1 ARG A 126     6943   7538   8826   -339    787    525       N  
ATOM    904  NH2 ARG A 126     583.124 -38.591 194.941  1.00 60.43           N  
ANISOU  904  NH2 ARG A 126     6925   7436   8601   -281    717    556       N  
ATOM    905  N   PHE A 127     579.234 -35.372 189.650  1.00 72.70           N  
ANISOU  905  N   PHE A 127     8175   9383  10063    -11    338    623       N  
ATOM    906  CA  PHE A 127     579.417 -33.970 189.408  1.00 73.41           C  
ANISOU  906  CA  PHE A 127     8323   9446  10126     64    320    752       C  
ATOM    907  C   PHE A 127     578.318 -33.187 190.105  1.00 73.77           C  
ANISOU  907  C   PHE A 127     8281   9426  10324    128    314    756       C  
ATOM    908  O   PHE A 127     578.564 -32.469 191.060  1.00 72.11           O  
ANISOU  908  O   PHE A 127     8104   9109  10186    133    401    784       O  
ATOM    909  CB  PHE A 127     579.406 -33.679 187.920  1.00 76.80           C  
ANISOU  909  CB  PHE A 127     8790   9987  10405    119    203    818       C  
ATOM    910  CG  PHE A 127     579.607 -32.233 187.604  1.00 77.39           C  
ANISOU  910  CG  PHE A 127     8946  10007  10452    191    184    984       C  
ATOM    911  CD1 PHE A 127     580.884 -31.651 187.710  1.00 74.48           C  
ANISOU  911  CD1 PHE A 127     8696   9572  10032    146    286   1076       C  
ATOM    912  CD2 PHE A 127     578.535 -31.439 187.234  1.00 79.02           C  
ANISOU  912  CD2 PHE A 127     9104  10211  10709    304     63   1047       C  
ATOM    913  CE1 PHE A 127     581.090 -30.309 187.435  1.00 74.40           C  
ANISOU  913  CE1 PHE A 127     8771   9479  10020    192    281   1237       C  
ATOM    914  CE2 PHE A 127     578.734 -30.103 186.957  1.00 78.59           C  
ANISOU  914  CE2 PHE A 127     9144  10069  10649    374     43   1216       C  
ATOM    915  CZ  PHE A 127     580.018 -29.532 187.061  1.00 76.54           C  
ANISOU  915  CZ  PHE A 127     9019   9727  10338    309    160   1316       C  
ATOM    916  N   ILE A 128     577.097 -33.349 189.617  1.00 51.70           N  
ANISOU  916  N   ILE A 128     5360   6703   7583    180    208    707       N  
ATOM    917  CA  ILE A 128     575.921 -32.697 190.173  1.00 51.64           C  
ANISOU  917  CA  ILE A 128     5224   6654   7744    256    196    681       C  
ATOM    918  C   ILE A 128     575.835 -32.741 191.702  1.00 49.65           C  
ANISOU  918  C   ILE A 128     4944   6308   7613    200    364    616       C  
ATOM    919  O   ILE A 128     575.678 -31.712 192.335  1.00 49.95           O  
ANISOU  919  O   ILE A 128     4985   6258   7736    264    412    641       O  
ATOM    920  CB  ILE A 128     574.669 -33.306 189.592  1.00 53.00           C  
ANISOU  920  CB  ILE A 128     5221   6937   7981    279     75    583       C  
ATOM    921  CG1 ILE A 128     574.744 -33.214 188.067  1.00 55.47           C  
ANISOU  921  CG1 ILE A 128     5579   7363   8132    345   -110    644       C  
ATOM    922  CG2 ILE A 128     573.446 -32.610 190.165  1.00 53.33           C  
ANISOU  922  CG2 ILE A 128     5096   6944   8223    368     70    541       C  
ATOM    923  CD1 ILE A 128     573.411 -33.241 187.392  1.00 57.43           C  
ANISOU  923  CD1 ILE A 128     5652   7717   8452    430   -292    580       C  
ATOM    924  N   ILE A 129     575.958 -33.905 192.318  1.00 63.40           N  
ANISOU  924  N   ILE A 129     6676   8060   9355     83    454    535       N  
ATOM    925  CA  ILE A 129     575.951 -33.928 193.781  1.00 61.16           C  
ANISOU  925  CA  ILE A 129     6401   7700   9136     28    616    496       C  
ATOM    926  C   ILE A 129     577.212 -33.227 194.314  1.00 59.70           C  
ANISOU  926  C   ILE A 129     6383   7431   8870     29    674    569       C  
ATOM    927  O   ILE A 129     577.296 -32.876 195.492  1.00 58.74           O  
ANISOU  927  O   ILE A 129     6294   7248   8776     12    785    543       O  
ATOM    928  CB  ILE A 129     575.855 -35.376 194.353  1.00 59.81           C  
ANISOU  928  CB  ILE A 129     6213   7540   8973   -105    702    426       C  
ATOM    929  CG1 ILE A 129     575.534 -35.341 195.848  1.00 58.36           C  
ANISOU  929  CG1 ILE A 129     6026   7305   8842   -156    872    393       C  
ATOM    930  CG2 ILE A 129     577.143 -36.168 194.103  1.00 58.74           C  
ANISOU  930  CG2 ILE A 129     6220   7388   8711   -166    688    462       C  
ATOM    931  CD1 ILE A 129     574.383 -34.502 196.191  1.00 59.44           C  
ANISOU  931  CD1 ILE A 129     6018   7456   9111    -87    914    336       C  
ATOM    932  N   GLY A 130     578.195 -33.001 193.454  1.00 64.08           N  
ANISOU  932  N   GLY A 130     7036   7991   9320     43    603    649       N  
ATOM    933  CA  GLY A 130     579.299 -32.156 193.862  1.00 63.20           C  
ANISOU  933  CA  GLY A 130     7046   7797   9170     43    648    711       C  
ATOM    934  C   GLY A 130     578.858 -30.695 193.910  1.00 65.43           C  
ANISOU  934  C   GLY A 130     7320   7998   9544    141    632    752       C  
ATOM    935  O   GLY A 130     579.175 -29.960 194.857  1.00 65.13           O  
ANISOU  935  O   GLY A 130     7331   7864   9553    141    707    731       O  
ATOM    936  N   VAL A 131     578.130 -30.266 192.878  1.00 57.08           N  
ANISOU  936  N   VAL A 131     6204   6969   8513    232    521    805       N  
ATOM    937  CA  VAL A 131     577.575 -28.920 192.847  1.00 58.55           C  
ANISOU  937  CA  VAL A 131     6374   7058   8816    350    483    851       C  
ATOM    938  C   VAL A 131     576.713 -28.699 194.081  1.00 57.84           C  
ANISOU  938  C   VAL A 131     6184   6920   8873    378    578    725       C  
ATOM    939  O   VAL A 131     576.905 -27.719 194.805  1.00 58.09           O  
ANISOU  939  O   VAL A 131     6262   6828   8981    412    640    708       O  
ATOM    940  CB  VAL A 131     576.749 -28.666 191.574  1.00 60.40           C  
ANISOU  940  CB  VAL A 131     6545   7351   9053    461    320    925       C  
ATOM    941  CG1 VAL A 131     576.038 -27.361 191.670  1.00 61.29           C  
ANISOU  941  CG1 VAL A 131     6621   7342   9324    606    273    962       C  
ATOM    942  CG2 VAL A 131     577.652 -28.645 190.374  1.00 61.13           C  
ANISOU  942  CG2 VAL A 131     6768   7488   8971    439    249   1063       C  
ATOM    943  N   TYR A 132     575.788 -29.623 194.332  1.00 75.02           N  
ANISOU  943  N   TYR A 132     8222   9194  11089    351    602    625       N  
ATOM    944  CA  TYR A 132     574.907 -29.515 195.487  1.00 74.64           C  
ANISOU  944  CA  TYR A 132     8063   9130  11167    363    724    498       C  
ATOM    945  C   TYR A 132     575.725 -29.377 196.751  1.00 73.35           C  
ANISOU  945  C   TYR A 132     8024   8900  10944    286    870    457       C  
ATOM    946  O   TYR A 132     575.405 -28.583 197.630  1.00 74.02           O  
ANISOU  946  O   TYR A 132     8093   8918  11114    335    958    378       O  
ATOM    947  CB  TYR A 132     573.983 -30.724 195.613  1.00 74.01           C  
ANISOU  947  CB  TYR A 132     7830   9168  11123    292    762    405       C  
ATOM    948  CG  TYR A 132     573.234 -30.792 196.944  1.00 73.48           C  
ANISOU  948  CG  TYR A 132     7668   9103  11147    258    945    278       C  
ATOM    949  CD1 TYR A 132     573.851 -31.281 198.098  1.00 71.87           C  
ANISOU  949  CD1 TYR A 132     7584   8886  10836    141   1101    255       C  
ATOM    950  CD2 TYR A 132     571.917 -30.377 197.044  1.00 74.79           C  
ANISOU  950  CD2 TYR A 132     7625   9295  11497    347    963    180       C  
ATOM    951  CE1 TYR A 132     573.187 -31.341 199.309  1.00 71.81           C  
ANISOU  951  CE1 TYR A 132     7514   8899  10870    101   1284    148       C  
ATOM    952  CE2 TYR A 132     571.241 -30.434 198.252  1.00 74.52           C  
ANISOU  952  CE2 TYR A 132     7498   9280  11534    308   1161     54       C  
ATOM    953  CZ  TYR A 132     571.882 -30.923 199.382  1.00 73.11           C  
ANISOU  953  CZ  TYR A 132     7466   9097  11214    178   1330     43       C  
ATOM    954  OH  TYR A 132     571.217 -30.995 200.595  1.00 73.19           O  
ANISOU  954  OH  TYR A 132     7407   9145  11255    129   1546    -74       O  
ATOM    955  N   CYS A 133     576.780 -30.165 196.858  1.00 89.42           N  
ANISOU  955  N   CYS A 133    10179  10961  12835    175    887    497       N  
ATOM    956  CA  CYS A 133     577.566 -30.131 198.074  1.00 88.36           C  
ANISOU  956  CA  CYS A 133    10161  10785  12628    106    996    457       C  
ATOM    957  C   CYS A 133     578.407 -28.856 198.147  1.00 89.72           C  
ANISOU  957  C   CYS A 133    10434  10839  12815    150    971    484       C  
ATOM    958  O   CYS A 133     578.722 -28.383 199.242  1.00 90.17           O  
ANISOU  958  O   CYS A 133    10554  10844  12862    132   1052    407       O  
ATOM    959  CB  CYS A 133     578.428 -31.386 198.179  1.00 86.13           C  
ANISOU  959  CB  CYS A 133     9961  10556  12209     -7   1000    490       C  
ATOM    960  SG  CYS A 133     577.526 -32.764 198.947  1.00 85.24           S  
ANISOU  960  SG  CYS A 133     9780  10519  12088    -98   1112    428       S  
ATOM    961  N   GLY A 134     578.736 -28.283 196.988  1.00 72.89           N  
ANISOU  961  N   GLY A 134     8325   8664  10707    200    862    591       N  
ATOM    962  CA  GLY A 134     579.488 -27.040 196.940  1.00 74.57           C  
ANISOU  962  CA  GLY A 134     8631   8739  10965    226    844    635       C  
ATOM    963  C   GLY A 134     578.661 -25.876 197.434  1.00 75.90           C  
ANISOU  963  C   GLY A 134     8754   8789  11296    334    872    563       C  
ATOM    964  O   GLY A 134     579.139 -25.025 198.192  1.00 76.45           O  
ANISOU  964  O   GLY A 134     8894   8741  11415    328    922    498       O  
ATOM    965  N   LEU A 135     577.406 -25.860 196.993  1.00 65.85           N  
ANISOU  965  N   LEU A 135     7350   7549  10121    438    832    556       N  
ATOM    966  CA  LEU A 135     576.432 -24.836 197.377  1.00 67.10           C  
ANISOU  966  CA  LEU A 135     7424   7603  10468    573    852    472       C  
ATOM    967  C   LEU A 135     576.085 -24.906 198.857  1.00 67.05           C  
ANISOU  967  C   LEU A 135     7382   7616  10477    544   1015    280       C  
ATOM    968  O   LEU A 135     575.859 -23.885 199.498  1.00 68.22           O  
ANISOU  968  O   LEU A 135     7531   7641  10747    620   1068    176       O  
ATOM    969  CB  LEU A 135     575.153 -24.964 196.536  1.00 67.78           C  
ANISOU  969  CB  LEU A 135     7343   7753  10656    694    753    497       C  
ATOM    970  CG  LEU A 135     575.288 -24.381 195.128  1.00 68.66           C  
ANISOU  970  CG  LEU A 135     7505   7803  10780    783    576    684       C  
ATOM    971  CD1 LEU A 135     574.506 -25.177 194.123  1.00 68.88           C  
ANISOU  971  CD1 LEU A 135     7411   7989  10770    820    451    729       C  
ATOM    972  CD2 LEU A 135     574.856 -22.934 195.112  1.00 69.85           C  
ANISOU  972  CD2 LEU A 135     7654   7754  11133    946    529    699       C  
ATOM    973  N   THR A 136     576.069 -26.115 199.395  1.00 93.01           N  
ANISOU  973  N   THR A 136    10654  11052  13634    432   1098    236       N  
ATOM    974  CA  THR A 136     575.595 -26.345 200.750  1.00 92.80           C  
ANISOU  974  CA  THR A 136    10596  11081  13584    394   1268     75       C  
ATOM    975  C   THR A 136     576.621 -25.938 201.827  1.00 93.26           C  
ANISOU  975  C   THR A 136    10819  11083  13533    329   1336      5       C  
ATOM    976  O   THR A 136     576.241 -25.629 202.955  1.00 93.99           O  
ANISOU  976  O   THR A 136    10909  11184  13620    336   1469   -151       O  
ATOM    977  CB  THR A 136     575.155 -27.842 200.910  1.00 91.00           C  
ANISOU  977  CB  THR A 136    10302  11017  13256    286   1334     80       C  
ATOM    978  OG1 THR A 136     573.808 -27.988 200.438  1.00 91.22           O  
ANISOU  978  OG1 THR A 136    10120  11102  13437    356   1332     41       O  
ATOM    979  CG2 THR A 136     575.211 -28.304 202.349  1.00 90.68           C  
ANISOU  979  CG2 THR A 136    10326  11041  13088    190   1511    -20       C  
ATOM    980  N   THR A 137     577.908 -25.892 201.492  1.00103.14           N  
ANISOU  980  N   THR A 137    12204  12285  14699    266   1246    100       N  
ATOM    981  CA  THR A 137     578.896 -25.391 202.456  1.00104.21           C  
ANISOU  981  CA  THR A 137    12475  12363  14758    211   1278     15       C  
ATOM    982  C   THR A 137     578.649 -23.910 202.785  1.00106.17           C  
ANISOU  982  C   THR A 137    12723  12444  15172    306   1299   -104       C  
ATOM    983  O   THR A 137     579.075 -23.418 203.829  1.00107.18           O  
ANISOU  983  O   THR A 137    12932  12535  15256    278   1357   -249       O  
ATOM    984  CB  THR A 137     580.354 -25.527 201.947  1.00103.96           C  
ANISOU  984  CB  THR A 137    12549  12303  14649    127   1172    128       C  
ATOM    985  OG1 THR A 137     580.388 -26.332 200.764  1.00102.08           O  
ANISOU  985  OG1 THR A 137    12269  12131  14386    114   1096    282       O  
ATOM    986  CG2 THR A 137     581.265 -26.124 203.026  1.00104.33           C  
ANISOU  986  CG2 THR A 137    12700  12427  14514     24   1197     65       C  
ATOM    987  N   GLY A 138     577.987 -23.199 201.874  1.00 58.43           N  
ANISOU  987  N   GLY A 138     6594   6291   9317    426   1238    -46       N  
ATOM    988  CA  GLY A 138     577.664 -21.802 202.078  1.00 59.74           C  
ANISOU  988  CA  GLY A 138     6753   6263   9682    540   1246   -147       C  
ATOM    989  C   GLY A 138     576.307 -21.583 202.725  1.00 60.22           C  
ANISOU  989  C   GLY A 138     6675   6353   9855    654   1360   -321       C  
ATOM    990  O   GLY A 138     576.201 -20.848 203.712  1.00 61.25           O  
ANISOU  990  O   GLY A 138     6829   6409  10035    688   1456   -518       O  
ATOM    991  N   PHE A 139     575.273 -22.219 202.169  1.00 75.31           N  
ANISOU  991  N   PHE A 139     8429   8377  11808    711   1354   -269       N  
ATOM    992  CA  PHE A 139     573.913 -22.105 202.695  1.00 75.77           C  
ANISOU  992  CA  PHE A 139     8307   8486  11995    815   1471   -436       C  
ATOM    993  C   PHE A 139     573.862 -22.399 204.179  1.00 75.91           C  
ANISOU  993  C   PHE A 139     8358   8613  11872    732   1677   -635       C  
ATOM    994  O   PHE A 139     573.364 -21.593 204.942  1.00 77.02           O  
ANISOU  994  O   PHE A 139     8456   8691  12117    819   1786   -836       O  
ATOM    995  CB  PHE A 139     572.941 -23.054 201.993  1.00 74.94           C  
ANISOU  995  CB  PHE A 139     8019   8537  11917    830   1443   -362       C  
ATOM    996  CG  PHE A 139     572.746 -22.778 200.535  1.00 75.13           C  
ANISOU  996  CG  PHE A 139     7991   8491  12066    937   1235   -187       C  
ATOM    997  CD1 PHE A 139     573.042 -21.541 199.998  1.00 75.95           C  
ANISOU  997  CD1 PHE A 139     8167   8378  12313   1059   1116   -119       C  
ATOM    998  CD2 PHE A 139     572.260 -23.776 199.693  1.00 74.57           C  
ANISOU  998  CD2 PHE A 139     7807   8569  11958    910   1154    -87       C  
ATOM    999  CE1 PHE A 139     572.865 -21.299 198.645  1.00 76.23           C  
ANISOU  999  CE1 PHE A 139     8180   8359  12424   1158    921     69       C  
ATOM   1000  CE2 PHE A 139     572.080 -23.546 198.338  1.00 75.01           C  
ANISOU 1000  CE2 PHE A 139     7829   8588  12085   1010    949     71       C  
ATOM   1001  CZ  PHE A 139     572.386 -22.309 197.811  1.00 75.83           C  
ANISOU 1001  CZ  PHE A 139     8021   8488  12301   1137    832    162       C  
ATOM   1002  N   VAL A 140     574.376 -23.552 204.595  1.00 66.48           N  
ANISOU 1002  N   VAL A 140     7248   7578  10432    570   1728   -581       N  
ATOM   1003  CA  VAL A 140     574.106 -24.033 205.954  1.00 66.58           C  
ANISOU 1003  CA  VAL A 140     7285   7735  10279    489   1934   -736       C  
ATOM   1004  C   VAL A 140     574.664 -23.153 207.072  1.00 68.12           C  
ANISOU 1004  C   VAL A 140     7619   7863  10402    491   2005   -922       C  
ATOM   1005  O   VAL A 140     573.876 -22.706 207.909  1.00 69.08           O  
ANISOU 1005  O   VAL A 140     7670   8013  10564    551   2173  -1131       O  
ATOM   1006  CB  VAL A 140     574.616 -25.473 206.188  1.00 65.10           C  
ANISOU 1006  CB  VAL A 140     7192   7707   9838    318   1956   -611       C  
ATOM   1007  CG1 VAL A 140     574.464 -25.823 207.655  1.00 65.47           C  
ANISOU 1007  CG1 VAL A 140     7314   7883   9678    235   2161   -748       C  
ATOM   1008  CG2 VAL A 140     573.883 -26.495 205.280  1.00 63.68           C  
ANISOU 1008  CG2 VAL A 140     6858   7613   9724    294   1926   -480       C  
ATOM   1009  N   PRO A 141     576.001 -22.887 207.095  1.00 85.81           N  
ANISOU 1009  N   PRO A 141    10041  10021  12544    426   1884   -871       N  
ATOM   1010  CA  PRO A 141     576.555 -22.150 208.248  1.00 87.48           C  
ANISOU 1010  CA  PRO A 141    10384  10192  12662    408   1942  -1076       C  
ATOM   1011  C   PRO A 141     575.923 -20.777 208.399  1.00 88.71           C  
ANISOU 1011  C   PRO A 141    10465  10176  13065    559   1990  -1279       C  
ATOM   1012  O   PRO A 141     575.718 -20.292 209.516  1.00 90.07           O  
ANISOU 1012  O   PRO A 141    10674  10371  13177    576   2125  -1524       O  
ATOM   1013  CB  PRO A 141     578.051 -22.025 207.913  1.00 87.67           C  
ANISOU 1013  CB  PRO A 141    10557  10128  12626    324   1764   -968       C  
ATOM   1014  CG  PRO A 141     578.317 -23.055 206.867  1.00 86.01           C  
ANISOU 1014  CG  PRO A 141    10318   9982  12379    269   1662   -711       C  
ATOM   1015  CD  PRO A 141     577.040 -23.131 206.074  1.00 85.02           C  
ANISOU 1015  CD  PRO A 141    10014   9857  12435    372   1694   -657       C  
ATOM   1016  N   MET A 142     575.618 -20.185 207.247  1.00 82.82           N  
ANISOU 1016  N   MET A 142     9621   9258  12588    673   1874  -1170       N  
ATOM   1017  CA  MET A 142     574.902 -18.915 207.119  1.00 83.81           C  
ANISOU 1017  CA  MET A 142     9651   9181  13012    851   1884  -1312       C  
ATOM   1018  C   MET A 142     573.584 -18.927 207.872  1.00 84.38           C  
ANISOU 1018  C   MET A 142     9561   9365  13134    944   2088  -1531       C  
ATOM   1019  O   MET A 142     573.435 -18.256 208.885  1.00 85.67           O  
ANISOU 1019  O   MET A 142     9752   9497  13302    984   2217  -1796       O  
ATOM   1020  CB  MET A 142     574.644 -18.626 205.644  1.00 83.18           C  
ANISOU 1020  CB  MET A 142     9485   8955  13162    957   1714  -1090       C  
ATOM   1021  CG  MET A 142     574.235 -17.230 205.323  1.00 84.37           C  
ANISOU 1021  CG  MET A 142     9593   8829  13635   1140   1658  -1165       C  
ATOM   1022  SD  MET A 142     574.467 -16.934 203.555  1.00 83.78           S  
ANISOU 1022  SD  MET A 142     9529   8581  13723   1207   1415   -825       S  
ATOM   1023  CE  MET A 142     576.072 -17.689 203.247  1.00 82.68           C  
ANISOU 1023  CE  MET A 142     9582   8525  13306    966   1340   -625       C  
ATOM   1024  N   TYR A 143     572.638 -19.704 207.353  1.00113.28           N  
ANISOU 1024  N   TYR A 143    13042  13162  16836    972   2119  -1433       N  
ATOM   1025  CA  TYR A 143     571.335 -19.917 207.965  1.00113.63           C  
ANISOU 1025  CA  TYR A 143    12889  13351  16934   1034   2328  -1617       C  
ATOM   1026  C   TYR A 143     571.421 -20.123 209.479  1.00114.47           C  
ANISOU 1026  C   TYR A 143    13093  13615  16786    933   2563  -1838       C  
ATOM   1027  O   TYR A 143     570.781 -19.402 210.252  1.00115.72           O  
ANISOU 1027  O   TYR A 143    13178  13757  17034   1032   2728  -2110       O  
ATOM   1028  CB  TYR A 143     570.656 -21.119 207.307  1.00112.13           C  
ANISOU 1028  CB  TYR A 143    12539  13340  16725    980   2326  -1447       C  
ATOM   1029  CG  TYR A 143     569.195 -21.290 207.671  1.00112.47           C  
ANISOU 1029  CG  TYR A 143    12313  13514  16905   1053   2522  -1617       C  
ATOM   1030  CD1 TYR A 143     568.198 -20.743 206.876  1.00113.03           C  
ANISOU 1030  CD1 TYR A 143    12137  13499  17311   1248   2439  -1643       C  
ATOM   1031  CD2 TYR A 143     568.810 -22.003 208.806  1.00112.39           C  
ANISOU 1031  CD2 TYR A 143    12290  13720  16692    926   2791  -1747       C  
ATOM   1032  CE1 TYR A 143     566.860 -20.891 207.197  1.00113.48           C  
ANISOU 1032  CE1 TYR A 143    11910  13684  17525   1317   2617  -1817       C  
ATOM   1033  CE2 TYR A 143     567.474 -22.156 209.137  1.00112.79           C  
ANISOU 1033  CE2 TYR A 143    12074  13899  16882    975   2999  -1911       C  
ATOM   1034  CZ  TYR A 143     566.503 -21.598 208.326  1.00113.32           C  
ANISOU 1034  CZ  TYR A 143    11865  13881  17311   1172   2911  -1956       C  
ATOM   1035  OH  TYR A 143     565.167 -21.742 208.637  1.00113.87           O  
ANISOU 1035  OH  TYR A 143    11629  14087  17551   1225   3114  -2137       O  
ATOM   1036  N   VAL A 144     572.224 -21.097 209.898  1.00 93.03           N  
ANISOU 1036  N   VAL A 144    10550  11050  13746    744   2573  -1723       N  
ATOM   1037  CA  VAL A 144     572.385 -21.397 211.318  1.00 93.96           C  
ANISOU 1037  CA  VAL A 144    10800  11339  13562    637   2772  -1890       C  
ATOM   1038  C   VAL A 144     572.964 -20.199 212.068  1.00 95.67           C  
ANISOU 1038  C   VAL A 144    11153  11425  13773    692   2768  -2133       C  
ATOM   1039  O   VAL A 144     572.691 -20.009 213.255  1.00 96.98           O  
ANISOU 1039  O   VAL A 144    11365  11704  13778    681   2967  -2378       O  
ATOM   1040  CB  VAL A 144     573.295 -22.616 211.545  1.00 93.17           C  
ANISOU 1040  CB  VAL A 144    10887  11387  13127    444   2724  -1688       C  
ATOM   1041  CG1 VAL A 144     573.261 -23.043 213.005  1.00 94.29           C  
ANISOU 1041  CG1 VAL A 144    11160  11733  12931    341   2941  -1829       C  
ATOM   1042  CG2 VAL A 144     572.881 -23.765 210.643  1.00 91.23           C  
ANISOU 1042  CG2 VAL A 144    10523  11218  12922    387   2684  -1443       C  
ATOM   1043  N   GLY A 145     573.745 -19.386 211.358  1.00148.48           N  
ANISOU 1043  N   GLY A 145    17904  17873  20639    745   2550  -2073       N  
ATOM   1044  CA  GLY A 145     574.419 -18.239 211.939  1.00149.90           C  
ANISOU 1044  CA  GLY A 145    18215  17886  20853    777   2510  -2291       C  
ATOM   1045  C   GLY A 145     573.662 -16.925 211.867  1.00150.61           C  
ANISOU 1045  C   GLY A 145    18180  17754  21292    975   2554  -2516       C  
ATOM   1046  O   GLY A 145     574.201 -15.886 212.244  1.00151.32           O  
ANISOU 1046  O   GLY A 145    18372  17654  21467   1008   2508  -2704       O  
ATOM   1047  N   GLU A 146     572.429 -16.956 211.362  1.00 95.06           N  
ANISOU 1047  N   GLU A 146    10913  10724  14480   1112   2628  -2503       N  
ATOM   1048  CA  GLU A 146     571.528 -15.811 211.515  1.00 96.20           C  
ANISOU 1048  CA  GLU A 146    10910  10698  14944   1323   2711  -2764       C  
ATOM   1049  C   GLU A 146     570.358 -16.201 212.424  1.00 96.74           C  
ANISOU 1049  C   GLU A 146    10815  11010  14930   1354   3008  -2995       C  
ATOM   1050  O   GLU A 146     569.895 -15.396 213.237  1.00 98.33           O  
ANISOU 1050  O   GLU A 146    10976  11169  15216   1461   3170  -3329       O  
ATOM   1051  CB  GLU A 146     570.999 -15.276 210.166  1.00 95.87           C  
ANISOU 1051  CB  GLU A 146    10706  10425  15297   1505   2535  -2594       C  
ATOM   1052  CG  GLU A 146     571.549 -15.917 208.913  1.00 94.54           C  
ANISOU 1052  CG  GLU A 146    10577  10244  15100   1427   2312  -2209       C  
ATOM   1053  CD  GLU A 146     572.116 -14.916 207.915  1.00 94.18           C  
ANISOU 1053  CD  GLU A 146    10609   9862  15312   1516   2079  -2059       C  
ATOM   1054  OE1 GLU A 146     571.497 -14.708 206.847  1.00 93.88           O  
ANISOU 1054  OE1 GLU A 146    10438   9717  15516   1663   1952  -1896       O  
ATOM   1055  OE2 GLU A 146     573.198 -14.357 208.190  1.00 94.21           O  
ANISOU 1055  OE2 GLU A 146    10811   9715  15271   1431   2018  -2095       O  
ATOM   1056  N   VAL A 147     569.895 -17.442 212.296  1.00 98.53           N  
ANISOU 1056  N   VAL A 147    10950  11490  14997   1249   3094  -2828       N  
ATOM   1057  CA  VAL A 147     568.795 -17.931 213.122  1.00 98.92           C  
ANISOU 1057  CA  VAL A 147    10838  11790  14959   1239   3401  -3013       C  
ATOM   1058  C   VAL A 147     569.148 -17.948 214.611  1.00100.10           C  
ANISOU 1058  C   VAL A 147    11178  12106  14751   1129   3619  -3255       C  
ATOM   1059  O   VAL A 147     568.344 -17.544 215.458  1.00101.35           O  
ANISOU 1059  O   VAL A 147    11230  12352  14925   1203   3876  -3564       O  
ATOM   1060  CB  VAL A 147     568.367 -19.353 212.705  1.00 97.42           C  
ANISOU 1060  CB  VAL A 147    10543  11823  14650   1103   3443  -2761       C  
ATOM   1061  CG1 VAL A 147     567.443 -19.971 213.749  1.00 97.86           C  
ANISOU 1061  CG1 VAL A 147    10488  12157  14536   1024   3797  -2935       C  
ATOM   1062  CG2 VAL A 147     567.687 -19.323 211.346  1.00 96.73           C  
ANISOU 1062  CG2 VAL A 147    10208  11624  14921   1236   3272  -2600       C  
ATOM   1063  N   SER A 148     570.354 -18.408 214.926  1.00112.75           N  
ANISOU 1063  N   SER A 148    13055  13762  16023    958   3510  -3123       N  
ATOM   1064  CA  SER A 148     570.736 -18.628 216.314  1.00113.87           C  
ANISOU 1064  CA  SER A 148    13403  14107  15756    835   3685  -3301       C  
ATOM   1065  C   SER A 148     570.943 -17.332 217.069  1.00115.76           C  
ANISOU 1065  C   SER A 148    13722  14217  16043    940   3723  -3672       C  
ATOM   1066  O   SER A 148     571.389 -16.345 216.487  1.00115.86           O  
ANISOU 1066  O   SER A 148    13742  13937  16343   1047   3521  -3709       O  
ATOM   1067  CB  SER A 148     572.009 -19.461 216.379  1.00113.27           C  
ANISOU 1067  CB  SER A 148    13586  14109  15343    648   3511  -3051       C  
ATOM   1068  OG  SER A 148     571.932 -20.539 215.466  1.00111.69           O  
ANISOU 1068  OG  SER A 148    13311  13955  15171    573   3423  -2708       O  
ATOM   1069  N   PRO A 149     570.609 -17.329 218.370  1.00128.78           N  
ANISOU 1069  N   PRO A 149    15439  16081  17410    903   3992  -3953       N  
ATOM   1070  CA  PRO A 149     570.997 -16.246 219.278  1.00130.72           C  
ANISOU 1070  CA  PRO A 149    15823  16251  17592    961   4025  -4330       C  
ATOM   1071  C   PRO A 149     572.508 -16.107 219.266  1.00130.82           C  
ANISOU 1071  C   PRO A 149    16100  16158  17449    855   3734  -4234       C  
ATOM   1072  O   PRO A 149     573.185 -17.133 219.224  1.00130.02           O  
ANISOU 1072  O   PRO A 149    16136  16206  17059    694   3633  -3953       O  
ATOM   1073  CB  PRO A 149     570.486 -16.722 220.643  1.00131.75           C  
ANISOU 1073  CB  PRO A 149    16025  16728  17306    876   4365  -4542       C  
ATOM   1074  CG  PRO A 149     570.272 -18.186 220.483  1.00130.39           C  
ANISOU 1074  CG  PRO A 149    15847  16794  16902    715   4439  -4193       C  
ATOM   1075  CD  PRO A 149     569.852 -18.376 219.069  1.00128.73           C  
ANISOU 1075  CD  PRO A 149    15395  16407  17109    789   4292  -3929       C  
ATOM   1076  N   THR A 150     573.021 -14.881 219.283  1.00205.09           N  
ANISOU 1076  N   THR A 150    25561  25299  27065    942   3599  -4465       N  
ATOM   1077  CA  THR A 150     574.447 -14.637 219.074  1.00205.10           C  
ANISOU 1077  CA  THR A 150    25757  25150  27021    845   3302  -4371       C  
ATOM   1078  C   THR A 150     575.332 -15.389 220.073  1.00205.95           C  
ANISOU 1078  C   THR A 150    26115  25539  26596    661   3278  -4365       C  
ATOM   1079  O   THR A 150     576.447 -15.801 219.736  1.00205.52           O  
ANISOU 1079  O   THR A 150    26182  25466  26440    544   3035  -4138       O  
ATOM   1080  CB  THR A 150     574.760 -13.133 219.144  1.00206.20           C  
ANISOU 1080  CB  THR A 150    25917  24962  27468    954   3211  -4690       C  
ATOM   1081  OG1 THR A 150     573.901 -12.430 218.238  1.00205.71           O  
ANISOU 1081  OG1 THR A 150    25633  24625  27902   1147   3223  -4680       O  
ATOM   1082  CG2 THR A 150     576.209 -12.863 218.764  1.00206.01           C  
ANISOU 1082  CG2 THR A 150    26049  24755  27470    839   2903  -4568       C  
ATOM   1083  N   ALA A 151     574.830 -15.579 221.290  1.00141.22           N  
ANISOU 1083  N   ALA A 151    17991  17612  18055    641   3529  -4610       N  
ATOM   1084  CA  ALA A 151     575.548 -16.355 222.299  1.00142.21           C  
ANISOU 1084  CA  ALA A 151    18368  18035  17631    480   3517  -4586       C  
ATOM   1085  C   ALA A 151     575.780 -17.788 221.821  1.00140.71           C  
ANISOU 1085  C   ALA A 151    18207  17999  17257    356   3447  -4130       C  
ATOM   1086  O   ALA A 151     576.921 -18.244 221.682  1.00140.56           O  
ANISOU 1086  O   ALA A 151    18334  17987  17086    254   3194  -3930       O  
ATOM   1087  CB  ALA A 151     574.780 -16.355 223.612  1.00143.82           C  
ANISOU 1087  CB  ALA A 151    18637  18518  17491    486   3846  -4900       C  
ATOM   1088  N   LEU A 152     574.678 -18.482 221.557  1.00129.30           N  
ANISOU 1088  N   LEU A 152    16604  16667  15856    369   3673  -3982       N  
ATOM   1089  CA  LEU A 152     574.705 -19.880 221.142  1.00127.80           C  
ANISOU 1089  CA  LEU A 152    16427  16617  15515    252   3652  -3576       C  
ATOM   1090  C   LEU A 152     575.119 -20.058 219.685  1.00126.05           C  
ANISOU 1090  C   LEU A 152    16085  16165  15643    269   3393  -3267       C  
ATOM   1091  O   LEU A 152     574.970 -21.139 219.129  1.00124.79           O  
ANISOU 1091  O   LEU A 152    15881  16075  15458    199   3383  -2952       O  
ATOM   1092  CB  LEU A 152     573.327 -20.514 221.357  1.00127.33           C  
ANISOU 1092  CB  LEU A 152    16217  16746  15419    244   3999  -3554       C  
ATOM   1093  CG  LEU A 152     572.621 -20.246 222.691  1.00129.21           C  
ANISOU 1093  CG  LEU A 152    16511  17215  15369    245   4338  -3888       C  
ATOM   1094  CD1 LEU A 152     571.211 -20.835 222.709  1.00128.70           C  
ANISOU 1094  CD1 LEU A 152    16232  17307  15364    233   4690  -3854       C  
ATOM   1095  CD2 LEU A 152     573.446 -20.790 223.847  1.00130.73           C  
ANISOU 1095  CD2 LEU A 152    17040  17651  14982    105   4318  -3873       C  
ATOM   1096  N   ARG A 153     575.629 -18.999 219.067  1.00133.38           N  
ANISOU 1096  N   ARG A 153    16968  16815  16895    357   3194  -3361       N  
ATOM   1097  CA  ARG A 153     576.011 -19.048 217.662  1.00131.79           C  
ANISOU 1097  CA  ARG A 153    16662  16395  17019    378   2966  -3082       C  
ATOM   1098  C   ARG A 153     577.347 -19.737 217.474  1.00131.52           C  
ANISOU 1098  C   ARG A 153    16791  16393  16787    246   2719  -2842       C  
ATOM   1099  O   ARG A 153     577.650 -20.254 216.397  1.00129.93           O  
ANISOU 1099  O   ARG A 153    16525  16110  16733    223   2572  -2549       O  
ATOM   1100  CB  ARG A 153     576.067 -17.645 217.068  1.00132.21           C  
ANISOU 1100  CB  ARG A 153    16622  16123  17490    511   2859  -3247       C  
ATOM   1101  CG  ARG A 153     574.804 -17.254 216.341  1.00131.18           C  
ANISOU 1101  CG  ARG A 153    16241  15868  17733    671   2975  -3258       C  
ATOM   1102  CD  ARG A 153     575.117 -16.344 215.172  1.00130.30           C  
ANISOU 1102  CD  ARG A 153    16056  15411  18041    769   2761  -3171       C  
ATOM   1103  NE  ARG A 153     575.440 -14.980 215.587  1.00131.59           N  
ANISOU 1103  NE  ARG A 153    16280  15342  18377    844   2725  -3480       N  
ATOM   1104  CZ  ARG A 153     576.061 -14.094 214.809  1.00131.51           C  
ANISOU 1104  CZ  ARG A 153    16285  15009  18672    881   2525  -3426       C  
ATOM   1105  NH1 ARG A 153     576.429 -14.441 213.576  1.00130.20           N  
ANISOU 1105  NH1 ARG A 153    16084  14746  18641    852   2351  -3073       N  
ATOM   1106  NH2 ARG A 153     576.317 -12.868 215.260  1.00132.73           N  
ANISOU 1106  NH2 ARG A 153    16499  14936  18997    938   2507  -3728       N  
ATOM   1107  N   GLY A 154     578.150 -19.737 218.529  1.00111.47           N  
ANISOU 1107  N   GLY A 154    14459  13981  13912    168   2669  -2982       N  
ATOM   1108  CA  GLY A 154     579.438 -20.396 218.481  1.00111.54           C  
ANISOU 1108  CA  GLY A 154    14613  14042  13726     56   2427  -2784       C  
ATOM   1109  C   GLY A 154     579.248 -21.894 218.562  1.00110.63           C  
ANISOU 1109  C   GLY A 154    14550  14145  13339    -26   2489  -2493       C  
ATOM   1110  O   GLY A 154     579.647 -22.636 217.664  1.00109.34           O  
ANISOU 1110  O   GLY A 154    14343  13933  13267    -63   2351  -2199       O  
ATOM   1111  N   ALA A 155     578.605 -22.326 219.643  1.00110.28           N  
ANISOU 1111  N   ALA A 155    14602  14333  12965    -58   2714  -2582       N  
ATOM   1112  CA  ALA A 155     578.392 -23.737 219.925  1.00109.67           C  
ANISOU 1112  CA  ALA A 155    14612  14461  12596   -154   2802  -2318       C  
ATOM   1113  C   ALA A 155     577.478 -24.420 218.906  1.00107.44           C  
ANISOU 1113  C   ALA A 155    14127  14125  12571   -149   2912  -2084       C  
ATOM   1114  O   ALA A 155     577.363 -25.640 218.904  1.00107.09           O  
ANISOU 1114  O   ALA A 155    14133  14192  12363   -237   2955  -1831       O  
ATOM   1115  CB  ALA A 155     577.824 -23.903 221.329  1.00111.27           C  
ANISOU 1115  CB  ALA A 155    14967  14919  12392   -195   3057  -2484       C  
ATOM   1116  N   LEU A 156     576.840 -23.644 218.036  1.00 90.77           N  
ANISOU 1116  N   LEU A 156    11790  11834  10865    -46   2942  -2168       N  
ATOM   1117  CA  LEU A 156     575.880 -24.202 217.081  1.00 88.95           C  
ANISOU 1117  CA  LEU A 156    11343  11566  10886    -29   3036  -1988       C  
ATOM   1118  C   LEU A 156     576.390 -24.274 215.645  1.00 87.52           C  
ANISOU 1118  C   LEU A 156    11061  11192  11002      0   2788  -1770       C  
ATOM   1119  O   LEU A 156     575.810 -24.969 214.822  1.00 86.01           O  
ANISOU 1119  O   LEU A 156    10729  10994  10958    -11   2811  -1582       O  
ATOM   1120  CB  LEU A 156     574.584 -23.391 217.100  1.00 89.24           C  
ANISOU 1120  CB  LEU A 156    11170  11573  11166     84   3264  -2226       C  
ATOM   1121  CG  LEU A 156     573.322 -23.965 217.747  1.00 89.18           C  
ANISOU 1121  CG  LEU A 156    11074  11771  11040     40   3605  -2280       C  
ATOM   1122  CD1 LEU A 156     573.576 -24.475 219.165  1.00 90.52           C  
ANISOU 1122  CD1 LEU A 156    11494  12181  10717    -79   3759  -2331       C  
ATOM   1123  CD2 LEU A 156     572.258 -22.887 217.750  1.00 89.98           C  
ANISOU 1123  CD2 LEU A 156    10952  11806  11431    190   3780  -2576       C  
ATOM   1124  N   GLY A 157     577.454 -23.546 215.329  1.00 91.79           N  
ANISOU 1124  N   GLY A 157    11666  11579  11633     28   2559  -1806       N  
ATOM   1125  CA  GLY A 157     578.059 -23.661 214.016  1.00 90.60           C  
ANISOU 1125  CA  GLY A 157    11445  11269  11710     36   2339  -1588       C  
ATOM   1126  C   GLY A 157     578.803 -24.975 214.041  1.00 90.07           C  
ANISOU 1126  C   GLY A 157    11498  11321  11401    -78   2240  -1347       C  
ATOM   1127  O   GLY A 157     579.157 -25.547 213.006  1.00 88.45           O  
ANISOU 1127  O   GLY A 157    11238  11054  11316    -95   2106  -1126       O  
ATOM   1128  N   THR A 158     579.033 -25.442 215.267  1.00116.45           N  
ANISOU 1128  N   THR A 158    15018  14839  14390   -147   2307  -1398       N  
ATOM   1129  CA  THR A 158     579.613 -26.748 215.558  1.00116.38           C  
ANISOU 1129  CA  THR A 158    15152  14956  14110   -244   2239  -1177       C  
ATOM   1130  C   THR A 158     578.926 -27.861 214.775  1.00113.92           C  
ANISOU 1130  C   THR A 158    14732  14652  13899   -281   2311   -936       C  
ATOM   1131  O   THR A 158     579.543 -28.844 214.381  1.00113.03           O  
ANISOU 1131  O   THR A 158    14673  14538  13734   -332   2180   -717       O  
ATOM   1132  CB  THR A 158     579.512 -27.059 217.066  1.00118.28           C  
ANISOU 1132  CB  THR A 158    15593  15404  13943   -301   2375  -1268       C  
ATOM   1133  OG1 THR A 158     580.041 -25.960 217.819  1.00120.59           O  
ANISOU 1133  OG1 THR A 158    15977  15699  14144   -264   2315  -1541       O  
ATOM   1134  CG2 THR A 158     580.263 -28.334 217.418  1.00118.49           C  
ANISOU 1134  CG2 THR A 158    15801  15533  13685   -383   2259  -1026       C  
ATOM   1135  N   LEU A 159     577.639 -27.695 214.534  1.00 86.55           N  
ANISOU 1135  N   LEU A 159    11096  11187  10600   -250   2513   -997       N  
ATOM   1136  CA  LEU A 159     576.883 -28.740 213.888  1.00 84.38           C  
ANISOU 1136  CA  LEU A 159    10704  10933  10422   -300   2595   -807       C  
ATOM   1137  C   LEU A 159     577.217 -28.911 212.389  1.00 82.45           C  
ANISOU 1137  C   LEU A 159    10333  10544  10451   -264   2393   -650       C  
ATOM   1138  O   LEU A 159     577.073 -30.022 211.867  1.00 80.81           O  
ANISOU 1138  O   LEU A 159    10096  10351  10259   -328   2380   -460       O  
ATOM   1139  CB  LEU A 159     575.384 -28.488 214.096  1.00 84.32           C  
ANISOU 1139  CB  LEU A 159    10519  10988  10530   -278   2871   -945       C  
ATOM   1140  CG  LEU A 159     574.936 -28.559 215.564  1.00 85.81           C  
ANISOU 1140  CG  LEU A 159    10833  11359  10412   -340   3126  -1077       C  
ATOM   1141  CD1 LEU A 159     573.454 -28.315 215.705  1.00 85.98           C  
ANISOU 1141  CD1 LEU A 159    10639  11448  10583   -319   3416  -1227       C  
ATOM   1142  CD2 LEU A 159     575.314 -29.896 216.206  1.00 85.54           C  
ANISOU 1142  CD2 LEU A 159    11009  11445  10048   -483   3156   -858       C  
ATOM   1143  N   HIS A 160     577.675 -27.863 211.698  1.00 87.08           N  
ANISOU 1143  N   HIS A 160    10858  10989  11241   -172   2243   -722       N  
ATOM   1144  CA  HIS A 160     578.001 -28.019 210.272  1.00 85.40           C  
ANISOU 1144  CA  HIS A 160    10544  10659  11246   -145   2068   -565       C  
ATOM   1145  C   HIS A 160     579.216 -28.896 210.139  1.00 85.11           C  
ANISOU 1145  C   HIS A 160    10641  10635  11061   -217   1903   -397       C  
ATOM   1146  O   HIS A 160     579.324 -29.682 209.208  1.00 83.34           O  
ANISOU 1146  O   HIS A 160    10362  10388  10916   -238   1823   -233       O  
ATOM   1147  CB  HIS A 160     578.264 -26.683 209.566  1.00 86.03           C  
ANISOU 1147  CB  HIS A 160    10552  10572  11564    -41   1954   -651       C  
ATOM   1148  CG  HIS A 160     578.683 -26.818 208.120  1.00 84.67           C  
ANISOU 1148  CG  HIS A 160    10308  10300  11565    -22   1782   -477       C  
ATOM   1149  ND1 HIS A 160     577.889 -27.407 207.158  1.00 82.77           N  
ANISOU 1149  ND1 HIS A 160     9924  10073  11453     -5   1789   -362       N  
ATOM   1150  CD2 HIS A 160     579.807 -26.413 207.475  1.00 85.11           C  
ANISOU 1150  CD2 HIS A 160    10411  10250  11677    -23   1609   -413       C  
ATOM   1151  CE1 HIS A 160     578.504 -27.363 205.985  1.00 82.00           C  
ANISOU 1151  CE1 HIS A 160     9808   9892  11456     11   1625   -233       C  
ATOM   1152  NE2 HIS A 160     579.670 -26.767 206.152  1.00 83.38           N  
ANISOU 1152  NE2 HIS A 160    10094   9994  11592     -3   1528   -254       N  
ATOM   1153  N   GLN A 161     580.146 -28.753 211.071  1.00120.08           N  
ANISOU 1153  N   GLN A 161    15239  15106  15280   -246   1842   -455       N  
ATOM   1154  CA  GLN A 161     581.341 -29.584 211.067  1.00120.45           C  
ANISOU 1154  CA  GLN A 161    15404  15173  15188   -297   1673   -312       C  
ATOM   1155  C   GLN A 161     580.949 -31.013 211.404  1.00119.39           C  
ANISOU 1155  C   GLN A 161    15336  15133  14893   -368   1755   -152       C  
ATOM   1156  O   GLN A 161     581.046 -31.915 210.567  1.00117.94           O  
ANISOU 1156  O   GLN A 161    15104  14911  14797   -390   1691     11       O  
ATOM   1157  CB  GLN A 161     582.354 -29.062 212.073  1.00123.38           C  
ANISOU 1157  CB  GLN A 161    15927  15581  15369   -304   1574   -434       C  
ATOM   1158  CG  GLN A 161     582.246 -27.570 212.317  1.00123.82           C  
ANISOU 1158  CG  GLN A 161    15947  15567  15532   -252   1602   -669       C  
ATOM   1159  CD  GLN A 161     582.867 -27.178 213.633  1.00126.90           C  
ANISOU 1159  CD  GLN A 161    16502  16045  15671   -273   1565   -837       C  
ATOM   1160  OE1 GLN A 161     583.426 -28.021 214.340  1.00128.11           O  
ANISOU 1160  OE1 GLN A 161    16799  16319  15557   -318   1498   -756       O  
ATOM   1161  NE2 GLN A 161     582.780 -25.895 213.974  1.00128.13           N  
ANISOU 1161  NE2 GLN A 161    16642  16134  15909   -234   1594  -1077       N  
ATOM   1162  N   LEU A 162     580.479 -31.188 212.635  1.00 75.09           N  
ANISOU 1162  N   LEU A 162     9844   9641   9048   -410   1910   -206       N  
ATOM   1163  CA  LEU A 162     580.014 -32.467 213.139  1.00 74.52           C  
ANISOU 1163  CA  LEU A 162     9861   9650   8803   -496   2028    -51       C  
ATOM   1164  C   LEU A 162     579.148 -33.179 212.131  1.00 71.86           C  
ANISOU 1164  C   LEU A 162     9358   9258   8689   -526   2104     62       C  
ATOM   1165  O   LEU A 162     579.224 -34.400 211.996  1.00 70.90           O  
ANISOU 1165  O   LEU A 162     9289   9123   8525   -593   2088    243       O  
ATOM   1166  CB  LEU A 162     579.234 -32.268 214.431  1.00 75.90           C  
ANISOU 1166  CB  LEU A 162    10129   9963   8747   -537   2264   -162       C  
ATOM   1167  CG  LEU A 162     580.067 -32.023 215.686  1.00 78.65           C  
ANISOU 1167  CG  LEU A 162    10711  10414   8757   -538   2197   -231       C  
ATOM   1168  CD1 LEU A 162     579.153 -31.667 216.837  1.00 80.04           C  
ANISOU 1168  CD1 LEU A 162    10953  10738   8721   -572   2466   -381       C  
ATOM   1169  CD2 LEU A 162     580.899 -33.251 216.025  1.00 78.84           C  
ANISOU 1169  CD2 LEU A 162    10929  10464   8564   -586   2056      1       C  
ATOM   1170  N   GLY A 163     578.333 -32.403 211.425  1.00 77.37           N  
ANISOU 1170  N   GLY A 163     9852   9913   9633   -472   2170    -51       N  
ATOM   1171  CA  GLY A 163     577.399 -32.952 210.462  1.00 75.10           C  
ANISOU 1171  CA  GLY A 163     9377   9591   9566   -493   2230     18       C  
ATOM   1172  C   GLY A 163     578.133 -33.691 209.370  1.00 73.29           C  
ANISOU 1172  C   GLY A 163     9137   9275   9434   -495   2030    174       C  
ATOM   1173  O   GLY A 163     577.701 -34.742 208.881  1.00 71.79           O  
ANISOU 1173  O   GLY A 163     8894   9071   9314   -560   2056    286       O  
ATOM   1174  N   ILE A 164     579.281 -33.140 209.011  1.00 80.16           N  
ANISOU 1174  N   ILE A 164    10058  10088  10312   -432   1838    165       N  
ATOM   1175  CA  ILE A 164     580.069 -33.669 207.918  1.00 78.50           C  
ANISOU 1175  CA  ILE A 164     9823   9806  10199   -421   1656    281       C  
ATOM   1176  C   ILE A 164     580.808 -34.930 208.351  1.00 78.55           C  
ANISOU 1176  C   ILE A 164     9983   9820  10044   -479   1592    422       C  
ATOM   1177  O   ILE A 164     580.719 -35.985 207.716  1.00 77.00           O  
ANISOU 1177  O   ILE A 164     9756   9583   9918   -515   1565    533       O  
ATOM   1178  CB  ILE A 164     581.053 -32.610 207.418  1.00 79.23           C  
ANISOU 1178  CB  ILE A 164     9904   9837  10364   -348   1500    221       C  
ATOM   1179  CG1 ILE A 164     580.282 -31.492 206.705  1.00 79.10           C  
ANISOU 1179  CG1 ILE A 164     9733   9769  10553   -278   1538    129       C  
ATOM   1180  CG2 ILE A 164     582.100 -33.238 206.510  1.00 77.85           C  
ANISOU 1180  CG2 ILE A 164     9732   9616  10231   -347   1330    333       C  
ATOM   1181  CD1 ILE A 164     581.067 -30.217 206.498  1.00 80.60           C  
ANISOU 1181  CD1 ILE A 164     9933   9878  10814   -220   1437     51       C  
ATOM   1182  N   VAL A 165     581.513 -34.826 209.465  1.00 68.21           N  
ANISOU 1182  N   VAL A 165     8841   8558   8518   -483   1561    409       N  
ATOM   1183  CA  VAL A 165     582.276 -35.948 209.976  1.00 68.90           C  
ANISOU 1183  CA  VAL A 165     9091   8647   8442   -514   1472    552       C  
ATOM   1184  C   VAL A 165     581.427 -37.193 210.314  1.00 68.10           C  
ANISOU 1184  C   VAL A 165     9048   8545   8283   -606   1619    688       C  
ATOM   1185  O   VAL A 165     581.822 -38.338 210.042  1.00 67.46           O  
ANISOU 1185  O   VAL A 165     9022   8392   8217   -627   1538    833       O  
ATOM   1186  CB  VAL A 165     583.038 -35.514 211.202  1.00 72.00           C  
ANISOU 1186  CB  VAL A 165     9655   9114   8588   -496   1409    500       C  
ATOM   1187  CG1 VAL A 165     583.983 -36.583 211.572  1.00 72.79           C  
ANISOU 1187  CG1 VAL A 165     9906   9201   8550   -494   1258    652       C  
ATOM   1188  CG2 VAL A 165     583.802 -34.265 210.886  1.00 73.39           C  
ANISOU 1188  CG2 VAL A 165     9760   9272   8853   -431   1283    350       C  
ATOM   1189  N   VAL A 166     580.280 -36.949 210.938  1.00 76.77           N  
ANISOU 1189  N   VAL A 166    10130   9715   9326   -663   1844    632       N  
ATOM   1190  CA  VAL A 166     579.306 -37.992 211.202  1.00 76.23           C  
ANISOU 1190  CA  VAL A 166    10076   9644   9243   -777   2029    743       C  
ATOM   1191  C   VAL A 166     578.777 -38.502 209.882  1.00 74.00           C  
ANISOU 1191  C   VAL A 166     9598   9272   9247   -796   2012    765       C  
ATOM   1192  O   VAL A 166     578.671 -39.706 209.664  1.00 73.57           O  
ANISOU 1192  O   VAL A 166     9577   9141   9237   -870   2016    900       O  
ATOM   1193  CB  VAL A 166     578.147 -37.483 212.056  1.00 77.19           C  
ANISOU 1193  CB  VAL A 166    10172   9879   9277   -834   2298    641       C  
ATOM   1194  CG1 VAL A 166     576.949 -38.395 211.922  1.00 76.40           C  
ANISOU 1194  CG1 VAL A 166     9979   9764   9284   -961   2506    717       C  
ATOM   1195  CG2 VAL A 166     578.589 -37.357 213.498  1.00 79.82           C  
ANISOU 1195  CG2 VAL A 166    10750  10316   9260   -848   2341    653       C  
ATOM   1196  N   GLY A 167     578.457 -37.567 208.997  1.00 77.28           N  
ANISOU 1196  N   GLY A 167     9818   9690   9855   -725   1981    631       N  
ATOM   1197  CA  GLY A 167     578.043 -37.906 207.650  1.00 75.43           C  
ANISOU 1197  CA  GLY A 167     9400   9393   9868   -722   1923    633       C  
ATOM   1198  C   GLY A 167     579.032 -38.856 207.005  1.00 74.64           C  
ANISOU 1198  C   GLY A 167     9369   9200   9790   -715   1742    747       C  
ATOM   1199  O   GLY A 167     578.651 -39.769 206.282  1.00 73.80           O  
ANISOU 1199  O   GLY A 167     9190   9032   9820   -767   1735    793       O  
ATOM   1200  N   ILE A 168     580.312 -38.642 207.279  1.00 83.87           N  
ANISOU 1200  N   ILE A 168    10669  10359  10838   -649   1592    773       N  
ATOM   1201  CA  ILE A 168     581.360 -39.512 206.759  1.00 83.60           C  
ANISOU 1201  CA  ILE A 168    10694  10241  10827   -623   1420    865       C  
ATOM   1202  C   ILE A 168     581.317 -40.906 207.380  1.00 84.56           C  
ANISOU 1202  C   ILE A 168    10961  10293  10872   -700   1457   1015       C  
ATOM   1203  O   ILE A 168     581.390 -41.923 206.679  1.00 84.01           O  
ANISOU 1203  O   ILE A 168    10867  10122  10929   -720   1403   1074       O  
ATOM   1204  CB  ILE A 168     582.744 -38.887 206.993  1.00 84.66           C  
ANISOU 1204  CB  ILE A 168    10905  10394  10866   -534   1253    840       C  
ATOM   1205  CG1 ILE A 168     583.146 -38.079 205.762  1.00 83.22           C  
ANISOU 1205  CG1 ILE A 168    10571  10206  10842   -467   1156    752       C  
ATOM   1206  CG2 ILE A 168     583.791 -39.953 207.318  1.00 85.87           C  
ANISOU 1206  CG2 ILE A 168    11199  10486  10940   -514   1116    959       C  
ATOM   1207  CD1 ILE A 168     583.748 -36.722 206.087  1.00 84.77           C  
ANISOU 1207  CD1 ILE A 168    10772  10446  10992   -415   1108    653       C  
ATOM   1208  N   LEU A 169     581.178 -40.946 208.699  1.00 80.79           N  
ANISOU 1208  N   LEU A 169    10648   9865  10185   -744   1555   1076       N  
ATOM   1209  CA  LEU A 169     581.240 -42.201 209.410  1.00 81.88           C  
ANISOU 1209  CA  LEU A 169    10969   9927  10216   -812   1582   1254       C  
ATOM   1210  C   LEU A 169     580.127 -43.114 208.943  1.00 81.01           C  
ANISOU 1210  C   LEU A 169    10771   9732  10277   -935   1732   1301       C  
ATOM   1211  O   LEU A 169     580.270 -44.334 208.964  1.00 81.62           O  
ANISOU 1211  O   LEU A 169    10949   9674  10388   -985   1707   1442       O  
ATOM   1212  CB  LEU A 169     581.144 -41.987 210.909  1.00 83.85           C  
ANISOU 1212  CB  LEU A 169    11416  10273  10171   -849   1688   1311       C  
ATOM   1213  CG  LEU A 169     581.319 -43.319 211.634  1.00 85.21           C  
ANISOU 1213  CG  LEU A 169    11813  10347  10213   -911   1693   1539       C  
ATOM   1214  CD1 LEU A 169     582.329 -43.184 212.728  1.00 87.46           C  
ANISOU 1214  CD1 LEU A 169    12329  10695  10205   -836   1556   1613       C  
ATOM   1215  CD2 LEU A 169     579.985 -43.798 212.190  1.00 85.39           C  
ANISOU 1215  CD2 LEU A 169    11865  10379  10199  -1078   1984   1613       C  
ATOM   1216  N   ILE A 170     579.022 -42.513 208.505  1.00 75.40           N  
ANISOU 1216  N   ILE A 170     9862   9089   9695   -979   1874   1174       N  
ATOM   1217  CA  ILE A 170     577.859 -43.271 208.043  1.00 75.00           C  
ANISOU 1217  CA  ILE A 170     9683   8980   9833  -1107   2018   1180       C  
ATOM   1218  C   ILE A 170     578.139 -43.875 206.670  1.00 74.07           C  
ANISOU 1218  C   ILE A 170     9450   8753   9941  -1076   1855   1150       C  
ATOM   1219  O   ILE A 170     577.875 -45.062 206.437  1.00 74.64           O  
ANISOU 1219  O   ILE A 170     9539   8693  10126  -1170   1876   1225       O  
ATOM   1220  CB  ILE A 170     576.579 -42.396 207.989  1.00 74.66           C  
ANISOU 1220  CB  ILE A 170     9430   9060   9876  -1145   2201   1031       C  
ATOM   1221  CG1 ILE A 170     576.100 -42.081 209.407  1.00 75.97           C  
ANISOU 1221  CG1 ILE A 170     9711   9330   9825  -1213   2425   1056       C  
ATOM   1222  CG2 ILE A 170     575.460 -43.106 207.232  1.00 74.48           C  
ANISOU 1222  CG2 ILE A 170     9210   8984  10104  -1260   2292    997       C  
ATOM   1223  CD1 ILE A 170     575.184 -40.873 209.495  1.00 76.14           C  
ANISOU 1223  CD1 ILE A 170     9544   9489   9895  -1183   2569    871       C  
ATOM   1224  N   ALA A 171     578.697 -43.065 205.777  1.00 84.55           N  
ANISOU 1224  N   ALA A 171    10671  10127  11325   -950   1699   1040       N  
ATOM   1225  CA  ALA A 171     579.100 -43.526 204.446  1.00 83.90           C  
ANISOU 1225  CA  ALA A 171    10495   9974  11411   -905   1541    995       C  
ATOM   1226  C   ALA A 171     579.975 -44.786 204.493  1.00 84.96           C  
ANISOU 1226  C   ALA A 171    10780   9955  11546   -905   1438   1108       C  
ATOM   1227  O   ALA A 171     579.827 -45.730 203.696  1.00 85.40           O  
ANISOU 1227  O   ALA A 171    10782   9902  11765   -943   1397   1092       O  
ATOM   1228  CB  ALA A 171     579.839 -42.417 203.737  1.00 82.87           C  
ANISOU 1228  CB  ALA A 171    10294   9922  11271   -770   1402    902       C  
ATOM   1229  N   GLN A 172     580.903 -44.761 205.443  1.00 72.70           N  
ANISOU 1229  N   GLN A 172     9413   8395   9813   -850   1383   1209       N  
ATOM   1230  CA  GLN A 172     581.805 -45.862 205.696  1.00 74.11           C  
ANISOU 1230  CA  GLN A 172     9753   8427   9976   -820   1269   1334       C  
ATOM   1231  C   GLN A 172     581.071 -47.082 206.248  1.00 75.21           C  
ANISOU 1231  C   GLN A 172    10003   8423  10151   -959   1396   1474       C  
ATOM   1232  O   GLN A 172     581.162 -48.160 205.675  1.00 75.90           O  
ANISOU 1232  O   GLN A 172    10092   8342  10403   -981   1342   1498       O  
ATOM   1233  CB  GLN A 172     582.898 -45.401 206.651  1.00 75.17           C  
ANISOU 1233  CB  GLN A 172    10047   8618   9896   -722   1163   1400       C  
ATOM   1234  CG  GLN A 172     583.734 -44.279 206.056  1.00 74.41           C  
ANISOU 1234  CG  GLN A 172     9836   8633   9803   -603   1034   1264       C  
ATOM   1235  CD  GLN A 172     584.747 -43.736 207.032  1.00 75.99           C  
ANISOU 1235  CD  GLN A 172    10165   8902   9807   -522    927   1296       C  
ATOM   1236  OE1 GLN A 172     584.519 -43.744 208.240  1.00 77.32           O  
ANISOU 1236  OE1 GLN A 172    10493   9105   9781   -562    992   1385       O  
ATOM   1237  NE2 GLN A 172     585.873 -43.258 206.514  1.00 76.20           N  
ANISOU 1237  NE2 GLN A 172    10119   8960   9874   -416    765   1216       N  
ATOM   1238  N   VAL A 173     580.328 -46.908 207.341  1.00 60.29           N  
ANISOU 1238  N   VAL A 173     8203   6592   8114  -1062   1580   1558       N  
ATOM   1239  CA  VAL A 173     579.536 -48.005 207.916  1.00 61.43           C  
ANISOU 1239  CA  VAL A 173     8451   6603   8286  -1226   1745   1707       C  
ATOM   1240  C   VAL A 173     578.542 -48.597 206.909  1.00 61.08           C  
ANISOU 1240  C   VAL A 173     8209   6471   8529  -1346   1825   1612       C  
ATOM   1241  O   VAL A 173     578.552 -49.797 206.657  1.00 62.13           O  
ANISOU 1241  O   VAL A 173     8399   6399   8810  -1411   1802   1687       O  
ATOM   1242  CB  VAL A 173     578.755 -47.571 209.166  1.00 62.22           C  
ANISOU 1242  CB  VAL A 173     8641   6826   8174  -1334   1978   1779       C  
ATOM   1243  CG1 VAL A 173     577.811 -48.692 209.591  1.00 65.06           C  
ANISOU 1243  CG1 VAL A 173     9069   7048   8602  -1537   2187   1924       C  
ATOM   1244  CG2 VAL A 173     579.716 -47.196 210.295  1.00 63.02           C  
ANISOU 1244  CG2 VAL A 173     8982   7002   7960  -1235   1892   1888       C  
ATOM   1245  N   PHE A 174     577.699 -47.756 206.310  1.00 75.73           N  
ANISOU 1245  N   PHE A 174     9827   8472  10475  -1366   1900   1436       N  
ATOM   1246  CA  PHE A 174     576.818 -48.216 205.230  1.00 75.69           C  
ANISOU 1246  CA  PHE A 174     9604   8413  10741  -1457   1924   1310       C  
ATOM   1247  C   PHE A 174     577.616 -48.897 204.135  1.00 76.00           C  
ANISOU 1247  C   PHE A 174     9632   8320  10923  -1374   1711   1257       C  
ATOM   1248  O   PHE A 174     577.061 -49.631 203.329  1.00 76.75           O  
ANISOU 1248  O   PHE A 174     9609   8317  11234  -1459   1707   1173       O  
ATOM   1249  CB  PHE A 174     576.033 -47.067 204.593  1.00 74.49           C  
ANISOU 1249  CB  PHE A 174     9194   8452  10656  -1426   1955   1120       C  
ATOM   1250  CG  PHE A 174     574.843 -46.618 205.381  1.00 74.62           C  
ANISOU 1250  CG  PHE A 174     9126   8578  10647  -1542   2201   1108       C  
ATOM   1251  CD1 PHE A 174     574.653 -47.039 206.689  1.00 75.61           C  
ANISOU 1251  CD1 PHE A 174     9433   8671  10624  -1658   2393   1269       C  
ATOM   1252  CD2 PHE A 174     573.914 -45.766 204.807  1.00 74.02           C  
ANISOU 1252  CD2 PHE A 174     8788   8644  10693  -1528   2242    935       C  
ATOM   1253  CE1 PHE A 174     573.562 -46.615 207.411  1.00 75.94           C  
ANISOU 1253  CE1 PHE A 174     9386   8834  10636  -1767   2647   1239       C  
ATOM   1254  CE2 PHE A 174     572.827 -45.337 205.519  1.00 74.40           C  
ANISOU 1254  CE2 PHE A 174     8729   8799  10741  -1619   2475    898       C  
ATOM   1255  CZ  PHE A 174     572.641 -45.763 206.825  1.00 75.33           C  
ANISOU 1255  CZ  PHE A 174     9017   8896  10708  -1746   2693   1041       C  
ATOM   1256  N   GLY A 175     578.914 -48.624 204.095  1.00 69.25           N  
ANISOU 1256  N   GLY A 175     8885   7474   9953  -1209   1538   1282       N  
ATOM   1257  CA  GLY A 175     579.758 -49.130 203.038  1.00 69.71           C  
ANISOU 1257  CA  GLY A 175     8915   7441  10132  -1109   1349   1203       C  
ATOM   1258  C   GLY A 175     580.092 -50.600 203.169  1.00 71.43           C  
ANISOU 1258  C   GLY A 175     9275   7403  10464  -1150   1311   1306       C  
ATOM   1259  O   GLY A 175     580.535 -51.212 202.198  1.00 72.17           O  
ANISOU 1259  O   GLY A 175     9317   7394  10710  -1095   1188   1205       O  
ATOM   1260  N   LEU A 176     579.879 -51.165 204.356  1.00 59.82           N  
ANISOU 1260  N   LEU A 176     7992   5821   8916  -1242   1421   1507       N  
ATOM   1261  CA  LEU A 176     580.225 -52.563 204.631  1.00 62.03           C  
ANISOU 1261  CA  LEU A 176     8449   5820   9299  -1275   1382   1651       C  
ATOM   1262  C   LEU A 176     579.747 -53.545 203.562  1.00 62.79           C  
ANISOU 1262  C   LEU A 176     8426   5736   9695  -1361   1369   1520       C  
ATOM   1263  O   LEU A 176     578.607 -53.449 203.092  1.00 62.97           O  
ANISOU 1263  O   LEU A 176     8270   5815   9841  -1504   1488   1401       O  
ATOM   1264  CB  LEU A 176     579.646 -52.993 205.981  1.00 64.72           C  
ANISOU 1264  CB  LEU A 176     8988   6081   9523  -1424   1565   1890       C  
ATOM   1265  CG  LEU A 176     580.316 -52.444 207.239  1.00 65.06           C  
ANISOU 1265  CG  LEU A 176     9243   6231   9248  -1336   1546   2065       C  
ATOM   1266  CD1 LEU A 176     579.492 -52.786 208.474  1.00 67.97           C  
ANISOU 1266  CD1 LEU A 176     9785   6565   9477  -1518   1778   2279       C  
ATOM   1267  CD2 LEU A 176     581.746 -52.948 207.370  1.00 65.29           C  
ANISOU 1267  CD2 LEU A 176     9439   6127   9241  -1148   1302   2162       C  
ATOM   1268  N   ASP A 177     580.627 -54.479 203.192  1.00126.80           N  
ANISOU 1268  N   ASP A 177    16623  13630  17927  -1265   1216   1527       N  
ATOM   1269  CA  ASP A 177     580.300 -55.634 202.343  1.00128.26           C  
ANISOU 1269  CA  ASP A 177    16751  13579  18403  -1344   1194   1417       C  
ATOM   1270  C   ASP A 177     578.912 -56.183 202.670  1.00128.80           C  
ANISOU 1270  C   ASP A 177    16795  13539  18605  -1606   1402   1469       C  
ATOM   1271  O   ASP A 177     578.140 -56.538 201.784  1.00129.30           O  
ANISOU 1271  O   ASP A 177    16681  13563  18885  -1721   1428   1282       O  
ATOM   1272  CB  ASP A 177     581.366 -56.728 202.533  1.00130.01           C  
ANISOU 1272  CB  ASP A 177    17167  13512  18717  -1227   1051   1525       C  
ATOM   1273  CG  ASP A 177     581.317 -57.823 201.465  1.00131.42           C  
ANISOU 1273  CG  ASP A 177    17274  13453  19206  -1250    983   1345       C  
ATOM   1274  OD1 ASP A 177     580.214 -58.209 201.023  1.00131.63           O  
ANISOU 1274  OD1 ASP A 177    17188  13419  19408  -1443   1093   1240       O  
ATOM   1275  OD2 ASP A 177     582.407 -58.312 201.082  1.00132.47           O  
ANISOU 1275  OD2 ASP A 177    17456  13460  19418  -1070    816   1292       O  
ATOM   1276  N   SER A 178     578.605 -56.209 203.962  1.00 83.23           N  
ANISOU 1276  N   SER A 178    11197   7740  12689  -1704   1552   1718       N  
ATOM   1277  CA  SER A 178     577.376 -56.781 204.493  1.00 84.10           C  
ANISOU 1277  CA  SER A 178    11316   7733  12904  -1970   1787   1818       C  
ATOM   1278  C   SER A 178     576.182 -55.822 204.561  1.00 82.75           C  
ANISOU 1278  C   SER A 178    10929   7835  12678  -2102   1979   1717       C  
ATOM   1279  O   SER A 178     575.079 -56.230 204.940  1.00 83.44           O  
ANISOU 1279  O   SER A 178    10971   7858  12875  -2336   2196   1766       O  
ATOM   1280  CB  SER A 178     577.647 -57.335 205.891  1.00 85.19           C  
ANISOU 1280  CB  SER A 178    11774   7706  12888  -2016   1874   2160       C  
ATOM   1281  OG  SER A 178     578.836 -56.784 206.442  1.00 84.28           O  
ANISOU 1281  OG  SER A 178    11822   7697  12504  -1789   1717   2268       O  
ATOM   1282  N   ILE A 179     576.383 -54.552 204.221  1.00 77.28           N  
ANISOU 1282  N   ILE A 179    10096   7434  11831  -1956   1908   1578       N  
ATOM   1283  CA  ILE A 179     575.244 -53.632 204.137  1.00 76.18           C  
ANISOU 1283  CA  ILE A 179     9721   7537  11686  -2049   2061   1449       C  
ATOM   1284  C   ILE A 179     574.948 -53.318 202.664  1.00 75.80           C  
ANISOU 1284  C   ILE A 179     9395   7589  11816  -1998   1925   1164       C  
ATOM   1285  O   ILE A 179     574.127 -53.996 202.021  1.00 76.82           O  
ANISOU 1285  O   ILE A 179     9369   7622  12197  -2147   1955   1038       O  
ATOM   1286  CB  ILE A 179     575.475 -52.325 204.941  1.00 74.64           C  
ANISOU 1286  CB  ILE A 179     9572   7599  11190  -1941   2111   1506       C  
ATOM   1287  CG1 ILE A 179     575.612 -52.635 206.440  1.00 75.41           C  
ANISOU 1287  CG1 ILE A 179     9947   7630  11075  -2012   2262   1780       C  
ATOM   1288  CG2 ILE A 179     574.342 -51.350 204.714  1.00 73.75           C  
ANISOU 1288  CG2 ILE A 179     9191   7718  11112  -1999   2241   1341       C  
ATOM   1289  CD1 ILE A 179     575.096 -51.566 207.377  1.00 75.08           C  
ANISOU 1289  CD1 ILE A 179     9894   7833  10801  -2037   2449   1803       C  
ATOM   1290  N   MET A 180     575.634 -52.328 202.107  1.00 78.90           N  
ANISOU 1290  N   MET A 180     9732   8169  12077  -1796   1767   1062       N  
ATOM   1291  CA  MET A 180     575.354 -51.947 200.736  1.00 78.81           C  
ANISOU 1291  CA  MET A 180     9483   8278  12183  -1741   1639    817       C  
ATOM   1292  C   MET A 180     576.627 -51.909 199.885  1.00 78.91           C  
ANISOU 1292  C   MET A 180     9552   8286  12145  -1543   1416    744       C  
ATOM   1293  O   MET A 180     576.576 -51.550 198.710  1.00 79.12           O  
ANISOU 1293  O   MET A 180     9418   8429  12214  -1475   1297    556       O  
ATOM   1294  CB  MET A 180     574.618 -50.597 200.712  1.00 77.42           C  
ANISOU 1294  CB  MET A 180     9119   8373  11925  -1712   1702    734       C  
ATOM   1295  CG  MET A 180     573.103 -50.674 200.986  1.00 78.02           C  
ANISOU 1295  CG  MET A 180     9004   8487  12152  -1910   1896    685       C  
ATOM   1296  SD  MET A 180     572.305 -49.076 201.293  1.00 76.54           S  
ANISOU 1296  SD  MET A 180     8627   8591  11864  -1850   1998    619       S  
ATOM   1297  CE  MET A 180     570.603 -49.438 200.852  1.00 77.86           C  
ANISOU 1297  CE  MET A 180     8463   8791  12329  -2050   2111    450       C  
ATOM   1298  N   GLY A 181     577.755 -52.300 200.473  1.00141.99           N  
ANISOU 1298  N   GLY A 181    17762  16147  20039  -1451   1359    892       N  
ATOM   1299  CA  GLY A 181     579.017 -52.335 199.753  1.00142.30           C  
ANISOU 1299  CA  GLY A 181    17842  16176  20051  -1268   1169    821       C  
ATOM   1300  C   GLY A 181     579.299 -53.666 199.081  1.00144.24           C  
ANISOU 1300  C   GLY A 181    18116  16181  20508  -1283   1084    738       C  
ATOM   1301  O   GLY A 181     580.286 -54.334 199.399  1.00145.05           O  
ANISOU 1301  O   GLY A 181    18382  16109  20621  -1193   1007    828       O  
ATOM   1302  N   ASN A 182     578.440 -54.041 198.137  1.00 62.69           N  
ANISOU 1302  N   ASN A 182     7621   5844  10355  -1388   1085    548       N  
ATOM   1303  CA  ASN A 182     578.506 -55.360 197.515  1.00 64.71           C  
ANISOU 1303  CA  ASN A 182     7892   5850  10842  -1436   1022    435       C  
ATOM   1304  C   ASN A 182     577.896 -55.374 196.107  1.00 65.66           C  
ANISOU 1304  C   ASN A 182     7797   6077  11075  -1471    946    146       C  
ATOM   1305  O   ASN A 182     577.060 -54.540 195.802  1.00 64.74           O  
ANISOU 1305  O   ASN A 182     7512   6182  10904  -1516    974     73       O  
ATOM   1306  CB  ASN A 182     577.803 -56.360 198.414  1.00 65.49           C  
ANISOU 1306  CB  ASN A 182     8094   5686  11103  -1636   1163    587       C  
ATOM   1307  CG  ASN A 182     576.389 -55.943 198.754  1.00 65.86           C  
ANISOU 1307  CG  ASN A 182     7996   5852  11178  -1833   1334    595       C  
ATOM   1308  OD1 ASN A 182     575.551 -55.811 197.874  1.00 66.00           O  
ANISOU 1308  OD1 ASN A 182     7792   5976  11310  -1909   1315    383       O  
ATOM   1309  ND2 ASN A 182     576.116 -55.745 200.036  1.00 66.58           N  
ANISOU 1309  ND2 ASN A 182     8203   5935  11159  -1913   1499    830       N  
ATOM   1310  N   LYS A 183     578.294 -56.327 195.266  1.00111.33           N  
ANISOU 1310  N   LYS A 183    13587  11701  17014  -1444    842    -26       N  
ATOM   1311  CA  LYS A 183     577.948 -56.339 193.832  1.00112.64           C  
ANISOU 1311  CA  LYS A 183    13574  11991  17231  -1441    735   -326       C  
ATOM   1312  C   LYS A 183     576.482 -56.008 193.508  1.00112.62           C  
ANISOU 1312  C   LYS A 183    13363  12131  17296  -1606    776   -434       C  
ATOM   1313  O   LYS A 183     576.174 -55.492 192.430  1.00113.25           O  
ANISOU 1313  O   LYS A 183    13287  12433  17310  -1564    673   -632       O  
ATOM   1314  CB  LYS A 183     578.298 -57.707 193.221  1.00114.79           C  
ANISOU 1314  CB  LYS A 183    13895  11993  17727  -1453    660   -500       C  
ATOM   1315  CG  LYS A 183     578.305 -57.726 191.691  1.00116.05           C  
ANISOU 1315  CG  LYS A 183    13916  12302  17876  -1397    527   -829       C  
ATOM   1316  CD  LYS A 183     579.192 -56.594 191.136  1.00115.64           C  
ANISOU 1316  CD  LYS A 183    13848  12552  17536  -1191    459   -843       C  
ATOM   1317  CE  LYS A 183     578.684 -56.058 189.787  1.00116.51           C  
ANISOU 1317  CE  LYS A 183    13791  12942  17534  -1180    362  -1088       C  
ATOM   1318  NZ  LYS A 183     577.371 -55.332 189.883  1.00116.07           N  
ANISOU 1318  NZ  LYS A 183    13584  13059  17459  -1301    386  -1057       N  
ATOM   1319  N   ASP A 184     575.585 -56.280 194.449  1.00 94.07           N  
ANISOU 1319  N   ASP A 184    11006   9667  15069  -1791    926   -299       N  
ATOM   1320  CA  ASP A 184     574.158 -56.144 194.193  1.00 94.37           C  
ANISOU 1320  CA  ASP A 184    10816   9806  15235  -1967    974   -420       C  
ATOM   1321  C   ASP A 184     573.558 -54.830 194.680  1.00 92.75           C  
ANISOU 1321  C   ASP A 184    10500   9869  14872  -1949   1058   -318       C  
ATOM   1322  O   ASP A 184     572.708 -54.262 194.000  1.00 93.11           O  
ANISOU 1322  O   ASP A 184    10323  10119  14935  -1967   1001   -475       O  
ATOM   1323  CB  ASP A 184     573.401 -57.315 194.829  1.00 95.20           C  
ANISOU 1323  CB  ASP A 184    10936   9614  15620  -2216   1113   -373       C  
ATOM   1324  CG  ASP A 184     573.307 -58.523 193.904  1.00 97.20           C  
ANISOU 1324  CG  ASP A 184    11149   9655  16127  -2300   1006   -620       C  
ATOM   1325  OD1 ASP A 184     572.877 -58.366 192.735  1.00 98.28           O  
ANISOU 1325  OD1 ASP A 184    11094   9959  16291  -2291    866   -898       O  
ATOM   1326  OD2 ASP A 184     573.663 -59.636 194.346  1.00 97.80           O  
ANISOU 1326  OD2 ASP A 184    11394   9390  16374  -2373   1053   -539       O  
ATOM   1327  N   LEU A 185     573.993 -54.360 195.850  1.00 79.27           N  
ANISOU 1327  N   LEU A 185     8948   8156  13015  -1904   1180    -67       N  
ATOM   1328  CA  LEU A 185     573.361 -53.222 196.530  1.00 77.67           C  
ANISOU 1328  CA  LEU A 185     8658   8162  12692  -1910   1299     32       C  
ATOM   1329  C   LEU A 185     574.213 -51.943 196.640  1.00 75.95           C  
ANISOU 1329  C   LEU A 185     8514   8145  12200  -1693   1241    116       C  
ATOM   1330  O   LEU A 185     574.032 -51.153 197.572  1.00 74.39           O  
ANISOU 1330  O   LEU A 185     8341   8041  11881  -1685   1364    253       O  
ATOM   1331  CB  LEU A 185     572.921 -53.635 197.940  1.00 77.25           C  
ANISOU 1331  CB  LEU A 185     8707   7963  12682  -2077   1532    243       C  
ATOM   1332  CG  LEU A 185     571.564 -54.335 198.041  1.00 78.41           C  
ANISOU 1332  CG  LEU A 185     8680   8019  13094  -2337   1673    171       C  
ATOM   1333  CD1 LEU A 185     571.247 -54.677 199.486  1.00 78.02           C  
ANISOU 1333  CD1 LEU A 185     8768   7841  13036  -2500   1932    414       C  
ATOM   1334  CD2 LEU A 185     570.449 -53.502 197.426  1.00 78.68           C  
ANISOU 1334  CD2 LEU A 185     8394   8310  13190  -2355   1653    -20       C  
ATOM   1335  N   TRP A 186     575.117 -51.712 195.696  1.00 73.89           N  
ANISOU 1335  N   TRP A 186     8281   7953  11842  -1528   1067     24       N  
ATOM   1336  CA  TRP A 186     575.837 -50.443 195.704  1.00 72.37           C  
ANISOU 1336  CA  TRP A 186     8128   7950  11418  -1348   1019     88       C  
ATOM   1337  C   TRP A 186     575.096 -49.317 194.957  1.00 72.16           C  
ANISOU 1337  C   TRP A 186     7900   8170  11345  -1296    959    -22       C  
ATOM   1338  O   TRP A 186     575.452 -48.152 195.116  1.00 70.41           O  
ANISOU 1338  O   TRP A 186     7699   8090  10963  -1175    952     48       O  
ATOM   1339  CB  TRP A 186     577.271 -50.609 195.144  1.00 73.00           C  
ANISOU 1339  CB  TRP A 186     8338   7999  11401  -1193    889     69       C  
ATOM   1340  CG  TRP A 186     577.413 -50.963 193.668  1.00 75.13           C  
ANISOU 1340  CG  TRP A 186     8520   8317  11709  -1147    741   -151       C  
ATOM   1341  CD1 TRP A 186     577.716 -52.192 193.146  1.00 76.87           C  
ANISOU 1341  CD1 TRP A 186     8778   8363  12066  -1178    684   -274       C  
ATOM   1342  CD2 TRP A 186     577.287 -50.073 192.539  1.00 75.95           C  
ANISOU 1342  CD2 TRP A 186     8504   8658  11697  -1057    634   -273       C  
ATOM   1343  NE1 TRP A 186     577.770 -52.125 191.773  1.00 78.65           N  
ANISOU 1343  NE1 TRP A 186     8909   8723  12252  -1118    556   -485       N  
ATOM   1344  CE2 TRP A 186     577.509 -50.837 191.377  1.00 78.29           C  
ANISOU 1344  CE2 TRP A 186     8773   8935  12039  -1045    521   -474       C  
ATOM   1345  CE3 TRP A 186     576.982 -48.711 192.400  1.00 75.05           C  
ANISOU 1345  CE3 TRP A 186     8311   8758  11446   -984    620   -230       C  
ATOM   1346  CZ2 TRP A 186     577.448 -50.286 190.096  1.00 79.96           C  
ANISOU 1346  CZ2 TRP A 186     8895   9360  12127   -967    398   -619       C  
ATOM   1347  CZ3 TRP A 186     576.920 -48.168 191.122  1.00 76.77           C  
ANISOU 1347  CZ3 TRP A 186     8443   9163  11566   -902    490   -354       C  
ATOM   1348  CH2 TRP A 186     577.154 -48.953 189.992  1.00 79.32           C  
ANISOU 1348  CH2 TRP A 186     8753   9486  11900   -897    381   -539       C  
ATOM   1349  N   PRO A 187     574.095 -49.644 194.114  1.00 67.50           N  
ANISOU 1349  N   PRO A 187     7119   7626  10903  -1378    899   -199       N  
ATOM   1350  CA  PRO A 187     573.384 -48.435 193.699  1.00 67.14           C  
ANISOU 1350  CA  PRO A 187     6901   7809  10801  -1307    850   -248       C  
ATOM   1351  C   PRO A 187     572.429 -47.867 194.770  1.00 65.66           C  
ANISOU 1351  C   PRO A 187     6616   7661  10671  -1380   1022   -165       C  
ATOM   1352  O   PRO A 187     572.173 -46.655 194.765  1.00 64.86           O  
ANISOU 1352  O   PRO A 187     6437   7720  10488  -1272   1007   -147       O  
ATOM   1353  CB  PRO A 187     572.627 -48.901 192.448  1.00 69.32           C  
ANISOU 1353  CB  PRO A 187     6991   8148  11198  -1353    701   -473       C  
ATOM   1354  CG  PRO A 187     573.503 -49.941 191.879  1.00 70.80           C  
ANISOU 1354  CG  PRO A 187     7311   8203  11389  -1354    624   -549       C  
ATOM   1355  CD  PRO A 187     573.989 -50.694 193.086  1.00 69.84           C  
ANISOU 1355  CD  PRO A 187     7361   7844  11332  -1436    782   -392       C  
ATOM   1356  N   LEU A 188     571.905 -48.697 195.668  1.00108.48           N  
ANISOU 1356  N   LEU A 188    12044  12938  16235  -1557   1191   -115       N  
ATOM   1357  CA  LEU A 188     571.056 -48.156 196.722  1.00107.40           C  
ANISOU 1357  CA  LEU A 188    11822  12857  16128  -1629   1387    -42       C  
ATOM   1358  C   LEU A 188     571.939 -47.459 197.755  1.00105.42           C  
ANISOU 1358  C   LEU A 188    11787  12610  15657  -1530   1477    144       C  
ATOM   1359  O   LEU A 188     571.484 -46.590 198.492  1.00104.41           O  
ANISOU 1359  O   LEU A 188    11609  12584  15478  -1511   1602    186       O  
ATOM   1360  CB  LEU A 188     570.194 -49.249 197.353  1.00108.27           C  
ANISOU 1360  CB  LEU A 188    11872  12820  16446  -1872   1566    -39       C  
ATOM   1361  CG  LEU A 188     568.716 -49.203 196.953  1.00109.46           C  
ANISOU 1361  CG  LEU A 188    11690  13074  16825  -1985   1591   -215       C  
ATOM   1362  CD1 LEU A 188     568.527 -48.935 195.451  1.00110.69           C  
ANISOU 1362  CD1 LEU A 188    11673  13362  17022  -1875   1321   -418       C  
ATOM   1363  CD2 LEU A 188     568.018 -50.504 197.355  1.00110.31           C  
ANISOU 1363  CD2 LEU A 188    11746  12996  17172  -2254   1747   -230       C  
ATOM   1364  N   LEU A 189     573.215 -47.825 197.779  1.00 78.61           N  
ANISOU 1364  N   LEU A 189     8618   9111  12139  -1458   1403    233       N  
ATOM   1365  CA  LEU A 189     574.191 -47.169 198.649  1.00 76.90           C  
ANISOU 1365  CA  LEU A 189     8600   8908  11711  -1351   1441    387       C  
ATOM   1366  C   LEU A 189     574.509 -45.769 198.168  1.00 75.79           C  
ANISOU 1366  C   LEU A 189     8408   8943  11447  -1177   1340    348       C  
ATOM   1367  O   LEU A 189     574.612 -44.838 198.972  1.00 74.40           O  
ANISOU 1367  O   LEU A 189     8279   8836  11154  -1122   1420    418       O  
ATOM   1368  CB  LEU A 189     575.493 -47.977 198.724  1.00 77.24           C  
ANISOU 1368  CB  LEU A 189     8866   8794  11687  -1309   1362    474       C  
ATOM   1369  CG  LEU A 189     576.623 -47.421 199.601  1.00 75.68           C  
ANISOU 1369  CG  LEU A 189     8870   8606  11281  -1198   1364    620       C  
ATOM   1370  CD1 LEU A 189     576.236 -47.416 201.083  1.00 75.24           C  
ANISOU 1370  CD1 LEU A 189     8919   8523  11145  -1292   1555    766       C  
ATOM   1371  CD2 LEU A 189     577.904 -48.213 199.385  1.00 76.29           C  
ANISOU 1371  CD2 LEU A 189     9106   8545  11338  -1126   1240    662       C  
ATOM   1372  N   LEU A 190     574.689 -45.640 196.853  1.00 61.33           N  
ANISOU 1372  N   LEU A 190     6494   7176   9635  -1095   1166    236       N  
ATOM   1373  CA  LEU A 190     574.965 -44.346 196.233  1.00 60.77           C  
ANISOU 1373  CA  LEU A 190     6380   7253   9456   -938   1061    214       C  
ATOM   1374  C   LEU A 190     573.696 -43.475 196.177  1.00 60.95           C  
ANISOU 1374  C   LEU A 190     6196   7402   9563   -928   1092    149       C  
ATOM   1375  O   LEU A 190     573.781 -42.249 196.150  1.00 60.21           O  
ANISOU 1375  O   LEU A 190     6087   7397   9393   -807   1065    173       O  
ATOM   1376  CB  LEU A 190     575.572 -44.517 194.824  1.00 62.33           C  
ANISOU 1376  CB  LEU A 190     6576   7492   9616   -859    877    130       C  
ATOM   1377  CG  LEU A 190     577.065 -44.912 194.719  1.00 62.23           C  
ANISOU 1377  CG  LEU A 190     6746   7405   9495   -799    827    180       C  
ATOM   1378  CD1 LEU A 190     577.668 -44.561 193.394  1.00 63.77           C  
ANISOU 1378  CD1 LEU A 190     6929   7703   9598   -694    685    108       C  
ATOM   1379  CD2 LEU A 190     577.898 -44.301 195.799  1.00 60.02           C  
ANISOU 1379  CD2 LEU A 190     6608   7098   9098   -748    899    319       C  
ATOM   1380  N   SER A 191     572.531 -44.113 196.228  1.00 75.42           N  
ANISOU 1380  N   SER A 191     7863   9224  11571  -1057   1157     67       N  
ATOM   1381  CA  SER A 191     571.261 -43.410 196.120  1.00 76.19           C  
ANISOU 1381  CA  SER A 191     7719   9442  11789  -1045   1176    -22       C  
ATOM   1382  C   SER A 191     570.580 -43.022 197.431  1.00 75.25           C  
ANISOU 1382  C   SER A 191     7550   9331  11711  -1106   1405     18       C  
ATOM   1383  O   SER A 191     569.863 -42.037 197.455  1.00 75.53           O  
ANISOU 1383  O   SER A 191     7425   9473  11799  -1025   1418    -37       O  
ATOM   1384  CB  SER A 191     570.290 -44.262 195.311  1.00 78.36           C  
ANISOU 1384  CB  SER A 191     7785   9730  12259  -1153   1101   -175       C  
ATOM   1385  OG  SER A 191     570.420 -43.977 193.935  1.00 78.42           O  
ANISOU 1385  OG  SER A 191     7737   9836  12225  -1036    864   -262       O  
ATOM   1386  N   ILE A 192     570.787 -43.774 198.513  1.00 64.78           N  
ANISOU 1386  N   ILE A 192     6363   7895  10355  -1241   1587    112       N  
ATOM   1387  CA  ILE A 192     570.005 -43.595 199.748  1.00 64.54           C  
ANISOU 1387  CA  ILE A 192     6278   7887  10356  -1336   1839    135       C  
ATOM   1388  C   ILE A 192     570.076 -42.152 200.286  1.00 63.57           C  
ANISOU 1388  C   ILE A 192     6163   7870  10120  -1186   1885    142       C  
ATOM   1389  O   ILE A 192     569.429 -41.826 201.284  1.00 63.62           O  
ANISOU 1389  O   ILE A 192     6116   7923  10135  -1237   2098    132       O  
ATOM   1390  CB  ILE A 192     570.455 -44.594 200.863  1.00 64.32           C  
ANISOU 1390  CB  ILE A 192     6477   7720  10242  -1489   2014    284       C  
ATOM   1391  CG1 ILE A 192     569.341 -44.847 201.888  1.00 65.05           C  
ANISOU 1391  CG1 ILE A 192     6465   7831  10421  -1663   2297    286       C  
ATOM   1392  CG2 ILE A 192     571.655 -44.079 201.579  1.00 62.96           C  
ANISOU 1392  CG2 ILE A 192     6570   7533   9820  -1381   2006    415       C  
ATOM   1393  CD1 ILE A 192     568.719 -46.243 201.830  1.00 66.49           C  
ANISOU 1393  CD1 ILE A 192     6584   7886  10795  -1892   2388    285       C  
ATOM   1394  N   ILE A 193     570.854 -41.299 199.613  1.00 70.06           N  
ANISOU 1394  N   ILE A 193     7051   8723  10844  -1009   1697    150       N  
ATOM   1395  CA  ILE A 193     570.792 -39.836 199.755  1.00 69.70           C  
ANISOU 1395  CA  ILE A 193     6966   8759  10760   -849   1686    121       C  
ATOM   1396  C   ILE A 193     569.367 -39.280 199.851  1.00 70.98           C  
ANISOU 1396  C   ILE A 193     6845   9015  11108   -835   1776     -7       C  
ATOM   1397  O   ILE A 193     569.081 -38.441 200.698  1.00 71.03           O  
ANISOU 1397  O   ILE A 193     6833   9061  11095   -785   1918    -34       O  
ATOM   1398  CB  ILE A 193     571.499 -39.128 198.551  1.00 69.62           C  
ANISOU 1398  CB  ILE A 193     6988   8767  10698   -683   1439    130       C  
ATOM   1399  CG1 ILE A 193     572.960 -38.833 198.857  1.00 68.10           C  
ANISOU 1399  CG1 ILE A 193     7055   8514  10306   -627   1402    239       C  
ATOM   1400  CG2 ILE A 193     570.810 -37.832 198.185  1.00 70.49           C  
ANISOU 1400  CG2 ILE A 193     6931   8953  10898   -532   1379     60       C  
ATOM   1401  CD1 ILE A 193     573.875 -40.018 198.663  1.00 67.90           C  
ANISOU 1401  CD1 ILE A 193     7183   8409  10207   -706   1351    305       C  
ATOM   1402  N   PHE A 194     568.486 -39.750 198.970  1.00 68.85           N  
ANISOU 1402  N   PHE A 194     6346   8788  11027   -874   1686   -104       N  
ATOM   1403  CA  PHE A 194     567.097 -39.286 198.902  1.00 70.22           C  
ANISOU 1403  CA  PHE A 194     6202   9062  11418   -849   1733   -246       C  
ATOM   1404  C   PHE A 194     566.367 -39.371 200.241  1.00 70.23           C  
ANISOU 1404  C   PHE A 194     6126   9086  11473   -971   2048   -281       C  
ATOM   1405  O   PHE A 194     565.557 -38.508 200.543  1.00 71.02           O  
ANISOU 1405  O   PHE A 194     6031   9267  11685   -885   2131   -384       O  
ATOM   1406  CB  PHE A 194     566.313 -40.071 197.836  1.00 71.70           C  
ANISOU 1406  CB  PHE A 194     6158   9287  11796   -920   1588   -355       C  
ATOM   1407  CG  PHE A 194     565.915 -41.462 198.266  1.00 71.89           C  
ANISOU 1407  CG  PHE A 194     6146   9249  11919  -1172   1750   -371       C  
ATOM   1408  CD1 PHE A 194     566.827 -42.507 198.235  1.00 71.31           C  
ANISOU 1408  CD1 PHE A 194     6312   9049  11734  -1281   1733   -271       C  
ATOM   1409  CD2 PHE A 194     564.621 -41.721 198.700  1.00 72.84           C  
ANISOU 1409  CD2 PHE A 194     5983   9427  12267  -1301   1926   -488       C  
ATOM   1410  CE1 PHE A 194     566.450 -43.768 198.641  1.00 71.76           C  
ANISOU 1410  CE1 PHE A 194     6349   9014  11901  -1514   1883   -272       C  
ATOM   1411  CE2 PHE A 194     564.236 -42.980 199.102  1.00 73.23           C  
ANISOU 1411  CE2 PHE A 194     6001   9401  12424  -1554   2094   -491       C  
ATOM   1412  CZ  PHE A 194     565.141 -44.002 199.075  1.00 72.73           C  
ANISOU 1412  CZ  PHE A 194     6200   9188  12248  -1661   2069   -375       C  
ATOM   1413  N   ILE A 195     566.652 -40.396 201.045  1.00 83.06           N  
ANISOU 1413  N   ILE A 195     7908  10637  13013  -1164   2230   -192       N  
ATOM   1414  CA  ILE A 195     565.992 -40.528 202.349  1.00 83.36           C  
ANISOU 1414  CA  ILE A 195     7906  10709  13060  -1299   2557   -204       C  
ATOM   1415  C   ILE A 195     566.357 -39.341 203.274  1.00 82.85           C  
ANISOU 1415  C   ILE A 195     7966  10692  12822  -1165   2666   -196       C  
ATOM   1416  O   ILE A 195     565.466 -38.738 203.880  1.00 83.82           O  
ANISOU 1416  O   ILE A 195     7907  10908  13033  -1150   2856   -312       O  
ATOM   1417  CB  ILE A 195     566.314 -41.875 203.024  1.00 83.21           C  
ANISOU 1417  CB  ILE A 195     8080  10581  12955  -1530   2716    -68       C  
ATOM   1418  CG1 ILE A 195     565.440 -42.970 202.414  1.00 84.34           C  
ANISOU 1418  CG1 ILE A 195     8001  10689  13354  -1711   2719   -141       C  
ATOM   1419  CG2 ILE A 195     566.095 -41.769 204.519  1.00 83.43           C  
ANISOU 1419  CG2 ILE A 195     8205  10648  12847  -1627   3043    -17       C  
ATOM   1420  CD1 ILE A 195     565.623 -44.368 203.033  1.00 84.71           C  
ANISOU 1420  CD1 ILE A 195     8223  10591  13373  -1958   2885     -3       C  
ATOM   1421  N   PRO A 196     567.657 -38.977 203.369  1.00 86.12           N  
ANISOU 1421  N   PRO A 196     8672  11043  13006  -1065   2546    -83       N  
ATOM   1422  CA  PRO A 196     567.928 -37.662 203.970  1.00 86.05           C  
ANISOU 1422  CA  PRO A 196     8730  11076  12890   -909   2587   -126       C  
ATOM   1423  C   PRO A 196     567.235 -36.489 203.260  1.00 86.99           C  
ANISOU 1423  C   PRO A 196     8597  11248  13205   -718   2472   -269       C  
ATOM   1424  O   PRO A 196     566.589 -35.663 203.912  1.00 87.86           O  
ANISOU 1424  O   PRO A 196     8589  11421  13374   -652   2628   -388       O  
ATOM   1425  CB  PRO A 196     569.448 -37.532 203.842  1.00 84.77           C  
ANISOU 1425  CB  PRO A 196     8870  10829  12509   -836   2411      4       C  
ATOM   1426  CG  PRO A 196     569.937 -38.910 203.900  1.00 84.23           C  
ANISOU 1426  CG  PRO A 196     8953  10687  12363   -995   2414    133       C  
ATOM   1427  CD  PRO A 196     568.881 -39.800 203.316  1.00 85.21           C  
ANISOU 1427  CD  PRO A 196     8845  10817  12713  -1121   2445     78       C  
ATOM   1428  N   ALA A 197     567.364 -36.442 201.936  1.00 91.98           N  
ANISOU 1428  N   ALA A 197     9158  11857  13934   -627   2202   -259       N  
ATOM   1429  CA  ALA A 197     566.961 -35.279 201.148  1.00 92.96           C  
ANISOU 1429  CA  ALA A 197     9114  12006  14202   -416   2031   -340       C  
ATOM   1430  C   ALA A 197     565.480 -34.987 201.263  1.00 94.45           C  
ANISOU 1430  C   ALA A 197     8954  12287  14647   -389   2138   -510       C  
ATOM   1431  O   ALA A 197     565.088 -33.875 201.616  1.00 95.39           O  
ANISOU 1431  O   ALA A 197     8979  12421  14845   -239   2190   -605       O  
ATOM   1432  CB  ALA A 197     567.338 -35.472 199.692  1.00 93.04           C  
ANISOU 1432  CB  ALA A 197     9128  11994  14229   -352   1731   -281       C  
ATOM   1433  N   LEU A 198     564.663 -35.988 200.961  1.00 91.61           N  
ANISOU 1433  N   LEU A 198     8389  11981  14438   -534   2170   -563       N  
ATOM   1434  CA  LEU A 198     563.222 -35.848 201.039  1.00 93.05           C  
ANISOU 1434  CA  LEU A 198     8195  12265  14894   -532   2275   -739       C  
ATOM   1435  C   LEU A 198     562.811 -35.473 202.440  1.00 93.27           C  
ANISOU 1435  C   LEU A 198     8196  12338  14905   -575   2617   -818       C  
ATOM   1436  O   LEU A 198     561.813 -34.790 202.630  1.00 94.57           O  
ANISOU 1436  O   LEU A 198     8077  12579  15275   -477   2705   -983       O  
ATOM   1437  CB  LEU A 198     562.530 -37.137 200.620  1.00 93.51           C  
ANISOU 1437  CB  LEU A 198     8062  12361  15107   -736   2284   -781       C  
ATOM   1438  CG  LEU A 198     561.003 -37.242 200.678  1.00 95.16           C  
ANISOU 1438  CG  LEU A 198     7839  12686  15633   -789   2403   -977       C  
ATOM   1439  CD1 LEU A 198     560.530 -38.174 199.570  1.00 95.83           C  
ANISOU 1439  CD1 LEU A 198     7731  12792  15887   -887   2197  -1029       C  
ATOM   1440  CD2 LEU A 198     560.531 -37.782 202.022  1.00 95.09           C  
ANISOU 1440  CD2 LEU A 198     7797  12708  15625  -1011   2815  -1006       C  
ATOM   1441  N   LEU A 199     563.571 -35.925 203.430  1.00 80.13           N  
ANISOU 1441  N   LEU A 199     6824  10634  12990   -714   2808   -708       N  
ATOM   1442  CA  LEU A 199     563.250 -35.560 204.801  1.00 80.61           C  
ANISOU 1442  CA  LEU A 199     6898  10755  12974   -757   3140   -781       C  
ATOM   1443  C   LEU A 199     563.368 -34.061 204.952  1.00 81.03           C  
ANISOU 1443  C   LEU A 199     6952  10802  13035   -509   3089   -881       C  
ATOM   1444  O   LEU A 199     562.448 -33.411 205.411  1.00 82.18           O  
ANISOU 1444  O   LEU A 199     6862  11024  13337   -435   3257  -1059       O  
ATOM   1445  CB  LEU A 199     564.155 -36.270 205.807  1.00 79.78           C  
ANISOU 1445  CB  LEU A 199     7150  10610  12553   -929   3309   -623       C  
ATOM   1446  CG  LEU A 199     563.966 -35.832 207.265  1.00 80.52           C  
ANISOU 1446  CG  LEU A 199     7319  10785  12489   -965   3641   -691       C  
ATOM   1447  CD1 LEU A 199     562.502 -35.802 207.673  1.00 81.87           C  
ANISOU 1447  CD1 LEU A 199     7133  11086  12887  -1031   3922   -877       C  
ATOM   1448  CD2 LEU A 199     564.753 -36.746 208.184  1.00 80.15           C  
ANISOU 1448  CD2 LEU A 199     7615  10708  12128  -1155   3785   -508       C  
ATOM   1449  N   GLN A 200     564.500 -33.512 204.544  1.00 84.92           N  
ANISOU 1449  N   GLN A 200     7695  11191  13377   -381   2862   -775       N  
ATOM   1450  CA  GLN A 200     564.686 -32.069 204.604  1.00 85.49           C  
ANISOU 1450  CA  GLN A 200     7787  11216  13479   -150   2790   -858       C  
ATOM   1451  C   GLN A 200     563.676 -31.407 203.693  1.00 86.79           C  
ANISOU 1451  C   GLN A 200     7615  11396  13966     33   2637   -978       C  
ATOM   1452  O   GLN A 200     563.105 -30.376 204.027  1.00 88.03           O  
ANISOU 1452  O   GLN A 200     7624  11556  14269    195   2707  -1133       O  
ATOM   1453  CB  GLN A 200     566.123 -31.679 204.221  1.00 84.49           C  
ANISOU 1453  CB  GLN A 200     7981  10966  13156    -76   2565   -707       C  
ATOM   1454  CG  GLN A 200     566.261 -30.590 203.173  1.00 85.22           C  
ANISOU 1454  CG  GLN A 200     8024  10967  13388    153   2291   -703       C  
ATOM   1455  CD  GLN A 200     567.568 -29.842 203.318  1.00 84.73           C  
ANISOU 1455  CD  GLN A 200     8263  10786  13146    222   2196   -619       C  
ATOM   1456  OE1 GLN A 200     567.932 -29.440 204.422  1.00 84.78           O  
ANISOU 1456  OE1 GLN A 200     8409  10781  13021    203   2363   -684       O  
ATOM   1457  NE2 GLN A 200     568.291 -29.660 202.209  1.00 84.48           N  
ANISOU 1457  NE2 GLN A 200     8329  10671  13097    291   1932   -482       N  
ATOM   1458  N   CYS A 201     563.409 -32.051 202.566  1.00 82.75           N  
ANISOU 1458  N   CYS A 201     6972  10900  13568      7   2428   -920       N  
ATOM   1459  CA  CYS A 201     562.487 -31.531 201.567  1.00 84.19           C  
ANISOU 1459  CA  CYS A 201     6843  11110  14037    185   2223  -1012       C  
ATOM   1460  C   CYS A 201     561.056 -31.456 202.083  1.00 85.49           C  
ANISOU 1460  C   CYS A 201     6622  11391  14471    186   2434  -1230       C  
ATOM   1461  O   CYS A 201     560.135 -31.082 201.353  1.00 86.80           O  
ANISOU 1461  O   CYS A 201     6471  11600  14910    333   2276  -1335       O  
ATOM   1462  CB  CYS A 201     562.540 -32.402 200.323  1.00 84.06           C  
ANISOU 1462  CB  CYS A 201     6787  11112  14040    122   1966   -918       C  
ATOM   1463  SG  CYS A 201     562.464 -31.515 198.784  1.00 85.33           S  
ANISOU 1463  SG  CYS A 201     6866  11237  14320    394   1549   -876       S  
ATOM   1464  N   ILE A 202     560.885 -31.823 203.348  1.00 96.79           N  
ANISOU 1464  N   ILE A 202     8079  12883  15815     20   2792  -1296       N  
ATOM   1465  CA  ILE A 202     559.596 -31.824 204.023  1.00 98.02           C  
ANISOU 1465  CA  ILE A 202     7885  13165  16192    -20   3072  -1508       C  
ATOM   1466  C   ILE A 202     559.673 -30.952 205.254  1.00 98.43           C  
ANISOU 1466  C   ILE A 202     8028  13221  16148     51   3344  -1624       C  
ATOM   1467  O   ILE A 202     558.785 -30.144 205.509  1.00 99.66           O  
ANISOU 1467  O   ILE A 202     7905  13425  16536    206   3445  -1835       O  
ATOM   1468  CB  ILE A 202     559.183 -33.237 204.449  1.00 97.70           C  
ANISOU 1468  CB  ILE A 202     7773  13216  16131   -337   3311  -1488       C  
ATOM   1469  CG1 ILE A 202     558.700 -34.041 203.243  1.00 98.17           C  
ANISOU 1469  CG1 ILE A 202     7610  13296  16392   -400   3070  -1471       C  
ATOM   1470  CG2 ILE A 202     558.123 -33.179 205.535  1.00 98.81           C  
ANISOU 1470  CG2 ILE A 202     7653  13490  16398   -420   3713  -1686       C  
ATOM   1471  CD1 ILE A 202     558.440 -35.486 203.567  1.00 97.13           C  
ANISOU 1471  CD1 ILE A 202     7453  13203  16247   -727   3274  -1428       C  
ATOM   1472  N   VAL A 203     560.746 -31.131 206.020  1.00 92.43           N  
ANISOU 1472  N   VAL A 203     7656  12415  15046    -57   3454  -1501       N  
ATOM   1473  CA  VAL A 203     560.971 -30.344 207.227  1.00 92.88           C  
ANISOU 1473  CA  VAL A 203     7856  12483  14951     -5   3695  -1613       C  
ATOM   1474  C   VAL A 203     561.021 -28.846 206.907  1.00 93.71           C  
ANISOU 1474  C   VAL A 203     7918  12478  15211    303   3519  -1729       C  
ATOM   1475  O   VAL A 203     560.469 -28.018 207.641  1.00 94.91           O  
ANISOU 1475  O   VAL A 203     7942  12662  15458    418   3718  -1947       O  
ATOM   1476  CB  VAL A 203     562.287 -30.743 207.940  1.00 91.70           C  
ANISOU 1476  CB  VAL A 203     8160  12290  14392   -146   3746  -1440       C  
ATOM   1477  CG1 VAL A 203     562.417 -30.001 209.250  1.00 92.53           C  
ANISOU 1477  CG1 VAL A 203     8397  12438  14322   -111   4008  -1587       C  
ATOM   1478  CG2 VAL A 203     562.329 -32.221 208.206  1.00 90.98           C  
ANISOU 1478  CG2 VAL A 203     8152  12262  14153   -432   3885  -1290       C  
ATOM   1479  N   LEU A 204     561.671 -28.521 205.789  1.00 94.20           N  
ANISOU 1479  N   LEU A 204     8088  12404  15302    432   3154  -1582       N  
ATOM   1480  CA  LEU A 204     562.030 -27.145 205.440  1.00 94.87           C  
ANISOU 1480  CA  LEU A 204     8236  12331  15479    697   2957  -1618       C  
ATOM   1481  C   LEU A 204     560.837 -26.189 205.258  1.00 96.51           C  
ANISOU 1481  C   LEU A 204     8078  12532  16058    941   2952  -1837       C  
ATOM   1482  O   LEU A 204     560.882 -25.073 205.772  1.00 97.41           O  
ANISOU 1482  O   LEU A 204     8227  12553  16233   1111   3012  -1978       O  
ATOM   1483  CB  LEU A 204     562.906 -27.143 204.178  1.00 94.09           C  
ANISOU 1483  CB  LEU A 204     8315  12107  15329    753   2583  -1386       C  
ATOM   1484  CG  LEU A 204     564.286 -26.505 204.325  1.00 93.65           C  
ANISOU 1484  CG  LEU A 204     8632  11896  15054    789   2485  -1274       C  
ATOM   1485  CD1 LEU A 204     564.827 -26.773 205.711  1.00 93.48           C  
ANISOU 1485  CD1 LEU A 204     8826  11930  14761    628   2763  -1327       C  
ATOM   1486  CD2 LEU A 204     565.248 -27.026 203.278  1.00 92.47           C  
ANISOU 1486  CD2 LEU A 204     8679  11690  14765    729   2216  -1026       C  
ATOM   1487  N   PRO A 205     559.769 -26.597 204.537  1.00 82.62           N  
ANISOU 1487  N   PRO A 205     5958  10867  14567    968   2869  -1884       N  
ATOM   1488  CA  PRO A 205     558.703 -25.593 204.477  1.00 86.06           C  
ANISOU 1488  CA  PRO A 205     6050  11287  15361   1229   2864  -2106       C  
ATOM   1489  C   PRO A 205     558.074 -25.290 205.834  1.00 89.05           C  
ANISOU 1489  C   PRO A 205     6289  11762  15784   1211   3274  -2377       C  
ATOM   1490  O   PRO A 205     557.322 -24.334 205.930  1.00 91.99           O  
ANISOU 1490  O   PRO A 205     6411  12098  16444   1448   3295  -2588       O  
ATOM   1491  CB  PRO A 205     557.692 -26.221 203.517  1.00 87.48           C  
ANISOU 1491  CB  PRO A 205     5856  11581  15801   1232   2701  -2117       C  
ATOM   1492  CG  PRO A 205     558.523 -27.065 202.608  1.00 84.10           C  
ANISOU 1492  CG  PRO A 205     5664  11129  15160   1091   2451  -1850       C  
ATOM   1493  CD  PRO A 205     559.560 -27.665 203.535  1.00 81.63           C  
ANISOU 1493  CD  PRO A 205     5724  10815  14478    847   2682  -1748       C  
ATOM   1494  N   PHE A 206     558.401 -26.053 206.868  1.00122.95           N  
ANISOU 1494  N   PHE A 206    10756  16169  19789    949   3590  -2371       N  
ATOM   1495  CA  PHE A 206     557.950 -25.721 208.218  1.00123.91           C  
ANISOU 1495  CA  PHE A 206    10815  16393  19873    923   3997  -2619       C  
ATOM   1496  C   PHE A 206     558.945 -24.813 208.938  1.00123.97           C  
ANISOU 1496  C   PHE A 206    11183  16271  19649   1007   4029  -2652       C  
ATOM   1497  O   PHE A 206     558.737 -24.438 210.095  1.00124.72           O  
ANISOU 1497  O   PHE A 206    11291  16442  19657    999   4349  -2867       O  
ATOM   1498  CB  PHE A 206     557.719 -26.990 209.041  1.00123.58           C  
ANISOU 1498  CB  PHE A 206    10782  16553  19621    591   4347  -2595       C  
ATOM   1499  CG  PHE A 206     556.796 -27.978 208.385  1.00123.34           C  
ANISOU 1499  CG  PHE A 206    10408  16638  19818    461   4332  -2567       C  
ATOM   1500  CD1 PHE A 206     555.490 -27.617 208.074  1.00125.30           C  
ANISOU 1500  CD1 PHE A 206    10285  16945  20377    596   4264  -2730       C  
ATOM   1501  CD2 PHE A 206     557.214 -29.279 208.126  1.00121.79           C  
ANISOU 1501  CD2 PHE A 206    10366  16472  19437    191   4299  -2337       C  
ATOM   1502  CE1 PHE A 206     554.633 -28.515 207.479  1.00125.92           C  
ANISOU 1502  CE1 PHE A 206    10105  17123  20617    465   4187  -2693       C  
ATOM   1503  CE2 PHE A 206     556.358 -30.188 207.537  1.00121.80           C  
ANISOU 1503  CE2 PHE A 206    10063  16564  19652     56   4273  -2330       C  
ATOM   1504  CZ  PHE A 206     555.065 -29.805 207.212  1.00123.91           C  
ANISOU 1504  CZ  PHE A 206     9961  16896  20222    190   4193  -2500       C  
ATOM   1505  N   CYS A 207     560.023 -24.464 208.240  1.00122.47           N  
ANISOU 1505  N   CYS A 207    11279  15893  19359   1081   3700  -2450       N  
ATOM   1506  CA  CYS A 207     561.121 -23.695 208.821  1.00122.42           C  
ANISOU 1506  CA  CYS A 207    11634  15750  19129   1125   3688  -2454       C  
ATOM   1507  C   CYS A 207     561.110 -22.238 208.362  1.00123.52           C  
ANISOU 1507  C   CYS A 207    11728  15661  19542   1436   3481  -2557       C  
ATOM   1508  O   CYS A 207     560.667 -21.937 207.253  1.00123.88           O  
ANISOU 1508  O   CYS A 207    11580  15614  19874   1609   3217  -2489       O  
ATOM   1509  CB  CYS A 207     562.458 -24.347 208.465  1.00120.83           C  
ANISOU 1509  CB  CYS A 207    11804  15493  18614    960   3495  -2157       C  
ATOM   1510  SG  CYS A 207     562.649 -26.031 209.093  1.00119.53           S  
ANISOU 1510  SG  CYS A 207    11765  15540  18111    605   3722  -2012       S  
ATOM   1511  N   PRO A 208     561.609 -21.330 209.219  1.00129.65           N  
ANISOU 1511  N   PRO A 208    12697  16338  20226   1507   3591  -2719       N  
ATOM   1512  CA  PRO A 208     561.516 -19.881 208.989  1.00130.87           C  
ANISOU 1512  CA  PRO A 208    12805  16250  20669   1800   3453  -2865       C  
ATOM   1513  C   PRO A 208     562.550 -19.286 208.026  1.00130.43           C  
ANISOU 1513  C   PRO A 208    12998  15929  20631   1890   3083  -2629       C  
ATOM   1514  O   PRO A 208     563.722 -19.630 208.099  1.00129.48           O  
ANISOU 1514  O   PRO A 208    13201  15787  20211   1721   3017  -2455       O  
ATOM   1515  CB  PRO A 208     561.715 -19.301 210.395  1.00131.88           C  
ANISOU 1515  CB  PRO A 208    13069  16398  20641   1788   3749  -3149       C  
ATOM   1516  CG  PRO A 208     562.566 -20.304 211.096  1.00130.80           C  
ANISOU 1516  CG  PRO A 208    13228  16430  20040   1488   3884  -3020       C  
ATOM   1517  CD  PRO A 208     562.170 -21.645 210.549  1.00129.56           C  
ANISOU 1517  CD  PRO A 208    12937  16452  19840   1313   3878  -2806       C  
ATOM   1518  N   GLU A 209     562.105 -18.389 207.147  1.00127.06           N  
ANISOU 1518  N   GLU A 209    12415  15303  20560   2156   2850  -2623       N  
ATOM   1519  CA  GLU A 209     563.010 -17.618 206.299  1.00127.03           C  
ANISOU 1519  CA  GLU A 209    12645  15015  20604   2260   2534  -2418       C  
ATOM   1520  C   GLU A 209     563.857 -16.693 207.175  1.00127.72           C  
ANISOU 1520  C   GLU A 209    13002  14923  20604   2268   2626  -2568       C  
ATOM   1521  O   GLU A 209     563.336 -16.056 208.092  1.00128.93           O  
ANISOU 1521  O   GLU A 209    13053  15059  20874   2373   2840  -2884       O  
ATOM   1522  CB  GLU A 209     562.230 -16.819 205.243  1.00127.96           C  
ANISOU 1522  CB  GLU A 209    12536  14955  21129   2562   2277  -2382       C  
ATOM   1523  CG  GLU A 209     561.560 -17.687 204.181  1.00128.25           C  
ANISOU 1523  CG  GLU A 209    12343  15153  21234   2556   2102  -2203       C  
ATOM   1524  CD  GLU A 209     560.841 -16.879 203.121  1.00128.85           C  
ANISOU 1524  CD  GLU A 209    12216  15057  21682   2869   1807  -2148       C  
ATOM   1525  OE1 GLU A 209     559.609 -17.045 202.965  1.00129.41           O  
ANISOU 1525  OE1 GLU A 209    11906  15257  22008   2996   1817  -2286       O  
ATOM   1526  OE2 GLU A 209     561.507 -16.075 202.439  1.00128.84           O  
ANISOU 1526  OE2 GLU A 209    12435  14793  21724   2986   1561  -1961       O  
ATOM   1527  N   SER A 210     565.157 -16.635 206.888  1.00112.66           N  
ANISOU 1527  N   SER A 210    11422  12889  18495   2151   2467  -2359       N  
ATOM   1528  CA  SER A 210     566.119 -15.959 207.757  1.00113.17           C  
ANISOU 1528  CA  SER A 210    11759  12819  18422   2094   2546  -2492       C  
ATOM   1529  C   SER A 210     565.734 -14.521 208.092  1.00114.90           C  
ANISOU 1529  C   SER A 210    11918  12774  18965   2341   2569  -2757       C  
ATOM   1530  O   SER A 210     565.361 -13.755 207.206  1.00115.56           O  
ANISOU 1530  O   SER A 210    11903  12623  19381   2563   2364  -2679       O  
ATOM   1531  CB  SER A 210     567.506 -15.978 207.115  1.00112.33           C  
ANISOU 1531  CB  SER A 210    11954  12575  18151   1969   2318  -2207       C  
ATOM   1532  OG  SER A 210     568.454 -15.312 207.935  1.00112.98           O  
ANISOU 1532  OG  SER A 210    12279  12526  18123   1906   2373  -2349       O  
ATOM   1533  N   PRO A 211     565.811 -14.163 209.385  1.00132.60           N  
ANISOU 1533  N   PRO A 211    14226  15053  21104   2309   2815  -3077       N  
ATOM   1534  CA  PRO A 211     565.494 -12.815 209.878  1.00134.29           C  
ANISOU 1534  CA  PRO A 211    14398  15016  21607   2530   2874  -3392       C  
ATOM   1535  C   PRO A 211     566.436 -11.736 209.326  1.00134.66           C  
ANISOU 1535  C   PRO A 211    14677  14670  21818   2601   2622  -3281       C  
ATOM   1536  O   PRO A 211     565.954 -10.684 208.906  1.00135.74           O  
ANISOU 1536  O   PRO A 211    14713  14514  22348   2856   2514  -3351       O  
ATOM   1537  CB  PRO A 211     565.645 -12.954 211.396  1.00134.85           C  
ANISOU 1537  CB  PRO A 211    14565  15282  21391   2396   3190  -3717       C  
ATOM   1538  CG  PRO A 211     565.448 -14.418 211.665  1.00133.60           C  
ANISOU 1538  CG  PRO A 211    14360  15511  20892   2172   3348  -3596       C  
ATOM   1539  CD  PRO A 211     566.072 -15.104 210.488  1.00132.06           C  
ANISOU 1539  CD  PRO A 211    14256  15293  20626   2066   3071  -3173       C  
ATOM   1540  N   ARG A 212     567.743 -11.998 209.316  1.00145.88           N  
ANISOU 1540  N   ARG A 212    16392  16076  22961   2381   2529  -3107       N  
ATOM   1541  CA  ARG A 212     568.710 -11.087 208.699  1.00145.95           C  
ANISOU 1541  CA  ARG A 212    16615  15724  23114   2402   2297  -2958       C  
ATOM   1542  C   ARG A 212     568.464 -10.942 207.204  1.00145.42           C  
ANISOU 1542  C   ARG A 212    16477  15489  23288   2536   2032  -2614       C  
ATOM   1543  O   ARG A 212     569.009 -10.052 206.561  1.00145.37           O  
ANISOU 1543  O   ARG A 212    16610  15147  23479   2602   1844  -2474       O  
ATOM   1544  CB  ARG A 212     570.154 -11.566 208.926  1.00145.08           C  
ANISOU 1544  CB  ARG A 212    16791  15684  22648   2120   2253  -2824       C  
ATOM   1545  CG  ARG A 212     570.852 -10.993 210.160  1.00146.41           C  
ANISOU 1545  CG  ARG A 212    17138  15796  22695   2031   2376  -3144       C  
ATOM   1546  CD  ARG A 212     572.283 -11.533 210.319  1.00145.54           C  
ANISOU 1546  CD  ARG A 212    17278  15775  22245   1761   2297  -2997       C  
ATOM   1547  NE  ARG A 212     572.476 -12.155 211.628  1.00145.67           N  
ANISOU 1547  NE  ARG A 212    17369  16091  21888   1612   2493  -3223       N  
ATOM   1548  CZ  ARG A 212     573.598 -12.741 212.036  1.00145.08           C  
ANISOU 1548  CZ  ARG A 212    17490  16159  21477   1391   2452  -3155       C  
ATOM   1549  NH1 ARG A 212     574.660 -12.794 211.240  1.00144.23           N  
ANISOU 1549  NH1 ARG A 212    17502  15926  21370   1282   2240  -2884       N  
ATOM   1550  NH2 ARG A 212     573.652 -13.275 213.248  1.00145.45           N  
ANISOU 1550  NH2 ARG A 212    17607  16480  21178   1284   2625  -3357       N  
ATOM   1551  N   PHE A 213     567.662 -11.839 206.649  1.00 94.76           N  
ANISOU 1551  N   PHE A 213     9852   9311  16841   2561   2015  -2472       N  
ATOM   1552  CA  PHE A 213     567.336 -11.791 205.237  1.00 94.47           C  
ANISOU 1552  CA  PHE A 213     9736   9167  16992   2694   1755  -2159       C  
ATOM   1553  C   PHE A 213     566.081 -10.958 205.015  1.00 95.88           C  
ANISOU 1553  C   PHE A 213     9654   9181  17596   3024   1712  -2304       C  
ATOM   1554  O   PHE A 213     566.063 -10.068 204.172  1.00 96.65           O  
ANISOU 1554  O   PHE A 213     9791   8965  17967   3212   1489  -2149       O  
ATOM   1555  CB  PHE A 213     567.153 -13.200 204.688  1.00 93.02           C  
ANISOU 1555  CB  PHE A 213     9460   9319  16563   2550   1725  -1942       C  
ATOM   1556  CG  PHE A 213     566.619 -13.237 203.295  1.00 93.08           C  
ANISOU 1556  CG  PHE A 213     9346   9279  16742   2701   1466  -1671       C  
ATOM   1557  CD1 PHE A 213     567.448 -13.001 202.216  1.00 92.77           C  
ANISOU 1557  CD1 PHE A 213     9516   9068  16666   2673   1224  -1340       C  
ATOM   1558  CD2 PHE A 213     565.289 -13.518 203.060  1.00 93.61           C  
ANISOU 1558  CD2 PHE A 213     9083   9488  16997   2866   1464  -1751       C  
ATOM   1559  CE1 PHE A 213     566.967 -13.033 200.928  1.00 93.05           C  
ANISOU 1559  CE1 PHE A 213     9463   9077  16815   2814    976  -1085       C  
ATOM   1560  CE2 PHE A 213     564.799 -13.556 201.771  1.00 93.91           C  
ANISOU 1560  CE2 PHE A 213     9010   9498  17173   3011   1193  -1509       C  
ATOM   1561  CZ  PHE A 213     565.646 -13.313 200.701  1.00 93.65           C  
ANISOU 1561  CZ  PHE A 213     9219   9298  17067   2988    945  -1170       C  
ATOM   1562  N   LEU A 214     565.031 -11.247 205.775  1.00107.59           N  
ANISOU 1562  N   LEU A 214    10868  10873  19139   3097   1931  -2598       N  
ATOM   1563  CA  LEU A 214     563.784 -10.507 205.654  1.00109.08           C  
ANISOU 1563  CA  LEU A 214    10761  10934  19750   3421   1912  -2781       C  
ATOM   1564  C   LEU A 214     563.989  -9.044 205.998  1.00110.77           C  
ANISOU 1564  C   LEU A 214    11086  10741  20262   3612   1893  -2971       C  
ATOM   1565  O   LEU A 214     563.334  -8.176 205.427  1.00112.78           O  
ANISOU 1565  O   LEU A 214    11208  10729  20914   3909   1730  -2966       O  
ATOM   1566  CB  LEU A 214     562.713 -11.111 206.553  1.00109.34           C  
ANISOU 1566  CB  LEU A 214    10483  11290  19771   3424   2210  -3100       C  
ATOM   1567  CG  LEU A 214     562.285 -12.542 206.256  1.00107.95           C  
ANISOU 1567  CG  LEU A 214    10140  11499  19377   3253   2252  -2954       C  
ATOM   1568  CD1 LEU A 214     561.637 -13.119 207.486  1.00107.91           C  
ANISOU 1568  CD1 LEU A 214     9951  11797  19252   3151   2631  -3281       C  
ATOM   1569  CD2 LEU A 214     561.327 -12.576 205.079  1.00108.54           C  
ANISOU 1569  CD2 LEU A 214     9931  11564  19747   3469   2004  -2798       C  
ATOM   1570  N   LEU A 215     564.910  -8.766 206.918  1.00147.74           N  
ANISOU 1570  N   LEU A 215    16015  15359  24760   3444   2042  -3138       N  
ATOM   1571  CA  LEU A 215     565.154  -7.393 207.370  1.00149.57           C  
ANISOU 1571  CA  LEU A 215    16362  15198  25269   3594   2047  -3371       C  
ATOM   1572  C   LEU A 215     566.117  -6.645 206.449  1.00149.29           C  
ANISOU 1572  C   LEU A 215    16602  14771  25352   3591   1768  -3055       C  
ATOM   1573  O   LEU A 215     565.757  -5.625 205.879  1.00151.51           O  
ANISOU 1573  O   LEU A 215    16854  14685  26029   3848   1601  -3011       O  
ATOM   1574  CB  LEU A 215     565.693  -7.392 208.804  1.00149.84           C  
ANISOU 1574  CB  LEU A 215    16534  15345  25052   3414   2325  -3727       C  
ATOM   1575  CG  LEU A 215     565.844  -6.066 209.547  1.00152.73           C  
ANISOU 1575  CG  LEU A 215    17000  15379  25654   3539   2387  -4074       C  
ATOM   1576  CD1 LEU A 215     565.088  -6.110 210.863  1.00154.95           C  
ANISOU 1576  CD1 LEU A 215    17148  15941  25784   3539   2684  -4489       C  
ATOM   1577  CD2 LEU A 215     567.310  -5.781 209.790  1.00151.60           C  
ANISOU 1577  CD2 LEU A 215    17204  15063  25334   3313   2331  -4033       C  
ATOM   1578  N   ILE A 216     567.336  -7.149 206.300  1.00112.53           N  
ANISOU 1578  N   ILE A 216    12207  10186  20362   3301   1720  -2830       N  
ATOM   1579  CA  ILE A 216     568.340  -6.464 205.488  1.00112.50           C  
ANISOU 1579  CA  ILE A 216    12468   9828  20447   3253   1498  -2539       C  
ATOM   1580  C   ILE A 216     568.177  -6.711 203.975  1.00111.94           C  
ANISOU 1580  C   ILE A 216    12380   9723  20427   3329   1232  -2083       C  
ATOM   1581  O   ILE A 216     568.134  -5.764 203.198  1.00112.99           O  
ANISOU 1581  O   ILE A 216    12582   9485  20863   3507   1037  -1908       O  
ATOM   1582  CB  ILE A 216     569.764  -6.866 205.922  1.00111.48           C  
ANISOU 1582  CB  ILE A 216    12607   9790  19960   2913   1553  -2497       C  
ATOM   1583  CG1 ILE A 216     569.953  -6.592 207.418  1.00112.35           C  
ANISOU 1583  CG1 ILE A 216    12755   9943  19989   2842   1788  -2953       C  
ATOM   1584  CG2 ILE A 216     570.806  -6.118 205.105  1.00111.30           C  
ANISOU 1584  CG2 ILE A 216    12836   9398  20056   2845   1354  -2214       C  
ATOM   1585  CD1 ILE A 216     571.053  -7.424 208.069  1.00111.38           C  
ANISOU 1585  CD1 ILE A 216    12808  10093  19418   2515   1876  -2962       C  
ATOM   1586  N   ASN A 217     568.074  -7.969 203.553  1.00125.28           N  
ANISOU 1586  N   ASN A 217    13990  11792  21819   3198   1218  -1892       N  
ATOM   1587  CA  ASN A 217     567.981  -8.286 202.121  1.00124.78           C  
ANISOU 1587  CA  ASN A 217    13927  11738  21744   3246    964  -1476       C  
ATOM   1588  C   ASN A 217     566.580  -8.053 201.519  1.00125.80           C  
ANISOU 1588  C   ASN A 217    13775  11842  22181   3574    829  -1465       C  
ATOM   1589  O   ASN A 217     566.453  -7.461 200.447  1.00126.33           O  
ANISOU 1589  O   ASN A 217    13892  11668  22438   3746    576  -1189       O  
ATOM   1590  CB  ASN A 217     568.420  -9.736 201.871  1.00122.96           C  
ANISOU 1590  CB  ASN A 217    13718  11910  21091   2983    990  -1298       C  
ATOM   1591  CG  ASN A 217     569.893  -9.973 202.196  1.00121.98           C  
ANISOU 1591  CG  ASN A 217    13874  11796  20678   2680   1055  -1232       C  
ATOM   1592  OD1 ASN A 217     570.292  -9.987 203.360  1.00121.88           O  
ANISOU 1592  OD1 ASN A 217    13914  11838  20556   2555   1248  -1506       O  
ATOM   1593  ND2 ASN A 217     570.702 -10.179 201.162  1.00121.36           N  
ANISOU 1593  ND2 ASN A 217    13967  11681  20462   2563    892   -876       N  
ATOM   1594  N   ARG A 218     565.538  -8.508 202.212  1.00139.64           N  
ANISOU 1594  N   ARG A 218    15229  13845  23984   3659    995  -1761       N  
ATOM   1595  CA  ARG A 218     564.166  -8.429 201.705  1.00140.51           C  
ANISOU 1595  CA  ARG A 218    15012  13991  24383   3955    877  -1787       C  
ATOM   1596  C   ARG A 218     563.489  -7.123 202.161  1.00143.29           C  
ANISOU 1596  C   ARG A 218    15248  14003  25194   4273    897  -2063       C  
ATOM   1597  O   ARG A 218     562.434  -6.741 201.655  1.00145.56           O  
ANISOU 1597  O   ARG A 218    15345  14281  25679   4513    734  -2032       O  
ATOM   1598  CB  ARG A 218     563.366  -9.662 202.164  1.00139.61           C  
ANISOU 1598  CB  ARG A 218    14603  14337  24106   3863   1059  -1960       C  
ATOM   1599  CG  ARG A 218     562.427 -10.266 201.116  1.00139.92           C  
ANISOU 1599  CG  ARG A 218    14381  14563  24218   3992    847  -1778       C  
ATOM   1600  CD  ARG A 218     561.814 -11.588 201.600  1.00138.60           C  
ANISOU 1600  CD  ARG A 218    13957  14843  23860   3824   1053  -1934       C  
ATOM   1601  NE  ARG A 218     560.450 -11.803 201.104  1.00139.84           N  
ANISOU 1601  NE  ARG A 218    13713  15141  24278   4041    942  -1993       N  
ATOM   1602  CZ  ARG A 218     559.808 -12.972 201.133  1.00138.71           C  
ANISOU 1602  CZ  ARG A 218    13315  15365  24023   3914   1033  -2050       C  
ATOM   1603  NH1 ARG A 218     560.403 -14.056 201.621  1.00136.26           N  
ANISOU 1603  NH1 ARG A 218    13131  15306  23338   3578   1235  -2033       N  
ATOM   1604  NH2 ARG A 218     558.569 -13.063 200.659  1.00140.38           N  
ANISOU 1604  NH2 ARG A 218    13141  15683  24515   4124    910  -2122       N  
ATOM   1605  N   ASN A 219     564.124  -6.454 203.119  1.00205.80           N  
ANISOU 1605  N   ASN A 219    23341  21723  33129   4199   1074  -2302       N  
ATOM   1606  CA  ASN A 219     563.668  -5.168 203.652  1.00209.28           C  
ANISOU 1606  CA  ASN A 219    23799  21919  33799   4373   1091  -2534       C  
ATOM   1607  C   ASN A 219     562.244  -5.189 204.186  1.00211.81           C  
ANISOU 1607  C   ASN A 219    23783  22474  34221   4542   1207  -2825       C  
ATOM   1608  O   ASN A 219     561.529  -4.187 204.145  1.00215.88           O  
ANISOU 1608  O   ASN A 219    24236  22800  34989   4775   1118  -2908       O  
ATOM   1609  CB  ASN A 219     563.816  -4.074 202.597  1.00211.29           C  
ANISOU 1609  CB  ASN A 219    24238  21766  34278   4544    777  -2219       C  
ATOM   1610  CG  ASN A 219     565.022  -3.184 202.854  1.00211.77           C  
ANISOU 1610  CG  ASN A 219    24645  21446  34372   4419    787  -2204       C  
ATOM   1611  OD1 ASN A 219     565.150  -2.590 203.926  1.00213.47           O  
ANISOU 1611  OD1 ASN A 219    24908  21569  34632   4388    970  -2550       O  
ATOM   1612  ND2 ASN A 219     565.920  -3.104 201.877  1.00210.45           N  
ANISOU 1612  ND2 ASN A 219    24722  21071  34170   4330    597  -1806       N  
ATOM   1613  N   GLU A 220     561.849  -6.347 204.691  1.00136.89           N  
ANISOU 1613  N   GLU A 220    14080  13397  24535   4412   1419  -2974       N  
ATOM   1614  CA  GLU A 220     560.610  -6.485 205.433  1.00139.44           C  
ANISOU 1614  CA  GLU A 220    14092  13986  24903   4497   1613  -3292       C  
ATOM   1615  C   GLU A 220     560.903  -6.250 206.912  1.00140.23           C  
ANISOU 1615  C   GLU A 220    14279  14135  24869   4371   1945  -3686       C  
ATOM   1616  O   GLU A 220     561.464  -7.109 207.584  1.00137.43           O  
ANISOU 1616  O   GLU A 220    13987  14012  24219   4128   2171  -3779       O  
ATOM   1617  CB  GLU A 220     559.989  -7.871 205.205  1.00137.33           C  
ANISOU 1617  CB  GLU A 220    13552  14144  24484   4396   1680  -3235       C  
ATOM   1618  CG  GLU A 220     559.160  -7.991 203.934  1.00138.41           C  
ANISOU 1618  CG  GLU A 220    13485  14309  24796   4584   1369  -2974       C  
ATOM   1619  CD  GLU A 220     557.886  -7.152 203.998  1.00143.30           C  
ANISOU 1619  CD  GLU A 220    13869  14876  25701   4859   1315  -3146       C  
ATOM   1620  OE1 GLU A 220     557.164  -7.247 205.015  1.00145.20           O  
ANISOU 1620  OE1 GLU A 220    13910  15320  25940   4839   1593  -3485       O  
ATOM   1621  OE2 GLU A 220     557.608  -6.382 203.050  1.00145.49           O  
ANISOU 1621  OE2 GLU A 220    14170  14909  26200   5096   1001  -2939       O  
ATOM   1622  N   GLU A 221     560.547  -5.076 207.419  1.00168.42           N  
ANISOU 1622  N   GLU A 221    17866  17485  28640   4538   1969  -3915       N  
ATOM   1623  CA  GLU A 221     560.792  -4.780 208.825  1.00169.72           C  
ANISOU 1623  CA  GLU A 221    18120  17700  28667   4432   2267  -4307       C  
ATOM   1624  C   GLU A 221     559.844  -5.594 209.692  1.00170.43           C  
ANISOU 1624  C   GLU A 221    17933  18232  28591   4366   2572  -4570       C  
ATOM   1625  O   GLU A 221     560.239  -6.137 210.724  1.00169.27           O  
ANISOU 1625  O   GLU A 221    17865  18315  28136   4152   2852  -4775       O  
ATOM   1626  CB  GLU A 221     560.626  -3.284 209.114  1.00174.44           C  
ANISOU 1626  CB  GLU A 221    18801  17935  29543   4635   2207  -4492       C  
ATOM   1627  CG  GLU A 221     561.489  -2.780 210.270  1.00175.10           C  
ANISOU 1627  CG  GLU A 221    19133  17918  29478   4488   2397  -4792       C  
ATOM   1628  CD  GLU A 221     560.677  -2.251 211.438  1.00179.93           C  
ANISOU 1628  CD  GLU A 221    19610  18631  30124   4583   2641  -5231       C  
ATOM   1629  OE1 GLU A 221     559.439  -2.142 211.311  1.00183.27           O  
ANISOU 1629  OE1 GLU A 221    19744  19152  30738   4783   2653  -5298       O  
ATOM   1630  OE2 GLU A 221     561.283  -1.942 212.487  1.00180.88           O  
ANISOU 1630  OE2 GLU A 221    19911  18740  30074   4456   2817  -5516       O  
ATOM   1631  N   ASN A 222     558.592  -5.688 209.253  1.00184.69           N  
ANISOU 1631  N   ASN A 222    19420  20162  30591   4542   2513  -4550       N  
ATOM   1632  CA  ASN A 222     557.552  -6.329 210.046  1.00186.30           C  
ANISOU 1632  CA  ASN A 222    19334  20757  30693   4494   2802  -4802       C  
ATOM   1633  C   ASN A 222     557.518  -7.850 209.896  1.00182.53           C  
ANISOU 1633  C   ASN A 222    18740  20661  29951   4261   2909  -4654       C  
ATOM   1634  O   ASN A 222     557.267  -8.554 210.871  1.00182.53           O  
ANISOU 1634  O   ASN A 222    18666  20985  29700   4080   3233  -4854       O  
ATOM   1635  CB  ASN A 222     556.184  -5.741 209.691  1.00191.38           C  
ANISOU 1635  CB  ASN A 222    19663  21366  31685   4779   2701  -4874       C  
ATOM   1636  CG  ASN A 222     555.088  -6.200 210.638  1.00194.21           C  
ANISOU 1636  CG  ASN A 222    19725  22089  31976   4736   3029  -5181       C  
ATOM   1637  OD1 ASN A 222     554.303  -7.094 210.315  1.00193.57           O  
ANISOU 1637  OD1 ASN A 222    19368  22294  31885   4689   3056  -5105       O  
ATOM   1638  ND2 ASN A 222     555.031  -5.588 211.817  1.00197.63           N  
ANISOU 1638  ND2 ASN A 222    20218  22513  32359   4741   3282  -5532       N  
ATOM   1639  N   ARG A 223     557.770  -8.354 208.687  1.00142.69           N  
ANISOU 1639  N   ARG A 223    13690  15577  24951   4261   2641  -4300       N  
ATOM   1640  CA  ARG A 223     557.758  -9.803 208.435  1.00139.33           C  
ANISOU 1640  CA  ARG A 223    13152  15486  24300   4043   2713  -4144       C  
ATOM   1641  C   ARG A 223     558.925 -10.491 209.149  1.00135.83           C  
ANISOU 1641  C   ARG A 223    12973  15151  23483   3752   2930  -4162       C  
ATOM   1642  O   ARG A 223     558.795 -11.624 209.618  1.00134.22           O  
ANISOU 1642  O   ARG A 223    12690  15286  23022   3531   3162  -4190       O  
ATOM   1643  CB  ARG A 223     557.807 -10.109 206.926  1.00137.43           C  
ANISOU 1643  CB  ARG A 223    12864  15161  24193   4125   2348  -3766       C  
ATOM   1644  CG  ARG A 223     556.924 -11.291 206.492  1.00136.70           C  
ANISOU 1644  CG  ARG A 223    12454  15419  24065   4043   2356  -3684       C  
ATOM   1645  CD  ARG A 223     557.121 -11.712 205.023  1.00134.52           C  
ANISOU 1645  CD  ARG A 223    12166  15092  23852   4090   1993  -3312       C  
ATOM   1646  NE  ARG A 223     557.974 -12.901 204.879  1.00130.49           N  
ANISOU 1646  NE  ARG A 223    11771  14744  23065   3821   2057  -3143       N  
ATOM   1647  CZ  ARG A 223     557.810 -13.850 203.954  1.00128.95           C  
ANISOU 1647  CZ  ARG A 223    11444  14713  22836   3754   1891  -2920       C  
ATOM   1648  NH1 ARG A 223     556.819 -13.770 203.072  1.00130.62           N  
ANISOU 1648  NH1 ARG A 223    11407  14967  23257   3931   1636  -2840       N  
ATOM   1649  NH2 ARG A 223     558.635 -14.887 203.909  1.00125.89           N  
ANISOU 1649  NH2 ARG A 223    11219  14471  22143   3480   1955  -2759       N  
ATOM   1650  N   ALA A 224     560.065  -9.804 209.222  1.00130.38           N  
ANISOU 1650  N   ALA A 224    12604  14168  22767   3747   2849  -4138       N  
ATOM   1651  CA  ALA A 224     561.232 -10.307 209.948  1.00128.06           C  
ANISOU 1651  CA  ALA A 224    12579  13948  22129   3491   3035  -4185       C  
ATOM   1652  C   ALA A 224     561.008 -10.213 211.446  1.00129.86           C  
ANISOU 1652  C   ALA A 224    12832  14370  22138   3396   3383  -4560       C  
ATOM   1653  O   ALA A 224     561.410 -11.096 212.200  1.00128.40           O  
ANISOU 1653  O   ALA A 224    12739  14454  21592   3156   3625  -4620       O  
ATOM   1654  CB  ALA A 224     562.491  -9.537 209.560  1.00127.14           C  
ANISOU 1654  CB  ALA A 224    12785  13443  22080   3510   2829  -4061       C  
ATOM   1655  N   LYS A 225     560.369  -9.125 211.865  1.00166.64           N  
ANISOU 1655  N   LYS A 225    17421  18888  27005   3590   3400  -4801       N  
ATOM   1656  CA  LYS A 225     560.044  -8.892 213.267  1.00169.54           C  
ANISOU 1656  CA  LYS A 225    17798  19427  27191   3538   3718  -5174       C  
ATOM   1657  C   LYS A 225     559.250 -10.074 213.826  1.00169.42           C  
ANISOU 1657  C   LYS A 225    17574  19866  26933   3372   4010  -5228       C  
ATOM   1658  O   LYS A 225     559.367 -10.423 215.000  1.00170.05           O  
ANISOU 1658  O   LYS A 225    17751  20185  26674   3200   4310  -5432       O  
ATOM   1659  CB  LYS A 225     559.252  -7.583 213.410  1.00174.43           C  
ANISOU 1659  CB  LYS A 225    18301  19825  28149   3813   3665  -5396       C  
ATOM   1660  CG  LYS A 225     559.160  -7.012 214.827  1.00178.11           C  
ANISOU 1660  CG  LYS A 225    18850  20362  28462   3791   3943  -5803       C  
ATOM   1661  CD  LYS A 225     558.408  -5.670 214.848  1.00183.75           C  
ANISOU 1661  CD  LYS A 225    19445  20811  29558   4085   3864  -6007       C  
ATOM   1662  CE  LYS A 225     558.428  -5.013 216.232  1.00187.92           C  
ANISOU 1662  CE  LYS A 225    20086  21377  29940   4070   4119  -6424       C  
ATOM   1663  NZ  LYS A 225     557.648  -3.732 216.281  1.00193.80           N  
ANISOU 1663  NZ  LYS A 225    20698  21867  31070   4361   4061  -6640       N  
ATOM   1664  N   SER A 226     558.472 -10.708 212.956  1.00138.42           N  
ANISOU 1664  N   SER A 226    13374  16053  23165   3411   3908  -5024       N  
ATOM   1665  CA  SER A 226     557.521 -11.737 213.356  1.00139.09           C  
ANISOU 1665  CA  SER A 226    13209  16529  23109   3272   4158  -5065       C  
ATOM   1666  C   SER A 226     558.153 -13.124 213.534  1.00135.07           C  
ANISOU 1666  C   SER A 226    12822  16284  22214   2956   4305  -4893       C  
ATOM   1667  O   SER A 226     557.660 -13.930 214.318  1.00135.90           O  
ANISOU 1667  O   SER A 226    12848  16713  22075   2771   4603  -4975       O  
ATOM   1668  CB  SER A 226     556.386 -11.803 212.324  1.00140.39           C  
ANISOU 1668  CB  SER A 226    13016  16697  23629   3445   3960  -4937       C  
ATOM   1669  OG  SER A 226     555.276 -12.538 212.806  1.00142.47           O  
ANISOU 1669  OG  SER A 226    12998  17299  23835   3345   4212  -5046       O  
ATOM   1670  N   VAL A 227     559.235 -13.391 212.804  1.00141.10           N  
ANISOU 1670  N   VAL A 227    13784  16899  22930   2896   4100  -4644       N  
ATOM   1671  CA  VAL A 227     559.905 -14.699 212.815  1.00137.73           C  
ANISOU 1671  CA  VAL A 227    13476  16684  22173   2616   4200  -4449       C  
ATOM   1672  C   VAL A 227     560.516 -15.060 214.169  1.00137.74           C  
ANISOU 1672  C   VAL A 227    13732  16880  21722   2389   4515  -4610       C  
ATOM   1673  O   VAL A 227     560.403 -16.199 214.634  1.00136.84           O  
ANISOU 1673  O   VAL A 227    13619  17068  21307   2151   4737  -4542       O  
ATOM   1674  CB  VAL A 227     561.026 -14.755 211.751  1.00134.84           C  
ANISOU 1674  CB  VAL A 227    13313  16088  21833   2608   3876  -4135       C  
ATOM   1675  CG1 VAL A 227     561.933 -15.962 211.967  1.00132.89           C  
ANISOU 1675  CG1 VAL A 227    13342  16050  21100   2269   3906  -3880       C  
ATOM   1676  CG2 VAL A 227     560.433 -14.771 210.361  1.00134.55           C  
ANISOU 1676  CG2 VAL A 227    13031  15946  22146   2777   3578  -3913       C  
ATOM   1677  N   LEU A 228     561.159 -14.078 214.794  1.00150.18           N  
ANISOU 1677  N   LEU A 228    15539  18278  23246   2460   4517  -4818       N  
ATOM   1678  CA  LEU A 228     561.886 -14.291 216.041  1.00150.40           C  
ANISOU 1678  CA  LEU A 228    15853  18467  22825   2265   4756  -4978       C  
ATOM   1679  C   LEU A 228     560.985 -14.734 217.192  1.00152.86           C  
ANISOU 1679  C   LEU A 228    16072  19128  22881   2151   5108  -5160       C  
ATOM   1680  O   LEU A 228     561.331 -15.665 217.921  1.00152.01           O  
ANISOU 1680  O   LEU A 228    16126  19287  22343   1905   5322  -5112       O  
ATOM   1681  CB  LEU A 228     562.639 -13.021 216.440  1.00151.72           C  
ANISOU 1681  CB  LEU A 228    16253  18352  23041   2384   4655  -5201       C  
ATOM   1682  CG  LEU A 228     563.916 -12.680 215.666  1.00149.49           C  
ANISOU 1682  CG  LEU A 228    16219  17761  22819   2379   4327  -4988       C  
ATOM   1683  CD1 LEU A 228     563.612 -12.018 214.328  1.00149.39           C  
ANISOU 1683  CD1 LEU A 228    16038  17418  23304   2618   4021  -4818       C  
ATOM   1684  CD2 LEU A 228     564.836 -11.806 216.503  1.00150.69           C  
ANISOU 1684  CD2 LEU A 228    16666  17762  22828   2363   4329  -5243       C  
ATOM   1685  N   LYS A 229     559.838 -14.072 217.350  1.00168.22           N  
ANISOU 1685  N   LYS A 229    17765  21065  25085   2330   5167  -5353       N  
ATOM   1686  CA  LYS A 229     558.911 -14.379 218.437  1.00171.69           C  
ANISOU 1686  CA  LYS A 229    18096  21817  25322   2242   5512  -5543       C  
ATOM   1687  C   LYS A 229     558.548 -15.861 218.445  1.00170.12           C  
ANISOU 1687  C   LYS A 229    17808  21933  24896   1989   5687  -5317       C  
ATOM   1688  O   LYS A 229     558.247 -16.430 219.491  1.00172.09           O  
ANISOU 1688  O   LYS A 229    18114  22470  24803   1811   5998  -5391       O  
ATOM   1689  CB  LYS A 229     557.648 -13.531 218.324  1.00176.12           C  
ANISOU 1689  CB  LYS A 229    18333  22303  26282   2490   5511  -5741       C  
ATOM   1690  CG  LYS A 229     556.722 -13.955 217.199  1.00175.52           C  
ANISOU 1690  CG  LYS A 229    17901  22228  26561   2569   5363  -5545       C  
ATOM   1691  CD  LYS A 229     555.798 -12.837 216.760  1.00179.60           C  
ANISOU 1691  CD  LYS A 229    18151  22541  27548   2884   5216  -5702       C  
ATOM   1692  CE  LYS A 229     554.745 -12.533 217.808  1.00185.59           C  
ANISOU 1692  CE  LYS A 229    18737  23490  28289   2922   5528  -6016       C  
ATOM   1693  NZ  LYS A 229     553.876 -11.403 217.378  1.00189.79           N  
ANISOU 1693  NZ  LYS A 229    19013  23805  29292   3245   5375  -6176       N  
ATOM   1694  N   LYS A 230     558.578 -16.480 217.269  1.00130.66           N  
ANISOU 1694  N   LYS A 230    12682  16872  20093   1971   5480  -5032       N  
ATOM   1695  CA  LYS A 230     558.434 -17.924 217.148  1.00128.64           C  
ANISOU 1695  CA  LYS A 230    12382  16862  19635   1713   5597  -4784       C  
ATOM   1696  C   LYS A 230     559.778 -18.559 217.431  1.00125.28           C  
ANISOU 1696  C   LYS A 230    12327  16471  18801   1502   5614  -4629       C  
ATOM   1697  O   LYS A 230     559.907 -19.405 218.313  1.00125.51           O  
ANISOU 1697  O   LYS A 230    12517  16752  18419   1262   5865  -4583       O  
ATOM   1698  CB  LYS A 230     557.940 -18.314 215.751  1.00126.86           C  
ANISOU 1698  CB  LYS A 230    11870  16552  19780   1783   5346  -4560       C  
ATOM   1699  CG  LYS A 230     556.485 -18.775 215.699  1.00129.55           C  
ANISOU 1699  CG  LYS A 230    11840  17085  20299   1763   5472  -4590       C  
ATOM   1700  CD  LYS A 230     555.934 -18.679 214.283  1.00128.85           C  
ANISOU 1700  CD  LYS A 230    11454  16853  20651   1936   5146  -4457       C  
ATOM   1701  CE  LYS A 230     555.911 -17.231 213.811  1.00130.32           C  
ANISOU 1701  CE  LYS A 230    11594  16741  21180   2278   4893  -4592       C  
ATOM   1702  NZ  LYS A 230     555.450 -17.085 212.403  1.00129.80           N  
ANISOU 1702  NZ  LYS A 230    11282  16528  21508   2465   4538  -4434       N  
ATOM   1703  N   LEU A 231     560.773 -18.116 216.670  1.00142.67           N  
ANISOU 1703  N   LEU A 231    14670  18411  21129   1601   5337  -4540       N  
ATOM   1704  CA  LEU A 231     562.150 -18.592 216.769  1.00140.11           C  
ANISOU 1704  CA  LEU A 231    14730  18068  20437   1421   5223  -4333       C  
ATOM   1705  C   LEU A 231     562.692 -18.524 218.191  1.00141.60           C  
ANISOU 1705  C   LEU A 231    15215  18416  20170   1294   5468  -4532       C  
ATOM   1706  O   LEU A 231     563.501 -19.361 218.607  1.00140.80           O  
ANISOU 1706  O   LEU A 231    15411  18450  19636   1065   5464  -4326       O  
ATOM   1707  CB  LEU A 231     563.040 -17.769 215.845  1.00139.60           C  
ANISOU 1707  CB  LEU A 231    14809  17659  20573   1568   4803  -4202       C  
ATOM   1708  CG  LEU A 231     564.247 -18.464 215.241  1.00137.79           C  
ANISOU 1708  CG  LEU A 231    14865  17376  20111   1397   4514  -3812       C  
ATOM   1709  CD1 LEU A 231     563.789 -19.728 214.550  1.00136.20           C  
ANISOU 1709  CD1 LEU A 231    14509  17328  19914   1262   4498  -3526       C  
ATOM   1710  CD2 LEU A 231     564.915 -17.524 214.260  1.00137.53           C  
ANISOU 1710  CD2 LEU A 231    14907  16999  20349   1563   4145  -3712       C  
ATOM   1711  N   ARG A 232     562.248 -17.505 218.924  1.00125.92           N  
ANISOU 1711  N   ARG A 232    13178  16407  18260   1447   5613  -4895       N  
ATOM   1712  CA  ARG A 232     562.555 -17.383 220.340  1.00128.28           C  
ANISOU 1712  CA  ARG A 232    13739  16891  18111   1341   5838  -5105       C  
ATOM   1713  C   ARG A 232     561.266 -17.447 221.133  1.00132.98           C  
ANISOU 1713  C   ARG A 232    14139  17722  18664   1335   6127  -5259       C  
ATOM   1714  O   ARG A 232     560.420 -16.571 220.997  1.00135.90           O  
ANISOU 1714  O   ARG A 232    14267  17981  19388   1548   6111  -5457       O  
ATOM   1715  CB  ARG A 232     563.292 -16.077 220.632  1.00129.42           C  
ANISOU 1715  CB  ARG A 232    14069  16794  18310   1499   5693  -5375       C  
ATOM   1716  CG  ARG A 232     564.811 -16.180 220.631  1.00127.24           C  
ANISOU 1716  CG  ARG A 232    14158  16424  17762   1381   5486  -5255       C  
ATOM   1717  CD  ARG A 232     565.366 -16.450 219.241  1.00124.57           C  
ANISOU 1717  CD  ARG A 232    13817  15859  17655   1382   5091  -4846       C  
ATOM   1718  NE  ARG A 232     566.588 -15.689 218.973  1.00124.55           N  
ANISOU 1718  NE  ARG A 232    14063  15582  17679   1418   4767  -4818       N  
ATOM   1719  CZ  ARG A 232     567.247 -15.719 217.819  1.00123.12           C  
ANISOU 1719  CZ  ARG A 232    13921  15177  17680   1424   4421  -4498       C  
ATOM   1720  NH1 ARG A 232     566.812 -16.475 216.820  1.00121.57           N  
ANISOU 1720  NH1 ARG A 232    13548  15005  17639   1407   4334  -4190       N  
ATOM   1721  NH2 ARG A 232     568.343 -14.995 217.661  1.00123.31           N  
ANISOU 1721  NH2 ARG A 232    14160  14960  17731   1436   4169  -4499       N  
ATOM   1722  N   GLY A 233     561.116 -18.488 221.946  1.00231.06           N  
ANISOU 1722  N   GLY A 233    26671  30458  30663   1095   6388  -5154       N  
ATOM   1723  CA  GLY A 233     559.923 -18.659 222.755  1.00235.49           C  
ANISOU 1723  CA  GLY A 233    27063  31262  31149   1057   6695  -5277       C  
ATOM   1724  C   GLY A 233     559.652 -17.452 223.634  1.00240.25           C  
ANISOU 1724  C   GLY A 233    27690  31846  31748   1228   6796  -5666       C  
ATOM   1725  O   GLY A 233     558.732 -16.671 223.368  1.00243.14           O  
ANISOU 1725  O   GLY A 233    27762  32105  32517   1436   6788  -5853       O  
ATOM   1726  N   THR A 234     560.462 -17.290 224.676  1.00193.20           N  
ANISOU 1726  N   THR A 234    22085  25989  25335   1147   6875  -5792       N  
ATOM   1727  CA  THR A 234     560.339 -16.135 225.553  1.00197.96           C  
ANISOU 1727  CA  THR A 234    22751  26567  25898   1299   6955  -6178       C  
ATOM   1728  C   THR A 234     561.619 -15.297 225.534  1.00196.14           C  
ANISOU 1728  C   THR A 234    22803  26100  25621   1378   6696  -6312       C  
ATOM   1729  O   THR A 234     562.365 -15.245 226.515  1.00197.45           O  
ANISOU 1729  O   THR A 234    23295  26394  25331   1281   6750  -6430       O  
ATOM   1730  CB  THR A 234     559.998 -16.552 227.006  1.00202.73           C  
ANISOU 1730  CB  THR A 234    23511  27533  25985   1147   7309  -6282       C  
ATOM   1731  OG1 THR A 234     560.311 -15.483 227.910  1.00206.34           O  
ANISOU 1731  OG1 THR A 234    24147  27963  26288   1264   7334  -6646       O  
ATOM   1732  CG2 THR A 234     560.766 -17.802 227.419  1.00200.32           C  
ANISOU 1732  CG2 THR A 234    23520  27452  25141    866   7368  -5982       C  
ATOM   1733  N   ALA A 235     561.871 -14.647 224.401  1.00212.04           N  
ANISOU 1733  N   ALA A 235    24692  27765  28108   1550   6402  -6284       N  
ATOM   1734  CA  ALA A 235     562.937 -13.659 224.310  1.00211.21           C  
ANISOU 1734  CA  ALA A 235    24801  27375  28073   1651   6150  -6444       C  
ATOM   1735  C   ALA A 235     562.382 -12.325 223.821  1.00213.69           C  
ANISOU 1735  C   ALA A 235    24896  27363  28934   1939   6013  -6661       C  
ATOM   1736  O   ALA A 235     562.463 -11.326 224.537  1.00217.54           O  
ANISOU 1736  O   ALA A 235    25482  27766  29406   2043   6034  -6984       O  
ATOM   1737  CB  ALA A 235     564.046 -14.143 223.401  1.00205.84           C  
ANISOU 1737  CB  ALA A 235    24259  26542  27407   1562   5895  -6165       C  
ATOM   1738  N   ASP A 236     561.798 -12.326 222.621  1.00279.63           N  
ANISOU 1738  N   ASP A 236    32956  35536  37755   2068   5867  -6478       N  
ATOM   1739  CA  ASP A 236     561.282 -11.108 221.987  1.00281.85           C  
ANISOU 1739  CA  ASP A 236    33032  35477  38579   2354   5688  -6614       C  
ATOM   1740  C   ASP A 236     562.335  -9.999 222.047  1.00281.88           C  
ANISOU 1740  C   ASP A 236    33290  35152  38660   2439   5468  -6782       C  
ATOM   1741  O   ASP A 236     562.246  -9.077 222.859  1.00286.28           O  
ANISOU 1741  O   ASP A 236    33921  35654  39200   2530   5538  -7110       O  
ATOM   1742  CB  ASP A 236     559.970 -10.665 222.647  1.00287.85           C  
ANISOU 1742  CB  ASP A 236    33554  36370  39446   2480   5928  -6878       C  
ATOM   1743  CG  ASP A 236     558.825 -11.634 222.379  1.00288.14           C  
ANISOU 1743  CG  ASP A 236    33278  36666  39535   2420   6101  -6709       C  
ATOM   1744  OD1 ASP A 236     558.756 -12.681 223.056  1.00287.90           O  
ANISOU 1744  OD1 ASP A 236    33322  36980  39089   2187   6351  -6627       O  
ATOM   1745  OD2 ASP A 236     557.993 -11.350 221.492  1.00288.85           O  
ANISOU 1745  OD2 ASP A 236    33055  36611  40082   2601   5975  -6650       O  
ATOM   1746  N   VAL A 237     563.323 -10.102 221.166  1.00228.52           N  
ANISOU 1746  N   VAL A 237    26658  28170  31999   2403   5202  -6554       N  
ATOM   1747  CA  VAL A 237     564.605  -9.432 221.347  1.00227.78           C  
ANISOU 1747  CA  VAL A 237    26872  27841  31834   2371   5019  -6662       C  
ATOM   1748  C   VAL A 237     564.760  -8.082 220.633  1.00228.99           C  
ANISOU 1748  C   VAL A 237    26998  27512  32497   2595   4743  -6723       C  
ATOM   1749  O   VAL A 237     564.756  -8.007 219.403  1.00226.63           O  
ANISOU 1749  O   VAL A 237    26583  26963  32563   2695   4519  -6461       O  
ATOM   1750  CB  VAL A 237     565.752 -10.361 220.883  1.00222.70           C  
ANISOU 1750  CB  VAL A 237    26420  27235  30961   2168   4899  -6381       C  
ATOM   1751  CG1 VAL A 237     566.801 -10.501 221.971  1.00223.24           C  
ANISOU 1751  CG1 VAL A 237    26831  27464  30527   1976   4956  -6551       C  
ATOM   1752  CG2 VAL A 237     565.209 -11.734 220.495  1.00220.18           C  
ANISOU 1752  CG2 VAL A 237    25938  27207  30512   2050   5035  -6088       C  
ATOM   1753  N   THR A 238     564.901  -7.019 221.424  1.00182.80           N  
ANISOU 1753  N   THR A 238    21269  21532  26656   2667   4758  -7061       N  
ATOM   1754  CA  THR A 238     565.328  -5.720 220.913  1.00184.09           C  
ANISOU 1754  CA  THR A 238    21495  21218  27233   2824   4494  -7127       C  
ATOM   1755  C   THR A 238     566.826  -5.794 220.652  1.00180.67           C  
ANISOU 1755  C   THR A 238    21345  20619  26684   2656   4284  -7010       C  
ATOM   1756  O   THR A 238     567.355  -5.153 219.739  1.00179.53           O  
ANISOU 1756  O   THR A 238    21243  20073  26896   2726   4016  -6859       O  
ATOM   1757  CB  THR A 238     565.018  -4.578 221.906  1.00189.95           C  
ANISOU 1757  CB  THR A 238    22281  21877  28013   2938   4589  -7548       C  
ATOM   1758  OG1 THR A 238     563.612  -4.546 222.180  1.00193.73           O  
ANISOU 1758  OG1 THR A 238    22484  22528  28598   3089   4803  -7669       O  
ATOM   1759  CG2 THR A 238     565.456  -3.226 221.347  1.00191.61           C  
ANISOU 1759  CG2 THR A 238    22565  21565  28675   3088   4313  -7593       C  
ATOM   1760  N   HIS A 239     567.496  -6.604 221.467  1.00252.23           N  
ANISOU 1760  N   HIS A 239    30604  30001  35232   2428   4408  -7067       N  
ATOM   1761  CA  HIS A 239     568.929  -6.832 221.350  1.00249.17           C  
ANISOU 1761  CA  HIS A 239    30478  29529  34665   2242   4230  -6980       C  
ATOM   1762  C   HIS A 239     569.288  -7.478 220.000  1.00245.15           C  
ANISOU 1762  C   HIS A 239    29904  28882  34359   2215   4057  -6565       C  
ATOM   1763  O   HIS A 239     570.251  -7.064 219.355  1.00244.02           O  
ANISOU 1763  O   HIS A 239    29894  28431  34390   2172   3789  -6416       O  
ATOM   1764  CB  HIS A 239     569.426  -7.700 222.521  1.00249.01           C  
ANISOU 1764  CB  HIS A 239    30664  29940  34007   2016   4406  -7103       C  
ATOM   1765  CG  HIS A 239     569.439  -6.997 223.852  1.00253.73           C  
ANISOU 1765  CG  HIS A 239    31406  30639  34360   2014   4512  -7512       C  
ATOM   1766  ND1 HIS A 239     569.472  -7.677 225.049  1.00255.12           N  
ANISOU 1766  ND1 HIS A 239    31731  31250  33954   1865   4723  -7646       N  
ATOM   1767  CD2 HIS A 239     569.440  -5.680 224.168  1.00257.71           C  
ANISOU 1767  CD2 HIS A 239    31942  30864  35112   2140   4431  -7805       C  
ATOM   1768  CE1 HIS A 239     569.484  -6.810 226.049  1.00259.79           C  
ANISOU 1768  CE1 HIS A 239    32433  31836  34437   1907   4766  -8017       C  
ATOM   1769  NE2 HIS A 239     569.466  -5.593 225.540  1.00261.39           N  
ANISOU 1769  NE2 HIS A 239    32563  31607  35148   2071   4596  -8130       N  
ATOM   1770  N   ASP A 240     568.517  -8.477 219.566  1.00285.54           N  
ANISOU 1770  N   ASP A 240    34821  34236  39436   2219   4182  -6334       N  
ATOM   1771  CA  ASP A 240     568.767  -9.126 218.274  1.00282.20           C  
ANISOU 1771  CA  ASP A 240    34355  33749  39118   2163   3937  -5809       C  
ATOM   1772  C   ASP A 240     568.525  -8.159 217.116  1.00282.38           C  
ANISOU 1772  C   ASP A 240    34248  33322  39724   2390   3715  -5704       C  
ATOM   1773  O   ASP A 240     569.250  -8.173 216.121  1.00280.97           O  
ANISOU 1773  O   ASP A 240    34162  32943  39652   2333   3434  -5346       O  
ATOM   1774  CB  ASP A 240     567.891 -10.374 218.095  1.00280.86           C  
ANISOU 1774  CB  ASP A 240    33989  33935  38788   2113   4104  -5592       C  
ATOM   1775  CG  ASP A 240     568.629 -11.672 218.413  1.00279.86           C  
ANISOU 1775  CG  ASP A 240    34062  34143  38129   1825   4105  -5328       C  
ATOM   1776  OD1 ASP A 240     569.878 -11.663 218.460  1.00279.35           O  
ANISOU 1776  OD1 ASP A 240    34259  34010  37872   1680   3903  -5222       O  
ATOM   1777  OD2 ASP A 240     567.956 -12.710 218.601  1.00279.67           O  
ANISOU 1777  OD2 ASP A 240    33923  34439  37900   1745   4304  -5224       O  
ATOM   1778  N   LEU A 241     567.505  -7.318 217.253  1.00158.52           N  
ANISOU 1778  N   LEU A 241    18365  17499  24365   2630   3811  -5960       N  
ATOM   1779  CA  LEU A 241     567.176  -6.346 216.213  1.00159.32           C  
ANISOU 1779  CA  LEU A 241    18362  17188  24983   2854   3570  -5818       C  
ATOM   1780  C   LEU A 241     568.231  -5.249 216.078  1.00160.17           C  
ANISOU 1780  C   LEU A 241    18711  16871  25275   2843   3351  -5864       C  
ATOM   1781  O   LEU A 241     568.599  -4.869 214.965  1.00159.31           O  
ANISOU 1781  O   LEU A 241    18631  16424  25476   2904   3104  -5581       O  
ATOM   1782  CB  LEU A 241     565.806  -5.716 216.479  1.00163.11           C  
ANISOU 1782  CB  LEU A 241    18604  17686  25682   3079   3670  -6007       C  
ATOM   1783  CG  LEU A 241     564.624  -6.455 215.853  1.00162.39           C  
ANISOU 1783  CG  LEU A 241    18196  17806  25699   3179   3722  -5813       C  
ATOM   1784  CD1 LEU A 241     563.390  -5.582 215.854  1.00167.01           C  
ANISOU 1784  CD1 LEU A 241    18550  18288  26617   3440   3731  -5968       C  
ATOM   1785  CD2 LEU A 241     564.966  -6.888 214.438  1.00158.76           C  
ANISOU 1785  CD2 LEU A 241    17708  17189  25425   3191   3469  -5389       C  
ATOM   1786  N   GLN A 242     568.711  -4.734 217.207  1.00174.45           N  
ANISOU 1786  N   GLN A 242    20696  18701  26886   2756   3439  -6210       N  
ATOM   1787  CA  GLN A 242     569.772  -3.737 217.169  1.00175.45           C  
ANISOU 1787  CA  GLN A 242    21050  18445  27167   2704   3239  -6277       C  
ATOM   1788  C   GLN A 242     571.065  -4.368 216.626  1.00172.13           C  
ANISOU 1788  C   GLN A 242    20804  17974  26624   2488   3094  -6027       C  
ATOM   1789  O   GLN A 242     571.841  -3.700 215.942  1.00171.93           O  
ANISOU 1789  O   GLN A 242    20899  17563  26863   2463   2868  -5875       O  
ATOM   1790  CB  GLN A 242     570.003  -3.113 218.557  1.00179.23           C  
ANISOU 1790  CB  GLN A 242    21672  18998  27428   2646   3360  -6728       C  
ATOM   1791  CG  GLN A 242     569.151  -1.860 218.854  1.00184.65           C  
ANISOU 1791  CG  GLN A 242    22266  19464  28428   2873   3383  -6976       C  
ATOM   1792  CD  GLN A 242     569.670  -1.040 220.037  1.00188.52           C  
ANISOU 1792  CD  GLN A 242    22946  19909  28775   2804   3425  -7396       C  
ATOM   1793  OE1 GLN A 242     570.690  -1.374 220.641  1.00187.23           O  
ANISOU 1793  OE1 GLN A 242    22986  19880  28273   2584   3415  -7503       O  
ATOM   1794  NE2 GLN A 242     568.965   0.042 220.366  1.00193.60           N  
ANISOU 1794  NE2 GLN A 242    23518  20362  29678   2997   3461  -7642       N  
ATOM   1795  N   GLU A 243     571.285  -5.652 216.915  1.00228.05           N  
ANISOU 1795  N   GLU A 243    27920  25495  33233   2294   3177  -5874       N  
ATOM   1796  CA  GLU A 243     572.471  -6.362 216.422  1.00226.11           C  
ANISOU 1796  CA  GLU A 243    27849  25330  32731   2043   2971  -5488       C  
ATOM   1797  C   GLU A 243     572.409  -6.523 214.915  1.00224.62           C  
ANISOU 1797  C   GLU A 243    27576  24958  32811   2097   2766  -5008       C  
ATOM   1798  O   GLU A 243     573.417  -6.384 214.224  1.00224.34           O  
ANISOU 1798  O   GLU A 243    27679  24730  32828   1973   2547  -4745       O  
ATOM   1799  CB  GLU A 243     572.613  -7.743 217.081  1.00225.14           C  
ANISOU 1799  CB  GLU A 243    27778  25722  32042   1845   3100  -5408       C  
ATOM   1800  CG  GLU A 243     573.918  -8.489 216.733  1.00223.86           C  
ANISOU 1800  CG  GLU A 243    27801  25658  31596   1591   2893  -5067       C  
ATOM   1801  CD  GLU A 243     573.710  -9.706 215.833  1.00221.61           C  
ANISOU 1801  CD  GLU A 243    27426  25581  31197   1533   2844  -4606       C  
ATOM   1802  OE1 GLU A 243     573.636  -9.536 214.597  1.00220.25           O  
ANISOU 1802  OE1 GLU A 243    27171  25182  31330   1608   2683  -4308       O  
ATOM   1803  OE2 GLU A 243     573.637 -10.838 216.359  1.00221.31           O  
ANISOU 1803  OE2 GLU A 243    27409  25924  30753   1410   2963  -4542       O  
ATOM   1804  N   MET A 244     571.215  -6.819 214.413  1.00162.41           N  
ANISOU 1804  N   MET A 244    19460  17156  25094   2278   2842  -4907       N  
ATOM   1805  CA  MET A 244     571.020  -7.060 212.990  1.00161.20           C  
ANISOU 1805  CA  MET A 244    19213  16884  25152   2345   2648  -4461       C  
ATOM   1806  C   MET A 244     571.192  -5.769 212.209  1.00161.96           C  
ANISOU 1806  C   MET A 244    19350  16458  25728   2502   2452  -4404       C  
ATOM   1807  O   MET A 244     571.520  -5.786 211.021  1.00161.23           O  
ANISOU 1807  O   MET A 244    19293  16200  25767   2493   2239  -4006       O  
ATOM   1808  CB  MET A 244     569.638  -7.664 212.730  1.00160.84           C  
ANISOU 1808  CB  MET A 244    18879  17060  25172   2506   2772  -4419       C  
ATOM   1809  CG  MET A 244     569.544  -9.158 213.039  1.00159.80           C  
ANISOU 1809  CG  MET A 244    18714  17411  24592   2313   2904  -4286       C  
ATOM   1810  SD  MET A 244     567.846  -9.776 213.105  1.00159.89           S  
ANISOU 1810  SD  MET A 244    18360  17704  24687   2475   3132  -4377       S  
ATOM   1811  CE  MET A 244     567.204  -9.171 211.549  1.00159.59           C  
ANISOU 1811  CE  MET A 244    18129  17334  25172   2742   2865  -4112       C  
ATOM   1812  N   LYS A 245     570.976  -4.651 212.893  1.00137.85           N  
ANISOU 1812  N   LYS A 245    16304  13142  22930   2642   2531  -4805       N  
ATOM   1813  CA  LYS A 245     571.120  -3.334 212.283  1.00139.84           C  
ANISOU 1813  CA  LYS A 245    16614  12850  23671   2798   2363  -4791       C  
ATOM   1814  C   LYS A 245     572.487  -2.715 212.634  1.00140.38           C  
ANISOU 1814  C   LYS A 245    16949  12681  23707   2587   2272  -4886       C  
ATOM   1815  O   LYS A 245     572.865  -1.671 212.101  1.00142.07           O  
ANISOU 1815  O   LYS A 245    17265  12451  24263   2630   2111  -4800       O  
ATOM   1816  CB  LYS A 245     569.954  -2.433 212.706  1.00143.30           C  
ANISOU 1816  CB  LYS A 245    16903  13202  24343   3052   2434  -5057       C  
ATOM   1817  CG  LYS A 245     568.585  -3.013 212.308  1.00142.99           C  
ANISOU 1817  CG  LYS A 245    16570  13404  24357   3249   2499  -4952       C  
ATOM   1818  CD  LYS A 245     567.403  -2.118 212.694  1.00147.79           C  
ANISOU 1818  CD  LYS A 245    17017  13947  25190   3497   2554  -5194       C  
ATOM   1819  CE  LYS A 245     566.071  -2.679 212.165  1.00147.80           C  
ANISOU 1819  CE  LYS A 245    16706  14171  25281   3684   2579  -5062       C  
ATOM   1820  NZ  LYS A 245     564.872  -1.821 212.449  1.00152.83           N  
ANISOU 1820  NZ  LYS A 245    17158  14740  26171   3941   2620  -5281       N  
ATOM   1821  N   GLU A 246     573.230  -3.385 213.516  1.00221.96           N  
ANISOU 1821  N   GLU A 246    27399  23343  33592   2340   2356  -5021       N  
ATOM   1822  CA  GLU A 246     574.635  -3.059 213.749  1.00221.83           C  
ANISOU 1822  CA  GLU A 246    27612  23187  33485   2096   2237  -5049       C  
ATOM   1823  C   GLU A 246     575.527  -4.043 212.990  1.00219.96           C  
ANISOU 1823  C   GLU A 246    27453  23146  32975   1865   2094  -4584       C  
ATOM   1824  O   GLU A 246     576.665  -3.719 212.651  1.00219.76           O  
ANISOU 1824  O   GLU A 246    27577  22922  33002   1688   1942  -4453       O  
ATOM   1825  CB  GLU A 246     574.971  -3.077 215.244  1.00223.33           C  
ANISOU 1825  CB  GLU A 246    27893  23599  33362   1981   2386  -5526       C  
ATOM   1826  CG  GLU A 246     574.965  -1.707 215.923  1.00227.07           C  
ANISOU 1826  CG  GLU A 246    28427  23723  34127   2075   2409  -5973       C  
ATOM   1827  CD  GLU A 246     576.357  -1.099 216.071  1.00227.65           C  
ANISOU 1827  CD  GLU A 246    28707  23550  34241   1849   2244  -6044       C  
ATOM   1828  OE1 GLU A 246     577.322  -1.659 215.504  1.00225.10           O  
ANISOU 1828  OE1 GLU A 246    28463  23274  33789   1641   2106  -5724       O  
ATOM   1829  OE2 GLU A 246     576.484  -0.055 216.752  1.00231.09           O  
ANISOU 1829  OE2 GLU A 246    29218  23814  34771   1855   2224  -6346       O  
ATOM   1830  N   GLU A 247     575.015  -5.248 212.735  1.00180.48           N  
ANISOU 1830  N   GLU A 247    22342  18534  27699   1860   2151  -4353       N  
ATOM   1831  CA  GLU A 247     575.692  -6.183 211.835  1.00178.72           C  
ANISOU 1831  CA  GLU A 247    22162  18467  27275   1689   2013  -3895       C  
ATOM   1832  C   GLU A 247     575.550  -5.642 210.423  1.00178.17           C  
ANISOU 1832  C   GLU A 247    22066  18052  27580   1804   1846  -3542       C  
ATOM   1833  O   GLU A 247     576.412  -5.864 209.579  1.00176.99           O  
ANISOU 1833  O   GLU A 247    22011  17846  27393   1655   1699  -3201       O  
ATOM   1834  CB  GLU A 247     575.117  -7.605 211.934  1.00177.48           C  
ANISOU 1834  CB  GLU A 247    21894  18787  26754   1659   2121  -3759       C  
ATOM   1835  CG  GLU A 247     575.731  -8.613 210.951  1.00175.90           C  
ANISOU 1835  CG  GLU A 247    21725  18743  26367   1506   1982  -3301       C  
ATOM   1836  CD  GLU A 247     576.603  -9.650 211.635  1.00174.96           C  
ANISOU 1836  CD  GLU A 247    21716  18972  25790   1267   2006  -3298       C  
ATOM   1837  OE1 GLU A 247     576.489  -9.800 212.869  1.00175.38           O  
ANISOU 1837  OE1 GLU A 247    21801  19225  25611   1235   2152  -3615       O  
ATOM   1838  OE2 GLU A 247     577.401 -10.315 210.939  1.00173.93           O  
ANISOU 1838  OE2 GLU A 247    21642  18917  25527   1119   1877  -2980       O  
ATOM   1839  N   SER A 248     574.455  -4.925 210.173  1.00149.89           N  
ANISOU 1839  N   SER A 248    18354  14243  24354   2078   1870  -3625       N  
ATOM   1840  CA  SER A 248     574.287  -4.237 208.900  1.00149.80           C  
ANISOU 1840  CA  SER A 248    18343  13855  24720   2219   1694  -3310       C  
ATOM   1841  C   SER A 248     574.804  -2.801 209.016  1.00151.39           C  
ANISOU 1841  C   SER A 248    18685  13539  25297   2243   1631  -3474       C  
ATOM   1842  O   SER A 248     574.579  -1.965 208.136  1.00152.07           O  
ANISOU 1842  O   SER A 248    18792  13226  25763   2395   1503  -3278       O  
ATOM   1843  CB  SER A 248     572.830  -4.260 208.442  1.00149.82           C  
ANISOU 1843  CB  SER A 248    18118  13875  24930   2519   1709  -3266       C  
ATOM   1844  OG  SER A 248     572.039  -3.389 209.219  1.00151.39           O  
ANISOU 1844  OG  SER A 248    18220  13893  25408   2739   1828  -3683       O  
ATOM   1845  N   ARG A 249     575.484  -2.521 210.124  1.00184.42           N  
ANISOU 1845  N   ARG A 249    22971  17728  29371   2093   1715  -3840       N  
ATOM   1846  CA  ARG A 249     576.379  -1.376 210.192  1.00185.69           C  
ANISOU 1846  CA  ARG A 249    23301  17441  29810   1998   1632  -3951       C  
ATOM   1847  C   ARG A 249     577.737  -1.822 209.652  1.00184.32           C  
ANISOU 1847  C   ARG A 249    23267  17326  29440   1692   1513  -3631       C  
ATOM   1848  O   ARG A 249     578.066  -1.569 208.497  1.00183.46           O  
ANISOU 1848  O   ARG A 249    23218  16976  29512   1666   1383  -3239       O  
ATOM   1849  CB  ARG A 249     576.515  -0.838 211.623  1.00188.05           C  
ANISOU 1849  CB  ARG A 249    23640  17721  30088   1972   1759  -4523       C  
ATOM   1850  CG  ARG A 249     575.534   0.271 212.024  1.00191.66           C  
ANISOU 1850  CG  ARG A 249    24034  17950  30837   2227   1805  -4799       C  
ATOM   1851  CD  ARG A 249     575.886   0.821 213.416  1.00194.51           C  
ANISOU 1851  CD  ARG A 249    24478  18360  31066   2134   1893  -5305       C  
ATOM   1852  NE  ARG A 249     575.139   2.018 213.803  1.00199.59           N  
ANISOU 1852  NE  ARG A 249    25096  18780  31959   2334   1909  -5540       N  
ATOM   1853  CZ  ARG A 249     575.309   2.665 214.956  1.00203.16           C  
ANISOU 1853  CZ  ARG A 249    25617  19231  32345   2293   1977  -5981       C  
ATOM   1854  NH1 ARG A 249     576.196   2.228 215.842  1.00202.21           N  
ANISOU 1854  NH1 ARG A 249    25596  19340  31895   2060   2018  -6230       N  
ATOM   1855  NH2 ARG A 249     574.594   3.752 215.228  1.00207.94           N  
ANISOU 1855  NH2 ARG A 249    26192  19609  33206   2489   1992  -6178       N  
ATOM   1856  N   GLN A 250     578.493  -2.534 210.484  1.00188.68           N  
ANISOU 1856  N   GLN A 250    23864  18222  29604   1468   1562  -3794       N  
ATOM   1857  CA  GLN A 250     579.871  -2.916 210.169  1.00187.74           C  
ANISOU 1857  CA  GLN A 250    23855  18167  29311   1173   1457  -3579       C  
ATOM   1858  C   GLN A 250     580.039  -3.749 208.883  1.00185.76           C  
ANISOU 1858  C   GLN A 250    23581  18058  28939   1119   1371  -3046       C  
ATOM   1859  O   GLN A 250     580.989  -3.521 208.132  1.00185.22           O  
ANISOU 1859  O   GLN A 250    23602  17808  28965    952   1270  -2789       O  
ATOM   1860  CB  GLN A 250     580.489  -3.672 211.351  1.00187.90           C  
ANISOU 1860  CB  GLN A 250    23904  18591  28901    990   1512  -3853       C  
ATOM   1861  CG  GLN A 250     580.816  -2.789 212.558  1.00190.01           C  
ANISOU 1861  CG  GLN A 250    24245  18701  29250    949   1549  -4370       C  
ATOM   1862  CD  GLN A 250     581.861  -3.407 213.474  1.00190.41           C  
ANISOU 1862  CD  GLN A 250    24366  19078  28903    707   1517  -4551       C  
ATOM   1863  OE1 GLN A 250     582.223  -4.576 213.322  1.00189.13           O  
ANISOU 1863  OE1 GLN A 250    24188  19286  28386    596   1491  -4310       O  
ATOM   1864  NE2 GLN A 250     582.358  -2.620 214.426  1.00192.36           N  
ANISOU 1864  NE2 GLN A 250    24692  19181  29217    631   1505  -4984       N  
ATOM   1865  N   MET A 251     579.144  -4.705 208.621  1.00201.03           N  
ANISOU 1865  N   MET A 251    25395  20316  30671   1246   1418  -2894       N  
ATOM   1866  CA  MET A 251     579.229  -5.488 207.379  1.00199.31           C  
ANISOU 1866  CA  MET A 251    25154  20233  30341   1211   1332  -2418       C  
ATOM   1867  C   MET A 251     578.848  -4.643 206.165  1.00199.50           C  
ANISOU 1867  C   MET A 251    25198  19862  30739   1361   1228  -2126       C  
ATOM   1868  O   MET A 251     579.084  -5.044 205.022  1.00198.36           O  
ANISOU 1868  O   MET A 251    25078  19752  30539   1315   1138  -1721       O  
ATOM   1869  CB  MET A 251     578.331  -6.733 207.426  1.00198.12           C  
ANISOU 1869  CB  MET A 251    24860  20518  29898   1301   1404  -2353       C  
ATOM   1870  CG  MET A 251     578.751  -7.818 208.411  1.00197.60           C  
ANISOU 1870  CG  MET A 251    24797  20879  29402   1136   1491  -2514       C  
ATOM   1871  SD  MET A 251     579.163  -9.377 207.597  1.00195.63           S  
ANISOU 1871  SD  MET A 251    24525  21005  28801    992   1432  -2110       S  
ATOM   1872  CE  MET A 251     577.841  -9.491 206.395  1.00195.49           C  
ANISOU 1872  CE  MET A 251    24364  20948  28965   1230   1396  -1832       C  
ATOM   1873  N   MET A 252     578.250  -3.478 206.415  1.00173.75           N  
ANISOU 1873  N   MET A 252    21938  16228  27852   1550   1239  -2334       N  
ATOM   1874  CA  MET A 252     577.811  -2.594 205.336  1.00174.38           C  
ANISOU 1874  CA  MET A 252    22051  15896  28310   1728   1127  -2064       C  
ATOM   1875  C   MET A 252     578.487  -1.217 205.409  1.00176.06           C  
ANISOU 1875  C   MET A 252    22419  15573  28901   1665   1088  -2160       C  
ATOM   1876  O   MET A 252     578.249  -0.366 204.553  1.00177.09           O  
ANISOU 1876  O   MET A 252    22618  15297  29370   1793    992  -1925       O  
ATOM   1877  CB  MET A 252     576.281  -2.426 205.354  1.00174.78           C  
ANISOU 1877  CB  MET A 252    21934  15931  28543   2073   1146  -2167       C  
ATOM   1878  CG  MET A 252     575.477  -3.705 205.661  1.00173.52           C  
ANISOU 1878  CG  MET A 252    21584  16295  28049   2131   1236  -2221       C  
ATOM   1879  SD  MET A 252     574.916  -4.743 204.287  1.00171.87           S  
ANISOU 1879  SD  MET A 252    21275  16357  27671   2201   1116  -1736       S  
ATOM   1880  CE  MET A 252     573.936  -3.580 203.346  1.00173.30           C  
ANISOU 1880  CE  MET A 252    21420  16086  28340   2546    960  -1568       C  
ATOM   1881  N   ARG A 253     579.331  -0.999 206.418  1.00216.80           N  
ANISOU 1881  N   ARG A 253    27641  20725  34006   1466   1152  -2499       N  
ATOM   1882  CA  ARG A 253     580.067   0.265 206.543  1.00218.63           C  
ANISOU 1882  CA  ARG A 253    28015  20453  34601   1363   1118  -2623       C  
ATOM   1883  C   ARG A 253     581.453   0.173 205.918  1.00217.78           C  
ANISOU 1883  C   ARG A 253    28025  20294  34426   1042   1058  -2335       C  
ATOM   1884  O   ARG A 253     582.001   1.165 205.437  1.00219.61           O  
ANISOU 1884  O   ARG A 253    28381  20064  34996    955   1008  -2216       O  
ATOM   1885  CB  ARG A 253     580.169   0.687 208.010  1.00220.43           C  
ANISOU 1885  CB  ARG A 253    28237  20669  34850   1336   1211  -3204       C  
ATOM   1886  CG  ARG A 253     578.909   1.383 208.487  1.00223.15           C  
ANISOU 1886  CG  ARG A 253    28503  20894  35388   1645   1258  -3470       C  
ATOM   1887  CD  ARG A 253     578.946   1.798 209.946  1.00225.44           C  
ANISOU 1887  CD  ARG A 253    28794  21262  35600   1619   1351  -4029       C  
ATOM   1888  NE  ARG A 253     577.864   2.743 210.224  1.00229.36           N  
ANISOU 1888  NE  ARG A 253    29242  21591  36311   1891   1370  -4209       N  
ATOM   1889  CZ  ARG A 253     577.657   3.340 211.394  1.00232.72           C  
ANISOU 1889  CZ  ARG A 253    29667  22028  36726   1931   1449  -4679       C  
ATOM   1890  NH1 ARG A 253     578.457   3.090 212.421  1.00232.43           N  
ANISOU 1890  NH1 ARG A 253    29685  22178  36449   1717   1505  -5020       N  
ATOM   1891  NH2 ARG A 253     576.645   4.188 211.536  1.00236.61           N  
ANISOU 1891  NH2 ARG A 253    30105  22353  37440   2190   1466  -4810       N  
ATOM   1892  N   GLU A 254     582.016  -1.028 205.937  1.00172.19           N  
ANISOU 1892  N   GLU A 254    22206  14989  28229    864   1071  -2229       N  
ATOM   1893  CA  GLU A 254     583.188  -1.327 205.136  1.00171.32           C  
ANISOU 1893  CA  GLU A 254    22165  14906  28023    597   1022  -1893       C  
ATOM   1894  C   GLU A 254     582.709  -1.926 203.821  1.00169.93           C  
ANISOU 1894  C   GLU A 254    21975  14855  27736    700    975  -1404       C  
ATOM   1895  O   GLU A 254     581.923  -2.876 203.816  1.00168.79           O  
ANISOU 1895  O   GLU A 254    21721  15079  27333    842    988  -1367       O  
ATOM   1896  CB  GLU A 254     584.124  -2.285 205.870  1.00170.53           C  
ANISOU 1896  CB  GLU A 254    22019  15229  27546    358   1046  -2059       C  
ATOM   1897  CG  GLU A 254     584.429  -1.868 207.300  1.00171.71           C  
ANISOU 1897  CG  GLU A 254    22171  15358  27713    292   1078  -2585       C  
ATOM   1898  CD  GLU A 254     585.349  -2.839 208.010  1.00171.12           C  
ANISOU 1898  CD  GLU A 254    22058  15712  27249     76   1069  -2724       C  
ATOM   1899  OE1 GLU A 254     586.303  -3.333 207.371  1.00169.94           O  
ANISOU 1899  OE1 GLU A 254    21906  15672  26991   -125   1023  -2456       O  
ATOM   1900  OE2 GLU A 254     585.115  -3.108 209.207  1.00171.95           O  
ANISOU 1900  OE2 GLU A 254    22136  16047  27151    116   1107  -3101       O  
ATOM   1901  N   LYS A 255     583.160  -1.352 202.711  1.00105.50           N  
ANISOU 1901  N   LYS A 255    13929   6383  19772    624    923  -1035       N  
ATOM   1902  CA  LYS A 255     582.781  -1.823 201.381  1.00104.46           C  
ANISOU 1902  CA  LYS A 255    13814   6350  19527    711    864   -557       C  
ATOM   1903  C   LYS A 255     583.052  -3.326 201.172  1.00102.42           C  
ANISOU 1903  C   LYS A 255    13463   6647  18804    607    881   -430       C  
ATOM   1904  O   LYS A 255     584.146  -3.832 201.467  1.00101.74           O  
ANISOU 1904  O   LYS A 255    13369   6755  18531    350    921   -491       O  
ATOM   1905  CB  LYS A 255     583.524  -1.010 200.318  1.00105.12           C  
ANISOU 1905  CB  LYS A 255    14064   6043  19833    566    833   -189       C  
ATOM   1906  CG  LYS A 255     583.413   0.486 200.530  1.00108.77           C  
ANISOU 1906  CG  LYS A 255    14638   5908  20781    630    818   -305       C  
ATOM   1907  CD  LYS A 255     584.137   1.304 199.463  1.00111.42           C  
ANISOU 1907  CD  LYS A 255    15158   5900  21278    465    796     93       C  
ATOM   1908  CE  LYS A 255     583.908   2.800 199.696  1.00116.60           C  
ANISOU 1908  CE  LYS A 255    15929   6141  22231    544    747    -23       C  
ATOM   1909  NZ  LYS A 255     584.494   3.658 198.629  1.00119.77           N  
ANISOU 1909  NZ  LYS A 255    16532   6258  22718    401    721    381       N  
ATOM   1910  N   LYS A 256     582.053  -4.051 200.680  1.00123.20           N  
ANISOU 1910  N   LYS A 256    16014   9530  21268    810    842   -271       N  
ATOM   1911  CA  LYS A 256     582.283  -5.429 200.273  1.00121.30           C  
ANISOU 1911  CA  LYS A 256    15705   9756  20628    718    847   -101       C  
ATOM   1912  C   LYS A 256     583.209  -5.378 199.069  1.00120.79           C  
ANISOU 1912  C   LYS A 256    15757   9612  20527    536    822    296       C  
ATOM   1913  O   LYS A 256     582.781  -5.097 197.950  1.00120.91           O  
ANISOU 1913  O   LYS A 256    15844   9490  20606    648    752    637       O  
ATOM   1914  CB  LYS A 256     580.972  -6.157 199.950  1.00120.64           C  
ANISOU 1914  CB  LYS A 256    15503   9927  20409    968    804    -23       C  
ATOM   1915  CG  LYS A 256     579.934  -5.292 199.224  1.00121.75           C  
ANISOU 1915  CG  LYS A 256    15667   9753  20838   1240    705    151       C  
ATOM   1916  CD  LYS A 256     578.551  -5.946 199.162  1.00121.60           C  
ANISOU 1916  CD  LYS A 256    15478   9989  20735   1499    664    120       C  
ATOM   1917  CE  LYS A 256     577.534  -5.053 198.448  1.00123.11           C  
ANISOU 1917  CE  LYS A 256    15678   9865  21236   1791    535    285       C  
ATOM   1918  NZ  LYS A 256     577.810  -4.901 196.990  1.00123.30           N  
ANISOU 1918  NZ  LYS A 256    15844   9779  21226   1776    408    762       N  
ATOM   1919  N   VAL A 257     584.495  -5.594 199.317  1.00 84.61           N  
ANISOU 1919  N   VAL A 257    11192   5106  15850    254    880    242       N  
ATOM   1920  CA  VAL A 257     585.449  -5.699 198.223  1.00 84.33           C  
ANISOU 1920  CA  VAL A 257    11236   5064  15740     54    893    592       C  
ATOM   1921  C   VAL A 257     585.281  -7.067 197.545  1.00 80.83           C  
ANISOU 1921  C   VAL A 257    10724   5070  14919     77    878    793       C  
ATOM   1922  O   VAL A 257     584.936  -8.087 198.178  1.00 78.10           O  
ANISOU 1922  O   VAL A 257    10256   5077  14341    131    881    604       O  
ATOM   1923  CB  VAL A 257     586.907  -5.463 198.705  1.00 84.75           C  
ANISOU 1923  CB  VAL A 257    11296   5052  15853   -259    962    447       C  
ATOM   1924  CG1 VAL A 257     586.921  -5.221 200.180  1.00 85.25           C  
ANISOU 1924  CG1 VAL A 257    11296   5092  16004   -260    970    -18       C  
ATOM   1925  CG2 VAL A 257     587.820  -6.613 198.353  1.00 81.70           C  
ANISOU 1925  CG2 VAL A 257    10839   5056  15149   -448    999    556       C  
ATOM   1926  N   THR A 258     585.466  -7.039 196.233  1.00 86.72           N  
ANISOU 1926  N   THR A 258    11561   5778  15608     44    862   1183       N  
ATOM   1927  CA  THR A 258     585.331  -8.222 195.424  1.00 85.16           C  
ANISOU 1927  CA  THR A 258    11320   5964  15074     63    842   1390       C  
ATOM   1928  C   THR A 258     586.632  -9.018 195.425  1.00 83.69           C  
ANISOU 1928  C   THR A 258    11085   6035  14678   -204    928   1373       C  
ATOM   1929  O   THR A 258     587.683  -8.549 195.872  1.00 84.08           O  
ANISOU 1929  O   THR A 258    11142   5943  14860   -414    995   1258       O  
ATOM   1930  CB  THR A 258     584.923  -7.867 193.977  1.00 85.76           C  
ANISOU 1930  CB  THR A 258    11526   5918  15140    158    779   1813       C  
ATOM   1931  OG1 THR A 258     585.693  -6.759 193.513  1.00 86.84           O  
ANISOU 1931  OG1 THR A 258    11819   5680  15496      6    831   2003       O  
ATOM   1932  CG2 THR A 258     583.462  -7.478 193.917  1.00 87.12           C  
ANISOU 1932  CG2 THR A 258    11691   5966  15446    476    655   1826       C  
ATOM   1933  N   ILE A 259     586.541 -10.252 194.957  1.00 80.49           N  
ANISOU 1933  N   ILE A 259    10613   6010  13961   -187    917   1463       N  
ATOM   1934  CA  ILE A 259     587.709 -11.103 194.828  1.00 78.98           C  
ANISOU 1934  CA  ILE A 259    10362   6077  13568   -404    990   1466       C  
ATOM   1935  C   ILE A 259     588.701 -10.407 193.921  1.00 80.30           C  
ANISOU 1935  C   ILE A 259    10634   6050  13826   -602   1070   1717       C  
ATOM   1936  O   ILE A 259     589.900 -10.349 194.205  1.00 80.34           O  
ANISOU 1936  O   ILE A 259    10594   6051  13882   -832   1154   1627       O  
ATOM   1937  CB  ILE A 259     587.339 -12.491 194.243  1.00 76.95           C  
ANISOU 1937  CB  ILE A 259    10040   6219  12981   -330    960   1562       C  
ATOM   1938  CG1 ILE A 259     586.264 -13.176 195.091  1.00 75.98           C  
ANISOU 1938  CG1 ILE A 259     9814   6274  12781   -145    898   1339       C  
ATOM   1939  CG2 ILE A 259     588.579 -13.358 194.076  1.00 75.43           C  
ANISOU 1939  CG2 ILE A 259     9781   6275  12606   -538   1037   1557       C  
ATOM   1940  CD1 ILE A 259     585.611 -14.284 194.361  1.00 74.66           C  
ANISOU 1940  CD1 ILE A 259     9601   6402  12364    -40    848   1467       C  
ATOM   1941  N   LEU A 260     588.166  -9.849 192.844  1.00104.33           N  
ANISOU 1941  N   LEU A 260    13814   8928  16898   -508   1042   2035       N  
ATOM   1942  CA  LEU A 260     588.962  -9.236 191.798  1.00105.04           C  
ANISOU 1942  CA  LEU A 260    14035   8850  17026   -683   1132   2346       C  
ATOM   1943  C   LEU A 260     589.824  -8.059 192.289  1.00106.55           C  
ANISOU 1943  C   LEU A 260    14270   8660  17555   -884   1216   2268       C  
ATOM   1944  O   LEU A 260     590.793  -7.686 191.648  1.00107.39           O  
ANISOU 1944  O   LEU A 260    14436   8667  17700  -1110   1335   2456       O  
ATOM   1945  CB  LEU A 260     588.030  -8.786 190.671  1.00106.04           C  
ANISOU 1945  CB  LEU A 260    14325   8847  17119   -499   1049   2698       C  
ATOM   1946  CG  LEU A 260     588.661  -8.456 189.320  1.00107.21           C  
ANISOU 1946  CG  LEU A 260    14635   8934  17164   -646   1138   3097       C  
ATOM   1947  CD1 LEU A 260     589.432  -9.649 188.805  1.00105.57           C  
ANISOU 1947  CD1 LEU A 260    14341   9147  16623   -794   1235   3119       C  
ATOM   1948  CD2 LEU A 260     587.592  -8.032 188.324  1.00109.47           C  
ANISOU 1948  CD2 LEU A 260    15092   9105  17398   -417   1007   3429       C  
ATOM   1949  N   GLU A 261     589.474  -7.484 193.431  1.00108.14           N  
ANISOU 1949  N   GLU A 261    14436   8652  18001   -812   1163   1975       N  
ATOM   1950  CA  GLU A 261     590.235  -6.379 193.983  1.00109.65           C  
ANISOU 1950  CA  GLU A 261    14659   8472  18530   -999   1225   1848       C  
ATOM   1951  C   GLU A 261     591.337  -6.891 194.901  1.00109.00           C  
ANISOU 1951  C   GLU A 261    14409   8588  18417  -1214   1277   1529       C  
ATOM   1952  O   GLU A 261     592.479  -6.419 194.837  1.00109.78           O  
ANISOU 1952  O   GLU A 261    14494   8547  18671  -1480   1373   1532       O  
ATOM   1953  CB  GLU A 261     589.299  -5.439 194.719  1.00111.07           C  
ANISOU 1953  CB  GLU A 261    14893   8311  19000   -803   1137   1674       C  
ATOM   1954  CG  GLU A 261     588.118  -5.066 193.853  1.00112.21           C  
ANISOU 1954  CG  GLU A 261    15170   8302  19161   -543   1049   1972       C  
ATOM   1955  CD  GLU A 261     587.154  -4.084 194.506  1.00113.72           C  
ANISOU 1955  CD  GLU A 261    15404   8128  19677   -322    963   1806       C  
ATOM   1956  OE1 GLU A 261     587.612  -3.117 195.154  1.00115.27           O  
ANISOU 1956  OE1 GLU A 261    15635   7968  20194   -434   1002   1623       O  
ATOM   1957  OE2 GLU A 261     585.928  -4.267 194.351  1.00113.49           O  
ANISOU 1957  OE2 GLU A 261    15363   8162  19597    -33    855   1847       O  
ATOM   1958  N   LEU A 262     590.976  -7.857 195.748  1.00 89.38           N  
ANISOU 1958  N   LEU A 262    11796   6427  15737  -1097   1209   1262       N  
ATOM   1959  CA  LEU A 262     591.932  -8.607 196.568  1.00 88.66           C  
ANISOU 1959  CA  LEU A 262    11545   6605  15535  -1254   1222    988       C  
ATOM   1960  C   LEU A 262     593.263  -8.850 195.830  1.00 88.23           C  
ANISOU 1960  C   LEU A 262    11435   6650  15438  -1520   1332   1145       C  
ATOM   1961  O   LEU A 262     594.350  -8.497 196.313  1.00 89.00           O  
ANISOU 1961  O   LEU A 262    11449   6667  15701  -1745   1372    975       O  
ATOM   1962  CB  LEU A 262     591.315  -9.947 196.988  1.00 87.19           C  
ANISOU 1962  CB  LEU A 262    11265   6829  15032  -1084   1154    870       C  
ATOM   1963  CG  LEU A 262     591.133 -10.228 198.477  1.00 87.49           C  
ANISOU 1963  CG  LEU A 262    11222   6978  15044  -1024   1087    479       C  
ATOM   1964  CD1 LEU A 262     590.113  -9.299 199.080  1.00 88.89           C  
ANISOU 1964  CD1 LEU A 262    11475   6876  15424   -856   1050    334       C  
ATOM   1965  CD2 LEU A 262     590.707 -11.651 198.674  1.00 86.10           C  
ANISOU 1965  CD2 LEU A 262    10965   7209  14538   -906   1049    444       C  
ATOM   1966  N   PHE A 263     593.147  -9.424 194.634  1.00 94.14           N  
ANISOU 1966  N   PHE A 263    12225   7573  15970  -1491   1381   1460       N  
ATOM   1967  CA  PHE A 263     594.287  -9.734 193.773  1.00 93.75           C  
ANISOU 1967  CA  PHE A 263    12126   7655  15840  -1717   1513   1635       C  
ATOM   1968  C   PHE A 263     595.051  -8.528 193.228  1.00 95.47           C  
ANISOU 1968  C   PHE A 263    12426   7516  16332  -1953   1642   1809       C  
ATOM   1969  O   PHE A 263     596.285  -8.569 193.154  1.00 95.71           O  
ANISOU 1969  O   PHE A 263    12339   7600  16425  -2209   1755   1767       O  
ATOM   1970  CB  PHE A 263     593.818 -10.565 192.585  1.00 92.51           C  
ANISOU 1970  CB  PHE A 263    12025   7757  15369  -1604   1534   1926       C  
ATOM   1971  CG  PHE A 263     593.229 -11.877 192.961  1.00 90.79           C  
ANISOU 1971  CG  PHE A 263    11712   7905  14880  -1421   1434   1780       C  
ATOM   1972  CD1 PHE A 263     593.653 -12.544 194.091  1.00 90.11           C  
ANISOU 1972  CD1 PHE A 263    11468   8001  14769  -1446   1384   1456       C  
ATOM   1973  CD2 PHE A 263     592.257 -12.455 192.175  1.00 90.06           C  
ANISOU 1973  CD2 PHE A 263    11691   7970  14556  -1229   1384   1973       C  
ATOM   1974  CE1 PHE A 263     593.104 -13.765 194.429  1.00 88.66           C  
ANISOU 1974  CE1 PHE A 263    11215   8131  14342  -1287   1303   1349       C  
ATOM   1975  CE2 PHE A 263     591.708 -13.671 192.510  1.00 88.59           C  
ANISOU 1975  CE2 PHE A 263    11414   8099  14146  -1081   1302   1838       C  
ATOM   1976  CZ  PHE A 263     592.128 -14.326 193.645  1.00 87.85           C  
ANISOU 1976  CZ  PHE A 263    11177   8163  14038  -1113   1270   1535       C  
ATOM   1977  N   ARG A 264     594.318  -7.489 192.813  1.00107.82           N  
ANISOU 1977  N   ARG A 264    14184   8718  18064  -1867   1629   2016       N  
ATOM   1978  CA  ARG A 264     594.919  -6.322 192.167  1.00109.63           C  
ANISOU 1978  CA  ARG A 264    14536   8570  18549  -2081   1759   2250       C  
ATOM   1979  C   ARG A 264     595.645  -5.460 193.190  1.00110.86           C  
ANISOU 1979  C   ARG A 264    14614   8430  19078  -2276   1772   1951       C  
ATOM   1980  O   ARG A 264     596.560  -4.720 192.848  1.00112.36           O  
ANISOU 1980  O   ARG A 264    14818   8383  19491  -2549   1909   2052       O  
ATOM   1981  CB  ARG A 264     593.872  -5.461 191.440  1.00110.98           C  
ANISOU 1981  CB  ARG A 264    14956   8413  18800  -1903   1713   2574       C  
ATOM   1982  CG  ARG A 264     592.993  -6.145 190.391  1.00110.32           C  
ANISOU 1982  CG  ARG A 264    14973   8575  18367  -1684   1660   2879       C  
ATOM   1983  CD  ARG A 264     593.653  -6.353 189.035  1.00110.48           C  
ANISOU 1983  CD  ARG A 264    15076   8729  18173  -1854   1819   3249       C  
ATOM   1984  NE  ARG A 264     594.071  -7.745 188.848  1.00108.38           N  
ANISOU 1984  NE  ARG A 264    14646   8970  17564  -1880   1859   3156       N  
ATOM   1985  CZ  ARG A 264     594.517  -8.270 187.705  1.00108.22           C  
ANISOU 1985  CZ  ARG A 264    14662   9192  17265  -1976   1986   3411       C  
ATOM   1986  NH1 ARG A 264     594.616  -7.526 186.604  1.00110.33           N  
ANISOU 1986  NH1 ARG A 264    15140   9263  17517  -2066   2094   3807       N  
ATOM   1987  NH2 ARG A 264     594.865  -9.553 187.667  1.00106.27           N  
ANISOU 1987  NH2 ARG A 264    14249   9384  16746  -1977   2009   3269       N  
ATOM   1988  N   SER A 265     595.228  -5.554 194.448  1.00112.59           N  
ANISOU 1988  N   SER A 265    14752   8669  19359  -2144   1634   1575       N  
ATOM   1989  CA  SER A 265     595.786  -4.699 195.491  1.00114.01           C  
ANISOU 1989  CA  SER A 265    14873   8564  19882  -2299   1615   1249       C  
ATOM   1990  C   SER A 265     596.944  -5.327 196.239  1.00113.59           C  
ANISOU 1990  C   SER A 265    14583   8787  19789  -2497   1615    936       C  
ATOM   1991  O   SER A 265     596.834  -6.438 196.760  1.00112.16           O  
ANISOU 1991  O   SER A 265    14282   9000  19334  -2378   1530    761       O  
ATOM   1992  CB  SER A 265     594.720  -4.319 196.509  1.00114.45           C  
ANISOU 1992  CB  SER A 265    14981   8464  20041  -2053   1470    980       C  
ATOM   1993  OG  SER A 265     595.339  -3.917 197.721  1.00115.77           O  
ANISOU 1993  OG  SER A 265    15040   8530  20417  -2190   1426    563       O  
ATOM   1994  N   PRO A 266     598.057  -4.597 196.324  1.00 93.28           N  
ANISOU 1994  N   PRO A 266    11939   5993  17509  -2802   1702    859       N  
ATOM   1995  CA  PRO A 266     599.207  -5.037 197.108  1.00 92.87           C  
ANISOU 1995  CA  PRO A 266    11642   6162  17481  -2997   1674    527       C  
ATOM   1996  C   PRO A 266     598.910  -5.049 198.608  1.00 92.07           C  
ANISOU 1996  C   PRO A 266    11483   6092  17406  -2879   1488     74       C  
ATOM   1997  O   PRO A 266     599.583  -5.778 199.337  1.00 90.64           O  
ANISOU 1997  O   PRO A 266    11113   6220  17107  -2933   1406   -196       O  
ATOM   1998  CB  PRO A 266     600.267  -3.996 196.771  1.00 97.20           C  
ANISOU 1998  CB  PRO A 266    12156   6375  18399  -3344   1814    575       C  
ATOM   1999  CG  PRO A 266     599.489  -2.796 196.379  1.00100.08           C  
ANISOU 1999  CG  PRO A 266    12786   6344  18896  -3245   1814    774       C  
ATOM   2000  CD  PRO A 266     598.320  -3.319 195.642  1.00 97.65           C  
ANISOU 2000  CD  PRO A 266    12636   6091  18376  -2982   1823   1093       C  
ATOM   2001  N   ALA A 267     597.923  -4.273 199.054  1.00 93.19           N  
ANISOU 2001  N   ALA A 267    11788   5932  17690  -2711   1422     -9       N  
ATOM   2002  CA  ALA A 267     597.549  -4.246 200.466  1.00 92.76           C  
ANISOU 2002  CA  ALA A 267    11701   5912  17631  -2587   1267   -444       C  
ATOM   2003  C   ALA A 267     597.118  -5.624 200.921  1.00 88.52           C  
ANISOU 2003  C   ALA A 267    11092   5869  16675  -2378   1174   -531       C  
ATOM   2004  O   ALA A 267     597.374  -6.028 202.058  1.00 87.77           O  
ANISOU 2004  O   ALA A 267    10895   5978  16475  -2368   1057   -883       O  
ATOM   2005  CB  ALA A 267     596.440  -3.257 200.705  1.00 94.65           C  
ANISOU 2005  CB  ALA A 267    12127   5762  18074  -2405   1240   -483       C  
ATOM   2006  N   TYR A 268     596.466  -6.341 200.009  1.00 90.83           N  
ANISOU 2006  N   TYR A 268    11444   6344  16722  -2218   1223   -201       N  
ATOM   2007  CA  TYR A 268     595.840  -7.620 200.307  1.00 89.31           C  
ANISOU 2007  CA  TYR A 268    11214   6567  16152  -2000   1149   -234       C  
ATOM   2008  C   TYR A 268     596.630  -8.784 199.772  1.00 87.77           C  
ANISOU 2008  C   TYR A 268    10881   6746  15719  -2088   1181   -104       C  
ATOM   2009  O   TYR A 268     596.379  -9.935 200.147  1.00 86.63           O  
ANISOU 2009  O   TYR A 268    10678   6956  15280  -1952   1110   -174       O  
ATOM   2010  CB  TYR A 268     594.446  -7.691 199.696  1.00 88.63           C  
ANISOU 2010  CB  TYR A 268    11273   6441  15959  -1738   1162      9       C  
ATOM   2011  CG  TYR A 268     593.401  -6.877 200.389  1.00 89.74           C  
ANISOU 2011  CG  TYR A 268    11520   6317  16261  -1558   1109   -167       C  
ATOM   2012  CD1 TYR A 268     593.320  -6.840 201.773  1.00 90.52           C  
ANISOU 2012  CD1 TYR A 268    11574   6468  16353  -1518   1028   -577       C  
ATOM   2013  CD2 TYR A 268     592.480  -6.160 199.652  1.00 90.12           C  
ANISOU 2013  CD2 TYR A 268    11712   6074  16454  -1414   1137     73       C  
ATOM   2014  CE1 TYR A 268     592.348  -6.106 202.399  1.00 91.56           C  
ANISOU 2014  CE1 TYR A 268    11792   6369  16627  -1346   1001   -762       C  
ATOM   2015  CE2 TYR A 268     591.512  -5.420 200.260  1.00 91.17           C  
ANISOU 2015  CE2 TYR A 268    11922   5959  16758  -1229   1093    -99       C  
ATOM   2016  CZ  TYR A 268     591.441  -5.386 201.634  1.00 91.85           C  
ANISOU 2016  CZ  TYR A 268    11953   6101  16845  -1197   1037   -527       C  
ATOM   2017  OH  TYR A 268     590.460  -4.620 202.240  1.00 92.98           O  
ANISOU 2017  OH  TYR A 268    12164   5996  17166  -1006   1013   -725       O  
ATOM   2018  N   ARG A 269     597.543  -8.485 198.856  1.00137.39           N  
ANISOU 2018  N   ARG A 269    17123  12941  22137  -2309   1301     97       N  
ATOM   2019  CA  ARG A 269     598.226  -9.514 198.103  1.00135.96           C  
ANISOU 2019  CA  ARG A 269    16822  13087  21748  -2380   1369    263       C  
ATOM   2020  C   ARG A 269     598.991 -10.434 199.024  1.00135.70           C  
ANISOU 2020  C   ARG A 269    16591  13381  21589  -2413   1260    -31       C  
ATOM   2021  O   ARG A 269     599.247 -11.588 198.692  1.00134.27           O  
ANISOU 2021  O   ARG A 269    16315  13533  21167  -2367   1263     41       O  
ATOM   2022  CB  ARG A 269     599.157  -8.890 197.090  1.00136.59           C  
ANISOU 2022  CB  ARG A 269    16877  12994  22027  -2644   1542    484       C  
ATOM   2023  CG  ARG A 269     598.945  -9.398 195.705  1.00135.39           C  
ANISOU 2023  CG  ARG A 269    16795  12980  21666  -2604   1670    868       C  
ATOM   2024  CD  ARG A 269     600.004  -8.804 194.829  1.00136.45           C  
ANISOU 2024  CD  ARG A 269    16887  12972  21984  -2899   1864   1053       C  
ATOM   2025  NE  ARG A 269     600.012  -9.387 193.497  1.00135.33           N  
ANISOU 2025  NE  ARG A 269    16791  13026  21602  -2893   2007   1393       N  
ATOM   2026  CZ  ARG A 269     601.056  -9.338 192.675  1.00135.95           C  
ANISOU 2026  CZ  ARG A 269    16779  13151  21724  -3140   2204   1539       C  
ATOM   2027  NH1 ARG A 269     602.182  -8.742 193.059  1.00137.63           N  
ANISOU 2027  NH1 ARG A 269    16830  13224  22239  -3420   2276   1374       N  
ATOM   2028  NH2 ARG A 269     600.981  -9.891 191.471  1.00135.09           N  
ANISOU 2028  NH2 ARG A 269    16732  13241  21355  -3115   2335   1834       N  
ATOM   2029  N   GLN A 270     599.344  -9.923 200.194  1.00 79.80           N  
ANISOU 2029  N   GLN A 270     9455   6199  14668  -2482   1151   -371       N  
ATOM   2030  CA  GLN A 270     600.027 -10.750 201.188  1.00 78.74           C  
ANISOU 2030  CA  GLN A 270     9149   6369  14398  -2491   1006   -662       C  
ATOM   2031  C   GLN A 270     599.099 -11.538 202.144  1.00 78.30           C  
ANISOU 2031  C   GLN A 270     9166   6536  14049  -2233    865   -813       C  
ATOM   2032  O   GLN A 270     599.299 -12.735 202.318  1.00 77.47           O  
ANISOU 2032  O   GLN A 270     8976   6766  13693  -2154    799   -824       O  
ATOM   2033  CB  GLN A 270     601.004  -9.893 202.006  1.00 81.99           C  
ANISOU 2033  CB  GLN A 270     9444   6611  15098  -2712    936   -979       C  
ATOM   2034  CG  GLN A 270     601.731 -10.662 203.103  1.00 81.49           C  
ANISOU 2034  CG  GLN A 270     9208   6856  14898  -2713    747  -1295       C  
ATOM   2035  CD  GLN A 270     602.663 -11.737 202.551  1.00 80.34           C  
ANISOU 2035  CD  GLN A 270     8860   7029  14639  -2769    765  -1189       C  
ATOM   2036  OE1 GLN A 270     602.791 -12.830 203.128  1.00 80.20           O  
ANISOU 2036  OE1 GLN A 270     8768   7333  14372  -2641    625  -1293       O  
ATOM   2037  NE2 GLN A 270     603.322 -11.430 201.430  1.00 81.52           N  
ANISOU 2037  NE2 GLN A 270     8921   7081  14972  -2960    946   -980       N  
ATOM   2038  N   PRO A 271     598.101 -10.875 202.783  1.00 76.76           N  
ANISOU 2038  N   PRO A 271     9123   6149  13894  -2105    830   -936       N  
ATOM   2039  CA  PRO A 271     597.150 -11.619 203.632  1.00 74.56           C  
ANISOU 2039  CA  PRO A 271     8915   6086  13327  -1872    738  -1057       C  
ATOM   2040  C   PRO A 271     596.449 -12.745 202.872  1.00 71.32           C  
ANISOU 2040  C   PRO A 271     8536   5913  12649  -1704    788   -776       C  
ATOM   2041  O   PRO A 271     596.066 -13.802 203.398  1.00 69.10           O  
ANISOU 2041  O   PRO A 271     8251   5912  12090  -1565    719   -827       O  
ATOM   2042  CB  PRO A 271     596.135 -10.550 204.034  1.00 76.21           C  
ANISOU 2042  CB  PRO A 271     9276   5990  13688  -1772    757  -1162       C  
ATOM   2043  CG  PRO A 271     596.869  -9.275 203.932  1.00 79.69           C  
ANISOU 2043  CG  PRO A 271     9701   6078  14499  -1985    787  -1246       C  
ATOM   2044  CD  PRO A 271     597.828  -9.419 202.814  1.00 79.84           C  
ANISOU 2044  CD  PRO A 271     9619   6108  14607  -2173    877   -991       C  
ATOM   2045  N   ILE A 272     596.282 -12.489 201.586  1.00 71.36           N  
ANISOU 2045  N   ILE A 272     8583   5790  12742  -1728    910   -469       N  
ATOM   2046  CA  ILE A 272     595.604 -13.433 200.739  1.00 68.76           C  
ANISOU 2046  CA  ILE A 272     8287   5655  12183  -1582    956   -207       C  
ATOM   2047  C   ILE A 272     596.554 -14.561 200.387  1.00 67.25           C  
ANISOU 2047  C   ILE A 272     7952   5764  11836  -1657    953   -154       C  
ATOM   2048  O   ILE A 272     596.133 -15.691 200.175  1.00 64.77           O  
ANISOU 2048  O   ILE A 272     7634   5699  11278  -1527    937    -63       O  
ATOM   2049  CB  ILE A 272     595.063 -12.758 199.477  1.00 69.68           C  
ANISOU 2049  CB  ILE A 272     8515   5544  12416  -1566   1069    103       C  
ATOM   2050  CG1 ILE A 272     593.912 -13.584 198.928  1.00 67.24           C  
ANISOU 2050  CG1 ILE A 272     8271   5409  11869  -1350   1069    290       C  
ATOM   2051  CG2 ILE A 272     596.156 -12.511 198.450  1.00 71.10           C  
ANISOU 2051  CG2 ILE A 272     8635   5669  12710  -1783   1180    293       C  
ATOM   2052  CD1 ILE A 272     594.048 -13.853 197.491  1.00 66.97           C  
ANISOU 2052  CD1 ILE A 272     8255   5426  11764  -1384   1158    613       C  
ATOM   2053  N   LEU A 273     597.848 -14.255 200.344  1.00 75.44           N  
ANISOU 2053  N   LEU A 273     8857   6769  13035  -1870    968   -227       N  
ATOM   2054  CA  LEU A 273     598.853 -15.272 200.071  1.00 74.65           C  
ANISOU 2054  CA  LEU A 273     8588   6946  12830  -1939    962   -216       C  
ATOM   2055  C   LEU A 273     598.785 -16.284 201.188  1.00 74.93           C  
ANISOU 2055  C   LEU A 273     8581   7239  12650  -1809    799   -421       C  
ATOM   2056  O   LEU A 273     598.826 -17.474 200.951  1.00 73.85           O  
ANISOU 2056  O   LEU A 273     8395   7353  12311  -1720    779   -345       O  
ATOM   2057  CB  LEU A 273     600.257 -14.650 199.964  1.00 75.75           C  
ANISOU 2057  CB  LEU A 273     8561   6994  13228  -2199   1003   -305       C  
ATOM   2058  CG  LEU A 273     601.514 -15.476 200.301  1.00 75.99           C  
ANISOU 2058  CG  LEU A 273     8354   7285  13233  -2282    925   -464       C  
ATOM   2059  CD1 LEU A 273     601.835 -16.474 199.204  1.00 74.25           C  
ANISOU 2059  CD1 LEU A 273     8049   7288  12874  -2262   1032   -254       C  
ATOM   2060  CD2 LEU A 273     602.719 -14.591 200.588  1.00 77.75           C  
ANISOU 2060  CD2 LEU A 273     8411   7366  13766  -2537    923   -648       C  
ATOM   2061  N   ILE A 274     598.646 -15.798 202.410  1.00 67.35           N  
ANISOU 2061  N   ILE A 274     7659   6206  11726  -1795    684   -678       N  
ATOM   2062  CA  ILE A 274     598.608 -16.670 203.561  1.00 66.26           C  
ANISOU 2062  CA  ILE A 274     7508   6305  11363  -1682    526   -869       C  
ATOM   2063  C   ILE A 274     597.345 -17.547 203.609  1.00 63.63           C  
ANISOU 2063  C   ILE A 274     7306   6112  10760  -1464    536   -751       C  
ATOM   2064  O   ILE A 274     597.431 -18.783 203.639  1.00 61.82           O  
ANISOU 2064  O   ILE A 274     7037   6128  10324  -1381    486   -697       O  
ATOM   2065  CB  ILE A 274     598.705 -15.857 204.822  1.00 68.41           C  
ANISOU 2065  CB  ILE A 274     7811   6468  11714  -1724    413  -1178       C  
ATOM   2066  CG1 ILE A 274     600.091 -15.259 204.915  1.00 71.02           C  
ANISOU 2066  CG1 ILE A 274     7969   6726  12291  -1948    362  -1336       C  
ATOM   2067  CG2 ILE A 274     598.433 -16.716 206.034  1.00 67.48           C  
ANISOU 2067  CG2 ILE A 274     7738   6594  11307  -1585    263  -1345       C  
ATOM   2068  CD1 ILE A 274     600.339 -14.615 206.218  1.00 73.32           C  
ANISOU 2068  CD1 ILE A 274     8268   6959  12631  -1995    213  -1683       C  
ATOM   2069  N   ALA A 275     596.178 -16.908 203.618  1.00 89.23           N  
ANISOU 2069  N   ALA A 275    10691   9185  14028  -1372    602   -719       N  
ATOM   2070  CA  ALA A 275     594.898 -17.624 203.647  1.00 88.53           C  
ANISOU 2070  CA  ALA A 275    10704   9209  13725  -1179    628   -621       C  
ATOM   2071  C   ALA A 275     594.839 -18.743 202.620  1.00 86.34           C  
ANISOU 2071  C   ALA A 275    10386   9109  13311  -1129    674   -376       C  
ATOM   2072  O   ALA A 275     594.439 -19.861 202.939  1.00 86.03           O  
ANISOU 2072  O   ALA A 275    10359   9276  13052  -1021    634   -362       O  
ATOM   2073  CB  ALA A 275     593.764 -16.672 203.414  1.00 88.67           C  
ANISOU 2073  CB  ALA A 275    10835   8992  13865  -1100    712   -576       C  
ATOM   2074  N   VAL A 276     595.247 -18.438 201.392  1.00 59.69           N  
ANISOU 2074  N   VAL A 276     6970   5647  10064  -1216    764   -187       N  
ATOM   2075  CA  VAL A 276     595.193 -19.408 200.310  1.00 57.95           C  
ANISOU 2075  CA  VAL A 276     6718   5586   9714  -1174    819     31       C  
ATOM   2076  C   VAL A 276     596.093 -20.593 200.569  1.00 56.99           C  
ANISOU 2076  C   VAL A 276     6476   5710   9469  -1189    747    -34       C  
ATOM   2077  O   VAL A 276     595.653 -21.745 200.435  1.00 55.10           O  
ANISOU 2077  O   VAL A 276     6248   5647   9042  -1075    729     35       O  
ATOM   2078  CB  VAL A 276     595.591 -18.805 198.962  1.00 59.03           C  
ANISOU 2078  CB  VAL A 276     6841   5599   9987  -1284    941    238       C  
ATOM   2079  CG1 VAL A 276     596.040 -19.909 198.001  1.00 57.73           C  
ANISOU 2079  CG1 VAL A 276     6597   5655   9682  -1285    988    380       C  
ATOM   2080  CG2 VAL A 276     594.454 -18.003 198.368  1.00 59.52           C  
ANISOU 2080  CG2 VAL A 276     7044   5462  10107  -1204   1002    398       C  
ATOM   2081  N   VAL A 277     597.346 -20.324 200.924  1.00 80.02           N  
ANISOU 2081  N   VAL A 277     9269   8627  12509  -1326    699   -171       N  
ATOM   2082  CA  VAL A 277     598.319 -21.393 201.149  1.00 80.20           C  
ANISOU 2082  CA  VAL A 277     9149   8870  12452  -1332    612   -241       C  
ATOM   2083  C   VAL A 277     597.813 -22.366 202.197  1.00 81.09           C  
ANISOU 2083  C   VAL A 277     9328   9140  12344  -1181    481   -328       C  
ATOM   2084  O   VAL A 277     597.886 -23.591 202.020  1.00 80.46           O  
ANISOU 2084  O   VAL A 277     9214   9233  12122  -1096    448   -264       O  
ATOM   2085  CB  VAL A 277     599.677 -20.842 201.595  1.00 81.76           C  
ANISOU 2085  CB  VAL A 277     9186   9039  12838  -1494    547   -423       C  
ATOM   2086  CG1 VAL A 277     600.452 -21.892 202.404  1.00 82.65           C  
ANISOU 2086  CG1 VAL A 277     9182   9375  12845  -1440    373   -567       C  
ATOM   2087  CG2 VAL A 277     600.467 -20.372 200.384  1.00 80.87           C  
ANISOU 2087  CG2 VAL A 277     8955   8857  12914  -1657    701   -303       C  
ATOM   2088  N   LEU A 278     597.287 -21.795 203.277  1.00 72.04           N  
ANISOU 2088  N   LEU A 278     8283   7920  11169  -1153    418   -476       N  
ATOM   2089  CA  LEU A 278     596.622 -22.547 204.332  1.00 73.39           C  
ANISOU 2089  CA  LEU A 278     8557   8220  11109  -1021    327   -546       C  
ATOM   2090  C   LEU A 278     595.568 -23.549 203.820  1.00 71.72           C  
ANISOU 2090  C   LEU A 278     8422   8097  10731   -889    399   -360       C  
ATOM   2091  O   LEU A 278     595.333 -24.578 204.445  1.00 72.45           O  
ANISOU 2091  O   LEU A 278     8558   8335  10632   -800    330   -366       O  
ATOM   2092  CB  LEU A 278     595.971 -21.572 205.306  1.00 75.22           C  
ANISOU 2092  CB  LEU A 278     8903   8331  11346  -1013    317   -713       C  
ATOM   2093  CG  LEU A 278     596.914 -20.801 206.221  1.00 77.60           C  
ANISOU 2093  CG  LEU A 278     9152   8587  11744  -1121    196   -964       C  
ATOM   2094  CD1 LEU A 278     596.176 -19.637 206.877  1.00 78.77           C  
ANISOU 2094  CD1 LEU A 278     9417   8558  11953  -1121    233  -1125       C  
ATOM   2095  CD2 LEU A 278     597.478 -21.738 207.263  1.00 79.59           C  
ANISOU 2095  CD2 LEU A 278     9392   9064  11787  -1073     16  -1079       C  
ATOM   2096  N   GLN A 279     594.941 -23.246 202.690  1.00 91.98           N  
ANISOU 2096  N   GLN A 279    11006  10569  13372   -883    529   -195       N  
ATOM   2097  CA  GLN A 279     593.980 -24.162 202.103  1.00 90.19           C  
ANISOU 2097  CA  GLN A 279    10829  10427  13013   -773    585    -38       C  
ATOM   2098  C   GLN A 279     594.700 -25.288 201.393  1.00 88.61           C  
ANISOU 2098  C   GLN A 279    10534  10370  12763   -773    569     51       C  
ATOM   2099  O   GLN A 279     594.292 -26.437 201.476  1.00 88.06           O  
ANISOU 2099  O   GLN A 279    10491  10419  12550   -685    544     98       O  
ATOM   2100  CB  GLN A 279     593.055 -23.439 201.132  1.00 88.74           C  
ANISOU 2100  CB  GLN A 279    10695  10107  12916   -751    698    100       C  
ATOM   2101  CG  GLN A 279     591.599 -23.453 201.555  1.00 89.39           C  
ANISOU 2101  CG  GLN A 279    10872  10171  12920   -633    726     96       C  
ATOM   2102  CD  GLN A 279     591.335 -22.608 202.797  1.00 91.37           C  
ANISOU 2102  CD  GLN A 279    11183  10330  13204   -629    705    -97       C  
ATOM   2103  OE1 GLN A 279     592.155 -21.772 203.184  1.00 93.15           O  
ANISOU 2103  OE1 GLN A 279    11390  10456  13548   -721    669   -218       O  
ATOM   2104  NE2 GLN A 279     590.193 -22.831 203.431  1.00 91.08           N  
ANISOU 2104  NE2 GLN A 279    11210  10332  13065   -529    735   -143       N  
ATOM   2105  N   LEU A 280     595.774 -24.956 200.689  1.00 55.58           N  
ANISOU 2105  N   LEU A 280     6238   6169   8713   -878    597     67       N  
ATOM   2106  CA  LEU A 280     596.621 -25.983 200.065  1.00 54.64           C  
ANISOU 2106  CA  LEU A 280     6000   6191   8568   -878    589    108       C  
ATOM   2107  C   LEU A 280     597.162 -26.942 201.128  1.00 56.46           C  
ANISOU 2107  C   LEU A 280     6194   6548   8710   -817    433    -10       C  
ATOM   2108  O   LEU A 280     597.292 -28.142 200.910  1.00 55.85           O  
ANISOU 2108  O   LEU A 280     6086   6584   8549   -740    401     33       O  
ATOM   2109  CB  LEU A 280     597.784 -25.332 199.286  1.00 54.58           C  
ANISOU 2109  CB  LEU A 280     5854   6147   8737  -1022    662    111       C  
ATOM   2110  CG  LEU A 280     597.426 -24.535 198.027  1.00 53.10           C  
ANISOU 2110  CG  LEU A 280     5710   5852   8616  -1089    824    277       C  
ATOM   2111  CD1 LEU A 280     598.528 -24.672 196.992  1.00 54.08           C  
ANISOU 2111  CD1 LEU A 280     5689   6047   8813  -1193    926    325       C  
ATOM   2112  CD2 LEU A 280     596.088 -24.956 197.416  1.00 51.53           C  
ANISOU 2112  CD2 LEU A 280     5641   5669   8271   -967    867    426       C  
ATOM   2113  N   SER A 281     597.481 -26.356 202.278  1.00 60.70           N  
ANISOU 2113  N   SER A 281     6743   7052   9267   -850    330   -163       N  
ATOM   2114  CA  SER A 281     598.000 -27.058 203.438  1.00 63.20           C  
ANISOU 2114  CA  SER A 281     7051   7481   9481   -794    153   -278       C  
ATOM   2115  C   SER A 281     597.012 -28.069 203.966  1.00 63.78           C  
ANISOU 2115  C   SER A 281     7272   7623   9338   -664    127   -207       C  
ATOM   2116  O   SER A 281     597.406 -29.029 204.606  1.00 65.46           O  
ANISOU 2116  O   SER A 281     7488   7938   9444   -592     -4   -226       O  
ATOM   2117  CB  SER A 281     598.353 -26.055 204.548  1.00 65.70           C  
ANISOU 2117  CB  SER A 281     7381   7745   9837   -862     54   -469       C  
ATOM   2118  OG  SER A 281     597.684 -26.356 205.767  1.00 67.93           O  
ANISOU 2118  OG  SER A 281     7819   8080   9910   -776    -33   -528       O  
ATOM   2119  N   GLN A 282     595.726 -27.820 203.724  1.00 74.16           N  
ANISOU 2119  N   GLN A 282     8705   8872  10601   -636    248   -125       N  
ATOM   2120  CA  GLN A 282     594.649 -28.667 204.227  1.00 74.65           C  
ANISOU 2120  CA  GLN A 282     8899   8985  10479   -539    258    -62       C  
ATOM   2121  C   GLN A 282     594.386 -29.856 203.289  1.00 72.06           C  
ANISOU 2121  C   GLN A 282     8547   8708  10125   -482    303     83       C  
ATOM   2122  O   GLN A 282     594.324 -31.001 203.736  1.00 73.24           O  
ANISOU 2122  O   GLN A 282     8742   8927  10157   -414    239    119       O  
ATOM   2123  CB  GLN A 282     593.368 -27.859 204.411  1.00 74.33           C  
ANISOU 2123  CB  GLN A 282     8962   8859  10422   -532    369    -68       C  
ATOM   2124  CG  GLN A 282     592.373 -28.540 205.328  1.00 75.87           C  
ANISOU 2124  CG  GLN A 282     9286   9119  10422   -461    381    -60       C  
ATOM   2125  CD  GLN A 282     590.918 -28.138 205.084  1.00 74.11           C  
ANISOU 2125  CD  GLN A 282     9115   8835  10209   -429    525    -21       C  
ATOM   2126  OE1 GLN A 282     590.446 -28.113 203.944  1.00 71.44           O  
ANISOU 2126  OE1 GLN A 282     8725   8451   9968   -418    599     86       O  
ATOM   2127  NE2 GLN A 282     590.198 -27.842 206.167  1.00 75.86           N  
ANISOU 2127  NE2 GLN A 282     9432   9068  10321   -408    560   -116       N  
ATOM   2128  N   GLN A 283     594.250 -29.580 201.993  1.00 75.08           N  
ANISOU 2128  N   GLN A 283     8866   9049  10611   -511    410    165       N  
ATOM   2129  CA  GLN A 283     594.035 -30.621 200.991  1.00 72.74           C  
ANISOU 2129  CA  GLN A 283     8539   8805  10293   -465    454    272       C  
ATOM   2130  C   GLN A 283     595.321 -31.310 200.487  1.00 73.02           C  
ANISOU 2130  C   GLN A 283     8442   8911  10390   -467    404    252       C  
ATOM   2131  O   GLN A 283     595.310 -32.523 200.256  1.00 72.98           O  
ANISOU 2131  O   GLN A 283     8432   8959  10337   -398    378    287       O  
ATOM   2132  CB  GLN A 283     593.277 -30.041 199.806  1.00 69.90           C  
ANISOU 2132  CB  GLN A 283     8183   8393   9981   -485    579    365       C  
ATOM   2133  CG  GLN A 283     591.973 -29.394 200.238  1.00 69.78           C  
ANISOU 2133  CG  GLN A 283     8268   8307   9938   -460    625    375       C  
ATOM   2134  CD  GLN A 283     590.950 -30.427 200.748  1.00 69.46           C  
ANISOU 2134  CD  GLN A 283     8298   8318   9774   -389    622    398       C  
ATOM   2135  OE1 GLN A 283     590.507 -31.289 199.985  1.00 67.62           O  
ANISOU 2135  OE1 GLN A 283     8049   8127   9515   -357    647    471       O  
ATOM   2136  NE2 GLN A 283     590.620 -30.378 202.046  1.00 71.60           N  
ANISOU 2136  NE2 GLN A 283     8647   8592   9966   -375    597    327       N  
ATOM   2137  N   LEU A 284     596.416 -30.566 200.281  1.00 56.40           N  
ANISOU 2137  N   LEU A 284     6220   6799   8411   -548    400    186       N  
ATOM   2138  CA  LEU A 284     597.662 -31.186 199.799  1.00 56.75           C  
ANISOU 2138  CA  LEU A 284     6104   6923   8537   -548    369    144       C  
ATOM   2139  C   LEU A 284     598.434 -31.824 200.944  1.00 59.66           C  
ANISOU 2139  C   LEU A 284     6435   7345   8890   -486    184     47       C  
ATOM   2140  O   LEU A 284     599.585 -32.201 200.779  1.00 60.35           O  
ANISOU 2140  O   LEU A 284     6361   7494   9076   -478    125    -22       O  
ATOM   2141  CB  LEU A 284     598.546 -30.178 199.075  1.00 56.29           C  
ANISOU 2141  CB  LEU A 284     5909   6845   8633   -675    458    114       C  
ATOM   2142  CG  LEU A 284     598.071 -29.751 197.693  1.00 53.93           C  
ANISOU 2142  CG  LEU A 284     5632   6520   8340   -727    637    237       C  
ATOM   2143  CD1 LEU A 284     599.105 -28.855 197.068  1.00 54.23           C  
ANISOU 2143  CD1 LEU A 284     5534   6542   8528   -867    734    217       C  
ATOM   2144  CD2 LEU A 284     597.773 -30.936 196.773  1.00 52.61           C  
ANISOU 2144  CD2 LEU A 284     5464   6443   8082   -643    684    299       C  
ATOM   2145  N   SER A 285     597.797 -31.947 202.105  1.00 89.87           N  
ANISOU 2145  N   SER A 285    10407  11156  12584   -437     94     43       N  
ATOM   2146  CA  SER A 285     598.384 -32.699 203.200  1.00 92.93           C  
ANISOU 2146  CA  SER A 285    10805  11601  12904   -357    -97    -11       C  
ATOM   2147  C   SER A 285     598.170 -34.183 202.912  1.00 92.87           C  
ANISOU 2147  C   SER A 285    10831  11612  12844   -244   -118     82       C  
ATOM   2148  O   SER A 285     598.966 -35.047 203.309  1.00 94.49           O  
ANISOU 2148  O   SER A 285    10983  11856  13062   -156   -268     58       O  
ATOM   2149  CB  SER A 285     597.763 -32.296 204.530  1.00 95.60           C  
ANISOU 2149  CB  SER A 285    11311  11928  13084   -353   -167    -42       C  
ATOM   2150  OG  SER A 285     596.778 -33.224 204.947  1.00 96.94           O  
ANISOU 2150  OG  SER A 285    11647  12098  13087   -275   -156     66       O  
ATOM   2151  N   GLY A 286     597.077 -34.460 202.207  1.00 72.03           N  
ANISOU 2151  N   GLY A 286     8274   8934  10159   -243     23    182       N  
ATOM   2152  CA  GLY A 286     596.795 -35.787 201.702  1.00 71.63           C  
ANISOU 2152  CA  GLY A 286     8244   8879  10093   -160     34    254       C  
ATOM   2153  C   GLY A 286     595.660 -36.528 202.375  1.00 72.88           C  
ANISOU 2153  C   GLY A 286     8586   8995  10109   -117     30    348       C  
ATOM   2154  O   GLY A 286     595.547 -37.724 202.197  1.00 72.94           O  
ANISOU 2154  O   GLY A 286     8623   8975  10117    -48      5    400       O  
ATOM   2155  N   ILE A 287     594.817 -35.830 203.130  1.00 78.59           N  
ANISOU 2155  N   ILE A 287     9430   9706  10725   -162     68    361       N  
ATOM   2156  CA  ILE A 287     593.715 -36.462 203.865  1.00 78.97           C  
ANISOU 2156  CA  ILE A 287     9646   9728  10631   -141     94    446       C  
ATOM   2157  C   ILE A 287     592.728 -37.241 203.026  1.00 75.25           C  
ANISOU 2157  C   ILE A 287     9193   9214  10185   -139    206    526       C  
ATOM   2158  O   ILE A 287     592.459 -38.413 203.288  1.00 75.20           O  
ANISOU 2158  O   ILE A 287     9263   9168  10140    -99    179    598       O  
ATOM   2159  CB  ILE A 287     592.883 -35.445 204.617  1.00 79.21           C  
ANISOU 2159  CB  ILE A 287     9769   9763  10562   -196    164    418       C  
ATOM   2160  CG1 ILE A 287     592.891 -34.121 203.859  1.00 75.94           C  
ANISOU 2160  CG1 ILE A 287     9256   9332  10265   -258    247    351       C  
ATOM   2161  CG2 ILE A 287     593.373 -35.346 206.045  1.00 83.71           C  
ANISOU 2161  CG2 ILE A 287    10438  10379  10990   -178     34    376       C  
ATOM   2162  CD1 ILE A 287     591.815 -33.180 204.290  1.00 75.77           C  
ANISOU 2162  CD1 ILE A 287     9309   9285  10195   -294    350    324       C  
ATOM   2163  N   ASN A 288     592.164 -36.580 202.029  1.00104.93           N  
ANISOU 2163  N   ASN A 288    12886  12972  14009   -185    324    515       N  
ATOM   2164  CA  ASN A 288     591.127 -37.209 201.245  1.00101.99           C  
ANISOU 2164  CA  ASN A 288    12522  12576  13653   -189    415    568       C  
ATOM   2165  C   ASN A 288     591.678 -38.440 200.542  1.00102.96           C  
ANISOU 2165  C   ASN A 288    12596  12683  13843   -139    369    573       C  
ATOM   2166  O   ASN A 288     590.927 -39.288 200.097  1.00101.82           O  
ANISOU 2166  O   ASN A 288    12474  12503  13710   -137    411    605       O  
ATOM   2167  CB  ASN A 288     590.514 -36.209 200.268  1.00 99.04           C  
ANISOU 2167  CB  ASN A 288    12087  12216  13328   -230    516    559       C  
ATOM   2168  CG  ASN A 288     589.561 -35.241 200.960  1.00 98.25           C  
ANISOU 2168  CG  ASN A 288    12047  12101  13184   -259    579    555       C  
ATOM   2169  OD1 ASN A 288     589.734 -34.020 200.901  1.00 98.24           O  
ANISOU 2169  OD1 ASN A 288    12020  12088  13219   -282    597    518       O  
ATOM   2170  ND2 ASN A 288     588.557 -35.790 201.638  1.00 98.00           N  
ANISOU 2170  ND2 ASN A 288    12092  12058  13084   -261    622    586       N  
ATOM   2171  N   ALA A 289     592.996 -38.561 200.484  1.00 64.62           N  
ANISOU 2171  N   ALA A 289     7660   7848   9043    -97    280    523       N  
ATOM   2172  CA  ALA A 289     593.600 -39.836 200.158  1.00 65.82           C  
ANISOU 2172  CA  ALA A 289     7777   7967   9263    -22    213    513       C  
ATOM   2173  C   ALA A 289     593.186 -40.882 201.218  1.00 66.52           C  
ANISOU 2173  C   ALA A 289     8015   7971   9288     19    142    599       C  
ATOM   2174  O   ALA A 289     592.789 -41.989 200.866  1.00 66.18           O  
ANISOU 2174  O   ALA A 289     8005   7851   9290     43    154    629       O  
ATOM   2175  CB  ALA A 289     595.117 -39.704 200.056  1.00 67.12           C  
ANISOU 2175  CB  ALA A 289     7807   8178   9516     25    124    430       C  
ATOM   2176  N   VAL A 290     593.229 -40.545 202.507  1.00 63.09           N  
ANISOU 2176  N   VAL A 290     7683   7545   8742     17     76    641       N  
ATOM   2177  CA  VAL A 290     592.803 -41.521 203.518  1.00 63.69           C  
ANISOU 2177  CA  VAL A 290     7928   7546   8726     43     27    753       C  
ATOM   2178  C   VAL A 290     591.269 -41.535 203.666  1.00 61.50           C  
ANISOU 2178  C   VAL A 290     7750   7242   8374    -46    181    820       C  
ATOM   2179  O   VAL A 290     590.694 -42.339 204.415  1.00 61.65           O  
ANISOU 2179  O   VAL A 290     7913   7193   8317    -58    193    928       O  
ATOM   2180  CB  VAL A 290     593.478 -41.269 204.900  1.00 66.23           C  
ANISOU 2180  CB  VAL A 290     8342   7907   8914     84   -119    778       C  
ATOM   2181  CG1 VAL A 290     594.662 -40.361 204.760  1.00 67.71           C  
ANISOU 2181  CG1 VAL A 290     8380   8181   9165    105   -211    654       C  
ATOM   2182  CG2 VAL A 290     592.510 -40.706 205.915  1.00 66.14           C  
ANISOU 2182  CG2 VAL A 290     8483   7933   8716     10    -37    826       C  
ATOM   2183  N   PHE A 291     590.597 -40.661 202.927  1.00 62.79           N  
ANISOU 2183  N   PHE A 291     7831   7456   8570   -108    302    762       N  
ATOM   2184  CA  PHE A 291     589.145 -40.619 202.979  1.00 60.50           C  
ANISOU 2184  CA  PHE A 291     7589   7154   8245   -183    443    800       C  
ATOM   2185  C   PHE A 291     588.523 -40.846 201.625  1.00 58.52           C  
ANISOU 2185  C   PHE A 291     7231   6891   8111   -206    514    763       C  
ATOM   2186  O   PHE A 291     587.318 -40.831 201.515  1.00 57.08           O  
ANISOU 2186  O   PHE A 291     7049   6706   7932   -264    616    776       O  
ATOM   2187  CB  PHE A 291     588.647 -39.295 203.553  1.00 59.81           C  
ANISOU 2187  CB  PHE A 291     7515   7137   8072   -225    514    763       C  
ATOM   2188  CG  PHE A 291     588.577 -39.281 205.042  1.00 62.03           C  
ANISOU 2188  CG  PHE A 291     7947   7436   8186   -235    502    806       C  
ATOM   2189  CD1 PHE A 291     588.076 -40.371 205.724  1.00 62.38           C  
ANISOU 2189  CD1 PHE A 291     8122   7428   8151   -255    530    918       C  
ATOM   2190  CD2 PHE A 291     589.033 -38.196 205.766  1.00 64.23           C  
ANISOU 2190  CD2 PHE A 291     8248   7781   8377   -230    463    735       C  
ATOM   2191  CE1 PHE A 291     588.011 -40.373 207.104  1.00 64.58           C  
ANISOU 2191  CE1 PHE A 291     8563   7740   8233   -267    528    974       C  
ATOM   2192  CE2 PHE A 291     588.974 -38.193 207.146  1.00 66.88           C  
ANISOU 2192  CE2 PHE A 291     8736   8155   8520   -236    447    761       C  
ATOM   2193  CZ  PHE A 291     588.462 -39.278 207.814  1.00 66.84           C  
ANISOU 2193  CZ  PHE A 291     8873   8118   8404   -253    483    888       C  
ATOM   2194  N   TYR A 292     589.314 -41.058 200.586  1.00 84.29           N  
ANISOU 2194  N   TYR A 292    10397  10163  11467   -162    463    705       N  
ATOM   2195  CA  TYR A 292     588.743 -41.595 199.351  1.00 83.43           C  
ANISOU 2195  CA  TYR A 292    10216  10041  11441   -177    511    666       C  
ATOM   2196  C   TYR A 292     589.218 -43.014 199.102  1.00 85.56           C  
ANISOU 2196  C   TYR A 292    10500  10218  11793   -130    448    656       C  
ATOM   2197  O   TYR A 292     588.678 -43.713 198.237  1.00 85.74           O  
ANISOU 2197  O   TYR A 292    10486  10206  11885   -148    479    611       O  
ATOM   2198  CB  TYR A 292     589.121 -40.776 198.124  1.00 82.63           C  
ANISOU 2198  CB  TYR A 292     9998  10031  11367   -169    529    595       C  
ATOM   2199  CG  TYR A 292     588.623 -39.362 198.058  1.00 80.22           C  
ANISOU 2199  CG  TYR A 292     9671   9790  11021   -205    587    604       C  
ATOM   2200  CD1 TYR A 292     587.605 -38.904 198.884  1.00 79.21           C  
ANISOU 2200  CD1 TYR A 292     9597   9648  10849   -241    640    641       C  
ATOM   2201  CD2 TYR A 292     589.181 -38.477 197.150  1.00 79.35           C  
ANISOU 2201  CD2 TYR A 292     9484   9745  10922   -203    600    575       C  
ATOM   2202  CE1 TYR A 292     587.164 -37.593 198.802  1.00 77.80           C  
ANISOU 2202  CE1 TYR A 292     9393   9506  10663   -255    686    635       C  
ATOM   2203  CE2 TYR A 292     588.755 -37.188 197.063  1.00 77.75           C  
ANISOU 2203  CE2 TYR A 292     9274   9566  10703   -228    644    596       C  
ATOM   2204  CZ  TYR A 292     587.751 -36.743 197.883  1.00 77.16           C  
ANISOU 2204  CZ  TYR A 292     9249   9462  10607   -245    678    620       C  
ATOM   2205  OH  TYR A 292     587.358 -35.433 197.749  1.00 76.37           O  
ANISOU 2205  OH  TYR A 292     9135   9364  10518   -252    715    629       O  
ATOM   2206  N   TYR A 293     590.239 -43.424 199.855  1.00 66.53           N  
ANISOU 2206  N   TYR A 293     8137   7761   9381    -62    347    687       N  
ATOM   2207  CA  TYR A 293     591.012 -44.611 199.510  1.00 68.49           C  
ANISOU 2207  CA  TYR A 293     8368   7917   9739     20    265    654       C  
ATOM   2208  C   TYR A 293     591.458 -45.415 200.735  1.00 69.78           C  
ANISOU 2208  C   TYR A 293     8661   7965   9887     81    155    760       C  
ATOM   2209  O   TYR A 293     592.257 -46.341 200.614  1.00 71.15           O  
ANISOU 2209  O   TYR A 293     8822   8046  10166    179     56    740       O  
ATOM   2210  CB  TYR A 293     592.223 -44.205 198.673  1.00 69.59           C  
ANISOU 2210  CB  TYR A 293     8357   8146   9937     85    230    538       C  
ATOM   2211  CG  TYR A 293     591.875 -43.497 197.381  1.00 68.73           C  
ANISOU 2211  CG  TYR A 293     8145   8148   9821     32    335    457       C  
ATOM   2212  CD1 TYR A 293     591.172 -44.147 196.385  1.00 68.82           C  
ANISOU 2212  CD1 TYR A 293     8138   8139   9871     10    387    399       C  
ATOM   2213  CD2 TYR A 293     592.257 -42.177 197.152  1.00 67.80           C  
ANISOU 2213  CD2 TYR A 293     7957   8149   9654      0    372    440       C  
ATOM   2214  CE1 TYR A 293     590.847 -43.511 195.191  1.00 67.81           C  
ANISOU 2214  CE1 TYR A 293     7935   8129   9703    -29    463    336       C  
ATOM   2215  CE2 TYR A 293     591.939 -41.530 195.956  1.00 65.60           C  
ANISOU 2215  CE2 TYR A 293     7611   7965   9351    -44    462    398       C  
ATOM   2216  CZ  TYR A 293     591.231 -42.210 194.979  1.00 65.60           C  
ANISOU 2216  CZ  TYR A 293     7603   7962   9358    -52    501    351       C  
ATOM   2217  OH  TYR A 293     590.907 -41.600 193.787  1.00 63.91           O  
ANISOU 2217  OH  TYR A 293     7339   7855   9088    -86    569    319       O  
ATOM   2218  N   SER A 294     590.914 -45.052 201.895  1.00 94.32           N  
ANISOU 2218  N   SER A 294    11897  11081  12857     29    173    870       N  
ATOM   2219  CA  SER A 294     591.157 -45.744 203.153  1.00 95.77           C  
ANISOU 2219  CA  SER A 294    12248  11172  12969     71     78   1006       C  
ATOM   2220  C   SER A 294     591.185 -47.252 202.988  1.00 96.69           C  
ANISOU 2220  C   SER A 294    12429  11095  13215    118     31   1062       C  
ATOM   2221  O   SER A 294     592.131 -47.907 203.406  1.00 98.38           O  
ANISOU 2221  O   SER A 294    12686  11225  13469    236   -122   1106       O  
ATOM   2222  CB  SER A 294     590.085 -45.356 204.172  1.00 94.93           C  
ANISOU 2222  CB  SER A 294    12283  11094  12691    -34    183   1112       C  
ATOM   2223  OG  SER A 294     590.312 -45.973 205.423  1.00 96.74           O  
ANISOU 2223  OG  SER A 294    12702  11253  12802     -1     99   1263       O  
ATOM   2224  N   THR A 295     590.161 -47.803 202.352  1.00 99.37           N  
ANISOU 2224  N   THR A 295    12764  11354  13639     30    150   1048       N  
ATOM   2225  CA  THR A 295     590.064 -49.252 202.216  1.00100.44           C  
ANISOU 2225  CA  THR A 295    12973  11271  13920     52    119   1094       C  
ATOM   2226  C   THR A 295     591.137 -49.822 201.280  1.00101.64           C  
ANISOU 2226  C   THR A 295    13002  11367  14248    188     13    956       C  
ATOM   2227  O   THR A 295     591.786 -50.807 201.615  1.00103.07           O  
ANISOU 2227  O   THR A 295    13254  11380  14527    295   -107   1010       O  
ATOM   2228  CB  THR A 295     588.669 -49.670 201.717  1.00 99.49           C  
ANISOU 2228  CB  THR A 295    12851  11082  13868    -94    273   1080       C  
ATOM   2229  OG1 THR A 295     587.671 -49.130 202.596  1.00 98.24           O  
ANISOU 2229  OG1 THR A 295    12781  10988  13560   -217    392   1192       O  
ATOM   2230  CG2 THR A 295     588.542 -51.185 201.670  1.00100.94           C  
ANISOU 2230  CG2 THR A 295    13127  11005  14221    -91    244   1130       C  
ATOM   2231  N   SER A 296     591.335 -49.191 200.124  1.00 87.89           N  
ANISOU 2231  N   SER A 296    11082   9768  12544    189     60    781       N  
ATOM   2232  CA  SER A 296     592.337 -49.641 199.148  1.00 88.96           C  
ANISOU 2232  CA  SER A 296    11081   9891  12830    308     -1    620       C  
ATOM   2233  C   SER A 296     593.770 -49.545 199.672  1.00 89.85           C  
ANISOU 2233  C   SER A 296    11149  10026  12964    458   -152    622       C  
ATOM   2234  O   SER A 296     594.645 -50.310 199.271  1.00 90.89           O  
ANISOU 2234  O   SER A 296    11207  10072  13255    589   -236    530       O  
ATOM   2235  CB  SER A 296     592.219 -48.824 197.861  1.00 88.37           C  
ANISOU 2235  CB  SER A 296    10844  10001  12733    259    102    456       C  
ATOM   2236  OG  SER A 296     593.254 -49.158 196.956  1.00 89.35           O  
ANISOU 2236  OG  SER A 296    10830  10146  12971    367     69    293       O  
ATOM   2237  N   ILE A 297     593.994 -48.581 200.559  1.00 61.90           N  
ANISOU 2237  N   ILE A 297     7639   6607   9273    440   -189    706       N  
ATOM   2238  CA  ILE A 297     595.297 -48.291 201.147  1.00 62.87           C  
ANISOU 2238  CA  ILE A 297     7702   6787   9398    562   -347    699       C  
ATOM   2239  C   ILE A 297     595.595 -49.275 202.264  1.00 64.16           C  
ANISOU 2239  C   ILE A 297     8030   6779   9571    668   -514    854       C  
ATOM   2240  O   ILE A 297     596.740 -49.698 202.447  1.00 65.17           O  
ANISOU 2240  O   ILE A 297     8091   6867   9804    827   -683    823       O  
ATOM   2241  CB  ILE A 297     595.341 -46.836 201.683  1.00 62.41           C  
ANISOU 2241  CB  ILE A 297     7623   6919   9170    486   -327    712       C  
ATOM   2242  CG1 ILE A 297     595.593 -45.862 200.534  1.00 61.46           C  
ANISOU 2242  CG1 ILE A 297     7308   6957   9087    433   -215    555       C  
ATOM   2243  CG2 ILE A 297     596.398 -46.658 202.756  1.00 63.78           C  
ANISOU 2243  CG2 ILE A 297     7808   7126   9300    588   -522    752       C  
ATOM   2244  CD1 ILE A 297     595.604 -44.376 200.952  1.00 61.10           C  
ANISOU 2244  CD1 ILE A 297     7238   7064   8913    347   -183    555       C  
ATOM   2245  N   PHE A 298     594.551 -49.648 202.996  1.00 81.47           N  
ANISOU 2245  N   PHE A 298    10434   8867  11655    579   -464   1026       N  
ATOM   2246  CA  PHE A 298     594.668 -50.601 204.092  1.00 82.64           C  
ANISOU 2246  CA  PHE A 298    10788   8836  11777    656   -601   1222       C  
ATOM   2247  C   PHE A 298     594.905 -52.035 203.571  1.00 83.40           C  
ANISOU 2247  C   PHE A 298    10894   8678  12116    761   -660   1209       C  
ATOM   2248  O   PHE A 298     595.731 -52.779 204.103  1.00 84.64           O  
ANISOU 2248  O   PHE A 298    11111   8699  12351    925   -852   1288       O  
ATOM   2249  CB  PHE A 298     593.416 -50.528 204.964  1.00 82.18           C  
ANISOU 2249  CB  PHE A 298    10946   8754  11523    500   -480   1406       C  
ATOM   2250  CG  PHE A 298     593.451 -49.426 205.993  1.00 82.23           C  
ANISOU 2250  CG  PHE A 298    11020   8952  11271    461   -502   1465       C  
ATOM   2251  CD1 PHE A 298     594.605 -49.169 206.724  1.00 83.57           C  
ANISOU 2251  CD1 PHE A 298    11192   9194  11367    596   -717   1480       C  
ATOM   2252  CD2 PHE A 298     592.322 -48.652 206.239  1.00 81.03           C  
ANISOU 2252  CD2 PHE A 298    10918   8908  10960    295   -314   1486       C  
ATOM   2253  CE1 PHE A 298     594.618 -48.164 207.680  1.00 83.99           C  
ANISOU 2253  CE1 PHE A 298    11313   9423  11177    554   -743   1508       C  
ATOM   2254  CE2 PHE A 298     592.338 -47.636 207.185  1.00 81.37           C  
ANISOU 2254  CE2 PHE A 298    11026   9120  10772    263   -325   1511       C  
ATOM   2255  CZ  PHE A 298     593.472 -47.405 207.906  1.00 82.97           C  
ANISOU 2255  CZ  PHE A 298    11248   9390  10888    386   -538   1520       C  
ATOM   2256  N   GLU A 299     594.171 -52.401 202.525  1.00 94.55           N  
ANISOU 2256  N   GLU A 299    12246  10025  13653    672   -507   1100       N  
ATOM   2257  CA  GLU A 299     594.425 -53.622 201.775  1.00 95.33           C  
ANISOU 2257  CA  GLU A 299    12309   9904  14008    765   -542   1009       C  
ATOM   2258  C   GLU A 299     595.893 -53.711 201.399  1.00 96.06           C  
ANISOU 2258  C   GLU A 299    12222  10030  14244    974   -693    860       C  
ATOM   2259  O   GLU A 299     596.632 -54.530 201.949  1.00 97.23           O  
ANISOU 2259  O   GLU A 299    12431  10004  14506   1142   -874    937       O  
ATOM   2260  CB  GLU A 299     593.554 -53.672 200.515  1.00 94.60           C  
ANISOU 2260  CB  GLU A 299    12118   9830  13996    637   -361    837       C  
ATOM   2261  CG  GLU A 299     593.943 -54.744 199.506  1.00 95.58           C  
ANISOU 2261  CG  GLU A 299    12155   9783  14380    738   -386    654       C  
ATOM   2262  CD  GLU A 299     593.051 -54.757 198.273  1.00 95.25           C  
ANISOU 2262  CD  GLU A 299    12025   9786  14378    605   -225    471       C  
ATOM   2263  OE1 GLU A 299     593.123 -53.812 197.464  1.00 94.43           O  
ANISOU 2263  OE1 GLU A 299    11766   9933  14180    568   -144    326       O  
ATOM   2264  OE2 GLU A 299     592.281 -55.724 198.104  1.00 95.95           O  
ANISOU 2264  OE2 GLU A 299    12204   9656  14597    535   -187    473       O  
ATOM   2265  N   LYS A 300     596.307 -52.848 200.479  1.00 91.83           N  
ANISOU 2265  N   LYS A 300    11464   9721  13706    961   -616    654       N  
ATOM   2266  CA  LYS A 300     597.667 -52.847 199.969  1.00 92.32           C  
ANISOU 2266  CA  LYS A 300    11309   9851  13917   1132   -709    476       C  
ATOM   2267  C   LYS A 300     598.694 -52.884 201.080  1.00 93.19           C  
ANISOU 2267  C   LYS A 300    11437   9944  14029   1292   -940    584       C  
ATOM   2268  O   LYS A 300     599.776 -53.421 200.881  1.00 93.94           O  
ANISOU 2268  O   LYS A 300    11394   9981  14319   1481  -1070    477       O  
ATOM   2269  CB  LYS A 300     597.910 -51.631 199.081  1.00 91.34           C  
ANISOU 2269  CB  LYS A 300    10977  10010  13720   1050   -574    303       C  
ATOM   2270  CG  LYS A 300     597.630 -51.904 197.621  1.00 91.14           C  
ANISOU 2270  CG  LYS A 300    10838  10005  13785   1012   -416     97       C  
ATOM   2271  CD  LYS A 300     597.075 -50.686 196.896  1.00 89.91           C  
ANISOU 2271  CD  LYS A 300    10613  10089  13460    845   -240     41       C  
ATOM   2272  CE  LYS A 300     596.490 -51.112 195.549  1.00 90.00           C  
ANISOU 2272  CE  LYS A 300    10581  10101  13513    792   -102   -126       C  
ATOM   2273  NZ  LYS A 300     595.717 -50.049 194.854  1.00 88.87           N  
ANISOU 2273  NZ  LYS A 300    10415  10158  13192    632     48   -142       N  
ATOM   2274  N   ALA A 301     598.366 -52.320 202.242  1.00 87.19           N  
ANISOU 2274  N   ALA A 301    10837   9243  13050   1224   -997    781       N  
ATOM   2275  CA  ALA A 301     599.208 -52.488 203.421  1.00 88.36           C  
ANISOU 2275  CA  ALA A 301    11053   9358  13162   1377  -1248    913       C  
ATOM   2276  C   ALA A 301     599.261 -53.974 203.752  1.00 89.44           C  
ANISOU 2276  C   ALA A 301    11347   9179  13456   1522  -1382   1042       C  
ATOM   2277  O   ALA A 301     599.915 -54.760 203.064  1.00 89.91           O  
ANISOU 2277  O   ALA A 301    11273   9108  13779   1676  -1438    902       O  
ATOM   2278  CB  ALA A 301     598.680 -51.694 204.584  1.00 88.32           C  
ANISOU 2278  CB  ALA A 301    11229   9468  12860   1262  -1261   1094       C  
ATOM   2279  N   GLY A 302     598.561 -54.387 204.791  1.00 73.99           N  
ANISOU 2279  N   GLY A 302     9682   7084  11347   1472  -1422   1308       N  
ATOM   2280  CA  GLY A 302     598.407 -55.808 204.987  1.00 75.30           C  
ANISOU 2280  CA  GLY A 302    10025   6911  11675   1568  -1502   1449       C  
ATOM   2281  C   GLY A 302     597.154 -56.020 205.766  1.00 75.50           C  
ANISOU 2281  C   GLY A 302    10352   6831  11503   1387  -1391   1710       C  
ATOM   2282  O   GLY A 302     596.931 -57.067 206.365  1.00 77.28           O  
ANISOU 2282  O   GLY A 302    10810   6780  11774   1431  -1468   1928       O  
ATOM   2283  N   VAL A 303     596.336 -54.989 205.793  1.00 81.30           N  
ANISOU 2283  N   VAL A 303    11085   7787  12019   1180  -1202   1694       N  
ATOM   2284  CA  VAL A 303     595.170 -55.036 206.643  1.00 81.16           C  
ANISOU 2284  CA  VAL A 303    11330   7721  11786   1002  -1079   1929       C  
ATOM   2285  C   VAL A 303     594.206 -56.099 206.108  1.00 81.20           C  
ANISOU 2285  C   VAL A 303    11425   7451  11977    893   -926   1967       C  
ATOM   2286  O   VAL A 303     593.994 -56.219 204.898  1.00 80.63           O  
ANISOU 2286  O   VAL A 303    11173   7361  12103    855   -815   1746       O  
ATOM   2287  CB  VAL A 303     594.511 -53.641 206.752  1.00 79.86           C  
ANISOU 2287  CB  VAL A 303    11111   7857  11374    821   -907   1869       C  
ATOM   2288  CG1 VAL A 303     593.345 -53.672 207.708  1.00 79.73           C  
ANISOU 2288  CG1 VAL A 303    11352   7813  11130    646   -768   2098       C  
ATOM   2289  CG2 VAL A 303     595.541 -52.625 207.221  1.00 80.24           C  
ANISOU 2289  CG2 VAL A 303    11056   8149  11282    925  -1070   1800       C  
ATOM   2290  N   GLN A 304     593.689 -56.922 207.010  1.00134.60           N  
ANISOU 2290  N   GLN A 304    18470  13990  18682    848   -933   2245       N  
ATOM   2291  CA  GLN A 304     592.608 -57.823 206.653  1.00134.72           C  
ANISOU 2291  CA  GLN A 304    18584  13751  18853    689   -757   2300       C  
ATOM   2292  C   GLN A 304     591.319 -57.215 207.166  1.00133.64           C  
ANISOU 2292  C   GLN A 304    18549  13753  18475    431   -520   2410       C  
ATOM   2293  O   GLN A 304     591.274 -56.716 208.292  1.00133.81           O  
ANISOU 2293  O   GLN A 304    18732  13905  18205    407   -537   2597       O  
ATOM   2294  CB  GLN A 304     592.825 -59.220 207.227  1.00136.60           C  
ANISOU 2294  CB  GLN A 304    19065  13603  19233    787   -890   2539       C  
ATOM   2295  CG  GLN A 304     593.692 -60.120 206.366  1.00137.54           C  
ANISOU 2295  CG  GLN A 304    19057  13487  19714    996  -1043   2372       C  
ATOM   2296  CD  GLN A 304     593.333 -61.585 206.538  1.00138.92           C  
ANISOU 2296  CD  GLN A 304    19454  13211  20120    989  -1056   2553       C  
ATOM   2297  OE1 GLN A 304     592.640 -61.962 207.486  1.00139.51           O  
ANISOU 2297  OE1 GLN A 304    19808  13143  20057    858   -992   2862       O  
ATOM   2298  NE2 GLN A 304     593.791 -62.417 205.613  1.00139.55           N  
ANISOU 2298  NE2 GLN A 304    19413  13057  20554   1122  -1124   2356       N  
ATOM   2299  N   GLN A 305     590.284 -57.257 206.329  1.00141.03           N  
ANISOU 2299  N   GLN A 305    19379  14671  19536    247   -306   2275       N  
ATOM   2300  CA  GLN A 305     589.049 -56.496 206.546  1.00139.67           C  
ANISOU 2300  CA  GLN A 305    19204  14682  19182     13    -68   2292       C  
ATOM   2301  C   GLN A 305     589.349 -55.004 206.675  1.00138.50           C  
ANISOU 2301  C   GLN A 305    18927  14898  18798     42    -74   2182       C  
ATOM   2302  O   GLN A 305     589.314 -54.460 207.775  1.00138.63           O  
ANISOU 2302  O   GLN A 305    19086  15044  18542     21    -72   2337       O  
ATOM   2303  CB  GLN A 305     588.307 -56.992 207.788  1.00140.47           C  
ANISOU 2303  CB  GLN A 305    19595  14652  19125   -125     34   2609       C  
ATOM   2304  CG  GLN A 305     588.154 -58.503 207.863  1.00142.06           C  
ANISOU 2304  CG  GLN A 305    19975  14449  19555   -143     15   2775       C  
ATOM   2305  CD  GLN A 305     588.463 -59.036 209.248  1.00143.49           C  
ANISOU 2305  CD  GLN A 305    20487  14486  19545    -93    -80   3136       C  
ATOM   2306  OE1 GLN A 305     588.955 -58.303 210.106  1.00143.43           O  
ANISOU 2306  OE1 GLN A 305    20562  14699  19234    -10   -172   3232       O  
ATOM   2307  NE2 GLN A 305     588.178 -60.317 209.474  1.00144.98           N  
ANISOU 2307  NE2 GLN A 305    20878  14302  19907   -145    -64   3340       N  
ATOM   2308  N   PRO A 306     589.640 -54.343 205.541  1.00 87.44           N  
ANISOU 2308  N   PRO A 306    12201   8591  12432     84    -75   1913       N  
ATOM   2309  CA  PRO A 306     590.126 -52.965 205.463  1.00 86.48           C  
ANISOU 2309  CA  PRO A 306    11933   8773  12153    131   -103   1784       C  
ATOM   2310  C   PRO A 306     589.057 -51.891 205.711  1.00 84.86           C  
ANISOU 2310  C   PRO A 306    11706   8776  11761    -42     92   1773       C  
ATOM   2311  O   PRO A 306     589.382 -50.774 206.144  1.00 84.36           O  
ANISOU 2311  O   PRO A 306    11612   8929  11513    -17     68   1743       O  
ATOM   2312  CB  PRO A 306     590.651 -52.869 204.019  1.00 86.05           C  
ANISOU 2312  CB  PRO A 306    11629   8759  12305    208   -133   1521       C  
ATOM   2313  CG  PRO A 306     590.704 -54.254 203.507  1.00 87.17           C  
ANISOU 2313  CG  PRO A 306    11802   8618  12700    253   -173   1508       C  
ATOM   2314  CD  PRO A 306     589.582 -54.941 204.202  1.00 87.41           C  
ANISOU 2314  CD  PRO A 306    12036   8469  12709     93    -54   1709       C  
ATOM   2315  N   VAL A 307     587.804 -52.224 205.426  1.00 94.22           N  
ANISOU 2315  N   VAL A 307    12892   9891  13017   -213    279   1780       N  
ATOM   2316  CA  VAL A 307     586.710 -51.289 205.616  1.00 92.48           C  
ANISOU 2316  CA  VAL A 307    12626   9851  12661   -366    470   1755       C  
ATOM   2317  C   VAL A 307     586.466 -51.023 207.098  1.00 92.96           C  
ANISOU 2317  C   VAL A 307    12896   9970  12455   -418    524   1956       C  
ATOM   2318  O   VAL A 307     585.973 -49.958 207.461  1.00 91.87           O  
ANISOU 2318  O   VAL A 307    12720  10033  12152   -481    633   1913       O  
ATOM   2319  CB  VAL A 307     585.415 -51.795 204.965  1.00 91.70           C  
ANISOU 2319  CB  VAL A 307    12452   9662  12729   -537    645   1703       C  
ATOM   2320  CG1 VAL A 307     585.498 -51.678 203.453  1.00 91.00           C  
ANISOU 2320  CG1 VAL A 307    12136   9611  12827   -500    610   1462       C  
ATOM   2321  CG2 VAL A 307     585.144 -53.229 205.382  1.00 93.58           C  
ANISOU 2321  CG2 VAL A 307    12867   9607  13083   -602    665   1874       C  
ATOM   2322  N   TYR A 308     586.813 -51.974 207.958  1.00113.06           N  
ANISOU 2322  N   TYR A 308    15670  12340  14950   -383    447   2173       N  
ATOM   2323  CA  TYR A 308     586.693 -51.741 209.389  1.00113.78           C  
ANISOU 2323  CA  TYR A 308    15987  12505  14738   -418    481   2371       C  
ATOM   2324  C   TYR A 308     587.770 -50.783 209.858  1.00114.20           C  
ANISOU 2324  C   TYR A 308    16034  12760  14599   -266    299   2316       C  
ATOM   2325  O   TYR A 308     587.576 -49.993 210.783  1.00114.17           O  
ANISOU 2325  O   TYR A 308    16121  12935  14324   -305    354   2352       O  
ATOM   2326  CB  TYR A 308     586.781 -53.042 210.154  1.00115.58           C  
ANISOU 2326  CB  TYR A 308    16484  12480  14952   -420    436   2646       C  
ATOM   2327  CG  TYR A 308     585.543 -53.878 210.016  1.00115.50           C  
ANISOU 2327  CG  TYR A 308    16518  12285  15082   -627    664   2734       C  
ATOM   2328  CD1 TYR A 308     584.396 -53.578 210.741  1.00115.08           C  
ANISOU 2328  CD1 TYR A 308    16542  12329  14853   -825    922   2826       C  
ATOM   2329  CD2 TYR A 308     585.515 -54.974 209.159  1.00116.07           C  
ANISOU 2329  CD2 TYR A 308    16542  12083  15476   -631    631   2706       C  
ATOM   2330  CE1 TYR A 308     583.247 -54.352 210.620  1.00115.19           C  
ANISOU 2330  CE1 TYR A 308    16571  12176  15021  -1036   1145   2898       C  
ATOM   2331  CE2 TYR A 308     584.376 -55.757 209.030  1.00116.27           C  
ANISOU 2331  CE2 TYR A 308    16596  11925  15658   -841    837   2771       C  
ATOM   2332  CZ  TYR A 308     583.243 -55.441 209.762  1.00115.80           C  
ANISOU 2332  CZ  TYR A 308    16599  11970  15431  -1049   1095   2872       C  
ATOM   2333  OH  TYR A 308     582.103 -56.212 209.636  1.00116.18           O  
ANISOU 2333  OH  TYR A 308    16646  11840  15656  -1275   1311   2927       O  
ATOM   2334  N   ALA A 309     588.919 -50.858 209.209  1.00111.83           N  
ANISOU 2334  N   ALA A 309    15612  12431  14449    -97     87   2207       N  
ATOM   2335  CA  ALA A 309     589.982 -49.932 209.509  1.00112.37           C  
ANISOU 2335  CA  ALA A 309    15622  12686  14388     35    -89   2117       C  
ATOM   2336  C   ALA A 309     589.587 -48.600 208.899  1.00110.71           C  
ANISOU 2336  C   ALA A 309    15203  12687  14174    -38     40   1902       C  
ATOM   2337  O   ALA A 309     590.053 -47.540 209.330  1.00110.90           O  
ANISOU 2337  O   ALA A 309    15196  12895  14046     -2    -21   1823       O  
ATOM   2338  CB  ALA A 309     591.310 -50.431 208.970  1.00113.45           C  
ANISOU 2338  CB  ALA A 309    15659  12731  14715    230   -333   2055       C  
ATOM   2339  N   THR A 310     588.712 -48.654 207.897  1.00 64.16           N  
ANISOU 2339  N   THR A 310     9170   6755   8454   -140    207   1805       N  
ATOM   2340  CA  THR A 310     588.177 -47.426 207.339  1.00 62.34           C  
ANISOU 2340  CA  THR A 310     8765   6704   8218   -210    334   1633       C  
ATOM   2341  C   THR A 310     587.237 -46.838 208.368  1.00 61.96           C  
ANISOU 2341  C   THR A 310     8834   6763   7946   -325    497   1701       C  
ATOM   2342  O   THR A 310     587.367 -45.678 208.734  1.00 61.92           O  
ANISOU 2342  O   THR A 310     8795   6927   7803   -315    501   1614       O  
ATOM   2343  CB  THR A 310     587.432 -47.622 205.997  1.00 60.56           C  
ANISOU 2343  CB  THR A 310     8363   6430   8216   -280    450   1512       C  
ATOM   2344  OG1 THR A 310     588.359 -47.983 204.970  1.00 60.99           O  
ANISOU 2344  OG1 THR A 310     8292   6428   8451   -168    316   1405       O  
ATOM   2345  CG2 THR A 310     586.760 -46.339 205.588  1.00 58.69           C  
ANISOU 2345  CG2 THR A 310     7982   6370   7948   -345    574   1378       C  
ATOM   2346  N   ILE A 311     586.302 -47.642 208.860  1.00 74.84           N  
ANISOU 2346  N   ILE A 311    10600   8289   9545   -440    641   1850       N  
ATOM   2347  CA  ILE A 311     585.385 -47.149 209.876  1.00 74.75           C  
ANISOU 2347  CA  ILE A 311    10698   8391   9313   -557    828   1911       C  
ATOM   2348  C   ILE A 311     586.161 -46.824 211.148  1.00 76.64           C  
ANISOU 2348  C   ILE A 311    11135   8727   9257   -480    706   2002       C  
ATOM   2349  O   ILE A 311     585.760 -45.961 211.923  1.00 76.68           O  
ANISOU 2349  O   ILE A 311    11192   8897   9045   -528    811   1965       O  
ATOM   2350  CB  ILE A 311     584.266 -48.145 210.173  1.00 74.79           C  
ANISOU 2350  CB  ILE A 311    10806   8261   9349   -715   1025   2064       C  
ATOM   2351  CG1 ILE A 311     583.424 -48.357 208.917  1.00 73.32           C  
ANISOU 2351  CG1 ILE A 311    10398   8008   9451   -800   1134   1935       C  
ATOM   2352  CG2 ILE A 311     583.372 -47.632 211.295  1.00 74.96           C  
ANISOU 2352  CG2 ILE A 311    10940   8422   9118   -836   1242   2123       C  
ATOM   2353  CD1 ILE A 311     582.482 -49.533 209.019  1.00 73.77           C  
ANISOU 2353  CD1 ILE A 311    10527   7883   9620   -959   1292   2067       C  
ATOM   2354  N   GLY A 312     587.293 -47.484 211.347  1.00 71.67           N  
ANISOU 2354  N   GLY A 312    10607   8003   8622   -349    471   2099       N  
ATOM   2355  CA  GLY A 312     588.211 -47.061 212.388  1.00 73.54           C  
ANISOU 2355  CA  GLY A 312    10984   8357   8600   -246    291   2140       C  
ATOM   2356  C   GLY A 312     588.617 -45.612 212.174  1.00 73.40           C  
ANISOU 2356  C   GLY A 312    10793   8538   8556   -208    248   1905       C  
ATOM   2357  O   GLY A 312     588.525 -44.787 213.089  1.00 74.35           O  
ANISOU 2357  O   GLY A 312    11002   8821   8425   -230    276   1867       O  
ATOM   2358  N   SER A 313     589.051 -45.295 210.953  1.00 71.02           N  
ANISOU 2358  N   SER A 313    10252   8220   8514   -157    191   1742       N  
ATOM   2359  CA  SER A 313     589.385 -43.914 210.598  1.00 70.95           C  
ANISOU 2359  CA  SER A 313    10068   8365   8525   -140    174   1529       C  
ATOM   2360  C   SER A 313     588.138 -43.035 210.728  1.00 69.62           C  
ANISOU 2360  C   SER A 313     9873   8294   8284   -265    419   1453       C  
ATOM   2361  O   SER A 313     588.237 -41.846 210.989  1.00 70.20           O  
ANISOU 2361  O   SER A 313     9899   8497   8277   -265    427   1315       O  
ATOM   2362  CB  SER A 313     589.977 -43.823 209.175  1.00 70.07           C  
ANISOU 2362  CB  SER A 313     9716   8208   8698    -83    108   1397       C  
ATOM   2363  OG  SER A 313     588.996 -43.552 208.183  1.00 67.60           O  
ANISOU 2363  OG  SER A 313     9266   7886   8533   -171    295   1319       O  
ATOM   2364  N   GLY A 314     586.965 -43.635 210.557  1.00 73.68           N  
ANISOU 2364  N   GLY A 314    10410   8735   8849   -370    617   1533       N  
ATOM   2365  CA  GLY A 314     585.724 -42.918 210.718  1.00 72.40           C  
ANISOU 2365  CA  GLY A 314    10206   8663   8642   -480    854   1462       C  
ATOM   2366  C   GLY A 314     585.539 -42.484 212.148  1.00 74.22           C  
ANISOU 2366  C   GLY A 314    10625   9018   8559   -510    918   1495       C  
ATOM   2367  O   GLY A 314     585.350 -41.304 212.420  1.00 74.54           O  
ANISOU 2367  O   GLY A 314    10613   9188   8522   -513    977   1341       O  
ATOM   2368  N   ILE A 315     585.581 -43.439 213.068  1.00 82.79           N  
ANISOU 2368  N   ILE A 315    11942  10060   9457   -532    909   1695       N  
ATOM   2369  CA  ILE A 315     585.352 -43.114 214.467  1.00 84.63           C  
ANISOU 2369  CA  ILE A 315    12385  10430   9341   -570    987   1741       C  
ATOM   2370  C   ILE A 315     586.400 -42.150 214.995  1.00 86.63           C  
ANISOU 2370  C   ILE A 315    12665  10821   9431   -463    783   1608       C  
ATOM   2371  O   ILE A 315     586.067 -41.202 215.699  1.00 87.54           O  
ANISOU 2371  O   ILE A 315    12818  11090   9355   -494    880   1482       O  
ATOM   2372  CB  ILE A 315     585.364 -44.352 215.373  1.00 86.01           C  
ANISOU 2372  CB  ILE A 315    12840  10527   9312   -601    981   2017       C  
ATOM   2373  CG1 ILE A 315     584.751 -45.571 214.675  1.00 84.32           C  
ANISOU 2373  CG1 ILE A 315    12596  10101   9340   -682   1085   2166       C  
ATOM   2374  CG2 ILE A 315     584.667 -44.031 216.679  1.00 87.59           C  
ANISOU 2374  CG2 ILE A 315    13241  10886   9154   -695   1178   2061       C  
ATOM   2375  CD1 ILE A 315     583.267 -45.743 214.881  1.00 83.78           C  
ANISOU 2375  CD1 ILE A 315    12528  10043   9263   -868   1425   2206       C  
ATOM   2376  N   VAL A 316     587.666 -42.402 214.669  1.00 92.12           N  
ANISOU 2376  N   VAL A 316    13329  11460  10212   -340    502   1618       N  
ATOM   2377  CA  VAL A 316     588.765 -41.594 215.200  1.00 94.39           C  
ANISOU 2377  CA  VAL A 316    13630  11872  10364   -245    277   1493       C  
ATOM   2378  C   VAL A 316     588.619 -40.147 214.764  1.00 94.23           C  
ANISOU 2378  C   VAL A 316    13413  11941  10449   -268    349   1231       C  
ATOM   2379  O   VAL A 316     588.808 -39.214 215.549  1.00 96.08           O  
ANISOU 2379  O   VAL A 316    13702  12312  10492   -264    319   1093       O  
ATOM   2380  CB  VAL A 316     590.134 -42.126 214.748  1.00 95.19           C  
ANISOU 2380  CB  VAL A 316    13664  11890  10613   -109    -25   1526       C  
ATOM   2381  CG1 VAL A 316     591.240 -41.156 215.141  1.00 97.34           C  
ANISOU 2381  CG1 VAL A 316    13881  12296  10807    -30   -249   1349       C  
ATOM   2382  CG2 VAL A 316     590.385 -43.503 215.356  1.00 95.82           C  
ANISOU 2382  CG2 VAL A 316    13970  11869  10567    -57   -139   1791       C  
ATOM   2383  N   ASN A 317     588.260 -39.988 213.498  1.00 83.18           N  
ANISOU 2383  N   ASN A 317    11797  10454   9354   -290    440   1165       N  
ATOM   2384  CA  ASN A 317     588.008 -38.694 212.888  1.00 82.65           C  
ANISOU 2384  CA  ASN A 317    11541  10427   9434   -310    522    955       C  
ATOM   2385  C   ASN A 317     586.913 -37.877 213.576  1.00 82.68           C  
ANISOU 2385  C   ASN A 317    11594  10528   9291   -383    745    856       C  
ATOM   2386  O   ASN A 317     587.104 -36.707 213.905  1.00 84.29           O  
ANISOU 2386  O   ASN A 317    11768  10809   9449   -372    730    673       O  
ATOM   2387  CB  ASN A 317     587.626 -38.913 211.442  1.00 79.68           C  
ANISOU 2387  CB  ASN A 317    10968   9941   9365   -324    595    956       C  
ATOM   2388  CG  ASN A 317     587.690 -37.670 210.645  1.00 79.43           C  
ANISOU 2388  CG  ASN A 317    10748   9923   9508   -318    612    779       C  
ATOM   2389  OD1 ASN A 317     586.683 -37.023 210.413  1.00 78.00           O  
ANISOU 2389  OD1 ASN A 317    10498   9755   9385   -363    786    706       O  
ATOM   2390  ND2 ASN A 317     588.883 -37.317 210.207  1.00 81.01           N  
ANISOU 2390  ND2 ASN A 317    10857  10116   9809   -260    431    711       N  
ATOM   2391  N   THR A 318     585.756 -38.500 213.764  1.00 75.50           N  
ANISOU 2391  N   THR A 318    10746   9606   8335   -463    962    964       N  
ATOM   2392  CA  THR A 318     584.672 -37.895 214.517  1.00 75.76           C  
ANISOU 2392  CA  THR A 318    10826   9744   8215   -533   1201    878       C  
ATOM   2393  C   THR A 318     585.131 -37.618 215.936  1.00 78.67           C  
ANISOU 2393  C   THR A 318    11418  10252   8222   -519   1142    851       C  
ATOM   2394  O   THR A 318     584.823 -36.576 216.493  1.00 79.72           O  
ANISOU 2394  O   THR A 318    11554  10490   8245   -526   1233    663       O  
ATOM   2395  CB  THR A 318     583.404 -38.797 214.531  1.00 73.94           C  
ANISOU 2395  CB  THR A 318    10618   9478   7996   -639   1451   1019       C  
ATOM   2396  OG1 THR A 318     583.074 -39.230 213.197  1.00 71.30           O  
ANISOU 2396  OG1 THR A 318    10090   9015   7987   -650   1461   1050       O  
ATOM   2397  CG2 THR A 318     582.216 -38.042 215.124  1.00 74.13           C  
ANISOU 2397  CG2 THR A 318    10620   9618   7928   -706   1727    887       C  
ATOM   2398  N   ALA A 319     585.891 -38.544 216.509  1.00101.88           N  
ANISOU 2398  N   ALA A 319    14547  13188  10976   -488    972   1029       N  
ATOM   2399  CA  ALA A 319     586.371 -38.389 217.881  1.00104.54           C  
ANISOU 2399  CA  ALA A 319    15121  13673  10925   -466    880   1025       C  
ATOM   2400  C   ALA A 319     587.194 -37.116 218.061  1.00106.55           C  
ANISOU 2400  C   ALA A 319    15305  14016  11164   -401    709    767       C  
ATOM   2401  O   ALA A 319     586.938 -36.324 218.967  1.00108.19           O  
ANISOU 2401  O   ALA A 319    15607  14365  11136   -422    785    609       O  
ATOM   2402  CB  ALA A 319     587.185 -39.593 218.297  1.00105.26           C  
ANISOU 2402  CB  ALA A 319    15405  13720  10870   -412    665   1272       C  
ATOM   2403  N   PHE A 320     588.168 -36.910 217.184  1.00 98.33           N  
ANISOU 2403  N   PHE A 320    14089  12887  10384   -332    492    709       N  
ATOM   2404  CA  PHE A 320     589.072 -35.778 217.330  1.00100.41           C  
ANISOU 2404  CA  PHE A 320    14276  13212  10664   -287    311    475       C  
ATOM   2405  C   PHE A 320     588.499 -34.475 216.778  1.00100.05           C  
ANISOU 2405  C   PHE A 320    14050  13138  10828   -326    473    245       C  
ATOM   2406  O   PHE A 320     589.022 -33.398 217.064  1.00101.94           O  
ANISOU 2406  O   PHE A 320    14250  13421  11063   -314    379     25       O  
ATOM   2407  CB  PHE A 320     590.416 -36.093 216.671  1.00100.99           C  
ANISOU 2407  CB  PHE A 320    14227  13212  10934   -207     23    506       C  
ATOM   2408  CG  PHE A 320     591.388 -36.763 217.599  1.00102.70           C  
ANISOU 2408  CG  PHE A 320    14617  13507  10898   -131   -246    605       C  
ATOM   2409  CD1 PHE A 320     591.114 -38.013 218.122  1.00102.20           C  
ANISOU 2409  CD1 PHE A 320    14765  13432  10633   -116   -239    866       C  
ATOM   2410  CD2 PHE A 320     592.561 -36.133 217.970  1.00104.78           C  
ANISOU 2410  CD2 PHE A 320    14834  13851  11128    -77   -513    439       C  
ATOM   2411  CE1 PHE A 320     591.994 -38.625 218.983  1.00103.85           C  
ANISOU 2411  CE1 PHE A 320    15149  13706  10603    -28   -507    978       C  
ATOM   2412  CE2 PHE A 320     593.447 -36.744 218.831  1.00106.16           C  
ANISOU 2412  CE2 PHE A 320    15158  14109  11068      9   -791    526       C  
ATOM   2413  CZ  PHE A 320     593.161 -37.991 219.337  1.00105.74           C  
ANISOU 2413  CZ  PHE A 320    15329  14042  10804     44   -795    805       C  
ATOM   2414  N   THR A 321     587.424 -34.562 216.000  1.00 73.59           N  
ANISOU 2414  N   THR A 321    10588   9704   7669   -368    703    290       N  
ATOM   2415  CA  THR A 321     586.668 -33.360 215.636  1.00 73.14           C  
ANISOU 2415  CA  THR A 321    10391   9623   7775   -390    876     91       C  
ATOM   2416  C   THR A 321     586.024 -32.782 216.894  1.00 74.41           C  
ANISOU 2416  C   THR A 321    10698   9922   7653   -418   1027    -55       C  
ATOM   2417  O   THR A 321     586.050 -31.575 217.111  1.00 75.62           O  
ANISOU 2417  O   THR A 321    10804  10087   7839   -406   1039   -294       O  
ATOM   2418  CB  THR A 321     585.568 -33.637 214.565  1.00 69.97           C  
ANISOU 2418  CB  THR A 321     9834   9123   7628   -418   1075    173       C  
ATOM   2419  OG1 THR A 321     586.168 -33.964 213.307  1.00 68.53           O  
ANISOU 2419  OG1 THR A 321     9505   8823   7710   -389    942    258       O  
ATOM   2420  CG2 THR A 321     584.700 -32.421 214.360  1.00 69.85           C  
ANISOU 2420  CG2 THR A 321     9695   9090   7753   -419   1246    -23       C  
ATOM   2421  N   VAL A 322     585.466 -33.650 217.734  1.00 73.69           N  
ANISOU 2421  N   VAL A 322    10791   9928   7280   -459   1151     87       N  
ATOM   2422  CA  VAL A 322     584.908 -33.203 219.004  1.00 76.66           C  
ANISOU 2422  CA  VAL A 322    11332  10467   7329   -491   1308    -44       C  
ATOM   2423  C   VAL A 322     586.024 -32.748 219.967  1.00 78.74           C  
ANISOU 2423  C   VAL A 322    11751  10847   7321   -449   1066   -175       C  
ATOM   2424  O   VAL A 322     585.887 -31.729 220.647  1.00 80.45           O  
ANISOU 2424  O   VAL A 322    12003  11154   7411   -448   1120   -431       O  
ATOM   2425  CB  VAL A 322     584.048 -34.299 219.670  1.00 78.59           C  
ANISOU 2425  CB  VAL A 322    11750  10792   7317   -565   1521    167       C  
ATOM   2426  CG1 VAL A 322     583.724 -33.934 221.116  1.00 82.24           C  
ANISOU 2426  CG1 VAL A 322    12432  11461   7356   -596   1652     49       C  
ATOM   2427  CG2 VAL A 322     582.760 -34.506 218.886  1.00 77.22           C  
ANISOU 2427  CG2 VAL A 322    11396  10536   7406   -623   1798    212       C  
ATOM   2428  N   VAL A 323     587.129 -33.484 220.021  1.00 99.20           N  
ANISOU 2428  N   VAL A 323    14422  13434   9838   -407    788    -20       N  
ATOM   2429  CA  VAL A 323     588.251 -33.089 220.870  1.00101.83           C  
ANISOU 2429  CA  VAL A 323    14872  13881   9939   -361    514   -149       C  
ATOM   2430  C   VAL A 323     588.831 -31.742 220.418  1.00102.80           C  
ANISOU 2430  C   VAL A 323    14799  13942  10319   -344    403   -445       C  
ATOM   2431  O   VAL A 323     589.256 -30.934 221.249  1.00104.81           O  
ANISOU 2431  O   VAL A 323    15128  14303  10391   -339    300   -679       O  
ATOM   2432  CB  VAL A 323     589.358 -34.171 220.877  1.00102.24           C  
ANISOU 2432  CB  VAL A 323    15000  13919   9927   -297    212     79       C  
ATOM   2433  CG1 VAL A 323     590.648 -33.648 221.513  1.00104.28           C  
ANISOU 2433  CG1 VAL A 323    15295  14280  10046   -238   -122    -89       C  
ATOM   2434  CG2 VAL A 323     588.871 -35.403 221.601  1.00101.94           C  
ANISOU 2434  CG2 VAL A 323    15219  13944   9568   -316    298    363       C  
ATOM   2435  N   SER A 324     588.819 -31.489 219.110  1.00113.50           N  
ANISOU 2435  N   SER A 324    15913  15120  12091   -343    430   -436       N  
ATOM   2436  CA  SER A 324     589.366 -30.246 218.567  1.00114.17           C  
ANISOU 2436  CA  SER A 324    15815  15111  12455   -342    341   -675       C  
ATOM   2437  C   SER A 324     588.630 -29.001 219.073  1.00114.49           C  
ANISOU 2437  C   SER A 324    15866  15172  12465   -366    519   -955       C  
ATOM   2438  O   SER A 324     589.266 -28.017 219.444  1.00116.00           O  
ANISOU 2438  O   SER A 324    16040  15367  12668   -370    390  -1204       O  
ATOM   2439  CB  SER A 324     589.340 -30.271 217.038  1.00112.43           C  
ANISOU 2439  CB  SER A 324    15364  14706  12650   -342    377   -574       C  
ATOM   2440  OG  SER A 324     590.130 -29.218 216.503  1.00113.14           O  
ANISOU 2440  OG  SER A 324    15294  14698  12997   -351    252   -753       O  
ATOM   2441  N   LEU A 325     587.298 -29.057 219.086  1.00 97.94           N  
ANISOU 2441  N   LEU A 325    13782  13081  10349   -381    814   -929       N  
ATOM   2442  CA  LEU A 325     586.448 -27.974 219.595  1.00 98.14           C  
ANISOU 2442  CA  LEU A 325    13811  13128  10349   -386   1020  -1196       C  
ATOM   2443  C   LEU A 325     586.881 -27.454 220.946  1.00100.44           C  
ANISOU 2443  C   LEU A 325    14285  13583  10293   -389    934  -1432       C  
ATOM   2444  O   LEU A 325     586.831 -26.258 221.219  1.00101.11           O  
ANISOU 2444  O   LEU A 325    14335  13634  10448   -384    961  -1735       O  
ATOM   2445  CB  LEU A 325     585.006 -28.446 219.695  1.00 96.72           C  
ANISOU 2445  CB  LEU A 325    13649  12998  10101   -404   1341  -1103       C  
ATOM   2446  CG  LEU A 325     584.447 -28.773 218.320  1.00 94.28           C  
ANISOU 2446  CG  LEU A 325    13134  12527  10163   -398   1428   -929       C  
ATOM   2447  CD1 LEU A 325     583.412 -29.855 218.433  1.00 92.86           C  
ANISOU 2447  CD1 LEU A 325    12997  12418   9866   -440   1650   -726       C  
ATOM   2448  CD2 LEU A 325     583.851 -27.532 217.685  1.00 93.63           C  
ANISOU 2448  CD2 LEU A 325    12864  12303  10408   -359   1539  -1131       C  
ATOM   2449  N   PHE A 326     587.300 -28.368 221.799  1.00141.54           N  
ANISOU 2449  N   PHE A 326    19698  18962  15118   -395    823  -1294       N  
ATOM   2450  CA  PHE A 326     587.765 -27.994 223.110  1.00143.87           C  
ANISOU 2450  CA  PHE A 326    20193  19446  15025   -394    708  -1499       C  
ATOM   2451  C   PHE A 326     589.130 -27.373 223.008  1.00145.27           C  
ANISOU 2451  C   PHE A 326    20291  19573  15331   -380    368  -1665       C  
ATOM   2452  O   PHE A 326     589.328 -26.234 223.407  1.00146.47           O  
ANISOU 2452  O   PHE A 326    20425  19724  15504   -390    331  -1994       O  
ATOM   2453  CB  PHE A 326     587.776 -29.213 224.002  1.00144.40           C  
ANISOU 2453  CB  PHE A 326    20521  19708  14638   -399    683  -1257       C  
ATOM   2454  CG  PHE A 326     586.474 -29.927 224.007  1.00142.67           C  
ANISOU 2454  CG  PHE A 326    20356  19515  14335   -440   1026  -1062       C  
ATOM   2455  CD1 PHE A 326     585.291 -29.204 224.026  1.00142.11           C  
ANISOU 2455  CD1 PHE A 326    20206  19440  14349   -465   1356  -1252       C  
ATOM   2456  CD2 PHE A 326     586.419 -31.308 223.950  1.00141.52           C  
ANISOU 2456  CD2 PHE A 326    20320  19381  14069   -456   1023   -698       C  
ATOM   2457  CE1 PHE A 326     584.076 -29.840 224.021  1.00140.53           C  
ANISOU 2457  CE1 PHE A 326    20020  19273  14103   -514   1681  -1093       C  
ATOM   2458  CE2 PHE A 326     585.202 -31.960 223.944  1.00139.91           C  
ANISOU 2458  CE2 PHE A 326    20150  19190  13819   -518   1353   -528       C  
ATOM   2459  CZ  PHE A 326     584.027 -31.219 223.979  1.00139.44           C  
ANISOU 2459  CZ  PHE A 326    19992  19150  13838   -553   1685   -730       C  
ATOM   2460  N   VAL A 327     590.061 -28.121 222.434  1.00 98.13           N  
ANISOU 2460  N   VAL A 327    14255  13551   9479   -359    130  -1449       N  
ATOM   2461  CA  VAL A 327     591.431 -27.659 222.302  1.00 99.13           C  
ANISOU 2461  CA  VAL A 327    14274  13643   9747   -352   -199  -1586       C  
ATOM   2462  C   VAL A 327     591.537 -26.382 221.452  1.00 98.60           C  
ANISOU 2462  C   VAL A 327    13972  13368  10122   -391   -159  -1813       C  
ATOM   2463  O   VAL A 327     592.443 -25.581 221.655  1.00 99.59           O  
ANISOU 2463  O   VAL A 327    14033  13477  10331   -418   -363  -2053       O  
ATOM   2464  CB  VAL A 327     592.322 -28.768 221.703  1.00 98.65           C  
ANISOU 2464  CB  VAL A 327    14147  13549   9784   -311   -423  -1301       C  
ATOM   2465  CG1 VAL A 327     593.804 -28.401 221.814  1.00 99.69           C  
ANISOU 2465  CG1 VAL A 327    14178  13703   9996   -301   -784  -1456       C  
ATOM   2466  CG2 VAL A 327     592.054 -30.086 222.417  1.00 98.81           C  
ANISOU 2466  CG2 VAL A 327    14410  13718   9416   -270   -425  -1026       C  
ATOM   2467  N   VAL A 328     590.610 -26.168 220.525  1.00 90.63           N  
ANISOU 2467  N   VAL A 328    12841  12197   9397   -398     96  -1742       N  
ATOM   2468  CA  VAL A 328     590.679 -24.983 219.662  1.00 89.91           C  
ANISOU 2468  CA  VAL A 328    12548  11887   9726   -428    134  -1910       C  
ATOM   2469  C   VAL A 328     590.423 -23.683 220.423  1.00 90.86           C  
ANISOU 2469  C   VAL A 328    12716  11994   9810   -446    193  -2282       C  
ATOM   2470  O   VAL A 328     591.137 -22.692 220.238  1.00 91.19           O  
ANISOU 2470  O   VAL A 328    12654  11908  10087   -489     64  -2497       O  
ATOM   2471  CB  VAL A 328     589.693 -25.089 218.478  1.00 87.68           C  
ANISOU 2471  CB  VAL A 328    12135  11443   9737   -413    373  -1730       C  
ATOM   2472  CG1 VAL A 328     589.261 -23.729 217.984  1.00 87.04           C  
ANISOU 2472  CG1 VAL A 328    11932  11162   9977   -421    494  -1936       C  
ATOM   2473  CG2 VAL A 328     590.331 -25.871 217.350  1.00 86.68           C  
ANISOU 2473  CG2 VAL A 328    11876  11238   9819   -413    260  -1464       C  
ATOM   2474  N   GLN A 329     589.415 -23.677 221.284  1.00121.21           N  
ANISOU 2474  N   GLN A 329    16715  15967  13372   -422    398  -2373       N  
ATOM   2475  CA  GLN A 329     589.176 -22.505 222.099  1.00122.31           C  
ANISOU 2475  CA  GLN A 329    16915  16114  13444   -428    457  -2756       C  
ATOM   2476  C   GLN A 329     590.366 -22.252 223.031  1.00124.61           C  
ANISOU 2476  C   GLN A 329    17303  16538  13504   -461    156  -2973       C  
ATOM   2477  O   GLN A 329     590.654 -21.111 223.374  1.00125.54           O  
ANISOU 2477  O   GLN A 329    17398  16582  13721   -491     97  -3318       O  
ATOM   2478  CB  GLN A 329     587.879 -22.662 222.889  1.00122.36           C  
ANISOU 2478  CB  GLN A 329    17066  16272  13154   -395    753  -2810       C  
ATOM   2479  CG  GLN A 329     586.626 -22.461 222.046  1.00120.28           C  
ANISOU 2479  CG  GLN A 329    16658  15849  13193   -358   1052  -2734       C  
ATOM   2480  CD  GLN A 329     585.344 -22.841 222.782  1.00120.31           C  
ANISOU 2480  CD  GLN A 329    16774  16030  12908   -336   1363  -2744       C  
ATOM   2481  OE1 GLN A 329     585.352 -23.703 223.665  1.00121.57           O  
ANISOU 2481  OE1 GLN A 329    17130  16430  12632   -360   1373  -2643       O  
ATOM   2482  NE2 GLN A 329     584.233 -22.197 222.416  1.00118.93           N  
ANISOU 2482  NE2 GLN A 329    16471  15735  12982   -289   1621  -2861       N  
ATOM   2483  N   ARG A 330     591.082 -23.308 223.406  1.00152.93           N  
ANISOU 2483  N   ARG A 330    20990  20306  16811   -453    -54  -2777       N  
ATOM   2484  CA  ARG A 330     592.160 -23.180 224.389  1.00155.13           C  
ANISOU 2484  CA  ARG A 330    21373  20754  16817   -468   -365  -2973       C  
ATOM   2485  C   ARG A 330     593.443 -22.560 223.841  1.00155.02           C  
ANISOU 2485  C   ARG A 330    21151  20594  17156   -520   -645  -3107       C  
ATOM   2486  O   ARG A 330     593.925 -21.561 224.368  1.00156.00           O  
ANISOU 2486  O   ARG A 330    21264  20707  17303   -567   -771  -3463       O  
ATOM   2487  CB  ARG A 330     592.499 -24.543 224.988  1.00156.01           C  
ANISOU 2487  CB  ARG A 330    21665  21101  16512   -422   -517  -2698       C  
ATOM   2488  CG  ARG A 330     591.296 -25.313 225.455  1.00155.62           C  
ANISOU 2488  CG  ARG A 330    21817  21186  16127   -395   -232  -2504       C  
ATOM   2489  CD  ARG A 330     591.477 -25.876 226.845  1.00157.22           C  
ANISOU 2489  CD  ARG A 330    22318  21688  15729   -371   -351  -2502       C  
ATOM   2490  NE  ARG A 330     590.350 -26.728 227.213  1.00156.41           N  
ANISOU 2490  NE  ARG A 330    22404  21701  15325   -367    -54  -2262       N  
ATOM   2491  CZ  ARG A 330     589.183 -26.271 227.649  1.00156.59           C  
ANISOU 2491  CZ  ARG A 330    22502  21782  15214   -391    290  -2415       C  
ATOM   2492  NH1 ARG A 330     588.984 -24.965 227.772  1.00157.49           N  
ANISOU 2492  NH1 ARG A 330    22530  21834  15474   -404    370  -2814       N  
ATOM   2493  NH2 ARG A 330     588.213 -27.119 227.960  1.00155.82           N  
ANISOU 2493  NH2 ARG A 330    22556  21792  14857   -406    563  -2178       N  
ATOM   2494  N   ALA A 331     594.004 -23.161 222.798  1.00131.18           N  
ANISOU 2494  N   ALA A 331    17962  17467  14412   -521   -735  -2837       N  
ATOM   2495  CA  ALA A 331     595.349 -22.805 222.352  1.00131.16           C  
ANISOU 2495  CA  ALA A 331    17759  17377  14697   -576  -1014  -2927       C  
ATOM   2496  C   ALA A 331     595.365 -21.783 221.224  1.00129.67           C  
ANISOU 2496  C   ALA A 331    17345  16890  15033   -653   -897  -3009       C  
ATOM   2497  O   ALA A 331     594.316 -21.373 220.728  1.00128.49           O  
ANISOU 2497  O   ALA A 331    17192  16590  15036   -643   -617  -2978       O  
ATOM   2498  CB  ALA A 331     596.095 -24.054 221.920  1.00130.77           C  
ANISOU 2498  CB  ALA A 331    17648  17400  14637   -527  -1198  -2611       C  
ATOM   2499  N   GLY A 332     596.572 -21.393 220.819  1.00121.44           N  
ANISOU 2499  N   GLY A 332    16110  15763  14268   -728  -1115  -3103       N  
ATOM   2500  CA  GLY A 332     596.762 -20.449 219.732  1.00120.01           C  
ANISOU 2500  CA  GLY A 332    15720  15295  14583   -822  -1023  -3153       C  
ATOM   2501  C   GLY A 332     596.222 -20.951 218.408  1.00117.96           C  
ANISOU 2501  C   GLY A 332    15368  14898  14552   -792   -815  -2808       C  
ATOM   2502  O   GLY A 332     595.730 -22.073 218.315  1.00117.70           O  
ANISOU 2502  O   GLY A 332    15417  14987  14318   -705   -749  -2541       O  
ATOM   2503  N   ARG A 333     596.305 -20.119 217.378  1.00117.06           N  
ANISOU 2503  N   ARG A 333    15094  14526  14855   -871   -712  -2812       N  
ATOM   2504  CA  ARG A 333     595.761 -20.487 216.081  1.00114.98           C  
ANISOU 2504  CA  ARG A 333    14753  14135  14799   -844   -519  -2504       C  
ATOM   2505  C   ARG A 333     596.769 -21.295 215.293  1.00114.17           C  
ANISOU 2505  C   ARG A 333    14489  14077  14812   -867   -646  -2296       C  
ATOM   2506  O   ARG A 333     596.442 -22.339 214.738  1.00113.40           O  
ANISOU 2506  O   ARG A 333    14397  14045  14643   -793   -580  -2021       O  
ATOM   2507  CB  ARG A 333     595.357 -19.250 215.286  1.00113.57           C  
ANISOU 2507  CB  ARG A 333    14498  13658  14993   -905   -350  -2567       C  
ATOM   2508  CG  ARG A 333     594.043 -19.390 214.537  1.00111.96           C  
ANISOU 2508  CG  ARG A 333    14335  13359  14844   -819    -97  -2353       C  
ATOM   2509  CD  ARG A 333     592.840 -19.011 215.415  1.00112.75           C  
ANISOU 2509  CD  ARG A 333    14593  13484  14765   -737     47  -2521       C  
ATOM   2510  NE  ARG A 333     592.577 -19.974 216.491  1.00114.27           N  
ANISOU 2510  NE  ARG A 333    14935  13960  14522   -671     11  -2524       N  
ATOM   2511  CZ  ARG A 333     591.529 -19.915 217.309  1.00114.76           C  
ANISOU 2511  CZ  ARG A 333    15139  14110  14355   -602    159  -2637       C  
ATOM   2512  NH1 ARG A 333     590.641 -18.939 217.168  1.00113.94           N  
ANISOU 2512  NH1 ARG A 333    15027  13826  14439   -572    341  -2776       N  
ATOM   2513  NH2 ARG A 333     591.367 -20.828 218.262  1.00116.07           N  
ANISOU 2513  NH2 ARG A 333    15454  14537  14108   -560    132  -2606       N  
ATOM   2514  N   ARG A 334     598.004 -20.811 215.246  1.00101.00           N  
ANISOU 2514  N   ARG A 334    12664  12373  13339   -972   -824  -2447       N  
ATOM   2515  CA  ARG A 334     599.047 -21.503 214.502  1.00100.15           C  
ANISOU 2515  CA  ARG A 334    12367  12311  13374   -997   -937  -2290       C  
ATOM   2516  C   ARG A 334     599.815 -22.453 215.437  1.00101.75           C  
ANISOU 2516  C   ARG A 334    12591  12771  13296   -927  -1214  -2324       C  
ATOM   2517  O   ARG A 334     600.752 -23.132 215.016  1.00101.35           O  
ANISOU 2517  O   ARG A 334    12379  12791  13336   -919  -1349  -2225       O  
ATOM   2518  CB  ARG A 334     599.984 -20.492 213.801  1.00 99.24           C  
ANISOU 2518  CB  ARG A 334    12032  12008  13666  -1163   -952  -2410       C  
ATOM   2519  CG  ARG A 334     601.060 -19.829 214.670  1.00100.99           C  
ANISOU 2519  CG  ARG A 334    12162  12268  13940  -1267  -1196  -2743       C  
ATOM   2520  CD  ARG A 334     601.992 -18.852 213.890  1.00100.13           C  
ANISOU 2520  CD  ARG A 334    11814  11953  14277  -1461  -1179  -2843       C  
ATOM   2521  NE  ARG A 334     603.335 -18.832 214.481  1.00101.41           N  
ANISOU 2521  NE  ARG A 334    11797  12240  14493  -1542  -1463  -3072       N  
ATOM   2522  CZ  ARG A 334     604.474 -18.903 213.795  1.00100.44           C  
ANISOU 2522  CZ  ARG A 334    11401  12111  14651  -1649  -1522  -3050       C  
ATOM   2523  NH1 ARG A 334     604.455 -18.961 212.472  1.00 98.12           N  
ANISOU 2523  NH1 ARG A 334    11001  11688  14594  -1700  -1302  -2808       N  
ATOM   2524  NH2 ARG A 334     605.636 -18.907 214.435  1.00101.81           N  
ANISOU 2524  NH2 ARG A 334    11401  12419  14865  -1707  -1802  -3283       N  
ATOM   2525  N   THR A 335     599.396 -22.498 216.703  1.00123.76           N  
ANISOU 2525  N   THR A 335    15584  15703  15738   -866  -1294  -2462       N  
ATOM   2526  CA  THR A 335     599.848 -23.523 217.644  1.00125.17           C  
ANISOU 2526  CA  THR A 335    15857  16134  15568   -766  -1538  -2429       C  
ATOM   2527  C   THR A 335     599.312 -24.871 217.202  1.00124.53           C  
ANISOU 2527  C   THR A 335    15853  16114  15351   -647  -1442  -2077       C  
ATOM   2528  O   THR A 335     600.059 -25.812 216.924  1.00124.32           O  
ANISOU 2528  O   THR A 335    15729  16162  15344   -588  -1596  -1927       O  
ATOM   2529  CB  THR A 335     599.352 -23.275 219.085  1.00126.99           C  
ANISOU 2529  CB  THR A 335    16335  16513  15402   -729  -1600  -2630       C  
ATOM   2530  OG1 THR A 335     599.768 -21.986 219.539  1.00127.74           O  
ANISOU 2530  OG1 THR A 335    16374  16539  15621   -840  -1683  -2995       O  
ATOM   2531  CG2 THR A 335     599.894 -24.344 220.022  1.00128.30           C  
ANISOU 2531  CG2 THR A 335    16614  16939  15195   -622  -1876  -2563       C  
ATOM   2532  N   LEU A 336     597.988 -24.942 217.157  1.00 94.45           N  
ANISOU 2532  N   LEU A 336    12208  12260  11417   -611  -1186  -1966       N  
ATOM   2533  CA  LEU A 336     597.291 -26.128 216.731  1.00 93.85           C  
ANISOU 2533  CA  LEU A 336    12213  12215  11233   -522  -1058  -1653       C  
ATOM   2534  C   LEU A 336     597.631 -26.453 215.291  1.00 92.03           C  
ANISOU 2534  C   LEU A 336    11774  11857  11337   -538   -991  -1471       C  
ATOM   2535  O   LEU A 336     597.740 -27.615 214.933  1.00 91.60           O  
ANISOU 2535  O   LEU A 336    11713  11851  11239   -462  -1023  -1249       O  
ATOM   2536  CB  LEU A 336     595.792 -25.935 216.904  1.00 93.79           C  
ANISOU 2536  CB  LEU A 336    12372  12172  11090   -506   -779  -1619       C  
ATOM   2537  CG  LEU A 336     595.486 -25.476 218.329  1.00 95.54           C  
ANISOU 2537  CG  LEU A 336    12792  12529  10978   -502   -817  -1846       C  
ATOM   2538  CD1 LEU A 336     594.023 -25.099 218.486  1.00 95.39           C  
ANISOU 2538  CD1 LEU A 336    12898  12470  10878   -493   -516  -1869       C  
ATOM   2539  CD2 LEU A 336     595.892 -26.560 219.320  1.00 96.78           C  
ANISOU 2539  CD2 LEU A 336    13115  12912  10745   -425  -1023  -1747       C  
ATOM   2540  N   HIS A 337     597.820 -25.436 214.461  1.00 83.09           N  
ANISOU 2540  N   HIS A 337    10479  10555  10535   -637   -898  -1564       N  
ATOM   2541  CA  HIS A 337     598.124 -25.708 213.062  1.00 81.06           C  
ANISOU 2541  CA  HIS A 337    10039  10194  10565   -660   -813  -1390       C  
ATOM   2542  C   HIS A 337     599.503 -26.327 212.905  1.00 81.04           C  
ANISOU 2542  C   HIS A 337     9862  10279  10650   -650  -1035  -1381       C  
ATOM   2543  O   HIS A 337     599.754 -27.054 211.955  1.00 79.94           O  
ANISOU 2543  O   HIS A 337     9611  10126  10638   -620   -993  -1205       O  
ATOM   2544  CB  HIS A 337     598.039 -24.444 212.205  1.00 79.37           C  
ANISOU 2544  CB  HIS A 337     9711   9773  10673   -776   -658  -1468       C  
ATOM   2545  CG  HIS A 337     598.089 -24.718 210.730  1.00 76.92           C  
ANISOU 2545  CG  HIS A 337     9264   9369  10594   -795   -521  -1260       C  
ATOM   2546  ND1 HIS A 337     597.320 -25.693 210.127  1.00 75.85           N  
ANISOU 2546  ND1 HIS A 337     9186   9260  10372   -706   -402  -1024       N  
ATOM   2547  CD2 HIS A 337     598.815 -24.146 209.741  1.00 75.30           C  
ANISOU 2547  CD2 HIS A 337     8873   9049  10688   -901   -479  -1259       C  
ATOM   2548  CE1 HIS A 337     597.567 -25.704 208.827  1.00 73.46           C  
ANISOU 2548  CE1 HIS A 337     8746   8877  10288   -745   -303   -898       C  
ATOM   2549  NE2 HIS A 337     598.469 -24.775 208.567  1.00 73.09           N  
ANISOU 2549  NE2 HIS A 337     8555   8747  10469   -864   -337  -1026       N  
ATOM   2550  N   LEU A 338     600.402 -26.035 213.834  1.00 96.76           N  
ANISOU 2550  N   LEU A 338    11819  12368  12579   -671  -1278  -1590       N  
ATOM   2551  CA  LEU A 338     601.754 -26.564 213.732  1.00 96.77           C  
ANISOU 2551  CA  LEU A 338    11617  12459  12691   -653  -1512  -1612       C  
ATOM   2552  C   LEU A 338     601.802 -27.982 214.276  1.00 97.70           C  
ANISOU 2552  C   LEU A 338    11850  12732  12538   -489  -1671  -1445       C  
ATOM   2553  O   LEU A 338     602.147 -28.913 213.545  1.00 96.50           O  
ANISOU 2553  O   LEU A 338    11593  12582  12492   -419  -1676  -1273       O  
ATOM   2554  CB  LEU A 338     602.752 -25.665 214.468  1.00 97.88           C  
ANISOU 2554  CB  LEU A 338    11642  12641  12906   -746  -1736  -1919       C  
ATOM   2555  CG  LEU A 338     603.884 -25.019 213.650  1.00 96.86           C  
ANISOU 2555  CG  LEU A 338    11194  12426  13184   -885  -1756  -2038       C  
ATOM   2556  CD1 LEU A 338     603.649 -25.107 212.156  1.00 94.76           C  
ANISOU 2556  CD1 LEU A 338    10817  12018  13168   -928  -1486  -1832       C  
ATOM   2557  CD2 LEU A 338     604.079 -23.573 214.052  1.00 97.41           C  
ANISOU 2557  CD2 LEU A 338    11224  12391  13395  -1048  -1769  -2328       C  
ATOM   2558  N   ILE A 339     601.451 -28.140 215.550  1.00 89.65           N  
ANISOU 2558  N   ILE A 339    11059  11837  11169   -426  -1795  -1495       N  
ATOM   2559  CA  ILE A 339     601.324 -29.460 216.158  1.00 90.24           C  
ANISOU 2559  CA  ILE A 339    11305  12037  10946   -274  -1924  -1299       C  
ATOM   2560  C   ILE A 339     600.527 -30.408 215.265  1.00 88.80           C  
ANISOU 2560  C   ILE A 339    11171  11765  10803   -218  -1702  -1010       C  
ATOM   2561  O   ILE A 339     600.907 -31.563 215.082  1.00 88.31           O  
ANISOU 2561  O   ILE A 339    11092  11731  10732   -108  -1810   -837       O  
ATOM   2562  CB  ILE A 339     600.645 -29.384 217.533  1.00 91.98           C  
ANISOU 2562  CB  ILE A 339    11825  12381  10742   -243  -1967  -1352       C  
ATOM   2563  CG1 ILE A 339     601.612 -28.825 218.570  1.00 93.63           C  
ANISOU 2563  CG1 ILE A 339    12008  12731  10838   -255  -2283  -1621       C  
ATOM   2564  CG2 ILE A 339     600.139 -30.762 217.970  1.00 92.13           C  
ANISOU 2564  CG2 ILE A 339    12072  12477  10458   -110  -1985  -1072       C  
ATOM   2565  CD1 ILE A 339     601.067 -28.855 219.977  1.00 95.36           C  
ANISOU 2565  CD1 ILE A 339    12538  13112  10584   -211  -2355  -1674       C  
ATOM   2566  N   GLY A 340     599.433 -29.908 214.703  1.00 98.27           N  
ANISOU 2566  N   GLY A 340    12424  12850  12064   -288  -1405   -972       N  
ATOM   2567  CA  GLY A 340     598.622 -30.684 213.785  1.00 96.97           C  
ANISOU 2567  CA  GLY A 340    12285  12600  11960   -254  -1191   -732       C  
ATOM   2568  C   GLY A 340     599.410 -31.135 212.571  1.00 95.28           C  
ANISOU 2568  C   GLY A 340    11834  12325  12044   -242  -1208   -657       C  
ATOM   2569  O   GLY A 340     599.465 -32.330 212.262  1.00 94.63           O  
ANISOU 2569  O   GLY A 340    11763  12247  11946   -146  -1238   -478       O  
ATOM   2570  N   LEU A 341     600.029 -30.174 211.890  1.00 87.27           N  
ANISOU 2570  N   LEU A 341    10609  11246  11305   -344  -1177   -799       N  
ATOM   2571  CA  LEU A 341     600.880 -30.458 210.738  1.00 85.43           C  
ANISOU 2571  CA  LEU A 341    10129  10975  11356   -353  -1171   -761       C  
ATOM   2572  C   LEU A 341     602.010 -31.429 211.087  1.00 85.94           C  
ANISOU 2572  C   LEU A 341    10091  11146  11415   -240  -1439   -757       C  
ATOM   2573  O   LEU A 341     602.300 -32.347 210.318  1.00 84.77           O  
ANISOU 2573  O   LEU A 341     9844  10984  11380   -166  -1422   -636       O  
ATOM   2574  CB  LEU A 341     601.478 -29.164 210.178  1.00 84.38           C  
ANISOU 2574  CB  LEU A 341     9797  10767  11496   -505  -1111   -931       C  
ATOM   2575  CG  LEU A 341     600.638 -28.207 209.327  1.00 82.87           C  
ANISOU 2575  CG  LEU A 341     9625  10425  11436   -613   -839   -902       C  
ATOM   2576  CD1 LEU A 341     601.386 -26.897 209.145  1.00 82.67           C  
ANISOU 2576  CD1 LEU A 341     9437  10320  11656   -769   -839  -1091       C  
ATOM   2577  CD2 LEU A 341     600.279 -28.805 207.981  1.00 80.16           C  
ANISOU 2577  CD2 LEU A 341     9229  10030  11199   -591   -653   -705       C  
ATOM   2578  N   ALA A 342     602.637 -31.220 212.246  1.00 90.35           N  
ANISOU 2578  N   ALA A 342    10674  11812  11844   -216  -1695   -901       N  
ATOM   2579  CA  ALA A 342     603.751 -32.059 212.699  1.00 90.97           C  
ANISOU 2579  CA  ALA A 342    10650  11999  11916    -90  -1998   -913       C  
ATOM   2580  C   ALA A 342     603.384 -33.548 212.752  1.00 90.90           C  
ANISOU 2580  C   ALA A 342    10793  11991  11755     78  -2034   -666       C  
ATOM   2581  O   ALA A 342     603.927 -34.358 211.994  1.00 89.82           O  
ANISOU 2581  O   ALA A 342    10498  11824  11805    159  -2056   -590       O  
ATOM   2582  CB  ALA A 342     604.238 -31.594 214.059  1.00 92.89           C  
ANISOU 2582  CB  ALA A 342    10957  12370  11965    -83  -2276  -1094       C  
ATOM   2583  N   GLY A 343     602.463 -33.894 213.649  1.00100.12           N  
ANISOU 2583  N   GLY A 343    12267  13185  12590    123  -2028   -551       N  
ATOM   2584  CA  GLY A 343     602.025 -35.264 213.825  1.00 99.99           C  
ANISOU 2584  CA  GLY A 343    12433  13145  12413    259  -2052   -304       C  
ATOM   2585  C   GLY A 343     601.682 -35.904 212.504  1.00 98.19           C  
ANISOU 2585  C   GLY A 343    12109  12788  12409    267  -1839   -168       C  
ATOM   2586  O   GLY A 343     602.076 -37.040 212.244  1.00 97.67           O  
ANISOU 2586  O   GLY A 343    12012  12686  12412    396  -1937    -45       O  
ATOM   2587  N   MET A 344     600.972 -35.159 211.660  1.00 82.57           N  
ANISOU 2587  N   MET A 344    10085  10738  10551    138  -1559   -200       N  
ATOM   2588  CA  MET A 344     600.588 -35.662 210.341  1.00 80.69           C  
ANISOU 2588  CA  MET A 344     9760  10395  10505    133  -1351    -91       C  
ATOM   2589  C   MET A 344     601.805 -36.003 209.480  1.00 79.39           C  
ANISOU 2589  C   MET A 344     9312  10231  10620    183  -1438   -153       C  
ATOM   2590  O   MET A 344     601.816 -37.006 208.762  1.00 78.13           O  
ANISOU 2590  O   MET A 344     9113  10013  10560    265  -1395    -48       O  
ATOM   2591  CB  MET A 344     599.708 -34.652 209.594  1.00 79.96           C  
ANISOU 2591  CB  MET A 344     9653  10239  10488     -9  -1072   -128       C  
ATOM   2592  CG  MET A 344     598.220 -34.625 210.001  1.00 80.80           C  
ANISOU 2592  CG  MET A 344    10004  10314  10382    -40   -899    -27       C  
ATOM   2593  SD  MET A 344     597.147 -34.226 208.583  1.00 79.08           S  
ANISOU 2593  SD  MET A 344     9730   9988  10327   -126   -585     29       S  
ATOM   2594  CE  MET A 344     598.034 -32.844 207.894  1.00 77.74           C  
ANISOU 2594  CE  MET A 344     9333   9803  10403   -232   -568   -147       C  
ATOM   2595  N   ALA A 345     602.831 -35.167 209.541  1.00 81.59           N  
ANISOU 2595  N   ALA A 345     9384  10575  11043    128  -1548   -342       N  
ATOM   2596  CA  ALA A 345     604.037 -35.457 208.786  1.00 80.48           C  
ANISOU 2596  CA  ALA A 345     8947  10456  11178    168  -1619   -423       C  
ATOM   2597  C   ALA A 345     604.684 -36.738 209.310  1.00 81.21           C  
ANISOU 2597  C   ALA A 345     9040  10578  11239    370  -1883   -357       C  
ATOM   2598  O   ALA A 345     605.010 -37.637 208.538  1.00 80.15           O  
ANISOU 2598  O   ALA A 345     8790  10400  11265    466  -1857   -305       O  
ATOM   2599  CB  ALA A 345     604.995 -34.300 208.856  1.00 80.73           C  
ANISOU 2599  CB  ALA A 345     8749  10550  11375     52  -1689   -644       C  
ATOM   2600  N   GLY A 346     604.842 -36.823 210.628  1.00 70.61           N  
ANISOU 2600  N   GLY A 346     7841   9306   9680    441  -2137   -358       N  
ATOM   2601  CA  GLY A 346     605.397 -38.001 211.266  1.00 72.01           C  
ANISOU 2601  CA  GLY A 346     8064   9502   9793    646  -2420   -266       C  
ATOM   2602  C   GLY A 346     604.557 -39.258 211.102  1.00 71.19           C  
ANISOU 2602  C   GLY A 346     8185   9276   9589    750  -2332    -19       C  
ATOM   2603  O   GLY A 346     605.102 -40.360 210.985  1.00 71.60           O  
ANISOU 2603  O   GLY A 346     8184   9276   9744    921  -2482     56       O  
ATOM   2604  N   CYS A 347     603.234 -39.107 211.104  1.00 80.91           N  
ANISOU 2604  N   CYS A 347     9654  10448  10639    649  -2095     98       N  
ATOM   2605  CA  CYS A 347     602.352 -40.247 210.859  1.00 80.11           C  
ANISOU 2605  CA  CYS A 347     9747  10217  10475    709  -1977    318       C  
ATOM   2606  C   CYS A 347     602.488 -40.773 209.435  1.00 78.29           C  
ANISOU 2606  C   CYS A 347     9322   9890  10535    728  -1821    308       C  
ATOM   2607  O   CYS A 347     602.484 -41.986 209.204  1.00 77.80           O  
ANISOU 2607  O   CYS A 347     9306   9718  10536    854  -1862    428       O  
ATOM   2608  CB  CYS A 347     600.905 -39.874 211.124  1.00 80.14           C  
ANISOU 2608  CB  CYS A 347     9999  10197  10253    580  -1740    412       C  
ATOM   2609  SG  CYS A 347     600.460 -39.839 212.863  1.00 82.12           S  
ANISOU 2609  SG  CYS A 347    10581  10536  10085    595  -1884    507       S  
ATOM   2610  N   ALA A 348     602.614 -39.850 208.482  1.00 91.08           N  
ANISOU 2610  N   ALA A 348    10734  11545  12327    603  -1642    161       N  
ATOM   2611  CA  ALA A 348     602.822 -40.206 207.076  1.00 89.26           C  
ANISOU 2611  CA  ALA A 348    10308  11260  12346    606  -1481    122       C  
ATOM   2612  C   ALA A 348     604.210 -40.806 206.874  1.00 89.40           C  
ANISOU 2612  C   ALA A 348    10077  11304  12587    754  -1677     24       C  
ATOM   2613  O   ALA A 348     604.568 -41.253 205.784  1.00 88.24           O  
ANISOU 2613  O   ALA A 348     9750  11126  12652    789  -1571    -31       O  
ATOM   2614  CB  ALA A 348     602.639 -38.992 206.184  1.00 87.96           C  
ANISOU 2614  CB  ALA A 348    10009  11137  12275    429  -1248     12       C  
ATOM   2615  N   ILE A 349     604.999 -40.790 207.938  1.00 95.42           N  
ANISOU 2615  N   ILE A 349    10820  12136  13298    845  -1966    -15       N  
ATOM   2616  CA  ILE A 349     606.295 -41.433 207.937  1.00 95.87           C  
ANISOU 2616  CA  ILE A 349    10645  12219  13563   1018  -2202   -101       C  
ATOM   2617  C   ILE A 349     606.106 -42.862 208.424  1.00 96.49           C  
ANISOU 2617  C   ILE A 349    10921  12171  13570   1220  -2367     87       C  
ATOM   2618  O   ILE A 349     606.548 -43.816 207.781  1.00 96.00           O  
ANISOU 2618  O   ILE A 349    10734  12021  13719   1361  -2387     81       O  
ATOM   2619  CB  ILE A 349     607.308 -40.666 208.826  1.00 97.31           C  
ANISOU 2619  CB  ILE A 349    10678  12548  13746   1020  -2468   -255       C  
ATOM   2620  CG1 ILE A 349     607.909 -39.478 208.054  1.00 96.66           C  
ANISOU 2620  CG1 ILE A 349    10287  12559  13881    845  -2314   -476       C  
ATOM   2621  CG2 ILE A 349     608.395 -41.605 209.351  1.00 98.37           C  
ANISOU 2621  CG2 ILE A 349    10692  12696  13987   1262  -2817   -268       C  
ATOM   2622  CD1 ILE A 349     608.567 -38.429 208.929  1.00 97.32           C  
ANISOU 2622  CD1 ILE A 349    10270  12771  13936    766  -2509   -640       C  
ATOM   2623  N   LEU A 350     605.416 -42.993 209.554  1.00 86.67           N  
ANISOU 2623  N   LEU A 350     9996  10909  12025   1227  -2469    254       N  
ATOM   2624  CA  LEU A 350     605.023 -44.293 210.092  1.00 87.09           C  
ANISOU 2624  CA  LEU A 350    10307  10818  11966   1381  -2588    484       C  
ATOM   2625  C   LEU A 350     604.353 -45.129 209.028  1.00 85.54           C  
ANISOU 2625  C   LEU A 350    10139  10449  11913   1379  -2350    560       C  
ATOM   2626  O   LEU A 350     604.606 -46.318 208.906  1.00 85.64           O  
ANISOU 2626  O   LEU A 350    10174  10316  12052   1549  -2456    646       O  
ATOM   2627  CB  LEU A 350     604.080 -44.124 211.276  1.00 88.04           C  
ANISOU 2627  CB  LEU A 350    10789  10956  11705   1313  -2604    659       C  
ATOM   2628  CG  LEU A 350     604.753 -44.422 212.606  1.00 89.83           C  
ANISOU 2628  CG  LEU A 350    11137  11249  11747   1469  -2978    733       C  
ATOM   2629  CD1 LEU A 350     605.906 -43.464 212.822  1.00 90.93           C  
ANISOU 2629  CD1 LEU A 350    10998  11577  11976   1471  -3180    484       C  
ATOM   2630  CD2 LEU A 350     603.751 -44.313 213.729  1.00 90.21           C  
ANISOU 2630  CD2 LEU A 350    11566  11324  11386   1392  -2950    914       C  
ATOM   2631  N   MET A 351     603.487 -44.480 208.263  1.00 89.97           N  
ANISOU 2631  N   MET A 351    10701  11024  12460   1190  -2039    520       N  
ATOM   2632  CA  MET A 351     602.833 -45.106 207.131  1.00 88.48           C  
ANISOU 2632  CA  MET A 351    10509  10706  12404   1161  -1804    547       C  
ATOM   2633  C   MET A 351     603.846 -45.687 206.156  1.00 88.09           C  
ANISOU 2633  C   MET A 351    10176  10624  12669   1291  -1838    403       C  
ATOM   2634  O   MET A 351     603.932 -46.903 205.998  1.00 88.31           O  
ANISOU 2634  O   MET A 351    10247  10493  12812   1441  -1908    470       O  
ATOM   2635  CB  MET A 351     601.940 -44.097 206.420  1.00 87.29           C  
ANISOU 2635  CB  MET A 351    10348  10619  12200    947  -1505    490       C  
ATOM   2636  CG  MET A 351     600.481 -44.409 206.567  1.00 86.74           C  
ANISOU 2636  CG  MET A 351    10548  10452  11957    857  -1337    658       C  
ATOM   2637  SD  MET A 351     600.199 -46.077 205.990  1.00 86.12           S  
ANISOU 2637  SD  MET A 351    10540  10153  12028    973  -1321    761       S  
ATOM   2638  CE  MET A 351     598.430 -46.231 206.236  1.00 85.41           C  
ANISOU 2638  CE  MET A 351    10737   9977  11738    817  -1106    938       C  
ATOM   2639  N   THR A 352     604.624 -44.819 205.522  1.00107.47           N  
ANISOU 2639  N   THR A 352    12341  13222  15270   1232  -1780    200       N  
ATOM   2640  CA  THR A 352     605.616 -45.247 204.541  1.00107.01           C  
ANISOU 2640  CA  THR A 352    11980  13171  15508   1336  -1768     31       C  
ATOM   2641  C   THR A 352     606.611 -46.294 205.076  1.00108.38           C  
ANISOU 2641  C   THR A 352    12074  13271  15834   1594  -2073     31       C  
ATOM   2642  O   THR A 352     607.249 -46.997 204.298  1.00108.31           O  
ANISOU 2642  O   THR A 352    11862  13211  16077   1723  -2061    -85       O  
ATOM   2643  CB  THR A 352     606.391 -44.047 204.021  1.00106.42           C  
ANISOU 2643  CB  THR A 352    11609  13278  15547   1214  -1678   -171       C  
ATOM   2644  OG1 THR A 352     606.370 -43.032 205.026  1.00107.29           O  
ANISOU 2644  OG1 THR A 352    11792  13486  15487   1116  -1788   -156       O  
ATOM   2645  CG2 THR A 352     605.729 -43.495 202.780  1.00104.55           C  
ANISOU 2645  CG2 THR A 352    11345  13068  15312   1036  -1337   -213       C  
ATOM   2646  N   ILE A 353     606.738 -46.392 206.398  1.00 95.63           N  
ANISOU 2646  N   ILE A 353    10621  11653  14059   1679  -2348    155       N  
ATOM   2647  CA  ILE A 353     607.517 -47.459 207.037  1.00 97.03           C  
ANISOU 2647  CA  ILE A 353    10793  11733  14341   1944  -2673    214       C  
ATOM   2648  C   ILE A 353     606.761 -48.772 207.017  1.00 97.06           C  
ANISOU 2648  C   ILE A 353    11063  11484  14331   2045  -2653    416       C  
ATOM   2649  O   ILE A 353     607.260 -49.780 206.529  1.00 97.14           O  
ANISOU 2649  O   ILE A 353    10964  11354  14592   2229  -2718    373       O  
ATOM   2650  CB  ILE A 353     607.849 -47.142 208.503  1.00 98.63           C  
ANISOU 2650  CB  ILE A 353    11123  12025  14328   2003  -2994    305       C  
ATOM   2651  CG1 ILE A 353     608.784 -45.944 208.606  1.00 98.90           C  
ANISOU 2651  CG1 ILE A 353    10858  12291  14428   1927  -3075     75       C  
ATOM   2652  CG2 ILE A 353     608.474 -48.341 209.172  1.00100.06           C  
ANISOU 2652  CG2 ILE A 353    11363  12074  14582   2289  -3336    424       C  
ATOM   2653  CD1 ILE A 353     609.169 -45.627 210.022  1.00100.42           C  
ANISOU 2653  CD1 ILE A 353    11158  12591  14408   1990  -3415    125       C  
ATOM   2654  N   ALA A 354     605.563 -48.748 207.592  1.00 94.72           N  
ANISOU 2654  N   ALA A 354    11112  11126  13751   1920  -2564    627       N  
ATOM   2655  CA  ALA A 354     604.656 -49.882 207.559  1.00 94.50           C  
ANISOU 2655  CA  ALA A 354    11354  10853  13698   1951  -2491    827       C  
ATOM   2656  C   ALA A 354     604.539 -50.392 206.139  1.00 93.24           C  
ANISOU 2656  C   ALA A 354    11033  10591  13804   1947  -2269    685       C  
ATOM   2657  O   ALA A 354     604.803 -51.562 205.876  1.00 93.77           O  
ANISOU 2657  O   ALA A 354    11100  10454  14073   2120  -2351    705       O  
ATOM   2658  CB  ALA A 354     603.291 -49.497 208.097  1.00 94.04           C  
ANISOU 2658  CB  ALA A 354    11611  10797  13322   1746  -2320   1009       C  
ATOM   2659  N   LEU A 355     604.171 -49.498 205.224  1.00107.20           N  
ANISOU 2659  N   LEU A 355    12666  12499  15567   1756  -1997    536       N  
ATOM   2660  CA  LEU A 355     604.027 -49.853 203.816  1.00106.08           C  
ANISOU 2660  CA  LEU A 355    12376  12306  15625   1732  -1771    384       C  
ATOM   2661  C   LEU A 355     605.337 -50.375 203.232  1.00106.57           C  
ANISOU 2661  C   LEU A 355    12134  12363  15997   1934  -1878    185       C  
ATOM   2662  O   LEU A 355     605.326 -51.082 202.224  1.00106.16           O  
ANISOU 2662  O   LEU A 355    11994  12209  16131   1986  -1752     69       O  
ATOM   2663  CB  LEU A 355     603.535 -48.657 202.999  1.00104.66           C  
ANISOU 2663  CB  LEU A 355    12100  12309  15358   1502  -1494    272       C  
ATOM   2664  CG  LEU A 355     602.089 -48.206 203.205  1.00103.94           C  
ANISOU 2664  CG  LEU A 355    12263  12210  15019   1303  -1322    420       C  
ATOM   2665  CD1 LEU A 355     601.863 -46.942 202.421  1.00102.76           C  
ANISOU 2665  CD1 LEU A 355    11981  12245  14820   1120  -1102    298       C  
ATOM   2666  CD2 LEU A 355     601.087 -49.265 202.786  1.00103.85           C  
ANISOU 2666  CD2 LEU A 355    12428  11996  15036   1292  -1210    509       C  
ATOM   2667  N   ALA A 356     606.457 -50.030 203.869  1.00117.80           N  
ANISOU 2667  N   ALA A 356    13383  13899  17477   2049  -2112    125       N  
ATOM   2668  CA  ALA A 356     607.772 -50.497 203.427  1.00118.42           C  
ANISOU 2668  CA  ALA A 356    13135  13987  17871   2258  -2235    -76       C  
ATOM   2669  C   ALA A 356     608.173 -51.833 204.062  1.00119.90           C  
ANISOU 2669  C   ALA A 356    13417  13941  18200   2540  -2527     35       C  
ATOM   2670  O   ALA A 356     608.411 -52.800 203.346  1.00120.16           O  
ANISOU 2670  O   ALA A 356    13359  13814  18481   2687  -2494    -62       O  
ATOM   2671  CB  ALA A 356     608.827 -49.450 203.714  1.00118.66           C  
ANISOU 2671  CB  ALA A 356    12882  14263  17942   2237  -2343   -226       C  
ATOM   2672  N   LEU A 357     608.250 -51.886 205.393  1.00105.07           N  
ANISOU 2672  N   LEU A 357    11727  12036  16157   2621  -2815    236       N  
ATOM   2673  CA  LEU A 357     608.637 -53.113 206.106  1.00106.63           C  
ANISOU 2673  CA  LEU A 357    12050  12001  16462   2899  -3127    388       C  
ATOM   2674  C   LEU A 357     607.549 -54.189 206.153  1.00106.69           C  
ANISOU 2674  C   LEU A 357    12418  11702  16416   2897  -3049    619       C  
ATOM   2675  O   LEU A 357     607.760 -55.250 206.740  1.00108.01           O  
ANISOU 2675  O   LEU A 357    12737  11633  16669   3114  -3291    784       O  
ATOM   2676  CB  LEU A 357     609.044 -52.791 207.540  1.00108.00           C  
ANISOU 2676  CB  LEU A 357    12340  12266  16429   2979  -3471    547       C  
ATOM   2677  CG  LEU A 357     610.200 -51.823 207.694  1.00108.46           C  
ANISOU 2677  CG  LEU A 357    12045  12605  16560   3001  -3621    326       C  
ATOM   2678  CD1 LEU A 357     610.562 -51.718 209.157  1.00110.17           C  
ANISOU 2678  CD1 LEU A 357    12414  12882  16562   3114  -4008    491       C  
ATOM   2679  CD2 LEU A 357     611.368 -52.303 206.864  1.00108.73           C  
ANISOU 2679  CD2 LEU A 357    11668  12627  17016   3208  -3674     67       C  
ATOM   2680  N   LEU A 358     606.392 -53.905 205.559  1.00111.60           N  
ANISOU 2680  N   LEU A 358    13174  12322  16907   2651  -2724    636       N  
ATOM   2681  CA  LEU A 358     605.266 -54.838 205.535  1.00111.57           C  
ANISOU 2681  CA  LEU A 358    13486  12042  16863   2599  -2612    829       C  
ATOM   2682  C   LEU A 358     605.707 -56.208 205.053  1.00112.51           C  
ANISOU 2682  C   LEU A 358    13556  11868  17323   2834  -2704    777       C  
ATOM   2683  O   LEU A 358     605.321 -57.231 205.614  1.00113.43           O  
ANISOU 2683  O   LEU A 358    13947  11694  17457   2924  -2821   1007       O  
ATOM   2684  CB  LEU A 358     604.149 -54.300 204.630  1.00109.97           C  
ANISOU 2684  CB  LEU A 358    13309  11915  16559   2322  -2243    753       C  
ATOM   2685  CG  LEU A 358     602.719 -54.859 204.629  1.00109.61           C  
ANISOU 2685  CG  LEU A 358    13574  11669  16403   2165  -2066    937       C  
ATOM   2686  CD1 LEU A 358     602.624 -56.259 204.032  1.00110.38           C  
ANISOU 2686  CD1 LEU A 358    13714  11445  16782   2289  -2060    912       C  
ATOM   2687  CD2 LEU A 358     602.117 -54.829 206.018  1.00110.06           C  
ANISOU 2687  CD2 LEU A 358    13964  11684  16170   2107  -2174   1253       C  
ATOM   2688  N   GLU A 359     606.523 -56.207 204.005  1.00158.91           N  
ANISOU 2688  N   GLU A 359    19083  17820  23476   2929  -2638    470       N  
ATOM   2689  CA  GLU A 359     606.920 -57.429 203.320  1.00159.70           C  
ANISOU 2689  CA  GLU A 359    19091  17661  23929   3141  -2666    342       C  
ATOM   2690  C   GLU A 359     607.871 -58.292 204.149  1.00161.53           C  
ANISOU 2690  C   GLU A 359    19324  17699  24352   3472  -3047    444       C  
ATOM   2691  O   GLU A 359     607.858 -59.514 204.038  1.00162.55           O  
ANISOU 2691  O   GLU A 359    19554  17494  24713   3648  -3128    487       O  
ATOM   2692  CB  GLU A 359     607.565 -57.081 201.977  1.00159.01           C  
ANISOU 2692  CB  GLU A 359    18612  17755  24049   3143  -2465    -37       C  
ATOM   2693  CG  GLU A 359     607.964 -58.288 201.138  1.00160.27           C  
ANISOU 2693  CG  GLU A 359    18649  17672  24573   3354  -2452   -234       C  
ATOM   2694  CD  GLU A 359     608.667 -57.905 199.847  1.00159.31           C  
ANISOU 2694  CD  GLU A 359    18136  17772  24625   3355  -2238   -617       C  
ATOM   2695  OE1 GLU A 359     609.833 -58.320 199.664  1.00160.40           O  
ANISOU 2695  OE1 GLU A 359    17987  17897  25062   3609  -2369   -813       O  
ATOM   2696  OE2 GLU A 359     608.058 -57.191 199.021  1.00157.58           O  
ANISOU 2696  OE2 GLU A 359    17892  17741  24239   3107  -1939   -718       O  
ATOM   2697  N   GLN A 360     608.694 -57.654 204.974  1.00136.41           N  
ANISOU 2697  N   GLN A 360    16029  14719  21083   3560  -3293    477       N  
ATOM   2698  CA  GLN A 360     609.632 -58.366 205.836  1.00138.25           C  
ANISOU 2698  CA  GLN A 360    16254  14806  21468   3886  -3700    584       C  
ATOM   2699  C   GLN A 360     609.008 -58.586 207.215  1.00139.13           C  
ANISOU 2699  C   GLN A 360    16805  14793  21266   3869  -3904    995       C  
ATOM   2700  O   GLN A 360     609.224 -59.609 207.866  1.00140.69           O  
ANISOU 2700  O   GLN A 360    17190  14708  21558   4104  -4177   1206       O  
ATOM   2701  CB  GLN A 360     610.947 -57.585 205.942  1.00138.51           C  
ANISOU 2701  CB  GLN A 360    15884  15142  21601   4003  -3880    362       C  
ATOM   2702  CG  GLN A 360     611.536 -57.160 204.587  1.00137.36           C  
ANISOU 2702  CG  GLN A 360    15297  15182  21710   3961  -3619    -40       C  
ATOM   2703  CD  GLN A 360     612.842 -56.374 204.711  1.00138.10           C  
ANISOU 2703  CD  GLN A 360    14971  15574  21928   4050  -3780   -261       C  
ATOM   2704  OE1 GLN A 360     613.018 -55.582 205.636  1.00138.42           O  
ANISOU 2704  OE1 GLN A 360    15046  15801  21745   3987  -3962   -157       O  
ATOM   2705  NE2 GLN A 360     613.766 -56.600 203.777  1.00138.57           N  
ANISOU 2705  NE2 GLN A 360    14621  15681  22350   4193  -3706   -586       N  
ATOM   2706  N   LEU A 361     608.224 -57.605 207.642  1.00110.98           N  
ANISOU 2706  N   LEU A 361    13408  11439  17322   3589  -3759   1107       N  
ATOM   2707  CA  LEU A 361     607.476 -57.660 208.895  1.00111.64           C  
ANISOU 2707  CA  LEU A 361    13918  11457  17043   3512  -3870   1478       C  
ATOM   2708  C   LEU A 361     605.970 -57.563 208.618  1.00110.32           C  
ANISOU 2708  C   LEU A 361    14018  11225  16675   3202  -3507   1595       C  
ATOM   2709  O   LEU A 361     605.472 -56.494 208.266  1.00108.86           O  
ANISOU 2709  O   LEU A 361    13754  11291  16318   2954  -3261   1475       O  
ATOM   2710  CB  LEU A 361     607.918 -56.530 209.830  1.00111.93           C  
ANISOU 2710  CB  LEU A 361    13917  11827  16786   3469  -4051   1495       C  
ATOM   2711  CG  LEU A 361     609.085 -56.767 210.790  1.00113.83           C  
ANISOU 2711  CG  LEU A 361    14101  12095  17054   3767  -4519   1564       C  
ATOM   2712  CD1 LEU A 361     610.069 -57.797 210.276  1.00114.73           C  
ANISOU 2712  CD1 LEU A 361    13977  11993  17622   4097  -4714   1441       C  
ATOM   2713  CD2 LEU A 361     609.782 -55.454 211.038  1.00113.46           C  
ANISOU 2713  CD2 LEU A 361    13782  12436  16891   3699  -4607   1356       C  
ATOM   2714  N   PRO A 362     605.243 -58.683 208.773  1.00126.97           N  
ANISOU 2714  N   PRO A 362    16433  12985  18826   3216  -3478   1828       N  
ATOM   2715  CA  PRO A 362     603.823 -58.742 208.401  1.00125.84           C  
ANISOU 2715  CA  PRO A 362    16498  12748  18565   2931  -3133   1909       C  
ATOM   2716  C   PRO A 362     602.953 -57.720 209.139  1.00124.96           C  
ANISOU 2716  C   PRO A 362    16581  12878  18020   2667  -2998   2058       C  
ATOM   2717  O   PRO A 362     602.172 -56.989 208.523  1.00123.45           O  
ANISOU 2717  O   PRO A 362    16323  12842  17741   2421  -2698   1931       O  
ATOM   2718  CB  PRO A 362     603.424 -60.171 208.788  1.00127.24           C  
ANISOU 2718  CB  PRO A 362    16992  12491  18861   3031  -3221   2186       C  
ATOM   2719  CG  PRO A 362     604.690 -60.934 208.759  1.00128.74           C  
ANISOU 2719  CG  PRO A 362    17026  12516  19372   3389  -3539   2119       C  
ATOM   2720  CD  PRO A 362     605.735 -59.987 209.252  1.00128.89           C  
ANISOU 2720  CD  PRO A 362    16823  12878  19269   3505  -3770   2018       C  
ATOM   2721  N   TRP A 363     603.118 -57.666 210.454  1.00136.99           N  
ANISOU 2721  N   TRP A 363    18339  14438  19272   2733  -3232   2318       N  
ATOM   2722  CA  TRP A 363     602.238 -56.906 211.336  1.00136.55           C  
ANISOU 2722  CA  TRP A 363    18534  14563  18787   2505  -3117   2498       C  
ATOM   2723  C   TRP A 363     602.372 -55.384 211.185  1.00135.45           C  
ANISOU 2723  C   TRP A 363    18165  14816  18482   2362  -3018   2259       C  
ATOM   2724  O   TRP A 363     601.847 -54.616 211.992  1.00135.50           O  
ANISOU 2724  O   TRP A 363    18341  15009  18135   2209  -2967   2360       O  
ATOM   2725  CB  TRP A 363     602.527 -57.325 212.766  1.00138.40           C  
ANISOU 2725  CB  TRP A 363    19080  14736  18769   2648  -3425   2825       C  
ATOM   2726  CG  TRP A 363     603.968 -57.414 212.968  1.00139.84           C  
ANISOU 2726  CG  TRP A 363    19059  14970  19103   2951  -3809   2730       C  
ATOM   2727  CD1 TRP A 363     604.744 -58.528 212.878  1.00141.32           C  
ANISOU 2727  CD1 TRP A 363    19216  14882  19596   3242  -4066   2786       C  
ATOM   2728  CD2 TRP A 363     604.846 -56.330 213.229  1.00140.03           C  
ANISOU 2728  CD2 TRP A 363    18838  15340  19029   2999  -3981   2529       C  
ATOM   2729  NE1 TRP A 363     606.057 -58.206 213.099  1.00142.38           N  
ANISOU 2729  NE1 TRP A 363    19091  15186  19819   3479  -4400   2636       N  
ATOM   2730  CE2 TRP A 363     606.144 -56.854 213.318  1.00141.57           C  
ANISOU 2730  CE2 TRP A 363    18850  15470  19471   3323  -4352   2473       C  
ATOM   2731  CE3 TRP A 363     604.655 -54.957 213.418  1.00139.13           C  
ANISOU 2731  CE3 TRP A 363    18637  15572  18654   2799  -3863   2383       C  
ATOM   2732  CZ2 TRP A 363     607.251 -56.061 213.589  1.00142.28           C  
ANISOU 2732  CZ2 TRP A 363    18660  15844  19556   3439  -4608   2274       C  
ATOM   2733  CZ3 TRP A 363     605.749 -54.170 213.685  1.00139.88           C  
ANISOU 2733  CZ3 TRP A 363    18475  15928  18744   2905  -4111   2189       C  
ATOM   2734  CH2 TRP A 363     607.033 -54.720 213.764  1.00141.39           C  
ANISOU 2734  CH2 TRP A 363    18473  16064  19186   3215  -4478   2132       C  
ATOM   2735  N   MET A 364     603.089 -54.959 210.150  1.00111.36           N  
ANISOU 2735  N   MET A 364    14734  11881  15697   2410  -2984   1939       N  
ATOM   2736  CA  MET A 364     603.129 -53.558 209.748  1.00110.17           C  
ANISOU 2736  CA  MET A 364    14352  12050  15457   2244  -2831   1702       C  
ATOM   2737  C   MET A 364     601.774 -53.163 209.191  1.00108.68           C  
ANISOU 2737  C   MET A 364    14253  11877  15165   1966  -2456   1696       C  
ATOM   2738  O   MET A 364     601.459 -51.986 209.053  1.00107.75           O  
ANISOU 2738  O   MET A 364    14047  11992  14902   1792  -2299   1578       O  
ATOM   2739  CB  MET A 364     604.225 -53.326 208.714  1.00109.72           C  
ANISOU 2739  CB  MET A 364    13875  12086  15728   2358  -2860   1383       C  
ATOM   2740  CG  MET A 364     605.593 -53.580 209.271  1.00111.36           C  
ANISOU 2740  CG  MET A 364    13938  12319  16056   2629  -3237   1352       C  
ATOM   2741  SD  MET A 364     605.818 -52.591 210.747  1.00112.86           S  
ANISOU 2741  SD  MET A 364    14262  12767  15853   2592  -3471   1461       S  
ATOM   2742  CE  MET A 364     606.762 -51.247 210.051  1.00112.71           C  
ANISOU 2742  CE  MET A 364    13775  13063  15986   2524  -3426   1080       C  
ATOM   2743  N   SER A 365     600.983 -54.178 208.870  1.00102.13           N  
ANISOU 2743  N   SER A 365    13590  10780  14433   1933  -2326   1822       N  
ATOM   2744  CA  SER A 365     599.591 -54.005 208.530  1.00100.93           C  
ANISOU 2744  CA  SER A 365    13564  10609  14177   1681  -2007   1864       C  
ATOM   2745  C   SER A 365     598.959 -53.235 209.647  1.00101.00           C  
ANISOU 2745  C   SER A 365    13790  10783  13805   1536  -1971   2027       C  
ATOM   2746  O   SER A 365     598.081 -52.409 209.435  1.00 99.90           O  
ANISOU 2746  O   SER A 365    13641  10786  13530   1327  -1729   1967       O  
ATOM   2747  CB  SER A 365     598.906 -55.347 208.376  1.00101.47           C  
ANISOU 2747  CB  SER A 365    13831  10336  14387   1679  -1940   2027       C  
ATOM   2748  OG  SER A 365     599.799 -56.294 207.831  1.00102.17           O  
ANISOU 2748  OG  SER A 365    13793  10223  14806   1906  -2103   1939       O  
ATOM   2749  N   TYR A 366     599.421 -53.518 210.852  1.00163.24           N  
ANISOU 2749  N   TYR A 366    21871  18647  21508   1661  -2222   2230       N  
ATOM   2750  CA  TYR A 366     598.899 -52.832 211.998  1.00163.68           C  
ANISOU 2750  CA  TYR A 366    22150  18873  21169   1541  -2203   2376       C  
ATOM   2751  C   TYR A 366     599.447 -51.425 212.067  1.00163.63           C  
ANISOU 2751  C   TYR A 366    21934  19186  21051   1510  -2247   2150       C  
ATOM   2752  O   TYR A 366     598.713 -50.489 212.374  1.00163.32           O  
ANISOU 2752  O   TYR A 366    21956  19319  20778   1327  -2070   2124       O  
ATOM   2753  CB  TYR A 366     599.225 -53.580 213.275  1.00165.64           C  
ANISOU 2753  CB  TYR A 366    22702  19015  21220   1685  -2469   2673       C  
ATOM   2754  CG  TYR A 366     598.462 -53.017 214.433  1.00166.10           C  
ANISOU 2754  CG  TYR A 366    23042  19232  20838   1530  -2385   2843       C  
ATOM   2755  CD1 TYR A 366     597.144 -53.389 214.659  1.00165.34           C  
ANISOU 2755  CD1 TYR A 366    23195  19022  20605   1333  -2107   3038       C  
ATOM   2756  CD2 TYR A 366     599.036 -52.081 215.280  1.00167.34           C  
ANISOU 2756  CD2 TYR A 366    23199  19664  20720   1568  -2567   2781       C  
ATOM   2757  CE1 TYR A 366     596.421 -52.859 215.716  1.00165.76           C  
ANISOU 2757  CE1 TYR A 366    23495  19239  20246   1186  -1996   3175       C  
ATOM   2758  CE2 TYR A 366     598.324 -51.546 216.343  1.00167.89           C  
ANISOU 2758  CE2 TYR A 366    23531  19894  20367   1427  -2475   2908       C  
ATOM   2759  CZ  TYR A 366     597.015 -51.934 216.555  1.00167.05           C  
ANISOU 2759  CZ  TYR A 366    23672  19680  20120   1239  -2178   3105       C  
ATOM   2760  OH  TYR A 366     596.305 -51.400 217.610  1.00167.63           O  
ANISOU 2760  OH  TYR A 366    23994  19928  19769   1099  -2059   3214       O  
ATOM   2761  N   LEU A 367     600.733 -51.268 211.777  1.00118.94           N  
ANISOU 2761  N   LEU A 367    16016  13596  15580   1685  -2476   1976       N  
ATOM   2762  CA  LEU A 367     601.346 -49.949 211.854  1.00119.13           C  
ANISOU 2762  CA  LEU A 367    15826  13904  15534   1647  -2533   1755       C  
ATOM   2763  C   LEU A 367     600.676 -48.986 210.861  1.00117.42           C  
ANISOU 2763  C   LEU A 367    15439  13796  15381   1433  -2203   1559       C  
ATOM   2764  O   LEU A 367     600.605 -47.776 211.106  1.00117.47           O  
ANISOU 2764  O   LEU A 367    15389  14010  15235   1314  -2147   1442       O  
ATOM   2765  CB  LEU A 367     602.852 -50.025 211.599  1.00119.95           C  
ANISOU 2765  CB  LEU A 367    15637  14051  15886   1862  -2814   1586       C  
ATOM   2766  CG  LEU A 367     603.594 -48.740 211.983  1.00120.60           C  
ANISOU 2766  CG  LEU A 367    15533  14416  15874   1831  -2940   1389       C  
ATOM   2767  CD1 LEU A 367     603.770 -48.635 213.491  1.00122.26           C  
ANISOU 2767  CD1 LEU A 367    15988  14724  15740   1894  -3212   1543       C  
ATOM   2768  CD2 LEU A 367     604.938 -48.620 211.279  1.00120.98           C  
ANISOU 2768  CD2 LEU A 367    15182  14526  16257   1969  -3088   1141       C  
ATOM   2769  N   SER A 368     600.172 -49.536 209.755  1.00107.78           N  
ANISOU 2769  N   SER A 368    14147  12425  14381   1389  -1997   1525       N  
ATOM   2770  CA  SER A 368     599.386 -48.773 208.784  1.00106.20           C  
ANISOU 2770  CA  SER A 368    13826  12302  14223   1196  -1690   1382       C  
ATOM   2771  C   SER A 368     598.217 -48.094 209.476  1.00105.89           C  
ANISOU 2771  C   SER A 368    13998  12349  13887   1009  -1521   1483       C  
ATOM   2772  O   SER A 368     598.058 -46.878 209.433  1.00105.53           O  
ANISOU 2772  O   SER A 368    13863  12483  13749    894  -1423   1354       O  
ATOM   2773  CB  SER A 368     598.862 -49.684 207.668  1.00105.18           C  
ANISOU 2773  CB  SER A 368    13661  11979  14324   1182  -1523   1369       C  
ATOM   2774  OG  SER A 368     599.912 -50.430 207.083  1.00105.51           O  
ANISOU 2774  OG  SER A 368    13526  11922  14642   1372  -1671   1270       O  
ATOM   2775  N   ILE A 369     597.408 -48.919 210.119  1.00 88.47           N  
ANISOU 2775  N   ILE A 369    12070   9999  11547    981  -1481   1714       N  
ATOM   2776  CA  ILE A 369     596.253 -48.482 210.878  1.00 88.20           C  
ANISOU 2776  CA  ILE A 369    12254  10032  11228    813  -1308   1831       C  
ATOM   2777  C   ILE A 369     596.602 -47.458 211.959  1.00 89.36           C  
ANISOU 2777  C   ILE A 369    12464  10400  11089    807  -1424   1801       C  
ATOM   2778  O   ILE A 369     595.919 -46.447 212.100  1.00 88.74           O  
ANISOU 2778  O   ILE A 369    12388  10464  10866    661  -1249   1719       O  
ATOM   2779  CB  ILE A 369     595.570 -49.696 211.527  1.00 88.58           C  
ANISOU 2779  CB  ILE A 369    12600   9875  11181    805  -1284   2113       C  
ATOM   2780  CG1 ILE A 369     595.475 -50.844 210.513  1.00 87.87           C  
ANISOU 2780  CG1 ILE A 369    12444   9530  11413    847  -1238   2124       C  
ATOM   2781  CG2 ILE A 369     594.203 -49.323 212.070  1.00 87.97           C  
ANISOU 2781  CG2 ILE A 369    12706   9857  10862    600  -1024   2211       C  
ATOM   2782  CD1 ILE A 369     595.077 -52.166 211.113  1.00 88.60           C  
ANISOU 2782  CD1 ILE A 369    12816   9365  11482    869  -1267   2405       C  
ATOM   2783  N   VAL A 370     597.654 -47.719 212.726  1.00 83.35           N  
ANISOU 2783  N   VAL A 370    11751   9665  10253    972  -1730   1853       N  
ATOM   2784  CA  VAL A 370     598.095 -46.759 213.738  1.00 84.71           C  
ANISOU 2784  CA  VAL A 370    11968  10059  10159    974  -1879   1788       C  
ATOM   2785  C   VAL A 370     598.414 -45.417 213.115  1.00 84.33           C  
ANISOU 2785  C   VAL A 370    11640  10178  10224    895  -1809   1501       C  
ATOM   2786  O   VAL A 370     597.843 -44.386 213.498  1.00 84.45           O  
ANISOU 2786  O   VAL A 370    11701  10332  10053    760  -1676   1421       O  
ATOM   2787  CB  VAL A 370     599.350 -47.221 214.478  1.00 86.63           C  
ANISOU 2787  CB  VAL A 370    12238  10318  10361   1188  -2268   1845       C  
ATOM   2788  CG1 VAL A 370     599.687 -46.244 215.569  1.00 88.50           C  
ANISOU 2788  CG1 VAL A 370    12544  10792  10289   1172  -2420   1768       C  
ATOM   2789  CG2 VAL A 370     599.141 -48.574 215.061  1.00 87.25           C  
ANISOU 2789  CG2 VAL A 370    12602  10199  10351   1287  -2364   2151       C  
ATOM   2790  N   ALA A 371     599.350 -45.460 212.167  1.00 95.71           N  
ANISOU 2790  N   ALA A 371    12795  11595  11977    982  -1895   1349       N  
ATOM   2791  CA  ALA A 371     599.768 -44.296 211.404  1.00 95.31           C  
ANISOU 2791  CA  ALA A 371    12458  11670  12085    906  -1820   1094       C  
ATOM   2792  C   ALA A 371     598.572 -43.426 211.078  1.00 94.39           C  
ANISOU 2792  C   ALA A 371    12381  11595  11888    708  -1512   1050       C  
ATOM   2793  O   ALA A 371     598.423 -42.319 211.586  1.00 95.07           O  
ANISOU 2793  O   ALA A 371    12482  11816  11824    617  -1482    951       O  
ATOM   2794  CB  ALA A 371     600.473 -44.723 210.123  1.00 94.29           C  
ANISOU 2794  CB  ALA A 371    12052  11462  12311    982  -1813    983       C  
ATOM   2795  N   ILE A 372     597.689 -43.974 210.269  1.00 80.17           N  
ANISOU 2795  N   ILE A 372    10602   9668  10192    651  -1294   1122       N  
ATOM   2796  CA  ILE A 372     596.587 -43.214 209.724  1.00 78.86           C  
ANISOU 2796  CA  ILE A 372    10419   9530  10015    486  -1013   1067       C  
ATOM   2797  C   ILE A 372     595.559 -42.768 210.766  1.00 79.35           C  
ANISOU 2797  C   ILE A 372    10709   9654   9784    384   -903   1146       C  
ATOM   2798  O   ILE A 372     594.884 -41.762 210.576  1.00 79.14           O  
ANISOU 2798  O   ILE A 372    10642   9699   9729    268   -726   1047       O  
ATOM   2799  CB  ILE A 372     595.883 -44.021 208.675  1.00 76.76           C  
ANISOU 2799  CB  ILE A 372    10125   9120   9920    459   -842   1122       C  
ATOM   2800  CG1 ILE A 372     594.885 -43.154 207.932  1.00 75.18           C  
ANISOU 2800  CG1 ILE A 372     9852   8965   9747    312   -588   1039       C  
ATOM   2801  CG2 ILE A 372     595.196 -45.156 209.327  1.00 76.56           C  
ANISOU 2801  CG2 ILE A 372    10345   8963   9780    469   -831   1338       C  
ATOM   2802  CD1 ILE A 372     593.998 -43.948 207.054  1.00 73.54           C  
ANISOU 2802  CD1 ILE A 372     9648   8634   9660    269   -427   1095       C  
ATOM   2803  N   PHE A 373     595.437 -43.494 211.870  1.00 80.36           N  
ANISOU 2803  N   PHE A 373    11082   9759   9693    430  -1001   1322       N  
ATOM   2804  CA  PHE A 373     594.433 -43.122 212.859  1.00 80.74           C  
ANISOU 2804  CA  PHE A 373    11351   9882   9444    325   -863   1393       C  
ATOM   2805  C   PHE A 373     594.843 -41.855 213.585  1.00 82.62           C  
ANISOU 2805  C   PHE A 373    11574  10306   9511    306   -946   1226       C  
ATOM   2806  O   PHE A 373     594.043 -40.928 213.748  1.00 82.93           O  
ANISOU 2806  O   PHE A 373    11630  10425   9454    192   -757   1132       O  
ATOM   2807  CB  PHE A 373     594.201 -44.246 213.864  1.00 81.31           C  
ANISOU 2807  CB  PHE A 373    11714   9883   9296    368   -930   1649       C  
ATOM   2808  CG  PHE A 373     593.288 -45.309 213.360  1.00 79.54           C  
ANISOU 2808  CG  PHE A 373    11562   9472   9187    311   -747   1815       C  
ATOM   2809  CD1 PHE A 373     592.959 -45.369 212.013  1.00 77.62           C  
ANISOU 2809  CD1 PHE A 373    11108   9139   9245    269   -605   1717       C  
ATOM   2810  CD2 PHE A 373     592.742 -46.238 214.223  1.00 79.94           C  
ANISOU 2810  CD2 PHE A 373    11895   9439   9041    289   -713   2065       C  
ATOM   2811  CE1 PHE A 373     592.124 -46.351 211.529  1.00 76.14           C  
ANISOU 2811  CE1 PHE A 373    10972   8778   9179    209   -451   1839       C  
ATOM   2812  CE2 PHE A 373     591.900 -47.219 213.746  1.00 78.54           C  
ANISOU 2812  CE2 PHE A 373    11770   9069   9003    216   -539   2206       C  
ATOM   2813  CZ  PHE A 373     591.590 -47.272 212.395  1.00 76.63           C  
ANISOU 2813  CZ  PHE A 373    11299   8739   9080    176   -416   2078       C  
ATOM   2814  N   GLY A 374     596.098 -41.838 214.026  1.00105.32           N  
ANISOU 2814  N   GLY A 374    14407  13243  12364    423  -1239   1176       N  
ATOM   2815  CA  GLY A 374     596.671 -40.672 214.660  1.00107.08           C  
ANISOU 2815  CA  GLY A 374    14585  13635  12466    408  -1362    984       C  
ATOM   2816  C   GLY A 374     596.854 -39.587 213.626  1.00106.77           C  
ANISOU 2816  C   GLY A 374    14268  13606  12693    331  -1254    761       C  
ATOM   2817  O   GLY A 374     596.868 -38.421 213.967  1.00108.00           O  
ANISOU 2817  O   GLY A 374    14391  13862  12783    259  -1236    588       O  
ATOM   2818  N   PHE A 375     596.981 -39.980 212.361  1.00 75.95           N  
ANISOU 2818  N   PHE A 375    10180   9593   9086    344  -1178    768       N  
ATOM   2819  CA  PHE A 375     597.174 -39.052 211.239  1.00 75.44           C  
ANISOU 2819  CA  PHE A 375     9861   9527   9275    271  -1062    594       C  
ATOM   2820  C   PHE A 375     595.924 -38.266 210.891  1.00 74.93           C  
ANISOU 2820  C   PHE A 375     9828   9450   9190    139   -782    564       C  
ATOM   2821  O   PHE A 375     596.005 -37.124 210.471  1.00 75.51           O  
ANISOU 2821  O   PHE A 375     9770   9552   9370     65   -712    412       O  
ATOM   2822  CB  PHE A 375     597.637 -39.812 210.001  1.00 73.76           C  
ANISOU 2822  CB  PHE A 375     9468   9217   9340    331  -1054    619       C  
ATOM   2823  CG  PHE A 375     597.616 -39.007 208.732  1.00 72.68           C  
ANISOU 2823  CG  PHE A 375     9115   9073   9426    243   -884    493       C  
ATOM   2824  CD1 PHE A 375     598.686 -38.200 208.392  1.00 72.98           C  
ANISOU 2824  CD1 PHE A 375     8936   9174   9620    228   -965    327       C  
ATOM   2825  CD2 PHE A 375     596.549 -39.098 207.855  1.00 70.97           C  
ANISOU 2825  CD2 PHE A 375     8911   8786   9267    175   -650    548       C  
ATOM   2826  CE1 PHE A 375     598.689 -37.471 207.210  1.00 71.65           C  
ANISOU 2826  CE1 PHE A 375     8590   8992   9640    139   -797    240       C  
ATOM   2827  CE2 PHE A 375     596.547 -38.375 206.671  1.00 69.76           C  
ANISOU 2827  CE2 PHE A 375     8583   8633   9291    105   -510    455       C  
ATOM   2828  CZ  PHE A 375     597.621 -37.558 206.349  1.00 70.12           C  
ANISOU 2828  CZ  PHE A 375     8437   8735   9472     85   -576    314       C  
ATOM   2829  N   VAL A 376     594.764 -38.889 211.041  1.00 75.43           N  
ANISOU 2829  N   VAL A 376    10058   9461   9142    110   -623    710       N  
ATOM   2830  CA  VAL A 376     593.510 -38.162 210.905  1.00 74.73           C  
ANISOU 2830  CA  VAL A 376    10001   9377   9016      1   -375    676       C  
ATOM   2831  C   VAL A 376     593.134 -37.540 212.239  1.00 76.53           C  
ANISOU 2831  C   VAL A 376    10405   9711   8963    -35   -366    629       C  
ATOM   2832  O   VAL A 376     592.458 -36.529 212.280  1.00 77.13           O  
ANISOU 2832  O   VAL A 376    10464   9817   9024   -108   -215    514       O  
ATOM   2833  CB  VAL A 376     592.369 -39.066 210.409  1.00 71.89           C  
ANISOU 2833  CB  VAL A 376     9701   8922   8691    -32   -188    826       C  
ATOM   2834  CG1 VAL A 376     592.814 -39.805 209.179  1.00 70.38           C  
ANISOU 2834  CG1 VAL A 376     9361   8635   8747     15   -221    856       C  
ATOM   2835  CG2 VAL A 376     591.937 -40.062 211.485  1.00 71.85           C  
ANISOU 2835  CG2 VAL A 376     9939   8907   8452    -20   -198   1004       C  
ATOM   2836  N   ALA A 377     593.573 -38.141 213.336  1.00 85.75           N  
ANISOU 2836  N   ALA A 377    11747  10936   9899     26   -534    713       N  
ATOM   2837  CA  ALA A 377     593.376 -37.531 214.635  1.00 87.42           C  
ANISOU 2837  CA  ALA A 377    12132  11278   9805      0   -552    644       C  
ATOM   2838  C   ALA A 377     594.162 -36.231 214.658  1.00 89.29           C  
ANISOU 2838  C   ALA A 377    12223  11584  10120    -15   -664    394       C  
ATOM   2839  O   ALA A 377     593.621 -35.181 214.988  1.00 90.10           O  
ANISOU 2839  O   ALA A 377    12345  11735  10155    -86   -541    242       O  
ATOM   2840  CB  ALA A 377     593.820 -38.461 215.750  1.00 88.30           C  
ANISOU 2840  CB  ALA A 377    12468  11445   9638     80   -747    800       C  
ATOM   2841  N   PHE A 378     595.437 -36.301 214.279  1.00104.39           N  
ANISOU 2841  N   PHE A 378    13974  13488  12200     49   -891    340       N  
ATOM   2842  CA  PHE A 378     596.296 -35.123 214.288  1.00105.73           C  
ANISOU 2842  CA  PHE A 378    13984  13711  12476     18  -1010    102       C  
ATOM   2843  C   PHE A 378     595.781 -34.094 213.319  1.00105.35           C  
ANISOU 2843  C   PHE A 378    13784  13583  12662    -82   -789    -11       C  
ATOM   2844  O   PHE A 378     596.000 -32.898 213.486  1.00106.17           O  
ANISOU 2844  O   PHE A 378    13822  13706  12814   -146   -794   -210       O  
ATOM   2845  CB  PHE A 378     597.742 -35.473 213.947  1.00105.63           C  
ANISOU 2845  CB  PHE A 378    13785  13704  12644     97  -1269     69       C  
ATOM   2846  CG  PHE A 378     598.641 -35.511 215.142  1.00107.07           C  
ANISOU 2846  CG  PHE A 378    14043  14017  12621    168  -1574      1       C  
ATOM   2847  CD1 PHE A 378     598.803 -36.676 215.866  1.00107.33           C  
ANISOU 2847  CD1 PHE A 378    14255  14083  12441    289  -1745    187       C  
ATOM   2848  CD2 PHE A 378     599.296 -34.376 215.559  1.00108.10           C  
ANISOU 2848  CD2 PHE A 378    14075  14231  12767    114  -1697   -247       C  
ATOM   2849  CE1 PHE A 378     599.616 -36.708 216.970  1.00108.81           C  
ANISOU 2849  CE1 PHE A 378    14524  14404  12415    367  -2052    135       C  
ATOM   2850  CE2 PHE A 378     600.114 -34.403 216.660  1.00109.48           C  
ANISOU 2850  CE2 PHE A 378    14313  14544  12741    180  -2002   -329       C  
ATOM   2851  CZ  PHE A 378     600.274 -35.569 217.370  1.00109.93           C  
ANISOU 2851  CZ  PHE A 378    14552  14653  12564    315  -2188   -134       C  
ATOM   2852  N   PHE A 379     595.076 -34.556 212.304  1.00 75.16           N  
ANISOU 2852  N   PHE A 379     9912   9660   8985    -94   -602    116       N  
ATOM   2853  CA  PHE A 379     594.527 -33.640 211.313  1.00 74.74           C  
ANISOU 2853  CA  PHE A 379     9729   9528   9142   -172   -405     43       C  
ATOM   2854  C   PHE A 379     593.442 -32.712 211.853  1.00 75.07           C  
ANISOU 2854  C   PHE A 379     9874   9579   9071   -232   -234    -49       C  
ATOM   2855  O   PHE A 379     593.418 -31.518 211.570  1.00 75.25           O  
ANISOU 2855  O   PHE A 379     9808   9556   9227   -288   -175   -197       O  
ATOM   2856  CB  PHE A 379     593.949 -34.419 210.150  1.00 72.87           C  
ANISOU 2856  CB  PHE A 379     9432   9203   9051   -162   -265    196       C  
ATOM   2857  CG  PHE A 379     593.121 -33.590 209.242  1.00 71.64           C  
ANISOU 2857  CG  PHE A 379     9193   8979   9048   -227    -62    159       C  
ATOM   2858  CD1 PHE A 379     593.715 -32.846 208.243  1.00 70.31           C  
ANISOU 2858  CD1 PHE A 379     8848   8761   9107   -263    -57     87       C  
ATOM   2859  CD2 PHE A 379     591.745 -33.550 209.380  1.00 69.55           C  
ANISOU 2859  CD2 PHE A 379     9021   8699   8704   -251    124    203       C  
ATOM   2860  CE1 PHE A 379     592.949 -32.087 207.382  1.00 66.91           C  
ANISOU 2860  CE1 PHE A 379     8359   8257   8806   -309    112     81       C  
ATOM   2861  CE2 PHE A 379     590.971 -32.785 208.526  1.00 66.56           C  
ANISOU 2861  CE2 PHE A 379     8556   8255   8478   -288    283    173       C  
ATOM   2862  CZ  PHE A 379     591.568 -32.054 207.530  1.00 65.22           C  
ANISOU 2862  CZ  PHE A 379     8235   8026   8517   -311    267    122       C  
ATOM   2863  N   GLU A 380     592.515 -33.282 212.599  1.00109.94           N  
ANISOU 2863  N   GLU A 380    14473  14041  13257   -222   -140     44       N  
ATOM   2864  CA  GLU A 380     591.339 -32.542 212.968  1.00109.53           C  
ANISOU 2864  CA  GLU A 380    14492  13998  13127   -270     67    -36       C  
ATOM   2865  C   GLU A 380     591.641 -31.511 214.037  1.00111.36           C  
ANISOU 2865  C   GLU A 380    14796  14308  13207   -289     -3   -252       C  
ATOM   2866  O   GLU A 380     590.869 -30.580 214.232  1.00111.24           O  
ANISOU 2866  O   GLU A 380    14792  14278  13197   -323    152   -388       O  
ATOM   2867  CB  GLU A 380     590.258 -33.495 213.439  1.00107.67           C  
ANISOU 2867  CB  GLU A 380    14413  13797  12698   -271    216    122       C  
ATOM   2868  CG  GLU A 380     588.900 -33.055 213.008  1.00105.28           C  
ANISOU 2868  CG  GLU A 380    14063  13450  12490   -313    476     99       C  
ATOM   2869  CD  GLU A 380     588.672 -33.188 211.511  1.00102.88           C  
ANISOU 2869  CD  GLU A 380    13578  13029  12483   -313    533    172       C  
ATOM   2870  OE1 GLU A 380     589.075 -32.272 210.769  1.00103.46           O  
ANISOU 2870  OE1 GLU A 380    13514  13039  12759   -315    500     73       O  
ATOM   2871  OE2 GLU A 380     588.079 -34.199 211.076  1.00100.11           O  
ANISOU 2871  OE2 GLU A 380    13231  12648  12158   -318    612    327       O  
ATOM   2872  N   VAL A 381     592.757 -31.674 214.738  1.00 89.74           N  
ANISOU 2872  N   VAL A 381    12102  11655  10341   -259   -245   -300       N  
ATOM   2873  CA  VAL A 381     593.131 -30.678 215.730  1.00 91.30           C  
ANISOU 2873  CA  VAL A 381    12358  11934  10398   -283   -341   -537       C  
ATOM   2874  C   VAL A 381     593.859 -29.518 215.047  1.00 91.53           C  
ANISOU 2874  C   VAL A 381    12180  11862  10734   -334   -401   -725       C  
ATOM   2875  O   VAL A 381     593.704 -28.362 215.443  1.00 92.16           O  
ANISOU 2875  O   VAL A 381    12265  11923  10828   -381   -360   -945       O  
ATOM   2876  CB  VAL A 381     594.006 -31.270 216.858  1.00 92.59           C  
ANISOU 2876  CB  VAL A 381    12661  12249  10270   -229   -604   -529       C  
ATOM   2877  CG1 VAL A 381     593.143 -32.033 217.851  1.00 92.47           C  
ANISOU 2877  CG1 VAL A 381    12911  12344   9880   -207   -507   -393       C  
ATOM   2878  CG2 VAL A 381     595.072 -32.151 216.292  1.00 92.27           C  
ANISOU 2878  CG2 VAL A 381    12504  12182  10371   -167   -814   -393       C  
ATOM   2879  N   GLY A 382     594.632 -29.825 214.009  1.00 63.33           N  
ANISOU 2879  N   GLY A 382     8429   8218   7417   -330   -479   -640       N  
ATOM   2880  CA  GLY A 382     595.367 -28.802 213.286  1.00 62.66           C  
ANISOU 2880  CA  GLY A 382     8145   8033   7631   -398   -514   -784       C  
ATOM   2881  C   GLY A 382     594.749 -28.338 211.979  1.00 60.68           C  
ANISOU 2881  C   GLY A 382     7779   7627   7649   -439   -301   -716       C  
ATOM   2882  O   GLY A 382     593.750 -27.630 211.979  1.00 60.03           O  
ANISOU 2882  O   GLY A 382     7749   7476   7582   -458   -128   -767       O  
ATOM   2883  N   PRO A 383     595.332 -28.754 210.843  1.00 81.82           N  
ANISOU 2883  N   PRO A 383    10299  10254  10534   -442   -315   -601       N  
ATOM   2884  CA  PRO A 383     594.958 -28.260 209.507  1.00 79.00           C  
ANISOU 2884  CA  PRO A 383     9828   9764  10425   -486   -146   -535       C  
ATOM   2885  C   PRO A 383     593.470 -28.388 209.184  1.00 77.89           C  
ANISOU 2885  C   PRO A 383     9777   9579  10239   -453     58   -425       C  
ATOM   2886  O   PRO A 383     593.005 -27.891 208.160  1.00 75.11           O  
ANISOU 2886  O   PRO A 383     9355   9120  10064   -476    187   -373       O  
ATOM   2887  CB  PRO A 383     595.783 -29.143 208.560  1.00 77.42           C  
ANISOU 2887  CB  PRO A 383     9488   9583  10345   -466   -204   -410       C  
ATOM   2888  CG  PRO A 383     596.104 -30.349 209.358  1.00 79.65           C  
ANISOU 2888  CG  PRO A 383     9852   9984  10428   -380   -358   -353       C  
ATOM   2889  CD  PRO A 383     596.296 -29.864 210.759  1.00 82.11           C  
ANISOU 2889  CD  PRO A 383    10274  10371  10555   -385   -487   -510       C  
ATOM   2890  N   GLY A 384     592.728 -29.054 210.056  1.00 86.48           N  
ANISOU 2890  N   GLY A 384    11016  10753  11089   -404     85   -386       N  
ATOM   2891  CA  GLY A 384     591.301 -29.198 209.865  1.00 85.22           C  
ANISOU 2891  CA  GLY A 384    10918  10567  10893   -382    281   -306       C  
ATOM   2892  C   GLY A 384     590.620 -27.852 209.930  1.00 84.45           C  
ANISOU 2892  C   GLY A 384    10816  10380  10892   -405    399   -450       C  
ATOM   2893  O   GLY A 384     590.249 -27.301 208.900  1.00 82.05           O  
ANISOU 2893  O   GLY A 384    10418   9960  10796   -412    488   -411       O  
ATOM   2894  N   PRO A 385     590.472 -27.309 211.148  1.00 81.97           N  
ANISOU 2894  N   PRO A 385    10609  10116  10419   -409    392   -622       N  
ATOM   2895  CA  PRO A 385     589.760 -26.057 211.419  1.00 81.73           C  
ANISOU 2895  CA  PRO A 385    10592   9999  10465   -414    510   -797       C  
ATOM   2896  C   PRO A 385     590.583 -24.765 211.226  1.00 81.63           C  
ANISOU 2896  C   PRO A 385    10500   9849  10665   -470    428   -966       C  
ATOM   2897  O   PRO A 385     590.022 -23.739 210.820  1.00 80.58           O  
ANISOU 2897  O   PRO A 385    10330   9562  10726   -468    533  -1035       O  
ATOM   2898  CB  PRO A 385     589.359 -26.217 212.892  1.00 83.51           C  
ANISOU 2898  CB  PRO A 385    10981  10368  10381   -397    533   -919       C  
ATOM   2899  CG  PRO A 385     590.437 -27.062 213.473  1.00 85.18           C  
ANISOU 2899  CG  PRO A 385    11256  10710  10398   -405    332   -872       C  
ATOM   2900  CD  PRO A 385     590.803 -28.028 212.392  1.00 84.24           C  
ANISOU 2900  CD  PRO A 385    11039  10562  10405   -393    287   -642       C  
ATOM   2901  N   ILE A 386     591.886 -24.811 211.503  1.00 85.72           N  
ANISOU 2901  N   ILE A 386    10987  10411  11170   -520    241  -1030       N  
ATOM   2902  CA  ILE A 386     592.678 -23.585 211.616  1.00 85.96           C  
ANISOU 2902  CA  ILE A 386    10957  10327  11378   -597    159  -1235       C  
ATOM   2903  C   ILE A 386     592.714 -22.723 210.340  1.00 83.63           C  
ANISOU 2903  C   ILE A 386    10537   9815  11424   -646    243  -1176       C  
ATOM   2904  O   ILE A 386     592.498 -21.527 210.437  1.00 83.64           O  
ANISOU 2904  O   ILE A 386    10543   9657  11580   -677    293  -1329       O  
ATOM   2905  CB  ILE A 386     594.122 -23.897 212.072  1.00 87.33           C  
ANISOU 2905  CB  ILE A 386    11080  10604  11497   -645    -75  -1310       C  
ATOM   2906  CG1 ILE A 386     594.126 -24.450 213.499  1.00 89.68           C  
ANISOU 2906  CG1 ILE A 386    11534  11100  11441   -597   -187  -1405       C  
ATOM   2907  CG2 ILE A 386     594.965 -22.665 212.002  1.00 87.22           C  
ANISOU 2907  CG2 ILE A 386    10963  10453  11722   -751   -148  -1510       C  
ATOM   2908  CD1 ILE A 386     593.425 -23.584 214.500  1.00 90.71           C  
ANISOU 2908  CD1 ILE A 386    11794  11228  11444   -596   -113  -1637       C  
ATOM   2909  N   PRO A 387     592.974 -23.304 209.150  1.00 78.56           N  
ANISOU 2909  N   PRO A 387     9795   9159  10893   -652    262   -959       N  
ATOM   2910  CA  PRO A 387     592.960 -22.445 207.957  1.00 76.26           C  
ANISOU 2910  CA  PRO A 387     9418   8671  10886   -701    352   -885       C  
ATOM   2911  C   PRO A 387     591.632 -21.760 207.610  1.00 75.28           C  
ANISOU 2911  C   PRO A 387     9347   8405  10852   -637    508   -855       C  
ATOM   2912  O   PRO A 387     591.667 -20.778 206.846  1.00 74.15           O  
ANISOU 2912  O   PRO A 387     9163   8063  10949   -678    558   -828       O  
ATOM   2913  CB  PRO A 387     593.342 -23.396 206.826  1.00 74.10           C  
ANISOU 2913  CB  PRO A 387     9055   8463  10638   -700    356   -659       C  
ATOM   2914  CG  PRO A 387     593.280 -24.724 207.389  1.00 75.18           C  
ANISOU 2914  CG  PRO A 387     9239   8792  10535   -630    292   -608       C  
ATOM   2915  CD  PRO A 387     593.578 -24.601 208.836  1.00 78.33           C  
ANISOU 2915  CD  PRO A 387     9719   9274  10769   -632    179   -804       C  
ATOM   2916  N   TRP A 388     590.499 -22.227 208.133  1.00 70.53           N  
ANISOU 2916  N   TRP A 388     8825   7891  10081   -541    585   -854       N  
ATOM   2917  CA  TRP A 388     589.278 -21.441 207.970  1.00 70.18           C  
ANISOU 2917  CA  TRP A 388     8805   7711  10149   -470    718   -883       C  
ATOM   2918  C   TRP A 388     589.349 -20.286 208.952  1.00 72.03           C  
ANISOU 2918  C   TRP A 388     9094   7839  10437   -490    709  -1157       C  
ATOM   2919  O   TRP A 388     589.387 -19.136 208.525  1.00 71.66           O  
ANISOU 2919  O   TRP A 388     9022   7566  10641   -512    731  -1208       O  
ATOM   2920  CB  TRP A 388     588.010 -22.273 208.164  1.00 70.19           C  
ANISOU 2920  CB  TRP A 388     8840   7841   9989   -372    825   -810       C  
ATOM   2921  CG  TRP A 388     587.704 -23.167 206.974  1.00 67.95           C  
ANISOU 2921  CG  TRP A 388     8491   7601   9728   -345    849   -558       C  
ATOM   2922  CD1 TRP A 388     587.665 -24.531 206.970  1.00 67.63           C  
ANISOU 2922  CD1 TRP A 388     8458   7729   9511   -338    836   -436       C  
ATOM   2923  CD2 TRP A 388     587.429 -22.759 205.624  1.00 65.66           C  
ANISOU 2923  CD2 TRP A 388     8131   7179   9639   -324    878   -406       C  
ATOM   2924  NE1 TRP A 388     587.382 -24.998 205.709  1.00 65.00           N  
ANISOU 2924  NE1 TRP A 388     8052   7382   9263   -318    857   -247       N  
ATOM   2925  CE2 TRP A 388     587.228 -23.929 204.863  1.00 63.84           C  
ANISOU 2925  CE2 TRP A 388     7861   7068   9329   -306    880   -221       C  
ATOM   2926  CE3 TRP A 388     587.330 -21.516 204.980  1.00 65.10           C  
ANISOU 2926  CE3 TRP A 388     8038   6892   9803   -317    898   -403       C  
ATOM   2927  CZ2 TRP A 388     586.934 -23.897 203.493  1.00 61.41           C  
ANISOU 2927  CZ2 TRP A 388     7494   6700   9138   -281    896    -48       C  
ATOM   2928  CZ3 TRP A 388     587.038 -21.482 203.614  1.00 63.00           C  
ANISOU 2928  CZ3 TRP A 388     7726   6560   9652   -288    913   -198       C  
ATOM   2929  CH2 TRP A 388     586.842 -22.663 202.891  1.00 61.20           C  
ANISOU 2929  CH2 TRP A 388     7459   6484   9310   -270    910    -31       C  
ATOM   2930  N   PHE A 389     589.424 -20.591 210.249  1.00115.53           N  
ANISOU 2930  N   PHE A 389    14685  13504  15706   -487    671  -1332       N  
ATOM   2931  CA  PHE A 389     589.564 -19.577 211.316  1.00117.42           C  
ANISOU 2931  CA  PHE A 389    14988  13679  15945   -510    647  -1639       C  
ATOM   2932  C   PHE A 389     590.457 -18.375 210.987  1.00117.37           C  
ANISOU 2932  C   PHE A 389    14926  13442  16229   -609    571  -1757       C  
ATOM   2933  O   PHE A 389     590.149 -17.246 211.362  1.00118.09           O  
ANISOU 2933  O   PHE A 389    15047  13357  16464   -602    613  -1967       O  
ATOM   2934  CB  PHE A 389     590.111 -20.224 212.595  1.00119.61           C  
ANISOU 2934  CB  PHE A 389    15358  14193  15897   -534    536  -1773       C  
ATOM   2935  CG  PHE A 389     589.048 -20.738 213.530  1.00120.24           C  
ANISOU 2935  CG  PHE A 389    15554  14443  15688   -452    656  -1826       C  
ATOM   2936  CD1 PHE A 389     588.101 -19.879 214.072  1.00120.50           C  
ANISOU 2936  CD1 PHE A 389    15632  14404  15749   -396    799  -2037       C  
ATOM   2937  CD2 PHE A 389     589.008 -22.073 213.885  1.00120.56           C  
ANISOU 2937  CD2 PHE A 389    15659  14710  15439   -434    637  -1670       C  
ATOM   2938  CE1 PHE A 389     587.123 -20.345 214.936  1.00120.91           C  
ANISOU 2938  CE1 PHE A 389    15777  14630  15533   -333    942  -2095       C  
ATOM   2939  CE2 PHE A 389     588.039 -22.543 214.746  1.00120.86           C  
ANISOU 2939  CE2 PHE A 389    15810  14902  15210   -382    773  -1703       C  
ATOM   2940  CZ  PHE A 389     587.096 -21.677 215.275  1.00121.00           C  
ANISOU 2940  CZ  PHE A 389    15858  14871  15245   -337    935  -1919       C  
ATOM   2941  N   ILE A 390     591.558 -18.624 210.290  1.00 72.78           N  
ANISOU 2941  N   ILE A 390     9188   7786  10678   -704    469  -1628       N  
ATOM   2942  CA  ILE A 390     592.559 -17.595 210.059  1.00 72.90           C  
ANISOU 2942  CA  ILE A 390     9136   7606  10956   -834    396  -1741       C  
ATOM   2943  C   ILE A 390     592.092 -16.574 209.013  1.00 71.49           C  
ANISOU 2943  C   ILE A 390     8934   7127  11101   -836    513  -1638       C  
ATOM   2944  O   ILE A 390     592.385 -15.382 209.130  1.00 72.21           O  
ANISOU 2944  O   ILE A 390     9026   6981  11427   -910    506  -1802       O  
ATOM   2945  CB  ILE A 390     593.921 -18.217 209.638  1.00 72.42           C  
ANISOU 2945  CB  ILE A 390     8959   7650  10907   -942    267  -1643       C  
ATOM   2946  CG1 ILE A 390     594.521 -19.007 210.809  1.00 74.38           C  
ANISOU 2946  CG1 ILE A 390     9235   8156  10869   -936    103  -1784       C  
ATOM   2947  CG2 ILE A 390     594.903 -17.132 209.180  1.00 72.29           C  
ANISOU 2947  CG2 ILE A 390     8843   7410  11213  -1101    234  -1721       C  
ATOM   2948  CD1 ILE A 390     595.960 -19.453 210.602  1.00 74.34           C  
ANISOU 2948  CD1 ILE A 390     9090   8244  10912  -1033    -58  -1764       C  
ATOM   2949  N   VAL A 391     591.354 -17.025 208.005  1.00 70.96           N  
ANISOU 2949  N   VAL A 391     8855   7059  11048   -754    611  -1371       N  
ATOM   2950  CA  VAL A 391     590.851 -16.108 206.988  1.00 69.79           C  
ANISOU 2950  CA  VAL A 391     8704   6639  11175   -733    701  -1240       C  
ATOM   2951  C   VAL A 391     589.850 -15.113 207.584  1.00 70.94           C  
ANISOU 2951  C   VAL A 391     8920   6601  11432   -633    769  -1434       C  
ATOM   2952  O   VAL A 391     589.884 -13.932 207.248  1.00 71.16           O  
ANISOU 2952  O   VAL A 391     8962   6332  11746   -662    790  -1470       O  
ATOM   2953  CB  VAL A 391     590.204 -16.866 205.824  1.00 67.69           C  
ANISOU 2953  CB  VAL A 391     8412   6446  10861   -649    767   -929       C  
ATOM   2954  CG1 VAL A 391     589.792 -15.922 204.722  1.00 66.70           C  
ANISOU 2954  CG1 VAL A 391     8297   6050  10998   -627    831   -765       C  
ATOM   2955  CG2 VAL A 391     591.184 -17.859 205.284  1.00 66.48           C  
ANISOU 2955  CG2 VAL A 391     8187   6473  10600   -736    711   -775       C  
ATOM   2956  N   ALA A 392     588.977 -15.570 208.480  1.00109.31           N  
ANISOU 2956  N   ALA A 392    13826  11629  16080   -519    812  -1564       N  
ATOM   2957  CA  ALA A 392     587.977 -14.677 209.079  1.00110.35           C  
ANISOU 2957  CA  ALA A 392    14006  11610  16311   -408    897  -1777       C  
ATOM   2958  C   ALA A 392     588.646 -13.615 209.928  1.00112.02           C  
ANISOU 2958  C   ALA A 392    14259  11658  16645   -497    840  -2095       C  
ATOM   2959  O   ALA A 392     588.054 -12.571 210.231  1.00112.74           O  
ANISOU 2959  O   ALA A 392    14385  11525  16927   -428    899  -2286       O  
ATOM   2960  CB  ALA A 392     586.975 -15.461 209.916  1.00110.87           C  
ANISOU 2960  CB  ALA A 392    14102  11926  16098   -292    981  -1861       C  
ATOM   2961  N   GLU A 393     589.887 -13.894 210.307  1.00 94.02           N  
ANISOU 2961  N   GLU A 393    11965   9489  14268   -644    715  -2167       N  
ATOM   2962  CA  GLU A 393     590.668 -12.968 211.102  1.00 95.66           C  
ANISOU 2962  CA  GLU A 393    12194   9566  14585   -755    629  -2484       C  
ATOM   2963  C   GLU A 393     591.737 -12.249 210.271  1.00 95.12           C  
ANISOU 2963  C   GLU A 393    12054   9247  14840   -923    570  -2403       C  
ATOM   2964  O   GLU A 393     592.350 -11.294 210.741  1.00 96.35           O  
ANISOU 2964  O   GLU A 393    12212   9216  15182  -1033    510  -2655       O  
ATOM   2965  CB  GLU A 393     591.296 -13.712 212.274  1.00 97.07           C  
ANISOU 2965  CB  GLU A 393    12402  10056  14424   -802    509  -2671       C  
ATOM   2966  CG  GLU A 393     590.264 -14.295 213.214  1.00 97.69           C  
ANISOU 2966  CG  GLU A 393    12575  10365  14176   -662    591  -2774       C  
ATOM   2967  CD  GLU A 393     590.807 -15.432 214.049  1.00 98.76           C  
ANISOU 2967  CD  GLU A 393    12754  10851  13918   -688    477  -2790       C  
ATOM   2968  OE1 GLU A 393     591.660 -16.197 213.546  1.00 98.26           O  
ANISOU 2968  OE1 GLU A 393    12622  10893  13819   -756    369  -2589       O  
ATOM   2969  OE2 GLU A 393     590.378 -15.566 215.214  1.00100.16           O  
ANISOU 2969  OE2 GLU A 393    13039  11200  13818   -635    499  -3004       O  
ATOM   2970  N   LEU A 394     591.953 -12.697 209.038  1.00101.75           N  
ANISOU 2970  N   LEU A 394    12830  10082  15748   -952    598  -2060       N  
ATOM   2971  CA  LEU A 394     592.850 -11.985 208.132  1.00101.20           C  
ANISOU 2971  CA  LEU A 394    12699   9767  15987  -1114    590  -1943       C  
ATOM   2972  C   LEU A 394     592.097 -10.949 207.307  1.00100.73           C  
ANISOU 2972  C   LEU A 394    12696   9349  16229  -1054    697  -1811       C  
ATOM   2973  O   LEU A 394     592.713 -10.183 206.572  1.00100.53           O  
ANISOU 2973  O   LEU A 394    12652   9062  16484  -1189    715  -1706       O  
ATOM   2974  CB  LEU A 394     593.588 -12.948 207.182  1.00 99.56           C  
ANISOU 2974  CB  LEU A 394    12395   9739  15696  -1191    576  -1651       C  
ATOM   2975  CG  LEU A 394     594.909 -13.616 207.594  1.00 99.86           C  
ANISOU 2975  CG  LEU A 394    12323  10003  15617  -1327    447  -1742       C  
ATOM   2976  CD1 LEU A 394     595.969 -13.503 206.499  1.00 98.79           C  
ANISOU 2976  CD1 LEU A 394    12066   9785  15684  -1499    470  -1553       C  
ATOM   2977  CD2 LEU A 394     595.441 -13.064 208.909  1.00101.90           C  
ANISOU 2977  CD2 LEU A 394    12586  10251  15879  -1401    322  -2128       C  
ATOM   2978  N   PHE A 395     590.775 -10.921 207.397  1.00 85.47           N  
ANISOU 2978  N   PHE A 395    10828   7397  14251   -854    770  -1801       N  
ATOM   2979  CA  PHE A 395     590.027  -9.957 206.596  1.00 85.19           C  
ANISOU 2979  CA  PHE A 395    10842   7019  14509   -766    845  -1661       C  
ATOM   2980  C   PHE A 395     588.833  -9.361 207.370  1.00 86.44           C  
ANISOU 2980  C   PHE A 395    11056   7061  14725   -577    896  -1905       C  
ATOM   2981  O   PHE A 395     588.057 -10.100 207.989  1.00 86.46           O  
ANISOU 2981  O   PHE A 395    11052   7327  14472   -445    929  -1993       O  
ATOM   2982  CB  PHE A 395     589.550 -10.614 205.291  1.00 83.20           C  
ANISOU 2982  CB  PHE A 395    10572   6848  14191   -686    890  -1258       C  
ATOM   2983  CG  PHE A 395     590.665 -11.004 204.325  1.00 81.96           C  
ANISOU 2983  CG  PHE A 395    10364   6747  14029   -863    875  -1005       C  
ATOM   2984  CD1 PHE A 395     591.356 -12.204 204.468  1.00 81.06           C  
ANISOU 2984  CD1 PHE A 395    10173   6975  13650   -935    831   -983       C  
ATOM   2985  CD2 PHE A 395     590.978 -10.191 203.236  1.00 81.79           C  
ANISOU 2985  CD2 PHE A 395    10376   6434  14265   -947    915   -774       C  
ATOM   2986  CE1 PHE A 395     592.357 -12.566 203.561  1.00 79.90           C  
ANISOU 2986  CE1 PHE A 395     9959   6887  13511  -1084    835   -772       C  
ATOM   2987  CE2 PHE A 395     591.981 -10.547 202.331  1.00 80.72           C  
ANISOU 2987  CE2 PHE A 395    10188   6369  14113  -1115    935   -547       C  
ATOM   2988  CZ  PHE A 395     592.662 -11.734 202.496  1.00 79.71           C  
ANISOU 2988  CZ  PHE A 395     9961   6593  13732  -1179    899   -561       C  
ATOM   2989  N   SER A 396     588.688  -8.034 207.349  1.00113.15           N  
ANISOU 2989  N   SER A 396    14491  10046  18454   -568    912  -2020       N  
ATOM   2990  CA  SER A 396     587.587  -7.395 208.064  1.00114.35           C  
ANISOU 2990  CA  SER A 396    14682  10064  18702   -379    968  -2280       C  
ATOM   2991  C   SER A 396     586.266  -7.598 207.330  1.00113.51           C  
ANISOU 2991  C   SER A 396    14559   9952  18619   -147   1032  -2046       C  
ATOM   2992  O   SER A 396     586.236  -8.160 206.240  1.00112.15           O  
ANISOU 2992  O   SER A 396    14362   9857  18391   -143   1022  -1683       O  
ATOM   2993  CB  SER A 396     587.844  -5.909 208.245  1.00115.87           C  
ANISOU 2993  CB  SER A 396    14935   9799  19292   -430    957  -2485       C  
ATOM   2994  OG  SER A 396     587.598  -5.206 207.042  1.00115.59           O  
ANISOU 2994  OG  SER A 396    14936   9412  19572   -388    974  -2178       O  
ATOM   2995  N   GLN A 397     585.181  -7.100 207.919  1.00160.55           N  
ANISOU 2995  N   GLN A 397    20519  15813  24670     48   1095  -2272       N  
ATOM   2996  CA  GLN A 397     583.814  -7.337 207.433  1.00159.98           C  
ANISOU 2996  CA  GLN A 397    20393  15780  24614    290   1152  -2124       C  
ATOM   2997  C   GLN A 397     583.614  -7.026 205.941  1.00159.13           C  
ANISOU 2997  C   GLN A 397    20295  15442  24723    347   1105  -1715       C  
ATOM   2998  O   GLN A 397     582.595  -7.392 205.352  1.00158.58           O  
ANISOU 2998  O   GLN A 397    20166  15452  24634    529   1115  -1534       O  
ATOM   2999  CB  GLN A 397     582.816  -6.510 208.256  1.00161.48           C  
ANISOU 2999  CB  GLN A 397    20573  15799  24984    483   1228  -2470       C  
ATOM   3000  CG  GLN A 397     582.708  -6.901 209.737  1.00162.26           C  
ANISOU 3000  CG  GLN A 397    20665  16180  24806    473   1306  -2872       C  
ATOM   3001  CD  GLN A 397     583.945  -6.541 210.555  1.00163.29           C  
ANISOU 3001  CD  GLN A 397    20877  16275  24891    259   1244  -3137       C  
ATOM   3002  OE1 GLN A 397     584.737  -5.680 210.165  1.00163.68           O  
ANISOU 3002  OE1 GLN A 397    20976  15995  25220    139   1169  -3114       O  
ATOM   3003  NE2 GLN A 397     584.120  -7.213 211.690  1.00163.84           N  
ANISOU 3003  NE2 GLN A 397    20961  16690  24603    203   1272  -3384       N  
ATOM   3004  N   GLY A 398     584.599  -6.358 205.342  1.00 89.85           N  
ANISOU 3004  N   GLY A 398    11598   6394  16148    182   1052  -1572       N  
ATOM   3005  CA  GLY A 398     584.537  -5.895 203.961  1.00 89.47           C  
ANISOU 3005  CA  GLY A 398    11601   6086  16308    212   1012  -1182       C  
ATOM   3006  C   GLY A 398     585.175  -6.790 202.905  1.00 87.74           C  
ANISOU 3006  C   GLY A 398    11374   6089  15872     78    987   -806       C  
ATOM   3007  O   GLY A 398     584.484  -7.234 201.984  1.00 86.76           O  
ANISOU 3007  O   GLY A 398    11233   6059  15672    210    965   -521       O  
ATOM   3008  N   PRO A 399     586.495  -7.053 203.008  1.00 80.73           N  
ANISOU 3008  N   PRO A 399    10489   5292  14892   -179    984   -817       N  
ATOM   3009  CA  PRO A 399     587.081  -8.011 202.066  1.00 78.05           C  
ANISOU 3009  CA  PRO A 399    10124   5206  14328   -291    977   -500       C  
ATOM   3010  C   PRO A 399     586.893  -9.468 202.518  1.00 74.63           C  
ANISOU 3010  C   PRO A 399     9597   5244  13516   -258    977   -565       C  
ATOM   3011  O   PRO A 399     587.254 -10.377 201.768  1.00 72.35           O  
ANISOU 3011  O   PRO A 399     9276   5183  13029   -320    971   -329       O  
ATOM   3012  CB  PRO A 399     588.554  -7.625 202.063  1.00 79.10           C  
ANISOU 3012  CB  PRO A 399    10269   5222  14563   -571    982   -523       C  
ATOM   3013  CG  PRO A 399     588.795  -7.151 203.437  1.00 80.69           C  
ANISOU 3013  CG  PRO A 399    10458   5355  14846   -616    967   -950       C  
ATOM   3014  CD  PRO A 399     587.518  -6.499 203.914  1.00 82.43           C  
ANISOU 3014  CD  PRO A 399    10717   5388  15215   -375    979  -1118       C  
ATOM   3015  N   ARG A 400     586.325  -9.688 203.705  1.00 76.86           N  
ANISOU 3015  N   ARG A 400     9844   5661  13699   -162    992   -875       N  
ATOM   3016  CA  ARG A 400     586.210 -11.045 204.229  1.00 76.08           C  
ANISOU 3016  CA  ARG A 400     9677   5981  13247   -153   1000   -932       C  
ATOM   3017  C   ARG A 400     585.430 -11.995 203.319  1.00 74.52           C  
ANISOU 3017  C   ARG A 400     9433   5990  12892    -35   1005   -653       C  
ATOM   3018  O   ARG A 400     585.860 -13.135 203.144  1.00 73.16           O  
ANISOU 3018  O   ARG A 400     9222   6105  12471   -111    993   -550       O  
ATOM   3019  CB  ARG A 400     585.595 -11.056 205.623  1.00 77.44           C  
ANISOU 3019  CB  ARG A 400     9841   6255  13329    -61   1041  -1291       C  
ATOM   3020  CG  ARG A 400     586.084 -12.253 206.425  1.00 77.04           C  
ANISOU 3020  CG  ARG A 400     9765   6582  12926   -150   1030  -1393       C  
ATOM   3021  CD  ARG A 400     585.372 -12.393 207.747  1.00 78.31           C  
ANISOU 3021  CD  ARG A 400     9933   6889  12933    -56   1093  -1705       C  
ATOM   3022  NE  ARG A 400     585.406 -11.173 208.544  1.00 79.90           N  
ANISOU 3022  NE  ARG A 400    10184   6843  13330    -50   1105  -2026       N  
ATOM   3023  CZ  ARG A 400     584.472 -10.857 209.437  1.00 81.10           C  
ANISOU 3023  CZ  ARG A 400    10341   7004  13469     87   1194  -2298       C  
ATOM   3024  NH1 ARG A 400     583.438 -11.682 209.629  1.00 80.87           N  
ANISOU 3024  NH1 ARG A 400    10260   7223  13244    213   1287  -2266       N  
ATOM   3025  NH2 ARG A 400     584.563  -9.722 210.129  1.00 82.54           N  
ANISOU 3025  NH2 ARG A 400    10572   6946  13843     90   1201  -2613       N  
ATOM   3026  N   PRO A 401     584.306 -11.536 202.721  1.00 85.72           N  
ANISOU 3026  N   PRO A 401    10847   7257  14465    154   1009   -538       N  
ATOM   3027  CA  PRO A 401     583.619 -12.437 201.783  1.00 84.39           C  
ANISOU 3027  CA  PRO A 401    10624   7291  14150    251    990   -279       C  
ATOM   3028  C   PRO A 401     584.495 -12.827 200.581  1.00 82.97           C  
ANISOU 3028  C   PRO A 401    10478   7158  13887    117    951     34       C  
ATOM   3029  O   PRO A 401     584.699 -14.015 200.348  1.00 81.67           O  
ANISOU 3029  O   PRO A 401    10266   7290  13476     67    948    119       O  
ATOM   3030  CB  PRO A 401     582.402 -11.617 201.334  1.00 85.21           C  
ANISOU 3030  CB  PRO A 401    10719   7165  14493    475    970   -221       C  
ATOM   3031  CG  PRO A 401     582.794 -10.194 201.580  1.00 86.60           C  
ANISOU 3031  CG  PRO A 401    10985   6944  14975    451    968   -325       C  
ATOM   3032  CD  PRO A 401     583.591 -10.251 202.842  1.00 87.20           C  
ANISOU 3032  CD  PRO A 401    11068   7095  14969    299   1016   -641       C  
ATOM   3033  N   ALA A 402     584.996 -11.840 199.838  1.00 74.90           N  
ANISOU 3033  N   ALA A 402     9541   5842  13073     57    934    198       N  
ATOM   3034  CA  ALA A 402     585.924 -12.079 198.732  1.00 73.82           C  
ANISOU 3034  CA  ALA A 402     9444   5739  12864    -94    930    479       C  
ATOM   3035  C   ALA A 402     587.030 -13.069 199.119  1.00 72.69           C  
ANISOU 3035  C   ALA A 402     9241   5874  12505   -279    954    394       C  
ATOM   3036  O   ALA A 402     587.361 -13.979 198.367  1.00 71.36           O  
ANISOU 3036  O   ALA A 402     9044   5925  12143   -328    954    572       O  
ATOM   3037  CB  ALA A 402     586.528 -10.776 198.281  1.00 74.90           C  
ANISOU 3037  CB  ALA A 402     9686   5497  13275   -191    943    588       C  
ATOM   3038  N   ALA A 403     587.574 -12.877 200.314  1.00 66.70           N  
ANISOU 3038  N   ALA A 403     8461   5100  11780   -365    961    106       N  
ATOM   3039  CA  ALA A 403     588.603 -13.735 200.865  1.00 65.10           C  
ANISOU 3039  CA  ALA A 403     8196   5144  11396   -515    953    -10       C  
ATOM   3040  C   ALA A 403     588.170 -15.192 200.971  1.00 62.27           C  
ANISOU 3040  C   ALA A 403     7778   5141  10743   -438    941     12       C  
ATOM   3041  O   ALA A 403     588.981 -16.104 200.770  1.00 60.68           O  
ANISOU 3041  O   ALA A 403     7528   5149  10380   -538    929     69       O  
ATOM   3042  CB  ALA A 403     589.008 -13.224 202.220  1.00 66.48           C  
ANISOU 3042  CB  ALA A 403     8370   5246  11643   -577    935   -346       C  
ATOM   3043  N   ILE A 404     586.899 -15.420 201.304  1.00 61.89           N  
ANISOU 3043  N   ILE A 404     7721   5151  10641   -263    951    -44       N  
ATOM   3044  CA  ILE A 404     586.415 -16.785 201.538  1.00 59.56           C  
ANISOU 3044  CA  ILE A 404     7371   5169  10089   -204    953    -46       C  
ATOM   3045  C   ILE A 404     586.194 -17.523 200.224  1.00 58.06           C  
ANISOU 3045  C   ILE A 404     7156   5098   9807   -174    939    230       C  
ATOM   3046  O   ILE A 404     586.514 -18.691 200.113  1.00 56.15           O  
ANISOU 3046  O   ILE A 404     6875   5091   9369   -217    930    275       O  
ATOM   3047  CB  ILE A 404     585.098 -16.795 202.363  1.00 59.97           C  
ANISOU 3047  CB  ILE A 404     7404   5258  10125    -45    993   -213       C  
ATOM   3048  CG1 ILE A 404     585.238 -15.954 203.648  1.00 61.93           C  
ANISOU 3048  CG1 ILE A 404     7691   5382  10459    -60   1017   -513       C  
ATOM   3049  CG2 ILE A 404     584.626 -18.223 202.638  1.00 57.86           C  
ANISOU 3049  CG2 ILE A 404     7084   5297   9604    -14   1013   -205       C  
ATOM   3050  CD1 ILE A 404     585.888 -16.616 204.820  1.00 61.35           C  
ANISOU 3050  CD1 ILE A 404     7628   5512  10168   -154   1009   -707       C  
ATOM   3051  N   ALA A 405     585.668 -16.835 199.222  1.00 79.82           N  
ANISOU 3051  N   ALA A 405     9943   7685  12700    -97    928    412       N  
ATOM   3052  CA  ALA A 405     585.486 -17.452 197.921  1.00 78.44           C  
ANISOU 3052  CA  ALA A 405     9760   7626  12417    -71    902    667       C  
ATOM   3053  C   ALA A 405     586.812 -17.955 197.356  1.00 76.96           C  
ANISOU 3053  C   ALA A 405     9576   7544  12123   -243    918    772       C  
ATOM   3054  O   ALA A 405     586.861 -19.047 196.791  1.00 75.57           O  
ANISOU 3054  O   ALA A 405     9361   7589  11762   -247    909    862       O  
ATOM   3055  CB  ALA A 405     584.846 -16.488 196.966  1.00 79.19           C  
ANISOU 3055  CB  ALA A 405     9913   7504  12672     34    868    856       C  
ATOM   3056  N   VAL A 406     587.884 -17.176 197.524  1.00 71.74           N  
ANISOU 3056  N   VAL A 406     8946   6721  11591   -386    945    739       N  
ATOM   3057  CA  VAL A 406     589.213 -17.597 197.064  1.00 70.64           C  
ANISOU 3057  CA  VAL A 406     8776   6683  11382   -559    976    807       C  
ATOM   3058  C   VAL A 406     589.763 -18.750 197.898  1.00 69.95           C  
ANISOU 3058  C   VAL A 406     8604   6842  11132   -603    953    635       C  
ATOM   3059  O   VAL A 406     590.343 -19.698 197.352  1.00 68.46           O  
ANISOU 3059  O   VAL A 406     8363   6845  10804   -653    961    712       O  
ATOM   3060  CB  VAL A 406     590.248 -16.469 197.107  1.00 71.75           C  
ANISOU 3060  CB  VAL A 406     8942   6586  11732   -723   1017    791       C  
ATOM   3061  CG1 VAL A 406     591.302 -16.731 196.068  1.00 71.10           C  
ANISOU 3061  CG1 VAL A 406     8834   6581  11598   -872   1081    968       C  
ATOM   3062  CG2 VAL A 406     589.620 -15.145 196.846  1.00 72.77           C  
ANISOU 3062  CG2 VAL A 406     9173   6396  12081   -663   1023    874       C  
ATOM   3063  N   ALA A 407     589.599 -18.652 199.216  1.00 60.36           N  
ANISOU 3063  N   ALA A 407     7383   5619   9933   -579    924    403       N  
ATOM   3064  CA  ALA A 407     589.956 -19.747 200.114  1.00 59.66           C  
ANISOU 3064  CA  ALA A 407     7243   5758   9668   -592    884    256       C  
ATOM   3065  C   ALA A 407     589.275 -21.029 199.662  1.00 58.03           C  
ANISOU 3065  C   ALA A 407     7014   5764   9272   -499    882    364       C  
ATOM   3066  O   ALA A 407     589.951 -21.991 199.284  1.00 56.84           O  
ANISOU 3066  O   ALA A 407     6814   5775   9007   -547    869    420       O  
ATOM   3067  CB  ALA A 407     589.572 -19.429 201.543  1.00 61.08           C  
ANISOU 3067  CB  ALA A 407     7452   5908   9847   -551    862     13       C  
ATOM   3068  N   GLY A 408     587.941 -21.026 199.685  1.00 55.97           N  
ANISOU 3068  N   GLY A 408     6775   5493   8999   -365    896    379       N  
ATOM   3069  CA  GLY A 408     587.159 -22.142 199.191  1.00 54.72           C  
ANISOU 3069  CA  GLY A 408     6586   5509   8698   -284    894    474       C  
ATOM   3070  C   GLY A 408     587.526 -22.583 197.779  1.00 52.75           C  
ANISOU 3070  C   GLY A 408     6320   5325   8398   -313    889    673       C  
ATOM   3071  O   GLY A 408     587.319 -23.739 197.416  1.00 51.52           O  
ANISOU 3071  O   GLY A 408     6129   5343   8104   -289    876    717       O  
ATOM   3072  N   PHE A 409     588.063 -21.681 196.965  1.00 64.18           N  
ANISOU 3072  N   PHE A 409     7800   6635   9952   -371    907    792       N  
ATOM   3073  CA  PHE A 409     588.429 -22.089 195.616  1.00 62.80           C  
ANISOU 3073  CA  PHE A 409     7623   6546   9692   -405    921    977       C  
ATOM   3074  C   PHE A 409     589.742 -22.858 195.607  1.00 61.62           C  
ANISOU 3074  C   PHE A 409     7414   6535   9466   -525    943    936       C  
ATOM   3075  O   PHE A 409     589.960 -23.717 194.748  1.00 60.42           O  
ANISOU 3075  O   PHE A 409     7233   6535   9188   -530    955   1019       O  
ATOM   3076  CB  PHE A 409     588.540 -20.907 194.670  1.00 63.63           C  
ANISOU 3076  CB  PHE A 409     7801   6465   9909   -433    950   1154       C  
ATOM   3077  CG  PHE A 409     589.109 -21.277 193.344  1.00 62.73           C  
ANISOU 3077  CG  PHE A 409     7700   6460   9677   -495    990   1334       C  
ATOM   3078  CD1 PHE A 409     588.387 -22.034 192.464  1.00 62.26           C  
ANISOU 3078  CD1 PHE A 409     7645   6555   9456   -403    954   1436       C  
ATOM   3079  CD2 PHE A 409     590.376 -20.912 192.992  1.00 62.70           C  
ANISOU 3079  CD2 PHE A 409     7689   6417   9716   -654   1071   1381       C  
ATOM   3080  CE1 PHE A 409     588.905 -22.395 191.237  1.00 61.85           C  
ANISOU 3080  CE1 PHE A 409     7613   6623   9263   -459    997   1581       C  
ATOM   3081  CE2 PHE A 409     590.902 -21.275 191.762  1.00 62.23           C  
ANISOU 3081  CE2 PHE A 409     7639   6481   9526   -715   1135   1536       C  
ATOM   3082  CZ  PHE A 409     590.162 -22.009 190.889  1.00 61.84           C  
ANISOU 3082  CZ  PHE A 409     7615   6590   9291   -613   1098   1634       C  
ATOM   3083  N   SER A 410     590.621 -22.539 196.554  1.00 70.52           N  
ANISOU 3083  N   SER A 410     8511   7609  10675   -613    940    792       N  
ATOM   3084  CA  SER A 410     591.862 -23.297 196.724  1.00 70.03           C  
ANISOU 3084  CA  SER A 410     8362   7682  10563   -705    934    721       C  
ATOM   3085  C   SER A 410     591.539 -24.685 197.229  1.00 69.12           C  
ANISOU 3085  C   SER A 410     8219   7750  10292   -624    879    650       C  
ATOM   3086  O   SER A 410     592.067 -25.685 196.757  1.00 67.90           O  
ANISOU 3086  O   SER A 410     8007   7739  10051   -633    878    673       O  
ATOM   3087  CB  SER A 410     592.807 -22.620 197.715  1.00 71.79           C  
ANISOU 3087  CB  SER A 410     8549   7813  10916   -809    909    560       C  
ATOM   3088  OG  SER A 410     593.028 -21.276 197.381  1.00 72.59           O  
ANISOU 3088  OG  SER A 410     8685   7701  11195   -894    963    610       O  
ATOM   3089  N   ASN A 411     590.673 -24.713 198.228  1.00 59.22           N  
ANISOU 3089  N   ASN A 411     7010   6478   9013   -548    843    557       N  
ATOM   3090  CA  ASN A 411     590.245 -25.940 198.846  1.00 58.75           C  
ANISOU 3090  CA  ASN A 411     6948   6562   8814   -482    804    503       C  
ATOM   3091  C   ASN A 411     589.617 -26.921 197.848  1.00 56.64           C  
ANISOU 3091  C   ASN A 411     6666   6401   8454   -424    819    619       C  
ATOM   3092  O   ASN A 411     589.984 -28.081 197.824  1.00 55.61           O  
ANISOU 3092  O   ASN A 411     6503   6390   8237   -421    793    609       O  
ATOM   3093  CB  ASN A 411     589.268 -25.638 199.963  1.00 60.48           C  
ANISOU 3093  CB  ASN A 411     7224   6737   9020   -420    804    401       C  
ATOM   3094  CG  ASN A 411     589.230 -26.734 200.987  1.00 61.02           C  
ANISOU 3094  CG  ASN A 411     7308   6933   8942   -398    767    321       C  
ATOM   3095  OD1 ASN A 411     588.871 -27.878 200.679  1.00 59.28           O  
ANISOU 3095  OD1 ASN A 411     7077   6816   8631   -363    766    386       O  
ATOM   3096  ND2 ASN A 411     589.609 -26.405 202.216  1.00 63.74           N  
ANISOU 3096  ND2 ASN A 411     7691   7268   9260   -422    731    180       N  
ATOM   3097  N   TRP A 412     588.687 -26.469 197.017  1.00 66.08           N  
ANISOU 3097  N   TRP A 412     7884   7549   9675   -372    846    721       N  
ATOM   3098  CA  TRP A 412     588.139 -27.348 195.997  1.00 64.69           C  
ANISOU 3098  CA  TRP A 412     7688   7482   9408   -324    841    812       C  
ATOM   3099  C   TRP A 412     589.182 -27.650 194.916  1.00 63.85           C  
ANISOU 3099  C   TRP A 412     7553   7447   9259   -388    864    884       C  
ATOM   3100  O   TRP A 412     589.051 -28.608 194.178  1.00 63.04           O  
ANISOU 3100  O   TRP A 412     7429   7464   9061   -364    857    913       O  
ATOM   3101  CB  TRP A 412     586.879 -26.751 195.346  1.00 65.54           C  
ANISOU 3101  CB  TRP A 412     7817   7535   9549   -240    835    900       C  
ATOM   3102  CG  TRP A 412     585.597 -26.731 196.204  1.00 66.73           C  
ANISOU 3102  CG  TRP A 412     7956   7661   9736   -157    830    820       C  
ATOM   3103  CD1 TRP A 412     584.986 -25.628 196.751  1.00 68.80           C  
ANISOU 3103  CD1 TRP A 412     8236   7787  10117   -106    843    779       C  
ATOM   3104  CD2 TRP A 412     584.785 -27.853 196.573  1.00 66.25           C  
ANISOU 3104  CD2 TRP A 412     7853   7712   9606   -122    827    764       C  
ATOM   3105  NE1 TRP A 412     583.862 -25.999 197.441  1.00 69.97           N  
ANISOU 3105  NE1 TRP A 412     8344   7976  10264    -39    860    693       N  
ATOM   3106  CE2 TRP A 412     583.713 -27.359 197.350  1.00 68.30           C  
ANISOU 3106  CE2 TRP A 412     8097   7916   9939    -58    855    692       C  
ATOM   3107  CE3 TRP A 412     584.859 -29.231 196.329  1.00 64.53           C  
ANISOU 3107  CE3 TRP A 412     7607   7622   9288   -143    812    762       C  
ATOM   3108  CZ2 TRP A 412     582.723 -28.199 197.884  1.00 68.40           C  
ANISOU 3108  CZ2 TRP A 412     8059   8011   9919    -32    884    628       C  
ATOM   3109  CZ3 TRP A 412     583.874 -30.066 196.862  1.00 64.46           C  
ANISOU 3109  CZ3 TRP A 412     7563   7669   9259   -119    828    706       C  
ATOM   3110  CH2 TRP A 412     582.825 -29.546 197.633  1.00 66.18           C  
ANISOU 3110  CH2 TRP A 412     7759   7844   9542    -72    871    645       C  
ATOM   3111  N   THR A 413     590.232 -26.855 194.803  1.00 66.62           N  
ANISOU 3111  N   THR A 413     7898   7731   9686   -477    901    898       N  
ATOM   3112  CA  THR A 413     591.189 -27.120 193.730  1.00 66.28           C  
ANISOU 3112  CA  THR A 413     7814   7771   9598   -544    956    963       C  
ATOM   3113  C   THR A 413     592.256 -28.157 194.117  1.00 65.94           C  
ANISOU 3113  C   THR A 413     7678   7841   9534   -576    942    849       C  
ATOM   3114  O   THR A 413     592.500 -29.133 193.387  1.00 65.46           O  
ANISOU 3114  O   THR A 413     7577   7908   9387   -559    958    852       O  
ATOM   3115  CB  THR A 413     591.880 -25.838 193.288  1.00 67.33           C  
ANISOU 3115  CB  THR A 413     7965   7782   9833   -646   1028   1047       C  
ATOM   3116  OG1 THR A 413     590.882 -24.846 193.018  1.00 68.01           O  
ANISOU 3116  OG1 THR A 413     8148   7731   9964   -595   1020   1158       O  
ATOM   3117  CG2 THR A 413     592.717 -26.089 192.039  1.00 67.35           C  
ANISOU 3117  CG2 THR A 413     7934   7892   9763   -719   1119   1134       C  
ATOM   3118  N   SER A 414     592.892 -27.932 195.264  1.00 93.66           N  
ANISOU 3118  N   SER A 414    11155  11302  13128   -614    901    736       N  
ATOM   3119  CA  SER A 414     593.876 -28.867 195.792  1.00 94.07           C  
ANISOU 3119  CA  SER A 414    11118  11449  13176   -620    851    626       C  
ATOM   3120  C   SER A 414     593.199 -30.179 196.145  1.00 93.39           C  
ANISOU 3120  C   SER A 414    11061  11438  12984   -518    788    600       C  
ATOM   3121  O   SER A 414     593.841 -31.224 196.199  1.00 93.52           O  
ANISOU 3121  O   SER A 414    11017  11537  12981   -493    750    547       O  
ATOM   3122  CB  SER A 414     594.595 -28.277 197.012  1.00 95.91           C  
ANISOU 3122  CB  SER A 414    11321  11617  13505   -672    788    507       C  
ATOM   3123  OG  SER A 414     593.697 -27.586 197.867  1.00 96.52           O  
ANISOU 3123  OG  SER A 414    11495  11591  13586   -645    760    482       O  
ATOM   3124  N   ASN A 415     591.891 -30.122 196.372  1.00 70.04           N  
ANISOU 3124  N   ASN A 415     8189   8443   9980   -462    782    637       N  
ATOM   3125  CA  ASN A 415     591.101 -31.340 196.518  1.00 69.28           C  
ANISOU 3125  CA  ASN A 415     8118   8406   9797   -389    749    632       C  
ATOM   3126  C   ASN A 415     591.054 -32.134 195.202  1.00 68.38           C  
ANISOU 3126  C   ASN A 415     7971   8380   9633   -370    778    677       C  
ATOM   3127  O   ASN A 415     591.356 -33.327 195.194  1.00 68.54           O  
ANISOU 3127  O   ASN A 415     7961   8456   9624   -340    747    631       O  
ATOM   3128  CB  ASN A 415     589.684 -31.012 196.981  1.00 69.04           C  
ANISOU 3128  CB  ASN A 415     8156   8325   9752   -346    757    650       C  
ATOM   3129  CG  ASN A 415     589.003 -32.180 197.669  1.00 68.74           C  
ANISOU 3129  CG  ASN A 415     8145   8325   9648   -304    731    621       C  
ATOM   3130  OD1 ASN A 415     588.876 -33.256 197.101  1.00 68.03           O  
ANISOU 3130  OD1 ASN A 415     8035   8291   9524   -285    722    636       O  
ATOM   3131  ND2 ASN A 415     588.578 -31.976 198.908  1.00 69.73           N  
ANISOU 3131  ND2 ASN A 415     8325   8417   9754   -298    729    574       N  
ATOM   3132  N   PHE A 416     590.671 -31.480 194.101  1.00 62.13           N  
ANISOU 3132  N   PHE A 416     7192   7591   8822   -381    829    763       N  
ATOM   3133  CA  PHE A 416     590.658 -32.143 192.796  1.00 62.14           C  
ANISOU 3133  CA  PHE A 416     7173   7697   8740   -367    856    792       C  
ATOM   3134  C   PHE A 416     591.984 -32.844 192.485  1.00 62.65           C  
ANISOU 3134  C   PHE A 416     7157   7840   8808   -394    884    722       C  
ATOM   3135  O   PHE A 416     591.983 -33.931 191.919  1.00 63.07           O  
ANISOU 3135  O   PHE A 416     7185   7973   8807   -357    879    673       O  
ATOM   3136  CB  PHE A 416     590.353 -31.150 191.675  1.00 62.65           C  
ANISOU 3136  CB  PHE A 416     7279   7761   8763   -386    904    913       C  
ATOM   3137  CG  PHE A 416     590.373 -31.769 190.297  1.00 63.45           C  
ANISOU 3137  CG  PHE A 416     7377   7996   8736   -375    932    937       C  
ATOM   3138  CD1 PHE A 416     591.540 -31.816 189.558  1.00 64.03           C  
ANISOU 3138  CD1 PHE A 416     7409   8149   8770   -435   1021    932       C  
ATOM   3139  CD2 PHE A 416     589.223 -32.312 189.752  1.00 64.12           C  
ANISOU 3139  CD2 PHE A 416     7489   8138   8737   -310    873    943       C  
ATOM   3140  CE1 PHE A 416     591.566 -32.389 188.313  1.00 65.19           C  
ANISOU 3140  CE1 PHE A 416     7560   8435   8774   -425   1059    931       C  
ATOM   3141  CE2 PHE A 416     589.238 -32.871 188.504  1.00 65.52           C  
ANISOU 3141  CE2 PHE A 416     7670   8448   8777   -300    886    940       C  
ATOM   3142  CZ  PHE A 416     590.420 -32.911 187.779  1.00 66.01           C  
ANISOU 3142  CZ  PHE A 416     7710   8595   8776   -356    985    933       C  
ATOM   3143  N   ILE A 417     593.103 -32.207 192.844  1.00 74.34           N  
ANISOU 3143  N   ILE A 417     8583   9292  10371   -458    914    700       N  
ATOM   3144  CA  ILE A 417     594.449 -32.706 192.526  1.00 75.24           C  
ANISOU 3144  CA  ILE A 417     8582   9485  10521   -486    952    623       C  
ATOM   3145  C   ILE A 417     594.791 -33.992 193.290  1.00 75.89           C  
ANISOU 3145  C   ILE A 417     8616   9584  10634   -412    859    512       C  
ATOM   3146  O   ILE A 417     595.284 -34.965 192.702  1.00 76.62           O  
ANISOU 3146  O   ILE A 417     8642   9754  10718   -373    876    445       O  
ATOM   3147  CB  ILE A 417     595.517 -31.634 192.832  1.00 75.95           C  
ANISOU 3147  CB  ILE A 417     8602   9531  10725   -587    996    615       C  
ATOM   3148  CG1 ILE A 417     595.112 -30.287 192.227  1.00 75.75           C  
ANISOU 3148  CG1 ILE A 417     8653   9435  10693   -662   1080    749       C  
ATOM   3149  CG2 ILE A 417     596.871 -32.061 192.307  1.00 76.91           C  
ANISOU 3149  CG2 ILE A 417     8572   9754  10897   -624   1064    534       C  
ATOM   3150  CD1 ILE A 417     595.931 -29.127 192.750  1.00 76.67           C  
ANISOU 3150  CD1 ILE A 417     8723   9453  10955   -774   1109    737       C  
ATOM   3151  N   VAL A 418     594.534 -33.986 194.600  1.00 45.12           N  
ANISOU 3151  N   VAL A 418     4763   5610   6769   -387    763    493       N  
ATOM   3152  CA  VAL A 418     594.690 -35.193 195.410  1.00 45.15           C  
ANISOU 3152  CA  VAL A 418     4766   5608   6781   -309    660    430       C  
ATOM   3153  C   VAL A 418     593.752 -36.283 194.906  1.00 44.80           C  
ANISOU 3153  C   VAL A 418     4777   5572   6672   -251    662    445       C  
ATOM   3154  O   VAL A 418     594.194 -37.361 194.584  1.00 46.03           O  
ANISOU 3154  O   VAL A 418     4886   5753   6851   -199    642    384       O  
ATOM   3155  CB  VAL A 418     594.427 -34.944 196.917  1.00 46.09           C  
ANISOU 3155  CB  VAL A 418     4960   5657   6894   -299    567    429       C  
ATOM   3156  CG1 VAL A 418     594.052 -36.252 197.636  1.00 47.54           C  
ANISOU 3156  CG1 VAL A 418     5210   5816   7036   -220    481    428       C  
ATOM   3157  CG2 VAL A 418     595.634 -34.264 197.575  1.00 47.66           C  
ANISOU 3157  CG2 VAL A 418     5077   5858   7174   -340    513    361       C  
ATOM   3158  N   GLY A 419     592.466 -36.001 194.799  1.00 75.87           N  
ANISOU 3158  N   GLY A 419     8799   9482  10547   -260    685    510       N  
ATOM   3159  CA  GLY A 419     591.535 -36.999 194.319  1.00 75.94           C  
ANISOU 3159  CA  GLY A 419     8841   9497  10514   -223    680    507       C  
ATOM   3160  C   GLY A 419     591.815 -37.519 192.919  1.00 76.65           C  
ANISOU 3160  C   GLY A 419     8877   9673  10573   -212    726    461       C  
ATOM   3161  O   GLY A 419     591.664 -38.719 192.673  1.00 77.92           O  
ANISOU 3161  O   GLY A 419     9033   9831  10742   -171    699    396       O  
ATOM   3162  N   MET A 420     592.218 -36.645 191.998  1.00 57.42           N  
ANISOU 3162  N   MET A 420     6411   7311   8097   -254    801    491       N  
ATOM   3163  CA  MET A 420     592.383 -37.080 190.618  1.00 58.49           C  
ANISOU 3163  CA  MET A 420     6515   7555   8154   -248    860    448       C  
ATOM   3164  C   MET A 420     593.716 -37.796 190.450  1.00 59.79           C  
ANISOU 3164  C   MET A 420     6575   7764   8378   -225    889    332       C  
ATOM   3165  O   MET A 420     593.821 -38.769 189.687  1.00 61.34           O  
ANISOU 3165  O   MET A 420     6743   8018   8545   -184    906    232       O  
ATOM   3166  CB  MET A 420     592.280 -35.902 189.648  1.00 58.19           C  
ANISOU 3166  CB  MET A 420     6505   7584   8021   -303    940    547       C  
ATOM   3167  CG  MET A 420     592.417 -36.281 188.188  1.00 59.81           C  
ANISOU 3167  CG  MET A 420     6703   7930   8092   -302   1008    511       C  
ATOM   3168  SD  MET A 420     591.273 -37.606 187.818  1.00 61.21           S  
ANISOU 3168  SD  MET A 420     6912   8130   8216   -234    917    414       S  
ATOM   3169  CE  MET A 420     591.365 -37.739 186.024  1.00 63.67           C  
ANISOU 3169  CE  MET A 420     7241   8635   8316   -240    990    373       C  
ATOM   3170  N   CYS A 421     594.729 -37.344 191.183  1.00 81.78           N  
ANISOU 3170  N   CYS A 421     9292  10520  11261   -246    887    325       N  
ATOM   3171  CA  CYS A 421     596.086 -37.800 190.919  1.00 83.03           C  
ANISOU 3171  CA  CYS A 421     9311  10740  11496   -227    927    212       C  
ATOM   3172  C   CYS A 421     596.693 -38.702 191.988  1.00 84.26           C  
ANISOU 3172  C   CYS A 421     9412  10821  11782   -143    806    132       C  
ATOM   3173  O   CYS A 421     597.827 -39.143 191.839  1.00 85.45           O  
ANISOU 3173  O   CYS A 421     9425  11015  12026   -103    818     23       O  
ATOM   3174  CB  CYS A 421     596.999 -36.602 190.731  1.00 82.68           C  
ANISOU 3174  CB  CYS A 421     9186  10744  11486   -324   1023    245       C  
ATOM   3175  SG  CYS A 421     596.259 -35.296 189.779  1.00 81.83           S  
ANISOU 3175  SG  CYS A 421     9185  10668  11237   -424   1136    402       S  
ATOM   3176  N   PHE A 422     595.975 -38.984 193.064  1.00 56.85           N  
ANISOU 3176  N   PHE A 422     6043   7242   8316   -110    692    186       N  
ATOM   3177  CA  PHE A 422     596.578 -39.811 194.095  1.00 58.59           C  
ANISOU 3177  CA  PHE A 422     6237   7388   8635    -25    564    140       C  
ATOM   3178  C   PHE A 422     596.778 -41.248 193.589  1.00 60.10           C  
ANISOU 3178  C   PHE A 422     6393   7557   8885     74    544     41       C  
ATOM   3179  O   PHE A 422     597.732 -41.926 193.980  1.00 61.56           O  
ANISOU 3179  O   PHE A 422     6491   7712   9188    164    464    -35       O  
ATOM   3180  CB  PHE A 422     595.744 -39.830 195.366  1.00 58.88           C  
ANISOU 3180  CB  PHE A 422     6416   7323   8633    -20    465    234       C  
ATOM   3181  CG  PHE A 422     596.219 -40.843 196.377  1.00 61.16           C  
ANISOU 3181  CG  PHE A 422     6722   7529   8987     78    322    220       C  
ATOM   3182  CD1 PHE A 422     597.238 -40.533 197.272  1.00 62.25           C  
ANISOU 3182  CD1 PHE A 422     6798   7676   9179    107    216    199       C  
ATOM   3183  CD2 PHE A 422     595.664 -42.125 196.421  1.00 62.38           C  
ANISOU 3183  CD2 PHE A 422     6957   7587   9158    142    282    231       C  
ATOM   3184  CE1 PHE A 422     597.678 -41.477 198.208  1.00 64.23           C  
ANISOU 3184  CE1 PHE A 422     7079   7851   9474    216     57    206       C  
ATOM   3185  CE2 PHE A 422     596.091 -43.058 197.352  1.00 64.18           C  
ANISOU 3185  CE2 PHE A 422     7226   7714   9445    238    144    250       C  
ATOM   3186  CZ  PHE A 422     597.095 -42.735 198.247  1.00 64.99           C  
ANISOU 3186  CZ  PHE A 422     7278   7836   9577    284     25    246       C  
ATOM   3187  N   GLN A 423     595.878 -41.718 192.728  1.00 91.45           N  
ANISOU 3187  N   GLN A 423    10427  11533  12786     65    602     28       N  
ATOM   3188  CA  GLN A 423     596.028 -43.041 192.148  1.00 93.09           C  
ANISOU 3188  CA  GLN A 423    10604  11709  13057    149    593    -95       C  
ATOM   3189  C   GLN A 423     597.187 -43.064 191.146  1.00 93.42           C  
ANISOU 3189  C   GLN A 423    10483  11875  13135    176    691   -238       C  
ATOM   3190  O   GLN A 423     597.910 -44.046 191.078  1.00 94.70           O  
ANISOU 3190  O   GLN A 423    10561  11999  13422    280    657   -366       O  
ATOM   3191  CB  GLN A 423     594.720 -43.491 191.487  1.00 93.34           C  
ANISOU 3191  CB  GLN A 423    10738  11724  13005    117    620    -95       C  
ATOM   3192  CG  GLN A 423     593.570 -43.736 192.465  1.00 93.19           C  
ANISOU 3192  CG  GLN A 423    10852  11572  12983     93    543     19       C  
ATOM   3193  CD  GLN A 423     592.743 -44.978 192.128  1.00 95.10           C  
ANISOU 3193  CD  GLN A 423    11149  11715  13267    109    518    -46       C  
ATOM   3194  OE1 GLN A 423     592.502 -45.289 190.959  1.00 96.26           O  
ANISOU 3194  OE1 GLN A 423    11266  11933  13377    102    568   -159       O  
ATOM   3195  NE2 GLN A 423     592.315 -45.698 193.161  1.00 95.65           N  
ANISOU 3195  NE2 GLN A 423    11309  11622  13413    121    443     25       N  
ATOM   3196  N   TYR A 424     597.355 -41.990 190.376  1.00115.61           N  
ANISOU 3196  N   TYR A 424    13253  14830  15845     83    821   -215       N  
ATOM   3197  CA  TYR A 424     598.498 -41.823 189.469  1.00115.99           C  
ANISOU 3197  CA  TYR A 424    13141  15020  15912     76    954   -332       C  
ATOM   3198  C   TYR A 424     599.806 -42.093 190.171  1.00116.82           C  
ANISOU 3198  C   TYR A 424    13079  15098  16209    150    894   -419       C  
ATOM   3199  O   TYR A 424     600.733 -42.693 189.633  1.00118.01           O  
ANISOU 3199  O   TYR A 424    13075  15310  16453    219    952   -581       O  
ATOM   3200  CB  TYR A 424     598.542 -40.394 188.932  1.00114.72           C  
ANISOU 3200  CB  TYR A 424    12982  14975  15633    -59   1086   -228       C  
ATOM   3201  CG  TYR A 424     598.802 -40.256 187.457  1.00115.28           C  
ANISOU 3201  CG  TYR A 424    13013  15216  15572   -106   1270   -292       C  
ATOM   3202  CD1 TYR A 424     599.415 -41.274 186.726  1.00117.00           C  
ANISOU 3202  CD1 TYR A 424    13126  15509  15817    -27   1337   -488       C  
ATOM   3203  CD2 TYR A 424     598.423 -39.093 186.787  1.00114.32           C  
ANISOU 3203  CD2 TYR A 424    12970  15179  15287   -224   1379   -154       C  
ATOM   3204  CE1 TYR A 424     599.638 -41.133 185.361  1.00117.77           C  
ANISOU 3204  CE1 TYR A 424    13203  15790  15754    -75   1522   -555       C  
ATOM   3205  CE2 TYR A 424     598.640 -38.942 185.433  1.00115.22           C  
ANISOU 3205  CE2 TYR A 424    13077  15463  15238   -273   1551   -187       C  
ATOM   3206  CZ  TYR A 424     599.245 -39.962 184.724  1.00116.96           C  
ANISOU 3206  CZ  TYR A 424    13196  15784  15458   -203   1629   -392       C  
ATOM   3207  OH  TYR A 424     599.452 -39.796 183.374  1.00118.02           O  
ANISOU 3207  OH  TYR A 424    13338  16112  15393   -256   1815   -432       O  
ATOM   3208  N   VAL A 425     599.830 -41.634 191.410  1.00 66.36           N  
ANISOU 3208  N   VAL A 425     6719   8621   9874    141    768   -317       N  
ATOM   3209  CA  VAL A 425     601.043 -41.345 192.141  1.00 66.93           C  
ANISOU 3209  CA  VAL A 425     6630   8704  10096    164    702   -363       C  
ATOM   3210  C   VAL A 425     601.226 -42.426 193.196  1.00 68.19           C  
ANISOU 3210  C   VAL A 425     6807   8728  10374    315    496   -384       C  
ATOM   3211  O   VAL A 425     602.225 -42.462 193.887  1.00 68.69           O  
ANISOU 3211  O   VAL A 425     6737   8788  10574    379    386   -436       O  
ATOM   3212  CB  VAL A 425     600.976 -39.881 192.744  1.00 66.02           C  
ANISOU 3212  CB  VAL A 425     6545   8601   9938     30    704   -242       C  
ATOM   3213  CG1 VAL A 425     602.115 -39.556 193.688  1.00 66.96           C  
ANISOU 3213  CG1 VAL A 425     6510   8722  10210     45    593   -296       C  
ATOM   3214  CG2 VAL A 425     600.971 -38.867 191.622  1.00 64.94           C  
ANISOU 3214  CG2 VAL A 425     6383   8579   9711   -110    912   -211       C  
ATOM   3215  N   GLU A 426     600.277 -43.345 193.295  1.00 99.48           N  
ANISOU 3215  N   GLU A 426    10930  12573  14293    373    438   -343       N  
ATOM   3216  CA  GLU A 426     600.511 -44.542 194.104  1.00100.89           C  
ANISOU 3216  CA  GLU A 426    11135  12603  14597    526    262   -359       C  
ATOM   3217  C   GLU A 426     601.076 -45.657 193.220  1.00101.80           C  
ANISOU 3217  C   GLU A 426    11131  12704  14844    646    303   -541       C  
ATOM   3218  O   GLU A 426     601.859 -46.479 193.681  1.00102.81           O  
ANISOU 3218  O   GLU A 426    11175  12746  15143    797    173   -609       O  
ATOM   3219  CB  GLU A 426     599.231 -44.993 194.823  1.00101.11           C  
ANISOU 3219  CB  GLU A 426    11401  12480  14537    514    181   -211       C  
ATOM   3220  CG  GLU A 426     598.611 -46.299 194.323  1.00101.98           C  
ANISOU 3220  CG  GLU A 426    11592  12464  14692    578    185   -260       C  
ATOM   3221  CD  GLU A 426     597.341 -46.667 195.088  1.00102.20           C  
ANISOU 3221  CD  GLU A 426    11839  12347  14647    534    127   -104       C  
ATOM   3222  OE1 GLU A 426     596.383 -47.195 194.463  1.00102.41           O  
ANISOU 3222  OE1 GLU A 426    11942  12321  14648    492    193   -125       O  
ATOM   3223  OE2 GLU A 426     597.305 -46.423 196.320  1.00102.33           O  
ANISOU 3223  OE2 GLU A 426    11944  12310  14626    536     20     31       O  
ATOM   3224  N   GLN A 427     600.700 -45.658 191.945  1.00105.60           N  
ANISOU 3224  N   GLN A 427    11604  13276  15241    587    476   -627       N  
ATOM   3225  CA  GLN A 427     601.268 -46.596 190.992  1.00106.60           C  
ANISOU 3225  CA  GLN A 427    11608  13424  15472    690    547   -837       C  
ATOM   3226  C   GLN A 427     602.732 -46.238 190.715  1.00106.72           C  
ANISOU 3226  C   GLN A 427    11358  13581  15611    727    617   -977       C  
ATOM   3227  O   GLN A 427     603.634 -46.977 191.096  1.00107.72           O  
ANISOU 3227  O   GLN A 427    11345  13639  15945    884    512  -1086       O  
ATOM   3228  CB  GLN A 427     600.449 -46.615 189.699  1.00106.46           C  
ANISOU 3228  CB  GLN A 427    11664  13496  15288    606    710   -899       C  
ATOM   3229  CG  GLN A 427     599.022 -47.125 189.911  1.00106.77           C  
ANISOU 3229  CG  GLN A 427    11923  13393  15252    575    635   -803       C  
ATOM   3230  CD  GLN A 427     598.125 -46.990 188.681  1.00106.78           C  
ANISOU 3230  CD  GLN A 427    11996  13507  15069    482    761   -855       C  
ATOM   3231  OE1 GLN A 427     598.356 -46.145 187.812  1.00106.09           O  
ANISOU 3231  OE1 GLN A 427    11853  13618  14839    404    906   -875       O  
ATOM   3232  NE2 GLN A 427     597.089 -47.828 188.611  1.00107.75           N  
ANISOU 3232  NE2 GLN A 427    12247  13502  15192    486    701   -871       N  
ATOM   3233  N   LEU A 428     602.976 -45.093 190.083  1.00115.02           N  
ANISOU 3233  N   LEU A 428    12332  14821  16549    584    790   -966       N  
ATOM   3234  CA  LEU A 428     604.336 -44.731 189.681  1.00115.33           C  
ANISOU 3234  CA  LEU A 428    12099  15012  16708    586    904  -1110       C  
ATOM   3235  C   LEU A 428     605.312 -44.534 190.845  1.00115.68           C  
ANISOU 3235  C   LEU A 428    11987  15016  16952    650    734  -1104       C  
ATOM   3236  O   LEU A 428     606.503 -44.352 190.611  1.00116.21           O  
ANISOU 3236  O   LEU A 428    11789  15197  17168    668    804  -1247       O  
ATOM   3237  CB  LEU A 428     604.314 -43.460 188.824  1.00114.37           C  
ANISOU 3237  CB  LEU A 428    11962  15079  16415    389   1133  -1055       C  
ATOM   3238  CG  LEU A 428     603.731 -43.568 187.410  1.00114.26           C  
ANISOU 3238  CG  LEU A 428    12035  15184  16193    330   1334  -1107       C  
ATOM   3239  CD1 LEU A 428     603.478 -42.174 186.832  1.00112.84           C  
ANISOU 3239  CD1 LEU A 428    11917  15141  15817    130   1504   -958       C  
ATOM   3240  CD2 LEU A 428     604.637 -44.381 186.476  1.00115.89           C  
ANISOU 3240  CD2 LEU A 428    12045  15501  16485    425   1478  -1370       C  
ATOM   3241  N   CYS A 429     604.839 -44.598 192.088  1.00 95.11           N  
ANISOU 3241  N   CYS A 429     9532  12260  14347    688    511   -954       N  
ATOM   3242  CA  CYS A 429     605.687 -44.222 193.230  1.00 95.50           C  
ANISOU 3242  CA  CYS A 429     9457  12298  14531    726    332   -934       C  
ATOM   3243  C   CYS A 429     605.726 -45.231 194.408  1.00 96.67           C  
ANISOU 3243  C   CYS A 429     9682  12263  14784    917     46   -888       C  
ATOM   3244  O   CYS A 429     606.640 -45.191 195.238  1.00 97.51           O  
ANISOU 3244  O   CYS A 429     9644  12373  15031   1004   -132   -920       O  
ATOM   3245  CB  CYS A 429     605.256 -42.827 193.722  1.00 94.29           C  
ANISOU 3245  CB  CYS A 429     9402  12189  14235    539    349   -777       C  
ATOM   3246  SG  CYS A 429     605.540 -42.395 195.472  1.00 95.21           S  
ANISOU 3246  SG  CYS A 429     9549  12234  14391    566     64   -682       S  
ATOM   3247  N   GLY A 430     604.765 -46.145 194.479  1.00101.61           N  
ANISOU 3247  N   GLY A 430    10531  12730  15347    981     -5   -811       N  
ATOM   3248  CA  GLY A 430     604.826 -47.221 195.463  1.00102.82           C  
ANISOU 3248  CA  GLY A 430    10771  12688  15606   1164   -252   -755       C  
ATOM   3249  C   GLY A 430     604.569 -46.790 196.894  1.00103.05           C  
ANISOU 3249  C   GLY A 430    10954  12663  15537   1144   -453   -563       C  
ATOM   3250  O   GLY A 430     603.903 -45.789 197.117  1.00102.26           O  
ANISOU 3250  O   GLY A 430    10968  12629  15256    977   -384   -453       O  
ATOM   3251  N   PRO A 431     605.096 -47.543 197.876  1.00101.53           N  
ANISOU 3251  N   PRO A 431    10771  12349  15455   1324   -707   -523       N  
ATOM   3252  CA  PRO A 431     604.869 -47.304 199.314  1.00102.22           C  
ANISOU 3252  CA  PRO A 431    11035  12386  15419   1329   -922   -338       C  
ATOM   3253  C   PRO A 431     605.509 -46.029 199.853  1.00102.19           C  
ANISOU 3253  C   PRO A 431    10899  12558  15371   1237   -976   -366       C  
ATOM   3254  O   PRO A 431     605.713 -45.920 201.057  1.00103.23           O  
ANISOU 3254  O   PRO A 431    11108  12675  15440   1290  -1202   -275       O  
ATOM   3255  CB  PRO A 431     605.503 -48.537 199.980  1.00103.73           C  
ANISOU 3255  CB  PRO A 431    11226  12412  15773   1578  -1182   -319       C  
ATOM   3256  CG  PRO A 431     606.514 -49.026 198.998  1.00103.83           C  
ANISOU 3256  CG  PRO A 431    10940  12459  16051   1705  -1126   -556       C  
ATOM   3257  CD  PRO A 431     605.907 -48.754 197.645  1.00102.44           C  
ANISOU 3257  CD  PRO A 431    10745  12358  15818   1551   -810   -654       C  
ATOM   3258  N   TYR A 432     605.803 -45.089 198.962  1.00124.34           N  
ANISOU 3258  N   TYR A 432    13519  15523  18202   1096   -770   -490       N  
ATOM   3259  CA  TYR A 432     606.493 -43.858 199.308  1.00124.29           C  
ANISOU 3259  CA  TYR A 432    13351  15669  18206    987   -792   -549       C  
ATOM   3260  C   TYR A 432     605.602 -42.655 199.140  1.00123.09           C  
ANISOU 3260  C   TYR A 432    13336  15571  17862    760   -613   -464       C  
ATOM   3261  O   TYR A 432     606.027 -41.531 199.363  1.00122.91           O  
ANISOU 3261  O   TYR A 432    13208  15648  17845    638   -600   -507       O  
ATOM   3262  CB  TYR A 432     607.732 -43.693 198.440  1.00124.20           C  
ANISOU 3262  CB  TYR A 432    12979  15788  18423    999   -692   -766       C  
ATOM   3263  CG  TYR A 432     608.718 -44.814 198.616  1.00125.45           C  
ANISOU 3263  CG  TYR A 432    12954  15900  18813   1244   -880   -880       C  
ATOM   3264  CD1 TYR A 432     609.194 -45.142 199.878  1.00127.00           C  
ANISOU 3264  CD1 TYR A 432    13162  16042  19049   1395  -1209   -832       C  
ATOM   3265  CD2 TYR A 432     609.159 -45.555 197.530  1.00125.20           C  
ANISOU 3265  CD2 TYR A 432    12744  15875  18952   1337   -738  -1040       C  
ATOM   3266  CE1 TYR A 432     610.089 -46.162 200.056  1.00128.15           C  
ANISOU 3266  CE1 TYR A 432    13140  16129  19420   1642  -1406   -925       C  
ATOM   3267  CE2 TYR A 432     610.056 -46.581 197.697  1.00126.41           C  
ANISOU 3267  CE2 TYR A 432    12719  15966  19345   1582   -914  -1158       C  
ATOM   3268  CZ  TYR A 432     610.520 -46.882 198.965  1.00127.84           C  
ANISOU 3268  CZ  TYR A 432    12909  16079  19583   1740  -1257  -1092       C  
ATOM   3269  OH  TYR A 432     611.420 -47.907 199.145  1.00129.09           O  
ANISOU 3269  OH  TYR A 432    12888  16162  19997   2008  -1460  -1199       O  
ATOM   3270  N   VAL A 433     604.372 -42.901 198.715  1.00 83.75           N  
ANISOU 3270  N   VAL A 433     8574  10513  12734    707   -478   -355       N  
ATOM   3271  CA  VAL A 433     603.395 -41.841 198.499  1.00 82.42           C  
ANISOU 3271  CA  VAL A 433     8546  10378  12394    519   -315   -267       C  
ATOM   3272  C   VAL A 433     603.304 -40.884 199.676  1.00 83.13           C  
ANISOU 3272  C   VAL A 433     8718  10484  12384    445   -433   -204       C  
ATOM   3273  O   VAL A 433     603.153 -39.688 199.501  1.00 82.35           O  
ANISOU 3273  O   VAL A 433     8602  10444  12242    292   -320   -208       O  
ATOM   3274  CB  VAL A 433     601.997 -42.423 198.251  1.00 81.76           C  
ANISOU 3274  CB  VAL A 433     8704  10189  12171    509   -235   -146       C  
ATOM   3275  CG1 VAL A 433     601.745 -42.591 196.787  1.00 80.32           C  
ANISOU 3275  CG1 VAL A 433     8463  10050  12005    467    -25   -215       C  
ATOM   3276  CG2 VAL A 433     601.859 -43.752 198.960  1.00 83.37           C  
ANISOU 3276  CG2 VAL A 433     9029  10249  12399    668   -410    -84       C  
ATOM   3277  N   PHE A 434     603.417 -41.420 200.880  1.00 92.59           N  
ANISOU 3277  N   PHE A 434    10014  11624  13543    558   -664   -148       N  
ATOM   3278  CA  PHE A 434     603.265 -40.609 202.075  1.00 93.61           C  
ANISOU 3278  CA  PHE A 434    10252  11777  13538    498   -787   -101       C  
ATOM   3279  C   PHE A 434     604.540 -39.863 202.411  1.00 94.32           C  
ANISOU 3279  C   PHE A 434    10107  11976  13757    478   -906   -247       C  
ATOM   3280  O   PHE A 434     604.622 -39.190 203.437  1.00 95.53           O  
ANISOU 3280  O   PHE A 434    10318  12163  13818    438  -1042   -253       O  
ATOM   3281  CB  PHE A 434     602.820 -41.487 203.229  1.00 94.92           C  
ANISOU 3281  CB  PHE A 434    10646  11852  13566    617   -978     34       C  
ATOM   3282  CG  PHE A 434     601.531 -42.167 202.962  1.00 94.27           C  
ANISOU 3282  CG  PHE A 434    10784  11657  13376    605   -850    172       C  
ATOM   3283  CD1 PHE A 434     600.336 -41.571 203.323  1.00 94.12           C  
ANISOU 3283  CD1 PHE A 434    10964  11629  13169    485   -741    269       C  
ATOM   3284  CD2 PHE A 434     601.497 -43.378 202.300  1.00 93.87           C  
ANISOU 3284  CD2 PHE A 434    10722  11507  13436    709   -827    183       C  
ATOM   3285  CE1 PHE A 434     599.128 -42.184 203.055  1.00 93.41           C  
ANISOU 3285  CE1 PHE A 434    11043  11444  13004    461   -618    381       C  
ATOM   3286  CE2 PHE A 434     600.282 -43.992 202.023  1.00 93.27           C  
ANISOU 3286  CE2 PHE A 434    10834  11322  13281    677   -708    292       C  
ATOM   3287  CZ  PHE A 434     599.102 -43.393 202.405  1.00 92.94           C  
ANISOU 3287  CZ  PHE A 434    10973  11285  13056    548   -605    393       C  
ATOM   3288  N   ILE A 435     605.528 -39.991 201.532  1.00 83.95           N  
ANISOU 3288  N   ILE A 435     8517  10722  12658    501   -847   -383       N  
ATOM   3289  CA  ILE A 435     606.754 -39.205 201.615  1.00 84.39           C  
ANISOU 3289  CA  ILE A 435     8293  10890  12882    444   -905   -545       C  
ATOM   3290  C   ILE A 435     606.564 -37.966 200.749  1.00 83.04           C  
ANISOU 3290  C   ILE A 435     8059  10764  12726    223   -638   -574       C  
ATOM   3291  O   ILE A 435     607.099 -36.898 201.055  1.00 83.50           O  
ANISOU 3291  O   ILE A 435     7999  10875  12851     96   -656   -658       O  
ATOM   3292  CB  ILE A 435     608.005 -40.031 201.186  1.00 84.81           C  
ANISOU 3292  CB  ILE A 435     8046  10992  13184    594   -981   -690       C  
ATOM   3293  CG1 ILE A 435     608.675 -40.639 202.423  1.00 86.74           C  
ANISOU 3293  CG1 ILE A 435     8265  11229  13462    780  -1339   -707       C  
ATOM   3294  CG2 ILE A 435     608.984 -39.189 200.363  1.00 84.34           C  
ANISOU 3294  CG2 ILE A 435     7659  11056  13329    458   -817   -861       C  
ATOM   3295  CD1 ILE A 435     609.362 -41.945 202.163  1.00 86.83           C  
ANISOU 3295  CD1 ILE A 435     8131  11203  13658   1011  -1452   -763       C  
ATOM   3296  N   ILE A 436     605.781 -38.111 199.681  1.00 68.70           N  
ANISOU 3296  N   ILE A 436     6337   8917  10848    175   -402   -499       N  
ATOM   3297  CA  ILE A 436     605.280 -36.949 198.959  1.00 67.23           C  
ANISOU 3297  CA  ILE A 436     6189   8743  10612    -21   -167   -460       C  
ATOM   3298  C   ILE A 436     604.535 -36.052 199.945  1.00 67.71           C  
ANISOU 3298  C   ILE A 436     6448   8745  10532   -105   -240   -386       C  
ATOM   3299  O   ILE A 436     604.888 -34.890 200.129  1.00 67.89           O  
ANISOU 3299  O   ILE A 436     6397   8782  10615   -244   -215   -442       O  
ATOM   3300  CB  ILE A 436     604.329 -37.327 197.798  1.00 65.51           C  
ANISOU 3300  CB  ILE A 436     6098   8501  10292    -33     46   -367       C  
ATOM   3301  CG1 ILE A 436     605.090 -38.072 196.697  1.00 65.42           C  
ANISOU 3301  CG1 ILE A 436     5884   8565  10409     28    159   -474       C  
ATOM   3302  CG2 ILE A 436     603.621 -36.087 197.268  1.00 63.86           C  
ANISOU 3302  CG2 ILE A 436     5989   8280   9996   -213    235   -283       C  
ATOM   3303  CD1 ILE A 436     604.855 -37.514 195.289  1.00 64.20           C  
ANISOU 3303  CD1 ILE A 436     5710   8475  10209   -107    445   -454       C  
ATOM   3304  N   PHE A 437     603.525 -36.608 200.606  1.00 80.77           N  
ANISOU 3304  N   PHE A 437     8349  10328  12011    -22   -323   -272       N  
ATOM   3305  CA  PHE A 437     602.740 -35.851 201.571  1.00 81.56           C  
ANISOU 3305  CA  PHE A 437     8646  10384  11960    -85   -374   -216       C  
ATOM   3306  C   PHE A 437     603.561 -35.434 202.791  1.00 83.64           C  
ANISOU 3306  C   PHE A 437     8846  10690  12246    -78   -600   -321       C  
ATOM   3307  O   PHE A 437     603.184 -34.514 203.512  1.00 84.43           O  
ANISOU 3307  O   PHE A 437     9050  10771  12257   -163   -625   -336       O  
ATOM   3308  CB  PHE A 437     601.527 -36.652 202.028  1.00 81.96           C  
ANISOU 3308  CB  PHE A 437     8954  10365  11822     -1   -398    -77       C  
ATOM   3309  CG  PHE A 437     600.582 -37.011 200.919  1.00 79.90           C  
ANISOU 3309  CG  PHE A 437     8766  10064  11529    -18   -201     10       C  
ATOM   3310  CD1 PHE A 437     600.385 -36.157 199.843  1.00 77.84           C  
ANISOU 3310  CD1 PHE A 437     8446   9820  11310   -136     -4      8       C  
ATOM   3311  CD2 PHE A 437     599.897 -38.217 200.948  1.00 80.02           C  
ANISOU 3311  CD2 PHE A 437     8912  10021  11472     83   -222     97       C  
ATOM   3312  CE1 PHE A 437     599.510 -36.498 198.811  1.00 75.86           C  
ANISOU 3312  CE1 PHE A 437     8265   9552  11008   -142    149     82       C  
ATOM   3313  CE2 PHE A 437     599.031 -38.567 199.928  1.00 78.21           C  
ANISOU 3313  CE2 PHE A 437     8735   9762  11219     63    -62    152       C  
ATOM   3314  CZ  PHE A 437     598.837 -37.708 198.856  1.00 76.11           C  
ANISOU 3314  CZ  PHE A 437     8407   9538  10974    -43    114    139       C  
ATOM   3315  N   THR A 438     604.685 -36.094 203.025  1.00 82.87           N  
ANISOU 3315  N   THR A 438     8567  10650  12270     30   -773   -410       N  
ATOM   3316  CA  THR A 438     605.544 -35.692 204.129  1.00 84.68           C  
ANISOU 3316  CA  THR A 438     8707  10940  12528     40  -1016   -528       C  
ATOM   3317  C   THR A 438     606.418 -34.494 203.719  1.00 84.31           C  
ANISOU 3317  C   THR A 438     8408  10942  12684   -130   -939   -686       C  
ATOM   3318  O   THR A 438     606.756 -33.641 204.544  1.00 85.60           O  
ANISOU 3318  O   THR A 438     8546  11129  12852   -209  -1065   -792       O  
ATOM   3319  CB  THR A 438     606.411 -36.873 204.603  1.00 85.71           C  
ANISOU 3319  CB  THR A 438     8735  11110  12722    243  -1269   -559       C  
ATOM   3320  OG1 THR A 438     605.546 -37.939 205.012  1.00 86.01           O  
ANISOU 3320  OG1 THR A 438     9036  11071  12574    378  -1326   -390       O  
ATOM   3321  CG2 THR A 438     607.298 -36.481 205.780  1.00 87.64           C  
ANISOU 3321  CG2 THR A 438     8885  11437  12977    267  -1562   -687       C  
ATOM   3322  N   VAL A 439     606.758 -34.417 202.435  1.00 80.06           N  
ANISOU 3322  N   VAL A 439     7693  10417  12310   -199   -719   -705       N  
ATOM   3323  CA  VAL A 439     607.581 -33.317 201.946  1.00 79.91           C  
ANISOU 3323  CA  VAL A 439     7435  10432  12495   -383   -605   -831       C  
ATOM   3324  C   VAL A 439     606.747 -32.035 201.917  1.00 79.28           C  
ANISOU 3324  C   VAL A 439     7527  10259  12337   -563   -455   -772       C  
ATOM   3325  O   VAL A 439     607.258 -30.944 202.184  1.00 79.98           O  
ANISOU 3325  O   VAL A 439     7507  10332  12549   -716   -463   -883       O  
ATOM   3326  CB  VAL A 439     608.186 -33.618 200.540  1.00 78.79           C  
ANISOU 3326  CB  VAL A 439     7066  10346  12525   -413   -381   -857       C  
ATOM   3327  CG1 VAL A 439     607.336 -33.066 199.407  1.00 76.93           C  
ANISOU 3327  CG1 VAL A 439     6963  10055  12213   -545    -74   -725       C  
ATOM   3328  CG2 VAL A 439     609.566 -33.035 200.434  1.00 79.73           C  
ANISOU 3328  CG2 VAL A 439     6835  10548  12911   -523   -387  -1042       C  
ATOM   3329  N   LEU A 440     605.454 -32.177 201.621  1.00 64.52           N  
ANISOU 3329  N   LEU A 440     5917   8314  10282   -539   -330   -608       N  
ATOM   3330  CA  LEU A 440     604.534 -31.049 201.591  1.00 63.93           C  
ANISOU 3330  CA  LEU A 440     6018   8137  10135   -670   -199   -542       C  
ATOM   3331  C   LEU A 440     604.313 -30.603 203.012  1.00 65.82           C  
ANISOU 3331  C   LEU A 440     6381   8352  10275   -661   -395   -615       C  
ATOM   3332  O   LEU A 440     604.631 -29.470 203.365  1.00 66.45           O  
ANISOU 3332  O   LEU A 440     6411   8387  10449   -796   -407   -723       O  
ATOM   3333  CB  LEU A 440     603.217 -31.430 200.920  1.00 62.25           C  
ANISOU 3333  CB  LEU A 440     6020   7871   9762   -622    -42   -364       C  
ATOM   3334  CG  LEU A 440     603.364 -31.771 199.434  1.00 60.30           C  
ANISOU 3334  CG  LEU A 440     5674   7660   9577   -643    163   -302       C  
ATOM   3335  CD1 LEU A 440     602.086 -32.290 198.828  1.00 58.58           C  
ANISOU 3335  CD1 LEU A 440     5655   7408   9194   -578    270   -151       C  
ATOM   3336  CD2 LEU A 440     603.827 -30.571 198.672  1.00 59.62           C  
ANISOU 3336  CD2 LEU A 440     5475   7546   9632   -831    341   -314       C  
ATOM   3337  N   LEU A 441     603.818 -31.527 203.831  1.00 72.18           N  
ANISOU 3337  N   LEU A 441     7349   9186  10890   -506   -548   -563       N  
ATOM   3338  CA  LEU A 441     603.661 -31.311 205.267  1.00 74.48           C  
ANISOU 3338  CA  LEU A 441     7774   9493  11033   -472   -752   -632       C  
ATOM   3339  C   LEU A 441     604.836 -30.554 205.917  1.00 75.79           C  
ANISOU 3339  C   LEU A 441     7751   9708  11338   -553   -925   -842       C  
ATOM   3340  O   LEU A 441     604.648 -29.779 206.856  1.00 77.10           O  
ANISOU 3340  O   LEU A 441     8015   9858  11420   -608  -1017   -942       O  
ATOM   3341  CB  LEU A 441     603.449 -32.657 205.971  1.00 75.81           C  
ANISOU 3341  CB  LEU A 441     8073   9714  11018   -284   -923   -547       C  
ATOM   3342  CG  LEU A 441     601.971 -32.994 206.150  1.00 75.77           C  
ANISOU 3342  CG  LEU A 441     8353   9649  10789   -244   -814   -387       C  
ATOM   3343  CD1 LEU A 441     601.719 -34.485 206.409  1.00 76.51           C  
ANISOU 3343  CD1 LEU A 441     8558   9755  10756    -80   -906   -255       C  
ATOM   3344  CD2 LEU A 441     601.427 -32.145 207.279  1.00 77.62           C  
ANISOU 3344  CD2 LEU A 441     8756   9879  10858   -297   -865   -452       C  
ATOM   3345  N   VAL A 442     606.044 -30.772 205.419  1.00 84.37           N  
ANISOU 3345  N   VAL A 442     8553  10859  12643   -563   -967   -930       N  
ATOM   3346  CA  VAL A 442     607.181 -30.077 205.966  1.00 85.50           C  
ANISOU 3346  CA  VAL A 442     8477  11055  12954   -652  -1131  -1144       C  
ATOM   3347  C   VAL A 442     607.217 -28.661 205.412  1.00 84.80           C  
ANISOU 3347  C   VAL A 442     8316  10863  13043   -886   -930  -1210       C  
ATOM   3348  O   VAL A 442     607.195 -27.698 206.177  1.00 85.93           O  
ANISOU 3348  O   VAL A 442     8507  10959  13185   -986  -1011  -1339       O  
ATOM   3349  CB  VAL A 442     608.462 -30.824 205.660  1.00 85.49           C  
ANISOU 3349  CB  VAL A 442     8168  11166  13150   -576  -1247  -1229       C  
ATOM   3350  CG1 VAL A 442     609.675 -29.940 205.929  1.00 86.34           C  
ANISOU 3350  CG1 VAL A 442     7980  11320  13504   -719  -1355  -1465       C  
ATOM   3351  CG2 VAL A 442     608.503 -32.081 206.504  1.00 86.61           C  
ANISOU 3351  CG2 VAL A 442     8402  11383  13121   -338  -1518  -1182       C  
ATOM   3352  N   LEU A 443     607.269 -28.539 204.086  1.00 76.00           N  
ANISOU 3352  N   LEU A 443     7099   9706  12072   -972   -668  -1119       N  
ATOM   3353  CA  LEU A 443     607.177 -27.241 203.408  1.00 75.02           C  
ANISOU 3353  CA  LEU A 443     6950   9453  12102  -1191   -442  -1117       C  
ATOM   3354  C   LEU A 443     606.126 -26.336 204.021  1.00 75.34           C  
ANISOU 3354  C   LEU A 443     7254   9356  12017  -1239   -428  -1102       C  
ATOM   3355  O   LEU A 443     606.431 -25.248 204.502  1.00 76.31           O  
ANISOU 3355  O   LEU A 443     7336   9396  12262  -1382   -468  -1249       O  
ATOM   3356  CB  LEU A 443     606.846 -27.431 201.939  1.00 72.81           C  
ANISOU 3356  CB  LEU A 443     6671   9146  11847  -1222   -153   -937       C  
ATOM   3357  CG  LEU A 443     607.983 -27.650 200.961  1.00 72.02           C  
ANISOU 3357  CG  LEU A 443     6268   9134  11962  -1295    -28   -980       C  
ATOM   3358  CD1 LEU A 443     607.439 -28.430 199.768  1.00 69.90           C  
ANISOU 3358  CD1 LEU A 443     6076   8900  11585  -1214    175   -801       C  
ATOM   3359  CD2 LEU A 443     608.529 -26.303 200.535  1.00 72.91           C  
ANISOU 3359  CD2 LEU A 443     6248   9150  12306  -1554    133  -1036       C  
ATOM   3360  N   PHE A 444     604.885 -26.802 203.994  1.00 80.50           N  
ANISOU 3360  N   PHE A 444     8163   9981  12441  -1119   -368   -939       N  
ATOM   3361  CA  PHE A 444     603.788 -26.114 204.655  1.00 81.04           C  
ANISOU 3361  CA  PHE A 444     8480   9941  12372  -1123   -359   -933       C  
ATOM   3362  C   PHE A 444     604.123 -25.760 206.082  1.00 83.60           C  
ANISOU 3362  C   PHE A 444     8826  10302  12639  -1123   -597  -1140       C  
ATOM   3363  O   PHE A 444     603.973 -24.607 206.480  1.00 84.47           O  
ANISOU 3363  O   PHE A 444     8982  10295  12817  -1238   -582  -1260       O  
ATOM   3364  CB  PHE A 444     602.528 -26.962 204.625  1.00 80.35           C  
ANISOU 3364  CB  PHE A 444     8621   9870  12039   -968   -308   -757       C  
ATOM   3365  CG  PHE A 444     601.902 -27.034 203.276  1.00 77.63           C  
ANISOU 3365  CG  PHE A 444     8307   9465  11722   -982    -73   -569       C  
ATOM   3366  CD1 PHE A 444     601.991 -25.965 202.401  1.00 76.23           C  
ANISOU 3366  CD1 PHE A 444     8077   9167  11719  -1133    103   -537       C  
ATOM   3367  CD2 PHE A 444     601.248 -28.168 202.862  1.00 76.54           C  
ANISOU 3367  CD2 PHE A 444     8256   9388  11438   -849    -34   -423       C  
ATOM   3368  CE1 PHE A 444     601.424 -26.019 201.145  1.00 73.83           C  
ANISOU 3368  CE1 PHE A 444     7819   8825  11409  -1139    302   -354       C  
ATOM   3369  CE2 PHE A 444     600.681 -28.226 201.600  1.00 73.91           C  
ANISOU 3369  CE2 PHE A 444     7950   9018  11116   -862    163   -270       C  
ATOM   3370  CZ  PHE A 444     600.770 -27.144 200.745  1.00 72.58           C  
ANISOU 3370  CZ  PHE A 444     7739   8750  11089  -1002    325   -231       C  
ATOM   3371  N   PHE A 445     604.581 -26.746 206.845  1.00 82.18           N  
ANISOU 3371  N   PHE A 445     8619  10276  12330   -988   -824  -1186       N  
ATOM   3372  CA  PHE A 445     605.007 -26.502 208.214  1.00 84.58           C  
ANISOU 3372  CA  PHE A 445     8940  10652  12544   -975  -1086  -1387       C  
ATOM   3373  C   PHE A 445     605.954 -25.310 208.279  1.00 85.06           C  
ANISOU 3373  C   PHE A 445     8793  10654  12871  -1167  -1126  -1612       C  
ATOM   3374  O   PHE A 445     605.713 -24.357 209.026  1.00 86.28           O  
ANISOU 3374  O   PHE A 445     9043  10738  13003  -1248  -1175  -1769       O  
ATOM   3375  CB  PHE A 445     605.693 -27.733 208.798  1.00 85.64           C  
ANISOU 3375  CB  PHE A 445     9008  10961  12569   -809  -1344  -1393       C  
ATOM   3376  CG  PHE A 445     606.048 -27.595 210.249  1.00 88.02           C  
ANISOU 3376  CG  PHE A 445     9368  11364  12712   -769  -1642  -1574       C  
ATOM   3377  CD1 PHE A 445     605.186 -28.062 211.229  1.00 89.45           C  
ANISOU 3377  CD1 PHE A 445     9841  11599  12546   -645  -1728  -1507       C  
ATOM   3378  CD2 PHE A 445     607.240 -27.000 210.636  1.00 88.88           C  
ANISOU 3378  CD2 PHE A 445     9238  11526  13007   -863  -1834  -1818       C  
ATOM   3379  CE1 PHE A 445     605.501 -27.945 212.568  1.00 91.56           C  
ANISOU 3379  CE1 PHE A 445    10188  11982  12620   -605  -2003  -1670       C  
ATOM   3380  CE2 PHE A 445     607.560 -26.875 211.973  1.00 91.02           C  
ANISOU 3380  CE2 PHE A 445     9570  11909  13106   -821  -2133  -1998       C  
ATOM   3381  CZ  PHE A 445     606.684 -27.349 212.944  1.00 92.32           C  
ANISOU 3381  CZ  PHE A 445    10053  12137  12887   -687  -2219  -1920       C  
ATOM   3382  N   ILE A 446     607.026 -25.383 207.491  1.00110.95           N  
ANISOU 3382  N   ILE A 446    11781  13963  16413  -1245  -1093  -1640       N  
ATOM   3383  CA  ILE A 446     608.005 -24.307 207.393  1.00111.41           C  
ANISOU 3383  CA  ILE A 446    11598  13958  16774  -1458  -1096  -1840       C  
ATOM   3384  C   ILE A 446     607.343 -22.969 207.092  1.00110.90           C  
ANISOU 3384  C   ILE A 446    11659  13666  16810  -1631   -886  -1838       C  
ATOM   3385  O   ILE A 446     607.565 -21.984 207.807  1.00112.23           O  
ANISOU 3385  O   ILE A 446    11820  13755  17069  -1753   -982  -2051       O  
ATOM   3386  CB  ILE A 446     609.040 -24.586 206.301  1.00110.33           C  
ANISOU 3386  CB  ILE A 446    11143  13870  16908  -1532   -983  -1816       C  
ATOM   3387  CG1 ILE A 446     609.926 -25.770 206.685  1.00111.46           C  
ANISOU 3387  CG1 ILE A 446    11096  14222  17031  -1365  -1231  -1881       C  
ATOM   3388  CG2 ILE A 446     609.880 -23.360 206.068  1.00110.70           C  
ANISOU 3388  CG2 ILE A 446    10963  13814  17286  -1794   -914  -1988       C  
ATOM   3389  CD1 ILE A 446     611.087 -25.989 205.736  1.00110.98           C  
ANISOU 3389  CD1 ILE A 446    10668  14229  17270  -1439  -1135  -1923       C  
ATOM   3390  N   PHE A 447     606.529 -22.956 206.033  1.00 73.97           N  
ANISOU 3390  N   PHE A 447     7103   8884  12120  -1633   -615  -1602       N  
ATOM   3391  CA  PHE A 447     605.851 -21.748 205.569  1.00 73.28           C  
ANISOU 3391  CA  PHE A 447     7141   8560  12142  -1771   -404  -1549       C  
ATOM   3392  C   PHE A 447     605.127 -21.043 206.706  1.00 74.79           C  
ANISOU 3392  C   PHE A 447     7541   8659  12215  -1753   -509  -1696       C  
ATOM   3393  O   PHE A 447     605.248 -19.834 206.887  1.00 75.48           O  
ANISOU 3393  O   PHE A 447     7620   8566  12491  -1912   -480  -1837       O  
ATOM   3394  CB  PHE A 447     604.861 -22.084 204.444  1.00 71.05           C  
ANISOU 3394  CB  PHE A 447     7009   8222  11763  -1702   -162  -1258       C  
ATOM   3395  CG  PHE A 447     604.055 -20.895 203.959  1.00 70.45           C  
ANISOU 3395  CG  PHE A 447     7088   7898  11783  -1805     32  -1171       C  
ATOM   3396  CD1 PHE A 447     602.894 -20.501 204.623  1.00 71.06           C  
ANISOU 3396  CD1 PHE A 447     7406   7875  11717  -1719     12  -1187       C  
ATOM   3397  CD2 PHE A 447     604.450 -20.177 202.834  1.00 69.50           C  
ANISOU 3397  CD2 PHE A 447     6871   7639  11895  -1981    240  -1066       C  
ATOM   3398  CE1 PHE A 447     602.152 -19.413 204.184  1.00 70.60           C  
ANISOU 3398  CE1 PHE A 447     7480   7574  11772  -1788    172  -1112       C  
ATOM   3399  CE2 PHE A 447     603.704 -19.089 202.385  1.00 69.39           C  
ANISOU 3399  CE2 PHE A 447     7016   7374  11973  -2058    399   -960       C  
ATOM   3400  CZ  PHE A 447     602.559 -18.710 203.061  1.00 69.63           C  
ANISOU 3400  CZ  PHE A 447     7275   7297  11885  -1951    354   -988       C  
ATOM   3401  N   THR A 448     604.368 -21.809 207.474  1.00 88.11           N  
ANISOU 3401  N   THR A 448     9419  10464  13593  -1563   -620  -1668       N  
ATOM   3402  CA  THR A 448     603.527 -21.210 208.497  1.00 89.50           C  
ANISOU 3402  CA  THR A 448     9816  10573  13618  -1530   -674  -1795       C  
ATOM   3403  C   THR A 448     604.369 -20.708 209.663  1.00 91.55           C  
ANISOU 3403  C   THR A 448     9992  10886  13909  -1603   -922  -2112       C  
ATOM   3404  O   THR A 448     603.902 -19.903 210.463  1.00 92.31           O  
ANISOU 3404  O   THR A 448    10226  10893  13952  -1630   -957  -2288       O  
ATOM   3405  CB  THR A 448     602.453 -22.205 209.021  1.00 89.82           C  
ANISOU 3405  CB  THR A 448    10087  10742  13300  -1321   -698  -1670       C  
ATOM   3406  OG1 THR A 448     603.041 -23.117 209.953  1.00 91.17           O  
ANISOU 3406  OG1 THR A 448    10233  11130  13276  -1219   -952  -1752       O  
ATOM   3407  CG2 THR A 448     601.812 -22.987 207.871  1.00 87.83           C  
ANISOU 3407  CG2 THR A 448     9869  10489  13012  -1239   -508  -1375       C  
ATOM   3408  N   TYR A 449     605.607 -21.183 209.757  1.00101.95           N  
ANISOU 3408  N   TYR A 449    11070  12350  15315  -1628  -1100  -2202       N  
ATOM   3409  CA  TYR A 449     606.464 -20.822 210.875  1.00104.01           C  
ANISOU 3409  CA  TYR A 449    11229  12697  15592  -1683  -1380  -2512       C  
ATOM   3410  C   TYR A 449     607.029 -19.418 210.712  1.00104.31           C  
ANISOU 3410  C   TYR A 449    11120  12531  15981  -1931  -1327  -2721       C  
ATOM   3411  O   TYR A 449     607.274 -18.721 211.693  1.00105.96           O  
ANISOU 3411  O   TYR A 449    11342  12725  16195  -1999  -1501  -3008       O  
ATOM   3412  CB  TYR A 449     607.607 -21.825 211.035  1.00104.55           C  
ANISOU 3412  CB  TYR A 449    11067  12994  15661  -1609  -1614  -2544       C  
ATOM   3413  CG  TYR A 449     608.488 -21.515 212.225  1.00106.78           C  
ANISOU 3413  CG  TYR A 449    11241  13396  15936  -1645  -1947  -2867       C  
ATOM   3414  CD1 TYR A 449     608.083 -21.831 213.515  1.00108.55           C  
ANISOU 3414  CD1 TYR A 449    11687  13761  15796  -1504  -2175  -2963       C  
ATOM   3415  CD2 TYR A 449     609.717 -20.886 212.063  1.00107.22           C  
ANISOU 3415  CD2 TYR A 449    10970  13428  16341  -1832  -2032  -3083       C  
ATOM   3416  CE1 TYR A 449     608.887 -21.537 214.614  1.00110.61           C  
ANISOU 3416  CE1 TYR A 449    11859  14149  16018  -1532  -2504  -3270       C  
ATOM   3417  CE2 TYR A 449     610.524 -20.584 213.154  1.00109.32           C  
ANISOU 3417  CE2 TYR A 449    11119  13810  16607  -1870  -2362  -3404       C  
ATOM   3418  CZ  TYR A 449     610.105 -20.913 214.426  1.00110.96           C  
ANISOU 3418  CZ  TYR A 449    11564  14168  16427  -1712  -2610  -3498       C  
ATOM   3419  OH  TYR A 449     610.904 -20.616 215.510  1.00113.04           O  
ANISOU 3419  OH  TYR A 449    11724  14567  16660  -1743  -2960  -3824       O  
ATOM   3420  N   PHE A 450     607.212 -19.000 209.466  1.00152.69           N  
ANISOU 3420  N   PHE A 450    17123  18496  22396  -2071  -1079  -2575       N  
ATOM   3421  CA  PHE A 450     607.846 -17.722 209.184  1.00153.04           C  
ANISOU 3421  CA  PHE A 450    17010  18326  22814  -2331  -1004  -2736       C  
ATOM   3422  C   PHE A 450     606.918 -16.683 208.572  1.00152.06           C  
ANISOU 3422  C   PHE A 450    17072  17891  22812  -2420   -736  -2617       C  
ATOM   3423  O   PHE A 450     607.214 -15.495 208.627  1.00152.81           O  
ANISOU 3423  O   PHE A 450    17118  17759  23184  -2620   -698  -2781       O  
ATOM   3424  CB  PHE A 450     609.035 -17.923 208.248  1.00152.35           C  
ANISOU 3424  CB  PHE A 450    16587  18286  23014  -2470   -932  -2686       C  
ATOM   3425  CG  PHE A 450     610.205 -18.596 208.896  1.00153.65           C  
ANISOU 3425  CG  PHE A 450    16488  18704  23189  -2434  -1225  -2889       C  
ATOM   3426  CD1 PHE A 450     610.781 -18.063 210.039  1.00155.96           C  
ANISOU 3426  CD1 PHE A 450    16698  19031  23530  -2506  -1501  -3231       C  
ATOM   3427  CD2 PHE A 450     610.739 -19.755 208.361  1.00152.65           C  
ANISOU 3427  CD2 PHE A 450    16187  18781  23034  -2321  -1237  -2752       C  
ATOM   3428  CE1 PHE A 450     611.870 -18.679 210.640  1.00157.19           C  
ANISOU 3428  CE1 PHE A 450    16599  19430  23697  -2459  -1804  -3418       C  
ATOM   3429  CE2 PHE A 450     611.827 -20.379 208.954  1.00153.90           C  
ANISOU 3429  CE2 PHE A 450    16086  19165  23225  -2264  -1527  -2938       C  
ATOM   3430  CZ  PHE A 450     612.392 -19.842 210.097  1.00156.17           C  
ANISOU 3430  CZ  PHE A 450    16290  19494  23554  -2330  -1820  -3264       C  
ATOM   3431  N   LYS A 451     605.807 -17.117 207.986  1.00103.96           N  
ANISOU 3431  N   LYS A 451    11188  11776  16536  -2272   -560  -2336       N  
ATOM   3432  CA  LYS A 451     604.990 -16.212 207.181  1.00102.74           C  
ANISOU 3432  CA  LYS A 451    11180  11332  16523  -2340   -305  -2172       C  
ATOM   3433  C   LYS A 451     603.575 -15.956 207.729  1.00102.96           C  
ANISOU 3433  C   LYS A 451    11505  11268  16346  -2185   -279  -2167       C  
ATOM   3434  O   LYS A 451     603.040 -14.859 207.548  1.00103.07           O  
ANISOU 3434  O   LYS A 451    11629  11001  16533  -2257   -156  -2180       O  
ATOM   3435  CB  LYS A 451     604.912 -16.740 205.743  1.00100.32           C  
ANISOU 3435  CB  LYS A 451    10832  11042  16242  -2331    -83  -1835       C  
ATOM   3436  CG  LYS A 451     606.274 -16.811 205.048  1.00100.16           C  
ANISOU 3436  CG  LYS A 451    10510  11079  16469  -2512    -38  -1838       C  
ATOM   3437  CD  LYS A 451     606.373 -15.854 203.862  1.00 99.66           C  
ANISOU 3437  CD  LYS A 451    10426  10758  16682  -2718    234  -1666       C  
ATOM   3438  CE  LYS A 451     607.828 -15.615 203.460  1.00100.66           C  
ANISOU 3438  CE  LYS A 451    10228  10908  17111  -2959    275  -1761       C  
ATOM   3439  NZ  LYS A 451     608.536 -16.885 203.139  1.00100.54           N  
ANISOU 3439  NZ  LYS A 451    10001  11204  16995  -2871    236  -1722       N  
ATOM   3440  N   VAL A 452     602.978 -16.943 208.400  1.00 80.41           N  
ANISOU 3440  N   VAL A 452     8773   8637  13143  -1977   -386  -2152       N  
ATOM   3441  CA  VAL A 452     601.639 -16.765 208.979  1.00 80.71           C  
ANISOU 3441  CA  VAL A 452     9068   8620  12978  -1833   -345  -2166       C  
ATOM   3442  C   VAL A 452     601.773 -16.375 210.454  1.00 83.08           C  
ANISOU 3442  C   VAL A 452     9427   8975  13165  -1831   -546  -2515       C  
ATOM   3443  O   VAL A 452     602.548 -16.970 211.205  1.00 84.37           O  
ANISOU 3443  O   VAL A 452     9505   9363  13189  -1816   -767  -2658       O  
ATOM   3444  CB  VAL A 452     600.697 -18.051 208.823  1.00 79.69           C  
ANISOU 3444  CB  VAL A 452     9069   8687  12521  -1615   -297  -1924       C  
ATOM   3445  CG1 VAL A 452     600.897 -18.778 207.470  1.00 77.39           C  
ANISOU 3445  CG1 VAL A 452     8675   8440  12288  -1610   -170  -1624       C  
ATOM   3446  CG2 VAL A 452     600.818 -19.038 209.991  1.00 81.31           C  
ANISOU 3446  CG2 VAL A 452     9323   9170  12401  -1489   -507  -2035       C  
ATOM   3447  N   PRO A 453     601.035 -15.337 210.862  1.00 88.92           N  
ANISOU 3447  N   PRO A 453    10312   9504  13970  -1842   -478  -2665       N  
ATOM   3448  CA  PRO A 453     601.126 -14.747 212.199  1.00 91.16           C  
ANISOU 3448  CA  PRO A 453    10662   9799  14174  -1862   -641  -3038       C  
ATOM   3449  C   PRO A 453     600.015 -15.241 213.097  1.00 92.00           C  
ANISOU 3449  C   PRO A 453    10994  10066  13897  -1664   -644  -3074       C  
ATOM   3450  O   PRO A 453     599.097 -15.875 212.593  1.00 90.77           O  
ANISOU 3450  O   PRO A 453    10932   9953  13606  -1530   -496  -2810       O  
ATOM   3451  CB  PRO A 453     600.971 -13.260 211.915  1.00 91.39           C  
ANISOU 3451  CB  PRO A 453    10706   9452  14564  -2001   -521  -3164       C  
ATOM   3452  CG  PRO A 453     599.995 -13.229 210.762  1.00 89.46           C  
ANISOU 3452  CG  PRO A 453    10549   9041  14402  -1924   -271  -2824       C  
ATOM   3453  CD  PRO A 453     600.174 -14.533 209.980  1.00 87.56           C  
ANISOU 3453  CD  PRO A 453    10230   9035  14003  -1852   -245  -2504       C  
ATOM   3454  N   GLU A 454     600.084 -14.962 214.392  1.00139.80           N  
ANISOU 3454  N   GLU A 454    17131  16215  19771  -1653   -802  -3400       N  
ATOM   3455  CA  GLU A 454     599.020 -15.393 215.292  1.00140.75           C  
ANISOU 3455  CA  GLU A 454    17473  16500  19507  -1480   -775  -3444       C  
ATOM   3456  C   GLU A 454     597.775 -14.545 215.101  1.00140.16           C  
ANISOU 3456  C   GLU A 454    17529  16180  19545  -1427   -542  -3464       C  
ATOM   3457  O   GLU A 454     597.864 -13.405 214.657  1.00139.87           O  
ANISOU 3457  O   GLU A 454    17442  15835  19866  -1534   -469  -3558       O  
ATOM   3458  CB  GLU A 454     599.466 -15.327 216.748  1.00143.24           C  
ANISOU 3458  CB  GLU A 454    17855  17010  19558  -1483  -1010  -3795       C  
ATOM   3459  CG  GLU A 454     599.121 -16.580 217.524  1.00144.11           C  
ANISOU 3459  CG  GLU A 454    18112  17463  19181  -1323  -1093  -3694       C  
ATOM   3460  CD  GLU A 454     599.984 -17.748 217.109  1.00143.25           C  
ANISOU 3460  CD  GLU A 454    17870  17540  19019  -1303  -1241  -3455       C  
ATOM   3461  OE1 GLU A 454     599.537 -18.907 217.251  1.00142.95           O  
ANISOU 3461  OE1 GLU A 454    17940  17700  18675  -1165  -1229  -3229       O  
ATOM   3462  OE2 GLU A 454     601.119 -17.502 216.642  1.00142.92           O  
ANISOU 3462  OE2 GLU A 454    17607  17436  19261  -1430  -1361  -3501       O  
ATOM   3463  N   THR A 455     596.615 -15.108 215.440  1.00 89.57           N  
ANISOU 3463  N   THR A 455    11282   9902  12846  -1261   -425  -3373       N  
ATOM   3464  CA  THR A 455     595.336 -14.418 215.270  1.00 89.00           C  
ANISOU 3464  CA  THR A 455    11314   9629  12873  -1177   -202  -3387       C  
ATOM   3465  C   THR A 455     594.349 -14.742 216.406  1.00 90.23           C  
ANISOU 3465  C   THR A 455    11651   9986  12647  -1037   -145  -3534       C  
ATOM   3466  O   THR A 455     594.178 -13.969 217.360  1.00 91.78           O  
ANISOU 3466  O   THR A 455    11934  10149  12789  -1041   -163  -3883       O  
ATOM   3467  CB  THR A 455     594.697 -14.782 213.909  1.00 86.72           C  
ANISOU 3467  CB  THR A 455    10980   9232  12736  -1116    -22  -2998       C  
ATOM   3468  OG1 THR A 455     594.808 -16.196 213.694  1.00 86.08           O  
ANISOU 3468  OG1 THR A 455    10883   9423  12402  -1057    -60  -2738       O  
ATOM   3469  CG2 THR A 455     595.396 -14.060 212.762  1.00 85.49           C  
ANISOU 3469  CG2 THR A 455    10686   8798  12996  -1256     -4  -2887       C  
TER    3470      THR A 455                                                      
HETATM 3471  C1  BNG A 601     587.073 -31.390 206.254  1.00 83.63           C  
ANISOU 3471  C1  BNG A 601    10540  10249  10986   -308    804    216       C  
HETATM 3472  C2  BNG A 601     587.764 -31.239 204.908  1.00 81.10           C  
ANISOU 3472  C2  BNG A 601    10110   9877  10830   -308    741    267       C  
HETATM 3473  C3  BNG A 601     587.255 -32.359 204.016  1.00 77.66           C  
ANISOU 3473  C3  BNG A 601     9631   9457  10420   -296    769    386       C  
HETATM 3474  C4  BNG A 601     587.587 -33.700 204.667  1.00 78.45           C  
ANISOU 3474  C4  BNG A 601     9810   9604  10394   -297    717    444       C  
HETATM 3475  C5  BNG A 601     586.983 -33.768 206.072  1.00 80.79           C  
ANISOU 3475  C5  BNG A 601    10230   9942  10524   -310    778    417       C  
HETATM 3476  C6  BNG A 601     587.356 -35.028 206.840  1.00 82.18           C  
ANISOU 3476  C6  BNG A 601    10523  10150  10551   -310    716    503       C  
HETATM 3477  C1' BNG A 601     586.529 -30.388 208.279  1.00 89.34           C  
ANISOU 3477  C1' BNG A 601    11413  11029  11506   -315    887     14       C  
HETATM 3478  C2' BNG A 601     587.218 -29.829 209.512  1.00 93.53           C  
ANISOU 3478  C2' BNG A 601    12046  11606  11885   -328    813   -129       C  
HETATM 3479  C3' BNG A 601     586.279 -28.917 210.282  1.00 94.18           C  
ANISOU 3479  C3' BNG A 601    12169  11693  11921   -319    954   -287       C  
HETATM 3480  C4' BNG A 601     586.171 -27.548 209.624  1.00 93.87           C  
ANISOU 3480  C4' BNG A 601    12028  11515  12126   -300    975   -396       C  
HETATM 3481  C5' BNG A 601     585.597 -26.579 210.644  1.00 95.73           C  
ANISOU 3481  C5' BNG A 601    12321  11750  12301   -283   1072   -609       C  
HETATM 3482  C6' BNG A 601     585.601 -25.137 210.162  1.00 95.47           C  
ANISOU 3482  C6' BNG A 601    12212  11543  12520   -261   1074   -737       C  
HETATM 3483  C7' BNG A 601     585.643 -24.250 211.399  1.00 97.23           C  
ANISOU 3483  C7' BNG A 601    12523  11774  12645   -262   1095   -997       C  
HETATM 3484  C8' BNG A 601     585.059 -22.874 211.135  1.00 97.03           C  
ANISOU 3484  C8' BNG A 601    12435  11566  12868   -211   1174  -1148       C  
HETATM 3485  C9' BNG A 601     585.279 -22.000 212.349  1.00 98.67           C  
ANISOU 3485  C9' BNG A 601    12734  11772  12984   -221   1174  -1438       C  
HETATM 3486  O1  BNG A 601     587.399 -30.331 207.149  1.00 87.70           O  
ANISOU 3486  O1  BNG A 601    11106  10759  11459   -317    785     72       O  
HETATM 3487  O2  BNG A 601     587.469 -29.960 204.340  1.00 80.85           O  
ANISOU 3487  O2  BNG A 601    10018   9761  10939   -305    787    220       O  
HETATM 3488  O3  BNG A 601     587.828 -32.269 202.710  1.00 75.74           O  
ANISOU 3488  O3  BNG A 601     9294   9188  10295   -294    729    429       O  
HETATM 3489  O4  BNG A 601     587.074 -34.747 203.842  1.00 75.77           O  
ANISOU 3489  O4  BNG A 601     9431   9256  10103   -294    748    532       O  
HETATM 3490  O5  BNG A 601     587.425 -32.648 206.835  1.00 84.10           O  
ANISOU 3490  O5  BNG A 601    10685  10371  10897   -312    747    294       O  
HETATM 3491  O6  BNG A 601     587.085 -34.821 208.228  1.00 85.64           O  
ANISOU 3491  O6  BNG A 601    11098  10648  10792   -325    754    465       O  
CONECT 3471 3472 3486 3490                                                      
CONECT 3472 3471 3473 3487                                                      
CONECT 3473 3472 3474 3488                                                      
CONECT 3474 3473 3475 3489                                                      
CONECT 3475 3474 3476 3490                                                      
CONECT 3476 3475 3491                                                           
CONECT 3477 3478 3486                                                           
CONECT 3478 3477 3479                                                           
CONECT 3479 3478 3480                                                           
CONECT 3480 3479 3481                                                           
CONECT 3481 3480 3482                                                           
CONECT 3482 3481 3483                                                           
CONECT 3483 3482 3484                                                           
CONECT 3484 3483 3485                                                           
CONECT 3485 3484                                                                
CONECT 3486 3471 3477                                                           
CONECT 3487 3472                                                                
CONECT 3488 3473                                                                
CONECT 3489 3474                                                                
CONECT 3490 3471 3475                                                           
CONECT 3491 3476                                                                
MASTER      350    0    1   28    0    0    2    6 3490    1   21   39          
END                                                                             


A second structure was input as follows:


HEADER    TRANSPORT PROTEIN                       30-OCT-08   3F3A              
TITLE     CRYSTAL STRUCTURE OF LEUT BOUND TO L-TRYPTOPHAN AND SODIUM            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSPORTER;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LEUCINE TRANSPORTER;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE   3 ORGANISM_TAXID: 63363;                                               
SOURCE   4 STRAIN: VF5;                                                         
SOURCE   5 GENE: SNF, AQ_2077;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET16B                                    
KEYWDS    SLC6, NSS, TRANSMEMBRANE, SODIUM-COUPLED, TRANSPORTER,                
KEYWDS   2 SYMPORT, TRANSPORT PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.K.SINGH,C.L.PISCITELLI,A.YAMASHITA,E.GOUAUX                         
REVDAT   2   10-MAR-09 3F3A    1       JRNL                                     
REVDAT   1   23-DEC-08 3F3A    0                                                
JRNL        AUTH   S.K.SINGH,C.L.PISCITELLI,A.YAMASHITA,E.GOUAUX                
JRNL        TITL   A COMPETITIVE INHIBITOR TRAPS LEUT IN AN                     
JRNL        TITL 2 OPEN-TO-OUT CONFORMATION.                                    
JRNL        REF    SCIENCE                       V. 322  1655 2008              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   19074341                                                     
JRNL        DOI    10.1126/SCIENCE.1166777                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40334                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2040                            
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 48.2461 -  4.9308    0.96     2586   141  0.2099 0.2248        
REMARK   3     2  4.9308 -  3.9143    0.96     2544   140  0.1735 0.1629        
REMARK   3     3  3.9143 -  3.4196    0.98     2554   128  0.1744 0.2130        
REMARK   3     4  3.4196 -  3.1070    0.99     2605   139  0.1839 0.2287        
REMARK   3     5  3.1070 -  2.8844    0.99     2581   136  0.1867 0.2439        
REMARK   3     6  2.8844 -  2.7143    0.98     2580   123  0.1832 0.2408        
REMARK   3     7  2.7143 -  2.5784    0.99     2554   147  0.1859 0.2121        
REMARK   3     8  2.5784 -  2.4662    0.99     2550   143  0.1847 0.2418        
REMARK   3     9  2.4662 -  2.3712    0.98     2551   138  0.1934 0.2464        
REMARK   3    10  2.3712 -  2.2894    0.99     2563   141  0.2016 0.2628        
REMARK   3    11  2.2894 -  2.2178    0.99     2597   124  0.2166 0.2664        
REMARK   3    12  2.2178 -  2.1544    0.99     2563   140  0.2378 0.2823        
REMARK   3    13  2.1544 -  2.0977    0.98     2567   135  0.2585 0.3094        
REMARK   3    14  2.0977 -  2.0465    0.97     2459   148  0.2854 0.3304        
REMARK   3    15  2.0465 -  2.0000    0.91     2440   117  0.2945 0.3295        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 50.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.79                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.97                          
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      :  0.008           NULL                                  
REMARK   3   ANGLE     :  1.049           NULL                                  
REMARK   3   CHIRALITY :  0.069           NULL                                  
REMARK   3   PLANARITY :  0.005           NULL                                  
REMARK   3   DIHEDRAL  : 18.628           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3F3A COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050092.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41152                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2A65                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 0.4M NACL, 17-22% PEG-       
REMARK 280  MME 550, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       44.28300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.60900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.28300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.60900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      -83.78697            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -82.13508            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 612  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PRO A   132                                                      
REMARK 465     ASN A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     SER A   512                                                      
REMARK 465     ALA A   513                                                      
REMARK 465     GLY A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     LEU A   516                                                      
REMARK 465     VAL A   517                                                      
REMARK 465     PRO A   518                                                      
REMARK 465     ARG A   519                                                      
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     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     GLU A 470    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 471    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    VAL A  54      -51.00   -124.48                                   
REMARK 500    TRP A  85       92.64   -162.47                                   
REMARK 500    PRO A 160       44.38    -81.04                                   
REMARK 500    ILE A 297      -77.29    -99.06                                   
REMARK 500    ILE A 325      -56.32   -121.73                                   
REMARK 500    LYS A 398       -0.64     76.37                                   
REMARK 500    THR A 409      -75.86   -127.97                                   
REMARK 500    TYR A 454      -52.20   -122.99                                   
REMARK 500    VAL A 465      -76.55    -80.32                                   
REMARK 500    TYR A 471      -54.44   -127.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 601                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 602                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 603                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 604                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 701                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 702                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 704                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 705                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 706                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C14 A 707                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 708                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 751                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 752                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2A65   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH L-LEUCINE AND SODIUM                     
REMARK 900 RELATED ID: 2QEI   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH L-ALANINE, SODIUM, AND                   
REMARK 900 CLOMIPRAMINE                                                         
REMARK 900 RELATED ID: 3F3C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LEUT BOUND TO 4-FLUORO-L-PHENYLALANINE          
REMARK 900 AND SODIUM                                                           
REMARK 900 RELATED ID: 3F3D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LEUT BOUND TO L-METHIONINE AND SODIUM           
REMARK 900 RELATED ID: 3F3E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LEUT BOUND TO L-LEUCINE(30 MM) AND              
REMARK 900 SODIUM                                                               
REMARK 900 RELATED ID: 3F48   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LEUT BOUND TO L-ALANINE AND SODIUM              
REMARK 900 RELATED ID: 3F4I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LEUT BOUND TO L-SELENOMETHIONINE AND            
REMARK 900 SODIUM                                                               
REMARK 900 RELATED ID: 3F4J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LEUT BOUND TO GLYCINE AND SODIUM                
DBREF  3F3A A    1   513  UNP    O67854   O67854_AQUAE     1    513             
SEQADV 3F3A GLY A  514  UNP  O67854              EXPRESSION TAG                 
SEQADV 3F3A THR A  515  UNP  O67854              EXPRESSION TAG                 
SEQADV 3F3A LEU A  516  UNP  O67854              EXPRESSION TAG                 
SEQADV 3F3A VAL A  517  UNP  O67854              EXPRESSION TAG                 
SEQADV 3F3A PRO A  518  UNP  O67854              EXPRESSION TAG                 
SEQADV 3F3A ARG A  519  UNP  O67854              EXPRESSION TAG                 
SEQRES   1 A  519  MET GLU VAL LYS ARG GLU HIS TRP ALA THR ARG LEU GLY          
SEQRES   2 A  519  LEU ILE LEU ALA MET ALA GLY ASN ALA VAL GLY LEU GLY          
SEQRES   3 A  519  ASN PHE LEU ARG PHE PRO VAL GLN ALA ALA GLU ASN GLY          
SEQRES   4 A  519  GLY GLY ALA PHE MET ILE PRO TYR ILE ILE ALA PHE LEU          
SEQRES   5 A  519  LEU VAL GLY ILE PRO LEU MET TRP ILE GLU TRP ALA MET          
SEQRES   6 A  519  GLY ARG TYR GLY GLY ALA GLN GLY HIS GLY THR THR PRO          
SEQRES   7 A  519  ALA ILE PHE TYR LEU LEU TRP ARG ASN ARG PHE ALA LYS          
SEQRES   8 A  519  ILE LEU GLY VAL PHE GLY LEU TRP ILE PRO LEU VAL VAL          
SEQRES   9 A  519  ALA ILE TYR TYR VAL TYR ILE GLU SER TRP THR LEU GLY          
SEQRES  10 A  519  PHE ALA ILE LYS PHE LEU VAL GLY LEU VAL PRO GLU PRO          
SEQRES  11 A  519  PRO PRO ASN ALA THR ASP PRO ASP SER ILE LEU ARG PRO          
SEQRES  12 A  519  PHE LYS GLU PHE LEU TYR SER TYR ILE GLY VAL PRO LYS          
SEQRES  13 A  519  GLY ASP GLU PRO ILE LEU LYS PRO SER LEU PHE ALA TYR          
SEQRES  14 A  519  ILE VAL PHE LEU ILE THR MET PHE ILE ASN VAL SER ILE          
SEQRES  15 A  519  LEU ILE ARG GLY ILE SER LYS GLY ILE GLU ARG PHE ALA          
SEQRES  16 A  519  LYS ILE ALA MET PRO THR LEU PHE ILE LEU ALA VAL PHE          
SEQRES  17 A  519  LEU VAL ILE ARG VAL PHE LEU LEU GLU THR PRO ASN GLY          
SEQRES  18 A  519  THR ALA ALA ASP GLY LEU ASN PHE LEU TRP THR PRO ASP          
SEQRES  19 A  519  PHE GLU LYS LEU LYS ASP PRO GLY VAL TRP ILE ALA ALA          
SEQRES  20 A  519  VAL GLY GLN ILE PHE PHE THR LEU SER LEU GLY PHE GLY          
SEQRES  21 A  519  ALA ILE ILE THR TYR ALA SER TYR VAL ARG LYS ASP GLN          
SEQRES  22 A  519  ASP ILE VAL LEU SER GLY LEU THR ALA ALA THR LEU ASN          
SEQRES  23 A  519  GLU LYS ALA GLU VAL ILE LEU GLY GLY SER ILE SER ILE          
SEQRES  24 A  519  PRO ALA ALA VAL ALA PHE PHE GLY VAL ALA ASN ALA VAL          
SEQRES  25 A  519  ALA ILE ALA LYS ALA GLY ALA PHE ASN LEU GLY PHE ILE          
SEQRES  26 A  519  THR LEU PRO ALA ILE PHE SER GLN THR ALA GLY GLY THR          
SEQRES  27 A  519  PHE LEU GLY PHE LEU TRP PHE PHE LEU LEU PHE PHE ALA          
SEQRES  28 A  519  GLY LEU THR SER SER ILE ALA ILE MET GLN PRO MET ILE          
SEQRES  29 A  519  ALA PHE LEU GLU ASP GLU LEU LYS LEU SER ARG LYS HIS          
SEQRES  30 A  519  ALA VAL LEU TRP THR ALA ALA ILE VAL PHE PHE SER ALA          
SEQRES  31 A  519  HIS LEU VAL MET PHE LEU ASN LYS SER LEU ASP GLU MET          
SEQRES  32 A  519  ASP PHE TRP ALA GLY THR ILE GLY VAL VAL PHE PHE GLY          
SEQRES  33 A  519  LEU THR GLU LEU ILE ILE PHE PHE TRP ILE PHE GLY ALA          
SEQRES  34 A  519  ASP LYS ALA TRP GLU GLU ILE ASN ARG GLY GLY ILE ILE          
SEQRES  35 A  519  LYS VAL PRO ARG ILE TYR TYR TYR VAL MET ARG TYR ILE          
SEQRES  36 A  519  THR PRO ALA PHE LEU ALA VAL LEU LEU VAL VAL TRP ALA          
SEQRES  37 A  519  ARG GLU TYR ILE PRO LYS ILE MET GLU GLU THR HIS TRP          
SEQRES  38 A  519  THR VAL TRP ILE THR ARG PHE TYR ILE ILE GLY LEU PHE          
SEQRES  39 A  519  LEU PHE LEU THR PHE LEU VAL PHE LEU ALA GLU ARG ARG          
SEQRES  40 A  519  ARG ASN HIS GLU SER ALA GLY THR LEU VAL PRO ARG              
HET    TRP  A 601      15                                                       
HET    TRP  A 602      15                                                       
HET    TRP  A 603      15                                                       
HET    TRP  A 604      15                                                       
HET    BOG  A 701      20                                                       
HET    BOG  A 702      20                                                       
HET    BOG  A 703      20                                                       
HET    BOG  A 704      20                                                       
HET    BOG  A 705      20                                                       
HET    BOG  A 706      20                                                       
HET    C14  A 707      14                                                       
HET    BOG  A 708      20                                                       
HET     NA  A 751       1                                                       
HET     NA  A 752       1                                                       
HETNAM     TRP TRYPTOPHAN                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     C14 TETRADECANE                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   2  TRP    4(C11 H12 N2 O2)                                             
FORMUL   3  BOG    7(C14 H28 O6)                                                
FORMUL   9  C14    C14 H30                                                      
FORMUL  11   NA    2(NA 1+)                                                     
FORMUL  13  HOH   *101(H2 O)                                                    
HELIX    1   1 THR A   10  VAL A   23  1                                  14    
HELIX    2   2 GLY A   24  LEU A   29  1                                   6    
HELIX    3   3 LEU A   29  ASN A   38  1                                  10    
HELIX    4   4 GLY A   39  ALA A   42  5                                   4    
HELIX    5   5 PHE A   43  VAL A   54  1                                  12    
HELIX    6   6 VAL A   54  GLN A   72  1                                  19    
HELIX    7   7 THR A   76  TRP A   85  1                                  10    
HELIX    8   8 ASN A   87  GLY A  125  1                                  39    
HELIX    9   9 ASP A  136  GLY A  153  1                                  18    
HELIX   10  10 SER A  165  ILE A  184  1                                  20    
HELIX   11  11 ARG A  185  GLY A  190  1                                   6    
HELIX   12  12 GLY A  190  LEU A  216  1                                  27    
HELIX   13  13 ALA A  223  THR A  232  1                                  10    
HELIX   14  14 ASP A  234  LYS A  239  5                                   6    
HELIX   15  15 ASP A  240  LEU A  255  1                                  16    
HELIX   16  16 GLY A  260  SER A  267  1                                   8    
HELIX   17  17 ILE A  275  ILE A  292  1                                  18    
HELIX   18  18 ILE A  297  GLY A  307  1                                  11    
HELIX   19  19 ASN A  310  ALA A  317  1                                   8    
HELIX   20  20 GLY A  318  ILE A  325  1                                   8    
HELIX   21  21 ILE A  325  SER A  332  1                                   8    
HELIX   22  22 GLY A  336  LYS A  372  1                                  37    
HELIX   23  23 SER A  374  LEU A  396  1                                  23    
HELIX   24  24 LYS A  398  ALA A  407  1                                  10    
HELIX   25  25 THR A  409  TRP A  425  1                                  17    
HELIX   26  26 GLY A  428  ARG A  438  1                                  11    
HELIX   27  27 ILE A  447  TYR A  454  1                                   8    
HELIX   28  28 TYR A  454  GLU A  470  1                                  17    
HELIX   29  29 TYR A  471  GLU A  478  1                                   8    
HELIX   30  30 THR A  482  GLU A  511  1                                  30    
SHEET    1   A 2 GLU A 217  THR A 218  0                                        
SHEET    2   A 2 GLY A 221  THR A 222 -1  O  GLY A 221   N  THR A 218           
CISPEP   1 PRO A  130    PRO A  131          0         1.87                     
SITE     1 AC1 16 ALA A  22  GLY A  24  LEU A  25  GLY A  26                    
SITE     2 AC1 16 ASN A  27  TYR A 108  PHE A 253  THR A 254                    
SITE     3 AC1 16 SER A 256  PHE A 259  SER A 355  HOH A 539                    
SITE     4 AC1 16 HOH A 544  HOH A 572  C14 A 707   NA A 752                    
SITE     1 AC2  9 ARG A  30  GLY A 249  PHE A 253  PHE A 259                    
SITE     2 AC2  9 ASP A 404  GLY A 408  THR A 409  HOH A 593                    
SITE     3 AC2  9 BOG A 708                                                     
SITE     1 AC3  7 ARG A  11  ASP A 272  GLN A 273  ASP A 274                    
SITE     2 AC3  7 GLY A 439  HOH A 522  BOG A 706                               
SITE     1 AC4  6 PHE A 306  ASN A 310  ALA A 313  ILE A 314                    
SITE     2 AC4  6 ALA A 317  ASN A 321                                          
SITE     1 AC5  7 LYS A 121  LEU A 126  PHE A 147  PHE A 167                    
SITE     2 AC5  7 LYS A 443  HOH A 580  BOG A 702                               
SITE     1 AC6  6 LEU A 166  PHE A 167  GLY A 439  LYS A 443                    
SITE     2 AC6  6 HOH A 526  BOG A 701                                          
SITE     1 AC7  7 LYS A 163  PRO A 164  LEU A 166  HIS A 391                    
SITE     2 AC7  7 PHE A 395  HOH A 587  BOG A 704                               
SITE     1 AC8  8 LYS A 163  LYS A 431  MET A 476  GLU A 477                    
SITE     2 AC8  8 TRP A 484  PHE A 488  BOG A 703  BOG A 705                    
SITE     1 AC9  9 ILE A 161  LYS A 431  MET A 476  GLU A 477                    
SITE     2 AC9  9 THR A 479  VAL A 483  TRP A 484  ARG A 487                    
SITE     3 AC9  9 BOG A 704                                                     
SITE     1 BC1 12 ARG A  11  ARG A 212  LEU A 215  LEU A 216                    
SITE     2 BC1 12 GLU A 217  ALA A 335  GLY A 336  LEU A 340                    
SITE     3 BC1 12 ILE A 441  HOH A 530  TRP A 603  HOH A 606                    
SITE     1 BC2  6 TYR A 108  PHE A 253  PHE A 320  ASP A 404                    
SITE     2 BC2  6 TRP A 601  HOH A 616                                          
SITE     1 BC3 10 ARG A  30  PHE A 405  THR A 409  ILE A 410                    
SITE     2 BC3 10 VAL A 413  LEU A 463  LEU A 464  TRP A 467                    
SITE     3 BC3 10 HOH A 573  TRP A 602                                          
SITE     1 BC4  5 GLY A  20  VAL A  23  ALA A 351  THR A 354                    
SITE     2 BC4  5 SER A 355                                                     
SITE     1 BC5  5 ALA A  22  ASN A  27  THR A 254  ASN A 286                    
SITE     2 BC5  5 TRP A 601                                                     
CRYST1   88.566   85.218   82.274  90.00  93.33  90.00 C 1 2 1       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      0.011291  0.000000  0.000657        0.00000                         
SCALE2      0.000000  0.011735  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012175        0.00000                         
ATOM      1  N   ARG A   5     -33.078  22.537 -23.904  1.00 58.90           N  
ATOM      2  CA  ARG A   5     -32.892  21.102 -23.732  1.00 52.46           C  
ATOM      3  C   ARG A   5     -33.026  20.649 -22.273  1.00 41.88           C  
ATOM      4  O   ARG A   5     -32.637  21.366 -21.345  1.00 41.80           O  
ATOM      5  CB  ARG A   5     -31.527  20.663 -24.287  1.00 47.42           C  
ATOM      6  CG  ARG A   5     -31.321  19.149 -24.310  1.00 44.88           C  
ATOM      7  CD  ARG A   5     -30.009  18.747 -24.992  1.00 48.16           C  
ATOM      8  NE  ARG A   5     -29.995  17.326 -25.366  1.00 36.26           N  
ATOM      9  CZ  ARG A   5     -30.669  16.831 -26.401  1.00 34.17           C  
ATOM     10  NH1 ARG A   5     -30.614  15.534 -26.687  1.00 30.31           N  
ATOM     11  NH2 ARG A   5     -31.414  17.637 -27.148  1.00 32.39           N  
ATOM     12  N   GLU A   6     -33.573  19.455 -22.073  1.00 38.01           N  
ATOM     13  CA  GLU A   6     -33.615  18.846 -20.749  1.00 35.59           C  
ATOM     14  C   GLU A   6     -32.199  18.657 -20.218  1.00 36.35           C  
ATOM     15  O   GLU A   6     -31.248  18.498 -20.986  1.00 34.83           O  
ATOM     16  CB  GLU A   6     -34.325  17.496 -20.800  1.00 41.14           C  
ATOM     17  CG  GLU A   6     -35.837  17.568 -20.972  1.00 49.18           C  
ATOM     18  CD  GLU A   6     -36.477  16.190 -21.212  1.00 61.60           C  
ATOM     19  OE1 GLU A   6     -36.972  15.584 -20.235  1.00 44.95           O  
ATOM     20  OE2 GLU A   6     -36.481  15.722 -22.380  1.00 51.98           O  
ATOM     21  N   HIS A   7     -32.059  18.677 -18.900  1.00 33.25           N  
ATOM     22  CA  HIS A   7     -30.772  18.409 -18.267  1.00 35.98           C  
ATOM     23  C   HIS A   7     -30.976  17.627 -16.984  1.00 32.62           C  
ATOM     24  O   HIS A   7     -32.024  17.728 -16.357  1.00 36.83           O  
ATOM     25  CB  HIS A   7     -30.027  19.718 -17.970  1.00 36.65           C  
ATOM     26  CG  HIS A   7     -29.546  20.418 -19.200  1.00 36.40           C  
ATOM     27  ND1 HIS A   7     -30.038  21.640 -19.606  1.00 42.69           N  
ATOM     28  CD2 HIS A   7     -28.643  20.048 -20.136  1.00 32.92           C  
ATOM     29  CE1 HIS A   7     -29.454  21.999 -20.732  1.00 33.85           C  
ATOM     30  NE2 HIS A   7     -28.594  21.047 -21.076  1.00 35.24           N  
ATOM     31  N   TRP A   8     -29.980  16.836 -16.606  1.00 29.85           N  
ATOM     32  CA  TRP A   8     -29.969  16.199 -15.294  1.00 32.51           C  
ATOM     33  C   TRP A   8     -29.996  17.281 -14.210  1.00 38.59           C  
ATOM     34  O   TRP A   8     -29.380  18.330 -14.373  1.00 34.14           O  
ATOM     35  CB  TRP A   8     -28.718  15.332 -15.160  1.00 31.96           C  
ATOM     36  CG  TRP A   8     -28.612  14.306 -16.259  1.00 35.00           C  
ATOM     37  CD1 TRP A   8     -27.827  14.367 -17.375  1.00 28.49           C  
ATOM     38  CD2 TRP A   8     -29.338  13.080 -16.344  1.00 26.25           C  
ATOM     39  NE1 TRP A   8     -28.017  13.246 -18.149  1.00 28.01           N  
ATOM     40  CE2 TRP A   8     -28.936  12.437 -17.531  1.00 26.92           C  
ATOM     41  CE3 TRP A   8     -30.285  12.461 -15.522  1.00 27.25           C  
ATOM     42  CZ2 TRP A   8     -29.458  11.206 -17.925  1.00 28.41           C  
ATOM     43  CZ3 TRP A   8     -30.782  11.238 -15.890  1.00 29.08           C  
ATOM     44  CH2 TRP A   8     -30.382  10.624 -17.095  1.00 33.79           C  
ATOM     45  N   ALA A   9     -30.716  17.029 -13.118  1.00 34.50           N  
ATOM     46  CA  ALA A   9     -30.845  18.011 -12.044  1.00 38.48           C  
ATOM     47  C   ALA A   9     -29.637  17.979 -11.116  1.00 37.69           C  
ATOM     48  O   ALA A   9     -29.140  19.021 -10.678  1.00 41.40           O  
ATOM     49  CB  ALA A   9     -32.119  17.762 -11.245  1.00 32.56           C  
ATOM     50  N   THR A  10     -29.170  16.775 -10.816  1.00 32.53           N  
ATOM     51  CA  THR A  10     -28.098  16.603  -9.857  1.00 37.21           C  
ATOM     52  C   THR A  10     -26.966  15.725 -10.383  1.00 47.04           C  
ATOM     53  O   THR A  10     -27.147  14.895 -11.290  1.00 38.41           O  
ATOM     54  CB  THR A  10     -28.623  16.032  -8.517  1.00 39.87           C  
ATOM     55  OG1 THR A  10     -29.040  14.669  -8.685  1.00 36.67           O  
ATOM     56  CG2 THR A  10     -29.797  16.854  -8.018  1.00 34.27           C  
ATOM     57  N   ARG A  11     -25.788  15.925  -9.807  1.00 40.00           N  
ATOM     58  CA  ARG A  11     -24.626  15.145 -10.169  1.00 35.82           C  
ATOM     59  C   ARG A  11     -24.924  13.719  -9.793  1.00 40.49           C  
ATOM     60  O   ARG A  11     -24.669  12.792 -10.559  1.00 35.25           O  
ATOM     61  CB  ARG A  11     -23.402  15.628  -9.399  1.00 31.39           C  
ATOM     62  CG  ARG A  11     -22.095  15.081  -9.923  1.00 35.58           C  
ATOM     63  CD  ARG A  11     -21.061  16.180  -9.939  1.00 50.01           C  
ATOM     64  NE  ARG A  11     -20.884  16.766 -11.255  1.00 57.03           N  
ATOM     65  CZ  ARG A  11     -20.359  17.965 -11.486  1.00 45.40           C  
ATOM     66  NH1 ARG A  11     -19.964  18.747 -10.484  1.00 41.75           N  
ATOM     67  NH2 ARG A  11     -20.238  18.384 -12.733  1.00 42.27           N  
ATOM     68  N   LEU A  12     -25.479  13.558  -8.599  1.00 34.90           N  
ATOM     69  CA  LEU A  12     -25.789  12.245  -8.063  1.00 37.07           C  
ATOM     70  C   LEU A  12     -26.805  11.526  -8.948  1.00 33.90           C  
ATOM     71  O   LEU A  12     -26.649  10.345  -9.250  1.00 32.21           O  
ATOM     72  CB  LEU A  12     -26.341  12.364  -6.640  1.00 32.83           C  
ATOM     73  CG  LEU A  12     -26.839  11.047  -6.048  1.00 40.04           C  
ATOM     74  CD1 LEU A  12     -25.697  10.028  -5.937  1.00 35.25           C  
ATOM     75  CD2 LEU A  12     -27.493  11.282  -4.679  1.00 40.53           C  
ATOM     76  N   GLY A  13     -27.856  12.235  -9.336  1.00 34.84           N  
ATOM     77  CA  GLY A  13     -28.873  11.658 -10.194  1.00 32.44           C  
ATOM     78  C   GLY A  13     -28.306  11.234 -11.541  1.00 30.71           C  
ATOM     79  O   GLY A  13     -28.600  10.147 -12.034  1.00 28.48           O  
ATOM     80  N   LEU A  14     -27.487  12.090 -12.139  1.00 29.16           N  
ATOM     81  CA  LEU A  14     -26.832  11.742 -13.396  1.00 28.09           C  
ATOM     82  C   LEU A  14     -26.081  10.443 -13.230  1.00 32.74           C  
ATOM     83  O   LEU A  14     -26.228   9.507 -14.027  1.00 28.69           O  
ATOM     84  CB  LEU A  14     -25.866  12.849 -13.819  1.00 34.85           C  
ATOM     85  CG  LEU A  14     -24.767  12.551 -14.843  1.00 36.61           C  
ATOM     86  CD1 LEU A  14     -25.362  12.129 -16.222  1.00 28.40           C  
ATOM     87  CD2 LEU A  14     -23.855  13.782 -15.003  1.00 27.72           C  
ATOM     88  N   ILE A  15     -25.299  10.367 -12.158  1.00 28.37           N  
ATOM     89  CA  ILE A  15     -24.395   9.249 -11.978  1.00 25.66           C  
ATOM     90  C   ILE A  15     -25.148   7.962 -11.687  1.00 31.82           C  
ATOM     91  O   ILE A  15     -24.748   6.895 -12.139  1.00 31.55           O  
ATOM     92  CB  ILE A  15     -23.382   9.516 -10.846  1.00 34.46           C  
ATOM     93  CG1 ILE A  15     -22.347  10.558 -11.295  1.00 34.09           C  
ATOM     94  CG2 ILE A  15     -22.720   8.224 -10.394  1.00 24.22           C  
ATOM     95  CD1 ILE A  15     -21.472  11.074 -10.152  1.00 31.26           C  
ATOM     96  N   LEU A  16     -26.227   8.064 -10.919  1.00 27.65           N  
ATOM     97  CA  LEU A  16     -27.027   6.895 -10.595  1.00 22.46           C  
ATOM     98  C   LEU A  16     -27.804   6.405 -11.828  1.00 25.38           C  
ATOM     99  O   LEU A  16     -28.008   5.210 -12.007  1.00 33.17           O  
ATOM    100  CB  LEU A  16     -27.980   7.190  -9.442  1.00 23.83           C  
ATOM    101  CG  LEU A  16     -27.266   7.440  -8.108  1.00 33.70           C  
ATOM    102  CD1 LEU A  16     -28.288   7.651  -6.989  1.00 31.98           C  
ATOM    103  CD2 LEU A  16     -26.315   6.282  -7.810  1.00 27.04           C  
ATOM    104  N   ALA A  17     -28.216   7.336 -12.676  1.00 30.89           N  
ATOM    105  CA  ALA A  17     -28.903   6.978 -13.940  1.00 29.31           C  
ATOM    106  C   ALA A  17     -27.970   6.260 -14.909  1.00 26.01           C  
ATOM    107  O   ALA A  17     -28.320   5.240 -15.525  1.00 28.92           O  
ATOM    108  CB  ALA A  17     -29.470   8.213 -14.577  1.00 26.14           C  
ATOM    109  N   MET A  18     -26.773   6.810 -15.051  1.00 30.22           N  
ATOM    110  CA  MET A  18     -25.734   6.211 -15.882  1.00 28.34           C  
ATOM    111  C   MET A  18     -25.281   4.872 -15.318  1.00 30.02           C  
ATOM    112  O   MET A  18     -25.028   3.926 -16.058  1.00 29.44           O  
ATOM    113  CB  MET A  18     -24.545   7.161 -15.975  1.00 27.37           C  
ATOM    114  CG  MET A  18     -24.755   8.295 -16.943  1.00 29.79           C  
ATOM    115  SD  MET A  18     -24.641   7.714 -18.649  1.00 30.86           S  
ATOM    116  CE  MET A  18     -24.359   9.285 -19.461  1.00 30.09           C  
ATOM    117  N   ALA A  19     -25.179   4.795 -13.998  1.00 27.03           N  
ATOM    118  CA  ALA A  19     -24.864   3.525 -13.348  1.00 30.51           C  
ATOM    119  C   ALA A  19     -26.025   2.553 -13.555  1.00 27.75           C  
ATOM    120  O   ALA A  19     -25.821   1.377 -13.800  1.00 24.96           O  
ATOM    121  CB  ALA A  19     -24.616   3.733 -11.842  1.00 26.87           C  
ATOM    122  N   GLY A  20     -27.247   3.055 -13.452  1.00 27.27           N  
ATOM    123  CA  GLY A  20     -28.408   2.224 -13.686  1.00 30.04           C  
ATOM    124  C   GLY A  20     -28.392   1.753 -15.138  1.00 33.47           C  
ATOM    125  O   GLY A  20     -28.724   0.612 -15.419  1.00 30.62           O  
ATOM    126  N   ASN A  21     -27.988   2.591 -16.079  1.00 31.25           N  
ATOM    127  CA  ASN A  21     -27.926   2.092 -17.457  1.00 29.45           C  
ATOM    128  C   ASN A  21     -27.019   0.855 -17.548  1.00 29.68           C  
ATOM    129  O   ASN A  21     -27.372  -0.152 -18.156  1.00 29.87           O  
ATOM    130  CB  ASN A  21     -27.460   3.173 -18.430  1.00 27.29           C  
ATOM    131  CG  ASN A  21     -27.225   2.621 -19.842  1.00 30.23           C  
ATOM    132  OD1 ASN A  21     -28.087   1.946 -20.406  1.00 32.72           O  
ATOM    133  ND2 ASN A  21     -26.048   2.890 -20.400  1.00 32.03           N  
ATOM    134  N   ALA A  22     -25.856   0.924 -16.914  1.00 30.90           N  
ATOM    135  CA  ALA A  22     -24.898  -0.180 -16.960  1.00 31.90           C  
ATOM    136  C   ALA A  22     -25.329  -1.414 -16.172  1.00 33.13           C  
ATOM    137  O   ALA A  22     -25.271  -2.520 -16.692  1.00 26.20           O  
ATOM    138  CB  ALA A  22     -23.522   0.283 -16.490  1.00 28.75           C  
ATOM    139  N   VAL A  23     -25.730  -1.236 -14.912  1.00 29.67           N  
ATOM    140  CA  VAL A  23     -26.077  -2.362 -14.056  1.00 21.92           C  
ATOM    141  C   VAL A  23     -27.333  -3.093 -14.541  1.00 31.41           C  
ATOM    142  O   VAL A  23     -28.439  -2.591 -14.402  1.00 27.15           O  
ATOM    143  CB  VAL A  23     -26.292  -1.892 -12.583  1.00 34.13           C  
ATOM    144  CG1 VAL A  23     -26.730  -3.042 -11.707  1.00 24.87           C  
ATOM    145  CG2 VAL A  23     -25.011  -1.284 -12.029  1.00 28.21           C  
ATOM    146  N   GLY A  24     -27.176  -4.275 -15.120  1.00 28.72           N  
ATOM    147  CA  GLY A  24     -28.332  -5.012 -15.610  1.00 30.05           C  
ATOM    148  C   GLY A  24     -28.274  -6.469 -15.192  1.00 34.14           C  
ATOM    149  O   GLY A  24     -27.563  -6.818 -14.263  1.00 27.51           O  
ATOM    150  N   LEU A  25     -29.003  -7.332 -15.897  1.00 32.18           N  
ATOM    151  CA  LEU A  25     -29.006  -8.745 -15.545  1.00 29.52           C  
ATOM    152  C   LEU A  25     -27.607  -9.344 -15.679  1.00 39.80           C  
ATOM    153  O   LEU A  25     -27.262 -10.285 -14.956  1.00 32.92           O  
ATOM    154  CB  LEU A  25     -30.011  -9.526 -16.411  1.00 28.19           C  
ATOM    155  CG  LEU A  25     -31.476  -9.357 -15.985  1.00 33.81           C  
ATOM    156  CD1 LEU A  25     -31.996  -7.955 -16.310  1.00 31.94           C  
ATOM    157  CD2 LEU A  25     -32.364 -10.429 -16.629  1.00 38.46           C  
ATOM    158  N   GLY A  26     -26.812  -8.799 -16.604  1.00 30.03           N  
ATOM    159  CA  GLY A  26     -25.454  -9.272 -16.820  1.00 28.38           C  
ATOM    160  C   GLY A  26     -24.587  -9.285 -15.557  1.00 32.21           C  
ATOM    161  O   GLY A  26     -23.774 -10.201 -15.340  1.00 31.22           O  
ATOM    162  N   ASN A  27     -24.747  -8.264 -14.723  1.00 30.17           N  
ATOM    163  CA  ASN A  27     -23.932  -8.155 -13.529  1.00 31.10           C  
ATOM    164  C   ASN A  27     -24.081  -9.395 -12.676  1.00 32.94           C  
ATOM    165  O   ASN A  27     -23.107  -9.902 -12.127  1.00 38.70           O  
ATOM    166  CB  ASN A  27     -24.348  -6.949 -12.689  1.00 32.67           C  
ATOM    167  CG  ASN A  27     -24.039  -5.652 -13.352  1.00 35.91           C  
ATOM    168  OD1 ASN A  27     -24.592  -5.340 -14.403  1.00 36.44           O  
ATOM    169  ND2 ASN A  27     -23.157  -4.865 -12.738  1.00 33.94           N  
ATOM    170  N   PHE A  28     -25.314  -9.879 -12.575  1.00 34.49           N  
ATOM    171  CA  PHE A  28     -25.657 -10.945 -11.640  1.00 29.54           C  
ATOM    172  C   PHE A  28     -25.690 -12.334 -12.263  1.00 40.98           C  
ATOM    173  O   PHE A  28     -25.709 -13.336 -11.541  1.00 36.84           O  
ATOM    174  CB  PHE A  28     -26.995 -10.621 -10.966  1.00 33.45           C  
ATOM    175  CG  PHE A  28     -27.002  -9.283 -10.282  1.00 33.85           C  
ATOM    176  CD1 PHE A  28     -27.639  -8.196 -10.857  1.00 30.31           C  
ATOM    177  CD2 PHE A  28     -26.341  -9.111  -9.077  1.00 33.21           C  
ATOM    178  CE1 PHE A  28     -27.622  -6.952 -10.241  1.00 33.87           C  
ATOM    179  CE2 PHE A  28     -26.320  -7.880  -8.457  1.00 31.92           C  
ATOM    180  CZ  PHE A  28     -26.964  -6.800  -9.033  1.00 38.13           C  
ATOM    181  N   LEU A  29     -25.691 -12.401 -13.596  1.00 36.38           N  
ATOM    182  CA  LEU A  29     -25.785 -13.689 -14.275  1.00 31.48           C  
ATOM    183  C   LEU A  29     -24.692 -13.936 -15.317  1.00 46.05           C  
ATOM    184  O   LEU A  29     -24.095 -15.020 -15.347  1.00 40.62           O  
ATOM    185  CB  LEU A  29     -27.162 -13.850 -14.917  1.00 36.66           C  
ATOM    186  CG  LEU A  29     -28.277 -13.996 -13.888  1.00 40.03           C  
ATOM    187  CD1 LEU A  29     -29.667 -13.913 -14.539  1.00 31.73           C  
ATOM    188  CD2 LEU A  29     -28.086 -15.300 -13.160  1.00 30.83           C  
ATOM    189  N   ARG A  30     -24.435 -12.952 -16.179  1.00 35.79           N  
ATOM    190  CA  ARG A  30     -23.452 -13.156 -17.243  1.00 39.97           C  
ATOM    191  C   ARG A  30     -22.009 -13.111 -16.727  1.00 38.23           C  
ATOM    192  O   ARG A  30     -21.212 -14.006 -17.009  1.00 37.40           O  
ATOM    193  CB  ARG A  30     -23.654 -12.184 -18.414  1.00 31.42           C  
ATOM    194  CG  ARG A  30     -22.898 -12.592 -19.691  1.00 35.87           C  
ATOM    195  CD  ARG A  30     -23.313 -11.730 -20.907  1.00 42.88           C  
ATOM    196  NE  ARG A  30     -22.921 -12.311 -22.201  1.00 50.42           N  
ATOM    197  CZ  ARG A  30     -21.679 -12.326 -22.688  1.00 44.69           C  
ATOM    198  NH1 ARG A  30     -20.673 -11.814 -21.987  1.00 37.19           N  
ATOM    199  NH2 ARG A  30     -21.434 -12.870 -23.873  1.00 36.49           N  
ATOM    200  N   PHE A  31     -21.662 -12.081 -15.972  1.00 34.61           N  
ATOM    201  CA  PHE A  31     -20.289 -11.992 -15.514  1.00 39.17           C  
ATOM    202  C   PHE A  31     -19.846 -13.257 -14.781  1.00 38.28           C  
ATOM    203  O   PHE A  31     -18.789 -13.804 -15.085  1.00 41.97           O  
ATOM    204  CB  PHE A  31     -20.075 -10.788 -14.618  1.00 31.90           C  
ATOM    205  CG  PHE A  31     -18.798 -10.852 -13.831  1.00 37.51           C  
ATOM    206  CD1 PHE A  31     -17.601 -10.449 -14.399  1.00 36.11           C  
ATOM    207  CD2 PHE A  31     -18.790 -11.330 -12.532  1.00 34.85           C  
ATOM    208  CE1 PHE A  31     -16.423 -10.507 -13.682  1.00 46.08           C  
ATOM    209  CE2 PHE A  31     -17.615 -11.389 -11.808  1.00 40.42           C  
ATOM    210  CZ  PHE A  31     -16.430 -10.976 -12.378  1.00 44.03           C  
ATOM    211  N   PRO A  32     -20.656 -13.728 -13.813  1.00 40.73           N  
ATOM    212  CA  PRO A  32     -20.210 -14.888 -13.035  1.00 44.77           C  
ATOM    213  C   PRO A  32     -20.046 -16.113 -13.924  1.00 35.86           C  
ATOM    214  O   PRO A  32     -19.141 -16.899 -13.674  1.00 40.95           O  
ATOM    215  CB  PRO A  32     -21.345 -15.095 -12.018  1.00 41.69           C  
ATOM    216  CG  PRO A  32     -22.083 -13.790 -11.987  1.00 43.33           C  
ATOM    217  CD  PRO A  32     -21.984 -13.261 -13.378  1.00 44.26           C  
ATOM    218  N   VAL A  33     -20.888 -16.257 -14.944  1.00 39.09           N  
ATOM    219  CA  VAL A  33     -20.785 -17.400 -15.858  1.00 36.56           C  
ATOM    220  C   VAL A  33     -19.551 -17.296 -16.762  1.00 40.79           C  
ATOM    221  O   VAL A  33     -18.871 -18.297 -17.025  1.00 42.14           O  
ATOM    222  CB  VAL A  33     -22.066 -17.575 -16.700  1.00 35.50           C  
ATOM    223  CG1 VAL A  33     -21.749 -18.215 -18.046  1.00 40.25           C  
ATOM    224  CG2 VAL A  33     -23.096 -18.402 -15.932  1.00 32.32           C  
ATOM    225  N   GLN A  34     -19.257 -16.081 -17.221  1.00 39.15           N  
ATOM    226  CA  GLN A  34     -18.092 -15.840 -18.064  1.00 44.97           C  
ATOM    227  C   GLN A  34     -16.783 -15.985 -17.281  1.00 48.12           C  
ATOM    228  O   GLN A  34     -15.795 -16.491 -17.806  1.00 48.41           O  
ATOM    229  CB  GLN A  34     -18.174 -14.449 -18.712  1.00 54.86           C  
ATOM    230  CG  GLN A  34     -19.416 -14.230 -19.566  1.00 41.23           C  
ATOM    231  CD  GLN A  34     -19.389 -15.028 -20.850  1.00 49.12           C  
ATOM    232  OE1 GLN A  34     -18.383 -15.037 -21.561  1.00 49.33           O  
ATOM    233  NE2 GLN A  34     -20.501 -15.698 -21.163  1.00 44.97           N  
ATOM    234  N   ALA A  35     -16.773 -15.540 -16.030  1.00 43.01           N  
ATOM    235  CA  ALA A  35     -15.588 -15.691 -15.186  1.00 45.19           C  
ATOM    236  C   ALA A  35     -15.314 -17.164 -14.851  1.00 58.13           C  
ATOM    237  O   ALA A  35     -14.169 -17.612 -14.859  1.00 62.33           O  
ATOM    238  CB  ALA A  35     -15.733 -14.875 -13.911  1.00 48.04           C  
ATOM    239  N   ALA A  36     -16.370 -17.922 -14.576  1.00 58.31           N  
ATOM    240  CA  ALA A  36     -16.222 -19.333 -14.235  1.00 56.83           C  
ATOM    241  C   ALA A  36     -15.717 -20.154 -15.427  1.00 59.21           C  
ATOM    242  O   ALA A  36     -15.003 -21.139 -15.252  1.00 64.03           O  
ATOM    243  CB  ALA A  36     -17.539 -19.896 -13.707  1.00 48.31           C  
ATOM    244  N   GLU A  37     -16.083 -19.729 -16.635  1.00 66.29           N  
ATOM    245  CA  GLU A  37     -15.733 -20.439 -17.861  1.00 57.02           C  
ATOM    246  C   GLU A  37     -14.413 -19.997 -18.470  1.00 59.89           C  
ATOM    247  O   GLU A  37     -13.864 -20.672 -19.340  1.00 57.10           O  
ATOM    248  CB  GLU A  37     -16.810 -20.214 -18.919  1.00 51.64           C  
ATOM    249  CG  GLU A  37     -18.072 -21.015 -18.728  1.00 66.21           C  
ATOM    250  CD  GLU A  37     -18.954 -20.943 -19.948  1.00 74.93           C  
ATOM    251  OE1 GLU A  37     -18.424 -20.595 -21.026  1.00 79.74           O  
ATOM    252  OE2 GLU A  37     -20.167 -21.222 -19.836  1.00 76.52           O  
ATOM    253  N   ASN A  38     -13.913 -18.852 -18.035  1.00 58.36           N  
ATOM    254  CA  ASN A  38     -12.754 -18.265 -18.686  1.00 57.42           C  
ATOM    255  C   ASN A  38     -11.618 -17.985 -17.707  1.00 57.18           C  
ATOM    256  O   ASN A  38     -10.912 -16.984 -17.830  1.00 61.69           O  
ATOM    257  CB  ASN A  38     -13.158 -17.000 -19.451  1.00 54.09           C  
ATOM    258  CG  ASN A  38     -14.060 -17.299 -20.648  1.00 57.64           C  
ATOM    259  OD1 ASN A  38     -13.578 -17.595 -21.741  1.00 67.83           O  
ATOM    260  ND2 ASN A  38     -15.372 -17.208 -20.446  1.00 54.47           N  
ATOM    261  N   GLY A  39     -11.459 -18.870 -16.725  1.00 53.86           N  
ATOM    262  CA  GLY A  39     -10.285 -18.860 -15.870  1.00 58.73           C  
ATOM    263  C   GLY A  39     -10.492 -18.557 -14.396  1.00 61.65           C  
ATOM    264  O   GLY A  39      -9.518 -18.352 -13.671  1.00 54.94           O  
ATOM    265  N   GLY A  40     -11.745 -18.532 -13.945  1.00 51.97           N  
ATOM    266  CA  GLY A  40     -12.046 -18.180 -12.566  1.00 50.06           C  
ATOM    267  C   GLY A  40     -11.400 -16.873 -12.142  1.00 51.02           C  
ATOM    268  O   GLY A  40     -11.569 -15.854 -12.801  1.00 53.05           O  
ATOM    269  N   GLY A  41     -10.649 -16.898 -11.046  1.00 49.92           N  
ATOM    270  CA  GLY A  41      -9.934 -15.719 -10.598  1.00 54.32           C  
ATOM    271  C   GLY A  41      -8.996 -15.158 -11.655  1.00 55.61           C  
ATOM    272  O   GLY A  41      -8.759 -13.949 -11.711  1.00 53.60           O  
ATOM    273  N   ALA A  42      -8.453 -16.037 -12.490  1.00 49.02           N  
ATOM    274  CA  ALA A  42      -7.526 -15.617 -13.538  1.00 66.96           C  
ATOM    275  C   ALA A  42      -8.204 -14.631 -14.484  1.00 57.12           C  
ATOM    276  O   ALA A  42      -7.565 -13.736 -15.037  1.00 52.20           O  
ATOM    277  CB  ALA A  42      -7.016 -16.828 -14.317  1.00 60.80           C  
ATOM    278  N   PHE A  43      -9.507 -14.809 -14.656  1.00 56.19           N  
ATOM    279  CA  PHE A  43     -10.304 -14.000 -15.575  1.00 59.77           C  
ATOM    280  C   PHE A  43     -10.241 -12.499 -15.257  1.00 55.73           C  
ATOM    281  O   PHE A  43     -10.469 -11.670 -16.138  1.00 48.29           O  
ATOM    282  CB  PHE A  43     -11.748 -14.510 -15.571  1.00 55.74           C  
ATOM    283  CG  PHE A  43     -12.640 -13.845 -16.574  1.00 49.17           C  
ATOM    284  CD1 PHE A  43     -12.544 -14.156 -17.920  1.00 40.12           C  
ATOM    285  CD2 PHE A  43     -13.599 -12.931 -16.163  1.00 44.14           C  
ATOM    286  CE1 PHE A  43     -13.378 -13.554 -18.843  1.00 58.02           C  
ATOM    287  CE2 PHE A  43     -14.440 -12.325 -17.083  1.00 49.06           C  
ATOM    288  CZ  PHE A  43     -14.329 -12.632 -18.422  1.00 44.49           C  
ATOM    289  N   MET A  44      -9.928 -12.155 -14.006  1.00 49.05           N  
ATOM    290  CA AMET A  44      -9.830 -10.756 -13.601  0.80 54.28           C  
ATOM    291  CA BMET A  44      -9.817 -10.750 -13.595  0.20 54.15           C  
ATOM    292  C   MET A  44      -8.628 -10.071 -14.249  1.00 52.03           C  
ATOM    293  O   MET A  44      -8.535  -8.842 -14.269  1.00 46.54           O  
ATOM    294  CB AMET A  44      -9.761 -10.639 -12.072  0.80 48.69           C  
ATOM    295  CB BMET A  44      -9.668 -10.625 -12.076  0.20 48.89           C  
ATOM    296  CG AMET A  44     -11.056 -11.010 -11.343  0.80 54.34           C  
ATOM    297  CG BMET A  44     -10.886 -11.017 -11.276  0.20 54.23           C  
ATOM    298  SD AMET A  44     -12.462  -9.943 -11.751  0.80 48.95           S  
ATOM    299  SD BMET A  44     -11.266 -12.757 -11.489  0.20 54.47           S  
ATOM    300  CE AMET A  44     -13.070 -10.769 -13.214  0.80 55.51           C  
ATOM    301  CE BMET A  44     -12.500 -12.679 -12.786  0.20 53.74           C  
ATOM    302  N   ILE A  45      -7.707 -10.878 -14.762  1.00 62.28           N  
ATOM    303  CA  ILE A  45      -6.539 -10.349 -15.451  1.00 64.00           C  
ATOM    304  C   ILE A  45      -6.981  -9.689 -16.748  1.00 48.94           C  
ATOM    305  O   ILE A  45      -6.903  -8.470 -16.878  1.00 53.08           O  
ATOM    306  CB  ILE A  45      -5.484 -11.449 -15.733  1.00 57.82           C  
ATOM    307  CG1 ILE A  45      -4.929 -12.009 -14.416  1.00 58.37           C  
ATOM    308  CG2 ILE A  45      -4.381 -10.918 -16.640  1.00 45.81           C  
ATOM    309  CD1 ILE A  45      -4.359 -10.947 -13.483  1.00 55.18           C  
ATOM    310  N   PRO A  46      -7.473 -10.488 -17.706  1.00 52.44           N  
ATOM    311  CA  PRO A  46      -7.917  -9.898 -18.971  1.00 51.46           C  
ATOM    312  C   PRO A  46      -9.129  -8.988 -18.782  1.00 53.30           C  
ATOM    313  O   PRO A  46      -9.359  -8.104 -19.607  1.00 49.49           O  
ATOM    314  CB  PRO A  46      -8.309 -11.116 -19.804  1.00 46.38           C  
ATOM    315  CG  PRO A  46      -8.612 -12.176 -18.816  1.00 48.70           C  
ATOM    316  CD  PRO A  46      -7.711 -11.941 -17.658  1.00 53.06           C  
ATOM    317  N   TYR A  47      -9.889  -9.204 -17.711  1.00 53.97           N  
ATOM    318  CA  TYR A  47     -11.078  -8.401 -17.433  1.00 51.22           C  
ATOM    319  C   TYR A  47     -10.705  -6.997 -16.980  1.00 42.04           C  
ATOM    320  O   TYR A  47     -11.247  -6.010 -17.468  1.00 44.83           O  
ATOM    321  CB  TYR A  47     -11.942  -9.093 -16.384  1.00 51.50           C  
ATOM    322  CG  TYR A  47     -13.231  -8.391 -16.006  1.00 48.04           C  
ATOM    323  CD1 TYR A  47     -14.401  -8.588 -16.739  1.00 41.67           C  
ATOM    324  CD2 TYR A  47     -13.289  -7.575 -14.887  1.00 42.09           C  
ATOM    325  CE1 TYR A  47     -15.586  -7.961 -16.372  1.00 43.39           C  
ATOM    326  CE2 TYR A  47     -14.465  -6.951 -14.513  1.00 43.23           C  
ATOM    327  CZ  TYR A  47     -15.608  -7.148 -15.256  1.00 35.27           C  
ATOM    328  OH  TYR A  47     -16.769  -6.525 -14.869  1.00 41.40           O  
ATOM    329  N   ILE A  48      -9.785  -6.906 -16.030  1.00 43.76           N  
ATOM    330  CA  ILE A  48      -9.298  -5.602 -15.593  1.00 43.69           C  
ATOM    331  C   ILE A  48      -8.557  -4.882 -16.734  1.00 44.69           C  
ATOM    332  O   ILE A  48      -8.657  -3.668 -16.887  1.00 49.20           O  
ATOM    333  CB  ILE A  48      -8.391  -5.727 -14.368  1.00 44.56           C  
ATOM    334  CG1 ILE A  48      -9.211  -6.225 -13.171  1.00 54.04           C  
ATOM    335  CG2 ILE A  48      -7.717  -4.385 -14.070  1.00 41.87           C  
ATOM    336  CD1 ILE A  48      -8.391  -6.692 -11.993  1.00 50.84           C  
ATOM    337  N   ILE A  49      -7.818  -5.640 -17.530  1.00 42.66           N  
ATOM    338  CA  ILE A  49      -7.115  -5.082 -18.675  1.00 54.78           C  
ATOM    339  C   ILE A  49      -8.095  -4.487 -19.691  1.00 47.08           C  
ATOM    340  O   ILE A  49      -7.909  -3.373 -20.185  1.00 46.16           O  
ATOM    341  CB  ILE A  49      -6.245  -6.158 -19.356  1.00 46.22           C  
ATOM    342  CG1 ILE A  49      -5.091  -6.564 -18.429  1.00 57.25           C  
ATOM    343  CG2 ILE A  49      -5.712  -5.654 -20.685  1.00 47.75           C  
ATOM    344  CD1 ILE A  49      -4.133  -7.551 -19.062  1.00 49.89           C  
ATOM    345  N   ALA A  50      -9.138  -5.251 -19.997  1.00 49.60           N  
ATOM    346  CA  ALA A  50     -10.189  -4.811 -20.903  1.00 42.22           C  
ATOM    347  C   ALA A  50     -10.864  -3.557 -20.369  1.00 42.92           C  
ATOM    348  O   ALA A  50     -11.166  -2.627 -21.122  1.00 49.61           O  
ATOM    349  CB  ALA A  50     -11.212  -5.922 -21.092  1.00 38.13           C  
ATOM    350  N   PHE A  51     -11.111  -3.537 -19.066  1.00 40.23           N  
ATOM    351  CA  PHE A  51     -11.749  -2.395 -18.438  1.00 39.40           C  
ATOM    352  C   PHE A  51     -10.930  -1.139 -18.671  1.00 41.75           C  
ATOM    353  O   PHE A  51     -11.470  -0.100 -19.049  1.00 44.31           O  
ATOM    354  CB  PHE A  51     -11.918  -2.647 -16.938  1.00 38.43           C  
ATOM    355  CG  PHE A  51     -12.646  -1.552 -16.210  1.00 38.71           C  
ATOM    356  CD1 PHE A  51     -13.993  -1.328 -16.440  1.00 44.37           C  
ATOM    357  CD2 PHE A  51     -11.989  -0.757 -15.285  1.00 44.48           C  
ATOM    358  CE1 PHE A  51     -14.676  -0.318 -15.769  1.00 49.49           C  
ATOM    359  CE2 PHE A  51     -12.668   0.255 -14.595  1.00 50.16           C  
ATOM    360  CZ  PHE A  51     -14.015   0.470 -14.841  1.00 45.37           C  
ATOM    361  N   LEU A  52      -9.624  -1.240 -18.437  1.00 39.77           N  
ATOM    362  CA  LEU A  52      -8.731  -0.089 -18.554  1.00 42.22           C  
ATOM    363  C   LEU A  52      -8.445   0.312 -20.000  1.00 41.69           C  
ATOM    364  O   LEU A  52      -8.288   1.497 -20.295  1.00 43.45           O  
ATOM    365  CB  LEU A  52      -7.411  -0.370 -17.835  1.00 47.62           C  
ATOM    366  CG  LEU A  52      -7.528  -0.787 -16.367  1.00 52.53           C  
ATOM    367  CD1 LEU A  52      -6.159  -1.096 -15.805  1.00 48.66           C  
ATOM    368  CD2 LEU A  52      -8.209   0.304 -15.556  1.00 47.87           C  
ATOM    369  N   LEU A  53      -8.378  -0.668 -20.896  1.00 41.84           N  
ATOM    370  CA  LEU A  53      -7.953  -0.405 -22.271  1.00 41.21           C  
ATOM    371  C   LEU A  53      -9.099  -0.259 -23.262  1.00 48.89           C  
ATOM    372  O   LEU A  53      -8.913   0.309 -24.339  1.00 39.50           O  
ATOM    373  CB  LEU A  53      -6.980  -1.483 -22.760  1.00 43.30           C  
ATOM    374  CG  LEU A  53      -5.668  -1.553 -21.972  1.00 52.79           C  
ATOM    375  CD1 LEU A  53      -4.731  -2.588 -22.584  1.00 62.36           C  
ATOM    376  CD2 LEU A  53      -4.996  -0.186 -21.897  1.00 49.90           C  
ATOM    377  N   VAL A  54     -10.276  -0.772 -22.910  1.00 39.07           N  
ATOM    378  CA  VAL A  54     -11.435  -0.649 -23.799  1.00 34.14           C  
ATOM    379  C   VAL A  54     -12.639   0.006 -23.131  1.00 32.80           C  
ATOM    380  O   VAL A  54     -13.195   0.955 -23.655  1.00 37.78           O  
ATOM    381  CB  VAL A  54     -11.868  -2.016 -24.357  1.00 53.10           C  
ATOM    382  CG1 VAL A  54     -13.126  -1.867 -25.208  1.00 42.10           C  
ATOM    383  CG2 VAL A  54     -10.727  -2.646 -25.167  1.00 41.69           C  
ATOM    384  N   GLY A  55     -13.030  -0.488 -21.959  1.00 37.26           N  
ATOM    385  CA  GLY A  55     -14.252  -0.029 -21.326  1.00 30.68           C  
ATOM    386  C   GLY A  55     -14.232   1.428 -20.903  1.00 39.40           C  
ATOM    387  O   GLY A  55     -15.104   2.211 -21.275  1.00 32.29           O  
ATOM    388  N   ILE A  56     -13.238   1.798 -20.109  1.00 31.89           N  
ATOM    389  CA  ILE A  56     -13.116   3.178 -19.655  1.00 35.79           C  
ATOM    390  C   ILE A  56     -12.967   4.167 -20.812  1.00 32.50           C  
ATOM    391  O   ILE A  56     -13.707   5.147 -20.888  1.00 36.69           O  
ATOM    392  CB  ILE A  56     -11.954   3.338 -18.647  1.00 36.93           C  
ATOM    393  CG1 ILE A  56     -12.349   2.734 -17.308  1.00 45.44           C  
ATOM    394  CG2 ILE A  56     -11.614   4.792 -18.460  1.00 39.27           C  
ATOM    395  CD1 ILE A  56     -13.598   3.381 -16.726  1.00 54.81           C  
ATOM    396  N   PRO A  57     -12.006   3.914 -21.714  1.00 36.15           N  
ATOM    397  CA  PRO A  57     -11.740   4.801 -22.856  1.00 34.58           C  
ATOM    398  C   PRO A  57     -12.977   5.033 -23.718  1.00 31.27           C  
ATOM    399  O   PRO A  57     -13.292   6.164 -24.077  1.00 34.13           O  
ATOM    400  CB  PRO A  57     -10.716   4.016 -23.684  1.00 36.80           C  
ATOM    401  CG  PRO A  57     -10.089   3.073 -22.761  1.00 38.94           C  
ATOM    402  CD  PRO A  57     -11.072   2.776 -21.658  1.00 37.41           C  
ATOM    403  N   LEU A  58     -13.670   3.961 -24.072  1.00 35.59           N  
ATOM    404  CA  LEU A  58     -14.825   4.095 -24.954  1.00 28.44           C  
ATOM    405  C   LEU A  58     -15.973   4.788 -24.230  1.00 28.68           C  
ATOM    406  O   LEU A  58     -16.681   5.606 -24.812  1.00 31.38           O  
ATOM    407  CB  LEU A  58     -15.280   2.733 -25.468  1.00 33.84           C  
ATOM    408  CG  LEU A  58     -15.684   2.617 -26.936  1.00 45.70           C  
ATOM    409  CD1 LEU A  58     -16.619   1.418 -27.115  1.00 43.08           C  
ATOM    410  CD2 LEU A  58     -16.315   3.915 -27.461  1.00 39.22           C  
ATOM    411  N   MET A  59     -16.161   4.447 -22.958  1.00 26.42           N  
ATOM    412  CA  MET A  59     -17.155   5.123 -22.140  1.00 32.21           C  
ATOM    413  C   MET A  59     -16.991   6.643 -22.135  1.00 29.53           C  
ATOM    414  O   MET A  59     -17.958   7.373 -22.337  1.00 33.32           O  
ATOM    415  CB  MET A  59     -17.114   4.575 -20.704  1.00 36.14           C  
ATOM    416  CG  MET A  59     -17.922   5.362 -19.690  1.00 36.15           C  
ATOM    417  SD  MET A  59     -16.878   6.460 -18.719  1.00 52.50           S  
ATOM    418  CE  MET A  59     -17.343   8.068 -19.310  1.00 43.65           C  
ATOM    419  N   TRP A  60     -15.779   7.126 -21.868  1.00 32.77           N  
ATOM    420  CA  TRP A  60     -15.521   8.573 -21.880  1.00 30.46           C  
ATOM    421  C   TRP A  60     -15.837   9.169 -23.253  1.00 32.82           C  
ATOM    422  O   TRP A  60     -16.391  10.265 -23.375  1.00 34.30           O  
ATOM    423  CB  TRP A  60     -14.063   8.876 -21.512  1.00 30.41           C  
ATOM    424  CG  TRP A  60     -13.770   8.890 -20.024  1.00 34.28           C  
ATOM    425  CD1 TRP A  60     -14.593   9.323 -19.026  1.00 32.79           C  
ATOM    426  CD2 TRP A  60     -12.546   8.498 -19.391  1.00 30.04           C  
ATOM    427  NE1 TRP A  60     -13.966   9.195 -17.806  1.00 35.75           N  
ATOM    428  CE2 TRP A  60     -12.709   8.689 -18.008  1.00 37.55           C  
ATOM    429  CE3 TRP A  60     -11.335   7.984 -19.864  1.00 36.07           C  
ATOM    430  CZ2 TRP A  60     -11.702   8.400 -17.095  1.00 40.25           C  
ATOM    431  CZ3 TRP A  60     -10.344   7.696 -18.958  1.00 35.22           C  
ATOM    432  CH2 TRP A  60     -10.529   7.901 -17.590  1.00 39.26           C  
ATOM    433  N   ILE A  61     -15.468   8.439 -24.290  1.00 30.78           N  
ATOM    434  CA  ILE A  61     -15.700   8.896 -25.649  1.00 30.17           C  
ATOM    435  C   ILE A  61     -17.186   9.072 -25.937  1.00 38.75           C  
ATOM    436  O   ILE A  61     -17.602  10.116 -26.457  1.00 35.96           O  
ATOM    437  CB  ILE A  61     -15.067   7.945 -26.640  1.00 29.94           C  
ATOM    438  CG1 ILE A  61     -13.553   8.176 -26.646  1.00 28.86           C  
ATOM    439  CG2 ILE A  61     -15.719   8.107 -28.034  1.00 34.29           C  
ATOM    440  CD1 ILE A  61     -12.766   7.180 -27.476  1.00 39.89           C  
ATOM    441  N   GLU A  62     -17.985   8.069 -25.576  1.00 28.17           N  
ATOM    442  CA  GLU A  62     -19.440   8.174 -25.720  1.00 30.58           C  
ATOM    443  C   GLU A  62     -20.061   9.316 -24.907  1.00 31.10           C  
ATOM    444  O   GLU A  62     -20.931  10.032 -25.404  1.00 28.49           O  
ATOM    445  CB  GLU A  62     -20.108   6.828 -25.398  1.00 29.44           C  
ATOM    446  CG  GLU A  62     -19.782   5.779 -26.464  1.00 32.96           C  
ATOM    447  CD  GLU A  62     -20.434   4.425 -26.215  1.00 44.16           C  
ATOM    448  OE1 GLU A  62     -21.124   4.250 -25.186  1.00 35.95           O  
ATOM    449  OE2 GLU A  62     -20.243   3.522 -27.055  1.00 38.84           O  
ATOM    450  N   TRP A  63     -19.630   9.469 -23.647  1.00 27.95           N  
ATOM    451  CA  TRP A  63     -20.049  10.617 -22.850  1.00 31.11           C  
ATOM    452  C   TRP A  63     -19.691  11.902 -23.584  1.00 29.21           C  
ATOM    453  O   TRP A  63     -20.501  12.824 -23.677  1.00 30.43           O  
ATOM    454  CB  TRP A  63     -19.362  10.645 -21.478  1.00 25.25           C  
ATOM    455  CG  TRP A  63     -19.956   9.771 -20.388  1.00 29.06           C  
ATOM    456  CD1 TRP A  63     -19.976   8.402 -20.341  1.00 32.39           C  
ATOM    457  CD2 TRP A  63     -20.547  10.217 -19.156  1.00 32.91           C  
ATOM    458  NE1 TRP A  63     -20.551   7.973 -19.166  1.00 27.20           N  
ATOM    459  CE2 TRP A  63     -20.912   9.068 -18.424  1.00 32.76           C  
ATOM    460  CE3 TRP A  63     -20.808  11.476 -18.605  1.00 41.67           C  
ATOM    461  CZ2 TRP A  63     -21.526   9.143 -17.164  1.00 30.40           C  
ATOM    462  CZ3 TRP A  63     -21.417  11.543 -17.341  1.00 27.28           C  
ATOM    463  CH2 TRP A  63     -21.770  10.381 -16.648  1.00 28.26           C  
ATOM    464  N   ALA A  64     -18.479  11.966 -24.124  1.00 30.79           N  
ATOM    465  CA  ALA A  64     -18.032  13.186 -24.794  1.00 28.76           C  
ATOM    466  C   ALA A  64     -18.863  13.474 -26.044  1.00 34.58           C  
ATOM    467  O   ALA A  64     -19.233  14.618 -26.322  1.00 32.73           O  
ATOM    468  CB  ALA A  64     -16.554  13.092 -25.134  1.00 34.24           C  
ATOM    469  N   MET A  65     -19.150  12.425 -26.802  1.00 31.37           N  
ATOM    470  CA  MET A  65     -19.944  12.583 -28.005  1.00 30.46           C  
ATOM    471  C   MET A  65     -21.354  13.075 -27.699  1.00 23.66           C  
ATOM    472  O   MET A  65     -21.853  13.965 -28.362  1.00 29.28           O  
ATOM    473  CB  MET A  65     -19.984  11.273 -28.786  1.00 30.90           C  
ATOM    474  CG  MET A  65     -18.643  10.873 -29.364  1.00 35.68           C  
ATOM    475  SD  MET A  65     -18.851   9.478 -30.497  1.00 45.73           S  
ATOM    476  CE  MET A  65     -19.843   8.432 -29.459  1.00 38.06           C  
ATOM    477  N   GLY A  66     -21.984  12.500 -26.684  1.00 24.36           N  
ATOM    478  CA  GLY A  66     -23.316  12.919 -26.288  1.00 24.02           C  
ATOM    479  C   GLY A  66     -23.352  14.326 -25.721  1.00 27.56           C  
ATOM    480  O   GLY A  66     -24.229  15.114 -26.059  1.00 32.88           O  
ATOM    481  N   ARG A  67     -22.407  14.656 -24.843  1.00 29.54           N  
ATOM    482  CA  ARG A  67     -22.390  16.008 -24.294  1.00 34.30           C  
ATOM    483  C   ARG A  67     -22.232  17.005 -25.435  1.00 29.29           C  
ATOM    484  O   ARG A  67     -22.920  18.020 -25.486  1.00 33.64           O  
ATOM    485  CB  ARG A  67     -21.279  16.187 -23.261  1.00 33.83           C  
ATOM    486  CG  ARG A  67     -21.237  17.595 -22.696  1.00 33.17           C  
ATOM    487  CD  ARG A  67     -20.193  17.701 -21.588  1.00 37.84           C  
ATOM    488  NE  ARG A  67     -18.828  17.642 -22.110  1.00 31.94           N  
ATOM    489  CZ  ARG A  67     -17.760  18.044 -21.425  1.00 43.57           C  
ATOM    490  NH1 ARG A  67     -17.908  18.541 -20.198  1.00 36.77           N  
ATOM    491  NH2 ARG A  67     -16.548  17.961 -21.967  1.00 34.16           N  
ATOM    492  N   TYR A  68     -21.340  16.676 -26.365  1.00 34.26           N  
ATOM    493  CA  TYR A  68     -21.060  17.497 -27.540  1.00 33.82           C  
ATOM    494  C   TYR A  68     -22.291  17.702 -28.408  1.00 40.85           C  
ATOM    495  O   TYR A  68     -22.599  18.828 -28.826  1.00 31.28           O  
ATOM    496  CB  TYR A  68     -19.967  16.828 -28.367  1.00 37.17           C  
ATOM    497  CG  TYR A  68     -19.584  17.563 -29.625  1.00 40.03           C  
ATOM    498  CD1 TYR A  68     -18.687  18.622 -29.583  1.00 44.33           C  
ATOM    499  CD2 TYR A  68     -20.102  17.185 -30.870  1.00 52.40           C  
ATOM    500  CE1 TYR A  68     -18.324  19.291 -30.735  1.00 48.75           C  
ATOM    501  CE2 TYR A  68     -19.740  17.851 -32.029  1.00 38.80           C  
ATOM    502  CZ  TYR A  68     -18.847  18.903 -31.950  1.00 48.81           C  
ATOM    503  OH  TYR A  68     -18.474  19.586 -33.085  1.00 69.61           O  
ATOM    504  N   GLY A  69     -22.988  16.610 -28.706  1.00 35.88           N  
ATOM    505  CA  GLY A  69     -24.182  16.720 -29.522  1.00 31.86           C  
ATOM    506  C   GLY A  69     -25.252  17.480 -28.769  1.00 31.21           C  
ATOM    507  O   GLY A  69     -25.964  18.309 -29.338  1.00 31.10           O  
ATOM    508  N   GLY A  70     -25.359  17.192 -27.475  1.00 34.08           N  
ATOM    509  CA  GLY A  70     -26.369  17.818 -26.644  1.00 40.95           C  
ATOM    510  C   GLY A  70     -26.293  19.333 -26.690  1.00 35.80           C  
ATOM    511  O   GLY A  70     -27.315  20.021 -26.681  1.00 31.40           O  
ATOM    512  N   ALA A  71     -25.072  19.854 -26.753  1.00 35.96           N  
ATOM    513  CA  ALA A  71     -24.864  21.299 -26.764  1.00 34.48           C  
ATOM    514  C   ALA A  71     -25.434  21.911 -28.035  1.00 40.14           C  
ATOM    515  O   ALA A  71     -25.738  23.105 -28.086  1.00 39.02           O  
ATOM    516  CB  ALA A  71     -23.384  21.626 -26.624  1.00 29.95           C  
ATOM    517  N   GLN A  72     -25.580  21.088 -29.067  1.00 37.33           N  
ATOM    518  CA  GLN A  72     -26.131  21.570 -30.325  1.00 34.46           C  
ATOM    519  C   GLN A  72     -27.557  21.061 -30.557  1.00 39.04           C  
ATOM    520  O   GLN A  72     -28.061  21.109 -31.679  1.00 42.37           O  
ATOM    521  CB  GLN A  72     -25.210  21.196 -31.492  1.00 30.94           C  
ATOM    522  CG  GLN A  72     -23.799  21.785 -31.374  1.00 35.62           C  
ATOM    523  CD  GLN A  72     -22.959  21.563 -32.625  1.00 48.38           C  
ATOM    524  OE1 GLN A  72     -23.395  21.856 -33.742  1.00 52.06           O  
ATOM    525  NE2 GLN A  72     -21.744  21.047 -32.442  1.00 55.15           N  
ATOM    526  N   GLY A  73     -28.198  20.578 -29.495  1.00 37.07           N  
ATOM    527  CA  GLY A  73     -29.580  20.136 -29.567  1.00 31.72           C  
ATOM    528  C   GLY A  73     -29.790  18.725 -30.100  1.00 38.26           C  
ATOM    529  O   GLY A  73     -30.916  18.365 -30.464  1.00 34.45           O  
ATOM    530  N   HIS A  74     -28.723  17.923 -30.130  1.00 35.44           N  
ATOM    531  CA  HIS A  74     -28.768  16.584 -30.734  1.00 38.67           C  
ATOM    532  C   HIS A  74     -28.266  15.479 -29.798  1.00 43.11           C  
ATOM    533  O   HIS A  74     -27.094  15.464 -29.418  1.00 35.90           O  
ATOM    534  CB  HIS A  74     -27.958  16.559 -32.031  1.00 33.99           C  
ATOM    535  CG  HIS A  74     -28.446  17.530 -33.067  1.00 44.06           C  
ATOM    536  ND1 HIS A  74     -29.667  17.397 -33.694  1.00 38.73           N  
ATOM    537  CD2 HIS A  74     -27.884  18.652 -33.576  1.00 39.72           C  
ATOM    538  CE1 HIS A  74     -29.837  18.394 -34.544  1.00 44.15           C  
ATOM    539  NE2 HIS A  74     -28.769  19.172 -34.490  1.00 44.58           N  
ATOM    540  N   GLY A  75     -29.143  14.544 -29.446  1.00 32.62           N  
ATOM    541  CA  GLY A  75     -28.750  13.428 -28.592  1.00 25.05           C  
ATOM    542  C   GLY A  75     -28.516  12.068 -29.252  1.00 31.84           C  
ATOM    543  O   GLY A  75     -28.174  11.108 -28.556  1.00 26.03           O  
ATOM    544  N   THR A  76     -28.708  11.967 -30.575  1.00 31.63           N  
ATOM    545  CA  THR A  76     -28.566  10.696 -31.295  1.00 29.72           C  
ATOM    546  C   THR A  76     -27.570  10.786 -32.470  1.00 29.29           C  
ATOM    547  O   THR A  76     -27.238  11.876 -32.945  1.00 29.86           O  
ATOM    548  CB  THR A  76     -29.923  10.141 -31.789  1.00 30.02           C  
ATOM    549  OG1 THR A  76     -30.538  11.073 -32.683  1.00 28.07           O  
ATOM    550  CG2 THR A  76     -30.842   9.906 -30.608  1.00 26.72           C  
ATOM    551  N   THR A  77     -27.085   9.630 -32.906  1.00 25.80           N  
ATOM    552  CA  THR A  77     -25.909   9.571 -33.757  1.00 27.32           C  
ATOM    553  C   THR A  77     -26.086   9.960 -35.239  1.00 26.75           C  
ATOM    554  O   THR A  77     -25.104  10.307 -35.886  1.00 34.28           O  
ATOM    555  CB  THR A  77     -25.192   8.219 -33.628  1.00 25.11           C  
ATOM    556  OG1 THR A  77     -26.137   7.155 -33.817  1.00 25.69           O  
ATOM    557  CG2 THR A  77     -24.551   8.099 -32.228  1.00 26.94           C  
ATOM    558  N   PRO A  78     -27.319   9.919 -35.779  1.00 25.12           N  
ATOM    559  CA  PRO A  78     -27.353  10.423 -37.161  1.00 29.62           C  
ATOM    560  C   PRO A  78     -26.876  11.877 -37.196  1.00 29.98           C  
ATOM    561  O   PRO A  78     -26.048  12.232 -38.035  1.00 31.03           O  
ATOM    562  CB  PRO A  78     -28.834  10.334 -37.538  1.00 24.48           C  
ATOM    563  CG  PRO A  78     -29.391   9.249 -36.642  1.00 27.76           C  
ATOM    564  CD  PRO A  78     -28.641   9.443 -35.331  1.00 26.93           C  
ATOM    565  N   ALA A  79     -27.384  12.686 -36.271  1.00 34.05           N  
ATOM    566  CA  ALA A  79     -27.030  14.105 -36.201  1.00 31.21           C  
ATOM    567  C   ALA A  79     -25.625  14.287 -35.648  1.00 34.17           C  
ATOM    568  O   ALA A  79     -24.832  15.083 -36.154  1.00 31.66           O  
ATOM    569  CB  ALA A  79     -28.021  14.851 -35.347  1.00 29.07           C  
ATOM    570  N   ILE A  80     -25.314  13.542 -34.595  1.00 31.75           N  
ATOM    571  CA  ILE A  80     -24.044  13.723 -33.927  1.00 33.84           C  
ATOM    572  C   ILE A  80     -22.897  13.292 -34.825  1.00 35.94           C  
ATOM    573  O   ILE A  80     -21.883  13.978 -34.920  1.00 36.56           O  
ATOM    574  CB  ILE A  80     -24.004  12.956 -32.595  1.00 27.16           C  
ATOM    575  CG1 ILE A  80     -24.934  13.631 -31.590  1.00 26.43           C  
ATOM    576  CG2 ILE A  80     -22.592  12.896 -32.057  1.00 36.08           C  
ATOM    577  CD1 ILE A  80     -25.022  12.894 -30.269  1.00 25.60           C  
ATOM    578  N   PHE A  81     -23.058  12.155 -35.494  1.00 29.93           N  
ATOM    579  CA  PHE A  81     -22.017  11.677 -36.381  1.00 30.78           C  
ATOM    580  C   PHE A  81     -21.746  12.718 -37.462  1.00 34.90           C  
ATOM    581  O   PHE A  81     -20.612  12.915 -37.893  1.00 35.02           O  
ATOM    582  CB  PHE A  81     -22.414  10.333 -36.992  1.00 31.37           C  
ATOM    583  CG  PHE A  81     -21.861   9.154 -36.246  1.00 32.54           C  
ATOM    584  CD1 PHE A  81     -21.685   9.216 -34.872  1.00 28.50           C  
ATOM    585  CD2 PHE A  81     -21.506   7.990 -36.916  1.00 34.53           C  
ATOM    586  CE1 PHE A  81     -21.166   8.135 -34.172  1.00 30.76           C  
ATOM    587  CE2 PHE A  81     -20.982   6.914 -36.225  1.00 30.36           C  
ATOM    588  CZ  PHE A  81     -20.814   6.984 -34.848  1.00 33.52           C  
ATOM    589  N   TYR A  82     -22.798  13.392 -37.887  1.00 27.72           N  
ATOM    590  CA  TYR A  82     -22.689  14.339 -38.976  1.00 35.47           C  
ATOM    591  C   TYR A  82     -21.973  15.584 -38.466  1.00 42.51           C  
ATOM    592  O   TYR A  82     -21.221  16.226 -39.211  1.00 45.41           O  
ATOM    593  CB  TYR A  82     -24.075  14.684 -39.498  1.00 37.64           C  
ATOM    594  CG  TYR A  82     -24.071  15.596 -40.704  1.00 43.44           C  
ATOM    595  CD1 TYR A  82     -23.637  15.136 -41.943  1.00 40.25           C  
ATOM    596  CD2 TYR A  82     -24.504  16.915 -40.605  1.00 46.32           C  
ATOM    597  CE1 TYR A  82     -23.636  15.965 -43.057  1.00 47.33           C  
ATOM    598  CE2 TYR A  82     -24.502  17.759 -41.717  1.00 46.15           C  
ATOM    599  CZ  TYR A  82     -24.070  17.278 -42.934  1.00 53.28           C  
ATOM    600  OH  TYR A  82     -24.077  18.110 -44.040  1.00 70.59           O  
ATOM    601  N   LEU A  83     -22.211  15.919 -37.197  1.00 32.99           N  
ATOM    602  CA  LEU A  83     -21.510  17.023 -36.544  1.00 33.78           C  
ATOM    603  C   LEU A  83     -20.012  16.753 -36.415  1.00 34.66           C  
ATOM    604  O   LEU A  83     -19.213  17.682 -36.456  1.00 42.60           O  
ATOM    605  CB  LEU A  83     -22.102  17.304 -35.167  1.00 42.12           C  
ATOM    606  CG  LEU A  83     -23.562  17.762 -35.129  1.00 47.25           C  
ATOM    607  CD1 LEU A  83     -23.952  18.084 -33.679  1.00 36.68           C  
ATOM    608  CD2 LEU A  83     -23.763  18.968 -36.023  1.00 35.51           C  
ATOM    609  N   LEU A  84     -19.637  15.483 -36.290  1.00 33.05           N  
ATOM    610  CA  LEU A  84     -18.230  15.091 -36.163  1.00 35.88           C  
ATOM    611  C   LEU A  84     -17.572  14.902 -37.522  1.00 42.39           C  
ATOM    612  O   LEU A  84     -16.345  14.889 -37.641  1.00 40.11           O  
ATOM    613  CB  LEU A  84     -18.111  13.776 -35.387  1.00 32.24           C  
ATOM    614  CG  LEU A  84     -18.730  13.789 -34.002  1.00 39.85           C  
ATOM    615  CD1 LEU A  84     -18.774  12.374 -33.402  1.00 39.53           C  
ATOM    616  CD2 LEU A  84     -17.934  14.737 -33.079  1.00 40.36           C  
ATOM    617  N   TRP A  85     -18.403  14.764 -38.547  1.00 31.36           N  
ATOM    618  CA  TRP A  85     -17.932  14.449 -39.884  1.00 46.59           C  
ATOM    619  C   TRP A  85     -19.039  14.788 -40.877  1.00 42.66           C  
ATOM    620  O   TRP A  85     -19.924  13.975 -41.131  1.00 42.50           O  
ATOM    621  CB  TRP A  85     -17.549  12.966 -39.957  1.00 44.93           C  
ATOM    622  CG  TRP A  85     -17.030  12.532 -41.284  1.00 49.20           C  
ATOM    623  CD1 TRP A  85     -16.378  13.302 -42.201  1.00 45.52           C  
ATOM    624  CD2 TRP A  85     -17.088  11.210 -41.834  1.00 56.45           C  
ATOM    625  NE1 TRP A  85     -16.039  12.544 -43.294  1.00 45.22           N  
ATOM    626  CE2 TRP A  85     -16.464  11.257 -43.097  1.00 55.69           C  
ATOM    627  CE3 TRP A  85     -17.611   9.993 -41.380  1.00 52.78           C  
ATOM    628  CZ2 TRP A  85     -16.349  10.131 -43.919  1.00 51.34           C  
ATOM    629  CZ3 TRP A  85     -17.499   8.877 -42.194  1.00 60.62           C  
ATOM    630  CH2 TRP A  85     -16.876   8.954 -43.455  1.00 62.92           C  
ATOM    631  N   ARG A  86     -18.995  16.006 -41.405  1.00 38.23           N  
ATOM    632  CA  ARG A  86     -20.057  16.514 -42.265  1.00 47.09           C  
ATOM    633  C   ARG A  86     -20.064  15.843 -43.632  1.00 52.85           C  
ATOM    634  O   ARG A  86     -19.660  16.432 -44.635  1.00 49.36           O  
ATOM    635  CB  ARG A  86     -19.934  18.020 -42.442  1.00 47.75           C  
ATOM    636  CG  ARG A  86     -20.059  18.783 -41.150  1.00 62.64           C  
ATOM    637  CD  ARG A  86     -20.939  19.986 -41.344  1.00 68.47           C  
ATOM    638  NE  ARG A  86     -21.395  20.513 -40.063  1.00 78.30           N  
ATOM    639  CZ  ARG A  86     -22.547  21.152 -39.886  1.00 83.02           C  
ATOM    640  NH1 ARG A  86     -23.372  21.332 -40.911  1.00 64.29           N  
ATOM    641  NH2 ARG A  86     -22.874  21.600 -38.680  1.00 80.24           N  
ATOM    642  N   ASN A  87     -20.560  14.615 -43.652  1.00 53.67           N  
ATOM    643  CA  ASN A  87     -20.534  13.767 -44.825  1.00 54.01           C  
ATOM    644  C   ASN A  87     -21.772  12.879 -44.782  1.00 58.15           C  
ATOM    645  O   ASN A  87     -22.158  12.398 -43.709  1.00 43.05           O  
ATOM    646  CB  ASN A  87     -19.253  12.929 -44.802  1.00 48.62           C  
ATOM    647  CG  ASN A  87     -19.102  12.066 -46.019  1.00 60.49           C  
ATOM    648  OD1 ASN A  87     -19.828  11.086 -46.187  1.00 57.79           O  
ATOM    649  ND2 ASN A  87     -18.149  12.415 -46.879  1.00 53.94           N  
ATOM    650  N   ARG A  88     -22.413  12.685 -45.931  1.00 49.47           N  
ATOM    651  CA  ARG A  88     -23.655  11.917 -45.982  1.00 51.40           C  
ATOM    652  C   ARG A  88     -23.491  10.520 -45.411  1.00 49.42           C  
ATOM    653  O   ARG A  88     -24.423   9.974 -44.831  1.00 50.16           O  
ATOM    654  CB  ARG A  88     -24.185  11.817 -47.419  1.00 68.95           C  
ATOM    655  CG  ARG A  88     -25.487  11.025 -47.541  1.00 74.58           C  
ATOM    656  CD  ARG A  88     -26.275  11.379 -48.805  1.00 82.00           C  
ATOM    657  NE  ARG A  88     -26.598  12.805 -48.902  1.00 80.47           N  
ATOM    658  CZ  ARG A  88     -27.467  13.442 -48.118  1.00 87.07           C  
ATOM    659  NH1 ARG A  88     -28.100  12.791 -47.150  1.00 78.34           N  
ATOM    660  NH2 ARG A  88     -27.695  14.739 -48.295  1.00 85.36           N  
ATOM    661  N   PHE A  89     -22.308   9.943 -45.587  1.00 39.58           N  
ATOM    662  CA  PHE A  89     -22.058   8.597 -45.117  1.00 41.29           C  
ATOM    663  C   PHE A  89     -21.990   8.586 -43.597  1.00 47.58           C  
ATOM    664  O   PHE A  89     -22.217   7.560 -42.968  1.00 42.11           O  
ATOM    665  CB  PHE A  89     -20.763   8.044 -45.703  1.00 45.72           C  
ATOM    666  CG  PHE A  89     -20.472   6.632 -45.289  1.00 68.21           C  
ATOM    667  CD1 PHE A  89     -21.380   5.609 -45.563  1.00 73.63           C  
ATOM    668  CD2 PHE A  89     -19.291   6.318 -44.631  1.00 67.73           C  
ATOM    669  CE1 PHE A  89     -21.115   4.297 -45.179  1.00 67.39           C  
ATOM    670  CE2 PHE A  89     -19.016   5.009 -44.247  1.00 66.31           C  
ATOM    671  CZ  PHE A  89     -19.930   3.998 -44.521  1.00 72.11           C  
ATOM    672  N   ALA A  90     -21.666   9.736 -43.013  1.00 49.19           N  
ATOM    673  CA  ALA A  90     -21.638   9.873 -41.564  1.00 43.01           C  
ATOM    674  C   ALA A  90     -23.053   9.760 -41.005  1.00 38.10           C  
ATOM    675  O   ALA A  90     -23.282   9.068 -40.014  1.00 36.13           O  
ATOM    676  CB  ALA A  90     -21.017  11.195 -41.169  1.00 39.18           C  
ATOM    677  N   LYS A  91     -23.995  10.440 -41.654  1.00 37.24           N  
ATOM    678  CA  LYS A  91     -25.399  10.359 -41.272  1.00 44.79           C  
ATOM    679  C   LYS A  91     -25.895   8.916 -41.314  1.00 42.57           C  
ATOM    680  O   LYS A  91     -26.656   8.478 -40.447  1.00 34.18           O  
ATOM    681  CB  LYS A  91     -26.257  11.205 -42.210  1.00 41.30           C  
ATOM    682  CG  LYS A  91     -26.553  12.603 -41.714  1.00 48.74           C  
ATOM    683  CD  LYS A  91     -27.238  13.434 -42.786  1.00 53.19           C  
ATOM    684  CE  LYS A  91     -27.772  14.731 -42.193  1.00 71.84           C  
ATOM    685  NZ  LYS A  91     -27.927  15.820 -43.207  1.00 63.58           N  
ATOM    686  N   ILE A  92     -25.465   8.182 -42.331  1.00 35.74           N  
ATOM    687  CA AILE A  92     -25.874   6.797 -42.528  0.70 39.25           C  
ATOM    688  CA BILE A  92     -25.935   6.812 -42.485  0.30 39.16           C  
ATOM    689  C   ILE A  92     -25.301   5.865 -41.467  1.00 35.14           C  
ATOM    690  O   ILE A  92     -25.987   4.999 -40.930  1.00 33.95           O  
ATOM    691  CB AILE A  92     -25.444   6.298 -43.920  0.70 41.22           C  
ATOM    692  CB BILE A  92     -25.760   6.270 -43.918  0.30 40.44           C  
ATOM    693  CG1AILE A  92     -26.503   6.669 -44.951  0.70 35.76           C  
ATOM    694  CG1BILE A  92     -26.540   4.959 -44.079  0.30 33.37           C  
ATOM    695  CG2AILE A  92     -25.202   4.785 -43.901  0.70 36.43           C  
ATOM    696  CG2BILE A  92     -24.295   6.057 -44.230  0.30 40.40           C  
ATOM    697  CD1AILE A  92     -26.533   8.136 -45.311  0.70 47.58           C  
ATOM    698  CD1BILE A  92     -28.046   5.135 -44.011  0.30 31.26           C  
ATOM    699  N   LEU A  93     -24.013   6.023 -41.189  1.00 36.08           N  
ATOM    700  CA  LEU A  93     -23.415   5.247 -40.116  1.00 36.26           C  
ATOM    701  C   LEU A  93     -24.116   5.637 -38.820  1.00 31.64           C  
ATOM    702  O   LEU A  93     -24.272   4.821 -37.914  1.00 31.75           O  
ATOM    703  CB  LEU A  93     -21.921   5.518 -39.992  1.00 41.12           C  
ATOM    704  CG  LEU A  93     -21.040   4.732 -40.956  1.00 52.79           C  
ATOM    705  CD1 LEU A  93     -19.580   4.985 -40.629  1.00 60.60           C  
ATOM    706  CD2 LEU A  93     -21.353   3.265 -40.826  1.00 53.54           C  
ATOM    707  N   GLY A  94     -24.545   6.896 -38.754  1.00 29.16           N  
ATOM    708  CA  GLY A  94     -25.212   7.427 -37.577  1.00 27.78           C  
ATOM    709  C   GLY A  94     -26.558   6.757 -37.383  1.00 35.78           C  
ATOM    710  O   GLY A  94     -27.005   6.531 -36.250  1.00 27.47           O  
ATOM    711  N   VAL A  95     -27.212   6.434 -38.497  1.00 29.62           N  
ATOM    712  CA  VAL A  95     -28.508   5.764 -38.432  1.00 31.25           C  
ATOM    713  C   VAL A  95     -28.334   4.419 -37.729  1.00 27.33           C  
ATOM    714  O   VAL A  95     -29.159   4.007 -36.927  1.00 29.98           O  
ATOM    715  CB  VAL A  95     -29.116   5.534 -39.837  1.00 29.57           C  
ATOM    716  CG1 VAL A  95     -30.270   4.545 -39.772  1.00 30.30           C  
ATOM    717  CG2 VAL A  95     -29.557   6.854 -40.440  1.00 29.76           C  
ATOM    718  N   PHE A  96     -27.239   3.742 -38.037  1.00 26.42           N  
ATOM    719  CA  PHE A  96     -26.954   2.448 -37.451  1.00 29.04           C  
ATOM    720  C   PHE A  96     -26.906   2.548 -35.925  1.00 29.06           C  
ATOM    721  O   PHE A  96     -27.321   1.634 -35.210  1.00 30.01           O  
ATOM    722  CB  PHE A  96     -25.636   1.922 -38.021  1.00 34.39           C  
ATOM    723  CG  PHE A  96     -25.427   0.461 -37.815  1.00 37.02           C  
ATOM    724  CD1 PHE A  96     -24.609   0.011 -36.795  1.00 43.37           C  
ATOM    725  CD2 PHE A  96     -26.036  -0.473 -38.655  1.00 36.40           C  
ATOM    726  CE1 PHE A  96     -24.398  -1.346 -36.600  1.00 46.07           C  
ATOM    727  CE2 PHE A  96     -25.838  -1.830 -38.458  1.00 42.45           C  
ATOM    728  CZ  PHE A  96     -25.017  -2.270 -37.424  1.00 40.42           C  
ATOM    729  N   GLY A  97     -26.420   3.677 -35.424  1.00 33.54           N  
ATOM    730  CA  GLY A  97     -26.288   3.873 -33.992  1.00 26.12           C  
ATOM    731  C   GLY A  97     -27.593   4.168 -33.289  1.00 31.85           C  
ATOM    732  O   GLY A  97     -27.658   4.130 -32.046  1.00 35.08           O  
ATOM    733  N   LEU A  98     -28.630   4.492 -34.057  1.00 24.60           N  
ATOM    734  CA  LEU A  98     -29.971   4.673 -33.486  1.00 26.23           C  
ATOM    735  C   LEU A  98     -30.803   3.405 -33.671  1.00 30.59           C  
ATOM    736  O   LEU A  98     -31.653   3.068 -32.849  1.00 30.49           O  
ATOM    737  CB  LEU A  98     -30.686   5.843 -34.143  1.00 26.00           C  
ATOM    738  CG  LEU A  98     -32.132   6.170 -33.762  1.00 26.01           C  
ATOM    739  CD1 LEU A  98     -32.256   6.480 -32.278  1.00 33.85           C  
ATOM    740  CD2 LEU A  98     -32.586   7.380 -34.604  1.00 27.09           C  
ATOM    741  N   TRP A  99     -30.539   2.708 -34.764  1.00 29.08           N  
ATOM    742  CA  TRP A  99     -31.163   1.420 -35.042  1.00 26.74           C  
ATOM    743  C   TRP A  99     -30.828   0.367 -33.959  1.00 24.72           C  
ATOM    744  O   TRP A  99     -31.694  -0.376 -33.510  1.00 25.06           O  
ATOM    745  CB  TRP A  99     -30.749   0.983 -36.446  1.00 22.84           C  
ATOM    746  CG  TRP A  99     -31.148  -0.424 -36.876  1.00 29.00           C  
ATOM    747  CD1 TRP A  99     -32.350  -0.832 -37.415  1.00 24.43           C  
ATOM    748  CD2 TRP A  99     -30.311  -1.576 -36.852  1.00 24.37           C  
ATOM    749  NE1 TRP A  99     -32.307  -2.171 -37.701  1.00 20.67           N  
ATOM    750  CE2 TRP A  99     -31.064  -2.653 -37.377  1.00 27.50           C  
ATOM    751  CE3 TRP A  99     -28.998  -1.809 -36.425  1.00 21.11           C  
ATOM    752  CZ2 TRP A  99     -30.545  -3.957 -37.468  1.00 21.90           C  
ATOM    753  CZ3 TRP A  99     -28.474  -3.103 -36.543  1.00 29.78           C  
ATOM    754  CH2 TRP A  99     -29.255  -4.162 -37.055  1.00 22.06           C  
ATOM    755  N   ILE A 100     -29.573   0.320 -33.529  1.00 25.64           N  
ATOM    756  CA  ILE A 100     -29.166  -0.616 -32.476  1.00 26.82           C  
ATOM    757  C   ILE A 100     -30.049  -0.543 -31.218  1.00 24.41           C  
ATOM    758  O   ILE A 100     -30.625  -1.549 -30.822  1.00 23.96           O  
ATOM    759  CB  ILE A 100     -27.696  -0.425 -32.097  1.00 29.46           C  
ATOM    760  CG1 ILE A 100     -26.794  -0.974 -33.208  1.00 26.04           C  
ATOM    761  CG2 ILE A 100     -27.394  -1.073 -30.731  1.00 22.10           C  
ATOM    762  CD1 ILE A 100     -25.320  -0.536 -33.027  1.00 29.24           C  
ATOM    763  N   PRO A 101     -30.180   0.652 -30.600  1.00 27.33           N  
ATOM    764  CA  PRO A 101     -30.974   0.671 -29.362  1.00 30.95           C  
ATOM    765  C   PRO A 101     -32.467   0.482 -29.618  1.00 29.51           C  
ATOM    766  O   PRO A 101     -33.177   0.007 -28.742  1.00 27.92           O  
ATOM    767  CB  PRO A 101     -30.703   2.075 -28.784  1.00 28.07           C  
ATOM    768  CG  PRO A 101     -30.229   2.897 -30.009  1.00 24.90           C  
ATOM    769  CD  PRO A 101     -29.417   1.904 -30.780  1.00 25.44           C  
ATOM    770  N   LEU A 102     -32.943   0.883 -30.785  1.00 24.61           N  
ATOM    771  CA  LEU A 102     -34.320   0.584 -31.150  1.00 28.39           C  
ATOM    772  C   LEU A 102     -34.525  -0.938 -31.226  1.00 27.70           C  
ATOM    773  O   LEU A 102     -35.478  -1.474 -30.666  1.00 27.72           O  
ATOM    774  CB  LEU A 102     -34.679   1.227 -32.497  1.00 32.48           C  
ATOM    775  CG  LEU A 102     -36.026   0.816 -33.106  1.00 33.83           C  
ATOM    776  CD1 LEU A 102     -37.158   1.183 -32.170  1.00 30.73           C  
ATOM    777  CD2 LEU A 102     -36.228   1.458 -34.499  1.00 26.54           C  
ATOM    778  N   VAL A 103     -33.642  -1.634 -31.929  1.00 27.36           N  
ATOM    779  CA  VAL A 103     -33.808  -3.081 -32.060  1.00 25.15           C  
ATOM    780  C   VAL A 103     -33.652  -3.754 -30.696  1.00 28.57           C  
ATOM    781  O   VAL A 103     -34.404  -4.671 -30.361  1.00 25.97           O  
ATOM    782  CB  VAL A 103     -32.857  -3.705 -33.086  1.00 26.96           C  
ATOM    783  CG1 VAL A 103     -32.941  -5.246 -33.037  1.00 28.93           C  
ATOM    784  CG2 VAL A 103     -33.207  -3.216 -34.512  1.00 27.25           C  
ATOM    785  N   VAL A 104     -32.691  -3.286 -29.902  1.00 25.45           N  
ATOM    786  CA  VAL A 104     -32.460  -3.887 -28.597  1.00 21.64           C  
ATOM    787  C   VAL A 104     -33.663  -3.686 -27.680  1.00 25.49           C  
ATOM    788  O   VAL A 104     -34.084  -4.614 -26.985  1.00 27.75           O  
ATOM    789  CB  VAL A 104     -31.159  -3.370 -27.918  1.00 23.43           C  
ATOM    790  CG1 VAL A 104     -31.056  -3.893 -26.512  1.00 26.19           C  
ATOM    791  CG2 VAL A 104     -29.931  -3.810 -28.701  1.00 25.81           C  
ATOM    792  N   ALA A 105     -34.219  -2.473 -27.678  1.00 24.98           N  
ATOM    793  CA  ALA A 105     -35.412  -2.189 -26.888  1.00 23.21           C  
ATOM    794  C   ALA A 105     -36.490  -3.217 -27.223  1.00 26.72           C  
ATOM    795  O   ALA A 105     -37.267  -3.656 -26.363  1.00 31.28           O  
ATOM    796  CB  ALA A 105     -35.923  -0.774 -27.186  1.00 21.63           C  
ATOM    797  N   ILE A 106     -36.524  -3.590 -28.488  1.00 24.97           N  
ATOM    798  CA  ILE A 106     -37.601  -4.394 -29.037  1.00 25.02           C  
ATOM    799  C   ILE A 106     -37.584  -5.812 -28.507  1.00 30.01           C  
ATOM    800  O   ILE A 106     -38.638  -6.450 -28.394  1.00 26.90           O  
ATOM    801  CB  ILE A 106     -37.563  -4.381 -30.569  1.00 25.53           C  
ATOM    802  CG1 ILE A 106     -38.081  -3.015 -31.063  1.00 21.32           C  
ATOM    803  CG2 ILE A 106     -38.390  -5.529 -31.124  1.00 25.71           C  
ATOM    804  CD1 ILE A 106     -37.779  -2.728 -32.531  1.00 24.04           C  
ATOM    805  N   TYR A 107     -36.402  -6.307 -28.148  1.00 24.02           N  
ATOM    806  CA  TYR A 107     -36.384  -7.539 -27.365  1.00 28.33           C  
ATOM    807  C   TYR A 107     -36.134  -7.382 -25.862  1.00 28.03           C  
ATOM    808  O   TYR A 107     -36.517  -8.261 -25.080  1.00 28.28           O  
ATOM    809  CB  TYR A 107     -35.456  -8.593 -27.965  1.00 28.16           C  
ATOM    810  CG  TYR A 107     -33.980  -8.266 -27.952  1.00 26.17           C  
ATOM    811  CD1 TYR A 107     -33.153  -8.701 -26.927  1.00 31.56           C  
ATOM    812  CD2 TYR A 107     -33.400  -7.566 -28.998  1.00 28.10           C  
ATOM    813  CE1 TYR A 107     -31.787  -8.423 -26.938  1.00 31.06           C  
ATOM    814  CE2 TYR A 107     -32.054  -7.279 -29.010  1.00 26.63           C  
ATOM    815  CZ  TYR A 107     -31.244  -7.719 -28.000  1.00 26.85           C  
ATOM    816  OH  TYR A 107     -29.891  -7.424 -28.042  1.00 31.31           O  
ATOM    817  N   TYR A 108     -35.486  -6.296 -25.442  1.00 29.75           N  
ATOM    818  CA  TYR A 108     -35.040  -6.237 -24.045  1.00 24.33           C  
ATOM    819  C   TYR A 108     -36.201  -6.011 -23.101  1.00 25.55           C  
ATOM    820  O   TYR A 108     -36.220  -6.555 -22.011  1.00 26.94           O  
ATOM    821  CB  TYR A 108     -33.944  -5.184 -23.819  1.00 24.86           C  
ATOM    822  CG  TYR A 108     -33.281  -5.246 -22.440  1.00 24.59           C  
ATOM    823  CD1 TYR A 108     -32.287  -6.183 -22.160  1.00 27.71           C  
ATOM    824  CD2 TYR A 108     -33.646  -4.360 -21.428  1.00 25.82           C  
ATOM    825  CE1 TYR A 108     -31.674  -6.232 -20.895  1.00 31.01           C  
ATOM    826  CE2 TYR A 108     -33.049  -4.396 -20.178  1.00 25.07           C  
ATOM    827  CZ  TYR A 108     -32.070  -5.335 -19.916  1.00 25.99           C  
ATOM    828  OH  TYR A 108     -31.469  -5.360 -18.686  1.00 30.07           O  
ATOM    829  N   VAL A 109     -37.184  -5.221 -23.513  1.00 25.27           N  
ATOM    830  CA  VAL A 109     -38.266  -4.918 -22.584  1.00 28.42           C  
ATOM    831  C   VAL A 109     -39.053  -6.202 -22.294  1.00 29.40           C  
ATOM    832  O   VAL A 109     -39.548  -6.408 -21.188  1.00 25.88           O  
ATOM    833  CB  VAL A 109     -39.185  -3.785 -23.073  1.00 27.21           C  
ATOM    834  CG1 VAL A 109     -40.260  -3.508 -22.034  1.00 30.09           C  
ATOM    835  CG2 VAL A 109     -38.380  -2.518 -23.349  1.00 24.58           C  
ATOM    836  N   TYR A 110     -39.146  -7.073 -23.290  1.00 22.78           N  
ATOM    837  CA  TYR A 110     -39.800  -8.364 -23.106  1.00 25.92           C  
ATOM    838  C   TYR A 110     -39.034  -9.241 -22.107  1.00 27.31           C  
ATOM    839  O   TYR A 110     -39.627  -9.862 -21.211  1.00 27.18           O  
ATOM    840  CB  TYR A 110     -39.974  -9.072 -24.468  1.00 25.55           C  
ATOM    841  CG  TYR A 110     -40.810 -10.328 -24.389  1.00 28.70           C  
ATOM    842  CD1 TYR A 110     -42.017 -10.335 -23.690  1.00 27.79           C  
ATOM    843  CD2 TYR A 110     -40.394 -11.509 -25.000  1.00 25.94           C  
ATOM    844  CE1 TYR A 110     -42.796 -11.499 -23.615  1.00 32.07           C  
ATOM    845  CE2 TYR A 110     -41.158 -12.664 -24.931  1.00 24.31           C  
ATOM    846  CZ  TYR A 110     -42.357 -12.653 -24.247  1.00 32.89           C  
ATOM    847  OH  TYR A 110     -43.111 -13.800 -24.181  1.00 34.44           O  
ATOM    848  N   ILE A 111     -37.712  -9.288 -22.242  1.00 24.19           N  
ATOM    849  CA  ILE A 111     -36.884 -10.010 -21.270  1.00 27.02           C  
ATOM    850  C   ILE A 111     -37.121  -9.459 -19.858  1.00 31.23           C  
ATOM    851  O   ILE A 111     -37.332 -10.200 -18.894  1.00 28.61           O  
ATOM    852  CB  ILE A 111     -35.394  -9.863 -21.606  1.00 26.39           C  
ATOM    853  CG1 ILE A 111     -35.053 -10.696 -22.848  1.00 27.03           C  
ATOM    854  CG2 ILE A 111     -34.539 -10.279 -20.412  1.00 28.99           C  
ATOM    855  CD1 ILE A 111     -33.666 -10.422 -23.384  1.00 28.03           C  
ATOM    856  N   GLU A 112     -37.090  -8.143 -19.754  1.00 30.93           N  
ATOM    857  CA  GLU A 112     -37.405  -7.478 -18.512  1.00 30.97           C  
ATOM    858  C   GLU A 112     -38.779  -7.896 -17.974  1.00 27.87           C  
ATOM    859  O   GLU A 112     -38.944  -8.146 -16.769  1.00 23.97           O  
ATOM    860  CB  GLU A 112     -37.342  -5.971 -18.718  1.00 26.15           C  
ATOM    861  CG  GLU A 112     -37.760  -5.157 -17.524  1.00 30.72           C  
ATOM    862  CD  GLU A 112     -37.580  -3.680 -17.789  1.00 31.87           C  
ATOM    863  OE1 GLU A 112     -36.477  -3.301 -18.249  1.00 31.14           O  
ATOM    864  OE2 GLU A 112     -38.533  -2.905 -17.546  1.00 30.89           O  
ATOM    865  N   SER A 113     -39.773  -7.965 -18.849  1.00 25.65           N  
ATOM    866  CA  SER A 113     -41.106  -8.307 -18.368  1.00 28.02           C  
ATOM    867  C   SER A 113     -41.113  -9.677 -17.667  1.00 27.25           C  
ATOM    868  O   SER A 113     -41.867  -9.883 -16.699  1.00 28.41           O  
ATOM    869  CB  SER A 113     -42.143  -8.253 -19.486  1.00 24.18           C  
ATOM    870  OG  SER A 113     -41.952  -9.304 -20.420  1.00 28.00           O  
ATOM    871  N   TRP A 114     -40.270 -10.601 -18.140  1.00 29.49           N  
ATOM    872  CA  TRP A 114     -40.229 -11.930 -17.537  1.00 27.03           C  
ATOM    873  C   TRP A 114     -39.803 -11.848 -16.079  1.00 29.65           C  
ATOM    874  O   TRP A 114     -40.277 -12.641 -15.263  1.00 28.63           O  
ATOM    875  CB  TRP A 114     -39.254 -12.887 -18.216  1.00 22.32           C  
ATOM    876  CG  TRP A 114     -39.319 -13.000 -19.688  1.00 27.63           C  
ATOM    877  CD1 TRP A 114     -40.391 -12.737 -20.512  1.00 25.81           C  
ATOM    878  CD2 TRP A 114     -38.262 -13.452 -20.532  1.00 32.51           C  
ATOM    879  NE1 TRP A 114     -40.038 -12.977 -21.825  1.00 25.99           N  
ATOM    880  CE2 TRP A 114     -38.741 -13.421 -21.863  1.00 31.36           C  
ATOM    881  CE3 TRP A 114     -36.950 -13.869 -20.294  1.00 30.68           C  
ATOM    882  CZ2 TRP A 114     -37.951 -13.795 -22.945  1.00 34.30           C  
ATOM    883  CZ3 TRP A 114     -36.166 -14.233 -21.370  1.00 37.60           C  
ATOM    884  CH2 TRP A 114     -36.669 -14.196 -22.681  1.00 29.89           C  
ATOM    885  N   THR A 115     -38.889 -10.926 -15.752  1.00 27.78           N  
ATOM    886  CA  THR A 115     -38.396 -10.849 -14.368  1.00 27.06           C  
ATOM    887  C   THR A 115     -39.515 -10.324 -13.475  1.00 30.37           C  
ATOM    888  O   THR A 115     -39.668 -10.764 -12.340  1.00 30.45           O  
ATOM    889  CB  THR A 115     -37.109  -9.986 -14.189  1.00 28.30           C  
ATOM    890  OG1 THR A 115     -37.372  -8.617 -14.516  1.00 27.16           O  
ATOM    891  CG2 THR A 115     -35.951 -10.523 -15.054  1.00 24.18           C  
ATOM    892  N   LEU A 116     -40.323  -9.413 -14.011  1.00 28.16           N  
ATOM    893  CA  LEU A 116     -41.454  -8.889 -13.267  1.00 28.59           C  
ATOM    894  C   LEU A 116     -42.512  -9.979 -13.049  1.00 35.93           C  
ATOM    895  O   LEU A 116     -43.062 -10.120 -11.949  1.00 31.05           O  
ATOM    896  CB  LEU A 116     -42.048  -7.658 -13.964  1.00 25.66           C  
ATOM    897  CG  LEU A 116     -43.304  -7.121 -13.272  1.00 28.26           C  
ATOM    898  CD1 LEU A 116     -43.037  -6.802 -11.770  1.00 28.01           C  
ATOM    899  CD2 LEU A 116     -43.880  -5.926 -13.995  1.00 24.83           C  
ATOM    900  N   GLY A 117     -42.781 -10.759 -14.091  1.00 32.23           N  
ATOM    901  CA  GLY A 117     -43.761 -11.821 -13.986  1.00 31.73           C  
ATOM    902  C   GLY A 117     -43.327 -12.853 -12.962  1.00 33.74           C  
ATOM    903  O   GLY A 117     -44.135 -13.341 -12.174  1.00 30.27           O  
ATOM    904  N   PHE A 118     -42.044 -13.200 -12.986  1.00 26.51           N  
ATOM    905  CA  PHE A 118     -41.503 -14.153 -12.022  1.00 32.53           C  
ATOM    906  C   PHE A 118     -41.482 -13.570 -10.598  1.00 32.88           C  
ATOM    907  O   PHE A 118     -41.678 -14.292  -9.634  1.00 32.49           O  
ATOM    908  CB  PHE A 118     -40.103 -14.602 -12.435  1.00 27.82           C  
ATOM    909  CG  PHE A 118     -40.091 -15.743 -13.417  1.00 34.99           C  
ATOM    910  CD1 PHE A 118     -40.771 -15.651 -14.624  1.00 37.61           C  
ATOM    911  CD2 PHE A 118     -39.375 -16.900 -13.141  1.00 35.30           C  
ATOM    912  CE1 PHE A 118     -40.758 -16.703 -15.539  1.00 39.13           C  
ATOM    913  CE2 PHE A 118     -39.348 -17.950 -14.043  1.00 38.98           C  
ATOM    914  CZ  PHE A 118     -40.043 -17.852 -15.258  1.00 36.75           C  
ATOM    915  N   ALA A 119     -41.238 -12.270 -10.463  1.00 31.67           N  
ATOM    916  CA  ALA A 119     -41.252 -11.660  -9.133  1.00 31.89           C  
ATOM    917  C   ALA A 119     -42.655 -11.769  -8.526  1.00 35.18           C  
ATOM    918  O   ALA A 119     -42.824 -12.196  -7.370  1.00 33.51           O  
ATOM    919  CB  ALA A 119     -40.803 -10.219  -9.198  1.00 29.07           C  
ATOM    920  N   ILE A 120     -43.657 -11.403  -9.321  1.00 31.70           N  
ATOM    921  CA  ILE A 120     -45.052 -11.525  -8.907  1.00 31.41           C  
ATOM    922  C   ILE A 120     -45.418 -12.962  -8.513  1.00 37.53           C  
ATOM    923  O   ILE A 120     -45.946 -13.195  -7.416  1.00 32.48           O  
ATOM    924  CB  ILE A 120     -46.014 -11.068 -10.014  1.00 37.48           C  
ATOM    925  CG1 ILE A 120     -45.872  -9.560 -10.272  1.00 31.62           C  
ATOM    926  CG2 ILE A 120     -47.458 -11.452  -9.653  1.00 36.21           C  
ATOM    927  CD1 ILE A 120     -46.418  -9.130 -11.657  1.00 35.91           C  
ATOM    928  N   LYS A 121     -45.128 -13.918  -9.398  1.00 28.82           N  
ATOM    929  CA  LYS A 121     -45.440 -15.322  -9.146  1.00 31.85           C  
ATOM    930  C   LYS A 121     -44.761 -15.838  -7.871  1.00 44.23           C  
ATOM    931  O   LYS A 121     -45.367 -16.558  -7.077  1.00 30.35           O  
ATOM    932  CB  LYS A 121     -45.018 -16.192 -10.326  1.00 32.08           C  
ATOM    933  CG  LYS A 121     -45.741 -15.855 -11.628  1.00 50.20           C  
ATOM    934  CD  LYS A 121     -47.161 -16.403 -11.652  1.00 44.73           C  
ATOM    935  CE  LYS A 121     -47.171 -17.901 -11.903  1.00 56.71           C  
ATOM    936  NZ  LYS A 121     -46.873 -18.248 -13.325  1.00 61.77           N  
ATOM    937  N   PHE A 122     -43.491 -15.483  -7.708  1.00 30.49           N  
ATOM    938  CA  PHE A 122     -42.733 -15.889  -6.547  1.00 35.08           C  
ATOM    939  C   PHE A 122     -43.238 -15.204  -5.274  1.00 36.92           C  
ATOM    940  O   PHE A 122     -43.358 -15.846  -4.243  1.00 36.22           O  
ATOM    941  CB  PHE A 122     -41.236 -15.663  -6.760  1.00 32.60           C  
ATOM    942  CG  PHE A 122     -40.510 -16.890  -7.245  1.00 29.81           C  
ATOM    943  CD1 PHE A 122     -40.348 -17.128  -8.601  1.00 38.28           C  
ATOM    944  CD2 PHE A 122     -40.002 -17.806  -6.339  1.00 36.14           C  
ATOM    945  CE1 PHE A 122     -39.686 -18.258  -9.049  1.00 41.72           C  
ATOM    946  CE2 PHE A 122     -39.338 -18.940  -6.771  1.00 39.67           C  
ATOM    947  CZ  PHE A 122     -39.181 -19.169  -8.133  1.00 47.66           C  
ATOM    948  N   LEU A 123     -43.567 -13.921  -5.367  1.00 35.20           N  
ATOM    949  CA  LEU A 123     -44.139 -13.204  -4.237  1.00 39.74           C  
ATOM    950  C   LEU A 123     -45.406 -13.864  -3.698  1.00 42.69           C  
ATOM    951  O   LEU A 123     -45.560 -14.036  -2.493  1.00 39.61           O  
ATOM    952  CB  LEU A 123     -44.445 -11.745  -4.603  1.00 36.58           C  
ATOM    953  CG  LEU A 123     -45.112 -10.952  -3.470  1.00 36.19           C  
ATOM    954  CD1 LEU A 123     -44.235 -10.946  -2.215  1.00 32.98           C  
ATOM    955  CD2 LEU A 123     -45.460  -9.536  -3.899  1.00 31.56           C  
ATOM    956  N   VAL A 124     -46.325 -14.221  -4.585  1.00 39.65           N  
ATOM    957  CA  VAL A 124     -47.593 -14.792  -4.137  1.00 38.37           C  
ATOM    958  C   VAL A 124     -47.505 -16.298  -3.967  1.00 37.57           C  
ATOM    959  O   VAL A 124     -48.469 -16.936  -3.546  1.00 37.61           O  
ATOM    960  CB  VAL A 124     -48.741 -14.439  -5.093  1.00 41.04           C  
ATOM    961  CG1 VAL A 124     -48.891 -12.933  -5.175  1.00 37.03           C  
ATOM    962  CG2 VAL A 124     -48.480 -15.031  -6.467  1.00 38.16           C  
ATOM    963  N   GLY A 125     -46.346 -16.867  -4.289  1.00 37.18           N  
ATOM    964  CA  GLY A 125     -46.120 -18.283  -4.072  1.00 32.46           C  
ATOM    965  C   GLY A 125     -46.737 -19.165  -5.140  1.00 42.36           C  
ATOM    966  O   GLY A 125     -46.859 -20.375  -4.969  1.00 38.00           O  
ATOM    967  N   LEU A 126     -47.124 -18.566  -6.259  1.00 37.11           N  
ATOM    968  CA  LEU A 126     -47.673 -19.341  -7.360  1.00 38.28           C  
ATOM    969  C   LEU A 126     -46.552 -19.947  -8.207  1.00 47.62           C  
ATOM    970  O   LEU A 126     -46.390 -19.621  -9.381  1.00 50.23           O  
ATOM    971  CB  LEU A 126     -48.598 -18.476  -8.202  1.00 43.16           C  
ATOM    972  CG  LEU A 126     -49.874 -18.044  -7.476  1.00 46.66           C  
ATOM    973  CD1 LEU A 126     -50.677 -17.066  -8.351  1.00 47.25           C  
ATOM    974  CD2 LEU A 126     -50.706 -19.257  -7.109  1.00 40.21           C  
ATOM    975  N   VAL A 127     -45.772 -20.831  -7.596  1.00 42.11           N  
ATOM    976  CA  VAL A 127     -44.652 -21.454  -8.282  1.00 42.07           C  
ATOM    977  C   VAL A 127     -44.698 -22.961  -8.089  1.00 43.32           C  
ATOM    978  O   VAL A 127     -45.485 -23.455  -7.282  1.00 44.16           O  
ATOM    979  CB  VAL A 127     -43.318 -20.891  -7.774  1.00 43.61           C  
ATOM    980  CG1 VAL A 127     -43.260 -19.393  -8.044  1.00 46.02           C  
ATOM    981  CG2 VAL A 127     -43.143 -21.201  -6.293  1.00 44.96           C  
ATOM    982  N   PRO A 128     -43.864 -23.700  -8.838  1.00 43.09           N  
ATOM    983  CA  PRO A 128     -43.897 -25.160  -8.729  1.00 40.27           C  
ATOM    984  C   PRO A 128     -43.344 -25.604  -7.384  1.00 56.11           C  
ATOM    985  O   PRO A 128     -42.625 -24.845  -6.731  1.00 47.42           O  
ATOM    986  CB  PRO A 128     -42.961 -25.627  -9.854  1.00 48.86           C  
ATOM    987  CG  PRO A 128     -42.693 -24.413 -10.700  1.00 40.09           C  
ATOM    988  CD  PRO A 128     -42.844 -23.240  -9.798  1.00 42.35           C  
ATOM    989  N   GLU A 129     -43.668 -26.823  -6.975  1.00 53.24           N  
ATOM    990  CA  GLU A 129     -43.153 -27.333  -5.715  1.00 64.05           C  
ATOM    991  C   GLU A 129     -42.725 -28.788  -5.816  1.00 68.99           C  
ATOM    992  O   GLU A 129     -43.541 -29.692  -5.639  1.00 93.11           O  
ATOM    993  CB  GLU A 129     -44.190 -27.137  -4.607  1.00 62.25           C  
ATOM    994  CG  GLU A 129     -44.405 -25.669  -4.257  1.00 77.75           C  
ATOM    995  CD  GLU A 129     -45.782 -25.389  -3.689  1.00 93.96           C  
ATOM    996  OE1 GLU A 129     -46.170 -26.054  -2.701  1.00 92.25           O  
ATOM    997  OE2 GLU A 129     -46.473 -24.496  -4.232  1.00 84.56           O  
ATOM    998  N   PRO A 130     -41.437 -29.018  -6.113  1.00 61.25           N  
ATOM    999  CA  PRO A 130     -40.856 -30.363  -6.093  1.00 76.63           C  
ATOM   1000  C   PRO A 130     -40.410 -30.721  -4.669  1.00 80.70           C  
ATOM   1001  O   PRO A 130     -40.237 -29.801  -3.863  1.00 83.18           O  
ATOM   1002  CB  PRO A 130     -39.629 -30.230  -6.993  1.00 65.49           C  
ATOM   1003  CG  PRO A 130     -39.257 -28.785  -6.938  1.00 58.06           C  
ATOM   1004  CD  PRO A 130     -40.456 -27.991  -6.495  1.00 62.75           C  
ATOM   1005  N   PRO A 131     -40.223 -32.022  -4.352  1.00 89.37           N  
ATOM   1006  CA  PRO A 131     -40.332 -33.252  -5.147  1.00 90.37           C  
ATOM   1007  C   PRO A 131     -41.305 -33.189  -6.321  1.00 85.55           C  
ATOM   1008  O   PRO A 131     -41.289 -34.110  -7.141  1.00 84.79           O  
ATOM   1009  CB  PRO A 131     -40.829 -34.265  -4.116  1.00 72.17           C  
ATOM   1010  CG  PRO A 131     -40.137 -33.845  -2.859  1.00 82.16           C  
ATOM   1011  CD  PRO A 131     -39.929 -32.340  -2.941  1.00 70.23           C  
ATOM   1012  N   THR A 135     -35.168 -34.898  -3.934  1.00 88.10           N  
ATOM   1013  CA  THR A 135     -34.674 -36.092  -4.608  1.00 98.26           C  
ATOM   1014  C   THR A 135     -33.376 -35.793  -5.364  1.00100.85           C  
ATOM   1015  O   THR A 135     -32.379 -35.392  -4.760  1.00 93.09           O  
ATOM   1016  CB  THR A 135     -35.735 -36.673  -5.572  1.00103.23           C  
ATOM   1017  OG1 THR A 135     -37.036 -36.550  -4.982  1.00103.51           O  
ATOM   1018  CG2 THR A 135     -35.451 -38.143  -5.874  1.00 96.28           C  
ATOM   1019  N   ASP A 136     -33.397 -35.981  -6.683  1.00103.33           N  
ATOM   1020  CA  ASP A 136     -32.215 -35.774  -7.522  1.00 92.92           C  
ATOM   1021  C   ASP A 136     -32.338 -34.531  -8.420  1.00 89.50           C  
ATOM   1022  O   ASP A 136     -33.444 -34.057  -8.674  1.00 69.63           O  
ATOM   1023  CB  ASP A 136     -31.920 -37.036  -8.339  1.00 86.25           C  
ATOM   1024  CG  ASP A 136     -31.163 -38.082  -7.535  1.00102.86           C  
ATOM   1025  OD1 ASP A 136     -30.156 -37.720  -6.887  1.00 98.39           O  
ATOM   1026  OD2 ASP A 136     -31.568 -39.265  -7.553  1.00101.57           O  
ATOM   1027  N   PRO A 137     -31.195 -34.010  -8.905  1.00 85.05           N  
ATOM   1028  CA  PRO A 137     -31.080 -32.707  -9.577  1.00 85.05           C  
ATOM   1029  C   PRO A 137     -32.160 -32.413 -10.618  1.00 76.21           C  
ATOM   1030  O   PRO A 137     -32.789 -31.360 -10.561  1.00 70.22           O  
ATOM   1031  CB  PRO A 137     -29.700 -32.790 -10.257  1.00 83.67           C  
ATOM   1032  CG  PRO A 137     -29.348 -34.253 -10.233  1.00 88.19           C  
ATOM   1033  CD  PRO A 137     -29.906 -34.716  -8.934  1.00 86.86           C  
ATOM   1034  N   ASP A 138     -32.364 -33.323 -11.561  1.00 76.58           N  
ATOM   1035  CA  ASP A 138     -33.309 -33.079 -12.644  1.00 61.73           C  
ATOM   1036  C   ASP A 138     -34.747 -33.027 -12.123  1.00 57.92           C  
ATOM   1037  O   ASP A 138     -35.601 -32.344 -12.682  1.00 51.70           O  
ATOM   1038  CB  ASP A 138     -33.160 -34.147 -13.731  1.00 67.92           C  
ATOM   1039  CG  ASP A 138     -33.327 -33.582 -15.132  1.00 93.30           C  
ATOM   1040  OD1 ASP A 138     -34.045 -34.206 -15.945  1.00 94.40           O  
ATOM   1041  OD2 ASP A 138     -32.742 -32.509 -15.418  1.00 83.18           O  
ATOM   1042  N   SER A 139     -34.998 -33.740 -11.031  1.00 65.09           N  
ATOM   1043  CA  SER A 139     -36.329 -33.828 -10.446  1.00 59.59           C  
ATOM   1044  C   SER A 139     -36.736 -32.506  -9.800  1.00 57.61           C  
ATOM   1045  O   SER A 139     -37.922 -32.240  -9.582  1.00 51.58           O  
ATOM   1046  CB  SER A 139     -36.368 -34.960  -9.411  1.00 76.85           C  
ATOM   1047  OG  SER A 139     -37.652 -35.091  -8.821  1.00 72.26           O  
ATOM   1048  N   ILE A 140     -35.746 -31.681  -9.486  1.00 43.86           N  
ATOM   1049  CA  ILE A 140     -36.011 -30.357  -8.931  1.00 57.38           C  
ATOM   1050  C   ILE A 140     -36.037 -29.293 -10.035  1.00 41.43           C  
ATOM   1051  O   ILE A 140     -36.835 -28.366  -9.994  1.00 48.75           O  
ATOM   1052  CB  ILE A 140     -34.967 -29.975  -7.861  1.00 52.46           C  
ATOM   1053  CG1 ILE A 140     -34.769 -31.145  -6.891  1.00 65.46           C  
ATOM   1054  CG2 ILE A 140     -35.390 -28.710  -7.126  1.00 48.63           C  
ATOM   1055  CD1 ILE A 140     -33.780 -30.861  -5.756  1.00 71.09           C  
ATOM   1056  N   LEU A 141     -35.168 -29.449 -11.027  1.00 40.80           N  
ATOM   1057  CA  LEU A 141     -35.065 -28.481 -12.115  1.00 41.09           C  
ATOM   1058  C   LEU A 141     -36.260 -28.530 -13.059  1.00 45.11           C  
ATOM   1059  O   LEU A 141     -36.803 -27.490 -13.429  1.00 45.11           O  
ATOM   1060  CB  LEU A 141     -33.771 -28.695 -12.902  1.00 40.84           C  
ATOM   1061  CG  LEU A 141     -32.468 -28.575 -12.106  1.00 47.13           C  
ATOM   1062  CD1 LEU A 141     -31.317 -29.117 -12.939  1.00 52.85           C  
ATOM   1063  CD2 LEU A 141     -32.199 -27.132 -11.651  1.00 40.66           C  
ATOM   1064  N   ARG A 142     -36.675 -29.735 -13.438  1.00 35.95           N  
ATOM   1065  CA  ARG A 142     -37.629 -29.891 -14.542  1.00 44.32           C  
ATOM   1066  C   ARG A 142     -38.920 -29.085 -14.352  1.00 41.42           C  
ATOM   1067  O   ARG A 142     -39.406 -28.469 -15.295  1.00 36.77           O  
ATOM   1068  CB  ARG A 142     -37.924 -31.374 -14.818  1.00 41.51           C  
ATOM   1069  CG  ARG A 142     -38.656 -31.633 -16.129  1.00 64.05           C  
ATOM   1070  CD  ARG A 142     -38.677 -33.117 -16.460  1.00 61.08           C  
ATOM   1071  NE  ARG A 142     -38.931 -33.915 -15.266  1.00 75.17           N  
ATOM   1072  CZ  ARG A 142     -38.056 -34.763 -14.730  1.00 81.90           C  
ATOM   1073  NH1 ARG A 142     -36.868 -34.943 -15.298  1.00 82.30           N  
ATOM   1074  NH2 ARG A 142     -38.376 -35.444 -13.635  1.00 66.82           N  
ATOM   1075  N   PRO A 143     -39.478 -29.086 -13.131  1.00 40.85           N  
ATOM   1076  CA  PRO A 143     -40.686 -28.292 -12.870  1.00 39.27           C  
ATOM   1077  C   PRO A 143     -40.462 -26.796 -13.062  1.00 38.84           C  
ATOM   1078  O   PRO A 143     -41.398 -26.065 -13.409  1.00 35.54           O  
ATOM   1079  CB  PRO A 143     -40.978 -28.580 -11.395  1.00 38.39           C  
ATOM   1080  CG  PRO A 143     -40.404 -29.928 -11.167  1.00 37.99           C  
ATOM   1081  CD  PRO A 143     -39.153 -29.977 -12.002  1.00 45.96           C  
ATOM   1082  N   PHE A 144     -39.237 -26.343 -12.815  1.00 32.32           N  
ATOM   1083  CA  PHE A 144     -38.914 -24.947 -13.031  1.00 35.15           C  
ATOM   1084  C   PHE A 144     -38.632 -24.652 -14.498  1.00 34.63           C  
ATOM   1085  O   PHE A 144     -38.966 -23.584 -14.990  1.00 32.32           O  
ATOM   1086  CB  PHE A 144     -37.800 -24.500 -12.094  1.00 36.34           C  
ATOM   1087  CG  PHE A 144     -38.278 -24.355 -10.687  1.00 40.83           C  
ATOM   1088  CD1 PHE A 144     -38.823 -23.159 -10.253  1.00 43.69           C  
ATOM   1089  CD2 PHE A 144     -38.286 -25.442  -9.836  1.00 38.43           C  
ATOM   1090  CE1 PHE A 144     -39.308 -23.031  -8.959  1.00 48.27           C  
ATOM   1091  CE2 PHE A 144     -38.774 -25.326  -8.549  1.00 38.31           C  
ATOM   1092  CZ  PHE A 144     -39.285 -24.123  -8.114  1.00 43.70           C  
ATOM   1093  N   LYS A 145     -38.043 -25.617 -15.188  1.00 29.07           N  
ATOM   1094  CA  LYS A 145     -37.854 -25.494 -16.632  1.00 31.46           C  
ATOM   1095  C   LYS A 145     -39.214 -25.403 -17.306  1.00 37.92           C  
ATOM   1096  O   LYS A 145     -39.435 -24.584 -18.223  1.00 35.83           O  
ATOM   1097  CB  LYS A 145     -37.097 -26.707 -17.168  1.00 29.17           C  
ATOM   1098  CG  LYS A 145     -36.708 -26.583 -18.637  1.00 39.56           C  
ATOM   1099  CD  LYS A 145     -35.805 -27.725 -19.068  1.00 52.39           C  
ATOM   1100  CE  LYS A 145     -34.788 -27.250 -20.110  1.00 73.41           C  
ATOM   1101  NZ  LYS A 145     -34.161 -28.369 -20.888  1.00 66.50           N  
ATOM   1102  N   GLU A 146     -40.126 -26.266 -16.873  1.00 31.94           N  
ATOM   1103  CA  GLU A 146     -41.465 -26.287 -17.443  1.00 39.14           C  
ATOM   1104  C   GLU A 146     -42.201 -24.986 -17.142  1.00 37.47           C  
ATOM   1105  O   GLU A 146     -42.845 -24.413 -18.029  1.00 37.14           O  
ATOM   1106  CB  GLU A 146     -42.263 -27.506 -16.965  1.00 35.14           C  
ATOM   1107  CG  GLU A 146     -41.607 -28.814 -17.367  1.00 52.51           C  
ATOM   1108  CD  GLU A 146     -42.511 -30.038 -17.222  1.00 62.41           C  
ATOM   1109  OE1 GLU A 146     -43.726 -29.883 -16.952  1.00 65.51           O  
ATOM   1110  OE2 GLU A 146     -41.991 -31.163 -17.389  1.00 57.69           O  
ATOM   1111  N   PHE A 147     -42.090 -24.528 -15.899  1.00 29.49           N  
ATOM   1112  CA  PHE A 147     -42.653 -23.257 -15.468  1.00 30.98           C  
ATOM   1113  C   PHE A 147     -42.221 -22.112 -16.394  1.00 35.29           C  
ATOM   1114  O   PHE A 147     -43.052 -21.346 -16.875  1.00 35.80           O  
ATOM   1115  CB  PHE A 147     -42.215 -22.963 -14.029  1.00 36.76           C  
ATOM   1116  CG  PHE A 147     -42.808 -21.717 -13.449  1.00 39.14           C  
ATOM   1117  CD1 PHE A 147     -44.080 -21.729 -12.905  1.00 38.49           C  
ATOM   1118  CD2 PHE A 147     -42.087 -20.535 -13.428  1.00 42.38           C  
ATOM   1119  CE1 PHE A 147     -44.627 -20.590 -12.354  1.00 42.69           C  
ATOM   1120  CE2 PHE A 147     -42.631 -19.386 -12.882  1.00 57.31           C  
ATOM   1121  CZ  PHE A 147     -43.905 -19.416 -12.336  1.00 49.82           C  
ATOM   1122  N   LEU A 148     -40.920 -22.001 -16.636  1.00 31.07           N  
ATOM   1123  CA  LEU A 148     -40.387 -21.006 -17.561  1.00 31.31           C  
ATOM   1124  C   LEU A 148     -40.883 -21.234 -19.006  1.00 29.61           C  
ATOM   1125  O   LEU A 148     -41.362 -20.315 -19.673  1.00 31.32           O  
ATOM   1126  CB  LEU A 148     -38.863 -21.050 -17.529  1.00 28.96           C  
ATOM   1127  CG  LEU A 148     -38.140 -20.158 -18.526  1.00 41.67           C  
ATOM   1128  CD1 LEU A 148     -38.342 -18.681 -18.177  1.00 38.46           C  
ATOM   1129  CD2 LEU A 148     -36.668 -20.520 -18.561  1.00 36.96           C  
ATOM   1130  N   TYR A 149     -40.770 -22.462 -19.484  1.00 29.64           N  
ATOM   1131  CA  TYR A 149     -41.199 -22.788 -20.850  1.00 35.29           C  
ATOM   1132  C   TYR A 149     -42.674 -22.473 -21.108  1.00 32.67           C  
ATOM   1133  O   TYR A 149     -43.055 -22.099 -22.223  1.00 31.75           O  
ATOM   1134  CB  TYR A 149     -40.904 -24.261 -21.175  1.00 37.04           C  
ATOM   1135  CG  TYR A 149     -39.448 -24.528 -21.502  1.00 36.96           C  
ATOM   1136  CD1 TYR A 149     -38.449 -23.633 -21.114  1.00 31.00           C  
ATOM   1137  CD2 TYR A 149     -39.068 -25.683 -22.182  1.00 45.28           C  
ATOM   1138  CE1 TYR A 149     -37.119 -23.879 -21.407  1.00 37.89           C  
ATOM   1139  CE2 TYR A 149     -37.734 -25.934 -22.481  1.00 46.90           C  
ATOM   1140  CZ  TYR A 149     -36.768 -25.029 -22.088  1.00 42.96           C  
ATOM   1141  OH  TYR A 149     -35.446 -25.275 -22.387  1.00 54.10           O  
ATOM   1142  N   SER A 150     -43.495 -22.637 -20.077  1.00 30.26           N  
ATOM   1143  CA  SER A 150     -44.922 -22.369 -20.164  1.00 30.79           C  
ATOM   1144  C   SER A 150     -45.185 -20.881 -20.188  1.00 33.58           C  
ATOM   1145  O   SER A 150     -46.125 -20.428 -20.827  1.00 35.19           O  
ATOM   1146  CB  SER A 150     -45.670 -22.992 -18.975  1.00 36.46           C  
ATOM   1147  OG  SER A 150     -45.958 -24.352 -19.222  1.00 47.24           O  
ATOM   1148  N   TYR A 151     -44.368 -20.129 -19.456  1.00 30.87           N  
ATOM   1149  CA  TYR A 151     -44.474 -18.681 -19.424  1.00 32.01           C  
ATOM   1150  C   TYR A 151     -44.143 -18.086 -20.801  1.00 29.66           C  
ATOM   1151  O   TYR A 151     -44.931 -17.321 -21.380  1.00 30.31           O  
ATOM   1152  CB  TYR A 151     -43.490 -18.142 -18.375  1.00 32.31           C  
ATOM   1153  CG  TYR A 151     -43.616 -16.663 -18.094  1.00 30.76           C  
ATOM   1154  CD1 TYR A 151     -44.445 -16.210 -17.090  1.00 27.42           C  
ATOM   1155  CD2 TYR A 151     -42.901 -15.721 -18.834  1.00 30.46           C  
ATOM   1156  CE1 TYR A 151     -44.573 -14.856 -16.815  1.00 34.71           C  
ATOM   1157  CE2 TYR A 151     -43.019 -14.360 -18.566  1.00 32.21           C  
ATOM   1158  CZ  TYR A 151     -43.862 -13.937 -17.547  1.00 29.34           C  
ATOM   1159  OH  TYR A 151     -44.011 -12.594 -17.255  1.00 31.77           O  
ATOM   1160  N   ILE A 152     -42.965 -18.440 -21.310  1.00 26.16           N  
ATOM   1161  CA  ILE A 152     -42.476 -17.934 -22.599  1.00 30.44           C  
ATOM   1162  C   ILE A 152     -43.179 -18.594 -23.790  1.00 35.55           C  
ATOM   1163  O   ILE A 152     -43.279 -18.010 -24.871  1.00 34.50           O  
ATOM   1164  CB  ILE A 152     -40.946 -18.140 -22.727  1.00 37.28           C  
ATOM   1165  CG1 ILE A 152     -40.217 -17.231 -21.738  1.00 29.49           C  
ATOM   1166  CG2 ILE A 152     -40.467 -17.868 -24.155  1.00 43.16           C  
ATOM   1167  CD1 ILE A 152     -40.756 -15.849 -21.724  1.00 43.41           C  
ATOM   1168  N   GLY A 153     -43.666 -19.815 -23.588  1.00 34.05           N  
ATOM   1169  CA  GLY A 153     -44.311 -20.559 -24.653  1.00 24.28           C  
ATOM   1170  C   GLY A 153     -43.337 -21.178 -25.644  1.00 36.47           C  
ATOM   1171  O   GLY A 153     -43.558 -21.133 -26.869  1.00 29.56           O  
ATOM   1172  N   VAL A 154     -42.253 -21.749 -25.123  1.00 27.02           N  
ATOM   1173  CA  VAL A 154     -41.299 -22.507 -25.941  1.00 32.16           C  
ATOM   1174  C   VAL A 154     -42.050 -23.525 -26.815  1.00 34.50           C  
ATOM   1175  O   VAL A 154     -42.983 -24.176 -26.342  1.00 33.90           O  
ATOM   1176  CB  VAL A 154     -40.268 -23.236 -25.026  1.00 36.34           C  
ATOM   1177  CG1 VAL A 154     -39.300 -24.095 -25.836  1.00 35.16           C  
ATOM   1178  CG2 VAL A 154     -39.508 -22.211 -24.178  1.00 37.93           C  
ATOM   1179  N   PRO A 155     -41.655 -23.660 -28.099  1.00 34.78           N  
ATOM   1180  CA  PRO A 155     -42.399 -24.553 -28.992  1.00 43.38           C  
ATOM   1181  C   PRO A 155     -42.388 -25.987 -28.478  1.00 42.21           C  
ATOM   1182  O   PRO A 155     -41.333 -26.498 -28.097  1.00 37.86           O  
ATOM   1183  CB  PRO A 155     -41.626 -24.469 -30.321  1.00 33.71           C  
ATOM   1184  CG  PRO A 155     -40.829 -23.219 -30.225  1.00 39.81           C  
ATOM   1185  CD  PRO A 155     -40.485 -23.075 -28.769  1.00 32.57           C  
ATOM   1186  N   LYS A 156     -43.552 -26.625 -28.470  1.00 36.54           N  
ATOM   1187  CA  LYS A 156     -43.632 -28.027 -28.093  1.00 42.95           C  
ATOM   1188  C   LYS A 156     -43.495 -28.901 -29.331  1.00 49.63           C  
ATOM   1189  O   LYS A 156     -43.140 -30.068 -29.232  1.00 52.25           O  
ATOM   1190  CB  LYS A 156     -44.933 -28.315 -27.334  1.00 37.22           C  
ATOM   1191  CG  LYS A 156     -44.901 -27.789 -25.904  1.00 44.11           C  
ATOM   1192  CD  LYS A 156     -46.230 -27.968 -25.165  1.00 53.97           C  
ATOM   1193  CE  LYS A 156     -47.098 -26.717 -25.260  1.00 59.99           C  
ATOM   1194  NZ  LYS A 156     -47.635 -26.512 -26.631  1.00 57.46           N  
ATOM   1195  N   GLY A 157     -43.753 -28.314 -30.497  1.00 53.30           N  
ATOM   1196  CA  GLY A 157     -43.669 -29.029 -31.756  1.00 57.15           C  
ATOM   1197  C   GLY A 157     -42.549 -28.523 -32.647  1.00 48.16           C  
ATOM   1198  O   GLY A 157     -41.620 -27.866 -32.184  1.00 57.52           O  
ATOM   1199  N   ASP A 158     -42.643 -28.818 -33.936  1.00 58.10           N  
ATOM   1200  CA  ASP A 158     -41.582 -28.464 -34.872  1.00 63.50           C  
ATOM   1201  C   ASP A 158     -41.749 -27.079 -35.515  1.00 64.21           C  
ATOM   1202  O   ASP A 158     -40.874 -26.636 -36.262  1.00 65.73           O  
ATOM   1203  CB  ASP A 158     -41.429 -29.549 -35.942  1.00 81.24           C  
ATOM   1204  CG  ASP A 158     -41.049 -30.906 -35.352  1.00 94.32           C  
ATOM   1205  OD1 ASP A 158     -41.585 -31.274 -34.281  1.00 85.95           O  
ATOM   1206  OD2 ASP A 158     -40.218 -31.614 -35.966  1.00 98.35           O  
ATOM   1207  N   GLU A 159     -42.859 -26.397 -35.230  1.00 43.03           N  
ATOM   1208  CA  GLU A 159     -43.035 -25.019 -35.696  1.00 53.13           C  
ATOM   1209  C   GLU A 159     -42.290 -24.055 -34.762  1.00 46.14           C  
ATOM   1210  O   GLU A 159     -42.382 -24.164 -33.534  1.00 40.19           O  
ATOM   1211  CB  GLU A 159     -44.517 -24.641 -35.776  1.00 49.25           C  
ATOM   1212  CG  GLU A 159     -45.429 -25.740 -36.317  1.00 58.26           C  
ATOM   1213  CD  GLU A 159     -45.645 -25.665 -37.815  1.00 70.85           C  
ATOM   1214  OE1 GLU A 159     -44.669 -25.397 -38.556  1.00 69.84           O  
ATOM   1215  OE2 GLU A 159     -46.801 -25.879 -38.252  1.00 77.95           O  
ATOM   1216  N   PRO A 160     -41.538 -23.112 -35.338  1.00 38.07           N  
ATOM   1217  CA  PRO A 160     -40.732 -22.242 -34.478  1.00 37.06           C  
ATOM   1218  C   PRO A 160     -41.621 -21.138 -33.919  1.00 30.88           C  
ATOM   1219  O   PRO A 160     -41.256 -19.976 -33.927  1.00 34.01           O  
ATOM   1220  CB  PRO A 160     -39.695 -21.657 -35.442  1.00 35.54           C  
ATOM   1221  CG  PRO A 160     -40.172 -22.035 -36.873  1.00 38.96           C  
ATOM   1222  CD  PRO A 160     -41.539 -22.652 -36.736  1.00 42.49           C  
ATOM   1223  N   ILE A 161     -42.808 -21.520 -33.471  1.00 35.83           N  
ATOM   1224  CA  ILE A 161     -43.785 -20.578 -32.981  1.00 30.20           C  
ATOM   1225  C   ILE A 161     -43.800 -20.586 -31.463  1.00 39.62           C  
ATOM   1226  O   ILE A 161     -43.781 -21.651 -30.842  1.00 32.87           O  
ATOM   1227  CB  ILE A 161     -45.181 -20.943 -33.449  1.00 36.13           C  
ATOM   1228  CG1 ILE A 161     -45.250 -20.879 -34.977  1.00 45.87           C  
ATOM   1229  CG2 ILE A 161     -46.187 -19.992 -32.837  1.00 36.69           C  
ATOM   1230  CD1 ILE A 161     -44.666 -19.602 -35.540  1.00 45.31           C  
ATOM   1231  N   LEU A 162     -43.830 -19.393 -30.877  1.00 34.28           N  
ATOM   1232  CA  LEU A 162     -43.882 -19.250 -29.426  1.00 27.22           C  
ATOM   1233  C   LEU A 162     -45.311 -18.892 -29.045  1.00 38.48           C  
ATOM   1234  O   LEU A 162     -46.041 -18.301 -29.843  1.00 34.79           O  
ATOM   1235  CB  LEU A 162     -42.934 -18.148 -28.966  1.00 27.25           C  
ATOM   1236  CG  LEU A 162     -41.448 -18.320 -29.279  1.00 27.57           C  
ATOM   1237  CD1 LEU A 162     -40.647 -17.045 -28.921  1.00 26.49           C  
ATOM   1238  CD2 LEU A 162     -40.905 -19.502 -28.534  1.00 34.82           C  
ATOM   1239  N   LYS A 163     -45.717 -19.254 -27.833  1.00 35.43           N  
ATOM   1240  CA  LYS A 163     -47.040 -18.880 -27.350  1.00 38.84           C  
ATOM   1241  C   LYS A 163     -46.948 -18.469 -25.880  1.00 43.97           C  
ATOM   1242  O   LYS A 163     -47.147 -19.287 -24.996  1.00 32.79           O  
ATOM   1243  CB  LYS A 163     -48.026 -20.042 -27.523  1.00 43.34           C  
ATOM   1244  CG  LYS A 163     -49.472 -19.712 -27.146  1.00 45.90           C  
ATOM   1245  CD  LYS A 163     -49.881 -18.332 -27.629  1.00 51.94           C  
ATOM   1246  CE  LYS A 163     -51.405 -18.180 -27.725  1.00 59.72           C  
ATOM   1247  NZ  LYS A 163     -51.790 -16.825 -28.264  1.00 54.03           N  
ATOM   1248  N   PRO A 164     -46.640 -17.190 -25.621  1.00 38.62           N  
ATOM   1249  CA  PRO A 164     -46.492 -16.752 -24.231  1.00 37.23           C  
ATOM   1250  C   PRO A 164     -47.814 -16.918 -23.503  1.00 39.22           C  
ATOM   1251  O   PRO A 164     -48.874 -16.803 -24.137  1.00 34.07           O  
ATOM   1252  CB  PRO A 164     -46.166 -15.265 -24.365  1.00 37.14           C  
ATOM   1253  CG  PRO A 164     -45.711 -15.082 -25.781  1.00 40.15           C  
ATOM   1254  CD  PRO A 164     -46.469 -16.089 -26.576  1.00 37.85           C  
ATOM   1255  N   SER A 165     -47.764 -17.179 -22.196  1.00 32.39           N  
ATOM   1256  CA  SER A 165     -48.989 -17.302 -21.442  1.00 25.09           C  
ATOM   1257  C   SER A 165     -49.679 -15.950 -21.472  1.00 29.15           C  
ATOM   1258  O   SER A 165     -49.058 -14.925 -21.766  1.00 28.59           O  
ATOM   1259  CB  SER A 165     -48.715 -17.758 -19.994  1.00 31.41           C  
ATOM   1260  OG  SER A 165     -48.014 -16.758 -19.256  1.00 34.63           O  
ATOM   1261  N   LEU A 166     -50.971 -15.940 -21.192  1.00 28.76           N  
ATOM   1262  CA  LEU A 166     -51.688 -14.687 -21.122  1.00 29.62           C  
ATOM   1263  C   LEU A 166     -51.070 -13.808 -20.038  1.00 36.45           C  
ATOM   1264  O   LEU A 166     -50.843 -12.615 -20.253  1.00 36.66           O  
ATOM   1265  CB  LEU A 166     -53.164 -14.938 -20.860  1.00 33.00           C  
ATOM   1266  CG  LEU A 166     -53.930 -13.713 -20.367  1.00 37.48           C  
ATOM   1267  CD1 LEU A 166     -54.022 -12.680 -21.457  1.00 40.35           C  
ATOM   1268  CD2 LEU A 166     -55.317 -14.120 -19.884  1.00 43.46           C  
ATOM   1269  N   PHE A 167     -50.782 -14.412 -18.884  1.00 35.02           N  
ATOM   1270  CA  PHE A 167     -50.108 -13.718 -17.789  1.00 31.92           C  
ATOM   1271  C   PHE A 167     -48.839 -13.041 -18.294  1.00 32.49           C  
ATOM   1272  O   PHE A 167     -48.625 -11.856 -18.050  1.00 30.26           O  
ATOM   1273  CB  PHE A 167     -49.783 -14.683 -16.633  1.00 39.58           C  
ATOM   1274  CG  PHE A 167     -49.027 -14.037 -15.493  1.00 35.43           C  
ATOM   1275  CD1 PHE A 167     -49.678 -13.219 -14.583  1.00 45.96           C  
ATOM   1276  CD2 PHE A 167     -47.668 -14.242 -15.342  1.00 39.83           C  
ATOM   1277  CE1 PHE A 167     -48.988 -12.621 -13.532  1.00 48.91           C  
ATOM   1278  CE2 PHE A 167     -46.970 -13.651 -14.296  1.00 35.85           C  
ATOM   1279  CZ  PHE A 167     -47.629 -12.841 -13.391  1.00 39.29           C  
ATOM   1280  N   ALA A 168     -48.013 -13.790 -19.017  1.00 31.41           N  
ATOM   1281  CA  ALA A 168     -46.772 -13.243 -19.576  1.00 34.56           C  
ATOM   1282  C   ALA A 168     -47.040 -12.034 -20.462  1.00 33.84           C  
ATOM   1283  O   ALA A 168     -46.316 -11.038 -20.411  1.00 28.87           O  
ATOM   1284  CB  ALA A 168     -46.010 -14.299 -20.358  1.00 31.00           C  
ATOM   1285  N   TYR A 169     -48.091 -12.118 -21.259  1.00 29.70           N  
ATOM   1286  CA  TYR A 169     -48.395 -11.058 -22.208  1.00 30.62           C  
ATOM   1287  C   TYR A 169     -48.854  -9.824 -21.459  1.00 34.09           C  
ATOM   1288  O   TYR A 169     -48.411  -8.706 -21.744  1.00 31.86           O  
ATOM   1289  CB  TYR A 169     -49.471 -11.508 -23.195  1.00 28.72           C  
ATOM   1290  CG  TYR A 169     -49.746 -10.522 -24.319  1.00 30.00           C  
ATOM   1291  CD1 TYR A 169     -48.941 -10.488 -25.457  1.00 26.46           C  
ATOM   1292  CD2 TYR A 169     -50.822  -9.640 -24.251  1.00 35.66           C  
ATOM   1293  CE1 TYR A 169     -49.194  -9.594 -26.491  1.00 29.83           C  
ATOM   1294  CE2 TYR A 169     -51.083  -8.751 -25.270  1.00 34.18           C  
ATOM   1295  CZ  TYR A 169     -50.265  -8.734 -26.390  1.00 30.41           C  
ATOM   1296  OH  TYR A 169     -50.525  -7.860 -27.397  1.00 29.82           O  
ATOM   1297  N   ILE A 170     -49.746 -10.032 -20.497  1.00 28.75           N  
ATOM   1298  CA  ILE A 170     -50.225  -8.936 -19.678  1.00 28.62           C  
ATOM   1299  C   ILE A 170     -49.071  -8.291 -18.909  1.00 30.29           C  
ATOM   1300  O   ILE A 170     -48.986  -7.064 -18.803  1.00 30.97           O  
ATOM   1301  CB  ILE A 170     -51.306  -9.407 -18.705  1.00 37.52           C  
ATOM   1302  CG1 ILE A 170     -52.595  -9.716 -19.476  1.00 32.86           C  
ATOM   1303  CG2 ILE A 170     -51.549  -8.346 -17.629  1.00 36.08           C  
ATOM   1304  CD1 ILE A 170     -53.672 -10.326 -18.590  1.00 40.08           C  
ATOM   1305  N   VAL A 171     -48.173  -9.112 -18.385  1.00 29.74           N  
ATOM   1306  CA  VAL A 171     -47.033  -8.556 -17.675  1.00 30.97           C  
ATOM   1307  C   VAL A 171     -46.153  -7.731 -18.620  1.00 28.27           C  
ATOM   1308  O   VAL A 171     -45.596  -6.693 -18.225  1.00 29.96           O  
ATOM   1309  CB  VAL A 171     -46.233  -9.638 -16.914  1.00 34.36           C  
ATOM   1310  CG1 VAL A 171     -44.889  -9.086 -16.442  1.00 27.73           C  
ATOM   1311  CG2 VAL A 171     -47.058 -10.140 -15.735  1.00 33.82           C  
ATOM   1312  N   PHE A 172     -46.037  -8.175 -19.870  1.00 31.07           N  
ATOM   1313  CA  PHE A 172     -45.351  -7.357 -20.873  1.00 30.75           C  
ATOM   1314  C   PHE A 172     -46.035  -6.003 -21.045  1.00 27.27           C  
ATOM   1315  O   PHE A 172     -45.378  -4.978 -21.098  1.00 25.62           O  
ATOM   1316  CB  PHE A 172     -45.256  -8.059 -22.238  1.00 30.02           C  
ATOM   1317  CG  PHE A 172     -44.534  -7.244 -23.272  1.00 30.78           C  
ATOM   1318  CD1 PHE A 172     -43.236  -6.809 -23.039  1.00 29.65           C  
ATOM   1319  CD2 PHE A 172     -45.156  -6.886 -24.472  1.00 35.75           C  
ATOM   1320  CE1 PHE A 172     -42.558  -6.046 -23.981  1.00 29.44           C  
ATOM   1321  CE2 PHE A 172     -44.486  -6.117 -25.415  1.00 31.04           C  
ATOM   1322  CZ  PHE A 172     -43.183  -5.695 -25.174  1.00 27.88           C  
ATOM   1323  N   LEU A 173     -47.360  -5.998 -21.138  1.00 30.67           N  
ATOM   1324  CA  LEU A 173     -48.101  -4.741 -21.196  1.00 32.47           C  
ATOM   1325  C   LEU A 173     -47.801  -3.857 -19.983  1.00 30.30           C  
ATOM   1326  O   LEU A 173     -47.573  -2.654 -20.114  1.00 34.12           O  
ATOM   1327  CB  LEU A 173     -49.605  -5.006 -21.277  1.00 31.03           C  
ATOM   1328  CG  LEU A 173     -50.165  -5.201 -22.681  1.00 47.06           C  
ATOM   1329  CD1 LEU A 173     -51.640  -5.529 -22.616  1.00 48.02           C  
ATOM   1330  CD2 LEU A 173     -49.939  -3.922 -23.468  1.00 56.94           C  
ATOM   1331  N   ILE A 174     -47.811  -4.461 -18.798  1.00 29.96           N  
ATOM   1332  CA  ILE A 174     -47.561  -3.710 -17.571  1.00 31.20           C  
ATOM   1333  C   ILE A 174     -46.138  -3.151 -17.610  1.00 28.46           C  
ATOM   1334  O   ILE A 174     -45.899  -1.994 -17.282  1.00 30.77           O  
ATOM   1335  CB  ILE A 174     -47.761  -4.598 -16.316  1.00 29.31           C  
ATOM   1336  CG1 ILE A 174     -49.229  -5.001 -16.186  1.00 32.90           C  
ATOM   1337  CG2 ILE A 174     -47.340  -3.864 -15.058  1.00 32.96           C  
ATOM   1338  CD1 ILE A 174     -49.483  -6.040 -15.110  1.00 35.38           C  
ATOM   1339  N   THR A 175     -45.195  -3.980 -18.044  1.00 27.78           N  
ATOM   1340  CA  THR A 175     -43.799  -3.570 -18.069  1.00 24.73           C  
ATOM   1341  C   THR A 175     -43.603  -2.380 -19.002  1.00 26.42           C  
ATOM   1342  O   THR A 175     -42.893  -1.430 -18.658  1.00 29.98           O  
ATOM   1343  CB  THR A 175     -42.900  -4.730 -18.493  1.00 22.88           C  
ATOM   1344  OG1 THR A 175     -43.067  -5.810 -17.574  1.00 30.26           O  
ATOM   1345  CG2 THR A 175     -41.454  -4.308 -18.521  1.00 29.47           C  
ATOM   1346  N   MET A 176     -44.234  -2.424 -20.182  1.00 28.53           N  
ATOM   1347  CA  MET A 176     -44.208  -1.293 -21.108  1.00 26.41           C  
ATOM   1348  C   MET A 176     -44.825  -0.057 -20.457  1.00 27.44           C  
ATOM   1349  O   MET A 176     -44.303   1.051 -20.554  1.00 27.52           O  
ATOM   1350  CB  MET A 176     -44.977  -1.616 -22.396  1.00 30.98           C  
ATOM   1351  CG  MET A 176     -44.265  -2.540 -23.372  1.00 40.39           C  
ATOM   1352  SD  MET A 176     -42.677  -1.900 -23.984  1.00 50.73           S  
ATOM   1353  CE  MET A 176     -43.042  -0.151 -24.160  1.00 26.32           C  
ATOM   1354  N   PHE A 177     -45.963  -0.252 -19.809  1.00 30.62           N  
ATOM   1355  CA  PHE A 177     -46.606   0.811 -19.054  1.00 31.05           C  
ATOM   1356  C   PHE A 177     -45.654   1.442 -18.032  1.00 28.83           C  
ATOM   1357  O   PHE A 177     -45.593   2.667 -17.907  1.00 29.93           O  
ATOM   1358  CB  PHE A 177     -47.827   0.281 -18.298  1.00 31.33           C  
ATOM   1359  CG  PHE A 177     -48.525   1.333 -17.489  1.00 37.06           C  
ATOM   1360  CD1 PHE A 177     -49.323   2.284 -18.111  1.00 40.03           C  
ATOM   1361  CD2 PHE A 177     -48.376   1.383 -16.116  1.00 37.56           C  
ATOM   1362  CE1 PHE A 177     -49.961   3.262 -17.381  1.00 39.17           C  
ATOM   1363  CE2 PHE A 177     -49.004   2.363 -15.375  1.00 45.97           C  
ATOM   1364  CZ  PHE A 177     -49.803   3.301 -16.002  1.00 45.20           C  
ATOM   1365  N   ILE A 178     -44.932   0.608 -17.289  1.00 24.58           N  
ATOM   1366  CA  ILE A 178     -44.025   1.119 -16.258  1.00 26.57           C  
ATOM   1367  C   ILE A 178     -42.897   1.908 -16.913  1.00 28.22           C  
ATOM   1368  O   ILE A 178     -42.560   3.007 -16.478  1.00 27.59           O  
ATOM   1369  CB  ILE A 178     -43.477  -0.014 -15.332  1.00 34.41           C  
ATOM   1370  CG1 ILE A 178     -44.604  -0.582 -14.464  1.00 27.09           C  
ATOM   1371  CG2 ILE A 178     -42.328   0.491 -14.431  1.00 29.05           C  
ATOM   1372  CD1 ILE A 178     -44.259  -1.922 -13.839  1.00 30.52           C  
ATOM   1373  N   ASN A 179     -42.331   1.372 -17.986  1.00 33.11           N  
ATOM   1374  CA  ASN A 179     -41.318   2.132 -18.707  1.00 26.59           C  
ATOM   1375  C   ASN A 179     -41.847   3.473 -19.179  1.00 25.25           C  
ATOM   1376  O   ASN A 179     -41.187   4.491 -19.036  1.00 29.86           O  
ATOM   1377  CB  ASN A 179     -40.780   1.342 -19.882  1.00 27.54           C  
ATOM   1378  CG  ASN A 179     -39.760   0.320 -19.465  1.00 26.58           C  
ATOM   1379  OD1 ASN A 179     -38.556   0.561 -19.540  1.00 31.05           O  
ATOM   1380  ND2 ASN A 179     -40.232  -0.826 -19.006  1.00 22.64           N  
ATOM   1381  N   VAL A 180     -43.056   3.470 -19.728  1.00 28.20           N  
ATOM   1382  CA  VAL A 180     -43.647   4.690 -20.259  1.00 27.68           C  
ATOM   1383  C   VAL A 180     -43.913   5.707 -19.157  1.00 30.19           C  
ATOM   1384  O   VAL A 180     -43.683   6.900 -19.344  1.00 31.60           O  
ATOM   1385  CB  VAL A 180     -44.943   4.406 -21.063  1.00 27.28           C  
ATOM   1386  CG1 VAL A 180     -45.671   5.692 -21.381  1.00 28.26           C  
ATOM   1387  CG2 VAL A 180     -44.615   3.655 -22.334  1.00 27.88           C  
ATOM   1388  N   SER A 181     -44.388   5.233 -18.012  1.00 29.42           N  
ATOM   1389  CA  SER A 181     -44.665   6.112 -16.875  1.00 31.20           C  
ATOM   1390  C   SER A 181     -43.418   6.865 -16.456  1.00 32.48           C  
ATOM   1391  O   SER A 181     -43.471   8.057 -16.163  1.00 35.48           O  
ATOM   1392  CB  SER A 181     -45.224   5.320 -15.693  1.00 31.27           C  
ATOM   1393  OG  SER A 181     -46.454   4.722 -16.069  1.00 47.69           O  
ATOM   1394  N   ILE A 182     -42.290   6.173 -16.428  1.00 25.64           N  
ATOM   1395  CA  ILE A 182     -41.034   6.826 -16.102  1.00 27.21           C  
ATOM   1396  C   ILE A 182     -40.590   7.772 -17.214  1.00 34.13           C  
ATOM   1397  O   ILE A 182     -40.355   8.962 -16.975  1.00 30.82           O  
ATOM   1398  CB  ILE A 182     -39.930   5.796 -15.822  1.00 27.58           C  
ATOM   1399  CG1 ILE A 182     -40.278   5.018 -14.545  1.00 31.74           C  
ATOM   1400  CG2 ILE A 182     -38.587   6.515 -15.704  1.00 28.81           C  
ATOM   1401  CD1 ILE A 182     -39.468   3.736 -14.349  1.00 28.74           C  
ATOM   1402  N   LEU A 183     -40.513   7.247 -18.435  1.00 28.49           N  
ATOM   1403  CA  LEU A 183     -39.985   8.008 -19.559  1.00 23.86           C  
ATOM   1404  C   LEU A 183     -40.791   9.256 -19.843  1.00 24.18           C  
ATOM   1405  O   LEU A 183     -40.242  10.291 -20.216  1.00 27.37           O  
ATOM   1406  CB  LEU A 183     -39.930   7.129 -20.817  1.00 23.40           C  
ATOM   1407  CG  LEU A 183     -38.816   6.088 -20.783  1.00 27.90           C  
ATOM   1408  CD1 LEU A 183     -39.027   5.036 -21.847  1.00 26.60           C  
ATOM   1409  CD2 LEU A 183     -37.469   6.784 -20.954  1.00 30.13           C  
ATOM   1410  N   ILE A 184     -42.099   9.169 -19.673  1.00 23.62           N  
ATOM   1411  CA  ILE A 184     -42.948  10.269 -20.094  1.00 27.75           C  
ATOM   1412  C   ILE A 184     -42.785  11.477 -19.169  1.00 33.36           C  
ATOM   1413  O   ILE A 184     -43.208  12.583 -19.498  1.00 30.66           O  
ATOM   1414  CB  ILE A 184     -44.423   9.847 -20.196  1.00 24.77           C  
ATOM   1415  CG1 ILE A 184     -45.150  10.734 -21.227  1.00 41.25           C  
ATOM   1416  CG2 ILE A 184     -45.076   9.847 -18.822  1.00 32.37           C  
ATOM   1417  CD1 ILE A 184     -46.440  10.142 -21.770  1.00 39.54           C  
ATOM   1418  N   ARG A 185     -42.161  11.264 -18.015  1.00 29.32           N  
ATOM   1419  CA  ARG A 185     -41.860  12.382 -17.124  1.00 33.24           C  
ATOM   1420  C   ARG A 185     -40.531  13.031 -17.489  1.00 31.84           C  
ATOM   1421  O   ARG A 185     -40.206  14.104 -16.993  1.00 42.94           O  
ATOM   1422  CB  ARG A 185     -41.888  11.947 -15.659  1.00 34.66           C  
ATOM   1423  CG  ARG A 185     -43.295  11.731 -15.121  1.00 34.49           C  
ATOM   1424  CD  ARG A 185     -43.301  10.735 -13.976  1.00 45.75           C  
ATOM   1425  NE  ARG A 185     -44.618  10.635 -13.350  1.00 66.58           N  
ATOM   1426  CZ  ARG A 185     -45.644   9.950 -13.856  1.00 79.68           C  
ATOM   1427  NH1 ARG A 185     -46.804   9.921 -13.207  1.00 76.77           N  
ATOM   1428  NH2 ARG A 185     -45.522   9.293 -15.010  1.00 55.76           N  
ATOM   1429  N   GLY A 186     -39.763  12.389 -18.361  1.00 30.40           N  
ATOM   1430  CA  GLY A 186     -38.570  13.024 -18.890  1.00 33.58           C  
ATOM   1431  C   GLY A 186     -37.316  12.743 -18.080  1.00 27.91           C  
ATOM   1432  O   GLY A 186     -37.314  11.885 -17.211  1.00 33.23           O  
ATOM   1433  N   ILE A 187     -36.257  13.491 -18.361  1.00 32.32           N  
ATOM   1434  CA  ILE A 187     -34.931  13.155 -17.860  1.00 31.86           C  
ATOM   1435  C   ILE A 187     -34.799  13.307 -16.344  1.00 35.89           C  
ATOM   1436  O   ILE A 187     -34.484  12.346 -15.652  1.00 34.60           O  
ATOM   1437  CB  ILE A 187     -33.822  13.967 -18.573  1.00 32.90           C  
ATOM   1438  CG1 ILE A 187     -33.791  13.626 -20.076  1.00 38.66           C  
ATOM   1439  CG2 ILE A 187     -32.458  13.734 -17.892  1.00 29.59           C  
ATOM   1440  CD1 ILE A 187     -33.849  12.108 -20.403  1.00 31.55           C  
ATOM   1441  N   SER A 188     -35.046  14.510 -15.830  1.00 36.36           N  
ATOM   1442  CA  SER A 188     -34.828  14.770 -14.414  1.00 35.45           C  
ATOM   1443  C   SER A 188     -35.976  14.282 -13.544  1.00 35.73           C  
ATOM   1444  O   SER A 188     -35.732  13.687 -12.500  1.00 40.94           O  
ATOM   1445  CB  SER A 188     -34.527  16.251 -14.149  1.00 34.19           C  
ATOM   1446  OG  SER A 188     -35.645  17.060 -14.456  1.00 40.09           O  
ATOM   1447  N   LYS A 189     -37.219  14.513 -13.962  1.00 30.19           N  
ATOM   1448  CA  LYS A 189     -38.368  14.109 -13.140  1.00 31.18           C  
ATOM   1449  C   LYS A 189     -38.790  12.654 -13.349  1.00 35.48           C  
ATOM   1450  O   LYS A 189     -39.630  12.140 -12.622  1.00 36.15           O  
ATOM   1451  CB  LYS A 189     -39.573  15.031 -13.379  1.00 41.71           C  
ATOM   1452  CG  LYS A 189     -39.296  16.498 -13.073  1.00 46.77           C  
ATOM   1453  CD  LYS A 189     -40.579  17.301 -12.963  1.00 55.86           C  
ATOM   1454  CE  LYS A 189     -40.274  18.782 -12.724  1.00 74.59           C  
ATOM   1455  NZ  LYS A 189     -39.256  18.981 -11.644  1.00 76.27           N  
ATOM   1456  N   GLY A 190     -38.223  11.993 -14.350  1.00 38.56           N  
ATOM   1457  CA  GLY A 190     -38.578  10.613 -14.620  1.00 30.50           C  
ATOM   1458  C   GLY A 190     -37.379   9.715 -14.419  1.00 28.60           C  
ATOM   1459  O   GLY A 190     -37.274   9.007 -13.415  1.00 28.55           O  
ATOM   1460  N   ILE A 191     -36.452   9.749 -15.371  1.00 27.97           N  
ATOM   1461  CA  ILE A 191     -35.336   8.818 -15.316  1.00 24.81           C  
ATOM   1462  C   ILE A 191     -34.492   9.047 -14.044  1.00 26.65           C  
ATOM   1463  O   ILE A 191     -34.192   8.106 -13.319  1.00 28.09           O  
ATOM   1464  CB  ILE A 191     -34.456   8.899 -16.556  1.00 27.75           C  
ATOM   1465  CG1 ILE A 191     -35.261   8.495 -17.820  1.00 25.07           C  
ATOM   1466  CG2 ILE A 191     -33.249   7.989 -16.397  1.00 24.56           C  
ATOM   1467  CD1 ILE A 191     -34.504   8.733 -19.097  1.00 26.16           C  
ATOM   1468  N   GLU A 192     -34.119  10.296 -13.802  1.00 27.76           N  
ATOM   1469  CA  GLU A 192     -33.220  10.637 -12.705  1.00 29.06           C  
ATOM   1470  C   GLU A 192     -33.852  10.317 -11.370  1.00 29.32           C  
ATOM   1471  O   GLU A 192     -33.247   9.669 -10.528  1.00 27.79           O  
ATOM   1472  CB  GLU A 192     -32.877  12.110 -12.745  1.00 35.70           C  
ATOM   1473  CG  GLU A 192     -31.660  12.459 -11.951  1.00 33.11           C  
ATOM   1474  CD  GLU A 192     -31.445  13.945 -11.911  1.00 39.89           C  
ATOM   1475  OE1 GLU A 192     -31.938  14.616 -12.845  1.00 36.87           O  
ATOM   1476  OE2 GLU A 192     -30.802  14.435 -10.951  1.00 31.62           O  
ATOM   1477  N   ARG A 193     -35.082  10.779 -11.201  1.00 30.11           N  
ATOM   1478  CA  ARG A 193     -35.852  10.525  -9.994  1.00 35.71           C  
ATOM   1479  C   ARG A 193     -35.961   9.031  -9.736  1.00 37.09           C  
ATOM   1480  O   ARG A 193     -35.801   8.593  -8.599  1.00 34.82           O  
ATOM   1481  CB  ARG A 193     -37.233  11.168 -10.127  1.00 38.98           C  
ATOM   1482  CG  ARG A 193     -38.143  11.009  -8.935  1.00 46.10           C  
ATOM   1483  CD  ARG A 193     -39.341  11.949  -9.058  1.00 54.48           C  
ATOM   1484  NE  ARG A 193     -40.330  11.712  -8.009  1.00 68.66           N  
ATOM   1485  CZ  ARG A 193     -41.233  10.734  -8.039  1.00 79.70           C  
ATOM   1486  NH1 ARG A 193     -41.269   9.892  -9.065  1.00 80.19           N  
ATOM   1487  NH2 ARG A 193     -42.099  10.592  -7.039  1.00 74.99           N  
ATOM   1488  N   PHE A 194     -36.219   8.247 -10.787  1.00 27.27           N  
ATOM   1489  CA  PHE A 194     -36.309   6.793 -10.642  1.00 28.28           C  
ATOM   1490  C   PHE A 194     -34.966   6.172 -10.251  1.00 29.50           C  
ATOM   1491  O   PHE A 194     -34.913   5.327  -9.364  1.00 31.14           O  
ATOM   1492  CB  PHE A 194     -36.841   6.104 -11.915  1.00 26.78           C  
ATOM   1493  CG  PHE A 194     -36.963   4.607 -11.776  1.00 33.39           C  
ATOM   1494  CD1 PHE A 194     -37.934   4.054 -10.951  1.00 31.79           C  
ATOM   1495  CD2 PHE A 194     -36.091   3.751 -12.443  1.00 29.11           C  
ATOM   1496  CE1 PHE A 194     -38.040   2.676 -10.800  1.00 32.86           C  
ATOM   1497  CE2 PHE A 194     -36.191   2.375 -12.298  1.00 24.29           C  
ATOM   1498  CZ  PHE A 194     -37.167   1.836 -11.479  1.00 33.14           C  
ATOM   1499  N   ALA A 195     -33.892   6.600 -10.907  1.00 27.24           N  
ATOM   1500  CA  ALA A 195     -32.552   6.121 -10.588  1.00 30.68           C  
ATOM   1501  C   ALA A 195     -32.224   6.303  -9.095  1.00 30.90           C  
ATOM   1502  O   ALA A 195     -31.590   5.450  -8.470  1.00 37.07           O  
ATOM   1503  CB  ALA A 195     -31.514   6.848 -11.444  1.00 26.75           C  
ATOM   1504  N   LYS A 196     -32.648   7.424  -8.530  1.00 33.12           N  
ATOM   1505  CA  LYS A 196     -32.319   7.729  -7.126  1.00 32.44           C  
ATOM   1506  C   LYS A 196     -32.987   6.800  -6.128  1.00 35.52           C  
ATOM   1507  O   LYS A 196     -32.460   6.559  -5.041  1.00 44.50           O  
ATOM   1508  CB  LYS A 196     -32.645   9.178  -6.815  1.00 34.27           C  
ATOM   1509  CG  LYS A 196     -31.599  10.118  -7.342  1.00 35.49           C  
ATOM   1510  CD  LYS A 196     -32.026  11.536  -7.163  1.00 42.08           C  
ATOM   1511  CE  LYS A 196     -30.836  12.392  -6.803  1.00 51.37           C  
ATOM   1512  NZ  LYS A 196     -31.287  13.705  -6.250  1.00 52.64           N  
ATOM   1513  N   ILE A 197     -34.143   6.270  -6.492  1.00 31.28           N  
ATOM   1514  CA  ILE A 197     -34.778   5.225  -5.698  1.00 31.02           C  
ATOM   1515  C   ILE A 197     -34.239   3.859  -6.085  1.00 34.92           C  
ATOM   1516  O   ILE A 197     -33.978   3.022  -5.229  1.00 30.91           O  
ATOM   1517  CB  ILE A 197     -36.296   5.219  -5.912  1.00 36.01           C  
ATOM   1518  CG1 ILE A 197     -36.890   6.547  -5.450  1.00 41.85           C  
ATOM   1519  CG2 ILE A 197     -36.939   4.051  -5.174  1.00 45.52           C  
ATOM   1520  CD1 ILE A 197     -38.285   6.794  -5.964  1.00 56.86           C  
ATOM   1521  N   ALA A 198     -34.067   3.638  -7.390  1.00 32.27           N  
ATOM   1522  CA  ALA A 198     -33.813   2.310  -7.920  1.00 27.33           C  
ATOM   1523  C   ALA A 198     -32.440   1.766  -7.572  1.00 31.10           C  
ATOM   1524  O   ALA A 198     -32.295   0.575  -7.304  1.00 29.64           O  
ATOM   1525  CB  ALA A 198     -33.996   2.304  -9.445  1.00 27.76           C  
ATOM   1526  N   MET A 199     -31.421   2.612  -7.645  1.00 24.16           N  
ATOM   1527  CA  MET A 199     -30.069   2.132  -7.391  1.00 29.84           C  
ATOM   1528  C   MET A 199     -29.878   1.717  -5.911  1.00 33.81           C  
ATOM   1529  O   MET A 199     -29.306   0.662  -5.630  1.00 32.75           O  
ATOM   1530  CB  MET A 199     -29.028   3.164  -7.833  1.00 28.80           C  
ATOM   1531  CG  MET A 199     -29.047   3.460  -9.337  1.00 39.93           C  
ATOM   1532  SD  MET A 199     -29.175   1.940 -10.319  1.00 43.38           S  
ATOM   1533  CE  MET A 199     -27.536   1.262 -10.080  1.00 31.46           C  
ATOM   1534  N   PRO A 200     -30.375   2.532  -4.965  1.00 32.91           N  
ATOM   1535  CA  PRO A 200     -30.255   2.106  -3.557  1.00 35.14           C  
ATOM   1536  C   PRO A 200     -31.037   0.828  -3.265  1.00 33.48           C  
ATOM   1537  O   PRO A 200     -30.529  -0.058  -2.587  1.00 36.15           O  
ATOM   1538  CB  PRO A 200     -30.859   3.283  -2.777  1.00 29.06           C  
ATOM   1539  CG  PRO A 200     -30.673   4.454  -3.641  1.00 30.43           C  
ATOM   1540  CD  PRO A 200     -30.885   3.911  -5.069  1.00 33.47           C  
ATOM   1541  N   THR A 201     -32.264   0.747  -3.761  1.00 34.11           N  
ATOM   1542  CA  THR A 201     -33.071  -0.462  -3.652  1.00 30.99           C  
ATOM   1543  C   THR A 201     -32.306  -1.663  -4.184  1.00 37.52           C  
ATOM   1544  O   THR A 201     -32.263  -2.720  -3.561  1.00 32.81           O  
ATOM   1545  CB  THR A 201     -34.362  -0.320  -4.462  1.00 35.72           C  
ATOM   1546  OG1 THR A 201     -35.142   0.746  -3.907  1.00 38.32           O  
ATOM   1547  CG2 THR A 201     -35.170  -1.604  -4.424  1.00 37.59           C  
ATOM   1548  N   LEU A 202     -31.704  -1.485  -5.350  1.00 33.78           N  
ATOM   1549  CA  LEU A 202     -30.971  -2.547  -6.011  1.00 36.17           C  
ATOM   1550  C   LEU A 202     -29.805  -2.981  -5.136  1.00 31.30           C  
ATOM   1551  O   LEU A 202     -29.557  -4.173  -4.945  1.00 33.96           O  
ATOM   1552  CB  LEU A 202     -30.449  -2.018  -7.349  1.00 41.40           C  
ATOM   1553  CG  LEU A 202     -30.523  -2.912  -8.572  1.00 48.25           C  
ATOM   1554  CD1 LEU A 202     -31.791  -3.750  -8.549  1.00 39.80           C  
ATOM   1555  CD2 LEU A 202     -30.461  -2.036  -9.817  1.00 39.86           C  
ATOM   1556  N   PHE A 203     -29.086  -1.994  -4.618  1.00 36.89           N  
ATOM   1557  CA  PHE A 203     -27.955  -2.229  -3.736  1.00 39.34           C  
ATOM   1558  C   PHE A 203     -28.417  -3.025  -2.529  1.00 35.06           C  
ATOM   1559  O   PHE A 203     -27.801  -4.023  -2.145  1.00 37.11           O  
ATOM   1560  CB  PHE A 203     -27.367  -0.890  -3.297  1.00 44.60           C  
ATOM   1561  CG  PHE A 203     -26.332  -0.999  -2.210  1.00 56.20           C  
ATOM   1562  CD1 PHE A 203     -25.155  -1.704  -2.417  1.00 65.98           C  
ATOM   1563  CD2 PHE A 203     -26.523  -0.369  -0.989  1.00 72.76           C  
ATOM   1564  CE1 PHE A 203     -24.193  -1.793  -1.420  1.00 55.46           C  
ATOM   1565  CE2 PHE A 203     -25.566  -0.454   0.011  1.00 59.60           C  
ATOM   1566  CZ  PHE A 203     -24.400  -1.169  -0.208  1.00 51.16           C  
ATOM   1567  N   ILE A 204     -29.524  -2.592  -1.942  1.00 39.20           N  
ATOM   1568  CA  ILE A 204     -30.040  -3.245  -0.735  1.00 48.43           C  
ATOM   1569  C   ILE A 204     -30.417  -4.701  -0.985  1.00 38.92           C  
ATOM   1570  O   ILE A 204     -30.051  -5.583  -0.211  1.00 33.13           O  
ATOM   1571  CB  ILE A 204     -31.243  -2.475  -0.147  1.00 47.21           C  
ATOM   1572  CG1 ILE A 204     -30.748  -1.219   0.568  1.00 44.95           C  
ATOM   1573  CG2 ILE A 204     -32.056  -3.369   0.797  1.00 38.03           C  
ATOM   1574  CD1 ILE A 204     -31.726  -0.083   0.533  1.00 46.39           C  
ATOM   1575  N   LEU A 205     -31.146  -4.944  -2.070  1.00 33.25           N  
ATOM   1576  CA  LEU A 205     -31.567  -6.296  -2.405  1.00 32.76           C  
ATOM   1577  C   LEU A 205     -30.364  -7.186  -2.629  1.00 36.22           C  
ATOM   1578  O   LEU A 205     -30.345  -8.333  -2.190  1.00 37.97           O  
ATOM   1579  CB  LEU A 205     -32.416  -6.304  -3.675  1.00 30.17           C  
ATOM   1580  CG  LEU A 205     -33.794  -5.676  -3.546  1.00 32.71           C  
ATOM   1581  CD1 LEU A 205     -34.335  -5.283  -4.913  1.00 34.34           C  
ATOM   1582  CD2 LEU A 205     -34.721  -6.645  -2.853  1.00 35.06           C  
ATOM   1583  N   ALA A 206     -29.372  -6.661  -3.344  1.00 33.11           N  
ATOM   1584  CA  ALA A 206     -28.199  -7.447  -3.694  1.00 29.99           C  
ATOM   1585  C   ALA A 206     -27.423  -7.817  -2.428  1.00 27.36           C  
ATOM   1586  O   ALA A 206     -26.966  -8.945  -2.281  1.00 36.36           O  
ATOM   1587  CB  ALA A 206     -27.320  -6.680  -4.671  1.00 30.70           C  
ATOM   1588  N   VAL A 207     -27.283  -6.866  -1.512  1.00 34.58           N  
ATOM   1589  CA  VAL A 207     -26.544  -7.138  -0.281  1.00 36.15           C  
ATOM   1590  C   VAL A 207     -27.295  -8.168   0.544  1.00 36.47           C  
ATOM   1591  O   VAL A 207     -26.713  -9.164   0.978  1.00 39.84           O  
ATOM   1592  CB  VAL A 207     -26.260  -5.871   0.526  1.00 37.31           C  
ATOM   1593  CG1 VAL A 207     -25.834  -6.227   1.966  1.00 38.85           C  
ATOM   1594  CG2 VAL A 207     -25.178  -5.055  -0.168  1.00 37.83           C  
ATOM   1595  N   PHE A 208     -28.595  -7.956   0.728  1.00 35.01           N  
ATOM   1596  CA  PHE A 208     -29.399  -8.951   1.425  1.00 41.41           C  
ATOM   1597  C   PHE A 208     -29.219 -10.330   0.795  1.00 44.39           C  
ATOM   1598  O   PHE A 208     -29.058 -11.336   1.488  1.00 38.28           O  
ATOM   1599  CB  PHE A 208     -30.874  -8.581   1.423  1.00 32.75           C  
ATOM   1600  CG  PHE A 208     -31.716  -9.540   2.192  1.00 41.59           C  
ATOM   1601  CD1 PHE A 208     -31.886  -9.386   3.569  1.00 45.11           C  
ATOM   1602  CD2 PHE A 208     -32.307 -10.623   1.565  1.00 31.64           C  
ATOM   1603  CE1 PHE A 208     -32.652 -10.291   4.294  1.00 44.91           C  
ATOM   1604  CE2 PHE A 208     -33.079 -11.525   2.279  1.00 39.97           C  
ATOM   1605  CZ  PHE A 208     -33.255 -11.356   3.649  1.00 48.75           C  
ATOM   1606  N   LEU A 209     -29.245 -10.370  -0.534  1.00 36.95           N  
ATOM   1607  CA  LEU A 209     -29.105 -11.629  -1.246  1.00 35.56           C  
ATOM   1608  C   LEU A 209     -27.735 -12.271  -0.988  1.00 36.42           C  
ATOM   1609  O   LEU A 209     -27.631 -13.477  -0.772  1.00 35.57           O  
ATOM   1610  CB  LEU A 209     -29.346 -11.411  -2.743  1.00 37.08           C  
ATOM   1611  CG  LEU A 209     -30.836 -11.280  -3.092  1.00 36.73           C  
ATOM   1612  CD1 LEU A 209     -31.072 -10.598  -4.438  1.00 43.83           C  
ATOM   1613  CD2 LEU A 209     -31.481 -12.647  -3.077  1.00 40.63           C  
ATOM   1614  N   VAL A 210     -26.686 -11.460  -1.023  1.00 36.78           N  
ATOM   1615  CA  VAL A 210     -25.338 -11.967  -0.783  1.00 41.87           C  
ATOM   1616  C   VAL A 210     -25.210 -12.586   0.607  1.00 41.47           C  
ATOM   1617  O   VAL A 210     -24.635 -13.661   0.785  1.00 36.75           O  
ATOM   1618  CB  VAL A 210     -24.297 -10.852  -0.927  1.00 43.77           C  
ATOM   1619  CG1 VAL A 210     -23.022 -11.234  -0.193  1.00 41.39           C  
ATOM   1620  CG2 VAL A 210     -24.041 -10.576  -2.415  1.00 36.42           C  
ATOM   1621  N   ILE A 211     -25.766 -11.895   1.589  1.00 37.27           N  
ATOM   1622  CA  ILE A 211     -25.764 -12.390   2.948  1.00 40.72           C  
ATOM   1623  C   ILE A 211     -26.528 -13.701   3.036  1.00 47.30           C  
ATOM   1624  O   ILE A 211     -25.997 -14.703   3.516  1.00 42.17           O  
ATOM   1625  CB  ILE A 211     -26.371 -11.366   3.907  1.00 39.56           C  
ATOM   1626  CG1 ILE A 211     -25.441 -10.158   4.014  1.00 34.48           C  
ATOM   1627  CG2 ILE A 211     -26.624 -12.012   5.277  1.00 42.24           C  
ATOM   1628  CD1 ILE A 211     -26.070  -8.970   4.694  1.00 40.70           C  
ATOM   1629  N   ARG A 212     -27.773 -13.699   2.572  1.00 38.82           N  
ATOM   1630  CA  ARG A 212     -28.575 -14.912   2.638  1.00 35.80           C  
ATOM   1631  C   ARG A 212     -27.836 -16.054   1.962  1.00 35.31           C  
ATOM   1632  O   ARG A 212     -27.777 -17.166   2.479  1.00 39.12           O  
ATOM   1633  CB  ARG A 212     -29.942 -14.698   1.988  1.00 35.97           C  
ATOM   1634  CG  ARG A 212     -30.958 -15.783   2.311  1.00 43.89           C  
ATOM   1635  CD  ARG A 212     -30.698 -17.068   1.526  1.00 37.30           C  
ATOM   1636  NE  ARG A 212     -31.497 -18.165   2.057  1.00 54.69           N  
ATOM   1637  CZ  ARG A 212     -31.128 -18.921   3.091  1.00 55.60           C  
ATOM   1638  NH1 ARG A 212     -29.960 -18.703   3.683  1.00 36.47           N  
ATOM   1639  NH2 ARG A 212     -31.924 -19.896   3.521  1.00 39.23           N  
ATOM   1640  N   VAL A 213     -27.272 -15.775   0.794  1.00 39.92           N  
ATOM   1641  CA  VAL A 213     -26.587 -16.812   0.042  1.00 41.23           C  
ATOM   1642  C   VAL A 213     -25.396 -17.367   0.813  1.00 38.72           C  
ATOM   1643  O   VAL A 213     -25.138 -18.566   0.773  1.00 37.23           O  
ATOM   1644  CB  VAL A 213     -26.139 -16.319  -1.351  1.00 39.88           C  
ATOM   1645  CG1 VAL A 213     -25.132 -17.284  -1.969  1.00 37.97           C  
ATOM   1646  CG2 VAL A 213     -27.354 -16.182  -2.271  1.00 41.23           C  
ATOM   1647  N   PHE A 214     -24.677 -16.490   1.503  1.00 36.04           N  
ATOM   1648  CA  PHE A 214     -23.449 -16.892   2.165  1.00 39.19           C  
ATOM   1649  C   PHE A 214     -23.742 -17.807   3.331  1.00 41.73           C  
ATOM   1650  O   PHE A 214     -22.829 -18.410   3.883  1.00 49.86           O  
ATOM   1651  CB  PHE A 214     -22.654 -15.680   2.658  1.00 33.75           C  
ATOM   1652  CG  PHE A 214     -21.788 -15.058   1.611  1.00 40.26           C  
ATOM   1653  CD1 PHE A 214     -21.960 -15.379   0.269  1.00 52.03           C  
ATOM   1654  CD2 PHE A 214     -20.831 -14.116   1.955  1.00 46.27           C  
ATOM   1655  CE1 PHE A 214     -21.175 -14.785  -0.716  1.00 48.17           C  
ATOM   1656  CE2 PHE A 214     -20.041 -13.515   0.982  1.00 52.39           C  
ATOM   1657  CZ  PHE A 214     -20.211 -13.855  -0.357  1.00 50.74           C  
ATOM   1658  N   LEU A 215     -25.010 -17.914   3.714  1.00 42.65           N  
ATOM   1659  CA  LEU A 215     -25.366 -18.734   4.875  1.00 50.35           C  
ATOM   1660  C   LEU A 215     -25.790 -20.120   4.447  1.00 46.47           C  
ATOM   1661  O   LEU A 215     -25.892 -21.023   5.270  1.00 45.83           O  
ATOM   1662  CB  LEU A 215     -26.497 -18.087   5.672  1.00 40.35           C  
ATOM   1663  CG  LEU A 215     -26.178 -16.739   6.304  1.00 41.96           C  
ATOM   1664  CD1 LEU A 215     -27.462 -16.066   6.732  1.00 52.29           C  
ATOM   1665  CD2 LEU A 215     -25.245 -16.924   7.489  1.00 51.10           C  
ATOM   1666  N   LEU A 216     -26.040 -20.275   3.152  1.00 39.47           N  
ATOM   1667  CA  LEU A 216     -26.538 -21.534   2.612  1.00 42.97           C  
ATOM   1668  C   LEU A 216     -25.604 -22.703   2.879  1.00 44.65           C  
ATOM   1669  O   LEU A 216     -24.416 -22.651   2.553  1.00 39.15           O  
ATOM   1670  CB  LEU A 216     -26.784 -21.424   1.098  1.00 40.89           C  
ATOM   1671  CG  LEU A 216     -27.974 -20.568   0.671  1.00 48.30           C  
ATOM   1672  CD1 LEU A 216     -28.092 -20.515  -0.850  1.00 45.96           C  
ATOM   1673  CD2 LEU A 216     -29.248 -21.108   1.291  1.00 42.72           C  
ATOM   1674  N   GLU A 217     -26.170 -23.761   3.449  1.00 37.70           N  
ATOM   1675  CA  GLU A 217     -25.455 -25.001   3.694  1.00 46.12           C  
ATOM   1676  C   GLU A 217     -26.343 -26.154   3.261  1.00 44.48           C  
ATOM   1677  O   GLU A 217     -27.519 -26.205   3.622  1.00 42.71           O  
ATOM   1678  CB  GLU A 217     -25.131 -25.158   5.185  1.00 49.12           C  
ATOM   1679  CG  GLU A 217     -23.945 -24.344   5.703  1.00 53.55           C  
ATOM   1680  CD  GLU A 217     -23.781 -24.466   7.226  1.00 58.34           C  
ATOM   1681  OE1 GLU A 217     -24.812 -24.448   7.936  1.00 41.93           O  
ATOM   1682  OE2 GLU A 217     -22.629 -24.564   7.710  1.00 53.60           O  
ATOM   1683  N   THR A 218     -25.780 -27.075   2.484  1.00 40.37           N  
ATOM   1684  CA  THR A 218     -26.475 -28.298   2.098  1.00 45.49           C  
ATOM   1685  C   THR A 218     -25.482 -29.445   2.205  1.00 36.30           C  
ATOM   1686  O   THR A 218     -24.286 -29.216   2.336  1.00 42.00           O  
ATOM   1687  CB  THR A 218     -27.025 -28.234   0.634  1.00 44.22           C  
ATOM   1688  OG1 THR A 218     -25.969 -28.519  -0.294  1.00 41.75           O  
ATOM   1689  CG2 THR A 218     -27.631 -26.868   0.325  1.00 41.14           C  
ATOM   1690  N   PRO A 219     -25.969 -30.689   2.147  1.00 46.61           N  
ATOM   1691  CA  PRO A 219     -25.022 -31.810   2.169  1.00 50.12           C  
ATOM   1692  C   PRO A 219     -24.063 -31.736   0.981  1.00 58.26           C  
ATOM   1693  O   PRO A 219     -22.963 -32.291   1.041  1.00 61.69           O  
ATOM   1694  CB  PRO A 219     -25.925 -33.039   2.040  1.00 56.69           C  
ATOM   1695  CG  PRO A 219     -27.277 -32.580   2.491  1.00 58.54           C  
ATOM   1696  CD  PRO A 219     -27.372 -31.135   2.094  1.00 47.84           C  
ATOM   1697  N   ASN A 220     -24.470 -31.046  -0.083  1.00 53.40           N  
ATOM   1698  CA  ASN A 220     -23.643 -30.959  -1.283  1.00 47.28           C  
ATOM   1699  C   ASN A 220     -22.549 -29.907  -1.204  1.00 44.64           C  
ATOM   1700  O   ASN A 220     -21.555 -29.980  -1.930  1.00 52.45           O  
ATOM   1701  CB  ASN A 220     -24.507 -30.725  -2.521  1.00 50.80           C  
ATOM   1702  CG  ASN A 220     -25.497 -31.843  -2.747  1.00 60.09           C  
ATOM   1703  OD1 ASN A 220     -25.159 -33.025  -2.616  1.00 48.45           O  
ATOM   1704  ND2 ASN A 220     -26.730 -31.481  -3.085  1.00 56.92           N  
ATOM   1705  N   GLY A 221     -22.728 -28.921  -0.333  1.00 44.73           N  
ATOM   1706  CA  GLY A 221     -21.702 -27.915  -0.157  1.00 46.97           C  
ATOM   1707  C   GLY A 221     -22.217 -26.650   0.482  1.00 43.11           C  
ATOM   1708  O   GLY A 221     -23.327 -26.607   1.010  1.00 47.24           O  
ATOM   1709  N   THR A 222     -21.389 -25.619   0.443  1.00 42.85           N  
ATOM   1710  CA  THR A 222     -21.719 -24.349   1.063  1.00 46.30           C  
ATOM   1711  C   THR A 222     -21.424 -23.230   0.084  1.00 46.42           C  
ATOM   1712  O   THR A 222     -20.859 -23.463  -0.991  1.00 44.42           O  
ATOM   1713  CB  THR A 222     -20.888 -24.101   2.345  1.00 50.76           C  
ATOM   1714  OG1 THR A 222     -19.527 -23.826   1.986  1.00 46.81           O  
ATOM   1715  CG2 THR A 222     -20.944 -25.310   3.280  1.00 42.57           C  
ATOM   1716  N   ALA A 223     -21.810 -22.017   0.460  1.00 40.25           N  
ATOM   1717  CA  ALA A 223     -21.571 -20.848  -0.370  1.00 58.09           C  
ATOM   1718  C   ALA A 223     -20.071 -20.633  -0.564  1.00 60.94           C  
ATOM   1719  O   ALA A 223     -19.621 -20.261  -1.653  1.00 44.57           O  
ATOM   1720  CB  ALA A 223     -22.218 -19.612   0.255  1.00 54.10           C  
ATOM   1721  N   ALA A 224     -19.306 -20.867   0.500  1.00 50.43           N  
ATOM   1722  CA  ALA A 224     -17.849 -20.799   0.425  1.00 58.98           C  
ATOM   1723  C   ALA A 224     -17.297 -21.649  -0.727  1.00 58.26           C  
ATOM   1724  O   ALA A 224     -16.448 -21.195  -1.492  1.00 61.46           O  
ATOM   1725  CB  ALA A 224     -17.234 -21.228   1.743  1.00 63.40           C  
ATOM   1726  N   ASP A 225     -17.784 -22.880  -0.848  1.00 51.86           N  
ATOM   1727  CA  ASP A 225     -17.360 -23.758  -1.935  1.00 58.64           C  
ATOM   1728  C   ASP A 225     -17.594 -23.081  -3.281  1.00 60.81           C  
ATOM   1729  O   ASP A 225     -16.816 -23.249  -4.221  1.00 51.76           O  
ATOM   1730  CB  ASP A 225     -18.136 -25.083  -1.914  1.00 50.02           C  
ATOM   1731  CG  ASP A 225     -17.940 -25.859  -0.631  1.00 66.83           C  
ATOM   1732  OD1 ASP A 225     -16.949 -25.593   0.089  1.00 71.39           O  
ATOM   1733  OD2 ASP A 225     -18.784 -26.736  -0.342  1.00 61.99           O  
ATOM   1734  N   GLY A 226     -18.687 -22.330  -3.364  1.00 56.77           N  
ATOM   1735  CA  GLY A 226     -19.055 -21.638  -4.583  1.00 48.45           C  
ATOM   1736  C   GLY A 226     -18.074 -20.543  -4.937  1.00 54.37           C  
ATOM   1737  O   GLY A 226     -17.629 -20.456  -6.090  1.00 62.28           O  
ATOM   1738  N   LEU A 227     -17.756 -19.699  -3.956  1.00 40.50           N  
ATOM   1739  CA  LEU A 227     -16.751 -18.655  -4.129  1.00 61.72           C  
ATOM   1740  C   LEU A 227     -15.416 -19.280  -4.503  1.00 59.33           C  
ATOM   1741  O   LEU A 227     -14.726 -18.817  -5.414  1.00 61.04           O  
ATOM   1742  CB  LEU A 227     -16.600 -17.824  -2.851  1.00 50.74           C  
ATOM   1743  CG  LEU A 227     -17.716 -16.824  -2.547  1.00 55.42           C  
ATOM   1744  CD1 LEU A 227     -17.442 -16.083  -1.243  1.00 62.35           C  
ATOM   1745  CD2 LEU A 227     -17.864 -15.842  -3.687  1.00 46.89           C  
ATOM   1746  N   ASN A 228     -15.059 -20.337  -3.784  1.00 61.57           N  
ATOM   1747  CA  ASN A 228     -13.882 -21.123  -4.102  1.00 59.90           C  
ATOM   1748  C   ASN A 228     -13.821 -21.456  -5.593  1.00 61.52           C  
ATOM   1749  O   ASN A 228     -12.939 -20.989  -6.314  1.00 64.81           O  
ATOM   1750  CB  ASN A 228     -13.893 -22.414  -3.283  1.00 69.65           C  
ATOM   1751  CG  ASN A 228     -12.561 -23.120  -3.302  1.00 73.84           C  
ATOM   1752  OD1 ASN A 228     -11.646 -22.759  -2.562  1.00 85.69           O  
ATOM   1753  ND2 ASN A 228     -12.440 -24.135  -4.151  1.00 69.24           N  
ATOM   1754  N   PHE A 229     -14.770 -22.263  -6.053  1.00 56.98           N  
ATOM   1755  CA  PHE A 229     -14.829 -22.652  -7.455  1.00 61.03           C  
ATOM   1756  C   PHE A 229     -14.772 -21.436  -8.390  1.00 70.57           C  
ATOM   1757  O   PHE A 229     -14.056 -21.439  -9.393  1.00 64.69           O  
ATOM   1758  CB  PHE A 229     -16.094 -23.480  -7.717  1.00 54.28           C  
ATOM   1759  CG  PHE A 229     -16.514 -23.499  -9.154  1.00 70.61           C  
ATOM   1760  CD1 PHE A 229     -15.834 -24.280 -10.077  1.00 75.30           C  
ATOM   1761  CD2 PHE A 229     -17.581 -22.727  -9.589  1.00 63.90           C  
ATOM   1762  CE1 PHE A 229     -16.209 -24.291 -11.403  1.00 60.25           C  
ATOM   1763  CE2 PHE A 229     -17.963 -22.736 -10.912  1.00 60.10           C  
ATOM   1764  CZ  PHE A 229     -17.277 -23.517 -11.821  1.00 73.57           C  
ATOM   1765  N   LEU A 230     -15.521 -20.393  -8.051  1.00 62.92           N  
ATOM   1766  CA  LEU A 230     -15.595 -19.213  -8.900  1.00 68.04           C  
ATOM   1767  C   LEU A 230     -14.258 -18.494  -9.008  1.00 63.68           C  
ATOM   1768  O   LEU A 230     -13.865 -18.054 -10.085  1.00 60.94           O  
ATOM   1769  CB  LEU A 230     -16.655 -18.238  -8.379  1.00 62.52           C  
ATOM   1770  CG  LEU A 230     -16.831 -16.952  -9.193  1.00 66.51           C  
ATOM   1771  CD1 LEU A 230     -17.046 -17.268 -10.664  1.00 47.04           C  
ATOM   1772  CD2 LEU A 230     -17.984 -16.120  -8.654  1.00 59.74           C  
ATOM   1773  N   TRP A 231     -13.552 -18.380  -7.890  1.00 60.18           N  
ATOM   1774  CA  TRP A 231     -12.425 -17.457  -7.832  1.00 70.84           C  
ATOM   1775  C   TRP A 231     -11.023 -18.073  -7.878  1.00 77.04           C  
ATOM   1776  O   TRP A 231     -10.052 -17.365  -8.152  1.00 75.39           O  
ATOM   1777  CB  TRP A 231     -12.573 -16.511  -6.637  1.00 58.32           C  
ATOM   1778  CG  TRP A 231     -13.684 -15.530  -6.825  1.00 72.26           C  
ATOM   1779  CD1 TRP A 231     -14.746 -15.321  -5.997  1.00 80.57           C  
ATOM   1780  CD2 TRP A 231     -13.852 -14.631  -7.928  1.00 84.00           C  
ATOM   1781  NE1 TRP A 231     -15.561 -14.336  -6.510  1.00 81.46           N  
ATOM   1782  CE2 TRP A 231     -15.034 -13.898  -7.695  1.00 73.25           C  
ATOM   1783  CE3 TRP A 231     -13.118 -14.372  -9.088  1.00 82.04           C  
ATOM   1784  CZ2 TRP A 231     -15.495 -12.926  -8.578  1.00 81.20           C  
ATOM   1785  CZ3 TRP A 231     -13.583 -13.411  -9.963  1.00 75.80           C  
ATOM   1786  CH2 TRP A 231     -14.755 -12.697  -9.703  1.00 81.06           C  
ATOM   1787  N   THR A 232     -10.901 -19.371  -7.621  1.00 65.17           N  
ATOM   1788  CA  THR A 232      -9.593 -20.000  -7.774  1.00 76.30           C  
ATOM   1789  C   THR A 232      -9.134 -19.846  -9.224  1.00 61.67           C  
ATOM   1790  O   THR A 232      -9.871 -20.178 -10.159  1.00 61.10           O  
ATOM   1791  CB  THR A 232      -9.566 -21.495  -7.339  1.00 73.70           C  
ATOM   1792  OG1 THR A 232     -10.243 -22.308  -8.308  1.00 77.28           O  
ATOM   1793  CG2 THR A 232     -10.205 -21.670  -5.972  1.00 63.26           C  
ATOM   1794  N   PRO A 233      -7.915 -19.324  -9.412  1.00 64.84           N  
ATOM   1795  CA  PRO A 233      -7.406 -19.013 -10.749  1.00 64.18           C  
ATOM   1796  C   PRO A 233      -7.074 -20.255 -11.560  1.00 64.50           C  
ATOM   1797  O   PRO A 233      -6.628 -21.261 -11.012  1.00 85.13           O  
ATOM   1798  CB  PRO A 233      -6.117 -18.234 -10.459  1.00 65.67           C  
ATOM   1799  CG  PRO A 233      -6.234 -17.783  -9.041  1.00 67.38           C  
ATOM   1800  CD  PRO A 233      -7.004 -18.858  -8.354  1.00 62.76           C  
ATOM   1801  N   ASP A 234      -7.306 -20.171 -12.862  1.00 69.94           N  
ATOM   1802  CA  ASP A 234      -6.802 -21.151 -13.809  1.00 67.02           C  
ATOM   1803  C   ASP A 234      -6.012 -20.369 -14.853  1.00 72.42           C  
ATOM   1804  O   ASP A 234      -6.530 -20.028 -15.918  1.00 63.51           O  
ATOM   1805  CB  ASP A 234      -7.950 -21.918 -14.457  1.00 59.06           C  
ATOM   1806  CG  ASP A 234      -7.470 -22.965 -15.444  1.00 82.61           C  
ATOM   1807  OD1 ASP A 234      -6.256 -23.269 -15.453  1.00 81.04           O  
ATOM   1808  OD2 ASP A 234      -8.311 -23.485 -16.211  1.00 85.65           O  
ATOM   1809  N   PHE A 235      -4.756 -20.076 -14.529  1.00 70.52           N  
ATOM   1810  CA  PHE A 235      -3.930 -19.194 -15.348  1.00 59.90           C  
ATOM   1811  C   PHE A 235      -3.605 -19.759 -16.724  1.00 72.32           C  
ATOM   1812  O   PHE A 235      -3.051 -19.055 -17.566  1.00 84.48           O  
ATOM   1813  CB  PHE A 235      -2.627 -18.862 -14.626  1.00 55.27           C  
ATOM   1814  CG  PHE A 235      -2.815 -18.060 -13.376  1.00 70.84           C  
ATOM   1815  CD1 PHE A 235      -2.569 -18.620 -12.132  1.00 72.86           C  
ATOM   1816  CD2 PHE A 235      -3.239 -16.744 -13.442  1.00 63.58           C  
ATOM   1817  CE1 PHE A 235      -2.733 -17.881 -10.977  1.00 66.43           C  
ATOM   1818  CE2 PHE A 235      -3.410 -16.000 -12.293  1.00 65.28           C  
ATOM   1819  CZ  PHE A 235      -3.155 -16.569 -11.057  1.00 77.72           C  
ATOM   1820  N   GLU A 236      -3.941 -21.025 -16.951  1.00 79.07           N  
ATOM   1821  CA  GLU A 236      -3.623 -21.675 -18.220  1.00 82.86           C  
ATOM   1822  C   GLU A 236      -4.581 -21.235 -19.321  1.00 78.62           C  
ATOM   1823  O   GLU A 236      -4.255 -21.298 -20.506  1.00 74.71           O  
ATOM   1824  CB  GLU A 236      -3.667 -23.199 -18.074  1.00 77.98           C  
ATOM   1825  CG  GLU A 236      -2.639 -23.936 -18.920  1.00 76.78           C  
ATOM   1826  CD  GLU A 236      -1.235 -23.862 -18.331  1.00 85.84           C  
ATOM   1827  OE1 GLU A 236      -0.605 -24.926 -18.162  1.00 90.28           O  
ATOM   1828  OE2 GLU A 236      -0.764 -22.745 -18.027  1.00 74.93           O  
ATOM   1829  N   LYS A 237      -5.768 -20.789 -18.921  1.00 79.20           N  
ATOM   1830  CA  LYS A 237      -6.786 -20.388 -19.879  1.00 70.59           C  
ATOM   1831  C   LYS A 237      -6.452 -19.046 -20.519  1.00 64.93           C  
ATOM   1832  O   LYS A 237      -6.983 -18.705 -21.572  1.00 78.92           O  
ATOM   1833  CB  LYS A 237      -8.166 -20.347 -19.222  1.00 70.23           C  
ATOM   1834  CG  LYS A 237      -8.634 -21.688 -18.689  1.00 69.01           C  
ATOM   1835  CD  LYS A 237     -10.066 -21.941 -19.113  1.00 75.60           C  
ATOM   1836  CE  LYS A 237     -10.198 -21.790 -20.622  1.00 78.77           C  
ATOM   1837  NZ  LYS A 237     -11.614 -21.761 -21.085  1.00 81.93           N  
ATOM   1838  N   LEU A 238      -5.565 -18.288 -19.883  1.00 68.49           N  
ATOM   1839  CA  LEU A 238      -5.126 -17.016 -20.442  1.00 69.46           C  
ATOM   1840  C   LEU A 238      -4.401 -17.229 -21.768  1.00 78.52           C  
ATOM   1841  O   LEU A 238      -4.395 -16.351 -22.633  1.00 75.94           O  
ATOM   1842  CB  LEU A 238      -4.242 -16.265 -19.448  1.00 71.09           C  
ATOM   1843  CG  LEU A 238      -4.943 -15.943 -18.126  1.00 65.15           C  
ATOM   1844  CD1 LEU A 238      -4.064 -15.078 -17.241  1.00 61.37           C  
ATOM   1845  CD2 LEU A 238      -6.283 -15.268 -18.388  1.00 60.68           C  
ATOM   1846  N   LYS A 239      -3.799 -18.404 -21.923  1.00 71.92           N  
ATOM   1847  CA  LYS A 239      -3.167 -18.769 -23.182  1.00 80.03           C  
ATOM   1848  C   LYS A 239      -4.186 -18.663 -24.306  1.00 73.73           C  
ATOM   1849  O   LYS A 239      -3.877 -18.193 -25.400  1.00 80.85           O  
ATOM   1850  CB  LYS A 239      -2.610 -20.195 -23.114  1.00 85.04           C  
ATOM   1851  CG  LYS A 239      -1.369 -20.351 -22.243  1.00 86.25           C  
ATOM   1852  CD  LYS A 239      -0.709 -21.711 -22.460  1.00 79.99           C  
ATOM   1853  CE  LYS A 239       0.661 -21.783 -21.788  1.00 87.41           C  
ATOM   1854  NZ  LYS A 239       1.384 -23.059 -22.086  1.00 79.15           N  
ATOM   1855  N   ASP A 240      -5.408 -19.098 -24.016  1.00 75.47           N  
ATOM   1856  CA  ASP A 240      -6.493 -19.105 -24.990  1.00 67.45           C  
ATOM   1857  C   ASP A 240      -6.891 -17.681 -25.357  1.00 70.65           C  
ATOM   1858  O   ASP A 240      -7.093 -16.842 -24.476  1.00 73.28           O  
ATOM   1859  CB  ASP A 240      -7.697 -19.866 -24.422  1.00 61.98           C  
ATOM   1860  CG  ASP A 240      -8.839 -19.992 -25.414  1.00 76.88           C  
ATOM   1861  OD1 ASP A 240      -8.757 -19.413 -26.517  1.00 87.69           O  
ATOM   1862  OD2 ASP A 240      -9.830 -20.680 -25.092  1.00 86.09           O  
ATOM   1863  N   PRO A 241      -6.982 -17.407 -26.666  1.00 75.19           N  
ATOM   1864  CA  PRO A 241      -7.451 -16.146 -27.261  1.00 77.25           C  
ATOM   1865  C   PRO A 241      -8.937 -15.858 -27.016  1.00 73.05           C  
ATOM   1866  O   PRO A 241      -9.324 -14.689 -26.947  1.00 70.62           O  
ATOM   1867  CB  PRO A 241      -7.230 -16.369 -28.763  1.00 72.61           C  
ATOM   1868  CG  PRO A 241      -6.164 -17.396 -28.845  1.00 77.67           C  
ATOM   1869  CD  PRO A 241      -6.379 -18.300 -27.672  1.00 68.01           C  
ATOM   1870  N   GLY A 242      -9.754 -16.901 -26.909  1.00 63.26           N  
ATOM   1871  CA  GLY A 242     -11.182 -16.728 -26.726  1.00 55.09           C  
ATOM   1872  C   GLY A 242     -11.524 -16.230 -25.334  1.00 57.99           C  
ATOM   1873  O   GLY A 242     -12.636 -15.764 -25.087  1.00 55.39           O  
ATOM   1874  N   VAL A 243     -10.563 -16.338 -24.423  1.00 56.21           N  
ATOM   1875  CA  VAL A 243     -10.723 -15.845 -23.061  1.00 60.78           C  
ATOM   1876  C   VAL A 243     -10.591 -14.328 -23.048  1.00 64.63           C  
ATOM   1877  O   VAL A 243     -11.260 -13.640 -22.272  1.00 56.17           O  
ATOM   1878  CB  VAL A 243      -9.674 -16.472 -22.115  1.00 67.36           C  
ATOM   1879  CG1 VAL A 243      -9.553 -15.675 -20.810  1.00 42.61           C  
ATOM   1880  CG2 VAL A 243     -10.019 -17.936 -21.842  1.00 66.35           C  
ATOM   1881  N   TRP A 244      -9.727 -13.812 -23.918  1.00 61.66           N  
ATOM   1882  CA  TRP A 244      -9.515 -12.373 -24.029  1.00 68.57           C  
ATOM   1883  C   TRP A 244     -10.667 -11.735 -24.784  1.00 53.75           C  
ATOM   1884  O   TRP A 244     -11.076 -10.615 -24.489  1.00 54.00           O  
ATOM   1885  CB  TRP A 244      -8.175 -12.079 -24.708  1.00 60.50           C  
ATOM   1886  CG  TRP A 244      -7.035 -12.438 -23.829  1.00 54.62           C  
ATOM   1887  CD1 TRP A 244      -6.496 -13.679 -23.650  1.00 56.77           C  
ATOM   1888  CD2 TRP A 244      -6.304 -11.555 -22.972  1.00 61.82           C  
ATOM   1889  NE1 TRP A 244      -5.464 -13.620 -22.744  1.00 61.56           N  
ATOM   1890  CE2 TRP A 244      -5.328 -12.326 -22.312  1.00 54.48           C  
ATOM   1891  CE3 TRP A 244      -6.378 -10.183 -22.701  1.00 58.49           C  
ATOM   1892  CZ2 TRP A 244      -4.433 -11.775 -21.402  1.00 57.00           C  
ATOM   1893  CZ3 TRP A 244      -5.487  -9.638 -21.800  1.00 47.79           C  
ATOM   1894  CH2 TRP A 244      -4.527 -10.431 -21.163  1.00 58.63           C  
ATOM   1895  N   ILE A 245     -11.196 -12.461 -25.754  1.00 45.64           N  
ATOM   1896  CA  ILE A 245     -12.389 -12.007 -26.441  1.00 53.54           C  
ATOM   1897  C   ILE A 245     -13.548 -11.960 -25.460  1.00 54.46           C  
ATOM   1898  O   ILE A 245     -14.287 -10.981 -25.417  1.00 47.49           O  
ATOM   1899  CB  ILE A 245     -12.742 -12.909 -27.620  1.00 41.75           C  
ATOM   1900  CG1 ILE A 245     -11.985 -12.446 -28.861  1.00 58.63           C  
ATOM   1901  CG2 ILE A 245     -14.239 -12.875 -27.892  1.00 50.12           C  
ATOM   1902  CD1 ILE A 245     -10.522 -12.125 -28.602  1.00 60.19           C  
ATOM   1903  N   ALA A 246     -13.694 -13.022 -24.669  1.00 50.35           N  
ATOM   1904  CA  ALA A 246     -14.765 -13.092 -23.687  1.00 49.22           C  
ATOM   1905  C   ALA A 246     -14.691 -11.913 -22.717  1.00 44.95           C  
ATOM   1906  O   ALA A 246     -15.707 -11.296 -22.403  1.00 39.20           O  
ATOM   1907  CB  ALA A 246     -14.708 -14.400 -22.931  1.00 48.98           C  
ATOM   1908  N   ALA A 247     -13.482 -11.606 -22.258  1.00 37.03           N  
ATOM   1909  CA  ALA A 247     -13.267 -10.534 -21.297  1.00 43.47           C  
ATOM   1910  C   ALA A 247     -13.588  -9.164 -21.891  1.00 50.88           C  
ATOM   1911  O   ALA A 247     -14.251  -8.342 -21.254  1.00 45.38           O  
ATOM   1912  CB  ALA A 247     -11.836 -10.562 -20.774  1.00 47.64           C  
ATOM   1913  N   VAL A 248     -13.101  -8.917 -23.103  1.00 40.19           N  
ATOM   1914  CA  VAL A 248     -13.336  -7.639 -23.755  1.00 45.84           C  
ATOM   1915  C   VAL A 248     -14.830  -7.487 -24.031  1.00 37.95           C  
ATOM   1916  O   VAL A 248     -15.416  -6.424 -23.810  1.00 43.85           O  
ATOM   1917  CB  VAL A 248     -12.540  -7.519 -25.077  1.00 47.55           C  
ATOM   1918  CG1 VAL A 248     -13.056  -6.361 -25.899  1.00 42.85           C  
ATOM   1919  CG2 VAL A 248     -11.049  -7.366 -24.783  1.00 43.28           C  
ATOM   1920  N   GLY A 249     -15.445  -8.562 -24.504  1.00 42.28           N  
ATOM   1921  CA  GLY A 249     -16.869  -8.568 -24.775  1.00 35.58           C  
ATOM   1922  C   GLY A 249     -17.668  -8.358 -23.496  1.00 38.37           C  
ATOM   1923  O   GLY A 249     -18.665  -7.633 -23.501  1.00 36.78           O  
ATOM   1924  N   GLN A 250     -17.234  -8.981 -22.402  1.00 33.43           N  
ATOM   1925  CA  GLN A 250     -17.958  -8.858 -21.137  1.00 35.70           C  
ATOM   1926  C   GLN A 250     -17.913  -7.421 -20.643  1.00 37.02           C  
ATOM   1927  O   GLN A 250     -18.917  -6.911 -20.156  1.00 34.08           O  
ATOM   1928  CB  GLN A 250     -17.428  -9.823 -20.069  1.00 42.34           C  
ATOM   1929  CG  GLN A 250     -18.093  -9.663 -18.702  1.00 35.66           C  
ATOM   1930  CD  GLN A 250     -19.617  -9.681 -18.772  1.00 34.51           C  
ATOM   1931  OE1 GLN A 250     -20.216 -10.271 -19.676  1.00 39.30           O  
ATOM   1932  NE2 GLN A 250     -20.251  -9.026 -17.812  1.00 35.45           N  
ATOM   1933  N   ILE A 251     -16.757  -6.769 -20.793  1.00 39.62           N  
ATOM   1934  CA  ILE A 251     -16.603  -5.349 -20.457  1.00 41.06           C  
ATOM   1935  C   ILE A 251     -17.505  -4.444 -21.298  1.00 39.67           C  
ATOM   1936  O   ILE A 251     -18.171  -3.548 -20.777  1.00 38.06           O  
ATOM   1937  CB  ILE A 251     -15.143  -4.876 -20.623  1.00 44.94           C  
ATOM   1938  CG1 ILE A 251     -14.277  -5.385 -19.467  1.00 39.75           C  
ATOM   1939  CG2 ILE A 251     -15.081  -3.359 -20.662  1.00 38.11           C  
ATOM   1940  CD1 ILE A 251     -14.715  -4.896 -18.106  1.00 40.78           C  
ATOM   1941  N   PHE A 252     -17.512  -4.687 -22.605  1.00 41.71           N  
ATOM   1942  CA  PHE A 252     -18.370  -3.977 -23.529  1.00 36.12           C  
ATOM   1943  C   PHE A 252     -19.837  -4.070 -23.129  1.00 40.79           C  
ATOM   1944  O   PHE A 252     -20.570  -3.081 -23.113  1.00 41.64           O  
ATOM   1945  CB  PHE A 252     -18.220  -4.610 -24.917  1.00 41.52           C  
ATOM   1946  CG  PHE A 252     -18.259  -3.628 -26.029  1.00 41.66           C  
ATOM   1947  CD1 PHE A 252     -19.461  -3.238 -26.586  1.00 40.41           C  
ATOM   1948  CD2 PHE A 252     -17.088  -3.089 -26.524  1.00 49.98           C  
ATOM   1949  CE1 PHE A 252     -19.489  -2.334 -27.608  1.00 37.05           C  
ATOM   1950  CE2 PHE A 252     -17.123  -2.177 -27.555  1.00 43.01           C  
ATOM   1951  CZ  PHE A 252     -18.321  -1.802 -28.092  1.00 36.00           C  
ATOM   1952  N   PHE A 253     -20.267  -5.290 -22.857  1.00 29.13           N  
ATOM   1953  CA  PHE A 253     -21.650  -5.578 -22.529  1.00 37.44           C  
ATOM   1954  C   PHE A 253     -21.999  -4.964 -21.163  1.00 34.89           C  
ATOM   1955  O   PHE A 253     -23.004  -4.265 -21.026  1.00 27.80           O  
ATOM   1956  CB  PHE A 253     -21.824  -7.091 -22.509  1.00 29.95           C  
ATOM   1957  CG  PHE A 253     -23.176  -7.565 -22.050  1.00 35.01           C  
ATOM   1958  CD1 PHE A 253     -24.221  -7.697 -22.948  1.00 37.99           C  
ATOM   1959  CD2 PHE A 253     -23.383  -7.952 -20.731  1.00 37.63           C  
ATOM   1960  CE1 PHE A 253     -25.459  -8.177 -22.533  1.00 46.18           C  
ATOM   1961  CE2 PHE A 253     -24.622  -8.431 -20.310  1.00 36.71           C  
ATOM   1962  CZ  PHE A 253     -25.660  -8.540 -21.205  1.00 37.06           C  
ATOM   1963  N   THR A 254     -21.155  -5.221 -20.168  1.00 32.22           N  
ATOM   1964  CA  THR A 254     -21.418  -4.718 -18.818  1.00 30.20           C  
ATOM   1965  C   THR A 254     -21.552  -3.194 -18.791  1.00 28.92           C  
ATOM   1966  O   THR A 254     -22.412  -2.657 -18.119  1.00 34.76           O  
ATOM   1967  CB  THR A 254     -20.393  -5.214 -17.751  1.00 31.33           C  
ATOM   1968  OG1 THR A 254     -21.014  -5.211 -16.456  1.00 33.18           O  
ATOM   1969  CG2 THR A 254     -19.173  -4.313 -17.697  1.00 30.77           C  
ATOM   1970  N   LEU A 255     -20.726  -2.485 -19.543  1.00 30.31           N  
ATOM   1971  CA  LEU A 255     -20.795  -1.033 -19.528  1.00 27.58           C  
ATOM   1972  C   LEU A 255     -21.813  -0.485 -20.550  1.00 33.84           C  
ATOM   1973  O   LEU A 255     -21.974   0.733 -20.695  1.00 32.32           O  
ATOM   1974  CB  LEU A 255     -19.414  -0.456 -19.805  1.00 25.06           C  
ATOM   1975  CG  LEU A 255     -18.369  -0.664 -18.715  1.00 29.41           C  
ATOM   1976  CD1 LEU A 255     -17.080   0.021 -19.125  1.00 30.62           C  
ATOM   1977  CD2 LEU A 255     -18.859  -0.088 -17.397  1.00 34.63           C  
ATOM   1978  N   SER A 256     -22.488  -1.381 -21.260  1.00 31.01           N  
ATOM   1979  CA  SER A 256     -23.463  -0.985 -22.284  1.00 31.14           C  
ATOM   1980  C   SER A 256     -22.862  -0.130 -23.404  1.00 31.68           C  
ATOM   1981  O   SER A 256     -23.509   0.791 -23.930  1.00 26.54           O  
ATOM   1982  CB  SER A 256     -24.640  -0.239 -21.638  1.00 30.55           C  
ATOM   1983  OG  SER A 256     -25.333  -1.066 -20.712  1.00 33.76           O  
ATOM   1984  N   LEU A 257     -21.626  -0.423 -23.782  1.00 25.66           N  
ATOM   1985  CA  LEU A 257     -20.972   0.423 -24.775  1.00 32.72           C  
ATOM   1986  C   LEU A 257     -21.480   0.080 -26.191  1.00 26.31           C  
ATOM   1987  O   LEU A 257     -21.807  -1.072 -26.468  1.00 26.22           O  
ATOM   1988  CB  LEU A 257     -19.452   0.273 -24.694  1.00 35.92           C  
ATOM   1989  CG  LEU A 257     -18.785   0.585 -23.342  1.00 34.99           C  
ATOM   1990  CD1 LEU A 257     -17.313   0.225 -23.387  1.00 35.25           C  
ATOM   1991  CD2 LEU A 257     -18.972   2.064 -22.991  1.00 28.15           C  
ATOM   1992  N   GLY A 258     -21.557   1.098 -27.045  1.00 30.21           N  
ATOM   1993  CA  GLY A 258     -21.932   0.943 -28.451  1.00 29.13           C  
ATOM   1994  C   GLY A 258     -23.432   0.819 -28.691  1.00 28.68           C  
ATOM   1995  O   GLY A 258     -23.876   0.649 -29.827  1.00 31.21           O  
ATOM   1996  N   PHE A 259     -24.210   0.925 -27.614  1.00 30.27           N  
ATOM   1997  CA  PHE A 259     -25.640   0.637 -27.638  1.00 31.13           C  
ATOM   1998  C   PHE A 259     -26.455   1.918 -27.769  1.00 29.88           C  
ATOM   1999  O   PHE A 259     -27.674   1.884 -27.920  1.00 32.88           O  
ATOM   2000  CB  PHE A 259     -26.051  -0.053 -26.334  1.00 27.56           C  
ATOM   2001  CG  PHE A 259     -25.794  -1.531 -26.295  1.00 28.43           C  
ATOM   2002  CD1 PHE A 259     -26.797  -2.437 -26.645  1.00 27.24           C  
ATOM   2003  CD2 PHE A 259     -24.567  -2.027 -25.881  1.00 25.58           C  
ATOM   2004  CE1 PHE A 259     -26.572  -3.809 -26.586  1.00 34.37           C  
ATOM   2005  CE2 PHE A 259     -24.335  -3.412 -25.817  1.00 29.67           C  
ATOM   2006  CZ  PHE A 259     -25.337  -4.301 -26.166  1.00 33.30           C  
ATOM   2007  N   GLY A 260     -25.791   3.058 -27.650  1.00 34.00           N  
ATOM   2008  CA  GLY A 260     -26.464   4.329 -27.839  1.00 34.96           C  
ATOM   2009  C   GLY A 260     -27.017   5.029 -26.605  1.00 29.66           C  
ATOM   2010  O   GLY A 260     -27.241   6.223 -26.657  1.00 32.38           O  
ATOM   2011  N   ALA A 261     -27.256   4.302 -25.513  1.00 34.08           N  
ATOM   2012  CA  ALA A 261     -27.864   4.901 -24.321  1.00 30.94           C  
ATOM   2013  C   ALA A 261     -26.950   5.902 -23.635  1.00 30.43           C  
ATOM   2014  O   ALA A 261     -27.402   6.958 -23.180  1.00 30.43           O  
ATOM   2015  CB  ALA A 261     -28.321   3.827 -23.318  1.00 29.76           C  
ATOM   2016  N   ILE A 262     -25.667   5.578 -23.555  1.00 25.34           N  
ATOM   2017  CA  ILE A 262     -24.716   6.481 -22.908  1.00 27.27           C  
ATOM   2018  C   ILE A 262     -24.656   7.791 -23.666  1.00 28.72           C  
ATOM   2019  O   ILE A 262     -24.675   8.867 -23.073  1.00 28.79           O  
ATOM   2020  CB  ILE A 262     -23.300   5.876 -22.833  1.00 26.90           C  
ATOM   2021  CG1 ILE A 262     -23.319   4.568 -22.029  1.00 32.96           C  
ATOM   2022  CG2 ILE A 262     -22.310   6.890 -22.243  1.00 26.52           C  
ATOM   2023  CD1 ILE A 262     -21.982   3.831 -22.032  1.00 32.42           C  
ATOM   2024  N   ILE A 263     -24.591   7.707 -24.991  1.00 28.43           N  
ATOM   2025  CA  ILE A 263     -24.513   8.921 -25.785  1.00 27.44           C  
ATOM   2026  C   ILE A 263     -25.725   9.803 -25.543  1.00 28.22           C  
ATOM   2027  O   ILE A 263     -25.601  11.008 -25.321  1.00 29.87           O  
ATOM   2028  CB  ILE A 263     -24.451   8.612 -27.277  1.00 28.71           C  
ATOM   2029  CG1 ILE A 263     -23.084   8.036 -27.659  1.00 24.47           C  
ATOM   2030  CG2 ILE A 263     -24.743   9.875 -28.075  1.00 28.88           C  
ATOM   2031  CD1 ILE A 263     -23.012   7.648 -29.199  1.00 26.74           C  
ATOM   2032  N   THR A 264     -26.908   9.202 -25.586  1.00 25.26           N  
ATOM   2033  CA  THR A 264     -28.132   9.996 -25.417  1.00 30.57           C  
ATOM   2034  C   THR A 264     -28.253  10.547 -23.990  1.00 29.17           C  
ATOM   2035  O   THR A 264     -28.632  11.695 -23.808  1.00 30.42           O  
ATOM   2036  CB  THR A 264     -29.414   9.193 -25.837  1.00 23.14           C  
ATOM   2037  OG1 THR A 264     -29.390   8.994 -27.248  1.00 26.57           O  
ATOM   2038  CG2 THR A 264     -30.677   9.949 -25.510  1.00 24.26           C  
ATOM   2039  N   TYR A 265     -27.927   9.734 -22.985  1.00 24.64           N  
ATOM   2040  CA  TYR A 265     -27.966  10.217 -21.603  1.00 28.25           C  
ATOM   2041  C   TYR A 265     -26.991  11.383 -21.425  1.00 29.84           C  
ATOM   2042  O   TYR A 265     -27.339  12.414 -20.862  1.00 30.65           O  
ATOM   2043  CB  TYR A 265     -27.573   9.123 -20.627  1.00 23.56           C  
ATOM   2044  CG  TYR A 265     -28.719   8.330 -20.048  1.00 28.38           C  
ATOM   2045  CD1 TYR A 265     -29.989   8.383 -20.605  1.00 29.86           C  
ATOM   2046  CD2 TYR A 265     -28.513   7.497 -18.960  1.00 29.25           C  
ATOM   2047  CE1 TYR A 265     -31.027   7.643 -20.076  1.00 28.47           C  
ATOM   2048  CE2 TYR A 265     -29.532   6.748 -18.427  1.00 32.15           C  
ATOM   2049  CZ  TYR A 265     -30.794   6.823 -18.983  1.00 27.93           C  
ATOM   2050  OH  TYR A 265     -31.806   6.057 -18.440  1.00 27.67           O  
ATOM   2051  N   ALA A 266     -25.767  11.201 -21.910  1.00 30.29           N  
ATOM   2052  CA  ALA A 266     -24.753  12.248 -21.858  1.00 32.50           C  
ATOM   2053  C   ALA A 266     -25.173  13.533 -22.598  1.00 35.71           C  
ATOM   2054  O   ALA A 266     -24.654  14.618 -22.314  1.00 31.26           O  
ATOM   2055  CB  ALA A 266     -23.422  11.721 -22.383  1.00 30.84           C  
ATOM   2056  N   SER A 267     -26.126  13.426 -23.525  1.00 28.80           N  
ATOM   2057  CA  SER A 267     -26.586  14.610 -24.253  1.00 32.77           C  
ATOM   2058  C   SER A 267     -27.408  15.545 -23.364  1.00 29.90           C  
ATOM   2059  O   SER A 267     -27.695  16.664 -23.756  1.00 30.65           O  
ATOM   2060  CB  SER A 267     -27.382  14.240 -25.531  1.00 31.44           C  
ATOM   2061  OG  SER A 267     -28.747  13.982 -25.235  1.00 31.08           O  
ATOM   2062  N   TYR A 268     -27.796  15.088 -22.177  1.00 31.70           N  
ATOM   2063  CA  TYR A 268     -28.465  15.976 -21.226  1.00 33.49           C  
ATOM   2064  C   TYR A 268     -27.525  16.509 -20.140  1.00 41.20           C  
ATOM   2065  O   TYR A 268     -27.953  17.208 -19.211  1.00 36.30           O  
ATOM   2066  CB  TYR A 268     -29.682  15.292 -20.618  1.00 29.03           C  
ATOM   2067  CG  TYR A 268     -30.570  14.714 -21.694  1.00 33.51           C  
ATOM   2068  CD1 TYR A 268     -31.384  15.540 -22.460  1.00 35.48           C  
ATOM   2069  CD2 TYR A 268     -30.569  13.356 -21.961  1.00 28.86           C  
ATOM   2070  CE1 TYR A 268     -32.193  15.025 -23.450  1.00 34.46           C  
ATOM   2071  CE2 TYR A 268     -31.373  12.824 -22.955  1.00 35.44           C  
ATOM   2072  CZ  TYR A 268     -32.184  13.659 -23.692  1.00 35.25           C  
ATOM   2073  OH  TYR A 268     -32.982  13.143 -24.683  1.00 32.45           O  
ATOM   2074  N   VAL A 269     -26.247  16.161 -20.265  1.00 36.56           N  
ATOM   2075  CA  VAL A 269     -25.184  16.784 -19.477  1.00 31.65           C  
ATOM   2076  C   VAL A 269     -24.847  18.154 -20.065  1.00 32.89           C  
ATOM   2077  O   VAL A 269     -24.731  18.306 -21.296  1.00 38.00           O  
ATOM   2078  CB  VAL A 269     -23.933  15.900 -19.477  1.00 32.98           C  
ATOM   2079  CG1 VAL A 269     -22.725  16.654 -18.899  1.00 35.54           C  
ATOM   2080  CG2 VAL A 269     -24.207  14.628 -18.671  1.00 29.63           C  
ATOM   2081  N   ARG A 270     -24.702  19.166 -19.213  1.00 31.39           N  
ATOM   2082  CA  ARG A 270     -24.486  20.530 -19.721  1.00 28.87           C  
ATOM   2083  C   ARG A 270     -23.126  20.680 -20.425  1.00 32.86           C  
ATOM   2084  O   ARG A 270     -22.215  19.867 -20.235  1.00 30.11           O  
ATOM   2085  CB  ARG A 270     -24.702  21.575 -18.617  1.00 38.43           C  
ATOM   2086  CG  ARG A 270     -26.159  21.641 -18.129  1.00 36.66           C  
ATOM   2087  CD  ARG A 270     -26.335  22.450 -16.841  1.00 39.73           C  
ATOM   2088  NE  ARG A 270     -27.733  22.452 -16.405  1.00 50.45           N  
ATOM   2089  CZ  ARG A 270     -28.650  23.340 -16.795  1.00 53.75           C  
ATOM   2090  NH1 ARG A 270     -28.332  24.322 -17.632  1.00 55.55           N  
ATOM   2091  NH2 ARG A 270     -29.895  23.251 -16.344  1.00 55.12           N  
ATOM   2092  N   LYS A 271     -23.002  21.710 -21.253  1.00 30.24           N  
ATOM   2093  CA  LYS A 271     -21.880  21.818 -22.178  1.00 36.36           C  
ATOM   2094  C   LYS A 271     -20.513  21.629 -21.529  1.00 43.17           C  
ATOM   2095  O   LYS A 271     -19.650  20.957 -22.086  1.00 40.81           O  
ATOM   2096  CB  LYS A 271     -21.923  23.158 -22.903  1.00 47.91           C  
ATOM   2097  N   ASP A 272     -20.315  22.238 -20.362  1.00 38.01           N  
ATOM   2098  CA  ASP A 272     -19.016  22.212 -19.694  1.00 42.48           C  
ATOM   2099  C   ASP A 272     -19.069  21.439 -18.395  1.00 39.73           C  
ATOM   2100  O   ASP A 272     -18.092  21.394 -17.659  1.00 37.99           O  
ATOM   2101  CB  ASP A 272     -18.513  23.633 -19.398  1.00 53.17           C  
ATOM   2102  CG  ASP A 272     -18.400  24.485 -20.644  1.00 59.49           C  
ATOM   2103  OD1 ASP A 272     -17.980  23.957 -21.697  1.00 48.11           O  
ATOM   2104  OD2 ASP A 272     -18.743  25.685 -20.570  1.00 67.99           O  
ATOM   2105  N   GLN A 273     -20.213  20.835 -18.109  1.00 38.03           N  
ATOM   2106  CA  GLN A 273     -20.330  19.986 -16.935  1.00 36.58           C  
ATOM   2107  C   GLN A 273     -19.480  18.723 -17.090  1.00 44.01           C  
ATOM   2108  O   GLN A 273     -19.471  18.086 -18.151  1.00 43.97           O  
ATOM   2109  CB  GLN A 273     -21.784  19.616 -16.696  1.00 34.45           C  
ATOM   2110  CG  GLN A 273     -21.958  18.470 -15.756  1.00 30.57           C  
ATOM   2111  CD  GLN A 273     -23.411  18.142 -15.542  1.00 42.04           C  
ATOM   2112  OE1 GLN A 273     -24.294  18.807 -16.089  1.00 36.41           O  
ATOM   2113  NE2 GLN A 273     -23.675  17.117 -14.736  1.00 36.52           N  
ATOM   2114  N   ASP A 274     -18.770  18.371 -16.025  1.00 32.64           N  
ATOM   2115  CA  ASP A 274     -17.842  17.251 -16.023  1.00 27.61           C  
ATOM   2116  C   ASP A 274     -18.448  15.954 -16.546  1.00 36.17           C  
ATOM   2117  O   ASP A 274     -19.608  15.647 -16.279  1.00 35.70           O  
ATOM   2118  CB  ASP A 274     -17.315  17.009 -14.592  1.00 28.34           C  
ATOM   2119  CG  ASP A 274     -16.780  15.594 -14.394  1.00 34.56           C  
ATOM   2120  OD1 ASP A 274     -15.539  15.402 -14.424  1.00 37.87           O  
ATOM   2121  OD2 ASP A 274     -17.603  14.659 -14.218  1.00 42.59           O  
ATOM   2122  N   ILE A 275     -17.633  15.186 -17.257  1.00 33.68           N  
ATOM   2123  CA  ILE A 275     -17.995  13.842 -17.671  1.00 36.18           C  
ATOM   2124  C   ILE A 275     -16.880  12.860 -17.308  1.00 31.63           C  
ATOM   2125  O   ILE A 275     -17.103  11.657 -17.258  1.00 33.44           O  
ATOM   2126  CB  ILE A 275     -18.284  13.769 -19.190  1.00 34.05           C  
ATOM   2127  CG1 ILE A 275     -17.053  14.195 -19.990  1.00 35.57           C  
ATOM   2128  CG2 ILE A 275     -19.476  14.636 -19.548  1.00 28.06           C  
ATOM   2129  CD1 ILE A 275     -17.150  13.883 -21.510  1.00 42.29           C  
ATOM   2130  N   VAL A 276     -15.684  13.376 -17.029  1.00 35.92           N  
ATOM   2131  CA  VAL A 276     -14.545  12.505 -16.743  1.00 29.73           C  
ATOM   2132  C   VAL A 276     -14.750  11.747 -15.440  1.00 36.83           C  
ATOM   2133  O   VAL A 276     -14.696  10.503 -15.401  1.00 34.98           O  
ATOM   2134  CB  VAL A 276     -13.214  13.285 -16.638  1.00 35.81           C  
ATOM   2135  CG1 VAL A 276     -12.091  12.354 -16.178  1.00 34.54           C  
ATOM   2136  CG2 VAL A 276     -12.864  13.905 -17.960  1.00 35.84           C  
ATOM   2137  N   LEU A 277     -14.979  12.491 -14.366  1.00 31.56           N  
ATOM   2138  CA  LEU A 277     -15.132  11.863 -13.064  1.00 36.56           C  
ATOM   2139  C   LEU A 277     -16.512  11.217 -12.953  1.00 30.28           C  
ATOM   2140  O   LEU A 277     -16.642  10.134 -12.414  1.00 33.73           O  
ATOM   2141  CB  LEU A 277     -14.929  12.883 -11.928  1.00 37.82           C  
ATOM   2142  CG  LEU A 277     -15.126  12.369 -10.496  1.00 34.78           C  
ATOM   2143  CD1 LEU A 277     -14.091  11.309 -10.129  1.00 38.39           C  
ATOM   2144  CD2 LEU A 277     -15.091  13.526  -9.485  1.00 41.97           C  
ATOM   2145  N   SER A 278     -17.541  11.900 -13.441  1.00 28.59           N  
ATOM   2146  CA  SER A 278     -18.880  11.334 -13.415  1.00 33.23           C  
ATOM   2147  C   SER A 278     -18.935   9.994 -14.163  1.00 30.40           C  
ATOM   2148  O   SER A 278     -19.458   9.014 -13.653  1.00 33.49           O  
ATOM   2149  CB  SER A 278     -19.882  12.318 -14.006  1.00 33.15           C  
ATOM   2150  OG  SER A 278     -19.856  13.508 -13.236  1.00 37.38           O  
ATOM   2151  N   GLY A 279     -18.374   9.955 -15.364  1.00 35.25           N  
ATOM   2152  CA  GLY A 279     -18.334   8.718 -16.121  1.00 32.61           C  
ATOM   2153  C   GLY A 279     -17.555   7.647 -15.397  1.00 34.97           C  
ATOM   2154  O   GLY A 279     -18.031   6.531 -15.229  1.00 37.37           O  
ATOM   2155  N   LEU A 280     -16.351   7.981 -14.953  1.00 40.31           N  
ATOM   2156  CA  LEU A 280     -15.566   7.044 -14.150  1.00 39.15           C  
ATOM   2157  C   LEU A 280     -16.352   6.494 -12.949  1.00 34.90           C  
ATOM   2158  O   LEU A 280     -16.333   5.291 -12.672  1.00 42.19           O  
ATOM   2159  CB  LEU A 280     -14.284   7.719 -13.668  1.00 39.62           C  
ATOM   2160  CG  LEU A 280     -13.250   6.859 -12.952  1.00 54.18           C  
ATOM   2161  CD1 LEU A 280     -12.865   5.628 -13.781  1.00 51.29           C  
ATOM   2162  CD2 LEU A 280     -12.024   7.719 -12.633  1.00 56.94           C  
ATOM   2163  N   THR A 281     -17.047   7.373 -12.236  1.00 34.85           N  
ATOM   2164  CA  THR A 281     -17.779   6.957 -11.039  1.00 31.05           C  
ATOM   2165  C   THR A 281     -18.925   5.999 -11.365  1.00 38.03           C  
ATOM   2166  O   THR A 281     -19.162   5.041 -10.623  1.00 35.62           O  
ATOM   2167  CB  THR A 281     -18.302   8.181 -10.236  1.00 36.39           C  
ATOM   2168  OG1 THR A 281     -17.191   8.985  -9.817  1.00 37.16           O  
ATOM   2169  CG2 THR A 281     -19.091   7.739  -8.996  1.00 32.23           C  
ATOM   2170  N   ALA A 282     -19.619   6.245 -12.479  1.00 36.80           N  
ATOM   2171  CA  ALA A 282     -20.723   5.378 -12.895  1.00 35.94           C  
ATOM   2172  C   ALA A 282     -20.202   4.012 -13.296  1.00 28.23           C  
ATOM   2173  O   ALA A 282     -20.828   2.988 -13.010  1.00 32.53           O  
ATOM   2174  CB  ALA A 282     -21.516   6.003 -14.048  1.00 34.27           C  
ATOM   2175  N   ALA A 283     -19.054   3.996 -13.965  1.00 31.88           N  
ATOM   2176  CA  ALA A 283     -18.416   2.738 -14.353  1.00 32.47           C  
ATOM   2177  C   ALA A 283     -18.008   1.935 -13.121  1.00 35.83           C  
ATOM   2178  O   ALA A 283     -18.212   0.719 -13.053  1.00 38.50           O  
ATOM   2179  CB  ALA A 283     -17.211   3.020 -15.221  1.00 34.95           C  
ATOM   2180  N   THR A 284     -17.427   2.619 -12.139  1.00 36.19           N  
ATOM   2181  CA  THR A 284     -16.970   1.938 -10.920  1.00 34.33           C  
ATOM   2182  C   THR A 284     -18.128   1.326 -10.160  1.00 27.17           C  
ATOM   2183  O   THR A 284     -18.010   0.237  -9.608  1.00 30.11           O  
ATOM   2184  CB  THR A 284     -16.247   2.913  -9.967  1.00 37.00           C  
ATOM   2185  OG1 THR A 284     -15.131   3.494 -10.644  1.00 43.80           O  
ATOM   2186  CG2 THR A 284     -15.757   2.191  -8.734  1.00 47.48           C  
ATOM   2187  N   LEU A 285     -19.240   2.047 -10.090  1.00 31.51           N  
ATOM   2188  CA  LEU A 285     -20.438   1.509  -9.458  1.00 25.73           C  
ATOM   2189  C   LEU A 285     -20.861   0.214 -10.143  1.00 28.52           C  
ATOM   2190  O   LEU A 285     -21.184  -0.773  -9.480  1.00 30.43           O  
ATOM   2191  CB  LEU A 285     -21.579   2.529  -9.498  1.00 36.71           C  
ATOM   2192  CG  LEU A 285     -21.448   3.741  -8.570  1.00 43.42           C  
ATOM   2193  CD1 LEU A 285     -22.654   4.647  -8.691  1.00 35.39           C  
ATOM   2194  CD2 LEU A 285     -21.287   3.280  -7.132  1.00 47.62           C  
ATOM   2195  N   ASN A 286     -20.857   0.219 -11.476  1.00 29.21           N  
ATOM   2196  CA  ASN A 286     -21.222  -0.980 -12.214  1.00 23.47           C  
ATOM   2197  C   ASN A 286     -20.281  -2.141 -11.918  1.00 26.58           C  
ATOM   2198  O   ASN A 286     -20.709  -3.265 -11.745  1.00 29.47           O  
ATOM   2199  CB  ASN A 286     -21.199  -0.732 -13.718  1.00 25.05           C  
ATOM   2200  CG  ASN A 286     -21.423  -1.996 -14.476  1.00 34.70           C  
ATOM   2201  OD1 ASN A 286     -22.551  -2.472 -14.547  1.00 29.94           O  
ATOM   2202  ND2 ASN A 286     -20.346  -2.605 -14.978  1.00 33.17           N  
ATOM   2203  N   GLU A 287     -18.986  -1.847 -11.872  1.00 31.68           N  
ATOM   2204  CA  GLU A 287     -17.972  -2.851 -11.576  1.00 34.92           C  
ATOM   2205  C   GLU A 287     -18.131  -3.440 -10.175  1.00 33.87           C  
ATOM   2206  O   GLU A 287     -18.032  -4.650  -9.989  1.00 39.71           O  
ATOM   2207  CB  GLU A 287     -16.572  -2.261 -11.776  1.00 37.79           C  
ATOM   2208  CG  GLU A 287     -16.297  -1.912 -13.231  1.00 39.55           C  
ATOM   2209  CD  GLU A 287     -16.621  -3.079 -14.167  1.00 42.30           C  
ATOM   2210  OE1 GLU A 287     -16.043  -4.178 -13.995  1.00 41.86           O  
ATOM   2211  OE2 GLU A 287     -17.459  -2.898 -15.066  1.00 35.26           O  
ATOM   2212  N   LYS A 288     -18.394  -2.597  -9.186  1.00 36.89           N  
ATOM   2213  CA  LYS A 288     -18.633  -3.120  -7.839  1.00 40.95           C  
ATOM   2214  C   LYS A 288     -19.869  -4.010  -7.824  1.00 44.59           C  
ATOM   2215  O   LYS A 288     -19.845  -5.105  -7.252  1.00 40.38           O  
ATOM   2216  CB  LYS A 288     -18.766  -1.993  -6.811  1.00 35.57           C  
ATOM   2217  CG  LYS A 288     -17.437  -1.371  -6.442  1.00 44.31           C  
ATOM   2218  CD  LYS A 288     -17.611  -0.031  -5.746  1.00 47.31           C  
ATOM   2219  CE  LYS A 288     -16.273   0.482  -5.228  1.00 55.56           C  
ATOM   2220  NZ  LYS A 288     -16.187   1.967  -5.334  1.00 58.11           N  
ATOM   2221  N   ALA A 289     -20.947  -3.547  -8.455  1.00 32.50           N  
ATOM   2222  CA  ALA A 289     -22.166  -4.342  -8.468  1.00 36.34           C  
ATOM   2223  C   ALA A 289     -21.896  -5.658  -9.185  1.00 36.40           C  
ATOM   2224  O   ALA A 289     -22.390  -6.717  -8.789  1.00 36.17           O  
ATOM   2225  CB  ALA A 289     -23.305  -3.582  -9.126  1.00 25.01           C  
ATOM   2226  N   GLU A 290     -21.080  -5.583 -10.232  1.00 36.76           N  
ATOM   2227  CA  GLU A 290     -20.742  -6.762 -11.019  1.00 40.04           C  
ATOM   2228  C   GLU A 290     -19.822  -7.755 -10.306  1.00 35.80           C  
ATOM   2229  O   GLU A 290     -20.181  -8.917 -10.129  1.00 35.21           O  
ATOM   2230  CB  GLU A 290     -20.105  -6.354 -12.345  1.00 34.49           C  
ATOM   2231  CG  GLU A 290     -19.616  -7.534 -13.163  1.00 41.54           C  
ATOM   2232  CD  GLU A 290     -19.958  -7.377 -14.641  1.00 43.52           C  
ATOM   2233  OE1 GLU A 290     -21.162  -7.233 -14.948  1.00 37.11           O  
ATOM   2234  OE2 GLU A 290     -19.029  -7.390 -15.479  1.00 35.97           O  
ATOM   2235  N   VAL A 291     -18.624  -7.326  -9.929  1.00 33.21           N  
ATOM   2236  CA  VAL A 291     -17.688  -8.291  -9.348  1.00 45.52           C  
ATOM   2237  C   VAL A 291     -17.972  -8.616  -7.883  1.00 40.04           C  
ATOM   2238  O   VAL A 291     -17.869  -9.772  -7.484  1.00 38.13           O  
ATOM   2239  CB  VAL A 291     -16.180  -7.944  -9.581  1.00 51.65           C  
ATOM   2240  CG1 VAL A 291     -16.004  -6.518 -10.045  1.00 53.13           C  
ATOM   2241  CG2 VAL A 291     -15.355  -8.234  -8.329  1.00 51.07           C  
ATOM   2242  N   ILE A 292     -18.347  -7.620  -7.086  1.00 41.22           N  
ATOM   2243  CA  ILE A 292     -18.572  -7.886  -5.658  1.00 38.77           C  
ATOM   2244  C   ILE A 292     -19.912  -8.572  -5.416  1.00 48.31           C  
ATOM   2245  O   ILE A 292     -19.979  -9.607  -4.762  1.00 43.45           O  
ATOM   2246  CB  ILE A 292     -18.520  -6.613  -4.793  1.00 39.81           C  
ATOM   2247  CG1 ILE A 292     -17.151  -5.939  -4.917  1.00 47.34           C  
ATOM   2248  CG2 ILE A 292     -18.819  -6.949  -3.332  1.00 39.49           C  
ATOM   2249  CD1 ILE A 292     -16.015  -6.938  -5.131  1.00 58.26           C  
ATOM   2250  N   LEU A 293     -20.981  -7.985  -5.942  1.00 40.14           N  
ATOM   2251  CA  LEU A 293     -22.313  -8.499  -5.671  1.00 31.59           C  
ATOM   2252  C   LEU A 293     -22.651  -9.657  -6.583  1.00 36.59           C  
ATOM   2253  O   LEU A 293     -22.966 -10.749  -6.114  1.00 40.37           O  
ATOM   2254  CB  LEU A 293     -23.342  -7.377  -5.784  1.00 38.52           C  
ATOM   2255  CG  LEU A 293     -23.010  -6.171  -4.891  1.00 39.16           C  
ATOM   2256  CD1 LEU A 293     -23.990  -5.027  -5.121  1.00 37.28           C  
ATOM   2257  CD2 LEU A 293     -22.977  -6.572  -3.407  1.00 39.58           C  
ATOM   2258  N   GLY A 294     -22.569  -9.422  -7.892  1.00 45.37           N  
ATOM   2259  CA  GLY A 294     -22.891 -10.446  -8.867  1.00 34.12           C  
ATOM   2260  C   GLY A 294     -22.025 -11.677  -8.727  1.00 36.48           C  
ATOM   2261  O   GLY A 294     -22.476 -12.798  -8.942  1.00 36.83           O  
ATOM   2262  N   GLY A 295     -20.768 -11.470  -8.361  1.00 41.46           N  
ATOM   2263  CA  GLY A 295     -19.847 -12.580  -8.185  1.00 41.45           C  
ATOM   2264  C   GLY A 295     -20.182 -13.410  -6.961  1.00 41.86           C  
ATOM   2265  O   GLY A 295     -19.726 -14.550  -6.835  1.00 50.55           O  
ATOM   2266  N   SER A 296     -21.012 -12.855  -6.079  1.00 36.35           N  
ATOM   2267  CA  SER A 296     -21.269 -13.457  -4.768  1.00 40.39           C  
ATOM   2268  C   SER A 296     -22.610 -14.178  -4.628  1.00 43.86           C  
ATOM   2269  O   SER A 296     -22.823 -14.913  -3.666  1.00 45.00           O  
ATOM   2270  CB  SER A 296     -21.164 -12.390  -3.687  1.00 39.32           C  
ATOM   2271  OG  SER A 296     -19.850 -11.889  -3.621  1.00 42.08           O  
ATOM   2272  N   ILE A 297     -23.523 -13.960  -5.571  1.00 38.74           N  
ATOM   2273  CA  ILE A 297     -24.874 -14.514  -5.441  1.00 38.32           C  
ATOM   2274  C   ILE A 297     -25.122 -15.803  -6.227  1.00 34.50           C  
ATOM   2275  O   ILE A 297     -25.135 -16.897  -5.668  1.00 36.31           O  
ATOM   2276  CB  ILE A 297     -25.962 -13.467  -5.824  1.00 37.61           C  
ATOM   2277  CG1 ILE A 297     -25.817 -12.203  -4.979  1.00 32.03           C  
ATOM   2278  CG2 ILE A 297     -27.364 -14.064  -5.680  1.00 31.44           C  
ATOM   2279  CD1 ILE A 297     -26.662 -11.025  -5.487  1.00 35.51           C  
ATOM   2280  N   SER A 298     -25.316 -15.672  -7.535  1.00 37.11           N  
ATOM   2281  CA  SER A 298     -25.850 -16.771  -8.339  1.00 33.47           C  
ATOM   2282  C   SER A 298     -24.995 -18.034  -8.339  1.00 35.84           C  
ATOM   2283  O   SER A 298     -25.513 -19.140  -8.138  1.00 38.37           O  
ATOM   2284  CB  SER A 298     -26.127 -16.305  -9.776  1.00 35.93           C  
ATOM   2285  OG  SER A 298     -24.934 -15.958 -10.447  1.00 33.23           O  
ATOM   2286  N   ILE A 299     -23.700 -17.893  -8.596  1.00 33.84           N  
ATOM   2287  CA  ILE A 299     -22.865 -19.087  -8.692  1.00 44.21           C  
ATOM   2288  C   ILE A 299     -22.684 -19.745  -7.319  1.00 35.71           C  
ATOM   2289  O   ILE A 299     -22.896 -20.944  -7.176  1.00 38.14           O  
ATOM   2290  CB  ILE A 299     -21.507 -18.811  -9.352  1.00 47.94           C  
ATOM   2291  CG1 ILE A 299     -21.709 -18.457 -10.829  1.00 36.30           C  
ATOM   2292  CG2 ILE A 299     -20.584 -20.028  -9.186  1.00 49.91           C  
ATOM   2293  CD1 ILE A 299     -22.254 -19.601 -11.649  1.00 45.95           C  
ATOM   2294  N   PRO A 300     -22.300 -18.956  -6.307  1.00 40.18           N  
ATOM   2295  CA  PRO A 300     -22.165 -19.543  -4.969  1.00 40.26           C  
ATOM   2296  C   PRO A 300     -23.431 -20.271  -4.518  1.00 44.82           C  
ATOM   2297  O   PRO A 300     -23.313 -21.300  -3.862  1.00 45.81           O  
ATOM   2298  CB  PRO A 300     -21.901 -18.326  -4.090  1.00 40.62           C  
ATOM   2299  CG  PRO A 300     -21.205 -17.364  -5.009  1.00 44.00           C  
ATOM   2300  CD  PRO A 300     -21.914 -17.532  -6.323  1.00 36.84           C  
ATOM   2301  N   ALA A 301     -24.611 -19.753  -4.863  1.00 38.10           N  
ATOM   2302  CA  ALA A 301     -25.858 -20.410  -4.499  1.00 31.62           C  
ATOM   2303  C   ALA A 301     -25.939 -21.756  -5.179  1.00 37.70           C  
ATOM   2304  O   ALA A 301     -26.190 -22.776  -4.543  1.00 37.49           O  
ATOM   2305  CB  ALA A 301     -27.054 -19.546  -4.877  1.00 39.13           C  
ATOM   2306  N   ALA A 302     -25.706 -21.751  -6.485  1.00 39.62           N  
ATOM   2307  CA  ALA A 302     -25.854 -22.948  -7.291  1.00 42.15           C  
ATOM   2308  C   ALA A 302     -24.878 -24.023  -6.870  1.00 34.81           C  
ATOM   2309  O   ALA A 302     -25.221 -25.193  -6.843  1.00 38.60           O  
ATOM   2310  CB  ALA A 302     -25.691 -22.626  -8.793  1.00 32.49           C  
ATOM   2311  N   VAL A 303     -23.654 -23.622  -6.572  1.00 41.13           N  
ATOM   2312  CA  VAL A 303     -22.646 -24.567  -6.115  1.00 45.50           C  
ATOM   2313  C   VAL A 303     -22.879 -24.987  -4.656  1.00 44.64           C  
ATOM   2314  O   VAL A 303     -22.633 -26.130  -4.296  1.00 45.72           O  
ATOM   2315  CB  VAL A 303     -21.224 -24.007  -6.295  1.00 51.43           C  
ATOM   2316  CG1 VAL A 303     -20.201 -25.013  -5.811  1.00 49.29           C  
ATOM   2317  CG2 VAL A 303     -20.979 -23.662  -7.764  1.00 53.84           C  
ATOM   2318  N   ALA A 304     -23.360 -24.077  -3.818  1.00 40.73           N  
ATOM   2319  CA  ALA A 304     -23.678 -24.468  -2.450  1.00 46.49           C  
ATOM   2320  C   ALA A 304     -24.677 -25.610  -2.506  1.00 59.27           C  
ATOM   2321  O   ALA A 304     -24.540 -26.617  -1.799  1.00 52.18           O  
ATOM   2322  CB  ALA A 304     -24.255 -23.305  -1.658  1.00 43.17           C  
ATOM   2323  N   PHE A 305     -25.669 -25.461  -3.380  1.00 49.93           N  
ATOM   2324  CA  PHE A 305     -26.785 -26.388  -3.405  1.00 45.76           C  
ATOM   2325  C   PHE A 305     -26.489 -27.642  -4.206  1.00 45.98           C  
ATOM   2326  O   PHE A 305     -26.852 -28.745  -3.802  1.00 50.76           O  
ATOM   2327  CB  PHE A 305     -28.045 -25.715  -3.946  1.00 45.15           C  
ATOM   2328  CG  PHE A 305     -29.254 -26.589  -3.880  1.00 46.57           C  
ATOM   2329  CD1 PHE A 305     -30.087 -26.552  -2.774  1.00 48.96           C  
ATOM   2330  CD2 PHE A 305     -29.537 -27.476  -4.903  1.00 46.37           C  
ATOM   2331  CE1 PHE A 305     -31.198 -27.372  -2.697  1.00 45.83           C  
ATOM   2332  CE2 PHE A 305     -30.650 -28.299  -4.837  1.00 59.41           C  
ATOM   2333  CZ  PHE A 305     -31.483 -28.243  -3.726  1.00 58.94           C  
ATOM   2334  N   PHE A 306     -25.831 -27.480  -5.342  1.00 41.98           N  
ATOM   2335  CA  PHE A 306     -25.577 -28.614  -6.210  1.00 47.08           C  
ATOM   2336  C   PHE A 306     -24.181 -29.183  -6.012  1.00 47.52           C  
ATOM   2337  O   PHE A 306     -23.903 -30.308  -6.417  1.00 48.46           O  
ATOM   2338  CB  PHE A 306     -25.803 -28.241  -7.677  1.00 42.78           C  
ATOM   2339  CG  PHE A 306     -27.252 -28.064  -8.034  1.00 50.91           C  
ATOM   2340  CD1 PHE A 306     -28.091 -29.168  -8.161  1.00 49.56           C  
ATOM   2341  CD2 PHE A 306     -27.781 -26.795  -8.236  1.00 42.22           C  
ATOM   2342  CE1 PHE A 306     -29.435 -29.008  -8.491  1.00 61.52           C  
ATOM   2343  CE2 PHE A 306     -29.118 -26.626  -8.555  1.00 53.24           C  
ATOM   2344  CZ  PHE A 306     -29.949 -27.734  -8.687  1.00 49.69           C  
ATOM   2345  N   GLY A 307     -23.306 -28.400  -5.393  1.00 50.46           N  
ATOM   2346  CA  GLY A 307     -21.966 -28.862  -5.090  1.00 44.80           C  
ATOM   2347  C   GLY A 307     -21.008 -28.651  -6.239  1.00 51.00           C  
ATOM   2348  O   GLY A 307     -21.396 -28.753  -7.403  1.00 51.21           O  
ATOM   2349  N   VAL A 308     -19.752 -28.370  -5.905  1.00 44.98           N  
ATOM   2350  CA  VAL A 308     -18.704 -28.128  -6.893  1.00 57.51           C  
ATOM   2351  C   VAL A 308     -18.619 -29.236  -7.953  1.00 61.48           C  
ATOM   2352  O   VAL A 308     -18.088 -29.022  -9.048  1.00 64.65           O  
ATOM   2353  CB  VAL A 308     -17.334 -27.953  -6.200  1.00 64.09           C  
ATOM   2354  CG1 VAL A 308     -16.941 -29.237  -5.489  1.00 70.75           C  
ATOM   2355  CG2 VAL A 308     -16.263 -27.538  -7.205  1.00 70.37           C  
ATOM   2356  N   ALA A 309     -19.153 -30.413  -7.632  1.00 57.56           N  
ATOM   2357  CA  ALA A 309     -19.217 -31.517  -8.588  1.00 68.70           C  
ATOM   2358  C   ALA A 309     -19.899 -31.110  -9.899  1.00 67.84           C  
ATOM   2359  O   ALA A 309     -19.487 -31.535 -10.977  1.00 66.20           O  
ATOM   2360  CB  ALA A 309     -19.925 -32.729  -7.969  1.00 66.97           C  
ATOM   2361  N   ASN A 310     -20.936 -30.283  -9.804  1.00 59.77           N  
ATOM   2362  CA  ASN A 310     -21.671 -29.845 -10.983  1.00 56.00           C  
ATOM   2363  C   ASN A 310     -21.393 -28.392 -11.371  1.00 55.31           C  
ATOM   2364  O   ASN A 310     -22.035 -27.851 -12.274  1.00 59.43           O  
ATOM   2365  CB  ASN A 310     -23.165 -30.054 -10.767  1.00 49.41           C  
ATOM   2366  CG  ASN A 310     -23.504 -31.493 -10.480  1.00 55.74           C  
ATOM   2367  OD1 ASN A 310     -23.266 -32.368 -11.309  1.00 64.87           O  
ATOM   2368  ND2 ASN A 310     -24.052 -31.753  -9.299  1.00 60.23           N  
ATOM   2369  N   ALA A 311     -20.436 -27.767 -10.691  1.00 50.34           N  
ATOM   2370  CA  ALA A 311     -20.102 -26.368 -10.947  1.00 47.83           C  
ATOM   2371  C   ALA A 311     -19.887 -26.087 -12.427  1.00 57.79           C  
ATOM   2372  O   ALA A 311     -20.497 -25.175 -12.993  1.00 59.35           O  
ATOM   2373  CB  ALA A 311     -18.875 -25.968 -10.166  1.00 50.79           C  
ATOM   2374  N   VAL A 312     -19.010 -26.870 -13.048  1.00 60.16           N  
ATOM   2375  CA  VAL A 312     -18.662 -26.662 -14.450  1.00 52.64           C  
ATOM   2376  C   VAL A 312     -19.885 -26.809 -15.345  1.00 53.36           C  
ATOM   2377  O   VAL A 312     -20.215 -25.900 -16.098  1.00 55.70           O  
ATOM   2378  CB  VAL A 312     -17.535 -27.616 -14.912  1.00 60.63           C  
ATOM   2379  CG1 VAL A 312     -17.538 -27.769 -16.434  1.00 57.05           C  
ATOM   2380  CG2 VAL A 312     -16.186 -27.101 -14.424  1.00 57.40           C  
ATOM   2381  N   ALA A 313     -20.567 -27.944 -15.253  1.00 47.10           N  
ATOM   2382  CA  ALA A 313     -21.754 -28.159 -16.073  1.00 59.50           C  
ATOM   2383  C   ALA A 313     -22.749 -27.010 -15.901  1.00 59.68           C  
ATOM   2384  O   ALA A 313     -23.381 -26.573 -16.862  1.00 55.52           O  
ATOM   2385  CB  ALA A 313     -22.405 -29.489 -15.740  1.00 59.29           C  
ATOM   2386  N   ILE A 314     -22.879 -26.521 -14.671  1.00 52.44           N  
ATOM   2387  CA  ILE A 314     -23.784 -25.416 -14.387  1.00 49.94           C  
ATOM   2388  C   ILE A 314     -23.342 -24.129 -15.083  1.00 50.20           C  
ATOM   2389  O   ILE A 314     -24.157 -23.427 -15.678  1.00 46.04           O  
ATOM   2390  CB  ILE A 314     -23.937 -25.174 -12.871  1.00 52.79           C  
ATOM   2391  CG1 ILE A 314     -24.782 -26.286 -12.246  1.00 57.98           C  
ATOM   2392  CG2 ILE A 314     -24.573 -23.821 -12.609  1.00 46.61           C  
ATOM   2393  CD1 ILE A 314     -24.696 -26.338 -10.729  1.00 61.17           C  
ATOM   2394  N   ALA A 315     -22.054 -23.819 -15.019  1.00 45.81           N  
ATOM   2395  CA  ALA A 315     -21.553 -22.624 -15.683  1.00 47.01           C  
ATOM   2396  C   ALA A 315     -21.790 -22.710 -17.189  1.00 56.43           C  
ATOM   2397  O   ALA A 315     -22.172 -21.725 -17.829  1.00 43.65           O  
ATOM   2398  CB  ALA A 315     -20.078 -22.434 -15.395  1.00 57.63           C  
ATOM   2399  N   LYS A 316     -21.561 -23.896 -17.745  1.00 43.87           N  
ATOM   2400  CA  LYS A 316     -21.678 -24.099 -19.186  1.00 59.44           C  
ATOM   2401  C   LYS A 316     -23.128 -24.000 -19.649  1.00 54.60           C  
ATOM   2402  O   LYS A 316     -23.390 -23.620 -20.785  1.00 49.05           O  
ATOM   2403  CB  LYS A 316     -21.085 -25.453 -19.595  1.00 63.01           C  
ATOM   2404  CG  LYS A 316     -19.559 -25.504 -19.596  1.00 72.52           C  
ATOM   2405  CD  LYS A 316     -19.060 -26.893 -20.010  1.00 76.13           C  
ATOM   2406  CE  LYS A 316     -17.549 -26.912 -20.235  1.00 78.56           C  
ATOM   2407  NZ  LYS A 316     -17.144 -26.146 -21.457  1.00 78.59           N  
ATOM   2408  N   ALA A 317     -24.069 -24.346 -18.773  1.00 40.68           N  
ATOM   2409  CA  ALA A 317     -25.482 -24.293 -19.139  1.00 45.68           C  
ATOM   2410  C   ALA A 317     -25.965 -22.855 -19.341  1.00 41.37           C  
ATOM   2411  O   ALA A 317     -27.070 -22.637 -19.836  1.00 44.45           O  
ATOM   2412  CB  ALA A 317     -26.333 -24.999 -18.108  1.00 46.61           C  
ATOM   2413  N   GLY A 318     -25.150 -21.885 -18.925  1.00 39.18           N  
ATOM   2414  CA  GLY A 318     -25.394 -20.489 -19.247  1.00 40.70           C  
ATOM   2415  C   GLY A 318     -26.148 -19.597 -18.261  1.00 44.65           C  
ATOM   2416  O   GLY A 318     -26.827 -20.061 -17.335  1.00 36.51           O  
ATOM   2417  N   ALA A 319     -26.032 -18.292 -18.504  1.00 38.21           N  
ATOM   2418  CA  ALA A 319     -26.598 -17.240 -17.659  1.00 37.56           C  
ATOM   2419  C   ALA A 319     -28.121 -17.287 -17.536  1.00 37.07           C  
ATOM   2420  O   ALA A 319     -28.677 -17.058 -16.457  1.00 30.57           O  
ATOM   2421  CB  ALA A 319     -26.169 -15.878 -18.182  1.00 38.09           C  
ATOM   2422  N   PHE A 320     -28.791 -17.536 -18.656  1.00 39.68           N  
ATOM   2423  CA  PHE A 320     -30.245 -17.611 -18.673  1.00 33.98           C  
ATOM   2424  C   PHE A 320     -30.788 -18.801 -17.875  1.00 37.16           C  
ATOM   2425  O   PHE A 320     -31.712 -18.640 -17.089  1.00 32.89           O  
ATOM   2426  CB  PHE A 320     -30.776 -17.674 -20.101  1.00 37.66           C  
ATOM   2427  CG  PHE A 320     -32.261 -17.894 -20.176  1.00 38.29           C  
ATOM   2428  CD1 PHE A 320     -33.144 -16.866 -19.872  1.00 35.62           C  
ATOM   2429  CD2 PHE A 320     -32.775 -19.129 -20.550  1.00 45.34           C  
ATOM   2430  CE1 PHE A 320     -34.507 -17.062 -19.938  1.00 39.60           C  
ATOM   2431  CE2 PHE A 320     -34.147 -19.334 -20.629  1.00 47.81           C  
ATOM   2432  CZ  PHE A 320     -35.014 -18.292 -20.324  1.00 43.24           C  
ATOM   2433  N   ASN A 321     -30.252 -19.997 -18.100  1.00 32.05           N  
ATOM   2434  CA  ASN A 321     -30.675 -21.148 -17.303  1.00 35.42           C  
ATOM   2435  C   ASN A 321     -30.389 -20.909 -15.826  1.00 33.35           C  
ATOM   2436  O   ASN A 321     -31.171 -21.284 -14.952  1.00 34.29           O  
ATOM   2437  CB  ASN A 321     -29.986 -22.432 -17.764  1.00 40.52           C  
ATOM   2438  CG  ASN A 321     -30.735 -23.123 -18.896  1.00 56.83           C  
ATOM   2439  OD1 ASN A 321     -31.334 -22.474 -19.745  1.00 49.00           O  
ATOM   2440  ND2 ASN A 321     -30.707 -24.448 -18.901  1.00 56.29           N  
ATOM   2441  N   LEU A 322     -29.253 -20.278 -15.561  1.00 26.23           N  
ATOM   2442  CA  LEU A 322     -28.832 -20.020 -14.209  1.00 32.43           C  
ATOM   2443  C   LEU A 322     -29.816 -19.110 -13.478  1.00 41.99           C  
ATOM   2444  O   LEU A 322     -30.151 -19.337 -12.304  1.00 28.78           O  
ATOM   2445  CB  LEU A 322     -27.456 -19.362 -14.214  1.00 31.63           C  
ATOM   2446  CG  LEU A 322     -26.956 -19.032 -12.816  1.00 34.13           C  
ATOM   2447  CD1 LEU A 322     -26.902 -20.305 -11.941  1.00 38.30           C  
ATOM   2448  CD2 LEU A 322     -25.594 -18.364 -12.905  1.00 28.22           C  
ATOM   2449  N   GLY A 323     -30.275 -18.070 -14.170  1.00 30.09           N  
ATOM   2450  CA  GLY A 323     -31.018 -17.019 -13.500  1.00 31.09           C  
ATOM   2451  C   GLY A 323     -32.487 -17.364 -13.429  1.00 34.27           C  
ATOM   2452  O   GLY A 323     -33.187 -16.980 -12.489  1.00 31.10           O  
ATOM   2453  N   PHE A 324     -32.941 -18.133 -14.414  1.00 25.08           N  
ATOM   2454  CA  PHE A 324     -34.363 -18.348 -14.603  1.00 32.59           C  
ATOM   2455  C   PHE A 324     -34.833 -19.757 -14.341  1.00 31.97           C  
ATOM   2456  O   PHE A 324     -36.032 -19.998 -14.257  1.00 35.10           O  
ATOM   2457  CB  PHE A 324     -34.782 -17.922 -16.026  1.00 28.63           C  
ATOM   2458  CG  PHE A 324     -34.977 -16.445 -16.166  1.00 27.91           C  
ATOM   2459  CD1 PHE A 324     -36.224 -15.879 -15.959  1.00 27.46           C  
ATOM   2460  CD2 PHE A 324     -33.908 -15.617 -16.461  1.00 28.80           C  
ATOM   2461  CE1 PHE A 324     -36.409 -14.508 -16.078  1.00 28.66           C  
ATOM   2462  CE2 PHE A 324     -34.086 -14.250 -16.573  1.00 32.31           C  
ATOM   2463  CZ  PHE A 324     -35.337 -13.699 -16.385  1.00 29.94           C  
ATOM   2464  N   ILE A 325     -33.912 -20.704 -14.247  1.00 29.34           N  
ATOM   2465  CA  ILE A 325     -34.336 -22.052 -13.908  1.00 27.43           C  
ATOM   2466  C   ILE A 325     -33.648 -22.538 -12.643  1.00 41.08           C  
ATOM   2467  O   ILE A 325     -34.304 -22.914 -11.666  1.00 35.74           O  
ATOM   2468  CB  ILE A 325     -34.061 -23.041 -15.034  1.00 34.68           C  
ATOM   2469  CG1 ILE A 325     -34.732 -22.573 -16.341  1.00 37.10           C  
ATOM   2470  CG2 ILE A 325     -34.564 -24.432 -14.647  1.00 32.46           C  
ATOM   2471  CD1 ILE A 325     -34.655 -23.604 -17.450  1.00 36.71           C  
ATOM   2472  N   THR A 326     -32.320 -22.517 -12.662  1.00 36.56           N  
ATOM   2473  CA  THR A 326     -31.542 -23.134 -11.602  1.00 35.69           C  
ATOM   2474  C   THR A 326     -31.720 -22.428 -10.255  1.00 34.40           C  
ATOM   2475  O   THR A 326     -31.900 -23.078  -9.219  1.00 37.19           O  
ATOM   2476  CB  THR A 326     -30.063 -23.233 -12.008  1.00 35.19           C  
ATOM   2477  OG1 THR A 326     -29.963 -24.038 -13.191  1.00 34.83           O  
ATOM   2478  CG2 THR A 326     -29.233 -23.869 -10.894  1.00 37.72           C  
ATOM   2479  N   LEU A 327     -31.674 -21.104 -10.244  1.00 37.97           N  
ATOM   2480  CA  LEU A 327     -31.853 -20.389  -8.973  1.00 34.26           C  
ATOM   2481  C   LEU A 327     -33.263 -20.518  -8.377  1.00 42.38           C  
ATOM   2482  O   LEU A 327     -33.408 -20.812  -7.188  1.00 35.11           O  
ATOM   2483  CB  LEU A 327     -31.434 -18.931  -9.087  1.00 41.22           C  
ATOM   2484  CG  LEU A 327     -30.079 -18.605  -8.466  1.00 44.23           C  
ATOM   2485  CD1 LEU A 327     -29.006 -19.507  -9.035  1.00 42.34           C  
ATOM   2486  CD2 LEU A 327     -29.748 -17.144  -8.707  1.00 46.51           C  
ATOM   2487  N   PRO A 328     -34.305 -20.284  -9.200  1.00 42.79           N  
ATOM   2488  CA  PRO A 328     -35.680 -20.607  -8.805  1.00 43.16           C  
ATOM   2489  C   PRO A 328     -35.736 -21.974  -8.121  1.00 39.12           C  
ATOM   2490  O   PRO A 328     -36.257 -22.098  -7.014  1.00 42.57           O  
ATOM   2491  CB  PRO A 328     -36.414 -20.669 -10.152  1.00 44.97           C  
ATOM   2492  CG  PRO A 328     -35.697 -19.689 -10.995  1.00 36.52           C  
ATOM   2493  CD  PRO A 328     -34.249 -19.709 -10.559  1.00 36.10           C  
ATOM   2494  N   ALA A 329     -35.187 -22.988  -8.773  1.00 31.42           N  
ATOM   2495  CA  ALA A 329     -35.186 -24.337  -8.218  1.00 37.14           C  
ATOM   2496  C   ALA A 329     -34.476 -24.396  -6.857  1.00 36.37           C  
ATOM   2497  O   ALA A 329     -34.995 -24.967  -5.891  1.00 40.35           O  
ATOM   2498  CB  ALA A 329     -34.557 -25.314  -9.211  1.00 38.05           C  
ATOM   2499  N   ILE A 330     -33.287 -23.813  -6.784  1.00 34.35           N  
ATOM   2500  CA  ILE A 330     -32.544 -23.759  -5.531  1.00 37.14           C  
ATOM   2501  C   ILE A 330     -33.351 -23.039  -4.436  1.00 41.29           C  
ATOM   2502  O   ILE A 330     -33.388 -23.480  -3.291  1.00 44.79           O  
ATOM   2503  CB  ILE A 330     -31.190 -23.066  -5.727  1.00 36.32           C  
ATOM   2504  CG1 ILE A 330     -30.254 -23.980  -6.512  1.00 33.07           C  
ATOM   2505  CG2 ILE A 330     -30.587 -22.705  -4.385  1.00 43.20           C  
ATOM   2506  CD1 ILE A 330     -29.008 -23.270  -6.988  1.00 43.67           C  
ATOM   2507  N   PHE A 331     -34.017 -21.946  -4.802  1.00 43.61           N  
ATOM   2508  CA  PHE A 331     -34.900 -21.234  -3.884  1.00 42.90           C  
ATOM   2509  C   PHE A 331     -36.057 -22.111  -3.393  1.00 50.34           C  
ATOM   2510  O   PHE A 331     -36.536 -21.941  -2.275  1.00 55.47           O  
ATOM   2511  CB  PHE A 331     -35.466 -19.969  -4.533  1.00 51.93           C  
ATOM   2512  CG  PHE A 331     -34.421 -18.978  -4.961  1.00 47.60           C  
ATOM   2513  CD1 PHE A 331     -33.263 -18.816  -4.229  1.00 55.16           C  
ATOM   2514  CD2 PHE A 331     -34.611 -18.193  -6.090  1.00 56.75           C  
ATOM   2515  CE1 PHE A 331     -32.299 -17.900  -4.615  1.00 57.39           C  
ATOM   2516  CE2 PHE A 331     -33.650 -17.274  -6.482  1.00 52.61           C  
ATOM   2517  CZ  PHE A 331     -32.492 -17.130  -5.737  1.00 46.66           C  
ATOM   2518  N   SER A 332     -36.505 -23.050  -4.221  1.00 45.34           N  
ATOM   2519  CA  SER A 332     -37.627 -23.908  -3.844  1.00 46.79           C  
ATOM   2520  C   SER A 332     -37.219 -24.970  -2.819  1.00 54.33           C  
ATOM   2521  O   SER A 332     -38.051 -25.756  -2.361  1.00 52.83           O  
ATOM   2522  CB  SER A 332     -38.243 -24.581  -5.075  1.00 42.85           C  
ATOM   2523  OG  SER A 332     -37.552 -25.773  -5.416  1.00 45.27           O  
ATOM   2524  N   GLN A 333     -35.941 -24.987  -2.456  1.00 45.90           N  
ATOM   2525  CA  GLN A 333     -35.419 -26.044  -1.598  1.00 44.16           C  
ATOM   2526  C   GLN A 333     -34.755 -25.488  -0.355  1.00 51.12           C  
ATOM   2527  O   GLN A 333     -34.150 -26.231   0.419  1.00 54.27           O  
ATOM   2528  CB  GLN A 333     -34.403 -26.893  -2.356  1.00 43.87           C  
ATOM   2529  CG  GLN A 333     -34.958 -27.575  -3.569  1.00 42.14           C  
ATOM   2530  CD  GLN A 333     -36.088 -28.505  -3.223  1.00 61.47           C  
ATOM   2531  OE1 GLN A 333     -37.258 -28.186  -3.442  1.00 59.70           O  
ATOM   2532  NE2 GLN A 333     -35.749 -29.666  -2.666  1.00 57.65           N  
ATOM   2533  N   THR A 334     -34.860 -24.182  -0.157  1.00 37.53           N  
ATOM   2534  CA  THR A 334     -34.193 -23.560   0.969  1.00 43.28           C  
ATOM   2535  C   THR A 334     -35.176 -22.733   1.780  1.00 42.91           C  
ATOM   2536  O   THR A 334     -36.236 -22.347   1.283  1.00 39.55           O  
ATOM   2537  CB  THR A 334     -33.007 -22.698   0.515  1.00 48.29           C  
ATOM   2538  OG1 THR A 334     -33.485 -21.608  -0.279  1.00 52.89           O  
ATOM   2539  CG2 THR A 334     -32.043 -23.531  -0.316  1.00 45.48           C  
ATOM   2540  N   ALA A 335     -34.819 -22.477   3.036  1.00 41.52           N  
ATOM   2541  CA  ALA A 335     -35.712 -21.805   3.967  1.00 39.05           C  
ATOM   2542  C   ALA A 335     -36.028 -20.390   3.518  1.00 34.19           C  
ATOM   2543  O   ALA A 335     -35.122 -19.597   3.286  1.00 38.38           O  
ATOM   2544  CB  ALA A 335     -35.109 -21.799   5.396  1.00 35.11           C  
ATOM   2545  N   GLY A 336     -37.318 -20.077   3.423  1.00 34.92           N  
ATOM   2546  CA  GLY A 336     -37.764 -18.764   2.976  1.00 34.19           C  
ATOM   2547  C   GLY A 336     -37.497 -18.520   1.478  1.00 30.30           C  
ATOM   2548  O   GLY A 336     -37.524 -17.385   1.015  1.00 31.58           O  
ATOM   2549  N   GLY A 337     -37.245 -19.591   0.736  1.00 30.02           N  
ATOM   2550  CA  GLY A 337     -36.752 -19.500  -0.634  1.00 36.39           C  
ATOM   2551  C   GLY A 337     -37.694 -18.909  -1.669  1.00 36.81           C  
ATOM   2552  O   GLY A 337     -37.260 -18.376  -2.690  1.00 40.96           O  
ATOM   2553  N   THR A 338     -38.992 -19.012  -1.425  1.00 33.83           N  
ATOM   2554  CA  THR A 338     -39.971 -18.471  -2.356  1.00 43.19           C  
ATOM   2555  C   THR A 338     -39.898 -16.953  -2.279  1.00 45.45           C  
ATOM   2556  O   THR A 338     -39.900 -16.250  -3.289  1.00 35.47           O  
ATOM   2557  CB  THR A 338     -41.387 -18.948  -1.999  1.00 47.15           C  
ATOM   2558  OG1 THR A 338     -41.484 -20.356  -2.254  1.00 48.64           O  
ATOM   2559  CG2 THR A 338     -42.419 -18.219  -2.835  1.00 55.46           C  
ATOM   2560  N   PHE A 339     -39.795 -16.451  -1.061  1.00 31.41           N  
ATOM   2561  CA  PHE A 339     -39.718 -15.027  -0.858  1.00 33.04           C  
ATOM   2562  C   PHE A 339     -38.370 -14.528  -1.326  1.00 30.17           C  
ATOM   2563  O   PHE A 339     -38.249 -13.411  -1.807  1.00 34.18           O  
ATOM   2564  CB  PHE A 339     -39.897 -14.688   0.621  1.00 28.53           C  
ATOM   2565  CG  PHE A 339     -39.791 -13.227   0.906  1.00 29.33           C  
ATOM   2566  CD1 PHE A 339     -40.853 -12.379   0.625  1.00 32.16           C  
ATOM   2567  CD2 PHE A 339     -38.627 -12.691   1.425  1.00 35.20           C  
ATOM   2568  CE1 PHE A 339     -40.762 -11.027   0.880  1.00 35.90           C  
ATOM   2569  CE2 PHE A 339     -38.528 -11.333   1.691  1.00 32.81           C  
ATOM   2570  CZ  PHE A 339     -39.593 -10.501   1.414  1.00 39.02           C  
ATOM   2571  N   LEU A 340     -37.356 -15.362  -1.150  1.00 34.71           N  
ATOM   2572  CA  LEU A 340     -36.025 -15.066  -1.639  1.00 30.99           C  
ATOM   2573  C   LEU A 340     -36.089 -14.961  -3.172  1.00 34.77           C  
ATOM   2574  O   LEU A 340     -35.431 -14.114  -3.775  1.00 33.21           O  
ATOM   2575  CB  LEU A 340     -35.098 -16.218  -1.286  1.00 33.02           C  
ATOM   2576  CG  LEU A 340     -33.640 -15.889  -0.983  1.00 50.30           C  
ATOM   2577  CD1 LEU A 340     -32.740 -16.928  -1.630  1.00 44.22           C  
ATOM   2578  CD2 LEU A 340     -33.287 -14.520  -1.465  1.00 50.64           C  
ATOM   2579  N   GLY A 341     -36.879 -15.837  -3.787  1.00 30.15           N  
ATOM   2580  CA  GLY A 341     -37.033 -15.847  -5.232  1.00 34.32           C  
ATOM   2581  C   GLY A 341     -37.626 -14.538  -5.716  1.00 32.29           C  
ATOM   2582  O   GLY A 341     -37.169 -13.948  -6.693  1.00 36.10           O  
ATOM   2583  N   PHE A 342     -38.655 -14.078  -5.019  1.00 30.42           N  
ATOM   2584  CA  PHE A 342     -39.203 -12.756  -5.265  1.00 28.00           C  
ATOM   2585  C   PHE A 342     -38.123 -11.675  -5.167  1.00 30.87           C  
ATOM   2586  O   PHE A 342     -38.002 -10.844  -6.050  1.00 31.06           O  
ATOM   2587  CB  PHE A 342     -40.322 -12.446  -4.278  1.00 31.32           C  
ATOM   2588  CG  PHE A 342     -40.599 -10.983  -4.130  1.00 35.37           C  
ATOM   2589  CD1 PHE A 342     -41.230 -10.282  -5.150  1.00 30.96           C  
ATOM   2590  CD2 PHE A 342     -40.232 -10.304  -2.975  1.00 33.90           C  
ATOM   2591  CE1 PHE A 342     -41.490  -8.930  -5.020  1.00 32.69           C  
ATOM   2592  CE2 PHE A 342     -40.493  -8.956  -2.837  1.00 30.17           C  
ATOM   2593  CZ  PHE A 342     -41.121  -8.263  -3.866  1.00 34.89           C  
ATOM   2594  N   LEU A 343     -37.343 -11.682  -4.089  1.00 30.72           N  
ATOM   2595  CA  LEU A 343     -36.270 -10.702  -3.942  1.00 31.00           C  
ATOM   2596  C   LEU A 343     -35.289 -10.768  -5.125  1.00 27.30           C  
ATOM   2597  O   LEU A 343     -34.810  -9.746  -5.609  1.00 29.35           O  
ATOM   2598  CB  LEU A 343     -35.506 -10.903  -2.622  1.00 27.55           C  
ATOM   2599  CG  LEU A 343     -36.272 -10.604  -1.325  1.00 30.18           C  
ATOM   2600  CD1 LEU A 343     -35.346 -10.758  -0.092  1.00 29.05           C  
ATOM   2601  CD2 LEU A 343     -36.916  -9.213  -1.361  1.00 31.25           C  
ATOM   2602  N   TRP A 344     -34.971 -11.981  -5.552  1.00 28.85           N  
ATOM   2603  CA  TRP A 344     -34.040 -12.182  -6.646  1.00 30.07           C  
ATOM   2604  C   TRP A 344     -34.603 -11.585  -7.943  1.00 31.95           C  
ATOM   2605  O   TRP A 344     -33.932 -10.811  -8.628  1.00 36.80           O  
ATOM   2606  CB  TRP A 344     -33.756 -13.672  -6.816  1.00 30.04           C  
ATOM   2607  CG  TRP A 344     -33.137 -14.036  -8.148  1.00 30.23           C  
ATOM   2608  CD1 TRP A 344     -33.730 -14.717  -9.185  1.00 32.85           C  
ATOM   2609  CD2 TRP A 344     -31.804 -13.747  -8.570  1.00 28.73           C  
ATOM   2610  NE1 TRP A 344     -32.835 -14.872 -10.224  1.00 30.60           N  
ATOM   2611  CE2 TRP A 344     -31.645 -14.286  -9.868  1.00 27.76           C  
ATOM   2612  CE3 TRP A 344     -30.721 -13.090  -7.970  1.00 29.64           C  
ATOM   2613  CZ2 TRP A 344     -30.447 -14.189 -10.572  1.00 35.01           C  
ATOM   2614  CZ3 TRP A 344     -29.539 -12.988  -8.669  1.00 36.57           C  
ATOM   2615  CH2 TRP A 344     -29.413 -13.524  -9.968  1.00 34.57           C  
ATOM   2616  N   PHE A 345     -35.849 -11.913  -8.265  1.00 30.97           N  
ATOM   2617  CA  PHE A 345     -36.457 -11.396  -9.492  1.00 28.75           C  
ATOM   2618  C   PHE A 345     -36.780  -9.917  -9.420  1.00 32.84           C  
ATOM   2619  O   PHE A 345     -36.721  -9.219 -10.427  1.00 30.24           O  
ATOM   2620  CB  PHE A 345     -37.652 -12.253  -9.926  1.00 28.80           C  
ATOM   2621  CG  PHE A 345     -37.229 -13.567 -10.471  1.00 33.84           C  
ATOM   2622  CD1 PHE A 345     -36.556 -13.638 -11.690  1.00 29.22           C  
ATOM   2623  CD2 PHE A 345     -37.456 -14.726  -9.764  1.00 25.23           C  
ATOM   2624  CE1 PHE A 345     -36.126 -14.856 -12.182  1.00 28.66           C  
ATOM   2625  CE2 PHE A 345     -37.027 -15.942 -10.236  1.00 26.22           C  
ATOM   2626  CZ  PHE A 345     -36.361 -16.015 -11.458  1.00 31.67           C  
ATOM   2627  N   PHE A 346     -37.093  -9.436  -8.220  1.00 30.25           N  
ATOM   2628  CA  PHE A 346     -37.287  -8.007  -8.000  1.00 31.71           C  
ATOM   2629  C   PHE A 346     -35.965  -7.285  -8.289  1.00 32.97           C  
ATOM   2630  O   PHE A 346     -35.933  -6.255  -8.976  1.00 31.37           O  
ATOM   2631  CB  PHE A 346     -37.802  -7.782  -6.572  1.00 40.20           C  
ATOM   2632  CG  PHE A 346     -37.988  -6.342  -6.190  1.00 39.79           C  
ATOM   2633  CD1 PHE A 346     -38.097  -5.357  -7.143  1.00 54.03           C  
ATOM   2634  CD2 PHE A 346     -38.083  -5.985  -4.848  1.00 57.01           C  
ATOM   2635  CE1 PHE A 346     -38.268  -4.030  -6.776  1.00 49.08           C  
ATOM   2636  CE2 PHE A 346     -38.260  -4.666  -4.470  1.00 47.85           C  
ATOM   2637  CZ  PHE A 346     -38.354  -3.687  -5.440  1.00 55.56           C  
ATOM   2638  N   LEU A 347     -34.870  -7.845  -7.793  1.00 25.73           N  
ATOM   2639  CA  LEU A 347     -33.553  -7.299  -8.094  1.00 23.89           C  
ATOM   2640  C   LEU A 347     -33.343  -7.236  -9.615  1.00 27.29           C  
ATOM   2641  O   LEU A 347     -32.901  -6.225 -10.141  1.00 29.11           O  
ATOM   2642  CB  LEU A 347     -32.459  -8.177  -7.512  1.00 28.48           C  
ATOM   2643  CG  LEU A 347     -31.071  -7.721  -7.952  1.00 31.33           C  
ATOM   2644  CD1 LEU A 347     -30.563  -6.625  -7.055  1.00 42.22           C  
ATOM   2645  CD2 LEU A 347     -30.100  -8.895  -7.965  1.00 40.23           C  
ATOM   2646  N   LEU A 348     -33.644  -8.333 -10.304  1.00 24.11           N  
ATOM   2647  CA  LEU A 348     -33.408  -8.394 -11.746  1.00 27.65           C  
ATOM   2648  C   LEU A 348     -34.308  -7.380 -12.451  1.00 27.27           C  
ATOM   2649  O   LEU A 348     -33.882  -6.703 -13.393  1.00 32.59           O  
ATOM   2650  CB  LEU A 348     -33.640  -9.812 -12.276  1.00 25.50           C  
ATOM   2651  CG  LEU A 348     -32.659 -10.903 -11.842  1.00 28.30           C  
ATOM   2652  CD1 LEU A 348     -32.929 -12.166 -12.648  1.00 29.26           C  
ATOM   2653  CD2 LEU A 348     -31.207 -10.457 -11.984  1.00 29.83           C  
ATOM   2654  N   PHE A 349     -35.548  -7.258 -11.983  1.00 24.60           N  
ATOM   2655  CA  PHE A 349     -36.491  -6.333 -12.605  1.00 23.76           C  
ATOM   2656  C   PHE A 349     -36.002  -4.878 -12.574  1.00 31.72           C  
ATOM   2657  O   PHE A 349     -36.009  -4.187 -13.593  1.00 29.98           O  
ATOM   2658  CB  PHE A 349     -37.890  -6.465 -11.997  1.00 28.55           C  
ATOM   2659  CG  PHE A 349     -38.864  -5.456 -12.526  1.00 31.54           C  
ATOM   2660  CD1 PHE A 349     -39.220  -5.463 -13.875  1.00 27.19           C  
ATOM   2661  CD2 PHE A 349     -39.396  -4.483 -11.695  1.00 26.94           C  
ATOM   2662  CE1 PHE A 349     -40.103  -4.520 -14.379  1.00 31.05           C  
ATOM   2663  CE2 PHE A 349     -40.278  -3.541 -12.186  1.00 28.49           C  
ATOM   2664  CZ  PHE A 349     -40.636  -3.559 -13.539  1.00 28.97           C  
ATOM   2665  N   PHE A 350     -35.570  -4.415 -11.408  1.00 27.93           N  
ATOM   2666  CA  PHE A 350     -35.056  -3.062 -11.287  1.00 27.47           C  
ATOM   2667  C   PHE A 350     -33.758  -2.946 -12.052  1.00 22.37           C  
ATOM   2668  O   PHE A 350     -33.420  -1.879 -12.561  1.00 27.47           O  
ATOM   2669  CB  PHE A 350     -34.848  -2.679  -9.807  1.00 26.37           C  
ATOM   2670  CG  PHE A 350     -36.002  -1.916  -9.222  1.00 37.51           C  
ATOM   2671  CD1 PHE A 350     -37.298  -2.151  -9.665  1.00 35.81           C  
ATOM   2672  CD2 PHE A 350     -35.798  -0.953  -8.241  1.00 42.71           C  
ATOM   2673  CE1 PHE A 350     -38.372  -1.443  -9.134  1.00 37.87           C  
ATOM   2674  CE2 PHE A 350     -36.868  -0.242  -7.708  1.00 38.71           C  
ATOM   2675  CZ  PHE A 350     -38.157  -0.487  -8.158  1.00 37.20           C  
ATOM   2676  N   ALA A 351     -33.006  -4.037 -12.104  1.00 26.93           N  
ATOM   2677  CA  ALA A 351     -31.782  -4.014 -12.871  1.00 27.12           C  
ATOM   2678  C   ALA A 351     -32.160  -3.817 -14.337  1.00 29.27           C  
ATOM   2679  O   ALA A 351     -31.560  -3.014 -15.027  1.00 26.22           O  
ATOM   2680  CB  ALA A 351     -30.987  -5.305 -12.684  1.00 26.49           C  
ATOM   2681  N   GLY A 352     -33.162  -4.535 -14.821  1.00 24.22           N  
ATOM   2682  CA  GLY A 352     -33.541  -4.390 -16.223  1.00 23.85           C  
ATOM   2683  C   GLY A 352     -34.207  -3.044 -16.479  1.00 30.71           C  
ATOM   2684  O   GLY A 352     -33.872  -2.333 -17.430  1.00 30.11           O  
ATOM   2685  N   LEU A 353     -35.148  -2.682 -15.612  1.00 28.53           N  
ATOM   2686  CA  LEU A 353     -35.911  -1.439 -15.763  1.00 27.95           C  
ATOM   2687  C   LEU A 353     -35.013  -0.192 -15.846  1.00 34.88           C  
ATOM   2688  O   LEU A 353     -35.240   0.699 -16.656  1.00 24.81           O  
ATOM   2689  CB  LEU A 353     -36.883  -1.286 -14.581  1.00 26.37           C  
ATOM   2690  CG  LEU A 353     -37.753  -0.032 -14.594  1.00 29.55           C  
ATOM   2691  CD1 LEU A 353     -38.451   0.110 -15.949  1.00 31.27           C  
ATOM   2692  CD2 LEU A 353     -38.760  -0.086 -13.445  1.00 23.89           C  
ATOM   2693  N   THR A 354     -34.001  -0.115 -14.989  1.00 28.03           N  
ATOM   2694  CA  THR A 354     -33.084   1.018 -15.064  1.00 24.56           C  
ATOM   2695  C   THR A 354     -32.300   1.054 -16.397  1.00 25.80           C  
ATOM   2696  O   THR A 354     -31.724   2.085 -16.760  1.00 26.95           O  
ATOM   2697  CB  THR A 354     -32.103   1.061 -13.851  1.00 27.05           C  
ATOM   2698  OG1 THR A 354     -31.456  -0.212 -13.709  1.00 29.86           O  
ATOM   2699  CG2 THR A 354     -32.839   1.386 -12.547  1.00 23.91           C  
ATOM   2700  N   SER A 355     -32.260  -0.071 -17.109  1.00 29.07           N  
ATOM   2701  CA  SER A 355     -31.560  -0.133 -18.409  1.00 29.40           C  
ATOM   2702  C   SER A 355     -32.498   0.063 -19.592  1.00 29.84           C  
ATOM   2703  O   SER A 355     -32.105   0.657 -20.595  1.00 29.00           O  
ATOM   2704  CB  SER A 355     -30.756  -1.436 -18.578  1.00 28.32           C  
ATOM   2705  OG  SER A 355     -29.709  -1.515 -17.596  1.00 26.79           O  
ATOM   2706  N   SER A 356     -33.730  -0.431 -19.479  1.00 26.66           N  
ATOM   2707  CA  SER A 356     -34.684  -0.312 -20.574  1.00 25.63           C  
ATOM   2708  C   SER A 356     -35.148   1.141 -20.761  1.00 28.28           C  
ATOM   2709  O   SER A 356     -35.359   1.598 -21.882  1.00 25.63           O  
ATOM   2710  CB  SER A 356     -35.863  -1.268 -20.372  1.00 27.97           C  
ATOM   2711  OG  SER A 356     -36.601  -0.925 -19.221  1.00 28.51           O  
ATOM   2712  N   ILE A 357     -35.292   1.887 -19.674  1.00 25.58           N  
ATOM   2713  CA  ILE A 357     -35.592   3.309 -19.844  1.00 20.25           C  
ATOM   2714  C   ILE A 357     -34.446   3.966 -20.585  1.00 28.03           C  
ATOM   2715  O   ILE A 357     -34.673   4.794 -21.466  1.00 30.47           O  
ATOM   2716  CB  ILE A 357     -35.910   4.045 -18.520  1.00 26.39           C  
ATOM   2717  CG1 ILE A 357     -34.790   3.846 -17.482  1.00 26.40           C  
ATOM   2718  CG2 ILE A 357     -37.270   3.586 -17.999  1.00 24.49           C  
ATOM   2719  CD1 ILE A 357     -35.026   4.581 -16.116  1.00 25.90           C  
ATOM   2720  N   ALA A 358     -33.218   3.554 -20.274  1.00 22.56           N  
ATOM   2721  CA  ALA A 358     -32.044   4.106 -20.948  1.00 26.94           C  
ATOM   2722  C   ALA A 358     -32.008   3.750 -22.452  1.00 29.87           C  
ATOM   2723  O   ALA A 358     -31.641   4.575 -23.299  1.00 27.98           O  
ATOM   2724  CB  ALA A 358     -30.772   3.614 -20.265  1.00 23.59           C  
ATOM   2725  N   ILE A 359     -32.398   2.527 -22.789  1.00 27.00           N  
ATOM   2726  CA  ILE A 359     -32.282   2.068 -24.183  1.00 26.68           C  
ATOM   2727  C   ILE A 359     -33.421   2.576 -25.055  1.00 21.54           C  
ATOM   2728  O   ILE A 359     -33.342   2.558 -26.284  1.00 27.80           O  
ATOM   2729  CB  ILE A 359     -32.169   0.514 -24.274  1.00 26.59           C  
ATOM   2730  CG1 ILE A 359     -31.457   0.104 -25.573  1.00 23.15           C  
ATOM   2731  CG2 ILE A 359     -33.547  -0.148 -24.199  1.00 26.23           C  
ATOM   2732  CD1 ILE A 359     -30.038   0.692 -25.712  1.00 24.29           C  
ATOM   2733  N   MET A 360     -34.504   3.003 -24.431  1.00 23.66           N  
ATOM   2734  CA  MET A 360     -35.597   3.595 -25.188  1.00 27.37           C  
ATOM   2735  C   MET A 360     -35.431   5.101 -25.390  1.00 32.44           C  
ATOM   2736  O   MET A 360     -36.041   5.688 -26.293  1.00 27.07           O  
ATOM   2737  CB  MET A 360     -36.926   3.287 -24.518  1.00 29.16           C  
ATOM   2738  CG  MET A 360     -37.343   1.836 -24.721  1.00 41.88           C  
ATOM   2739  SD  MET A 360     -39.048   1.532 -24.277  1.00 41.10           S  
ATOM   2740  CE  MET A 360     -38.896   1.458 -22.528  1.00 41.38           C  
ATOM   2741  N   GLN A 361     -34.616   5.733 -24.549  1.00 26.45           N  
ATOM   2742  CA  GLN A 361     -34.452   7.189 -24.630  1.00 26.07           C  
ATOM   2743  C   GLN A 361     -33.871   7.704 -25.971  1.00 23.53           C  
ATOM   2744  O   GLN A 361     -34.216   8.797 -26.401  1.00 25.96           O  
ATOM   2745  CB  GLN A 361     -33.675   7.735 -23.408  1.00 25.33           C  
ATOM   2746  CG  GLN A 361     -33.604   9.286 -23.296  1.00 24.94           C  
ATOM   2747  CD  GLN A 361     -34.962   9.991 -23.232  1.00 27.75           C  
ATOM   2748  OE1 GLN A 361     -35.957   9.424 -22.780  1.00 26.15           O  
ATOM   2749  NE2 GLN A 361     -34.998  11.248 -23.693  1.00 27.73           N  
ATOM   2750  N   PRO A 362     -32.988   6.928 -26.630  1.00 21.60           N  
ATOM   2751  CA  PRO A 362     -32.439   7.410 -27.909  1.00 29.43           C  
ATOM   2752  C   PRO A 362     -33.501   7.615 -28.995  1.00 29.82           C  
ATOM   2753  O   PRO A 362     -33.452   8.626 -29.714  1.00 25.36           O  
ATOM   2754  CB  PRO A 362     -31.469   6.298 -28.331  1.00 23.70           C  
ATOM   2755  CG  PRO A 362     -31.074   5.631 -27.036  1.00 26.52           C  
ATOM   2756  CD  PRO A 362     -32.299   5.715 -26.147  1.00 22.51           C  
ATOM   2757  N   MET A 363     -34.445   6.682 -29.123  1.00 27.66           N  
ATOM   2758  CA  MET A 363     -35.501   6.878 -30.124  1.00 27.49           C  
ATOM   2759  C   MET A 363     -36.346   8.079 -29.703  1.00 28.07           C  
ATOM   2760  O   MET A 363     -36.809   8.842 -30.533  1.00 26.71           O  
ATOM   2761  CB  MET A 363     -36.371   5.630 -30.248  1.00 24.57           C  
ATOM   2762  CG  MET A 363     -37.444   5.735 -31.305  1.00 35.33           C  
ATOM   2763  SD  MET A 363     -36.709   5.672 -32.954  1.00 37.39           S  
ATOM   2764  CE  MET A 363     -38.053   6.429 -33.871  1.00 42.31           C  
ATOM   2765  N   ILE A 364     -36.551   8.230 -28.395  1.00 27.10           N  
ATOM   2766  CA  ILE A 364     -37.291   9.375 -27.862  1.00 24.61           C  
ATOM   2767  C   ILE A 364     -36.580  10.705 -28.150  1.00 25.13           C  
ATOM   2768  O   ILE A 364     -37.194  11.668 -28.602  1.00 29.65           O  
ATOM   2769  CB  ILE A 364     -37.546   9.209 -26.358  1.00 29.46           C  
ATOM   2770  CG1 ILE A 364     -38.507   8.036 -26.133  1.00 26.58           C  
ATOM   2771  CG2 ILE A 364     -38.098  10.504 -25.768  1.00 26.01           C  
ATOM   2772  CD1 ILE A 364     -38.567   7.527 -24.696  1.00 23.92           C  
ATOM   2773  N   ALA A 365     -35.279  10.738 -27.896  1.00 23.20           N  
ATOM   2774  CA  ALA A 365     -34.451  11.906 -28.179  1.00 25.22           C  
ATOM   2775  C   ALA A 365     -34.511  12.235 -29.664  1.00 31.11           C  
ATOM   2776  O   ALA A 365     -34.646  13.404 -30.054  1.00 28.03           O  
ATOM   2777  CB  ALA A 365     -33.001  11.638 -27.779  1.00 20.32           C  
ATOM   2778  N   PHE A 366     -34.412  11.207 -30.499  1.00 25.62           N  
ATOM   2779  CA  PHE A 366     -34.422  11.455 -31.939  1.00 23.58           C  
ATOM   2780  C   PHE A 366     -35.709  12.132 -32.371  1.00 25.02           C  
ATOM   2781  O   PHE A 366     -35.685  13.135 -33.088  1.00 29.19           O  
ATOM   2782  CB  PHE A 366     -34.214  10.182 -32.761  1.00 25.73           C  
ATOM   2783  CG  PHE A 366     -34.390  10.412 -34.246  1.00 27.94           C  
ATOM   2784  CD1 PHE A 366     -33.331  10.872 -35.017  1.00 23.66           C  
ATOM   2785  CD2 PHE A 366     -35.628  10.234 -34.843  1.00 27.33           C  
ATOM   2786  CE1 PHE A 366     -33.491  11.124 -36.372  1.00 27.33           C  
ATOM   2787  CE2 PHE A 366     -35.805  10.480 -36.210  1.00 31.20           C  
ATOM   2788  CZ  PHE A 366     -34.734  10.929 -36.967  1.00 30.10           C  
ATOM   2789  N   LEU A 367     -36.844  11.584 -31.953  1.00 26.58           N  
ATOM   2790  CA  LEU A 367     -38.114  12.167 -32.353  1.00 23.07           C  
ATOM   2791  C   LEU A 367     -38.231  13.594 -31.835  1.00 26.68           C  
ATOM   2792  O   LEU A 367     -38.727  14.465 -32.532  1.00 29.69           O  
ATOM   2793  CB  LEU A 367     -39.280  11.308 -31.880  1.00 24.13           C  
ATOM   2794  CG  LEU A 367     -39.230   9.867 -32.406  1.00 28.77           C  
ATOM   2795  CD1 LEU A 367     -40.301   8.995 -31.776  1.00 22.54           C  
ATOM   2796  CD2 LEU A 367     -39.342   9.860 -33.955  1.00 30.64           C  
ATOM   2797  N   GLU A 368     -37.778  13.821 -30.597  1.00 32.42           N  
ATOM   2798  CA  GLU A 368     -37.751  15.157 -30.009  1.00 30.42           C  
ATOM   2799  C   GLU A 368     -36.817  16.110 -30.740  1.00 29.08           C  
ATOM   2800  O   GLU A 368     -37.228  17.186 -31.148  1.00 33.20           O  
ATOM   2801  CB  GLU A 368     -37.305  15.098 -28.530  1.00 25.25           C  
ATOM   2802  CG  GLU A 368     -38.335  14.488 -27.610  1.00 27.13           C  
ATOM   2803  CD  GLU A 368     -37.796  14.229 -26.213  1.00 34.08           C  
ATOM   2804  OE1 GLU A 368     -36.597  14.454 -25.978  1.00 34.39           O  
ATOM   2805  OE2 GLU A 368     -38.574  13.788 -25.354  1.00 28.49           O  
ATOM   2806  N   ASP A 369     -35.551  15.717 -30.875  1.00 30.98           N  
ATOM   2807  CA  ASP A 369     -34.518  16.620 -31.377  1.00 28.71           C  
ATOM   2808  C   ASP A 369     -34.694  16.870 -32.871  1.00 36.55           C  
ATOM   2809  O   ASP A 369     -34.495  17.994 -33.346  1.00 32.49           O  
ATOM   2810  CB  ASP A 369     -33.114  16.040 -31.155  1.00 24.34           C  
ATOM   2811  CG  ASP A 369     -32.824  15.701 -29.689  1.00 27.68           C  
ATOM   2812  OD1 ASP A 369     -33.592  16.108 -28.798  1.00 35.06           O  
ATOM   2813  OD2 ASP A 369     -31.811  15.017 -29.437  1.00 31.23           O  
ATOM   2814  N   GLU A 370     -35.053  15.823 -33.612  1.00 26.40           N  
ATOM   2815  CA  GLU A 370     -34.977  15.884 -35.074  1.00 28.64           C  
ATOM   2816  C   GLU A 370     -36.325  16.049 -35.765  1.00 31.61           C  
ATOM   2817  O   GLU A 370     -36.402  16.617 -36.853  1.00 34.10           O  
ATOM   2818  CB  GLU A 370     -34.255  14.641 -35.605  1.00 31.82           C  
ATOM   2819  CG  GLU A 370     -33.064  14.212 -34.741  1.00 32.44           C  
ATOM   2820  CD  GLU A 370     -31.944  15.256 -34.700  1.00 43.91           C  
ATOM   2821  OE1 GLU A 370     -32.035  16.283 -35.415  1.00 37.42           O  
ATOM   2822  OE2 GLU A 370     -30.958  15.041 -33.964  1.00 35.06           O  
ATOM   2823  N   LEU A 371     -37.386  15.529 -35.159  1.00 30.23           N  
ATOM   2824  CA  LEU A 371     -38.721  15.678 -35.734  1.00 32.40           C  
ATOM   2825  C   LEU A 371     -39.586  16.602 -34.876  1.00 38.04           C  
ATOM   2826  O   LEU A 371     -40.742  16.874 -35.209  1.00 37.25           O  
ATOM   2827  CB  LEU A 371     -39.397  14.320 -35.939  1.00 33.55           C  
ATOM   2828  CG  LEU A 371     -38.711  13.429 -36.990  1.00 36.26           C  
ATOM   2829  CD1 LEU A 371     -39.387  12.052 -37.126  1.00 31.91           C  
ATOM   2830  CD2 LEU A 371     -38.643  14.134 -38.342  1.00 39.35           C  
ATOM   2831  N   LYS A 372     -39.005  17.084 -33.781  1.00 27.37           N  
ATOM   2832  CA  LYS A 372     -39.641  18.072 -32.925  1.00 30.20           C  
ATOM   2833  C   LYS A 372     -40.969  17.575 -32.375  1.00 31.68           C  
ATOM   2834  O   LYS A 372     -41.896  18.353 -32.214  1.00 37.56           O  
ATOM   2835  CB  LYS A 372     -39.836  19.405 -33.675  1.00 37.07           C  
ATOM   2836  CG  LYS A 372     -38.592  19.905 -34.403  1.00 35.99           C  
ATOM   2837  CD  LYS A 372     -37.470  20.236 -33.426  1.00 47.14           C  
ATOM   2838  CE  LYS A 372     -36.173  20.576 -34.165  1.00 45.72           C  
ATOM   2839  NZ  LYS A 372     -35.071  20.851 -33.185  1.00 57.88           N  
ATOM   2840  N   LEU A 373     -41.075  16.280 -32.095  1.00 29.35           N  
ATOM   2841  CA  LEU A 373     -42.247  15.788 -31.387  1.00 26.34           C  
ATOM   2842  C   LEU A 373     -42.148  16.232 -29.938  1.00 27.14           C  
ATOM   2843  O   LEU A 373     -41.053  16.420 -29.430  1.00 30.34           O  
ATOM   2844  CB  LEU A 373     -42.310  14.266 -31.430  1.00 33.65           C  
ATOM   2845  CG  LEU A 373     -43.046  13.646 -32.619  1.00 44.97           C  
ATOM   2846  CD1 LEU A 373     -42.425  14.100 -33.917  1.00 38.85           C  
ATOM   2847  CD2 LEU A 373     -43.039  12.130 -32.520  1.00 35.08           C  
ATOM   2848  N   SER A 374     -43.290  16.384 -29.278  1.00 30.25           N  
ATOM   2849  CA  SER A 374     -43.308  16.676 -27.856  1.00 30.27           C  
ATOM   2850  C   SER A 374     -42.811  15.434 -27.149  1.00 30.25           C  
ATOM   2851  O   SER A 374     -42.850  14.341 -27.709  1.00 29.00           O  
ATOM   2852  CB  SER A 374     -44.730  16.983 -27.384  1.00 33.04           C  
ATOM   2853  OG  SER A 374     -45.535  15.805 -27.429  1.00 30.85           O  
ATOM   2854  N   ARG A 375     -42.376  15.587 -25.900  1.00 25.23           N  
ATOM   2855  CA  ARG A 375     -41.898  14.444 -25.150  1.00 22.98           C  
ATOM   2856  C   ARG A 375     -42.989  13.395 -25.049  1.00 26.62           C  
ATOM   2857  O   ARG A 375     -42.713  12.218 -25.193  1.00 25.77           O  
ATOM   2858  CB  ARG A 375     -41.424  14.851 -23.748  1.00 30.04           C  
ATOM   2859  CG  ARG A 375     -41.063  13.647 -22.876  1.00 36.84           C  
ATOM   2860  CD  ARG A 375     -40.425  14.049 -21.564  1.00 32.33           C  
ATOM   2861  NE  ARG A 375     -41.392  14.654 -20.665  1.00 39.57           N  
ATOM   2862  CZ  ARG A 375     -41.244  15.848 -20.099  1.00 48.78           C  
ATOM   2863  NH1 ARG A 375     -40.150  16.562 -20.331  1.00 40.83           N  
ATOM   2864  NH2 ARG A 375     -42.183  16.313 -19.287  1.00 43.84           N  
ATOM   2865  N   LYS A 376     -44.227  13.812 -24.792  1.00 26.79           N  
ATOM   2866  CA  LYS A 376     -45.315  12.838 -24.655  1.00 29.68           C  
ATOM   2867  C   LYS A 376     -45.503  12.010 -25.931  1.00 32.50           C  
ATOM   2868  O   LYS A 376     -45.646  10.792 -25.873  1.00 36.64           O  
ATOM   2869  CB  LYS A 376     -46.645  13.507 -24.300  1.00 33.79           C  
ATOM   2870  CG  LYS A 376     -47.851  12.620 -24.649  1.00 36.75           C  
ATOM   2871  CD  LYS A 376     -49.184  13.141 -24.109  1.00 53.59           C  
ATOM   2872  CE  LYS A 376     -49.707  14.317 -24.911  1.00 57.24           C  
ATOM   2873  NZ  LYS A 376     -50.907  14.942 -24.265  1.00 68.56           N  
ATOM   2874  N   HIS A 377     -45.510  12.693 -27.074  1.00 26.40           N  
ATOM   2875  CA  HIS A 377     -45.710  12.049 -28.369  1.00 30.87           C  
ATOM   2876  C   HIS A 377     -44.520  11.176 -28.722  1.00 28.71           C  
ATOM   2877  O   HIS A 377     -44.687  10.140 -29.341  1.00 31.96           O  
ATOM   2878  CB  HIS A 377     -45.928  13.094 -29.462  1.00 29.54           C  
ATOM   2879  CG  HIS A 377     -47.303  13.690 -29.461  1.00 37.38           C  
ATOM   2880  ND1 HIS A 377     -47.592  14.895 -30.070  1.00 28.77           N  
ATOM   2881  CD2 HIS A 377     -48.464  13.247 -28.926  1.00 38.29           C  
ATOM   2882  CE1 HIS A 377     -48.878  15.164 -29.913  1.00 37.87           C  
ATOM   2883  NE2 HIS A 377     -49.430  14.176 -29.223  1.00 36.07           N  
ATOM   2884  N   ALA A 378     -43.319  11.592 -28.307  1.00 28.73           N  
ATOM   2885  CA  ALA A 378     -42.114  10.863 -28.674  1.00 24.25           C  
ATOM   2886  C   ALA A 378     -42.053   9.574 -27.885  1.00 28.92           C  
ATOM   2887  O   ALA A 378     -41.669   8.526 -28.419  1.00 26.55           O  
ATOM   2888  CB  ALA A 378     -40.864  11.698 -28.432  1.00 25.93           C  
ATOM   2889  N   VAL A 379     -42.421   9.665 -26.603  1.00 28.70           N  
ATOM   2890  CA  VAL A 379     -42.431   8.502 -25.730  1.00 27.86           C  
ATOM   2891  C   VAL A 379     -43.511   7.535 -26.173  1.00 25.30           C  
ATOM   2892  O   VAL A 379     -43.275   6.337 -26.241  1.00 28.88           O  
ATOM   2893  CB  VAL A 379     -42.665   8.886 -24.214  1.00 27.93           C  
ATOM   2894  CG1 VAL A 379     -42.774   7.640 -23.344  1.00 26.70           C  
ATOM   2895  CG2 VAL A 379     -41.563   9.810 -23.713  1.00 23.79           C  
ATOM   2896  N   LEU A 380     -44.709   8.040 -26.442  1.00 22.11           N  
ATOM   2897  CA  LEU A 380     -45.809   7.162 -26.843  1.00 29.73           C  
ATOM   2898  C   LEU A 380     -45.556   6.471 -28.199  1.00 30.09           C  
ATOM   2899  O   LEU A 380     -45.851   5.286 -28.372  1.00 28.08           O  
ATOM   2900  CB  LEU A 380     -47.139   7.927 -26.867  1.00 29.97           C  
ATOM   2901  CG  LEU A 380     -47.575   8.490 -25.508  1.00 33.02           C  
ATOM   2902  CD1 LEU A 380     -48.929   9.174 -25.610  1.00 30.79           C  
ATOM   2903  CD2 LEU A 380     -47.607   7.401 -24.448  1.00 34.54           C  
ATOM   2904  N   TRP A 381     -45.002   7.200 -29.157  1.00 26.24           N  
ATOM   2905  CA  TRP A 381     -44.752   6.601 -30.471  1.00 27.19           C  
ATOM   2906  C   TRP A 381     -43.605   5.592 -30.384  1.00 29.48           C  
ATOM   2907  O   TRP A 381     -43.626   4.548 -31.029  1.00 25.63           O  
ATOM   2908  CB  TRP A 381     -44.443   7.671 -31.509  1.00 21.67           C  
ATOM   2909  CG  TRP A 381     -45.683   8.203 -32.163  1.00 32.98           C  
ATOM   2910  CD1 TRP A 381     -46.204   9.464 -32.048  1.00 34.06           C  
ATOM   2911  CD2 TRP A 381     -46.569   7.481 -33.026  1.00 34.47           C  
ATOM   2912  NE1 TRP A 381     -47.353   9.566 -32.797  1.00 30.83           N  
ATOM   2913  CE2 TRP A 381     -47.600   8.363 -33.402  1.00 35.80           C  
ATOM   2914  CE3 TRP A 381     -46.593   6.169 -33.512  1.00 34.70           C  
ATOM   2915  CZ2 TRP A 381     -48.641   7.979 -34.254  1.00 31.43           C  
ATOM   2916  CZ3 TRP A 381     -47.635   5.794 -34.365  1.00 33.50           C  
ATOM   2917  CH2 TRP A 381     -48.643   6.689 -34.709  1.00 31.52           C  
ATOM   2918  N   THR A 382     -42.595   5.931 -29.591  1.00 30.16           N  
ATOM   2919  CA  THR A 382     -41.521   4.993 -29.305  1.00 29.87           C  
ATOM   2920  C   THR A 382     -42.078   3.728 -28.640  1.00 29.33           C  
ATOM   2921  O   THR A 382     -41.786   2.617 -29.067  1.00 24.33           O  
ATOM   2922  CB  THR A 382     -40.444   5.608 -28.398  1.00 25.95           C  
ATOM   2923  OG1 THR A 382     -39.795   6.684 -29.092  1.00 27.95           O  
ATOM   2924  CG2 THR A 382     -39.412   4.535 -28.029  1.00 26.43           C  
ATOM   2925  N   ALA A 383     -42.900   3.896 -27.609  1.00 29.32           N  
ATOM   2926  CA  ALA A 383     -43.536   2.734 -26.991  1.00 30.46           C  
ATOM   2927  C   ALA A 383     -44.380   1.932 -27.996  1.00 25.97           C  
ATOM   2928  O   ALA A 383     -44.398   0.700 -27.968  1.00 27.17           O  
ATOM   2929  CB  ALA A 383     -44.381   3.145 -25.800  1.00 29.82           C  
ATOM   2930  N   ALA A 384     -45.097   2.638 -28.862  1.00 27.39           N  
ATOM   2931  CA  ALA A 384     -45.914   1.995 -29.908  1.00 29.39           C  
ATOM   2932  C   ALA A 384     -45.065   1.147 -30.839  1.00 27.91           C  
ATOM   2933  O   ALA A 384     -45.401   0.005 -31.121  1.00 25.38           O  
ATOM   2934  CB  ALA A 384     -46.698   3.028 -30.709  1.00 25.34           C  
ATOM   2935  N   ILE A 385     -43.965   1.715 -31.315  1.00 24.61           N  
ATOM   2936  CA  ILE A 385     -43.085   0.993 -32.211  1.00 31.80           C  
ATOM   2937  C   ILE A 385     -42.456  -0.219 -31.522  1.00 29.65           C  
ATOM   2938  O   ILE A 385     -42.373  -1.290 -32.113  1.00 31.01           O  
ATOM   2939  CB  ILE A 385     -42.006   1.907 -32.843  1.00 31.91           C  
ATOM   2940  CG1 ILE A 385     -42.689   3.045 -33.611  1.00 47.25           C  
ATOM   2941  CG2 ILE A 385     -41.148   1.097 -33.827  1.00 34.75           C  
ATOM   2942  CD1 ILE A 385     -41.744   4.167 -34.126  1.00 44.11           C  
ATOM   2943  N   VAL A 386     -42.038  -0.047 -30.267  1.00 28.22           N  
ATOM   2944  CA  VAL A 386     -41.392  -1.133 -29.535  1.00 19.89           C  
ATOM   2945  C   VAL A 386     -42.419  -2.201 -29.233  1.00 28.04           C  
ATOM   2946  O   VAL A 386     -42.184  -3.383 -29.476  1.00 25.24           O  
ATOM   2947  CB  VAL A 386     -40.702  -0.631 -28.237  1.00 26.71           C  
ATOM   2948  CG1 VAL A 386     -40.280  -1.823 -27.306  1.00 23.11           C  
ATOM   2949  CG2 VAL A 386     -39.509   0.249 -28.606  1.00 28.09           C  
ATOM   2950  N   PHE A 387     -43.570  -1.780 -28.722  1.00 28.46           N  
ATOM   2951  CA  PHE A 387     -44.639  -2.717 -28.421  1.00 32.10           C  
ATOM   2952  C   PHE A 387     -45.025  -3.544 -29.647  1.00 27.91           C  
ATOM   2953  O   PHE A 387     -45.065  -4.777 -29.583  1.00 27.61           O  
ATOM   2954  CB  PHE A 387     -45.863  -1.986 -27.875  1.00 31.88           C  
ATOM   2955  CG  PHE A 387     -47.012  -2.895 -27.553  1.00 35.85           C  
ATOM   2956  CD1 PHE A 387     -46.931  -3.791 -26.498  1.00 36.26           C  
ATOM   2957  CD2 PHE A 387     -48.177  -2.846 -28.300  1.00 34.04           C  
ATOM   2958  CE1 PHE A 387     -47.995  -4.631 -26.205  1.00 38.41           C  
ATOM   2959  CE2 PHE A 387     -49.240  -3.681 -28.011  1.00 36.11           C  
ATOM   2960  CZ  PHE A 387     -49.148  -4.578 -26.976  1.00 37.12           C  
ATOM   2961  N   PHE A 388     -45.322  -2.868 -30.756  1.00 28.62           N  
ATOM   2962  CA  PHE A 388     -45.697  -3.573 -31.980  1.00 21.28           C  
ATOM   2963  C   PHE A 388     -44.619  -4.600 -32.351  1.00 25.91           C  
ATOM   2964  O   PHE A 388     -44.893  -5.796 -32.526  1.00 22.67           O  
ATOM   2965  CB  PHE A 388     -45.924  -2.606 -33.155  1.00 23.27           C  
ATOM   2966  CG  PHE A 388     -46.038  -3.300 -34.484  1.00 24.84           C  
ATOM   2967  CD1 PHE A 388     -47.180  -4.011 -34.807  1.00 26.03           C  
ATOM   2968  CD2 PHE A 388     -44.992  -3.264 -35.395  1.00 24.58           C  
ATOM   2969  CE1 PHE A 388     -47.281  -4.662 -36.012  1.00 24.01           C  
ATOM   2970  CE2 PHE A 388     -45.090  -3.920 -36.612  1.00 30.16           C  
ATOM   2971  CZ  PHE A 388     -46.238  -4.615 -36.916  1.00 28.88           C  
ATOM   2972  N   SER A 389     -43.390  -4.107 -32.423  1.00 19.87           N  
ATOM   2973  CA  SER A 389     -42.256  -4.851 -32.939  1.00 21.52           C  
ATOM   2974  C   SER A 389     -41.956  -6.062 -32.113  1.00 22.29           C  
ATOM   2975  O   SER A 389     -41.560  -7.097 -32.645  1.00 24.40           O  
ATOM   2976  CB  SER A 389     -41.020  -3.941 -32.994  1.00 19.73           C  
ATOM   2977  OG  SER A 389     -41.193  -2.946 -34.015  1.00 22.93           O  
ATOM   2978  N   ALA A 390     -42.143  -5.912 -30.795  1.00 24.12           N  
ATOM   2979  CA  ALA A 390     -41.839  -6.945 -29.824  1.00 23.90           C  
ATOM   2980  C   ALA A 390     -42.671  -8.196 -30.054  1.00 24.61           C  
ATOM   2981  O   ALA A 390     -42.323  -9.270 -29.569  1.00 24.45           O  
ATOM   2982  CB  ALA A 390     -42.077  -6.409 -28.408  1.00 20.14           C  
ATOM   2983  N   HIS A 391     -43.786  -8.054 -30.762  1.00 24.88           N  
ATOM   2984  CA  HIS A 391     -44.624  -9.212 -31.072  1.00 30.46           C  
ATOM   2985  C   HIS A 391     -43.902 -10.248 -31.914  1.00 28.29           C  
ATOM   2986  O   HIS A 391     -44.198 -11.439 -31.822  1.00 27.83           O  
ATOM   2987  CB  HIS A 391     -45.944  -8.808 -31.730  1.00 28.64           C  
ATOM   2988  CG  HIS A 391     -46.912  -8.185 -30.781  1.00 30.03           C  
ATOM   2989  ND1 HIS A 391     -46.737  -6.915 -30.267  1.00 28.35           N  
ATOM   2990  CD2 HIS A 391     -48.055  -8.657 -30.225  1.00 31.52           C  
ATOM   2991  CE1 HIS A 391     -47.737  -6.629 -29.455  1.00 35.76           C  
ATOM   2992  NE2 HIS A 391     -48.549  -7.671 -29.406  1.00 32.66           N  
ATOM   2993  N   LEU A 392     -42.946  -9.806 -32.723  1.00 29.50           N  
ATOM   2994  CA  LEU A 392     -42.106 -10.750 -33.454  1.00 26.84           C  
ATOM   2995  C   LEU A 392     -41.275 -11.557 -32.454  1.00 28.52           C  
ATOM   2996  O   LEU A 392     -41.137 -12.771 -32.557  1.00 25.83           O  
ATOM   2997  CB  LEU A 392     -41.183  -9.996 -34.403  1.00 29.33           C  
ATOM   2998  CG  LEU A 392     -40.424 -10.781 -35.465  1.00 36.08           C  
ATOM   2999  CD1 LEU A 392     -41.400 -11.597 -36.302  1.00 31.34           C  
ATOM   3000  CD2 LEU A 392     -39.607  -9.820 -36.327  1.00 25.80           C  
ATOM   3001  N   VAL A 393     -40.722 -10.848 -31.475  1.00 28.95           N  
ATOM   3002  CA  VAL A 393     -39.867 -11.457 -30.470  1.00 29.45           C  
ATOM   3003  C   VAL A 393     -40.661 -12.405 -29.571  1.00 30.56           C  
ATOM   3004  O   VAL A 393     -40.157 -13.442 -29.131  1.00 27.88           O  
ATOM   3005  CB  VAL A 393     -39.214 -10.348 -29.613  1.00 30.89           C  
ATOM   3006  CG1 VAL A 393     -38.580 -10.914 -28.360  1.00 29.34           C  
ATOM   3007  CG2 VAL A 393     -38.215  -9.562 -30.479  1.00 27.54           C  
ATOM   3008  N   MET A 394     -41.901 -12.038 -29.288  1.00 23.04           N  
ATOM   3009  CA  MET A 394     -42.728 -12.815 -28.387  1.00 26.78           C  
ATOM   3010  C   MET A 394     -43.262 -14.081 -29.053  1.00 29.29           C  
ATOM   3011  O   MET A 394     -43.530 -15.070 -28.371  1.00 26.91           O  
ATOM   3012  CB  MET A 394     -43.906 -11.975 -27.886  1.00 27.29           C  
ATOM   3013  CG  MET A 394     -43.510 -10.833 -26.961  1.00 32.94           C  
ATOM   3014  SD  MET A 394     -44.947 -10.024 -26.220  1.00 36.93           S  
ATOM   3015  CE  MET A 394     -45.435  -8.908 -27.529  1.00 29.56           C  
ATOM   3016  N   PHE A 395     -43.415 -14.048 -30.375  1.00 23.92           N  
ATOM   3017  CA  PHE A 395     -44.119 -15.130 -31.088  1.00 27.32           C  
ATOM   3018  C   PHE A 395     -43.283 -15.972 -32.037  1.00 28.20           C  
ATOM   3019  O   PHE A 395     -43.671 -17.095 -32.377  1.00 31.25           O  
ATOM   3020  CB  PHE A 395     -45.363 -14.589 -31.819  1.00 30.83           C  
ATOM   3021  CG  PHE A 395     -46.460 -14.204 -30.884  1.00 35.26           C  
ATOM   3022  CD1 PHE A 395     -47.305 -15.172 -30.355  1.00 36.24           C  
ATOM   3023  CD2 PHE A 395     -46.610 -12.889 -30.482  1.00 26.99           C  
ATOM   3024  CE1 PHE A 395     -48.302 -14.831 -29.457  1.00 35.10           C  
ATOM   3025  CE2 PHE A 395     -47.599 -12.538 -29.588  1.00 37.29           C  
ATOM   3026  CZ  PHE A 395     -48.448 -13.510 -29.059  1.00 37.20           C  
ATOM   3027  N   LEU A 396     -42.147 -15.442 -32.470  1.00 27.74           N  
ATOM   3028  CA  LEU A 396     -41.290 -16.179 -33.387  1.00 26.06           C  
ATOM   3029  C   LEU A 396     -40.032 -16.672 -32.671  1.00 27.75           C  
ATOM   3030  O   LEU A 396     -39.208 -15.887 -32.208  1.00 26.94           O  
ATOM   3031  CB  LEU A 396     -40.958 -15.332 -34.619  1.00 23.93           C  
ATOM   3032  CG  LEU A 396     -40.053 -16.008 -35.654  1.00 27.84           C  
ATOM   3033  CD1 LEU A 396     -40.737 -17.224 -36.272  1.00 23.44           C  
ATOM   3034  CD2 LEU A 396     -39.590 -15.000 -36.719  1.00 30.68           C  
ATOM   3035  N   ASN A 397     -39.897 -17.989 -32.574  1.00 27.48           N  
ATOM   3036  CA  ASN A 397     -38.782 -18.565 -31.842  1.00 25.85           C  
ATOM   3037  C   ASN A 397     -37.456 -18.128 -32.459  1.00 30.93           C  
ATOM   3038  O   ASN A 397     -37.306 -18.129 -33.677  1.00 29.91           O  
ATOM   3039  CB  ASN A 397     -38.894 -20.096 -31.824  1.00 26.05           C  
ATOM   3040  CG  ASN A 397     -37.986 -20.730 -30.804  1.00 33.05           C  
ATOM   3041  OD1 ASN A 397     -37.803 -20.211 -29.702  1.00 32.22           O  
ATOM   3042  ND2 ASN A 397     -37.399 -21.857 -31.169  1.00 35.73           N  
ATOM   3043  N   LYS A 398     -36.507 -17.728 -31.615  1.00 35.10           N  
ATOM   3044  CA  LYS A 398     -35.167 -17.335 -32.069  1.00 30.90           C  
ATOM   3045  C   LYS A 398     -35.100 -15.954 -32.705  1.00 23.92           C  
ATOM   3046  O   LYS A 398     -34.028 -15.507 -33.119  1.00 29.54           O  
ATOM   3047  CB  LYS A 398     -34.573 -18.375 -33.026  1.00 37.67           C  
ATOM   3048  CG  LYS A 398     -34.386 -19.740 -32.386  1.00 41.10           C  
ATOM   3049  CD  LYS A 398     -34.013 -19.594 -30.920  1.00 38.58           C  
ATOM   3050  CE  LYS A 398     -33.567 -20.928 -30.332  1.00 63.85           C  
ATOM   3051  NZ  LYS A 398     -33.567 -20.893 -28.842  1.00 46.63           N  
ATOM   3052  N   SER A 399     -36.235 -15.275 -32.791  1.00 26.70           N  
ATOM   3053  CA  SER A 399     -36.221 -13.911 -33.278  1.00 24.04           C  
ATOM   3054  C   SER A 399     -35.380 -13.062 -32.338  1.00 30.71           C  
ATOM   3055  O   SER A 399     -34.520 -12.296 -32.777  1.00 27.80           O  
ATOM   3056  CB  SER A 399     -37.631 -13.348 -33.339  1.00 26.12           C  
ATOM   3057  OG  SER A 399     -37.581 -12.025 -33.832  1.00 29.51           O  
ATOM   3058  N   LEU A 400     -35.643 -13.195 -31.036  1.00 26.41           N  
ATOM   3059  CA  LEU A 400     -34.853 -12.506 -30.030  1.00 21.28           C  
ATOM   3060  C   LEU A 400     -33.359 -12.681 -30.315  1.00 29.88           C  
ATOM   3061  O   LEU A 400     -32.579 -11.713 -30.288  1.00 27.64           O  
ATOM   3062  CB  LEU A 400     -35.201 -13.044 -28.629  1.00 25.08           C  
ATOM   3063  CG  LEU A 400     -34.547 -12.411 -27.390  1.00 40.07           C  
ATOM   3064  CD1 LEU A 400     -35.420 -12.621 -26.136  1.00 35.50           C  
ATOM   3065  CD2 LEU A 400     -33.112 -12.910 -27.149  1.00 31.16           C  
ATOM   3066  N   ASP A 401     -32.969 -13.924 -30.588  1.00 27.28           N  
ATOM   3067  CA  ASP A 401     -31.567 -14.278 -30.763  1.00 30.05           C  
ATOM   3068  C   ASP A 401     -30.941 -13.597 -31.977  1.00 30.60           C  
ATOM   3069  O   ASP A 401     -29.787 -13.183 -31.932  1.00 28.76           O  
ATOM   3070  CB  ASP A 401     -31.406 -15.803 -30.888  1.00 33.09           C  
ATOM   3071  CG  ASP A 401     -31.967 -16.553 -29.689  1.00 43.50           C  
ATOM   3072  OD1 ASP A 401     -33.198 -16.488 -29.456  1.00 44.14           O  
ATOM   3073  OD2 ASP A 401     -31.177 -17.205 -28.971  1.00 49.65           O  
ATOM   3074  N   GLU A 402     -31.702 -13.505 -33.066  1.00 25.55           N  
ATOM   3075  CA  GLU A 402     -31.217 -12.887 -34.279  1.00 30.42           C  
ATOM   3076  C   GLU A 402     -31.028 -11.365 -34.073  1.00 33.51           C  
ATOM   3077  O   GLU A 402     -30.047 -10.780 -34.544  1.00 27.05           O  
ATOM   3078  CB  GLU A 402     -32.192 -13.203 -35.427  1.00 25.22           C  
ATOM   3079  CG  GLU A 402     -31.656 -13.008 -36.823  1.00 35.34           C  
ATOM   3080  CD  GLU A 402     -30.556 -13.982 -37.203  1.00 35.77           C  
ATOM   3081  OE1 GLU A 402     -30.453 -15.073 -36.608  1.00 40.67           O  
ATOM   3082  OE2 GLU A 402     -29.781 -13.643 -38.105  1.00 42.21           O  
ATOM   3083  N   MET A 403     -31.958 -10.732 -33.359  1.00 26.48           N  
ATOM   3084  CA  MET A 403     -31.852  -9.297 -33.101  1.00 29.44           C  
ATOM   3085  C   MET A 403     -30.653  -9.047 -32.188  1.00 24.84           C  
ATOM   3086  O   MET A 403     -29.850  -8.147 -32.422  1.00 26.02           O  
ATOM   3087  CB  MET A 403     -33.120  -8.755 -32.432  1.00 20.84           C  
ATOM   3088  CG  MET A 403     -34.375  -8.946 -33.223  1.00 23.28           C  
ATOM   3089  SD  MET A 403     -35.709  -7.944 -32.572  1.00 26.95           S  
ATOM   3090  CE  MET A 403     -37.094  -8.603 -33.500  1.00 27.47           C  
ATOM   3091  N   ASP A 404     -30.552  -9.867 -31.143  1.00 29.23           N  
ATOM   3092  CA  ASP A 404     -29.472  -9.739 -30.185  1.00 28.74           C  
ATOM   3093  C   ASP A 404     -28.124  -9.909 -30.860  1.00 29.26           C  
ATOM   3094  O   ASP A 404     -27.133  -9.292 -30.454  1.00 32.01           O  
ATOM   3095  CB  ASP A 404     -29.603 -10.767 -29.061  1.00 29.86           C  
ATOM   3096  CG  ASP A 404     -28.491 -10.633 -28.034  1.00 29.99           C  
ATOM   3097  OD1 ASP A 404     -28.382  -9.553 -27.408  1.00 30.08           O  
ATOM   3098  OD2 ASP A 404     -27.713 -11.592 -27.886  1.00 31.30           O  
ATOM   3099  N   PHE A 405     -28.079 -10.757 -31.878  1.00 29.82           N  
ATOM   3100  CA  PHE A 405     -26.838 -10.937 -32.615  1.00 25.87           C  
ATOM   3101  C   PHE A 405     -26.462  -9.755 -33.512  1.00 31.94           C  
ATOM   3102  O   PHE A 405     -25.415  -9.122 -33.290  1.00 30.62           O  
ATOM   3103  CB  PHE A 405     -26.844 -12.210 -33.445  1.00 30.07           C  
ATOM   3104  CG  PHE A 405     -25.567 -12.413 -34.197  1.00 33.65           C  
ATOM   3105  CD1 PHE A 405     -24.449 -12.937 -33.555  1.00 34.77           C  
ATOM   3106  CD2 PHE A 405     -25.466 -12.047 -35.521  1.00 34.25           C  
ATOM   3107  CE1 PHE A 405     -23.260 -13.112 -34.234  1.00 38.45           C  
ATOM   3108  CE2 PHE A 405     -24.282 -12.225 -36.206  1.00 43.71           C  
ATOM   3109  CZ  PHE A 405     -23.176 -12.760 -35.559  1.00 40.74           C  
ATOM   3110  N   TRP A 406     -27.298  -9.464 -34.519  1.00 25.02           N  
ATOM   3111  CA  TRP A 406     -26.999  -8.390 -35.489  1.00 26.80           C  
ATOM   3112  C   TRP A 406     -26.964  -6.986 -34.892  1.00 28.30           C  
ATOM   3113  O   TRP A 406     -26.027  -6.235 -35.121  1.00 35.04           O  
ATOM   3114  CB  TRP A 406     -27.966  -8.417 -36.687  1.00 29.75           C  
ATOM   3115  CG  TRP A 406     -27.851  -9.679 -37.458  1.00 35.38           C  
ATOM   3116  CD1 TRP A 406     -28.704 -10.739 -37.422  1.00 34.22           C  
ATOM   3117  CD2 TRP A 406     -26.785 -10.049 -38.341  1.00 35.07           C  
ATOM   3118  NE1 TRP A 406     -28.247 -11.740 -38.248  1.00 35.69           N  
ATOM   3119  CE2 TRP A 406     -27.068 -11.342 -38.819  1.00 35.14           C  
ATOM   3120  CE3 TRP A 406     -25.619  -9.409 -38.776  1.00 36.42           C  
ATOM   3121  CZ2 TRP A 406     -26.235 -12.009 -39.725  1.00 45.47           C  
ATOM   3122  CZ3 TRP A 406     -24.792 -10.075 -39.677  1.00 37.06           C  
ATOM   3123  CH2 TRP A 406     -25.107 -11.360 -40.139  1.00 36.55           C  
ATOM   3124  N   ALA A 407     -27.993  -6.619 -34.145  1.00 32.62           N  
ATOM   3125  CA  ALA A 407     -28.010  -5.314 -33.499  1.00 27.21           C  
ATOM   3126  C   ALA A 407     -27.228  -5.360 -32.194  1.00 33.59           C  
ATOM   3127  O   ALA A 407     -26.344  -4.536 -31.953  1.00 32.47           O  
ATOM   3128  CB  ALA A 407     -29.438  -4.865 -33.239  1.00 30.12           C  
ATOM   3129  N   GLY A 408     -27.536  -6.352 -31.366  1.00 29.07           N  
ATOM   3130  CA  GLY A 408     -27.082  -6.345 -29.993  1.00 30.61           C  
ATOM   3131  C   GLY A 408     -25.634  -6.746 -29.820  1.00 33.29           C  
ATOM   3132  O   GLY A 408     -25.058  -6.458 -28.793  1.00 31.98           O  
ATOM   3133  N   THR A 409     -25.024  -7.365 -30.833  1.00 31.28           N  
ATOM   3134  CA  THR A 409     -23.695  -7.952 -30.638  1.00 31.48           C  
ATOM   3135  C   THR A 409     -22.694  -7.483 -31.699  1.00 31.05           C  
ATOM   3136  O   THR A 409     -21.826  -6.640 -31.423  1.00 29.98           O  
ATOM   3137  CB  THR A 409     -23.788  -9.500 -30.571  1.00 34.53           C  
ATOM   3138  OG1 THR A 409     -24.764  -9.862 -29.588  1.00 33.30           O  
ATOM   3139  CG2 THR A 409     -22.450 -10.120 -30.174  1.00 38.94           C  
ATOM   3140  N   ILE A 410     -22.814  -8.034 -32.903  1.00 35.57           N  
ATOM   3141  CA  ILE A 410     -22.061  -7.566 -34.059  1.00 31.39           C  
ATOM   3142  C   ILE A 410     -22.201  -6.064 -34.172  1.00 35.13           C  
ATOM   3143  O   ILE A 410     -21.208  -5.328 -34.235  1.00 32.09           O  
ATOM   3144  CB  ILE A 410     -22.646  -8.142 -35.354  1.00 34.26           C  
ATOM   3145  CG1 ILE A 410     -22.473  -9.647 -35.384  1.00 43.40           C  
ATOM   3146  CG2 ILE A 410     -21.971  -7.517 -36.563  1.00 41.39           C  
ATOM   3147  CD1 ILE A 410     -21.123 -10.071 -35.914  1.00 64.10           C  
ATOM   3148  N   GLY A 411     -23.457  -5.630 -34.211  1.00 28.05           N  
ATOM   3149  CA  GLY A 411     -23.796  -4.230 -34.281  1.00 26.90           C  
ATOM   3150  C   GLY A 411     -23.032  -3.349 -33.319  1.00 35.72           C  
ATOM   3151  O   GLY A 411     -22.323  -2.437 -33.754  1.00 31.97           O  
ATOM   3152  N   VAL A 412     -23.168  -3.593 -32.013  1.00 29.24           N  
ATOM   3153  CA  VAL A 412     -22.587  -2.659 -31.060  1.00 29.46           C  
ATOM   3154  C   VAL A 412     -21.066  -2.641 -31.134  1.00 29.43           C  
ATOM   3155  O   VAL A 412     -20.455  -1.603 -30.927  1.00 30.49           O  
ATOM   3156  CB  VAL A 412     -23.023  -2.904 -29.578  1.00 37.05           C  
ATOM   3157  CG1 VAL A 412     -24.539  -2.867 -29.435  1.00 27.52           C  
ATOM   3158  CG2 VAL A 412     -22.435  -4.213 -29.048  1.00 35.20           C  
ATOM   3159  N   VAL A 413     -20.443  -3.783 -31.401  1.00 29.17           N  
ATOM   3160  CA  VAL A 413     -18.984  -3.798 -31.380  1.00 38.11           C  
ATOM   3161  C   VAL A 413     -18.432  -3.063 -32.591  1.00 39.64           C  
ATOM   3162  O   VAL A 413     -17.515  -2.246 -32.472  1.00 37.79           O  
ATOM   3163  CB  VAL A 413     -18.391  -5.206 -31.299  1.00 35.86           C  
ATOM   3164  CG1 VAL A 413     -16.890  -5.144 -31.591  1.00 43.46           C  
ATOM   3165  CG2 VAL A 413     -18.636  -5.805 -29.905  1.00 32.04           C  
ATOM   3166  N   PHE A 414     -19.005  -3.346 -33.755  1.00 36.35           N  
ATOM   3167  CA  PHE A 414     -18.682  -2.590 -34.951  1.00 33.65           C  
ATOM   3168  C   PHE A 414     -18.963  -1.111 -34.723  1.00 31.08           C  
ATOM   3169  O   PHE A 414     -18.177  -0.256 -35.124  1.00 33.00           O  
ATOM   3170  CB  PHE A 414     -19.480  -3.118 -36.148  1.00 40.38           C  
ATOM   3171  CG  PHE A 414     -19.752  -2.084 -37.212  1.00 51.61           C  
ATOM   3172  CD1 PHE A 414     -18.731  -1.620 -38.034  1.00 57.89           C  
ATOM   3173  CD2 PHE A 414     -21.042  -1.591 -37.407  1.00 55.00           C  
ATOM   3174  CE1 PHE A 414     -18.988  -0.670 -39.022  1.00 60.96           C  
ATOM   3175  CE2 PHE A 414     -21.306  -0.643 -38.395  1.00 54.81           C  
ATOM   3176  CZ  PHE A 414     -20.281  -0.186 -39.202  1.00 50.50           C  
ATOM   3177  N   PHE A 415     -20.081  -0.796 -34.077  1.00 33.71           N  
ATOM   3178  CA  PHE A 415     -20.415   0.612 -33.874  1.00 36.05           C  
ATOM   3179  C   PHE A 415     -19.435   1.306 -32.939  1.00 32.19           C  
ATOM   3180  O   PHE A 415     -19.073   2.460 -33.165  1.00 35.38           O  
ATOM   3181  CB  PHE A 415     -21.843   0.804 -33.367  1.00 27.72           C  
ATOM   3182  CG  PHE A 415     -22.324   2.216 -33.488  1.00 30.95           C  
ATOM   3183  CD1 PHE A 415     -22.573   2.765 -34.740  1.00 35.40           C  
ATOM   3184  CD2 PHE A 415     -22.504   3.002 -32.369  1.00 34.25           C  
ATOM   3185  CE1 PHE A 415     -23.008   4.070 -34.869  1.00 31.18           C  
ATOM   3186  CE2 PHE A 415     -22.942   4.318 -32.488  1.00 35.78           C  
ATOM   3187  CZ  PHE A 415     -23.187   4.853 -33.746  1.00 35.00           C  
ATOM   3188  N   GLY A 416     -19.028   0.606 -31.881  1.00 37.48           N  
ATOM   3189  CA  GLY A 416     -18.026   1.117 -30.965  1.00 34.67           C  
ATOM   3190  C   GLY A 416     -16.733   1.462 -31.698  1.00 37.16           C  
ATOM   3191  O   GLY A 416     -16.189   2.547 -31.529  1.00 34.50           O  
ATOM   3192  N   LEU A 417     -16.245   0.535 -32.519  1.00 38.06           N  
ATOM   3193  CA  LEU A 417     -15.076   0.782 -33.360  1.00 34.24           C  
ATOM   3194  C   LEU A 417     -15.291   2.030 -34.207  1.00 36.03           C  
ATOM   3195  O   LEU A 417     -14.395   2.868 -34.358  1.00 36.50           O  
ATOM   3196  CB  LEU A 417     -14.797  -0.427 -34.262  1.00 31.87           C  
ATOM   3197  CG  LEU A 417     -13.581  -0.253 -35.182  1.00 40.51           C  
ATOM   3198  CD1 LEU A 417     -12.396   0.304 -34.403  1.00 39.56           C  
ATOM   3199  CD2 LEU A 417     -13.198  -1.560 -35.871  1.00 37.56           C  
ATOM   3200  N   THR A 418     -16.495   2.149 -34.755  1.00 35.79           N  
ATOM   3201  CA  THR A 418     -16.861   3.294 -35.567  1.00 31.66           C  
ATOM   3202  C   THR A 418     -16.770   4.569 -34.739  1.00 43.45           C  
ATOM   3203  O   THR A 418     -16.300   5.600 -35.221  1.00 35.63           O  
ATOM   3204  CB  THR A 418     -18.287   3.148 -36.136  1.00 36.48           C  
ATOM   3205  OG1 THR A 418     -18.321   2.056 -37.065  1.00 45.36           O  
ATOM   3206  CG2 THR A 418     -18.707   4.407 -36.853  1.00 39.01           C  
ATOM   3207  N   GLU A 419     -17.239   4.494 -33.499  1.00 33.03           N  
ATOM   3208  CA  GLU A 419     -17.177   5.637 -32.590  1.00 37.03           C  
ATOM   3209  C   GLU A 419     -15.738   6.090 -32.377  1.00 36.96           C  
ATOM   3210  O   GLU A 419     -15.429   7.274 -32.491  1.00 38.65           O  
ATOM   3211  CB  GLU A 419     -17.805   5.276 -31.239  1.00 33.43           C  
ATOM   3212  CG  GLU A 419     -19.324   5.285 -31.265  1.00 32.64           C  
ATOM   3213  CD  GLU A 419     -19.933   4.809 -29.959  1.00 31.65           C  
ATOM   3214  OE1 GLU A 419     -21.103   5.149 -29.697  1.00 34.55           O  
ATOM   3215  OE2 GLU A 419     -19.246   4.100 -29.198  1.00 35.92           O  
ATOM   3216  N   LEU A 420     -14.868   5.134 -32.072  1.00 36.54           N  
ATOM   3217  CA  LEU A 420     -13.443   5.396 -31.916  1.00 37.34           C  
ATOM   3218  C   LEU A 420     -12.835   6.122 -33.113  1.00 50.38           C  
ATOM   3219  O   LEU A 420     -12.093   7.098 -32.950  1.00 43.95           O  
ATOM   3220  CB  LEU A 420     -12.697   4.081 -31.687  1.00 39.23           C  
ATOM   3221  CG  LEU A 420     -12.822   3.547 -30.262  1.00 43.12           C  
ATOM   3222  CD1 LEU A 420     -12.442   2.074 -30.167  1.00 45.54           C  
ATOM   3223  CD2 LEU A 420     -11.959   4.393 -29.339  1.00 46.35           C  
ATOM   3224  N   ILE A 421     -13.161   5.648 -34.315  1.00 40.80           N  
ATOM   3225  CA  ILE A 421     -12.574   6.174 -35.538  1.00 32.72           C  
ATOM   3226  C   ILE A 421     -13.114   7.546 -35.893  1.00 35.33           C  
ATOM   3227  O   ILE A 421     -12.354   8.462 -36.189  1.00 43.08           O  
ATOM   3228  CB  ILE A 421     -12.801   5.204 -36.705  1.00 45.19           C  
ATOM   3229  CG1 ILE A 421     -12.049   3.903 -36.442  1.00 40.37           C  
ATOM   3230  CG2 ILE A 421     -12.366   5.824 -38.027  1.00 38.17           C  
ATOM   3231  CD1 ILE A 421     -12.431   2.791 -37.400  1.00 42.35           C  
ATOM   3232  N   ILE A 422     -14.428   7.698 -35.867  1.00 34.00           N  
ATOM   3233  CA  ILE A 422     -15.020   8.994 -36.159  1.00 35.53           C  
ATOM   3234  C   ILE A 422     -14.525  10.087 -35.191  1.00 40.36           C  
ATOM   3235  O   ILE A 422     -14.260  11.221 -35.604  1.00 38.13           O  
ATOM   3236  CB  ILE A 422     -16.563   8.940 -36.119  1.00 37.38           C  
ATOM   3237  CG1 ILE A 422     -17.132   8.558 -37.484  1.00 52.10           C  
ATOM   3238  CG2 ILE A 422     -17.139  10.294 -35.736  1.00 54.73           C  
ATOM   3239  CD1 ILE A 422     -18.519   9.154 -37.751  1.00 48.20           C  
ATOM   3240  N   PHE A 423     -14.423   9.742 -33.908  1.00 37.29           N  
ATOM   3241  CA  PHE A 423     -14.074  10.711 -32.871  1.00 42.24           C  
ATOM   3242  C   PHE A 423     -12.574  10.994 -32.844  1.00 29.64           C  
ATOM   3243  O   PHE A 423     -12.153  12.128 -33.022  1.00 41.44           O  
ATOM   3244  CB  PHE A 423     -14.545  10.227 -31.486  1.00 38.02           C  
ATOM   3245  CG  PHE A 423     -14.781  11.337 -30.489  1.00 30.27           C  
ATOM   3246  CD1 PHE A 423     -15.574  12.426 -30.816  1.00 37.12           C  
ATOM   3247  CD2 PHE A 423     -14.232  11.273 -29.213  1.00 32.94           C  
ATOM   3248  CE1 PHE A 423     -15.805  13.450 -29.897  1.00 39.67           C  
ATOM   3249  CE2 PHE A 423     -14.461  12.297 -28.273  1.00 36.82           C  
ATOM   3250  CZ  PHE A 423     -15.251  13.381 -28.623  1.00 41.83           C  
ATOM   3251  N   PHE A 424     -11.771   9.961 -32.629  1.00 36.09           N  
ATOM   3252  CA  PHE A 424     -10.334  10.153 -32.480  1.00 40.34           C  
ATOM   3253  C   PHE A 424      -9.512  10.225 -33.756  1.00 51.59           C  
ATOM   3254  O   PHE A 424      -8.329  10.560 -33.707  1.00 50.57           O  
ATOM   3255  CB  PHE A 424      -9.738   9.112 -31.545  1.00 45.13           C  
ATOM   3256  CG  PHE A 424      -9.406   9.661 -30.204  1.00 46.77           C  
ATOM   3257  CD1 PHE A 424     -10.400   9.846 -29.260  1.00 44.68           C  
ATOM   3258  CD2 PHE A 424      -8.110  10.039 -29.898  1.00 43.28           C  
ATOM   3259  CE1 PHE A 424     -10.111  10.385 -28.038  1.00 40.51           C  
ATOM   3260  CE2 PHE A 424      -7.811  10.571 -28.663  1.00 45.87           C  
ATOM   3261  CZ  PHE A 424      -8.814  10.746 -27.735  1.00 48.85           C  
ATOM   3262  N   TRP A 425     -10.116   9.908 -34.892  1.00 42.46           N  
ATOM   3263  CA  TRP A 425      -9.364   9.956 -36.136  1.00 44.84           C  
ATOM   3264  C   TRP A 425      -9.914  10.972 -37.115  1.00 50.73           C  
ATOM   3265  O   TRP A 425      -9.163  11.760 -37.679  1.00 66.78           O  
ATOM   3266  CB  TRP A 425      -9.265   8.568 -36.765  1.00 40.82           C  
ATOM   3267  CG  TRP A 425      -8.320   7.696 -36.016  1.00 43.38           C  
ATOM   3268  CD1 TRP A 425      -8.594   6.955 -34.904  1.00 47.68           C  
ATOM   3269  CD2 TRP A 425      -6.929   7.491 -36.303  1.00 54.10           C  
ATOM   3270  NE1 TRP A 425      -7.461   6.295 -34.481  1.00 52.97           N  
ATOM   3271  CE2 TRP A 425      -6.426   6.607 -35.325  1.00 60.49           C  
ATOM   3272  CE3 TRP A 425      -6.060   7.972 -37.288  1.00 60.18           C  
ATOM   3273  CZ2 TRP A 425      -5.094   6.185 -35.312  1.00 65.72           C  
ATOM   3274  CZ3 TRP A 425      -4.736   7.551 -37.272  1.00 61.49           C  
ATOM   3275  CH2 TRP A 425      -4.268   6.667 -36.293  1.00 59.63           C  
ATOM   3276  N   ILE A 426     -11.223  10.962 -37.316  1.00 42.71           N  
ATOM   3277  CA  ILE A 426     -11.825  11.851 -38.293  1.00 35.83           C  
ATOM   3278  C   ILE A 426     -12.114  13.226 -37.697  1.00 46.50           C  
ATOM   3279  O   ILE A 426     -11.681  14.256 -38.215  1.00 38.71           O  
ATOM   3280  CB  ILE A 426     -13.101  11.235 -38.873  1.00 33.71           C  
ATOM   3281  CG1 ILE A 426     -12.734   9.974 -39.673  1.00 45.09           C  
ATOM   3282  CG2 ILE A 426     -13.835  12.267 -39.722  1.00 38.87           C  
ATOM   3283  CD1 ILE A 426     -13.926   9.136 -40.149  1.00 43.53           C  
ATOM   3284  N   PHE A 427     -12.838  13.242 -36.590  1.00 45.40           N  
ATOM   3285  CA  PHE A 427     -13.119  14.498 -35.919  1.00 41.56           C  
ATOM   3286  C   PHE A 427     -11.792  15.162 -35.552  1.00 46.50           C  
ATOM   3287  O   PHE A 427     -11.633  16.372 -35.708  1.00 53.83           O  
ATOM   3288  CB  PHE A 427     -13.975  14.238 -34.686  1.00 39.39           C  
ATOM   3289  CG  PHE A 427     -14.374  15.476 -33.931  1.00 40.74           C  
ATOM   3290  CD1 PHE A 427     -15.165  16.449 -34.521  1.00 45.99           C  
ATOM   3291  CD2 PHE A 427     -13.985  15.645 -32.613  1.00 42.80           C  
ATOM   3292  CE1 PHE A 427     -15.547  17.575 -33.813  1.00 45.75           C  
ATOM   3293  CE2 PHE A 427     -14.366  16.766 -31.898  1.00 41.54           C  
ATOM   3294  CZ  PHE A 427     -15.145  17.737 -32.500  1.00 37.49           C  
ATOM   3295  N   GLY A 428     -10.838  14.360 -35.089  1.00 43.90           N  
ATOM   3296  CA  GLY A 428      -9.532  14.865 -34.708  1.00 39.75           C  
ATOM   3297  C   GLY A 428      -9.138  14.402 -33.319  1.00 44.02           C  
ATOM   3298  O   GLY A 428      -9.871  14.620 -32.353  1.00 41.00           O  
ATOM   3299  N   ALA A 429      -7.981  13.757 -33.206  1.00 34.05           N  
ATOM   3300  CA  ALA A 429      -7.554  13.209 -31.927  1.00 40.03           C  
ATOM   3301  C   ALA A 429      -7.383  14.292 -30.857  1.00 51.60           C  
ATOM   3302  O   ALA A 429      -7.680  14.070 -29.675  1.00 47.01           O  
ATOM   3303  CB  ALA A 429      -6.275  12.397 -32.092  1.00 44.98           C  
ATOM   3304  N   ASP A 430      -6.911  15.466 -31.263  1.00 42.28           N  
ATOM   3305  CA  ASP A 430      -6.715  16.550 -30.306  1.00 45.17           C  
ATOM   3306  C   ASP A 430      -8.026  17.242 -29.949  1.00 45.68           C  
ATOM   3307  O   ASP A 430      -8.247  17.576 -28.793  1.00 41.46           O  
ATOM   3308  CB  ASP A 430      -5.672  17.552 -30.808  1.00 44.89           C  
ATOM   3309  CG  ASP A 430      -4.253  17.020 -30.693  1.00 57.39           C  
ATOM   3310  OD1 ASP A 430      -4.057  15.782 -30.723  1.00 51.07           O  
ATOM   3311  OD2 ASP A 430      -3.326  17.846 -30.569  1.00 80.53           O  
ATOM   3312  N   LYS A 431      -8.891  17.456 -30.938  1.00 39.92           N  
ATOM   3313  CA  LYS A 431     -10.247  17.934 -30.665  1.00 44.94           C  
ATOM   3314  C   LYS A 431     -11.022  16.961 -29.772  1.00 45.12           C  
ATOM   3315  O   LYS A 431     -11.715  17.379 -28.851  1.00 40.07           O  
ATOM   3316  CB  LYS A 431     -11.015  18.142 -31.968  1.00 42.46           C  
ATOM   3317  CG  LYS A 431     -10.475  19.269 -32.824  1.00 55.51           C  
ATOM   3318  CD  LYS A 431     -11.070  19.231 -34.227  1.00 53.41           C  
ATOM   3319  CE  LYS A 431     -12.589  19.273 -34.186  1.00 62.56           C  
ATOM   3320  NZ  LYS A 431     -13.116  20.417 -33.387  1.00 70.57           N  
ATOM   3321  N   ALA A 432     -10.908  15.663 -30.060  1.00 38.25           N  
ATOM   3322  CA  ALA A 432     -11.550  14.640 -29.243  1.00 37.80           C  
ATOM   3323  C   ALA A 432     -11.091  14.786 -27.801  1.00 41.59           C  
ATOM   3324  O   ALA A 432     -11.903  14.831 -26.875  1.00 36.54           O  
ATOM   3325  CB  ALA A 432     -11.203  13.256 -29.746  1.00 33.27           C  
ATOM   3326  N   TRP A 433      -9.773  14.830 -27.630  1.00 42.54           N  
ATOM   3327  CA  TRP A 433      -9.159  14.891 -26.308  1.00 44.81           C  
ATOM   3328  C   TRP A 433      -9.667  16.089 -25.512  1.00 43.97           C  
ATOM   3329  O   TRP A 433     -10.013  15.968 -24.336  1.00 37.85           O  
ATOM   3330  CB  TRP A 433      -7.636  14.968 -26.428  1.00 44.56           C  
ATOM   3331  CG  TRP A 433      -6.932  14.887 -25.092  1.00 39.49           C  
ATOM   3332  CD1 TRP A 433      -6.276  15.901 -24.436  1.00 42.19           C  
ATOM   3333  CD2 TRP A 433      -6.821  13.732 -24.259  1.00 39.78           C  
ATOM   3334  NE1 TRP A 433      -5.757  15.434 -23.245  1.00 39.05           N  
ATOM   3335  CE2 TRP A 433      -6.082  14.109 -23.110  1.00 37.90           C  
ATOM   3336  CE3 TRP A 433      -7.276  12.409 -24.370  1.00 41.68           C  
ATOM   3337  CZ2 TRP A 433      -5.793  13.217 -22.086  1.00 35.94           C  
ATOM   3338  CZ3 TRP A 433      -6.982  11.522 -23.350  1.00 47.73           C  
ATOM   3339  CH2 TRP A 433      -6.246  11.931 -22.219  1.00 43.10           C  
ATOM   3340  N   GLU A 434      -9.712  17.244 -26.161  1.00 43.55           N  
ATOM   3341  CA  GLU A 434     -10.182  18.453 -25.499  1.00 47.70           C  
ATOM   3342  C   GLU A 434     -11.666  18.343 -25.182  1.00 50.69           C  
ATOM   3343  O   GLU A 434     -12.118  18.786 -24.125  1.00 42.81           O  
ATOM   3344  CB  GLU A 434      -9.894  19.686 -26.360  1.00 47.23           C  
ATOM   3345  CG  GLU A 434      -8.396  19.941 -26.558  1.00 57.86           C  
ATOM   3346  CD  GLU A 434      -7.665  20.286 -25.253  1.00 66.46           C  
ATOM   3347  OE1 GLU A 434      -8.063  21.268 -24.594  1.00 53.35           O  
ATOM   3348  OE2 GLU A 434      -6.686  19.586 -24.897  1.00 53.58           O  
ATOM   3349  N   GLU A 435     -12.420  17.735 -26.096  1.00 42.86           N  
ATOM   3350  CA  GLU A 435     -13.848  17.541 -25.892  1.00 36.73           C  
ATOM   3351  C   GLU A 435     -14.149  16.665 -24.664  1.00 41.49           C  
ATOM   3352  O   GLU A 435     -15.117  16.908 -23.953  1.00 43.16           O  
ATOM   3353  CB  GLU A 435     -14.490  16.953 -27.154  1.00 41.47           C  
ATOM   3354  CG  GLU A 435     -15.997  17.082 -27.199  1.00 46.29           C  
ATOM   3355  CD  GLU A 435     -16.480  18.516 -27.034  1.00 49.72           C  
ATOM   3356  OE1 GLU A 435     -15.855  19.437 -27.610  1.00 47.48           O  
ATOM   3357  OE2 GLU A 435     -17.504  18.711 -26.342  1.00 42.60           O  
ATOM   3358  N   ILE A 436     -13.326  15.648 -24.418  1.00 36.52           N  
ATOM   3359  CA  ILE A 436     -13.524  14.772 -23.265  1.00 35.76           C  
ATOM   3360  C   ILE A 436     -13.176  15.494 -21.962  1.00 46.06           C  
ATOM   3361  O   ILE A 436     -13.924  15.431 -20.977  1.00 31.77           O  
ATOM   3362  CB  ILE A 436     -12.639  13.508 -23.346  1.00 29.02           C  
ATOM   3363  CG1 ILE A 436     -13.039  12.645 -24.549  1.00 30.34           C  
ATOM   3364  CG2 ILE A 436     -12.743  12.714 -22.070  1.00 30.13           C  
ATOM   3365  CD1 ILE A 436     -11.960  11.648 -24.946  1.00 32.59           C  
ATOM   3366  N   ASN A 437     -12.038  16.186 -21.984  1.00 41.08           N  
ATOM   3367  CA  ASN A 437     -11.466  16.816 -20.801  1.00 42.61           C  
ATOM   3368  C   ASN A 437     -12.115  18.131 -20.376  1.00 41.76           C  
ATOM   3369  O   ASN A 437     -12.056  18.498 -19.199  1.00 42.12           O  
ATOM   3370  CB  ASN A 437      -9.959  17.010 -20.999  1.00 41.00           C  
ATOM   3371  CG  ASN A 437      -9.180  15.738 -20.769  1.00 37.21           C  
ATOM   3372  OD1 ASN A 437      -9.054  15.283 -19.642  1.00 37.96           O  
ATOM   3373  ND2 ASN A 437      -8.669  15.145 -21.841  1.00 41.24           N  
ATOM   3374  N   ARG A 438     -12.720  18.846 -21.324  1.00 34.90           N  
ATOM   3375  CA  ARG A 438     -13.343  20.127 -20.994  1.00 38.29           C  
ATOM   3376  C   ARG A 438     -14.290  19.977 -19.804  1.00 40.48           C  
ATOM   3377  O   ARG A 438     -15.143  19.099 -19.791  1.00 35.09           O  
ATOM   3378  CB  ARG A 438     -14.059  20.725 -22.208  1.00 40.17           C  
ATOM   3379  CG  ARG A 438     -14.543  22.153 -22.018  1.00 40.82           C  
ATOM   3380  CD  ARG A 438     -14.967  22.767 -23.345  1.00 48.50           C  
ATOM   3381  NE  ARG A 438     -15.671  21.782 -24.167  1.00 62.50           N  
ATOM   3382  CZ  ARG A 438     -16.957  21.503 -24.019  1.00 50.44           C  
ATOM   3383  NH1 ARG A 438     -17.656  22.145 -23.100  1.00 62.00           N  
ATOM   3384  NH2 ARG A 438     -17.541  20.595 -24.769  1.00 41.90           N  
ATOM   3385  N   GLY A 439     -14.115  20.825 -18.792  1.00 45.72           N  
ATOM   3386  CA  GLY A 439     -14.992  20.829 -17.633  1.00 38.82           C  
ATOM   3387  C   GLY A 439     -14.789  19.662 -16.681  1.00 36.76           C  
ATOM   3388  O   GLY A 439     -15.509  19.515 -15.682  1.00 34.97           O  
ATOM   3389  N   GLY A 440     -13.805  18.825 -16.983  1.00 29.67           N  
ATOM   3390  CA  GLY A 440     -13.550  17.660 -16.163  1.00 33.21           C  
ATOM   3391  C   GLY A 440     -13.173  18.063 -14.752  1.00 40.51           C  
ATOM   3392  O   GLY A 440     -12.381  18.991 -14.564  1.00 39.07           O  
ATOM   3393  N   ILE A 441     -13.751  17.380 -13.764  1.00 37.06           N  
ATOM   3394  CA  ILE A 441     -13.423  17.626 -12.359  1.00 39.52           C  
ATOM   3395  C   ILE A 441     -12.004  17.152 -12.124  1.00 43.14           C  
ATOM   3396  O   ILE A 441     -11.228  17.796 -11.412  1.00 41.72           O  
ATOM   3397  CB  ILE A 441     -14.387  16.889 -11.422  1.00 32.92           C  
ATOM   3398  CG1 ILE A 441     -15.784  17.506 -11.522  1.00 40.63           C  
ATOM   3399  CG2 ILE A 441     -13.859  16.905  -9.964  1.00 38.95           C  
ATOM   3400  CD1 ILE A 441     -16.872  16.680 -10.859  1.00 44.73           C  
ATOM   3401  N   ILE A 442     -11.691  16.002 -12.718  1.00 41.53           N  
ATOM   3402  CA  ILE A 442     -10.321  15.525 -12.871  1.00 37.84           C  
ATOM   3403  C   ILE A 442     -10.063  15.395 -14.367  1.00 40.67           C  
ATOM   3404  O   ILE A 442     -11.000  15.369 -15.153  1.00 36.29           O  
ATOM   3405  CB  ILE A 442     -10.127  14.142 -12.261  1.00 39.36           C  
ATOM   3406  CG1 ILE A 442     -11.157  13.171 -12.840  1.00 44.16           C  
ATOM   3407  CG2 ILE A 442     -10.227  14.203 -10.746  1.00 48.99           C  
ATOM   3408  CD1 ILE A 442     -10.854  11.735 -12.550  1.00 45.33           C  
ATOM   3409  N   LYS A 443      -8.800  15.293 -14.752  1.00 37.33           N  
ATOM   3410  CA  LYS A 443      -8.438  15.153 -16.154  1.00 46.73           C  
ATOM   3411  C   LYS A 443      -8.089  13.700 -16.479  1.00 48.75           C  
ATOM   3412  O   LYS A 443      -7.628  12.959 -15.610  1.00 42.51           O  
ATOM   3413  CB  LYS A 443      -7.263  16.074 -16.474  1.00 44.97           C  
ATOM   3414  CG  LYS A 443      -7.527  17.508 -16.057  1.00 56.00           C  
ATOM   3415  CD  LYS A 443      -8.567  18.160 -16.976  1.00 56.04           C  
ATOM   3416  CE  LYS A 443      -9.258  19.325 -16.263  1.00 57.17           C  
ATOM   3417  NZ  LYS A 443     -10.220  20.020 -17.145  1.00 52.89           N  
ATOM   3418  N   VAL A 444      -8.316  13.280 -17.721  1.00 42.70           N  
ATOM   3419  CA  VAL A 444      -7.957  11.919 -18.090  1.00 40.06           C  
ATOM   3420  C   VAL A 444      -6.431  11.850 -18.127  1.00 40.59           C  
ATOM   3421  O   VAL A 444      -5.790  12.745 -18.671  1.00 40.85           O  
ATOM   3422  CB  VAL A 444      -8.553  11.506 -19.462  1.00 44.84           C  
ATOM   3423  CG1 VAL A 444      -8.070  10.120 -19.850  1.00 42.91           C  
ATOM   3424  CG2 VAL A 444     -10.073  11.550 -19.425  1.00 42.54           C  
ATOM   3425  N   PRO A 445      -5.839  10.810 -17.515  1.00 44.20           N  
ATOM   3426  CA  PRO A 445      -4.382  10.674 -17.615  1.00 42.74           C  
ATOM   3427  C   PRO A 445      -3.893  10.771 -19.069  1.00 46.22           C  
ATOM   3428  O   PRO A 445      -4.444  10.130 -19.979  1.00 44.24           O  
ATOM   3429  CB  PRO A 445      -4.129   9.283 -17.026  1.00 42.32           C  
ATOM   3430  CG  PRO A 445      -5.210   9.136 -15.986  1.00 43.10           C  
ATOM   3431  CD  PRO A 445      -6.424   9.836 -16.573  1.00 39.97           C  
ATOM   3432  N   ARG A 446      -2.864  11.588 -19.270  1.00 39.67           N  
ATOM   3433  CA  ARG A 446      -2.312  11.859 -20.595  1.00 47.46           C  
ATOM   3434  C   ARG A 446      -2.043  10.574 -21.371  1.00 43.80           C  
ATOM   3435  O   ARG A 446      -2.177  10.533 -22.603  1.00 45.18           O  
ATOM   3436  CB  ARG A 446      -1.021  12.673 -20.459  1.00 47.52           C  
ATOM   3437  CG  ARG A 446      -0.528  13.339 -21.740  1.00 49.45           C  
ATOM   3438  CD  ARG A 446       0.632  14.295 -21.411  1.00 69.03           C  
ATOM   3439  NE  ARG A 446       1.251  14.879 -22.597  1.00 54.22           N  
ATOM   3440  CZ  ARG A 446       0.969  16.090 -23.069  1.00 60.53           C  
ATOM   3441  NH1 ARG A 446       0.063  16.852 -22.457  1.00 42.53           N  
ATOM   3442  NH2 ARG A 446       1.589  16.539 -24.158  1.00 43.84           N  
ATOM   3443  N   ILE A 447      -1.670   9.526 -20.646  1.00 38.03           N  
ATOM   3444  CA  ILE A 447      -1.380   8.239 -21.261  1.00 46.35           C  
ATOM   3445  C   ILE A 447      -2.595   7.652 -22.004  1.00 52.35           C  
ATOM   3446  O   ILE A 447      -2.435   6.913 -22.982  1.00 43.52           O  
ATOM   3447  CB  ILE A 447      -0.859   7.239 -20.234  1.00 38.63           C  
ATOM   3448  CG1 ILE A 447      -0.335   5.983 -20.932  1.00 52.58           C  
ATOM   3449  CG2 ILE A 447      -1.948   6.903 -19.229  1.00 49.64           C  
ATOM   3450  CD1 ILE A 447       0.617   6.274 -22.085  1.00 53.55           C  
ATOM   3451  N   TYR A 448      -3.807   7.992 -21.566  1.00 47.71           N  
ATOM   3452  CA  TYR A 448      -5.005   7.522 -22.278  1.00 49.03           C  
ATOM   3453  C   TYR A 448      -5.188   8.125 -23.663  1.00 46.71           C  
ATOM   3454  O   TYR A 448      -6.039   7.667 -24.421  1.00 46.47           O  
ATOM   3455  CB  TYR A 448      -6.276   7.768 -21.469  1.00 45.22           C  
ATOM   3456  CG  TYR A 448      -6.727   6.572 -20.664  1.00 48.04           C  
ATOM   3457  CD1 TYR A 448      -6.584   6.559 -19.292  1.00 40.25           C  
ATOM   3458  CD2 TYR A 448      -7.301   5.456 -21.280  1.00 44.16           C  
ATOM   3459  CE1 TYR A 448      -6.988   5.482 -18.540  1.00 40.90           C  
ATOM   3460  CE2 TYR A 448      -7.708   4.362 -20.528  1.00 37.04           C  
ATOM   3461  CZ  TYR A 448      -7.551   4.390 -19.149  1.00 38.26           C  
ATOM   3462  OH  TYR A 448      -7.951   3.330 -18.357  1.00 40.98           O  
ATOM   3463  N   TYR A 449      -4.424   9.165 -23.988  1.00 40.65           N  
ATOM   3464  CA  TYR A 449      -4.521   9.750 -25.317  1.00 37.61           C  
ATOM   3465  C   TYR A 449      -4.073   8.706 -26.320  1.00 42.20           C  
ATOM   3466  O   TYR A 449      -4.684   8.548 -27.363  1.00 45.86           O  
ATOM   3467  CB  TYR A 449      -3.662  11.012 -25.442  1.00 38.54           C  
ATOM   3468  CG  TYR A 449      -3.612  11.607 -26.839  1.00 42.62           C  
ATOM   3469  CD1 TYR A 449      -4.538  12.557 -27.245  1.00 33.85           C  
ATOM   3470  CD2 TYR A 449      -2.632  11.220 -27.751  1.00 49.82           C  
ATOM   3471  CE1 TYR A 449      -4.495  13.104 -28.512  1.00 42.66           C  
ATOM   3472  CE2 TYR A 449      -2.580  11.764 -29.030  1.00 44.13           C  
ATOM   3473  CZ  TYR A 449      -3.513  12.701 -29.406  1.00 53.12           C  
ATOM   3474  OH  TYR A 449      -3.461  13.251 -30.678  1.00 55.48           O  
ATOM   3475  N   TYR A 450      -3.011   7.983 -25.990  1.00 46.70           N  
ATOM   3476  CA  TYR A 450      -2.455   6.992 -26.906  1.00 56.03           C  
ATOM   3477  C   TYR A 450      -3.276   5.715 -26.889  1.00 45.82           C  
ATOM   3478  O   TYR A 450      -3.520   5.111 -27.931  1.00 46.03           O  
ATOM   3479  CB  TYR A 450      -0.986   6.729 -26.569  1.00 49.54           C  
ATOM   3480  CG  TYR A 450      -0.219   8.024 -26.460  1.00 63.65           C  
ATOM   3481  CD1 TYR A 450       0.330   8.626 -27.589  1.00 61.45           C  
ATOM   3482  CD2 TYR A 450      -0.083   8.672 -25.235  1.00 59.13           C  
ATOM   3483  CE1 TYR A 450       1.017   9.822 -27.499  1.00 59.22           C  
ATOM   3484  CE2 TYR A 450       0.599   9.869 -25.135  1.00 63.59           C  
ATOM   3485  CZ  TYR A 450       1.150  10.439 -26.273  1.00 62.40           C  
ATOM   3486  OH  TYR A 450       1.832  11.632 -26.180  1.00 71.14           O  
ATOM   3487  N   VAL A 451      -3.704   5.312 -25.699  1.00 44.88           N  
ATOM   3488  CA  VAL A 451      -4.644   4.210 -25.574  1.00 50.35           C  
ATOM   3489  C   VAL A 451      -5.845   4.435 -26.501  1.00 51.65           C  
ATOM   3490  O   VAL A 451      -6.182   3.579 -27.330  1.00 46.36           O  
ATOM   3491  CB  VAL A 451      -5.108   4.046 -24.111  1.00 48.58           C  
ATOM   3492  CG1 VAL A 451      -6.270   3.067 -24.011  1.00 48.67           C  
ATOM   3493  CG2 VAL A 451      -3.947   3.585 -23.240  1.00 45.13           C  
ATOM   3494  N   MET A 452      -6.472   5.600 -26.383  1.00 42.23           N  
ATOM   3495  CA  MET A 452      -7.653   5.899 -27.182  1.00 45.37           C  
ATOM   3496  C   MET A 452      -7.381   5.930 -28.686  1.00 49.55           C  
ATOM   3497  O   MET A 452      -8.201   5.465 -29.484  1.00 43.26           O  
ATOM   3498  CB  MET A 452      -8.281   7.215 -26.730  1.00 47.96           C  
ATOM   3499  CG  MET A 452      -8.973   7.143 -25.382  1.00 43.57           C  
ATOM   3500  SD  MET A 452      -9.530   8.787 -24.911  1.00 47.33           S  
ATOM   3501  CE  MET A 452     -10.274   8.472 -23.318  1.00 41.92           C  
ATOM   3502  N   ARG A 453      -6.231   6.464 -29.077  1.00 47.08           N  
ATOM   3503  CA  ARG A 453      -5.950   6.629 -30.499  1.00 49.43           C  
ATOM   3504  C   ARG A 453      -5.473   5.339 -31.168  1.00 45.16           C  
ATOM   3505  O   ARG A 453      -5.718   5.130 -32.347  1.00 48.66           O  
ATOM   3506  CB  ARG A 453      -4.925   7.739 -30.730  1.00 50.94           C  
ATOM   3507  CG  ARG A 453      -4.920   8.266 -32.162  1.00 52.90           C  
ATOM   3508  CD  ARG A 453      -3.669   9.069 -32.443  1.00 62.39           C  
ATOM   3509  NE  ARG A 453      -3.823   9.968 -33.580  1.00 66.20           N  
ATOM   3510  CZ  ARG A 453      -2.888  10.826 -33.975  1.00 70.88           C  
ATOM   3511  NH1 ARG A 453      -1.732  10.897 -33.324  1.00 72.91           N  
ATOM   3512  NH2 ARG A 453      -3.108  11.614 -35.015  1.00 70.07           N  
ATOM   3513  N   TYR A 454      -4.801   4.480 -30.410  1.00 52.56           N  
ATOM   3514  CA  TYR A 454      -4.168   3.301 -30.986  1.00 50.77           C  
ATOM   3515  C   TYR A 454      -4.634   1.993 -30.364  1.00 50.26           C  
ATOM   3516  O   TYR A 454      -5.045   1.076 -31.073  1.00 54.75           O  
ATOM   3517  CB  TYR A 454      -2.648   3.402 -30.864  1.00 52.83           C  
ATOM   3518  CG  TYR A 454      -2.098   4.687 -31.419  1.00 55.41           C  
ATOM   3519  CD1 TYR A 454      -2.093   4.927 -32.788  1.00 58.29           C  
ATOM   3520  CD2 TYR A 454      -1.594   5.670 -30.576  1.00 52.91           C  
ATOM   3521  CE1 TYR A 454      -1.595   6.106 -33.304  1.00 59.69           C  
ATOM   3522  CE2 TYR A 454      -1.093   6.855 -31.082  1.00 63.91           C  
ATOM   3523  CZ  TYR A 454      -1.095   7.066 -32.448  1.00 62.78           C  
ATOM   3524  OH  TYR A 454      -0.599   8.249 -32.950  1.00 73.46           O  
ATOM   3525  N   ILE A 455      -4.571   1.911 -29.041  1.00 50.63           N  
ATOM   3526  CA  ILE A 455      -4.823   0.653 -28.345  1.00 47.37           C  
ATOM   3527  C   ILE A 455      -6.289   0.218 -28.397  1.00 49.28           C  
ATOM   3528  O   ILE A 455      -6.595  -0.891 -28.831  1.00 46.82           O  
ATOM   3529  CB  ILE A 455      -4.366   0.718 -26.882  1.00 50.94           C  
ATOM   3530  CG1 ILE A 455      -2.925   1.232 -26.799  1.00 49.70           C  
ATOM   3531  CG2 ILE A 455      -4.506  -0.650 -26.226  1.00 45.15           C  
ATOM   3532  CD1 ILE A 455      -1.957   0.457 -27.654  1.00 53.81           C  
ATOM   3533  N   THR A 456      -7.184   1.089 -27.943  1.00 39.27           N  
ATOM   3534  CA  THR A 456      -8.611   0.787 -27.917  1.00 45.24           C  
ATOM   3535  C   THR A 456      -9.199   0.362 -29.276  1.00 52.14           C  
ATOM   3536  O   THR A 456      -9.932  -0.630 -29.344  1.00 43.88           O  
ATOM   3537  CB  THR A 456      -9.424   1.958 -27.346  1.00 43.28           C  
ATOM   3538  OG1 THR A 456      -8.919   2.302 -26.045  1.00 42.06           O  
ATOM   3539  CG2 THR A 456     -10.891   1.576 -27.243  1.00 35.12           C  
ATOM   3540  N   PRO A 457      -8.888   1.115 -30.357  1.00 50.12           N  
ATOM   3541  CA  PRO A 457      -9.405   0.740 -31.685  1.00 48.29           C  
ATOM   3542  C   PRO A 457      -8.824  -0.586 -32.175  1.00 53.33           C  
ATOM   3543  O   PRO A 457      -9.546  -1.389 -32.769  1.00 47.10           O  
ATOM   3544  CB  PRO A 457      -8.964   1.899 -32.595  1.00 43.85           C  
ATOM   3545  CG  PRO A 457      -7.883   2.607 -31.852  1.00 45.92           C  
ATOM   3546  CD  PRO A 457      -8.106   2.366 -30.386  1.00 44.48           C  
ATOM   3547  N   ALA A 458      -7.538  -0.812 -31.925  1.00 50.66           N  
ATOM   3548  CA  ALA A 458      -6.922  -2.094 -32.240  1.00 48.95           C  
ATOM   3549  C   ALA A 458      -7.678  -3.222 -31.533  1.00 59.04           C  
ATOM   3550  O   ALA A 458      -8.165  -4.153 -32.180  1.00 58.62           O  
ATOM   3551  CB  ALA A 458      -5.458  -2.093 -31.841  1.00 54.42           C  
ATOM   3552  N   PHE A 459      -7.786  -3.126 -30.209  1.00 52.35           N  
ATOM   3553  CA  PHE A 459      -8.564  -4.084 -29.433  1.00 49.34           C  
ATOM   3554  C   PHE A 459      -9.904  -4.373 -30.089  1.00 57.44           C  
ATOM   3555  O   PHE A 459     -10.205  -5.520 -30.414  1.00 65.36           O  
ATOM   3556  CB  PHE A 459      -8.801  -3.577 -28.005  1.00 62.82           C  
ATOM   3557  CG  PHE A 459      -7.991  -4.292 -26.956  1.00 56.66           C  
ATOM   3558  CD1 PHE A 459      -6.841  -3.717 -26.433  1.00 78.10           C  
ATOM   3559  CD2 PHE A 459      -8.393  -5.529 -26.477  1.00 62.06           C  
ATOM   3560  CE1 PHE A 459      -6.102  -4.369 -25.459  1.00 62.51           C  
ATOM   3561  CE2 PHE A 459      -7.658  -6.190 -25.509  1.00 52.98           C  
ATOM   3562  CZ  PHE A 459      -6.511  -5.610 -24.999  1.00 69.74           C  
ATOM   3563  N   LEU A 460     -10.709  -3.333 -30.277  1.00 44.74           N  
ATOM   3564  CA  LEU A 460     -12.034  -3.506 -30.856  1.00 52.28           C  
ATOM   3565  C   LEU A 460     -11.973  -4.103 -32.262  1.00 67.63           C  
ATOM   3566  O   LEU A 460     -12.837  -4.895 -32.637  1.00 66.27           O  
ATOM   3567  CB  LEU A 460     -12.811  -2.189 -30.882  1.00 44.25           C  
ATOM   3568  CG  LEU A 460     -13.450  -1.749 -29.568  1.00 51.76           C  
ATOM   3569  CD1 LEU A 460     -14.551  -0.733 -29.826  1.00 50.88           C  
ATOM   3570  CD2 LEU A 460     -13.998  -2.958 -28.811  1.00 57.07           C  
ATOM   3571  N   ALA A 461     -10.961  -3.723 -33.038  1.00 61.29           N  
ATOM   3572  CA  ALA A 461     -10.805  -4.262 -34.387  1.00 59.64           C  
ATOM   3573  C   ALA A 461     -10.598  -5.780 -34.340  1.00 64.04           C  
ATOM   3574  O   ALA A 461     -11.049  -6.506 -35.219  1.00 60.52           O  
ATOM   3575  CB  ALA A 461      -9.660  -3.575 -35.119  1.00 45.92           C  
ATOM   3576  N   VAL A 462      -9.912  -6.254 -33.308  1.00 57.41           N  
ATOM   3577  CA  VAL A 462      -9.711  -7.685 -33.124  1.00 64.25           C  
ATOM   3578  C   VAL A 462     -10.987  -8.386 -32.653  1.00 63.50           C  
ATOM   3579  O   VAL A 462     -11.356  -9.443 -33.160  1.00 58.40           O  
ATOM   3580  CB  VAL A 462      -8.587  -7.942 -32.121  1.00 53.40           C  
ATOM   3581  CG1 VAL A 462      -8.780  -9.288 -31.430  1.00 66.57           C  
ATOM   3582  CG2 VAL A 462      -7.235  -7.852 -32.813  1.00 61.88           C  
ATOM   3583  N   LEU A 463     -11.657  -7.796 -31.672  1.00 68.15           N  
ATOM   3584  CA  LEU A 463     -12.910  -8.356 -31.182  1.00 72.34           C  
ATOM   3585  C   LEU A 463     -13.869  -8.492 -32.353  1.00 64.51           C  
ATOM   3586  O   LEU A 463     -14.506  -9.528 -32.525  1.00 66.63           O  
ATOM   3587  CB  LEU A 463     -13.516  -7.481 -30.073  1.00 58.78           C  
ATOM   3588  CG  LEU A 463     -14.852  -7.955 -29.489  1.00 54.42           C  
ATOM   3589  CD1 LEU A 463     -14.704  -9.344 -28.913  1.00 53.49           C  
ATOM   3590  CD2 LEU A 463     -15.386  -6.992 -28.434  1.00 49.02           C  
ATOM   3591  N   LEU A 464     -13.949  -7.455 -33.179  1.00 62.61           N  
ATOM   3592  CA  LEU A 464     -14.843  -7.504 -34.322  1.00 65.01           C  
ATOM   3593  C   LEU A 464     -14.366  -8.603 -35.277  1.00 76.68           C  
ATOM   3594  O   LEU A 464     -15.159  -9.438 -35.699  1.00 65.58           O  
ATOM   3595  CB  LEU A 464     -14.914  -6.152 -35.036  1.00 60.84           C  
ATOM   3596  CG  LEU A 464     -16.285  -5.707 -35.571  1.00 62.99           C  
ATOM   3597  CD1 LEU A 464     -16.137  -4.661 -36.671  1.00 56.52           C  
ATOM   3598  CD2 LEU A 464     -17.115  -6.874 -36.080  1.00 58.87           C  
ATOM   3599  N   VAL A 465     -13.070  -8.627 -35.585  1.00 64.21           N  
ATOM   3600  CA  VAL A 465     -12.560  -9.475 -36.661  1.00 67.00           C  
ATOM   3601  C   VAL A 465     -12.360 -10.941 -36.278  1.00 75.16           C  
ATOM   3602  O   VAL A 465     -13.146 -11.804 -36.684  1.00 66.32           O  
ATOM   3603  CB  VAL A 465     -11.249  -8.913 -37.259  1.00 69.21           C  
ATOM   3604  CG1 VAL A 465     -10.619  -9.942 -38.189  1.00 64.46           C  
ATOM   3605  CG2 VAL A 465     -11.525  -7.620 -38.003  1.00 56.10           C  
ATOM   3606  N   VAL A 466     -11.286 -11.220 -35.543  1.00 67.07           N  
ATOM   3607  CA  VAL A 466     -10.964 -12.581 -35.125  1.00 73.19           C  
ATOM   3608  C   VAL A 466     -12.233 -13.316 -34.721  1.00 71.24           C  
ATOM   3609  O   VAL A 466     -12.450 -14.472 -35.090  1.00 62.18           O  
ATOM   3610  CB  VAL A 466      -9.962 -12.596 -33.954  1.00 71.73           C  
ATOM   3611  CG1 VAL A 466      -9.968 -13.951 -33.259  1.00 67.21           C  
ATOM   3612  CG2 VAL A 466      -8.558 -12.240 -34.439  1.00 73.38           C  
ATOM   3613  N   TRP A 467     -13.085 -12.617 -33.985  1.00 62.44           N  
ATOM   3614  CA  TRP A 467     -14.342 -13.186 -33.533  1.00 60.57           C  
ATOM   3615  C   TRP A 467     -15.397 -13.318 -34.650  1.00 68.36           C  
ATOM   3616  O   TRP A 467     -15.974 -14.387 -34.820  1.00 57.31           O  
ATOM   3617  CB  TRP A 467     -14.872 -12.400 -32.331  1.00 64.48           C  
ATOM   3618  CG  TRP A 467     -16.271 -12.740 -31.962  1.00 61.00           C  
ATOM   3619  CD1 TRP A 467     -16.683 -13.630 -31.010  1.00 59.50           C  
ATOM   3620  CD2 TRP A 467     -17.454 -12.194 -32.543  1.00 51.11           C  
ATOM   3621  NE1 TRP A 467     -18.057 -13.673 -30.970  1.00 64.73           N  
ATOM   3622  CE2 TRP A 467     -18.554 -12.796 -31.899  1.00 67.69           C  
ATOM   3623  CE3 TRP A 467     -17.690 -11.257 -33.547  1.00 64.98           C  
ATOM   3624  CZ2 TRP A 467     -19.873 -12.486 -32.230  1.00 65.89           C  
ATOM   3625  CZ3 TRP A 467     -18.990 -10.953 -33.876  1.00 73.44           C  
ATOM   3626  CH2 TRP A 467     -20.069 -11.562 -33.219  1.00 68.99           C  
ATOM   3627  N   ALA A 468     -15.647 -12.246 -35.406  1.00 69.66           N  
ATOM   3628  CA  ALA A 468     -16.660 -12.270 -36.476  1.00 65.70           C  
ATOM   3629  C   ALA A 468     -16.448 -13.385 -37.501  1.00 65.53           C  
ATOM   3630  O   ALA A 468     -17.414 -13.945 -38.029  1.00 56.92           O  
ATOM   3631  CB  ALA A 468     -16.751 -10.931 -37.182  1.00 65.27           C  
ATOM   3632  N   ARG A 469     -15.189 -13.687 -37.804  1.00 56.45           N  
ATOM   3633  CA  ARG A 469     -14.877 -14.835 -38.641  1.00 53.81           C  
ATOM   3634  C   ARG A 469     -15.465 -16.100 -38.020  1.00 74.94           C  
ATOM   3635  O   ARG A 469     -15.928 -16.996 -38.727  1.00 75.62           O  
ATOM   3636  CB  ARG A 469     -13.364 -15.005 -38.790  1.00 57.91           C  
ATOM   3637  CG  ARG A 469     -12.594 -13.747 -39.173  1.00 71.03           C  
ATOM   3638  CD  ARG A 469     -11.302 -14.120 -39.895  1.00 80.59           C  
ATOM   3639  NE  ARG A 469     -10.288 -13.065 -39.866  1.00 84.58           N  
ATOM   3640  CZ  ARG A 469      -9.150 -13.105 -40.557  1.00 84.09           C  
ATOM   3641  NH1 ARG A 469      -8.882 -14.142 -41.341  1.00 77.75           N  
ATOM   3642  NH2 ARG A 469      -8.281 -12.106 -40.469  1.00 73.33           N  
ATOM   3643  N   GLU A 470     -15.448 -16.162 -36.691  1.00 67.99           N  
ATOM   3644  CA  GLU A 470     -15.841 -17.364 -35.965  1.00 61.09           C  
ATOM   3645  C   GLU A 470     -17.315 -17.392 -35.568  1.00 63.97           C  
ATOM   3646  O   GLU A 470     -17.736 -18.299 -34.855  1.00 77.16           O  
ATOM   3647  CB  GLU A 470     -14.985 -17.518 -34.706  1.00 71.01           C  
ATOM   3648  N   TYR A 471     -18.101 -16.420 -36.021  1.00 58.95           N  
ATOM   3649  CA  TYR A 471     -19.518 -16.363 -35.651  1.00 57.14           C  
ATOM   3650  C   TYR A 471     -20.471 -16.247 -36.843  1.00 64.20           C  
ATOM   3651  O   TYR A 471     -21.385 -17.062 -36.991  1.00 61.79           O  
ATOM   3652  CB  TYR A 471     -19.774 -15.229 -34.648  1.00 59.30           C  
ATOM   3653  N   ILE A 472     -20.254 -15.244 -37.691  1.00 56.83           N  
ATOM   3654  CA  ILE A 472     -21.168 -14.971 -38.810  1.00 57.10           C  
ATOM   3655  C   ILE A 472     -21.450 -16.167 -39.749  1.00 53.63           C  
ATOM   3656  O   ILE A 472     -22.599 -16.373 -40.156  1.00 53.94           O  
ATOM   3657  CB  ILE A 472     -20.723 -13.726 -39.634  1.00 53.57           C  
ATOM   3658  CG1 ILE A 472     -20.683 -12.480 -38.746  1.00 66.62           C  
ATOM   3659  CG2 ILE A 472     -21.654 -13.490 -40.822  1.00 47.81           C  
ATOM   3660  CD1 ILE A 472     -20.410 -11.177 -39.503  1.00 58.84           C  
ATOM   3661  N   PRO A 473     -20.410 -16.950 -40.109  1.00 63.48           N  
ATOM   3662  CA  PRO A 473     -20.642 -18.086 -41.021  1.00 60.13           C  
ATOM   3663  C   PRO A 473     -21.659 -19.076 -40.458  1.00 56.56           C  
ATOM   3664  O   PRO A 473     -22.507 -19.584 -41.192  1.00 56.32           O  
ATOM   3665  CB  PRO A 473     -19.270 -18.761 -41.110  1.00 65.50           C  
ATOM   3666  CG  PRO A 473     -18.286 -17.697 -40.734  1.00 65.72           C  
ATOM   3667  CD  PRO A 473     -18.990 -16.825 -39.730  1.00 59.03           C  
ATOM   3668  N   LYS A 474     -21.557 -19.349 -39.161  1.00 59.32           N  
ATOM   3669  CA  LYS A 474     -22.503 -20.221 -38.475  1.00 71.23           C  
ATOM   3670  C   LYS A 474     -23.925 -19.645 -38.534  1.00 72.45           C  
ATOM   3671  O   LYS A 474     -24.875 -20.346 -38.896  1.00 57.11           O  
ATOM   3672  CB  LYS A 474     -22.071 -20.423 -37.020  1.00 70.09           C  
ATOM   3673  CG  LYS A 474     -20.555 -20.534 -36.817  1.00 76.73           C  
ATOM   3674  CD  LYS A 474     -20.063 -21.981 -36.879  1.00 81.58           C  
ATOM   3675  CE  LYS A 474     -18.616 -22.099 -36.398  1.00 76.57           C  
ATOM   3676  NZ  LYS A 474     -17.652 -21.356 -37.264  1.00 80.33           N  
ATOM   3677  N   ILE A 475     -24.067 -18.368 -38.178  1.00 56.28           N  
ATOM   3678  CA  ILE A 475     -25.374 -17.713 -38.181  1.00 46.09           C  
ATOM   3679  C   ILE A 475     -25.967 -17.629 -39.598  1.00 62.16           C  
ATOM   3680  O   ILE A 475     -27.181 -17.739 -39.781  1.00 56.31           O  
ATOM   3681  CB  ILE A 475     -25.309 -16.292 -37.564  1.00 49.90           C  
ATOM   3682  CG1 ILE A 475     -24.697 -16.329 -36.160  1.00 67.65           C  
ATOM   3683  CG2 ILE A 475     -26.698 -15.658 -37.527  1.00 50.60           C  
ATOM   3684  CD1 ILE A 475     -25.715 -16.431 -35.032  1.00 58.44           C  
ATOM   3685  N   MET A 476     -25.111 -17.430 -40.596  1.00 56.35           N  
ATOM   3686  CA  MET A 476     -25.564 -17.322 -41.978  1.00 54.80           C  
ATOM   3687  C   MET A 476     -25.887 -18.678 -42.606  1.00 76.83           C  
ATOM   3688  O   MET A 476     -26.711 -18.769 -43.525  1.00 71.54           O  
ATOM   3689  CB  MET A 476     -24.508 -16.609 -42.829  1.00 54.91           C  
ATOM   3690  CG  MET A 476     -24.370 -15.127 -42.539  1.00 58.29           C  
ATOM   3691  SD  MET A 476     -25.936 -14.267 -42.745  1.00 65.08           S  
ATOM   3692  CE  MET A 476     -26.234 -14.519 -44.502  1.00 45.44           C  
ATOM   3693  N   GLU A 477     -25.239 -19.730 -42.110  1.00 67.73           N  
ATOM   3694  CA  GLU A 477     -25.298 -21.037 -42.763  1.00 78.27           C  
ATOM   3695  C   GLU A 477     -26.093 -22.078 -41.982  1.00 78.94           C  
ATOM   3696  O   GLU A 477     -26.808 -22.897 -42.570  1.00 73.15           O  
ATOM   3697  CB  GLU A 477     -23.880 -21.563 -43.009  1.00 74.02           C  
ATOM   3698  CG  GLU A 477     -23.100 -20.799 -44.063  1.00 74.75           C  
ATOM   3699  CD  GLU A 477     -23.605 -21.069 -45.466  1.00 92.90           C  
ATOM   3700  OE1 GLU A 477     -22.868 -21.714 -46.245  1.00 91.39           O  
ATOM   3701  OE2 GLU A 477     -24.740 -20.646 -45.787  1.00 89.77           O  
ATOM   3702  N   GLU A 478     -25.970 -22.043 -40.659  1.00 65.14           N  
ATOM   3703  CA  GLU A 478     -26.517 -23.104 -39.818  1.00 72.78           C  
ATOM   3704  C   GLU A 478     -27.860 -22.765 -39.160  1.00 69.35           C  
ATOM   3705  O   GLU A 478     -28.312 -23.487 -38.273  1.00 74.64           O  
ATOM   3706  CB  GLU A 478     -25.493 -23.514 -38.746  1.00 65.23           C  
ATOM   3707  CG  GLU A 478     -24.103 -23.862 -39.287  1.00 58.17           C  
ATOM   3708  CD  GLU A 478     -24.086 -25.139 -40.122  1.00 77.61           C  
ATOM   3709  OE1 GLU A 478     -24.937 -26.028 -39.888  1.00 77.71           O  
ATOM   3710  OE2 GLU A 478     -23.215 -25.256 -41.013  1.00 63.03           O  
ATOM   3711  N   THR A 479     -28.501 -21.683 -39.594  1.00 65.76           N  
ATOM   3712  CA  THR A 479     -29.758 -21.255 -38.976  1.00 46.52           C  
ATOM   3713  C   THR A 479     -31.013 -21.669 -39.753  1.00 54.07           C  
ATOM   3714  O   THR A 479     -30.964 -21.913 -40.964  1.00 49.60           O  
ATOM   3715  CB  THR A 479     -29.788 -19.730 -38.777  1.00 52.26           C  
ATOM   3716  OG1 THR A 479     -29.416 -19.084 -40.002  1.00 51.90           O  
ATOM   3717  CG2 THR A 479     -28.829 -19.313 -37.653  1.00 58.13           C  
ATOM   3718  N   HIS A 480     -32.133 -21.749 -39.039  1.00 41.29           N  
ATOM   3719  CA  HIS A 480     -33.440 -21.991 -39.643  1.00 39.78           C  
ATOM   3720  C   HIS A 480     -33.830 -20.837 -40.588  1.00 34.50           C  
ATOM   3721  O   HIS A 480     -33.440 -19.691 -40.373  1.00 34.47           O  
ATOM   3722  CB  HIS A 480     -34.481 -22.165 -38.538  1.00 36.93           C  
ATOM   3723  CG  HIS A 480     -35.778 -22.737 -39.012  1.00 41.94           C  
ATOM   3724  ND1 HIS A 480     -36.914 -21.971 -39.167  1.00 38.47           N  
ATOM   3725  CD2 HIS A 480     -36.125 -23.999 -39.365  1.00 45.72           C  
ATOM   3726  CE1 HIS A 480     -37.903 -22.736 -39.599  1.00 45.00           C  
ATOM   3727  NE2 HIS A 480     -37.450 -23.972 -39.726  1.00 39.74           N  
ATOM   3728  N   TRP A 481     -34.580 -21.144 -41.643  1.00 39.91           N  
ATOM   3729  CA  TRP A 481     -34.931 -20.132 -42.652  1.00 36.20           C  
ATOM   3730  C   TRP A 481     -35.652 -18.939 -42.020  1.00 36.07           C  
ATOM   3731  O   TRP A 481     -35.568 -17.810 -42.520  1.00 31.46           O  
ATOM   3732  CB  TRP A 481     -35.775 -20.724 -43.787  1.00 33.89           C  
ATOM   3733  CG  TRP A 481     -37.174 -21.131 -43.404  1.00 29.07           C  
ATOM   3734  CD1 TRP A 481     -37.607 -22.389 -43.120  1.00 30.13           C  
ATOM   3735  CD2 TRP A 481     -38.335 -20.280 -43.316  1.00 31.19           C  
ATOM   3736  NE1 TRP A 481     -38.956 -22.377 -42.848  1.00 30.97           N  
ATOM   3737  CE2 TRP A 481     -39.426 -21.097 -42.959  1.00 30.65           C  
ATOM   3738  CE3 TRP A 481     -38.552 -18.915 -43.500  1.00 32.88           C  
ATOM   3739  CZ2 TRP A 481     -40.708 -20.594 -42.776  1.00 27.37           C  
ATOM   3740  CZ3 TRP A 481     -39.832 -18.417 -43.321  1.00 34.82           C  
ATOM   3741  CH2 TRP A 481     -40.889 -19.254 -42.951  1.00 30.82           C  
ATOM   3742  N   THR A 482     -36.353 -19.197 -40.915  1.00 31.73           N  
ATOM   3743  CA  THR A 482     -37.162 -18.165 -40.275  1.00 26.89           C  
ATOM   3744  C   THR A 482     -36.326 -16.985 -39.796  1.00 28.71           C  
ATOM   3745  O   THR A 482     -36.875 -15.927 -39.494  1.00 27.88           O  
ATOM   3746  CB  THR A 482     -38.003 -18.728 -39.117  1.00 35.01           C  
ATOM   3747  OG1 THR A 482     -37.153 -19.464 -38.227  1.00 31.01           O  
ATOM   3748  CG2 THR A 482     -39.103 -19.641 -39.645  1.00 30.83           C  
ATOM   3749  N   VAL A 483     -35.005 -17.152 -39.736  1.00 21.39           N  
ATOM   3750  CA  VAL A 483     -34.147 -16.034 -39.375  1.00 25.10           C  
ATOM   3751  C   VAL A 483     -34.335 -14.879 -40.343  1.00 25.85           C  
ATOM   3752  O   VAL A 483     -34.221 -13.718 -39.949  1.00 28.87           O  
ATOM   3753  CB  VAL A 483     -32.648 -16.402 -39.312  1.00 29.60           C  
ATOM   3754  CG1 VAL A 483     -32.401 -17.467 -38.251  1.00 33.24           C  
ATOM   3755  CG2 VAL A 483     -32.134 -16.822 -40.685  1.00 29.69           C  
ATOM   3756  N   TRP A 484     -34.623 -15.203 -41.604  1.00 28.32           N  
ATOM   3757  CA  TRP A 484     -34.829 -14.185 -42.624  1.00 29.58           C  
ATOM   3758  C   TRP A 484     -36.010 -13.259 -42.335  1.00 27.46           C  
ATOM   3759  O   TRP A 484     -36.021 -12.108 -42.764  1.00 25.46           O  
ATOM   3760  CB  TRP A 484     -34.913 -14.815 -44.029  1.00 28.11           C  
ATOM   3761  CG  TRP A 484     -33.554 -15.162 -44.487  1.00 27.78           C  
ATOM   3762  CD1 TRP A 484     -32.990 -16.405 -44.537  1.00 31.53           C  
ATOM   3763  CD2 TRP A 484     -32.537 -14.238 -44.880  1.00 27.27           C  
ATOM   3764  NE1 TRP A 484     -31.686 -16.312 -44.977  1.00 34.61           N  
ATOM   3765  CE2 TRP A 484     -31.385 -14.991 -45.195  1.00 38.94           C  
ATOM   3766  CE3 TRP A 484     -32.497 -12.848 -45.023  1.00 30.58           C  
ATOM   3767  CZ2 TRP A 484     -30.201 -14.399 -45.643  1.00 36.86           C  
ATOM   3768  CZ3 TRP A 484     -31.323 -12.256 -45.472  1.00 40.20           C  
ATOM   3769  CH2 TRP A 484     -30.193 -13.034 -45.783  1.00 35.77           C  
ATOM   3770  N   ILE A 485     -36.995 -13.778 -41.611  1.00 26.59           N  
ATOM   3771  CA  ILE A 485     -38.133 -12.981 -41.200  1.00 25.21           C  
ATOM   3772  C   ILE A 485     -37.635 -11.850 -40.312  1.00 27.87           C  
ATOM   3773  O   ILE A 485     -37.992 -10.699 -40.514  1.00 23.42           O  
ATOM   3774  CB  ILE A 485     -39.134 -13.825 -40.411  1.00 32.31           C  
ATOM   3775  CG1 ILE A 485     -39.685 -14.961 -41.291  1.00 30.72           C  
ATOM   3776  CG2 ILE A 485     -40.255 -12.949 -39.815  1.00 23.67           C  
ATOM   3777  CD1 ILE A 485     -40.453 -16.009 -40.462  1.00 28.02           C  
ATOM   3778  N   THR A 486     -36.803 -12.187 -39.333  1.00 23.82           N  
ATOM   3779  CA  THR A 486     -36.311 -11.185 -38.405  1.00 30.91           C  
ATOM   3780  C   THR A 486     -35.370 -10.236 -39.109  1.00 25.90           C  
ATOM   3781  O   THR A 486     -35.520  -9.014 -38.983  1.00 24.35           O  
ATOM   3782  CB  THR A 486     -35.632 -11.820 -37.188  1.00 33.01           C  
ATOM   3783  OG1 THR A 486     -36.607 -12.609 -36.504  1.00 28.50           O  
ATOM   3784  CG2 THR A 486     -35.119 -10.734 -36.265  1.00 23.98           C  
ATOM   3785  N   ARG A 487     -34.443 -10.797 -39.891  1.00 24.60           N  
ATOM   3786  CA  ARG A 487     -33.549  -9.979 -40.719  1.00 26.39           C  
ATOM   3787  C   ARG A 487     -34.305  -8.999 -41.602  1.00 26.40           C  
ATOM   3788  O   ARG A 487     -33.965  -7.822 -41.672  1.00 24.26           O  
ATOM   3789  CB  ARG A 487     -32.615 -10.842 -41.562  1.00 25.60           C  
ATOM   3790  CG  ARG A 487     -31.718 -11.734 -40.706  1.00 29.58           C  
ATOM   3791  CD  ARG A 487     -30.947 -12.717 -41.561  1.00 32.31           C  
ATOM   3792  NE  ARG A 487     -30.204 -13.638 -40.707  1.00 28.19           N  
ATOM   3793  CZ  ARG A 487     -29.412 -14.608 -41.146  1.00 42.03           C  
ATOM   3794  NH1 ARG A 487     -29.247 -14.807 -42.448  1.00 30.86           N  
ATOM   3795  NH2 ARG A 487     -28.799 -15.387 -40.271  1.00 34.35           N  
ATOM   3796  N   PHE A 488     -35.320  -9.501 -42.290  1.00 29.05           N  
ATOM   3797  CA  PHE A 488     -36.161  -8.676 -43.155  1.00 26.09           C  
ATOM   3798  C   PHE A 488     -36.692  -7.529 -42.314  1.00 27.78           C  
ATOM   3799  O   PHE A 488     -36.511  -6.363 -42.644  1.00 24.84           O  
ATOM   3800  CB  PHE A 488     -37.341  -9.500 -43.679  1.00 26.56           C  
ATOM   3801  CG  PHE A 488     -38.351  -8.695 -44.482  1.00 28.94           C  
ATOM   3802  CD1 PHE A 488     -38.037  -8.232 -45.747  1.00 24.38           C  
ATOM   3803  CD2 PHE A 488     -39.612  -8.419 -43.969  1.00 29.50           C  
ATOM   3804  CE1 PHE A 488     -38.959  -7.492 -46.489  1.00 32.77           C  
ATOM   3805  CE2 PHE A 488     -40.536  -7.687 -44.695  1.00 28.95           C  
ATOM   3806  CZ  PHE A 488     -40.211  -7.224 -45.959  1.00 30.44           C  
ATOM   3807  N   TYR A 489     -37.354  -7.880 -41.217  1.00 21.75           N  
ATOM   3808  CA  TYR A 489     -37.988  -6.869 -40.390  1.00 27.37           C  
ATOM   3809  C   TYR A 489     -37.016  -5.821 -39.867  1.00 22.90           C  
ATOM   3810  O   TYR A 489     -37.293  -4.624 -39.954  1.00 27.60           O  
ATOM   3811  CB  TYR A 489     -38.764  -7.468 -39.233  1.00 28.72           C  
ATOM   3812  CG  TYR A 489     -39.590  -6.416 -38.544  1.00 31.27           C  
ATOM   3813  CD1 TYR A 489     -40.692  -5.854 -39.180  1.00 32.06           C  
ATOM   3814  CD2 TYR A 489     -39.250  -5.952 -37.276  1.00 27.61           C  
ATOM   3815  CE1 TYR A 489     -41.461  -4.875 -38.558  1.00 39.89           C  
ATOM   3816  CE2 TYR A 489     -40.003  -4.978 -36.645  1.00 29.47           C  
ATOM   3817  CZ  TYR A 489     -41.109  -4.439 -37.286  1.00 34.85           C  
ATOM   3818  OH  TYR A 489     -41.850  -3.470 -36.652  1.00 31.94           O  
ATOM   3819  N   ILE A 490     -35.875  -6.243 -39.339  1.00 24.76           N  
ATOM   3820  CA  ILE A 490     -34.970  -5.252 -38.758  1.00 24.56           C  
ATOM   3821  C   ILE A 490     -34.258  -4.442 -39.838  1.00 22.22           C  
ATOM   3822  O   ILE A 490     -33.906  -3.285 -39.631  1.00 27.32           O  
ATOM   3823  CB  ILE A 490     -33.985  -5.850 -37.708  1.00 26.61           C  
ATOM   3824  CG1 ILE A 490     -32.987  -6.807 -38.348  1.00 28.80           C  
ATOM   3825  CG2 ILE A 490     -34.751  -6.546 -36.571  1.00 24.26           C  
ATOM   3826  CD1 ILE A 490     -32.054  -7.476 -37.284  1.00 24.95           C  
ATOM   3827  N   ILE A 491     -34.060  -5.030 -41.013  1.00 27.19           N  
ATOM   3828  CA  ILE A 491     -33.591  -4.233 -42.146  1.00 24.13           C  
ATOM   3829  C   ILE A 491     -34.659  -3.202 -42.506  1.00 24.31           C  
ATOM   3830  O   ILE A 491     -34.347  -2.050 -42.790  1.00 24.02           O  
ATOM   3831  CB  ILE A 491     -33.201  -5.098 -43.331  1.00 22.76           C  
ATOM   3832  CG1 ILE A 491     -31.912  -5.851 -42.986  1.00 29.53           C  
ATOM   3833  CG2 ILE A 491     -33.052  -4.232 -44.613  1.00 26.28           C  
ATOM   3834  CD1 ILE A 491     -31.583  -6.974 -43.943  1.00 33.07           C  
ATOM   3835  N   GLY A 492     -35.919  -3.613 -42.456  1.00 22.06           N  
ATOM   3836  CA  GLY A 492     -37.018  -2.679 -42.593  1.00 20.28           C  
ATOM   3837  C   GLY A 492     -36.938  -1.526 -41.599  1.00 33.72           C  
ATOM   3838  O   GLY A 492     -37.111  -0.349 -41.975  1.00 23.09           O  
ATOM   3839  N   LEU A 493     -36.685  -1.861 -40.324  1.00 20.44           N  
ATOM   3840  CA  LEU A 493     -36.537  -0.842 -39.304  1.00 24.44           C  
ATOM   3841  C   LEU A 493     -35.389   0.084 -39.670  1.00 24.03           C  
ATOM   3842  O   LEU A 493     -35.455   1.280 -39.425  1.00 24.29           O  
ATOM   3843  CB  LEU A 493     -36.265  -1.463 -37.923  1.00 23.01           C  
ATOM   3844  CG  LEU A 493     -37.413  -2.208 -37.241  1.00 27.04           C  
ATOM   3845  CD1 LEU A 493     -36.983  -2.756 -35.839  1.00 27.79           C  
ATOM   3846  CD2 LEU A 493     -38.596  -1.258 -37.110  1.00 25.85           C  
ATOM   3847  N   PHE A 494     -34.316  -0.466 -40.226  1.00 23.89           N  
ATOM   3848  CA  PHE A 494     -33.217   0.395 -40.603  1.00 23.82           C  
ATOM   3849  C   PHE A 494     -33.653   1.360 -41.703  1.00 31.49           C  
ATOM   3850  O   PHE A 494     -33.286   2.532 -41.688  1.00 30.08           O  
ATOM   3851  CB  PHE A 494     -32.013  -0.404 -41.065  1.00 27.58           C  
ATOM   3852  CG  PHE A 494     -30.805   0.440 -41.327  1.00 33.91           C  
ATOM   3853  CD1 PHE A 494     -29.852   0.629 -40.334  1.00 25.64           C  
ATOM   3854  CD2 PHE A 494     -30.629   1.065 -42.556  1.00 35.57           C  
ATOM   3855  CE1 PHE A 494     -28.734   1.415 -40.567  1.00 29.88           C  
ATOM   3856  CE2 PHE A 494     -29.513   1.856 -42.795  1.00 34.26           C  
ATOM   3857  CZ  PHE A 494     -28.567   2.031 -41.800  1.00 33.33           C  
ATOM   3858  N   LEU A 495     -34.451   0.869 -42.644  1.00 24.78           N  
ATOM   3859  CA  LEU A 495     -34.917   1.687 -43.770  1.00 26.17           C  
ATOM   3860  C   LEU A 495     -35.861   2.770 -43.252  1.00 26.86           C  
ATOM   3861  O   LEU A 495     -35.826   3.912 -43.704  1.00 25.51           O  
ATOM   3862  CB  LEU A 495     -35.613   0.810 -44.826  1.00 22.65           C  
ATOM   3863  CG  LEU A 495     -36.280   1.524 -46.012  1.00 35.47           C  
ATOM   3864  CD1 LEU A 495     -35.254   2.264 -46.856  1.00 28.20           C  
ATOM   3865  CD2 LEU A 495     -37.088   0.521 -46.874  1.00 37.23           C  
ATOM   3866  N   PHE A 496     -36.680   2.390 -42.272  1.00 28.16           N  
ATOM   3867  CA  PHE A 496     -37.633   3.281 -41.642  1.00 27.23           C  
ATOM   3868  C   PHE A 496     -36.895   4.452 -40.983  1.00 30.99           C  
ATOM   3869  O   PHE A 496     -37.265   5.604 -41.164  1.00 28.35           O  
ATOM   3870  CB  PHE A 496     -38.460   2.492 -40.626  1.00 29.32           C  
ATOM   3871  CG  PHE A 496     -39.286   3.343 -39.698  1.00 29.00           C  
ATOM   3872  CD1 PHE A 496     -40.337   4.103 -40.174  1.00 32.21           C  
ATOM   3873  CD2 PHE A 496     -39.019   3.356 -38.342  1.00 33.96           C  
ATOM   3874  CE1 PHE A 496     -41.106   4.866 -39.320  1.00 35.12           C  
ATOM   3875  CE2 PHE A 496     -39.781   4.138 -37.460  1.00 38.24           C  
ATOM   3876  CZ  PHE A 496     -40.833   4.887 -37.956  1.00 31.75           C  
ATOM   3877  N   LEU A 497     -35.841   4.149 -40.232  1.00 26.65           N  
ATOM   3878  CA  LEU A 497     -35.038   5.194 -39.604  1.00 31.69           C  
ATOM   3879  C   LEU A 497     -34.335   6.075 -40.634  1.00 27.97           C  
ATOM   3880  O   LEU A 497     -34.252   7.289 -40.461  1.00 30.62           O  
ATOM   3881  CB  LEU A 497     -34.007   4.589 -38.652  1.00 24.49           C  
ATOM   3882  CG  LEU A 497     -34.593   3.943 -37.394  1.00 28.41           C  
ATOM   3883  CD1 LEU A 497     -33.485   3.321 -36.553  1.00 26.24           C  
ATOM   3884  CD2 LEU A 497     -35.392   4.966 -36.580  1.00 27.12           C  
ATOM   3885  N   THR A 498     -33.798   5.467 -41.683  1.00 26.52           N  
ATOM   3886  CA  THR A 498     -33.210   6.254 -42.763  1.00 29.83           C  
ATOM   3887  C   THR A 498     -34.260   7.237 -43.291  1.00 36.71           C  
ATOM   3888  O   THR A 498     -33.966   8.410 -43.536  1.00 33.43           O  
ATOM   3889  CB  THR A 498     -32.678   5.363 -43.924  1.00 37.15           C  
ATOM   3890  OG1 THR A 498     -31.652   4.483 -43.439  1.00 34.34           O  
ATOM   3891  CG2 THR A 498     -32.099   6.218 -45.022  1.00 37.33           C  
ATOM   3892  N   PHE A 499     -35.489   6.760 -43.463  1.00 28.04           N  
ATOM   3893  CA  PHE A 499     -36.556   7.626 -43.948  1.00 25.88           C  
ATOM   3894  C   PHE A 499     -36.850   8.778 -42.977  1.00 26.82           C  
ATOM   3895  O   PHE A 499     -36.960   9.930 -43.385  1.00 27.75           O  
ATOM   3896  CB  PHE A 499     -37.827   6.814 -44.272  1.00 26.12           C  
ATOM   3897  CG  PHE A 499     -38.914   7.623 -44.918  1.00 23.37           C  
ATOM   3898  CD1 PHE A 499     -38.681   8.311 -46.100  1.00 23.28           C  
ATOM   3899  CD2 PHE A 499     -40.170   7.706 -44.337  1.00 30.30           C  
ATOM   3900  CE1 PHE A 499     -39.683   9.061 -46.692  1.00 27.52           C  
ATOM   3901  CE2 PHE A 499     -41.178   8.459 -44.920  1.00 32.75           C  
ATOM   3902  CZ  PHE A 499     -40.931   9.140 -46.099  1.00 28.57           C  
ATOM   3903  N   LEU A 500     -36.967   8.483 -41.689  1.00 29.47           N  
ATOM   3904  CA  LEU A 500     -37.138   9.546 -40.701  1.00 29.20           C  
ATOM   3905  C   LEU A 500     -35.996  10.579 -40.712  1.00 28.22           C  
ATOM   3906  O   LEU A 500     -36.233  11.788 -40.560  1.00 26.84           O  
ATOM   3907  CB  LEU A 500     -37.290   8.958 -39.297  1.00 23.04           C  
ATOM   3908  CG  LEU A 500     -38.518   8.070 -39.079  1.00 25.04           C  
ATOM   3909  CD1 LEU A 500     -38.740   7.871 -37.571  1.00 26.82           C  
ATOM   3910  CD2 LEU A 500     -39.771   8.649 -39.722  1.00 25.54           C  
ATOM   3911  N   VAL A 501     -34.764  10.111 -40.872  1.00 22.19           N  
ATOM   3912  CA  VAL A 501     -33.635  11.032 -40.934  1.00 27.17           C  
ATOM   3913  C   VAL A 501     -33.784  11.891 -42.189  1.00 38.32           C  
ATOM   3914  O   VAL A 501     -33.528  13.101 -42.170  1.00 31.65           O  
ATOM   3915  CB  VAL A 501     -32.282  10.287 -40.975  1.00 25.48           C  
ATOM   3916  CG1 VAL A 501     -31.157  11.240 -41.375  1.00 31.98           C  
ATOM   3917  CG2 VAL A 501     -32.002   9.614 -39.623  1.00 25.23           C  
ATOM   3918  N   PHE A 502     -34.225  11.259 -43.276  1.00 25.29           N  
ATOM   3919  CA  PHE A 502     -34.481  11.991 -44.517  1.00 26.49           C  
ATOM   3920  C   PHE A 502     -35.519  13.097 -44.277  1.00 30.36           C  
ATOM   3921  O   PHE A 502     -35.362  14.221 -44.752  1.00 30.69           O  
ATOM   3922  CB  PHE A 502     -34.959  11.042 -45.629  1.00 31.34           C  
ATOM   3923  CG  PHE A 502     -35.553  11.758 -46.812  1.00 30.18           C  
ATOM   3924  CD1 PHE A 502     -34.752  12.159 -47.879  1.00 30.91           C  
ATOM   3925  CD2 PHE A 502     -36.910  12.058 -46.838  1.00 33.06           C  
ATOM   3926  CE1 PHE A 502     -35.303  12.840 -48.958  1.00 27.15           C  
ATOM   3927  CE2 PHE A 502     -37.468  12.745 -47.915  1.00 28.53           C  
ATOM   3928  CZ  PHE A 502     -36.660  13.134 -48.976  1.00 28.63           C  
ATOM   3929  N   LEU A 503     -36.570  12.767 -43.530  1.00 25.29           N  
ATOM   3930  CA  LEU A 503     -37.625  13.718 -43.218  1.00 33.62           C  
ATOM   3931  C   LEU A 503     -37.110  14.795 -42.274  1.00 36.65           C  
ATOM   3932  O   LEU A 503     -37.508  15.958 -42.369  1.00 32.48           O  
ATOM   3933  CB  LEU A 503     -38.821  13.020 -42.576  1.00 29.68           C  
ATOM   3934  CG  LEU A 503     -39.558  11.995 -43.441  1.00 35.13           C  
ATOM   3935  CD1 LEU A 503     -40.755  11.450 -42.683  1.00 27.09           C  
ATOM   3936  CD2 LEU A 503     -39.991  12.663 -44.727  1.00 33.59           C  
ATOM   3937  N   ALA A 504     -36.236  14.398 -41.354  1.00 33.81           N  
ATOM   3938  CA  ALA A 504     -35.666  15.344 -40.413  1.00 34.12           C  
ATOM   3939  C   ALA A 504     -34.887  16.399 -41.183  1.00 37.01           C  
ATOM   3940  O   ALA A 504     -35.019  17.591 -40.920  1.00 33.29           O  
ATOM   3941  CB  ALA A 504     -34.744  14.634 -39.423  1.00 30.60           C  
ATOM   3942  N   GLU A 505     -34.061  15.950 -42.123  1.00 28.68           N  
ATOM   3943  CA  GLU A 505     -33.226  16.872 -42.866  1.00 42.70           C  
ATOM   3944  C   GLU A 505     -34.059  17.706 -43.843  1.00 45.39           C  
ATOM   3945  O   GLU A 505     -33.685  18.829 -44.160  1.00 44.36           O  
ATOM   3946  CB  GLU A 505     -32.036  16.169 -43.549  1.00 41.86           C  
ATOM   3947  CG  GLU A 505     -32.305  14.782 -44.072  1.00 55.38           C  
ATOM   3948  CD  GLU A 505     -31.174  14.231 -44.951  1.00 61.15           C  
ATOM   3949  OE1 GLU A 505     -29.990  14.329 -44.564  1.00 54.62           O  
ATOM   3950  OE2 GLU A 505     -31.480  13.689 -46.037  1.00 62.21           O  
ATOM   3951  N   ARG A 506     -35.199  17.183 -44.284  1.00 35.93           N  
ATOM   3952  CA  ARG A 506     -36.082  17.980 -45.131  1.00 45.38           C  
ATOM   3953  C   ARG A 506     -36.772  19.048 -44.284  1.00 54.30           C  
ATOM   3954  O   ARG A 506     -36.919  20.196 -44.708  1.00 50.06           O  
ATOM   3955  CB  ARG A 506     -37.108  17.103 -45.861  1.00 40.83           C  
ATOM   3956  CG  ARG A 506     -36.487  16.197 -46.913  1.00 38.83           C  
ATOM   3957  CD  ARG A 506     -35.989  17.016 -48.095  1.00 47.00           C  
ATOM   3958  NE  ARG A 506     -34.625  16.723 -48.555  1.00 55.77           N  
ATOM   3959  CZ  ARG A 506     -33.760  15.884 -47.985  1.00 56.96           C  
ATOM   3960  NH1 ARG A 506     -34.076  15.206 -46.893  1.00 46.04           N  
ATOM   3961  NH2 ARG A 506     -32.554  15.722 -48.520  1.00 61.93           N  
ATOM   3962  N   ARG A 507     -37.187  18.669 -43.081  1.00 49.44           N  
ATOM   3963  CA  ARG A 507     -37.841  19.608 -42.184  1.00 52.03           C  
ATOM   3964  C   ARG A 507     -36.876  20.727 -41.822  1.00 53.65           C  
ATOM   3965  O   ARG A 507     -37.269  21.886 -41.732  1.00 54.95           O  
ATOM   3966  CB  ARG A 507     -38.330  18.915 -40.912  1.00 46.44           C  
ATOM   3967  CG  ARG A 507     -39.447  19.673 -40.201  1.00 58.91           C  
ATOM   3968  CD  ARG A 507     -39.402  19.433 -38.704  1.00 52.81           C  
ATOM   3969  NE  ARG A 507     -38.048  19.649 -38.204  1.00 76.65           N  
ATOM   3970  CZ  ARG A 507     -37.576  20.825 -37.797  1.00 82.92           C  
ATOM   3971  NH1 ARG A 507     -38.357  21.903 -37.805  1.00 64.50           N  
ATOM   3972  NH2 ARG A 507     -36.320  20.919 -37.376  1.00 67.05           N  
ATOM   3973  N   ARG A 508     -35.612  20.372 -41.624  1.00 45.51           N  
ATOM   3974  CA  ARG A 508     -34.589  21.352 -41.283  1.00 65.16           C  
ATOM   3975  C   ARG A 508     -34.333  22.331 -42.433  1.00 64.75           C  
ATOM   3976  O   ARG A 508     -34.204  23.534 -42.225  1.00 58.20           O  
ATOM   3977  CB  ARG A 508     -33.284  20.657 -40.873  1.00 48.70           C  
ATOM   3978  CG  ARG A 508     -32.346  21.550 -40.070  1.00 71.11           C  
ATOM   3979  CD  ARG A 508     -31.246  20.755 -39.362  1.00 70.83           C  
ATOM   3980  NE  ARG A 508     -29.972  20.645 -40.085  1.00 86.21           N  
ATOM   3981  CZ  ARG A 508     -29.633  21.301 -41.197  1.00 90.66           C  
ATOM   3982  NH1 ARG A 508     -30.464  22.153 -41.782  1.00 86.68           N  
ATOM   3983  NH2 ARG A 508     -28.435  21.098 -41.734  1.00 86.78           N  
ATOM   3984  N   ASN A 509     -34.259  21.812 -43.649  1.00 59.05           N  
ATOM   3985  CA  ASN A 509     -34.022  22.661 -44.805  1.00 67.89           C  
ATOM   3986  C   ASN A 509     -35.169  23.636 -45.014  1.00 70.44           C  
ATOM   3987  O   ASN A 509     -34.962  24.776 -45.431  1.00 70.50           O  
ATOM   3988  CB  ASN A 509     -33.788  21.813 -46.050  1.00 56.07           C  
ATOM   3989  CG  ASN A 509     -32.511  21.001 -45.962  1.00 68.74           C  
ATOM   3990  OD1 ASN A 509     -32.357  19.989 -46.643  1.00 82.70           O  
ATOM   3991  ND2 ASN A 509     -31.587  21.440 -45.114  1.00 71.08           N  
ATOM   3992  N   HIS A 510     -36.381  23.187 -44.711  1.00 61.85           N  
ATOM   3993  CA  HIS A 510     -37.546  24.048 -44.823  1.00 67.94           C  
ATOM   3994  C   HIS A 510     -37.499  25.186 -43.803  1.00 80.66           C  
ATOM   3995  O   HIS A 510     -37.694  26.350 -44.151  1.00 78.74           O  
ATOM   3996  CB  HIS A 510     -38.834  23.244 -44.661  1.00 50.38           C  
ATOM   3997  CG  HIS A 510     -40.071  24.051 -44.892  1.00 77.25           C  
ATOM   3998  ND1 HIS A 510     -41.014  24.269 -43.910  1.00 83.43           N  
ATOM   3999  CD2 HIS A 510     -40.511  24.711 -45.989  1.00 77.79           C  
ATOM   4000  CE1 HIS A 510     -41.987  25.019 -44.397  1.00 88.35           C  
ATOM   4001  NE2 HIS A 510     -41.706  25.301 -45.657  1.00 83.75           N  
ATOM   4002  N   GLU A 511     -37.240  24.846 -42.543  1.00 66.43           N  
ATOM   4003  CA  GLU A 511     -37.169  25.849 -41.491  1.00 69.97           C  
ATOM   4004  C   GLU A 511     -35.821  26.557 -41.513  1.00 71.99           C  
ATOM   4005  O   GLU A 511     -35.745  27.742 -41.831  1.00 81.68           O  
ATOM   4006  CB  GLU A 511     -37.433  25.219 -40.119  1.00 67.33           C  
ATOM   4007  CG  GLU A 511     -36.373  24.226 -39.660  1.00 80.38           C  
ATOM   4008  CD  GLU A 511     -35.279  24.870 -38.823  1.00 92.77           C  
ATOM   4009  OE1 GLU A 511     -35.415  26.069 -38.492  1.00 98.74           O  
ATOM   4010  OE2 GLU A 511     -34.290  24.175 -38.489  1.00 85.25           O  
TER    4011      GLU A 511                                                      
HETATM 4012  N   TRP A 601     -25.177  -3.433 -19.182  1.00 25.51           N  
HETATM 4013  CA  TRP A 601     -26.158  -4.504 -19.119  1.00 27.26           C  
HETATM 4014  C   TRP A 601     -25.791  -5.578 -18.088  1.00 33.93           C  
HETATM 4015  O   TRP A 601     -26.620  -6.370 -17.651  1.00 33.24           O  
HETATM 4016  CB  TRP A 601     -26.289  -5.175 -20.497  1.00 28.22           C  
HETATM 4017  CG  TRP A 601     -26.681  -4.269 -21.611  1.00 28.41           C  
HETATM 4018  CD1 TRP A 601     -25.881  -3.835 -22.635  1.00 32.64           C  
HETATM 4019  CD2 TRP A 601     -27.976  -3.698 -21.844  1.00 29.19           C  
HETATM 4020  NE1 TRP A 601     -26.599  -3.038 -23.492  1.00 29.64           N  
HETATM 4021  CE2 TRP A 601     -27.888  -2.939 -23.040  1.00 29.57           C  
HETATM 4022  CE3 TRP A 601     -29.203  -3.769 -21.171  1.00 26.65           C  
HETATM 4023  CZ2 TRP A 601     -28.974  -2.240 -23.572  1.00 25.03           C  
HETATM 4024  CZ3 TRP A 601     -30.291  -3.072 -21.699  1.00 32.12           C  
HETATM 4025  CH2 TRP A 601     -30.166  -2.318 -22.901  1.00 31.76           C  
HETATM 4026  OXT TRP A 601     -24.638  -5.700 -17.673  1.00 28.07           O  
HETATM 4027  N   TRP A 602     -25.065 -12.048 -27.469  1.00 45.52           N  
HETATM 4028  CA  TRP A 602     -24.595 -12.213 -26.102  1.00 56.68           C  
HETATM 4029  C   TRP A 602     -25.113 -13.502 -25.481  1.00 70.41           C  
HETATM 4030  O   TRP A 602     -24.483 -14.055 -24.576  1.00 62.94           O  
HETATM 4031  CB  TRP A 602     -25.015 -11.014 -25.253  1.00 49.40           C  
HETATM 4032  CG  TRP A 602     -24.519  -9.744 -25.831  1.00 43.14           C  
HETATM 4033  CD1 TRP A 602     -25.259  -8.773 -26.427  1.00 36.52           C  
HETATM 4034  CD2 TRP A 602     -23.152  -9.319 -25.908  1.00 42.83           C  
HETATM 4035  NE1 TRP A 602     -24.442  -7.755 -26.852  1.00 40.69           N  
HETATM 4036  CE2 TRP A 602     -23.143  -8.067 -26.549  1.00 42.88           C  
HETATM 4037  CE3 TRP A 602     -21.937  -9.872 -25.485  1.00 46.92           C  
HETATM 4038  CZ2 TRP A 602     -21.967  -7.357 -26.783  1.00 36.37           C  
HETATM 4039  CZ3 TRP A 602     -20.769  -9.165 -25.715  1.00 39.08           C  
HETATM 4040  CH2 TRP A 602     -20.793  -7.922 -26.359  1.00 47.84           C  
HETATM 4041  OXT TRP A 602     -26.170 -13.994 -25.889  1.00 69.23           O  
HETATM 4042  N   TRP A 603     -16.985  21.788 -15.187  1.00 42.57           N  
HETATM 4043  CA  TRP A 603     -17.300  22.016 -13.780  1.00 40.39           C  
HETATM 4044  C   TRP A 603     -18.032  20.829 -13.142  1.00 44.62           C  
HETATM 4045  O   TRP A 603     -18.120  20.722 -11.920  1.00 43.07           O  
HETATM 4046  CB  TRP A 603     -18.123  23.304 -13.619  1.00 43.62           C  
HETATM 4047  CG  TRP A 603     -19.387  23.348 -14.459  1.00 41.54           C  
HETATM 4048  CD1 TRP A 603     -19.535  23.922 -15.686  1.00 49.16           C  
HETATM 4049  CD2 TRP A 603     -20.672  22.810 -14.110  1.00 43.48           C  
HETATM 4050  NE1 TRP A 603     -20.831  23.767 -16.132  1.00 49.35           N  
HETATM 4051  CE2 TRP A 603     -21.547  23.087 -15.181  1.00 44.98           C  
HETATM 4052  CE3 TRP A 603     -21.162  22.113 -12.998  1.00 40.60           C  
HETATM 4053  CZ2 TRP A 603     -22.883  22.699 -15.172  1.00 37.89           C  
HETATM 4054  CZ3 TRP A 603     -22.485  21.729 -12.992  1.00 47.17           C  
HETATM 4055  CH2 TRP A 603     -23.334  22.025 -14.073  1.00 39.29           C  
HETATM 4056  OXT TRP A 603     -18.561  19.949 -13.820  1.00 37.11           O  
HETATM 4057  N   TRP A 604     -29.131 -29.412 -16.730  1.00 82.99           N  
HETATM 4058  CA  TRP A 604     -28.702 -28.077 -16.333  1.00 81.25           C  
HETATM 4059  C   TRP A 604     -29.170 -27.054 -17.357  1.00 77.20           C  
HETATM 4060  O   TRP A 604     -29.701 -26.005 -17.003  1.00 60.79           O  
HETATM 4061  CB  TRP A 604     -27.174 -28.016 -16.190  1.00 65.29           C  
HETATM 4062  CG  TRP A 604     -26.632 -29.091 -15.316  1.00 77.50           C  
HETATM 4063  CD1 TRP A 604     -25.919 -30.187 -15.705  1.00 80.88           C  
HETATM 4064  CD2 TRP A 604     -26.773 -29.186 -13.895  1.00 79.27           C  
HETATM 4065  NE1 TRP A 604     -25.600 -30.956 -14.611  1.00 82.09           N  
HETATM 4066  CE2 TRP A 604     -26.114 -30.364 -13.488  1.00 71.48           C  
HETATM 4067  CE3 TRP A 604     -27.390 -28.388 -12.926  1.00 65.39           C  
HETATM 4068  CZ2 TRP A 604     -26.056 -30.763 -12.157  1.00 70.71           C  
HETATM 4069  CZ3 TRP A 604     -27.328 -28.783 -11.603  1.00 69.81           C  
HETATM 4070  CH2 TRP A 604     -26.665 -29.960 -11.230  1.00 75.67           C  
HETATM 4071  OXT TRP A 604     -29.023 -27.277 -18.560  1.00 65.29           O  
HETATM 4072  C1  BOG A 701     -51.289 -18.058 -12.949  1.00 83.91           C  
HETATM 4073  O1  BOG A 701     -50.814 -16.710 -12.894  1.00 75.48           O  
HETATM 4074  C2  BOG A 701     -51.724 -18.415 -14.384  1.00 91.85           C  
HETATM 4075  O2  BOG A 701     -50.885 -17.754 -15.345  1.00 72.53           O  
HETATM 4076  C3  BOG A 701     -51.789 -19.926 -14.682  1.00100.43           C  
HETATM 4077  O3  BOG A 701     -51.728 -20.150 -16.104  1.00 75.90           O  
HETATM 4078  C4  BOG A 701     -50.680 -20.704 -13.978  1.00 93.02           C  
HETATM 4079  O4  BOG A 701     -50.937 -22.112 -14.077  1.00 85.70           O  
HETATM 4080  C5  BOG A 701     -50.614 -20.283 -12.514  1.00 88.51           C  
HETATM 4081  O5  BOG A 701     -50.242 -18.909 -12.475  1.00 80.79           O  
HETATM 4082  C6  BOG A 701     -49.600 -21.104 -11.722  1.00 83.61           C  
HETATM 4083  O6  BOG A 701     -48.297 -20.956 -12.299  1.00 74.13           O  
HETATM 4084  C1' BOG A 701     -51.511 -15.946 -11.908  1.00 67.48           C  
HETATM 4085  C2' BOG A 701     -50.592 -14.878 -11.324  1.00 59.51           C  
HETATM 4086  C3' BOG A 701     -51.334 -13.570 -11.065  1.00 56.94           C  
HETATM 4087  C4' BOG A 701     -51.855 -13.447  -9.640  1.00 52.49           C  
HETATM 4088  C5' BOG A 701     -51.082 -12.407  -8.835  1.00 68.07           C  
HETATM 4089  C6' BOG A 701     -52.056 -11.409  -8.213  1.00 78.30           C  
HETATM 4090  C7' BOG A 701     -51.650 -10.971  -6.810  1.00 66.49           C  
HETATM 4091  C8' BOG A 701     -50.929  -9.638  -6.815  1.00 80.69           C  
HETATM 4092  C1  BOG A 702     -55.126 -16.435 -16.739  1.00 75.50           C  
HETATM 4093  O1  BOG A 702     -55.177 -15.243 -15.950  1.00 66.12           O  
HETATM 4094  C2  BOG A 702     -55.059 -17.670 -15.838  1.00 76.98           C  
HETATM 4095  O2  BOG A 702     -56.124 -17.651 -14.881  1.00 79.48           O  
HETATM 4096  C3  BOG A 702     -55.135 -18.967 -16.645  1.00 78.72           C  
HETATM 4097  O3  BOG A 702     -55.333 -20.092 -15.775  1.00 70.86           O  
HETATM 4098  C4  BOG A 702     -56.261 -18.927 -17.669  1.00 62.89           C  
HETATM 4099  O4  BOG A 702     -56.128 -20.075 -18.510  1.00 53.24           O  
HETATM 4100  C5  BOG A 702     -56.192 -17.636 -18.484  1.00 67.11           C  
HETATM 4101  O5  BOG A 702     -56.273 -16.516 -17.596  1.00 71.38           O  
HETATM 4102  C6  BOG A 702     -57.271 -17.560 -19.565  1.00 73.31           C  
HETATM 4103  O6  BOG A 702     -58.579 -17.657 -18.987  1.00 71.10           O  
HETATM 4104  C1' BOG A 702     -53.920 -14.563 -16.019  1.00 70.70           C  
HETATM 4105  C2' BOG A 702     -54.072 -13.044 -15.959  1.00 64.17           C  
HETATM 4106  C3' BOG A 702     -53.764 -12.488 -14.574  1.00 64.08           C  
HETATM 4107  C4' BOG A 702     -52.848 -11.267 -14.648  1.00 67.68           C  
HETATM 4108  C5' BOG A 702     -52.936 -10.423 -13.380  1.00 67.30           C  
HETATM 4109  C6' BOG A 702     -51.556 -10.159 -12.774  1.00 70.68           C  
HETATM 4110  C7' BOG A 702     -51.046  -8.744 -13.030  1.00 59.41           C  
HETATM 4111  C8' BOG A 702     -51.253  -7.849 -11.826  1.00 60.65           C  
HETATM 4112  C1  BOG A 703     -52.710 -12.309 -27.303  1.00 51.91           C  
HETATM 4113  O1  BOG A 703     -52.824 -11.950 -28.679  1.00 54.52           O  
HETATM 4114  C2  BOG A 703     -54.089 -12.716 -26.753  1.00 62.82           C  
HETATM 4115  O2  BOG A 703     -54.965 -13.106 -27.821  1.00 61.24           O  
HETATM 4116  C3  BOG A 703     -54.098 -13.806 -25.662  1.00 67.30           C  
HETATM 4117  O3  BOG A 703     -55.208 -14.684 -25.898  1.00 55.21           O  
HETATM 4118  C4  BOG A 703     -52.828 -14.645 -25.605  1.00 48.31           C  
HETATM 4119  O4  BOG A 703     -52.756 -15.279 -24.328  1.00 53.28           O  
HETATM 4120  C5  BOG A 703     -51.641 -13.729 -25.809  1.00 39.93           C  
HETATM 4121  O5  BOG A 703     -51.729 -13.336 -27.166  1.00 40.81           O  
HETATM 4122  C6  BOG A 703     -50.300 -14.389 -25.515  1.00 39.38           C  
HETATM 4123  O6  BOG A 703     -50.079 -15.489 -26.404  1.00 44.07           O  
HETATM 4124  C1' BOG A 703     -51.773 -11.075 -29.082  1.00 52.72           C  
HETATM 4125  C2' BOG A 703     -52.119 -10.504 -30.445  1.00 51.14           C  
HETATM 4126  C3' BOG A 703     -50.870 -10.332 -31.299  1.00 68.49           C  
HETATM 4127  C4' BOG A 703     -51.234 -10.005 -32.751  1.00 78.18           C  
HETATM 4128  C5' BOG A 703     -50.478  -8.772 -33.248  1.00 84.64           C  
HETATM 4129  C6' BOG A 703     -51.295  -7.508 -32.995  1.00 89.41           C  
HETATM 4130  C7' BOG A 703     -50.494  -6.402 -32.303  1.00 76.24           C  
HETATM 4131  C8' BOG A 703     -51.419  -5.467 -31.541  1.00 62.48           C  
HETATM 4132  C1  BOG A 704     -53.220 -17.105 -33.381  1.00 85.10           C  
HETATM 4133  O1  BOG A 704     -52.744 -15.933 -32.719  1.00 90.00           O  
HETATM 4134  C2  BOG A 704     -53.426 -18.210 -32.337  1.00 88.03           C  
HETATM 4135  O2  BOG A 704     -53.968 -17.647 -31.134  1.00 92.91           O  
HETATM 4136  C3  BOG A 704     -54.323 -19.353 -32.811  1.00 87.38           C  
HETATM 4137  O3  BOG A 704     -54.784 -20.084 -31.666  1.00 82.81           O  
HETATM 4138  C4  BOG A 704     -55.513 -18.833 -33.605  1.00 88.36           C  
HETATM 4139  O4  BOG A 704     -56.203 -19.932 -34.206  1.00 92.19           O  
HETATM 4140  C5  BOG A 704     -55.022 -17.897 -34.697  1.00 87.28           C  
HETATM 4141  O5  BOG A 704     -54.439 -16.770 -34.052  1.00 87.62           O  
HETATM 4142  C6  BOG A 704     -56.148 -17.460 -35.638  1.00 87.35           C  
HETATM 4143  O6  BOG A 704     -57.190 -16.781 -34.921  1.00 89.37           O  
HETATM 4144  C1' BOG A 704     -51.478 -15.500 -33.223  1.00 68.21           C  
HETATM 4145  C2' BOG A 704     -51.367 -13.981 -33.135  1.00 59.61           C  
HETATM 4146  C3' BOG A 704     -49.935 -13.551 -32.846  1.00 59.54           C  
HETATM 4147  C4' BOG A 704     -48.965 -14.044 -33.912  1.00 49.41           C  
HETATM 4148  C5' BOG A 704     -48.512 -12.921 -34.840  1.00 46.89           C  
HETATM 4149  C6' BOG A 704     -47.469 -12.044 -34.165  1.00 46.76           C  
HETATM 4150  C7' BOG A 704     -46.663 -11.258 -35.192  1.00 40.86           C  
HETATM 4151  C8' BOG A 704     -45.363 -11.950 -35.525  1.00 34.59           C  
HETATM 4152  C1  BOG A 705     -51.752 -20.087 -37.016  1.00 68.14           C  
HETATM 4153  O1  BOG A 705     -51.522 -19.991 -35.601  1.00 68.84           O  
HETATM 4154  C2  BOG A 705     -52.223 -21.489 -37.422  1.00 77.78           C  
HETATM 4155  O2  BOG A 705     -51.826 -22.435 -36.419  1.00 71.60           O  
HETATM 4156  C3  BOG A 705     -53.735 -21.588 -37.648  1.00 74.49           C  
HETATM 4157  O3  BOG A 705     -54.415 -21.528 -36.389  1.00 85.19           O  
HETATM 4158  C4  BOG A 705     -54.269 -20.488 -38.568  1.00 71.88           C  
HETATM 4159  O4  BOG A 705     -54.618 -21.016 -39.856  1.00 61.62           O  
HETATM 4160  C5  BOG A 705     -53.248 -19.364 -38.704  1.00 62.53           C  
HETATM 4161  O5  BOG A 705     -52.706 -19.100 -37.411  1.00 62.39           O  
HETATM 4162  C6  BOG A 705     -53.856 -18.102 -39.314  1.00 59.60           C  
HETATM 4163  O6  BOG A 705     -54.914 -17.600 -38.492  1.00 70.89           O  
HETATM 4164  C1' BOG A 705     -50.150 -19.702 -35.307  1.00 52.87           C  
HETATM 4165  C2' BOG A 705     -49.994 -18.332 -34.653  1.00 54.79           C  
HETATM 4166  C3' BOG A 705     -48.533 -17.987 -34.359  1.00 53.61           C  
HETATM 4167  C4' BOG A 705     -47.805 -17.321 -35.526  1.00 46.31           C  
HETATM 4168  C5' BOG A 705     -46.515 -16.646 -35.059  1.00 44.28           C  
HETATM 4169  C6' BOG A 705     -45.697 -16.100 -36.222  1.00 39.12           C  
HETATM 4170  C7' BOG A 705     -44.551 -15.202 -35.762  1.00 43.54           C  
HETATM 4171  C8' BOG A 705     -43.797 -14.633 -36.952  1.00 48.24           C  
HETATM 4172  C1  BOG A 706     -30.119 -21.077   7.042  1.00 65.79           C  
HETATM 4173  O1  BOG A 706     -30.518 -19.866   6.386  1.00 57.41           O  
HETATM 4174  C2  BOG A 706     -30.293 -22.264   6.078  1.00 58.17           C  
HETATM 4175  O2  BOG A 706     -30.524 -21.774   4.751  1.00 54.69           O  
HETATM 4176  C3  BOG A 706     -29.169 -23.315   6.022  1.00 44.82           C  
HETATM 4177  O3  BOG A 706     -28.629 -23.397   4.697  1.00 48.27           O  
HETATM 4178  C4  BOG A 706     -28.015 -23.139   7.013  1.00 47.76           C  
HETATM 4179  O4  BOG A 706     -27.669 -24.425   7.542  1.00 46.74           O  
HETATM 4180  C5  BOG A 706     -28.336 -22.178   8.144  1.00 47.80           C  
HETATM 4181  O5  BOG A 706     -28.788 -20.960   7.561  1.00 51.04           O  
HETATM 4182  C6  BOG A 706     -27.096 -21.929   8.998  1.00 53.48           C  
HETATM 4183  O6  BOG A 706     -27.346 -20.897   9.961  1.00 44.22           O  
HETATM 4184  C1' BOG A 706     -31.006 -18.900   7.319  1.00 64.18           C  
HETATM 4185  C2' BOG A 706     -31.732 -17.753   6.613  1.00 52.83           C  
HETATM 4186  C3' BOG A 706     -33.245 -17.977   6.584  1.00 55.80           C  
HETATM 4187  C4' BOG A 706     -34.017 -16.682   6.319  1.00 54.58           C  
HETATM 4188  C5' BOG A 706     -34.456 -16.539   4.868  1.00 48.33           C  
HETATM 4189  C6' BOG A 706     -35.539 -15.469   4.752  1.00 57.14           C  
HETATM 4190  C7' BOG A 706     -35.320 -14.569   3.538  1.00 58.38           C  
HETATM 4191  C8' BOG A 706     -34.928 -15.365   2.315  1.00 57.78           C  
HETATM 4192  C01 C14 A 707     -28.917  -6.277 -24.250  1.00 42.43           C  
HETATM 4193  C02 C14 A 707     -29.232  -7.548 -23.480  1.00 31.16           C  
HETATM 4194  C03 C14 A 707     -28.901  -8.876 -24.160  1.00 46.50           C  
HETATM 4195  C04 C14 A 707     -29.172 -10.161 -23.359  1.00 42.91           C  
HETATM 4196  C05 C14 A 707     -27.974 -11.008 -22.917  1.00 45.34           C  
HETATM 4197  C06 C14 A 707     -28.081 -11.895 -21.663  1.00 43.09           C  
HETATM 4198  C07 C14 A 707     -27.943 -11.249 -20.274  1.00 41.72           C  
HETATM 4199  C08 C14 A 707     -27.809 -12.161 -19.028  1.00 47.92           C  
HETATM 4200  C09 C14 A 707     -29.064 -12.812 -18.425  1.00 40.05           C  
HETATM 4201  C10 C14 A 707     -29.751 -13.932 -19.214  1.00 53.17           C  
HETATM 4202  C11 C14 A 707     -31.188 -13.731 -19.730  1.00 55.55           C  
HETATM 4203  C12 C14 A 707     -31.386 -13.255 -21.170  1.00 43.33           C  
HETATM 4204  C13 C14 A 707     -32.327 -14.037 -22.090  1.00 47.86           C  
HETATM 4205  C14 C14 A 707     -31.821 -14.456 -23.471  1.00 40.43           C  
HETATM 4206  C1  BOG A 708     -21.473 -14.620 -27.688  1.00 81.06           C  
HETATM 4207  O1  BOG A 708     -21.004 -13.577 -26.839  1.00 66.38           O  
HETATM 4208  C2  BOG A 708     -21.750 -15.913 -26.897  1.00 76.38           C  
HETATM 4209  O2  BOG A 708     -22.325 -15.617 -25.612  1.00 76.87           O  
HETATM 4210  C3  BOG A 708     -22.629 -16.916 -27.660  1.00 71.21           C  
HETATM 4211  O3  BOG A 708     -23.200 -17.859 -26.741  1.00 83.84           O  
HETATM 4212  C4  BOG A 708     -23.741 -16.220 -28.437  1.00 74.61           C  
HETATM 4213  O4  BOG A 708     -24.406 -17.170 -29.272  1.00 76.36           O  
HETATM 4214  C5  BOG A 708     -23.118 -15.115 -29.281  1.00 88.79           C  
HETATM 4215  O5  BOG A 708     -22.638 -14.137 -28.361  1.00 78.00           O  
HETATM 4216  C6  BOG A 708     -24.069 -14.491 -30.308  1.00 60.38           C  
HETATM 4217  O6  BOG A 708     -24.955 -13.532 -29.713  1.00 53.89           O  
HETATM 4218  C1' BOG A 708     -19.670 -13.227 -27.188  1.00 63.73           C  
HETATM 4219  C2' BOG A 708     -19.657 -11.887 -27.906  1.00 57.61           C  
HETATM 4220  C3' BOG A 708     -18.374 -11.136 -27.579  1.00 66.39           C  
HETATM 4221  C4' BOG A 708     -17.748 -10.541 -28.830  1.00 55.34           C  
HETATM 4222  C5' BOG A 708     -18.804  -9.906 -29.719  1.00 63.20           C  
HETATM 4223  C6' BOG A 708     -18.146  -9.135 -30.856  1.00 73.54           C  
HETATM 4224  C7' BOG A 708     -19.189  -8.567 -31.811  1.00 70.79           C  
HETATM 4225  C8' BOG A 708     -18.535  -7.948 -33.030  1.00 73.37           C  
HETATM 4226 NA    NA A 751     -30.038  -1.290 -15.356  1.00 27.17          NA  
HETATM 4227 NA    NA A 752     -23.379  -3.966 -16.236  1.00 28.89          NA  
HETATM 4228  O   HOH A 520     -48.523 -18.625 -31.184  1.00 47.37           O  
HETATM 4229  O   HOH A 521     -27.938 -24.436 -14.843  1.00 44.34           O  
HETATM 4230  O   HOH A 522     -60.012 -18.699 -16.215  1.00 44.30           O  
HETATM 4231  O   HOH A 523     -40.579 -18.334   1.194  1.00 42.30           O  
HETATM 4232  O   HOH A 524     -23.980   3.840 -18.537  1.00 35.28           O  
HETATM 4233  O   HOH A 525     -17.661 -12.453  -5.769  1.00 55.22           O  
HETATM 4234  O   HOH A 526     -58.621 -16.079 -21.675  1.00 70.08           O  
HETATM 4235  O   HOH A 527     -45.367 -22.602 -28.664  1.00 43.96           O  
HETATM 4236  O   HOH A 528     -26.103  16.727 -13.417  1.00 42.23           O  
HETATM 4237  O   HOH A 529      -3.620  17.168 -21.873  1.00 61.01           O  
HETATM 4238  O   HOH A 530     -32.173 -23.966   3.722  1.00 46.75           O  
HETATM 4239  O   HOH A 531     -34.828 -28.475 -23.559  1.00 73.43           O  
HETATM 4240  O   HOH A 532     -30.583 -25.174 -40.896  1.00 68.61           O  
HETATM 4241  O   HOH A 533     -23.329 -16.371 -20.497  1.00 47.38           O  
HETATM 4242  O   HOH A 534     -10.185  20.570 -22.463  1.00 50.56           O  
HETATM 4243  O   HOH A 535     -31.847 -21.092 -36.094  1.00 52.88           O  
HETATM 4244  O   HOH A 536     -24.276  19.460 -23.527  1.00 44.57           O  
HETATM 4245  O   HOH A 537     -39.256 -26.110 -32.676  1.00 62.54           O  
HETATM 4246  O   HOH A 538     -43.673 -11.282 -19.578  1.00 25.77           O  
HETATM 4247  O   HOH A 539     -22.859  -7.694 -17.241  1.00 31.77           O  
HETATM 4248  O   HOH A 540     -30.307   6.975 -23.394  1.00 27.17           O  
HETATM 4249  O   HOH A 541     -39.194  -5.657 -25.825  1.00 29.14           O  
HETATM 4250  O   HOH A 542     -29.862  12.582 -34.734  1.00 31.48           O  
HETATM 4251  O   HOH A 543     -38.012 -14.585 -30.116  1.00 25.20           O  
HETATM 4252  O   HOH A 544     -29.232  -6.857 -18.731  1.00 28.01           O  
HETATM 4253  O   HOH A 545     -34.298   3.648 -28.874  1.00 31.29           O  
HETATM 4254  O   HOH A 546     -38.358 -21.456 -13.425  1.00 37.78           O  
HETATM 4255  O   HOH A 547     -26.533 -22.285 -15.612  1.00 41.25           O  
HETATM 4256  O   HOH A 548     -25.728  18.693  -8.441  1.00 48.21           O  
HETATM 4257  O   HOH A 549     -31.170  13.536 -31.853  1.00 33.52           O  
HETATM 4258  O   HOH A 550     -45.794  16.394 -31.086  1.00 29.93           O  
HETATM 4259  O   HOH A 551     -41.899 -24.292 -39.988  0.50 30.49           O  
HETATM 4260  O   HOH A 552     -37.953  10.912 -21.629  1.00 31.89           O  
HETATM 4261  O   HOH A 553     -23.791   4.941 -26.060  1.00 32.12           O  
HETATM 4262  O   HOH A 554     -36.435 -14.974 -36.723  1.00 33.94           O  
HETATM 4263  O   HOH A 555     -28.240   7.207 -31.521  1.00 30.87           O  
HETATM 4264  O   HOH A 556     -22.236  24.439 -18.959  1.00 34.05           O  
HETATM 4265  O   HOH A 557     -31.182   4.604 -16.118  1.00 28.16           O  
HETATM 4266  O   HOH A 558     -21.854 -15.470  -8.771  1.00 37.31           O  
HETATM 4267  O   HOH A 559     -23.411   4.091 -28.704  1.00 32.74           O  
HETATM 4268  O   HOH A 560     -42.616 -15.576 -25.952  1.00 25.99           O  
HETATM 4269  O   HOH A 561      -9.273   5.640 -32.317  1.00 49.08           O  
HETATM 4270  O   HOH A 562     -38.108  15.800 -16.456  1.00 29.64           O  
HETATM 4271  O   HOH A 563     -18.333  16.679 -24.773  1.00 37.58           O  
HETATM 4272  O   HOH A 564     -25.095 -12.840  -8.883  1.00 43.03           O  
HETATM 4273  O   HOH A 565     -52.492 -18.431 -20.594  1.00 41.07           O  
HETATM 4274  O   HOH A 566     -37.682  13.034 -23.125  1.00 28.53           O  
HETATM 4275  O   HOH A 567     -28.612 -20.423 -20.374  1.00 41.59           O  
HETATM 4276  O   HOH A 568     -21.095  15.675 -14.153  1.00 32.30           O  
HETATM 4277  O   HOH A 569     -18.217 -12.088 -23.709  1.00 46.41           O  
HETATM 4278  O   HOH A 570     -25.291   3.076 -30.476  1.00 35.05           O  
HETATM 4279  O   HOH A 571     -37.032 -16.922 -28.942  1.00 34.14           O  
HETATM 4280  O   HOH A 572     -27.702   0.133 -22.341  1.00 37.89           O  
HETATM 4281  O   HOH A 573     -27.942 -13.815 -30.095  1.00 36.31           O  
HETATM 4282  O   HOH A 574     -44.888  16.559 -23.560  1.00 34.75           O  
HETATM 4283  O   HOH A 575     -32.518  14.724  -8.771  1.00 39.63           O  
HETATM 4284  O   HOH A 576     -13.369  18.090 -36.861  1.00 53.98           O  
HETATM 4285  O   HOH A 577     -42.409  18.206 -24.867  1.00 39.73           O  
HETATM 4286  O   HOH A 578     -34.171  15.107 -26.163  1.00 31.67           O  
HETATM 4287  O   HOH A 579     -35.949  16.517 -17.516  1.00 42.94           O  
HETATM 4288  O   HOH A 580     -51.737 -17.192 -18.150  1.00 39.61           O  
HETATM 4289  O   HOH A 581      -7.379  17.231 -33.860  1.00 44.18           O  
HETATM 4290  O   HOH A 582     -37.032 -22.984 -34.732  1.00 63.47           O  
HETATM 4291  O   HOH A 583      -7.288   3.859 -37.075  1.00 49.77           O  
HETATM 4292  O   HOH A 584     -47.948  16.764 -26.809  1.00 40.36           O  
HETATM 4293  O   HOH A 585     -35.034  18.380 -28.101  1.00 39.25           O  
HETATM 4294  O   HOH A 586     -21.147  21.053 -29.085  1.00 43.56           O  
HETATM 4295  O   HOH A 587     -51.935 -17.551 -24.043  1.00 37.70           O  
HETATM 4296  O   HOH A 588     -34.373 -23.846 -42.736  1.00 49.71           O  
HETATM 4297  O   HOH A 589     -45.602 -20.614 -16.211  1.00 46.07           O  
HETATM 4298  O   HOH A 590     -21.629   2.652 -18.738  1.00 31.74           O  
HETATM 4299  O   HOH A 591     -32.945  19.851 -31.618  1.00 53.18           O  
HETATM 4300  O   HOH A 592     -25.734   2.257 -23.688  1.00 43.15           O  
HETATM 4301  O   HOH A 593     -25.329 -14.509 -21.977  1.00 41.73           O  
HETATM 4302  O   HOH A 594     -15.132  16.531 -18.716  1.00 36.92           O  
HETATM 4303  O   HOH A 595     -44.180 -26.260 -32.483  1.00 45.75           O  
HETATM 4304  O   HOH A 596     -27.701   7.494 -28.880  1.00 36.60           O  
HETATM 4305  O   HOH A 597     -25.336  23.258 -21.606  1.00 43.22           O  
HETATM 4306  O   HOH A 598     -36.091  10.148  -6.478  1.00 43.92           O  
HETATM 4307  O   HOH A 599     -50.498 -17.298 -30.543  1.00 50.39           O  
HETATM 4308  O   HOH A 600     -39.503  27.780 -41.708  1.00 65.90           O  
HETATM 4309  O   HOH A 605     -33.720 -19.436   0.544  1.00 48.43           O  
HETATM 4310  O   HOH A 606     -28.848 -26.516   6.335  1.00 52.75           O  
HETATM 4311  O   HOH A 607     -22.306 -21.260   3.023  1.00 41.87           O  
HETATM 4312  O   HOH A 608     -28.383 -24.147 -22.117  1.00 54.06           O  
HETATM 4313  O   HOH A 609     -26.987  19.187 -22.925  1.00 50.06           O  
HETATM 4314  O   HOH A 610     -24.588  18.946 -10.995  1.00 52.87           O  
HETATM 4315  O   HOH A 611     -34.449 -17.391 -27.424  1.00 44.10           O  
HETATM 4316  O   HOH A 612     -41.892  27.282 -41.067  0.50 47.60           O  
HETATM 4317  O   HOH A 613     -40.361  25.420 -40.848  1.00 78.54           O  
HETATM 4318  O   HOH A 614     -34.714  17.512 -24.176  1.00 43.35           O  
HETATM 4319  O   HOH A 615     -31.789 -38.245  -4.153  1.00 66.99           O  
HETATM 4320  O   HOH A 616     -29.122  -8.494 -20.704  1.00 41.20           O  
HETATM 4321  O   HOH A 617     -47.655 -18.139 -16.824  1.00 33.25           O  
HETATM 4322  O   HOH A 618     -36.243 -17.875 -36.049  1.00 43.75           O  
HETATM 4323  O   HOH A 619     -21.934   5.717 -18.833  1.00 42.26           O  
HETATM 4324  O   HOH A 620     -18.549 -14.557 -24.537  1.00 43.22           O  
HETATM 4325  O   HOH A 621     -17.399 -28.967 -11.545  1.00 49.74           O  
HETATM 4326  O   HOH A 622     -40.284   8.403 -11.763  1.00 51.64           O  
HETATM 4327  O   HOH A 623     -18.626 -16.263 -30.199  1.00 60.77           O  
HETATM 4328  O   HOH A 624     -44.426  19.596 -33.591  1.00 56.61           O  
CONECT 4072 4073 4074 4081                                                      
CONECT 4073 4072 4084                                                           
CONECT 4074 4072 4075 4076                                                      
CONECT 4075 4074                                                                
CONECT 4076 4074 4077 4078                                                      
CONECT 4077 4076                                                                
CONECT 4078 4076 4079 4080                                                      
CONECT 4079 4078                                                                
CONECT 4080 4078 4081 4082                                                      
CONECT 4081 4072 4080                                                           
CONECT 4082 4080 4083                                                           
CONECT 4083 4082                                                                
CONECT 4084 4073 4085                                                           
CONECT 4085 4084 4086                                                           
CONECT 4086 4085 4087                                                           
CONECT 4087 4086 4088                                                           
CONECT 4088 4087 4089                                                           
CONECT 4089 4088 4090                                                           
CONECT 4090 4089 4091                                                           
CONECT 4091 4090                                                                
CONECT 4092 4093 4094 4101                                                      
CONECT 4093 4092 4104                                                           
CONECT 4094 4092 4095 4096                                                      
CONECT 4095 4094                                                                
CONECT 4096 4094 4097 4098                                                      
CONECT 4097 4096                                                                
CONECT 4098 4096 4099 4100                                                      
CONECT 4099 4098                                                                
CONECT 4100 4098 4101 4102                                                      
CONECT 4101 4092 4100                                                           
CONECT 4102 4100 4103                                                           
CONECT 4103 4102                                                                
CONECT 4104 4093 4105                                                           
CONECT 4105 4104 4106                                                           
CONECT 4106 4105 4107                                                           
CONECT 4107 4106 4108                                                           
CONECT 4108 4107 4109                                                           
CONECT 4109 4108 4110                                                           
CONECT 4110 4109 4111                                                           
CONECT 4111 4110                                                                
CONECT 4112 4113 4114 4121                                                      
CONECT 4113 4112 4124                                                           
CONECT 4114 4112 4115 4116                                                      
CONECT 4115 4114                                                                
CONECT 4116 4114 4117 4118                                                      
CONECT 4117 4116                                                                
CONECT 4118 4116 4119 4120                                                      
CONECT 4119 4118                                                                
CONECT 4120 4118 4121 4122                                                      
CONECT 4121 4112 4120                                                           
CONECT 4122 4120 4123                                                           
CONECT 4123 4122                                                                
CONECT 4124 4113 4125                                                           
CONECT 4125 4124 4126                                                           
CONECT 4126 4125 4127                                                           
CONECT 4127 4126 4128                                                           
CONECT 4128 4127 4129                                                           
CONECT 4129 4128 4130                                                           
CONECT 4130 4129 4131                                                           
CONECT 4131 4130                                                                
CONECT 4132 4133 4134 4141                                                      
CONECT 4133 4132 4144                                                           
CONECT 4134 4132 4135 4136                                                      
CONECT 4135 4134                                                                
CONECT 4136 4134 4137 4138                                                      
CONECT 4137 4136                                                                
CONECT 4138 4136 4139 4140                                                      
CONECT 4139 4138                                                                
CONECT 4140 4138 4141 4142                                                      
CONECT 4141 4132 4140                                                           
CONECT 4142 4140 4143                                                           
CONECT 4143 4142                                                                
CONECT 4144 4133 4145                                                           
CONECT 4145 4144 4146                                                           
CONECT 4146 4145 4147                                                           
CONECT 4147 4146 4148                                                           
CONECT 4148 4147 4149                                                           
CONECT 4149 4148 4150                                                           
CONECT 4150 4149 4151                                                           
CONECT 4151 4150                                                                
CONECT 4152 4153 4154 4161                                                      
CONECT 4153 4152 4164                                                           
CONECT 4154 4152 4155 4156                                                      
CONECT 4155 4154                                                                
CONECT 4156 4154 4157 4158                                                      
CONECT 4157 4156                                                                
CONECT 4158 4156 4159 4160                                                      
CONECT 4159 4158                                                                
CONECT 4160 4158 4161 4162                                                      
CONECT 4161 4152 4160                                                           
CONECT 4162 4160 4163                                                           
CONECT 4163 4162                                                                
CONECT 4164 4153 4165                                                           
CONECT 4165 4164 4166                                                           
CONECT 4166 4165 4167                                                           
CONECT 4167 4166 4168                                                           
CONECT 4168 4167 4169                                                           
CONECT 4169 4168 4170                                                           
CONECT 4170 4169 4171                                                           
CONECT 4171 4170                                                                
CONECT 4172 4173 4174 4181                                                      
CONECT 4173 4172 4184                                                           
CONECT 4174 4172 4175 4176                                                      
CONECT 4175 4174                                                                
CONECT 4176 4174 4177 4178                                                      
CONECT 4177 4176                                                                
CONECT 4178 4176 4179 4180                                                      
CONECT 4179 4178                                                                
CONECT 4180 4178 4181 4182                                                      
CONECT 4181 4172 4180                                                           
CONECT 4182 4180 4183                                                           
CONECT 4183 4182                                                                
CONECT 4184 4173 4185                                                           
CONECT 4185 4184 4186                                                           
CONECT 4186 4185 4187                                                           
CONECT 4187 4186 4188                                                           
CONECT 4188 4187 4189                                                           
CONECT 4189 4188 4190                                                           
CONECT 4190 4189 4191                                                           
CONECT 4191 4190                                                                
CONECT 4192 4193                                                                
CONECT 4193 4192 4194                                                           
CONECT 4194 4193 4195                                                           
CONECT 4195 4194 4196                                                           
CONECT 4196 4195 4197                                                           
CONECT 4197 4196 4198                                                           
CONECT 4198 4197 4199                                                           
CONECT 4199 4198 4200                                                           
CONECT 4200 4199 4201                                                           
CONECT 4201 4200 4202                                                           
CONECT 4202 4201 4203                                                           
CONECT 4203 4202 4204                                                           
CONECT 4204 4203 4205                                                           
CONECT 4205 4204                                                                
CONECT 4206 4207 4208 4215                                                      
CONECT 4207 4206 4218                                                           
CONECT 4208 4206 4209 4210                                                      
CONECT 4209 4208                                                                
CONECT 4210 4208 4211 4212                                                      
CONECT 4211 4210                                                                
CONECT 4212 4210 4213 4214                                                      
CONECT 4213 4212                                                                
CONECT 4214 4212 4215 4216                                                      
CONECT 4215 4206 4214                                                           
CONECT 4216 4214 4217                                                           
CONECT 4217 4216                                                                
CONECT 4218 4207 4219                                                           
CONECT 4219 4218 4220                                                           
CONECT 4220 4219 4221                                                           
CONECT 4221 4220 4222                                                           
CONECT 4222 4221 4223                                                           
CONECT 4223 4222 4224                                                           
CONECT 4224 4223 4225                                                           
CONECT 4225 4224                                                                
MASTER      350    0   14   30    2    0   34    6 4327    1  154   40          
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.