CNRS Nantes University UFIP UFIP
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***  erb3  ***

elNémo ID: 22042816094868572

Job options:

ID        	=	 22042816094868572
JOBID     	=	 erb3
USERID    	=	 val
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER erb3

HEADER    TRANSFERASE/IMMUNE SYSTEM               26-JUN-13   4LEO              
TITLE     CRYSTAL STRUCTURE OF ANTI-HER3 FAB RG7116 IN COMPLEX WITH THE         
TITLE    2 EXTRACELLULAR DOMAINS OF HUMAN HER3 (ERBB3)                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RG7116 FAB HEAVY CHAIN;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RG7116 FAB LIGHT CHAIN;                                    
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3;                   
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 20-631;                                       
COMPND  13 SYNONYM: HER3 (ERBB3) EXTRACELLULAR DOMAINS, PROTO-ONCOGENE-LIKE     
COMPND  14 PROTEIN C-ERBB-3, TYROSINE KINASE-TYPE CELL SURFACE RECEPTOR HER3;   
COMPND  15 EC: 2.7.10.1;                                                        
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   9 ORGANISM_COMMON: MOUSE;                                              
SOURCE  10 ORGANISM_TAXID: 10090;                                               
SOURCE  11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: ERBB3, HER3;                                                   
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    FAB FRAGMENT, THERAPEUTIC ANTIBODY, HER3 RECEPTOR, TRANSFERASE-IMMUNE 
KEYWDS   2 SYSTEM COMPLEX                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.B.SCHILLER,K.P.HOPFNER                                              
REVDAT   5   29-JUL-20 4LEO    1       COMPND REMARK SEQADV HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   24-JAN-18 4LEO    1       AUTHOR                                   
REVDAT   3   15-NOV-17 4LEO    1       REMARK                                   
REVDAT   2   28-AUG-13 4LEO    1       JRNL                                     
REVDAT   1   10-JUL-13 4LEO    0                                                
JRNL        AUTH   C.MIRSCHBERGER,C.B.SCHILLER,M.SCHRAML,N.DIMOUDIS,T.FRIESS,   
JRNL        AUTH 2 C.A.GERDES,U.REIFF,V.LIFKE,G.HOELZLWIMMER,I.KOLM,            
JRNL        AUTH 3 K.P.HOPFNER,G.NIEDERFELLNER,B.BOSSENMAIER                    
JRNL        TITL   RG7116, A THERAPEUTIC ANTIBODY THAT BINDS THE INACTIVE HER3  
JRNL        TITL 2 RECEPTOR AND IS OPTIMIZED FOR IMMUNE EFFECTOR ACTIVATION.    
JRNL        REF    CANCER RES.                   V.  73  5183 2013              
JRNL        REFN                   ISSN 0008-5472                               
JRNL        PMID   23780344                                                     
JRNL        DOI    10.1158/0008-5472.CAN-13-0099                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34214                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1710                            
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 48.8300 -  6.0414    0.96     2698   142  0.2048 0.2180        
REMARK   3     2  6.0414 -  4.7966    0.95     2722   143  0.2005 0.2261        
REMARK   3     3  4.7966 -  4.1906    0.96     2656   140  0.1811 0.2166        
REMARK   3     4  4.1906 -  3.8076    0.96     2733   144  0.2041 0.2583        
REMARK   3     5  3.8076 -  3.5348    0.96     2711   142  0.2214 0.2604        
REMARK   3     6  3.5348 -  3.3264    0.97     2739   145  0.2327 0.2556        
REMARK   3     7  3.3264 -  3.1599    0.97     2733   143  0.2561 0.2749        
REMARK   3     8  3.1599 -  3.0224    0.97     2701   143  0.2741 0.2825        
REMARK   3     9  3.0224 -  2.9060    0.95     2715   141  0.2832 0.3281        
REMARK   3    10  2.9060 -  2.8058    0.96     2716   144  0.3002 0.3358        
REMARK   3    11  2.8058 -  2.7180    0.96     2694   141  0.3005 0.3197        
REMARK   3    12  2.7180 -  2.6400    0.93     2686   142  0.3192 0.3421        
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)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           8259                                  
REMARK   3   ANGLE     :  0.764          11172                                  
REMARK   3   CHIRALITY :  0.054           1235                                  
REMARK   3   PLANARITY :  0.004           1454                                  
REMARK   3   DIHEDRAL  : 14.757           2970                                  
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):  19.7348   8.4950 -20.5218              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4435 T22:   0.2906                                     
REMARK   3      T33:   0.2822 T12:  -0.0287                                     
REMARK   3      T13:  -0.0454 T23:  -0.0802                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4813 L22:   0.1959                                     
REMARK   3      L33:   0.2041 L12:   0.0832                                     
REMARK   3      L13:  -0.1984 L23:  -0.0906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0862 S12:  -0.0004 S13:   0.0208                       
REMARK   3      S21:  -0.0132 S22:  -0.0260 S23:   0.0263                       
REMARK   3      S31:   0.0633 S32:  -0.0047 S33:  -0.0542                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SEVERAL ATOMS IN NAG C702 HAS BEEN SET    
REMARK   3  TO ZERO OCCUPANCY BY PURPOSE, SINCE THEY ARE NOT COVERED BY THE     
REMARK   3  2FO-FC DENSITY AT 1.0 ANG SIGMA CONTOUR LEVEL                       
REMARK   4                                                                      
REMARK   4 4LEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080534.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : PH 8.5                             
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY SIDE DIFFRACTING      
REMARK 200                                   SILICON 111 CRYSTAL. FIXED         
REMARK 200                                   WAVELENGTH (0.873)                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.640                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
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) : 2.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM SODIUM TARTRATE          
REMARK 280  TETRAHYDRATE, 20% W/V POLYETHYLENE GLYCOL 3350 , PH PH 8.5,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     SER A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     GLY A   140                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     CYS A   223                                                      
REMARK 465     ASP A   224                                                      
REMARK 465     LYS A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     HIS A   227                                                      
REMARK 465     CYS B   220                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     THR C    20                                                      
REMARK 465     GLY C    21                                                      
REMARK 465     ASP C    22                                                      
REMARK 465     GLY C   612                                                      
REMARK 465     ALA C   613                                                      
REMARK 465     ALA C   614                                                      
REMARK 465     ALA C   615                                                      
REMARK 465     LEU C   616                                                      
REMARK 465     GLU C   617                                                      
REMARK 465     VAL C   618                                                      
REMARK 465     LEU C   619                                                      
REMARK 465     PHE C   620                                                      
REMARK 465     GLN C   621                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A    1   CG   CD   OE1  NE2                                  
REMARK 480     GLN A    3   CD   OE1  NE2                                       
REMARK 480     LYS A   12   NZ                                                  
REMARK 480     LYS A   13   CG   CD   CE   NZ                                   
REMARK 480     LYS A   19   NZ                                                  
REMARK 480     ARG A   30   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN A   62   CD   OE1  NE2                                       
REMARK 480     LYS A   63   CG   CD   CE   NZ                                   
REMARK 480     VAL A   68   CG2                                                 
REMARK 480     ARG A   84   CZ   NH1  NH2                                       
REMARK 480     ARG A   87   NE   CZ   NH1  NH2                                  
REMARK 480     ASP A   89   OD1  OD2                                            
REMARK 480     SER A  122   OG                                                  
REMARK 480     ILE A  202   CD1                                                 
REMARK 480     ASN A  206   OD1  ND2                                            
REMARK 480     LYS A  208   CG   CD   CE   NZ                                   
REMARK 480     ASN A  211   CG   OD1  ND2                                       
REMARK 480     LYS A  213   CG   CD   CE   NZ                                   
REMARK 480     LYS A  216   CD   CE   NZ                                        
REMARK 480     LYS A  217   CD   CE   NZ                                        
REMARK 480     GLU A  219   CD   OE1  OE2                                       
REMARK 480     GLU B   17   OE1  OE2                                            
REMARK 480     LYS B   24   CE   NZ                                             
REMARK 480     GLN B   27   NE2                                                 
REMARK 480     LYS B   51   CE   NZ                                             
REMARK 480     ASP B   76   OD2                                                 
REMARK 480     LYS B  109   CD   CE   NZ                                        
REMARK 480     LYS B  113   NZ                                                  
REMARK 480     ASP B  128   CG   OD1  OD2                                       
REMARK 480     GLU B  129   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  132   CD   CE   NZ                                        
REMARK 480     LYS B  151   CD   CE   NZ                                        
REMARK 480     LYS B  155   CE   NZ                                             
REMARK 480     ASN B  158   CG   OD1  ND2                                       
REMARK 480     GLU B  167   OE1                                                 
REMARK 480     LYS B  175   CD   CE   NZ                                        
REMARK 480     LYS B  189   NZ                                                  
REMARK 480     GLU B  193   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  194   CG   CD   CE   NZ                                   
REMARK 480     LYS B  196   CG   CD   CE   NZ                                   
REMARK 480     GLN B  205   CG   CD   OE1  NE2                                  
REMARK 480     LEU B  207   CD1                                                 
REMARK 480     SER B  208   OG                                                  
REMARK 480     ASN B  216   OD1  ND2                                            
REMARK 480     GLY B  218   O                                                   
REMARK 480     GLU B  219   O    CG   CD   OE1  OE2                             
REMARK 480     LEU C   14   C    CB   CG   CD1  CD2                             
REMARK 480     VAL C   19   CG1  CG2                                            
REMARK 480     ASN C   25   OD1  ND2                                            
REMARK 480     GLN C   26   CG   CD   OE1  NE2                                  
REMARK 480     LEU C   30   CD1  CD2                                            
REMARK 480     TYR C   31   CZ                                                  
REMARK 480     LYS C   32   CG   CD   CE   NZ                                   
REMARK 480     LEU C   33   CD1  CD2                                            
REMARK 480     ARG C   36   CD   NE   CZ   NH1  NH2                             
REMARK 480     MET C   41   SD   CE                                             
REMARK 480     GLU C   74   OE1  OE2                                            
REMARK 480     SER C   76   OG                                                  
REMARK 480     ARG C   84   NH1  NH2                                            
REMARK 480     ASN C  107   CG   OD1  ND2                                       
REMARK 480     SER C  109   OG                                                  
REMARK 480     ARG C  116   NH1  NH2                                            
REMARK 480     GLN C  119   OE1  NE2                                            
REMARK 480     LYS C  135   CE   NZ                                             
REMARK 480     ARG C  149   NE   CZ   NH1  NH2                                  
REMARK 480     ARG C  151   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     SER C  163   OG                                                  
REMARK 480     GLU C  169   CG   CD   OE1  OE2                                  
REMARK 480     LYS C  172   CD   CE   NZ                                        
REMARK 480     GLU C  181   OE1  OE2                                            
REMARK 480     LYS C  188   CB   CG   CD   CE   NZ                              
REMARK 480     THR C  189   OG1  CG2                                            
REMARK 480     ILE C  190   O    CG1  CG2  CD1                                  
REMARK 480     GLN C  194   CD   OE1  NE2                                       
REMARK 480     ASN C  205   ND2                                                 
REMARK 480     ASP C  210   CG   OD1  OD2                                       
REMARK 480     ARG C  239   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLN C  242   CG   CD   OE1  NE2                                  
REMARK 480     LYS C  248   NZ                                                  
REMARK 480     LYS C  260   NZ                                                  
REMARK 480     TYR C  263   OH                                                  
REMARK 480     HIS C  273   N    CB   CG   ND1  CD2  CE1  NE2                   
REMARK 480     ASN C  274   CG   OD1  ND2                                       
REMARK 480     GLN C  279   CG   CD   OE1  NE2                                  
REMARK 480     ARG C  284   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ASP C  289   CB   CG   OD1  OD2                                  
REMARK 480     LYS C  290   CE   NZ                                             
REMARK 480     ASP C  294   N    CA   CB   CG   OD1  OD2                        
REMARK 480     LYS C  295   CD   CE   NZ                                        
REMARK 480     LYS C  299   CE   NZ                                             
REMARK 480     GLU C  302   CD   OE1  OE2                                       
REMARK 480     LYS C  310   NZ                                                  
REMARK 480     GLU C  313   CD   OE1  OE2                                       
REMARK 480     GLN C  322   CD   OE1  NE2                                       
REMARK 480     ILE C  346   CG1  CD1                                            
REMARK 480     TRP C  354   CE3  CZ2  CZ3  CH2                                  
REMARK 480     ILE C  357   CD1                                                 
REMARK 480     GLU C  363   CG   CD   OE1  OE2                                  
REMARK 480     ARG C  372   NE   CZ   NH1  NH2                                  
REMARK 480     ARG C  407   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS C  415   CD   CE   NZ                                        
REMARK 480     ARG C  425   CZ   NH1  NH2                                       
REMARK 480     LYS C  428   CD   CE   NZ                                        
REMARK 480     ARG C  441   NE   CZ   NH1  NH2                                  
REMARK 480     GLN C  442   OE1  NE2                                            
REMARK 480     SER C  448   OG                                                  
REMARK 480     LYS C  453   CG   CD   CE   NZ                                   
REMARK 480     GLU C  460   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  461   CG   CD   OE1  OE2                                  
REMARK 480     LYS C  466   CE   NZ                                             
REMARK 480     ARG C  472   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LEU C  484   CD1  CD2                                            
REMARK 480     ARG C  502   NH1  NH2                                            
REMARK 480     GLU C  520   O    CG   CD   OE1  OE2                             
REMARK 480     GLU C  527   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  529   CD   OE1  OE2                                       
REMARK 480     GLU C  536   OE1  OE2                                            
REMARK 480     GLU C  541   CG   CD   OE1  OE2                                  
REMARK 480     ARG C  561   CZ   NH1  NH2                                       
REMARK 480     HIS C  572   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS C  578   CG   CD   CE   NZ                                   
REMARK 480     VAL C  587   CA   CB   CG1  CG2                                  
REMARK 480     GLN C  588   CD   OE1  NE2                                       
REMARK 480     GLU C  590   CD   OE1  OE2                                       
REMARK 480     ARG C  592   CZ   NH1  NH2                                       
REMARK 480     GLN C  600   CG   CD   OE1  NE2                                  
REMARK 480     LYS C  603   CG   CD   CE   NZ                                   
REMARK 480     GLU C  606   CD   OE1  OE2                                       
REMARK 480     LEU C  611   CD1  CD2                                            
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    ARG C 116   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    LEU C 307   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  31       59.81    -92.01                                   
REMARK 500    ASP A 151       78.12     56.98                                   
REMARK 500    PHE A 153      129.26   -171.33                                   
REMARK 500    ALA B  57      -51.39     74.54                                   
REMARK 500    ALA B  90     -177.66   -171.59                                   
REMARK 500    LYS B 175      -60.48    -95.60                                   
REMARK 500    ASN C  52       49.31   -108.39                                   
REMARK 500    MET C  72       56.81     34.57                                   
REMARK 500    LYS C  95      -35.59   -131.51                                   
REMARK 500    ASN C 107      -57.25   -142.71                                   
REMARK 500    SER C 108      158.23    -46.12                                   
REMARK 500    LEU C 117       59.77   -115.48                                   
REMARK 500    HIS C 138       -3.75     67.15                                   
REMARK 500    ASN C 160     -147.43   -112.79                                   
REMARK 500    ASN C 205       32.29    -99.14                                   
REMARK 500    HIS C 229      -77.97   -132.93                                   
REMARK 500    PRO C 272      179.93    -57.93                                   
REMARK 500    ASN C 274       49.16   -106.54                                   
REMARK 500    GLN C 279     -115.01     59.47                                   
REMARK 500    PHE C 393       47.39   -100.22                                   
REMARK 500    ASN C 406     -120.48     55.50                                   
REMARK 500    ARG C 407       57.52    -90.00                                   
REMARK 500    TYR C 445      -23.68     85.12                                   
REMARK 500    ASN C 468     -160.00    -97.49                                   
REMARK 500    ASN C 503      -81.34   -114.92                                   
REMARK 500    GLU C 536       12.29     81.55                                   
REMARK 500    HIS C 559      -84.23   -105.46                                   
REMARK 500    ASN C 589       14.28     59.27                                   
REMARK 500    GLN C 600      -55.53   -126.36                                   
REMARK 500    CYS C 602      -70.89   -125.82                                   
REMARK 500    LYS C 603      -54.73     66.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     NAG C   702                                                      
DBREF  4LEO C    1   612  UNP    P21860   ERBB3_HUMAN     20    631             
DBREF  4LEO A    1   227  PDB    4LEO     4LEO             1    227             
DBREF  4LEO B    1   220  PDB    4LEO     4LEO             1    220             
SEQADV 4LEO ALA C  613  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO ALA C  614  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO ALA C  615  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO LEU C  616  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO GLU C  617  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO VAL C  618  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO LEU C  619  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO PHE C  620  UNP  P21860              EXPRESSION TAG                 
SEQADV 4LEO GLN C  621  UNP  P21860              EXPRESSION TAG                 
SEQRES   1 A  227  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 A  227  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 A  227  TYR THR PHE ARG SER SER TYR ILE SER TRP VAL ARG GLN          
SEQRES   4 A  227  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE TYR          
SEQRES   5 A  227  ALA GLY THR GLY SER PRO SER TYR ASN GLN LYS LEU GLN          
SEQRES   6 A  227  GLY ARG VAL THR MET THR THR ASP THR SER THR SER THR          
SEQRES   7 A  227  ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR          
SEQRES   8 A  227  ALA VAL TYR TYR CYS ALA ARG HIS ARG ASP TYR TYR SER          
SEQRES   9 A  227  ASN SER LEU THR TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 A  227  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 A  227  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 A  227  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 A  227  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 A  227  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 A  227  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 A  227  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 A  227  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 A  227  SER CYS ASP LYS THR HIS                                      
SEQRES   1 B  220  ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL          
SEQRES   2 B  220  SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER          
SEQRES   3 B  220  GLN SER VAL LEU ASN SER GLY ASN GLN LYS ASN TYR LEU          
SEQRES   4 B  220  THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU          
SEQRES   5 B  220  LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO          
SEQRES   6 B  220  ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 B  220  LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL          
SEQRES   8 B  220  TYR TYR CYS GLN SER ASP TYR SER TYR PRO TYR THR PHE          
SEQRES   9 B  220  GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 B  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 B  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 B  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 B  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 B  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 B  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 B  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 B  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
SEQRES   1 C  621  SER GLU VAL GLY ASN SER GLN ALA VAL CYS PRO GLY THR          
SEQRES   2 C  621  LEU ASN GLY LEU SER VAL THR GLY ASP ALA GLU ASN GLN          
SEQRES   3 C  621  TYR GLN THR LEU TYR LYS LEU TYR GLU ARG CYS GLU VAL          
SEQRES   4 C  621  VAL MET GLY ASN LEU GLU ILE VAL LEU THR GLY HIS ASN          
SEQRES   5 C  621  ALA ASP LEU SER PHE LEU GLN TRP ILE ARG GLU VAL THR          
SEQRES   6 C  621  GLY TYR VAL LEU VAL ALA MET ASN GLU PHE SER THR LEU          
SEQRES   7 C  621  PRO LEU PRO ASN LEU ARG VAL VAL ARG GLY THR GLN VAL          
SEQRES   8 C  621  TYR ASP GLY LYS PHE ALA ILE PHE VAL MET LEU ASN TYR          
SEQRES   9 C  621  ASN THR ASN SER SER HIS ALA LEU ARG GLN LEU ARG LEU          
SEQRES  10 C  621  THR GLN LEU THR GLU ILE LEU SER GLY GLY VAL TYR ILE          
SEQRES  11 C  621  GLU LYS ASN ASP LYS LEU CYS HIS MET ASP THR ILE ASP          
SEQRES  12 C  621  TRP ARG ASP ILE VAL ARG ASP ARG ASP ALA GLU ILE VAL          
SEQRES  13 C  621  VAL LYS ASP ASN GLY ARG SER CYS PRO PRO CYS HIS GLU          
SEQRES  14 C  621  VAL CYS LYS GLY ARG CYS TRP GLY PRO GLY SER GLU ASP          
SEQRES  15 C  621  CYS GLN THR LEU THR LYS THR ILE CYS ALA PRO GLN CYS          
SEQRES  16 C  621  ASN GLY HIS CYS PHE GLY PRO ASN PRO ASN GLN CYS CYS          
SEQRES  17 C  621  HIS ASP GLU CYS ALA GLY GLY CYS SER GLY PRO GLN ASP          
SEQRES  18 C  621  THR ASP CYS PHE ALA CYS ARG HIS PHE ASN ASP SER GLY          
SEQRES  19 C  621  ALA CYS VAL PRO ARG CYS PRO GLN PRO LEU VAL TYR ASN          
SEQRES  20 C  621  LYS LEU THR PHE GLN LEU GLU PRO ASN PRO HIS THR LYS          
SEQRES  21 C  621  TYR GLN TYR GLY GLY VAL CYS VAL ALA SER CYS PRO HIS          
SEQRES  22 C  621  ASN PHE VAL VAL ASP GLN THR SER CYS VAL ARG ALA CYS          
SEQRES  23 C  621  PRO PRO ASP LYS MET GLU VAL ASP LYS ASN GLY LEU LYS          
SEQRES  24 C  621  MET CYS GLU PRO CYS GLY GLY LEU CYS PRO LYS ALA CYS          
SEQRES  25 C  621  GLU GLY THR GLY SER GLY SER ARG PHE GLN THR VAL ASP          
SEQRES  26 C  621  SER SER ASN ILE ASP GLY PHE VAL ASN CYS THR LYS ILE          
SEQRES  27 C  621  LEU GLY ASN LEU ASP PHE LEU ILE THR GLY LEU ASN GLY          
SEQRES  28 C  621  ASP PRO TRP HIS LYS ILE PRO ALA LEU ASP PRO GLU LYS          
SEQRES  29 C  621  LEU ASN VAL PHE ARG THR VAL ARG GLU ILE THR GLY TYR          
SEQRES  30 C  621  LEU ASN ILE GLN SER TRP PRO PRO HIS MET HIS ASN PHE          
SEQRES  31 C  621  SER VAL PHE SER ASN LEU THR THR ILE GLY GLY ARG SER          
SEQRES  32 C  621  LEU TYR ASN ARG GLY PHE SER LEU LEU ILE MET LYS ASN          
SEQRES  33 C  621  LEU ASN VAL THR SER LEU GLY PHE ARG SER LEU LYS GLU          
SEQRES  34 C  621  ILE SER ALA GLY ARG ILE TYR ILE SER ALA ASN ARG GLN          
SEQRES  35 C  621  LEU CYS TYR HIS HIS SER LEU ASN TRP THR LYS VAL LEU          
SEQRES  36 C  621  ARG GLY PRO THR GLU GLU ARG LEU ASP ILE LYS HIS ASN          
SEQRES  37 C  621  ARG PRO ARG ARG ASP CYS VAL ALA GLU GLY LYS VAL CYS          
SEQRES  38 C  621  ASP PRO LEU CYS SER SER GLY GLY CYS TRP GLY PRO GLY          
SEQRES  39 C  621  PRO GLY GLN CYS LEU SER CYS ARG ASN TYR SER ARG GLY          
SEQRES  40 C  621  GLY VAL CYS VAL THR HIS CYS ASN PHE LEU ASN GLY GLU          
SEQRES  41 C  621  PRO ARG GLU PHE ALA HIS GLU ALA GLU CYS PHE SER CYS          
SEQRES  42 C  621  HIS PRO GLU CYS GLN PRO MET GLU GLY THR ALA THR CYS          
SEQRES  43 C  621  ASN GLY SER GLY SER ASP THR CYS ALA GLN CYS ALA HIS          
SEQRES  44 C  621  PHE ARG ASP GLY PRO HIS CYS VAL SER SER CYS PRO HIS          
SEQRES  45 C  621  GLY VAL LEU GLY ALA LYS GLY PRO ILE TYR LYS TYR PRO          
SEQRES  46 C  621  ASP VAL GLN ASN GLU CYS ARG PRO CYS HIS GLU ASN CYS          
SEQRES  47 C  621  THR GLN GLY CYS LYS GLY PRO GLU LEU GLN ASP CYS LEU          
SEQRES  48 C  621  GLY ALA ALA ALA LEU GLU VAL LEU PHE GLN                      
MODRES 4LEO ASN C  334  ASN  GLYCOSYLATION SITE                                 
MODRES 4LEO ASN C  418  ASN  GLYCOSYLATION SITE                                 
MODRES 4LEO ASN C  389  ASN  GLYCOSYLATION SITE                                 
MODRES 4LEO ASN C  231  ASN  GLYCOSYLATION SITE                                 
MODRES 4LEO ASN C  395  ASN  GLYCOSYLATION SITE                                 
MODRES 4LEO ASN C  597  ASN  GLYCOSYLATION SITE                                 
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  C 701      14                                                       
HET    NAG  C 702      14                                                       
HET    NAG  C 705      14                                                       
HET    NAG  C 706      14                                                       
HET    NAG  C 707      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   4  NAG    7(C8 H15 N O6)                                               
FORMUL  10  HOH   *150(H2 O)                                                    
HELIX    1   1 GLU C   24  GLU C   35  1                                  12
HELIX    2   2 LEU C   55  GLN C   59  1                                   5
HELIX    3   3 VAL C   91  GLY C   94  1                                   4
HELIX    4   4 ASP C  143  ILE C  147  1                                   5
HELIX    5   5 HIS C  168  LYS C  172  1                                   5
HELIX    6   6 ASN C  328  VAL C  333  1                                   6
HELIX    7   7 LEU C  345  GLY C  351  1                                   7
HELIX    8   8 ASP C  361  VAL C  371  1                                  11
HELIX    9   9 PHE C  390  SER C  394  1                                   5
HELIX   10  10 TYR C  445  LEU C  455  1                                  11
HELIX   11  11 PRO C  470  GLU C  477  1                                   8
HELIX   12  12 GLU C  606  CYS C  610  1                                   5
SHEET    1   1 1 VAL C   9  PRO C  11  0
SHEET    2   2 1 VAL C  39  MET C  41  0
SHEET    3   3 1 LEU C  44  VAL C  47  0
SHEET    4   4 1 GLU C  63  VAL C  64  0
SHEET    5   5 1 VAL C  68  ALA C  71  0
SHEET    6   6 1 THR C  77  PRO C  79  0
SHEET    7   7 1 VAL C  85  VAL C  86  0
SHEET    8   8 1 PHE C  96  MET C 101  0
SHEET    9   9 1 GLN C 114  ARG C 116  0
SHEET   10  10 1 GLU C 122  ILE C 123  0
SHEET   11  11 1 GLY C 127  GLU C 131  0
SHEET   12  12 1 ILE C 155  LYS C 158  0
SHEET   13  13 1 PHE C 230  ASP C 232  0
SHEET   14  14 1 ALA C 235  VAL C 237  0
SHEET   15  15 1 LEU C 244  ASN C 247  0
SHEET   16  16 1 GLN C 252  PRO C 255  0
SHEET   17  17 1 TYR C 261  TYR C 263  0
SHEET   18  18 1 VAL C 266  VAL C 268  0
SHEET   19  19 1 VAL C 276  ASP C 278  0
SHEET   20  20 1 SER C 281  VAL C 283  0
SHEET   21  21 1 LYS C 290  LYS C 295  0
SHEET   22  22 1 LEU C 298  PRO C 303  0
SHEET   23  23 1 ALA C 311  GLU C 313  0
SHEET   24  24 1 LYS C 337  LEU C 339  0
SHEET   25  25 1 LEU C 342  PHE C 344  0
SHEET   26  26 1 GLU C 373  ILE C 374  0
SHEET   27  27 1 LEU C 378  ILE C 380  0
SHEET   28  28 1 THR C 398  ILE C 399  0
SHEET   29  29 1 PHE C 409  MET C 414  0
SHEET   30  30 1 GLU C 429  ILE C 430  0
SHEET   31  31 1 ARG C 434  SER C 438  0
SHEET   32  32 1 LEU C 463  LYS C 466  0
SHEET   33  33 1 TYR C 504  SER C 505  0
SHEET   34  34 1 CYS C 510  VAL C 511  0
SHEET   35  35 1 GLU C 523  ALA C 525  0
SHEET   36  36 1 CYS C 530  SER C 532  0
SHEET   37  37 1 PHE C 560  ASP C 562  0
SHEET   38  38 1 HIS C 565  VAL C 567  0
SHEET   39  39 1 HIS C 572  LEU C 575  0
SHEET   40  40 1 PRO C 580  PRO C 585  0
SHEET   41  41 1 CYS C 591  PRO C 593  0
SSBOND   1 CYS A   22    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  147    CYS A  203                          1555   1555  2.03  
SSBOND   3 CYS B   23    CYS B   94                          1555   1555  2.03  
SSBOND   4 CYS B  140    CYS B  200                          1555   1555  2.03  
SSBOND   5 CYS C   10    CYS C   37                          1555   1555  2.00  
SSBOND   6 CYS C  137    CYS C  164                          1555   1555  2.03  
SSBOND   7 CYS C  167    CYS C  175                          1555   1555  2.03  
SSBOND   8 CYS C  171    CYS C  183                          1555   1555  2.03  
SSBOND   9 CYS C  191    CYS C  199                          1555   1555  2.03  
SSBOND  10 CYS C  195    CYS C  207                          1555   1555  2.02  
SSBOND  11 CYS C  208    CYS C  216                          1555   1555  2.03  
SSBOND  12 CYS C  212    CYS C  224                          1555   1555  2.03  
SSBOND  13 CYS C  227    CYS C  236                          1555   1555  2.03  
SSBOND  14 CYS C  240    CYS C  267                          1555   1555  2.03  
SSBOND  15 CYS C  271    CYS C  282                          1555   1555  2.03  
SSBOND  16 CYS C  286    CYS C  301                          1555   1555  2.03  
SSBOND  17 CYS C  304    CYS C  308                          1555   1555  2.04  
SSBOND  18 CYS C  312    CYS C  335                          1555   1555  2.03  
SSBOND  19 CYS C  444    CYS C  474                          1555   1555  2.01  
SSBOND  20 CYS C  481    CYS C  490                          1555   1555  2.03  
SSBOND  21 CYS C  485    CYS C  498                          1555   1555  2.03  
SSBOND  22 CYS C  501    CYS C  510                          1555   1555  2.03  
SSBOND  23 CYS C  514    CYS C  530                          1555   1555  2.03  
SSBOND  24 CYS C  533    CYS C  546                          1555   1555  2.01  
SSBOND  25 CYS C  537    CYS C  554                          1555   1555  2.02  
SSBOND  26 CYS C  557    CYS C  566                          1555   1555  2.03  
SSBOND  27 CYS C  570    CYS C  591                          1555   1555  2.03  
SSBOND  28 CYS C  594    CYS C  602                          1555   1555  2.03  
SSBOND  29 CYS C  598    CYS C  610                          1555   1555  2.03  
LINK         ND2 ASN C 231                 C1  NAG C 701     1555   1555  1.44  
LINK         ND2 ASN C 334                 C1  NAG C 702     1555   1555  1.43  
LINK         ND2 ASN C 389                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN C 395                 C1  NAG C 705     1555   1555  1.44  
LINK         ND2 ASN C 418                 C1  NAG C 706     1555   1555  1.44  
LINK         ND2 ASN C 597                 C1  NAG C 707     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.45  
CISPEP   1 PHE A  153    PRO A  154          0        -0.92                     
CISPEP   2 GLU A  155    PRO A  156          0        -1.55                     
CISPEP   3 SER B    7    PRO B    8          0         0.02                     
CISPEP   4 TYR B  100    PRO B  101          0         0.12                     
CISPEP   5 TYR B  146    PRO B  147          0        -2.24                     
CISPEP   6 GLU C   35    ARG C   36          0        -2.26                     
CISPEP   7 GLU C  520    PRO C  521          0        -0.73                     
CRYST1   54.458   59.359  103.661  97.64 106.85  96.83 P 1           1          
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      0.018363  0.002200  0.006042        0.00000                         
SCALE2      0.000000  0.016967  0.003038        0.00000                         
SCALE3      0.000000  0.000000  0.010240        0.00000                         
ATOM      1  N   ALA C   8      29.574  34.781 -25.373  1.00 53.56           N
ANISOU    1  N   ALA C   8     7354   6031   6967   -138    561   -800       N
ATOM      2  CA  ALA C   8      28.368  34.957 -26.174  1.00 54.37           C
ANISOU    2  CA  ALA C   8     7446   6124   7088   -106    568   -745       C
ATOM      3  C   ALA C   8      27.674  33.618 -26.416  1.00 54.98           C
ANISOU    3  C   ALA C   8     7549   6236   7104    -94    496   -728       C
ATOM      4  O   ALA C   8      26.454  33.519 -26.321  1.00 55.54           O
ANISOU    4  O   ALA C   8     7617   6304   7181    -94    493   -709       O
ATOM      5  CB  ALA C   8      28.703  35.629 -27.497  1.00 55.25           C
ANISOU    5  CB  ALA C   8     7538   6224   7229    -61    595   -695       C
ATOM      6  N   VAL C   9      28.455  32.591 -26.732  1.00 61.51           N
ANISOU    6  N   VAL C   9     8400   7097   7874    -85    441   -733       N
ATOM      7  CA  VAL C   9      27.895  31.266 -26.982  1.00 61.53           C
ANISOU    7  CA  VAL C   9     8428   7131   7819    -75    374   -720       C
ATOM      8  C   VAL C   9      28.609  30.186 -26.164  1.00 60.77           C
ANISOU    8  C   VAL C   9     8360   7060   7671   -101    325   -764       C
ATOM      9  O   VAL C   9      29.829  30.071 -26.203  1.00 60.87           O
ANISOU    9  O   VAL C   9     8376   7081   7670   -100    319   -781       O
ATOM     10  CB  VAL C   9      27.910  30.915 -28.489  1.00 62.46           C
ANISOU   10  CB  VAL C   9     8549   7269   7915    -27    348   -670       C
ATOM     11  CG1 VAL C   9      29.287  31.191 -29.093  1.00 62.89           C
ANISOU   11  CG1 VAL C   9     8601   7326   7970     -8    360   -671       C
ATOM     12  CG2 VAL C   9      27.489  29.471 -28.703  1.00 62.40           C
ANISOU   12  CG2 VAL C   9     8571   7294   7845    -21    278   -666       C
ATOM     13  N   CYS C  10      27.844  29.399 -25.413  1.00 63.45           N
ANISOU   13  N   CYS C  10     8715   7410   7983   -123    292   -778       N
ATOM     14  CA  CYS C  10      28.414  28.358 -24.554  1.00 62.43           C
ANISOU   14  CA  CYS C  10     8610   7304   7807   -149    247   -815       C
ATOM     15  C   CYS C  10      27.846  26.976 -24.856  1.00 62.43           C
ANISOU   15  C   CYS C  10     8636   7328   7755   -137    183   -800       C
ATOM     16  O   CYS C  10      26.718  26.856 -25.335  1.00 62.77           O
ANISOU   16  O   CYS C  10     8678   7370   7802   -124    175   -770       O
ATOM     17  CB  CYS C  10      28.148  28.708 -23.085  1.00 61.57           C
ANISOU   17  CB  CYS C  10     8496   7186   7713   -198    270   -857       C
ATOM     18  SG  CYS C  10      26.510  29.406 -22.768  1.00 71.27           S
ANISOU   18  SG  CYS C  10     9708   8388   8984   -208    308   -844       S
ATOM     19  N   PRO C  11      28.636  25.929 -24.583  1.00 56.40           N
ANISOU   19  N   PRO C  11     7895   6588   6948   -143    138   -819       N
ATOM     20  CA  PRO C  11      28.211  24.530 -24.721  1.00 56.24           C
ANISOU   20  CA  PRO C  11     7901   6587   6879   -137     78   -811       C
ATOM     21  C   PRO C  11      27.227  24.046 -23.643  1.00 55.97           C
ANISOU   21  C   PRO C  11     7876   6555   6835   -170     62   -826       C
ATOM     22  O   PRO C  11      27.051  24.722 -22.628  1.00 55.71           O
ANISOU   22  O   PRO C  11     7830   6511   6826   -202     95   -850       O
ATOM     23  CB  PRO C  11      29.527  23.758 -24.593  1.00 55.63           C
ANISOU   23  CB  PRO C  11     7840   6528   6768   -135     48   -830       C
ATOM     24  CG  PRO C  11      30.572  24.723 -25.014  1.00 56.19           C
ANISOU   24  CG  PRO C  11     7893   6592   6867   -123     86   -831       C
ATOM     25  CD  PRO C  11      30.102  26.051 -24.507  1.00 56.56           C
ANISOU   25  CD  PRO C  11     7913   6614   6963   -144    143   -839       C
ATOM     26  N   GLY C  12      26.612  22.882 -23.869  1.00 60.88           N
ANISOU   26  N   GLY C  12     8519   7190   7422   -163     14   -814       N
ATOM     27  CA  GLY C  12      25.644  22.300 -22.945  1.00 60.38           C
ANISOU   27  CA  GLY C  12     8465   7129   7347   -191     -6   -824       C
ATOM     28  C   GLY C  12      26.210  21.080 -22.228  1.00 59.59           C
ANISOU   28  C   GLY C  12     8389   7048   7205   -207    -51   -844       C
ATOM     29  O   GLY C  12      27.210  20.512 -22.674  1.00 59.26           O
ANISOU   29  O   GLY C  12     8359   7017   7141   -189    -74   -845       O
ATOM     30  N   THR C  13      25.571  20.655 -21.139  1.00 70.96           N
ANISOU   30  N   THR C  13     9835   8491   8635   -239    -62   -859       N
ATOM     31  CA  THR C  13      26.233  19.748 -20.191  1.00 70.87           C
ANISOU   31  CA  THR C  13     9839   8498   8591   -261    -94   -880       C
ATOM     32  C   THR C  13      26.110  18.232 -20.464  1.00 70.65           C
ANISOU   32  C   THR C  13     9837   8480   8525   -249   -150   -868       C
ATOM     33  O   THR C  13      27.040  17.468 -20.178  1.00 70.51           O
ANISOU   33  O   THR C  13     9833   8476   8483   -249   -176   -876       O
ATOM     34  CB  THR C  13      25.871  20.095 -18.718  1.00 71.11           C
ANISOU   34  CB  THR C  13     9861   8531   8627   -306    -75   -906       C
ATOM     35  OG1 THR C  13      27.004  19.847 -17.881  1.00 71.19           O
ANISOU   35  OG1 THR C  13     9873   8561   8616   -326    -84   -930       O
ATOM     36  CG2 THR C  13      24.683  19.281 -18.220  1.00 71.17           C
ANISOU   36  CG2 THR C  13     9882   8541   8619   -321   -101   -900       C
ATOM     37  N   LEU C  14      24.966  17.815 -21.003  1.00 55.20           N
ANISOU   37  N   LEU C  14     7890   6518   6567   -239   -166   -848       N
ATOM     38  CA  LEU C  14      24.735  16.432 -21.442  1.00 54.91           C
ANISOU   38  CA  LEU C  14     7878   6487   6499   -226   -216   -837       C
ATOM     39  C   LEU C  14      24.612  15.382 -20.329  0.00 54.47           C
ANISOU   39  C   LEU C  14     7838   6439   6419   -253   -247   -848       C
ATOM     40  O   LEU C  14      24.442  14.197 -20.617  1.00 54.25           O
ANISOU   40  O   LEU C  14     7831   6413   6369   -245   -285   -840       O
ATOM     41  CB  LEU C  14      25.783  15.979 -22.476  0.00 53.14           C
ANISOU   41  CB  LEU C  14     7664   6267   6259   -193   -233   -830       C
ATOM     42  CG  LEU C  14      25.303  15.473 -23.846  0.00 53.30           C
ANISOU   42  CG  LEU C  14     7696   6286   6268   -163   -254   -809       C
ATOM     43  CD1 LEU C  14      26.400  14.655 -24.515  0.00 53.13           C
ANISOU   43  CD1 LEU C  14     7693   6270   6223   -138   -278   -811       C
ATOM     44  CD2 LEU C  14      23.988  14.682 -23.788  0.00 53.16           C
ANISOU   44  CD2 LEU C  14     7691   6268   6240   -174   -282   -801       C
ATOM     45  N   ASN C  15      24.693  15.790 -19.067  1.00 74.37           N
ANISOU   45  N   ASN C  15    10348   8966   8944   -286   -229   -866       N
ATOM     46  CA  ASN C  15      24.468  14.832 -17.987  1.00 74.35           C
ANISOU   46  CA  ASN C  15    10358   8974   8919   -312   -256   -872       C
ATOM     47  C   ASN C  15      22.971  14.637 -17.757  1.00 74.32           C
ANISOU   47  C   ASN C  15    10356   8962   8921   -327   -260   -863       C
ATOM     48  O   ASN C  15      22.161  15.026 -18.596  1.00 74.80           O
ANISOU   48  O   ASN C  15    10411   9011   8999   -312   -251   -849       O
ATOM     49  CB  ASN C  15      25.193  15.249 -16.703  1.00 74.47           C
ANISOU   49  CB  ASN C  15    10362   9005   8929   -344   -240   -895       C
ATOM     50  CG  ASN C  15      26.699  15.350 -16.891  1.00 74.79           C
ANISOU   50  CG  ASN C  15    10398   9056   8962   -331   -240   -903       C
ATOM     51  OD1 ASN C  15      27.377  14.346 -17.119  1.00 74.85           O
ANISOU   51  OD1 ASN C  15    10420   9070   8948   -314   -273   -894       O
ATOM     52  ND2 ASN C  15      27.229  16.565 -16.789  1.00 74.82           N
ANISOU   52  ND2 ASN C  15    10382   9060   8987   -338   -200   -919       N
ATOM     53  N   GLY C  16      22.603  14.024 -16.637  1.00 55.65           N
ANISOU   53  N   GLY C  16     7999   6606   6541   -357   -275   -870       N
ATOM     54  CA  GLY C  16      21.201  13.826 -16.315  1.00 55.60           C
ANISOU   54  CA  GLY C  16     7993   6593   6541   -373   -278   -862       C
ATOM     55  C   GLY C  16      20.892  14.343 -14.928  1.00 56.03           C
ANISOU   55  C   GLY C  16     8035   6657   6599   -413   -253   -880       C
ATOM     56  O   GLY C  16      21.107  15.519 -14.634  1.00 56.52           O
ANISOU   56  O   GLY C  16     8078   6718   6680   -423   -211   -896       O
ATOM     57  N   LEU C  17      20.384  13.466 -14.070  1.00 60.69           N
ANISOU   57  N   LEU C  17     8636   7254   7169   -435   -276   -877       N
ATOM     58  CA  LEU C  17      20.206  13.809 -12.669  1.00 60.53           C
ANISOU   58  CA  LEU C  17     8606   7248   7143   -475   -256   -895       C
ATOM     59  C   LEU C  17      21.467  13.399 -11.925  1.00 60.76           C
ANISOU   59  C   LEU C  17     8639   7302   7144   -486   -271   -906       C
ATOM     60  O   LEU C  17      21.566  13.548 -10.706  1.00 60.95           O
ANISOU   60  O   LEU C  17     8657   7347   7154   -520   -261   -922       O
ATOM     61  CB  LEU C  17      18.974  13.114 -12.085  1.00 60.31           C
ANISOU   61  CB  LEU C  17     8586   7220   7110   -494   -271   -885       C
ATOM     62  CG  LEU C  17      17.614  13.513 -12.668  1.00 60.35           C
ANISOU   62  CG  LEU C  17     8582   7203   7143   -488   -256   -872       C
ATOM     63  CD1 LEU C  17      17.601  14.977 -13.079  1.00 60.23           C
ANISOU   63  CD1 LEU C  17     8546   7178   7162   -481   -208   -882       C
ATOM     64  CD2 LEU C  17      17.227  12.624 -13.835  1.00 60.57           C
ANISOU   64  CD2 LEU C  17     8626   7220   7169   -459   -293   -848       C
ATOM     65  N   SER C  18      22.433  12.887 -12.682  1.00 75.01           N
ANISOU   65  N   SER C  18    10454   9107   8940   -457   -295   -897       N
ATOM     66  CA  SER C  18      23.705  12.456 -12.125  1.00 75.20           C
ANISOU   66  CA  SER C  18    10480   9155   8939   -461   -311   -902       C
ATOM     67  C   SER C  18      24.543  13.644 -11.709  1.00 74.95           C
ANISOU   67  C   SER C  18    10427   9137   8914   -476   -275   -927       C
ATOM     68  O   SER C  18      24.690  14.614 -12.453  1.00 74.92           O
ANISOU   68  O   SER C  18    10413   9119   8936   -461   -246   -935       O
ATOM     69  CB  SER C  18      24.492  11.633 -13.144  1.00 75.24           C
ANISOU   69  CB  SER C  18    10499   9151   8937   -423   -342   -885       C
ATOM     70  OG  SER C  18      23.756  10.505 -13.571  1.00 75.03           O
ANISOU   70  OG  SER C  18    10493   9110   8906   -410   -374   -865       O
ATOM     71  N   VAL C  19      25.102  13.555 -10.509  1.00 82.40           N
ANISOU   71  N   VAL C  19    11363  10111   9833   -507   -277   -940       N
ATOM     72  CA  VAL C  19      26.056  14.546 -10.045  1.00 82.50           C
ANISOU   72  CA  VAL C  19    11357  10144   9847   -525   -248   -966       C
ATOM     73  C   VAL C  19      27.452  13.940  -9.992  1.00 82.67           C
ANISOU   73  C   VAL C  19    11378  10188   9844   -515   -276   -959       C
ATOM     74  O   VAL C  19      27.664  12.920  -9.339  1.00 82.80           O
ANISOU   74  O   VAL C  19    11402  10226   9832   -523   -309   -944       O
ATOM     75  CB  VAL C  19      25.682  15.083  -8.656  1.00 79.37           C
ANISOU   75  CB  VAL C  19    10947   9770   9439   -575   -224   -992       C
ATOM     76  CG1 VAL C  19      26.833  15.887  -8.079  0.00 79.48           C
ANISOU   76  CG1 VAL C  19    10942   9812   9445   -598   -202  -1020       C
ATOM     77  CG2 VAL C  19      24.412  15.923  -8.740  0.00 79.27           C
ANISOU   77  CG2 VAL C  19    10930   9731   9457   -585   -186  -1002       C
ATOM     78  N   ALA C  23      29.821  18.751  -3.909  1.00102.66           N
ANISOU   78  N   ALA C  23    13796  12903  12307   -776   -114  -1165       N
ATOM     79  CA  ALA C  23      28.808  19.786  -3.756  1.00102.23           C
ANISOU   79  CA  ALA C  23    13738  12819  12283   -797    -61  -1196       C
ATOM     80  C   ALA C  23      29.305  21.148  -4.244  1.00102.17           C
ANISOU   80  C   ALA C  23    13715  12789  12317   -799    -11  -1229       C
ATOM     81  O   ALA C  23      28.617  21.826  -5.001  1.00102.26           O
ANISOU   81  O   ALA C  23    13727  12753  12375   -780     23  -1230       O
ATOM     82  CB  ALA C  23      28.351  19.873  -2.307  1.00101.99           C
ANISOU   82  CB  ALA C  23    13704  12828  12221   -853    -50  -1223       C
ATOM     83  N   GLU C  24      30.493  21.552  -3.807  1.00 92.66           N
ANISOU   83  N   GLU C  24    12492  11619  11095   -824     -6  -1255       N
ATOM     84  CA  GLU C  24      31.001  22.870  -4.165  1.00 92.07           C
ANISOU   84  CA  GLU C  24    12399  11523  11059   -832     44  -1290       C
ATOM     85  C   GLU C  24      31.514  22.921  -5.615  1.00 92.22           C
ANISOU   85  C   GLU C  24    12420  11505  11113   -777     39  -1263       C
ATOM     86  O   GLU C  24      31.218  23.870  -6.349  1.00 92.01           O
ANISOU   86  O   GLU C  24    12389  11434  11135   -762     83  -1272       O
ATOM     87  CB  GLU C  24      32.035  23.363  -3.134  1.00 91.64           C
ANISOU   87  CB  GLU C  24    12324  11521  10976   -885     55  -1333       C
ATOM     88  CG  GLU C  24      32.565  24.782  -3.348  1.00 91.35           C
ANISOU   88  CG  GLU C  24    12266  11463  10978   -903    113  -1377       C
ATOM     89  CD  GLU C  24      31.492  25.768  -3.785  1.00 91.02           C
ANISOU   89  CD  GLU C  24    12226  11361  10994   -897    172  -1393       C
ATOM     90  OE1 GLU C  24      30.331  25.649  -3.328  1.00 90.90           O
ANISOU   90  OE1 GLU C  24    12222  11337  10978   -909    182  -1394       O
ATOM     91  OE2 GLU C  24      31.815  26.668  -4.594  1.00 90.93           O
ANISOU   91  OE2 GLU C  24    12206  11313  11032   -879    209  -1401       O
ATOM     92  N   ASN C  25      32.242  21.884  -6.029  1.00113.94           N
ANISOU   92  N   ASN C  25    15179  14274  13838   -746    -13  -1227       N
ATOM     93  CA  ASN C  25      32.698  21.743  -7.414  1.00114.41           C
ANISOU   93  CA  ASN C  25    15244  14303  13925   -692    -24  -1197       C
ATOM     94  C   ASN C  25      31.565  21.821  -8.432  1.00114.40           C
ANISOU   94  C   ASN C  25    15257  14248  13960   -654    -11  -1174       C
ATOM     95  O   ASN C  25      31.707  22.463  -9.473  1.00114.49           O
ANISOU   95  O   ASN C  25    15265  14226  14010   -624     13  -1169       O
ATOM     96  CB  ASN C  25      33.483  20.436  -7.594  1.00114.79           C
ANISOU   96  CB  ASN C  25    15300  14378  13936   -665    -84  -1160       C
ATOM     97  CG  ASN C  25      33.535  19.967  -9.044  1.00114.94           C
ANISOU   97  CG  ASN C  25    15335  14361  13978   -605   -101  -1123       C
ATOM     98  OD1 ASN C  25      34.483  20.264  -9.769  0.00115.19           O
ANISOU   98  OD1 ASN C  25    15357  14386  14024   -582    -96  -1120       O
ATOM     99  ND2 ASN C  25      32.523  19.208  -9.461  0.00114.80           N
ANISOU   99  ND2 ASN C  25    15339  14321  13961   -580   -123  -1095       N
ATOM    100  N   GLN C  26      30.448  21.162  -8.132  1.00 81.37           N
ANISOU  100  N   GLN C  26    11091  10062   9765   -656    -28  -1159       N
ATOM    101  CA  GLN C  26      29.318  21.128  -9.058  1.00 80.95           C
ANISOU  101  CA  GLN C  26    11050   9964   9743   -622    -22  -1134       C
ATOM    102  C   GLN C  26      28.817  22.527  -9.390  1.00 80.54           C
ANISOU  102  C   GLN C  26    10984   9876   9742   -626     40  -1155       C
ATOM    103  O   GLN C  26      28.486  22.827 -10.540  1.00 80.62           O
ANISOU  103  O   GLN C  26    10996   9850   9787   -588     52  -1134       O
ATOM    104  CB  GLN C  26      28.182  20.256  -8.513  1.00 80.77           C
ANISOU  104  CB  GLN C  26    11043   9946   9698   -631    -47  -1119       C
ATOM    105  CG  GLN C  26      27.059  19.986  -9.509  0.00 80.78           C
ANISOU  105  CG  GLN C  26    11059   9908   9725   -594    -52  -1088       C
ATOM    106  CD  GLN C  26      27.519  19.228 -10.749  0.00 80.82           C
ANISOU  106  CD  GLN C  26    11077   9902   9729   -544    -89  -1053       C
ATOM    107  OE1 GLN C  26      28.683  18.842 -10.875  0.00 80.88           O
ANISOU  107  OE1 GLN C  26    11084   9929   9718   -534   -112  -1049       O
ATOM    108  NE2 GLN C  26      26.593  19.008 -11.672  0.00 80.83           N
ANISOU  108  NE2 GLN C  26    11089   9874   9749   -514    -94  -1027       N
ATOM    109  N   TYR C  27      28.785  23.387  -8.379  1.00 72.96           N
ANISOU  109  N   TYR C  27    10009   8926   8786   -673     80  -1197       N
ATOM    110  CA  TYR C  27      28.432  24.780  -8.596  1.00 72.67           C
ANISOU  110  CA  TYR C  27     9957   8854   8802   -681    146  -1221       C
ATOM    111  C   TYR C  27      29.504  25.513  -9.399  1.00 72.77           C
ANISOU  111  C   TYR C  27     9955   8853   8842   -662    167  -1226       C
ATOM    112  O   TYR C  27      29.188  26.317 -10.275  1.00 72.67           O
ANISOU  112  O   TYR C  27     9935   8798   8878   -637    204  -1217       O
ATOM    113  CB  TYR C  27      28.191  25.504  -7.274  1.00 71.99           C
ANISOU  113  CB  TYR C  27     9858   8782   8713   -740    187  -1271       C
ATOM    114  CG  TYR C  27      27.793  26.937  -7.493  1.00 71.82           C
ANISOU  114  CG  TYR C  27     9820   8718   8751   -748    259  -1296       C
ATOM    115  CD1 TYR C  27      26.518  27.255  -7.932  1.00 71.96           C
ANISOU  115  CD1 TYR C  27     9839   8693   8808   -729    285  -1278       C
ATOM    116  CD2 TYR C  27      28.696  27.971  -7.295  1.00 71.61           C
ANISOU  116  CD2 TYR C  27     9774   8691   8745   -772    301  -1336       C
ATOM    117  CE1 TYR C  27      26.146  28.558  -8.152  1.00 72.02           C
ANISOU  117  CE1 TYR C  27     9829   8659   8874   -733    354  -1297       C
ATOM    118  CE2 TYR C  27      28.333  29.281  -7.513  1.00 71.64           C
ANISOU  118  CE2 TYR C  27     9761   8650   8808   -778    370  -1358       C
ATOM    119  CZ  TYR C  27      27.055  29.568  -7.942  1.00 71.84           C
ANISOU  119  CZ  TYR C  27     9789   8633   8873   -757    397  -1336       C
ATOM    120  OH  TYR C  27      26.682  30.872  -8.161  1.00 72.04           O
ANISOU  120  OH  TYR C  27     9796   8612   8962   -760    469  -1354       O
ATOM    121  N   GLN C  28      30.768  25.241  -9.091  1.00 80.49           N
ANISOU  121  N   GLN C  28    10927   9866   9789   -674    144  -1237       N
ATOM    122  CA  GLN C  28      31.877  25.854  -9.813  1.00 80.50           C
ANISOU  122  CA  GLN C  28    10915   9859   9814   -657    160  -1241       C
ATOM    123  C   GLN C  28      31.819  25.508 -11.294  1.00 80.56           C
ANISOU  123  C   GLN C  28    10933   9837   9841   -595    143  -1195       C
ATOM    124  O   GLN C  28      31.933  26.384 -12.155  1.00 80.95           O
ANISOU  124  O   GLN C  28    10971   9852   9934   -573    180  -1191       O
ATOM    125  CB  GLN C  28      33.211  25.397  -9.228  1.00 80.60           C
ANISOU  125  CB  GLN C  28    10919   9920   9783   -677    128  -1253       C
ATOM    126  CG  GLN C  28      34.137  26.541  -8.898  1.00 80.71           C
ANISOU  126  CG  GLN C  28    10909   9941   9818   -709    172  -1296       C
ATOM    127  CD  GLN C  28      33.449  27.595  -8.062  1.00 80.44           C
ANISOU  127  CD  GLN C  28    10863   9893   9806   -757    230  -1342       C
ATOM    128  OE1 GLN C  28      33.279  28.734  -8.495  1.00 80.69           O
ANISOU  128  OE1 GLN C  28    10883   9884   9891   -755    286  -1359       O
ATOM    129  NE2 GLN C  28      33.037  27.216  -6.858  1.00 79.94           N
ANISOU  129  NE2 GLN C  28    10805   9865   9705   -799    217  -1363       N
ATOM    130  N   THR C  29      31.644  24.220 -11.572  1.00 67.47           N
ANISOU  130  N   THR C  29     9295   8191   8148   -569     86  -1160       N
ATOM    131  CA  THR C  29      31.481  23.722 -12.931  1.00 67.28           C
ANISOU  131  CA  THR C  29     9284   8144   8134   -514     64  -1118       C
ATOM    132  C   THR C  29      30.325  24.415 -13.647  1.00 67.22           C
ANISOU  132  C   THR C  29     9276   8095   8172   -495    100  -1104       C
ATOM    133  O   THR C  29      30.457  24.814 -14.800  1.00 67.61           O
ANISOU  133  O   THR C  29     9321   8120   8249   -458    114  -1083       O
ATOM    134  CB  THR C  29      31.264  22.192 -12.935  1.00 67.27           C
ANISOU  134  CB  THR C  29     9307   8162   8091   -497      2  -1088       C
ATOM    135  OG1 THR C  29      32.532  21.531 -12.844  1.00 67.45           O
ANISOU  135  OG1 THR C  29     9330   8215   8084   -491    -33  -1085       O
ATOM    136  CG2 THR C  29      30.555  21.737 -14.204  1.00 67.46           C
ANISOU  136  CG2 THR C  29     9347   8158   8128   -449    -15  -1050       C
ATOM    137  N   LEU C  30      29.200  24.575 -12.957  1.00 67.43           N
ANISOU  137  N   LEU C  30     9302   8113   8203   -520    116  -1114       N
ATOM    138  CA  LEU C  30      28.035  25.218 -13.556  1.00 67.39           C
ANISOU  138  CA  LEU C  30     9294   8071   8241   -503    150  -1099       C
ATOM    139  C   LEU C  30      28.294  26.691 -13.863  1.00 67.65           C
ANISOU  139  C   LEU C  30     9302   8073   8327   -505    215  -1116       C
ATOM    140  O   LEU C  30      27.986  27.167 -14.957  1.00 67.94           O
ANISOU  140  O   LEU C  30     9333   8081   8400   -469    235  -1088       O
ATOM    141  CB  LEU C  30      26.811  25.074 -12.648  1.00 67.21           C
ANISOU  141  CB  LEU C  30     9275   8047   8213   -532    156  -1108       C
ATOM    142  CG  LEU C  30      25.501  24.744 -13.363  1.00 67.12           C
ANISOU  142  CG  LEU C  30     9272   8014   8217   -503    146  -1071       C
ATOM    143  CD1 LEU C  30      25.771  23.656 -14.379  0.00 67.20           C
ANISOU  143  CD1 LEU C  30     9301   8032   8201   -461     91  -1034       C
ATOM    144  CD2 LEU C  30      24.423  24.301 -12.379  0.00 66.90           C
ANISOU  144  CD2 LEU C  30     9252   7994   8173   -533    139  -1078       C
ATOM    145  N   TYR C  31      28.861  27.405 -12.893  1.00 71.91           N
ANISOU  145  N   TYR C  31     9828   8622   8871   -549    249  -1161       N
ATOM    146  CA  TYR C  31      29.121  28.836 -13.040  1.00 72.03           C
ANISOU  146  CA  TYR C  31     9820   8608   8940   -557    316  -1183       C
ATOM    147  C   TYR C  31      30.058  29.136 -14.211  1.00 72.44           C
ANISOU  147  C   TYR C  31     9865   8648   9012   -519    319  -1162       C
ATOM    148  O   TYR C  31      29.637  29.761 -15.182  1.00 72.62           O
ANISOU  148  O   TYR C  31     9879   8635   9078   -486    349  -1135       O
ATOM    149  CB  TYR C  31      29.657  29.441 -11.735  1.00 71.38           C
ANISOU  149  CB  TYR C  31     9725   8543   8852   -616    347  -1241       C
ATOM    150  CG  TYR C  31      29.998  30.916 -11.824  1.00 71.64           C
ANISOU  150  CG  TYR C  31     9734   8544   8943   -630    419  -1270       C
ATOM    151  CD1 TYR C  31      29.078  31.891 -11.455  1.00 71.69           C
ANISOU  151  CD1 TYR C  31     9728   8515   8996   -650    481  -1290       C
ATOM    152  CD2 TYR C  31      31.246  31.333 -12.270  1.00 71.87           C
ANISOU  152  CD2 TYR C  31     9751   8575   8982   -624    428  -1277       C
ATOM    153  CE1 TYR C  31      29.395  33.242 -11.534  1.00 71.89           C
ANISOU  153  CE1 TYR C  31     9732   8506   9078   -664    551  -1317       C
ATOM    154  CE2 TYR C  31      31.567  32.673 -12.355  1.00 72.08           C
ANISOU  154  CE2 TYR C  31     9754   8568   9063   -637    496  -1303       C
ATOM    155  CZ  TYR C  31      30.642  33.622 -11.987  0.00 72.11           C
ANISOU  155  CZ  TYR C  31     9748   8536   9115   -657    557  -1323       C
ATOM    156  OH  TYR C  31      30.978  34.953 -12.075  1.00 72.40           O
ANISOU  156  OH  TYR C  31     9761   8536   9211   -671    628  -1350       O
ATOM    157  N   LYS C  32      31.310  28.685 -14.123  1.00 64.40           N
ANISOU  157  N   LYS C  32     8849   7661   7961   -522    289  -1171       N
ATOM    158  CA  LYS C  32      32.299  28.930 -15.178  1.00 64.89           C
ANISOU  158  CA  LYS C  32     8903   7715   8038   -488    291  -1152       C
ATOM    159  C   LYS C  32      31.762  28.586 -16.566  1.00 65.46           C
ANISOU  159  C   LYS C  32     8985   7765   8121   -431    275  -1100       C
ATOM    160  O   LYS C  32      32.140  29.202 -17.563  1.00 65.78           O
ANISOU  160  O   LYS C  32     9014   7784   8194   -400    299  -1081       O
ATOM    161  CB  LYS C  32      33.578  28.126 -14.926  1.00 64.94           C
ANISOU  161  CB  LYS C  32     8914   7762   7999   -492    245  -1159       C
ATOM    162  CG  LYS C  32      34.345  28.513 -13.669  0.00 64.69           C
ANISOU  162  CG  LYS C  32     8868   7759   7954   -548    259  -1209       C
ATOM    163  CD  LYS C  32      35.606  27.670 -13.516  0.00 64.72           C
ANISOU  163  CD  LYS C  32     8873   7806   7913   -547    211  -1207       C
ATOM    164  CE  LYS C  32      36.379  28.040 -12.259  0.00 64.57           C
ANISOU  164  CE  LYS C  32     8837   7823   7876   -604    222  -1255       C
ATOM    165  NZ  LYS C  32      37.596  27.196 -12.082  0.00 64.73           N
ANISOU  165  NZ  LYS C  32     8855   7888   7853   -602    173  -1248       N
ATOM    166  N   LEU C  33      30.866  27.607 -16.609  1.00 83.21           N
ANISOU  166  N   LEU C  33    11253  10021  10341   -418    233  -1077       N
ATOM    167  CA  LEU C  33      30.331  27.080 -17.858  1.00 83.34           C
ANISOU  167  CA  LEU C  33    11282  10027  10357   -369    208  -1030       C
ATOM    168  C   LEU C  33      29.309  27.993 -18.543  1.00 83.50           C
ANISOU  168  C   LEU C  33    11289  10010  10427   -350    252  -1007       C
ATOM    169  O   LEU C  33      29.359  28.167 -19.761  1.00 84.03           O
ANISOU  169  O   LEU C  33    11353  10065  10510   -308    256   -972       O
ATOM    170  CB  LEU C  33      29.745  25.685 -17.608  1.00 83.06           C
ANISOU  170  CB  LEU C  33    11272  10013  10274   -367    148  -1016       C
ATOM    171  CG  LEU C  33      28.781  24.975 -18.556  1.00 83.32           C
ANISOU  171  CG  LEU C  33    11320  10038  10299   -330    118   -975       C
ATOM    172  CD1 LEU C  33      29.355  24.850 -19.952  0.00 83.68           C
ANISOU  172  CD1 LEU C  33    11369  10081  10346   -284    106   -944       C
ATOM    173  CD2 LEU C  33      28.464  23.601 -17.988  0.00 83.00           C
ANISOU  173  CD2 LEU C  33    11303  10023  10212   -341     62   -973       C
ATOM    174  N   TYR C  34      28.398  28.587 -17.775  1.00 67.57           N
ANISOU  174  N   TYR C  34     9263   7977   8435   -379    288  -1024       N
ATOM    175  CA  TYR C  34      27.292  29.343 -18.375  1.00 67.95           C
ANISOU  175  CA  TYR C  34     9296   7990   8530   -359    327   -997       C
ATOM    176  C   TYR C  34      27.449  30.875 -18.411  1.00 68.23           C
ANISOU  176  C   TYR C  34     9304   7991   8630   -366    403  -1010       C
ATOM    177  O   TYR C  34      26.932  31.524 -19.321  1.00 68.79           O
ANISOU  177  O   TYR C  34     9362   8034   8743   -335    433   -975       O
ATOM    178  CB  TYR C  34      25.947  28.920 -17.768  1.00 67.73           C
ANISOU  178  CB  TYR C  34     9277   7963   8494   -375    316   -995       C
ATOM    179  CG  TYR C  34      25.571  27.486 -18.092  1.00 67.28           C
ANISOU  179  CG  TYR C  34     9245   7931   8387   -357    247   -969       C
ATOM    180  CD1 TYR C  34      25.050  27.147 -19.334  1.00 67.53           C
ANISOU  180  CD1 TYR C  34     9281   7959   8419   -313    225   -922       C
ATOM    181  CD2 TYR C  34      25.742  26.474 -17.159  1.00 66.65           C
ANISOU  181  CD2 TYR C  34     9185   7881   8259   -384    204   -990       C
ATOM    182  CE1 TYR C  34      24.710  25.840 -19.636  1.00 67.45           C
ANISOU  182  CE1 TYR C  34     9294   7970   8365   -300    164   -903       C
ATOM    183  CE2 TYR C  34      25.403  25.167 -17.452  1.00 66.60           C
ANISOU  183  CE2 TYR C  34     9200   7893   8211   -368    144   -967       C
ATOM    184  CZ  TYR C  34      24.889  24.854 -18.690  1.00 67.03           C
ANISOU  184  CZ  TYR C  34     9259   7940   8268   -327    125   -926       C
ATOM    185  OH  TYR C  34      24.552  23.552 -18.979  1.00 66.79           O
ANISOU  185  OH  TYR C  34     9252   7927   8198   -313     68   -907       O
ATOM    186  N   GLU C  35      28.144  31.454 -17.433  1.00 87.30           N
ANISOU  186  N   GLU C  35    11711  10407  11053   -408    434  -1059       N
ATOM    187  CA  GLU C  35      28.535  32.860 -17.543  1.00 87.59           C
ANISOU  187  CA  GLU C  35    11722  10409  11150   -415    505  -1075       C
ATOM    188  C   GLU C  35      29.590  32.948 -18.635  1.00 88.62           C
ANISOU  188  C   GLU C  35    11848  10541  11284   -379    498  -1051       C
ATOM    189  O   GLU C  35      30.436  32.058 -18.743  1.00 88.88           O
ANISOU  189  O   GLU C  35    11895  10606  11268   -373    446  -1051       O
ATOM    190  CB  GLU C  35      29.071  33.423 -16.213  1.00 86.68           C
ANISOU  190  CB  GLU C  35    11598  10298  11039   -473    539  -1139       C
ATOM    191  CG  GLU C  35      30.280  32.699 -15.619  1.00 86.32           C
ANISOU  191  CG  GLU C  35    11563  10297  10938   -498    494  -1169       C
ATOM    192  CD  GLU C  35      31.613  33.338 -15.975  1.00 86.38           C
ANISOU  192  CD  GLU C  35    11555  10302  10964   -496    517  -1182       C
ATOM    193  OE1 GLU C  35      31.817  34.528 -15.650  1.00 86.46           O
ANISOU  193  OE1 GLU C  35    11543  10284  11022   -522    581  -1214       O
ATOM    194  OE2 GLU C  35      32.465  32.642 -16.570  1.00 86.37           O
ANISOU  194  OE2 GLU C  35    11561  10324  10930   -471    472  -1162       O
ATOM    195  N   ARG C  36      29.539  33.983 -19.470  1.00 75.90           N
ANISOU  195  N   ARG C  36    10215   8893   9729   -353    549  -1027       N
ATOM    196  CA  ARG C  36      28.517  35.024 -19.451  1.00 75.53           C
ANISOU  196  CA  ARG C  36    10148   8803   9744   -354    612  -1019       C
ATOM    197  C   ARG C  36      27.621  34.769 -20.677  1.00 76.01           C
ANISOU  197  C   ARG C  36    10210   8858   9812   -301    595   -953       C
ATOM    198  O   ARG C  36      26.990  35.666 -21.244  1.00 76.54           O
ANISOU  198  O   ARG C  36    10256   8891   9936   -280    644   -922       O
ATOM    199  CB  ARG C  36      29.215  36.396 -19.472  1.00 75.19           C
ANISOU  199  CB  ARG C  36    10079   8725   9763   -365    685  -1040       C
ATOM    200  CG  ARG C  36      28.342  37.606 -19.786  1.00 75.58           C
ANISOU  200  CG  ARG C  36    10104   8723   9890   -353    758  -1019       C
ATOM    201  CD  ARG C  36      29.069  38.924 -19.679  0.00 75.58           C
ANISOU  201  CD  ARG C  36    10078   8685   9952   -370    832  -1046       C
ATOM    202  NE  ARG C  36      28.167  40.002 -20.066  0.00 76.06           N
ANISOU  202  NE  ARG C  36    10115   8694  10089   -352    901  -1017       N
ATOM    203  CZ  ARG C  36      28.508  41.047 -20.810  0.00 76.56           C
ANISOU  203  CZ  ARG C  36    10153   8719  10215   -329    958   -994       C
ATOM    204  NH1 ARG C  36      29.751  41.183 -21.255  0.00 76.64           N
ANISOU  204  NH1 ARG C  36    10161   8737  10221   -323    955   -998       N
ATOM    205  NH2 ARG C  36      27.597  41.962 -21.107  0.00 76.97           N
ANISOU  205  NH2 ARG C  36    10183   8726  10337   -312   1019   -963       N
ATOM    206  N   CYS C  37      27.548  33.499 -21.064  1.00 92.60           N
ANISOU  206  N   CYS C  37    12335  10995  11854   -282    524   -931       N
ATOM    207  CA  CYS C  37      26.940  33.101 -22.346  1.00 93.18           C
ANISOU  207  CA  CYS C  37    12411  11073  11921   -232    497   -870       C
ATOM    208  C   CYS C  37      25.477  33.501 -22.555  1.00 92.56           C
ANISOU  208  C   CYS C  37    12318  10972  11878   -220    521   -837       C
ATOM    209  O   CYS C  37      24.726  33.725 -21.603  1.00 91.86           O
ANISOU  209  O   CYS C  37    12226  10870  11805   -251    544   -860       O
ATOM    210  CB  CYS C  37      27.085  31.597 -22.563  1.00 93.53           C
ANISOU  210  CB  CYS C  37    12485  11158  11893   -221    417   -862       C
ATOM    211  SG  CYS C  37      26.088  30.975 -23.925  1.00 95.72           S
ANISOU  211  SG  CYS C  37    12769  11447  12155   -171    379   -797       S
ATOM    212  N   GLU C  38      25.100  33.581 -23.826  1.00 45.11           N
ANISOU  212  N   GLU C  38     6300   4962   5879   -174    517   -780       N
ATOM    213  CA  GLU C  38      23.811  34.109 -24.246  1.00 45.39           C
ANISOU  213  CA  GLU C  38     6315   4976   5954   -155    546   -737       C
ATOM    214  C   GLU C  38      23.025  33.027 -24.991  1.00 45.72           C
ANISOU  214  C   GLU C  38     6372   5051   5950   -128    483   -696       C
ATOM    215  O   GLU C  38      21.795  32.976 -24.921  1.00 46.22           O
ANISOU  215  O   GLU C  38     6427   5110   6024   -127    483   -674       O
ATOM    216  CB  GLU C  38      24.048  35.313 -25.164  1.00 45.82           C
ANISOU  216  CB  GLU C  38     6339   5001   6068   -123    603   -700       C
ATOM    217  CG  GLU C  38      22.927  36.330 -25.243  1.00 46.29           C
ANISOU  217  CG  GLU C  38     6368   5025   6195   -114    663   -668       C
ATOM    218  CD  GLU C  38      23.328  37.569 -26.032  1.00 46.52           C
ANISOU  218  CD  GLU C  38     6366   5021   6287    -86    725   -635       C
ATOM    219  OE1 GLU C  38      24.542  37.854 -26.119  1.00 46.35           O
ANISOU  219  OE1 GLU C  38     6347   4997   6268    -89    738   -657       O
ATOM    220  OE2 GLU C  38      22.432  38.253 -26.573  1.00 47.18           O
ANISOU  220  OE2 GLU C  38     6422   5083   6419    -60    762   -585       O
ATOM    221  N   VAL C  39      23.751  32.165 -25.701  1.00 40.17           N
ANISOU  221  N   VAL C  39     5688   4378   5195   -108    430   -687       N
ATOM    222  CA  VAL C  39      23.164  31.055 -26.451  1.00 40.35           C
ANISOU  222  CA  VAL C  39     5728   4434   5168    -85    368   -655       C
ATOM    223  C   VAL C  39      23.810  29.731 -26.052  1.00 39.43           C
ANISOU  223  C   VAL C  39     5646   4347   4987   -101    305   -689       C
ATOM    224  O   VAL C  39      25.000  29.522 -26.283  1.00 39.65           O
ANISOU  224  O   VAL C  39     5684   4385   4994    -95    293   -703       O
ATOM    225  CB  VAL C  39      23.337  31.252 -27.974  1.00 40.71           C
ANISOU  225  CB  VAL C  39     5763   4491   5214    -38    365   -602       C
ATOM    226  CG1 VAL C  39      23.102  29.949 -28.722  1.00 40.90           C
ANISOU  226  CG1 VAL C  39     5811   4555   5175    -20    295   -583       C
ATOM    227  CG2 VAL C  39      22.395  32.323 -28.475  1.00 41.40           C
ANISOU  227  CG2 VAL C  39     5815   4556   5359    -18    415   -554       C
ATOM    228  N   VAL C  40      23.025  28.833 -25.465  1.00 28.86           N
ANISOU  228  N   VAL C  40     4325   3023   3619   -120    267   -699       N
ATOM    229  CA  VAL C  40      23.551  27.542 -25.034  1.00 28.18           C
ANISOU  229  CA  VAL C  40     4271   2963   3474   -135    209   -728       C
ATOM    230  C   VAL C  40      23.467  26.500 -26.149  1.00 28.35           C
ANISOU  230  C   VAL C  40     4310   3011   3450   -104    153   -699       C
ATOM    231  O   VAL C  40      22.374  26.064 -26.520  1.00 28.62           O
ANISOU  231  O   VAL C  40     4345   3054   3474    -96    130   -673       O
ATOM    232  CB  VAL C  40      22.828  27.026 -23.769  1.00 27.75           C
ANISOU  232  CB  VAL C  40     4227   2910   3408   -173    194   -756       C
ATOM    233  CG1 VAL C  40      23.489  25.758 -23.251  1.00 27.54           C
ANISOU  233  CG1 VAL C  40     4230   2907   3325   -189    140   -784       C
ATOM    234  CG2 VAL C  40      22.836  28.093 -22.690  1.00 27.92           C
ANISOU  234  CG2 VAL C  40     4230   2906   3474   -206    253   -787       C
ATOM    235  N   MET C  41      24.623  26.118 -26.689  1.00 42.94           N
ANISOU  235  N   MET C  41     6171   4873   5272    -87    134   -704       N
ATOM    236  CA  MET C  41      24.690  25.057 -27.689  1.00 43.30           C
ANISOU  236  CA  MET C  41     6237   4944   5271    -61     82   -684       C
ATOM    237  C   MET C  41      24.600  23.697 -27.009  1.00 42.96           C
ANISOU  237  C   MET C  41     6224   4916   5184    -82     29   -710       C
ATOM    238  O   MET C  41      25.601  22.988 -26.866  1.00 42.78           O
ANISOU  238  O   MET C  41     6220   4903   5131    -83      3   -731       O
ATOM    239  CB  MET C  41      25.979  25.151 -28.512  1.00 43.15           C
ANISOU  239  CB  MET C  41     6221   4932   5243    -35     85   -681       C
ATOM    240  CG  MET C  41      25.943  26.188 -29.628  1.00 44.32           C
ANISOU  240  CG  MET C  41     6344   5075   5422     -2    123   -641       C
ATOM    241  SD  MET C  41      24.587  25.934 -30.794  0.00 46.61           S
ANISOU  241  SD  MET C  41     6628   5384   5699     25    101   -589       S
ATOM    242  CE  MET C  41      24.726  24.178 -31.131  0.00 45.70           C
ANISOU  242  CE  MET C  41     6552   5299   5512     27     26   -604       C
ATOM    243  N   GLY C  42      23.391  23.342 -26.589  1.00 39.95           N
ANISOU  243  N   GLY C  42     5844   4534   4800    -98     15   -705       N
ATOM    244  CA  GLY C  42      23.159  22.096 -25.885  1.00 38.62           C
ANISOU  244  CA  GLY C  42     5702   4378   4595   -120    -32   -726       C
ATOM    245  C   GLY C  42      22.057  22.239 -24.856  1.00 38.76           C
ANISOU  245  C   GLY C  42     5713   4386   4630   -151    -21   -734       C
ATOM    246  O   GLY C  42      21.104  22.994 -25.053  1.00 39.17           O
ANISOU  246  O   GLY C  42     5742   4426   4713   -148      8   -711       O
ATOM    247  N   ASN C  43      22.190  21.523 -23.746  1.00 38.39           N
ANISOU  247  N   ASN C  43     5682   4342   4562   -181    -42   -764       N
ATOM    248  CA  ASN C  43      21.143  21.504 -22.734  1.00 37.95           C
ANISOU  248  CA  ASN C  43     5622   4280   4516   -212    -36   -772       C
ATOM    249  C   ASN C  43      21.513  22.261 -21.462  1.00 37.83           C
ANISOU  249  C   ASN C  43     5596   4254   4523   -245      3   -805       C
ATOM    250  O   ASN C  43      22.628  22.141 -20.954  1.00 37.48           O
ANISOU  250  O   ASN C  43     5559   4216   4464   -256      0   -832       O
ATOM    251  CB  ASN C  43      20.760  20.062 -22.403  1.00 37.35           C
ANISOU  251  CB  ASN C  43     5573   4219   4399   -224    -91   -777       C
ATOM    252  CG  ASN C  43      20.745  19.174 -23.629  1.00 37.96           C
ANISOU  252  CG  ASN C  43     5667   4310   4448   -195   -133   -756       C
ATOM    253  OD1 ASN C  43      19.931  19.359 -24.534  1.00 39.07           O
ANISOU  253  OD1 ASN C  43     5797   4452   4595   -176   -134   -727       O
ATOM    254  ND2 ASN C  43      21.651  18.203 -23.669  1.00 37.02           N
ANISOU  254  ND2 ASN C  43     5571   4200   4294   -190   -168   -770       N
ATOM    255  N   LEU C  44      20.566  23.048 -20.962  1.00 32.88           N
ANISOU  255  N   LEU C  44     4951   3612   3932   -261     41   -804       N
ATOM    256  CA  LEU C  44      20.754  23.790 -19.723  1.00 32.34           C
ANISOU  256  CA  LEU C  44     4872   3533   3885   -296     83   -839       C
ATOM    257  C   LEU C  44      20.262  22.957 -18.546  1.00 31.43           C
ANISOU  257  C   LEU C  44     4772   3430   3742   -331     57   -859       C
ATOM    258  O   LEU C  44      19.060  22.850 -18.312  1.00 31.73           O
ANISOU  258  O   LEU C  44     4805   3461   3788   -340     58   -848       O
ATOM    259  CB  LEU C  44      19.997  25.118 -19.784  1.00 33.08           C
ANISOU  259  CB  LEU C  44     4936   3599   4036   -295    144   -828       C
ATOM    260  CG  LEU C  44      20.059  26.009 -18.543  1.00 32.91           C
ANISOU  260  CG  LEU C  44     4900   3561   4042   -334    196   -866       C
ATOM    261  CD1 LEU C  44      21.489  26.438 -18.260  1.00 32.51           C
ANISOU  261  CD1 LEU C  44     4849   3513   3990   -344    213   -898       C
ATOM    262  CD2 LEU C  44      19.153  27.220 -18.708  1.00 33.46           C
ANISOU  262  CD2 LEU C  44     4940   3600   4172   -328    256   -850       C
ATOM    263  N   GLU C  45      21.194  22.366 -17.807  1.00 42.33           N
ANISOU  263  N   GLU C  45     6167   4827   5089   -351     34   -887       N
ATOM    264  CA  GLU C  45      20.830  21.476 -16.711  1.00 42.27           C
ANISOU  264  CA  GLU C  45     6174   4835   5050   -382      6   -903       C
ATOM    265  C   GLU C  45      21.269  22.011 -15.350  1.00 41.65           C
ANISOU  265  C   GLU C  45     6090   4763   4974   -424     37   -943       C
ATOM    266  O   GLU C  45      22.461  22.103 -15.057  1.00 41.99           O
ANISOU  266  O   GLU C  45     6133   4818   5002   -432     37   -965       O
ATOM    267  CB  GLU C  45      21.393  20.076 -16.956  1.00 42.49           C
ANISOU  267  CB  GLU C  45     6229   4883   5032   -371    -55   -895       C
ATOM    268  CG  GLU C  45      20.961  19.479 -18.292  1.00 42.75           C
ANISOU  268  CG  GLU C  45     6271   4914   5059   -333    -86   -861       C
ATOM    269  CD  GLU C  45      21.401  18.041 -18.456  1.00 42.77           C
ANISOU  269  CD  GLU C  45     6300   4931   5019   -325   -143   -857       C
ATOM    270  OE1 GLU C  45      21.960  17.490 -17.485  1.00 42.72           O
ANISOU  270  OE1 GLU C  45     6305   4939   4990   -348   -159   -876       O
ATOM    271  OE2 GLU C  45      21.186  17.471 -19.549  1.00 42.73           O
ANISOU  271  OE2 GLU C  45     6305   4925   5004   -297   -170   -834       O
ATOM    272  N   ILE C  46      20.286  22.362 -14.526  1.00 30.31           N
ANISOU  272  N   ILE C  46     4644   3319   3552   -452     63   -953       N
ATOM    273  CA  ILE C  46      20.537  22.909 -13.200  1.00 30.33           C
ANISOU  273  CA  ILE C  46     4640   3329   3556   -496     96   -994       C
ATOM    274  C   ILE C  46      20.064  21.928 -12.133  1.00 30.31           C
ANISOU  274  C   ILE C  46     4653   3350   3515   -526     63  -1002       C
ATOM    275  O   ILE C  46      18.889  21.914 -11.766  1.00 30.98           O
ANISOU  275  O   ILE C  46     4734   3426   3611   -538     73   -997       O
ATOM    276  CB  ILE C  46      19.813  24.255 -13.013  1.00 30.73           C
ANISOU  276  CB  ILE C  46     4666   3350   3659   -507    163  -1005       C
ATOM    277  CG1 ILE C  46      20.095  25.177 -14.203  1.00 30.82           C
ANISOU  277  CG1 ILE C  46     4660   3336   3713   -471    194   -986       C
ATOM    278  CG2 ILE C  46      20.228  24.909 -11.703  1.00 30.26           C
ANISOU  278  CG2 ILE C  46     4598   3299   3601   -554    202  -1054       C
ATOM    279  CD1 ILE C  46      19.205  26.400 -14.254  1.00 31.44           C
ANISOU  279  CD1 ILE C  46     4714   3380   3851   -472    258   -982       C
ATOM    280  N   VAL C  47      20.987  21.107 -11.638  1.00 43.37           N
ANISOU  280  N   VAL C  47     6321   5033   5126   -537     26  -1013       N
ATOM    281  CA  VAL C  47      20.642  20.026 -10.720  1.00 43.22           C
ANISOU  281  CA  VAL C  47     6316   5037   5066   -561    -11  -1013       C
ATOM    282  C   VAL C  47      21.396  20.122  -9.394  1.00 43.49           C
ANISOU  282  C   VAL C  47     6348   5102   5073   -604     -4  -1049       C
ATOM    283  O   VAL C  47      22.611  20.317  -9.373  1.00 43.97           O
ANISOU  283  O   VAL C  47     6406   5178   5124   -605     -5  -1064       O
ATOM    284  CB  VAL C  47      20.920  18.647 -11.360  1.00 43.20           C
ANISOU  284  CB  VAL C  47     6337   5045   5033   -533    -74   -983       C
ATOM    285  CG1 VAL C  47      20.482  17.526 -10.432  1.00 42.88           C
ANISOU  285  CG1 VAL C  47     6311   5025   4958   -556   -109   -979       C
ATOM    286  CG2 VAL C  47      20.217  18.533 -12.705  1.00 43.47           C
ANISOU  286  CG2 VAL C  47     6373   5054   5089   -493    -83   -951       C
ATOM    287  N   LEU C  48      20.658  19.983  -8.294  1.00 52.20           N
ANISOU  287  N   LEU C  48     7452   6217   6163   -639      4  -1062       N
ATOM    288  CA  LEU C  48      21.225  19.981  -6.944  1.00 52.48           C
ANISOU  288  CA  LEU C  48     7485   6289   6166   -684      8  -1094       C
ATOM    289  C   LEU C  48      22.047  21.229  -6.623  1.00 53.08           C
ANISOU  289  C   LEU C  48     7542   6368   6258   -706     56  -1135       C
ATOM    290  O   LEU C  48      23.267  21.164  -6.475  1.00 53.42           O
ANISOU  290  O   LEU C  48     7583   6436   6279   -712     43  -1147       O
ATOM    291  CB  LEU C  48      22.021  18.693  -6.684  1.00 52.23           C
ANISOU  291  CB  LEU C  48     7468   6292   6084   -681    -51  -1078       C
ATOM    292  CG  LEU C  48      21.130  17.477  -6.390  1.00 52.08           C
ANISOU  292  CG  LEU C  48     7466   6279   6043   -681    -91  -1050       C
ATOM    293  CD1 LEU C  48      21.910  16.172  -6.310  1.00 52.07           C
ANISOU  293  CD1 LEU C  48     7480   6303   6001   -671   -147  -1028       C
ATOM    294  CD2 LEU C  48      20.342  17.696  -5.107  1.00 51.82           C
ANISOU  294  CD2 LEU C  48     7429   6262   6000   -727    -67  -1071       C
ATOM    295  N   THR C  49      21.356  22.361  -6.511  1.00 48.16           N
ANISOU  295  N   THR C  49     6904   5718   5676   -719    114  -1155       N
ATOM    296  CA  THR C  49      21.988  23.640  -6.206  1.00 47.50           C
ANISOU  296  CA  THR C  49     6802   5630   5616   -743    169  -1197       C
ATOM    297  C   THR C  49      21.422  24.224  -4.911  1.00 47.26           C
ANISOU  297  C   THR C  49     6763   5609   5585   -795    212  -1238       C
ATOM    298  O   THR C  49      20.213  24.180  -4.678  1.00 47.02           O
ANISOU  298  O   THR C  49     6735   5564   5568   -800    226  -1230       O
ATOM    299  CB  THR C  49      21.790  24.645  -7.360  1.00 47.62           C
ANISOU  299  CB  THR C  49     6804   5597   5692   -709    210  -1187       C
ATOM    300  OG1 THR C  49      22.225  24.054  -8.592  1.00 47.74           O
ANISOU  300  OG1 THR C  49     6828   5605   5705   -661    169  -1147       O
ATOM    301  CG2 THR C  49      22.583  25.917  -7.112  1.00 47.67           C
ANISOU  301  CG2 THR C  49     6791   5596   5725   -732    266  -1229       C
ATOM    302  N   GLY C  50      22.304  24.768  -4.074  1.00 44.52           N
ANISOU  302  N   GLY C  50     6407   5289   5221   -835    235  -1283       N
ATOM    303  CA  GLY C  50      21.925  25.298  -2.775  1.00 44.54           C
ANISOU  303  CA  GLY C  50     6401   5308   5213   -890    275  -1329       C
ATOM    304  C   GLY C  50      20.936  26.449  -2.822  1.00 45.25           C
ANISOU  304  C   GLY C  50     6479   5352   5363   -896    346  -1348       C
ATOM    305  O   GLY C  50      20.671  27.008  -3.886  1.00 45.54           O
ANISOU  305  O   GLY C  50     6508   5342   5452   -859    369  -1327       O
ATOM    306  N   HIS C  51      20.398  26.809  -1.660  1.00 75.44           N
ANISOU  306  N   HIS C  51    10298   9188   9178   -944    382  -1386       N
ATOM    307  CA  HIS C  51      19.362  27.836  -1.580  1.00 76.03           C
ANISOU  307  CA  HIS C  51    10361   9218   9310   -952    452  -1404       C
ATOM    308  C   HIS C  51      19.909  29.250  -1.774  1.00 76.22           C
ANISOU  308  C   HIS C  51    10365   9211   9384   -963    519  -1444       C
ATOM    309  O   HIS C  51      19.242  30.104  -2.357  1.00 76.32           O
ANISOU  309  O   HIS C  51    10366   9170   9461   -942    571  -1438       O
ATOM    310  CB  HIS C  51      18.591  27.735  -0.258  1.00 76.33           C
ANISOU  310  CB  HIS C  51    10401   9280   9321  -1000    471  -1434       C
ATOM    311  CG  HIS C  51      19.368  28.194   0.936  1.00 77.24           C
ANISOU  311  CG  HIS C  51    10510   9435   9401  -1061    496  -1496       C
ATOM    312  ND1 HIS C  51      20.310  27.399   1.563  1.00 77.68           N
ANISOU  312  ND1 HIS C  51    10574   9553   9387  -1084    443  -1502       N
ATOM    313  CD2 HIS C  51      19.341  29.355   1.624  1.00 77.38           C
ANISOU  313  CD2 HIS C  51    10514   9442   9444  -1104    568  -1556       C
ATOM    314  CE1 HIS C  51      20.828  28.059   2.579  1.00 77.52           C
ANISOU  314  CE1 HIS C  51    10544   9563   9347  -1140    480  -1562       C
ATOM    315  NE2 HIS C  51      20.260  29.251   2.643  1.00 77.31           N
ANISOU  315  NE2 HIS C  51    10505   9492   9376  -1154    556  -1599       N
ATOM    316  N   ASN C  52      21.122  29.494  -1.287  1.00 85.94           N
ANISOU  316  N   ASN C  52    11592  10474  10587   -994    519  -1484       N
ATOM    317  CA  ASN C  52      21.744  30.808  -1.422  1.00 86.51           C
ANISOU  317  CA  ASN C  52    11646  10519  10705  -1009    582  -1526       C
ATOM    318  C   ASN C  52      22.897  30.826  -2.420  1.00 86.31           C
ANISOU  318  C   ASN C  52    11617  10489  10686   -975    557  -1506       C
ATOM    319  O   ASN C  52      23.983  31.324  -2.123  1.00 86.40           O
ANISOU  319  O   ASN C  52    11619  10519  10690  -1003    572  -1545       O
ATOM    320  CB  ASN C  52      22.206  31.336  -0.061  1.00 86.50           C
ANISOU  320  CB  ASN C  52    11638  10553  10675  -1079    617  -1597       C
ATOM    321  CG  ASN C  52      21.102  32.053   0.691  1.00 86.81           C
ANISOU  321  CG  ASN C  52    11671  10567  10744  -1112    685  -1633       C
ATOM    322  OD1 ASN C  52      19.942  32.039   0.277  1.00 86.73           O
ANISOU  322  OD1 ASN C  52    11663  10519  10772  -1082    699  -1600       O
ATOM    323  ND2 ASN C  52      21.457  32.686   1.803  1.00 86.96           N
ANISOU  323  ND2 ASN C  52    11683  10611  10746  -1174    727  -1701       N
ATOM    324  N   ALA C  53      22.651  30.281  -3.606  1.00 57.70           N
ANISOU  324  N   ALA C  53     8000   6843   7078   -916    521  -1446       N
ATOM    325  CA  ALA C  53      23.642  30.295  -4.674  1.00 57.76           C
ANISOU  325  CA  ALA C  53     8006   6844   7096   -879    499  -1422       C
ATOM    326  C   ALA C  53      23.353  31.433  -5.645  1.00 57.98           C
ANISOU  326  C   ALA C  53     8017   6810   7203   -848    558  -1412       C
ATOM    327  O   ALA C  53      22.196  31.722  -5.948  1.00 58.48           O
ANISOU  327  O   ALA C  53     8076   6835   7306   -830    587  -1391       O
ATOM    328  CB  ALA C  53      23.653  28.964  -5.405  1.00 57.39           C
ANISOU  328  CB  ALA C  53     7977   6814   7014   -834    422  -1364       C
ATOM    329  N   ASP C  54      24.410  32.079  -6.126  1.00 58.49           N
ANISOU  329  N   ASP C  54     8071   6865   7289   -843    577  -1425       N
ATOM    330  CA  ASP C  54      24.262  33.183  -7.065  1.00 59.06           C
ANISOU  330  CA  ASP C  54     8125   6879   7436   -813    635  -1413       C
ATOM    331  C   ASP C  54      23.771  32.676  -8.416  1.00 59.17           C
ANISOU  331  C   ASP C  54     8144   6872   7465   -748    600  -1343       C
ATOM    332  O   ASP C  54      24.408  31.828  -9.041  1.00 59.02           O
ANISOU  332  O   ASP C  54     8137   6877   7410   -719    541  -1312       O
ATOM    333  CB  ASP C  54      25.585  33.933  -7.228  1.00 59.44           C
ANISOU  333  CB  ASP C  54     8159   6925   7499   -825    660  -1443       C
ATOM    334  CG  ASP C  54      25.456  35.156  -8.114  1.00 60.12           C
ANISOU  334  CG  ASP C  54     8225   6951   7668   -798    727  -1433       C
ATOM    335  OD1 ASP C  54      24.358  35.751  -8.152  1.00 60.27           O
ANISOU  335  OD1 ASP C  54     8236   6928   7736   -793    776  -1426       O
ATOM    336  OD2 ASP C  54      26.453  35.523  -8.771  1.00 60.59           O
ANISOU  336  OD2 ASP C  54     8275   7002   7742   -782    731  -1429       O
ATOM    337  N   LEU C  55      22.632  33.198  -8.860  1.00 42.52           N
ANISOU  337  N   LEU C  55     6027   4720   5410   -726    640  -1318       N
ATOM    338  CA  LEU C  55      22.032  32.774 -10.119  1.00 42.73           C
ANISOU  338  CA  LEU C  55     6056   4729   5451   -667    610  -1251       C
ATOM    339  C   LEU C  55      22.019  33.907 -11.139  1.00 43.49           C
ANISOU  339  C   LEU C  55     6129   4775   5619   -633    666  -1229       C
ATOM    340  O   LEU C  55      21.299  33.850 -12.137  1.00 44.03           O
ANISOU  340  O   LEU C  55     6193   4823   5714   -588    660  -1175       O
ATOM    341  CB  LEU C  55      20.610  32.261  -9.882  1.00 42.33           C
ANISOU  341  CB  LEU C  55     6012   4676   5397   -663    599  -1228       C
ATOM    342  CG  LEU C  55      20.490  30.984  -9.048  1.00 41.53           C
ANISOU  342  CG  LEU C  55     5933   4622   5223   -687    536  -1236       C
ATOM    343  CD1 LEU C  55      19.038  30.695  -8.713  1.00 41.86           C
ANISOU  343  CD1 LEU C  55     5976   4655   5272   -690    540  -1219       C
ATOM    344  CD2 LEU C  55      21.115  29.808  -9.783  1.00 41.37           C
ANISOU  344  CD2 LEU C  55     5931   4632   5155   -655    459  -1200       C
ATOM    345  N   SER C  56      22.823  34.934 -10.886  1.00 52.67           N
ANISOU  345  N   SER C  56     7276   5920   6814   -656    720  -1270       N
ATOM    346  CA  SER C  56      22.882  36.094 -11.767  1.00 52.87           C
ANISOU  346  CA  SER C  56     7279   5895   6913   -628    780  -1251       C
ATOM    347  C   SER C  56      23.725  35.820 -13.009  1.00 52.89           C
ANISOU  347  C   SER C  56     7284   5905   6908   -582    743  -1210       C
ATOM    348  O   SER C  56      23.720  36.605 -13.955  1.00 53.76           O
ANISOU  348  O   SER C  56     7375   5977   7073   -548    782  -1179       O
ATOM    349  CB  SER C  56      23.431  37.310 -11.017  1.00 52.82           C
ANISOU  349  CB  SER C  56     7255   5864   6948   -673    856  -1314       C
ATOM    350  OG  SER C  56      24.753  37.077 -10.564  1.00 52.43           O
ANISOU  350  OG  SER C  56     7214   5853   6856   -703    830  -1354       O
ATOM    351  N   PHE C  57      24.446  34.703 -13.005  1.00 43.43           N
ANISOU  351  N   PHE C  57     6106   4754   5642   -581    671  -1207       N
ATOM    352  CA  PHE C  57      25.287  34.338 -14.141  1.00 43.71           C
ANISOU  352  CA  PHE C  57     6144   4799   5663   -538    633  -1171       C
ATOM    353  C   PHE C  57      24.463  33.683 -15.247  1.00 44.03           C
ANISOU  353  C   PHE C  57     6193   4838   5699   -486    594  -1105       C
ATOM    354  O   PHE C  57      24.987  33.343 -16.308  1.00 44.15           O
ANISOU  354  O   PHE C  57     6211   4861   5702   -446    563  -1069       O
ATOM    355  CB  PHE C  57      26.425  33.413 -13.700  1.00 43.62           C
ANISOU  355  CB  PHE C  57     6151   4838   5585   -557    575  -1194       C
ATOM    356  CG  PHE C  57      25.982  32.014 -13.369  1.00 44.09           C
ANISOU  356  CG  PHE C  57     6236   4936   5581   -557    504  -1180       C
ATOM    357  CD1 PHE C  57      26.160  30.984 -14.279  1.00 44.56           C
ANISOU  357  CD1 PHE C  57     6310   5014   5605   -516    442  -1136       C
ATOM    358  CD2 PHE C  57      25.392  31.728 -12.149  1.00 43.95           C
ANISOU  358  CD2 PHE C  57     6225   4935   5540   -600    502  -1211       C
ATOM    359  CE1 PHE C  57      25.757  29.696 -13.979  1.00 44.47           C
ANISOU  359  CE1 PHE C  57     6322   5034   5541   -516    380  -1124       C
ATOM    360  CE2 PHE C  57      24.985  30.441 -11.844  1.00 43.89           C
ANISOU  360  CE2 PHE C  57     6239   4961   5477   -599    439  -1196       C
ATOM    361  CZ  PHE C  57      25.168  29.424 -12.760  1.00 44.14           C
ANISOU  361  CZ  PHE C  57     6286   5007   5478   -558    379  -1152       C
ATOM    362  N   LEU C  58      23.171  33.511 -14.988  1.00 48.43           N
ANISOU  362  N   LEU C  58     6751   5387   6263   -487    597  -1091       N
ATOM    363  CA  LEU C  58      22.260  32.907 -15.952  1.00 48.89           C
ANISOU  363  CA  LEU C  58     6814   5446   6317   -443    561  -1031       C
ATOM    364  C   LEU C  58      21.275  33.936 -16.495  1.00 49.35           C
ANISOU  364  C   LEU C  58     6846   5459   6446   -420    621   -999       C
ATOM    365  O   LEU C  58      20.290  33.578 -17.140  1.00 49.39           O
ANISOU  365  O   LEU C  58     6849   5464   6454   -390    601   -951       O
ATOM    366  CB  LEU C  58      21.484  31.760 -15.301  1.00 48.38           C
ANISOU  366  CB  LEU C  58     6770   5410   6203   -459    510  -1032       C
ATOM    367  CG  LEU C  58      22.278  30.554 -14.801  1.00 47.90           C
ANISOU  367  CG  LEU C  58     6736   5395   6071   -476    444  -1053       C
ATOM    368  CD1 LEU C  58      21.397  29.660 -13.944  1.00 47.73           C
ANISOU  368  CD1 LEU C  58     6729   5394   6012   -500    411  -1059       C
ATOM    369  CD2 LEU C  58      22.850  29.774 -15.971  1.00 48.44           C
ANISOU  369  CD2 LEU C  58     6816   5480   6109   -433    389  -1014       C
ATOM    370  N   GLN C  59      21.540  35.212 -16.234  1.00 54.76           N
ANISOU  370  N   GLN C  59     7508   6107   7189   -435    695  -1024       N
ATOM    371  CA  GLN C  59      20.606  36.269 -16.611  1.00 55.30           C
ANISOU  371  CA  GLN C  59     7549   6129   7332   -417    761   -996       C
ATOM    372  C   GLN C  59      20.779  36.725 -18.057  1.00 55.52           C
ANISOU  372  C   GLN C  59     7560   6140   7394   -363    771   -938       C
ATOM    373  O   GLN C  59      19.968  37.495 -18.567  1.00 56.52           O
ANISOU  373  O   GLN C  59     7663   6233   7581   -339    817   -899       O
ATOM    374  CB  GLN C  59      20.732  37.472 -15.671  1.00 55.79           C
ANISOU  374  CB  GLN C  59     7595   6155   7449   -458    843  -1049       C
ATOM    375  CG  GLN C  59      21.970  38.316 -15.912  1.00 56.25           C
ANISOU  375  CG  GLN C  59     7641   6194   7536   -461    882  -1072       C
ATOM    376  CD  GLN C  59      22.011  39.567 -15.054  1.00 56.63           C
ANISOU  376  CD  GLN C  59     7671   6201   7645   -501    970  -1125       C
ATOM    377  OE1 GLN C  59      22.985  39.813 -14.341  1.00 56.14           O
ANISOU  377  OE1 GLN C  59     7612   6147   7571   -542    984  -1183       O
ATOM    378  NE2 GLN C  59      20.956  40.371 -15.127  1.00 57.23           N
ANISOU  378  NE2 GLN C  59     7726   6232   7789   -490   1031  -1104       N
ATOM    379  N   TRP C  60      21.832  36.252 -18.716  1.00 58.76           N
ANISOU  379  N   TRP C  60     7983   6576   7768   -345    729   -929       N
ATOM    380  CA  TRP C  60      22.111  36.673 -20.086  1.00 60.17           C
ANISOU  380  CA  TRP C  60     8146   6743   7974   -296    738   -876       C
ATOM    381  C   TRP C  60      21.707  35.619 -21.114  1.00 61.16           C
ANISOU  381  C   TRP C  60     8284   6901   8052   -255    668   -821       C
ATOM    382  O   TRP C  60      21.709  35.886 -22.315  1.00 62.27           O
ANISOU  382  O   TRP C  60     8412   7038   8211   -212    671   -769       O
ATOM    383  CB  TRP C  60      23.590  37.033 -20.252  1.00 60.63           C
ANISOU  383  CB  TRP C  60     8205   6801   8032   -300    749   -901       C
ATOM    384  CG  TRP C  60      24.148  37.809 -19.100  1.00 61.13           C
ANISOU  384  CG  TRP C  60     8261   6844   8123   -350    802   -968       C
ATOM    385  CD1 TRP C  60      25.038  37.362 -18.169  1.00 61.09           C
ANISOU  385  CD1 TRP C  60     8273   6866   8071   -392    778  -1025       C
ATOM    386  CD2 TRP C  60      23.845  39.165 -18.749  1.00 61.34           C
ANISOU  386  CD2 TRP C  60     8260   6818   8227   -365    891   -984       C
ATOM    387  NE1 TRP C  60      25.313  38.356 -17.262  1.00 60.87           N
ANISOU  387  NE1 TRP C  60     8231   6811   8086   -435    844  -1079       N
ATOM    388  CE2 TRP C  60      24.596  39.472 -17.596  1.00 61.16           C
ANISOU  388  CE2 TRP C  60     8242   6797   8201   -420    915  -1057       C
ATOM    389  CE3 TRP C  60      23.017  40.147 -19.298  1.00 62.00           C
ANISOU  389  CE3 TRP C  60     8316   6855   8385   -338    952   -944       C
ATOM    390  CZ2 TRP C  60      24.538  40.721 -16.982  1.00 61.34           C
ANISOU  390  CZ2 TRP C  60     8243   6773   8290   -450   1001  -1096       C
ATOM    391  CZ3 TRP C  60      22.963  41.386 -18.687  1.00 62.11           C
ANISOU  391  CZ3 TRP C  60     8309   6820   8471   -365   1039   -978       C
ATOM    392  CH2 TRP C  60      23.717  41.660 -17.540  1.00 61.72           C
ANISOU  392  CH2 TRP C  60     8266   6771   8415   -422   1063  -1056       C
ATOM    393  N   ILE C  61      21.363  34.426 -20.640  1.00 32.45           N
ANISOU  393  N   ILE C  61     4674   3300   4356   -270    606   -833       N
ATOM    394  CA  ILE C  61      20.945  33.342 -21.524  1.00 32.02           C
ANISOU  394  CA  ILE C  61     4634   3277   4254   -237    539   -789       C
ATOM    395  C   ILE C  61      19.655  33.697 -22.257  1.00 32.91           C
ANISOU  395  C   ILE C  61     4725   3377   4404   -207    555   -731       C
ATOM    396  O   ILE C  61      18.608  33.875 -21.635  1.00 33.48           O
ANISOU  396  O   ILE C  61     4788   3435   4499   -223    576   -733       O
ATOM    397  CB  ILE C  61      20.759  32.036 -20.728  1.00 40.97           C
ANISOU  397  CB  ILE C  61     5798   4445   5325   -265    476   -816       C
ATOM    398  CG1 ILE C  61      22.102  31.552 -20.176  1.00 40.82           C
ANISOU  398  CG1 ILE C  61     5799   4447   5263   -288    450   -862       C
ATOM    399  CG2 ILE C  61      20.120  30.967 -21.600  1.00 40.77           C
ANISOU  399  CG2 ILE C  61     5785   4447   5258   -234    413   -772       C
ATOM    400  CD1 ILE C  61      21.979  30.431 -19.170  1.00 40.63           C
ANISOU  400  CD1 ILE C  61     5801   4452   5185   -321    401   -893       C
ATOM    401  N   ARG C  62      19.738  33.800 -23.579  1.00 39.50           N
ANISOU  401  N   ARG C  62     5548   4217   5242   -162    546   -679       N
ATOM    402  CA  ARG C  62      18.579  34.149 -24.392  1.00 40.55           C
ANISOU  402  CA  ARG C  62     5657   4343   5407   -130    559   -618       C
ATOM    403  C   ARG C  62      17.970  32.923 -25.064  1.00 41.68           C
ANISOU  403  C   ARG C  62     5817   4529   5493   -111    485   -585       C
ATOM    404  O   ARG C  62      16.750  32.818 -25.195  1.00 42.54           O
ANISOU  404  O   ARG C  62     5913   4640   5611   -104    480   -552       O
ATOM    405  CB  ARG C  62      18.958  35.177 -25.461  1.00 41.57           C
ANISOU  405  CB  ARG C  62     5758   4453   5583    -92    604   -574       C
ATOM    406  CG  ARG C  62      17.762  35.750 -26.209  1.00 43.08           C
ANISOU  406  CG  ARG C  62     5917   4634   5819    -60    630   -508       C
ATOM    407  CD  ARG C  62      18.162  36.378 -27.536  1.00 44.27           C
ANISOU  407  CD  ARG C  62     6045   4784   5992    -14    649   -452       C
ATOM    408  NE  ARG C  62      18.470  35.373 -28.550  1.00 45.89           N
ANISOU  408  NE  ARG C  62     6270   5038   6129     10    579   -427       N
ATOM    409  CZ  ARG C  62      19.700  35.032 -28.920  1.00 46.53           C
ANISOU  409  CZ  ARG C  62     6370   5134   6173     16    555   -446       C
ATOM    410  NH1 ARG C  62      20.751  35.622 -28.366  1.00 45.86           N
ANISOU  410  NH1 ARG C  62     6287   5023   6114     -2    594   -488       N
ATOM    411  NH2 ARG C  62      19.881  34.105 -29.851  1.00 47.29           N
ANISOU  411  NH2 ARG C  62     6483   5274   6210     38    494   -423       N
ATOM    412  N   GLU C  63      18.825  31.999 -25.488  1.00 35.90           N
ANISOU  412  N   GLU C  63     5111   3828   4701   -104    429   -595       N
ATOM    413  CA  GLU C  63      18.377  30.841 -26.251  1.00 36.28           C
ANISOU  413  CA  GLU C  63     5175   3915   4694    -86    361   -566       C
ATOM    414  C   GLU C  63      19.039  29.548 -25.782  1.00 35.38           C
ANISOU  414  C   GLU C  63     5100   3827   4514   -107    300   -608       C
ATOM    415  O   GLU C  63      20.226  29.528 -25.456  1.00 34.73           O
ANISOU  415  O   GLU C  63     5031   3743   4420   -117    302   -643       O
ATOM    416  CB  GLU C  63      18.645  31.064 -27.744  1.00 38.24           C
ANISOU  416  CB  GLU C  63     5412   4178   4940    -41    356   -514       C
ATOM    417  CG  GLU C  63      18.230  29.913 -28.646  1.00 39.64           C
ANISOU  417  CG  GLU C  63     5605   4398   5059    -22    288   -486       C
ATOM    418  CD  GLU C  63      18.483  30.204 -30.114  1.00 41.54           C
ANISOU  418  CD  GLU C  63     5831   4656   5296     21    286   -436       C
ATOM    419  OE1 GLU C  63      19.162  29.390 -30.775  1.00 41.81           O
ANISOU  419  OE1 GLU C  63     5889   4720   5278     33    241   -440       O
ATOM    420  OE2 GLU C  63      17.999  31.245 -30.608  1.00 42.58           O
ANISOU  420  OE2 GLU C  63     5928   4773   5477     42    332   -391       O
ATOM    421  N   VAL C  64      18.254  28.475 -25.743  1.00 31.70           N
ANISOU  421  N   VAL C  64     4651   3385   4008   -113    248   -602       N
ATOM    422  CA  VAL C  64      18.764  27.143 -25.441  1.00 30.87           C
ANISOU  422  CA  VAL C  64     4583   3306   3843   -127    187   -633       C
ATOM    423  C   VAL C  64      18.385  26.192 -26.573  1.00 31.73           C
ANISOU  423  C   VAL C  64     4703   3445   3908   -101    131   -599       C
ATOM    424  O   VAL C  64      17.203  25.979 -26.845  1.00 32.15           O
ANISOU  424  O   VAL C  64     4747   3508   3963    -97    118   -570       O
ATOM    425  CB  VAL C  64      18.200  26.606 -24.111  1.00 30.22           C
ANISOU  425  CB  VAL C  64     4513   3221   3750   -167    175   -667       C
ATOM    426  CG1 VAL C  64      18.659  25.174 -23.878  1.00 29.72           C
ANISOU  426  CG1 VAL C  64     4484   3183   3624   -178    111   -690       C
ATOM    427  CG2 VAL C  64      18.619  27.500 -22.954  1.00 29.79           C
ANISOU  427  CG2 VAL C  64     4449   3140   3731   -197    229   -706       C
ATOM    428  N   THR C  65      19.389  25.627 -27.235  1.00 35.12           N
ANISOU  428  N   THR C  65     5150   3892   4300    -84    101   -604       N
ATOM    429  CA  THR C  65      19.155  24.792 -28.411  1.00 36.26           C
ANISOU  429  CA  THR C  65     5306   4067   4404    -59     53   -575       C
ATOM    430  C   THR C  65      18.608  23.410 -28.059  1.00 35.94           C
ANISOU  430  C   THR C  65     5293   4043   4318    -78     -4   -591       C
ATOM    431  O   THR C  65      17.931  22.779 -28.872  1.00 36.38           O
ANISOU  431  O   THR C  65     5353   4123   4349    -66    -40   -567       O
ATOM    432  CB  THR C  65      20.433  24.636 -29.261  1.00 36.13           C
ANISOU  432  CB  THR C  65     5302   4062   4363    -35     42   -577       C
ATOM    433  OG1 THR C  65      21.451  23.988 -28.489  1.00 35.66           O
ANISOU  433  OG1 THR C  65     5269   4001   4279    -54     24   -622       O
ATOM    434  CG2 THR C  65      20.938  25.996 -29.719  1.00 36.13           C
ANISOU  434  CG2 THR C  65     5274   4045   4408    -14     99   -556       C
ATOM    435  N   GLY C  66      18.903  22.944 -26.850  1.00 31.93           N
ANISOU  435  N   GLY C  66     4803   3527   3802   -109    -12   -632       N
ATOM    436  CA  GLY C  66      18.436  21.644 -26.400  1.00 31.06           C
ANISOU  436  CA  GLY C  66     4718   3430   3654   -129    -63   -648       C
ATOM    437  C   GLY C  66      17.233  21.751 -25.483  1.00 31.28           C
ANISOU  437  C   GLY C  66     4735   3447   3702   -156    -52   -648       C
ATOM    438  O   GLY C  66      16.216  22.341 -25.848  1.00 32.25           O
ANISOU  438  O   GLY C  66     4834   3568   3853   -148    -33   -617       O
ATOM    439  N   TYR C  67      17.346  21.178 -24.288  1.00 35.73           N
ANISOU  439  N   TYR C  67     5316   4007   4253   -188    -64   -683       N
ATOM    440  CA  TYR C  67      16.267  21.234 -23.308  1.00 35.80           C
ANISOU  440  CA  TYR C  67     5318   4007   4279   -216    -54   -687       C
ATOM    441  C   TYR C  67      16.726  21.885 -22.006  1.00 35.45           C
ANISOU  441  C   TYR C  67     5268   3945   4256   -245    -14   -722       C
ATOM    442  O   TYR C  67      17.923  21.977 -21.737  1.00 34.93           O
ANISOU  442  O   TYR C  67     5212   3880   4181   -248     -8   -747       O
ATOM    443  CB  TYR C  67      15.704  19.834 -23.032  1.00 34.52           C
ANISOU  443  CB  TYR C  67     5179   3858   4077   -232   -108   -693       C
ATOM    444  CG  TYR C  67      16.724  18.837 -22.525  1.00 34.17           C
ANISOU  444  CG  TYR C  67     5166   3822   3996   -243   -141   -724       C
ATOM    445  CD1 TYR C  67      17.068  18.786 -21.179  1.00 33.84           C
ANISOU  445  CD1 TYR C  67     5131   3775   3953   -275   -131   -755       C
ATOM    446  CD2 TYR C  67      17.335  17.939 -23.391  1.00 33.94           C
ANISOU  446  CD2 TYR C  67     5157   3806   3931   -223   -182   -721       C
ATOM    447  CE1 TYR C  67      17.999  17.877 -20.712  1.00 33.06           C
ANISOU  447  CE1 TYR C  67     5057   3686   3820   -284   -162   -778       C
ATOM    448  CE2 TYR C  67      18.266  17.024 -22.933  1.00 33.46           C
ANISOU  448  CE2 TYR C  67     5123   3750   3839   -231   -210   -746       C
ATOM    449  CZ  TYR C  67      18.594  16.999 -21.592  1.00 33.14           C
ANISOU  449  CZ  TYR C  67     5087   3706   3800   -261   -201   -772       C
ATOM    450  OH  TYR C  67      19.520  16.092 -21.129  1.00 32.39           O
ANISOU  450  OH  TYR C  67     5014   3617   3675   -268   -229   -791       O
ATOM    451  N   VAL C  68      15.767  22.332 -21.200  1.00 29.90           N
ANISOU  451  N   VAL C  68     4551   3230   3581   -267     14   -725       N
ATOM    452  CA  VAL C  68      16.077  22.946 -19.915  1.00 29.50           C
ANISOU  452  CA  VAL C  68     4495   3165   3548   -299     54   -761       C
ATOM    453  C   VAL C  68      15.677  22.029 -18.762  1.00 28.95           C
ANISOU  453  C   VAL C  68     4443   3105   3450   -334     27   -784       C
ATOM    454  O   VAL C  68      14.502  21.705 -18.593  1.00 29.35           O
ANISOU  454  O   VAL C  68     4490   3156   3504   -342     18   -769       O
ATOM    455  CB  VAL C  68      15.383  24.312 -19.754  1.00 30.06           C
ANISOU  455  CB  VAL C  68     4533   3210   3678   -301    119   -751       C
ATOM    456  CG1 VAL C  68      15.690  24.904 -18.387  1.00 29.65           C
ANISOU  456  CG1 VAL C  68     4479   3146   3643   -339    161   -795       C
ATOM    457  CG2 VAL C  68      15.822  25.261 -20.857  1.00 30.64           C
ANISOU  457  CG2 VAL C  68     4587   3273   3783   -266    150   -726       C
ATOM    458  N   LEU C  69      16.664  21.614 -17.974  1.00 38.90           N
ANISOU  458  N   LEU C  69     5722   4376   4683   -355     14   -818       N
ATOM    459  CA  LEU C  69      16.434  20.683 -16.876  1.00 38.73           C
ANISOU  459  CA  LEU C  69     5718   4368   4630   -387    -14   -837       C
ATOM    460  C   LEU C  69      16.654  21.342 -15.518  1.00 38.72           C
ANISOU  460  C   LEU C  69     5710   4364   4640   -425     27   -874       C
ATOM    461  O   LEU C  69      17.781  21.680 -15.156  1.00 39.09           O
ANISOU  461  O   LEU C  69     5757   4416   4680   -434     40   -900       O
ATOM    462  CB  LEU C  69      17.351  19.466 -17.015  1.00 38.28           C
ANISOU  462  CB  LEU C  69     5689   4331   4526   -381    -68   -842       C
ATOM    463  CG  LEU C  69      17.244  18.399 -15.924  1.00 37.84           C
ANISOU  463  CG  LEU C  69     5652   4290   4435   -411   -101   -857       C
ATOM    464  CD1 LEU C  69      15.894  17.706 -15.982  1.00 37.91           C
ANISOU  464  CD1 LEU C  69     5665   4298   4442   -414   -124   -836       C
ATOM    465  CD2 LEU C  69      18.375  17.390 -16.048  1.00 37.49           C
ANISOU  465  CD2 LEU C  69     5630   4261   4352   -402   -144   -863       C
ATOM    466  N   VAL C  70      15.571  21.520 -14.770  1.00 32.46           N
ANISOU  466  N   VAL C  70     4907   3564   3861   -448     47   -877       N
ATOM    467  CA  VAL C  70      15.651  22.092 -13.432  1.00 32.03           C
ANISOU  467  CA  VAL C  70     4847   3509   3814   -488     86   -915       C
ATOM    468  C   VAL C  70      15.158  21.074 -12.412  1.00 31.78           C
ANISOU  468  C   VAL C  70     4832   3497   3747   -518     54   -923       C
ATOM    469  O   VAL C  70      13.955  20.937 -12.191  1.00 32.18           O
ANISOU  469  O   VAL C  70     4877   3541   3809   -526     57   -910       O
ATOM    470  CB  VAL C  70      14.814  23.379 -13.316  1.00 32.41           C
ANISOU  470  CB  VAL C  70     4867   3529   3918   -493    151   -915       C
ATOM    471  CG1 VAL C  70      15.027  24.030 -11.959  1.00 31.94           C
ANISOU  471  CG1 VAL C  70     4801   3469   3864   -536    195   -961       C
ATOM    472  CG2 VAL C  70      15.176  24.344 -14.432  1.00 32.67           C
ANISOU  472  CG2 VAL C  70     4882   3542   3990   -459    181   -897       C
ATOM    473  N   ALA C  71      16.091  20.358 -11.794  1.00 40.38           N
ANISOU  473  N   ALA C  71     5939   4611   4794   -535     23   -943       N
ATOM    474  CA  ALA C  71      15.732  19.270 -10.892  1.00 40.25           C
ANISOU  474  CA  ALA C  71     5938   4614   4740   -560    -12   -945       C
ATOM    475  C   ALA C  71      16.394  19.374  -9.520  1.00 40.33           C
ANISOU  475  C   ALA C  71     5951   4648   4725   -601      1   -982       C
ATOM    476  O   ALA C  71      17.554  19.767  -9.406  1.00 40.28           O
ANISOU  476  O   ALA C  71     5942   4651   4711   -605     10  -1004       O
ATOM    477  CB  ALA C  71      16.051  17.928 -11.533  1.00 39.88           C
ANISOU  477  CB  ALA C  71     5915   4579   4660   -537    -75   -921       C
ATOM    478  N   MET C  72      15.632  18.991  -8.495  1.00 43.82           N
ANISOU  478  N   MET C  72     6395   5100   5152   -632      0   -989       N
ATOM    479  CA  MET C  72      16.064  18.962  -7.091  1.00 43.50           C
ANISOU  479  CA  MET C  72     6358   5089   5082   -675      9  -1021       C
ATOM    480  C   MET C  72      17.037  20.057  -6.645  1.00 43.43           C
ANISOU  480  C   MET C  72     6335   5087   5080   -695     51  -1061       C
ATOM    481  O   MET C  72      18.121  19.775  -6.139  1.00 43.04           O
ANISOU  481  O   MET C  72     6291   5067   4996   -710     34  -1077       O
ATOM    482  CB  MET C  72      16.561  17.565  -6.685  1.00 43.13           C
ANISOU  482  CB  MET C  72     6331   5073   4984   -680    -50  -1009       C
ATOM    483  CG  MET C  72      17.553  16.920  -7.637  1.00 42.91           C
ANISOU  483  CG  MET C  72     6316   5046   4942   -645    -92   -990       C
ATOM    484  SD  MET C  72      17.265  15.146  -7.794  1.00 44.17           S
ANISOU  484  SD  MET C  72     6500   5215   5069   -631   -160   -954       S
ATOM    485  CE  MET C  72      18.649  14.666  -8.823  1.00 41.51           C
ANISOU  485  CE  MET C  72     6173   4878   4720   -594   -194   -943       C
ATOM    486  N   ASN C  73      16.625  21.306  -6.832  1.00 42.35           N
ANISOU  486  N   ASN C  73     6180   4922   4990   -696    109  -1075       N
ATOM    487  CA  ASN C  73      17.384  22.454  -6.359  1.00 41.51           C
ANISOU  487  CA  ASN C  73     6058   4816   4897   -720    159  -1117       C
ATOM    488  C   ASN C  73      16.713  23.045  -5.126  1.00 42.90           C
ANISOU  488  C   ASN C  73     6225   4995   5079   -765    206  -1152       C
ATOM    489  O   ASN C  73      15.533  22.796  -4.879  1.00 43.63           O
ANISOU  489  O   ASN C  73     6318   5079   5179   -770    210  -1138       O
ATOM    490  CB  ASN C  73      17.491  23.506  -7.459  1.00 41.19           C
ANISOU  490  CB  ASN C  73     6002   4738   4911   -688    197  -1110       C
ATOM    491  CG  ASN C  73      18.187  22.983  -8.700  1.00 41.71           C
ANISOU  491  CG  ASN C  73     6076   4802   4969   -644    154  -1078       C
ATOM    492  OD1 ASN C  73      19.253  22.373  -8.618  1.00 41.92           O
ANISOU  492  OD1 ASN C  73     6115   4855   4959   -644    118  -1083       O
ATOM    493  ND2 ASN C  73      17.580  23.210  -9.859  1.00 42.29           N
ANISOU  493  ND2 ASN C  73     6143   4846   5078   -605    159  -1044       N
ATOM    494  N   GLU C  74      17.458  23.831  -4.355  1.00 59.67           N
ANISOU  494  N   GLU C  74     8340   7133   7199   -800    244  -1198       N
ATOM    495  CA  GLU C  74      16.937  24.361  -3.099  1.00 59.25           C
ANISOU  495  CA  GLU C  74     8279   7088   7144   -849    289  -1238       C
ATOM    496  C   GLU C  74      16.714  25.873  -3.112  1.00 59.24           C
ANISOU  496  C   GLU C  74     8256   7050   7201   -860    368  -1271       C
ATOM    497  O   GLU C  74      16.179  26.427  -2.151  1.00 60.22           O
ANISOU  497  O   GLU C  74     8374   7175   7333   -898    415  -1306       O
ATOM    498  CB  GLU C  74      17.849  23.971  -1.931  1.00 59.42           C
ANISOU  498  CB  GLU C  74     8307   7164   7106   -893    269  -1271       C
ATOM    499  CG  GLU C  74      17.921  22.473  -1.674  1.00 59.43           C
ANISOU  499  CG  GLU C  74     8327   7202   7051   -889    198  -1239       C
ATOM    500  CD  GLU C  74      18.887  22.116  -0.561  1.00 59.03           C
ANISOU  500  CD  GLU C  74     8279   7208   6941   -929    178  -1266       C
ATOM    501  OE1 GLU C  74      19.891  21.429  -0.843  0.00 58.96           O
ANISOU  501  OE1 GLU C  74     8277   7222   6901   -914    131  -1249       O
ATOM    502  OE2 GLU C  74      18.642  22.518   0.596  0.00 59.01           O
ANISOU  502  OE2 GLU C  74     8271   7228   6922   -977    211  -1303       O
ATOM    503  N   PHE C  75      17.115  26.540  -4.190  1.00 40.27           N
ANISOU  503  N   PHE C  75     5845   4616   4842   -825    386  -1259       N
ATOM    504  CA  PHE C  75      16.932  27.989  -4.276  1.00 40.29           C
ANISOU  504  CA  PHE C  75     5825   4577   4906   -832    465  -1286       C
ATOM    505  C   PHE C  75      15.467  28.379  -4.458  1.00 40.80           C
ANISOU  505  C   PHE C  75     5878   4603   5020   -819    502  -1265       C
ATOM    506  O   PHE C  75      14.695  27.657  -5.086  1.00 41.44           O
ANISOU  506  O   PHE C  75     5965   4678   5101   -787    465  -1217       O
ATOM    507  CB  PHE C  75      17.820  28.621  -5.359  1.00 40.02           C
ANISOU  507  CB  PHE C  75     5782   4520   4906   -799    476  -1277       C
ATOM    508  CG  PHE C  75      17.773  27.919  -6.688  1.00 40.25           C
ANISOU  508  CG  PHE C  75     5818   4540   4935   -743    424  -1218       C
ATOM    509  CD1 PHE C  75      16.657  28.012  -7.504  1.00 40.76           C
ANISOU  509  CD1 PHE C  75     5876   4572   5040   -708    433  -1176       C
ATOM    510  CD2 PHE C  75      18.866  27.195  -7.139  1.00 40.21           C
ANISOU  510  CD2 PHE C  75     5826   4561   4890   -727    370  -1206       C
ATOM    511  CE1 PHE C  75      16.622  27.375  -8.731  1.00 41.11           C
ANISOU  511  CE1 PHE C  75     5926   4613   5081   -660    386  -1125       C
ATOM    512  CE2 PHE C  75      18.838  26.560  -8.366  1.00 40.39           C
ANISOU  512  CE2 PHE C  75     5857   4578   4913   -677    325  -1157       C
ATOM    513  CZ  PHE C  75      17.714  26.649  -9.163  1.00 40.70           C
ANISOU  513  CZ  PHE C  75     5889   4587   4988   -645    333  -1117       C
ATOM    514  N   SER C  76      15.095  29.528  -3.900  1.00 41.72           N
ANISOU  514  N   SER C  76     5978   4693   5180   -846    578  -1303       N
ATOM    515  CA  SER C  76      13.704  29.968  -3.886  1.00 42.02           C
ANISOU  515  CA  SER C  76     6003   4695   5267   -840    622  -1288       C
ATOM    516  C   SER C  76      13.184  30.367  -5.265  1.00 42.69           C
ANISOU  516  C   SER C  76     6072   4736   5411   -784    633  -1236       C
ATOM    517  O   SER C  76      12.044  30.061  -5.616  1.00 43.39           O
ANISOU  517  O   SER C  76     6157   4812   5518   -762    625  -1195       O
ATOM    518  CB  SER C  76      13.520  31.127  -2.903  1.00 41.67           C
ANISOU  518  CB  SER C  76     5945   4633   5256   -884    706  -1347       C
ATOM    519  OG  SER C  76      13.847  30.733  -1.582  0.00 41.27           O
ANISOU  519  OG  SER C  76     5907   4628   5147   -938    696  -1394       O
ATOM    520  N   THR C  77      14.014  31.058  -6.039  1.00 47.24           N
ANISOU  520  N   THR C  77     6639   5292   6017   -763    652  -1235       N
ATOM    521  CA  THR C  77      13.606  31.524  -7.361  1.00 47.93           C
ANISOU  521  CA  THR C  77     6709   5341   6160   -711    665  -1184       C
ATOM    522  C   THR C  77      14.641  31.201  -8.432  1.00 47.81           C
ANISOU  522  C   THR C  77     6701   5336   6128   -675    620  -1158       C
ATOM    523  O   THR C  77      15.843  31.205  -8.171  1.00 47.28           O
ANISOU  523  O   THR C  77     6642   5288   6032   -693    610  -1191       O
ATOM    524  CB  THR C  77      13.354  33.047  -7.378  1.00 48.48           C
ANISOU  524  CB  THR C  77     6751   5359   6310   -713    759  -1201       C
ATOM    525  OG1 THR C  77      14.565  33.739  -7.048  1.00 48.16           O
ANISOU  525  OG1 THR C  77     6710   5317   6272   -739    790  -1252       O
ATOM    526  CG2 THR C  77      12.265  33.430  -6.385  1.00 48.57           C
ANISOU  526  CG2 THR C  77     6753   5354   6345   -745    811  -1226       C
ATOM    527  N   LEU C  78      14.159  30.919  -9.638  1.00 47.43           N
ANISOU  527  N   LEU C  78     6648   5277   6096   -626    593  -1099       N
ATOM    528  CA  LEU C  78      15.026  30.731 -10.794  1.00 47.44           C
ANISOU  528  CA  LEU C  78     6653   5283   6088   -588    558  -1070       C
ATOM    529  C   LEU C  78      14.742  31.830 -11.809  1.00 48.32           C
ANISOU  529  C   LEU C  78     6737   5351   6271   -551    610  -1037       C
ATOM    530  O   LEU C  78      13.798  31.729 -12.593  1.00 49.26           O
ANISOU  530  O   LEU C  78     6845   5459   6412   -517    602   -986       O
ATOM    531  CB  LEU C  78      14.794  29.360 -11.428  1.00 47.51           C
ANISOU  531  CB  LEU C  78     6681   5321   6048   -562    476  -1027       C
ATOM    532  CG  LEU C  78      15.634  29.049 -12.669  1.00 47.49           C
ANISOU  532  CG  LEU C  78     6685   5327   6032   -521    437   -996       C
ATOM    533  CD1 LEU C  78      17.103  28.885 -12.307  1.00 47.00           C
ANISOU  533  CD1 LEU C  78     6636   5287   5934   -539    420  -1034       C
ATOM    534  CD2 LEU C  78      15.108  27.815 -13.379  1.00 47.10           C
ANISOU  534  CD2 LEU C  78     6650   5298   5946   -494    367   -952       C
ATOM    535  N   PRO C  79      15.558  32.894 -11.792  1.00 55.09           N
ANISOU  535  N   PRO C  79     7582   6186   7166   -559    664  -1065       N
ATOM    536  CA  PRO C  79      15.331  34.056 -12.652  1.00 55.85           C
ANISOU  536  CA  PRO C  79     7649   6236   7336   -527    723  -1036       C
ATOM    537  C   PRO C  79      16.060  33.967 -13.990  1.00 56.56           C
ANISOU  537  C   PRO C  79     7738   6330   7423   -481    693   -995       C
ATOM    538  O   PRO C  79      17.281  34.113 -14.048  1.00 56.53           O
ANISOU  538  O   PRO C  79     7740   6333   7405   -487    690  -1020       O
ATOM    539  CB  PRO C  79      15.887  35.213 -11.817  1.00 55.15           C
ANISOU  539  CB  PRO C  79     7549   6120   7286   -565    799  -1095       C
ATOM    540  CG  PRO C  79      16.867  34.572 -10.839  1.00 54.46           C
ANISOU  540  CG  PRO C  79     7487   6075   7132   -609    763  -1151       C
ATOM    541  CD  PRO C  79      16.749  33.072 -10.948  1.00 54.28           C
ANISOU  541  CD  PRO C  79     7488   6098   7036   -599    673  -1126       C
ATOM    542  N   LEU C  80      15.303  33.727 -15.055  1.00 44.76           N
ANISOU  542  N   LEU C  80     6235   4833   5940   -437    671   -932       N
ATOM    543  CA  LEU C  80      15.839  33.737 -16.411  1.00 44.96           C
ANISOU  543  CA  LEU C  80     6255   4861   5968   -391    649   -888       C
ATOM    544  C   LEU C  80      15.090  34.785 -17.228  1.00 45.98           C
ANISOU  544  C   LEU C  80     6350   4952   6170   -356    705   -839       C
ATOM    545  O   LEU C  80      14.241  34.445 -18.051  1.00 47.09           O
ANISOU  545  O   LEU C  80     6481   5100   6311   -323    679   -783       O
ATOM    546  CB  LEU C  80      15.687  32.358 -17.056  1.00 44.89           C
ANISOU  546  CB  LEU C  80     6268   4893   5895   -369    563   -854       C
ATOM    547  CG  LEU C  80      16.455  31.202 -16.411  1.00 43.49           C
ANISOU  547  CG  LEU C  80     6124   4755   5645   -396    502   -891       C
ATOM    548  CD1 LEU C  80      15.913  29.865 -16.889  1.00 43.31           C
ANISOU  548  CD1 LEU C  80     6121   4764   5572   -379    427   -858       C
ATOM    549  CD2 LEU C  80      17.941  31.311 -16.712  1.00 42.72           C
ANISOU  549  CD2 LEU C  80     6035   4666   5532   -392    495   -910       C
ATOM    550  N   PRO C  81      15.408  36.070 -17.001  1.00 49.88           N
ANISOU  550  N   PRO C  81     6822   5404   6727   -365    783   -860       N
ATOM    551  CA  PRO C  81      14.645  37.180 -17.582  1.00 50.19           C
ANISOU  551  CA  PRO C  81     6824   5398   6846   -336    849   -816       C
ATOM    552  C   PRO C  81      14.911  37.390 -19.070  1.00 50.61           C
ANISOU  552  C   PRO C  81     6862   5452   6914   -283    838   -753       C
ATOM    553  O   PRO C  81      14.105  38.031 -19.742  1.00 51.80           O
ANISOU  553  O   PRO C  81     6983   5579   7119   -250    873   -699       O
ATOM    554  CB  PRO C  81      15.139  38.387 -16.785  1.00 49.60           C
ANISOU  554  CB  PRO C  81     6737   5281   6828   -367    933   -869       C
ATOM    555  CG  PRO C  81      16.539  38.036 -16.431  1.00 49.00           C
ANISOU  555  CG  PRO C  81     6686   5230   6702   -393    904   -920       C
ATOM    556  CD  PRO C  81      16.548  36.548 -16.199  1.00 48.95           C
ANISOU  556  CD  PRO C  81     6712   5279   6610   -403    815   -925       C
ATOM    557  N   ASN C  82      16.021  36.864 -19.575  1.00 39.04           N
ANISOU  557  N   ASN C  82     5417   4016   5401   -273    791   -758       N
ATOM    558  CA  ASN C  82      16.361  37.030 -20.985  1.00 39.77           C
ANISOU  558  CA  ASN C  82     5497   4112   5501   -225    780   -701       C
ATOM    559  C   ASN C  82      16.031  35.811 -21.842  1.00 40.23           C
ANISOU  559  C   ASN C  82     5571   4217   5496   -197    696   -658       C
ATOM    560  O   ASN C  82      16.131  35.864 -23.067  1.00 41.12           O
ANISOU  560  O   ASN C  82     5674   4341   5610   -155    682   -605       O
ATOM    561  CB  ASN C  82      17.834  37.411 -21.148  1.00 39.69           C
ANISOU  561  CB  ASN C  82     5493   4097   5489   -228    793   -729       C
ATOM    562  CG  ASN C  82      18.077  38.893 -20.939  1.00 40.03           C
ANISOU  562  CG  ASN C  82     5507   4086   5614   -234    886   -742       C
ATOM    563  OD1 ASN C  82      18.244  39.355 -19.811  1.00 40.07           O
ANISOU  563  OD1 ASN C  82     5514   4069   5640   -277    929   -802       O
ATOM    564  ND2 ASN C  82      18.096  39.647 -22.032  1.00 40.69           N
ANISOU  564  ND2 ASN C  82     5564   4149   5746   -191    919   -687       N
ATOM    565  N   LEU C  83      15.637  34.717 -21.195  1.00 34.14           N
ANISOU  565  N   LEU C  83     4825   3475   4671   -221    643   -680       N
ATOM    566  CA  LEU C  83      15.277  33.493 -21.906  1.00 34.32           C
ANISOU  566  CA  LEU C  83     4864   3540   4634   -201    564   -647       C
ATOM    567  C   LEU C  83      14.044  33.703 -22.789  1.00 35.34           C
ANISOU  567  C   LEU C  83     4966   3669   4791   -166    568   -579       C
ATOM    568  O   LEU C  83      12.950  33.956 -22.278  1.00 35.07           O
ANISOU  568  O   LEU C  83     4916   3620   4790   -177    594   -571       O
ATOM    569  CB  LEU C  83      15.036  32.350 -20.914  1.00 33.79           C
ANISOU  569  CB  LEU C  83     4827   3499   4512   -237    515   -686       C
ATOM    570  CG  LEU C  83      14.628  31.008 -21.528  1.00 33.91           C
ANISOU  570  CG  LEU C  83     4863   3556   4467   -222    434   -658       C
ATOM    571  CD1 LEU C  83      15.763  30.418 -22.355  1.00 34.06           C
ANISOU  571  CD1 LEU C  83     4901   3599   4439   -202    389   -655       C
ATOM    572  CD2 LEU C  83      14.180  30.032 -20.453  1.00 33.02           C
ANISOU  572  CD2 LEU C  83     4773   3459   4313   -259    398   -692       C
ATOM    573  N   ARG C  84      14.239  33.604 -24.105  1.00 47.81           N
ANISOU  573  N   ARG C  84     6539   5268   6360   -126    543   -529       N
ATOM    574  CA  ARG C  84      13.170  33.811 -25.076  1.00 49.58           C
ANISOU  574  CA  ARG C  84     6733   5499   6605    -90    543   -459       C
ATOM    575  C   ARG C  84      12.757  32.517 -25.778  1.00 50.02           C
ANISOU  575  C   ARG C  84     6807   5605   6593    -78    461   -433       C
ATOM    576  O   ARG C  84      11.567  32.261 -25.971  1.00 50.57           O
ANISOU  576  O   ARG C  84     6862   5687   6666    -72    445   -398       O
ATOM    577  CB  ARG C  84      13.583  34.870 -26.103  1.00 50.67           C
ANISOU  577  CB  ARG C  84     6843   5621   6790    -52    588   -414       C
ATOM    578  CG  ARG C  84      13.768  36.269 -25.576  1.00 51.66           C
ANISOU  578  CG  ARG C  84     6942   5691   6995    -58    677   -426       C
ATOM    579  CD  ARG C  84      13.243  37.272 -26.636  1.00 53.51           C
ANISOU  579  CD  ARG C  84     7132   5909   7289    -14    722   -350       C
ATOM    580  NE  ARG C  84      12.040  38.034 -26.308  1.00 54.36           N
ANISOU  580  NE  ARG C  84     7205   5985   7465    -11    777   -321       N
ATOM    581  CZ  ARG C  84      11.548  38.938 -27.151  1.00 55.39           C
ANISOU  581  CZ  ARG C  84     7294   6100   7653     28    820   -252       C
ATOM    582  NH1 ARG C  84      10.453  39.637 -26.887  0.00 56.18           N
ANISOU  582  NH1 ARG C  84     7359   6169   7818     33    872   -221       N
ATOM    583  NH2 ARG C  84      12.221  39.217 -28.259  0.00 55.24           N
ANISOU  583  NH2 ARG C  84     7265   6093   7631     62    818   -213       N
ATOM    584  N   VAL C  85      13.739  31.681 -26.101  1.00 31.34           N
ANISOU  584  N   VAL C  85     4473   3267   4169    -78    410   -455       N
ATOM    585  CA  VAL C  85      13.500  30.521 -26.944  1.00 31.81           C
ANISOU  585  CA  VAL C  85     4549   3371   4166    -63    337   -431       C
ATOM    586  C   VAL C  85      14.203  29.260 -26.450  1.00 30.75           C
ANISOU  586  C   VAL C  85     4459   3259   3966    -87    278   -482       C
ATOM    587  O   VAL C  85      15.398  29.276 -26.150  1.00 30.13           O
ANISOU  587  O   VAL C  85     4398   3174   3876    -96    283   -520       O
ATOM    588  CB  VAL C  85      13.940  30.804 -28.402  1.00 32.45           C
ANISOU  588  CB  VAL C  85     4617   3471   4242    -20    331   -383       C
ATOM    589  CG1 VAL C  85      13.969  29.522 -29.219  1.00 32.62           C
ANISOU  589  CG1 VAL C  85     4663   3540   4190    -10    255   -374       C
ATOM    590  CG2 VAL C  85      13.026  31.832 -29.050  1.00 33.49           C
ANISOU  590  CG2 VAL C  85     4703   3592   4430      8    376   -319       C
ATOM    591  N   VAL C  86      13.442  28.174 -26.358  1.00 32.37           N
ANISOU  591  N   VAL C  86     4679   3488   4131    -99    225   -481       N
ATOM    592  CA  VAL C  86      14.005  26.845 -26.169  1.00 31.57           C
ANISOU  592  CA  VAL C  86     4618   3412   3965   -114    163   -516       C
ATOM    593  C   VAL C  86      13.750  26.044 -27.443  1.00 32.20           C
ANISOU  593  C   VAL C  86     4704   3529   4002    -88    109   -480       C
ATOM    594  O   VAL C  86      12.613  25.664 -27.725  1.00 32.71           O
ANISOU  594  O   VAL C  86     4759   3610   4060    -87     85   -452       O
ATOM    595  CB  VAL C  86      13.372  26.120 -24.968  1.00 30.92           C
ANISOU  595  CB  VAL C  86     4551   3328   3868   -152    143   -548       C
ATOM    596  CG1 VAL C  86      13.926  24.710 -24.848  1.00 30.10           C
ANISOU  596  CG1 VAL C  86     4487   3248   3701   -164     79   -577       C
ATOM    597  CG2 VAL C  86      13.614  26.903 -23.686  1.00 30.42           C
ANISOU  597  CG2 VAL C  86     4483   3233   3844   -180    198   -586       C
ATOM    598  N   ARG C  87      14.807  25.798 -28.213  1.00 31.16           N
ANISOU  598  N   ARG C  87     4587   3412   3841    -69     90   -483       N
ATOM    599  CA  ARG C  87      14.673  25.175 -29.530  1.00 31.76           C
ANISOU  599  CA  ARG C  87     4667   3524   3876    -43     46   -450       C
ATOM    600  C   ARG C  87      14.191  23.729 -29.464  1.00 30.99           C
ANISOU  600  C   ARG C  87     4597   3451   3726    -60    -19   -465       C
ATOM    601  O   ARG C  87      13.271  23.340 -30.183  1.00 31.34           O
ANISOU  601  O   ARG C  87     4633   3521   3753    -52    -48   -433       O
ATOM    602  CB  ARG C  87      15.990  25.253 -30.307  1.00 31.41           C
ANISOU  602  CB  ARG C  87     4634   3487   3813    -19     45   -454       C
ATOM    603  CG  ARG C  87      16.510  26.666 -30.517  1.00 31.95           C
ANISOU  603  CG  ARG C  87     4674   3532   3933      0    108   -435       C
ATOM    604  CD  ARG C  87      17.583  26.696 -31.591  1.00 31.72           C
ANISOU  604  CD  ARG C  87     4652   3519   3882     29    101   -424       C
ATOM    605  NE  ARG C  87      17.022  26.470 -32.920  1.00 33.23           N
ANISOU  605  NE  ARG C  87     4831   3746   4047     57     75   -375       N
ATOM    606  CZ  ARG C  87      16.853  27.421 -33.832  1.00 34.12           C
ANISOU  606  CZ  ARG C  87     4912   3864   4188     88    107   -323       C
ATOM    607  NH1 ARG C  87      17.214  28.669 -33.567  1.00 34.25           N
ANISOU  607  NH1 ARG C  87     4904   3847   4263     95    170   -314       N
ATOM    608  NH2 ARG C  87      16.332  27.123 -35.014  1.00 35.21           N
ANISOU  608  NH2 ARG C  87     5041   4043   4295    110     77   -280       N
ATOM    609  N   GLY C  88      14.823  22.934 -28.607  1.00 38.59           N
ANISOU  609  N   GLY C  88     5593   4407   4663    -84    -41   -513       N
ATOM    610  CA  GLY C  88      14.425  21.551 -28.422  1.00 37.30           C
ANISOU  610  CA  GLY C  88     5457   4261   4455   -102    -98   -531       C
ATOM    611  C   GLY C  88      14.979  20.600 -29.467  1.00 37.12           C
ANISOU  611  C   GLY C  88     5458   4266   4381    -85   -145   -531       C
ATOM    612  O   GLY C  88      14.345  19.596 -29.790  1.00 37.48           O
ANISOU  612  O   GLY C  88     5516   4331   4393    -92   -190   -529       O
ATOM    613  N   THR C  89      16.159  20.914 -29.997  1.00 40.39           N
ANISOU  613  N   THR C  89     5878   4680   4790    -64   -133   -535       N
ATOM    614  CA  THR C  89      16.830  20.032 -30.948  1.00 39.87           C
ANISOU  614  CA  THR C  89     5836   4637   4676    -48   -172   -541       C
ATOM    615  C   THR C  89      17.153  18.709 -30.265  1.00 38.66           C
ANISOU  615  C   THR C  89     5720   4481   4489    -71   -213   -582       C
ATOM    616  O   THR C  89      17.173  17.652 -30.897  1.00 38.91           O
ANISOU  616  O   THR C  89     5773   4532   4480    -67   -256   -587       O
ATOM    617  CB  THR C  89      18.123  20.660 -31.501  1.00 39.82           C
ANISOU  617  CB  THR C  89     5828   4628   4674    -23   -147   -540       C
ATOM    618  OG1 THR C  89      19.028  20.924 -30.422  1.00 39.60           O
ANISOU  618  OG1 THR C  89     5808   4574   4665    -38   -123   -575       O
ATOM    619  CG2 THR C  89      17.816  21.958 -32.228  1.00 41.08           C
ANISOU  619  CG2 THR C  89     5951   4790   4870      2   -105   -495       C
ATOM    620  N   GLN C  90      17.411  18.789 -28.964  1.00 50.23           N
ANISOU  620  N   GLN C  90     7190   5923   5971    -95   -198   -610       N
ATOM    621  CA  GLN C  90      17.505  17.613 -28.114  1.00 49.14           C
ANISOU  621  CA  GLN C  90     7082   5782   5809   -120   -233   -642       C
ATOM    622  C   GLN C  90      16.470  17.785 -27.008  1.00 49.34           C
ANISOU  622  C   GLN C  90     7095   5795   5858   -150   -221   -644       C
ATOM    623  O   GLN C  90      16.435  18.822 -26.346  1.00 49.72           O
ANISOU  623  O   GLN C  90     7122   5826   5943   -157   -177   -645       O
ATOM    624  CB  GLN C  90      18.913  17.488 -27.527  1.00 48.37           C
ANISOU  624  CB  GLN C  90     7001   5673   5705   -123   -227   -674       C
ATOM    625  CG  GLN C  90      19.235  16.123 -26.939  1.00 48.40           C
ANISOU  625  CG  GLN C  90     7037   5677   5676   -140   -268   -701       C
ATOM    626  CD  GLN C  90      20.714  15.951 -26.637  1.00 49.04           C
ANISOU  626  CD  GLN C  90     7131   5753   5747   -135   -265   -725       C
ATOM    627  OE1 GLN C  90      21.165  16.197 -25.517  1.00 48.96           O
ANISOU  627  OE1 GLN C  90     7119   5733   5748   -155   -249   -744       O
ATOM    628  NE2 GLN C  90      21.477  15.526 -27.639  1.00 49.01           N
ANISOU  628  NE2 GLN C  90     7141   5759   5721   -109   -282   -723       N
ATOM    629  N   VAL C  91      15.608  16.788 -26.825  1.00 35.59           N
ANISOU  629  N   VAL C  91     5366   4060   4096   -167   -258   -646       N
ATOM    630  CA  VAL C  91      14.571  16.870 -25.799  1.00 35.07           C
ANISOU  630  CA  VAL C  91     5290   3984   4051   -195   -249   -647       C
ATOM    631  C   VAL C  91      14.766  15.835 -24.703  1.00 33.12           C
ANISOU  631  C   VAL C  91     5071   3731   3784   -223   -274   -678       C
ATOM    632  O   VAL C  91      15.403  14.801 -24.916  1.00 33.47           O
ANISOU  632  O   VAL C  91     5141   3780   3795   -220   -310   -693       O
ATOM    633  CB  VAL C  91      13.155  16.712 -26.384  1.00 36.60           C
ANISOU  633  CB  VAL C  91     5469   4192   4246   -195   -265   -617       C
ATOM    634  CG1 VAL C  91      12.749  17.967 -27.138  1.00 37.97           C
ANISOU  634  CG1 VAL C  91     5607   4370   4452   -172   -229   -580       C
ATOM    635  CG2 VAL C  91      13.077  15.477 -27.270  1.00 37.32           C
ANISOU  635  CG2 VAL C  91     5583   4304   4294   -189   -318   -617       C
ATOM    636  N   TYR C  92      14.200  16.116 -23.534  1.00 41.54           N
ANISOU  636  N   TYR C  92     6127   4785   4871   -250   -255   -687       N
ATOM    637  CA  TYR C  92      14.362  15.238 -22.384  1.00 40.88           C
ANISOU  637  CA  TYR C  92     6066   4697   4770   -278   -274   -713       C
ATOM    638  C   TYR C  92      13.362  14.081 -22.400  1.00 41.37           C
ANISOU  638  C   TYR C  92     6140   4765   4813   -292   -316   -706       C
ATOM    639  O   TYR C  92      12.155  14.294 -22.543  1.00 42.08           O
ANISOU  639  O   TYR C  92     6213   4858   4919   -297   -312   -686       O
ATOM    640  CB  TYR C  92      14.251  16.026 -21.079  1.00 41.23           C
ANISOU  640  CB  TYR C  92     6096   4729   4840   -303   -234   -727       C
ATOM    641  CG  TYR C  92      14.708  15.221 -19.895  1.00 40.81           C
ANISOU  641  CG  TYR C  92     6064   4676   4765   -330   -251   -754       C
ATOM    642  CD1 TYR C  92      16.051  15.149 -19.562  1.00 40.49           C
ANISOU  642  CD1 TYR C  92     6036   4638   4710   -329   -251   -775       C
ATOM    643  CD2 TYR C  92      13.802  14.508 -19.129  1.00 40.69           C
ANISOU  643  CD2 TYR C  92     6055   4661   4743   -356   -269   -755       C
ATOM    644  CE1 TYR C  92      16.475  14.401 -18.493  1.00 40.00           C
ANISOU  644  CE1 TYR C  92     5991   4581   4627   -352   -268   -795       C
ATOM    645  CE2 TYR C  92      14.217  13.758 -18.059  1.00 40.04           C
ANISOU  645  CE2 TYR C  92     5991   4582   4640   -379   -285   -775       C
ATOM    646  CZ  TYR C  92      15.552  13.708 -17.745  1.00 39.88           C
ANISOU  646  CZ  TYR C  92     5981   4566   4604   -377   -284   -793       C
ATOM    647  OH  TYR C  92      15.965  12.959 -16.677  1.00 39.54           O
ANISOU  647  OH  TYR C  92     5953   4530   4539   -400   -301   -808       O
ATOM    648  N   ASP C  93      13.884  12.862 -22.249  1.00 54.67           N
ANISOU  648  N   ASP C  93     7854   6451   6466   -297   -353   -722       N
ATOM    649  CA  ASP C  93      13.089  11.631 -22.288  1.00 54.40           C
ANISOU  649  CA  ASP C  93     7836   6420   6414   -311   -394   -720       C
ATOM    650  C   ASP C  93      12.261  11.521 -23.566  1.00 54.87           C
ANISOU  650  C   ASP C  93     7887   6492   6469   -297   -412   -698       C
ATOM    651  O   ASP C  93      11.195  10.902 -23.575  1.00 55.49           O
ANISOU  651  O   ASP C  93     7966   6575   6545   -312   -434   -690       O
ATOM    652  CB  ASP C  93      12.196  11.513 -21.047  1.00 54.83           C
ANISOU  652  CB  ASP C  93     7884   6467   6480   -344   -387   -722       C
ATOM    653  CG  ASP C  93      12.444  10.234 -20.261  1.00 55.18           C
ANISOU  653  CG  ASP C  93     7956   6507   6502   -363   -418   -738       C
ATOM    654  OD1 ASP C  93      11.646   9.282 -20.393  1.00 55.25           O
ANISOU  654  OD1 ASP C  93     7975   6516   6502   -374   -449   -733       O
ATOM    655  OD2 ASP C  93      13.436  10.182 -19.504  1.00 55.50           O
ANISOU  655  OD2 ASP C  93     8007   6545   6536   -368   -412   -755       O
ATOM    656  N   GLY C  94      12.762  12.123 -24.642  1.00 34.07           N
ANISOU  656  N   GLY C  94     5245   3867   3834   -268   -402   -688       N
ATOM    657  CA  GLY C  94      12.086  12.098 -25.926  1.00 34.54           C
ANISOU  657  CA  GLY C  94     5294   3946   3885   -253   -418   -665       C
ATOM    658  C   GLY C  94      10.819  12.932 -25.982  1.00 36.00           C
ANISOU  658  C   GLY C  94     5444   4137   4098   -257   -398   -635       C
ATOM    659  O   GLY C  94      10.121  12.933 -26.998  1.00 36.65           O
ANISOU  659  O   GLY C  94     5513   4240   4173   -247   -413   -612       O
ATOM    660  N   LYS C  95      10.528  13.660 -24.906  1.00 44.47           N
ANISOU  660  N   LYS C  95     6500   5194   5201   -271   -364   -636       N
ATOM    661  CA  LYS C  95       9.229  14.309 -24.773  1.00 45.26           C
ANISOU  661  CA  LYS C  95     6569   5296   5331   -279   -345   -609       C
ATOM    662  C   LYS C  95       9.262  15.781 -24.372  1.00 46.12           C
ANISOU  662  C   LYS C  95     6649   5392   5484   -272   -287   -598       C
ATOM    663  O   LYS C  95       8.429  16.565 -24.826  1.00 47.19           O
ANISOU  663  O   LYS C  95     6753   5533   5646   -262   -267   -565       O
ATOM    664  CB  LYS C  95       8.358  13.527 -23.783  1.00 44.77           C
ANISOU  664  CB  LYS C  95     6514   5227   5268   -312   -362   -619       C
ATOM    665  CG  LYS C  95       7.399  12.565 -24.453  1.00 45.69           C
ANISOU  665  CG  LYS C  95     6634   5361   5365   -319   -405   -606       C
ATOM    666  CD  LYS C  95       6.955  11.455 -23.522  1.00 44.95           C
ANISOU  666  CD  LYS C  95     6560   5258   5260   -351   -431   -624       C
ATOM    667  CE  LYS C  95       6.686  10.190 -24.317  1.00 44.74           C
ANISOU  667  CE  LYS C  95     6552   5244   5201   -355   -481   -628       C
ATOM    668  NZ  LYS C  95       5.787  10.452 -25.476  1.00 45.44           N
ANISOU  668  NZ  LYS C  95     6616   5358   5289   -345   -493   -599       N
ATOM    669  N   PHE C  96      10.213  16.158 -23.525  1.00 31.36           N
ANISOU  669  N   PHE C  96     4789   3505   3622   -278   -261   -624       N
ATOM    670  CA  PHE C  96      10.135  17.461 -22.868  1.00 31.91           C
ANISOU  670  CA  PHE C  96     4833   3557   3735   -281   -204   -623       C
ATOM    671  C   PHE C  96      11.307  18.416 -23.124  1.00 31.48           C
ANISOU  671  C   PHE C  96     4773   3494   3694   -261   -169   -629       C
ATOM    672  O   PHE C  96      12.470  18.069 -22.909  1.00 30.37           O
ANISOU  672  O   PHE C  96     4655   3353   3532   -262   -178   -656       O
ATOM    673  CB  PHE C  96       9.923  17.274 -21.361  1.00 30.47           C
ANISOU  673  CB  PHE C  96     4658   3361   3558   -316   -192   -649       C
ATOM    674  CG  PHE C  96       8.737  16.412 -21.016  1.00 30.46           C
ANISOU  674  CG  PHE C  96     4659   3365   3548   -337   -221   -642       C
ATOM    675  CD1 PHE C  96       8.916  15.145 -20.479  1.00 29.62           C
ANISOU  675  CD1 PHE C  96     4583   3263   3408   -357   -262   -662       C
ATOM    676  CD2 PHE C  96       7.445  16.865 -21.233  1.00 31.36           C
ANISOU  676  CD2 PHE C  96     4744   3481   3690   -337   -208   -612       C
ATOM    677  CE1 PHE C  96       7.827  14.349 -20.162  1.00 29.63           C
ANISOU  677  CE1 PHE C  96     4586   3268   3404   -378   -287   -655       C
ATOM    678  CE2 PHE C  96       6.353  16.072 -20.918  1.00 31.38           C
ANISOU  678  CE2 PHE C  96     4748   3490   3686   -358   -234   -604       C
ATOM    679  CZ  PHE C  96       6.545  14.814 -20.381  1.00 30.49           C
ANISOU  679  CZ  PHE C  96     4666   3380   3540   -379   -274   -627       C
ATOM    680  N   ALA C  97      10.977  19.624 -23.579  1.00 27.74           N
ANISOU  680  N   ALA C  97     4267   3014   3260   -243   -126   -602       N
ATOM    681  CA  ALA C  97      11.955  20.694 -23.748  1.00 27.75           C
ANISOU  681  CA  ALA C  97     4258   3002   3284   -227    -84   -606       C
ATOM    682  C   ALA C  97      12.225  21.385 -22.413  1.00 27.73           C
ANISOU  682  C   ALA C  97     4251   2976   3311   -252    -38   -638       C
ATOM    683  O   ALA C  97      13.310  21.923 -22.190  1.00 27.68           O
ANISOU  683  O   ALA C  97     4248   2959   3311   -251    -12   -659       O
ATOM    684  CB  ALA C  97      11.465  21.701 -24.774  1.00 27.97           C
ANISOU  684  CB  ALA C  97     4251   3031   3346   -197    -55   -562       C
ATOM    685  N   ILE C  98      11.225  21.381 -21.537  1.00 33.28           N
ANISOU  685  N   ILE C  98     4945   3670   4030   -277    -27   -640       N
ATOM    686  CA  ILE C  98      11.382  21.917 -20.188  1.00 32.42           C
ANISOU  686  CA  ILE C  98     4834   3542   3941   -307     14   -674       C
ATOM    687  C   ILE C  98      10.976  20.881 -19.142  1.00 31.91           C
ANISOU  687  C   ILE C  98     4791   3486   3848   -341    -17   -697       C
ATOM    688  O   ILE C  98       9.844  20.396 -19.141  1.00 32.71           O
ANISOU  688  O   ILE C  98     4888   3593   3948   -347    -36   -678       O
ATOM    689  CB  ILE C  98      10.564  23.206 -19.978  1.00 33.25           C
ANISOU  689  CB  ILE C  98     4903   3624   4105   -307     77   -658       C
ATOM    690  CG1 ILE C  98      11.064  24.316 -20.906  1.00 33.74           C
ANISOU  690  CG1 ILE C  98     4944   3675   4202   -274    114   -636       C
ATOM    691  CG2 ILE C  98      10.651  23.659 -18.531  1.00 32.50           C
ANISOU  691  CG2 ILE C  98     4809   3512   4028   -343    117   -699       C
ATOM    692  CD1 ILE C  98      10.366  25.643 -20.701  1.00 34.45           C
ANISOU  692  CD1 ILE C  98     4997   3737   4356   -272    182   -620       C
ATOM    693  N   PHE C  99      11.906  20.552 -18.252  1.00 33.06           N
ANISOU  693  N   PHE C  99     4958   3634   3970   -362    -22   -735       N
ATOM    694  CA  PHE C  99      11.677  19.522 -17.245  1.00 32.40           C
ANISOU  694  CA  PHE C  99     4895   3561   3855   -393    -53   -754       C
ATOM    695  C   PHE C  99      11.985  20.052 -15.846  1.00 31.88           C
ANISOU  695  C   PHE C  99     4827   3488   3797   -427    -14   -791       C
ATOM    696  O   PHE C  99      13.145  20.258 -15.492  1.00 31.63           O
ANISOU  696  O   PHE C  99     4804   3460   3754   -434     -6   -818       O
ATOM    697  CB  PHE C  99      12.544  18.298 -17.550  1.00 32.21           C
ANISOU  697  CB  PHE C  99     4902   3554   3783   -387   -109   -762       C
ATOM    698  CG  PHE C  99      12.083  17.036 -16.875  1.00 31.73           C
ANISOU  698  CG  PHE C  99     4862   3503   3691   -410   -150   -767       C
ATOM    699  CD1 PHE C  99      11.247  16.150 -17.534  1.00 31.61           C
ANISOU  699  CD1 PHE C  99     4852   3493   3663   -402   -190   -743       C
ATOM    700  CD2 PHE C  99      12.494  16.730 -15.588  1.00 31.05           C
ANISOU  700  CD2 PHE C  99     4788   3422   3588   -441   -148   -795       C
ATOM    701  CE1 PHE C  99      10.827  14.984 -16.922  1.00 31.25           C
ANISOU  701  CE1 PHE C  99     4826   3455   3594   -423   -226   -748       C
ATOM    702  CE2 PHE C  99      12.076  15.567 -14.970  1.00 31.06           C
ANISOU  702  CE2 PHE C  99     4807   3432   3562   -461   -185   -796       C
ATOM    703  CZ  PHE C  99      11.241  14.693 -15.637  1.00 30.92           C
ANISOU  703  CZ  PHE C  99     4796   3415   3536   -452   -222   -772       C
ATOM    704  N   VAL C 100      10.938  20.270 -15.055  1.00 27.73           N
ANISOU  704  N   VAL C 100     4289   2955   3290   -450      9   -792       N
ATOM    705  CA  VAL C 100      11.085  20.810 -13.706  1.00 27.84           C
ANISOU  705  CA  VAL C 100     4300   2964   3312   -486     50   -829       C
ATOM    706  C   VAL C 100      10.515  19.844 -12.671  1.00 27.83           C
ANISOU  706  C   VAL C 100     4314   2978   3282   -518     23   -838       C
ATOM    707  O   VAL C 100       9.318  19.560 -12.679  1.00 27.90           O
ANISOU  707  O   VAL C 100     4315   2983   3301   -520     17   -817       O
ATOM    708  CB  VAL C 100      10.370  22.170 -13.572  1.00 28.07           C
ANISOU  708  CB  VAL C 100     4299   2969   3399   -487    117   -826       C
ATOM    709  CG1 VAL C 100      10.618  22.771 -12.198  1.00 28.22           C
ANISOU  709  CG1 VAL C 100     4315   2984   3424   -527    163   -870       C
ATOM    710  CG2 VAL C 100      10.828  23.124 -14.664  1.00 28.11           C
ANISOU  710  CG2 VAL C 100     4286   2958   3437   -453    145   -809       C
ATOM    711  N   MET C 101      11.365  19.346 -11.776  1.00 30.65           N
ANISOU  711  N   MET C 101     4690   3352   3602   -542      8   -868       N
ATOM    712  CA  MET C 101      10.938  18.326 -10.821  1.00 30.40           C
ANISOU  712  CA  MET C 101     4674   3337   3538   -570    -21   -873       C
ATOM    713  C   MET C 101      11.705  18.343  -9.495  1.00 30.06           C
ANISOU  713  C   MET C 101     4640   3312   3468   -606     -9   -911       C
ATOM    714  O   MET C 101      12.924  18.508  -9.473  1.00 29.83           O
ANISOU  714  O   MET C 101     4616   3293   3424   -605    -11   -929       O
ATOM    715  CB  MET C 101      11.047  16.937 -11.458  1.00 30.18           C
ANISOU  715  CB  MET C 101     4670   3321   3477   -553    -87   -850       C
ATOM    716  CG  MET C 101      10.383  15.828 -10.659  1.00 30.04           C
ANISOU  716  CG  MET C 101     4666   3315   3433   -578   -118   -846       C
ATOM    717  SD  MET C 101      10.747  14.182 -11.300  1.00 29.83           S
ANISOU  717  SD  MET C 101     4667   3297   3368   -561   -191   -827       S
ATOM    718  CE  MET C 101      12.492  14.049 -10.918  1.00 29.33           C
ANISOU  718  CE  MET C 101     4619   3250   3273   -562   -200   -851       C
ATOM    719  N   LEU C 102      10.968  18.174  -8.397  1.00 38.77           N
ANISOU  719  N   LEU C 102     5742   4422   4565   -639      2   -921       N
ATOM    720  CA  LEU C 102      11.539  17.957  -7.063  1.00 38.32           C
ANISOU  720  CA  LEU C 102     5694   4391   4473   -678      4   -952       C
ATOM    721  C   LEU C 102      12.378  19.100  -6.499  1.00 38.74           C
ANISOU  721  C   LEU C 102     5737   4449   4535   -697     53   -992       C
ATOM    722  O   LEU C 102      13.266  18.869  -5.679  1.00 39.18           O
ANISOU  722  O   LEU C 102     5801   4532   4554   -721     44  -1016       O
ATOM    723  CB  LEU C 102      12.362  16.665  -7.027  1.00 38.06           C
ANISOU  723  CB  LEU C 102     5686   4383   4392   -674    -56   -943       C
ATOM    724  CG  LEU C 102      11.640  15.370  -6.662  1.00 38.31           C
ANISOU  724  CG  LEU C 102     5732   4424   4399   -683    -98   -921       C
ATOM    725  CD1 LEU C 102      12.624  14.217  -6.678  1.00 38.32           C
ANISOU  725  CD1 LEU C 102     5755   4445   4359   -676   -151   -913       C
ATOM    726  CD2 LEU C 102      10.980  15.490  -5.300  1.00 38.16           C
ANISOU  726  CD2 LEU C 102     5709   4419   4373   -724    -72   -937       C
ATOM    727  N   ASN C 103      12.092  20.327  -6.913  1.00 37.76           N
ANISOU  727  N   ASN C 103     5592   4297   4459   -688    106   -998       N
ATOM    728  CA  ASN C 103      12.876  21.467  -6.450  1.00 36.88           C
ANISOU  728  CA  ASN C 103     5468   4183   4360   -706    157  -1038       C
ATOM    729  C   ASN C 103      12.453  21.974  -5.071  1.00 37.74           C
ANISOU  729  C   ASN C 103     5570   4301   4468   -753    202  -1075       C
ATOM    730  O   ASN C 103      11.916  23.075  -4.940  1.00 38.17           O
ANISOU  730  O   ASN C 103     5606   4330   4568   -761    262  -1091       O
ATOM    731  CB  ASN C 103      12.844  22.594  -7.482  1.00 36.80           C
ANISOU  731  CB  ASN C 103     5439   4138   4406   -676    198  -1029       C
ATOM    732  CG  ASN C 103      13.438  22.177  -8.813  1.00 37.34           C
ANISOU  732  CG  ASN C 103     5515   4204   4470   -632    157   -998       C
ATOM    733  OD1 ASN C 103      14.656  22.181  -8.992  1.00 37.11           O
ANISOU  733  OD1 ASN C 103     5492   4186   4423   -627    144  -1011       O
ATOM    734  ND2 ASN C 103      12.578  21.807  -9.754  1.00 37.60           N
ANISOU  734  ND2 ASN C 103     5545   4223   4518   -602    135   -957       N
ATOM    735  N   TYR C 104      12.703  21.160  -4.047  1.00 50.89           N
ANISOU  735  N   TYR C 104     7250   6002   6082   -784    173  -1088       N
ATOM    736  CA  TYR C 104      12.412  21.540  -2.666  1.00 51.01           C
ANISOU  736  CA  TYR C 104     7261   6035   6085   -833    211  -1126       C
ATOM    737  C   TYR C 104      13.215  20.698  -1.668  1.00 51.36           C
ANISOU  737  C   TYR C 104     7320   6128   6065   -864    173  -1141       C
ATOM    738  O   TYR C 104      13.644  19.589  -1.984  1.00 51.28           O
ANISOU  738  O   TYR C 104     7326   6135   6022   -846    113  -1113       O
ATOM    739  CB  TYR C 104      10.909  21.447  -2.380  1.00 51.10           C
ANISOU  739  CB  TYR C 104     7267   6032   6119   -839    228  -1110       C
ATOM    740  CG  TYR C 104      10.339  20.049  -2.431  1.00 51.26           C
ANISOU  740  CG  TYR C 104     7303   6066   6109   -830    168  -1072       C
ATOM    741  CD1 TYR C 104      10.192  19.301  -1.272  1.00 50.85           C
ANISOU  741  CD1 TYR C 104     7262   6047   6011   -865    150  -1079       C
ATOM    742  CD2 TYR C 104       9.938  19.482  -3.634  1.00 51.16           C
ANISOU  742  CD2 TYR C 104     7293   6033   6112   -789    130  -1028       C
ATOM    743  CE1 TYR C 104       9.668  18.024  -1.308  1.00 51.00           C
ANISOU  743  CE1 TYR C 104     7295   6076   6007   -858     98  -1044       C
ATOM    744  CE2 TYR C 104       9.413  18.205  -3.679  1.00 50.84           C
ANISOU  744  CE2 TYR C 104     7267   6003   6046   -783     78   -996       C
ATOM    745  CZ  TYR C 104       9.280  17.481  -2.513  1.00 50.81           C
ANISOU  745  CZ  TYR C 104     7274   6029   6002   -817     62  -1003       C
ATOM    746  OH  TYR C 104       8.759  16.210  -2.549  1.00 51.09           O
ANISOU  746  OH  TYR C 104     7323   6071   6016   -812     13   -971       O
ATOM    747  N   ASN C 105      13.406  21.233  -0.465  1.00 78.76           N
ANISOU  747  N   ASN C 105    10786   9623   9518   -910    210  -1185       N
ATOM    748  CA  ASN C 105      14.260  20.615   0.550  1.00 79.22           C
ANISOU  748  CA  ASN C 105    10853   9733   9513   -944    181  -1202       C
ATOM    749  C   ASN C 105      13.580  19.463   1.309  1.00 79.74           C
ANISOU  749  C   ASN C 105    10931   9826   9539   -960    145  -1179       C
ATOM    750  O   ASN C 105      12.357  19.322   1.270  1.00 79.94           O
ANISOU  750  O   ASN C 105    10956   9831   9587   -955    154  -1161       O
ATOM    751  CB  ASN C 105      14.746  21.692   1.524  1.00 79.17           C
ANISOU  751  CB  ASN C 105    10834   9745   9500   -991    236  -1261       C
ATOM    752  CG  ASN C 105      16.020  21.304   2.245  1.00 79.00           C
ANISOU  752  CG  ASN C 105    10818   9780   9420  -1018    206  -1280       C
ATOM    753  OD1 ASN C 105      16.216  20.145   2.605  1.00 79.05           O
ANISOU  753  OD1 ASN C 105    10836   9821   9379  -1020    152  -1253       O
ATOM    754  ND2 ASN C 105      16.894  22.281   2.468  1.00 78.85           N
ANISOU  754  ND2 ASN C 105    10787   9769   9405  -1040    242  -1325       N
ATOM    755  N   THR C 106      14.384  18.647   1.989  1.00 71.84           N
ANISOU  755  N   THR C 106     9940   8874   8481   -978    104  -1177       N
ATOM    756  CA  THR C 106      13.907  17.475   2.725  1.00 71.77           C
ANISOU  756  CA  THR C 106     9944   8895   8432   -992     66  -1151       C
ATOM    757  C   THR C 106      12.781  17.847   3.698  1.00 71.53           C
ANISOU  757  C   THR C 106     9906   8867   8404  -1029    109  -1171       C
ATOM    758  O   THR C 106      11.773  17.146   3.817  1.00 71.51           O
ANISOU  758  O   THR C 106     9910   8858   8403  -1025     94  -1142       O
ATOM    759  CB  THR C 106      15.090  16.797   3.477  1.00 71.97           C
ANISOU  759  CB  THR C 106     9974   8976   8395  -1013     27  -1153       C
ATOM    760  OG1 THR C 106      15.320  15.481   2.958  1.00 72.60           O
ANISOU  760  OG1 THR C 106    10069   9058   8459   -981    -36  -1104       O
ATOM    761  CG2 THR C 106      14.836  16.707   4.975  1.00 71.97           C
ANISOU  761  CG2 THR C 106     9971   9024   8349  -1065     41  -1173       C
ATOM    762  N   ASN C 107      12.954  18.980   4.364  1.00 71.45           N
ANISOU  762  N   ASN C 107     9884   8866   8398  -1064    166  -1222       N
ATOM    763  CA  ASN C 107      11.998  19.456   5.342  1.00 71.69           C
ANISOU  763  CA  ASN C 107     9907   8901   8431  -1103    214  -1249       C
ATOM    764  C   ASN C 107      11.946  20.959   5.194  1.00 71.67           C
ANISOU  764  C   ASN C 107     9889   8867   8477  -1112    286  -1295       C
ATOM    765  O   ASN C 107      10.889  21.539   4.942  1.00 71.89           O
ANISOU  765  O   ASN C 107     9908   8853   8555  -1104    329  -1295       O
ATOM    766  CB  ASN C 107      12.377  19.040   6.764  1.00 75.69           C
ANISOU  766  CB  ASN C 107    10417   9472   8869  -1153    205  -1268       C
ATOM    767  CG  ASN C 107      12.193  17.555   7.006  0.00 75.58           C
ANISOU  767  CG  ASN C 107    10417   9485   8814  -1145    142  -1219       C
ATOM    768  OD1 ASN C 107      11.419  16.893   6.316  0.00 75.32           O
ANISOU  768  OD1 ASN C 107    10392   9420   8807  -1111    117  -1176       O
ATOM    769  ND2 ASN C 107      12.906  17.023   7.993  0.00 75.80           N
ANISOU  769  ND2 ASN C 107    10448   9575   8779  -1177    117  -1223       N
ATOM    770  N   SER C 108      13.123  21.565   5.346  1.00110.55           N
ANISOU  770  N   SER C 108    14808  13810  13386  -1129    298  -1332       N
ATOM    771  CA  SER C 108      13.305  23.012   5.401  1.00110.46           C
ANISOU  771  CA  SER C 108    14781  13775  13413  -1147    369  -1385       C
ATOM    772  C   SER C 108      12.561  23.798   4.333  1.00110.57           C
ANISOU  772  C   SER C 108    14784  13721  13507  -1109    409  -1372       C
ATOM    773  O   SER C 108      12.221  23.278   3.267  1.00110.63           O
ANISOU  773  O   SER C 108    14796  13700  13539  -1061    374  -1322       O
ATOM    774  CB  SER C 108      14.796  23.343   5.312  1.00105.97           C
ANISOU  774  CB  SER C 108    14209  13231  12824  -1155    360  -1411       C
ATOM    775  OG  SER C 108      15.325  22.979   4.049  1.00105.57           O
ANISOU  775  OG  SER C 108    14163  13157  12793  -1103    318  -1371       O
ATOM    776  N   SER C 109      12.350  25.072   4.635  1.00 86.75           N
ANISOU  776  N   SER C 109    11752  10679  10528  -1133    485  -1420       N
ATOM    777  CA  SER C 109      11.594  25.980   3.791  1.00 86.88           C
ANISOU  777  CA  SER C 109    11755  10632  10624  -1102    536  -1412       C
ATOM    778  C   SER C 109      12.372  26.361   2.530  1.00 86.98           C
ANISOU  778  C   SER C 109    11762  10614  10671  -1060    526  -1395       C
ATOM    779  O   SER C 109      11.955  27.243   1.777  1.00 87.16           O
ANISOU  779  O   SER C 109    11770  10585  10761  -1034    572  -1390       O
ATOM    780  CB  SER C 109      11.238  27.226   4.601  1.00 86.71           C
ANISOU  780  CB  SER C 109    11718  10594  10633  -1144    623  -1471       C
ATOM    781  OG  SER C 109      10.943  26.877   5.945  0.00 86.75           O
ANISOU  781  OG  SER C 109    11730  10644  10586  -1194    628  -1500       O
ATOM    782  N   HIS C 110      13.499  25.689   2.307  1.00 59.85           N
ANISOU  782  N   HIS C 110     8338   7212   7191  -1052    469  -1385       N
ATOM    783  CA  HIS C 110      14.308  25.894   1.111  1.00 59.53           C
ANISOU  783  CA  HIS C 110     8294   7148   7175  -1011    452  -1365       C
ATOM    784  C   HIS C 110      13.688  25.216  -0.108  1.00 59.01           C
ANISOU  784  C   HIS C 110     8234   7054   7133   -955    410  -1301       C
ATOM    785  O   HIS C 110      14.134  24.150  -0.534  1.00 58.39           O
ANISOU  785  O   HIS C 110     8170   6997   7019   -932    343  -1267       O
ATOM    786  CB  HIS C 110      15.731  25.373   1.333  1.00 59.50           C
ANISOU  786  CB  HIS C 110     8300   7193   7116  -1023    405  -1376       C
ATOM    787  CG  HIS C 110      16.456  26.062   2.442  1.00 59.53           C
ANISOU  787  CG  HIS C 110     8296   7229   7093  -1079    442  -1440       C
ATOM    788  ND1 HIS C 110      17.623  25.567   2.994  1.00 59.49           N
ANISOU  788  ND1 HIS C 110     8296   7280   7028  -1103    403  -1454       N
ATOM    789  CD2 HIS C 110      16.191  27.210   3.111  1.00 59.66           C
ANISOU  789  CD2 HIS C 110     8300   7232   7137  -1118    517  -1494       C
ATOM    790  CE1 HIS C 110      18.036  26.374   3.947  1.00 59.49           C
ANISOU  790  CE1 HIS C 110     8286   7303   7015  -1156    449  -1514       C
ATOM    791  NE2 HIS C 110      17.183  27.384   4.040  1.00 59.52           N
ANISOU  791  NE2 HIS C 110     8280   7264   7071  -1167    520  -1542       N
ATOM    792  N   ALA C 111      12.663  25.849  -0.668  1.00 53.29           N
ANISOU  792  N   ALA C 111     7496   6282   6469   -933    451  -1286       N
ATOM    793  CA  ALA C 111      11.975  25.319  -1.838  1.00 53.31           C
ANISOU  793  CA  ALA C 111     7499   6259   6496   -882    417  -1226       C
ATOM    794  C   ALA C 111      11.871  26.377  -2.927  1.00 53.62           C
ANISOU  794  C   ALA C 111     7520   6250   6605   -847    460  -1214       C
ATOM    795  O   ALA C 111      11.832  27.575  -2.640  1.00 53.80           O
ANISOU  795  O   ALA C 111     7525   6247   6669   -863    530  -1248       O
ATOM    796  CB  ALA C 111      10.595  24.827  -1.455  1.00 53.63           C
ANISOU  796  CB  ALA C 111     7540   6297   6540   -887    415  -1205       C
ATOM    797  N   LEU C 112      11.822  25.929  -4.176  1.00 38.92           N
ANISOU  797  N   LEU C 112     5660   4375   4754   -799    420  -1165       N
ATOM    798  CA  LEU C 112      11.628  26.828  -5.307  1.00 38.58           C
ANISOU  798  CA  LEU C 112     5597   4288   4773   -760    454  -1142       C
ATOM    799  C   LEU C 112      10.171  27.272  -5.368  1.00 38.87           C
ANISOU  799  C   LEU C 112     5615   4293   4860   -753    495  -1121       C
ATOM    800  O   LEU C 112       9.265  26.437  -5.431  1.00 38.81           O
ANISOU  800  O   LEU C 112     5613   4294   4839   -744    459  -1088       O
ATOM    801  CB  LEU C 112      12.011  26.125  -6.607  1.00 37.77           C
ANISOU  801  CB  LEU C 112     5503   4189   4659   -713    394  -1095       C
ATOM    802  CG  LEU C 112      11.477  26.725  -7.907  1.00 38.35           C
ANISOU  802  CG  LEU C 112     5557   4225   4788   -667    414  -1053       C
ATOM    803  CD1 LEU C 112      12.353  27.877  -8.351  1.00 38.28           C
ANISOU  803  CD1 LEU C 112     5533   4193   4817   -657    460  -1070       C
ATOM    804  CD2 LEU C 112      11.384  25.661  -8.988  1.00 38.39           C
ANISOU  804  CD2 LEU C 112     5575   4243   4770   -629    344  -1004       C
ATOM    805  N   ARG C 113       9.948  28.582  -5.348  1.00 48.60           N
ANISOU  805  N   ARG C 113     6825   5489   6153   -755    571  -1139       N
ATOM    806  CA  ARG C 113       8.596  29.127  -5.287  1.00 49.29           C
ANISOU  806  CA  ARG C 113     6890   5543   6293   -751    619  -1123       C
ATOM    807  C   ARG C 113       8.200  29.860  -6.562  1.00 50.01           C
ANISOU  807  C   ARG C 113     6957   5594   6450   -702    645  -1077       C
ATOM    808  O   ARG C 113       7.014  30.022  -6.848  1.00 50.72           O
ANISOU  808  O   ARG C 113     7028   5663   6580   -685    664  -1042       O
ATOM    809  CB  ARG C 113       8.466  30.066  -4.087  1.00 49.73           C
ANISOU  809  CB  ARG C 113     6937   5586   6371   -796    696  -1180       C
ATOM    810  CG  ARG C 113       8.785  29.395  -2.768  1.00 49.31           C
ANISOU  810  CG  ARG C 113     6906   5578   6252   -847    674  -1224       C
ATOM    811  CD  ARG C 113       8.635  30.329  -1.584  1.00 49.42           C
ANISOU  811  CD  ARG C 113     6910   5581   6284   -895    751  -1285       C
ATOM    812  NE  ARG C 113       8.311  29.567  -0.383  1.00 49.69           N
ANISOU  812  NE  ARG C 113     6961   5657   6263   -936    730  -1307       N
ATOM    813  CZ  ARG C 113       9.198  28.881   0.331  1.00 49.37           C
ANISOU  813  CZ  ARG C 113     6941   5667   6151   -968    688  -1334       C
ATOM    814  NH1 ARG C 113      10.476  28.865  -0.025  1.00 48.85           N
ANISOU  814  NH1 ARG C 113     6882   5616   6062   -963    661  -1345       N
ATOM    815  NH2 ARG C 113       8.807  28.210   1.404  1.00 49.37           N
ANISOU  815  NH2 ARG C 113     6952   5703   6103  -1004    672  -1349       N
ATOM    816  N   GLN C 114       9.197  30.303  -7.321  1.00 52.56           N
ANISOU  816  N   GLN C 114     7278   5908   6784   -681    647  -1076       N
ATOM    817  CA  GLN C 114       8.944  31.079  -8.531  1.00 53.10           C
ANISOU  817  CA  GLN C 114     7321   5940   6914   -635    675  -1033       C
ATOM    818  C   GLN C 114       9.788  30.643  -9.722  1.00 52.80           C
ANISOU  818  C   GLN C 114     7292   5916   6853   -598    621  -1000       C
ATOM    819  O   GLN C 114      10.998  30.447  -9.603  1.00 52.25           O
ANISOU  819  O   GLN C 114     7240   5866   6748   -609    599  -1029       O
ATOM    820  CB  GLN C 114       9.177  32.569  -8.271  1.00 53.73           C
ANISOU  820  CB  GLN C 114     7379   5978   7059   -646    766  -1066       C
ATOM    821  CG  GLN C 114       7.944  33.317  -7.804  1.00 54.70           C
ANISOU  821  CG  GLN C 114     7478   6066   7242   -654    834  -1065       C
ATOM    822  CD  GLN C 114       8.282  34.636  -7.140  1.00 55.07           C
ANISOU  822  CD  GLN C 114     7510   6075   7338   -683    925  -1118       C
ATOM    823  OE1 GLN C 114       8.706  35.588  -7.796  1.00 55.76           O
ANISOU  823  OE1 GLN C 114     7580   6128   7479   -661    969  -1111       O
ATOM    824  NE2 GLN C 114       8.103  34.694  -5.826  1.00 54.52           N
ANISOU  824  NE2 GLN C 114     7449   6014   7253   -733    955  -1174       N
ATOM    825  N   LEU C 115       9.131  30.501 -10.870  1.00 45.89           N
ANISOU  825  N   LEU C 115     6404   5033   6000   -554    600   -940       N
ATOM    826  CA  LEU C 115       9.810  30.272 -12.138  1.00 46.07           C
ANISOU  826  CA  LEU C 115     6430   5064   6012   -514    560   -905       C
ATOM    827  C   LEU C 115       9.662  31.519 -13.004  1.00 46.52           C
ANISOU  827  C   LEU C 115     6454   5081   6140   -481    619   -875       C
ATOM    828  O   LEU C 115       8.645  31.689 -13.678  1.00 47.47           O
ANISOU  828  O   LEU C 115     6552   5189   6296   -452    626   -824       O
ATOM    829  CB  LEU C 115       9.195  29.081 -12.871  1.00 46.79           C
ANISOU  829  CB  LEU C 115     6530   5181   6065   -489    487   -858       C
ATOM    830  CG  LEU C 115       9.923  27.736 -12.881  1.00 46.27           C
ANISOU  830  CG  LEU C 115     6499   5156   5926   -495    408   -866       C
ATOM    831  CD1 LEU C 115       9.327  26.823 -13.945  1.00 46.59           C
ANISOU  831  CD1 LEU C 115     6542   5213   5946   -462    348   -814       C
ATOM    832  CD2 LEU C 115      11.411  27.928 -13.114  1.00 45.83           C
ANISOU  832  CD2 LEU C 115     6455   5106   5853   -491    404   -890       C
ATOM    833  N   ARG C 116      10.672  32.388 -12.988  1.00 50.58           N
ANISOU  833  N   ARG C 116     6964   5577   6678   -485    662   -904       N
ATOM    834  CA  ARG C 116      10.630  33.643 -13.744  1.00 51.51           C
ANISOU  834  CA  ARG C 116     7050   5653   6868   -455    724   -878       C
ATOM    835  C   ARG C 116      11.124  33.482 -15.176  1.00 52.44           C
ANISOU  835  C   ARG C 116     7165   5780   6978   -408    687   -828       C
ATOM    836  O   ARG C 116      12.304  33.703 -15.473  1.00 52.41           O
ANISOU  836  O   ARG C 116     7169   5779   6966   -404    687   -845       O
ATOM    837  CB  ARG C 116      11.443  34.734 -13.040  1.00 54.45           C
ANISOU  837  CB  ARG C 116     7416   5996   7275   -484    795   -934       C
ATOM    838  CG  ARG C 116      10.807  35.175 -11.729  1.00 54.47           C
ANISOU  838  CG  ARG C 116     7414   5980   7300   -528    850   -980       C
ATOM    839  CD  ARG C 116      11.619  36.240 -11.009  1.00 54.41           C
ANISOU  839  CD  ARG C 116     7401   5946   7325   -561    920  -1042       C
ATOM    840  NE  ARG C 116      10.932  37.356 -10.386  1.00 54.72           N
ANISOU  840  NE  ARG C 116     7417   5938   7434   -579   1011  -1064       N
ATOM    841  CZ  ARG C 116       9.614  37.520 -10.174  1.00 55.03           C
ANISOU  841  CZ  ARG C 116     7439   5958   7511   -575   1041  -1042       C
ATOM    842  NH1 ARG C 116       9.215  38.619  -9.517  0.00 55.28           N
ANISOU  842  NH1 ARG C 116     7452   5945   7608   -596   1131  -1074       N
ATOM    843  NH2 ARG C 116       8.654  36.674 -10.590  0.00 55.14           N
ANISOU  843  NH2 ARG C 116     7453   5993   7504   -551    989   -989       N
ATOM    844  N   LEU C 117      10.209  33.095 -16.057  1.00 43.94           N
ANISOU  844  N   LEU C 117     6076   4713   5905   -374    657   -768       N
ATOM    845  CA  LEU C 117      10.473  33.045 -17.484  1.00 44.55           C
ANISOU  845  CA  LEU C 117     6146   4801   5982   -327    629   -714       C
ATOM    846  C   LEU C 117       9.552  34.075 -18.127  1.00 45.90           C
ANISOU  846  C   LEU C 117     6275   4938   6227   -295    685   -661       C
ATOM    847  O   LEU C 117       8.715  33.739 -18.964  1.00 46.95           O
ANISOU  847  O   LEU C 117     6394   5087   6358   -265    655   -604       O
ATOM    848  CB  LEU C 117      10.180  31.643 -18.018  1.00 44.59           C
ANISOU  848  CB  LEU C 117     6172   4850   5921   -315    541   -687       C
ATOM    849  CG  LEU C 117      10.598  30.527 -17.052  1.00 43.73           C
ANISOU  849  CG  LEU C 117     6100   4769   5746   -353    491   -737       C
ATOM    850  CD1 LEU C 117       9.961  29.193 -17.415  1.00 44.17           C
ANISOU  850  CD1 LEU C 117     6172   4860   5751   -346    416   -709       C
ATOM    851  CD2 LEU C 117      12.113  30.397 -16.985  1.00 43.21           C
ANISOU  851  CD2 LEU C 117     6057   4714   5647   -361    476   -774       C
ATOM    852  N   THR C 118       9.715  35.332 -17.716  1.00 41.63           N
ANISOU  852  N   THR C 118     5713   4353   5751   -303    767   -681       N
ATOM    853  CA  THR C 118       8.826  36.417 -18.127  1.00 42.41           C
ANISOU  853  CA  THR C 118     5770   4413   5931   -277    833   -635       C
ATOM    854  C   THR C 118       8.945  36.772 -19.606  1.00 43.06           C
ANISOU  854  C   THR C 118     5829   4497   6034   -225    828   -566       C
ATOM    855  O   THR C 118       8.036  37.373 -20.182  1.00 43.82           O
ANISOU  855  O   THR C 118     5889   4575   6184   -194    861   -508       O
ATOM    856  CB  THR C 118       9.053  37.684 -17.274  1.00 41.88           C
ANISOU  856  CB  THR C 118     5688   4293   5932   -301    928   -680       C
ATOM    857  OG1 THR C 118      10.452  37.841 -17.005  1.00 41.32           O
ANISOU  857  OG1 THR C 118     5638   4222   5840   -322    932   -732       O
ATOM    858  CG2 THR C 118       8.308  37.579 -15.955  1.00 40.74           C
ANISOU  858  CG2 THR C 118     5549   4140   5790   -344    952   -723       C
ATOM    859  N   GLN C 119      10.067  36.400 -20.211  1.00 39.29           N
ANISOU  859  N   GLN C 119     5372   4042   5513   -214    787   -572       N
ATOM    860  CA  GLN C 119      10.303  36.675 -21.623  1.00 40.03           C
ANISOU  860  CA  GLN C 119     5448   4144   5618   -166    779   -510       C
ATOM    861  C   GLN C 119      10.283  35.410 -22.481  1.00 40.35           C
ANISOU  861  C   GLN C 119     5508   4239   5583   -147    687   -480       C
ATOM    862  O   GLN C 119      10.615  35.453 -23.665  1.00 40.94           O
ANISOU  862  O   GLN C 119     5574   4330   5650   -111    668   -435       O
ATOM    863  CB  GLN C 119      11.625  37.422 -21.810  1.00 39.56           C
ANISOU  863  CB  GLN C 119     5389   4062   5578   -163    816   -533       C
ATOM    864  CG  GLN C 119      11.547  38.903 -21.473  1.00 39.51           C
ANISOU  864  CG  GLN C 119     5352   3997   5665   -164    916   -538       C
ATOM    865  CD  GLN C 119      10.714  39.680 -22.472  1.00 40.47           C
ANISOU  865  CD  GLN C 119     5429   4099   5849   -117    953   -457       C
ATOM    866  OE1 GLN C 119      11.083  39.807 -23.639  0.00 40.99           O
ANISOU  866  OE1 GLN C 119     5483   4177   5912    -79    939   -407       O
ATOM    867  NE2 GLN C 119       9.579  40.200 -22.019  0.00 40.73           N
ANISOU  867  NE2 GLN C 119     5435   4102   5938   -120   1001   -441       N
ATOM    868  N   LEU C 120       9.897  34.287 -21.882  1.00 30.56           N
ANISOU  868  N   LEU C 120     4294   3029   4289   -173    632   -505       N
ATOM    869  CA  LEU C 120       9.772  33.036 -22.624  1.00 30.32           C
ANISOU  869  CA  LEU C 120     4283   3047   4190   -160    547   -480       C
ATOM    870  C   LEU C 120       8.649  33.151 -23.647  1.00 31.40           C
ANISOU  870  C   LEU C 120     4386   3197   4346   -124    539   -405       C
ATOM    871  O   LEU C 120       7.482  33.307 -23.286  1.00 31.92           O
ANISOU  871  O   LEU C 120     4431   3253   4443   -129    558   -386       O
ATOM    872  CB  LEU C 120       9.508  31.863 -21.679  1.00 30.02           C
ANISOU  872  CB  LEU C 120     4277   3032   4097   -197    497   -522       C
ATOM    873  CG  LEU C 120       9.459  30.483 -22.341  1.00 29.77           C
ANISOU  873  CG  LEU C 120     4270   3047   3994   -188    409   -506       C
ATOM    874  CD1 LEU C 120      10.800  30.143 -22.977  1.00 29.52           C
ANISOU  874  CD1 LEU C 120     4261   3033   3922   -175    378   -519       C
ATOM    875  CD2 LEU C 120       9.048  29.413 -21.342  1.00 29.54           C
ANISOU  875  CD2 LEU C 120     4267   3034   3923   -225    369   -542       C
ATOM    876  N   THR C 121       9.005  33.071 -24.924  1.00 36.09           N
ANISOU  876  N   THR C 121     4975   3816   4923    -88    511   -362       N
ATOM    877  CA  THR C 121       8.046  33.321 -25.992  1.00 37.77           C
ANISOU  877  CA  THR C 121     5151   4044   5155    -52    509   -285       C
ATOM    878  C   THR C 121       7.811  32.101 -26.878  1.00 38.41           C
ANISOU  878  C   THR C 121     5248   4181   5165    -41    424   -260       C
ATOM    879  O   THR C 121       6.736  31.949 -27.459  1.00 39.72           O
ANISOU  879  O   THR C 121     5389   4370   5332    -25    405   -208       O
ATOM    880  CB  THR C 121       8.501  34.499 -26.881  1.00 38.87           C
ANISOU  880  CB  THR C 121     5260   4164   5345    -14    560   -241       C
ATOM    881  OG1 THR C 121       9.052  35.537 -26.062  1.00 38.86           O
ANISOU  881  OG1 THR C 121     5252   4109   5402    -29    636   -279       O
ATOM    882  CG2 THR C 121       7.331  35.054 -27.680  1.00 40.16           C
ANISOU  882  CG2 THR C 121     5375   4333   5551     20    580   -161       C
ATOM    883  N   GLU C 122       8.806  31.226 -26.981  1.00 43.56           N
ANISOU  883  N   GLU C 122     5940   4856   5754    -50    374   -298       N
ATOM    884  CA  GLU C 122       8.719  30.146 -27.955  1.00 44.25           C
ANISOU  884  CA  GLU C 122     6042   4994   5776    -37    299   -276       C
ATOM    885  C   GLU C 122       9.454  28.866 -27.564  1.00 43.14           C
ANISOU  885  C   GLU C 122     5951   4873   5567    -62    240   -332       C
ATOM    886  O   GLU C 122      10.619  28.895 -27.167  1.00 42.39           O
ANISOU  886  O   GLU C 122     5880   4764   5462    -71    248   -375       O
ATOM    887  CB  GLU C 122       9.216  30.640 -29.316  1.00 45.02           C
ANISOU  887  CB  GLU C 122     6122   5108   5874      4    304   -228       C
ATOM    888  CG  GLU C 122       8.640  29.895 -30.502  1.00 46.30           C
ANISOU  888  CG  GLU C 122     6280   5324   5990     24    244   -182       C
ATOM    889  CD  GLU C 122       8.713  30.705 -31.781  1.00 47.45           C
ANISOU  889  CD  GLU C 122     6390   5484   6154     67    265   -117       C
ATOM    890  OE1 GLU C 122       9.819  30.829 -32.349  1.00 47.26           O
ANISOU  890  OE1 GLU C 122     6379   5464   6113     83    265   -123       O
ATOM    891  OE2 GLU C 122       7.663  31.225 -32.215  1.00 48.46           O
ANISOU  891  OE2 GLU C 122     6476   5619   6315     85    282    -57       O
ATOM    892  N   ILE C 123       8.748  27.746 -27.677  1.00 29.43           N
ANISOU  892  N   ILE C 123     4228   3168   3785    -73    181   -328       N
ATOM    893  CA  ILE C 123       9.349  26.423 -27.578  1.00 29.11           C
ANISOU  893  CA  ILE C 123     4231   3151   3678    -90    118   -369       C
ATOM    894  C   ILE C 123       9.109  25.710 -28.905  1.00 29.17           C
ANISOU  894  C   ILE C 123     4240   3203   3639    -68     63   -333       C
ATOM    895  O   ILE C 123       8.013  25.210 -29.161  1.00 29.29           O
ANISOU  895  O   ILE C 123     4244   3241   3642    -72     33   -308       O
ATOM    896  CB  ILE C 123       8.745  25.604 -26.422  1.00 28.96           C
ANISOU  896  CB  ILE C 123     4231   3128   3644   -128     96   -404       C
ATOM    897  CG1 ILE C 123       8.995  26.304 -25.085  1.00 28.93           C
ANISOU  897  CG1 ILE C 123     4227   3084   3681   -153    150   -443       C
ATOM    898  CG2 ILE C 123       9.327  24.198 -26.399  1.00 28.67           C
ANISOU  898  CG2 ILE C 123     4238   3114   3541   -142     31   -440       C
ATOM    899  CD1 ILE C 123       8.440  25.559 -23.890  1.00 28.81           C
ANISOU  899  CD1 ILE C 123     4230   3066   3650   -191    133   -478       C
ATOM    900  N   LEU C 124      10.137  25.683 -29.748  1.00 32.95           N
ANISOU  900  N   LEU C 124     4731   3696   4093    -46     52   -332       N
ATOM    901  CA  LEU C 124      10.013  25.186 -31.117  1.00 33.95           C
ANISOU  901  CA  LEU C 124     4856   3867   4178    -23      9   -297       C
ATOM    902  C   LEU C 124       9.640  23.708 -31.193  1.00 33.24           C
ANISOU  902  C   LEU C 124     4795   3807   4028    -42    -60   -317       C
ATOM    903  O   LEU C 124       8.873  23.298 -32.064  1.00 33.87           O
ANISOU  903  O   LEU C 124     4863   3923   4083    -34    -95   -284       O
ATOM    904  CB  LEU C 124      11.308  25.443 -31.892  1.00 34.12           C
ANISOU  904  CB  LEU C 124     4887   3892   4183      2     15   -299       C
ATOM    905  CG  LEU C 124      11.690  26.913 -32.080  1.00 34.86           C
ANISOU  905  CG  LEU C 124     4950   3961   4336     27     82   -270       C
ATOM    906  CD1 LEU C 124      13.087  27.038 -32.665  1.00 33.74           C
ANISOU  906  CD1 LEU C 124     4824   3822   4176     45     86   -282       C
ATOM    907  CD2 LEU C 124      10.672  27.619 -32.963  1.00 36.58           C
ANISOU  907  CD2 LEU C 124     5122   4197   4581     53     98   -199       C
ATOM    908  N   SER C 125      10.187  22.914 -30.280  1.00 29.42           N
ANISOU  908  N   SER C 125     4349   3308   3522    -69    -80   -372       N
ATOM    909  CA  SER C 125       9.907  21.484 -30.245  1.00 28.70           C
ANISOU  909  CA  SER C 125     4287   3237   3379    -89   -141   -395       C
ATOM    910  C   SER C 125       9.995  20.948 -28.823  1.00 28.44           C
ANISOU  910  C   SER C 125     4279   3179   3347   -124   -143   -443       C
ATOM    911  O   SER C 125      10.780  21.439 -28.012  1.00 28.30           O
ANISOU  911  O   SER C 125     4268   3133   3351   -131   -109   -471       O
ATOM    912  CB  SER C 125      10.876  20.723 -31.154  1.00 28.59           C
ANISOU  912  CB  SER C 125     4303   3248   3313    -76   -179   -409       C
ATOM    913  OG  SER C 125      10.689  19.323 -31.036  1.00 28.48           O
ANISOU  913  OG  SER C 125     4320   3247   3254    -97   -234   -438       O
ATOM    914  N   GLY C 126       9.188  19.935 -28.527  1.00 28.42           N
ANISOU  914  N   GLY C 126     4288   3187   3321   -147   -184   -451       N
ATOM    915  CA  GLY C 126       9.159  19.348 -27.201  1.00 28.23           C
ANISOU  915  CA  GLY C 126     4286   3143   3296   -180   -189   -491       C
ATOM    916  C   GLY C 126       8.052  19.932 -26.346  1.00 28.34           C
ANISOU  916  C   GLY C 126     4274   3141   3353   -197   -157   -478       C
ATOM    917  O   GLY C 126       7.466  20.959 -26.689  1.00 28.56           O
ANISOU  917  O   GLY C 126     4265   3166   3420   -181   -120   -441       O
ATOM    918  N   GLY C 127       7.767  19.276 -25.228  1.00 33.55           N
ANISOU  918  N   GLY C 127     4951   3789   4006   -229   -168   -508       N
ATOM    919  CA  GLY C 127       6.713  19.721 -24.336  1.00 33.85           C
ANISOU  919  CA  GLY C 127     4968   3813   4083   -248   -138   -500       C
ATOM    920  C   GLY C 127       7.235  20.275 -23.025  1.00 33.45           C
ANISOU  920  C   GLY C 127     4922   3732   4056   -267    -95   -536       C
ATOM    921  O   GLY C 127       8.425  20.562 -22.889  1.00 32.80           O
ANISOU  921  O   GLY C 127     4854   3641   3969   -263    -80   -560       O
ATOM    922  N   VAL C 128       6.337  20.427 -22.058  1.00 28.31           N
ANISOU  922  N   VAL C 128     4258   3068   3429   -291    -74   -539       N
ATOM    923  CA  VAL C 128       6.693  20.972 -20.753  1.00 28.26           C
ANISOU  923  CA  VAL C 128     4256   3037   3445   -314    -30   -574       C
ATOM    924  C   VAL C 128       6.292  20.015 -19.635  1.00 28.17           C
ANISOU  924  C   VAL C 128     4265   3027   3410   -350    -54   -600       C
ATOM    925  O   VAL C 128       5.166  19.519 -19.606  1.00 28.26           O
ANISOU  925  O   VAL C 128     4269   3047   3422   -360    -73   -581       O
ATOM    926  CB  VAL C 128       6.020  22.340 -20.516  1.00 28.51           C
ANISOU  926  CB  VAL C 128     4248   3045   3538   -309     37   -554       C
ATOM    927  CG1 VAL C 128       6.379  22.886 -19.141  1.00 28.50           C
ANISOU  927  CG1 VAL C 128     4252   3019   3557   -338     84   -596       C
ATOM    928  CG2 VAL C 128       6.419  23.324 -21.605  1.00 28.63           C
ANISOU  928  CG2 VAL C 128     4241   3057   3580   -273     64   -524       C
ATOM    929  N   TYR C 129       7.222  19.755 -18.721  1.00 33.90           N
ANISOU  929  N   TYR C 129     5017   3748   4116   -371    -53   -641       N
ATOM    930  CA  TYR C 129       6.952  18.896 -17.575  1.00 33.19           C
ANISOU  930  CA  TYR C 129     4946   3661   4004   -405    -72   -666       C
ATOM    931  C   TYR C 129       7.300  19.609 -16.272  1.00 32.81           C
ANISOU  931  C   TYR C 129     4896   3598   3972   -431    -23   -700       C
ATOM    932  O   TYR C 129       8.469  19.875 -15.993  1.00 32.29           O
ANISOU  932  O   TYR C 129     4841   3530   3896   -433    -11   -728       O
ATOM    933  CB  TYR C 129       7.736  17.587 -17.687  1.00 32.43           C
ANISOU  933  CB  TYR C 129     4887   3581   3856   -408   -129   -682       C
ATOM    934  CG  TYR C 129       7.500  16.623 -16.543  1.00 31.79           C
ANISOU  934  CG  TYR C 129     4825   3503   3749   -442   -151   -702       C
ATOM    935  CD1 TYR C 129       6.467  15.697 -16.593  1.00 32.22           C
ANISOU  935  CD1 TYR C 129     4883   3565   3794   -452   -186   -686       C
ATOM    936  CD2 TYR C 129       8.313  16.638 -15.416  1.00 31.05           C
ANISOU  936  CD2 TYR C 129     4746   3409   3643   -464   -138   -736       C
ATOM    937  CE1 TYR C 129       6.249  14.814 -15.551  1.00 31.75           C
ANISOU  937  CE1 TYR C 129     4841   3509   3714   -482   -205   -701       C
ATOM    938  CE2 TYR C 129       8.103  15.759 -14.371  1.00 30.84           C
ANISOU  938  CE2 TYR C 129     4737   3389   3593   -494   -158   -750       C
ATOM    939  CZ  TYR C 129       7.070  14.849 -14.443  1.00 31.51           C
ANISOU  939  CZ  TYR C 129     4824   3477   3669   -502   -190   -732       C
ATOM    940  OH  TYR C 129       6.857  13.973 -13.404  1.00 31.92           O
ANISOU  940  OH  TYR C 129     4892   3535   3699   -531   -209   -743       O
ATOM    941  N   ILE C 130       6.279  19.920 -15.481  1.00 29.68           N
ANISOU  941  N   ILE C 130     4484   3193   3602   -452      7   -699       N
ATOM    942  CA  ILE C 130       6.475  20.566 -14.188  1.00 29.34           C
ANISOU  942  CA  ILE C 130     4438   3137   3573   -481     55   -734       C
ATOM    943  C   ILE C 130       5.688  19.826 -13.111  1.00 29.12           C
ANISOU  943  C   ILE C 130     4419   3116   3529   -515     42   -744       C
ATOM    944  O   ILE C 130       4.482  20.022 -12.970  1.00 30.76           O
ANISOU  944  O   ILE C 130     4607   3317   3765   -520     60   -725       O
ATOM    945  CB  ILE C 130       6.030  22.044 -14.218  1.00 30.02           C
ANISOU  945  CB  ILE C 130     4490   3198   3720   -473    125   -727       C
ATOM    946  CG1 ILE C 130       6.740  22.797 -15.345  1.00 30.39           C
ANISOU  946  CG1 ILE C 130     4525   3236   3785   -438    139   -711       C
ATOM    947  CG2 ILE C 130       6.300  22.711 -12.877  1.00 29.63           C
ANISOU  947  CG2 ILE C 130     4439   3136   3682   -507    177   -770       C
ATOM    948  CD1 ILE C 130       6.335  24.249 -15.461  1.00 31.09           C
ANISOU  948  CD1 ILE C 130     4578   3296   3938   -426    210   -698       C
ATOM    949  N   GLU C 131       6.371  18.972 -12.356  1.00 34.60           N
ANISOU  949  N   GLU C 131     5141   3825   4179   -537     12   -771       N
ATOM    950  CA  GLU C 131       5.702  18.153 -11.350  1.00 35.60           C
ANISOU  950  CA  GLU C 131     5279   3962   4286   -569     -4   -778       C
ATOM    951  C   GLU C 131       6.471  18.023 -10.040  1.00 34.77           C
ANISOU  951  C   GLU C 131     5190   3868   4152   -602      5   -818       C
ATOM    952  O   GLU C 131       7.695  18.153 -10.004  1.00 33.49           O
ANISOU  952  O   GLU C 131     5041   3713   3972   -600      3   -839       O
ATOM    953  CB  GLU C 131       5.408  16.756 -11.901  1.00 35.67           C
ANISOU  953  CB  GLU C 131     5305   3984   4262   -562    -71   -756       C
ATOM    954  CG  GLU C 131       3.979  16.560 -12.365  1.00 37.16           C
ANISOU  954  CG  GLU C 131     5476   4170   4474   -556    -79   -721       C
ATOM    955  CD  GLU C 131       3.524  15.119 -12.243  1.00 36.91           C
ANISOU  955  CD  GLU C 131     5464   4151   4410   -570   -134   -712       C
ATOM    956  OE1 GLU C 131       4.158  14.237 -12.860  1.00 35.85           O
ANISOU  956  OE1 GLU C 131     5352   4024   4244   -557   -181   -711       O
ATOM    957  OE2 GLU C 131       2.537  14.868 -11.520  1.00 37.27           O
ANISOU  957  OE2 GLU C 131     5503   4196   4463   -592   -128   -708       O
ATOM    958  N   LYS C 132       5.724  17.756  -8.971  1.00 28.62           N
ANISOU  958  N   LYS C 132     4411   3094   3368   -634     15   -826       N
ATOM    959  CA  LYS C 132       6.280  17.471  -7.649  1.00 28.33           C
ANISOU  959  CA  LYS C 132     4390   3076   3298   -669     18   -859       C
ATOM    960  C   LYS C 132       7.205  18.560  -7.115  1.00 28.42           C
ANISOU  960  C   LYS C 132     4396   3086   3316   -682     66   -897       C
ATOM    961  O   LYS C 132       8.274  18.274  -6.577  1.00 28.37           O
ANISOU  961  O   LYS C 132     4406   3100   3274   -697     52   -921       O
ATOM    962  CB  LYS C 132       6.973  16.104  -7.633  1.00 28.15           C
ANISOU  962  CB  LYS C 132     4397   3075   3226   -670    -45   -855       C
ATOM    963  CG  LYS C 132       6.020  14.933  -7.833  1.00 28.13           C
ANISOU  963  CG  LYS C 132     4401   3073   3212   -669    -89   -825       C
ATOM    964  CD  LYS C 132       6.727  13.599  -7.658  1.00 28.00           C
ANISOU  964  CD  LYS C 132     4414   3075   3151   -673   -144   -823       C
ATOM    965  CE  LYS C 132       5.751  12.435  -7.758  1.00 28.02           C
ANISOU  965  CE  LYS C 132     4424   3075   3146   -676   -183   -796       C
ATOM    966  NZ  LYS C 132       5.092  12.357  -9.091  1.00 27.97           N
ANISOU  966  NZ  LYS C 132     4409   3054   3163   -648   -201   -770       N
ATOM    967  N   ASN C 133       6.781  19.809  -7.276  1.00 33.33           N
ANISOU  967  N   ASN C 133     4993   3685   3987   -677    124   -902       N
ATOM    968  CA  ASN C 133       7.454  20.943  -6.658  1.00 33.00           C
ANISOU  968  CA  ASN C 133     4943   3638   3960   -695    181   -942       C
ATOM    969  C   ASN C 133       6.543  21.529  -5.586  1.00 33.28           C
ANISOU  969  C   ASN C 133     4963   3665   4016   -727    234   -961       C
ATOM    970  O   ASN C 133       5.609  22.272  -5.887  1.00 34.25           O
ANISOU  970  O   ASN C 133     5063   3762   4190   -716    276   -947       O
ATOM    971  CB  ASN C 133       7.816  21.997  -7.704  1.00 32.91           C
ANISOU  971  CB  ASN C 133     4913   3600   3991   -663    212   -934       C
ATOM    972  CG  ASN C 133       8.662  21.432  -8.830  1.00 33.68           C
ANISOU  972  CG  ASN C 133     5024   3705   4068   -629    161   -913       C
ATOM    973  OD1 ASN C 133       9.878  21.296  -8.701  1.00 33.64           O
ANISOU  973  OD1 ASN C 133     5034   3715   4035   -633    147   -935       O
ATOM    974  ND2 ASN C 133       8.019  21.103  -9.944  1.00 33.06           N
ANISOU  974  ND2 ASN C 133     4939   3618   4003   -596    134   -871       N
ATOM    975  N   ASP C 134       6.831  21.175  -4.337  1.00 58.04           N
ANISOU  975  N   ASP C 134     8112   6827   7113   -767    234   -993       N
ATOM    976  CA  ASP C 134       5.952  21.430  -3.195  1.00 58.39           C
ANISOU  976  CA  ASP C 134     8149   6873   7164   -803    274  -1012       C
ATOM    977  C   ASP C 134       5.481  22.881  -3.049  1.00 58.80           C
ANISOU  977  C   ASP C 134     8174   6892   7274   -808    355  -1033       C
ATOM    978  O   ASP C 134       4.314  23.125  -2.746  1.00 59.79           O
ANISOU  978  O   ASP C 134     8285   7003   7430   -815    387  -1024       O
ATOM    979  CB  ASP C 134       6.637  20.953  -1.906  1.00 58.50           C
ANISOU  979  CB  ASP C 134     8182   6926   7121   -845    263  -1048       C
ATOM    980  CG  ASP C 134       5.690  20.888  -0.718  1.00 58.43           C
ANISOU  980  CG  ASP C 134     8169   6927   7106   -883    290  -1061       C
ATOM    981  OD1 ASP C 134       4.474  21.116  -0.894  1.00 58.55           O
ANISOU  981  OD1 ASP C 134     8168   6917   7160   -875    315  -1041       O
ATOM    982  OD2 ASP C 134       6.166  20.592   0.401  1.00 58.52           O
ANISOU  982  OD2 ASP C 134     8192   6973   7071   -920    287  -1090       O
ATOM    983  N   LYS C 135       6.375  23.840  -3.267  1.00 41.34           N
ANISOU  983  N   LYS C 135     5957   4669   5082   -804    390  -1059       N
ATOM    984  CA  LYS C 135       6.034  25.241  -3.026  1.00 41.77           C
ANISOU  984  CA  LYS C 135     5987   4691   5193   -813    473  -1084       C
ATOM    985  C   LYS C 135       6.085  26.141  -4.267  1.00 42.29           C
ANISOU  985  C   LYS C 135     6033   4718   5318   -771    500  -1060       C
ATOM    986  O   LYS C 135       6.062  27.367  -4.151  1.00 42.60           O
ANISOU  986  O   LYS C 135     6052   4727   5406   -776    570  -1083       O
ATOM    987  CB  LYS C 135       6.906  25.814  -1.904  1.00 41.19           C
ANISOU  987  CB  LYS C 135     5919   4632   5097   -858    511  -1147       C
ATOM    988  CG  LYS C 135       6.302  25.658  -0.512  1.00 40.60           C
ANISOU  988  CG  LYS C 135     5848   4578   4999   -905    535  -1178       C
ATOM    989  CD  LYS C 135       7.137  24.727   0.360  1.00 40.26           C
ANISOU  989  CD  LYS C 135     5830   4588   4879   -937    486  -1200       C
ATOM    990  CE  LYS C 135       6.585  24.643   1.777  0.00 40.30           C
ANISOU  990  CE  LYS C 135     5837   4617   4857   -986    513  -1231       C
ATOM    991  NZ  LYS C 135       5.913  23.344   2.056  0.00 39.89           N
ANISOU  991  NZ  LYS C 135     5799   4590   4768   -988    458  -1196       N
ATOM    992  N   LEU C 136       6.138  25.533  -5.448  1.00 41.78           N
ANISOU  992  N   LEU C 136     5971   4655   5248   -731    446  -1014       N
ATOM    993  CA  LEU C 136       6.141  26.286  -6.699  1.00 41.73           C
ANISOU  993  CA  LEU C 136     5945   4618   5293   -688    465   -983       C
ATOM    994  C   LEU C 136       4.719  26.661  -7.112  1.00 43.11           C
ANISOU  994  C   LEU C 136     6092   4766   5522   -668    494   -943       C
ATOM    995  O   LEU C 136       3.857  25.793  -7.253  1.00 43.62           O
ANISOU  995  O   LEU C 136     6159   4843   5571   -663    453   -911       O
ATOM    996  CB  LEU C 136       6.818  25.476  -7.806  1.00 41.99           C
ANISOU  996  CB  LEU C 136     5992   4667   5294   -655    396   -951       C
ATOM    997  CG  LEU C 136       6.914  26.125  -9.189  1.00 42.93           C
ANISOU  997  CG  LEU C 136     6093   4763   5456   -609    407   -915       C
ATOM    998  CD1 LEU C 136       7.744  27.400  -9.136  1.00 43.15           C
ANISOU  998  CD1 LEU C 136     6108   4766   5519   -611    468   -946       C
ATOM    999  CD2 LEU C 136       7.493  25.144 -10.197  1.00 42.65           C
ANISOU  999  CD2 LEU C 136     6076   4750   5380   -580    334   -887       C
ATOM   1000  N   CYS C 137       4.481  27.954  -7.309  1.00 43.47           N
ANISOU 1000  N   CYS C 137     6110   4774   5632   -658    565   -944       N
ATOM   1001  CA  CYS C 137       3.139  28.444  -7.613  1.00 44.47           C
ANISOU 1001  CA  CYS C 137     6206   4874   5817   -640    602   -907       C
ATOM   1002  C   CYS C 137       3.025  29.079  -8.997  1.00 45.57           C
ANISOU 1002  C   CYS C 137     6320   4989   6006   -590    613   -857       C
ATOM   1003  O   CYS C 137       4.011  29.196  -9.726  1.00 45.46           O
ANISOU 1003  O   CYS C 137     6312   4977   5982   -571    595   -854       O
ATOM   1004  CB  CYS C 137       2.685  29.449  -6.549  1.00 44.56           C
ANISOU 1004  CB  CYS C 137     6201   4857   5871   -670    687   -945       C
ATOM   1005  SG  CYS C 137       2.481  28.758  -4.891  1.00 46.44           S
ANISOU 1005  SG  CYS C 137     6464   5126   6057   -729    682   -996       S
ATOM   1006  N   HIS C 138       1.798  29.464  -9.347  1.00 49.72           N
ANISOU 1006  N   HIS C 138     6815   5495   6583   -571    641   -815       N
ATOM   1007  CA  HIS C 138       1.500  30.240 -10.553  1.00 50.69           C
ANISOU 1007  CA  HIS C 138     6904   5592   6762   -525    664   -763       C
ATOM   1008  C   HIS C 138       1.738  29.508 -11.878  1.00 51.57           C
ANISOU 1008  C   HIS C 138     7021   5730   6843   -489    591   -715       C
ATOM   1009  O   HIS C 138       1.446  30.047 -12.946  1.00 52.90           O
ANISOU 1009  O   HIS C 138     7162   5886   7052   -450    603   -665       O
ATOM   1010  CB  HIS C 138       2.256  31.575 -10.542  1.00 50.62           C
ANISOU 1010  CB  HIS C 138     6882   5546   6803   -522    737   -789       C
ATOM   1011  CG  HIS C 138       2.202  32.289  -9.223  1.00 50.74           C
ANISOU 1011  CG  HIS C 138     6897   5538   6844   -563    809   -847       C
ATOM   1012  ND1 HIS C 138       1.054  32.876  -8.742  1.00 51.19           N
ANISOU 1012  ND1 HIS C 138     6928   5567   6956   -569    869   -840       N
ATOM   1013  CD2 HIS C 138       3.160  32.503  -8.293  1.00 49.66           C
ANISOU 1013  CD2 HIS C 138     6781   5403   6683   -602    831   -914       C
ATOM   1014  CE1 HIS C 138       1.307  33.425  -7.566  1.00 50.39           C
ANISOU 1014  CE1 HIS C 138     6833   5450   6863   -610    927   -903       C
ATOM   1015  NE2 HIS C 138       2.571  33.216  -7.269  1.00 49.53           N
ANISOU 1015  NE2 HIS C 138     6752   5361   6705   -632    904   -949       N
ATOM   1016  N   MET C 139       2.257  28.287 -11.812  1.00 50.12           N
ANISOU 1016  N   MET C 139     6871   5583   6588   -501    518   -728       N
ATOM   1017  CA  MET C 139       2.549  27.522 -13.022  1.00 50.03           C
ANISOU 1017  CA  MET C 139     6870   5598   6543   -470    449   -690       C
ATOM   1018  C   MET C 139       1.286  26.975 -13.680  1.00 50.80           C
ANISOU 1018  C   MET C 139     6949   5708   6646   -451    415   -635       C
ATOM   1019  O   MET C 139       1.293  26.629 -14.861  1.00 51.83           O
ANISOU 1019  O   MET C 139     7074   5855   6763   -420    372   -594       O
ATOM   1020  CB  MET C 139       3.522  26.381 -12.721  1.00 49.19           C
ANISOU 1020  CB  MET C 139     6805   5522   6362   -489    386   -723       C
ATOM   1021  CG  MET C 139       4.938  26.831 -12.396  1.00 48.48           C
ANISOU 1021  CG  MET C 139     6732   5427   6261   -500    406   -769       C
ATOM   1022  SD  MET C 139       5.718  27.734 -13.748  1.00 49.31           S
ANISOU 1022  SD  MET C 139     6820   5516   6399   -455    424   -742       S
ATOM   1023  CE  MET C 139       5.654  29.411 -13.126  1.00 48.83           C
ANISOU 1023  CE  MET C 139     6730   5409   6413   -466    529   -766       C
ATOM   1024  N   ASP C 140       0.203  26.903 -12.914  1.00 41.20           N
ANISOU 1024  N   ASP C 140     5721   4486   5446   -472    435   -634       N
ATOM   1025  CA  ASP C 140      -1.058  26.372 -13.421  1.00 41.85           C
ANISOU 1025  CA  ASP C 140     5783   4582   5535   -459    404   -584       C
ATOM   1026  C   ASP C 140      -1.900  27.447 -14.104  1.00 42.93           C
ANISOU 1026  C   ASP C 140     5872   4696   5742   -427    454   -534       C
ATOM   1027  O   ASP C 140      -2.974  27.161 -14.632  1.00 43.73           O
ANISOU 1027  O   ASP C 140     5950   4810   5855   -413    433   -485       O
ATOM   1028  CB  ASP C 140      -1.857  25.723 -12.289  1.00 42.24           C
ANISOU 1028  CB  ASP C 140     5841   4638   5569   -495    399   -603       C
ATOM   1029  CG  ASP C 140      -2.146  26.687 -11.153  1.00 42.57           C
ANISOU 1029  CG  ASP C 140     5870   4649   5655   -519    479   -635       C
ATOM   1030  OD1 ASP C 140      -1.241  27.466 -10.787  1.00 42.51           O
ANISOU 1030  OD1 ASP C 140     5869   4623   5660   -526    523   -674       O
ATOM   1031  OD2 ASP C 140      -3.280  26.668 -10.631  1.00 43.03           O
ANISOU 1031  OD2 ASP C 140     5910   4702   5737   -531    499   -624       O
ATOM   1032  N   THR C 141      -1.407  28.681 -14.092  1.00 38.04           N
ANISOU 1032  N   THR C 141     5238   4044   5172   -416    521   -544       N
ATOM   1033  CA  THR C 141      -2.141  29.802 -14.669  1.00 38.98           C
ANISOU 1033  CA  THR C 141     5309   4136   5365   -385    578   -495       C
ATOM   1034  C   THR C 141      -1.621  30.168 -16.056  1.00 40.55           C
ANISOU 1034  C   THR C 141     5494   4340   5572   -342    564   -452       C
ATOM   1035  O   THR C 141      -2.310  30.831 -16.831  1.00 41.74           O
ANISOU 1035  O   THR C 141     5604   4482   5773   -309    590   -395       O
ATOM   1036  CB  THR C 141      -2.065  31.048 -13.764  1.00 39.17           C
ANISOU 1036  CB  THR C 141     5319   4113   5451   -399    673   -530       C
ATOM   1037  OG1 THR C 141      -0.705  31.488 -13.663  1.00 38.34           O
ANISOU 1037  OG1 THR C 141     5236   3997   5336   -405    691   -573       O
ATOM   1038  CG2 THR C 141      -2.599  30.735 -12.373  1.00 38.33           C
ANISOU 1038  CG2 THR C 141     5225   4003   5335   -442    691   -573       C
ATOM   1039  N   ILE C 142      -0.405  29.731 -16.363  1.00 49.80           N
ANISOU 1039  N   ILE C 142     6700   5529   6694   -342    524   -478       N
ATOM   1040  CA  ILE C 142       0.237  30.065 -17.630  1.00 50.56           C
ANISOU 1040  CA  ILE C 142     6787   5631   6792   -304    512   -444       C
ATOM   1041  C   ILE C 142      -0.333  29.280 -18.807  1.00 51.72           C
ANISOU 1041  C   ILE C 142     6924   5818   6909   -279    445   -387       C
ATOM   1042  O   ILE C 142      -0.454  28.057 -18.752  1.00 51.76           O
ANISOU 1042  O   ILE C 142     6955   5856   6855   -295    378   -397       O
ATOM   1043  CB  ILE C 142       1.759  29.842 -17.552  1.00 49.87           C
ANISOU 1043  CB  ILE C 142     6737   5549   6662   -314    493   -492       C
ATOM   1044  CG1 ILE C 142       2.391  30.886 -16.635  1.00 49.56           C
ANISOU 1044  CG1 ILE C 142     6698   5469   6662   -333    569   -541       C
ATOM   1045  CG2 ILE C 142       2.392  29.907 -18.933  1.00 50.04           C
ANISOU 1045  CG2 ILE C 142     6754   5586   6671   -275    465   -455       C
ATOM   1046  CD1 ILE C 142       3.344  30.301 -15.641  1.00 48.89           C
ANISOU 1046  CD1 ILE C 142     6655   5394   6525   -372    549   -609       C
ATOM   1047  N   ASP C 143      -0.688  29.999 -19.867  1.00 44.46           N
ANISOU 1047  N   ASP C 143     5966   4897   6029   -240    464   -327       N
ATOM   1048  CA  ASP C 143      -1.152  29.381 -21.102  1.00 46.01           C
ANISOU 1048  CA  ASP C 143     6150   5135   6195   -214    403   -271       C
ATOM   1049  C   ASP C 143       0.040  28.843 -21.886  1.00 45.26           C
ANISOU 1049  C   ASP C 143     6086   5066   6043   -203    352   -284       C
ATOM   1050  O   ASP C 143       0.658  29.565 -22.669  1.00 45.56           O
ANISOU 1050  O   ASP C 143     6111   5098   6100   -174    374   -261       O
ATOM   1051  CB  ASP C 143      -1.926  30.397 -21.943  1.00 47.85           C
ANISOU 1051  CB  ASP C 143     6327   5361   6491   -176    444   -199       C
ATOM   1052  CG  ASP C 143      -2.451  29.806 -23.236  1.00 50.03           C
ANISOU 1052  CG  ASP C 143     6587   5687   6735   -151    382   -139       C
ATOM   1053  OD1 ASP C 143      -2.771  28.599 -23.256  1.00 50.68           O
ANISOU 1053  OD1 ASP C 143     6690   5804   6760   -170    314   -149       O
ATOM   1054  OD2 ASP C 143      -2.545  30.552 -24.234  1.00 50.95           O
ANISOU 1054  OD2 ASP C 143     6667   5808   6882   -114    401    -82       O
ATOM   1055  N   TRP C 144       0.358  27.571 -21.671  1.00 30.31           N
ANISOU 1055  N   TRP C 144     4234   3200   4083   -227    287   -318       N
ATOM   1056  CA  TRP C 144       1.537  26.960 -22.277  1.00 30.02           C
ANISOU 1056  CA  TRP C 144     4231   3185   3991   -220    240   -338       C
ATOM   1057  C   TRP C 144       1.391  26.722 -23.779  1.00 30.11           C
ANISOU 1057  C   TRP C 144     4228   3233   3980   -187    197   -284       C
ATOM   1058  O   TRP C 144       2.387  26.594 -24.490  1.00 29.97           O
ANISOU 1058  O   TRP C 144     4227   3227   3932   -171    176   -289       O
ATOM   1059  CB  TRP C 144       1.895  25.656 -21.563  1.00 29.68           C
ANISOU 1059  CB  TRP C 144     4235   3157   3887   -254    186   -389       C
ATOM   1060  CG  TRP C 144       2.457  25.865 -20.191  1.00 29.56           C
ANISOU 1060  CG  TRP C 144     4241   3113   3879   -286    222   -447       C
ATOM   1061  CD1 TRP C 144       1.791  25.763 -19.005  1.00 29.62           C
ANISOU 1061  CD1 TRP C 144     4248   3106   3898   -317    242   -470       C
ATOM   1062  CD2 TRP C 144       3.806  26.221 -19.865  1.00 29.40           C
ANISOU 1062  CD2 TRP C 144     4243   3078   3852   -290    242   -489       C
ATOM   1063  NE1 TRP C 144       2.642  26.030 -17.960  1.00 29.51           N
ANISOU 1063  NE1 TRP C 144     4256   3073   3883   -342    273   -525       N
ATOM   1064  CE2 TRP C 144       3.884  26.314 -18.461  1.00 29.38           C
ANISOU 1064  CE2 TRP C 144     4252   3055   3856   -327    273   -538       C
ATOM   1065  CE3 TRP C 144       4.954  26.470 -20.623  1.00 29.30           C
ANISOU 1065  CE3 TRP C 144     4238   3068   3827   -268    238   -490       C
ATOM   1066  CZ2 TRP C 144       5.066  26.644 -17.800  1.00 29.27           C
ANISOU 1066  CZ2 TRP C 144     4258   3027   3835   -343    298   -587       C
ATOM   1067  CZ3 TRP C 144       6.126  26.797 -19.965  1.00 29.17           C
ANISOU 1067  CZ3 TRP C 144     4242   3035   3808   -283    263   -539       C
ATOM   1068  CH2 TRP C 144       6.173  26.881 -18.568  1.00 29.16           C
ANISOU 1068  CH2 TRP C 144     4252   3016   3812   -320    292   -587       C
ATOM   1069  N   ARG C 145       0.152  26.665 -24.257  1.00 39.62           N
ANISOU 1069  N   ARG C 145     5399   4456   5199   -177    185   -233       N
ATOM   1070  CA  ARG C 145      -0.103  26.493 -25.685  1.00 41.61           C
ANISOU 1070  CA  ARG C 145     5631   4749   5429   -147    146   -179       C
ATOM   1071  C   ARG C 145       0.311  27.731 -26.476  1.00 42.43           C
ANISOU 1071  C   ARG C 145     5704   4842   5575   -109    194   -138       C
ATOM   1072  O   ARG C 145       0.578  27.653 -27.675  1.00 43.65           O
ANISOU 1072  O   ARG C 145     5852   5030   5705    -83    165   -104       O
ATOM   1073  CB  ARG C 145      -1.576  26.164 -25.941  1.00 42.93           C
ANISOU 1073  CB  ARG C 145     5765   4942   5602   -149    123   -133       C
ATOM   1074  CG  ARG C 145      -1.965  24.744 -25.565  1.00 42.63           C
ANISOU 1074  CG  ARG C 145     5758   4928   5510   -183     59   -164       C
ATOM   1075  CD  ARG C 145      -1.137  23.729 -26.338  1.00 42.59           C
ANISOU 1075  CD  ARG C 145     5791   4957   5436   -182     -6   -184       C
ATOM   1076  NE  ARG C 145      -1.416  22.359 -25.919  1.00 41.63           N
ANISOU 1076  NE  ARG C 145     5701   4851   5266   -215    -63   -217       N
ATOM   1077  CZ  ARG C 145      -0.714  21.301 -26.313  1.00 40.78           C
ANISOU 1077  CZ  ARG C 145     5632   4763   5098   -223   -118   -247       C
ATOM   1078  NH1 ARG C 145       0.315  21.454 -27.135  1.00 40.39           N
ANISOU 1078  NH1 ARG C 145     5595   4723   5026   -200   -125   -248       N
ATOM   1079  NH2 ARG C 145      -1.038  20.090 -25.880  1.00 40.22           N
ANISOU 1079  NH2 ARG C 145     5589   4703   4992   -253   -164   -275       N
ATOM   1080  N   ASP C 146       0.364  28.871 -25.795  1.00 39.98           N
ANISOU 1080  N   ASP C 146     5375   4485   5331   -106    270   -143       N
ATOM   1081  CA  ASP C 146       0.797  30.119 -26.412  1.00 39.91           C
ANISOU 1081  CA  ASP C 146     5337   4456   5371    -71    325   -107       C
ATOM   1082  C   ASP C 146       2.306  30.101 -26.633  1.00 39.48           C
ANISOU 1082  C   ASP C 146     5317   4398   5287    -67    319   -145       C
ATOM   1083  O   ASP C 146       2.830  30.822 -27.481  1.00 40.11           O
ANISOU 1083  O   ASP C 146     5380   4476   5385    -36    342   -112       O
ATOM   1084  CB  ASP C 146       0.413  31.306 -25.525  1.00 39.59           C
ANISOU 1084  CB  ASP C 146     5268   4361   5413    -74    411   -108       C
ATOM   1085  CG  ASP C 146       0.578  32.642 -26.227  1.00 40.54           C
ANISOU 1085  CG  ASP C 146     5349   4460   5597    -35    473    -58       C
ATOM   1086  OD1 ASP C 146       1.716  33.154 -26.284  1.00 40.17           O
ANISOU 1086  OD1 ASP C 146     5316   4391   5557    -28    501    -82       O
ATOM   1087  OD2 ASP C 146      -0.435  33.188 -26.711  1.00 41.88           O
ANISOU 1087  OD2 ASP C 146     5469   4632   5809    -11    495      9       O
ATOM   1088  N   ILE C 147       2.998  29.265 -25.865  1.00 35.31           N
ANISOU 1088  N   ILE C 147     4835   3867   4713    -99    289   -211       N
ATOM   1089  CA  ILE C 147       4.452  29.177 -25.931  1.00 34.43           C
ANISOU 1089  CA  ILE C 147     4758   3751   4572    -99    283   -252       C
ATOM   1090  C   ILE C 147       4.914  27.986 -26.768  1.00 34.60           C
ANISOU 1090  C   ILE C 147     4809   3818   4517    -95    205   -255       C
ATOM   1091  O   ILE C 147       5.824  28.109 -27.589  1.00 34.61           O
ANISOU 1091  O   ILE C 147     4818   3831   4501    -73    197   -248       O
ATOM   1092  CB  ILE C 147       5.065  29.071 -24.520  1.00 32.97           C
ANISOU 1092  CB  ILE C 147     4604   3536   4386   -137    303   -324       C
ATOM   1093  CG1 ILE C 147       4.589  30.233 -23.647  1.00 32.91           C
ANISOU 1093  CG1 ILE C 147     4569   3483   4454   -145    383   -327       C
ATOM   1094  CG2 ILE C 147       6.584  29.037 -24.593  1.00 32.23           C
ANISOU 1094  CG2 ILE C 147     4541   3439   4266   -136    299   -363       C
ATOM   1095  CD1 ILE C 147       5.079  30.163 -22.220  1.00 31.79           C
ANISOU 1095  CD1 ILE C 147     4455   3315   4309   -186    406   -398       C
ATOM   1096  N   VAL C 148       4.278  26.837 -26.557  1.00 29.87           N
ANISOU 1096  N   VAL C 148     4227   3245   3877   -117    149   -265       N
ATOM   1097  CA  VAL C 148       4.647  25.608 -27.255  1.00 29.67           C
ANISOU 1097  CA  VAL C 148     4234   3261   3781   -117     76   -275       C
ATOM   1098  C   VAL C 148       4.093  25.566 -28.679  1.00 29.93           C
ANISOU 1098  C   VAL C 148     4240   3334   3798    -88     47   -214       C
ATOM   1099  O   VAL C 148       2.879  25.533 -28.884  1.00 30.39           O
ANISOU 1099  O   VAL C 148     4268   3409   3868    -88     39   -175       O
ATOM   1100  CB  VAL C 148       4.175  24.362 -26.477  1.00 29.48           C
ANISOU 1100  CB  VAL C 148     4238   3245   3719   -153     30   -310       C
ATOM   1101  CG1 VAL C 148       4.411  23.102 -27.292  1.00 29.35           C
ANISOU 1101  CG1 VAL C 148     4249   3269   3635   -153    -43   -315       C
ATOM   1102  CG2 VAL C 148       4.885  24.277 -25.135  1.00 29.23           C
ANISOU 1102  CG2 VAL C 148     4235   3181   3688   -183     50   -371       C
ATOM   1103  N   ARG C 149       4.996  25.565 -29.656  1.00 41.96           N
ANISOU 1103  N   ARG C 149     5773   4877   5293    -65     32   -207       N
ATOM   1104  CA  ARG C 149       4.621  25.580 -31.068  1.00 43.89           C
ANISOU 1104  CA  ARG C 149     5992   5165   5518    -36      6   -151       C
ATOM   1105  C   ARG C 149       3.983  24.271 -31.525  1.00 44.28           C
ANISOU 1105  C   ARG C 149     6057   5260   5508    -52    -66   -152       C
ATOM   1106  O   ARG C 149       2.950  24.277 -32.196  1.00 46.04           O
ANISOU 1106  O   ARG C 149     6247   5516   5730    -44    -83   -102       O
ATOM   1107  CB  ARG C 149       5.842  25.891 -31.938  1.00 44.47           C
ANISOU 1107  CB  ARG C 149     6076   5246   5573     -9     11   -148       C
ATOM   1108  CG  ARG C 149       6.378  27.306 -31.786  1.00 45.02           C
ANISOU 1108  CG  ARG C 149     6122   5277   5705     12     84   -132       C
ATOM   1109  CD  ARG C 149       5.543  28.309 -32.568  1.00 46.76           C
ANISOU 1109  CD  ARG C 149     6288   5509   5971     43    117    -56       C
ATOM   1110  NE  ARG C 149       5.666  28.118 -34.011  0.00 48.02           N
ANISOU 1110  NE  ARG C 149     6438   5719   6089     71     82    -12       N
ATOM   1111  CZ  ARG C 149       5.069  28.882 -34.920  0.00 49.21           C
ANISOU 1111  CZ  ARG C 149     6542   5891   6264    102    101     61       C
ATOM   1112  NH1 ARG C 149       4.304  29.895 -34.538  0.00 49.20           N
ANISOU 1112  NH1 ARG C 149     6498   5862   6335    111    156    100       N
ATOM   1113  NH2 ARG C 149       5.238  28.635 -36.211  0.00 50.09           N
ANISOU 1113  NH2 ARG C 149     6648   6055   6330    124     65     96       N
ATOM   1114  N   ASP C 150       4.601  23.151 -31.165  1.00 46.27           N
ANISOU 1114  N   ASP C 150     6356   5513   5712    -75   -108   -207       N
ATOM   1115  CA  ASP C 150       4.124  21.842 -31.602  1.00 46.25           C
ANISOU 1115  CA  ASP C 150     6372   5549   5653    -92   -175   -215       C
ATOM   1116  C   ASP C 150       2.852  21.423 -30.868  1.00 46.46           C
ANISOU 1116  C   ASP C 150     6387   5573   5692   -119   -187   -213       C
ATOM   1117  O   ASP C 150       2.851  21.263 -29.648  1.00 45.63           O
ANISOU 1117  O   ASP C 150     6299   5435   5605   -144   -172   -250       O
ATOM   1118  CB  ASP C 150       5.217  20.785 -31.423  1.00 44.68           C
ANISOU 1118  CB  ASP C 150     6226   5346   5403   -106   -211   -274       C
ATOM   1119  CG  ASP C 150       4.854  19.455 -32.057  1.00 45.01           C
ANISOU 1119  CG  ASP C 150     6288   5427   5387   -120   -278   -283       C
ATOM   1120  OD1 ASP C 150       3.954  19.430 -32.923  1.00 46.14           O
ANISOU 1120  OD1 ASP C 150     6404   5609   5519   -114   -299   -242       O
ATOM   1121  OD2 ASP C 150       5.475  18.433 -31.695  1.00 44.02           O
ANISOU 1121  OD2 ASP C 150     6206   5294   5227   -138   -308   -332       O
ATOM   1122  N   ARG C 151       1.789  21.243 -31.618  1.00 42.13           N
ANISOU 1122  N   ARG C 151     5810   5064   5135   -116   -214   -170       N
ATOM   1123  CA  ARG C 151       0.515  20.865 -31.079  1.00 42.41           C
ANISOU 1123  CA  ARG C 151     5829   5103   5182   -140   -227   -161       C
ATOM   1124  C   ARG C 151       0.478  19.458 -30.534  1.00 41.19           C
ANISOU 1124  C   ARG C 151     5715   4949   4985   -176   -276   -211       C
ATOM   1125  O   ARG C 151      -0.361  19.118 -29.758  1.00 41.21           O
ANISOU 1125  O   ARG C 151     5714   4942   5002   -200   -280   -217       O
ATOM   1126  CB  ARG C 151      -0.516  21.055 -32.143  1.00 44.42           C
ANISOU 1126  CB  ARG C 151     6040   5405   5434   -126   -245    -99       C
ATOM   1127  CG  ARG C 151      -0.685  22.520 -32.467  0.00 46.41           C
ANISOU 1127  CG  ARG C 151     6244   5650   5742    -92   -187    -42       C
ATOM   1128  CD  ARG C 151      -1.761  22.719 -33.507  0.00 48.37           C
ANISOU 1128  CD  ARG C 151     6442   5948   5987    -77   -206     27       C
ATOM   1129  NE  ARG C 151      -1.902  24.114 -33.894  0.00 49.82           N
ANISOU 1129  NE  ARG C 151     6577   6125   6225    -41   -151     88       N
ATOM   1130  CZ  ARG C 151      -2.696  24.538 -34.872  0.00 50.66           C
ANISOU 1130  CZ  ARG C 151     6634   6276   6336    -19   -157    159       C
ATOM   1131  NH1 ARG C 151      -3.425  23.669 -35.556  0.00 50.63           N
ANISOU 1131  NH1 ARG C 151     6624   6331   6284    -33   -218    173       N
ATOM   1132  NH2 ARG C 151      -2.756  25.832 -35.164  0.00 50.86           N
ANISOU 1132  NH2 ARG C 151     6616   6290   6417     16   -101    216       N
ATOM   1133  N   ASP C 152       1.379  18.624 -30.978  1.00 46.66           N
ANISOU 1133  N   ASP C 152     6447   5654   5627   -178   -313   -245       N
ATOM   1134  CA  ASP C 152       1.451  17.278 -30.475  1.00 44.59           C
ANISOU 1134  CA  ASP C 152     6227   5388   5328   -210   -357   -293       C
ATOM   1135  C   ASP C 152       2.323  17.081 -29.249  1.00 42.96           C
ANISOU 1135  C   ASP C 152     6057   5138   5130   -225   -338   -344       C
ATOM   1136  O   ASP C 152       2.475  15.974 -28.794  1.00 41.81           O
ANISOU 1136  O   ASP C 152     5945   4987   4956   -249   -372   -382       O
ATOM   1137  CB  ASP C 152       1.978  16.364 -31.560  1.00 43.76           C
ANISOU 1137  CB  ASP C 152     6147   5316   5163   -206   -407   -308       C
ATOM   1138  CG  ASP C 152       1.187  16.425 -32.784  1.00 45.01           C
ANISOU 1138  CG  ASP C 152     6273   5525   5303   -196   -432   -263       C
ATOM   1139  OD1 ASP C 152      -0.026  16.426 -32.708  1.00 45.56           O
ANISOU 1139  OD1 ASP C 152     6312   5610   5388   -209   -440   -235       O
ATOM   1140  OD2 ASP C 152       1.790  16.444 -33.836  1.00 45.68           O
ANISOU 1140  OD2 ASP C 152     6362   5637   5356   -176   -445   -256       O
ATOM   1141  N   ALA C 153       2.944  18.127 -28.747  1.00 29.27           N
ANISOU 1141  N   ALA C 153     4315   3374   3432   -211   -286   -345       N
ATOM   1142  CA  ALA C 153       3.781  18.006 -27.594  1.00 28.96           C
ANISOU 1142  CA  ALA C 153     4307   3299   3399   -226   -268   -392       C
ATOM   1143  C   ALA C 153       3.006  17.960 -26.309  1.00 28.93           C
ANISOU 1143  C   ALA C 153     4298   3273   3423   -255   -251   -404       C
ATOM   1144  O   ALA C 153       1.994  18.581 -26.181  1.00 29.14           O
ANISOU 1144  O   ALA C 153     4289   3298   3486   -254   -226   -372       O
ATOM   1145  CB  ALA C 153       4.761  19.121 -27.586  1.00 28.89           C
ANISOU 1145  CB  ALA C 153     4292   3270   3417   -203   -219   -392       C
ATOM   1146  N   GLU C 154       3.511  17.227 -25.362  1.00 55.92           N
ANISOU 1146  N   GLU C 154     7750   6673   6823   -278   -263   -448       N
ATOM   1147  CA  GLU C 154       2.815  16.995 -24.119  1.00 55.64           C
ANISOU 1147  CA  GLU C 154     7716   6620   6805   -309   -253   -462       C
ATOM   1148  C   GLU C 154       3.044  18.100 -23.125  1.00 55.95           C
ANISOU 1148  C   GLU C 154     7743   6629   6888   -312   -191   -472       C
ATOM   1149  O   GLU C 154       4.150  18.495 -22.917  1.00 55.58           O
ANISOU 1149  O   GLU C 154     7710   6568   6840   -305   -170   -495       O
ATOM   1150  CB  GLU C 154       3.282  15.661 -23.534  1.00 53.97           C
ANISOU 1150  CB  GLU C 154     7548   6406   6554   -334   -294   -503       C
ATOM   1151  CG  GLU C 154       2.168  14.657 -23.373  1.00 54.24           C
ANISOU 1151  CG  GLU C 154     7583   6451   6575   -358   -331   -498       C
ATOM   1152  CD  GLU C 154       2.571  13.348 -22.725  1.00 53.16           C
ANISOU 1152  CD  GLU C 154     7487   6307   6405   -383   -368   -535       C
ATOM   1153  OE1 GLU C 154       2.235  13.090 -21.557  1.00 52.89           O
ANISOU 1153  OE1 GLU C 154     7459   6258   6380   -409   -359   -549       O
ATOM   1154  OE2 GLU C 154       3.183  12.533 -23.409  1.00 52.45           O
ANISOU 1154  OE2 GLU C 154     7422   6227   6279   -377   -405   -547       O
ATOM   1155  N   ILE C 155       1.994  18.603 -22.504  1.00 32.00           N
ANISOU 1155  N   ILE C 155     4682   3585   3893   -323   -160   -456       N
ATOM   1156  CA  ILE C 155       2.192  19.564 -21.454  1.00 32.67           C
ANISOU 1156  CA  ILE C 155     4758   3639   4017   -331   -100   -473       C
ATOM   1157  C   ILE C 155       1.702  19.061 -20.132  1.00 32.23           C
ANISOU 1157  C   ILE C 155     4713   3571   3960   -367    -98   -499       C
ATOM   1158  O   ILE C 155       0.546  18.952 -19.942  1.00 33.63           O
ANISOU 1158  O   ILE C 155     4872   3752   4154   -378    -99   -479       O
ATOM   1159  CB  ILE C 155       1.409  20.821 -21.746  1.00 34.04           C
ANISOU 1159  CB  ILE C 155     4885   3803   4247   -313    -50   -432       C
ATOM   1160  CG1 ILE C 155       1.938  21.460 -23.003  1.00 34.76           C
ANISOU 1160  CG1 ILE C 155     4961   3904   4342   -275    -44   -402       C
ATOM   1161  CG2 ILE C 155       1.529  21.778 -20.591  1.00 32.99           C
ANISOU 1161  CG2 ILE C 155     4743   3635   4156   -325     16   -454       C
ATOM   1162  CD1 ILE C 155       1.051  22.516 -23.566  1.00 36.16           C
ANISOU 1162  CD1 ILE C 155     5089   4081   4570   -252     -6   -348       C
ATOM   1163  N   VAL C 156       2.574  18.789 -19.189  1.00 32.17           N
ANISOU 1163  N   VAL C 156     4736   3552   3934   -387    -94   -543       N
ATOM   1164  CA  VAL C 156       2.088  18.252 -17.932  1.00 31.53           C
ANISOU 1164  CA  VAL C 156     4666   3465   3849   -422    -95   -565       C
ATOM   1165  C   VAL C 156       2.483  19.099 -16.756  1.00 31.23           C
ANISOU 1165  C   VAL C 156     4627   3405   3835   -439    -38   -595       C
ATOM   1166  O   VAL C 156       3.579  19.016 -16.277  1.00 30.52           O
ANISOU 1166  O   VAL C 156     4560   3312   3724   -447    -37   -629       O
ATOM   1167  CB  VAL C 156       2.604  16.822 -17.683  1.00 30.59           C
ANISOU 1167  CB  VAL C 156     4588   3359   3678   -439   -151   -590       C
ATOM   1168  CG1 VAL C 156       1.853  16.155 -16.563  1.00 30.23           C
ANISOU 1168  CG1 VAL C 156     4548   3310   3626   -473   -158   -601       C
ATOM   1169  CG2 VAL C 156       2.515  15.982 -18.925  1.00 30.75           C
ANISOU 1169  CG2 VAL C 156     4615   3399   3669   -423   -206   -570       C
ATOM   1170  N   VAL C 157       1.555  19.881 -16.261  1.00 28.74           N
ANISOU 1170  N   VAL C 157     4282   3075   3564   -446      9   -584       N
ATOM   1171  CA  VAL C 157       1.851  20.737 -15.166  1.00 28.80           C
ANISOU 1171  CA  VAL C 157     4286   3061   3597   -464     67   -615       C
ATOM   1172  C   VAL C 157       0.839  20.463 -14.121  1.00 28.93           C
ANISOU 1172  C   VAL C 157     4297   3074   3620   -494     78   -621       C
ATOM   1173  O   VAL C 157      -0.279  20.825 -14.243  1.00 29.14           O
ANISOU 1173  O   VAL C 157     4295   3094   3682   -490     99   -591       O
ATOM   1174  CB  VAL C 157       1.778  22.181 -15.640  1.00 29.01           C
ANISOU 1174  CB  VAL C 157     4278   3065   3678   -439    127   -596       C
ATOM   1175  CG1 VAL C 157       2.110  23.124 -14.539  1.00 29.11           C
ANISOU 1175  CG1 VAL C 157     4287   3054   3720   -460    192   -633       C
ATOM   1176  CG2 VAL C 157       2.755  22.386 -16.758  1.00 28.89           C
ANISOU 1176  CG2 VAL C 157     4268   3057   3653   -408    112   -586       C
ATOM   1177  N   LYS C 158       1.250  19.797 -13.078  1.00 31.80           N
ANISOU 1177  N   LYS C 158     4689   3443   3950   -525     65   -657       N
ATOM   1178  CA  LYS C 158       0.338  19.418 -12.053  1.00 31.73           C
ANISOU 1178  CA  LYS C 158     4679   3436   3943   -555     71   -663       C
ATOM   1179  C   LYS C 158       1.086  19.044 -10.828  1.00 31.92           C
ANISOU 1179  C   LYS C 158     4730   3464   3931   -588     73   -707       C
ATOM   1180  O   LYS C 158       2.272  18.921 -10.858  1.00 30.42           O
ANISOU 1180  O   LYS C 158     4562   3281   3714   -585     59   -729       O
ATOM   1181  CB  LYS C 158      -0.570  18.284 -12.518  1.00 32.32           C
ANISOU 1181  CB  LYS C 158     4756   3527   3999   -555     16   -632       C
ATOM   1182  CG  LYS C 158       0.104  17.040 -13.015  1.00 31.26           C
ANISOU 1182  CG  LYS C 158     4654   3411   3814   -552    -52   -636       C
ATOM   1183  CD  LYS C 158      -0.953  16.101 -13.521  1.00 32.31           C
ANISOU 1183  CD  LYS C 158     4782   3556   3939   -553    -97   -606       C
ATOM   1184  CE  LYS C 158      -0.392  14.769 -13.890  1.00 31.24           C
ANISOU 1184  CE  LYS C 158     4680   3435   3756   -555   -161   -613       C
ATOM   1185  NZ  LYS C 158       0.063  14.052 -12.705  1.00 30.95           N
ANISOU 1185  NZ  LYS C 158     4671   3398   3689   -584   -170   -643       N
ATOM   1186  N   ASP C 159       0.353  18.871  -9.748  1.00 28.96           N
ANISOU 1186  N   ASP C 159     4354   3090   3559   -618     90   -717       N
ATOM   1187  CA  ASP C 159       0.871  18.388  -8.471  1.00 28.92           C
ANISOU 1187  CA  ASP C 159     4374   3098   3517   -653     87   -755       C
ATOM   1188  C   ASP C 159       2.016  19.246  -7.932  1.00 28.93           C
ANISOU 1188  C   ASP C 159     4381   3095   3516   -662    128   -795       C
ATOM   1189  O   ASP C 159       3.054  18.729  -7.520  1.00 28.79           O
ANISOU 1189  O   ASP C 159     4389   3094   3456   -675    102   -820       O
ATOM   1190  CB  ASP C 159       1.295  16.919  -8.582  1.00 28.71           C
ANISOU 1190  CB  ASP C 159     4379   3092   3438   -657     16   -751       C
ATOM   1191  CG  ASP C 159       1.315  16.213  -7.240  1.00 28.75           C
ANISOU 1191  CG  ASP C 159     4402   3112   3409   -695      9   -773       C
ATOM   1192  OD1 ASP C 159       2.037  15.203  -7.111  1.00 28.59           O
ANISOU 1192  OD1 ASP C 159     4410   3108   3346   -700    -37   -779       O
ATOM   1193  OD2 ASP C 159       0.607  16.665  -6.314  1.00 28.96           O
ANISOU 1193  OD2 ASP C 159     4415   3134   3452   -719     51   -783       O
ATOM   1194  N   ASN C 160       1.820  20.561  -7.946  1.00 29.12           N
ANISOU 1194  N   ASN C 160     4379   3096   3589   -657    191   -801       N
ATOM   1195  CA  ASN C 160       2.779  21.484  -7.351  1.00 29.19           C
ANISOU 1195  CA  ASN C 160     4390   3099   3603   -670    239   -844       C
ATOM   1196  C   ASN C 160       2.189  22.175  -6.126  1.00 29.49           C
ANISOU 1196  C   ASN C 160     4415   3127   3662   -704    301   -873       C
ATOM   1197  O   ASN C 160       1.376  21.589  -5.413  1.00 29.57           O
ANISOU 1197  O   ASN C 160     4428   3147   3660   -726    293   -870       O
ATOM   1198  CB  ASN C 160       3.254  22.520  -8.372  1.00 29.20           C
ANISOU 1198  CB  ASN C 160     4374   3078   3643   -637    268   -834       C
ATOM   1199  CG  ASN C 160       3.880  21.886  -9.598  1.00 28.93           C
ANISOU 1199  CG  ASN C 160     4352   3055   3585   -604    209   -808       C
ATOM   1200  OD1 ASN C 160       5.013  21.405  -9.555  1.00 28.74           O
ANISOU 1200  OD1 ASN C 160     4353   3047   3521   -607    178   -828       O
ATOM   1201  ND2 ASN C 160       3.146  21.890 -10.705  1.00 28.94           N
ANISOU 1201  ND2 ASN C 160     4336   3050   3611   -572    196   -763       N
ATOM   1202  N   GLY C 161       2.597  23.421  -5.898  1.00 29.67           N
ANISOU 1202  N   GLY C 161     4425   3129   3719   -708    365   -901       N
ATOM   1203  CA  GLY C 161       2.143  24.195  -4.754  1.00 29.99           C
ANISOU 1203  CA  GLY C 161     4454   3159   3784   -742    433   -936       C
ATOM   1204  C   GLY C 161       0.636  24.228  -4.595  1.00 30.19           C
ANISOU 1204  C   GLY C 161     4458   3170   3844   -742    455   -909       C
ATOM   1205  O   GLY C 161      -0.097  24.387  -5.569  1.00 30.20           O
ANISOU 1205  O   GLY C 161     4437   3154   3884   -708    452   -863       O
ATOM   1206  N   ARG C 162       0.174  24.073  -3.358  1.00 39.72           N
ANISOU 1206  N   ARG C 162     5669   4387   5036   -781    477   -936       N
ATOM   1207  CA  ARG C 162      -1.255  24.004  -3.079  1.00 40.30           C
ANISOU 1207  CA  ARG C 162     5723   4451   5138   -785    496   -912       C
ATOM   1208  C   ARG C 162      -1.782  25.258  -2.384  1.00 40.74           C
ANISOU 1208  C   ARG C 162     5755   4477   5248   -801    587   -939       C
ATOM   1209  O   ARG C 162      -2.869  25.739  -2.702  1.00 41.91           O
ANISOU 1209  O   ARG C 162     5874   4599   5451   -784    622   -909       O
ATOM   1210  CB  ARG C 162      -1.579  22.747  -2.264  1.00 39.94           C
ANISOU 1210  CB  ARG C 162     5699   4438   5038   -814    450   -913       C
ATOM   1211  CG  ARG C 162      -1.655  21.482  -3.110  1.00 39.58           C
ANISOU 1211  CG  ARG C 162     5667   4410   4962   -792    367   -870       C
ATOM   1212  CD  ARG C 162      -1.821  20.229  -2.264  1.00 39.15           C
ANISOU 1212  CD  ARG C 162     5636   4387   4854   -821    322   -873       C
ATOM   1213  NE  ARG C 162      -0.542  19.707  -1.793  1.00 38.61           N
ANISOU 1213  NE  ARG C 162     5597   4345   4727   -838    290   -903       N
ATOM   1214  CZ  ARG C 162      -0.234  19.519  -0.514  1.00 38.71           C
ANISOU 1214  CZ  ARG C 162     5624   4382   4702   -878    302   -937       C
ATOM   1215  NH1 ARG C 162      -1.118  19.808   0.431  1.00 39.25           N
ANISOU 1215  NH1 ARG C 162     5681   4449   4782   -906    347   -950       N
ATOM   1216  NH2 ARG C 162       0.956  19.037  -0.180  1.00 38.00           N
ANISOU 1216  NH2 ARG C 162     5559   4319   4560   -890    270   -958       N
ATOM   1217  N   SER C 163      -1.011  25.785  -1.438  1.00 51.61           N
ANISOU 1217  N   SER C 163     7144   5859   6608   -835    627   -997       N
ATOM   1218  CA  SER C 163      -1.386  27.019  -0.757  1.00 52.77           C
ANISOU 1218  CA  SER C 163     7270   5976   6805   -854    719  -1032       C
ATOM   1219  C   SER C 163      -0.736  28.216  -1.443  1.00 53.07           C
ANISOU 1219  C   SER C 163     7293   5979   6893   -831    765  -1041       C
ATOM   1220  O   SER C 163       0.205  28.810  -0.917  1.00 52.71           O
ANISOU 1220  O   SER C 163     7257   5934   6838   -856    799  -1093       O
ATOM   1221  CB  SER C 163      -0.985  26.966   0.719  1.00 52.52           C
ANISOU 1221  CB  SER C 163     7258   5970   6728   -909    742  -1093       C
ATOM   1222  OG  SER C 163       0.417  26.816   0.865  0.00 51.77           O
ANISOU 1222  OG  SER C 163     7187   5901   6584   -923    714  -1127       O
ATOM   1223  N   CYS C 164      -1.249  28.566  -2.619  1.00 60.72           N
ANISOU 1223  N   CYS C 164     8236   6919   7914   -786    768   -989       N
ATOM   1224  CA  CYS C 164      -0.647  29.614  -3.438  1.00 60.89           C
ANISOU 1224  CA  CYS C 164     8242   6908   7984   -758    805   -986       C
ATOM   1225  C   CYS C 164      -1.466  30.903  -3.456  1.00 61.51           C
ANISOU 1225  C   CYS C 164     8284   6938   8150   -747    896   -980       C
ATOM   1226  O   CYS C 164      -2.696  30.864  -3.454  1.00 62.28           O
ANISOU 1226  O   CYS C 164     8359   7024   8280   -738    911   -946       O
ATOM   1227  CB  CYS C 164      -0.434  29.110  -4.868  1.00 61.13           C
ANISOU 1227  CB  CYS C 164     8271   6947   8008   -711    740   -929       C
ATOM   1228  SG  CYS C 164       0.730  27.734  -5.002  1.00 61.69           S
ANISOU 1228  SG  CYS C 164     8384   7067   7987   -718    642   -938       S
ATOM   1229  N   PRO C 165      -0.774  32.054  -3.473  1.00 59.61           N
ANISOU 1229  N   PRO C 165     8034   6665   7949   -748    958  -1012       N
ATOM   1230  CA  PRO C 165      -1.410  33.373  -3.550  1.00 60.08           C
ANISOU 1230  CA  PRO C 165     8058   6670   8098   -735   1051  -1007       C
ATOM   1231  C   PRO C 165      -2.067  33.595  -4.908  1.00 61.28           C
ANISOU 1231  C   PRO C 165     8178   6801   8305   -678   1043   -929       C
ATOM   1232  O   PRO C 165      -1.573  33.081  -5.911  1.00 61.48           O
ANISOU 1232  O   PRO C 165     8210   6846   8303   -648    979   -893       O
ATOM   1233  CB  PRO C 165      -0.233  34.342  -3.382  1.00 59.32           C
ANISOU 1233  CB  PRO C 165     7967   6553   8019   -749   1102  -1061       C
ATOM   1234  CG  PRO C 165       0.861  33.531  -2.769  1.00 58.75           C
ANISOU 1234  CG  PRO C 165     7934   6528   7859   -785   1046  -1108       C
ATOM   1235  CD  PRO C 165       0.686  32.158  -3.325  1.00 58.80           C
ANISOU 1235  CD  PRO C 165     7956   6576   7808   -765    947  -1059       C
ATOM   1236  N   PRO C 166      -3.172  34.354  -4.939  1.00 66.22           N
ANISOU 1236  N   PRO C 166     8767   7389   9006   -662   1108   -902       N
ATOM   1237  CA  PRO C 166      -3.873  34.664  -6.189  1.00 67.19           C
ANISOU 1237  CA  PRO C 166     8852   7491   9185   -608   1108   -823       C
ATOM   1238  C   PRO C 166      -2.990  35.466  -7.138  1.00 67.85           C
ANISOU 1238  C   PRO C 166     8926   7551   9302   -577   1126   -810       C
ATOM   1239  O   PRO C 166      -2.123  36.215  -6.685  1.00 67.74           O
ANISOU 1239  O   PRO C 166     8922   7515   9302   -597   1177   -864       O
ATOM   1240  CB  PRO C 166      -5.055  35.523  -5.724  1.00 67.84           C
ANISOU 1240  CB  PRO C 166     8899   7532   9347   -608   1194   -814       C
ATOM   1241  CG  PRO C 166      -5.236  35.183  -4.283  1.00 67.85           C
ANISOU 1241  CG  PRO C 166     8922   7545   9311   -662   1211   -877       C
ATOM   1242  CD  PRO C 166      -3.858  34.922  -3.767  1.00 66.79           C
ANISOU 1242  CD  PRO C 166     8829   7436   9111   -696   1186   -942       C
ATOM   1243  N   CYS C 167      -3.207  35.305  -8.439  1.00 94.21           N
ANISOU 1243  N   CYS C 167    12246  10898  12653   -529   1086   -738       N
ATOM   1244  CA  CYS C 167      -2.442  36.040  -9.438  1.00 94.26           C
ANISOU 1244  CA  CYS C 167    12240  10883  12692   -495   1101   -716       C
ATOM   1245  C   CYS C 167      -2.871  37.506  -9.444  1.00 94.33           C
ANISOU 1245  C   CYS C 167    12208  10830  12802   -478   1207   -706       C
ATOM   1246  O   CYS C 167      -4.063  37.806  -9.359  1.00 95.32           O
ANISOU 1246  O   CYS C 167    12301  10936  12980   -467   1245   -671       O
ATOM   1247  CB  CYS C 167      -2.642  35.416 -10.821  1.00 95.36           C
ANISOU 1247  CB  CYS C 167    12368  11052  12811   -449   1027   -641       C
ATOM   1248  SG  CYS C 167      -1.409  35.893 -12.055  1.00106.74           S
ANISOU 1248  SG  CYS C 167    13810  12490  14258   -413   1016   -620       S
ATOM   1249  N   HIS C 168      -1.895  38.408  -9.535  1.00 58.66           N
ANISOU 1249  N   HIS C 168     7691   6281   8314   -478   1256   -736       N
ATOM   1250  CA  HIS C 168      -2.143  39.851  -9.491  1.00 58.30           C
ANISOU 1250  CA  HIS C 168     7610   6171   8369   -466   1363   -735       C
ATOM   1251  C   HIS C 168      -3.176  40.283 -10.531  1.00 59.94           C
ANISOU 1251  C   HIS C 168     7768   6359   8646   -411   1380   -642       C
ATOM   1252  O   HIS C 168      -3.247  39.716 -11.622  1.00 61.26           O
ANISOU 1252  O   HIS C 168     7929   6560   8786   -375   1311   -579       O
ATOM   1253  CB  HIS C 168      -0.836  40.626  -9.693  1.00 57.75           C
ANISOU 1253  CB  HIS C 168     7549   6077   8316   -468   1397   -771       C
ATOM   1254  CG  HIS C 168      -0.869  42.026  -9.154  1.00 58.11           C
ANISOU 1254  CG  HIS C 168     7572   6056   8451   -479   1514   -806       C
ATOM   1255  ND1 HIS C 168      -1.430  43.077  -9.849  1.00 58.52           N
ANISOU 1255  ND1 HIS C 168     7578   6055   8600   -436   1583   -749       N
ATOM   1256  CD2 HIS C 168      -0.403  42.544  -7.996  1.00 57.37           C
ANISOU 1256  CD2 HIS C 168     7496   5939   8365   -529   1576   -892       C
ATOM   1257  CE1 HIS C 168      -1.310  44.183  -9.135  1.00 57.67           C
ANISOU 1257  CE1 HIS C 168     7461   5891   8560   -459   1685   -800       C
ATOM   1258  NE2 HIS C 168      -0.692  43.890  -8.008  1.00 57.00           N
ANISOU 1258  NE2 HIS C 168     7414   5823   8421   -516   1682   -890       N
ATOM   1259  N   GLU C 169      -3.973  41.288 -10.182  1.00 62.29           N
ANISOU 1259  N   GLU C 169     8031   6604   9032   -406   1474   -634       N
ATOM   1260  CA  GLU C 169      -5.085  41.726 -11.023  1.00 63.18           C
ANISOU 1260  CA  GLU C 169     8092   6698   9216   -356   1497   -544       C
ATOM   1261  C   GLU C 169      -4.645  42.273 -12.383  1.00 63.35           C
ANISOU 1261  C   GLU C 169     8088   6710   9272   -304   1495   -479       C
ATOM   1262  O   GLU C 169      -5.409  42.240 -13.347  1.00 63.95           O
ANISOU 1262  O   GLU C 169     8128   6798   9374   -260   1475   -393       O
ATOM   1263  CB  GLU C 169      -5.940  42.756 -10.281  1.00 62.98           C
ANISOU 1263  CB  GLU C 169     8033   6612   9283   -362   1607   -555       C
ATOM   1264  CG  GLU C 169      -5.175  43.980  -9.807  0.00 62.33           C
ANISOU 1264  CG  GLU C 169     7952   6469   9262   -379   1705   -614       C
ATOM   1265  CD  GLU C 169      -5.583  45.239 -10.542  0.00 62.80           C
ANISOU 1265  CD  GLU C 169     7958   6468   9435   -331   1789   -552       C
ATOM   1266  OE1 GLU C 169      -5.205  45.389 -11.723  0.00 63.08           O
ANISOU 1266  OE1 GLU C 169     7979   6511   9480   -288   1762   -491       O
ATOM   1267  OE2 GLU C 169      -6.287  46.077  -9.941  0.00 62.87           O
ANISOU 1267  OE2 GLU C 169     7940   6422   9524   -336   1884   -562       O
ATOM   1268  N   VAL C 170      -3.416  42.773 -12.456  1.00 67.79           N
ANISOU 1268  N   VAL C 170     8668   7254   9834   -311   1516   -520       N
ATOM   1269  CA  VAL C 170      -2.881  43.296 -13.709  1.00 68.22           C
ANISOU 1269  CA  VAL C 170     8703   7300   9919   -265   1516   -463       C
ATOM   1270  C   VAL C 170      -2.616  42.160 -14.697  1.00 68.73           C
ANISOU 1270  C   VAL C 170     8784   7433   9899   -244   1402   -419       C
ATOM   1271  O   VAL C 170      -2.781  42.320 -15.907  1.00 69.77           O
ANISOU 1271  O   VAL C 170     8886   7574  10050   -196   1383   -341       O
ATOM   1272  CB  VAL C 170      -1.579  44.094 -13.477  1.00 67.11           C
ANISOU 1272  CB  VAL C 170     8580   7123   9798   -282   1568   -524       C
ATOM   1273  CG1 VAL C 170      -1.070  44.689 -14.782  1.00 67.60           C
ANISOU 1273  CG1 VAL C 170     8617   7173   9896   -233   1573   -461       C
ATOM   1274  CG2 VAL C 170      -1.807  45.190 -12.451  1.00 66.76           C
ANISOU 1274  CG2 VAL C 170     8521   7011   9833   -309   1682   -577       C
ATOM   1275  N   CYS C 171      -2.223  41.007 -14.165  1.00 63.59           N
ANISOU 1275  N   CYS C 171     8179   6829   9155   -280   1327   -470       N
ATOM   1276  CA  CYS C 171      -1.841  39.861 -14.986  1.00 63.74           C
ANISOU 1276  CA  CYS C 171     8220   6909   9088   -267   1220   -442       C
ATOM   1277  C   CYS C 171      -3.027  39.192 -15.679  1.00 64.64           C
ANISOU 1277  C   CYS C 171     8309   7059   9191   -239   1166   -366       C
ATOM   1278  O   CYS C 171      -2.843  38.384 -16.591  1.00 65.16           O
ANISOU 1278  O   CYS C 171     8384   7174   9200   -220   1085   -329       O
ATOM   1279  CB  CYS C 171      -1.090  38.835 -14.136  1.00 62.70           C
ANISOU 1279  CB  CYS C 171     8144   6814   8867   -315   1162   -519       C
ATOM   1280  SG  CYS C 171       0.348  39.500 -13.268  1.00 62.38           S
ANISOU 1280  SG  CYS C 171     8133   6743   8827   -355   1215   -613       S
ATOM   1281  N   LYS C 172      -4.235  39.531 -15.238  1.00 62.27           N
ANISOU 1281  N   LYS C 172     7977   6737   8945   -239   1213   -344       N
ATOM   1282  CA  LYS C 172      -5.468  38.981 -15.803  1.00 63.26           C
ANISOU 1282  CA  LYS C 172     8074   6895   9069   -215   1170   -272       C
ATOM   1283  C   LYS C 172      -5.535  37.454 -15.742  1.00 63.43           C
ANISOU 1283  C   LYS C 172     8131   6978   8992   -237   1066   -285       C
ATOM   1284  O   LYS C 172      -6.040  36.808 -16.661  1.00 64.21           O
ANISOU 1284  O   LYS C 172     8216   7120   9062   -213   1001   -225       O
ATOM   1285  CB  LYS C 172      -5.684  39.471 -17.240  1.00 63.99           C
ANISOU 1285  CB  LYS C 172     8123   6993   9200   -158   1167   -180       C
ATOM   1286  CG  LYS C 172      -5.933  40.967 -17.353  1.00 64.28           C
ANISOU 1286  CG  LYS C 172     8112   6965   9346   -130   1273   -148       C
ATOM   1287  CD  LYS C 172      -6.205  41.376 -18.791  0.00 65.12           C
ANISOU 1287  CD  LYS C 172     8174   7085   9485    -73   1265    -49       C
ATOM   1288  CE  LYS C 172      -6.503  42.863 -18.894  0.00 65.17           C
ANISOU 1288  CE  LYS C 172     8130   7024   9607    -43   1374    -11       C
ATOM   1289  NZ  LYS C 172      -6.765  43.280 -20.299  0.00 65.91           N
ANISOU 1289  NZ  LYS C 172     8177   7134   9733     14   1366     92       N
ATOM   1290  N   GLY C 173      -5.020  36.884 -14.657  1.00 53.06           N
ANISOU 1290  N   GLY C 173     6862   5671   7627   -285   1051   -364       N
ATOM   1291  CA  GLY C 173      -5.144  35.459 -14.413  1.00 52.45           C
ANISOU 1291  CA  GLY C 173     6819   5646   7464   -309    963   -381       C
ATOM   1292  C   GLY C 173      -3.993  34.606 -14.910  1.00 51.85           C
ANISOU 1292  C   GLY C 173     6784   5609   7307   -312    884   -401       C
ATOM   1293  O   GLY C 173      -4.015  33.386 -14.755  1.00 51.62           O
ANISOU 1293  O   GLY C 173     6785   5621   7207   -332    810   -415       O
ATOM   1294  N   ARG C 174      -2.990  35.236 -15.516  1.00 44.86           N
ANISOU 1294  N   ARG C 174     5901   4710   6435   -292    902   -401       N
ATOM   1295  CA  ARG C 174      -1.826  34.506 -16.016  1.00 44.05           C
ANISOU 1295  CA  ARG C 174     5836   4642   6261   -293    833   -420       C
ATOM   1296  C   ARG C 174      -0.525  35.198 -15.618  1.00 42.64           C
ANISOU 1296  C   ARG C 174     5676   4434   6090   -307    877   -477       C
ATOM   1297  O   ARG C 174      -0.276  36.339 -16.006  1.00 43.29           O
ANISOU 1297  O   ARG C 174     5732   4479   6236   -284    940   -460       O
ATOM   1298  CB  ARG C 174      -1.900  34.338 -17.537  1.00 45.12           C
ANISOU 1298  CB  ARG C 174     5951   4806   6388   -247    786   -347       C
ATOM   1299  CG  ARG C 174      -3.180  33.673 -18.024  1.00 46.34           C
ANISOU 1299  CG  ARG C 174     6082   4992   6532   -234    741   -289       C
ATOM   1300  CD  ARG C 174      -3.057  33.191 -19.459  1.00 47.68           C
ANISOU 1300  CD  ARG C 174     6245   5205   6666   -199    675   -232       C
ATOM   1301  NE  ARG C 174      -4.312  32.628 -19.949  1.00 48.90           N
ANISOU 1301  NE  ARG C 174     6372   5392   6814   -188    634   -175       N
ATOM   1302  CZ  ARG C 174      -4.701  31.373 -19.744  1.00 48.91           C
ANISOU 1302  CZ  ARG C 174     6397   5430   6755   -212    565   -188       C
ATOM   1303  NH1 ARG C 174      -3.934  30.542 -19.052  1.00 47.75           N
ANISOU 1303  NH1 ARG C 174     6301   5292   6549   -245    529   -253       N
ATOM   1304  NH2 ARG C 174      -5.860  30.949 -20.230  1.00 49.95           N
ANISOU 1304  NH2 ARG C 174     6500   5591   6886   -202    532   -135       N
ATOM   1305  N   CYS C 175       0.305  34.501 -14.848  1.00 37.71           N
ANISOU 1305  N   CYS C 175     5096   3828   5403   -344    843   -543       N
ATOM   1306  CA  CYS C 175       1.515  35.103 -14.301  1.00 37.21           C
ANISOU 1306  CA  CYS C 175     5053   3742   5344   -366    884   -604       C
ATOM   1307  C   CYS C 175       2.598  34.079 -13.971  1.00 36.20           C
ANISOU 1307  C   CYS C 175     4972   3652   5130   -392    817   -653       C
ATOM   1308  O   CYS C 175       2.314  32.896 -13.780  1.00 35.79           O
ANISOU 1308  O   CYS C 175     4943   3639   5019   -406    749   -654       O
ATOM   1309  CB  CYS C 175       1.171  35.900 -13.044  1.00 37.13           C
ANISOU 1309  CB  CYS C 175     5034   3691   5382   -400    967   -653       C
ATOM   1310  SG  CYS C 175       0.351  34.920 -11.766  1.00 36.81           S
ANISOU 1310  SG  CYS C 175     5015   3676   5296   -445    940   -688       S
ATOM   1311  N   TRP C 176       3.839  34.552 -13.902  1.00 43.18           N
ANISOU 1311  N   TRP C 176     5871   4525   6012   -400    837   -692       N
ATOM   1312  CA  TRP C 176       4.971  33.720 -13.511  1.00 42.56           C
ANISOU 1312  CA  TRP C 176     5834   4479   5858   -426    783   -741       C
ATOM   1313  C   TRP C 176       5.277  33.919 -12.031  1.00 42.42           C
ANISOU 1313  C   TRP C 176     5832   4452   5832   -479    822   -816       C
ATOM   1314  O   TRP C 176       5.946  33.097 -11.406  1.00 42.02           O
ANISOU 1314  O   TRP C 176     5816   4435   5717   -509    776   -857       O
ATOM   1315  CB  TRP C 176       6.205  34.061 -14.349  1.00 42.77           C
ANISOU 1315  CB  TRP C 176     5864   4504   5881   -403    777   -738       C
ATOM   1316  CG  TRP C 176       6.009  33.842 -15.816  1.00 44.19           C
ANISOU 1316  CG  TRP C 176     6030   4698   6061   -354    737   -667       C
ATOM   1317  CD1 TRP C 176       5.612  34.766 -16.737  1.00 45.13           C
ANISOU 1317  CD1 TRP C 176     6111   4792   6243   -314    779   -613       C
ATOM   1318  CD2 TRP C 176       6.197  32.616 -16.532  1.00 43.95           C
ANISOU 1318  CD2 TRP C 176     6021   4714   5963   -339    648   -644       C
ATOM   1319  NE1 TRP C 176       5.542  34.193 -17.983  1.00 45.73           N
ANISOU 1319  NE1 TRP C 176     6185   4900   6291   -277    720   -557       N
ATOM   1320  CE2 TRP C 176       5.896  32.873 -17.885  1.00 45.23           C
ANISOU 1320  CE2 TRP C 176     6159   4879   6148   -292    640   -577       C
ATOM   1321  CE3 TRP C 176       6.593  31.327 -16.163  1.00 43.11           C
ANISOU 1321  CE3 TRP C 176     5954   4647   5781   -362    577   -672       C
ATOM   1322  CZ2 TRP C 176       5.976  31.889 -18.868  1.00 45.71           C
ANISOU 1322  CZ2 TRP C 176     6232   4981   6155   -270    563   -543       C
ATOM   1323  CZ3 TRP C 176       6.669  30.351 -17.140  1.00 43.87           C
ANISOU 1323  CZ3 TRP C 176     6062   4778   5828   -338    503   -637       C
ATOM   1324  CH2 TRP C 176       6.364  30.637 -18.477  1.00 44.91           C
ANISOU 1324  CH2 TRP C 176     6170   4913   5982   -294    496   -576       C
ATOM   1325  N   GLY C 177       4.781  35.023 -11.482  1.00 56.19           N
ANISOU 1325  N   GLY C 177     7553   6154   7645   -489    907   -831       N
ATOM   1326  CA  GLY C 177       4.951  35.333 -10.075  1.00 55.84           C
ANISOU 1326  CA  GLY C 177     7520   6099   7599   -541    954   -903       C
ATOM   1327  C   GLY C 177       3.752  36.095  -9.543  1.00 56.41           C
ANISOU 1327  C   GLY C 177     7563   6133   7738   -547   1029   -900       C
ATOM   1328  O   GLY C 177       2.815  36.374 -10.290  1.00 57.51           O
ANISOU 1328  O   GLY C 177     7672   6254   7926   -509   1042   -838       O
ATOM   1329  N   PRO C 178       3.772  36.437  -8.247  1.00 54.82           N
ANISOU 1329  N   PRO C 178     7370   5920   7538   -595   1079   -965       N
ATOM   1330  CA  PRO C 178       2.656  37.148  -7.617  1.00 55.33           C
ANISOU 1330  CA  PRO C 178     7410   5948   7666   -606   1155   -970       C
ATOM   1331  C   PRO C 178       2.697  38.653  -7.873  1.00 55.99           C
ANISOU 1331  C   PRO C 178     7461   5969   7844   -590   1252   -971       C
ATOM   1332  O   PRO C 178       1.751  39.358  -7.523  1.00 56.39           O
ANISOU 1332  O   PRO C 178     7486   5981   7960   -591   1323   -966       O
ATOM   1333  CB  PRO C 178       2.872  36.867  -6.131  1.00 54.40           C
ANISOU 1333  CB  PRO C 178     7318   5850   7502   -667   1165  -1048       C
ATOM   1334  CG  PRO C 178       4.350  36.756  -6.002  1.00 53.61           C
ANISOU 1334  CG  PRO C 178     7245   5771   7353   -688   1140  -1095       C
ATOM   1335  CD  PRO C 178       4.835  36.112  -7.278  1.00 53.88           C
ANISOU 1335  CD  PRO C 178     7284   5828   7358   -644   1063  -1039       C
ATOM   1336  N   GLY C 179       3.778  39.133  -8.481  1.00 70.90           N
ANISOU 1336  N   GLY C 179     9351   7847   9741   -577   1258   -976       N
ATOM   1337  CA  GLY C 179       3.959  40.557  -8.704  1.00 71.07           C
ANISOU 1337  CA  GLY C 179     9344   7808   9852   -565   1352   -981       C
ATOM   1338  C   GLY C 179       3.145  41.120  -9.853  1.00 72.03           C
ANISOU 1338  C   GLY C 179     9424   7895  10047   -506   1377   -896       C
ATOM   1339  O   GLY C 179       2.482  40.383 -10.583  1.00 72.80           O
ANISOU 1339  O   GLY C 179     9515   8022  10124   -473   1316   -830       O
ATOM   1340  N   SER C 180       3.200  42.440 -10.011  1.00 49.78           N
ANISOU 1340  N   SER C 180     6578   5018   7319   -494   1469   -896       N
ATOM   1341  CA  SER C 180       2.477  43.122 -11.078  1.00 50.00           C
ANISOU 1341  CA  SER C 180     6561   5010   7426   -438   1504   -813       C
ATOM   1342  C   SER C 180       3.307  43.198 -12.357  1.00 49.78           C
ANISOU 1342  C   SER C 180     6529   4991   7394   -397   1470   -766       C
ATOM   1343  O   SER C 180       2.788  43.518 -13.426  1.00 50.27           O
ANISOU 1343  O   SER C 180     6557   5040   7501   -345   1475   -685       O
ATOM   1344  CB  SER C 180       2.066  44.527 -10.633  1.00 49.75           C
ANISOU 1344  CB  SER C 180     6498   4905   7501   -443   1627   -830       C
ATOM   1345  OG  SER C 180       3.200  45.307 -10.293  1.00 49.06           O
ANISOU 1345  OG  SER C 180     6421   4787   7433   -469   1679   -894       O
ATOM   1346  N   GLU C 181       4.598  42.908 -12.240  1.00 64.80           N
ANISOU 1346  N   GLU C 181     8463   6916   9240   -419   1435   -815       N
ATOM   1347  CA  GLU C 181       5.486  42.893 -13.396  1.00 65.24           C
ANISOU 1347  CA  GLU C 181     8520   6985   9283   -384   1398   -778       C
ATOM   1348  C   GLU C 181       5.857  41.460 -13.760  1.00 65.70           C
ANISOU 1348  C   GLU C 181     8611   7112   9238   -382   1283   -767       C
ATOM   1349  O   GLU C 181       6.696  41.225 -14.629  1.00 66.52           O
ANISOU 1349  O   GLU C 181     8724   7238   9314   -359   1239   -745       O
ATOM   1350  CB  GLU C 181       6.747  43.713 -13.116  1.00 64.52           C
ANISOU 1350  CB  GLU C 181     8437   6863   9214   -407   1450   -837       C
ATOM   1351  CG  GLU C 181       6.496  45.207 -12.990  1.00 64.89           C
ANISOU 1351  CG  GLU C 181     8448   6835   9372   -403   1567   -841       C
ATOM   1352  CD  GLU C 181       7.771  46.001 -12.784  1.00 64.14           C
ANISOU 1352  CD  GLU C 181     8360   6710   9298   -426   1615   -899       C
ATOM   1353  OE1 GLU C 181       8.312  45.978 -11.658  0.00 63.42           O
ANISOU 1353  OE1 GLU C 181     8294   6624   9178   -483   1630   -986       O
ATOM   1354  OE2 GLU C 181       8.234  46.646 -13.748  0.00 64.37           O
ANISOU 1354  OE2 GLU C 181     8370   6715   9374   -389   1638   -857       O
ATOM   1355  N   ASP C 182       5.217  40.507 -13.091  1.00 47.83           N
ANISOU 1355  N   ASP C 182     6367   4884   6924   -406   1237   -781       N
ATOM   1356  CA  ASP C 182       5.529  39.095 -13.266  1.00 47.61           C
ANISOU 1356  CA  ASP C 182     6372   4919   6799   -410   1132   -778       C
ATOM   1357  C   ASP C 182       4.497  38.425 -14.155  1.00 47.90           C
ANISOU 1357  C   ASP C 182     6394   4982   6826   -371   1079   -700       C
ATOM   1358  O   ASP C 182       4.426  37.199 -14.236  1.00 47.31           O
ANISOU 1358  O   ASP C 182     6343   4955   6677   -375    996   -694       O
ATOM   1359  CB  ASP C 182       5.572  38.400 -11.907  1.00 47.09           C
ANISOU 1359  CB  ASP C 182     6339   4878   6676   -465   1113   -848       C
ATOM   1360  CG  ASP C 182       6.643  38.965 -11.004  1.00 46.47           C
ANISOU 1360  CG  ASP C 182     6276   4784   6596   -509   1157   -928       C
ATOM   1361  OD1 ASP C 182       7.649  39.492 -11.530  1.00 46.28           O
ANISOU 1361  OD1 ASP C 182     6251   4748   6587   -497   1171   -934       O
ATOM   1362  OD2 ASP C 182       6.486  38.887  -9.768  1.00 46.25           O
ANISOU 1362  OD2 ASP C 182     6262   4760   6552   -556   1179   -987       O
ATOM   1363  N   CYS C 183       3.693  39.250 -14.812  1.00 48.95           N
ANISOU 1363  N   CYS C 183     6485   5081   7034   -333   1128   -640       N
ATOM   1364  CA  CYS C 183       2.615  38.767 -15.655  1.00 50.39           C
ANISOU 1364  CA  CYS C 183     6645   5287   7216   -297   1087   -562       C
ATOM   1365  C   CYS C 183       3.149  38.085 -16.908  1.00 50.86           C
ANISOU 1365  C   CYS C 183     6714   5389   7224   -263   1008   -517       C
ATOM   1366  O   CYS C 183       4.269  38.351 -17.347  1.00 49.84           O
ANISOU 1366  O   CYS C 183     6594   5256   7085   -255   1008   -529       O
ATOM   1367  CB  CYS C 183       1.696  39.927 -16.033  1.00 51.37           C
ANISOU 1367  CB  CYS C 183     6716   5362   7438   -264   1166   -507       C
ATOM   1368  SG  CYS C 183       1.074  40.848 -14.604  1.00 52.11           S
ANISOU 1368  SG  CYS C 183     6798   5399   7604   -301   1271   -562       S
ATOM   1369  N   GLN C 184       2.340  37.193 -17.468  1.00 50.10           N
ANISOU 1369  N   GLN C 184     6613   5333   7092   -246    943   -468       N
ATOM   1370  CA  GLN C 184       2.672  36.543 -18.726  1.00 50.19           C
ANISOU 1370  CA  GLN C 184     6629   5386   7056   -213    870   -420       C
ATOM   1371  C   GLN C 184       2.079  37.334 -19.884  1.00 50.84           C
ANISOU 1371  C   GLN C 184     6663   5457   7198   -163    900   -337       C
ATOM   1372  O   GLN C 184       0.900  37.689 -19.865  1.00 51.19           O
ANISOU 1372  O   GLN C 184     6671   5487   7291   -151    931   -295       O
ATOM   1373  CB  GLN C 184       2.133  35.114 -18.755  1.00 50.52           C
ANISOU 1373  CB  GLN C 184     6692   5480   7023   -224    782   -413       C
ATOM   1374  CG  GLN C 184       2.442  34.379 -20.048  1.00 51.50           C
ANISOU 1374  CG  GLN C 184     6823   5649   7095   -193    706   -369       C
ATOM   1375  CD  GLN C 184       1.470  33.251 -20.332  1.00 52.34           C
ANISOU 1375  CD  GLN C 184     6930   5799   7156   -193    636   -337       C
ATOM   1376  OE1 GLN C 184       0.600  32.943 -19.518  1.00 52.82           O
ANISOU 1376  OE1 GLN C 184     6991   5858   7222   -217    639   -350       O
ATOM   1377  NE2 GLN C 184       1.611  32.632 -21.498  1.00 52.44           N
ANISOU 1377  NE2 GLN C 184     6947   5853   7126   -167    573   -297       N
ATOM   1378  N   THR C 185       2.902  37.610 -20.889  1.00 45.98           N
ANISOU 1378  N   THR C 185     6045   4848   6579   -133    891   -310       N
ATOM   1379  CA  THR C 185       2.447  38.326 -22.074  1.00 47.42           C
ANISOU 1379  CA  THR C 185     6182   5025   6811    -83    914   -226       C
ATOM   1380  C   THR C 185       2.188  37.359 -23.225  1.00 48.34           C
ANISOU 1380  C   THR C 185     6299   5203   6864    -57    826   -171       C
ATOM   1381  O   THR C 185       3.118  36.764 -23.770  1.00 48.12           O
ANISOU 1381  O   THR C 185     6300   5207   6776    -54    773   -184       O
ATOM   1382  CB  THR C 185       3.466  39.392 -22.515  1.00 47.43           C
ANISOU 1382  CB  THR C 185     6173   4991   6857    -63    970   -224       C
ATOM   1383  OG1 THR C 185       4.734  38.771 -22.758  1.00 47.68           O
ANISOU 1383  OG1 THR C 185     6244   5051   6820    -72    917   -262       O
ATOM   1384  CG2 THR C 185       3.626  40.453 -21.437  1.00 46.47           C
ANISOU 1384  CG2 THR C 185     6045   4805   6808    -88   1065   -275       C
ATOM   1385  N   LEU C 186       0.918  37.203 -23.583  1.00 66.18           N
ANISOU 1385  N   LEU C 186     8526   7481   9138    -41    813   -112       N
ATOM   1386  CA  LEU C 186       0.518  36.307 -24.664  1.00 67.76           C
ANISOU 1386  CA  LEU C 186     8722   7742   9280    -20    732    -60       C
ATOM   1387  C   LEU C 186       0.947  36.866 -26.017  1.00 69.24           C
ANISOU 1387  C   LEU C 186     8885   7943   9480     26    735      3       C
ATOM   1388  O   LEU C 186       0.793  38.060 -26.275  1.00 69.85           O
ANISOU 1388  O   LEU C 186     8921   7983   9634     53    806     45       O
ATOM   1389  CB  LEU C 186      -0.997  36.091 -24.633  1.00 67.95           C
ANISOU 1389  CB  LEU C 186     8713   7782   9324    -17    723    -12       C
ATOM   1390  CG  LEU C 186      -1.556  35.438 -23.366  1.00 66.84           C
ANISOU 1390  CG  LEU C 186     8595   7635   9166    -60    714    -66       C
ATOM   1391  CD1 LEU C 186      -3.042  35.727 -23.216  1.00 67.16           C
ANISOU 1391  CD1 LEU C 186     8590   7669   9259    -53    741    -16       C
ATOM   1392  CD2 LEU C 186      -1.304  33.939 -23.382  1.00 66.64           C
ANISOU 1392  CD2 LEU C 186     8614   7661   9045    -85    619   -100       C
ATOM   1393  N   THR C 187       1.479  36.003 -26.879  1.00 76.57           N
ANISOU 1393  N   THR C 187     9836   8923  10333     34    660     10       N
ATOM   1394  CA  THR C 187       2.009  36.454 -28.164  1.00 77.46           C
ANISOU 1394  CA  THR C 187     9930   9053  10447     75    659     64       C
ATOM   1395  C   THR C 187       1.391  35.755 -29.378  1.00 78.95           C
ANISOU 1395  C   THR C 187    10103   9309  10586     98    589    128       C
ATOM   1396  O   THR C 187       1.433  36.286 -30.488  1.00 79.85           O
ANISOU 1396  O   THR C 187    10185   9440  10713    137    597    194       O
ATOM   1397  CB  THR C 187       3.543  36.309 -28.223  1.00 76.93           C
ANISOU 1397  CB  THR C 187     9904   8982  10342     67    647     11       C
ATOM   1398  OG1 THR C 187       4.087  36.419 -26.902  1.00 75.64           O
ANISOU 1398  OG1 THR C 187     9771   8776  10192     29    682    -69       O
ATOM   1399  CG2 THR C 187       4.143  37.390 -29.110  1.00 77.26           C
ANISOU 1399  CG2 THR C 187     9919   9008  10429    107    695     58       C
ATOM   1400  N   LYS C 188       0.827  34.567 -29.170  1.00 68.75           N
ANISOU 1400  N   LYS C 188     8832   8056   9235     73    521    110       N
ATOM   1401  CA  LYS C 188       0.163  33.855 -30.256  1.00 69.95           C
ANISOU 1401  CA  LYS C 188     8968   8272   9337     89    454    165       C
ATOM   1402  C   LYS C 188      -0.976  34.690 -30.814  1.00 71.08           C
ANISOU 1402  C   LYS C 188     9046   8420   9541    121    490    253       C
ATOM   1403  O   LYS C 188      -1.865  35.116 -30.078  1.00 71.28           O
ANISOU 1403  O   LYS C 188     9047   8415   9624    114    532    262       O
ATOM   1404  CB  LYS C 188      -0.353  32.492 -29.798  0.00 70.05           C
ANISOU 1404  CB  LYS C 188     9011   8317   9287     53    384    127       C
ATOM   1405  CG  LYS C 188       0.699  31.409 -29.855  0.00 69.68           C
ANISOU 1405  CG  LYS C 188     9021   8293   9160     33    323     67       C
ATOM   1406  CD  LYS C 188       0.089  30.055 -30.146  0.00 70.37           C
ANISOU 1406  CD  LYS C 188     9126   8434   9178     15    240     64       C
ATOM   1407  CE  LYS C 188       1.154  29.098 -30.643  0.00 70.23           C
ANISOU 1407  CE  LYS C 188     9155   8446   9083      9    181     25       C
ATOM   1408  NZ  LYS C 188       2.333  29.105 -29.738  0.00 68.69           N
ANISOU 1408  NZ  LYS C 188     9002   8210   8887    -10    202    -46       N
ATOM   1409  N   THR C 189      -0.928  34.943 -32.116  1.00 78.10           N
ANISOU 1409  N   THR C 189     9907   9347  10418    158    474    321       N
ATOM   1410  CA  THR C 189      -1.946  35.751 -32.769  1.00 78.56           C
ANISOU 1410  CA  THR C 189     9901   9417  10532    193    506    414       C
ATOM   1411  C   THR C 189      -2.595  35.018 -33.929  1.00 79.10           C
ANISOU 1411  C   THR C 189     9950   9567  10539    205    431    471       C
ATOM   1412  O   THR C 189      -2.155  33.941 -34.335  1.00 79.26           O
ANISOU 1412  O   THR C 189    10008   9632  10475    189    358    438       O
ATOM   1413  CB  THR C 189      -1.377  37.088 -33.275  1.00 78.36           C
ANISOU 1413  CB  THR C 189     9844   9358  10572    233    577    460       C
ATOM   1414  OG1 THR C 189      -0.278  36.841 -34.160  0.00 78.35           O
ANISOU 1414  OG1 THR C 189     9868   9387  10515    246    543    455       O
ATOM   1415  CG2 THR C 189      -0.903  37.936 -32.110  0.00 77.50           C
ANISOU 1415  CG2 THR C 189     9745   9166  10535    220    660    407       C
ATOM   1416  N   ILE C 190      -3.656  35.617 -34.453  1.00 97.19           N
ANISOU 1416  N   ILE C 190    12178  11875  12874    233    451    558       N
ATOM   1417  CA  ILE C 190      -4.374  35.042 -35.573  1.00 97.92           C
ANISOU 1417  CA  ILE C 190    12244  12048  12914    245    385    620       C
ATOM   1418  C   ILE C 190      -3.900  35.687 -36.866  1.00 97.88           C
ANISOU 1418  C   ILE C 190    12210  12075  12906    288    393    689       C
ATOM   1419  O   ILE C 190      -4.044  36.892 -37.069  0.00 97.62           O
ANISOU 1419  O   ILE C 190    12130  12012  12949    323    461    751       O
ATOM   1420  CB  ILE C 190      -5.901  35.184 -35.404  1.00 98.33           C
ANISOU 1420  CB  ILE C 190    12242  12112  13007    247    392    678       C
ATOM   1421  CG1 ILE C 190      -6.302  36.641 -35.153  0.00 98.21           C
ANISOU 1421  CG1 ILE C 190    12173  12041  13102    280    488    735       C
ATOM   1422  CG2 ILE C 190      -6.375  34.323 -34.250  0.00 98.36           C
ANISOU 1422  CG2 ILE C 190    12278  12099  12995    201    369    609       C
ATOM   1423  CD1 ILE C 190      -7.796  36.865 -35.101  0.00 98.43           C
ANISOU 1423  CD1 ILE C 190    12141  12084  13175    288    498    803       C
ATOM   1424  N   CYS C 191      -3.294  34.886 -37.729  1.00123.15           N
ANISOU 1424  N   CYS C 191    15439  15333  16020    285    326    677       N
ATOM   1425  CA  CYS C 191      -2.829  35.405 -39.002  1.00123.49           C
ANISOU 1425  CA  CYS C 191    15457  15414  16050    324    327    741       C
ATOM   1426  C   CYS C 191      -3.536  34.746 -40.179  1.00124.27           C
ANISOU 1426  C   CYS C 191    15529  15607  16079    329    255    798       C
ATOM   1427  O   CYS C 191      -4.188  33.712 -40.039  1.00125.20           O
ANISOU 1427  O   CYS C 191    15661  15763  16146    298    193    773       O
ATOM   1428  CB  CYS C 191      -1.311  35.272 -39.132  1.00123.14           C
ANISOU 1428  CB  CYS C 191    15465  15353  15969    322    325    683       C
ATOM   1429  SG  CYS C 191      -0.670  33.596 -38.932  1.00123.81           S
ANISOU 1429  SG  CYS C 191    15627  15470  15946    276    237    583       S
ATOM   1430  N   ALA C 192      -3.396  35.374 -41.338  1.00 83.68           N
ANISOU 1430  N   ALA C 192    10350  10505  10938    369    263    876       N
ATOM   1431  CA  ALA C 192      -4.005  34.931 -42.580  1.00 83.75           C
ANISOU 1431  CA  ALA C 192    10327  10610  10882    379    201    941       C
ATOM   1432  C   ALA C 192      -3.337  33.636 -43.080  1.00 84.15           C
ANISOU 1432  C   ALA C 192    10435  10715  10823    351    120    877       C
ATOM   1433  O   ALA C 192      -2.309  33.230 -42.540  1.00 84.09           O
ANISOU 1433  O   ALA C 192    10487  10667  10795    332    119    793       O
ATOM   1434  CB  ALA C 192      -3.875  36.054 -43.596  1.00 83.12           C
ANISOU 1434  CB  ALA C 192    10194  10550  10838    430    243   1039       C
ATOM   1435  N   PRO C 193      -3.922  32.975 -44.099  1.00 84.33           N
ANISOU 1435  N   PRO C 193    10439  10829  10773    347     52    916       N
ATOM   1436  CA  PRO C 193      -3.352  31.726 -44.632  1.00 84.28           C
ANISOU 1436  CA  PRO C 193    10485  10876  10663    320    -24    856       C
ATOM   1437  C   PRO C 193      -1.997  31.879 -45.317  1.00 83.90           C
ANISOU 1437  C   PRO C 193    10466  10831  10579    339    -18    841       C
ATOM   1438  O   PRO C 193      -1.250  30.903 -45.389  1.00 83.57           O
ANISOU 1438  O   PRO C 193    10482  10802  10469    314    -63    767       O
ATOM   1439  CB  PRO C 193      -4.361  31.290 -45.701  1.00 84.11           C
ANISOU 1439  CB  PRO C 193    10421  10955  10584    318    -84    920       C
ATOM   1440  CG  PRO C 193      -5.549  32.107 -45.525  1.00 84.46           C
ANISOU 1440  CG  PRO C 193    10396  10996  10701    337    -49   1002       C
ATOM   1441  CD  PRO C 193      -5.228  33.295 -44.701  1.00 84.37           C
ANISOU 1441  CD  PRO C 193    10373  10891  10792    363     42   1012       C
ATOM   1442  N   GLN C 194      -1.709  33.064 -45.849  1.00 83.40           N
ANISOU 1442  N   GLN C 194    10363  10760  10563    383     37    912       N
ATOM   1443  CA  GLN C 194      -0.495  33.274 -46.634  1.00 82.84           C
ANISOU 1443  CA  GLN C 194    10313  10702  10460    405     43    911       C
ATOM   1444  C   GLN C 194       0.753  32.954 -45.820  1.00 82.69           C
ANISOU 1444  C   GLN C 194    10363  10616  10441    386     58    811       C
ATOM   1445  O   GLN C 194       1.735  32.431 -46.346  1.00 82.63           O
ANISOU 1445  O   GLN C 194    10396  10631  10370    383     29    772       O
ATOM   1446  CB  GLN C 194      -0.428  34.704 -47.179  1.00 82.38           C
ANISOU 1446  CB  GLN C 194    10199  10634  10469    456    110   1006       C
ATOM   1447  CG  GLN C 194      -1.511  35.046 -48.198  1.00 82.52           C
ANISOU 1447  CG  GLN C 194    10146  10731  10479    480     93   1116       C
ATOM   1448  CD  GLN C 194      -2.826  35.427 -47.551  0.00 82.65           C
ANISOU 1448  CD  GLN C 194    10113  10727  10563    479    116   1159       C
ATOM   1449  OE1 GLN C 194      -2.942  35.428 -46.333  0.00 82.51           O
ANISOU 1449  OE1 GLN C 194    10116  10636  10598    459    145   1104       O
ATOM   1450  NE2 GLN C 194      -3.821  35.756 -48.365  0.00 82.88           N
ANISOU 1450  NE2 GLN C 194    10075  10824  10591    500    103   1259       N
ATOM   1451  N   CYS C 195       0.701  33.263 -44.529  1.00 78.79           N
ANISOU 1451  N   CYS C 195     9880  10041  10015    373    103    770       N
ATOM   1452  CA  CYS C 195       1.779  32.906 -43.619  1.00 78.68           C
ANISOU 1452  CA  CYS C 195     9929   9965  10001    350    113    673       C
ATOM   1453  C   CYS C 195       1.556  31.484 -43.119  1.00 79.04           C
ANISOU 1453  C   CYS C 195    10021  10027   9983    304     46    597       C
ATOM   1454  O   CYS C 195       0.445  31.125 -42.724  1.00 79.64           O
ANISOU 1454  O   CYS C 195    10081  10114  10065    285     25    604       O
ATOM   1455  CB  CYS C 195       1.811  33.868 -42.433  1.00 78.46           C
ANISOU 1455  CB  CYS C 195     9891   9846  10073    353    192    661       C
ATOM   1456  SG  CYS C 195       1.118  35.501 -42.778  1.00 79.57           S
ANISOU 1456  SG  CYS C 195     9951   9969  10313    401    271    774       S
ATOM   1457  N   ASN C 196       2.608  30.674 -43.136  1.00 85.44           N
ANISOU 1457  N   ASN C 196    10890  10838  10736    287     14    525       N
ATOM   1458  CA  ASN C 196       2.500  29.283 -42.706  1.00 85.64           C
ANISOU 1458  CA  ASN C 196    10963  10877  10700    245    -49    452       C
ATOM   1459  C   ASN C 196       2.618  29.124 -41.193  1.00 85.54           C
ANISOU 1459  C   ASN C 196    10981  10790  10729    216    -25    383       C
ATOM   1460  O   ASN C 196       3.407  28.317 -40.705  1.00 85.48           O
ANISOU 1460  O   ASN C 196    11029  10764  10687    193    -49    307       O
ATOM   1461  CB  ASN C 196       3.548  28.417 -43.409  1.00 85.59           C
ANISOU 1461  CB  ASN C 196    11004  10904  10613    239    -95    406       C
ATOM   1462  CG  ASN C 196       3.484  28.535 -44.918  1.00 85.63           C
ANISOU 1462  CG  ASN C 196    10980  10986  10569    265   -119    470       C
ATOM   1463  OD1 ASN C 196       2.579  27.998 -45.558  1.00 85.84           O
ANISOU 1463  OD1 ASN C 196    10987  11079  10551    255   -168    499       O
ATOM   1464  ND2 ASN C 196       4.453  29.235 -45.497  1.00 85.40           N
ANISOU 1464  ND2 ASN C 196    10949  10952  10547    296    -85    491       N
ATOM   1465  N   GLY C 197       1.822  29.893 -40.458  1.00 89.41           N
ANISOU 1465  N   GLY C 197    11436  11242  11294    219     22    412       N
ATOM   1466  CA  GLY C 197       1.851  29.853 -39.009  1.00 89.47           C
ANISOU 1466  CA  GLY C 197    11467  11182  11344    193     50    353       C
ATOM   1467  C   GLY C 197       2.892  30.799 -38.442  1.00 88.97           C
ANISOU 1467  C   GLY C 197    11415  11053  11337    206    118    330       C
ATOM   1468  O   GLY C 197       3.155  30.800 -37.238  1.00 89.00           O
ANISOU 1468  O   GLY C 197    11443  11000  11371    183    144    273       O
ATOM   1469  N   HIS C 198       3.488  31.605 -39.315  1.00 66.30           N
ANISOU 1469  N   HIS C 198     8522   8189   8478    242    147    376       N
ATOM   1470  CA  HIS C 198       4.497  32.575 -38.905  1.00 65.46           C
ANISOU 1470  CA  HIS C 198     8422   8023   8428    257    214    360       C
ATOM   1471  C   HIS C 198       4.029  33.991 -39.210  1.00 64.81           C
ANISOU 1471  C   HIS C 198     8279   7921   8426    293    283    441       C
ATOM   1472  O   HIS C 198       4.253  34.506 -40.306  1.00 64.95           O
ANISOU 1472  O   HIS C 198     8269   7969   8439    328    291    503       O
ATOM   1473  CB  HIS C 198       5.820  32.314 -39.624  1.00 65.70           C
ANISOU 1473  CB  HIS C 198     8485   8072   8407    268    196    337       C
ATOM   1474  CG  HIS C 198       6.223  30.873 -39.646  1.00 66.46           C
ANISOU 1474  CG  HIS C 198     8634   8200   8417    239    123    273       C
ATOM   1475  ND1 HIS C 198       6.848  30.260 -38.580  1.00 66.23           N
ANISOU 1475  ND1 HIS C 198     8654   8132   8378    207    115    190       N
ATOM   1476  CD2 HIS C 198       6.094  29.928 -40.604  1.00 67.12           C
ANISOU 1476  CD2 HIS C 198     8730   8351   8423    237     56    280       C
ATOM   1477  CE1 HIS C 198       7.084  28.995 -38.884  1.00 66.48           C
ANISOU 1477  CE1 HIS C 198     8725   8202   8333    188     48    151       C
ATOM   1478  NE2 HIS C 198       6.638  28.768 -40.105  1.00 66.96           N
ANISOU 1478  NE2 HIS C 198     8765   8326   8351    205     12    201       N
ATOM   1479  N   CYS C 199       3.387  34.617 -38.230  1.00 64.43           N
ANISOU 1479  N   CYS C 199     8209   7820   8452    286    335    442       N
ATOM   1480  CA  CYS C 199       2.879  35.973 -38.387  1.00 63.87           C
ANISOU 1480  CA  CYS C 199     8080   7720   8468    319    408    516       C
ATOM   1481  C   CYS C 199       3.141  36.814 -37.141  1.00 63.21           C
ANISOU 1481  C   CYS C 199     8000   7550   8468    308    486    476       C
ATOM   1482  O   CYS C 199       3.323  36.276 -36.046  1.00 63.00           O
ANISOU 1482  O   CYS C 199     8012   7493   8431    271    478    398       O
ATOM   1483  CB  CYS C 199       1.381  35.944 -38.704  1.00 63.94           C
ANISOU 1483  CB  CYS C 199     8040   7768   8488    327    391    586       C
ATOM   1484  SG  CYS C 199       0.415  34.785 -37.696  1.00 66.24           S
ANISOU 1484  SG  CYS C 199     8354   8065   8748    279    340    530       S
ATOM   1485  N   PHE C 200       3.176  38.132 -37.326  1.00 52.83           N
ANISOU 1485  N   PHE C 200     6643   6197   7235    341    562    529       N
ATOM   1486  CA  PHE C 200       3.301  39.076 -36.219  1.00 52.31           C
ANISOU 1486  CA  PHE C 200     6570   6047   7257    332    646    499       C
ATOM   1487  C   PHE C 200       2.064  39.967 -36.192  1.00 52.69           C
ANISOU 1487  C   PHE C 200     6557   6076   7388    355    700    574       C
ATOM   1488  O   PHE C 200       1.864  40.751 -35.262  1.00 52.12           O
ANISOU 1488  O   PHE C 200     6472   5936   7396    348    772    557       O
ATOM   1489  CB  PHE C 200       4.581  39.915 -36.344  1.00 51.35           C
ANISOU 1489  CB  PHE C 200     6457   5883   7170    348    701    485       C
ATOM   1490  CG  PHE C 200       4.564  40.898 -37.486  1.00 51.69           C
ANISOU 1490  CG  PHE C 200     6450   5936   7254    398    739    580       C
ATOM   1491  CD1 PHE C 200       4.242  42.232 -37.272  1.00 51.48           C
ANISOU 1491  CD1 PHE C 200     6377   5851   7333    421    830    626       C
ATOM   1492  CD2 PHE C 200       4.884  40.492 -38.770  1.00 52.18           C
ANISOU 1492  CD2 PHE C 200     6510   6066   7249    421    686    624       C
ATOM   1493  CE1 PHE C 200       4.230  43.136 -38.324  1.00 51.24           C
ANISOU 1493  CE1 PHE C 200     6298   5828   7342    468    866    718       C
ATOM   1494  CE2 PHE C 200       4.878  41.392 -39.820  1.00 51.90           C
ANISOU 1494  CE2 PHE C 200     6427   6043   7249    467    721    715       C
ATOM   1495  CZ  PHE C 200       4.547  42.714 -39.598  1.00 51.40           C
ANISOU 1495  CZ  PHE C 200     6316   5920   7292    492    811    764       C
ATOM   1496  N   GLY C 201       1.240  39.830 -37.229  1.00 72.29           N
ANISOU 1496  N   GLY C 201     8998   8620   9847    382    664    658       N
ATOM   1497  CA  GLY C 201      -0.043  40.506 -37.322  1.00 72.78           C
ANISOU 1497  CA  GLY C 201     8998   8679   9977    405    701    739       C
ATOM   1498  C   GLY C 201      -1.028  39.680 -38.136  1.00 74.09           C
ANISOU 1498  C   GLY C 201     9142   8930  10078    409    623    793       C
ATOM   1499  O   GLY C 201      -0.664  38.624 -38.657  1.00 74.82           O
ANISOU 1499  O   GLY C 201     9269   9082  10076    394    545    765       O
ATOM   1500  N   PRO C 202      -2.282  40.149 -38.247  1.00 74.72           N
ANISOU 1500  N   PRO C 202     9163   9018  10210    427    646    869       N
ATOM   1501  CA  PRO C 202      -3.330  39.440 -38.996  1.00 75.84           C
ANISOU 1501  CA  PRO C 202     9275   9243  10297    430    576    926       C
ATOM   1502  C   PRO C 202      -3.371  39.734 -40.503  1.00 76.54           C
ANISOU 1502  C   PRO C 202     9321   9400  10360    472    555   1023       C
ATOM   1503  O   PRO C 202      -3.939  38.938 -41.248  1.00 77.06           O
ANISOU 1503  O   PRO C 202     9377   9548  10354    467    481   1053       O
ATOM   1504  CB  PRO C 202      -4.619  39.919 -38.322  1.00 75.92           C
ANISOU 1504  CB  PRO C 202     9239   9223  10385    432    619    963       C
ATOM   1505  CG  PRO C 202      -4.293  41.280 -37.832  1.00 75.26           C
ANISOU 1505  CG  PRO C 202     9133   9053  10409    455    724    975       C
ATOM   1506  CD  PRO C 202      -2.828  41.277 -37.470  1.00 74.56           C
ANISOU 1506  CD  PRO C 202     9104   8923  10304    439    739    892       C
ATOM   1507  N   ASN C 203      -2.793  40.851 -40.933  1.00 85.28           N
ANISOU 1507  N   ASN C 203    10403  10476  11525    510    620   1070       N
ATOM   1508  CA  ASN C 203      -2.707  41.200 -42.353  1.00 85.74           C
ANISOU 1508  CA  ASN C 203    10422  10597  11560    551    606   1163       C
ATOM   1509  C   ASN C 203      -1.812  40.208 -43.122  1.00 85.88           C
ANISOU 1509  C   ASN C 203    10488  10679  11463    537    527   1122       C
ATOM   1510  O   ASN C 203      -0.748  39.832 -42.637  1.00 85.85           O
ANISOU 1510  O   ASN C 203    10545  10642  11433    514    523   1034       O
ATOM   1511  CB  ASN C 203      -2.214  42.654 -42.463  1.00 85.55           C
ANISOU 1511  CB  ASN C 203    10364  10509  11633    592    703   1214       C
ATOM   1512  CG  ASN C 203      -1.750  43.038 -43.857  1.00 85.87           C
ANISOU 1512  CG  ASN C 203    10376  10604  11646    633    695   1294       C
ATOM   1513  OD1 ASN C 203      -2.343  42.652 -44.861  1.00 86.34           O
ANISOU 1513  OD1 ASN C 203    10405  10752  11649    646    638   1362       O
ATOM   1514  ND2 ASN C 203      -0.682  43.828 -43.917  1.00 85.49           N
ANISOU 1514  ND2 ASN C 203    10337  10504  11639    652    754   1287       N
ATOM   1515  N   PRO C 204      -2.268  39.736 -44.300  1.00 83.07           N
ANISOU 1515  N   PRO C 204    10107  10420  11038    549    464   1185       N
ATOM   1516  CA  PRO C 204      -1.481  38.825 -45.146  1.00 82.77           C
ANISOU 1516  CA  PRO C 204    10111  10448  10891    539    392   1153       C
ATOM   1517  C   PRO C 204      -0.099  39.364 -45.507  1.00 81.96           C
ANISOU 1517  C   PRO C 204    10031  10317  10794    560    428   1140       C
ATOM   1518  O   PRO C 204       0.793  38.582 -45.849  1.00 81.98           O
ANISOU 1518  O   PRO C 204    10084  10349  10716    544    380   1084       O
ATOM   1519  CB  PRO C 204      -2.331  38.715 -46.411  1.00 83.17           C
ANISOU 1519  CB  PRO C 204    10107  10599  10896    560    346   1251       C
ATOM   1520  CG  PRO C 204      -3.716  38.826 -45.916  1.00 83.42           C
ANISOU 1520  CG  PRO C 204    10093  10628  10975    555    352   1290       C
ATOM   1521  CD  PRO C 204      -3.671  39.803 -44.746  1.00 83.22           C
ANISOU 1521  CD  PRO C 204    10062  10493  11065    563    445   1274       C
ATOM   1522  N   ASN C 205       0.058  40.683 -45.452  1.00 78.58           N
ANISOU 1522  N   ASN C 205     9564   9833  10460    595    514   1195       N
ATOM   1523  CA  ASN C 205       1.346  41.320 -45.689  1.00 78.40           C
ANISOU 1523  CA  ASN C 205     9559   9772  10458    615    559   1184       C
ATOM   1524  C   ASN C 205       1.998  41.652 -44.351  1.00 77.99           C
ANISOU 1524  C   ASN C 205     9545   9617  10470    593    618   1096       C
ATOM   1525  O   ASN C 205       2.712  42.649 -44.219  1.00 77.81           O
ANISOU 1525  O   ASN C 205     9515   9534  10516    613    691   1104       O
ATOM   1526  CB  ASN C 205       1.181  42.576 -46.544  1.00 78.64           C
ANISOU 1526  CB  ASN C 205     9522   9806  10552    669    619   1301       C
ATOM   1527  CG  ASN C 205       2.460  42.965 -47.273  1.00 78.90           C
ANISOU 1527  CG  ASN C 205     9570   9840  10569    692    637   1308       C
ATOM   1528  OD1 ASN C 205       2.466  43.881 -48.098  1.00 78.99           O
ANISOU 1528  OD1 ASN C 205     9531   9864  10618    736    678   1402       O
ATOM   1529  ND2 ASN C 205       3.546  42.259 -46.983  0.00 79.00           N
ANISOU 1529  ND2 ASN C 205     9649   9841  10525    664    608   1210       N
ATOM   1530  N   GLN C 206       1.723  40.803 -43.362  1.00 64.87           N
ANISOU 1530  N   GLN C 206     7924   7940   8785    549    584   1014       N
ATOM   1531  CA  GLN C 206       2.336  40.888 -42.042  1.00 64.00           C
ANISOU 1531  CA  GLN C 206     7856   7745   8715    519    625    919       C
ATOM   1532  C   GLN C 206       2.786  39.508 -41.566  1.00 63.72           C
ANISOU 1532  C   GLN C 206     7889   7730   8591    473    551    818       C
ATOM   1533  O   GLN C 206       2.516  39.126 -40.427  1.00 63.71           O
ANISOU 1533  O   GLN C 206     7913   7691   8602    439    551    753       O
ATOM   1534  CB  GLN C 206       1.355  41.462 -41.014  1.00 63.62           C
ANISOU 1534  CB  GLN C 206     7778   7638   8756    512    680    926       C
ATOM   1535  CG  GLN C 206       1.105  42.957 -41.112  1.00 63.00           C
ANISOU 1535  CG  GLN C 206     7640   7507   8789    553    776   1003       C
ATOM   1536  CD  GLN C 206       0.070  43.438 -40.111  1.00 62.67           C
ANISOU 1536  CD  GLN C 206     7570   7411   8832    545    828   1008       C
ATOM   1537  OE1 GLN C 206      -0.775  42.667 -39.654  1.00 62.64           O
ANISOU 1537  OE1 GLN C 206     7572   7430   8797    518    784    986       O
ATOM   1538  NE2 GLN C 206       0.133  44.716 -39.765  1.00 62.30           N
ANISOU 1538  NE2 GLN C 206     7490   7288   8892    567    925   1036       N
ATOM   1539  N   CYS C 207       3.456  38.754 -42.433  1.00 56.11           N
ANISOU 1539  N   CYS C 207     6954   6826   7538    473    490    806       N
ATOM   1540  CA  CYS C 207       4.008  37.463 -42.032  1.00 55.50           C
ANISOU 1540  CA  CYS C 207     6943   6765   7380    433    425    711       C
ATOM   1541  C   CYS C 207       5.441  37.650 -41.553  1.00 54.27           C
ANISOU 1541  C   CYS C 207     6831   6554   7233    425    456    642       C
ATOM   1542  O   CYS C 207       6.043  38.709 -41.760  1.00 54.33           O
ANISOU 1542  O   CYS C 207     6819   6526   7298    452    519    671       O
ATOM   1543  CB  CYS C 207       3.988  36.475 -43.198  1.00 55.48           C
ANISOU 1543  CB  CYS C 207     6951   6855   7275    434    342    728       C
ATOM   1544  SG  CYS C 207       2.413  36.365 -44.060  1.00 59.47           S
ANISOU 1544  SG  CYS C 207     7395   7439   7762    449    304    825       S
ATOM   1545  N   CYS C 208       5.980  36.627 -40.900  1.00 48.31           N
ANISOU 1545  N   CYS C 208     6135   5795   6426    387    412    550       N
ATOM   1546  CA  CYS C 208       7.363  36.661 -40.453  1.00 47.96           C
ANISOU 1546  CA  CYS C 208     6135   5709   6381    376    432    481       C
ATOM   1547  C   CYS C 208       8.291  36.447 -41.639  1.00 48.71           C
ANISOU 1547  C   CYS C 208     6241   5850   6416    398    404    498       C
ATOM   1548  O   CYS C 208       7.862  36.001 -42.704  1.00 49.48           O
ANISOU 1548  O   CYS C 208     6325   6018   6458    413    356    545       O
ATOM   1549  CB  CYS C 208       7.609  35.583 -39.397  1.00 47.64           C
ANISOU 1549  CB  CYS C 208     6149   5653   6299    330    392    384       C
ATOM   1550  SG  CYS C 208       6.596  35.762 -37.913  1.00 49.38           S
ANISOU 1550  SG  CYS C 208     6361   5820   6583    300    425    355       S
ATOM   1551  N   HIS C 209       9.562  36.780 -41.454  1.00 37.12           N
ANISOU 1551  N   HIS C 209     4799   4344   4962    400    435    458       N
ATOM   1552  CA  HIS C 209      10.557  36.563 -42.491  1.00 37.12           C
ANISOU 1552  CA  HIS C 209     4815   4383   4907    419    412    465       C
ATOM   1553  C   HIS C 209      10.727  35.062 -42.700  1.00 37.44           C
ANISOU 1553  C   HIS C 209     4903   4476   4847    394    327    412       C
ATOM   1554  O   HIS C 209      10.456  34.274 -41.795  1.00 37.46           O
ANISOU 1554  O   HIS C 209     4936   4466   4833    359    297    352       O
ATOM   1555  CB  HIS C 209      11.884  37.202 -42.084  1.00 36.55           C
ANISOU 1555  CB  HIS C 209     4761   4253   4874    421    465    425       C
ATOM   1556  CG  HIS C 209      12.868  37.322 -43.205  1.00 36.65           C
ANISOU 1556  CG  HIS C 209     4776   4297   4852    449    461    450       C
ATOM   1557  ND1 HIS C 209      13.676  36.276 -43.602  1.00 36.74           N
ANISOU 1557  ND1 HIS C 209     4833   4347   4779    439    403    404       N
ATOM   1558  CD2 HIS C 209      13.180  38.363 -44.010  1.00 36.67           C
ANISOU 1558  CD2 HIS C 209     4742   4298   4894    488    510    518       C
ATOM   1559  CE1 HIS C 209      14.438  36.670 -44.605  1.00 36.81           C
ANISOU 1559  CE1 HIS C 209     4833   4378   4776    469    416    441       C
ATOM   1560  NE2 HIS C 209      14.159  37.932 -44.873  1.00 36.77           N
ANISOU 1560  NE2 HIS C 209     4778   4349   4844    499    480    511       N
ATOM   1561  N   ASP C 210      11.172  34.668 -43.889  1.00 38.79           N
ANISOU 1561  N   ASP C 210     5080   4706   4954    412    290    436       N
ATOM   1562  CA  ASP C 210      11.346  33.254 -44.213  1.00 39.17           C
ANISOU 1562  CA  ASP C 210     5171   4805   4906    391    211    388       C
ATOM   1563  C   ASP C 210      12.442  32.594 -43.379  1.00 39.12           C
ANISOU 1563  C   ASP C 210     5221   4760   4881    363    201    294       C
ATOM   1564  O   ASP C 210      12.529  31.368 -43.315  1.00 39.36           O
ANISOU 1564  O   ASP C 210     5292   4817   4845    339    141    242       O
ATOM   1565  CB  ASP C 210      11.640  33.070 -45.704  1.00 39.49           C
ANISOU 1565  CB  ASP C 210     5204   4917   4884    417    181    434       C
ATOM   1566  CG  ASP C 210      10.442  33.381 -46.578  0.00 39.62           C
ANISOU 1566  CG  ASP C 210     5168   4990   4895    437    170    522       C
ATOM   1567  OD1 ASP C 210       9.311  33.417 -46.049  0.00 39.79           O
ANISOU 1567  OD1 ASP C 210     5167   5005   4947    425    169    539       O
ATOM   1568  OD2 ASP C 210      10.629  33.582 -47.797  0.00 39.50           O
ANISOU 1568  OD2 ASP C 210     5133   5029   4845    465    163    577       O
ATOM   1569  N   GLU C 211      13.274  33.409 -42.741  1.00 41.88           N
ANISOU 1569  N   GLU C 211     5573   5048   5290    367    260    273       N
ATOM   1570  CA  GLU C 211      14.374  32.895 -41.934  1.00 42.22           C
ANISOU 1570  CA  GLU C 211     5665   5056   5320    342    254    188       C
ATOM   1571  C   GLU C 211      14.018  32.780 -40.454  1.00 41.49           C
ANISOU 1571  C   GLU C 211     5587   4913   5265    306    266    135       C
ATOM   1572  O   GLU C 211      14.879  32.489 -39.623  1.00 40.84           O
ANISOU 1572  O   GLU C 211     5539   4796   5181    284    269     67       O
ATOM   1573  CB  GLU C 211      15.624  33.758 -42.118  1.00 41.97           C
ANISOU 1573  CB  GLU C 211     5631   4992   5322    362    306    189       C
ATOM   1574  CG  GLU C 211      16.370  33.481 -43.411  1.00 42.92           C
ANISOU 1574  CG  GLU C 211     5760   5163   5385    388    282    212       C
ATOM   1575  CD  GLU C 211      16.951  32.081 -43.452  1.00 43.85           C
ANISOU 1575  CD  GLU C 211     5929   5309   5421    367    216    147       C
ATOM   1576  OE1 GLU C 211      17.555  31.657 -42.444  1.00 43.73           O
ANISOU 1576  OE1 GLU C 211     5949   5257   5410    340    213     78       O
ATOM   1577  OE2 GLU C 211      16.797  31.401 -44.488  1.00 44.44           O
ANISOU 1577  OE2 GLU C 211     6010   5445   5429    377    169    167       O
ATOM   1578  N   CYS C 212      12.750  33.007 -40.129  1.00 43.50           N
ANISOU 1578  N   CYS C 212     5812   5165   5551    301    273    166       N
ATOM   1579  CA  CYS C 212      12.277  32.866 -38.757  1.00 42.21           C
ANISOU 1579  CA  CYS C 212     5660   4959   5420    267    283    119       C
ATOM   1580  C   CYS C 212      11.862  31.426 -38.477  1.00 43.12           C
ANISOU 1580  C   CYS C 212     5810   5106   5467    236    211     75       C
ATOM   1581  O   CYS C 212      11.087  30.837 -39.231  1.00 43.98           O
ANISOU 1581  O   CYS C 212     5910   5267   5532    241    164    108       O
ATOM   1582  CB  CYS C 212      11.107  33.812 -38.487  1.00 42.35           C
ANISOU 1582  CB  CYS C 212     5628   4954   5509    276    331    172       C
ATOM   1583  SG  CYS C 212      11.535  35.564 -38.541  1.00 43.90           S
ANISOU 1583  SG  CYS C 212     5782   5095   5803    307    429    216       S
ATOM   1584  N   ALA C 213      12.383  30.865 -37.390  1.00 33.97           N
ANISOU 1584  N   ALA C 213     4691   3916   4301    204    202      1       N
ATOM   1585  CA  ALA C 213      12.081  29.488 -37.016  1.00 33.72           C
ANISOU 1585  CA  ALA C 213     4695   3907   4209    174    137    -45       C
ATOM   1586  C   ALA C 213      10.616  29.325 -36.627  1.00 35.20           C
ANISOU 1586  C   ALA C 213     4861   4101   4411    159    126    -23       C
ATOM   1587  O   ALA C 213       9.964  28.356 -37.016  1.00 36.54           O
ANISOU 1587  O   ALA C 213     5040   4314   4531    149     68    -20       O
ATOM   1588  CB  ALA C 213      12.986  29.038 -35.881  1.00 32.26           C
ANISOU 1588  CB  ALA C 213     4552   3686   4020    144    137   -122       C
ATOM   1589  N   GLY C 214      10.104  30.279 -35.856  1.00 44.89           N
ANISOU 1589  N   GLY C 214     6060   5285   5710    156    182    -10       N
ATOM   1590  CA  GLY C 214       8.718  30.253 -35.430  1.00 44.65           C
ANISOU 1590  CA  GLY C 214     6005   5256   5703    144    180     12       C
ATOM   1591  C   GLY C 214       8.053  31.605 -35.584  1.00 44.94           C
ANISOU 1591  C   GLY C 214     5987   5272   5817    170    245     77       C
ATOM   1592  O   GLY C 214       7.812  32.066 -36.700  1.00 46.47           O
ANISOU 1592  O   GLY C 214     6147   5496   6012    203    248    144       O
ATOM   1593  N   GLY C 215       7.760  32.244 -34.457  1.00 37.25           N
ANISOU 1593  N   GLY C 215     5003   4244   4906    154    297     58       N
ATOM   1594  CA  GLY C 215       7.128  33.549 -34.462  1.00 37.36           C
ANISOU 1594  CA  GLY C 215     4966   4228   5002    177    367    114       C
ATOM   1595  C   GLY C 215       8.130  34.674 -34.627  1.00 36.93           C
ANISOU 1595  C   GLY C 215     4901   4135   4997    199    431    121       C
ATOM   1596  O   GLY C 215       9.335  34.436 -34.730  1.00 36.52           O
ANISOU 1596  O   GLY C 215     4882   4082   4913    196    420     81       O
ATOM   1597  N   CYS C 216       7.627  35.904 -34.647  1.00 39.93           N
ANISOU 1597  N   CYS C 216     5234   4482   5457    220    499    172       N
ATOM   1598  CA  CYS C 216       8.467  37.081 -34.827  1.00 38.65           C
ANISOU 1598  CA  CYS C 216     5056   4278   5352    243    568    186       C
ATOM   1599  C   CYS C 216       7.813  38.324 -34.232  1.00 39.02           C
ANISOU 1599  C   CYS C 216     5061   4267   5499    249    653    212       C
ATOM   1600  O   CYS C 216       6.620  38.324 -33.927  1.00 39.23           O
ANISOU 1600  O   CYS C 216     5063   4294   5550    246    656    238       O
ATOM   1601  CB  CYS C 216       8.747  37.308 -36.314  1.00 39.33           C
ANISOU 1601  CB  CYS C 216     5120   4407   5416    285    555    255       C
ATOM   1602  SG  CYS C 216       7.265  37.582 -37.309  1.00 41.54           S
ANISOU 1602  SG  CYS C 216     5341   4733   5711    319    546    363       S
ATOM   1603  N   SER C 217       8.602  39.381 -34.073  1.00 54.59           N
ANISOU 1603  N   SER C 217     7023   6188   7532    259    723    206       N
ATOM   1604  CA  SER C 217       8.097  40.653 -33.574  1.00 54.64           C
ANISOU 1604  CA  SER C 217     6989   6132   7641    267    813    230       C
ATOM   1605  C   SER C 217       7.791  41.591 -34.735  1.00 55.64           C
ANISOU 1605  C   SER C 217     7062   6264   7814    318    850    330       C
ATOM   1606  O   SER C 217       7.023  42.541 -34.588  1.00 56.25           O
ANISOU 1606  O   SER C 217     7095   6305   7974    335    914    377       O
ATOM   1607  CB  SER C 217       9.117  41.304 -32.642  1.00 53.67           C
ANISOU 1607  CB  SER C 217     6885   5944   7561    244    874    161       C
ATOM   1608  OG  SER C 217      10.178  41.884 -33.380  1.00 54.01           O
ANISOU 1608  OG  SER C 217     6924   5980   7616    268    898    178       O
ATOM   1609  N   GLY C 218       8.394  41.313 -35.888  1.00 67.67           N
ANISOU 1609  N   GLY C 218     8589   7836   9285    343    810    364       N
ATOM   1610  CA  GLY C 218       8.179  42.112 -37.082  1.00 68.02           C
ANISOU 1610  CA  GLY C 218     8585   7896   9363    392    838    462       C
ATOM   1611  C   GLY C 218       8.479  41.344 -38.357  1.00 68.56           C
ANISOU 1611  C   GLY C 218     8663   8044   9343    412    764    496       C
ATOM   1612  O   GLY C 218       8.755  40.145 -38.316  1.00 68.67           O
ANISOU 1612  O   GLY C 218     8721   8099   9271    388    690    445       O
ATOM   1613  N   PRO C 219       8.442  42.041 -39.502  1.00 51.93           N
ANISOU 1613  N   PRO C 219     6515   5959   7258    457    786    584       N
ATOM   1614  CA  PRO C 219       8.573  41.442 -40.834  1.00 52.23           C
ANISOU 1614  CA  PRO C 219     6552   6077   7215    480    722    632       C
ATOM   1615  C   PRO C 219      10.018  41.280 -41.311  1.00 52.26           C
ANISOU 1615  C   PRO C 219     6591   6090   7177    484    710    599       C
ATOM   1616  O   PRO C 219      10.224  40.725 -42.392  1.00 52.98           O
ANISOU 1616  O   PRO C 219     6686   6248   7196    500    657    629       O
ATOM   1617  CB  PRO C 219       7.859  42.459 -41.725  1.00 52.28           C
ANISOU 1617  CB  PRO C 219     6492   6095   7279    527    765    746       C
ATOM   1618  CG  PRO C 219       8.131  43.766 -41.057  1.00 51.57           C
ANISOU 1618  CG  PRO C 219     6379   5916   7300    535    866    747       C
ATOM   1619  CD  PRO C 219       8.184  43.490 -39.573  1.00 51.31           C
ANISOU 1619  CD  PRO C 219     6383   5827   7286    488    878    648       C
ATOM   1620  N   GLN C 220      10.997  41.735 -40.534  1.00 56.86           N
ANISOU 1620  N   GLN C 220     7196   6609   7801    468    759    537       N
ATOM   1621  CA  GLN C 220      12.378  41.774 -41.028  1.00 56.48           C
ANISOU 1621  CA  GLN C 220     7172   6563   7726    477    759    516       C
ATOM   1622  C   GLN C 220      13.286  40.608 -40.627  1.00 56.72           C
ANISOU 1622  C   GLN C 220     7265   6610   7677    442    699    424       C
ATOM   1623  O   GLN C 220      12.933  39.777 -39.786  1.00 56.35           O
ANISOU 1623  O   GLN C 220     7248   6564   7600    407    661    365       O
ATOM   1624  CB  GLN C 220      13.055  43.096 -40.646  1.00 55.48           C
ANISOU 1624  CB  GLN C 220     7025   6359   7694    486    853    516       C
ATOM   1625  CG  GLN C 220      12.462  44.319 -41.323  1.00 55.86           C
ANISOU 1625  CG  GLN C 220     7011   6392   7821    530    918    618       C
ATOM   1626  CD  GLN C 220      12.566  44.255 -42.832  1.00 57.43           C
ANISOU 1626  CD  GLN C 220     7189   6659   7972    571    887    699       C
ATOM   1627  OE1 GLN C 220      13.587  43.837 -43.379  1.00 58.28           O
ANISOU 1627  OE1 GLN C 220     7325   6795   8022    573    857    677       O
ATOM   1628  NE2 GLN C 220      11.505  44.664 -43.516  1.00 57.69           N
ANISOU 1628  NE2 GLN C 220     7170   6721   8028    603    895    794       N
ATOM   1629  N   ASP C 221      14.457  40.575 -41.267  1.00 58.29           N
ANISOU 1629  N   ASP C 221     7481   6823   7845    455    693    416       N
ATOM   1630  CA  ASP C 221      15.577  39.699 -40.926  1.00 57.73           C
ANISOU 1630  CA  ASP C 221     7465   6757   7713    428    653    333       C
ATOM   1631  C   ASP C 221      15.849  39.688 -39.425  1.00 56.07           C
ANISOU 1631  C   ASP C 221     7281   6487   7536    386    676    249       C
ATOM   1632  O   ASP C 221      16.194  38.657 -38.846  1.00 54.93           O
ANISOU 1632  O   ASP C 221     7181   6355   7336    354    625    179       O
ATOM   1633  CB  ASP C 221      16.839  40.232 -41.613  1.00 57.78           C
ANISOU 1633  CB  ASP C 221     7471   6757   7725    452    682    345       C
ATOM   1634  CG  ASP C 221      17.446  39.249 -42.592  1.00 59.29           C
ANISOU 1634  CG  ASP C 221     7690   7015   7821    461    614    342       C
ATOM   1635  OD1 ASP C 221      17.011  38.081 -42.624  1.00 60.66           O
ANISOU 1635  OD1 ASP C 221     7891   7234   7924    444    544    317       O
ATOM   1636  OD2 ASP C 221      18.375  39.648 -43.326  1.00 59.25           O
ANISOU 1636  OD2 ASP C 221     7682   7015   7814    485    634    363       O
ATOM   1637  N   THR C 222      15.687  40.856 -38.813  1.00 49.30           N
ANISOU 1637  N   THR C 222     6394   5567   6772    386    755    257       N
ATOM   1638  CA  THR C 222      16.142  41.120 -37.455  1.00 47.78           C
ANISOU 1638  CA  THR C 222     6221   5312   6620    348    793    179       C
ATOM   1639  C   THR C 222      15.026  41.033 -36.423  1.00 47.21           C
ANISOU 1639  C   THR C 222     6144   5218   6576    322    800    158       C
ATOM   1640  O   THR C 222      15.205  41.433 -35.273  1.00 46.31           O
ANISOU 1640  O   THR C 222     6038   5051   6508    291    844    102       O
ATOM   1641  CB  THR C 222      16.769  42.521 -37.381  1.00 46.93           C
ANISOU 1641  CB  THR C 222     6086   5144   6603    361    884    192       C
ATOM   1642  OG1 THR C 222      15.888  43.467 -38.001  1.00 47.31           O
ANISOU 1642  OG1 THR C 222     6080   5181   6714    398    932    281       O
ATOM   1643  CG2 THR C 222      18.090  42.537 -38.118  1.00 46.55           C
ANISOU 1643  CG2 THR C 222     6051   5110   6526    377    878    190       C
ATOM   1644  N   ASP C 223      13.880  40.501 -36.837  1.00 50.66           N
ANISOU 1644  N   ASP C 223     6568   5698   6983    332    757    203       N
ATOM   1645  CA  ASP C 223      12.684  40.513 -36.004  1.00 50.62           C
ANISOU 1645  CA  ASP C 223     6549   5673   7010    313    768    199       C
ATOM   1646  C   ASP C 223      12.242  39.121 -35.554  1.00 50.75           C
ANISOU 1646  C   ASP C 223     6604   5731   6950    282    689    153       C
ATOM   1647  O   ASP C 223      11.165  38.965 -34.979  1.00 50.67           O
ANISOU 1647  O   ASP C 223     6583   5716   6955    267    686    155       O
ATOM   1648  CB  ASP C 223      11.540  41.191 -36.756  1.00 51.24           C
ANISOU 1648  CB  ASP C 223     6572   5762   7133    351    794    296       C
ATOM   1649  CG  ASP C 223      11.802  42.660 -37.023  1.00 51.47           C
ANISOU 1649  CG  ASP C 223     6561   5741   7257    380    884    344       C
ATOM   1650  OD1 ASP C 223      12.482  43.306 -36.200  1.00 51.25           O
ANISOU 1650  OD1 ASP C 223     6541   5650   7281    361    943    292       O
ATOM   1651  OD2 ASP C 223      11.322  43.172 -38.055  1.00 51.71           O
ANISOU 1651  OD2 ASP C 223     6548   5793   7307    422    898    434       O
ATOM   1652  N   CYS C 224      13.071  38.115 -35.810  1.00 42.56           N
ANISOU 1652  N   CYS C 224     5608   4731   5833    272    627    113       N
ATOM   1653  CA  CYS C 224      12.731  36.741 -35.455  1.00 43.04           C
ANISOU 1653  CA  CYS C 224     5705   4828   5819    243    551     70       C
ATOM   1654  C   CYS C 224      12.921  36.480 -33.964  1.00 42.20           C
ANISOU 1654  C   CYS C 224     5629   4683   5723    198    560    -11       C
ATOM   1655  O   CYS C 224      13.725  37.141 -33.306  1.00 41.44           O
ANISOU 1655  O   CYS C 224     5537   4540   5668    186    611    -51       O
ATOM   1656  CB  CYS C 224      13.582  35.757 -36.262  1.00 43.57           C
ANISOU 1656  CB  CYS C 224     5806   4946   5801    249    485     56       C
ATOM   1657  SG  CYS C 224      13.465  35.964 -38.052  1.00 44.14           S
ANISOU 1657  SG  CYS C 224     5848   5074   5848    299    469    146       S
ATOM   1658  N   PHE C 225      12.168  35.521 -33.434  1.00 39.80           N
ANISOU 1658  N   PHE C 225     5342   4399   5380    173    511    -36       N
ATOM   1659  CA  PHE C 225      12.375  35.058 -32.068  1.00 38.59           C
ANISOU 1659  CA  PHE C 225     5222   4220   5220    129    507   -113       C
ATOM   1660  C   PHE C 225      13.549  34.090 -32.062  1.00 38.49           C
ANISOU 1660  C   PHE C 225     5256   4230   5138    115    455   -167       C
ATOM   1661  O   PHE C 225      14.335  34.046 -31.115  1.00 37.81           O
ANISOU 1661  O   PHE C 225     5195   4117   5053     87    468   -230       O
ATOM   1662  CB  PHE C 225      11.122  34.360 -31.536  1.00 39.06           C
ANISOU 1662  CB  PHE C 225     5283   4295   5264    108    474   -115       C
ATOM   1663  CG  PHE C 225       9.951  35.280 -31.329  1.00 39.48           C
ANISOU 1663  CG  PHE C 225     5290   4320   5389    117    528    -70       C
ATOM   1664  CD1 PHE C 225       8.656  34.785 -31.346  1.00 40.01           C
ANISOU 1664  CD1 PHE C 225     5344   4413   5446    114    497    -41       C
ATOM   1665  CD2 PHE C 225      10.143  36.634 -31.109  1.00 38.75           C
ANISOU 1665  CD2 PHE C 225     5168   4176   5378    129    612    -57       C
ATOM   1666  CE1 PHE C 225       7.574  35.625 -31.156  1.00 40.09           C
ANISOU 1666  CE1 PHE C 225     5310   4398   5525    124    548      4       C
ATOM   1667  CE2 PHE C 225       9.066  37.479 -30.916  1.00 38.61           C
ANISOU 1667  CE2 PHE C 225     5109   4131   5432    138    665    -14       C
ATOM   1668  CZ  PHE C 225       7.780  36.973 -30.939  1.00 39.72           C
ANISOU 1668  CZ  PHE C 225     5233   4297   5560    137    633     17       C
ATOM   1669  N   ALA C 226      13.656  33.317 -33.138  1.00 30.46           N
ANISOU 1669  N   ALA C 226     4250   3263   4060    134    397   -141       N
ATOM   1670  CA  ALA C 226      14.745  32.366 -33.315  1.00 30.13           C
ANISOU 1670  CA  ALA C 226     4250   3245   3952    127    348   -184       C
ATOM   1671  C   ALA C 226      15.037  32.191 -34.801  1.00 30.76           C
ANISOU 1671  C   ALA C 226     4325   3369   3994    163    320   -137       C
ATOM   1672  O   ALA C 226      14.124  32.218 -35.627  1.00 31.75           O
ANISOU 1672  O   ALA C 226     4425   3526   4113    184    306    -79       O
ATOM   1673  CB  ALA C 226      14.392  31.031 -32.680  1.00 29.82           C
ANISOU 1673  CB  ALA C 226     4246   3226   3857     95    286   -228       C
ATOM   1674  N   CYS C 227      16.311  32.016 -35.139  1.00 47.83           N
ANISOU 1674  N   CYS C 227     6509   5535   6128    170    312   -161       N
ATOM   1675  CA  CYS C 227      16.718  31.875 -36.534  1.00 48.38           C
ANISOU 1675  CA  CYS C 227     6576   5646   6160    204    289   -121       C
ATOM   1676  C   CYS C 227      16.500  30.458 -37.051  1.00 49.22           C
ANISOU 1676  C   CYS C 227     6712   5804   6184    198    211   -132       C
ATOM   1677  O   CYS C 227      16.724  29.483 -36.335  1.00 48.29           O
ANISOU 1677  O   CYS C 227     6631   5685   6032    170    174   -188       O
ATOM   1678  CB  CYS C 227      18.181  32.284 -36.712  1.00 47.32           C
ANISOU 1678  CB  CYS C 227     6452   5495   6031    214    316   -141       C
ATOM   1679  SG  CYS C 227      18.494  34.046 -36.451  1.00 49.84           S
ANISOU 1679  SG  CYS C 227     6731   5758   6448    228    412   -117       S
ATOM   1680  N   ARG C 228      16.061  30.352 -38.300  1.00 55.09           N
ANISOU 1680  N   ARG C 228     7439   6595   6898    225    188    -78       N
ATOM   1681  CA  ARG C 228      15.804  29.056 -38.914  1.00 55.32           C
ANISOU 1681  CA  ARG C 228     7494   6675   6850    219    117    -87       C
ATOM   1682  C   ARG C 228      17.113  28.366 -39.293  1.00 54.51           C
ANISOU 1682  C   ARG C 228     7429   6585   6697    222     91   -127       C
ATOM   1683  O   ARG C 228      17.173  27.141 -39.393  1.00 54.83           O
ANISOU 1683  O   ARG C 228     7504   6652   6678    208     35   -160       O
ATOM   1684  CB  ARG C 228      14.900  29.213 -40.141  1.00 56.91           C
ANISOU 1684  CB  ARG C 228     7662   6927   7033    245    102    -16       C
ATOM   1685  CG  ARG C 228      14.386  27.901 -40.716  1.00 57.84           C
ANISOU 1685  CG  ARG C 228     7802   7100   7075    233     30    -25       C
ATOM   1686  CD  ARG C 228      13.445  28.137 -41.888  1.00 59.70           C
ANISOU 1686  CD  ARG C 228     7999   7389   7293    255     16     47       C
ATOM   1687  NE  ARG C 228      12.200  28.781 -41.475  1.00 60.62           N
ANISOU 1687  NE  ARG C 228     8075   7494   7462    253     40     89       N
ATOM   1688  CZ  ARG C 228      11.084  28.125 -41.174  1.00 61.77           C
ANISOU 1688  CZ  ARG C 228     8219   7658   7592    231      4     87       C
ATOM   1689  NH1 ARG C 228      11.052  26.801 -41.241  1.00 61.69           N
ANISOU 1689  NH1 ARG C 228     8246   7676   7516    207    -58     43       N
ATOM   1690  NH2 ARG C 228       9.998  28.792 -40.808  1.00 62.28           N
ANISOU 1690  NH2 ARG C 228     8244   7710   7709    232     31    128       N
ATOM   1691  N   HIS C 229      18.161  29.159 -39.495  1.00 41.10           N
ANISOU 1691  N   HIS C 229     5724   4866   5025    241    133   -122       N
ATOM   1692  CA  HIS C 229      19.471  28.615 -39.841  1.00 40.04           C
ANISOU 1692  CA  HIS C 229     5622   4740   4850    247    116   -157       C
ATOM   1693  C   HIS C 229      20.594  29.229 -39.006  1.00 39.45           C
ANISOU 1693  C   HIS C 229     5554   4617   4819    239    160   -194       C
ATOM   1694  O   HIS C 229      21.079  28.611 -38.058  1.00 38.96           O
ANISOU 1694  O   HIS C 229     5522   4535   4746    212    145   -252       O
ATOM   1695  CB  HIS C 229      19.756  28.796 -41.335  1.00 41.47           C
ANISOU 1695  CB  HIS C 229     5791   4965   5001    282    112   -109       C
ATOM   1696  CG  HIS C 229      18.782  28.088 -42.225  1.00 43.08           C
ANISOU 1696  CG  HIS C 229     5991   5225   5150    287     62    -78       C
ATOM   1697  ND1 HIS C 229      17.769  28.749 -42.893  1.00 45.23           N
ANISOU 1697  ND1 HIS C 229     6222   5523   5439    305     74    -10       N
ATOM   1698  CD2 HIS C 229      18.658  26.785 -42.553  1.00 42.57           C
ANISOU 1698  CD2 HIS C 229     5959   5197   5017    273      1   -108       C
ATOM   1699  CE1 HIS C 229      17.071  27.880 -43.595  1.00 45.94           C
ANISOU 1699  CE1 HIS C 229     6319   5668   5470    301     21      1       C
ATOM   1700  NE2 HIS C 229      17.586  26.676 -43.408  1.00 44.33           N
ANISOU 1700  NE2 HIS C 229     6160   5470   5214    281    -23    -60       N
ATOM   1701  N   PHE C 230      21.003  30.444 -39.358  1.00 41.71           N
ANISOU 1701  N   PHE C 230     5810   4884   5153    263    217   -159       N
ATOM   1702  CA  PHE C 230      22.107  31.107 -38.669  1.00 40.48           C
ANISOU 1702  CA  PHE C 230     5657   4684   5041    256    262   -192       C
ATOM   1703  C   PHE C 230      21.754  32.529 -38.248  1.00 40.53           C
ANISOU 1703  C   PHE C 230     5623   4646   5129    259    333   -164       C
ATOM   1704  O   PHE C 230      20.801  33.118 -38.754  1.00 41.64           O
ANISOU 1704  O   PHE C 230     5731   4795   5295    278    351   -106       O
ATOM   1705  CB  PHE C 230      23.354  31.139 -39.558  1.00 41.29           C
ANISOU 1705  CB  PHE C 230     5767   4801   5119    281    265   -187       C
ATOM   1706  CG  PHE C 230      23.811  29.783 -40.017  1.00 41.35           C
ANISOU 1706  CG  PHE C 230     5814   4848   5049    279    202   -216       C
ATOM   1707  CD1 PHE C 230      23.447  29.300 -41.262  1.00 42.36           C
ANISOU 1707  CD1 PHE C 230     5942   5027   5127    302    168   -180       C
ATOM   1708  CD2 PHE C 230      24.610  28.995 -39.204  1.00 39.98           C
ANISOU 1708  CD2 PHE C 230     5675   4660   4854    255    179   -280       C
ATOM   1709  CE1 PHE C 230      23.867  28.054 -41.688  1.00 42.11           C
ANISOU 1709  CE1 PHE C 230     5946   5028   5025    299    115   -210       C
ATOM   1710  CE2 PHE C 230      25.033  27.748 -39.624  1.00 39.29           C
ANISOU 1710  CE2 PHE C 230     5623   4605   4702    255    126   -306       C
ATOM   1711  CZ  PHE C 230      24.661  27.277 -40.868  1.00 40.48           C
ANISOU 1711  CZ  PHE C 230     5775   4802   4804    277     95   -273       C
ATOM   1712  N   ASN C 231      22.533  33.071 -37.316  1.00 40.95           N
ANISOU 1712  N   ASN C 231     5679   4655   5224    241    373   -205       N
ATOM   1713  CA  ASN C 231      22.391  34.461 -36.895  1.00 40.94           C
ANISOU 1713  CA  ASN C 231     5643   4606   5305    242    447   -187       C
ATOM   1714  C   ASN C 231      23.673  35.232 -37.194  1.00 41.05           C
ANISOU 1714  C   ASN C 231     5649   4599   5348    256    491   -189       C
ATOM   1715  O   ASN C 231      24.754  34.853 -36.743  1.00 40.57           O
ANISOU 1715  O   ASN C 231     5615   4533   5268    239    480   -242       O
ATOM   1716  CB  ASN C 231      22.063  34.541 -35.400  1.00 39.87           C
ANISOU 1716  CB  ASN C 231     5514   4433   5203    201    465   -239       C
ATOM   1717  CG  ASN C 231      21.687  35.949 -34.949  1.00 40.11           C
ANISOU 1717  CG  ASN C 231     5506   4412   5321    200    543   -221       C
ATOM   1718  OD1 ASN C 231      21.900  36.927 -35.666  1.00 40.91           O
ANISOU 1718  OD1 ASN C 231     5578   4500   5465    229    590   -175       O
ATOM   1719  ND2 ASN C 231      21.130  36.054 -33.748  1.00 39.53           N
ANISOU 1719  ND2 ASN C 231     5434   4309   5276    167    560   -257       N
ATOM   1720  N   ASP C 232      23.547  36.314 -37.954  1.00 52.64           N
ANISOU 1720  N   ASP C 232     7080   6057   6863    287    541   -129       N
ATOM   1721  CA  ASP C 232      24.697  37.141 -38.298  1.00 52.87           C
ANISOU 1721  CA  ASP C 232     7097   6063   6926    303    588   -124       C
ATOM   1722  C   ASP C 232      24.548  38.544 -37.720  1.00 52.74           C
ANISOU 1722  C   ASP C 232     7047   5988   7004    297    670   -115       C
ATOM   1723  O   ASP C 232      23.973  39.427 -38.357  1.00 53.60           O
ANISOU 1723  O   ASP C 232     7119   6088   7160    326    712    -49       O
ATOM   1724  CB  ASP C 232      24.872  37.213 -39.817  1.00 54.45           C
ANISOU 1724  CB  ASP C 232     7285   6305   7100    347    580    -59       C
ATOM   1725  CG  ASP C 232      26.238  37.741 -40.228  1.00 54.48           C
ANISOU 1725  CG  ASP C 232     7286   6294   7118    361    613    -62       C
ATOM   1726  OD1 ASP C 232      26.967  38.272 -39.364  1.00 54.12           O
ANISOU 1726  OD1 ASP C 232     7242   6205   7118    339    653   -106       O
ATOM   1727  OD2 ASP C 232      26.582  37.629 -41.424  1.00 54.79           O
ANISOU 1727  OD2 ASP C 232     7323   6372   7125    394    600    -20       O
ATOM   1728  N   SER C 233      25.069  38.734 -36.510  1.00 68.65           N
ANISOU 1728  N   SER C 233     9073   7963   9047    260    694   -180       N
ATOM   1729  CA  SER C 233      25.077  40.036 -35.844  1.00 68.13           C
ANISOU 1729  CA  SER C 233     8978   7836   9070    248    775   -186       C
ATOM   1730  C   SER C 233      23.695  40.679 -35.731  1.00 68.35           C
ANISOU 1730  C   SER C 233     8975   7843   9152    255    811   -143       C
ATOM   1731  O   SER C 233      23.567  41.902 -35.775  1.00 69.01           O
ANISOU 1731  O   SER C 233     9023   7882   9314    267    884   -113       O
ATOM   1732  CB  SER C 233      26.050  40.992 -36.540  1.00 68.50           C
ANISOU 1732  CB  SER C 233     9005   7864   9160    273    828   -159       C
ATOM   1733  OG  SER C 233      27.376  40.495 -36.491  1.00 68.86           O
ANISOU 1733  OG  SER C 233     9077   7923   9165    262    803   -205       O
ATOM   1734  N   GLY C 234      22.664  39.851 -35.589  1.00 37.48           N
ANISOU 1734  N   GLY C 234     5076   3963   5202    249    761   -138       N
ATOM   1735  CA  GLY C 234      21.312  40.350 -35.420  1.00 37.78           C
ANISOU 1735  CA  GLY C 234     5085   3984   5286    254    789    -99       C
ATOM   1736  C   GLY C 234      20.342  39.898 -36.495  1.00 39.09           C
ANISOU 1736  C   GLY C 234     5238   4200   5415    287    746    -28       C
ATOM   1737  O   GLY C 234      19.127  39.931 -36.295  1.00 39.54           O
ANISOU 1737  O   GLY C 234     5277   4256   5489    286    747     -2       O
ATOM   1738  N   ALA C 235      20.872  39.473 -37.637  1.00 31.70           N
ANISOU 1738  N   ALA C 235     4308   3309   4426    315    709      3       N
ATOM   1739  CA  ALA C 235      20.032  39.062 -38.757  1.00 32.22           C
ANISOU 1739  CA  ALA C 235     4361   3430   4452    346    668     71       C
ATOM   1740  C   ALA C 235      20.064  37.553 -38.977  1.00 32.40           C
ANISOU 1740  C   ALA C 235     4424   3509   4377    335    580     40       C
ATOM   1741  O   ALA C 235      21.126  36.930 -38.933  1.00 32.01           O
ANISOU 1741  O   ALA C 235     4409   3470   4283    325    552     -8       O
ATOM   1742  CB  ALA C 235      20.447  39.793 -40.025  1.00 32.67           C
ANISOU 1742  CB  ALA C 235     4389   3500   4524    390    698    141       C
ATOM   1743  N   CYS C 236      18.893  36.971 -39.214  1.00 37.68           N
ANISOU 1743  N   CYS C 236     5088   4214   5016    336    539     68       N
ATOM   1744  CA  CYS C 236      18.789  35.548 -39.510  1.00 37.98           C
ANISOU 1744  CA  CYS C 236     5162   4306   4964    326    457     44       C
ATOM   1745  C   CYS C 236      19.088  35.288 -40.982  1.00 39.29           C
ANISOU 1745  C   CYS C 236     5324   4527   5077    360    427     92       C
ATOM   1746  O   CYS C 236      18.334  35.705 -41.862  1.00 39.51           O
ANISOU 1746  O   CYS C 236     5317   4584   5112    388    433    165       O
ATOM   1747  CB  CYS C 236      17.400  35.021 -39.148  1.00 38.38           C
ANISOU 1747  CB  CYS C 236     5207   4373   5003    310    424     52       C
ATOM   1748  SG  CYS C 236      17.020  35.090 -37.383  1.00 38.70           S
ANISOU 1748  SG  CYS C 236     5258   4356   5089    266    449    -11       S
ATOM   1749  N   VAL C 237      20.191  34.593 -41.242  1.00 45.93           N
ANISOU 1749  N   VAL C 237     6200   5386   5865    358    396     52       N
ATOM   1750  CA  VAL C 237      20.660  34.373 -42.605  1.00 46.62           C
ANISOU 1750  CA  VAL C 237     6288   5524   5903    389    374     90       C
ATOM   1751  C   VAL C 237      20.678  32.891 -42.975  1.00 47.02           C
ANISOU 1751  C   VAL C 237     6377   5625   5861    377    296     56       C
ATOM   1752  O   VAL C 237      20.885  32.036 -42.113  1.00 46.48           O
ANISOU 1752  O   VAL C 237     6346   5545   5771    346    265     -9       O
ATOM   1753  CB  VAL C 237      22.068  34.973 -42.806  1.00 45.45           C
ANISOU 1753  CB  VAL C 237     6143   5352   5776    403    414     79       C
ATOM   1754  CG1 VAL C 237      22.013  36.490 -42.727  1.00 44.98           C
ANISOU 1754  CG1 VAL C 237     6039   5246   5806    421    494    125       C
ATOM   1755  CG2 VAL C 237      23.037  34.416 -41.773  1.00 44.22           C
ANISOU 1755  CG2 VAL C 237     6026   5164   5610    371    403     -5       C
ATOM   1756  N   PRO C 238      20.448  32.582 -44.263  1.00 46.81           N
ANISOU 1756  N   PRO C 238     6344   5658   5783    402    266    102       N
ATOM   1757  CA  PRO C 238      20.512  31.201 -44.756  1.00 47.29           C
ANISOU 1757  CA  PRO C 238     6442   5770   5756    392    196     71       C
ATOM   1758  C   PRO C 238      21.914  30.626 -44.604  1.00 46.42           C
ANISOU 1758  C   PRO C 238     6372   5648   5618    386    185     11       C
ATOM   1759  O   PRO C 238      22.071  29.448 -44.285  1.00 46.00           O
ANISOU 1759  O   PRO C 238     6358   5605   5516    364    137    -43       O
ATOM   1760  CB  PRO C 238      20.175  31.345 -46.244  1.00 47.83           C
ANISOU 1760  CB  PRO C 238     6486   5901   5787    424    184    140       C
ATOM   1761  CG  PRO C 238      19.418  32.620 -46.345  1.00 48.11           C
ANISOU 1761  CG  PRO C 238     6469   5923   5889    444    235    212       C
ATOM   1762  CD  PRO C 238      20.021  33.521 -45.315  1.00 47.48           C
ANISOU 1762  CD  PRO C 238     6384   5769   5889    438    296    188       C
ATOM   1763  N   ARG C 239      22.921  31.461 -44.834  1.00 43.57           N
ANISOU 1763  N   ARG C 239     6000   5265   5290    406    232     23       N
ATOM   1764  CA  ARG C 239      24.309  31.034 -44.730  1.00 42.90           C
ANISOU 1764  CA  ARG C 239     5948   5169   5184    403    228    -27       C
ATOM   1765  C   ARG C 239      25.190  32.151 -44.187  1.00 42.21           C
ANISOU 1765  C   ARG C 239     5844   5027   5166    407    292    -32       C
ATOM   1766  O   ARG C 239      24.852  33.330 -44.290  1.00 42.70           O
ANISOU 1766  O   ARG C 239     5868   5069   5288    423    344     17       O
ATOM   1767  CB  ARG C 239      24.828  30.571 -46.095  1.00 43.56           C
ANISOU 1767  CB  ARG C 239     6042   5307   5204    429    203     -7       C
ATOM   1768  CG  ARG C 239      24.483  31.511 -47.240  1.00 44.91           C
ANISOU 1768  CG  ARG C 239     6171   5508   5386    465    233     75       C
ATOM   1769  CD  ARG C 239      25.107  31.055 -48.550  0.00 45.49           C
ANISOU 1769  CD  ARG C 239     6256   5636   5393    488    210     90       C
ATOM   1770  NE  ARG C 239      24.656  31.869 -49.674  0.00 46.23           N
ANISOU 1770  NE  ARG C 239     6309   5767   5489    521    232    173       N
ATOM   1771  CZ  ARG C 239      25.098  31.738 -50.920  0.00 46.17           C
ANISOU 1771  CZ  ARG C 239     6302   5812   5430    546    223    202       C
ATOM   1772  NH1 ARG C 239      26.014  30.824 -51.210  0.00 45.70           N
ANISOU 1772  NH1 ARG C 239     6282   5769   5315    543    194    152       N
ATOM   1773  NH2 ARG C 239      24.626  32.525 -51.876  0.00 46.32           N
ANISOU 1773  NH2 ARG C 239     6279   5866   5454    576    245    282       N
ATOM   1774  N   CYS C 240      26.318  31.771 -43.597  1.00 67.33           N
ANISOU 1774  N   CYS C 240     9055   8186   8343    393    290    -91       N
ATOM   1775  CA  CYS C 240      27.306  32.740 -43.146  1.00 66.46           C
ANISOU 1775  CA  CYS C 240     8931   8029   8291    394    347   -101       C
ATOM   1776  C   CYS C 240      28.099  33.230 -44.352  1.00 67.15           C
ANISOU 1776  C   CYS C 240     9005   8138   8372    431    370    -59       C
ATOM   1777  O   CYS C 240      28.271  32.486 -45.317  1.00 68.02           O
ANISOU 1777  O   CYS C 240     9132   8296   8417    447    332    -50       O
ATOM   1778  CB  CYS C 240      28.235  32.112 -42.105  1.00 64.90           C
ANISOU 1778  CB  CYS C 240     8767   7806   8085    364    332   -176       C
ATOM   1779  SG  CYS C 240      27.457  31.804 -40.500  1.00 69.00           S
ANISOU 1779  SG  CYS C 240     9297   8293   8627    319    321   -226       S
ATOM   1780  N   PRO C 241      28.570  34.489 -44.307  1.00 47.74           N
ANISOU 1780  N   PRO C 241     6516   5642   5980    443    435    -34       N
ATOM   1781  CA  PRO C 241      29.326  35.098 -45.408  1.00 48.30           C
ANISOU 1781  CA  PRO C 241     6569   5727   6054    478    466     11       C
ATOM   1782  C   PRO C 241      30.468  34.216 -45.911  1.00 48.50           C
ANISOU 1782  C   PRO C 241     6628   5781   6017    484    432    -22       C
ATOM   1783  O   PRO C 241      31.321  33.798 -45.128  1.00 47.83           O
ANISOU 1783  O   PRO C 241     6567   5673   5932    462    425    -83       O
ATOM   1784  CB  PRO C 241      29.881  36.374 -44.777  1.00 47.77           C
ANISOU 1784  CB  PRO C 241     6477   5601   6074    474    538     10       C
ATOM   1785  CG  PRO C 241      28.866  36.742 -43.756  1.00 47.36           C
ANISOU 1785  CG  PRO C 241     6411   5513   6069    450    554      2       C
ATOM   1786  CD  PRO C 241      28.353  35.440 -43.201  1.00 46.90           C
ANISOU 1786  CD  PRO C 241     6389   5477   5953    422    487    -46       C
ATOM   1787  N   GLN C 242      30.464  33.945 -47.214  1.00 49.96           N
ANISOU 1787  N   GLN C 242     6812   6019   6151    514    414     19       N
ATOM   1788  CA  GLN C 242      31.425  33.043 -47.842  1.00 49.79           C
ANISOU 1788  CA  GLN C 242     6822   6030   6066    523    381     -8       C
ATOM   1789  C   GLN C 242      32.876  33.448 -47.596  1.00 49.07           C
ANISOU 1789  C   GLN C 242     6732   5906   6005    525    417    -34       C
ATOM   1790  O   GLN C 242      33.185  34.635 -47.497  1.00 49.20           O
ANISOU 1790  O   GLN C 242     6719   5889   6087    534    475     -7       O
ATOM   1791  CB  GLN C 242      31.155  32.960 -49.347  1.00 51.35           C
ANISOU 1791  CB  GLN C 242     7010   6289   6212    556    368     50       C
ATOM   1792  CG  GLN C 242      29.805  32.361 -49.700  0.00 52.25           C
ANISOU 1792  CG  GLN C 242     7125   6447   6282    551    322     71       C
ATOM   1793  CD  GLN C 242      29.488  32.477 -51.176  0.00 53.49           C
ANISOU 1793  CD  GLN C 242     7264   6667   6393    583    316    136       C
ATOM   1794  OE1 GLN C 242      29.046  33.525 -51.646  0.00 54.07           O
ANISOU 1794  OE1 GLN C 242     7297   6745   6504    606    354    206       O
ATOM   1795  NE2 GLN C 242      29.717  31.399 -51.918  0.00 53.49           N
ANISOU 1795  NE2 GLN C 242     7295   6718   6313    585    269    115       N
ATOM   1796  N   PRO C 243      33.772  32.453 -47.491  1.00 55.98           N
ANISOU 1796  N   PRO C 243     7643   6790   6835    517    383    -87       N
ATOM   1797  CA  PRO C 243      35.201  32.699 -47.269  1.00 55.44           C
ANISOU 1797  CA  PRO C 243     7578   6696   6789    518    411   -115       C
ATOM   1798  C   PRO C 243      35.871  33.320 -48.491  1.00 56.00           C
ANISOU 1798  C   PRO C 243     7631   6788   6859    556    445    -65       C
ATOM   1799  O   PRO C 243      36.790  34.124 -48.346  1.00 55.89           O
ANISOU 1799  O   PRO C 243     7600   6743   6892    561    492    -63       O
ATOM   1800  CB  PRO C 243      35.767  31.293 -47.027  1.00 54.66           C
ANISOU 1800  CB  PRO C 243     7523   6613   6631    505    358   -175       C
ATOM   1801  CG  PRO C 243      34.584  30.440 -46.694  1.00 54.48           C
ANISOU 1801  CG  PRO C 243     7518   6607   6574    485    309   -190       C
ATOM   1802  CD  PRO C 243      33.457  31.015 -47.482  1.00 55.51           C
ANISOU 1802  CD  PRO C 243     7622   6763   6706    503    318   -126       C
ATOM   1803  N   LEU C 244      35.412  32.944 -49.681  1.00 53.38           N
ANISOU 1803  N   LEU C 244     7301   6511   6471    580    421    -26       N
ATOM   1804  CA  LEU C 244      36.010  33.429 -50.919  1.00 54.05           C
ANISOU 1804  CA  LEU C 244     7370   6623   6543    616    448     23       C
ATOM   1805  C   LEU C 244      35.032  34.273 -51.728  1.00 55.51           C
ANISOU 1805  C   LEU C 244     7517   6831   6741    640    471    103       C
ATOM   1806  O   LEU C 244      33.826  34.029 -51.715  1.00 56.30           O
ANISOU 1806  O   LEU C 244     7615   6952   6824    632    443    119       O
ATOM   1807  CB  LEU C 244      36.517  32.257 -51.762  1.00 53.95           C
ANISOU 1807  CB  LEU C 244     7390   6660   6447    627    405      2       C
ATOM   1808  CG  LEU C 244      37.679  31.455 -51.174  1.00 52.93           C
ANISOU 1808  CG  LEU C 244     7294   6511   6305    613    388    -67       C
ATOM   1809  CD1 LEU C 244      37.900  30.174 -51.961  1.00 53.03           C
ANISOU 1809  CD1 LEU C 244     7342   6572   6234    621    341    -90       C
ATOM   1810  CD2 LEU C 244      38.949  32.293 -51.146  1.00 52.71           C
ANISOU 1810  CD2 LEU C 244     7248   6453   6325    625    441    -62       C
ATOM   1811  N   VAL C 245      35.566  35.266 -52.433  1.00 57.22           N
ANISOU 1811  N   VAL C 245     7704   7047   6989    668    521    155       N
ATOM   1812  CA  VAL C 245      34.760  36.159 -53.258  1.00 57.84           C
ANISOU 1812  CA  VAL C 245     7743   7148   7084    695    549    239       C
ATOM   1813  C   VAL C 245      35.490  36.494 -54.556  1.00 58.22           C
ANISOU 1813  C   VAL C 245     7780   7235   7108    732    572    289       C
ATOM   1814  O   VAL C 245      36.668  36.854 -54.541  1.00 57.53           O
ANISOU 1814  O   VAL C 245     7690   7120   7046    739    607    276       O
ATOM   1815  CB  VAL C 245      34.399  37.458 -52.496  1.00 57.32           C
ANISOU 1815  CB  VAL C 245     7639   7021   7117    690    608    266       C
ATOM   1816  CG1 VAL C 245      34.145  38.608 -53.460  1.00 58.02           C
ANISOU 1816  CG1 VAL C 245     7683   7123   7240    727    658    358       C
ATOM   1817  CG2 VAL C 245      33.194  37.230 -51.596  1.00 57.31           C
ANISOU 1817  CG2 VAL C 245     7641   7004   7131    663    584    248       C
ATOM   1818  N   TYR C 246      34.788  36.363 -55.678  1.00 53.44           N
ANISOU 1818  N   TYR C 246     7162   6692   6449    754    553    345       N
ATOM   1819  CA  TYR C 246      35.366  36.651 -56.986  1.00 53.68           C
ANISOU 1819  CA  TYR C 246     7180   6768   6447    789    572    397       C
ATOM   1820  C   TYR C 246      35.598  38.148 -57.176  1.00 53.50           C
ANISOU 1820  C   TYR C 246     7110   6712   6505    814    645    466       C
ATOM   1821  O   TYR C 246      34.668  38.948 -57.079  1.00 53.30           O
ANISOU 1821  O   TYR C 246     7050   6675   6528    820    670    520       O
ATOM   1822  CB  TYR C 246      34.461  36.112 -58.097  1.00 54.09           C
ANISOU 1822  CB  TYR C 246     7230   6902   6417    803    529    440       C
ATOM   1823  CG  TYR C 246      35.028  36.260 -59.493  1.00 54.38           C
ANISOU 1823  CG  TYR C 246     7259   6998   6407    837    542    490       C
ATOM   1824  CD1 TYR C 246      35.892  35.308 -60.018  1.00 54.23           C
ANISOU 1824  CD1 TYR C 246     7277   7012   6317    838    515    444       C
ATOM   1825  CD2 TYR C 246      34.691  37.347 -60.289  1.00 54.73           C
ANISOU 1825  CD2 TYR C 246     7255   7062   6476    868    584    583       C
ATOM   1826  CE1 TYR C 246      36.409  35.438 -61.295  1.00 54.26           C
ANISOU 1826  CE1 TYR C 246     7271   7069   6274    868    528    488       C
ATOM   1827  CE2 TYR C 246      35.202  37.486 -61.566  1.00 54.65           C
ANISOU 1827  CE2 TYR C 246     7236   7108   6419    899    596    631       C
ATOM   1828  CZ  TYR C 246      36.060  36.529 -62.064  1.00 54.27           C
ANISOU 1828  CZ  TYR C 246     7227   7095   6300    898    568    582       C
ATOM   1829  OH  TYR C 246      36.570  36.664 -63.335  1.00 53.71           O
ANISOU 1829  OH  TYR C 246     7146   7081   6179    928    581    628       O
ATOM   1830  N   ASN C 247      36.846  38.515 -57.445  1.00 65.33           N
ANISOU 1830  N   ASN C 247     8607   8194   8022    828    682    463       N
ATOM   1831  CA  ASN C 247      37.205  39.907 -57.689  1.00 64.94           C
ANISOU 1831  CA  ASN C 247     8514   8112   8049    852    755    526       C
ATOM   1832  C   ASN C 247      37.264  40.187 -59.188  1.00 66.04           C
ANISOU 1832  C   ASN C 247     8632   8316   8145    892    767    605       C
ATOM   1833  O   ASN C 247      37.988  39.518 -59.925  1.00 66.79           O
ANISOU 1833  O   ASN C 247     8751   8455   8172    903    745    590       O
ATOM   1834  CB  ASN C 247      38.545  40.229 -57.022  1.00 63.95           C
ANISOU 1834  CB  ASN C 247     8395   7926   7976    842    793    477       C
ATOM   1835  CG  ASN C 247      38.837  41.720 -56.965  1.00 64.02           C
ANISOU 1835  CG  ASN C 247     8360   7884   8083    857    872    530       C
ATOM   1836  OD1 ASN C 247      38.582  42.457 -57.918  1.00 64.73           O
ANISOU 1836  OD1 ASN C 247     8415   7998   8182    890    905    614       O
ATOM   1837  ND2 ASN C 247      39.380  42.169 -55.839  1.00 63.13           N
ANISOU 1837  ND2 ASN C 247     8245   7698   8042    831    905    481       N
ATOM   1838  N   LYS C 248      36.499  41.180 -59.630  1.00 47.40           N
ANISOU 1838  N   LYS C 248     6225   5960   5823    915    802    692       N
ATOM   1839  CA  LYS C 248      36.389  41.495 -61.051  1.00 47.27           C
ANISOU 1839  CA  LYS C 248     6185   6012   5765    953    812    778       C
ATOM   1840  C   LYS C 248      37.683  42.049 -61.643  1.00 48.10           C
ANISOU 1840  C   LYS C 248     6279   6108   5887    978    861    799       C
ATOM   1841  O   LYS C 248      37.906  41.959 -62.850  1.00 48.88           O
ANISOU 1841  O   LYS C 248     6373   6272   5927   1005    858    846       O
ATOM   1842  CB  LYS C 248      35.242  42.480 -61.295  1.00 46.38           C
ANISOU 1842  CB  LYS C 248     6021   5903   5700    973    842    870       C
ATOM   1843  CG  LYS C 248      33.864  41.936 -60.952  1.00 46.52           C
ANISOU 1843  CG  LYS C 248     6042   5944   5690    954    791    865       C
ATOM   1844  CD  LYS C 248      32.781  42.966 -61.231  1.00 46.49           C
ANISOU 1844  CD  LYS C 248     5984   5944   5738    977    826    964       C
ATOM   1845  CE  LYS C 248      31.400  42.422 -60.903  1.00 46.46           C
ANISOU 1845  CE  LYS C 248     5981   5966   5707    958    775    960       C
ATOM   1846  NZ  LYS C 248      30.332  43.435 -61.132  0.00 46.33           N
ANISOU 1846  NZ  LYS C 248     5908   5950   5746    981    810   1058       N
ATOM   1847  N   LEU C 249      38.534  42.619 -60.795  1.00 60.55           N
ANISOU 1847  N   LEU C 249     7854   7608   7545    966    907    762       N
ATOM   1848  CA  LEU C 249      39.766  43.243 -61.271  1.00 60.63           C
ANISOU 1848  CA  LEU C 249     7851   7602   7584    987    959    783       C
ATOM   1849  C   LEU C 249      40.961  42.290 -61.303  1.00 60.48           C
ANISOU 1849  C   LEU C 249     7875   7596   7509    977    931    709       C
ATOM   1850  O   LEU C 249      41.906  42.501 -62.063  1.00 60.89           O
ANISOU 1850  O   LEU C 249     7922   7665   7550   1000    958    732       O
ATOM   1851  CB  LEU C 249      40.103  44.493 -60.452  1.00 60.18           C
ANISOU 1851  CB  LEU C 249     7763   7456   7648    982   1032    792       C
ATOM   1852  CG  LEU C 249      39.188  45.704 -60.652  1.00 60.28           C
ANISOU 1852  CG  LEU C 249     7723   7450   7730   1003   1082    883       C
ATOM   1853  CD1 LEU C 249      38.095  45.750 -59.593  1.00 59.87           C
ANISOU 1853  CD1 LEU C 249     7669   7358   7720    976   1070    860       C
ATOM   1854  CD2 LEU C 249      39.993  46.996 -60.663  1.00 59.79           C
ANISOU 1854  CD2 LEU C 249     7625   7329   7764   1019   1167    922       C
ATOM   1855  N   THR C 250      40.922  41.244 -60.483  1.00 63.38           N
ANISOU 1855  N   THR C 250     8283   7954   7845    944    879    623       N
ATOM   1856  CA  THR C 250      42.015  40.276 -60.454  1.00 63.04           C
ANISOU 1856  CA  THR C 250     8281   7921   7751    935    851    552       C
ATOM   1857  C   THR C 250      41.612  38.959 -61.117  1.00 63.34           C
ANISOU 1857  C   THR C 250     8355   8034   7679    934    782    530       C
ATOM   1858  O   THR C 250      42.443  38.070 -61.307  1.00 63.15           O
ANISOU 1858  O   THR C 250     8363   8028   7601    931    757    479       O
ATOM   1859  CB  THR C 250      42.515  40.015 -59.019  1.00 62.46           C
ANISOU 1859  CB  THR C 250     8228   7780   7724    897    845    466       C
ATOM   1860  OG1 THR C 250      43.841  39.474 -59.063  1.00 63.03           O
ANISOU 1860  OG1 THR C 250     8324   7851   7773    896    842    416       O
ATOM   1861  CG2 THR C 250      41.599  39.044 -58.299  1.00 62.01           C
ANISOU 1861  CG2 THR C 250     8201   7730   7630    867    784    413       C
ATOM   1862  N   PHE C 251      40.330  38.850 -61.458  1.00 42.02           N
ANISOU 1862  N   PHE C 251     5645   5375   4946    937    754    569       N
ATOM   1863  CA  PHE C 251      39.801  37.720 -62.224  1.00 41.93           C
ANISOU 1863  CA  PHE C 251     5661   5441   4829    937    693    559       C
ATOM   1864  C   PHE C 251      39.980  36.359 -61.549  1.00 41.76           C
ANISOU 1864  C   PHE C 251     5692   5414   4763    905    636    462       C
ATOM   1865  O   PHE C 251      40.127  35.341 -62.225  1.00 41.93           O
ANISOU 1865  O   PHE C 251     5744   5490   4699    906    596    436       O
ATOM   1866  CB  PHE C 251      40.401  37.695 -63.635  1.00 41.77           C
ANISOU 1866  CB  PHE C 251     5637   5486   4748    969    703    602       C
ATOM   1867  CG  PHE C 251      40.068  38.908 -64.457  1.00 42.10           C
ANISOU 1867  CG  PHE C 251     5628   5548   4819   1002    751    707       C
ATOM   1868  CD1 PHE C 251      40.853  40.048 -64.386  1.00 42.22           C
ANISOU 1868  CD1 PHE C 251     5613   5515   4915   1020    820    744       C
ATOM   1869  CD2 PHE C 251      38.971  38.907 -65.303  1.00 42.18           C
ANISOU 1869  CD2 PHE C 251     5620   5629   4778   1015    729    771       C
ATOM   1870  CE1 PHE C 251      40.548  41.165 -65.141  1.00 42.47           C
ANISOU 1870  CE1 PHE C 251     5596   5563   4978   1053    866    844       C
ATOM   1871  CE2 PHE C 251      38.661  40.021 -66.062  1.00 42.41           C
ANISOU 1871  CE2 PHE C 251     5599   5679   4834   1048    773    873       C
ATOM   1872  CZ  PHE C 251      39.451  41.151 -65.981  1.00 42.55           C
ANISOU 1872  CZ  PHE C 251     5587   5644   4935   1067    843    911       C
ATOM   1873  N   GLN C 252      39.961  36.345 -60.220  1.00 53.86           N
ANISOU 1873  N   GLN C 252     7233   6880   6352    876    635    409       N
ATOM   1874  CA  GLN C 252      40.039  35.095 -59.470  1.00 53.24           C
ANISOU 1874  CA  GLN C 252     7199   6792   6238    845    582    322       C
ATOM   1875  C   GLN C 252      39.428  35.241 -58.080  1.00 53.48           C
ANISOU 1875  C   GLN C 252     7229   6765   6328    814    576    289       C
ATOM   1876  O   GLN C 252      39.119  36.349 -57.641  1.00 53.39           O
ANISOU 1876  O   GLN C 252     7181   6711   6391    815    619    326       O
ATOM   1877  CB  GLN C 252      41.487  34.603 -59.370  1.00 52.28           C
ANISOU 1877  CB  GLN C 252     7103   6653   6107    845    588    267       C
ATOM   1878  CG  GLN C 252      42.421  35.545 -58.632  1.00 52.44           C
ANISOU 1878  CG  GLN C 252     7102   6606   6216    843    642    262       C
ATOM   1879  CD  GLN C 252      43.872  35.111 -58.714  1.00 52.52           C
ANISOU 1879  CD  GLN C 252     7132   6609   6214    848    650    220       C
ATOM   1880  OE1 GLN C 252      44.175  33.918 -58.753  1.00 52.13           O
ANISOU 1880  OE1 GLN C 252     7121   6581   6105    840    607    166       O
ATOM   1881  NE2 GLN C 252      44.778  36.082 -58.749  1.00 52.85           N
ANISOU 1881  NE2 GLN C 252     7147   6619   6315    862    707    244       N
ATOM   1882  N   LEU C 253      39.252  34.116 -57.396  1.00 54.67           N
ANISOU 1882  N   LEU C 253     7417   6911   6446    785    525    219       N
ATOM   1883  CA  LEU C 253      38.659  34.112 -56.063  1.00 54.10           C
ANISOU 1883  CA  LEU C 253     7348   6789   6420    753    515    182       C
ATOM   1884  C   LEU C 253      39.606  34.696 -55.021  1.00 53.67           C
ANISOU 1884  C   LEU C 253     7287   6665   6442    739    554    149       C
ATOM   1885  O   LEU C 253      40.724  34.213 -54.840  1.00 53.34           O
ANISOU 1885  O   LEU C 253     7266   6612   6390    735    551    102       O
ATOM   1886  CB  LEU C 253      38.243  32.693 -55.667  1.00 53.43           C
ANISOU 1886  CB  LEU C 253     7306   6721   6275    727    449    119       C
ATOM   1887  CG  LEU C 253      37.004  32.131 -56.367  1.00 53.82           C
ANISOU 1887  CG  LEU C 253     7360   6830   6261    728    405    144       C
ATOM   1888  CD1 LEU C 253      36.959  30.617 -56.247  1.00 52.81           C
ANISOU 1888  CD1 LEU C 253     7278   6723   6064    708    345     78       C
ATOM   1889  CD2 LEU C 253      35.739  32.749 -55.788  1.00 54.44           C
ANISOU 1889  CD2 LEU C 253     7411   6890   6383    716    409    176       C
ATOM   1890  N   GLU C 254      39.147  35.741 -54.341  1.00 75.45           N
ANISOU 1890  N   GLU C 254    10014   9378   9276    731    593    172       N
ATOM   1891  CA  GLU C 254      39.922  36.384 -53.287  1.00 74.84           C
ANISOU 1891  CA  GLU C 254     9926   9234   9274    713    633    139       C
ATOM   1892  C   GLU C 254      39.215  36.216 -51.945  1.00 74.33           C
ANISOU 1892  C   GLU C 254     9870   9131   9240    675    615     94       C
ATOM   1893  O   GLU C 254      37.989  36.112 -51.900  1.00 75.06           O
ANISOU 1893  O   GLU C 254     9959   9237   9323    670    594    114       O
ATOM   1894  CB  GLU C 254      40.117  37.869 -53.604  1.00 75.49           C
ANISOU 1894  CB  GLU C 254     9964   9289   9430    733    704    201       C
ATOM   1895  CG  GLU C 254      41.086  38.141 -54.745  1.00 76.47           C
ANISOU 1895  CG  GLU C 254    10079   9440   9537    767    731    238       C
ATOM   1896  CD  GLU C 254      42.532  37.893 -54.356  1.00 76.63           C
ANISOU 1896  CD  GLU C 254    10115   9436   9566    758    740    184       C
ATOM   1897  OE1 GLU C 254      42.856  38.013 -53.156  1.00 76.23           O
ANISOU 1897  OE1 GLU C 254    10067   9334   9563    727    748    132       O
ATOM   1898  OE2 GLU C 254      43.345  37.578 -55.251  1.00 77.04           O
ANISOU 1898  OE2 GLU C 254    10175   9522   9575    781    739    193       O
ATOM   1899  N   PRO C 255      39.986  36.180 -50.846  1.00 49.57           N
ANISOU 1899  N   PRO C 255     6745   5950   6141    648    623     35       N
ATOM   1900  CA  PRO C 255      39.400  36.040 -49.508  1.00 48.52           C
ANISOU 1900  CA  PRO C 255     6619   5780   6036    610    609    -11       C
ATOM   1901  C   PRO C 255      38.482  37.206 -49.148  1.00 48.56           C
ANISOU 1901  C   PRO C 255     6588   5751   6112    606    653     29       C
ATOM   1902  O   PRO C 255      38.876  38.366 -49.261  1.00 48.66           O
ANISOU 1902  O   PRO C 255     6569   5733   6188    617    714     61       O
ATOM   1903  CB  PRO C 255      40.626  36.021 -48.587  1.00 47.50           C
ANISOU 1903  CB  PRO C 255     6497   5613   5936    587    622    -70       C
ATOM   1904  CG  PRO C 255      41.724  36.642 -49.386  1.00 47.95           C
ANISOU 1904  CG  PRO C 255     6537   5671   6010    614    664    -41       C
ATOM   1905  CD  PRO C 255      41.457  36.234 -50.797  1.00 48.99           C
ANISOU 1905  CD  PRO C 255     6674   5860   6079    650    644      7       C
ATOM   1906  N   ASN C 256      37.265  36.884 -48.722  1.00 59.35           N
ANISOU 1906  N   ASN C 256     7959   7122   7468    591    624     26       N
ATOM   1907  CA  ASN C 256      36.277  37.890 -48.348  1.00 60.05           C
ANISOU 1907  CA  ASN C 256     8016   7179   7622    587    663     62       C
ATOM   1908  C   ASN C 256      36.578  38.491 -46.978  1.00 59.83           C
ANISOU 1908  C   ASN C 256     7980   7087   7665    552    699     15       C
ATOM   1909  O   ASN C 256      36.798  37.760 -46.013  1.00 59.69           O
ANISOU 1909  O   ASN C 256     7990   7059   7630    520    667    -51       O
ATOM   1910  CB  ASN C 256      34.877  37.272 -48.349  1.00 60.85           C
ANISOU 1910  CB  ASN C 256     8126   7310   7686    581    617     74       C
ATOM   1911  CG  ASN C 256      33.781  38.297 -48.126  1.00 61.69           C
ANISOU 1911  CG  ASN C 256     8194   7389   7855    583    658    122       C
ATOM   1912  OD1 ASN C 256      33.782  39.369 -48.731  1.00 62.44           O
ANISOU 1912  OD1 ASN C 256     8254   7475   7997    610    710    183       O
ATOM   1913  ND2 ASN C 256      32.838  37.971 -47.251  1.00 61.52           N
ANISOU 1913  ND2 ASN C 256     8181   7355   7839    556    635     95       N
ATOM   1914  N   PRO C 257      36.599  39.830 -46.892  1.00 62.56           N
ANISOU 1914  N   PRO C 257     8289   7390   8092    558    768     49       N
ATOM   1915  CA  PRO C 257      36.853  40.526 -45.626  1.00 61.80           C
ANISOU 1915  CA  PRO C 257     8182   7231   8067    523    810      4       C
ATOM   1916  C   PRO C 257      35.747  40.300 -44.598  1.00 61.69           C
ANISOU 1916  C   PRO C 257     8175   7200   8063    493    792    -24       C
ATOM   1917  O   PRO C 257      36.014  40.321 -43.397  1.00 60.89           O
ANISOU 1917  O   PRO C 257     8082   7063   7989    454    799    -85       O
ATOM   1918  CB  PRO C 257      36.884  42.002 -46.038  1.00 61.80           C
ANISOU 1918  CB  PRO C 257     8138   7195   8149    544    889     62       C
ATOM   1919  CG  PRO C 257      37.188  41.990 -47.496  1.00 62.85           C
ANISOU 1919  CG  PRO C 257     8263   7372   8246    589    887    126       C
ATOM   1920  CD  PRO C 257      36.516  40.764 -48.026  1.00 63.45           C
ANISOU 1920  CD  PRO C 257     8366   7511   8231    598    814    130       C
ATOM   1921  N   HIS C 258      34.521  40.087 -45.068  1.00 71.31           N
ANISOU 1921  N   HIS C 258     9389   8447   9260    508    769     20       N
ATOM   1922  CA  HIS C 258      33.375  39.927 -44.177  1.00 71.14           C
ANISOU 1922  CA  HIS C 258     9370   8410   9250    482    755      1       C
ATOM   1923  C   HIS C 258      33.155  38.471 -43.774  1.00 70.65           C
ANISOU 1923  C   HIS C 258     9350   8383   9111    461    678    -50       C
ATOM   1924  O   HIS C 258      32.080  38.111 -43.297  1.00 70.40           O
ANISOU 1924  O   HIS C 258     9323   8354   9070    446    653    -56       O
ATOM   1925  CB  HIS C 258      32.106  40.477 -44.835  1.00 72.21           C
ANISOU 1925  CB  HIS C 258     9474   8556   9405    509    772     77       C
ATOM   1926  CG  HIS C 258      32.220  41.902 -45.275  1.00 72.63           C
ANISOU 1926  CG  HIS C 258     9485   8575   9538    533    849    136       C
ATOM   1927  ND1 HIS C 258      32.607  42.258 -46.557  1.00 73.52           N
ANISOU 1927  ND1 HIS C 258     9578   8715   9640    574    865    200       N
ATOM   1928  CD2 HIS C 258      32.002  43.060 -44.619  1.00 72.31           C
ANISOU 1928  CD2 HIS C 258     9413   8472   9588    522    917    141       C
ATOM   1929  CE1 HIS C 258      32.618  43.568 -46.658  1.00 73.40           C
ANISOU 1929  CE1 HIS C 258     9524   8656   9709    588    940    245       C
ATOM   1930  NE2 HIS C 258      32.255  44.089 -45.497  1.00 72.81           N
ANISOU 1930  NE2 HIS C 258     9441   8525   9699    557    974    210       N
ATOM   1931  N   THR C 259      34.179  37.645 -43.962  1.00 59.07           N
ANISOU 1931  N   THR C 259     7912   6940   7592    460    643    -86       N
ATOM   1932  CA  THR C 259      34.085  36.211 -43.699  1.00 58.78           C
ANISOU 1932  CA  THR C 259     7916   6936   7482    444    571   -131       C
ATOM   1933  C   THR C 259      33.744  35.881 -42.245  1.00 57.86           C
ANISOU 1933  C   THR C 259     7814   6791   7379    401    557   -191       C
ATOM   1934  O   THR C 259      34.353  36.408 -41.315  1.00 57.19           O
ANISOU 1934  O   THR C 259     7724   6667   7341    376    590   -229       O
ATOM   1935  CB  THR C 259      35.395  35.487 -44.083  1.00 58.29           C
ANISOU 1935  CB  THR C 259     7879   6897   7373    452    547   -161       C
ATOM   1936  OG1 THR C 259      35.635  35.643 -45.487  1.00 59.44           O
ANISOU 1936  OG1 THR C 259     8015   7077   7494    492    553   -106       O
ATOM   1937  CG2 THR C 259      35.313  34.005 -43.751  1.00 57.41           C
ANISOU 1937  CG2 THR C 259     7809   6813   7192    435    477   -209       C
ATOM   1938  N   LYS C 260      32.755  35.010 -42.065  1.00 40.67           N
ANISOU 1938  N   LYS C 260     5656   4638   5161    390    507   -199       N
ATOM   1939  CA  LYS C 260      32.411  34.481 -40.751  1.00 39.54           C
ANISOU 1939  CA  LYS C 260     5531   4476   5016    350    484   -255       C
ATOM   1940  C   LYS C 260      32.201  32.973 -40.837  1.00 39.58           C
ANISOU 1940  C   LYS C 260     5574   4521   4944    344    410   -281       C
ATOM   1941  O   LYS C 260      31.826  32.451 -41.886  1.00 39.85           O
ANISOU 1941  O   LYS C 260     5614   4595   4930    369    380   -248       O
ATOM   1942  CB  LYS C 260      31.162  35.167 -40.193  1.00 39.58           C
ANISOU 1942  CB  LYS C 260     5513   4455   5070    337    511   -236       C
ATOM   1943  CG  LYS C 260      31.389  36.608 -39.767  1.00 39.38           C
ANISOU 1943  CG  LYS C 260     5454   4379   5130    333    587   -228       C
ATOM   1944  CD  LYS C 260      30.149  37.199 -39.120  1.00 39.57           C
ANISOU 1944  CD  LYS C 260     5458   4375   5203    318    614   -216       C
ATOM   1945  CE  LYS C 260      30.416  38.602 -38.600  1.00 39.38           C
ANISOU 1945  CE  LYS C 260     5402   4294   5267    309    694   -216       C
ATOM   1946  NZ  LYS C 260      29.210  39.198 -37.962  0.00 39.38           N
ANISOU 1946  NZ  LYS C 260     5381   4262   5318    295    725   -205       N
ATOM   1947  N   TYR C 261      32.444  32.276 -39.732  1.00 55.07           N
ANISOU 1947  N   TYR C 261     7560   6472   6893    311    383   -340       N
ATOM   1948  CA  TYR C 261      32.372  30.819 -39.726  1.00 54.49           C
ANISOU 1948  CA  TYR C 261     7523   6430   6751    304    317   -369       C
ATOM   1949  C   TYR C 261      31.196  30.299 -38.906  1.00 54.25           C
ANISOU 1949  C   TYR C 261     7503   6397   6713    277    288   -386       C
ATOM   1950  O   TYR C 261      30.631  31.020 -38.084  1.00 54.04           O
ANISOU 1950  O   TYR C 261     7458   6339   6734    257    319   -389       O
ATOM   1951  CB  TYR C 261      33.686  30.223 -39.219  1.00 53.45           C
ANISOU 1951  CB  TYR C 261     7414   6295   6602    291    302   -419       C
ATOM   1952  CG  TYR C 261      34.899  30.734 -39.962  1.00 54.03           C
ANISOU 1952  CG  TYR C 261     7476   6368   6684    316    332   -405       C
ATOM   1953  CD1 TYR C 261      35.742  31.677 -39.390  1.00 53.81           C
ANISOU 1953  CD1 TYR C 261     7429   6308   6710    305    381   -420       C
ATOM   1954  CD2 TYR C 261      35.191  30.285 -41.244  1.00 54.78           C
ANISOU 1954  CD2 TYR C 261     7580   6498   6735    350    314   -377       C
ATOM   1955  CE1 TYR C 261      36.850  32.151 -40.069  1.00 54.32           C
ANISOU 1955  CE1 TYR C 261     7482   6373   6786    327    409   -406       C
ATOM   1956  CE2 TYR C 261      36.296  30.753 -41.930  1.00 55.05           C
ANISOU 1956  CE2 TYR C 261     7604   6534   6778    374    343   -363       C
ATOM   1957  CZ  TYR C 261      37.121  31.685 -41.338  1.00 54.93           C
ANISOU 1957  CZ  TYR C 261     7568   6484   6818    362    391   -376       C
ATOM   1958  OH  TYR C 261      38.222  32.154 -42.018  1.00 55.32           O
ANISOU 1958  OH  TYR C 261     7606   6534   6878    385    421   -361       O
ATOM   1959  N   GLN C 262      30.839  29.040 -39.138  1.00 54.48           N
ANISOU 1959  N   GLN C 262     7561   6456   6682    275    230   -398       N
ATOM   1960  CA  GLN C 262      29.678  28.435 -38.495  1.00 54.01           C
ANISOU 1960  CA  GLN C 262     7512   6399   6610    252    198   -410       C
ATOM   1961  C   GLN C 262      30.025  27.782 -37.162  1.00 52.46           C
ANISOU 1961  C   GLN C 262     7338   6185   6408    216    177   -468       C
ATOM   1962  O   GLN C 262      30.727  26.772 -37.119  1.00 52.14           O
ANISOU 1962  O   GLN C 262     7326   6158   6327    213    141   -498       O
ATOM   1963  CB  GLN C 262      29.036  27.400 -39.423  1.00 54.36           C
ANISOU 1963  CB  GLN C 262     7576   6487   6593    266    146   -393       C
ATOM   1964  CG  GLN C 262      28.603  27.951 -40.772  1.00 56.09           C
ANISOU 1964  CG  GLN C 262     7771   6732   6806    300    159   -333       C
ATOM   1965  CD  GLN C 262      28.048  26.876 -41.689  1.00 56.56           C
ANISOU 1965  CD  GLN C 262     7852   6839   6801    309    106   -323       C
ATOM   1966  OE1 GLN C 262      27.818  25.742 -41.267  1.00 54.88           O
ANISOU 1966  OE1 GLN C 262     7667   6632   6551    289     61   -360       O
ATOM   1967  NE2 GLN C 262      27.833  27.228 -42.952  1.00 58.02           N
ANISOU 1967  NE2 GLN C 262     8020   7058   6969    339    113   -274       N
ATOM   1968  N   TYR C 263      29.528  28.366 -36.078  1.00 60.69           N
ANISOU 1968  N   TYR C 263     8366   7198   7493    188    203   -482       N
ATOM   1969  CA  TYR C 263      29.640  27.760 -34.758  1.00 60.02           C
ANISOU 1969  CA  TYR C 263     8301   7102   7403    151    182   -533       C
ATOM   1970  C   TYR C 263      28.240  27.556 -34.197  1.00 60.35           C
ANISOU 1970  C   TYR C 263     8342   7141   7448    132    168   -530       C
ATOM   1971  O   TYR C 263      27.680  28.447 -33.559  1.00 60.40           O
ANISOU 1971  O   TYR C 263     8327   7122   7502    116    207   -527       O
ATOM   1972  CB  TYR C 263      30.471  28.637 -33.821  1.00 60.02           C
ANISOU 1972  CB  TYR C 263     8285   7070   7448    130    227   -562       C
ATOM   1973  CG  TYR C 263      30.744  28.010 -32.470  1.00 59.45           C
ANISOU 1973  CG  TYR C 263     8232   6992   7365     92    206   -614       C
ATOM   1974  CD1 TYR C 263      31.749  27.065 -32.312  1.00 59.02           C
ANISOU 1974  CD1 TYR C 263     8201   6953   7271     89    170   -642       C
ATOM   1975  CD2 TYR C 263      30.002  28.369 -31.352  1.00 59.23           C
ANISOU 1975  CD2 TYR C 263     8196   6944   7364     59    222   -632       C
ATOM   1976  CE1 TYR C 263      32.004  26.490 -31.080  1.00 58.09           C
ANISOU 1976  CE1 TYR C 263     8097   6833   7141     55    150   -684       C
ATOM   1977  CE2 TYR C 263      30.251  27.800 -30.116  1.00 58.39           C
ANISOU 1977  CE2 TYR C 263     8105   6838   7243     23    202   -677       C
ATOM   1978  CZ  TYR C 263      31.252  26.862 -29.986  1.00 57.79           C
ANISOU 1978  CZ  TYR C 263     8051   6779   7127     21    165   -702       C
ATOM   1979  OH  TYR C 263      31.502  26.293 -28.758  0.00 56.98           O
ANISOU 1979  OH  TYR C 263     7961   6679   7009    -13    145   -742       O
ATOM   1980  N   GLY C 264      27.675  26.379 -34.447  1.00 54.49           N
ANISOU 1980  N   GLY C 264     7623   6424   6656    131    115   -531       N
ATOM   1981  CA  GLY C 264      26.304  26.100 -34.065  1.00 54.51           C
ANISOU 1981  CA  GLY C 264     7625   6428   6657    115     97   -524       C
ATOM   1982  C   GLY C 264      25.334  26.785 -35.007  1.00 55.82           C
ANISOU 1982  C   GLY C 264     7765   6604   6841    139    115   -469       C
ATOM   1983  O   GLY C 264      25.221  26.412 -36.174  1.00 56.46           O
ANISOU 1983  O   GLY C 264     7849   6716   6888    165     92   -441       O
ATOM   1984  N   GLY C 265      24.638  27.797 -34.500  1.00 52.09           N
ANISOU 1984  N   GLY C 265     7265   6107   6422    130    158   -454       N
ATOM   1985  CA  GLY C 265      23.704  28.559 -35.308  1.00 53.42           C
ANISOU 1985  CA  GLY C 265     7401   6281   6614    153    181   -397       C
ATOM   1986  C   GLY C 265      24.035  30.038 -35.320  1.00 53.92           C
ANISOU 1986  C   GLY C 265     7431   6313   6744    165    251   -375       C
ATOM   1987  O   GLY C 265      23.175  30.874 -35.594  1.00 55.06           O
ANISOU 1987  O   GLY C 265     7543   6449   6928    177    284   -331       O
ATOM   1988  N   VAL C 266      25.289  30.363 -35.017  1.00 58.92           N
ANISOU 1988  N   VAL C 266     8069   6927   7390    161    275   -404       N
ATOM   1989  CA  VAL C 266      25.734  31.751 -34.970  1.00 59.20           C
ANISOU 1989  CA  VAL C 266     8074   6929   7490    168    343   -391       C
ATOM   1990  C   VAL C 266      26.940  31.972 -35.880  1.00 59.52           C
ANISOU 1990  C   VAL C 266     8113   6979   7522    196    353   -378       C
ATOM   1991  O   VAL C 266      27.863  31.158 -35.910  1.00 59.09           O
ANISOU 1991  O   VAL C 266     8087   6942   7425    193    319   -410       O
ATOM   1992  CB  VAL C 266      26.111  32.174 -33.533  1.00 57.89           C
ANISOU 1992  CB  VAL C 266     7908   6724   7362    130    375   -444       C
ATOM   1993  CG1 VAL C 266      26.344  33.676 -33.464  1.00 58.10           C
ANISOU 1993  CG1 VAL C 266     7900   6711   7463    134    451   -428       C
ATOM   1994  CG2 VAL C 266      25.028  31.759 -32.549  1.00 57.36           C
ANISOU 1994  CG2 VAL C 266     7848   6652   7293     99    358   -464       C
ATOM   1995  N   CYS C 267      26.927  33.074 -36.624  1.00 46.74           N
ANISOU 1995  N   CYS C 267     6464   5350   5947    223    402   -330       N
ATOM   1996  CA  CYS C 267      28.047  33.429 -37.488  1.00 46.54           C
ANISOU 1996  CA  CYS C 267     6433   5331   5920    250    420   -313       C
ATOM   1997  C   CYS C 267      29.096  34.217 -36.711  1.00 45.54           C
ANISOU 1997  C   CYS C 267     6298   5163   5842    232    469   -350       C
ATOM   1998  O   CYS C 267      28.860  35.359 -36.317  1.00 45.46           O
ANISOU 1998  O   CYS C 267     6260   5115   5899    225    528   -340       O
ATOM   1999  CB  CYS C 267      27.564  34.242 -38.689  1.00 47.32           C
ANISOU 1999  CB  CYS C 267     6498   5439   6041    289    450   -240       C
ATOM   2000  SG  CYS C 267      26.396  33.371 -39.756  1.00 48.97           S
ANISOU 2000  SG  CYS C 267     6713   5706   6189    311    392   -192       S
ATOM   2001  N   VAL C 268      30.254  33.603 -36.494  1.00 52.10           N
ANISOU 2001  N   VAL C 268     7152   6002   6640    222    445   -392       N
ATOM   2002  CA  VAL C 268      31.322  34.233 -35.726  1.00 51.44           C
ANISOU 2002  CA  VAL C 268     7063   5888   6596    201    485   -432       C
ATOM   2003  C   VAL C 268      32.556  34.515 -36.580  1.00 52.53           C
ANISOU 2003  C   VAL C 268     7195   6031   6732    227    501   -418       C
ATOM   2004  O   VAL C 268      32.855  33.778 -37.520  1.00 53.19           O
ANISOU 2004  O   VAL C 268     7294   6151   6764    253    463   -400       O
ATOM   2005  CB  VAL C 268      31.726  33.373 -34.512  1.00 49.95           C
ANISOU 2005  CB  VAL C 268     6902   5701   6377    161    449   -497       C
ATOM   2006  CG1 VAL C 268      30.608  33.355 -33.483  1.00 49.46           C
ANISOU 2006  CG1 VAL C 268     6839   5623   6329    130    448   -516       C
ATOM   2007  CG2 VAL C 268      32.077  31.959 -34.953  1.00 49.76           C
ANISOU 2007  CG2 VAL C 268     6911   5718   6279    172    381   -507       C
ATOM   2008  N   ALA C 269      33.267  35.587 -36.244  1.00 65.65           N
ANISOU 2008  N   ALA C 269     8835   7658   8451    218    559   -428       N
ATOM   2009  CA  ALA C 269      34.465  35.975 -36.978  1.00 65.89           C
ANISOU 2009  CA  ALA C 269     8856   7690   8489    240    582   -415       C
ATOM   2010  C   ALA C 269      35.638  35.059 -36.645  1.00 65.78           C
ANISOU 2010  C   ALA C 269     8869   7696   8429    227    542   -463       C
ATOM   2011  O   ALA C 269      36.528  34.850 -37.470  1.00 66.24           O
ANISOU 2011  O   ALA C 269     8931   7773   8465    252    535   -449       O
ATOM   2012  CB  ALA C 269      34.822  37.424 -36.681  1.00 65.67           C
ANISOU 2012  CB  ALA C 269     8795   7616   8542    232    658   -413       C
ATOM   2013  N   SER C 270      35.633  34.515 -35.433  1.00 68.90           N
ANISOU 2013  N   SER C 270     9280   8087   8811    188    517   -516       N
ATOM   2014  CA  SER C 270      36.697  33.620 -34.995  1.00 68.91           C
ANISOU 2014  CA  SER C 270     9305   8108   8772    174    479   -560       C
ATOM   2015  C   SER C 270      36.171  32.549 -34.044  1.00 68.83           C
ANISOU 2015  C   SER C 270     9321   8111   8721    145    427   -597       C
ATOM   2016  O   SER C 270      35.345  32.826 -33.174  1.00 68.75           O
ANISOU 2016  O   SER C 270     9306   8083   8732    117    439   -612       O
ATOM   2017  CB  SER C 270      37.824  34.411 -34.329  1.00 68.65           C
ANISOU 2017  CB  SER C 270     9253   8050   8780    150    522   -593       C
ATOM   2018  OG  SER C 270      37.348  35.132 -33.206  1.00 68.52           O
ANISOU 2018  OG  SER C 270     9224   8003   8809    111    556   -622       O
ATOM   2019  N   CYS C 271      36.657  31.325 -34.221  1.00 82.32           N
ANISOU 2019  N   CYS C 271    11057   9850  10372    152    373   -610       N
ATOM   2020  CA  CYS C 271      36.261  30.203 -33.379  1.00 82.09           C
ANISOU 2020  CA  CYS C 271    11054   9834  10301    127    322   -642       C
ATOM   2021  C   CYS C 271      36.848  30.343 -31.977  1.00 81.84           C
ANISOU 2021  C   CYS C 271    11019   9791  10285     84    330   -692       C
ATOM   2022  O   CYS C 271      37.870  31.005 -31.796  1.00 81.94           O
ANISOU 2022  O   CYS C 271    11015   9793  10326     76    363   -707       O
ATOM   2023  CB  CYS C 271      36.714  28.887 -34.014  1.00 81.78           C
ANISOU 2023  CB  CYS C 271    11043   9827  10202    149    267   -640       C
ATOM   2024  SG  CYS C 271      35.978  28.557 -35.626  1.00 83.62           S
ANISOU 2024  SG  CYS C 271    11284  10084  10405    195    250   -588       S
ATOM   2025  N   PRO C 272      36.196  29.724 -30.976  1.00 90.32           N
ANISOU 2025  N   PRO C 272    12108  10869  11341     53    301   -718       N
ATOM   2026  CA  PRO C 272      36.673  29.740 -29.587  1.00 89.93           C
ANISOU 2026  CA  PRO C 272    12057  10816  11297      9    303   -767       C
ATOM   2027  C   PRO C 272      38.083  29.171 -29.411  1.00 90.24           C
ANISOU 2027  C   PRO C 272    12102  10875  11311      7    280   -789       C
ATOM   2028  O   PRO C 272      38.712  28.741 -30.379  1.00 91.00           O
ANISOU 2028  O   PRO C 272    12206  10985  11386     41    265   -769       O
ATOM   2029  CB  PRO C 272      35.655  28.856 -28.864  1.00 89.33           C
ANISOU 2029  CB  PRO C 272    12001  10750  11191    -11    262   -779       C
ATOM   2030  CG  PRO C 272      34.410  29.006 -29.659  1.00 89.71           C
ANISOU 2030  CG  PRO C 272    12049  10792  11246     13    266   -740       C
ATOM   2031  CD  PRO C 272      34.862  29.107 -31.087  1.00 90.31           C
ANISOU 2031  CD  PRO C 272    12121  10875  11316     57    270   -702       C
ATOM   2032  N   HIS C 273      38.557  29.167 -28.168  0.00 84.28           N
ANISOU 2032  N   HIS C 273    11343  10123  10556    -34    279   -830       N
ATOM   2033  CA  HIS C 273      39.932  28.790 -27.841  1.00 83.85           C
ANISOU 2033  CA  HIS C 273    11287  10087  10485    -42    264   -852       C
ATOM   2034  C   HIS C 273      40.347  27.417 -28.370  1.00 83.47           C
ANISOU 2034  C   HIS C 273    11265  10065  10386    -14    209   -840       C
ATOM   2035  O   HIS C 273      41.398  27.281 -28.997  1.00 83.63           O
ANISOU 2035  O   HIS C 273    11283  10094  10400      9    207   -832       O
ATOM   2036  CB  HIS C 273      40.151  28.853 -26.327  0.00 83.34           C
ANISOU 2036  CB  HIS C 273    11216  10029  10420    -94    263   -897       C
ATOM   2037  CG  HIS C 273      39.885  30.200 -25.736  0.00 83.29           C
ANISOU 2037  CG  HIS C 273    11185   9997  10465   -126    321   -918       C
ATOM   2038  ND1 HIS C 273      40.880  31.137 -25.534  0.00 83.45           N
ANISOU 2038  ND1 HIS C 273    11180  10009  10519   -143    363   -938       N
ATOM   2039  CD2 HIS C 273      38.739  30.777 -25.303  0.00 83.13           C
ANISOU 2039  CD2 HIS C 273    11160   9955  10470   -145    348   -923       C
ATOM   2040  CE1 HIS C 273      40.357  32.225 -25.003  0.00 83.35           C
ANISOU 2040  CE1 HIS C 273    11150   9969  10551   -172    413   -956       C
ATOM   2041  NE2 HIS C 273      39.057  32.034 -24.852  0.00 83.16           N
ANISOU 2041  NE2 HIS C 273    11138   9936  10524   -172    406   -947       N
ATOM   2042  N   ASN C 274      39.526  26.405 -28.116  1.00104.66           N
ANISOU 2042  N   ASN C 274    13972  12758  13034    -16    166   -839       N
ATOM   2043  CA  ASN C 274      39.846  25.047 -28.546  1.00104.16           C
ANISOU 2043  CA  ASN C 274    13935  12717  12926      7    115   -830       C
ATOM   2044  C   ASN C 274      39.004  24.580 -29.727  1.00104.16           C
ANISOU 2044  C   ASN C 274    13953  12716  12907     43     99   -798       C
ATOM   2045  O   ASN C 274      38.436  23.488 -29.704  1.00104.01           O
ANISOU 2045  O   ASN C 274    13958  12706  12853     46     56   -796       O
ATOM   2046  CB  ASN C 274      39.715  24.066 -27.379  1.00103.46           C
ANISOU 2046  CB  ASN C 274    13861  12643  12806    -22     74   -854       C
ATOM   2047  CG  ASN C 274      40.692  24.361 -26.259  0.00103.46           C
ANISOU 2047  CG  ASN C 274    13844  12654  12814    -57     83   -884       C
ATOM   2048  OD1 ASN C 274      41.853  23.956 -26.310  0.00103.65           O
ANISOU 2048  OD1 ASN C 274    13864  12693  12825    -48     70   -887       O
ATOM   2049  ND2 ASN C 274      40.224  25.069 -25.238  0.00103.26           N
ANISOU 2049  ND2 ASN C 274    13805  12622  12809    -98    105   -908       N
ATOM   2050  N   PHE C 275      38.929  25.412 -30.758  1.00 83.79           N
ANISOU 2050  N   PHE C 275    11360  10125  10350     70    132   -771       N
ATOM   2051  CA  PHE C 275      38.191  25.065 -31.965  1.00 83.63           C
ANISOU 2051  CA  PHE C 275    11353  10111  10311    104    119   -738       C
ATOM   2052  C   PHE C 275      38.962  25.446 -33.221  1.00 83.48           C
ANISOU 2052  C   PHE C 275    11326  10095  10296    142    140   -713       C
ATOM   2053  O   PHE C 275      39.506  26.546 -33.322  1.00 83.80           O
ANISOU 2053  O   PHE C 275    11342  10123  10375    143    185   -708       O
ATOM   2054  CB  PHE C 275      36.813  25.727 -31.969  1.00 84.15           C
ANISOU 2054  CB  PHE C 275    11410  10163  10400     97    138   -721       C
ATOM   2055  CG  PHE C 275      35.804  25.031 -31.102  1.00 83.70           C
ANISOU 2055  CG  PHE C 275    11368  10107  10325     70    106   -737       C
ATOM   2056  CD1 PHE C 275      35.632  25.403 -29.779  1.00 83.46           C
ANISOU 2056  CD1 PHE C 275    11330  10067  10316     30    119   -765       C
ATOM   2057  CD2 PHE C 275      35.029  24.002 -31.610  1.00 83.19           C
ANISOU 2057  CD2 PHE C 275    11328  10057  10223     84     64   -724       C
ATOM   2058  CE1 PHE C 275      34.705  24.762 -28.980  1.00 83.02           C
ANISOU 2058  CE1 PHE C 275    11287  10013  10242      6     91   -778       C
ATOM   2059  CE2 PHE C 275      34.101  23.357 -30.817  1.00 82.66           C
ANISOU 2059  CE2 PHE C 275    11274   9990  10141     59     36   -737       C
ATOM   2060  CZ  PHE C 275      33.938  23.737 -29.500  1.00 82.63           C
ANISOU 2060  CZ  PHE C 275    11262   9976  10159     21     49   -762       C
ATOM   2061  N   VAL C 276      39.007  24.524 -34.176  1.00 53.19           N
ANISOU 2061  N   VAL C 276     7512   6278   6421    172    109   -699       N
ATOM   2062  CA  VAL C 276      39.663  24.777 -35.451  1.00 53.20           C
ANISOU 2062  CA  VAL C 276     7509   6287   6420    209    126   -674       C
ATOM   2063  C   VAL C 276      38.635  25.012 -36.549  1.00 53.39           C
ANISOU 2063  C   VAL C 276     7532   6318   6435    233    131   -637       C
ATOM   2064  O   VAL C 276      37.480  24.596 -36.436  1.00 53.07           O
ANISOU 2064  O   VAL C 276     7504   6281   6379    225    107   -633       O
ATOM   2065  CB  VAL C 276      40.583  23.610 -35.856  1.00 52.62           C
ANISOU 2065  CB  VAL C 276     7458   6230   6306    229     93   -684       C
ATOM   2066  CG1 VAL C 276      41.782  23.534 -34.924  1.00 52.44           C
ANISOU 2066  CG1 VAL C 276     7427   6204   6295    211     95   -712       C
ATOM   2067  CG2 VAL C 276      39.812  22.299 -35.855  1.00 51.72           C
ANISOU 2067  CG2 VAL C 276     7374   6126   6149    227     44   -691       C
ATOM   2068  N   VAL C 277      39.059  25.688 -37.611  1.00 51.68           N
ANISOU 2068  N   VAL C 277     7302   6106   6229    263    161   -607       N
ATOM   2069  CA  VAL C 277      38.183  25.939 -38.745  1.00 52.21           C
ANISOU 2069  CA  VAL C 277     7366   6187   6286    288    166   -567       C
ATOM   2070  C   VAL C 277      38.413  24.915 -39.849  1.00 52.29           C
ANISOU 2070  C   VAL C 277     7400   6225   6241    317    133   -560       C
ATOM   2071  O   VAL C 277      39.463  24.907 -40.495  1.00 52.51           O
ANISOU 2071  O   VAL C 277     7428   6262   6263    340    145   -556       O
ATOM   2072  CB  VAL C 277      38.391  27.349 -39.330  1.00 52.77           C
ANISOU 2072  CB  VAL C 277     7403   6246   6400    305    222   -532       C
ATOM   2073  CG1 VAL C 277      37.320  27.649 -40.365  1.00 53.56           C
ANISOU 2073  CG1 VAL C 277     7496   6362   6491    328    226   -486       C
ATOM   2074  CG2 VAL C 277      38.366  28.387 -38.228  1.00 52.56           C
ANISOU 2074  CG2 VAL C 277     7352   6187   6431    276    261   -546       C
ATOM   2075  N   ASP C 278      37.432  24.041 -40.050  1.00 75.14           N
ANISOU 2075  N   ASP C 278    10317   9136   9099    315     94   -560       N
ATOM   2076  CA  ASP C 278      37.408  23.182 -41.226  1.00 75.89           C
ANISOU 2076  CA  ASP C 278    10433   9260   9143    340     67   -551       C
ATOM   2077  C   ASP C 278      36.287  23.598 -42.173  1.00 77.45           C
ANISOU 2077  C   ASP C 278    10620   9478   9328    354     71   -510       C
ATOM   2078  O   ASP C 278      35.134  23.721 -41.750  1.00 77.79           O
ANISOU 2078  O   ASP C 278    10657   9518   9380    337     62   -503       O
ATOM   2079  CB  ASP C 278      37.167  21.726 -40.836  1.00 75.39           C
ANISOU 2079  CB  ASP C 278    10404   9202   9040    326     17   -585       C
ATOM   2080  CG  ASP C 278      37.276  20.781 -42.020  1.00 75.90           C
ANISOU 2080  CG  ASP C 278    10492   9293   9051    350     -8   -583       C
ATOM   2081  OD1 ASP C 278      38.131  21.025 -42.899  1.00 76.75           O
ANISOU 2081  OD1 ASP C 278    10596   9414   9153    377     12   -571       O
ATOM   2082  OD2 ASP C 278      36.507  19.798 -42.075  1.00 75.28           O
ANISOU 2082  OD2 ASP C 278    10438   9226   8940    341    -46   -596       O
ATOM   2083  N   GLN C 279      36.632  23.821 -43.440  1.00 60.36           N
ANISOU 2083  N   GLN C 279     8451   7338   7145    386     84   -482       N
ATOM   2084  CA  GLN C 279      35.671  24.303 -44.431  1.00 61.30           C
ANISOU 2084  CA  GLN C 279     8556   7485   7253    402     90   -436       C
ATOM   2085  C   GLN C 279      35.120  25.645 -43.960  1.00 61.64           C
ANISOU 2085  C   GLN C 279     8563   7505   7354    395    131   -406       C
ATOM   2086  O   GLN C 279      35.841  26.640 -43.853  1.00 62.19           O
ANISOU 2086  O   GLN C 279     8609   7554   7467    402    175   -394       O
ATOM   2087  CB  GLN C 279      34.502  23.337 -44.626  1.00 61.23           C
ANISOU 2087  CB  GLN C 279     8567   7499   7199    391     43   -442       C
ATOM   2088  CG  GLN C 279      34.642  22.359 -45.768  0.00 61.11           C
ANISOU 2088  CG  GLN C 279     8577   7521   7121    408     14   -446       C
ATOM   2089  CD  GLN C 279      33.681  21.197 -45.618  0.00 60.71           C
ANISOU 2089  CD  GLN C 279     8552   7484   7031    388    -36   -470       C
ATOM   2090  OE1 GLN C 279      32.765  21.238 -44.794  0.00 60.27           O
ANISOU 2090  OE1 GLN C 279     8492   7413   6995    364    -47   -473       O
ATOM   2091  NE2 GLN C 279      33.892  20.148 -46.400  0.00 60.84           N
ANISOU 2091  NE2 GLN C 279     8596   7526   6994    396    -63   -489       N
ATOM   2092  N   THR C 280      33.821  25.641 -43.677  1.00 69.45           N
ANISOU 2092  N   THR C 280     9547   8496   8344    380    116   -395       N
ATOM   2093  CA  THR C 280      33.087  26.833 -43.287  1.00 70.30           C
ANISOU 2093  CA  THR C 280     9621   8583   8506    374    152   -364       C
ATOM   2094  C   THR C 280      32.733  26.877 -41.805  1.00 69.30           C
ANISOU 2094  C   THR C 280     9495   8421   8415    338    152   -398       C
ATOM   2095  O   THR C 280      32.183  27.869 -41.328  1.00 69.67           O
ANISOU 2095  O   THR C 280     9515   8444   8512    329    187   -380       O
ATOM   2096  CB  THR C 280      31.774  26.899 -44.089  1.00 71.71           C
ANISOU 2096  CB  THR C 280     9788   8794   8664    384    139   -320       C
ATOM   2097  OG1 THR C 280      30.867  27.808 -43.454  1.00 72.73           O
ANISOU 2097  OG1 THR C 280     9889   8898   8845    372    166   -298       O
ATOM   2098  CG2 THR C 280      31.123  25.520 -44.154  1.00 71.25           C
ANISOU 2098  CG2 THR C 280     9762   8761   8548    371     79   -345       C
ATOM   2099  N   SER C 281      33.049  25.811 -41.075  1.00 70.20           N
ANISOU 2099  N   SER C 281     9639   8530   8504    317    116   -446       N
ATOM   2100  CA  SER C 281      32.550  25.675 -39.709  1.00 69.32           C
ANISOU 2100  CA  SER C 281     9531   8393   8414    281    108   -477       C
ATOM   2101  C   SER C 281      33.633  25.464 -38.654  1.00 68.16           C
ANISOU 2101  C   SER C 281     9393   8223   8280    261    110   -522       C
ATOM   2102  O   SER C 281      34.728  24.984 -38.954  1.00 68.40           O
ANISOU 2102  O   SER C 281     9438   8262   8290    273    102   -538       O
ATOM   2103  CB  SER C 281      31.541  24.531 -39.637  1.00 68.84           C
ANISOU 2103  CB  SER C 281     9495   8351   8311    268     56   -488       C
ATOM   2104  OG  SER C 281      31.127  24.140 -40.934  1.00 70.19           O
ANISOU 2104  OG  SER C 281     9671   8558   8440    292     35   -460       O
ATOM   2105  N   CYS C 282      33.304  25.825 -37.416  1.00 64.68           N
ANISOU 2105  N   CYS C 282     8945   7757   7874    229    122   -543       N
ATOM   2106  CA  CYS C 282      34.184  25.591 -36.281  1.00 63.99           C
ANISOU 2106  CA  CYS C 282     8865   7653   7796    204    120   -587       C
ATOM   2107  C   CYS C 282      33.958  24.182 -35.754  1.00 63.70           C
ANISOU 2107  C   CYS C 282     8860   7627   7715    188     66   -616       C
ATOM   2108  O   CYS C 282      32.829  23.802 -35.444  1.00 63.90           O
ANISOU 2108  O   CYS C 282     8893   7655   7732    173     44   -616       O
ATOM   2109  CB  CYS C 282      33.904  26.604 -35.172  1.00 63.74           C
ANISOU 2109  CB  CYS C 282     8810   7592   7816    175    158   -598       C
ATOM   2110  SG  CYS C 282      33.961  28.333 -35.695  1.00 68.20           S
ANISOU 2110  SG  CYS C 282     9334   8135   8442    191    229   -561       S
ATOM   2111  N   VAL C 283      35.032  23.406 -35.653  1.00 59.05           N
ANISOU 2111  N   VAL C 283     8289   7044   7103    191     45   -641       N
ATOM   2112  CA  VAL C 283      34.921  22.028 -35.193  1.00 58.47           C
ANISOU 2112  CA  VAL C 283     8246   6979   6993    178     -4   -666       C
ATOM   2113  C   VAL C 283      35.841  21.724 -34.018  1.00 58.28           C
ANISOU 2113  C   VAL C 283     8224   6944   6974    155     -9   -701       C
ATOM   2114  O   VAL C 283      36.809  22.442 -33.768  1.00 58.29           O
ANISOU 2114  O   VAL C 283     8208   6938   7001    154     21   -707       O
ATOM   2115  CB  VAL C 283      35.184  21.030 -36.332  1.00 58.48           C
ANISOU 2115  CB  VAL C 283     8270   7001   6948    207    -33   -660       C
ATOM   2116  CG1 VAL C 283      33.973  20.964 -37.242  1.00 59.03           C
ANISOU 2116  CG1 VAL C 283     8344   7088   6999    218    -45   -633       C
ATOM   2117  CG2 VAL C 283      36.437  21.422 -37.107  1.00 58.97           C
ANISOU 2117  CG2 VAL C 283     8325   7068   7014    235     -9   -652       C
ATOM   2118  N   ARG C 284      35.520  20.653 -33.299  1.00 71.90           N
ANISOU 2118  N   ARG C 284     9971   8671   8675    136    -48   -721       N
ATOM   2119  CA  ARG C 284      36.271  20.260 -32.114  1.00 71.50           C
ANISOU 2119  CA  ARG C 284     9924   8617   8627    113    -58   -750       C
ATOM   2120  C   ARG C 284      37.682  19.806 -32.471  1.00 71.91           C
ANISOU 2120  C   ARG C 284     9980   8676   8666    133    -63   -757       C
ATOM   2121  O   ARG C 284      38.644  20.141 -31.780  1.00 72.05           O
ANISOU 2121  O   ARG C 284     9985   8692   8701    121    -49   -771       O
ATOM   2122  CB  ARG C 284      35.533  19.147 -31.367  1.00 70.45           C
ANISOU 2122  CB  ARG C 284     9813   8486   8471     91   -100   -765       C
ATOM   2123  CG  ARG C 284      34.126  19.525 -30.930  0.00 70.59           C
ANISOU 2123  CG  ARG C 284     9824   8496   8500     69    -97   -759       C
ATOM   2124  CD  ARG C 284      33.394  18.338 -30.327  0.00 70.09           C
ANISOU 2124  CD  ARG C 284     9785   8436   8411     51   -139   -771       C
ATOM   2125  NE  ARG C 284      32.046  18.692 -29.892  0.00 70.23           N
ANISOU 2125  NE  ARG C 284     9796   8447   8441     30   -135   -765       N
ATOM   2126  CZ  ARG C 284      31.172  17.827 -29.388  0.00 69.87           C
ANISOU 2126  CZ  ARG C 284     9767   8402   8378     12   -167   -772       C
ATOM   2127  NH1 ARG C 284      31.501  16.549 -29.256  0.00 69.39           N
ANISOU 2127  NH1 ARG C 284     9731   8346   8289     13   -204   -783       N
ATOM   2128  NH2 ARG C 284      29.967  18.239 -29.018  0.00 70.01           N
ANISOU 2128  NH2 ARG C 284     9776   8415   8410     -6   -159   -765       N
ATOM   2129  N   ALA C 285      37.799  19.045 -33.555  1.00 73.97           N
ANISOU 2129  N   ALA C 285    10261   8947   8898    163    -82   -747       N
ATOM   2130  CA  ALA C 285      39.092  18.534 -33.994  1.00 73.78           C
ANISOU 2130  CA  ALA C 285    10244   8929   8862    186    -86   -751       C
ATOM   2131  C   ALA C 285      39.162  18.414 -35.513  1.00 73.99           C
ANISOU 2131  C   ALA C 285    10279   8966   8869    223    -82   -733       C
ATOM   2132  O   ALA C 285      38.136  18.393 -36.193  1.00 74.03           O
ANISOU 2132  O   ALA C 285    10292   8978   8860    229    -89   -718       O
ATOM   2133  CB  ALA C 285      39.381  17.191 -33.340  1.00 73.27           C
ANISOU 2133  CB  ALA C 285    10200   8864   8774    177   -125   -771       C
ATOM   2134  N   CYS C 286      40.380  18.333 -36.037  1.00 85.66           N
ANISOU 2134  N   CYS C 286    11755  10447  10343    246    -71   -732       N
ATOM   2135  CA  CYS C 286      40.596  18.231 -37.475  1.00 85.91           C
ANISOU 2135  CA  CYS C 286    11794  10492  10354    282    -64   -716       C
ATOM   2136  C   CYS C 286      40.418  16.788 -37.941  1.00 85.82           C
ANISOU 2136  C   CYS C 286    11817  10487  10302    292   -102   -728       C
ATOM   2137  O   CYS C 286      40.848  15.857 -37.259  1.00 85.29           O
ANISOU 2137  O   CYS C 286    11764  10412  10230    284   -124   -748       O
ATOM   2138  CB  CYS C 286      41.997  18.734 -37.831  1.00 86.08           C
ANISOU 2138  CB  CYS C 286    11801  10515  10392    302    -35   -712       C
ATOM   2139  SG  CYS C 286      42.116  19.594 -39.417  1.00 95.41           S
ANISOU 2139  SG  CYS C 286    12970  11710  11570    338      0   -680       S
ATOM   2140  N   PRO C 287      39.777  16.598 -39.106  1.00 94.32           N
ANISOU 2140  N   PRO C 287    12907  11579  11353    310   -107   -716       N
ATOM   2141  CA  PRO C 287      39.558  15.266 -39.683  1.00 94.23           C
ANISOU 2141  CA  PRO C 287    12928  11573  11301    319   -139   -730       C
ATOM   2142  C   PRO C 287      40.875  14.575 -40.037  1.00 94.20           C
ANISOU 2142  C   PRO C 287    12936  11567  11288    343   -136   -743       C
ATOM   2143  O   PRO C 287      41.881  15.257 -40.231  1.00 94.38           O
ANISOU 2143  O   PRO C 287    12940  11591  11328    358   -107   -734       O
ATOM   2144  CB  PRO C 287      38.751  15.564 -40.953  1.00 94.57           C
ANISOU 2144  CB  PRO C 287    12974  11640  11320    334   -135   -710       C
ATOM   2145  CG  PRO C 287      39.054  16.985 -41.276  1.00 95.21           C
ANISOU 2145  CG  PRO C 287    13023  11727  11427    346    -95   -682       C
ATOM   2146  CD  PRO C 287      39.209  17.661 -39.952  1.00 95.04           C
ANISOU 2146  CD  PRO C 287    12980  11683  11448    321    -82   -687       C
ATOM   2147  N   PRO C 288      40.869  13.233 -40.113  1.00 89.89           N
ANISOU 2147  N   PRO C 288    12419  11016  10718    345   -164   -764       N
ATOM   2148  CA  PRO C 288      42.071  12.441 -40.401  1.00 90.00           C
ANISOU 2148  CA  PRO C 288    12446  11024  10726    367   -163   -777       C
ATOM   2149  C   PRO C 288      42.732  12.784 -41.736  1.00 90.39           C
ANISOU 2149  C   PRO C 288    12493  11091  10760    400   -137   -767       C
ATOM   2150  O   PRO C 288      43.925  12.532 -41.904  1.00 90.75           O
ANISOU 2150  O   PRO C 288    12539  11132  10812    420   -123   -771       O
ATOM   2151  CB  PRO C 288      41.539  11.005 -40.441  1.00 89.57           C
ANISOU 2151  CB  PRO C 288    12425  10961  10646    361   -196   -799       C
ATOM   2152  CG  PRO C 288      40.323  11.032 -39.589  1.00 89.17           C
ANISOU 2152  CG  PRO C 288    12375  10906  10601    329   -218   -799       C
ATOM   2153  CD  PRO C 288      39.705  12.376 -39.825  1.00 89.40           C
ANISOU 2153  CD  PRO C 288    12379  10950  10638    324   -198   -776       C
ATOM   2154  N   ASP C 289      41.971  13.349 -42.667  1.00 71.76           N
ANISOU 2154  N   ASP C 289    10132   8753   8382    406   -129   -751       N
ATOM   2155  CA  ASP C 289      42.495  13.660 -43.994  1.00 72.13           C
ANISOU 2155  CA  ASP C 289    10177   8820   8409    436   -105   -739       C
ATOM   2156  C   ASP C 289      43.103  15.059 -44.084  1.00 72.92           C
ANISOU 2156  C   ASP C 289    10243   8925   8538    447    -67   -712       C
ATOM   2157  O   ASP C 289      43.722  15.408 -45.090  1.00 73.76           O
ANISOU 2157  O   ASP C 289    10345   9047   8634    474    -43   -699       O
ATOM   2158  CB  ASP C 289      41.404  13.493 -45.056  0.00 72.37           C
ANISOU 2158  CB  ASP C 289    10222   8877   8399    438   -117   -734       C
ATOM   2159  CG  ASP C 289      41.012  12.043 -45.265  0.00 71.93           C
ANISOU 2159  CG  ASP C 289    10202   8818   8310    432   -149   -765       C
ATOM   2160  OD1 ASP C 289      40.159  11.539 -44.505  0.00 71.47           O
ANISOU 2160  OD1 ASP C 289    10154   8747   8255    406   -177   -777       O
ATOM   2161  OD2 ASP C 289      41.555  11.408 -46.194  0.00 72.06           O
ANISOU 2161  OD2 ASP C 289    10237   8844   8298    452   -144   -779       O
ATOM   2162  N   LYS C 290      42.928  15.856 -43.035  1.00 58.47           N
ANISOU 2162  N   LYS C 290     8389   7081   6745    426    -60   -704       N
ATOM   2163  CA  LYS C 290      43.445  17.222 -43.025  1.00 58.51           C
ANISOU 2163  CA  LYS C 290     8361   7086   6784    432    -22   -680       C
ATOM   2164  C   LYS C 290      44.322  17.499 -41.806  1.00 57.88           C
ANISOU 2164  C   LYS C 290     8263   6985   6743    416    -13   -691       C
ATOM   2165  O   LYS C 290      44.247  16.795 -40.800  1.00 56.94           O
ANISOU 2165  O   LYS C 290     8154   6853   6627    396    -39   -712       O
ATOM   2166  CB  LYS C 290      42.297  18.234 -43.094  1.00 58.86           C
ANISOU 2166  CB  LYS C 290     8388   7137   6839    420    -12   -655       C
ATOM   2167  CG  LYS C 290      41.510  18.187 -44.394  1.00 59.30           C
ANISOU 2167  CG  LYS C 290     8453   7221   6857    436    -15   -635       C
ATOM   2168  CD  LYS C 290      40.396  19.221 -44.411  1.00 59.51           C
ANISOU 2168  CD  LYS C 290     8457   7253   6900    426     -4   -605       C
ATOM   2169  CE  LYS C 290      39.638  19.190 -45.728  0.00 60.13           C
ANISOU 2169  CE  LYS C 290     8541   7367   6938    443     -9   -581       C
ATOM   2170  NZ  LYS C 290      38.536  20.191 -45.762  0.00 60.81           N
ANISOU 2170  NZ  LYS C 290     8603   7461   7042    435      3   -546       N
ATOM   2171  N   MET C 291      45.155  18.531 -41.908  1.00 54.96           N
ANISOU 2171  N   MET C 291     7866   6614   6403    426     24   -676       N
ATOM   2172  CA  MET C 291      46.055  18.902 -40.821  1.00 54.57           C
ANISOU 2172  CA  MET C 291     7795   6550   6389    410     35   -687       C
ATOM   2173  C   MET C 291      45.848  20.351 -40.391  1.00 55.16           C
ANISOU 2173  C   MET C 291     7837   6616   6504    393     68   -672       C
ATOM   2174  O   MET C 291      45.266  21.153 -41.122  1.00 55.49           O
ANISOU 2174  O   MET C 291     7869   6664   6550    403     89   -647       O
ATOM   2175  CB  MET C 291      47.513  18.671 -41.226  1.00 54.77           C
ANISOU 2175  CB  MET C 291     7816   6578   6416    435     50   -688       C
ATOM   2176  CG  MET C 291      47.948  19.449 -42.457  1.00 55.42           C
ANISOU 2176  CG  MET C 291     7886   6672   6499    465     86   -664       C
ATOM   2177  SD  MET C 291      49.656  19.109 -42.925  1.00 56.17           S
ANISOU 2177  SD  MET C 291     7976   6771   6596    495    104   -667       S
ATOM   2178  CE  MET C 291      49.836  20.184 -44.346  1.00 58.45           C
ANISOU 2178  CE  MET C 291     8248   7075   6885    525    148   -632       C
ATOM   2179  N   GLU C 292      46.337  20.678 -39.199  1.00 78.10           N
ANISOU 2179  N   GLU C 292    10725   9510   9440    367     72   -687       N
ATOM   2180  CA  GLU C 292      46.140  21.997 -38.611  1.00 79.16           C
ANISOU 2180  CA  GLU C 292    10830   9633   9616    345    104   -681       C
ATOM   2181  C   GLU C 292      47.252  22.966 -39.006  1.00 80.24           C
ANISOU 2181  C   GLU C 292    10938   9768   9783    358    147   -669       C
ATOM   2182  O   GLU C 292      48.430  22.710 -38.757  1.00 80.45           O
ANISOU 2182  O   GLU C 292    10957   9795   9814    362    148   -680       O
ATOM   2183  CB  GLU C 292      46.058  21.874 -37.089  1.00 79.34           C
ANISOU 2183  CB  GLU C 292    10847   9646   9654    305     88   -707       C
ATOM   2184  CG  GLU C 292      45.734  23.163 -36.362  1.00 80.10           C
ANISOU 2184  CG  GLU C 292    10914   9728   9791    276    120   -709       C
ATOM   2185  CD  GLU C 292      45.531  22.943 -34.876  1.00 79.93           C
ANISOU 2185  CD  GLU C 292    10892   9703   9776    234    101   -737       C
ATOM   2186  OE1 GLU C 292      44.810  21.991 -34.510  1.00 79.07           O
ANISOU 2186  OE1 GLU C 292    10806   9596   9639    226     63   -745       O
ATOM   2187  OE2 GLU C 292      46.101  23.713 -34.076  1.00 80.59           O
ANISOU 2187  OE2 GLU C 292    10951   9781   9891    209    124   -750       O
ATOM   2188  N   VAL C 293      46.869  24.077 -39.630  1.00 84.77           N
ANISOU 2188  N   VAL C 293    11494  10337  10378    367    183   -643       N
ATOM   2189  CA  VAL C 293      47.825  25.085 -40.081  1.00 85.60           C
ANISOU 2189  CA  VAL C 293    11571  10438  10515    381    228   -627       C
ATOM   2190  C   VAL C 293      47.316  26.493 -39.746  1.00 86.43           C
ANISOU 2190  C   VAL C 293    11647  10523  10667    362    269   -616       C
ATOM   2191  O   VAL C 293      46.109  26.737 -39.729  1.00 86.71           O
ANISOU 2191  O   VAL C 293    11686  10554  10704    354    267   -605       O
ATOM   2192  CB  VAL C 293      48.107  24.956 -41.603  1.00 86.07           C
ANISOU 2192  CB  VAL C 293    11638  10514  10550    424    239   -599       C
ATOM   2193  CG1 VAL C 293      49.024  26.061 -42.089  1.00 86.72           C
ANISOU 2193  CG1 VAL C 293    11690  10591  10667    439    289   -579       C
ATOM   2194  CG2 VAL C 293      48.723  23.601 -41.931  1.00 85.85           C
ANISOU 2194  CG2 VAL C 293    11638  10502  10481    443    206   -615       C
ATOM   2195  N   ASP C 294      48.242  27.407 -39.462  0.00 88.09           N
ANISOU 2195  N   ASP C 294    11829  10722  10920    353    307   -618       N
ATOM   2196  CA  ASP C 294      47.898  28.784 -39.129  0.00 88.26           C
ANISOU 2196  CA  ASP C 294    11821  10720  10993    335    352   -610       C
ATOM   2197  C   ASP C 294      47.770  29.666 -40.369  1.00 88.89           C
ANISOU 2197  C   ASP C 294    11887  10798  11090    367    393   -566       C
ATOM   2198  O   ASP C 294      48.738  29.875 -41.102  1.00 89.16           O
ANISOU 2198  O   ASP C 294    11910  10838  11127    391    415   -551       O
ATOM   2199  CB  ASP C 294      48.936  29.371 -38.172  0.00 87.92           C
ANISOU 2199  CB  ASP C 294    11753  10665  10989    305    375   -637       C
ATOM   2200  CG  ASP C 294      49.070  28.566 -36.896  0.00 87.46           C
ANISOU 2200  CG  ASP C 294    11705  10613  10913    271    336   -678       C
ATOM   2201  OD1 ASP C 294      49.964  27.695 -36.830  0.00 87.40           O
ANISOU 2201  OD1 ASP C 294    11705  10622  10880    279    309   -689       O
ATOM   2202  OD2 ASP C 294      48.279  28.799 -35.959  0.00 87.18           O
ANISOU 2202  OD2 ASP C 294    11668  10567  10890    237    333   -696       O
ATOM   2203  N   LYS C 295      46.564  30.183 -40.587  1.00 86.37           N
ANISOU 2203  N   LYS C 295    11565  10471  10782    368    405   -542       N
ATOM   2204  CA  LYS C 295      46.272  31.040 -41.731  1.00 86.85           C
ANISOU 2204  CA  LYS C 295    11610  10532  10859    398    443   -494       C
ATOM   2205  C   LYS C 295      45.548  32.308 -41.280  1.00 87.23           C
ANISOU 2205  C   LYS C 295    11631  10549  10965    379    486   -481       C
ATOM   2206  O   LYS C 295      44.525  32.231 -40.600  1.00 86.91           O
ANISOU 2206  O   LYS C 295    11596  10500  10926    357    472   -492       O
ATOM   2207  CB  LYS C 295      45.416  30.287 -42.754  1.00 86.50           C
ANISOU 2207  CB  LYS C 295    11589  10517  10761    427    411   -467       C
ATOM   2208  CG  LYS C 295      46.073  29.048 -43.350  1.00 86.07           C
ANISOU 2208  CG  LYS C 295    11563  10491  10650    448    373   -478       C
ATOM   2209  CD  LYS C 295      47.380  29.386 -44.035  0.00 86.39           C
ANISOU 2209  CD  LYS C 295    11589  10535  10700    473    404   -466       C
ATOM   2210  CE  LYS C 295      48.015  28.176 -44.710  0.00 86.21           C
ANISOU 2210  CE  LYS C 295    11594  10540  10623    497    371   -476       C
ATOM   2211  NZ  LYS C 295      47.316  27.755 -45.964  0.00 86.55           N
ANISOU 2211  NZ  LYS C 295    11654  10613  10618    527    357   -446       N
ATOM   2212  N   ASN C 296      46.083  33.463 -41.673  1.00110.87           N
ANISOU 2212  N   ASN C 296    14594  13525  14006    389    542   -457       N
ATOM   2213  CA  ASN C 296      45.548  34.779 -41.294  1.00110.84           C
ANISOU 2213  CA  ASN C 296    14561  13486  14068    373    594   -444       C
ATOM   2214  C   ASN C 296      45.081  34.911 -39.837  1.00110.30           C
ANISOU 2214  C   ASN C 296    14491  13394  14024    325    591   -489       C
ATOM   2215  O   ASN C 296      44.033  35.495 -39.559  1.00110.66           O
ANISOU 2215  O   ASN C 296    14528  13419  14099    315    610   -477       O
ATOM   2216  CB  ASN C 296      44.455  35.245 -42.272  1.00111.25           C
ANISOU 2216  CB  ASN C 296    14605  13542  14123    403    610   -387       C
ATOM   2217  CG  ASN C 296      43.223  34.364 -42.243  1.00111.30           C
ANISOU 2217  CG  ASN C 296    14636  13569  14082    402    560   -386       C
ATOM   2218  OD1 ASN C 296      43.150  33.355 -42.944  1.00111.43           O
ANISOU 2218  OD1 ASN C 296    14679  13622  14039    423    517   -379       O
ATOM   2219  ND2 ASN C 296      42.242  34.745 -41.434  1.00111.29           N
ANISOU 2219  ND2 ASN C 296    14630  13546  14111    376    568   -394       N
ATOM   2220  N   GLY C 297      45.872  34.362 -38.919  1.00 80.19           N
ANISOU 2220  N   GLY C 297    10686   9584  10199    297    567   -537       N
ATOM   2221  CA  GLY C 297      45.609  34.482 -37.496  1.00 79.54           C
ANISOU 2221  CA  GLY C 297    10602   9484  10136    249    565   -583       C
ATOM   2222  C   GLY C 297      44.859  33.307 -36.902  1.00 79.14           C
ANISOU 2222  C   GLY C 297    10582   9453  10036    235    506   -605       C
ATOM   2223  O   GLY C 297      44.879  33.089 -35.691  1.00 78.92           O
ANISOU 2223  O   GLY C 297    10557   9421  10008    196    491   -648       O
ATOM   2224  N   LEU C 298      44.202  32.539 -37.761  1.00 79.70           N
ANISOU 2224  N   LEU C 298    10674   9545  10061    266    472   -577       N
ATOM   2225  CA  LEU C 298      43.340  31.456 -37.305  1.00 78.86           C
ANISOU 2225  CA  LEU C 298    10597   9455   9911    255    418   -593       C
ATOM   2226  C   LEU C 298      43.908  30.074 -37.618  1.00 78.81           C
ANISOU 2226  C   LEU C 298    10620   9479   9846    271    365   -604       C
ATOM   2227  O   LEU C 298      44.688  29.903 -38.556  1.00 79.31           O
ANISOU 2227  O   LEU C 298    10684   9556   9894    302    368   -586       O
ATOM   2228  CB  LEU C 298      41.946  31.605 -37.911  1.00 79.05           C
ANISOU 2228  CB  LEU C 298    10624   9480   9932    271    418   -556       C
ATOM   2229  CG  LEU C 298      41.137  32.797 -37.396  1.00 79.23           C
ANISOU 2229  CG  LEU C 298    10622   9470  10013    251    464   -549       C
ATOM   2230  CD1 LEU C 298      40.284  33.389 -38.506  1.00 79.94           C
ANISOU 2230  CD1 LEU C 298    10698   9560  10115    285    488   -491       C
ATOM   2231  CD2 LEU C 298      40.269  32.367 -36.224  1.00 78.81           C
ANISOU 2231  CD2 LEU C 298    10581   9411   9952    215    438   -581       C
ATOM   2232  N   LYS C 299      43.520  29.092 -36.812  1.00 79.32           N
ANISOU 2232  N   LYS C 299    10707   9553   9879    249    320   -633       N
ATOM   2233  CA  LYS C 299      43.923  27.710 -37.033  1.00 78.73           C
ANISOU 2233  CA  LYS C 299    10660   9502   9751    263    270   -643       C
ATOM   2234  C   LYS C 299      42.953  27.039 -37.998  1.00 78.51           C
ANISOU 2234  C   LYS C 299    10655   9491   9683    289    242   -618       C
ATOM   2235  O   LYS C 299      41.831  26.697 -37.624  1.00 78.17           O
ANISOU 2235  O   LYS C 299    10625   9448   9629    275    220   -621       O
ATOM   2236  CB  LYS C 299      43.966  26.943 -35.710  1.00 78.24           C
ANISOU 2236  CB  LYS C 299    10610   9442   9675    228    235   -684       C
ATOM   2237  CG  LYS C 299      45.033  27.428 -34.742  1.00 78.20           C
ANISOU 2237  CG  LYS C 299    10584   9429   9699    199    254   -712       C
ATOM   2238  CD  LYS C 299      44.987  26.643 -33.442  1.00 77.63           C
ANISOU 2238  CD  LYS C 299    10523   9365   9608    164    217   -747       C
ATOM   2239  CE  LYS C 299      46.133  27.027 -32.518  0.00 77.70           C
ANISOU 2239  CE  LYS C 299    10509   9375   9638    136    231   -775       C
ATOM   2240  NZ  LYS C 299      46.119  26.231 -31.258  0.00 77.24           N
ANISOU 2240  NZ  LYS C 299    10461   9330   9557    102    193   -805       N
ATOM   2241  N   MET C 300      43.388  26.856 -39.241  1.00 90.46           N
ANISOU 2241  N   MET C 300    12173  11021  11175    327    245   -593       N
ATOM   2242  CA  MET C 300      42.542  26.254 -40.267  1.00 90.47           C
ANISOU 2242  CA  MET C 300    12196  11044  11136    351    221   -569       C
ATOM   2243  C   MET C 300      42.949  24.815 -40.567  1.00 89.91           C
ANISOU 2243  C   MET C 300    12156  10992  11012    364    176   -588       C
ATOM   2244  O   MET C 300      44.076  24.408 -40.288  1.00 90.18           O
ANISOU 2244  O   MET C 300    12194  11026  11045    365    172   -608       O
ATOM   2245  CB  MET C 300      42.580  27.083 -41.555  1.00 91.38           C
ANISOU 2245  CB  MET C 300    12294  11168  11259    385    257   -525       C
ATOM   2246  CG  MET C 300      41.246  27.712 -41.929  1.00 92.05           C
ANISOU 2246  CG  MET C 300    12367  11254  11354    388    268   -490       C
ATOM   2247  SD  MET C 300      41.004  29.353 -41.226  1.00 96.85           S
ANISOU 2247  SD  MET C 300    12935  11824  12039    368    327   -477       S
ATOM   2248  CE  MET C 300      41.883  30.360 -42.416  1.00 97.33           C
ANISOU 2248  CE  MET C 300    12970  11887  12123    405    379   -435       C
ATOM   2249  N   CYS C 301      42.022  24.051 -41.135  1.00 63.83           N
ANISOU 2249  N   CYS C 301     8876   7707   7669    373    144   -580       N
ATOM   2250  CA  CYS C 301      42.301  22.679 -41.542  1.00 63.35           C
ANISOU 2250  CA  CYS C 301     8847   7663   7559    385    105   -598       C
ATOM   2251  C   CYS C 301      42.528  22.590 -43.047  1.00 64.23           C
ANISOU 2251  C   CYS C 301     8965   7799   7640    422    113   -573       C
ATOM   2252  O   CYS C 301      41.661  22.961 -43.838  1.00 64.81           O
ANISOU 2252  O   CYS C 301     9034   7888   7701    433    118   -544       O
ATOM   2253  CB  CYS C 301      41.158  21.749 -41.130  1.00 62.69           C
ANISOU 2253  CB  CYS C 301     8789   7583   7449    367     62   -613       C
ATOM   2254  SG  CYS C 301      41.106  21.357 -39.367  1.00 62.37           S
ANISOU 2254  SG  CYS C 301     8752   7520   7428    325     41   -649       S
ATOM   2255  N   GLU C 302      43.700  22.099 -43.439  1.00 81.95           N
ANISOU 2255  N   GLU C 302    11218  10049   9871    442    114   -584       N
ATOM   2256  CA  GLU C 302      44.028  21.941 -44.851  1.00 82.83           C
ANISOU 2256  CA  GLU C 302    11336  10185   9950    476    123   -565       C
ATOM   2257  C   GLU C 302      44.477  20.516 -45.157  1.00 82.52           C
ANISOU 2257  C   GLU C 302    11330  10155   9867    487     91   -592       C
ATOM   2258  O   GLU C 302      45.162  19.894 -44.346  1.00 82.00           O
ANISOU 2258  O   GLU C 302    11272  10073   9810    477     78   -621       O
ATOM   2259  CB  GLU C 302      45.107  22.940 -45.268  1.00 83.25           C
ANISOU 2259  CB  GLU C 302    11362  10236  10033    496    169   -544       C
ATOM   2260  CG  GLU C 302      45.698  23.730 -44.119  1.00 83.17           C
ANISOU 2260  CG  GLU C 302    11326  10197  10077    473    193   -554       C
ATOM   2261  CD  GLU C 302      46.470  24.937 -44.596  0.00 83.80           C
ANISOU 2261  CD  GLU C 302    11375  10272  10193    490    243   -527       C
ATOM   2262  OE1 GLU C 302      45.865  26.026 -44.665  0.00 84.28           O
ANISOU 2262  OE1 GLU C 302    11412  10325  10283    486    272   -500       O
ATOM   2263  OE2 GLU C 302      47.673  24.797 -44.905  0.00 83.83           O
ANISOU 2263  OE2 GLU C 302    11376  10279  10197    507    256   -531       O
ATOM   2264  N   PRO C 303      44.080  19.993 -46.327  1.00 80.64           N
ANISOU 2264  N   PRO C 303    11112   9945   9584    506     80   -585       N
ATOM   2265  CA  PRO C 303      44.443  18.634 -46.752  1.00 80.42           C
ANISOU 2265  CA  PRO C 303    11117   9925   9514    517     54   -613       C
ATOM   2266  C   PRO C 303      45.960  18.408 -46.771  1.00 80.63           C
ANISOU 2266  C   PRO C 303    11141   9942   9552    536     72   -625       C
ATOM   2267  O   PRO C 303      46.697  19.248 -47.283  1.00 81.09           O
ANISOU 2267  O   PRO C 303    11179  10006   9626    555    108   -602       O
ATOM   2268  CB  PRO C 303      43.852  18.530 -48.167  1.00 80.86           C
ANISOU 2268  CB  PRO C 303    11183  10017   9522    536     53   -595       C
ATOM   2269  CG  PRO C 303      43.437  19.927 -48.550  1.00 81.59           C
ANISOU 2269  CG  PRO C 303    11244  10122   9636    542     84   -550       C
ATOM   2270  CD  PRO C 303      43.163  20.646 -47.276  1.00 81.41           C
ANISOU 2270  CD  PRO C 303    11199  10068   9665    516     90   -549       C
ATOM   2271  N   CYS C 304      46.408  17.281 -46.220  1.00 85.35           N
ANISOU 2271  N   CYS C 304    11760  10525  10143    530     48   -657       N
ATOM   2272  CA  CYS C 304      47.834  17.019 -45.995  1.00 85.46           C
ANISOU 2272  CA  CYS C 304    11769  10527  10175    544     62   -668       C
ATOM   2273  C   CYS C 304      48.680  16.899 -47.262  1.00 85.65           C
ANISOU 2273  C   CYS C 304    11798  10569  10177    580     85   -661       C
ATOM   2274  O   CYS C 304      49.907  16.991 -47.201  1.00 85.54           O
ANISOU 2274  O   CYS C 304    11772  10547  10183    595    106   -662       O
ATOM   2275  CB  CYS C 304      48.018  15.757 -45.148  1.00 85.14           C
ANISOU 2275  CB  CYS C 304    11750  10468  10132    532     29   -700       C
ATOM   2276  SG  CYS C 304      47.271  15.844 -43.512  1.00 96.55           S
ANISOU 2276  SG  CYS C 304    13187  11892  11604    490      4   -710       S
ATOM   2277  N   GLY C 305      48.033  16.692 -48.403  1.00105.06           N
ANISOU 2277  N   GLY C 305    14273  13052  12592    593     82   -655       N
ATOM   2278  CA  GLY C 305      48.758  16.458 -49.638  1.00105.48           C
ANISOU 2278  CA  GLY C 305    14335  13125  12616    625    103   -652       C
ATOM   2279  C   GLY C 305      49.453  15.110 -49.606  1.00105.09           C
ANISOU 2279  C   GLY C 305    14313  13063  12553    634     89   -687       C
ATOM   2280  O   GLY C 305      50.657  15.011 -49.847  1.00105.25           O
ANISOU 2280  O   GLY C 305    14328  13080  12584    657    112   -689       O
ATOM   2281  N   GLY C 306      48.683  14.067 -49.311  1.00 81.54           N
ANISOU 2281  N   GLY C 306    11358  10073   9549    618     54   -713       N
ATOM   2282  CA  GLY C 306      49.225  12.731 -49.150  1.00 80.57           C
ANISOU 2282  CA  GLY C 306    11262   9932   9419    624     40   -747       C
ATOM   2283  C   GLY C 306      48.749  12.130 -47.844  1.00 79.30           C
ANISOU 2283  C   GLY C 306    11108   9743   9278    595      7   -763       C
ATOM   2284  O   GLY C 306      47.563  11.821 -47.692  1.00 78.97           O
ANISOU 2284  O   GLY C 306    11081   9705   9219    574    -20   -772       O
ATOM   2285  N   LEU C 307      49.672  11.959 -46.899  1.00 56.28           N
ANISOU 2285  N   LEU C 307     8180   6804   6399    595      9   -767       N
ATOM   2286  CA  LEU C 307      49.303  11.508 -45.556  1.00 54.88           C
ANISOU 2286  CA  LEU C 307     8003   6604   6244    568    -20   -778       C
ATOM   2287  C   LEU C 307      49.684  12.548 -44.495  1.00 54.73           C
ANISOU 2287  C   LEU C 307     7948   6580   6267    552    -11   -760       C
ATOM   2288  O   LEU C 307      50.534  13.408 -44.734  1.00 54.82           O
ANISOU 2288  O   LEU C 307     7935   6599   6297    566     19   -743       O
ATOM   2289  CB  LEU C 307      49.823  10.081 -45.251  1.00 54.24           C
ANISOU 2289  CB  LEU C 307     7945   6501   6163    575    -35   -803       C
ATOM   2290  CG  LEU C 307      51.242   9.574 -44.917  1.00 54.51           C
ANISOU 2290  CG  LEU C 307     7971   6518   6223    596    -22   -805       C
ATOM   2291  CD1 LEU C 307      52.358  10.545 -45.250  1.00 55.18           C
ANISOU 2291  CD1 LEU C 307     8025   6615   6327    616     13   -784       C
ATOM   2292  CD2 LEU C 307      51.346   9.117 -43.462  1.00 54.51           C
ANISOU 2292  CD2 LEU C 307     7963   6497   6252    575    -46   -807       C
ATOM   2293  N   CYS C 308      49.019  12.506 -43.346  1.00 73.96           N
ANISOU 2293  N   CYS C 308    10380   9003   8717    521    -36   -764       N
ATOM   2294  CA  CYS C 308      49.267  13.504 -42.315  1.00 73.99           C
ANISOU 2294  CA  CYS C 308    10352   9004   8758    501    -27   -752       C
ATOM   2295  C   CYS C 308      50.494  13.148 -41.483  1.00 73.63           C
ANISOU 2295  C   CYS C 308    10291   8947   8737    504    -27   -756       C
ATOM   2296  O   CYS C 308      50.796  11.972 -41.288  1.00 73.01           O
ANISOU 2296  O   CYS C 308    10231   8858   8653    511    -45   -769       O
ATOM   2297  CB  CYS C 308      48.034  13.680 -41.419  1.00 74.03           C
ANISOU 2297  CB  CYS C 308    10357   9004   8766    466    -51   -755       C
ATOM   2298  SG  CYS C 308      46.593  14.390 -42.259  1.00 76.48           S
ANISOU 2298  SG  CYS C 308    10673   9331   9055    460    -48   -741       S
ATOM   2299  N   PRO C 309      51.223  14.172 -41.014  1.00 49.12           N
ANISOU 2299  N   PRO C 309     7153   5847   5665    498     -5   -744       N
ATOM   2300  CA  PRO C 309      52.371  13.981 -40.124  1.00 49.37           C
ANISOU 2300  CA  PRO C 309     7164   5874   5722    495     -5   -745       C
ATOM   2301  C   PRO C 309      51.948  13.268 -38.848  1.00 48.87           C
ANISOU 2301  C   PRO C 309     7106   5801   5661    467    -40   -756       C
ATOM   2302  O   PRO C 309      50.960  13.656 -38.226  1.00 48.50           O
ANISOU 2302  O   PRO C 309     7059   5754   5616    437    -53   -759       O
ATOM   2303  CB  PRO C 309      52.804  15.413 -39.807  1.00 49.59           C
ANISOU 2303  CB  PRO C 309     7153   5908   5779    482     23   -733       C
ATOM   2304  CG  PRO C 309      52.380  16.195 -40.997  1.00 49.56           C
ANISOU 2304  CG  PRO C 309     7152   5912   5766    498     50   -720       C
ATOM   2305  CD  PRO C 309      51.086  15.575 -41.441  1.00 49.26           C
ANISOU 2305  CD  PRO C 309     7148   5875   5695    496     26   -726       C
ATOM   2306  N   LYS C 310      52.681  12.226 -38.478  1.00 48.80           N
ANISOU 2306  N   LYS C 310     7101   5785   5655    477    -54   -761       N
ATOM   2307  CA  LYS C 310      52.403  11.486 -37.258  1.00 48.75           C
ANISOU 2307  CA  LYS C 310     7099   5772   5652    453    -87   -767       C
ATOM   2308  C   LYS C 310      53.718  11.216 -36.544  1.00 49.62           C
ANISOU 2308  C   LYS C 310     7183   5886   5783    458    -87   -759       C
ATOM   2309  O   LYS C 310      54.704  10.836 -37.173  1.00 50.44           O
ANISOU 2309  O   LYS C 310     7285   5988   5892    490    -72   -753       O
ATOM   2310  CB  LYS C 310      51.688  10.171 -37.577  1.00 48.64           C
ANISOU 2310  CB  LYS C 310     7123   5742   5614    462   -111   -778       C
ATOM   2311  CG  LYS C 310      51.323   9.345 -36.353  1.00 49.14           C
ANISOU 2311  CG  LYS C 310     7192   5797   5682    439   -144   -782       C
ATOM   2312  CD  LYS C 310      50.606   8.061 -36.741  1.00 49.23           C
ANISOU 2312  CD  LYS C 310     7243   5790   5674    447   -164   -794       C
ATOM   2313  CE  LYS C 310      50.248   7.236 -35.514  1.00 49.34           C
ANISOU 2313  CE  LYS C 310     7260   5793   5693    424   -195   -794       C
ATOM   2314  NZ  LYS C 310      49.530   5.982 -35.877  0.00 49.51           N
ANISOU 2314  NZ  LYS C 310     7320   5793   5700    431   -213   -807       N
ATOM   2315  N   ALA C 311      53.732  11.423 -35.232  1.00 49.42           N
ANISOU 2315  N   ALA C 311     7137   5868   5771    426   -103   -757       N
ATOM   2316  CA  ALA C 311      54.951  11.255 -34.452  1.00 49.45           C
ANISOU 2316  CA  ALA C 311     7111   5883   5794    426   -105   -747       C
ATOM   2317  C   ALA C 311      54.858  10.058 -33.513  1.00 49.52           C
ANISOU 2317  C   ALA C 311     7128   5887   5799    418   -139   -744       C
ATOM   2318  O   ALA C 311      53.934   9.959 -32.707  1.00 50.13           O
ANISOU 2318  O   ALA C 311     7214   5965   5869    388   -162   -749       O
ATOM   2319  CB  ALA C 311      55.262  12.524 -33.672  1.00 49.50           C
ANISOU 2319  CB  ALA C 311     7080   5909   5819    394    -94   -746       C
ATOM   2320  N   CYS C 312      55.824   9.151 -33.624  1.00 49.52           N
ANISOU 2320  N   CYS C 312     7125   5882   5807    446   -140   -733       N
ATOM   2321  CA  CYS C 312      55.865   7.963 -32.782  1.00 50.12           C
ANISOU 2321  CA  CYS C 312     7206   5952   5885    444   -169   -724       C
ATOM   2322  C   CYS C 312      57.126   7.971 -31.927  1.00 51.89           C
ANISOU 2322  C   CYS C 312     7390   6198   6129    442   -172   -704       C
ATOM   2323  O   CYS C 312      58.135   8.566 -32.304  1.00 52.89           O
ANISOU 2323  O   CYS C 312     7490   6336   6269    457   -149   -697       O
ATOM   2324  CB  CYS C 312      55.836   6.699 -33.642  1.00 50.13           C
ANISOU 2324  CB  CYS C 312     7241   5924   5881    481   -168   -726       C
ATOM   2325  SG  CYS C 312      54.644   6.736 -35.003  1.00 52.26           S
ANISOU 2325  SG  CYS C 312     7555   6175   6125    490   -158   -750       S
ATOM   2326  N   GLU C 313      57.068   7.313 -30.774  1.00 45.97           N
ANISOU 2326  N   GLU C 313     6632   5455   5380    424   -201   -692       N
ATOM   2327  CA  GLU C 313      58.248   7.175 -29.928  1.00 46.93           C
ANISOU 2327  CA  GLU C 313     6713   5601   5517    423   -208   -668       C
ATOM   2328  C   GLU C 313      59.165   6.092 -30.484  1.00 47.43           C
ANISOU 2328  C   GLU C 313     6779   5647   5596    470   -200   -650       C
ATOM   2329  O   GLU C 313      58.702   5.127 -31.091  1.00 47.24           O
ANISOU 2329  O   GLU C 313     6790   5590   5568    493   -201   -655       O
ATOM   2330  CB  GLU C 313      57.856   6.855 -28.484  1.00 46.89           C
ANISOU 2330  CB  GLU C 313     6696   5614   5504    388   -241   -658       C
ATOM   2331  CG  GLU C 313      57.132   7.986 -27.773  1.00 46.80           C
ANISOU 2331  CG  GLU C 313     6676   5626   5482    339   -246   -676       C
ATOM   2332  CD  GLU C 313      56.939   7.715 -26.294  0.00 47.28           C
ANISOU 2332  CD  GLU C 313     6719   5712   5533    303   -277   -665       C
ATOM   2333  OE1 GLU C 313      57.941   7.425 -25.605  0.00 48.48           O
ANISOU 2333  OE1 GLU C 313     6837   5890   5693    303   -287   -642       O
ATOM   2334  OE2 GLU C 313      55.786   7.788 -25.820  0.00 46.48           O
ANISOU 2334  OE2 GLU C 313     6636   5607   5417    274   -291   -678       O
ATOM   2335  N   GLY C 314      60.466   6.259 -30.275  1.00 40.90           N
ANISOU 2335  N   GLY C 314     5912   4840   4786    481   -191   -630       N
ATOM   2336  CA  GLY C 314      61.446   5.331 -30.808  1.00 41.19           C
ANISOU 2336  CA  GLY C 314     5946   4861   4842    527   -179   -611       C
ATOM   2337  C   GLY C 314      61.918   4.296 -29.806  1.00 42.52           C
ANISOU 2337  C   GLY C 314     6096   5037   5023    530   -203   -579       C
ATOM   2338  O   GLY C 314      61.202   3.951 -28.867  1.00 43.42           O
ANISOU 2338  O   GLY C 314     6215   5157   5126    503   -232   -575       O
ATOM   2339  N   THR C 315      63.133   3.798 -30.013  1.00 31.49           N
ANISOU 2339  N   THR C 315     4675   3640   3649    565   -191   -554       N
ATOM   2340  CA  THR C 315      63.710   2.777 -29.149  1.00 31.81           C
ANISOU 2340  CA  THR C 315     4693   3687   3706    576   -210   -516       C
ATOM   2341  C   THR C 315      65.070   3.216 -28.616  1.00 32.08           C
ANISOU 2341  C   THR C 315     4669   3762   3756    576   -209   -487       C
ATOM   2342  O   THR C 315      65.480   4.361 -28.803  1.00 31.98           O
ANISOU 2342  O   THR C 315     4635   3775   3742    561   -195   -500       O
ATOM   2343  CB  THR C 315      63.887   1.443 -29.900  1.00 32.08           C
ANISOU 2343  CB  THR C 315     4754   3674   3760    625   -196   -508       C
ATOM   2344  OG1 THR C 315      64.788   1.628 -30.999  1.00 32.24           O
ANISOU 2344  OG1 THR C 315     4770   3684   3796    662   -160   -511       O
ATOM   2345  CG2 THR C 315      62.551   0.940 -30.425  1.00 31.86           C
ANISOU 2345  CG2 THR C 315     4783   3607   3716    622   -198   -538       C
ATOM   2346  N   GLY C 316      65.763   2.298 -27.952  1.00 44.53           N
ANISOU 2346  N   GLY C 316     6220   5347   5351    592   -223   -447       N
ATOM   2347  CA  GLY C 316      67.106   2.555 -27.464  1.00 46.53           C
ANISOU 2347  CA  GLY C 316     6416   5641   5622    596   -223   -414       C
ATOM   2348  C   GLY C 316      67.168   3.490 -26.271  1.00 48.60           C
ANISOU 2348  C   GLY C 316     6639   5962   5866    543   -248   -412       C
ATOM   2349  O   GLY C 316      66.492   3.275 -25.265  1.00 49.25           O
ANISOU 2349  O   GLY C 316     6723   6061   5930    511   -279   -406       O
ATOM   2350  N   SER C 317      67.987   4.530 -26.391  1.00 85.24           N
ANISOU 2350  N   SER C 317    11243  10633  10510    532   -234   -417       N
ATOM   2351  CA  SER C 317      68.210   5.476 -25.302  1.00 86.91           C
ANISOU 2351  CA  SER C 317    11412  10902  10706    480   -253   -418       C
ATOM   2352  C   SER C 317      66.944   6.242 -24.935  1.00 85.94           C
ANISOU 2352  C   SER C 317    11317  10783  10555    432   -264   -456       C
ATOM   2353  O   SER C 317      66.370   6.948 -25.764  1.00 84.85           O
ANISOU 2353  O   SER C 317    11207  10618  10412    430   -241   -492       O
ATOM   2354  CB  SER C 317      69.322   6.461 -25.671  1.00 87.92           C
ANISOU 2354  CB  SER C 317    11500  11056  10848    480   -230   -421       C
ATOM   2355  OG  SER C 317      68.950   7.254 -26.786  1.00 86.91           O
ANISOU 2355  OG  SER C 317    11401  10898  10721    487   -197   -458       O
ATOM   2356  N   GLY C 318      66.517   6.101 -23.684  1.00 76.38           N
ANISOU 2356  N   GLY C 318    10093   9603   9323    393   -297   -447       N
ATOM   2357  CA  GLY C 318      65.342   6.798 -23.195  1.00 74.89           C
ANISOU 2357  CA  GLY C 318     9926   9421   9108    345   -307   -482       C
ATOM   2358  C   GLY C 318      64.044   6.186 -23.683  1.00 73.81           C
ANISOU 2358  C   GLY C 318     9847   9233   8963    358   -308   -498       C
ATOM   2359  O   GLY C 318      63.165   6.891 -24.179  1.00 72.54           O
ANISOU 2359  O   GLY C 318     9717   9053   8793    344   -295   -535       O
ATOM   2360  N   SER C 319      63.923   4.869 -23.540  1.00 63.90           N
ANISOU 2360  N   SER C 319     8607   7958   7714    385   -324   -469       N
ATOM   2361  CA  SER C 319      62.726   4.155 -23.970  1.00 62.26           C
ANISOU 2361  CA  SER C 319     8453   7702   7500    397   -326   -483       C
ATOM   2362  C   SER C 319      62.608   2.797 -23.285  1.00 62.51           C
ANISOU 2362  C   SER C 319     8488   7728   7536    410   -352   -446       C
ATOM   2363  O   SER C 319      63.498   2.386 -22.541  1.00 64.86           O
ANISOU 2363  O   SER C 319     8745   8058   7842    413   -366   -407       O
ATOM   2364  CB  SER C 319      62.724   3.977 -25.490  1.00 61.72           C
ANISOU 2364  CB  SER C 319     8419   7584   7447    442   -294   -501       C
ATOM   2365  OG  SER C 319      61.573   3.272 -25.919  1.00 61.46           O
ANISOU 2365  OG  SER C 319     8437   7508   7408    451   -297   -516       O
ATOM   2366  N   ARG C 320      61.504   2.104 -23.545  1.00 49.93           N
ANISOU 2366  N   ARG C 320     6940   6092   5937    416   -356   -458       N
ATOM   2367  CA  ARG C 320      61.253   0.798 -22.944  1.00 50.05           C
ANISOU 2367  CA  ARG C 320     6964   6094   5960    427   -377   -425       C
ATOM   2368  C   ARG C 320      61.730  -0.349 -23.833  1.00 50.66           C
ANISOU 2368  C   ARG C 320     7058   6122   6068    484   -358   -408       C
ATOM   2369  O   ARG C 320      61.935  -1.466 -23.358  1.00 51.75           O
ANISOU 2369  O   ARG C 320     7189   6250   6222    502   -370   -370       O
ATOM   2370  CB  ARG C 320      59.766   0.642 -22.611  1.00 48.94           C
ANISOU 2370  CB  ARG C 320     6862   5936   5797    398   -394   -447       C
ATOM   2371  CG  ARG C 320      58.831   1.228 -23.659  1.00 48.01           C
ANISOU 2371  CG  ARG C 320     6787   5784   5670    395   -375   -495       C
ATOM   2372  CD  ARG C 320      57.457   1.521 -23.073  1.00 47.25           C
ANISOU 2372  CD  ARG C 320     6714   5691   5548    352   -393   -517       C
ATOM   2373  NE  ARG C 320      56.664   0.312 -22.873  1.00 47.53           N
ANISOU 2373  NE  ARG C 320     6779   5693   5585    359   -408   -505       N
ATOM   2374  CZ  ARG C 320      55.612  -0.019 -23.615  1.00 46.39           C
ANISOU 2374  CZ  ARG C 320     6682   5506   5439    365   -402   -532       C
ATOM   2375  NH1 ARG C 320      55.219   0.773 -24.602  1.00 44.62           N
ANISOU 2375  NH1 ARG C 320     6478   5269   5207    366   -382   -569       N
ATOM   2376  NH2 ARG C 320      54.948  -1.140 -23.366  1.00 47.10           N
ANISOU 2376  NH2 ARG C 320     6796   5567   5534    370   -416   -520       N
ATOM   2377  N   PHE C 321      61.907  -0.068 -25.120  1.00 53.64           N
ANISOU 2377  N   PHE C 321     7456   6470   6455    511   -327   -435       N
ATOM   2378  CA  PHE C 321      62.402  -1.070 -26.058  1.00 53.57           C
ANISOU 2378  CA  PHE C 321     7463   6414   6475    564   -303   -425       C
ATOM   2379  C   PHE C 321      63.851  -0.780 -26.439  1.00 54.38           C
ANISOU 2379  C   PHE C 321     7527   6534   6599    593   -282   -406       C
ATOM   2380  O   PHE C 321      64.199   0.357 -26.758  1.00 54.47           O
ANISOU 2380  O   PHE C 321     7523   6571   6602    581   -270   -425       O
ATOM   2381  CB  PHE C 321      61.533  -1.112 -27.317  1.00 51.74           C
ANISOU 2381  CB  PHE C 321     7287   6135   6237    577   -282   -470       C
ATOM   2382  CG  PHE C 321      60.057  -1.061 -27.041  1.00 50.72           C
ANISOU 2382  CG  PHE C 321     7193   5996   6083    542   -301   -495       C
ATOM   2383  CD1 PHE C 321      59.413  -2.121 -26.425  1.00 51.05           C
ANISOU 2383  CD1 PHE C 321     7251   6017   6128    538   -321   -480       C
ATOM   2384  CD2 PHE C 321      59.310   0.046 -27.410  1.00 49.34           C
ANISOU 2384  CD2 PHE C 321     7034   5830   5882    514   -297   -533       C
ATOM   2385  CE1 PHE C 321      58.054  -2.074 -26.171  1.00 50.21           C
ANISOU 2385  CE1 PHE C 321     7177   5902   5999    506   -338   -503       C
ATOM   2386  CE2 PHE C 321      57.951   0.099 -27.162  1.00 48.45           C
ANISOU 2386  CE2 PHE C 321     6952   5709   5747    483   -314   -555       C
ATOM   2387  CZ  PHE C 321      57.322  -0.963 -26.543  1.00 48.79           C
ANISOU 2387  CZ  PHE C 321     7012   5733   5794    479   -335   -541       C
ATOM   2388  N   GLN C 322      64.693  -1.808 -26.403  1.00 54.07           N
ANISOU 2388  N   GLN C 322     7470   6481   6592    632   -275   -367       N
ATOM   2389  CA  GLN C 322      66.095  -1.657 -26.778  1.00 54.56           C
ANISOU 2389  CA  GLN C 322     7494   6556   6678    664   -254   -345       C
ATOM   2390  C   GLN C 322      66.275  -1.931 -28.269  1.00 53.44           C
ANISOU 2390  C   GLN C 322     7387   6366   6554    708   -213   -371       C
ATOM   2391  O   GLN C 322      67.314  -1.620 -28.851  1.00 53.62           O
ANISOU 2391  O   GLN C 322     7385   6395   6594    734   -189   -364       O
ATOM   2392  CB  GLN C 322      66.987  -2.585 -25.945  1.00 55.98           C
ANISOU 2392  CB  GLN C 322     7632   6751   6886    685   -266   -285       C
ATOM   2393  CG  GLN C 322      68.481  -2.314 -26.097  1.00 57.94           C
ANISOU 2393  CG  GLN C 322     7830   7027   7158    711   -250   -256       C
ATOM   2394  CD  GLN C 322      69.333  -3.143 -25.158  0.00 59.67           C
ANISOU 2394  CD  GLN C 322     8002   7269   7403    727   -266   -191       C
ATOM   2395  OE1 GLN C 322      68.821  -3.800 -24.252  0.00 60.32           O
ANISOU 2395  OE1 GLN C 322     8084   7356   7480    713   -293   -165       O
ATOM   2396  NE2 GLN C 322      70.645  -3.115 -25.369  0.00 59.96           N
ANISOU 2396  NE2 GLN C 322     7994   7321   7465    757   -249   -161       N
ATOM   2397  N   THR C 323      65.246  -2.507 -28.881  1.00 48.72           N
ANISOU 2397  N   THR C 323     6842   5719   5949    714   -207   -400       N
ATOM   2398  CA  THR C 323      65.257  -2.797 -30.309  1.00 47.34           C
ANISOU 2398  CA  THR C 323     6704   5499   5784    750   -170   -431       C
ATOM   2399  C   THR C 323      63.836  -3.020 -30.810  1.00 46.04           C
ANISOU 2399  C   THR C 323     6598   5299   5596    735   -173   -473       C
ATOM   2400  O   THR C 323      62.964  -3.448 -30.055  1.00 46.10           O
ANISOU 2400  O   THR C 323     6619   5302   5595    711   -200   -469       O
ATOM   2401  CB  THR C 323      66.112  -4.040 -30.631  1.00 47.61           C
ANISOU 2401  CB  THR C 323     6734   5496   5860    802   -147   -402       C
ATOM   2402  OG1 THR C 323      66.007  -4.349 -32.026  1.00 46.90           O
ANISOU 2402  OG1 THR C 323     6685   5361   5774    833   -110   -438       O
ATOM   2403  CG2 THR C 323      65.647  -5.237 -29.816  1.00 47.68           C
ANISOU 2403  CG2 THR C 323     6750   5481   5884    802   -167   -375       C
ATOM   2404  N   VAL C 324      63.601  -2.718 -32.082  1.00 48.39           N
ANISOU 2404  N   VAL C 324     6928   5575   5882    749   -145   -512       N
ATOM   2405  CA  VAL C 324      62.295  -2.961 -32.679  1.00 47.35           C
ANISOU 2405  CA  VAL C 324     6850   5412   5728    736   -146   -553       C
ATOM   2406  C   VAL C 324      62.119  -4.457 -32.927  1.00 47.56           C
ANISOU 2406  C   VAL C 324     6906   5386   5778    764   -137   -551       C
ATOM   2407  O   VAL C 324      63.038  -5.134 -33.391  1.00 47.94           O
ANISOU 2407  O   VAL C 324     6947   5410   5857    805   -109   -538       O
ATOM   2408  CB  VAL C 324      62.098  -2.154 -33.986  1.00 46.32           C
ANISOU 2408  CB  VAL C 324     6744   5282   5576    742   -121   -593       C
ATOM   2409  CG1 VAL C 324      63.205  -2.455 -34.978  1.00 46.38           C
ANISOU 2409  CG1 VAL C 324     6747   5272   5605    788    -81   -591       C
ATOM   2410  CG2 VAL C 324      60.732  -2.436 -34.596  1.00 45.78           C
ANISOU 2410  CG2 VAL C 324     6728   5185   5481    728   -124   -633       C
ATOM   2411  N   ASP C 325      60.945  -4.976 -32.589  1.00 54.15           N
ANISOU 2411  N   ASP C 325     7773   6201   6602    741   -158   -564       N
ATOM   2412  CA  ASP C 325      60.671  -6.398 -32.749  1.00 54.42           C
ANISOU 2412  CA  ASP C 325     7836   6182   6660    762   -149   -565       C
ATOM   2413  C   ASP C 325      59.227  -6.652 -33.167  1.00 53.83           C
ANISOU 2413  C   ASP C 325     7812   6081   6560    738   -158   -607       C
ATOM   2414  O   ASP C 325      58.539  -5.746 -33.636  1.00 53.27           O
ANISOU 2414  O   ASP C 325     7757   6029   6453    715   -163   -639       O
ATOM   2415  CB  ASP C 325      61.009  -7.157 -31.462  1.00 55.79           C
ANISOU 2415  CB  ASP C 325     7980   6356   6863    763   -170   -513       C
ATOM   2416  CG  ASP C 325      60.480  -6.466 -30.218  1.00 56.28           C
ANISOU 2416  CG  ASP C 325     8019   6464   6900    718   -211   -496       C
ATOM   2417  OD1 ASP C 325      61.256  -6.310 -29.251  1.00 57.61           O
ANISOU 2417  OD1 ASP C 325     8141   6669   7081    716   -226   -452       O
ATOM   2418  OD2 ASP C 325      59.290  -6.087 -30.203  1.00 55.14           O
ANISOU 2418  OD2 ASP C 325     7903   6323   6726    683   -228   -526       O
ATOM   2419  N   SER C 326      58.777  -7.890 -32.990  1.00 59.98           N
ANISOU 2419  N   SER C 326     8614   6815   7359    745   -159   -605       N
ATOM   2420  CA  SER C 326      57.440  -8.296 -33.408  1.00 58.93           C
ANISOU 2420  CA  SER C 326     8530   6654   7207    723   -165   -645       C
ATOM   2421  C   SER C 326      56.343  -7.550 -32.650  1.00 58.86           C
ANISOU 2421  C   SER C 326     8521   6678   7165    675   -203   -649       C
ATOM   2422  O   SER C 326      55.237  -7.373 -33.160  1.00 57.73           O
ANISOU 2422  O   SER C 326     8413   6528   6994    652   -209   -687       O
ATOM   2423  CB  SER C 326      57.265  -9.804 -33.227  1.00 59.01           C
ANISOU 2423  CB  SER C 326     8560   6609   7254    739   -158   -637       C
ATOM   2424  OG  SER C 326      58.279 -10.518 -33.912  1.00 59.59           O
ANISOU 2424  OG  SER C 326     8633   6648   7362    785   -119   -634       O
ATOM   2425  N   SER C 327      56.658  -7.111 -31.436  1.00 68.40           N
ANISOU 2425  N   SER C 327     9690   7923   8376    659   -228   -610       N
ATOM   2426  CA  SER C 327      55.681  -6.428 -30.596  1.00 68.55           C
ANISOU 2426  CA  SER C 327     9706   7973   8366    612   -262   -611       C
ATOM   2427  C   SER C 327      55.750  -4.909 -30.743  1.00 68.35           C
ANISOU 2427  C   SER C 327     9663   7995   8311    593   -264   -624       C
ATOM   2428  O   SER C 327      54.944  -4.188 -30.156  1.00 68.41           O
ANISOU 2428  O   SER C 327     9669   8031   8295    554   -287   -630       O
ATOM   2429  CB  SER C 327      55.872  -6.821 -29.129  1.00 69.79           C
ANISOU 2429  CB  SER C 327     9832   8147   8539    600   -288   -563       C
ATOM   2430  OG  SER C 327      57.161  -6.455 -28.667  1.00 70.67           O
ANISOU 2430  OG  SER C 327     9896   8291   8665    616   -285   -527       O
ATOM   2431  N   ASN C 328      56.709  -4.428 -31.529  1.00 55.19           N
ANISOU 2431  N   ASN C 328     7983   6338   6649    619   -238   -628       N
ATOM   2432  CA  ASN C 328      56.904  -2.990 -31.698  1.00 54.22           C
ANISOU 2432  CA  ASN C 328     7840   6257   6504    604   -235   -637       C
ATOM   2433  C   ASN C 328      56.536  -2.488 -33.088  1.00 53.16           C
ANISOU 2433  C   ASN C 328     7735   6113   6348    612   -212   -678       C
ATOM   2434  O   ASN C 328      55.963  -1.409 -33.235  1.00 52.77           O
ANISOU 2434  O   ASN C 328     7687   6090   6274    587   -217   -694       O
ATOM   2435  CB  ASN C 328      58.354  -2.603 -31.398  1.00 54.80           C
ANISOU 2435  CB  ASN C 328     7867   6358   6598    623   -225   -606       C
ATOM   2436  CG  ASN C 328      58.811  -3.061 -30.031  1.00 56.71           C
ANISOU 2436  CG  ASN C 328     8074   6616   6857    616   -248   -562       C
ATOM   2437  OD1 ASN C 328      59.993  -3.331 -29.818  1.00 58.25           O
ANISOU 2437  OD1 ASN C 328     8236   6819   7077    641   -239   -530       O
ATOM   2438  ND2 ASN C 328      57.874  -3.160 -29.098  1.00 56.93           N
ANISOU 2438  ND2 ASN C 328     8108   6652   6872    581   -278   -558       N
ATOM   2439  N   ILE C 329      56.873  -3.285 -34.099  1.00 58.90           N
ANISOU 2439  N   ILE C 329     8486   6806   7087    648   -186   -692       N
ATOM   2440  CA  ILE C 329      56.788  -2.877 -35.502  1.00 58.20           C
ANISOU 2440  CA  ILE C 329     8421   6713   6979    662   -159   -726       C
ATOM   2441  C   ILE C 329      55.421  -2.320 -35.925  1.00 57.48           C
ANISOU 2441  C   ILE C 329     8359   6629   6851    631   -171   -758       C
ATOM   2442  O   ILE C 329      55.345  -1.437 -36.779  1.00 57.72           O
ANISOU 2442  O   ILE C 329     8394   6678   6860    632   -157   -775       O
ATOM   2443  CB  ILE C 329      57.209  -4.040 -36.441  1.00 58.38           C
ANISOU 2443  CB  ILE C 329     8470   6693   7019    701   -130   -740       C
ATOM   2444  CG1 ILE C 329      57.393  -3.553 -37.881  1.00 58.07           C
ANISOU 2444  CG1 ILE C 329     8447   6657   6958    719    -99   -770       C
ATOM   2445  CG2 ILE C 329      56.221  -5.196 -36.359  1.00 57.89           C
ANISOU 2445  CG2 ILE C 329     8445   6590   6959    691   -142   -757       C
ATOM   2446  CD1 ILE C 329      58.804  -3.116 -38.198  1.00 58.63           C
ANISOU 2446  CD1 ILE C 329     8487   6743   7048    751    -71   -752       C
ATOM   2447  N   ASP C 330      54.351  -2.817 -35.313  1.00 69.94           N
ANISOU 2447  N   ASP C 330     9956   8195   8423    604   -198   -763       N
ATOM   2448  CA  ASP C 330      53.001  -2.388 -35.673  1.00 69.26           C
ANISOU 2448  CA  ASP C 330     9897   8115   8305    575   -211   -791       C
ATOM   2449  C   ASP C 330      52.680  -0.972 -35.197  1.00 68.64           C
ANISOU 2449  C   ASP C 330     9794   8078   8209    546   -223   -784       C
ATOM   2450  O   ASP C 330      51.717  -0.360 -35.657  1.00 67.91           O
ANISOU 2450  O   ASP C 330     9717   7996   8091    526   -228   -804       O
ATOM   2451  CB  ASP C 330      51.957  -3.368 -35.130  1.00 69.97           C
ANISOU 2451  CB  ASP C 330    10011   8177   8396    554   -235   -797       C
ATOM   2452  CG  ASP C 330      52.005  -4.716 -35.822  1.00 71.13           C
ANISOU 2452  CG  ASP C 330    10191   8279   8557    578   -218   -815       C
ATOM   2453  OD1 ASP C 330      52.601  -4.803 -36.916  1.00 71.20           O
ANISOU 2453  OD1 ASP C 330    10209   8279   8563    607   -189   -832       O
ATOM   2454  OD2 ASP C 330      51.439  -5.686 -35.275  1.00 71.93           O
ANISOU 2454  OD2 ASP C 330    10307   8352   8671    568   -233   -814       O
ATOM   2455  N   GLY C 331      53.487  -0.455 -34.277  1.00 49.98           N
ANISOU 2455  N   GLY C 331     7390   5737   5861    542   -228   -755       N
ATOM   2456  CA  GLY C 331      53.253   0.864 -33.717  1.00 49.77           C
ANISOU 2456  CA  GLY C 331     7339   5748   5823    512   -237   -749       C
ATOM   2457  C   GLY C 331      53.773   1.999 -34.579  1.00 49.38           C
ANISOU 2457  C   GLY C 331     7277   5719   5766    523   -211   -756       C
ATOM   2458  O   GLY C 331      53.502   3.168 -34.305  1.00 49.31           O
ANISOU 2458  O   GLY C 331     7250   5737   5749    499   -212   -756       O
ATOM   2459  N   PHE C 332      54.518   1.657 -35.625  1.00 38.29           N
ANISOU 2459  N   PHE C 332     5880   4302   4367    560   -184   -762       N
ATOM   2460  CA  PHE C 332      55.120   2.661 -36.496  1.00 37.74           C
ANISOU 2460  CA  PHE C 332     5798   4251   4292    575   -156   -765       C
ATOM   2461  C   PHE C 332      54.327   2.867 -37.785  1.00 37.50           C
ANISOU 2461  C   PHE C 332     5799   4216   4232    580   -143   -792       C
ATOM   2462  O   PHE C 332      54.854   3.396 -38.764  1.00 38.06           O
ANISOU 2462  O   PHE C 332     5867   4296   4297    602   -116   -796       O
ATOM   2463  CB  PHE C 332      56.563   2.278 -36.837  1.00 37.37           C
ANISOU 2463  CB  PHE C 332     5733   4198   4267    614   -132   -751       C
ATOM   2464  CG  PHE C 332      57.467   2.176 -35.641  1.00 38.92           C
ANISOU 2464  CG  PHE C 332     5891   4406   4491    611   -143   -720       C
ATOM   2465  CD1 PHE C 332      57.716   0.950 -35.046  1.00 39.37           C
ANISOU 2465  CD1 PHE C 332     5950   4442   4568    622   -155   -705       C
ATOM   2466  CD2 PHE C 332      58.073   3.306 -35.115  1.00 39.11           C
ANISOU 2466  CD2 PHE C 332     5874   4464   4521    597   -141   -705       C
ATOM   2467  CE1 PHE C 332      58.550   0.852 -33.947  1.00 40.34           C
ANISOU 2467  CE1 PHE C 332     6034   4580   4713    619   -167   -673       C
ATOM   2468  CE2 PHE C 332      58.908   3.215 -34.016  1.00 39.89           C
ANISOU 2468  CE2 PHE C 332     5935   4579   4642    591   -153   -677       C
ATOM   2469  CZ  PHE C 332      59.146   1.987 -33.432  1.00 40.86           C
ANISOU 2469  CZ  PHE C 332     6060   4685   4782    603   -167   -659       C
ATOM   2470  N   VAL C 333      53.063   2.452 -37.782  1.00 50.22           N
ANISOU 2470  N   VAL C 333     7441   5816   5825    560   -163   -809       N
ATOM   2471  CA  VAL C 333      52.219   2.572 -38.969  1.00 49.52           C
ANISOU 2471  CA  VAL C 333     7382   5727   5705    561   -155   -834       C
ATOM   2472  C   VAL C 333      51.874   4.027 -39.283  1.00 49.52           C
ANISOU 2472  C   VAL C 333     7366   5758   5690    548   -147   -830       C
ATOM   2473  O   VAL C 333      51.414   4.765 -38.411  1.00 49.75           O
ANISOU 2473  O   VAL C 333     7377   5802   5724    519   -162   -820       O
ATOM   2474  CB  VAL C 333      50.925   1.743 -38.832  1.00 48.82           C
ANISOU 2474  CB  VAL C 333     7327   5621   5603    540   -181   -852       C
ATOM   2475  CG1 VAL C 333      49.979   2.030 -39.987  1.00 48.06           C
ANISOU 2475  CG1 VAL C 333     7256   5534   5470    535   -176   -875       C
ATOM   2476  CG2 VAL C 333      51.253   0.261 -38.768  1.00 49.41           C
ANISOU 2476  CG2 VAL C 333     7421   5660   5693    557   -182   -859       C
ATOM   2477  N   ASN C 334      52.111   4.424 -40.532  1.00 52.76           N
ANISOU 2477  N   ASN C 334     7783   6178   6083    569   -122   -838       N
ATOM   2478  CA  ASN C 334      51.849   5.785 -41.001  1.00 52.81           C
ANISOU 2478  CA  ASN C 334     7774   6212   6077    562   -108   -831       C
ATOM   2479  C   ASN C 334      52.623   6.850 -40.224  1.00 53.21           C
ANISOU 2479  C   ASN C 334     7784   6279   6156    555    -99   -808       C
ATOM   2480  O   ASN C 334      52.177   7.990 -40.100  1.00 53.20           O
ANISOU 2480  O   ASN C 334     7766   6295   6153    537    -96   -800       O
ATOM   2481  CB  ASN C 334      50.348   6.094 -40.984  1.00 53.02           C
ANISOU 2481  CB  ASN C 334     7816   6247   6082    533   -129   -839       C
ATOM   2482  CG  ASN C 334      49.560   5.214 -41.934  1.00 53.51           C
ANISOU 2482  CG  ASN C 334     7917   6300   6113    538   -135   -863       C
ATOM   2483  OD1 ASN C 334      50.063   4.800 -42.978  1.00 53.86           O
ANISOU 2483  OD1 ASN C 334     7977   6344   6144    564   -115   -875       O
ATOM   2484  ND2 ASN C 334      48.314   4.924 -41.576  1.00 53.81           N
ANISOU 2484  ND2 ASN C 334     7972   6334   6139    510   -162   -872       N
ATOM   2485  N   CYS C 335      53.788   6.467 -39.713  1.00 59.66           N
ANISOU 2485  N   CYS C 335     8581   7089   6997    570    -94   -797       N
ATOM   2486  CA  CYS C 335      54.619   7.367 -38.925  1.00 60.00           C
ANISOU 2486  CA  CYS C 335     8583   7148   7066    561    -87   -777       C
ATOM   2487  C   CYS C 335      55.607   8.106 -39.825  1.00 60.15           C
ANISOU 2487  C   CYS C 335     8585   7180   7091    588    -51   -770       C
ATOM   2488  O   CYS C 335      56.341   7.484 -40.591  1.00 60.73           O
ANISOU 2488  O   CYS C 335     8666   7244   7163    621    -33   -772       O
ATOM   2489  CB  CYS C 335      55.370   6.576 -37.852  1.00 60.56           C
ANISOU 2489  CB  CYS C 335     8639   7211   7160    561   -102   -766       C
ATOM   2490  SG  CYS C 335      55.876   7.537 -36.409  1.00 67.84           S
ANISOU 2490  SG  CYS C 335     9513   8157   8105    529   -111   -747       S
ATOM   2491  N   THR C 336      55.619   9.433 -39.733  1.00 35.87           N
ANISOU 2491  N   THR C 336     5483   4124   4022    573    -37   -760       N
ATOM   2492  CA  THR C 336      56.504  10.247 -40.563  1.00 36.29           C
ANISOU 2492  CA  THR C 336     5517   4189   4082    596     -1   -751       C
ATOM   2493  C   THR C 336      57.700  10.774 -39.776  1.00 36.90           C
ANISOU 2493  C   THR C 336     5552   4277   4193    592      8   -735       C
ATOM   2494  O   THR C 336      58.780  10.976 -40.331  1.00 37.33           O
ANISOU 2494  O   THR C 336     5590   4336   4258    618     35   -726       O
ATOM   2495  CB  THR C 336      55.758  11.440 -41.191  1.00 36.23           C
ANISOU 2495  CB  THR C 336     5508   4195   4063    586     14   -748       C
ATOM   2496  OG1 THR C 336      55.247  12.288 -40.155  1.00 35.89           O
ANISOU 2496  OG1 THR C 336     5444   4157   4033    549      4   -744       O
ATOM   2497  CG2 THR C 336      54.608  10.954 -42.061  1.00 35.91           C
ANISOU 2497  CG2 THR C 336     5507   4150   3986    590      5   -762       C
ATOM   2498  N   LYS C 337      57.497  10.998 -38.482  1.00 39.54           N
ANISOU 2498  N   LYS C 337     5867   4616   4539    558    -14   -733       N
ATOM   2499  CA  LYS C 337      58.554  11.501 -37.613  1.00 40.12           C
ANISOU 2499  CA  LYS C 337     5898   4704   4640    547    -10   -720       C
ATOM   2500  C   LYS C 337      58.692  10.607 -36.390  1.00 40.56           C
ANISOU 2500  C   LYS C 337     5948   4759   4702    532    -43   -716       C
ATOM   2501  O   LYS C 337      57.699  10.239 -35.767  1.00 41.01           O
ANISOU 2501  O   LYS C 337     6024   4811   4748    508    -70   -724       O
ATOM   2502  CB  LYS C 337      58.246  12.936 -37.181  1.00 40.25           C
ANISOU 2502  CB  LYS C 337     5890   4735   4667    513      1   -720       C
ATOM   2503  CG  LYS C 337      59.279  13.546 -36.247  1.00 41.02           C
ANISOU 2503  CG  LYS C 337     5942   4850   4792    495      5   -712       C
ATOM   2504  CD  LYS C 337      58.843  14.925 -35.781  1.00 41.19           C
ANISOU 2504  CD  LYS C 337     5944   4882   4825    458     17   -718       C
ATOM   2505  CE  LYS C 337      59.885  15.561 -34.876  1.00 42.30           C
ANISOU 2505  CE  LYS C 337     6038   5042   4991    435     23   -715       C
ATOM   2506  NZ  LYS C 337      59.453  16.902 -34.394  1.00 42.34           N
ANISOU 2506  NZ  LYS C 337     6023   5053   5010    396     39   -725       N
ATOM   2507  N   ILE C 338      59.925  10.254 -36.044  1.00 32.36           N
ANISOU 2507  N   ILE C 338     4883   3727   3683    546    -40   -701       N
ATOM   2508  CA  ILE C 338      60.156   9.381 -34.899  1.00 32.75           C
ANISOU 2508  CA  ILE C 338     4923   3779   3740    535    -70   -691       C
ATOM   2509  C   ILE C 338      60.848  10.101 -33.745  1.00 33.31           C
ANISOU 2509  C   ILE C 338     4948   3881   3828    505    -76   -680       C
ATOM   2510  O   ILE C 338      62.007  10.504 -33.846  1.00 33.88           O
ANISOU 2510  O   ILE C 338     4987   3968   3919    516    -58   -668       O
ATOM   2511  CB  ILE C 338      60.926   8.108 -35.301  1.00 33.16           C
ANISOU 2511  CB  ILE C 338     4984   3815   3801    576    -67   -680       C
ATOM   2512  CG1 ILE C 338      60.016   7.205 -36.134  1.00 32.62           C
ANISOU 2512  CG1 ILE C 338     4965   3716   3711    595    -70   -696       C
ATOM   2513  CG2 ILE C 338      61.421   7.366 -34.069  1.00 33.83           C
ANISOU 2513  CG2 ILE C 338     5046   3908   3899    567    -94   -660       C
ATOM   2514  CD1 ILE C 338      60.655   5.916 -36.565  1.00 33.55           C
ANISOU 2514  CD1 ILE C 338     5096   3812   3840    634    -64   -690       C
ATOM   2515  N   LEU C 339      60.111  10.263 -32.651  1.00 30.04           N
ANISOU 2515  N   LEU C 339     4530   3477   3406    465   -102   -686       N
ATOM   2516  CA  LEU C 339      60.617  10.940 -31.467  1.00 30.07           C
ANISOU 2516  CA  LEU C 339     4492   3513   3420    428   -111   -680       C
ATOM   2517  C   LEU C 339      61.559  10.024 -30.700  1.00 30.34           C
ANISOU 2517  C   LEU C 339     4503   3562   3464    437   -131   -656       C
ATOM   2518  O   LEU C 339      61.147   9.326 -29.775  1.00 30.34           O
ANISOU 2518  O   LEU C 339     4507   3567   3455    420   -162   -650       O
ATOM   2519  CB  LEU C 339      59.457  11.372 -30.570  1.00 29.82           C
ANISOU 2519  CB  LEU C 339     4467   3487   3374    382   -131   -696       C
ATOM   2520  CG  LEU C 339      58.323  12.123 -31.270  1.00 29.55           C
ANISOU 2520  CG  LEU C 339     4460   3436   3331    375   -115   -716       C
ATOM   2521  CD1 LEU C 339      57.269  12.568 -30.266  1.00 29.34           C
ANISOU 2521  CD1 LEU C 339     4435   3417   3295    328   -132   -730       C
ATOM   2522  CD2 LEU C 339      58.863  13.312 -32.052  1.00 29.58           C
ANISOU 2522  CD2 LEU C 339     4445   3443   3350    382    -76   -719       C
ATOM   2523  N   GLY C 340      62.826  10.030 -31.094  1.00 30.60           N
ANISOU 2523  N   GLY C 340     4509   3603   3516    464   -113   -641       N
ATOM   2524  CA  GLY C 340      63.815   9.167 -30.481  1.00 30.91           C
ANISOU 2524  CA  GLY C 340     4522   3656   3568    477   -128   -613       C
ATOM   2525  C   GLY C 340      64.672   8.473 -31.519  1.00 31.17           C
ANISOU 2525  C   GLY C 340     4559   3668   3615    531   -106   -599       C
ATOM   2526  O   GLY C 340      65.019   9.057 -32.546  1.00 31.17           O
ANISOU 2526  O   GLY C 340     4561   3660   3622    551    -74   -607       O
ATOM   2527  N   ASN C 341      65.003   7.214 -31.258  1.00 37.86           N
ANISOU 2527  N   ASN C 341     5409   4505   4470    555   -121   -577       N
ATOM   2528  CA  ASN C 341      65.919   6.480 -32.117  1.00 38.44           C
ANISOU 2528  CA  ASN C 341     5482   4559   4563    606    -99   -561       C
ATOM   2529  C   ASN C 341      65.304   5.209 -32.687  1.00 37.97           C
ANISOU 2529  C   ASN C 341     5470   4458   4500    637   -100   -566       C
ATOM   2530  O   ASN C 341      64.211   4.803 -32.296  1.00 36.93           O
ANISOU 2530  O   ASN C 341     5366   4313   4351    617   -123   -577       O
ATOM   2531  CB  ASN C 341      67.186   6.129 -31.338  1.00 40.12           C
ANISOU 2531  CB  ASN C 341     5645   4799   4798    614   -108   -525       C
ATOM   2532  CG  ASN C 341      67.406   7.040 -30.148  1.00 41.11           C
ANISOU 2532  CG  ASN C 341     5727   4973   4919    565   -128   -520       C
ATOM   2533  OD1 ASN C 341      67.896   8.159 -30.291  1.00 41.41           O
ANISOU 2533  OD1 ASN C 341     5738   5032   4962    550   -110   -529       O
ATOM   2534  ND2 ASN C 341      67.048   6.561 -28.963  1.00 40.17           N
ANISOU 2534  ND2 ASN C 341     5600   4871   4791    539   -163   -507       N
ATOM   2535  N   LEU C 342      66.019   4.589 -33.619  1.00 32.01           N
ANISOU 2535  N   LEU C 342     4722   3680   3761    683    -73   -559       N
ATOM   2536  CA  LEU C 342      65.632   3.287 -34.141  1.00 32.15           C
ANISOU 2536  CA  LEU C 342     4780   3656   3781    714    -70   -564       C
ATOM   2537  C   LEU C 342      66.777   2.300 -33.974  1.00 32.60           C
ANISOU 2537  C   LEU C 342     4812   3705   3870    751    -63   -530       C
ATOM   2538  O   LEU C 342      67.893   2.547 -34.429  1.00 32.83           O
ANISOU 2538  O   LEU C 342     4814   3743   3918    777    -38   -517       O
ATOM   2539  CB  LEU C 342      65.229   3.385 -35.611  1.00 32.09           C
ANISOU 2539  CB  LEU C 342     4812   3622   3759    737    -40   -595       C
ATOM   2540  CG  LEU C 342      63.869   4.024 -35.890  1.00 31.70           C
ANISOU 2540  CG  LEU C 342     4796   3570   3676    707    -48   -626       C
ATOM   2541  CD1 LEU C 342      63.542   3.933 -37.369  1.00 31.72           C
ANISOU 2541  CD1 LEU C 342     4838   3550   3664    733    -19   -652       C
ATOM   2542  CD2 LEU C 342      62.788   3.358 -35.053  1.00 31.55           C
ANISOU 2542  CD2 LEU C 342     4799   3541   3647    681    -83   -629       C
ATOM   2543  N   ASP C 343      66.495   1.184 -33.312  1.00 43.07           N
ANISOU 2543  N   ASP C 343     6147   5014   5205    754    -84   -514       N
ATOM   2544  CA  ASP C 343      67.507   0.165 -33.069  1.00 44.22           C
ANISOU 2544  CA  ASP C 343     6268   5149   5385    790    -78   -477       C
ATOM   2545  C   ASP C 343      67.125  -1.159 -33.716  1.00 44.03           C
ANISOU 2545  C   ASP C 343     6288   5070   5372    823    -64   -486       C
ATOM   2546  O   ASP C 343      66.036  -1.683 -33.486  1.00 43.29           O
ANISOU 2546  O   ASP C 343     6228   4954   5264    807    -83   -501       O
ATOM   2547  CB  ASP C 343      67.718  -0.033 -31.567  1.00 44.99           C
ANISOU 2547  CB  ASP C 343     6326   5278   5489    766   -115   -438       C
ATOM   2548  CG  ASP C 343      68.332   1.179 -30.898  1.00 46.12           C
ANISOU 2548  CG  ASP C 343     6420   5478   5626    734   -126   -427       C
ATOM   2549  OD1 ASP C 343      69.544   1.143 -30.599  1.00 46.95           O
ANISOU 2549  OD1 ASP C 343     6478   5607   5755    751   -121   -393       O
ATOM   2550  OD2 ASP C 343      67.604   2.169 -30.673  1.00 45.78           O
ANISOU 2550  OD2 ASP C 343     6384   5456   5556    693   -138   -453       O
ATOM   2551  N   PHE C 344      68.031  -1.691 -34.529  1.00 43.16           N
ANISOU 2551  N   PHE C 344     6175   4936   5288    869    -29   -479       N
ATOM   2552  CA  PHE C 344      67.839  -2.996 -35.145  1.00 42.30           C
ANISOU 2552  CA  PHE C 344     6103   4772   5196    904     -9   -488       C
ATOM   2553  C   PHE C 344      68.935  -3.944 -34.673  1.00 43.17           C
ANISOU 2553  C   PHE C 344     6179   4873   5353    939     -1   -441       C
ATOM   2554  O   PHE C 344      70.026  -3.977 -35.241  1.00 43.75           O
ANISOU 2554  O   PHE C 344     6231   4943   5450    975     31   -429       O
ATOM   2555  CB  PHE C 344      67.857  -2.881 -36.671  1.00 41.39           C
ANISOU 2555  CB  PHE C 344     6022   4633   5071    930     32   -527       C
ATOM   2556  CG  PHE C 344      66.780  -1.990 -37.225  1.00 40.56           C
ANISOU 2556  CG  PHE C 344     5950   4538   4921    898     26   -569       C
ATOM   2557  CD1 PHE C 344      66.993  -0.628 -37.369  1.00 40.80           C
ANISOU 2557  CD1 PHE C 344     5960   4609   4935    881     28   -573       C
ATOM   2558  CD2 PHE C 344      65.556  -2.514 -37.606  1.00 39.50           C
ANISOU 2558  CD2 PHE C 344     5868   4374   4765    887     19   -604       C
ATOM   2559  CE1 PHE C 344      66.005   0.194 -37.879  1.00 39.68           C
ANISOU 2559  CE1 PHE C 344     5846   4476   4755    854     24   -607       C
ATOM   2560  CE2 PHE C 344      64.563  -1.696 -38.118  1.00 38.49           C
ANISOU 2560  CE2 PHE C 344     5768   4259   4597    860     13   -638       C
ATOM   2561  CZ  PHE C 344      64.789  -0.341 -38.254  1.00 38.33           C
ANISOU 2561  CZ  PHE C 344     5724   4278   4562    845     16   -638       C
ATOM   2562  N   LEU C 345      68.641  -4.706 -33.625  1.00 37.85           N
ANISOU 2562  N   LEU C 345     5497   4193   4691    930    -29   -412       N
ATOM   2563  CA  LEU C 345      69.622  -5.613 -33.041  1.00 38.67           C
ANISOU 2563  CA  LEU C 345     5564   4290   4840    962    -25   -359       C
ATOM   2564  C   LEU C 345      69.412  -7.054 -33.500  1.00 38.59           C
ANISOU 2564  C   LEU C 345     5589   4214   4860    997     -1   -363       C
ATOM   2565  O   LEU C 345      68.386  -7.383 -34.098  1.00 37.96           O
ANISOU 2565  O   LEU C 345     5563   4098   4763    989      4   -406       O
ATOM   2566  CB  LEU C 345      69.581  -5.533 -31.513  1.00 39.34           C
ANISOU 2566  CB  LEU C 345     5609   4417   4922    930    -70   -316       C
ATOM   2567  CG  LEU C 345      69.845  -4.153 -30.904  1.00 39.60           C
ANISOU 2567  CG  LEU C 345     5601   4516   4927    891    -94   -312       C
ATOM   2568  CD1 LEU C 345      69.714  -4.198 -29.390  1.00 40.43           C
ANISOU 2568  CD1 LEU C 345     5672   4663   5026    858   -138   -273       C
ATOM   2569  CD2 LEU C 345      71.216  -3.633 -31.310  1.00 39.96           C
ANISOU 2569  CD2 LEU C 345     5604   4587   4993    916    -69   -294       C
ATOM   2570  N   ILE C 346      70.395  -7.903 -33.215  1.00 41.52           N
ANISOU 2570  N   ILE C 346     5927   4570   5278   1036     14   -316       N
ATOM   2571  CA  ILE C 346      70.355  -9.309 -33.605  1.00 41.30           C
ANISOU 2571  CA  ILE C 346     5927   4477   5290   1073     42   -314       C
ATOM   2572  C   ILE C 346      69.140 -10.020 -33.018  1.00 41.05           C
ANISOU 2572  C   ILE C 346     5929   4418   5250   1048     16   -321       C
ATOM   2573  O   ILE C 346      68.437 -10.747 -33.719  1.00 40.63           O
ANISOU 2573  O   ILE C 346     5927   4311   5201   1057     36   -359       O
ATOM   2574  CB  ILE C 346      71.631 -10.048 -33.159  1.00 41.46           C
ANISOU 2574  CB  ILE C 346     5896   4491   5365   1116     58   -251       C
ATOM   2575  CG1 ILE C 346      72.877  -9.324 -33.671  0.00 41.85           C
ANISOU 2575  CG1 ILE C 346     5908   4571   5424   1140     82   -240       C
ATOM   2576  CG2 ILE C 346      71.611 -11.490 -33.644  1.00 41.48           C
ANISOU 2576  CG2 ILE C 346     5929   4419   5413   1157     95   -252       C
ATOM   2577  CD1 ILE C 346      74.176  -9.906 -33.157  0.00 42.67           C
ANISOU 2577  CD1 ILE C 346     5952   4679   5579   1179     94   -173       C
ATOM   2578  N   THR C 347      68.897  -9.801 -31.730  1.00 38.61           N
ANISOU 2578  N   THR C 347     5591   4150   4931   1017    -28   -284       N
ATOM   2579  CA  THR C 347      67.777 -10.433 -31.043  1.00 38.54           C
ANISOU 2579  CA  THR C 347     5609   4121   4915    991    -56   -284       C
ATOM   2580  C   THR C 347      66.435  -9.874 -31.507  1.00 37.69           C
ANISOU 2580  C   THR C 347     5552   4009   4759    952    -68   -346       C
ATOM   2581  O   THR C 347      65.426 -10.574 -31.493  1.00 37.39           O
ANISOU 2581  O   THR C 347     5554   3933   4718    941    -74   -366       O
ATOM   2582  CB  THR C 347      67.891 -10.277 -29.515  1.00 39.37           C
ANISOU 2582  CB  THR C 347     5666   4277   5016    965   -100   -227       C
ATOM   2583  OG1 THR C 347      68.046  -8.892 -29.183  1.00 39.81           O
ANISOU 2583  OG1 THR C 347     5693   4400   5032    930   -124   -234       O
ATOM   2584  CG2 THR C 347      69.086 -11.055 -28.989  1.00 40.23           C
ANISOU 2584  CG2 THR C 347     5724   4385   5176   1005    -90   -159       C
ATOM   2585  N   GLY C 348      66.427  -8.611 -31.918  1.00 36.73           N
ANISOU 2585  N   GLY C 348     5429   3928   4600    931    -72   -375       N
ATOM   2586  CA  GLY C 348      65.207  -7.978 -32.385  1.00 35.89           C
ANISOU 2586  CA  GLY C 348     5365   3822   4448    895    -82   -430       C
ATOM   2587  C   GLY C 348      64.760  -8.500 -33.737  1.00 35.24           C
ANISOU 2587  C   GLY C 348     5338   3687   4365    916    -47   -481       C
ATOM   2588  O   GLY C 348      63.565  -8.608 -34.008  1.00 34.62           O
ANISOU 2588  O   GLY C 348     5303   3590   4261    891    -57   -519       O
ATOM   2589  N   LEU C 349      65.729  -8.827 -34.586  1.00 55.50           N
ANISOU 2589  N   LEU C 349     7899   6230   6957    959     -6   -481       N
ATOM   2590  CA  LEU C 349      65.443  -9.288 -35.940  1.00 55.09           C
ANISOU 2590  CA  LEU C 349     7896   6133   6903    980     32   -531       C
ATOM   2591  C   LEU C 349      65.187 -10.791 -35.984  1.00 55.69           C
ANISOU 2591  C   LEU C 349     7999   6144   7015   1001     49   -532       C
ATOM   2592  O   LEU C 349      64.364 -11.267 -36.767  1.00 55.48           O
ANISOU 2592  O   LEU C 349     8024   6080   6977    996     63   -581       O
ATOM   2593  CB  LEU C 349      66.604  -8.934 -36.873  1.00 55.19           C
ANISOU 2593  CB  LEU C 349     7892   6150   6926   1016     72   -534       C
ATOM   2594  CG  LEU C 349      66.267  -8.166 -38.154  1.00 54.38           C
ANISOU 2594  CG  LEU C 349     7822   6056   6783   1011     92   -588       C
ATOM   2595  CD1 LEU C 349      65.279  -8.943 -39.010  1.00 53.84           C
ANISOU 2595  CD1 LEU C 349     7814   5940   6701   1009    108   -640       C
ATOM   2596  CD2 LEU C 349      65.730  -6.781 -37.825  1.00 53.75           C
ANISOU 2596  CD2 LEU C 349     7731   6031   6659    969     59   -594       C
ATOM   2597  N   ASN C 350      65.895 -11.533 -35.140  1.00 49.75           N
ANISOU 2597  N   ASN C 350     7213   5381   6311   1023     48   -478       N
ATOM   2598  CA  ASN C 350      65.824 -12.990 -35.162  1.00 50.49           C
ANISOU 2598  CA  ASN C 350     7326   5409   6449   1049     71   -471       C
ATOM   2599  C   ASN C 350      64.952 -13.583 -34.057  1.00 51.04           C
ANISOU 2599  C   ASN C 350     7401   5469   6525   1023     35   -448       C
ATOM   2600  O   ASN C 350      64.703 -14.789 -34.035  1.00 49.39           O
ANISOU 2600  O   ASN C 350     7211   5201   6352   1038     51   -445       O
ATOM   2601  CB  ASN C 350      67.230 -13.590 -35.103  1.00 51.34           C
ANISOU 2601  CB  ASN C 350     7394   5500   6614   1100    103   -423       C
ATOM   2602  CG  ASN C 350      68.064 -13.240 -36.320  1.00 51.10           C
ANISOU 2602  CG  ASN C 350     7366   5467   6585   1132    147   -450       C
ATOM   2603  OD1 ASN C 350      67.534 -13.035 -37.412  1.00 50.33           O
ANISOU 2603  OD1 ASN C 350     7312   5354   6456   1125    166   -511       O
ATOM   2604  ND2 ASN C 350      69.378 -13.172 -36.138  1.00 51.46           N
ANISOU 2604  ND2 ASN C 350     7361   5527   6664   1166    164   -404       N
ATOM   2605  N   GLY C 351      64.492 -12.735 -33.144  1.00 36.94           N
ANISOU 2605  N   GLY C 351     5594   3736   4703    982    -12   -432       N
ATOM   2606  CA  GLY C 351      63.634 -13.180 -32.061  1.00 37.09           C
ANISOU 2606  CA  GLY C 351     5617   3754   4723    953    -48   -410       C
ATOM   2607  C   GLY C 351      64.352 -13.255 -30.727  1.00 37.94           C
ANISOU 2607  C   GLY C 351     5666   3897   4852    957    -72   -336       C
ATOM   2608  O   GLY C 351      65.561 -13.480 -30.673  1.00 38.49           O
ANISOU 2608  O   GLY C 351     5697   3970   4958    994    -53   -295       O
ATOM   2609  N   ASP C 352      63.602 -13.058 -29.647  1.00 58.48           N
ANISOU 2609  N   ASP C 352     8261   6529   7432    917   -115   -318       N
ATOM   2610  CA  ASP C 352      64.159 -13.124 -28.301  1.00 59.93           C
ANISOU 2610  CA  ASP C 352     8390   6752   7628    914   -143   -247       C
ATOM   2611  C   ASP C 352      63.496 -14.247 -27.508  1.00 60.46           C
ANISOU 2611  C   ASP C 352     8466   6785   7719    910   -157   -218       C
ATOM   2612  O   ASP C 352      62.372 -14.094 -27.032  1.00 60.34           O
ANISOU 2612  O   ASP C 352     8474   6778   7673    869   -186   -234       O
ATOM   2613  CB  ASP C 352      63.971 -11.788 -27.579  1.00 60.61           C
ANISOU 2613  CB  ASP C 352     8450   6915   7664    869   -184   -247       C
ATOM   2614  CG  ASP C 352      64.805 -11.684 -26.317  1.00 62.47           C
ANISOU 2614  CG  ASP C 352     8622   7205   7909    867   -210   -177       C
ATOM   2615  OD1 ASP C 352      65.822 -10.960 -26.333  1.00 63.03           O
ANISOU 2615  OD1 ASP C 352     8652   7320   7977    875   -207   -161       O
ATOM   2616  OD2 ASP C 352      64.447 -12.330 -25.309  1.00 63.45           O
ANISOU 2616  OD2 ASP C 352     8735   7330   8041    856   -233   -137       O
ATOM   2617  N   PRO C 353      64.196 -15.383 -27.369  1.00 72.60           N
ANISOU 2617  N   PRO C 353     9988   8283   9315    953   -133   -172       N
ATOM   2618  CA  PRO C 353      63.671 -16.561 -26.669  1.00 73.17           C
ANISOU 2618  CA  PRO C 353    10067   8315   9420    955   -138   -137       C
ATOM   2619  C   PRO C 353      63.475 -16.306 -25.179  1.00 74.17           C
ANISOU 2619  C   PRO C 353    10155   8501   9525    923   -187    -83       C
ATOM   2620  O   PRO C 353      62.572 -16.879 -24.569  1.00 74.57           O
ANISOU 2620  O   PRO C 353    10223   8533   9577    903   -204    -73       O
ATOM   2621  CB  PRO C 353      64.771 -17.611 -26.874  1.00 73.27           C
ANISOU 2621  CB  PRO C 353    10056   8282   9500   1014    -98    -92       C
ATOM   2622  CG  PRO C 353      65.579 -17.116 -28.029  1.00 72.85           C
ANISOU 2622  CG  PRO C 353    10005   8226   9448   1041    -63   -127       C
ATOM   2623  CD  PRO C 353      65.535 -15.628 -27.927  1.00 72.75           C
ANISOU 2623  CD  PRO C 353     9979   8289   9375   1003    -95   -149       C
ATOM   2624  N   TRP C 354      64.319 -15.454 -24.605  1.00 75.15           N
ANISOU 2624  N   TRP C 354    10227   8697   9631    917   -207    -48       N
ATOM   2625  CA  TRP C 354      64.265 -15.163 -23.178  1.00 76.41           C
ANISOU 2625  CA  TRP C 354    10344   8921   9766    886   -253      4       C
ATOM   2626  C   TRP C 354      62.980 -14.429 -22.805  1.00 75.80           C
ANISOU 2626  C   TRP C 354    10296   8872   9633    828   -287    -38       C
ATOM   2627  O   TRP C 354      62.396 -14.678 -21.751  1.00 76.28           O
ANISOU 2627  O   TRP C 354    10349   8952   9682    801   -318     -7       O
ATOM   2628  CB  TRP C 354      65.485 -14.342 -22.755  1.00 77.80           C
ANISOU 2628  CB  TRP C 354    10459   9170   9933    890   -265     42       C
ATOM   2629  CG  TRP C 354      66.791 -14.989 -23.109  1.00 78.82           C
ANISOU 2629  CG  TRP C 354    10554   9276  10118    947   -231     86       C
ATOM   2630  CD1 TRP C 354      67.454 -15.942 -22.392  1.00 79.54           C
ANISOU 2630  CD1 TRP C 354    10604   9363  10254    978   -230    164       C
ATOM   2631  CD2 TRP C 354      67.592 -14.727 -24.268  1.00 78.83           C
ANISOU 2631  CD2 TRP C 354    10558   9257  10136    981   -193     57       C
ATOM   2632  NE1 TRP C 354      68.618 -16.291 -23.033  1.00 79.67           N
ANISOU 2632  NE1 TRP C 354    10598   9357  10318   1030   -192    185       N
ATOM   2633  CE2 TRP C 354      68.727 -15.560 -24.187  1.00 79.22           C
ANISOU 2633  CE2 TRP C 354    10568   9289  10244   1032   -168    119       C
ATOM   2634  CE3 TRP C 354      67.462 -13.871 -25.365  0.00 78.20           C
ANISOU 2634  CE3 TRP C 354    10510   9173  10029    973   -176    -12       C
ATOM   2635  CZ2 TRP C 354      69.723 -15.561 -25.161  0.00 78.97           C
ANISOU 2635  CZ2 TRP C 354    10527   9234  10243   1076   -127    111       C
ATOM   2636  CZ3 TRP C 354      68.452 -13.874 -26.332  0.00 78.01           C
ANISOU 2636  CZ3 TRP C 354    10479   9129  10034   1016   -135    -20       C
ATOM   2637  CH2 TRP C 354      69.568 -14.713 -26.223  0.00 78.36           C
ANISOU 2637  CH2 TRP C 354    10484   9155  10136   1066   -111     40       C
ATOM   2638  N   HIS C 355      62.544 -13.527 -23.678  1.00 62.06           N
ANISOU 2638  N   HIS C 355     8589   7134   7859    809   -281   -106       N
ATOM   2639  CA  HIS C 355      61.326 -12.759 -23.442  1.00 61.08           C
ANISOU 2639  CA  HIS C 355     8493   7033   7683    756   -310   -149       C
ATOM   2640  C   HIS C 355      60.175 -13.264 -24.307  1.00 59.45           C
ANISOU 2640  C   HIS C 355     8350   6761   7477    752   -293   -205       C
ATOM   2641  O   HIS C 355      59.135 -12.613 -24.411  1.00 58.40           O
ANISOU 2641  O   HIS C 355     8246   6639   7303    714   -309   -251       O
ATOM   2642  CB  HIS C 355      61.571 -11.269 -23.693  1.00 61.14           C
ANISOU 2642  CB  HIS C 355     8487   7097   7648    732   -318   -182       C
ATOM   2643  CG  HIS C 355      62.558 -10.655 -22.752  1.00 62.87           C
ANISOU 2643  CG  HIS C 355     8643   7388   7857    724   -339   -134       C
ATOM   2644  ND1 HIS C 355      62.183 -10.050 -21.568  1.00 63.88           N
ANISOU 2644  ND1 HIS C 355     8747   7577   7948    677   -378   -118       N
ATOM   2645  CD2 HIS C 355      63.906 -10.549 -22.812  1.00 63.60           C
ANISOU 2645  CD2 HIS C 355     8690   7503   7972    754   -327   -100       C
ATOM   2646  CE1 HIS C 355      63.256  -9.601 -20.945  1.00 64.84           C
ANISOU 2646  CE1 HIS C 355     8812   7758   8068    678   -390    -77       C
ATOM   2647  NE2 HIS C 355      64.317  -9.891 -21.680  1.00 64.63           N
ANISOU 2647  NE2 HIS C 355     8770   7709   8077    724   -360    -64       N
ATOM   2648  N   LYS C 356      60.378 -14.427 -24.921  1.00 68.62           N
ANISOU 2648  N   LYS C 356     9531   7854   8686    793   -259   -202       N
ATOM   2649  CA  LYS C 356      59.362 -15.083 -25.743  1.00 67.71           C
ANISOU 2649  CA  LYS C 356     9476   7673   8579    791   -241   -254       C
ATOM   2650  C   LYS C 356      58.801 -14.186 -26.847  1.00 66.97           C
ANISOU 2650  C   LYS C 356     9419   7581   8444    773   -233   -328       C
ATOM   2651  O   LYS C 356      57.587 -14.096 -27.031  1.00 66.32           O
ANISOU 2651  O   LYS C 356     9377   7487   8336    741   -245   -369       O
ATOM   2652  CB  LYS C 356      58.230 -15.634 -24.869  1.00 67.25           C
ANISOU 2652  CB  LYS C 356     9433   7603   8516    760   -267   -241       C
ATOM   2653  CG  LYS C 356      58.673 -16.727 -23.907  1.00 67.74           C
ANISOU 2653  CG  LYS C 356     9465   7649   8624    782   -269   -168       C
ATOM   2654  CD  LYS C 356      57.510 -17.243 -23.074  1.00 67.79           C
ANISOU 2654  CD  LYS C 356     9488   7645   8625    749   -294   -157       C
ATOM   2655  CE  LYS C 356      57.960 -18.331 -22.110  1.00 68.64           C
ANISOU 2655  CE  LYS C 356     9564   7738   8779    773   -294    -78       C
ATOM   2656  NZ  LYS C 356      58.502 -19.524 -22.820  1.00 68.66           N
ANISOU 2656  NZ  LYS C 356     9577   7662   8846    824   -248    -70       N
ATOM   2657  N   ILE C 357      59.695 -13.525 -27.577  1.00 44.94           N
ANISOU 2657  N   ILE C 357     6615   4809   5649    793   -214   -341       N
ATOM   2658  CA  ILE C 357      59.299 -12.676 -28.695  1.00 43.84           C
ANISOU 2658  CA  ILE C 357     6508   4675   5475    782   -203   -405       C
ATOM   2659  C   ILE C 357      59.763 -13.290 -30.012  1.00 43.12           C
ANISOU 2659  C   ILE C 357     6444   4529   5411    823   -156   -436       C
ATOM   2660  O   ILE C 357      60.961 -13.472 -30.226  1.00 43.30           O
ANISOU 2660  O   ILE C 357     6439   4548   5464    862   -131   -410       O
ATOM   2661  CB  ILE C 357      59.877 -11.255 -28.560  1.00 43.58           C
ANISOU 2661  CB  ILE C 357     6440   4709   5408    768   -216   -403       C
ATOM   2662  CG1 ILE C 357      59.493 -10.651 -27.207  1.00 44.47           C
ANISOU 2662  CG1 ILE C 357     6525   4878   5495    726   -260   -373       C
ATOM   2663  CG2 ILE C 357      59.394 -10.372 -29.701  1.00 41.74           C
ANISOU 2663  CG2 ILE C 357     6240   4480   5139    755   -204   -465       C
ATOM   2664  CD1 ILE C 357      60.078  -9.277 -26.964  0.00 45.45           C
ANISOU 2664  CD1 ILE C 357     6611   5067   5589    708   -272   -370       C
ATOM   2665  N   PRO C 358      58.808 -13.614 -30.899  1.00 52.92           N
ANISOU 2665  N   PRO C 358     7737   5729   6640    813   -143   -493       N
ATOM   2666  CA  PRO C 358      59.080 -14.296 -32.171  1.00 52.41           C
ANISOU 2666  CA  PRO C 358     7705   5610   6598    847    -97   -530       C
ATOM   2667  C   PRO C 358      59.975 -13.484 -33.102  1.00 52.55           C
ANISOU 2667  C   PRO C 358     7712   5652   6602    869    -73   -548       C
ATOM   2668  O   PRO C 358      60.166 -12.287 -32.889  1.00 52.92           O
ANISOU 2668  O   PRO C 358     7734   5756   6616    852    -92   -543       O
ATOM   2669  CB  PRO C 358      57.687 -14.447 -32.793  1.00 51.38           C
ANISOU 2669  CB  PRO C 358     7629   5454   6438    816   -102   -590       C
ATOM   2670  CG  PRO C 358      56.736 -14.334 -31.649  1.00 51.83           C
ANISOU 2670  CG  PRO C 358     7682   5533   6479    775   -145   -570       C
ATOM   2671  CD  PRO C 358      57.371 -13.362 -30.708  1.00 52.49           C
ANISOU 2671  CD  PRO C 358     7715   5681   6549    767   -172   -525       C
ATOM   2672  N   ALA C 359      60.513 -14.140 -34.126  1.00 60.41           N
ANISOU 2672  N   ALA C 359     8726   6602   7624    906    -27   -571       N
ATOM   2673  CA  ALA C 359      61.358 -13.474 -35.110  1.00 59.80           C
ANISOU 2673  CA  ALA C 359     8642   6542   7536    929      1   -590       C
ATOM   2674  C   ALA C 359      60.552 -12.461 -35.915  1.00 59.27           C
ANISOU 2674  C   ALA C 359     8605   6505   7411    899     -8   -645       C
ATOM   2675  O   ALA C 359      59.344 -12.616 -36.094  1.00 59.26           O
ANISOU 2675  O   ALA C 359     8642   6490   7384    869    -22   -681       O
ATOM   2676  CB  ALA C 359      62.007 -14.494 -36.032  1.00 59.24           C
ANISOU 2676  CB  ALA C 359     8590   6413   7507    974     54   -606       C
ATOM   2677  N   LEU C 360      61.230 -11.427 -36.400  1.00 61.52           N
ANISOU 2677  N   LEU C 360     8869   6830   7674    907      1   -648       N
ATOM   2678  CA  LEU C 360      60.570 -10.341 -37.115  1.00 60.82           C
ANISOU 2678  CA  LEU C 360     8802   6776   7532    881     -7   -690       C
ATOM   2679  C   LEU C 360      60.310 -10.710 -38.573  1.00 60.52           C
ANISOU 2679  C   LEU C 360     8809   6706   7480    894     29   -747       C
ATOM   2680  O   LEU C 360      61.185 -11.244 -39.254  1.00 61.13           O
ANISOU 2680  O   LEU C 360     8888   6756   7584    932     69   -751       O
ATOM   2681  CB  LEU C 360      61.418  -9.067 -37.027  1.00 61.54           C
ANISOU 2681  CB  LEU C 360     8851   6922   7609    883    -10   -668       C
ATOM   2682  CG  LEU C 360      60.744  -7.710 -37.245  1.00 61.23           C
ANISOU 2682  CG  LEU C 360     8815   6929   7519    848    -30   -691       C
ATOM   2683  CD1 LEU C 360      61.516  -6.626 -36.512  1.00 62.07           C
ANISOU 2683  CD1 LEU C 360     8870   7088   7625    842    -45   -653       C
ATOM   2684  CD2 LEU C 360      60.643  -7.368 -38.720  1.00 60.51           C
ANISOU 2684  CD2 LEU C 360     8755   6836   7400    859      0   -738       C
ATOM   2685  N   ASP C 361      59.100 -10.421 -39.042  1.00 57.60           N
ANISOU 2685  N   ASP C 361     8476   6342   7067    861     14   -790       N
ATOM   2686  CA  ASP C 361      58.737 -10.646 -40.437  1.00 56.90           C
ANISOU 2686  CA  ASP C 361     8430   6234   6954    866     43   -847       C
ATOM   2687  C   ASP C 361      59.257  -9.504 -41.303  1.00 56.33           C
ANISOU 2687  C   ASP C 361     8347   6204   6849    876     59   -858       C
ATOM   2688  O   ASP C 361      58.815  -8.365 -41.156  1.00 55.79           O
ANISOU 2688  O   ASP C 361     8269   6182   6746    849     34   -855       O
ATOM   2689  CB  ASP C 361      57.218 -10.765 -40.579  1.00 56.57           C
ANISOU 2689  CB  ASP C 361     8428   6188   6877    825     18   -885       C
ATOM   2690  CG  ASP C 361      56.774 -10.889 -42.024  1.00 56.54           C
ANISOU 2690  CG  ASP C 361     8467   6177   6840    825     43   -945       C
ATOM   2691  OD1 ASP C 361      57.485 -11.544 -42.815  1.00 56.92           O
ANISOU 2691  OD1 ASP C 361     8527   6193   6906    857     85   -964       O
ATOM   2692  OD2 ASP C 361      55.714 -10.328 -42.370  1.00 56.21           O
ANISOU 2692  OD2 ASP C 361     8444   6160   6751    792     22   -973       O
ATOM   2693  N   PRO C 362      60.199  -9.810 -42.210  1.00 47.03           N
ANISOU 2693  N   PRO C 362     7173   5010   5687    914    103   -869       N
ATOM   2694  CA  PRO C 362      60.864  -8.826 -43.073  1.00 46.42           C
ANISOU 2694  CA  PRO C 362     7083   4969   5585    929    125   -876       C
ATOM   2695  C   PRO C 362      59.894  -7.906 -43.812  1.00 45.83           C
ANISOU 2695  C   PRO C 362     7032   4930   5450    899    112   -911       C
ATOM   2696  O   PRO C 362      60.205  -6.734 -44.016  1.00 45.63           O
ANISOU 2696  O   PRO C 362     6985   4949   5403    897    111   -899       O
ATOM   2697  CB  PRO C 362      61.621  -9.702 -44.074  1.00 46.25           C
ANISOU 2697  CB  PRO C 362     7080   4908   5585    969    177   -900       C
ATOM   2698  CG  PRO C 362      61.901 -10.953 -43.324  1.00 47.01           C
ANISOU 2698  CG  PRO C 362     7172   4953   5737    985    183   -878       C
ATOM   2699  CD  PRO C 362      60.697 -11.176 -42.454  1.00 47.20           C
ANISOU 2699  CD  PRO C 362     7209   4972   5753    945    139   -877       C
ATOM   2700  N   GLU C 363      58.735  -8.430 -44.200  1.00 49.27           N
ANISOU 2700  N   GLU C 363     7510   5349   5861    875    103   -951       N
ATOM   2701  CA  GLU C 363      57.745  -7.635 -44.920  1.00 48.54           C
ANISOU 2701  CA  GLU C 363     7439   5292   5711    846     89   -983       C
ATOM   2702  C   GLU C 363      57.149  -6.521 -44.060  1.00 48.24           C
ANISOU 2702  C   GLU C 363     7377   5297   5656    813     47   -955       C
ATOM   2703  O   GLU C 363      56.626  -5.538 -44.583  1.00 47.81           O
ANISOU 2703  O   GLU C 363     7325   5280   5560    796     39   -966       O
ATOM   2704  CB  GLU C 363      56.637  -8.529 -45.484  1.00 48.30           C
ANISOU 2704  CB  GLU C 363     7458   5235   5661    826     87  -1032       C
ATOM   2705  CG  GLU C 363      57.079  -9.395 -46.654  0.00 48.47           C
ANISOU 2705  CG  GLU C 363     7509   5225   5683    852    134  -1074       C
ATOM   2706  CD  GLU C 363      55.938 -10.192 -47.256  0.00 48.12           C
ANISOU 2706  CD  GLU C 363     7512   5158   5612    826    131  -1128       C
ATOM   2707  OE1 GLU C 363      55.231 -10.889 -46.498  0.00 48.07           O
ANISOU 2707  OE1 GLU C 363     7516   5122   5626    805    108  -1127       O
ATOM   2708  OE2 GLU C 363      55.745 -10.118 -48.488  0.00 47.93           O
ANISOU 2708  OE2 GLU C 363     7514   5149   5547    825    152  -1170       O
ATOM   2709  N   LYS C 364      57.231  -6.676 -42.742  1.00 52.63           N
ANISOU 2709  N   LYS C 364     7909   5846   6245    805     21   -919       N
ATOM   2710  CA  LYS C 364      56.728  -5.657 -41.825  1.00 52.57           C
ANISOU 2710  CA  LYS C 364     7876   5875   6224    773    -16   -893       C
ATOM   2711  C   LYS C 364      57.679  -4.468 -41.715  1.00 53.06           C
ANISOU 2711  C   LYS C 364     7896   5976   6287    785     -8   -863       C
ATOM   2712  O   LYS C 364      57.313  -3.419 -41.185  1.00 52.61           O
ANISOU 2712  O   LYS C 364     7820   5955   6216    759    -32   -849       O
ATOM   2713  CB  LYS C 364      56.463  -6.248 -40.438  1.00 53.09           C
ANISOU 2713  CB  LYS C 364     7930   5924   6320    757    -46   -865       C
ATOM   2714  CG  LYS C 364      55.178  -7.054 -40.335  1.00 53.23           C
ANISOU 2714  CG  LYS C 364     7984   5914   6327    731    -65   -891       C
ATOM   2715  CD  LYS C 364      54.890  -7.431 -38.890  1.00 54.08           C
ANISOU 2715  CD  LYS C 364     8076   6013   6460    712    -97   -858       C
ATOM   2716  CE  LYS C 364      53.503  -8.028 -38.731  1.00 54.08           C
ANISOU 2716  CE  LYS C 364     8110   5993   6447    680   -120   -882       C
ATOM   2717  NZ  LYS C 364      53.170  -8.262 -37.298  1.00 54.69           N
ANISOU 2717  NZ  LYS C 364     8168   6067   6544    659   -152   -847       N
ATOM   2718  N   LEU C 365      58.899  -4.636 -42.219  1.00 42.44           N
ANISOU 2718  N   LEU C 365     6538   4624   4963    823     27   -856       N
ATOM   2719  CA  LEU C 365      59.887  -3.562 -42.203  1.00 42.32           C
ANISOU 2719  CA  LEU C 365     6483   4644   4953    836     38   -829       C
ATOM   2720  C   LEU C 365      59.506  -2.432 -43.154  1.00 41.76           C
ANISOU 2720  C   LEU C 365     6420   4608   4839    826     46   -849       C
ATOM   2721  O   LEU C 365      60.007  -1.315 -43.032  1.00 41.79           O
ANISOU 2721  O   LEU C 365     6391   4645   4842    825     49   -828       O
ATOM   2722  CB  LEU C 365      61.279  -4.096 -42.549  1.00 42.68           C
ANISOU 2722  CB  LEU C 365     6513   4671   5033    880     75   -816       C
ATOM   2723  CG  LEU C 365      61.966  -4.951 -41.484  1.00 43.42           C
ANISOU 2723  CG  LEU C 365     6581   4740   5176    895     69   -780       C
ATOM   2724  CD1 LEU C 365      63.221  -5.594 -42.048  1.00 44.17           C
ANISOU 2724  CD1 LEU C 365     6667   4810   5304    942    112   -773       C
ATOM   2725  CD2 LEU C 365      62.298  -4.113 -40.258  1.00 43.51           C
ANISOU 2725  CD2 LEU C 365     6545   4788   5197    876     40   -738       C
ATOM   2726  N   ASN C 366      58.608  -2.722 -44.091  1.00 44.29           N
ANISOU 2726  N   ASN C 366     6781   4921   5125    818     51   -888       N
ATOM   2727  CA  ASN C 366      58.128  -1.716 -45.036  1.00 43.47           C
ANISOU 2727  CA  ASN C 366     6687   4853   4979    809     57   -904       C
ATOM   2728  C   ASN C 366      57.282  -0.630 -44.374  1.00 43.01           C
ANISOU 2728  C   ASN C 366     6613   4825   4903    772     24   -890       C
ATOM   2729  O   ASN C 366      56.805   0.289 -45.038  1.00 42.96           O
ANISOU 2729  O   ASN C 366     6610   4849   4864    762     27   -897       O
ATOM   2730  CB  ASN C 366      57.336  -2.372 -46.168  1.00 43.17           C
ANISOU 2730  CB  ASN C 366     6696   4803   4905    807     68   -949       C
ATOM   2731  CG  ASN C 366      58.199  -3.249 -47.051  1.00 44.40           C
ANISOU 2731  CG  ASN C 366     6867   4931   5070    844    109   -969       C
ATOM   2732  OD1 ASN C 366      58.935  -2.755 -47.904  1.00 45.24           O
ANISOU 2732  OD1 ASN C 366     6966   5056   5166    867    140   -970       O
ATOM   2733  ND2 ASN C 366      58.109  -4.559 -46.854  1.00 44.74           N
ANISOU 2733  ND2 ASN C 366     6934   4931   5137    849    111   -986       N
ATOM   2734  N   VAL C 367      57.099  -0.744 -43.063  1.00 43.20           N
ANISOU 2734  N   VAL C 367     6620   4844   4951    752     -5   -868       N
ATOM   2735  CA  VAL C 367      56.327   0.228 -42.303  1.00 43.13           C
ANISOU 2735  CA  VAL C 367     6596   4861   4931    716    -35   -855       C
ATOM   2736  C   VAL C 367      57.105   1.537 -42.141  1.00 43.59           C
ANISOU 2736  C   VAL C 367     6613   4953   4998    719    -24   -830       C
ATOM   2737  O   VAL C 367      56.520   2.589 -41.877  1.00 43.72           O
ANISOU 2737  O   VAL C 367     6618   4994   5001    693    -36   -824       O
ATOM   2738  CB  VAL C 367      55.936  -0.336 -40.918  1.00 43.50           C
ANISOU 2738  CB  VAL C 367     6636   4893   5000    693    -68   -840       C
ATOM   2739  CG1 VAL C 367      57.126  -0.315 -39.969  1.00 43.97           C
ANISOU 2739  CG1 VAL C 367     6654   4954   5096    706    -67   -805       C
ATOM   2740  CG2 VAL C 367      54.773   0.441 -40.333  1.00 43.44           C
ANISOU 2740  CG2 VAL C 367     6626   4906   4972    653    -98   -840       C
ATOM   2741  N   PHE C 368      58.422   1.471 -42.319  1.00 38.07           N
ANISOU 2741  N   PHE C 368     5892   4251   4322    750      3   -815       N
ATOM   2742  CA  PHE C 368      59.281   2.638 -42.136  1.00 38.56           C
ANISOU 2742  CA  PHE C 368     5913   4342   4396    753     15   -791       C
ATOM   2743  C   PHE C 368      59.409   3.480 -43.403  1.00 39.28           C
ANISOU 2743  C   PHE C 368     6008   4453   4464    768     45   -800       C
ATOM   2744  O   PHE C 368      60.170   4.447 -43.435  1.00 40.03           O
ANISOU 2744  O   PHE C 368     6070   4570   4570    773     62   -781       O
ATOM   2745  CB  PHE C 368      60.675   2.218 -41.662  1.00 39.08           C
ANISOU 2745  CB  PHE C 368     5947   4400   4501    779     28   -766       C
ATOM   2746  CG  PHE C 368      60.690   1.573 -40.307  1.00 39.25           C
ANISOU 2746  CG  PHE C 368     5955   4412   4548    765     -2   -747       C
ATOM   2747  CD1 PHE C 368      60.863   0.205 -40.179  1.00 40.34           C
ANISOU 2747  CD1 PHE C 368     6109   4514   4704    784     -2   -747       C
ATOM   2748  CD2 PHE C 368      60.537   2.334 -39.161  1.00 40.19           C
ANISOU 2748  CD2 PHE C 368     6044   4556   4672    733    -28   -728       C
ATOM   2749  CE1 PHE C 368      60.882  -0.391 -38.934  1.00 41.14           C
ANISOU 2749  CE1 PHE C 368     6195   4608   4828    773    -29   -725       C
ATOM   2750  CE2 PHE C 368      60.554   1.743 -37.911  1.00 40.96           C
ANISOU 2750  CE2 PHE C 368     6127   4648   4788    719    -55   -708       C
ATOM   2751  CZ  PHE C 368      60.726   0.379 -37.798  1.00 41.49           C
ANISOU 2751  CZ  PHE C 368     6209   4682   4873    740    -56   -704       C
ATOM   2752  N   ARG C 369      58.668   3.114 -44.444  1.00 38.77           N
ANISOU 2752  N   ARG C 369     5982   4383   4366    772     52   -828       N
ATOM   2753  CA  ARG C 369      58.737   3.835 -45.712  1.00 38.10           C
ANISOU 2753  CA  ARG C 369     5903   4320   4253    786     81   -835       C
ATOM   2754  C   ARG C 369      58.105   5.222 -45.628  1.00 37.85           C
ANISOU 2754  C   ARG C 369     5855   4320   4208    760     72   -823       C
ATOM   2755  O   ARG C 369      58.365   6.081 -46.471  1.00 37.38           O
ANISOU 2755  O   ARG C 369     5786   4282   4134    772     98   -817       O
ATOM   2756  CB  ARG C 369      58.096   3.020 -46.838  1.00 37.49           C
ANISOU 2756  CB  ARG C 369     5870   4232   4140    794     89   -870       C
ATOM   2757  CG  ARG C 369      58.904   1.801 -47.255  1.00 37.77           C
ANISOU 2757  CG  ARG C 369     5922   4238   4190    827    112   -885       C
ATOM   2758  CD  ARG C 369      58.287   1.111 -48.461  1.00 37.73           C
ANISOU 2758  CD  ARG C 369     5962   4228   4147    832    125   -924       C
ATOM   2759  NE  ARG C 369      59.082  -0.032 -48.905  1.00 38.26           N
ANISOU 2759  NE  ARG C 369     6044   4263   4229    863    153   -942       N
ATOM   2760  CZ  ARG C 369      60.058   0.040 -49.805  1.00 38.15           C
ANISOU 2760  CZ  ARG C 369     6026   4254   4215    896    193   -944       C
ATOM   2761  NH1 ARG C 369      60.366   1.204 -50.362  1.00 37.93           N
ANISOU 2761  NH1 ARG C 369     5979   4264   4170    902    209   -928       N
ATOM   2762  NH2 ARG C 369      60.727  -1.052 -50.148  1.00 38.20           N
ANISOU 2762  NH2 ARG C 369     6048   4228   4240    923    220   -962       N
ATOM   2763  N   THR C 370      57.281   5.439 -44.608  1.00 47.27           N
ANISOU 2763  N   THR C 370     7043   5513   5405    726     40   -818       N
ATOM   2764  CA  THR C 370      56.624   6.728 -44.420  1.00 47.19           C
ANISOU 2764  CA  THR C 370     7017   5528   5387    701     33   -806       C
ATOM   2765  C   THR C 370      57.451   7.666 -43.542  1.00 47.49           C
ANISOU 2765  C   THR C 370     7009   5576   5458    693     38   -781       C
ATOM   2766  O   THR C 370      57.180   8.865 -43.478  1.00 47.50           O
ANISOU 2766  O   THR C 370     6991   5597   5460    677     44   -770       O
ATOM   2767  CB  THR C 370      55.222   6.566 -43.803  1.00 46.75           C
ANISOU 2767  CB  THR C 370     6979   5468   5317    665     -3   -816       C
ATOM   2768  OG1 THR C 370      55.323   5.866 -42.557  1.00 47.04           O
ANISOU 2768  OG1 THR C 370     7010   5486   5379    652    -28   -813       O
ATOM   2769  CG2 THR C 370      54.311   5.789 -44.742  1.00 46.50           C
ANISOU 2769  CG2 THR C 370     6990   5431   5249    668     -8   -843       C
ATOM   2770  N   VAL C 371      58.460   7.116 -42.873  1.00 35.85           N
ANISOU 2770  N   VAL C 371     5517   4091   4013    704     38   -771       N
ATOM   2771  CA  VAL C 371      59.294   7.892 -41.959  1.00 36.47           C
ANISOU 2771  CA  VAL C 371     5551   4183   4123    694     40   -749       C
ATOM   2772  C   VAL C 371      60.195   8.877 -42.699  1.00 36.27           C
ANISOU 2772  C   VAL C 371     5500   4174   4105    713     76   -736       C
ATOM   2773  O   VAL C 371      61.017   8.479 -43.524  1.00 36.87           O
ANISOU 2773  O   VAL C 371     5580   4247   4183    748    102   -736       O
ATOM   2774  CB  VAL C 371      60.169   6.976 -41.081  1.00 37.23           C
ANISOU 2774  CB  VAL C 371     5631   4266   4247    703     28   -737       C
ATOM   2775  CG1 VAL C 371      61.031   7.806 -40.141  1.00 37.14           C
ANISOU 2775  CG1 VAL C 371     5572   4276   4265    688     29   -715       C
ATOM   2776  CG2 VAL C 371      59.301   6.004 -40.297  1.00 37.23           C
ANISOU 2776  CG2 VAL C 371     5654   4249   4243    684     -7   -746       C
ATOM   2777  N   ARG C 372      60.042  10.163 -42.393  1.00 33.42           N
ANISOU 2777  N   ARG C 372     5114   3832   3752    690     81   -726       N
ATOM   2778  CA  ARG C 372      60.844  11.200 -43.035  1.00 34.03           C
ANISOU 2778  CA  ARG C 372     5165   3925   3840    705    117   -713       C
ATOM   2779  C   ARG C 372      61.955  11.724 -42.130  1.00 34.81           C
ANISOU 2779  C   ARG C 372     5218   4033   3976    696    122   -696       C
ATOM   2780  O   ARG C 372      62.983  12.195 -42.614  1.00 35.33           O
ANISOU 2780  O   ARG C 372     5260   4107   4057    716    152   -684       O
ATOM   2781  CB  ARG C 372      59.964  12.364 -43.498  1.00 33.50           C
ANISOU 2781  CB  ARG C 372     5100   3870   3759    689    127   -711       C
ATOM   2782  CG  ARG C 372      58.839  11.969 -44.439  1.00 33.38           C
ANISOU 2782  CG  ARG C 372     5126   3853   3704    695    122   -725       C
ATOM   2783  CD  ARG C 372      58.269  13.188 -45.147  1.00 33.31           C
ANISOU 2783  CD  ARG C 372     5111   3860   3684    690    142   -714       C
ATOM   2784  NE  ARG C 372      56.818  13.118 -45.283  0.00 32.87           N
ANISOU 2784  NE  ARG C 372     5082   3806   3600    672    121   -723       N
ATOM   2785  CZ  ARG C 372      55.964  13.656 -44.420  0.00 32.63           C
ANISOU 2785  CZ  ARG C 372     5045   3776   3579    638    102   -722       C
ATOM   2786  NH1 ARG C 372      56.416  14.307 -43.356  0.00 32.83           N
ANISOU 2786  NH1 ARG C 372     5037   3798   3638    617    102   -714       N
ATOM   2787  NH2 ARG C 372      54.658  13.546 -44.619  0.00 32.25           N
ANISOU 2787  NH2 ARG C 372     5020   3729   3504    624     83   -729       N
ATOM   2788  N   GLU C 373      61.748  11.647 -40.819  1.00 36.07           N
ANISOU 2788  N   GLU C 373     5363   4193   4147    664     92   -695       N
ATOM   2789  CA  GLU C 373      62.724  12.177 -39.873  1.00 36.44           C
ANISOU 2789  CA  GLU C 373     5364   4255   4225    649     93   -681       C
ATOM   2790  C   GLU C 373      62.911  11.292 -38.643  1.00 36.93           C
ANISOU 2790  C   GLU C 373     5417   4316   4296    635     59   -677       C
ATOM   2791  O   GLU C 373      61.946  10.796 -38.064  1.00 36.37           O
ANISOU 2791  O   GLU C 373     5369   4239   4212    615     30   -687       O
ATOM   2792  CB  GLU C 373      62.334  13.595 -39.437  1.00 36.34           C
ANISOU 2792  CB  GLU C 373     5329   4257   4222    613    100   -682       C
ATOM   2793  CG  GLU C 373      63.278  14.210 -38.409  1.00 38.03           C
ANISOU 2793  CG  GLU C 373     5495   4488   4465    590    100   -673       C
ATOM   2794  CD  GLU C 373      62.799  15.554 -37.894  1.00 38.65           C
ANISOU 2794  CD  GLU C 373     5554   4577   4555    550    108   -679       C
ATOM   2795  OE1 GLU C 373      63.000  15.836 -36.693  1.00 39.35           O
ANISOU 2795  OE1 GLU C 373     5616   4680   4657    515     92   -681       O
ATOM   2796  OE2 GLU C 373      62.229  16.332 -38.687  1.00 38.63           O
ANISOU 2796  OE2 GLU C 373     5562   4569   4548    553    131   -681       O
ATOM   2797  N   ILE C 374      64.168  11.096 -38.258  1.00 32.92           N
ANISOU 2797  N   ILE C 374     4876   3819   3813    647     64   -661       N
ATOM   2798  CA  ILE C 374      64.494  10.451 -36.995  1.00 33.39           C
ANISOU 2798  CA  ILE C 374     4916   3886   3884    631     34   -650       C
ATOM   2799  C   ILE C 374      65.215  11.457 -36.112  1.00 33.93           C
ANISOU 2799  C   ILE C 374     4935   3984   3974    601     35   -640       C
ATOM   2800  O   ILE C 374      66.286  11.949 -36.467  1.00 34.38           O
ANISOU 2800  O   ILE C 374     4961   4052   4049    616     60   -629       O
ATOM   2801  CB  ILE C 374      65.404   9.235 -37.193  1.00 33.86           C
ANISOU 2801  CB  ILE C 374     4975   3935   3957    671     36   -635       C
ATOM   2802  CG1 ILE C 374      64.726   8.206 -38.098  1.00 33.37           C
ANISOU 2802  CG1 ILE C 374     4964   3841   3876    699     39   -649       C
ATOM   2803  CG2 ILE C 374      65.760   8.619 -35.850  1.00 34.49           C
ANISOU 2803  CG2 ILE C 374     5029   4025   4049    655      4   -617       C
ATOM   2804  CD1 ILE C 374      65.576   6.989 -38.371  1.00 33.81           C
ANISOU 2804  CD1 ILE C 374     5021   3878   3947    740     47   -637       C
ATOM   2805  N   THR C 375      64.624  11.762 -34.963  1.00 30.84           N
ANISOU 2805  N   THR C 375     4535   3607   3578    558      8   -646       N
ATOM   2806  CA  THR C 375      65.164  12.783 -34.074  1.00 30.86           C
ANISOU 2806  CA  THR C 375     4492   3639   3596    521      8   -644       C
ATOM   2807  C   THR C 375      66.495  12.364 -33.459  1.00 31.19           C
ANISOU 2807  C   THR C 375     4491   3703   3656    528      1   -621       C
ATOM   2808  O   THR C 375      67.429  13.162 -33.370  1.00 31.34           O
ANISOU 2808  O   THR C 375     4470   3743   3695    521     19   -615       O
ATOM   2809  CB  THR C 375      64.168  13.127 -32.956  1.00 30.63           C
ANISOU 2809  CB  THR C 375     4464   3619   3553    471    -19   -658       C
ATOM   2810  OG1 THR C 375      62.960  13.636 -33.535  1.00 30.35           O
ANISOU 2810  OG1 THR C 375     4462   3565   3504    464     -9   -677       O
ATOM   2811  CG2 THR C 375      64.754  14.169 -32.025  1.00 30.70           C
ANISOU 2811  CG2 THR C 375     4426   3660   3577    430    -16   -661       C
ATOM   2812  N   GLY C 376      66.580  11.106 -33.043  1.00 31.31           N
ANISOU 2812  N   GLY C 376     4515   3714   3669    544    -25   -606       N
ATOM   2813  CA  GLY C 376      67.779  10.606 -32.400  1.00 31.65           C
ANISOU 2813  CA  GLY C 376     4516   3779   3729    552    -35   -579       C
ATOM   2814  C   GLY C 376      68.749   9.970 -33.375  1.00 31.94           C
ANISOU 2814  C   GLY C 376     4551   3800   3783    606    -10   -561       C
ATOM   2815  O   GLY C 376      69.179  10.602 -34.341  1.00 31.97           O
ANISOU 2815  O   GLY C 376     4553   3799   3796    625     25   -567       O
ATOM   2816  N   TYR C 377      69.093   8.712 -33.120  1.00 35.44           N
ANISOU 2816  N   TYR C 377     4996   4235   4234    632    -25   -539       N
ATOM   2817  CA  TYR C 377      70.055   8.006 -33.956  1.00 35.45           C
ANISOU 2817  CA  TYR C 377     4994   4219   4255    684      0   -522       C
ATOM   2818  C   TYR C 377      69.425   6.855 -34.734  1.00 34.76           C
ANISOU 2818  C   TYR C 377     4960   4089   4160    719      5   -530       C
ATOM   2819  O   TYR C 377      68.320   6.409 -34.424  1.00 34.33           O
ANISOU 2819  O   TYR C 377     4938   4019   4086    703    -18   -543       O
ATOM   2820  CB  TYR C 377      71.234   7.493 -33.117  1.00 36.54           C
ANISOU 2820  CB  TYR C 377     5083   4384   4418    691    -14   -484       C
ATOM   2821  CG  TYR C 377      70.873   6.466 -32.059  1.00 37.15           C
ANISOU 2821  CG  TYR C 377     5161   4463   4490    682    -52   -466       C
ATOM   2822  CD1 TYR C 377      70.667   5.131 -32.394  1.00 36.73           C
ANISOU 2822  CD1 TYR C 377     5139   4372   4443    719    -52   -456       C
ATOM   2823  CD2 TYR C 377      70.765   6.826 -30.721  1.00 38.10           C
ANISOU 2823  CD2 TYR C 377     5251   4623   4601    635    -86   -457       C
ATOM   2824  CE1 TYR C 377      70.343   4.192 -31.433  1.00 37.41           C
ANISOU 2824  CE1 TYR C 377     5225   4459   4529    712    -85   -435       C
ATOM   2825  CE2 TYR C 377      70.446   5.890 -29.751  1.00 38.57           C
ANISOU 2825  CE2 TYR C 377     5311   4688   4657    627   -120   -436       C
ATOM   2826  CZ  TYR C 377      70.234   4.576 -30.114  1.00 38.36           C
ANISOU 2826  CZ  TYR C 377     5315   4622   4638    666   -119   -424       C
ATOM   2827  OH  TYR C 377      69.915   3.641 -29.156  1.00 39.23           O
ANISOU 2827  OH  TYR C 377     5425   4735   4747    660   -151   -400       O
ATOM   2828  N   LEU C 378      70.145   6.381 -35.745  1.00 35.91           N
ANISOU 2828  N   LEU C 378     5110   4214   4320    766     37   -524       N
ATOM   2829  CA  LEU C 378      69.758   5.183 -36.476  1.00 35.14           C
ANISOU 2829  CA  LEU C 378     5057   4075   4219    802     45   -532       C
ATOM   2830  C   LEU C 378      70.822   4.112 -36.271  1.00 35.92           C
ANISOU 2830  C   LEU C 378     5132   4165   4350    839     51   -500       C
ATOM   2831  O   LEU C 378      71.985   4.307 -36.623  1.00 36.37           O
ANISOU 2831  O   LEU C 378     5156   4232   4429    864     76   -483       O
ATOM   2832  CB  LEU C 378      69.592   5.486 -37.965  1.00 34.83           C
ANISOU 2832  CB  LEU C 378     5051   4016   4168    828     83   -558       C
ATOM   2833  CG  LEU C 378      69.183   4.305 -38.847  1.00 34.59           C
ANISOU 2833  CG  LEU C 378     5069   3944   4131    862     97   -573       C
ATOM   2834  CD1 LEU C 378      67.854   3.726 -38.386  1.00 33.98           C
ANISOU 2834  CD1 LEU C 378     5030   3850   4033    838     65   -590       C
ATOM   2835  CD2 LEU C 378      69.114   4.722 -40.309  1.00 34.41           C
ANISOU 2835  CD2 LEU C 378     5073   3912   4091    884    135   -597       C
ATOM   2836  N   ASN C 379      70.419   2.985 -35.695  1.00 41.54           N
ANISOU 2836  N   ASN C 379     5859   4858   5066    843     28   -490       N
ATOM   2837  CA  ASN C 379      71.352   1.911 -35.376  1.00 42.42           C
ANISOU 2837  CA  ASN C 379     5947   4959   5211    877     31   -454       C
ATOM   2838  C   ASN C 379      70.944   0.585 -36.008  1.00 41.96           C
ANISOU 2838  C   ASN C 379     5935   4848   5160    912     45   -464       C
ATOM   2839  O   ASN C 379      69.986  -0.051 -35.569  1.00 42.17           O
ANISOU 2839  O   ASN C 379     5990   4856   5176    897     21   -471       O
ATOM   2840  CB  ASN C 379      71.475   1.754 -33.858  1.00 44.24           C
ANISOU 2840  CB  ASN C 379     6139   5221   5448    848    -10   -420       C
ATOM   2841  CG  ASN C 379      72.363   0.591 -33.458  1.00 45.41           C
ANISOU 2841  CG  ASN C 379     6261   5360   5634    884     -9   -376       C
ATOM   2842  OD1 ASN C 379      73.306   0.239 -34.167  1.00 45.60           O
ANISOU 2842  OD1 ASN C 379     6273   5369   5684    927     24   -364       O
ATOM   2843  ND2 ASN C 379      72.063  -0.013 -32.313  1.00 45.55           N
ANISOU 2843  ND2 ASN C 379     6267   5387   5652    867    -45   -351       N
ATOM   2844  N   ILE C 380      71.678   0.174 -37.036  1.00 34.36           N
ANISOU 2844  N   ILE C 380     4977   3861   4216    957     85   -466       N
ATOM   2845  CA  ILE C 380      71.390  -1.074 -37.735  1.00 34.60           C
ANISOU 2845  CA  ILE C 380     5051   3839   4256    991    106   -480       C
ATOM   2846  C   ILE C 380      72.528  -2.076 -37.565  1.00 35.14           C
ANISOU 2846  C   ILE C 380     5090   3890   4371   1034    123   -441       C
ATOM   2847  O   ILE C 380      73.614  -1.894 -38.116  1.00 35.41           O
ANISOU 2847  O   ILE C 380     5099   3930   4427   1065    156   -429       O
ATOM   2848  CB  ILE C 380      71.151  -0.835 -39.239  1.00 34.56           C
ANISOU 2848  CB  ILE C 380     5087   3815   4231   1010    144   -522       C
ATOM   2849  CG1 ILE C 380      70.077   0.235 -39.447  1.00 34.06           C
ANISOU 2849  CG1 ILE C 380     5048   3772   4123    969    128   -554       C
ATOM   2850  CG2 ILE C 380      70.762  -2.133 -39.930  1.00 34.83           C
ANISOU 2850  CG2 ILE C 380     5169   3795   4271   1039    164   -544       C
ATOM   2851  CD1 ILE C 380      69.800   0.550 -40.902  1.00 34.04           C
ANISOU 2851  CD1 ILE C 380     5081   3757   4095    985    163   -591       C
ATOM   2852  N   GLN C 381      72.274  -3.133 -36.800  1.00 45.11           N
ANISOU 2852  N   GLN C 381     6355   5131   5652   1037    104   -420       N
ATOM   2853  CA  GLN C 381      73.279  -4.162 -36.555  1.00 45.78           C
ANISOU 2853  CA  GLN C 381     6411   5196   5785   1079    120   -378       C
ATOM   2854  C   GLN C 381      72.803  -5.532 -37.028  1.00 45.49           C
ANISOU 2854  C   GLN C 381     6421   5097   5767   1107    140   -393       C
ATOM   2855  O   GLN C 381      73.509  -6.529 -36.883  1.00 46.51           O
ANISOU 2855  O   GLN C 381     6533   5199   5940   1144    158   -361       O
ATOM   2856  CB  GLN C 381      73.643  -4.220 -35.070  1.00 46.78           C
ANISOU 2856  CB  GLN C 381     6486   5360   5927   1061     80   -325       C
ATOM   2857  CG  GLN C 381      74.221  -2.928 -34.520  1.00 47.71           C
ANISOU 2857  CG  GLN C 381     6553   5542   6032   1031     62   -309       C
ATOM   2858  CD  GLN C 381      74.614  -3.043 -33.060  1.00 49.27           C
ANISOU 2858  CD  GLN C 381     6698   5780   6241   1012     23   -257       C
ATOM   2859  OE1 GLN C 381      74.360  -2.140 -32.263  1.00 49.70           O
ANISOU 2859  OE1 GLN C 381     6730   5883   6269    966    -11   -257       O
ATOM   2860  NE2 GLN C 381      75.242  -4.157 -32.702  1.00 49.83           N
ANISOU 2860  NE2 GLN C 381     6747   5834   6353   1047     28   -212       N
ATOM   2861  N   SER C 382      71.600  -5.573 -37.591  1.00 40.54           N
ANISOU 2861  N   SER C 382     5851   4446   5106   1088    138   -443       N
ATOM   2862  CA  SER C 382      71.034  -6.816 -38.097  1.00 40.33           C
ANISOU 2862  CA  SER C 382     5872   4359   5092   1108    157   -467       C
ATOM   2863  C   SER C 382      69.981  -6.529 -39.160  1.00 39.51           C
ANISOU 2863  C   SER C 382     5827   4242   4944   1092    167   -529       C
ATOM   2864  O   SER C 382      69.114  -5.676 -38.973  1.00 39.07           O
ANISOU 2864  O   SER C 382     5782   4214   4847   1051    137   -548       O
ATOM   2865  CB  SER C 382      70.425  -7.634 -36.957  1.00 40.61           C
ANISOU 2865  CB  SER C 382     5908   4380   5140   1092    122   -441       C
ATOM   2866  OG  SER C 382      69.975  -8.895 -37.419  1.00 41.06           O
ANISOU 2866  OG  SER C 382     6009   4375   5218   1113    145   -462       O
ATOM   2867  N   TRP C 383      70.062  -7.247 -40.275  1.00 41.14           N
ANISOU 2867  N   TRP C 383     6070   4404   5159   1123    209   -561       N
ATOM   2868  CA  TRP C 383      69.169  -7.014 -41.402  1.00 40.16           C
ANISOU 2868  CA  TRP C 383     5998   4270   4991   1111    223   -620       C
ATOM   2869  C   TRP C 383      68.932  -8.323 -42.148  1.00 40.02           C
ANISOU 2869  C   TRP C 383     6024   4190   4989   1136    257   -652       C
ATOM   2870  O   TRP C 383      69.853  -9.129 -42.290  1.00 40.50           O
ANISOU 2870  O   TRP C 383     6073   4220   5096   1177    291   -634       O
ATOM   2871  CB  TRP C 383      69.780  -5.964 -42.336  1.00 39.86           C
ANISOU 2871  CB  TRP C 383     5949   4264   4932   1121    249   -632       C
ATOM   2872  CG  TRP C 383      68.777  -5.190 -43.138  1.00 39.16           C
ANISOU 2872  CG  TRP C 383     5899   4193   4787   1093    244   -678       C
ATOM   2873  CD1 TRP C 383      68.609  -5.221 -44.492  1.00 38.84           C
ANISOU 2873  CD1 TRP C 383     5896   4142   4721   1107    279   -721       C
ATOM   2874  CD2 TRP C 383      67.801  -4.268 -42.635  1.00 38.72           C
ANISOU 2874  CD2 TRP C 383     5846   4172   4695   1047    203   -684       C
ATOM   2875  NE1 TRP C 383      67.591  -4.376 -44.863  1.00 38.25           N
ANISOU 2875  NE1 TRP C 383     5845   4094   4595   1073    260   -750       N
ATOM   2876  CE2 TRP C 383      67.078  -3.780 -43.741  1.00 38.15           C
ANISOU 2876  CE2 TRP C 383     5811   4107   4576   1037    215   -727       C
ATOM   2877  CE3 TRP C 383      67.468  -3.810 -41.356  1.00 38.81           C
ANISOU 2877  CE3 TRP C 383     5830   4210   4707   1013    158   -656       C
ATOM   2878  CZ2 TRP C 383      66.044  -2.856 -43.608  1.00 37.61           C
ANISOU 2878  CZ2 TRP C 383     5754   4070   4468    996    184   -740       C
ATOM   2879  CZ3 TRP C 383      66.441  -2.893 -41.226  1.00 38.26           C
ANISOU 2879  CZ3 TRP C 383     5773   4168   4596    972    130   -673       C
ATOM   2880  CH2 TRP C 383      65.741  -2.426 -42.346  1.00 37.64           C
ANISOU 2880  CH2 TRP C 383     5732   4094   4478    965    143   -714       C
ATOM   2881  N   PRO C 384      67.690  -8.547 -42.613  1.00 40.48           N
ANISOU 2881  N   PRO C 384     6135   4232   5012   1111    248   -700       N
ATOM   2882  CA  PRO C 384      67.323  -9.758 -43.358  1.00 40.42           C
ANISOU 2882  CA  PRO C 384     6175   4168   5016   1127    280   -740       C
ATOM   2883  C   PRO C 384      68.240 -10.009 -44.553  1.00 40.61           C
ANISOU 2883  C   PRO C 384     6205   4173   5051   1169    338   -760       C
ATOM   2884  O   PRO C 384      68.581  -9.067 -45.267  1.00 40.41           O
ANISOU 2884  O   PRO C 384     6174   4184   4997   1172    351   -770       O
ATOM   2885  CB  PRO C 384      65.903  -9.451 -43.837  1.00 39.76           C
ANISOU 2885  CB  PRO C 384     6138   4092   4875   1087    258   -790       C
ATOM   2886  CG  PRO C 384      65.365  -8.521 -42.811  1.00 39.53           C
ANISOU 2886  CG  PRO C 384     6086   4109   4826   1048    206   -763       C
ATOM   2887  CD  PRO C 384      66.529  -7.667 -42.392  1.00 39.90           C
ANISOU 2887  CD  PRO C 384     6077   4195   4890   1063    207   -718       C
ATOM   2888  N   PRO C 385      68.635 -11.275 -44.764  1.00 45.02           N
ANISOU 2888  N   PRO C 385     6777   4675   5655   1202    374   -765       N
ATOM   2889  CA  PRO C 385      69.602 -11.679 -45.794  1.00 44.85           C
ANISOU 2889  CA  PRO C 385     6759   4627   5654   1246    434   -780       C
ATOM   2890  C   PRO C 385      69.176 -11.318 -47.215  1.00 44.27           C
ANISOU 2890  C   PRO C 385     6730   4565   5528   1239    460   -843       C
ATOM   2891  O   PRO C 385      70.014 -10.905 -48.015  1.00 44.57           O
ANISOU 2891  O   PRO C 385     6757   4617   5561   1265    497   -847       O
ATOM   2892  CB  PRO C 385      69.658 -13.203 -45.640  1.00 44.86           C
ANISOU 2892  CB  PRO C 385     6778   4558   5710   1269    461   -783       C
ATOM   2893  CG  PRO C 385      69.220 -13.461 -44.243  1.00 45.58           C
ANISOU 2893  CG  PRO C 385     6848   4648   5823   1249    414   -740       C
ATOM   2894  CD  PRO C 385      68.183 -12.422 -43.958  1.00 45.19           C
ANISOU 2894  CD  PRO C 385     6808   4649   5713   1198    361   -752       C
ATOM   2895  N   HIS C 386      67.894 -11.476 -47.522  1.00 50.04           N
ANISOU 2895  N   HIS C 386     7506   5289   6216   1204    442   -890       N
ATOM   2896  CA  HIS C 386      67.392 -11.209 -48.865  1.00 49.64           C
ANISOU 2896  CA  HIS C 386     7499   5251   6111   1194    464   -950       C
ATOM   2897  C   HIS C 386      67.236  -9.711 -49.125  1.00 49.83           C
ANISOU 2897  C   HIS C 386     7509   5344   6082   1174    441   -944       C
ATOM   2898  O   HIS C 386      67.094  -9.286 -50.271  1.00 50.42           O
ANISOU 2898  O   HIS C 386     7606   5439   6111   1173    462   -981       O
ATOM   2899  CB  HIS C 386      66.055 -11.912 -49.071  1.00 48.85           C
ANISOU 2899  CB  HIS C 386     7451   5125   5986   1161    450  -1000       C
ATOM   2900  CG  HIS C 386      64.987 -11.444 -48.134  1.00 49.63           C
ANISOU 2900  CG  HIS C 386     7547   5248   6062   1117    388   -985       C
ATOM   2901  ND1 HIS C 386      65.026 -11.704 -46.780  1.00 50.10           N
ANISOU 2901  ND1 HIS C 386     7578   5295   6163   1113    357   -937       N
ATOM   2902  CD2 HIS C 386      63.865 -10.725 -48.349  1.00 48.92           C
ANISOU 2902  CD2 HIS C 386     7478   5195   5914   1077    354  -1009       C
ATOM   2903  CE1 HIS C 386      63.966 -11.162 -46.203  1.00 49.49           C
ANISOU 2903  CE1 HIS C 386     7505   5246   6053   1071    307   -935       C
ATOM   2904  NE2 HIS C 386      63.244 -10.567 -47.133  1.00 48.78           N
ANISOU 2904  NE2 HIS C 386     7445   5185   5904   1049    305   -978       N
ATOM   2905  N   MET C 387      67.250  -8.918 -48.057  1.00 47.47           N
ANISOU 2905  N   MET C 387     7170   5077   5788   1157    398   -897       N
ATOM   2906  CA  MET C 387      67.209  -7.463 -48.181  1.00 47.16           C
ANISOU 2906  CA  MET C 387     7111   5099   5710   1139    379   -885       C
ATOM   2907  C   MET C 387      68.621  -6.897 -48.282  1.00 47.57           C
ANISOU 2907  C   MET C 387     7117   5169   5787   1173    407   -849       C
ATOM   2908  O   MET C 387      69.316  -6.753 -47.277  1.00 48.49           O
ANISOU 2908  O   MET C 387     7188   5292   5943   1181    392   -800       O
ATOM   2909  CB  MET C 387      66.472  -6.836 -46.994  1.00 47.05           C
ANISOU 2909  CB  MET C 387     7078   5111   5687   1099    321   -858       C
ATOM   2910  CG  MET C 387      64.958  -6.932 -47.075  1.00 45.92           C
ANISOU 2910  CG  MET C 387     6977   4967   5502   1059    291   -894       C
ATOM   2911  SD  MET C 387      64.150  -6.186 -45.647  1.00 47.99           S
ANISOU 2911  SD  MET C 387     7216   5260   5758   1014    228   -861       S
ATOM   2912  CE  MET C 387      62.480  -5.988 -46.262  1.00 46.26           C
ANISOU 2912  CE  MET C 387     7046   5052   5477    973    205   -911       C
ATOM   2913  N   HIS C 388      69.037  -6.570 -49.502  1.00 43.21           N
ANISOU 2913  N   HIS C 388     6576   4630   5211   1192    447   -874       N
ATOM   2914  CA  HIS C 388      70.414  -6.159 -49.760  1.00 43.99           C
ANISOU 2914  CA  HIS C 388     6636   4742   5337   1229    482   -845       C
ATOM   2915  C   HIS C 388      70.613  -4.649 -49.669  1.00 43.77           C
ANISOU 2915  C   HIS C 388     6574   4771   5285   1213    465   -819       C
ATOM   2916  O   HIS C 388      71.667  -4.131 -50.039  1.00 44.03           O
ANISOU 2916  O   HIS C 388     6577   4822   5331   1239    494   -799       O
ATOM   2917  CB  HIS C 388      70.870  -6.671 -51.127  1.00 44.34           C
ANISOU 2917  CB  HIS C 388     6708   4766   5372   1261    540   -883       C
ATOM   2918  CG  HIS C 388      70.732  -8.151 -51.291  1.00 44.52           C
ANISOU 2918  CG  HIS C 388     6766   4729   5423   1277    565   -913       C
ATOM   2919  ND1 HIS C 388      69.561  -8.747 -51.715  1.00 43.96           N
ANISOU 2919  ND1 HIS C 388     6747   4638   5317   1252    558   -964       N
ATOM   2920  CD2 HIS C 388      71.608  -9.160 -51.078  1.00 45.10           C
ANISOU 2920  CD2 HIS C 388     6826   4756   5556   1314    598   -897       C
ATOM   2921  CE1 HIS C 388      69.728 -10.056 -51.761  1.00 44.12           C
ANISOU 2921  CE1 HIS C 388     6787   4600   5377   1272    586   -982       C
ATOM   2922  NE2 HIS C 388      70.961 -10.333 -51.379  1.00 44.87           N
ANISOU 2922  NE2 HIS C 388     6843   4676   5530   1311    612   -941       N
ATOM   2923  N   ASN C 389      69.599  -3.950 -49.172  1.00 42.80           N
ANISOU 2923  N   ASN C 389     6456   4676   5131   1171    419   -819       N
ATOM   2924  CA  ASN C 389      69.674  -2.504 -49.013  1.00 42.92           C
ANISOU 2924  CA  ASN C 389     6441   4741   5127   1153    402   -797       C
ATOM   2925  C   ASN C 389      68.707  -1.997 -47.950  1.00 43.27           C
ANISOU 2925  C   ASN C 389     6479   4804   5159   1108    348   -785       C
ATOM   2926  O   ASN C 389      67.926  -2.767 -47.391  1.00 43.68           O
ANISOU 2926  O   ASN C 389     6553   4830   5213   1091    322   -795       O
ATOM   2927  CB  ASN C 389      69.405  -1.802 -50.346  1.00 42.78           C
ANISOU 2927  CB  ASN C 389     6447   4750   5059   1153    428   -826       C
ATOM   2928  CG  ASN C 389      68.110  -2.253 -50.991  1.00 43.10           C
ANISOU 2928  CG  ASN C 389     6542   4781   5052   1132    419   -874       C
ATOM   2929  OD1 ASN C 389      67.024  -1.992 -50.476  1.00 43.16           O
ANISOU 2929  OD1 ASN C 389     6562   4799   5038   1096    378   -879       O
ATOM   2930  ND2 ASN C 389      68.218  -2.930 -52.130  1.00 43.10           N
ANISOU 2930  ND2 ASN C 389     6576   4764   5035   1154    458   -911       N
ATOM   2931  N   PHE C 390      68.764  -0.698 -47.674  1.00 37.79           N
ANISOU 2931  N   PHE C 390     5755   4151   4454   1089    333   -764       N
ATOM   2932  CA  PHE C 390      67.840  -0.084 -46.729  1.00 37.48           C
ANISOU 2932  CA  PHE C 390     5709   4131   4400   1045    285   -756       C
ATOM   2933  C   PHE C 390      66.857   0.825 -47.457  1.00 36.96           C
ANISOU 2933  C   PHE C 390     5667   4092   4284   1021    280   -779       C
ATOM   2934  O   PHE C 390      66.619   1.957 -47.035  1.00 36.79           O
ANISOU 2934  O   PHE C 390     5624   4102   4254    996    261   -763       O
ATOM   2935  CB  PHE C 390      68.595   0.707 -45.657  1.00 37.79           C
ANISOU 2935  CB  PHE C 390     5692   4196   4470   1036    268   -712       C
ATOM   2936  CG  PHE C 390      69.700  -0.067 -44.994  1.00 38.40           C
ANISOU 2936  CG  PHE C 390     5737   4256   4597   1062    275   -681       C
ATOM   2937  CD1 PHE C 390      71.026   0.263 -45.220  1.00 38.82           C
ANISOU 2937  CD1 PHE C 390     5752   4321   4677   1091    305   -657       C
ATOM   2938  CD2 PHE C 390      69.413  -1.128 -44.151  1.00 38.58           C
ANISOU 2938  CD2 PHE C 390     5767   4251   4641   1059    252   -674       C
ATOM   2939  CE1 PHE C 390      72.045  -0.447 -44.613  1.00 39.42           C
ANISOU 2939  CE1 PHE C 390     5794   4383   4800   1117    312   -625       C
ATOM   2940  CE2 PHE C 390      70.428  -1.842 -43.543  1.00 40.10           C
ANISOU 2940  CE2 PHE C 390     5927   4428   4880   1085    259   -640       C
ATOM   2941  CZ  PHE C 390      71.745  -1.500 -43.774  1.00 39.62           C
ANISOU 2941  CZ  PHE C 390     5825   4381   4845   1114    288   -615       C
ATOM   2942  N   SER C 391      66.281   0.321 -48.547  1.00 45.77           N
ANISOU 2942  N   SER C 391     6828   5196   5366   1028    298   -817       N
ATOM   2943  CA  SER C 391      65.296   1.075 -49.320  1.00 45.49           C
ANISOU 2943  CA  SER C 391     6818   5188   5279   1007    293   -838       C
ATOM   2944  C   SER C 391      64.017   1.289 -48.520  1.00 45.10           C
ANISOU 2944  C   SER C 391     6778   5144   5214    965    246   -841       C
ATOM   2945  O   SER C 391      63.146   2.063 -48.911  1.00 44.82           O
ANISOU 2945  O   SER C 391     6754   5134   5142    942    235   -850       O
ATOM   2946  CB  SER C 391      64.973   0.360 -50.633  1.00 45.15           C
ANISOU 2946  CB  SER C 391     6820   5133   5201   1023    321   -880       C
ATOM   2947  OG  SER C 391      64.434  -0.927 -50.392  1.00 45.14           O
ANISOU 2947  OG  SER C 391     6852   5094   5207   1018    309   -906       O
ATOM   2948  N   VAL C 392      63.909   0.581 -47.402  1.00 38.64           N
ANISOU 2948  N   VAL C 392     5954   4301   4425    954    219   -831       N
ATOM   2949  CA  VAL C 392      62.816   0.773 -46.462  1.00 38.45           C
ANISOU 2949  CA  VAL C 392     5934   4282   4393    914    174   -829       C
ATOM   2950  C   VAL C 392      62.839   2.201 -45.903  1.00 38.27           C
ANISOU 2950  C   VAL C 392     5874   4296   4370    892    160   -802       C
ATOM   2951  O   VAL C 392      61.792   2.785 -45.617  1.00 37.65           O
ANISOU 2951  O   VAL C 392     5803   4233   4271    859    134   -807       O
ATOM   2952  CB  VAL C 392      62.878  -0.290 -45.337  1.00 38.66           C
ANISOU 2952  CB  VAL C 392     5956   4276   4455    912    152   -818       C
ATOM   2953  CG1 VAL C 392      62.609   0.319 -43.972  1.00 39.30           C
ANISOU 2953  CG1 VAL C 392     6007   4376   4550    879    114   -790       C
ATOM   2954  CG2 VAL C 392      61.917  -1.432 -45.637  1.00 38.18           C
ANISOU 2954  CG2 VAL C 392     5944   4183   4380    905    145   -853       C
ATOM   2955  N   PHE C 393      64.038   2.766 -45.780  1.00 36.93           N
ANISOU 2955  N   PHE C 393     5664   4140   4227    910    180   -776       N
ATOM   2956  CA  PHE C 393      64.199   4.151 -45.344  1.00 37.10           C
ANISOU 2956  CA  PHE C 393     5649   4194   4252    890    174   -753       C
ATOM   2957  C   PHE C 393      64.447   5.088 -46.525  1.00 37.50           C
ANISOU 2957  C   PHE C 393     5698   4268   4283    904    208   -756       C
ATOM   2958  O   PHE C 393      65.352   5.921 -46.483  1.00 38.08           O
ANISOU 2958  O   PHE C 393     5734   4359   4375    912    226   -734       O
ATOM   2959  CB  PHE C 393      65.353   4.273 -44.347  1.00 38.04           C
ANISOU 2959  CB  PHE C 393     5720   4318   4415    895    172   -721       C
ATOM   2960  CG  PHE C 393      65.077   3.638 -43.014  1.00 38.14           C
ANISOU 2960  CG  PHE C 393     5725   4320   4446    875    135   -710       C
ATOM   2961  CD1 PHE C 393      65.616   2.404 -42.693  1.00 37.93           C
ANISOU 2961  CD1 PHE C 393     5700   4266   4446    897    135   -702       C
ATOM   2962  CD2 PHE C 393      64.280   4.279 -42.082  1.00 37.58           C
ANISOU 2962  CD2 PHE C 393     5646   4265   4367    833    101   -706       C
ATOM   2963  CE1 PHE C 393      65.365   1.821 -41.466  1.00 38.11           C
ANISOU 2963  CE1 PHE C 393     5715   4281   4486    879    101   -687       C
ATOM   2964  CE2 PHE C 393      64.025   3.701 -40.855  1.00 37.87           C
ANISOU 2964  CE2 PHE C 393     5675   4294   4418    814     67   -695       C
ATOM   2965  CZ  PHE C 393      64.568   2.470 -40.546  1.00 37.88           C
ANISOU 2965  CZ  PHE C 393     5676   4271   4444    837     66   -684       C
ATOM   2966  N   SER C 394      63.639   4.955 -47.572  1.00 53.73           N
ANISOU 2966  N   SER C 394     7792   6324   6298    906    216   -782       N
ATOM   2967  CA  SER C 394      63.830   5.742 -48.788  1.00 53.37           C
ANISOU 2967  CA  SER C 394     7748   6302   6227    921    249   -783       C
ATOM   2968  C   SER C 394      63.191   7.127 -48.721  1.00 52.74           C
ANISOU 2968  C   SER C 394     7654   6252   6134    894    240   -770       C
ATOM   2969  O   SER C 394      63.451   7.974 -49.573  1.00 52.88           O
ANISOU 2969  O   SER C 394     7662   6292   6139    906    268   -761       O
ATOM   2970  CB  SER C 394      63.307   4.982 -50.007  1.00 53.44           C
ANISOU 2970  CB  SER C 394     7803   6305   6196    936    264   -817       C
ATOM   2971  OG  SER C 394      62.014   4.462 -49.758  1.00 53.75           O
ANISOU 2971  OG  SER C 394     7875   6335   6212    909    231   -839       O
ATOM   2972  N   ASN C 395      62.349   7.353 -47.717  1.00 37.64           N
ANISOU 2972  N   ASN C 395     5737   4338   4225    859    204   -767       N
ATOM   2973  CA  ASN C 395      61.759   8.672 -47.507  1.00 37.28           C
ANISOU 2973  CA  ASN C 395     5674   4316   4174    832    197   -753       C
ATOM   2974  C   ASN C 395      62.421   9.416 -46.351  1.00 37.82           C
ANISOU 2974  C   ASN C 395     5697   4390   4284    816    191   -729       C
ATOM   2975  O   ASN C 395      62.099  10.573 -46.080  1.00 37.93           O
ANISOU 2975  O   ASN C 395     5691   4420   4302    794    191   -717       O
ATOM   2976  CB  ASN C 395      60.246   8.575 -47.287  1.00 36.72           C
ANISOU 2976  CB  ASN C 395     5630   4245   4076    802    164   -768       C
ATOM   2977  CG  ASN C 395      59.466   8.549 -48.589  1.00 36.91           C
ANISOU 2977  CG  ASN C 395     5687   4282   4053    809    175   -784       C
ATOM   2978  OD1 ASN C 395      59.930   9.050 -49.614  1.00 37.20           O
ANISOU 2978  OD1 ASN C 395     5721   4337   4078    831    207   -777       O
ATOM   2979  ND2 ASN C 395      58.269   7.971 -48.554  1.00 36.90           N
ANISOU 2979  ND2 ASN C 395     5718   4275   4026    790    147   -804       N
ATOM   2980  N   LEU C 396      63.347   8.741 -45.677  1.00 37.27           N
ANISOU 2980  N   LEU C 396     5610   4307   4243    827    188   -722       N
ATOM   2981  CA  LEU C 396      64.088   9.337 -44.571  1.00 37.66           C
ANISOU 2981  CA  LEU C 396     5614   4365   4329    811    181   -701       C
ATOM   2982  C   LEU C 396      64.942  10.499 -45.061  1.00 38.45           C
ANISOU 2982  C   LEU C 396     5682   4486   4444    822    216   -683       C
ATOM   2983  O   LEU C 396      65.851  10.313 -45.867  1.00 39.44           O
ANISOU 2983  O   LEU C 396     5802   4610   4574    856    247   -679       O
ATOM   2984  CB  LEU C 396      64.976   8.290 -43.898  1.00 38.07           C
ANISOU 2984  CB  LEU C 396     5653   4403   4409    827    173   -693       C
ATOM   2985  CG  LEU C 396      65.890   8.802 -42.784  1.00 38.68           C
ANISOU 2985  CG  LEU C 396     5680   4495   4522    812    166   -669       C
ATOM   2986  CD1 LEU C 396      65.070   9.314 -41.610  1.00 38.64           C
ANISOU 2986  CD1 LEU C 396     5666   4500   4516    766    131   -669       C
ATOM   2987  CD2 LEU C 396      66.857   7.716 -42.339  1.00 39.26           C
ANISOU 2987  CD2 LEU C 396     5740   4556   4621    836    163   -655       C
ATOM   2988  N   THR C 397      64.648  11.697 -44.566  1.00 40.97           N
ANISOU 2988  N   THR C 397     5976   4819   4771    791    213   -675       N
ATOM   2989  CA  THR C 397      65.339  12.899 -45.016  1.00 41.33           C
ANISOU 2989  CA  THR C 397     5990   4881   4832    797    247   -659       C
ATOM   2990  C   THR C 397      66.344  13.405 -43.985  1.00 41.61           C
ANISOU 2990  C   THR C 397     5976   4925   4907    781    246   -643       C
ATOM   2991  O   THR C 397      67.430  13.867 -44.339  1.00 41.91           O
ANISOU 2991  O   THR C 397     5985   4972   4966    798    276   -629       O
ATOM   2992  CB  THR C 397      64.337  14.027 -45.345  1.00 40.97           C
ANISOU 2992  CB  THR C 397     5950   4845   4772    775    253   -659       C
ATOM   2993  OG1 THR C 397      63.377  13.555 -46.297  1.00 40.41           O
ANISOU 2993  OG1 THR C 397     5923   4771   4661    788    250   -672       O
ATOM   2994  CG2 THR C 397      65.057  15.238 -45.919  1.00 41.61           C
ANISOU 2994  CG2 THR C 397     6000   4939   4871    784    293   -640       C
ATOM   2995  N   THR C 398      65.986  13.305 -42.709  1.00 41.78           N
ANISOU 2995  N   THR C 398     5988   4947   4938    747    212   -646       N
ATOM   2996  CA  THR C 398      66.806  13.882 -41.650  1.00 42.39           C
ANISOU 2996  CA  THR C 398     6018   5041   5048    724    207   -634       C
ATOM   2997  C   THR C 398      67.046  12.928 -40.482  1.00 42.85           C
ANISOU 2997  C   THR C 398     6068   5099   5116    713    172   -632       C
ATOM   2998  O   THR C 398      66.122  12.277 -39.994  1.00 42.20           O
ANISOU 2998  O   THR C 398     6012   5006   5016    699    141   -642       O
ATOM   2999  CB  THR C 398      66.171  15.181 -41.107  1.00 42.78           C
ANISOU 2999  CB  THR C 398     6052   5100   5104    681    206   -639       C
ATOM   3000  OG1 THR C 398      65.872  16.063 -42.196  1.00 43.21           O
ANISOU 3000  OG1 THR C 398     6113   5153   5151    692    240   -636       O
ATOM   3001  CG2 THR C 398      67.111  15.880 -40.132  1.00 42.70           C
ANISOU 3001  CG2 THR C 398     5990   5108   5127    655    208   -630       C
ATOM   3002  N   ILE C 399      68.300  12.850 -40.047  1.00 31.75           N
ANISOU 3002  N   ILE C 399     4621   3704   3736    720    177   -615       N
ATOM   3003  CA  ILE C 399      68.650  12.179 -38.803  1.00 31.81           C
ANISOU 3003  CA  ILE C 399     4609   3722   3756    705    144   -605       C
ATOM   3004  C   ILE C 399      69.226  13.217 -37.845  1.00 31.81           C
ANISOU 3004  C   ILE C 399     4559   3751   3778    668    141   -598       C
ATOM   3005  O   ILE C 399      70.358  13.669 -38.015  1.00 32.04           O
ANISOU 3005  O   ILE C 399     4551   3794   3831    678    164   -585       O
ATOM   3006  CB  ILE C 399      69.672  11.050 -39.023  1.00 32.16           C
ANISOU 3006  CB  ILE C 399     4646   3759   3815    747    150   -588       C
ATOM   3007  CG1 ILE C 399      69.117  10.011 -40.001  1.00 32.21           C
ANISOU 3007  CG1 ILE C 399     4703   3734   3801    782    157   -600       C
ATOM   3008  CG2 ILE C 399      70.035  10.393 -37.699  1.00 32.26           C
ANISOU 3008  CG2 ILE C 399     4633   3784   3841    731    115   -572       C
ATOM   3009  CD1 ILE C 399      70.050   8.845 -40.248  1.00 32.58           C
ANISOU 3009  CD1 ILE C 399     4747   3767   3865    824    166   -585       C
ATOM   3010  N   GLY C 400      68.433  13.595 -36.846  1.00 31.57           N
ANISOU 3010  N   GLY C 400     4527   3730   3740    623    114   -610       N
ATOM   3011  CA  GLY C 400      68.787  14.670 -35.935  1.00 31.76           C
ANISOU 3011  CA  GLY C 400     4508   3780   3780    579    113   -611       C
ATOM   3012  C   GLY C 400      70.063  14.454 -35.145  1.00 32.75           C
ANISOU 3012  C   GLY C 400     4584   3933   3927    575    103   -592       C
ATOM   3013  O   GLY C 400      70.911  15.341 -35.067  1.00 33.25           O
ANISOU 3013  O   GLY C 400     4606   4015   4011    563    123   -588       O
ATOM   3014  N   GLY C 401      70.203  13.274 -34.553  1.00 31.99           N
ANISOU 3014  N   GLY C 401     4489   3839   3825    585     73   -577       N
ATOM   3015  CA  GLY C 401      71.363  12.983 -33.733  1.00 32.30           C
ANISOU 3015  CA  GLY C 401     4481   3910   3883    582     59   -554       C
ATOM   3016  C   GLY C 401      71.275  13.702 -32.403  1.00 32.26           C
ANISOU 3016  C   GLY C 401     4442   3940   3876    523     36   -561       C
ATOM   3017  O   GLY C 401      72.289  13.968 -31.758  1.00 32.53           O
ANISOU 3017  O   GLY C 401     4426   4008   3926    508     31   -547       O
ATOM   3018  N   ARG C 402      70.050  14.022 -31.997  1.00 41.98           N
ANISOU 3018  N   ARG C 402     5700   5164   5087    490     21   -585       N
ATOM   3019  CA  ARG C 402      69.809  14.687 -30.723  1.00 43.38           C
ANISOU 3019  CA  ARG C 402     5852   5373   5258    431     -1   -597       C
ATOM   3020  C   ARG C 402      70.136  13.762 -29.554  1.00 44.95           C
ANISOU 3020  C   ARG C 402     6029   5601   5449    420    -41   -576       C
ATOM   3021  O   ARG C 402      70.433  14.218 -28.449  1.00 45.87           O
ANISOU 3021  O   ARG C 402     6107   5757   5562    375    -59   -578       O
ATOM   3022  CB  ARG C 402      68.361  15.173 -30.635  1.00 42.18           C
ANISOU 3022  CB  ARG C 402     5737   5203   5087    403     -4   -626       C
ATOM   3023  CG  ARG C 402      68.148  16.591 -31.141  1.00 41.93           C
ANISOU 3023  CG  ARG C 402     5701   5163   5068    384     32   -648       C
ATOM   3024  CD  ARG C 402      67.479  16.611 -32.504  1.00 40.61           C
ANISOU 3024  CD  ARG C 402     5577   4957   4897    421     58   -652       C
ATOM   3025  NE  ARG C 402      67.331  17.970 -33.016  1.00 40.47           N
ANISOU 3025  NE  ARG C 402     5552   4931   4893    407     95   -667       N
ATOM   3026  CZ  ARG C 402      66.662  18.282 -34.121  1.00 40.34           C
ANISOU 3026  CZ  ARG C 402     5568   4887   4874    430    120   -671       C
ATOM   3027  NH1 ARG C 402      66.071  17.329 -34.831  1.00 40.87           N
ANISOU 3027  NH1 ARG C 402     5677   4933   4919    465    111   -665       N
ATOM   3028  NH2 ARG C 402      66.581  19.545 -34.516  1.00 39.56           N
ANISOU 3028  NH2 ARG C 402     5457   4782   4793    417    155   -679       N
ATOM   3029  N   SER C 403      70.068  12.460 -29.810  1.00 53.41           N
ANISOU 3029  N   SER C 403     7124   6653   6516    460    -55   -556       N
ATOM   3030  CA  SER C 403      70.519  11.451 -28.859  1.00 54.29           C
ANISOU 3030  CA  SER C 403     7214   6788   6625    461    -89   -526       C
ATOM   3031  C   SER C 403      71.450  10.478 -29.577  1.00 54.47           C
ANISOU 3031  C   SER C 403     7232   6796   6669    519    -77   -495       C
ATOM   3032  O   SER C 403      71.144  10.014 -30.675  1.00 53.46           O
ANISOU 3032  O   SER C 403     7144   6626   6543    560    -56   -500       O
ATOM   3033  CB  SER C 403      69.329  10.714 -28.241  1.00 53.24           C
ANISOU 3033  CB  SER C 403     7116   6644   6467    447   -122   -531       C
ATOM   3034  OG  SER C 403      68.400  10.317 -29.232  1.00 52.08           O
ANISOU 3034  OG  SER C 403     7026   6449   6314    475   -109   -546       O
ATOM   3035  N   LEU C 404      72.588  10.178 -28.960  1.00 37.83           N
ANISOU 3035  N   LEU C 404     5075   4723   4577    522    -88   -463       N
ATOM   3036  CA  LEU C 404      73.629   9.395 -29.622  1.00 38.01           C
ANISOU 3036  CA  LEU C 404     5083   4733   4625    577    -71   -432       C
ATOM   3037  C   LEU C 404      73.753   7.966 -29.093  1.00 38.95           C
ANISOU 3037  C   LEU C 404     5203   4850   4748    602    -97   -396       C
ATOM   3038  O   LEU C 404      73.211   7.628 -28.041  1.00 39.85           O
ANISOU 3038  O   LEU C 404     5315   4982   4845    572   -132   -389       O
ATOM   3039  CB  LEU C 404      74.974  10.120 -29.526  1.00 38.97           C
ANISOU 3039  CB  LEU C 404     5145   4892   4768    571    -56   -417       C
ATOM   3040  CG  LEU C 404      74.995  11.512 -30.164  1.00 38.96           C
ANISOU 3040  CG  LEU C 404     5142   4890   4772    552    -24   -448       C
ATOM   3041  CD1 LEU C 404      76.313  12.219 -29.896  1.00 40.08           C
ANISOU 3041  CD1 LEU C 404     5220   5074   4936    539    -13   -434       C
ATOM   3042  CD2 LEU C 404      74.728  11.421 -31.661  1.00 36.80           C
ANISOU 3042  CD2 LEU C 404     4913   4567   4503    598     15   -461       C
ATOM   3043  N   TYR C 405      74.474   7.135 -29.841  1.00 43.66           N
ANISOU 3043  N   TYR C 405     5799   5421   5369    657    -76   -372       N
ATOM   3044  CA  TYR C 405      74.647   5.726 -29.504  1.00 43.70           C
ANISOU 3044  CA  TYR C 405     5805   5414   5386    689    -92   -335       C
ATOM   3045  C   TYR C 405      76.127   5.389 -29.352  1.00 44.93           C
ANISOU 3045  C   TYR C 405     5903   5594   5573    717    -86   -290       C
ATOM   3046  O   TYR C 405      76.960   5.869 -30.123  1.00 45.18           O
ANISOU 3046  O   TYR C 405     5916   5625   5624    738    -53   -291       O
ATOM   3047  CB  TYR C 405      74.014   4.850 -30.588  1.00 42.43           C
ANISOU 3047  CB  TYR C 405     5704   5189   5228    733    -70   -350       C
ATOM   3048  CG  TYR C 405      74.100   3.360 -30.332  1.00 42.36           C
ANISOU 3048  CG  TYR C 405     5701   5157   5236    768    -81   -316       C
ATOM   3049  CD1 TYR C 405      73.142   2.712 -29.564  1.00 42.31           C
ANISOU 3049  CD1 TYR C 405     5719   5144   5213    749   -113   -314       C
ATOM   3050  CD2 TYR C 405      75.130   2.600 -30.872  1.00 42.18           C
ANISOU 3050  CD2 TYR C 405     5662   5117   5248    820    -56   -286       C
ATOM   3051  CE1 TYR C 405      73.212   1.350 -29.334  1.00 42.43           C
ANISOU 3051  CE1 TYR C 405     5739   5134   5247    781   -120   -281       C
ATOM   3052  CE2 TYR C 405      75.209   1.240 -30.647  1.00 42.25           C
ANISOU 3052  CE2 TYR C 405     5676   5099   5277    853    -61   -254       C
ATOM   3053  CZ  TYR C 405      74.247   0.620 -29.878  1.00 42.35           C
ANISOU 3053  CZ  TYR C 405     5713   5105   5275    833    -94   -252       C
ATOM   3054  OH  TYR C 405      74.323  -0.736 -29.652  1.00 42.59           O
ANISOU 3054  OH  TYR C 405     5747   5106   5329    866    -97   -218       O
ATOM   3055  N   ASN C 406      76.441   4.563 -28.356  1.00 65.59           N
ANISOU 3055  N   ASN C 406     8490   8234   8196    717   -116   -248       N
ATOM   3056  CA  ASN C 406      77.814   4.146 -28.075  1.00 66.81           C
ANISOU 3056  CA  ASN C 406     8586   8418   8382    743   -115   -198       C
ATOM   3057  C   ASN C 406      78.753   5.333 -27.862  1.00 67.82           C
ANISOU 3057  C   ASN C 406     8658   8598   8513    714   -110   -198       C
ATOM   3058  O   ASN C 406      78.539   6.149 -26.966  1.00 68.53           O
ANISOU 3058  O   ASN C 406     8724   8734   8578    658   -137   -211       O
ATOM   3059  CB  ASN C 406      78.345   3.234 -29.185  1.00 66.46           C
ANISOU 3059  CB  ASN C 406     8558   8322   8372    811    -77   -182       C
ATOM   3060  CG  ASN C 406      79.307   2.182 -28.667  1.00 67.25           C
ANISOU 3060  CG  ASN C 406     8613   8434   8505    846    -85   -120       C
ATOM   3061  OD1 ASN C 406      80.470   2.470 -28.387  1.00 68.26           O
ANISOU 3061  OD1 ASN C 406     8681   8604   8651    848    -84    -88       O
ATOM   3062  ND2 ASN C 406      78.824   0.951 -28.542  1.00 66.87           N
ANISOU 3062  ND2 ASN C 406     8593   8349   8465    872    -92   -102       N
ATOM   3063  N   ARG C 407      79.787   5.428 -28.692  1.00 65.60           N
ANISOU 3063  N   ARG C 407     8354   8309   8262    752    -76   -186       N
ATOM   3064  CA  ARG C 407      80.732   6.537 -28.605  1.00 66.03           C
ANISOU 3064  CA  ARG C 407     8355   8409   8323    728    -67   -187       C
ATOM   3065  C   ARG C 407      80.307   7.718 -29.475  1.00 65.11           C
ANISOU 3065  C   ARG C 407     8268   8273   8197    712    -37   -239       C
ATOM   3066  O   ARG C 407      81.050   8.153 -30.355  1.00 64.65           O
ANISOU 3066  O   ARG C 407     8198   8206   8161    736      0   -241       O
ATOM   3067  CB  ARG C 407      82.147   6.083 -28.974  1.00 66.40           C
ANISOU 3067  CB  ARG C 407     8355   8464   8411    775    -45   -142       C
ATOM   3068  CG  ARG C 407      82.819   5.225 -27.913  1.00 67.01           C
ANISOU 3068  CG  ARG C 407     8381   8580   8501    781    -78    -83       C
ATOM   3069  CD  ARG C 407      84.294   5.015 -28.221  0.00 67.36           C
ANISOU 3069  CD  ARG C 407     8367   8640   8585    820    -57    -40       C
ATOM   3070  NE  ARG C 407      84.986   4.327 -27.134  0.00 68.08           N
ANISOU 3070  NE  ARG C 407     8400   8780   8687    821    -90     21       N
ATOM   3071  CZ  ARG C 407      86.290   4.071 -27.121  0.00 68.45           C
ANISOU 3071  CZ  ARG C 407     8387   8854   8769    850    -81     70       C
ATOM   3072  NH1 ARG C 407      87.052   4.446 -28.139  0.00 68.26           N
ANISOU 3072  NH1 ARG C 407     8353   8810   8772    881    -38     63       N
ATOM   3073  NH2 ARG C 407      86.833   3.440 -26.089  0.00 68.93           N
ANISOU 3073  NH2 ARG C 407     8393   8961   8836    849   -115    128       N
ATOM   3074  N   GLY C 408      79.105   8.226 -29.222  1.00 62.19           N
ANISOU 3074  N   GLY C 408     7937   7897   7796    671    -51   -278       N
ATOM   3075  CA  GLY C 408      78.611   9.412 -29.897  1.00 61.24           C
ANISOU 3075  CA  GLY C 408     7841   7761   7665    650    -25   -324       C
ATOM   3076  C   GLY C 408      78.271   9.220 -31.363  1.00 59.56           C
ANISOU 3076  C   GLY C 408     7680   7491   7459    697     15   -342       C
ATOM   3077  O   GLY C 408      78.606  10.061 -32.196  1.00 59.64           O
ANISOU 3077  O   GLY C 408     7688   7494   7479    702     50   -359       O
ATOM   3078  N   PHE C 409      77.598   8.118 -31.681  1.00 46.88           N
ANISOU 3078  N   PHE C 409     6121   5844   5846    728     11   -340       N
ATOM   3079  CA  PHE C 409      77.206   7.839 -33.059  1.00 45.77           C
ANISOU 3079  CA  PHE C 409     6033   5651   5707    771     47   -361       C
ATOM   3080  C   PHE C 409      75.739   8.178 -33.309  1.00 44.31           C
ANISOU 3080  C   PHE C 409     5905   5442   5490    747     42   -402       C
ATOM   3081  O   PHE C 409      74.881   7.931 -32.461  1.00 44.60           O
ANISOU 3081  O   PHE C 409     5955   5483   5506    717      7   -407       O
ATOM   3082  CB  PHE C 409      77.470   6.373 -33.411  1.00 45.70           C
ANISOU 3082  CB  PHE C 409     6040   5609   5716    825     53   -335       C
ATOM   3083  CG  PHE C 409      78.912   5.969 -33.289  1.00 46.64           C
ANISOU 3083  CG  PHE C 409     6104   5747   5871    856     63   -292       C
ATOM   3084  CD1 PHE C 409      79.335   5.171 -32.239  1.00 47.60           C
ANISOU 3084  CD1 PHE C 409     6190   5892   6005    856     33   -250       C
ATOM   3085  CD2 PHE C 409      79.846   6.392 -34.221  1.00 45.99           C
ANISOU 3085  CD2 PHE C 409     6003   5661   5809    885    104   -289       C
ATOM   3086  CE1 PHE C 409      80.661   4.798 -32.123  1.00 47.98           C
ANISOU 3086  CE1 PHE C 409     6185   5959   6087    886     42   -206       C
ATOM   3087  CE2 PHE C 409      81.174   6.023 -34.110  1.00 46.46           C
ANISOU 3087  CE2 PHE C 409     6010   5739   5904    914    114   -248       C
ATOM   3088  CZ  PHE C 409      81.582   5.225 -33.060  1.00 47.39           C
ANISOU 3088  CZ  PHE C 409     6092   5880   6035    915     83   -205       C
ATOM   3089  N   SER C 410      75.460   8.747 -34.478  1.00 35.70           N
ANISOU 3089  N   SER C 410     4844   4326   4394    761     76   -428       N
ATOM   3090  CA  SER C 410      74.092   9.065 -34.870  1.00 34.76           C
ANISOU 3090  CA  SER C 410     4778   4183   4246    744     75   -464       C
ATOM   3091  C   SER C 410      73.626   8.141 -35.990  1.00 34.02           C
ANISOU 3091  C   SER C 410     4738   4044   4145    789     94   -475       C
ATOM   3092  O   SER C 410      72.429   7.935 -36.185  1.00 33.33           O
ANISOU 3092  O   SER C 410     4697   3934   4033    780     84   -498       O
ATOM   3093  CB  SER C 410      73.979  10.527 -35.303  1.00 34.43           C
ANISOU 3093  CB  SER C 410     4730   4152   4200    719     98   -487       C
ATOM   3094  OG  SER C 410      74.926  10.839 -36.309  1.00 34.46           O
ANISOU 3094  OG  SER C 410     4719   4152   4224    753    139   -479       O
ATOM   3095  N   LEU C 411      74.587   7.592 -36.726  1.00 33.96           N
ANISOU 3095  N   LEU C 411     4721   4023   4160    836    123   -458       N
ATOM   3096  CA  LEU C 411      74.307   6.597 -37.753  1.00 33.85           C
ANISOU 3096  CA  LEU C 411     4754   3966   4142    881    144   -468       C
ATOM   3097  C   LEU C 411      75.274   5.434 -37.587  1.00 34.30           C
ANISOU 3097  C   LEU C 411     4790   4014   4231    920    149   -435       C
ATOM   3098  O   LEU C 411      76.486   5.636 -37.520  1.00 34.62           O
ANISOU 3098  O   LEU C 411     4783   4074   4298    935    163   -409       O
ATOM   3099  CB  LEU C 411      74.444   7.206 -39.149  1.00 33.84           C
ANISOU 3099  CB  LEU C 411     4771   3953   4135    904    188   -487       C
ATOM   3100  CG  LEU C 411      74.268   6.246 -40.328  1.00 34.01           C
ANISOU 3100  CG  LEU C 411     4838   3934   4150    950    216   -501       C
ATOM   3101  CD1 LEU C 411      72.904   5.576 -40.282  1.00 33.77           C
ANISOU 3101  CD1 LEU C 411     4861   3878   4091    938    193   -525       C
ATOM   3102  CD2 LEU C 411      74.466   6.974 -41.649  1.00 34.03           C
ANISOU 3102  CD2 LEU C 411     4852   3934   4142    969    259   -516       C
ATOM   3103  N   LEU C 412      74.742   4.219 -37.511  1.00 34.37           N
ANISOU 3103  N   LEU C 412     4832   3990   4238    937    138   -436       N
ATOM   3104  CA  LEU C 412      75.581   3.053 -37.258  1.00 34.82           C
ANISOU 3104  CA  LEU C 412     4869   4034   4329    974    141   -401       C
ATOM   3105  C   LEU C 412      75.131   1.823 -38.044  1.00 34.97           C
ANISOU 3105  C   LEU C 412     4939   3999   4349   1012    161   -417       C
ATOM   3106  O   LEU C 412      74.115   1.205 -37.727  1.00 34.81           O
ANISOU 3106  O   LEU C 412     4955   3958   4314    999    138   -430       O
ATOM   3107  CB  LEU C 412      75.623   2.747 -35.757  1.00 34.87           C
ANISOU 3107  CB  LEU C 412     4840   4067   4343    947     97   -369       C
ATOM   3108  CG  LEU C 412      76.790   1.901 -35.242  1.00 35.57           C
ANISOU 3108  CG  LEU C 412     4882   4162   4471    979     97   -319       C
ATOM   3109  CD1 LEU C 412      77.187   2.346 -33.844  1.00 36.42           C
ANISOU 3109  CD1 LEU C 412     4933   4324   4580    940     58   -287       C
ATOM   3110  CD2 LEU C 412      76.440   0.422 -35.244  1.00 35.60           C
ANISOU 3110  CD2 LEU C 412     4917   4121   4490   1010     97   -309       C
ATOM   3111  N   ILE C 413      75.903   1.473 -39.069  1.00 44.38           N
ANISOU 3111  N   ILE C 413     6133   5169   5560   1058    204   -416       N
ATOM   3112  CA  ILE C 413      75.632   0.288 -39.875  1.00 43.38           C
ANISOU 3112  CA  ILE C 413     6053   4992   5439   1096    229   -433       C
ATOM   3113  C   ILE C 413      76.726  -0.743 -39.624  1.00 43.92           C
ANISOU 3113  C   ILE C 413     6088   5043   5555   1138    245   -393       C
ATOM   3114  O   ILE C 413      77.852  -0.578 -40.094  1.00 44.25           O
ANISOU 3114  O   ILE C 413     6099   5092   5622   1169    277   -376       O
ATOM   3115  CB  ILE C 413      75.605   0.631 -41.376  1.00 42.74           C
ANISOU 3115  CB  ILE C 413     6005   4895   5340   1118    274   -469       C
ATOM   3116  CG1 ILE C 413      74.756   1.881 -41.625  1.00 41.24           C
ANISOU 3116  CG1 ILE C 413     5832   4729   5107   1078    262   -498       C
ATOM   3117  CG2 ILE C 413      75.094  -0.552 -42.186  1.00 42.55           C
ANISOU 3117  CG2 ILE C 413     6036   4820   5313   1147    296   -497       C
ATOM   3118  CD1 ILE C 413      73.310   1.736 -41.205  1.00 40.89           C
ANISOU 3118  CD1 ILE C 413     5829   4677   5032   1043    226   -522       C
ATOM   3119  N   MET C 414      76.413  -1.798 -38.878  1.00 49.33           N
ANISOU 3119  N   MET C 414     6779   5707   6256   1141    223   -376       N
ATOM   3120  CA  MET C 414      77.456  -2.727 -38.448  1.00 50.30           C
ANISOU 3120  CA  MET C 414     6864   5820   6429   1178    233   -328       C
ATOM   3121  C   MET C 414      77.200  -4.189 -38.814  1.00 50.07           C
ANISOU 3121  C   MET C 414     6872   5729   6423   1214    255   -334       C
ATOM   3122  O   MET C 414      76.087  -4.693 -38.666  1.00 49.44           O
ANISOU 3122  O   MET C 414     6836   5623   6325   1197    237   -357       O
ATOM   3123  CB  MET C 414      77.700  -2.596 -36.938  1.00 51.64           C
ANISOU 3123  CB  MET C 414     6981   6031   6608   1150    187   -281       C
ATOM   3124  CG  MET C 414      79.078  -3.064 -36.490  1.00 52.60           C
ANISOU 3124  CG  MET C 414     7041   6166   6779   1184    196   -223       C
ATOM   3125  SD  MET C 414      79.352  -2.917 -34.711  1.00 55.35           S
ANISOU 3125  SD  MET C 414     7326   6573   7131   1148    139   -167       S
ATOM   3126  CE  MET C 414      78.292  -4.217 -34.086  1.00 57.08           C
ANISOU 3126  CE  MET C 414     7584   6752   7353   1147    115   -161       C
ATOM   3127  N   LYS C 415      78.252  -4.850 -39.294  1.00 55.08           N
ANISOU 3127  N   LYS C 415     7488   6340   7101   1264    296   -312       N
ATOM   3128  CA  LYS C 415      78.251  -6.291 -39.554  1.00 55.05           C
ANISOU 3128  CA  LYS C 415     7510   6276   7133   1304    322   -309       C
ATOM   3129  C   LYS C 415      77.034  -6.794 -40.327  1.00 54.15           C
ANISOU 3129  C   LYS C 415     7470   6115   6990   1297    333   -368       C
ATOM   3130  O   LYS C 415      76.480  -7.850 -40.016  1.00 54.58           O
ANISOU 3130  O   LYS C 415     7550   6129   7061   1302    328   -368       O
ATOM   3131  CB  LYS C 415      78.420  -7.075 -38.246  1.00 55.96           C
ANISOU 3131  CB  LYS C 415     7589   6392   7282   1305    291   -254       C
ATOM   3132  CG  LYS C 415      79.793  -6.909 -37.615  1.00 56.81           C
ANISOU 3132  CG  LYS C 415     7621   6537   7428   1324    290   -190       C
ATOM   3133  CD  LYS C 415      79.974  -7.756 -36.369  0.00 57.52           C
ANISOU 3133  CD  LYS C 415     7675   6629   7552   1329    261   -131       C
ATOM   3134  CE  LYS C 415      81.382  -7.591 -35.816  0.00 58.22           C
ANISOU 3134  CE  LYS C 415     7686   6759   7677   1350    262    -66       C
ATOM   3135  NZ  LYS C 415      81.598  -8.349 -34.554  0.00 58.90           N
ANISOU 3135  NZ  LYS C 415     7729   6856   7793   1353    231     -1       N
ATOM   3136  N   ASN C 416      76.617  -6.025 -41.327  1.00 43.72           N
ANISOU 3136  N   ASN C 416     6182   4802   5627   1285    349   -417       N
ATOM   3137  CA  ASN C 416      75.546  -6.447 -42.217  1.00 43.22           C
ANISOU 3137  CA  ASN C 416     6188   4701   5534   1280    363   -475       C
ATOM   3138  C   ASN C 416      76.146  -7.007 -43.500  1.00 43.66           C
ANISOU 3138  C   ASN C 416     6264   4717   5606   1326    425   -500       C
ATOM   3139  O   ASN C 416      76.352  -6.285 -44.476  1.00 43.88           O
ANISOU 3139  O   ASN C 416     6302   4763   5609   1331    451   -526       O
ATOM   3140  CB  ASN C 416      74.590  -5.290 -42.511  1.00 42.52           C
ANISOU 3140  CB  ASN C 416     6124   4646   5385   1236    339   -513       C
ATOM   3141  CG  ASN C 416      73.871  -4.798 -41.266  1.00 42.71           C
ANISOU 3141  CG  ASN C 416     6134   4702   5392   1188    281   -495       C
ATOM   3142  OD1 ASN C 416      72.935  -5.437 -40.784  1.00 42.90           O
ANISOU 3142  OD1 ASN C 416     6187   4705   5411   1170    256   -504       O
ATOM   3143  ND2 ASN C 416      74.303  -3.656 -40.743  1.00 42.88           N
ANISOU 3143  ND2 ASN C 416     6111   4776   5406   1167    261   -472       N
ATOM   3144  N   LEU C 417      76.423  -8.306 -43.482  1.00 65.44           N
ANISOU 3144  N   LEU C 417     9031   7425   8409   1360    450   -490       N
ATOM   3145  CA  LEU C 417      77.207  -8.958 -44.526  1.00 66.11           C
ANISOU 3145  CA  LEU C 417     9125   7470   8523   1409    513   -504       C
ATOM   3146  C   LEU C 417      76.458  -9.165 -45.844  1.00 65.23           C
ANISOU 3146  C   LEU C 417     9080   7331   8373   1408    545   -575       C
ATOM   3147  O   LEU C 417      77.055  -9.577 -46.838  1.00 64.75           O
ANISOU 3147  O   LEU C 417     9032   7242   8326   1445    599   -595       O
ATOM   3148  CB  LEU C 417      77.738 -10.297 -44.008  1.00 66.96           C
ANISOU 3148  CB  LEU C 417     9216   7529   8697   1446    531   -468       C
ATOM   3149  CG  LEU C 417      78.524 -10.223 -42.696  1.00 67.93           C
ANISOU 3149  CG  LEU C 417     9270   7681   8860   1450    500   -393       C
ATOM   3150  CD1 LEU C 417      78.678 -11.602 -42.071  1.00 68.54           C
ANISOU 3150  CD1 LEU C 417     9340   7708   8995   1478    508   -358       C
ATOM   3151  CD2 LEU C 417      79.885  -9.581 -42.920  1.00 68.12           C
ANISOU 3151  CD2 LEU C 417     9240   7739   8904   1478    524   -359       C
ATOM   3152  N   ASN C 418      75.159  -8.880 -45.856  1.00 57.50           N
ANISOU 3152  N   ASN C 418     8142   6360   7344   1365    511   -612       N
ATOM   3153  CA  ASN C 418      74.351  -9.085 -47.057  1.00 56.88           C
ANISOU 3153  CA  ASN C 418     8127   6261   7224   1358    536   -679       C
ATOM   3154  C   ASN C 418      73.946  -7.802 -47.780  1.00 56.02           C
ANISOU 3154  C   ASN C 418     8031   6202   7053   1333    528   -708       C
ATOM   3155  O   ASN C 418      73.400  -7.851 -48.882  1.00 55.49           O
ANISOU 3155  O   ASN C 418     8010   6127   6947   1330    551   -760       O
ATOM   3156  CB  ASN C 418      73.105  -9.915 -46.737  1.00 57.33           C
ANISOU 3156  CB  ASN C 418     8228   6282   7271   1332    511   -708       C
ATOM   3157  CG  ASN C 418      73.337 -11.402 -46.905  1.00 58.40           C
ANISOU 3157  CG  ASN C 418     8383   6349   7457   1366    550   -717       C
ATOM   3158  OD1 ASN C 418      73.084 -12.189 -45.993  1.00 58.73           O
ANISOU 3158  OD1 ASN C 418     8419   6361   7533   1363    531   -692       O
ATOM   3159  ND2 ASN C 418      73.820 -11.796 -48.078  1.00 59.35           N
ANISOU 3159  ND2 ASN C 418     8525   6443   7581   1397    608   -752       N
ATOM   3160  N   VAL C 419      74.214  -6.657 -47.162  1.00 44.31           N
ANISOU 3160  N   VAL C 419     6505   4770   5561   1314    497   -672       N
ATOM   3161  CA  VAL C 419      73.830  -5.375 -47.743  1.00 43.29           C
ANISOU 3161  CA  VAL C 419     6382   4686   5379   1289    489   -692       C
ATOM   3162  C   VAL C 419      74.813  -4.929 -48.825  1.00 43.31           C
ANISOU 3162  C   VAL C 419     6374   4702   5380   1322    539   -696       C
ATOM   3163  O   VAL C 419      76.022  -4.883 -48.599  1.00 43.77           O
ANISOU 3163  O   VAL C 419     6387   4765   5481   1351    559   -658       O
ATOM   3164  CB  VAL C 419      73.702  -4.284 -46.664  1.00 43.62           C
ANISOU 3164  CB  VAL C 419     6385   4776   5414   1254    439   -656       C
ATOM   3165  CG1 VAL C 419      73.327  -2.954 -47.292  1.00 43.17           C
ANISOU 3165  CG1 VAL C 419     6333   4761   5307   1231    436   -675       C
ATOM   3166  CG2 VAL C 419      72.669  -4.692 -45.625  1.00 44.18           C
ANISOU 3166  CG2 VAL C 419     6468   4837   5481   1220    390   -654       C
ATOM   3167  N   THR C 420      74.283  -4.603 -50.001  1.00 37.66           N
ANISOU 3167  N   THR C 420     5699   3995   4616   1317    560   -742       N
ATOM   3168  CA  THR C 420      75.109  -4.222 -51.142  1.00 37.96           C
ANISOU 3168  CA  THR C 420     5732   4045   4646   1347    611   -751       C
ATOM   3169  C   THR C 420      75.149  -2.709 -51.348  1.00 37.57           C
ANISOU 3169  C   THR C 420     5661   4051   4563   1328    600   -738       C
ATOM   3170  O   THR C 420      76.151  -2.163 -51.811  1.00 37.75           O
ANISOU 3170  O   THR C 420     5654   4092   4598   1352    633   -720       O
ATOM   3171  CB  THR C 420      74.618  -4.894 -52.439  1.00 38.30           C
ANISOU 3171  CB  THR C 420     5834   4063   4654   1357    649   -809       C
ATOM   3172  OG1 THR C 420      73.258  -4.517 -52.688  1.00 37.91           O
ANISOU 3172  OG1 THR C 420     5825   4033   4547   1317    617   -844       O
ATOM   3173  CG2 THR C 420      74.706  -6.407 -52.320  1.00 38.77           C
ANISOU 3173  CG2 THR C 420     5914   4062   4754   1380    669   -824       C
ATOM   3174  N   SER C 421      74.053  -2.038 -51.008  1.00 37.06           N
ANISOU 3174  N   SER C 421     5609   4010   4461   1285    557   -746       N
ATOM   3175  CA  SER C 421      73.977  -0.586 -51.118  1.00 36.68           C
ANISOU 3175  CA  SER C 421     5540   4011   4385   1263    545   -734       C
ATOM   3176  C   SER C 421      73.171  -0.008 -49.960  1.00 36.14           C
ANISOU 3176  C   SER C 421     5459   3961   4310   1219    488   -718       C
ATOM   3177  O   SER C 421      72.326  -0.691 -49.384  1.00 36.01           O
ANISOU 3177  O   SER C 421     5467   3924   4292   1200    457   -730       O
ATOM   3178  CB  SER C 421      73.358  -0.175 -52.455  1.00 36.69           C
ANISOU 3178  CB  SER C 421     5582   4029   4329   1260    567   -772       C
ATOM   3179  OG  SER C 421      71.997  -0.563 -52.531  1.00 36.50           O
ANISOU 3179  OG  SER C 421     5605   3996   4267   1231    540   -807       O
ATOM   3180  N   LEU C 422      73.436   1.249 -49.621  1.00 37.93           N
ANISOU 3180  N   LEU C 422     5648   4226   4536   1201    476   -692       N
ATOM   3181  CA  LEU C 422      72.755   1.896 -48.504  1.00 37.74           C
ANISOU 3181  CA  LEU C 422     5608   4222   4508   1158    426   -677       C
ATOM   3182  C   LEU C 422      71.288   2.179 -48.819  1.00 37.18           C
ANISOU 3182  C   LEU C 422     5581   4157   4387   1126    403   -709       C
ATOM   3183  O   LEU C 422      70.395   1.732 -48.100  1.00 37.20           O
ANISOU 3183  O   LEU C 422     5602   4148   4385   1100    367   -717       O
ATOM   3184  CB  LEU C 422      73.486   3.178 -48.099  1.00 37.92           C
ANISOU 3184  CB  LEU C 422     5579   4282   4547   1148    425   -644       C
ATOM   3185  CG  LEU C 422      74.849   2.954 -47.440  1.00 38.52           C
ANISOU 3185  CG  LEU C 422     5603   4359   4675   1170    434   -606       C
ATOM   3186  CD1 LEU C 422      75.583   4.268 -47.237  1.00 38.70           C
ANISOU 3186  CD1 LEU C 422     5576   4420   4711   1159    439   -579       C
ATOM   3187  CD2 LEU C 422      74.688   2.220 -46.118  1.00 38.81           C
ANISOU 3187  CD2 LEU C 422     5626   4383   4737   1156    394   -588       C
ATOM   3188  N   GLY C 423      71.042   2.922 -49.892  1.00 43.09           N
ANISOU 3188  N   GLY C 423     6346   4928   5100   1127    425   -725       N
ATOM   3189  CA  GLY C 423      69.685   3.169 -50.347  1.00 41.54           C
ANISOU 3189  CA  GLY C 423     6190   4740   4854   1100    408   -754       C
ATOM   3190  C   GLY C 423      68.940   4.262 -49.601  1.00 41.30           C
ANISOU 3190  C   GLY C 423     6143   4735   4813   1058    371   -740       C
ATOM   3191  O   GLY C 423      67.710   4.296 -49.615  1.00 40.90           O
ANISOU 3191  O   GLY C 423     6122   4687   4730   1031    346   -759       O
ATOM   3192  N   PHE C 424      69.677   5.153 -48.945  1.00 36.86           N
ANISOU 3192  N   PHE C 424     5533   4193   4280   1052    369   -707       N
ATOM   3193  CA  PHE C 424      69.063   6.308 -48.296  1.00 36.63           C
ANISOU 3193  CA  PHE C 424     5486   4188   4245   1013    342   -696       C
ATOM   3194  C   PHE C 424      68.978   7.460 -49.291  1.00 36.60           C
ANISOU 3194  C   PHE C 424     5480   4211   4216   1014    369   -695       C
ATOM   3195  O   PHE C 424      69.701   8.449 -49.169  1.00 37.42           O
ANISOU 3195  O   PHE C 424     5545   4333   4340   1014    384   -671       O
ATOM   3196  CB  PHE C 424      69.869   6.740 -47.067  1.00 36.98           C
ANISOU 3196  CB  PHE C 424     5477   4242   4331   1001    327   -664       C
ATOM   3197  CG  PHE C 424      70.023   5.665 -46.028  1.00 37.33           C
ANISOU 3197  CG  PHE C 424     5517   4266   4401   1000    300   -657       C
ATOM   3198  CD1 PHE C 424      71.268   5.125 -45.750  1.00 37.95           C
ANISOU 3198  CD1 PHE C 424     5564   4337   4518   1028    315   -635       C
ATOM   3199  CD2 PHE C 424      68.924   5.195 -45.327  1.00 37.26           C
ANISOU 3199  CD2 PHE C 424     5532   4246   4380    972    261   -670       C
ATOM   3200  CE1 PHE C 424      71.414   4.138 -44.793  1.00 38.24           C
ANISOU 3200  CE1 PHE C 424     5594   4356   4580   1029    291   -623       C
ATOM   3201  CE2 PHE C 424      69.063   4.208 -44.370  1.00 37.20           C
ANISOU 3201  CE2 PHE C 424     5519   4220   4396    972    238   -659       C
ATOM   3202  CZ  PHE C 424      70.310   3.678 -44.103  1.00 38.27           C
ANISOU 3202  CZ  PHE C 424     5622   4348   4569   1001    253   -635       C
ATOM   3203  N   ARG C 425      68.090   7.332 -50.273  1.00 38.62           N
ANISOU 3203  N   ARG C 425     5778   4468   4427   1016    375   -720       N
ATOM   3204  CA  ARG C 425      68.054   8.271 -51.393  1.00 38.23           C
ANISOU 3204  CA  ARG C 425     5730   4446   4351   1024    405   -717       C
ATOM   3205  C   ARG C 425      67.407   9.621 -51.077  1.00 38.08           C
ANISOU 3205  C   ARG C 425     5693   4450   4327    992    391   -701       C
ATOM   3206  O   ARG C 425      67.464  10.543 -51.891  1.00 38.49           O
ANISOU 3206  O   ARG C 425     5737   4523   4363    998    417   -690       O
ATOM   3207  CB  ARG C 425      67.402   7.630 -52.625  1.00 38.14           C
ANISOU 3207  CB  ARG C 425     5767   4434   4291   1037    419   -747       C
ATOM   3208  CG  ARG C 425      65.949   7.209 -52.453  1.00 37.75           C
ANISOU 3208  CG  ARG C 425     5756   4380   4209   1009    382   -772       C
ATOM   3209  CD  ARG C 425      65.399   6.670 -53.768  1.00 37.95           C
ANISOU 3209  CD  ARG C 425     5826   4412   4183   1021    398   -803       C
ATOM   3210  NE  ARG C 425      63.976   6.349 -53.703  1.00 37.84           N
ANISOU 3210  NE  ARG C 425     5845   4398   4134    992    364   -825       N
ATOM   3211  CZ  ARG C 425      63.261   5.930 -54.742  0.00 37.69           C
ANISOU 3211  CZ  ARG C 425     5865   4390   4065    992    370   -854       C
ATOM   3212  NH1 ARG C 425      63.837   5.782 -55.927  0.00 37.94           N
ANISOU 3212  NH1 ARG C 425     5908   4435   4074   1021    409   -865       N
ATOM   3213  NH2 ARG C 425      61.972   5.660 -54.600  0.00 37.31           N
ANISOU 3213  NH2 ARG C 425     5844   4344   3989    964    336   -873       N
ATOM   3214  N   SER C 426      66.803   9.744 -49.899  1.00 36.96           N
ANISOU 3214  N   SER C 426     5542   4302   4197    958    352   -698       N
ATOM   3215  CA  SER C 426      66.192  11.007 -49.497  1.00 36.79           C
ANISOU 3215  CA  SER C 426     5503   4298   4177    926    341   -684       C
ATOM   3216  C   SER C 426      66.963  11.685 -48.369  1.00 37.01           C
ANISOU 3216  C   SER C 426     5482   4330   4251    909    336   -662       C
ATOM   3217  O   SER C 426      66.690  12.836 -48.027  1.00 36.96           O
ANISOU 3217  O   SER C 426     5454   4336   4253    884    335   -651       O
ATOM   3218  CB  SER C 426      64.734  10.801 -49.085  1.00 36.35           C
ANISOU 3218  CB  SER C 426     5477   4238   4096    895    303   -701       C
ATOM   3219  OG  SER C 426      63.963  10.306 -50.165  1.00 36.19           O
ANISOU 3219  OG  SER C 426     5498   4221   4031    905    307   -721       O
ATOM   3220  N   LEU C 427      67.924  10.967 -47.794  1.00 36.66           N
ANISOU 3220  N   LEU C 427     5420   4274   4236    922    333   -657       N
ATOM   3221  CA  LEU C 427      68.727  11.496 -46.695  1.00 37.34           C
ANISOU 3221  CA  LEU C 427     5457   4367   4362    906    326   -637       C
ATOM   3222  C   LEU C 427      69.566  12.689 -47.145  1.00 37.60           C
ANISOU 3222  C   LEU C 427     5455   4419   4414    912    362   -617       C
ATOM   3223  O   LEU C 427      70.442  12.554 -47.999  1.00 37.74           O
ANISOU 3223  O   LEU C 427     5466   4437   4435    947    397   -610       O
ATOM   3224  CB  LEU C 427      69.633  10.406 -46.121  1.00 37.50           C
ANISOU 3224  CB  LEU C 427     5465   4375   4408    924    318   -630       C
ATOM   3225  CG  LEU C 427      70.445  10.790 -44.882  1.00 38.14           C
ANISOU 3225  CG  LEU C 427     5495   4469   4529    904    304   -609       C
ATOM   3226  CD1 LEU C 427      69.527  11.064 -43.700  1.00 37.97           C
ANISOU 3226  CD1 LEU C 427     5472   4452   4503    858    262   -614       C
ATOM   3227  CD2 LEU C 427      71.457   9.707 -44.542  1.00 38.62           C
ANISOU 3227  CD2 LEU C 427     5540   4519   4614    931    304   -596       C
ATOM   3228  N   LYS C 428      69.294  13.854 -46.566  1.00 52.12           N
ANISOU 3228  N   LYS C 428     7268   6270   6265    878    357   -610       N
ATOM   3229  CA  LYS C 428      69.996  15.075 -46.949  1.00 52.78           C
ANISOU 3229  CA  LYS C 428     7317   6368   6369    880    392   -592       C
ATOM   3230  C   LYS C 428      70.767  15.713 -45.796  1.00 53.29           C
ANISOU 3230  C   LYS C 428     7331   6443   6476    853    385   -580       C
ATOM   3231  O   LYS C 428      71.689  16.495 -46.022  1.00 53.82           O
ANISOU 3231  O   LYS C 428     7361   6519   6567    858    416   -564       O
ATOM   3232  CB  LYS C 428      69.023  16.092 -47.551  1.00 52.28           C
ANISOU 3232  CB  LYS C 428     7267   6311   6286    867    404   -592       C
ATOM   3233  CG  LYS C 428      68.477  15.704 -48.916  1.00 52.43           C
ANISOU 3233  CG  LYS C 428     7327   6330   6263    896    421   -599       C
ATOM   3234  CD  LYS C 428      67.624  16.816 -49.505  0.00 52.24           C
ANISOU 3234  CD  LYS C 428     7308   6317   6223    884    435   -590       C
ATOM   3235  CE  LYS C 428      67.145  16.466 -50.904  0.00 52.04           C
ANISOU 3235  CE  LYS C 428     7320   6300   6152    913    452   -594       C
ATOM   3236  NZ  LYS C 428      66.315  17.550 -51.498  0.00 51.98           N
ANISOU 3236  NZ  LYS C 428     7314   6306   6129    904    466   -580       N
ATOM   3237  N   GLU C 429      70.393  15.384 -44.563  1.00 52.88           N
ANISOU 3237  N   GLU C 429     7274   6389   6428    822    346   -587       N
ATOM   3238  CA  GLU C 429      71.035  15.995 -43.403  1.00 53.60           C
ANISOU 3238  CA  GLU C 429     7318   6495   6553    790    336   -579       C
ATOM   3239  C   GLU C 429      71.176  15.067 -42.199  1.00 53.44           C
ANISOU 3239  C   GLU C 429     7289   6477   6539    776    295   -579       C
ATOM   3240  O   GLU C 429      70.216  14.425 -41.773  1.00 52.43           O
ANISOU 3240  O   GLU C 429     7192   6340   6390    763    263   -592       O
ATOM   3241  CB  GLU C 429      70.291  17.268 -42.985  1.00 54.37           C
ANISOU 3241  CB  GLU C 429     7405   6598   6655    747    336   -585       C
ATOM   3242  CG  GLU C 429      70.830  17.903 -41.709  1.00 55.62           C
ANISOU 3242  CG  GLU C 429     7516   6772   6844    707    323   -584       C
ATOM   3243  CD  GLU C 429      70.056  19.138 -41.292  1.00 56.03           C
ANISOU 3243  CD  GLU C 429     7561   6826   6903    664    327   -594       C
ATOM   3244  OE1 GLU C 429      70.207  19.569 -40.129  1.00 56.77           O
ANISOU 3244  OE1 GLU C 429     7625   6931   7014    623    311   -601       O
ATOM   3245  OE2 GLU C 429      69.300  19.679 -42.125  1.00 56.04           O
ANISOU 3245  OE2 GLU C 429     7585   6816   6892    671    347   -595       O
ATOM   3246  N   ILE C 430      72.390  15.006 -41.662  1.00 32.60           N
ANISOU 3246  N   ILE C 430     4606   3852   3929    778    297   -563       N
ATOM   3247  CA  ILE C 430      72.645  14.381 -40.372  1.00 32.63           C
ANISOU 3247  CA  ILE C 430     4589   3867   3943    758    259   -558       C
ATOM   3248  C   ILE C 430      73.151  15.476 -39.437  1.00 32.64           C
ANISOU 3248  C   ILE C 430     4539   3895   3968    715    257   -554       C
ATOM   3249  O   ILE C 430      74.337  15.807 -39.438  1.00 32.91           O
ANISOU 3249  O   ILE C 430     4531   3945   4029    722    275   -538       O
ATOM   3250  CB  ILE C 430      73.682  13.252 -40.481  1.00 32.98           C
ANISOU 3250  CB  ILE C 430     4621   3909   4001    798    262   -538       C
ATOM   3251  CG1 ILE C 430      73.270  12.261 -41.571  1.00 33.04           C
ANISOU 3251  CG1 ILE C 430     4678   3887   3987    841    274   -547       C
ATOM   3252  CG2 ILE C 430      73.839  12.544 -39.144  1.00 33.03           C
ANISOU 3252  CG2 ILE C 430     4607   3927   4015    778    220   -528       C
ATOM   3253  CD1 ILE C 430      74.244  11.118 -41.765  1.00 33.41           C
ANISOU 3253  CD1 ILE C 430     4718   3925   4052    883    283   -530       C
ATOM   3254  N   SER C 431      72.235  16.035 -38.650  1.00 32.36           N
ANISOU 3254  N   SER C 431     4508   3864   3922    670    235   -570       N
ATOM   3255  CA  SER C 431      72.475  17.272 -37.902  1.00 32.34           C
ANISOU 3255  CA  SER C 431     4465   3883   3940    624    239   -576       C
ATOM   3256  C   SER C 431      73.663  17.242 -36.938  1.00 32.63           C
ANISOU 3256  C   SER C 431     4447   3950   3999    607    227   -562       C
ATOM   3257  O   SER C 431      74.325  18.261 -36.738  1.00 32.76           O
ANISOU 3257  O   SER C 431     4423   3984   4040    584    246   -562       O
ATOM   3258  CB  SER C 431      71.207  17.696 -37.155  1.00 32.01           C
ANISOU 3258  CB  SER C 431     4442   3839   3881    579    216   -598       C
ATOM   3259  OG  SER C 431      70.117  17.848 -38.047  1.00 31.77           O
ANISOU 3259  OG  SER C 431     4456   3784   3832    592    229   -608       O
ATOM   3260  N   ALA C 432      73.929  16.085 -36.341  1.00 39.65           N
ANISOU 3260  N   ALA C 432     5334   4849   4884    618    195   -549       N
ATOM   3261  CA  ALA C 432      75.029  15.961 -35.388  1.00 41.89           C
ANISOU 3261  CA  ALA C 432     5564   5167   5186    602    178   -531       C
ATOM   3262  C   ALA C 432      75.438  14.508 -35.182  1.00 42.27           C
ANISOU 3262  C   ALA C 432     5615   5215   5233    636    155   -506       C
ATOM   3263  O   ALA C 432      74.734  13.591 -35.600  1.00 41.57           O
ANISOU 3263  O   ALA C 432     5572   5097   5126    664    148   -509       O
ATOM   3264  CB  ALA C 432      74.651  16.594 -34.055  1.00 42.06           C
ANISOU 3264  CB  ALA C 432     5562   5215   5201    540    150   -546       C
ATOM   3265  N   GLY C 433      76.583  14.309 -34.536  1.00 33.59           N
ANISOU 3265  N   GLY C 433     4465   4147   4153    634    145   -482       N
ATOM   3266  CA  GLY C 433      77.044  12.977 -34.192  1.00 33.84           C
ANISOU 3266  CA  GLY C 433     4489   4181   4188    664    123   -453       C
ATOM   3267  C   GLY C 433      78.098  12.420 -35.128  1.00 34.18           C
ANISOU 3267  C   GLY C 433     4521   4210   4254    721    154   -429       C
ATOM   3268  O   GLY C 433      78.504  13.073 -36.089  1.00 34.22           O
ANISOU 3268  O   GLY C 433     4524   4206   4271    738    193   -434       O
ATOM   3269  N   ARG C 434      78.542  11.202 -34.838  1.00 50.00           N
ANISOU 3269  N   ARG C 434     6517   6213   6266    750    138   -401       N
ATOM   3270  CA  ARG C 434      79.537  10.528 -35.661  1.00 50.03           C
ANISOU 3270  CA  ARG C 434     6511   6202   6295    807    168   -376       C
ATOM   3271  C   ARG C 434      78.883   9.436 -36.501  1.00 48.99           C
ANISOU 3271  C   ARG C 434     6440   6023   6154    851    178   -384       C
ATOM   3272  O   ARG C 434      77.748   9.037 -36.241  1.00 47.97           O
ANISOU 3272  O   ARG C 434     6352   5876   5999    837    155   -401       O
ATOM   3273  CB  ARG C 434      80.641   9.931 -34.785  1.00 50.83           C
ANISOU 3273  CB  ARG C 434     6556   6336   6421    813    148   -334       C
ATOM   3274  CG  ARG C 434      81.284  10.929 -33.834  1.00 51.95           C
ANISOU 3274  CG  ARG C 434     6636   6532   6570    763    132   -327       C
ATOM   3275  CD  ARG C 434      82.380  10.281 -33.004  1.00 52.88           C
ANISOU 3275  CD  ARG C 434     6695   6686   6709    771    111   -282       C
ATOM   3276  NE  ARG C 434      83.509   9.856 -33.826  1.00 53.49           N
ANISOU 3276  NE  ARG C 434     6751   6752   6820    826    146   -254       N
ATOM   3277  CZ  ARG C 434      84.121   8.683 -33.707  1.00 54.35           C
ANISOU 3277  CZ  ARG C 434     6844   6857   6950    867    141   -214       C
ATOM   3278  NH1 ARG C 434      83.712   7.809 -32.797  1.00 54.63           N
ANISOU 3278  NH1 ARG C 434     6883   6899   6976    861    103   -196       N
ATOM   3279  NH2 ARG C 434      85.142   8.382 -34.499  1.00 54.33           N
ANISOU 3279  NH2 ARG C 434     6821   6842   6979    916    178   -192       N
ATOM   3280  N   ILE C 435      79.605   8.957 -37.508  1.00 47.77           N
ANISOU 3280  N   ILE C 435     6288   5846   6018    903    215   -373       N
ATOM   3281  CA  ILE C 435      79.082   7.932 -38.403  1.00 46.92           C
ANISOU 3281  CA  ILE C 435     6235   5692   5901    945    232   -384       C
ATOM   3282  C   ILE C 435      79.973   6.695 -38.397  1.00 47.25           C
ANISOU 3282  C   ILE C 435     6260   5721   5973    991    239   -351       C
ATOM   3283  O   ILE C 435      81.181   6.788 -38.610  1.00 47.98           O
ANISOU 3283  O   ILE C 435     6309   5827   6095   1015    263   -326       O
ATOM   3284  CB  ILE C 435      78.945   8.464 -39.841  1.00 45.74           C
ANISOU 3284  CB  ILE C 435     6118   5522   5741    967    276   -409       C
ATOM   3285  CG1 ILE C 435      78.020   9.683 -39.864  1.00 45.53           C
ANISOU 3285  CG1 ILE C 435     6107   5505   5687    924    271   -437       C
ATOM   3286  CG2 ILE C 435      78.427   7.377 -40.769  1.00 44.48           C
ANISOU 3286  CG2 ILE C 435     6014   5318   5569   1008    294   -424       C
ATOM   3287  CD1 ILE C 435      77.888  10.327 -41.222  1.00 44.94           C
ANISOU 3287  CD1 ILE C 435     6058   5416   5601    943    313   -456       C
ATOM   3288  N   TYR C 436      79.372   5.537 -38.148  1.00 51.01           N
ANISOU 3288  N   TYR C 436     6768   6170   6444   1004    221   -350       N
ATOM   3289  CA  TYR C 436      80.123   4.290 -38.082  1.00 51.54           C
ANISOU 3289  CA  TYR C 436     6820   6220   6544   1049    229   -317       C
ATOM   3290  C   TYR C 436      79.559   3.250 -39.049  1.00 50.69           C
ANISOU 3290  C   TYR C 436     6773   6056   6430   1088    254   -339       C
ATOM   3291  O   TYR C 436      78.516   2.648 -38.795  1.00 50.60           O
ANISOU 3291  O   TYR C 436     6803   6023   6401   1077    232   -355       O
ATOM   3292  CB  TYR C 436      80.140   3.756 -36.645  1.00 52.60           C
ANISOU 3292  CB  TYR C 436     6923   6376   6686   1027    183   -284       C
ATOM   3293  CG  TYR C 436      81.002   2.532 -36.436  1.00 53.17           C
ANISOU 3293  CG  TYR C 436     6969   6435   6797   1072    190   -240       C
ATOM   3294  CD1 TYR C 436      82.388   2.620 -36.450  1.00 53.83           C
ANISOU 3294  CD1 TYR C 436     6995   6541   6916   1096    209   -203       C
ATOM   3295  CD2 TYR C 436      80.429   1.291 -36.201  1.00 52.99           C
ANISOU 3295  CD2 TYR C 436     6979   6377   6779   1089    178   -234       C
ATOM   3296  CE1 TYR C 436      83.178   1.502 -36.254  1.00 53.99           C
ANISOU 3296  CE1 TYR C 436     6989   6548   6975   1139    217   -160       C
ATOM   3297  CE2 TYR C 436      81.209   0.167 -36.007  1.00 53.31           C
ANISOU 3297  CE2 TYR C 436     6994   6401   6860   1131    188   -191       C
ATOM   3298  CZ  TYR C 436      82.583   0.278 -36.032  1.00 53.88           C
ANISOU 3298  CZ  TYR C 436     7007   6496   6967   1157    207   -153       C
ATOM   3299  OH  TYR C 436      83.365  -0.836 -35.835  1.00 54.17           O
ANISOU 3299  OH  TYR C 436     7018   6518   7048   1201    218   -107       O
ATOM   3300  N   ILE C 437      80.255   3.060 -40.166  1.00 38.03           N
ANISOU 3300  N   ILE C 437     5174   4432   4843   1132    302   -341       N
ATOM   3301  CA  ILE C 437      79.861   2.081 -41.173  1.00 37.55           C
ANISOU 3301  CA  ILE C 437     5167   4320   4779   1171    332   -365       C
ATOM   3302  C   ILE C 437      81.001   1.100 -41.418  1.00 37.99           C
ANISOU 3302  C   ILE C 437     5199   4355   4880   1224    364   -334       C
ATOM   3303  O   ILE C 437      81.939   1.397 -42.159  1.00 38.07           O
ANISOU 3303  O   ILE C 437     5189   4370   4908   1253    403   -327       O
ATOM   3304  CB  ILE C 437      79.488   2.758 -42.506  1.00 36.90           C
ANISOU 3304  CB  ILE C 437     5124   4229   4666   1176    367   -405       C
ATOM   3305  CG1 ILE C 437      78.400   3.812 -42.285  1.00 36.46           C
ANISOU 3305  CG1 ILE C 437     5087   4196   4571   1125    338   -431       C
ATOM   3306  CG2 ILE C 437      79.035   1.722 -43.524  1.00 36.49           C
ANISOU 3306  CG2 ILE C 437     5129   4129   4606   1211    396   -434       C
ATOM   3307  CD1 ILE C 437      78.032   4.584 -43.533  1.00 35.88           C
ANISOU 3307  CD1 ILE C 437     5045   4119   4467   1128    370   -464       C
ATOM   3308  N   SER C 438      80.920  -0.069 -40.791  1.00 54.31           N
ANISOU 3308  N   SER C 438     7267   6398   6968   1238    348   -313       N
ATOM   3309  CA  SER C 438      81.995  -1.050 -40.887  1.00 55.18           C
ANISOU 3309  CA  SER C 438     7350   6487   7128   1289    377   -278       C
ATOM   3310  C   SER C 438      81.502  -2.492 -40.875  1.00 54.88           C
ANISOU 3310  C   SER C 438     7350   6396   7105   1314    381   -281       C
ATOM   3311  O   SER C 438      80.361  -2.770 -40.501  1.00 54.26           O
ANISOU 3311  O   SER C 438     7310   6305   7002   1287    351   -302       O
ATOM   3312  CB  SER C 438      83.009  -0.840 -39.760  1.00 56.71           C
ANISOU 3312  CB  SER C 438     7468   6726   7354   1282    353   -220       C
ATOM   3313  OG  SER C 438      83.640   0.424 -39.873  1.00 57.40           O
ANISOU 3313  OG  SER C 438     7516   6857   7434   1264    357   -218       O
ATOM   3314  N   ALA C 439      82.385  -3.395 -41.298  1.00 44.44           N
ANISOU 3314  N   ALA C 439     6015   5042   5827   1366    422   -260       N
ATOM   3315  CA  ALA C 439      82.132  -4.836 -41.307  1.00 44.49           C
ANISOU 3315  CA  ALA C 439     6050   4992   5861   1397    435   -257       C
ATOM   3316  C   ALA C 439      80.977  -5.257 -42.215  1.00 43.83           C
ANISOU 3316  C   ALA C 439     6046   4864   5746   1394    451   -319       C
ATOM   3317  O   ALA C 439      80.461  -6.369 -42.104  1.00 44.21           O
ANISOU 3317  O   ALA C 439     6124   4865   5807   1406    453   -326       O
ATOM   3318  CB  ALA C 439      81.935  -5.360 -39.894  1.00 44.94           C
ANISOU 3318  CB  ALA C 439     6079   5060   5935   1380    387   -214       C
ATOM   3319  N   ASN C 440      80.578  -4.362 -43.110  1.00 38.43           N
ANISOU 3319  N   ASN C 440     5391   4194   5018   1378    463   -363       N
ATOM   3320  CA  ASN C 440      79.619  -4.699 -44.150  1.00 38.34           C
ANISOU 3320  CA  ASN C 440     5449   4145   4973   1379    485   -423       C
ATOM   3321  C   ASN C 440      80.388  -5.098 -45.405  1.00 38.82           C
ANISOU 3321  C   ASN C 440     5521   4176   5051   1427    550   -439       C
ATOM   3322  O   ASN C 440      80.601  -4.281 -46.300  1.00 38.73           O
ANISOU 3322  O   ASN C 440     5516   4186   5015   1429    574   -460       O
ATOM   3323  CB  ASN C 440      78.694  -3.515 -44.429  1.00 37.75           C
ANISOU 3323  CB  ASN C 440     5400   4104   4839   1334    462   -458       C
ATOM   3324  CG  ASN C 440      78.141  -2.900 -43.158  1.00 37.29           C
ANISOU 3324  CG  ASN C 440     5320   4083   4767   1285    402   -438       C
ATOM   3325  OD1 ASN C 440      77.203  -3.423 -42.558  1.00 37.12           O
ANISOU 3325  OD1 ASN C 440     5323   4045   4734   1263    370   -446       O
ATOM   3326  ND2 ASN C 440      78.724  -1.782 -42.739  1.00 37.13           N
ANISOU 3326  ND2 ASN C 440     5251   4111   4745   1267    388   -414       N
ATOM   3327  N   ARG C 441      80.795  -6.362 -45.457  1.00 48.66           N
ANISOU 3327  N   ARG C 441     6771   5374   6342   1467    579   -428       N
ATOM   3328  CA  ARG C 441      81.766  -6.849 -46.438  1.00 49.04           C
ANISOU 3328  CA  ARG C 441     6817   5393   6422   1518    643   -432       C
ATOM   3329  C   ARG C 441      81.373  -6.740 -47.912  1.00 48.57           C
ANISOU 3329  C   ARG C 441     6814   5318   6323   1526    686   -494       C
ATOM   3330  O   ARG C 441      82.215  -6.934 -48.788  1.00 48.88           O
ANISOU 3330  O   ARG C 441     6849   5343   6381   1565    740   -500       O
ATOM   3331  CB  ARG C 441      82.143  -8.299 -46.120  1.00 49.57           C
ANISOU 3331  CB  ARG C 441     6880   5405   6548   1557    665   -409       C
ATOM   3332  CG  ARG C 441      82.824  -8.472 -44.776  1.00 50.86           C
ANISOU 3332  CG  ARG C 441     6978   5587   6758   1561    633   -337       C
ATOM   3333  CD  ARG C 441      84.063  -7.599 -44.685  1.00 51.96           C
ANISOU 3333  CD  ARG C 441     7053   5776   6915   1574    640   -295       C
ATOM   3334  NE  ARG C 441      84.606  -7.540 -43.331  0.00 53.52           N
ANISOU 3334  NE  ARG C 441     7184   6007   7143   1566    599   -228       N
ATOM   3335  CZ  ARG C 441      85.847  -7.162 -43.048  0.00 54.37           C
ANISOU 3335  CZ  ARG C 441     7225   6148   7284   1585    607   -178       C
ATOM   3336  NH1 ARG C 441      86.671  -6.822 -44.028  0.00 54.14           N
ANISOU 3336  NH1 ARG C 441     7187   6120   7264   1615    656   -187       N
ATOM   3337  NH2 ARG C 441      86.268  -7.131 -41.790  0.00 55.16           N
ANISOU 3337  NH2 ARG C 441     7266   6283   7407   1574    565   -118       N
ATOM   3338  N   GLN C 442      80.109  -6.443 -48.190  1.00 44.60           N
ANISOU 3338  N   GLN C 442     6361   4820   5764   1488    662   -541       N
ATOM   3339  CA  GLN C 442      79.639  -6.404 -49.570  1.00 43.55           C
ANISOU 3339  CA  GLN C 442     6284   4676   5589   1491    699   -600       C
ATOM   3340  C   GLN C 442      78.940  -5.087 -49.869  1.00 43.55           C
ANISOU 3340  C   GLN C 442     6295   4725   5526   1451    672   -621       C
ATOM   3341  O   GLN C 442      78.269  -4.936 -50.893  1.00 43.42           O
ANISOU 3341  O   GLN C 442     6327   4709   5463   1443    688   -669       O
ATOM   3342  CB  GLN C 442      78.725  -7.599 -49.858  1.00 43.36           C
ANISOU 3342  CB  GLN C 442     6319   4598   5559   1491    707   -645       C
ATOM   3343  CG  GLN C 442      79.361  -8.944 -49.515  1.00 43.81           C
ANISOU 3343  CG  GLN C 442     6364   4599   5683   1531    735   -623       C
ATOM   3344  CD  GLN C 442      78.569 -10.127 -50.034  1.00 43.74           C
ANISOU 3344  CD  GLN C 442     6416   4532   5670   1533    758   -675       C
ATOM   3345  OE1 GLN C 442      77.550  -9.963 -50.704  0.00 43.31           O
ANISOU 3345  OE1 GLN C 442     6413   4482   5561   1505    752   -729       O
ATOM   3346  NE2 GLN C 442      79.039 -11.330 -49.728  0.00 44.17           N
ANISOU 3346  NE2 GLN C 442     6463   4532   5787   1567    784   -657       N
ATOM   3347  N   LEU C 443      79.113  -4.129 -48.964  1.00 41.31           N
ANISOU 3347  N   LEU C 443     5966   4484   5244   1426    632   -582       N
ATOM   3348  CA  LEU C 443      78.596  -2.789 -49.180  1.00 40.80           C
ANISOU 3348  CA  LEU C 443     5905   4467   5131   1390    611   -594       C
ATOM   3349  C   LEU C 443      79.478  -2.060 -50.186  1.00 40.86           C
ANISOU 3349  C   LEU C 443     5896   4497   5133   1414    656   -594       C
ATOM   3350  O   LEU C 443      80.672  -1.846 -49.951  1.00 41.23           O
ANISOU 3350  O   LEU C 443     5890   4555   5220   1438    673   -555       O
ATOM   3351  CB  LEU C 443      78.542  -1.999 -47.871  1.00 40.90           C
ANISOU 3351  CB  LEU C 443     5873   4517   5150   1354    557   -555       C
ATOM   3352  CG  LEU C 443      77.755  -0.684 -47.905  1.00 40.65           C
ANISOU 3352  CG  LEU C 443     5848   4527   5071   1311    529   -570       C
ATOM   3353  CD1 LEU C 443      76.344  -0.943 -48.394  1.00 39.94           C
ANISOU 3353  CD1 LEU C 443     5822   4421   4933   1288    517   -618       C
ATOM   3354  CD2 LEU C 443      77.730  -0.013 -46.537  1.00 40.64           C
ANISOU 3354  CD2 LEU C 443     5803   4558   5081   1274    479   -535       C
ATOM   3355  N   CYS C 444      78.883  -1.715 -51.323  1.00 58.25           N
ANISOU 3355  N   CYS C 444     8141   6705   7286   1409    677   -636       N
ATOM   3356  CA  CYS C 444      79.516  -0.844 -52.312  1.00 58.56           C
ANISOU 3356  CA  CYS C 444     8169   6772   7309   1425    715   -637       C
ATOM   3357  C   CYS C 444      78.723   0.470 -52.437  1.00 58.62           C
ANISOU 3357  C   CYS C 444     8183   6822   7267   1384    688   -645       C
ATOM   3358  O   CYS C 444      77.683   0.643 -51.776  1.00 59.03           O
ANISOU 3358  O   CYS C 444     8250   6880   7299   1346    641   -652       O
ATOM   3359  CB  CYS C 444      79.629  -1.532 -53.679  1.00 58.51           C
ANISOU 3359  CB  CYS C 444     8204   6740   7285   1458    771   -678       C
ATOM   3360  SG  CYS C 444      81.119  -2.550 -53.921  1.00 61.18           S
ANISOU 3360  SG  CYS C 444     8517   7042   7688   1518    830   -659       S
ATOM   3361  N   TYR C 445      79.244   1.386 -53.260  1.00 46.47           N
ANISOU 3361  N   TYR C 445     6631   5313   5714   1394    720   -641       N
ATOM   3362  CA  TYR C 445      78.643   2.707 -53.573  1.00 46.01           C
ANISOU 3362  CA  TYR C 445     6574   5294   5613   1363    707   -645       C
ATOM   3363  C   TYR C 445      78.965   3.840 -52.585  1.00 45.99           C
ANISOU 3363  C   TYR C 445     6519   5323   5633   1336    677   -605       C
ATOM   3364  O   TYR C 445      78.916   5.018 -52.941  1.00 46.09           O
ANISOU 3364  O   TYR C 445     6519   5367   5626   1322    682   -599       O
ATOM   3365  CB  TYR C 445      77.126   2.627 -53.815  1.00 45.52           C
ANISOU 3365  CB  TYR C 445     6567   5231   5497   1332    679   -683       C
ATOM   3366  CG  TYR C 445      76.725   1.747 -54.976  1.00 45.57           C
ANISOU 3366  CG  TYR C 445     6628   5217   5470   1351    711   -728       C
ATOM   3367  CD1 TYR C 445      76.308   0.443 -54.766  1.00 45.22           C
ANISOU 3367  CD1 TYR C 445     6617   5132   5434   1356    704   -753       C
ATOM   3368  CD2 TYR C 445      76.759   2.224 -56.279  1.00 45.44           C
ANISOU 3368  CD2 TYR C 445     6631   5222   5414   1364    749   -745       C
ATOM   3369  CE1 TYR C 445      75.937  -0.364 -55.817  1.00 45.03           C
ANISOU 3369  CE1 TYR C 445     6643   5088   5379   1370    735   -799       C
ATOM   3370  CE2 TYR C 445      76.387   1.421 -57.342  1.00 45.24           C
ANISOU 3370  CE2 TYR C 445     6655   5182   5352   1378    778   -790       C
ATOM   3371  CZ  TYR C 445      75.978   0.124 -57.100  1.00 45.11           C
ANISOU 3371  CZ  TYR C 445     6671   5124   5345   1380    771   -818       C
ATOM   3372  OH  TYR C 445      75.601  -0.704 -58.131  1.00 44.71           O
ANISOU 3372  OH  TYR C 445     6671   5057   5261   1391    802   -867       O
ATOM   3373  N   HIS C 446      79.303   3.476 -51.355  1.00 48.88           N
ANISOU 3373  N   HIS C 446     6851   5681   6040   1329    647   -579       N
ATOM   3374  CA  HIS C 446      79.486   4.445 -50.278  1.00 49.36           C
ANISOU 3374  CA  HIS C 446     6864   5772   6118   1296    612   -547       C
ATOM   3375  C   HIS C 446      80.854   5.129 -50.307  1.00 49.83           C
ANISOU 3375  C   HIS C 446     6865   5853   6213   1314    640   -513       C
ATOM   3376  O   HIS C 446      81.096   6.093 -49.575  1.00 50.67           O
ANISOU 3376  O   HIS C 446     6930   5989   6333   1285    618   -490       O
ATOM   3377  CB  HIS C 446      79.345   3.727 -48.944  1.00 49.96           C
ANISOU 3377  CB  HIS C 446     6926   5836   6222   1282    569   -531       C
ATOM   3378  CG  HIS C 446      80.486   2.806 -48.646  1.00 50.92           C
ANISOU 3378  CG  HIS C 446     7015   5938   6393   1320    587   -504       C
ATOM   3379  ND1 HIS C 446      80.586   1.538 -49.165  1.00 51.17           N
ANISOU 3379  ND1 HIS C 446     7078   5930   6435   1356    614   -518       N
ATOM   3380  CD2 HIS C 446      81.601   2.993 -47.891  1.00 51.96           C
ANISOU 3380  CD2 HIS C 446     7086   6088   6569   1326    583   -461       C
ATOM   3381  CE1 HIS C 446      81.699   0.972 -48.740  1.00 52.02           C
ANISOU 3381  CE1 HIS C 446     7143   6028   6594   1386    627   -483       C
ATOM   3382  NE2 HIS C 446      82.333   1.833 -47.967  1.00 52.44           N
ANISOU 3382  NE2 HIS C 446     7140   6119   6667   1369    608   -447       N
ATOM   3383  N   HIS C 447      81.750   4.612 -51.140  1.00 40.34           N
ANISOU 3383  N   HIS C 447     5662   4638   5029   1359    688   -511       N
ATOM   3384  CA  HIS C 447      83.133   5.077 -51.172  1.00 40.76           C
ANISOU 3384  CA  HIS C 447     5658   4708   5121   1380    717   -476       C
ATOM   3385  C   HIS C 447      83.269   6.513 -51.685  1.00 41.34           C
ANISOU 3385  C   HIS C 447     5714   4816   5179   1365    733   -471       C
ATOM   3386  O   HIS C 447      84.093   7.281 -51.184  1.00 41.77           O
ANISOU 3386  O   HIS C 447     5713   4894   5263   1356    732   -440       O
ATOM   3387  CB  HIS C 447      83.988   4.153 -52.044  1.00 40.96           C
ANISOU 3387  CB  HIS C 447     5690   4708   5167   1435    770   -478       C
ATOM   3388  CG  HIS C 447      84.059   2.727 -51.553  1.00 41.18           C
ANISOU 3388  CG  HIS C 447     5726   4697   5222   1456    763   -476       C
ATOM   3389  ND1 HIS C 447      84.993   2.322 -50.607  1.00 41.66           N
ANISOU 3389  ND1 HIS C 447     5734   4757   5337   1469    753   -434       N
ATOM   3390  CD2 HIS C 447      83.360   1.648 -51.899  1.00 41.02           C
ANISOU 3390  CD2 HIS C 447     5759   4640   5186   1467    768   -509       C
ATOM   3391  CE1 HIS C 447      84.828   1.041 -50.396  1.00 41.77           C
ANISOU 3391  CE1 HIS C 447     5769   4732   5368   1489    753   -440       C
ATOM   3392  NE2 HIS C 447      83.865   0.575 -51.140  1.00 41.39           N
ANISOU 3392  NE2 HIS C 447     5785   4659   5281   1488    762   -486       N
ATOM   3393  N   SER C 448      82.464   6.865 -52.686  1.00 65.05           N
ANISOU 3393  N   SER C 448     8763   7821   8134   1361    748   -501       N
ATOM   3394  CA  SER C 448      82.580   8.158 -53.362  1.00 64.79           C
ANISOU 3394  CA  SER C 448     8717   7817   8084   1353    772   -496       C
ATOM   3395  C   SER C 448      81.714   9.244 -52.731  1.00 64.09           C
ANISOU 3395  C   SER C 448     8624   7749   7979   1303    733   -495       C
ATOM   3396  O   SER C 448      81.719  10.391 -53.185  1.00 63.73           O
ANISOU 3396  O   SER C 448     8566   7726   7923   1292    750   -488       O
ATOM   3397  CB  SER C 448      82.210   8.013 -54.840  1.00 64.16           C
ANISOU 3397  CB  SER C 448     8686   7733   7960   1377    812   -524       C
ATOM   3398  OG  SER C 448      83.267   8.438 -55.681  0.00 64.29           O
ANISOU 3398  OG  SER C 448     8677   7761   7989   1407    864   -508       O
ATOM   3399  N   LEU C 449      80.976   8.886 -51.686  1.00 49.31           N
ANISOU 3399  N   LEU C 449     6760   5869   6106   1273    683   -501       N
ATOM   3400  CA  LEU C 449      80.031   9.813 -51.070  1.00 48.98           C
ANISOU 3400  CA  LEU C 449     6719   5844   6046   1225    647   -505       C
ATOM   3401  C   LEU C 449      80.725  10.932 -50.291  1.00 49.59           C
ANISOU 3401  C   LEU C 449     6737   5947   6159   1200    640   -476       C
ATOM   3402  O   LEU C 449      81.613  10.680 -49.474  1.00 50.06           O
ANISOU 3402  O   LEU C 449     6752   6011   6257   1201    630   -454       O
ATOM   3403  CB  LEU C 449      79.052   9.062 -50.162  1.00 48.22           C
ANISOU 3403  CB  LEU C 449     6650   5732   5940   1201    597   -520       C
ATOM   3404  CG  LEU C 449      77.730   9.781 -49.869  1.00 47.82           C
ANISOU 3404  CG  LEU C 449     6621   5691   5856   1157    564   -536       C
ATOM   3405  CD1 LEU C 449      76.555   8.830 -50.027  1.00 47.40           C
ANISOU 3405  CD1 LEU C 449     6626   5617   5769   1155    543   -566       C
ATOM   3406  CD2 LEU C 449      77.728  10.396 -48.479  1.00 47.94           C
ANISOU 3406  CD2 LEU C 449     6597   5722   5896   1116    526   -519       C
ATOM   3407  N   ASN C 450      80.315  12.168 -50.559  1.00 56.14           N
ANISOU 3407  N   ASN C 450     7562   6794   6974   1175    646   -477       N
ATOM   3408  CA  ASN C 450      80.833  13.321 -49.836  1.00 56.81           C
ANISOU 3408  CA  ASN C 450     7594   6901   7090   1145    641   -456       C
ATOM   3409  C   ASN C 450      79.988  13.608 -48.602  1.00 57.00           C
ANISOU 3409  C   ASN C 450     7616   6931   7112   1095    591   -464       C
ATOM   3410  O   ASN C 450      78.912  14.200 -48.694  1.00 56.82           O
ANISOU 3410  O   ASN C 450     7619   6908   7061   1069    580   -479       O
ATOM   3411  CB  ASN C 450      80.877  14.551 -50.742  1.00 56.69           C
ANISOU 3411  CB  ASN C 450     7573   6900   7067   1144    679   -451       C
ATOM   3412  CG  ASN C 450      81.595  15.722 -50.100  1.00 57.43           C
ANISOU 3412  CG  ASN C 450     7608   7013   7200   1116    683   -430       C
ATOM   3413  OD1 ASN C 450      82.380  15.547 -49.168  1.00 58.37           O
ANISOU 3413  OD1 ASN C 450     7684   7140   7353   1106    667   -416       O
ATOM   3414  ND2 ASN C 450      81.332  16.924 -50.598  1.00 56.96           N
ANISOU 3414  ND2 ASN C 450     7545   6963   7136   1102    706   -427       N
ATOM   3415  N   TRP C 451      80.486  13.186 -47.446  1.00 52.56           N
ANISOU 3415  N   TRP C 451     7020   6373   6576   1082    561   -451       N
ATOM   3416  CA  TRP C 451      79.736  13.297 -46.202  1.00 52.93           C
ANISOU 3416  CA  TRP C 451     7064   6426   6619   1036    512   -459       C
ATOM   3417  C   TRP C 451      79.654  14.731 -45.681  1.00 53.65           C
ANISOU 3417  C   TRP C 451     7123   6539   6722    991    508   -457       C
ATOM   3418  O   TRP C 451      78.874  15.022 -44.776  1.00 53.98           O
ANISOU 3418  O   TRP C 451     7168   6586   6755    949    473   -468       O
ATOM   3419  CB  TRP C 451      80.334  12.373 -45.138  1.00 53.41           C
ANISOU 3419  CB  TRP C 451     7098   6491   6705   1037    482   -442       C
ATOM   3420  CG  TRP C 451      80.194  10.917 -45.471  1.00 52.82           C
ANISOU 3420  CG  TRP C 451     7060   6389   6622   1076    481   -447       C
ATOM   3421  CD1 TRP C 451      81.140  10.107 -46.031  1.00 52.80           C
ANISOU 3421  CD1 TRP C 451     7050   6374   6639   1123    510   -433       C
ATOM   3422  CD2 TRP C 451      79.035  10.099 -45.270  1.00 52.10           C
ANISOU 3422  CD2 TRP C 451     7017   6276   6502   1069    451   -468       C
ATOM   3423  NE1 TRP C 451      80.641   8.835 -46.188  1.00 52.24           N
ANISOU 3423  NE1 TRP C 451     7021   6274   6555   1146    502   -446       N
ATOM   3424  CE2 TRP C 451      79.351   8.805 -45.728  1.00 51.85           C
ANISOU 3424  CE2 TRP C 451     7007   6219   6476   1112    465   -467       C
ATOM   3425  CE3 TRP C 451      77.760  10.338 -44.747  1.00 51.67           C
ANISOU 3425  CE3 TRP C 451     6990   6221   6419   1030    416   -488       C
ATOM   3426  CZ2 TRP C 451      78.439   7.752 -45.678  1.00 51.57           C
ANISOU 3426  CZ2 TRP C 451     7018   6156   6419   1117    445   -486       C
ATOM   3427  CZ3 TRP C 451      76.857   9.291 -44.698  1.00 50.87           C
ANISOU 3427  CZ3 TRP C 451     6936   6096   6297   1035    394   -505       C
ATOM   3428  CH2 TRP C 451      77.201   8.015 -45.160  1.00 50.99           C
ANISOU 3428  CH2 TRP C 451     6970   6084   6318   1077    409   -505       C
ATOM   3429  N   THR C 452      80.455  15.622 -46.255  1.00 54.99           N
ANISOU 3429  N   THR C 452     7262   6720   6912    999    547   -444       N
ATOM   3430  CA  THR C 452      80.440  17.027 -45.860  1.00 55.26           C
ANISOU 3430  CA  THR C 452     7264   6770   6961    957    552   -443       C
ATOM   3431  C   THR C 452      79.091  17.670 -46.182  1.00 54.29           C
ANISOU 3431  C   THR C 452     7182   6638   6809    936    549   -462       C
ATOM   3432  O   THR C 452      78.596  18.511 -45.431  1.00 54.80           O
ANISOU 3432  O   THR C 452     7232   6709   6879    891    533   -471       O
ATOM   3433  CB  THR C 452      81.581  17.816 -46.539  1.00 56.29           C
ANISOU 3433  CB  THR C 452     7355   6911   7122    974    600   -423       C
ATOM   3434  OG1 THR C 452      82.843  17.244 -46.171  1.00 58.14           O
ANISOU 3434  OG1 THR C 452     7548   7157   7387    992    600   -403       O
ATOM   3435  CG2 THR C 452      81.556  19.280 -46.120  1.00 56.36           C
ANISOU 3435  CG2 THR C 452     7330   6932   7150    929    607   -424       C
ATOM   3436  N   LYS C 453      78.492  17.254 -47.294  1.00 53.99           N
ANISOU 3436  N   LYS C 453     7192   6585   6739    968    566   -470       N
ATOM   3437  CA  LYS C 453      77.206  17.797 -47.722  1.00 52.95           C
ANISOU 3437  CA  LYS C 453     7097   6446   6576    952    565   -485       C
ATOM   3438  C   LYS C 453      76.042  17.262 -46.891  1.00 52.90           C
ANISOU 3438  C   LYS C 453     7121   6431   6546    925    517   -505       C
ATOM   3439  O   LYS C 453      75.005  17.915 -46.768  1.00 52.65           O
ANISOU 3439  O   LYS C 453     7106   6398   6501    897    507   -515       O
ATOM   3440  CB  LYS C 453      76.968  17.507 -49.205  1.00 52.14           C
ANISOU 3440  CB  LYS C 453     7034   6336   6442    994    597   -486       C
ATOM   3441  CG  LYS C 453      77.956  18.189 -50.135  0.00 52.35           C
ANISOU 3441  CG  LYS C 453     7034   6372   6486   1020    649   -465       C
ATOM   3442  CD  LYS C 453      77.657  17.865 -51.589  0.00 51.93           C
ANISOU 3442  CD  LYS C 453     7022   6315   6395   1059    680   -468       C
ATOM   3443  CE  LYS C 453      78.613  18.589 -52.522  0.00 52.14           C
ANISOU 3443  CE  LYS C 453     7021   6352   6437   1084    733   -445       C
ATOM   3444  NZ  LYS C 453      78.341  18.266 -53.949  0.00 51.81           N
ANISOU 3444  NZ  LYS C 453     7019   6313   6354   1122    763   -448       N
ATOM   3445  N   VAL C 454      76.214  16.073 -46.322  1.00 45.66           N
ANISOU 3445  N   VAL C 454     6210   5508   5628    934    488   -508       N
ATOM   3446  CA  VAL C 454      75.159  15.451 -45.530  1.00 44.96           C
ANISOU 3446  CA  VAL C 454     6151   5412   5520    910    443   -525       C
ATOM   3447  C   VAL C 454      75.357  15.708 -44.038  1.00 45.60           C
ANISOU 3447  C   VAL C 454     6194   5508   5625    868    409   -522       C
ATOM   3448  O   VAL C 454      74.461  16.214 -43.362  1.00 45.08           O
ANISOU 3448  O   VAL C 454     6135   5445   5550    828    385   -534       O
ATOM   3449  CB  VAL C 454      75.087  13.932 -45.777  1.00 44.91           C
ANISOU 3449  CB  VAL C 454     6179   5388   5497    943    431   -531       C
ATOM   3450  CG1 VAL C 454      73.876  13.341 -45.074  1.00 44.81           C
ANISOU 3450  CG1 VAL C 454     6200   5366   5461    919    387   -549       C
ATOM   3451  CG2 VAL C 454      75.033  13.639 -47.267  1.00 44.45           C
ANISOU 3451  CG2 VAL C 454     6156   5319   5415    985    467   -537       C
ATOM   3452  N   LEU C 455      76.536  15.358 -43.533  1.00 48.20           N
ANISOU 3452  N   LEU C 455     6483   5850   5983    876    408   -504       N
ATOM   3453  CA  LEU C 455      76.851  15.540 -42.120  1.00 48.84           C
ANISOU 3453  CA  LEU C 455     6523   5951   6084    837    375   -498       C
ATOM   3454  C   LEU C 455      77.091  17.012 -41.802  1.00 49.93           C
ANISOU 3454  C   LEU C 455     6622   6107   6241    798    390   -500       C
ATOM   3455  O   LEU C 455      77.950  17.656 -42.405  1.00 50.59           O
ANISOU 3455  O   LEU C 455     6679   6197   6347    812    427   -488       O
ATOM   3456  CB  LEU C 455      78.077  14.709 -41.735  1.00 49.40           C
ANISOU 3456  CB  LEU C 455     6559   6033   6179    860    370   -475       C
ATOM   3457  CG  LEU C 455      78.393  14.601 -40.243  1.00 50.82           C
ANISOU 3457  CG  LEU C 455     6698   6239   6373    823    330   -465       C
ATOM   3458  CD1 LEU C 455      77.268  13.883 -39.515  1.00 50.96           C
ANISOU 3458  CD1 LEU C 455     6751   6247   6364    804    287   -479       C
ATOM   3459  CD2 LEU C 455      79.719  13.891 -40.023  1.00 51.46           C
ANISOU 3459  CD2 LEU C 455     6738   6333   6482    851    332   -435       C
ATOM   3460  N   ARG C 456      76.328  17.537 -40.849  1.00 67.95           N
ANISOU 3460  N   ARG C 456     8904   8397   8519    749    362   -515       N
ATOM   3461  CA  ARG C 456      76.410  18.948 -40.491  1.00 68.51           C
ANISOU 3461  CA  ARG C 456     8941   8480   8608    708    377   -522       C
ATOM   3462  C   ARG C 456      77.604  19.221 -39.580  1.00 70.31           C
ANISOU 3462  C   ARG C 456     9108   8739   8868    684    371   -511       C
ATOM   3463  O   ARG C 456      77.858  18.475 -38.635  1.00 71.11           O
ANISOU 3463  O   ARG C 456     9194   8857   8967    674    335   -505       O
ATOM   3464  CB  ARG C 456      75.114  19.394 -39.811  1.00 67.81           C
ANISOU 3464  CB  ARG C 456     8875   8388   8503    664    353   -545       C
ATOM   3465  CG  ARG C 456      74.814  20.876 -39.945  1.00 68.11           C
ANISOU 3465  CG  ARG C 456     8900   8423   8557    633    382   -555       C
ATOM   3466  CD  ARG C 456      73.419  21.198 -39.435  1.00 67.93           C
ANISOU 3466  CD  ARG C 456     8905   8389   8515    598    362   -577       C
ATOM   3467  NE  ARG C 456      72.954  22.501 -39.902  1.00 68.28           N
ANISOU 3467  NE  ARG C 456     8949   8420   8573    582    397   -583       N
ATOM   3468  CZ  ARG C 456      72.311  22.694 -41.050  1.00 68.18           C
ANISOU 3468  CZ  ARG C 456     8970   8389   8548    610    422   -578       C
ATOM   3469  NH1 ARG C 456      72.057  21.669 -41.851  1.00 67.58           N
ANISOU 3469  NH1 ARG C 456     8931   8304   8441    653    415   -570       N
ATOM   3470  NH2 ARG C 456      71.923  23.914 -41.397  1.00 68.51           N
ANISOU 3470  NH2 ARG C 456     9006   8420   8606    595    455   -578       N
ATOM   3471  N   GLY C 457      78.336  20.292 -39.874  1.00 67.36           N
ANISOU 3471  N   GLY C 457     8698   8373   8523    675    406   -506       N
ATOM   3472  CA  GLY C 457      79.479  20.682 -39.068  1.00 68.74           C
ANISOU 3472  CA  GLY C 457     8811   8579   8728    649    403   -497       C
ATOM   3473  C   GLY C 457      80.802  20.189 -39.623  1.00 69.22           C
ANISOU 3473  C   GLY C 457     8844   8648   8810    692    423   -469       C
ATOM   3474  O   GLY C 457      80.868  19.737 -40.766  1.00 68.16           O
ANISOU 3474  O   GLY C 457     8736   8492   8668    742    449   -459       O
ATOM   3475  N   PRO C 458      81.870  20.282 -38.814  1.00 89.09           N
ANISOU 3475  N   PRO C 458    11303  11198  11351    671    412   -457       N
ATOM   3476  CA  PRO C 458      83.211  19.817 -39.187  1.00 89.45           C
ANISOU 3476  CA  PRO C 458    11312  11255  11420    709    429   -428       C
ATOM   3477  C   PRO C 458      83.247  18.301 -39.346  1.00 88.90           C
ANISOU 3477  C   PRO C 458    11267  11176  11335    756    410   -410       C
ATOM   3478  O   PRO C 458      82.829  17.584 -38.441  1.00 88.94           O
ANISOU 3478  O   PRO C 458    11279  11191  11324    741    367   -411       O
ATOM   3479  CB  PRO C 458      84.074  20.237 -37.990  1.00 90.78           C
ANISOU 3479  CB  PRO C 458    11416  11468  11611    663    408   -423       C
ATOM   3480  CG  PRO C 458      83.287  21.302 -37.294  1.00 91.04           C
ANISOU 3480  CG  PRO C 458    11449  11505  11638    601    399   -455       C
ATOM   3481  CD  PRO C 458      81.858  20.915 -37.485  1.00 90.11           C
ANISOU 3481  CD  PRO C 458    11395  11356  11485    607    385   -472       C
ATOM   3482  N   THR C 459      83.749  17.824 -40.480  1.00 77.43           N
ANISOU 3482  N   THR C 459     9827   9705   9889    812    443   -394       N
ATOM   3483  CA  THR C 459      83.737  16.397 -40.791  1.00 77.28           C
ANISOU 3483  CA  THR C 459     9837   9669   9859    860    434   -381       C
ATOM   3484  C   THR C 459      84.811  15.609 -40.033  1.00 78.75           C
ANISOU 3484  C   THR C 459     9974   9880  10068    870    414   -351       C
ATOM   3485  O   THR C 459      84.605  14.444 -39.689  1.00 79.09           O
ANISOU 3485  O   THR C 459    10034   9915  10101    889    388   -341       O
ATOM   3486  CB  THR C 459      83.890  16.163 -42.314  1.00 75.62           C
ANISOU 3486  CB  THR C 459     9657   9429   9645    915    482   -378       C
ATOM   3487  OG1 THR C 459      82.824  16.821 -43.009  1.00 74.77           O
ANISOU 3487  OG1 THR C 459     9595   9302   9513    907    497   -403       O
ATOM   3488  CG2 THR C 459      83.857  14.679 -42.648  1.00 74.63           C
ANISOU 3488  CG2 THR C 459     9564   9282   9510    963    476   -370       C
ATOM   3489  N   GLU C 460      85.939  16.262 -39.762  1.00 68.88           N
ANISOU 3489  N   GLU C 460     8663   8660   8849    856    426   -334       N
ATOM   3490  CA  GLU C 460      87.117  15.620 -39.166  1.00 69.43           C
ANISOU 3490  CA  GLU C 460     8678   8758   8944    869    412   -299       C
ATOM   3491  C   GLU C 460      86.846  14.666 -38.004  1.00 69.65           C
ANISOU 3491  C   GLU C 460     8702   8802   8961    856    360   -287       C
ATOM   3492  O   GLU C 460      86.206  15.033 -37.018  1.00 69.85           O
ANISOU 3492  O   GLU C 460     8726   8847   8968    804    324   -303       O
ATOM   3493  CB  GLU C 460      88.121  16.675 -38.707  1.00 70.30           C
ANISOU 3493  CB  GLU C 460     8719   8907   9083    833    420   -290       C
ATOM   3494  CG  GLU C 460      88.837  17.379 -39.831  0.00 69.89           C
ANISOU 3494  CG  GLU C 460     8655   8845   9056    858    475   -286       C
ATOM   3495  CD  GLU C 460      89.818  18.409 -39.321  0.00 70.78           C
ANISOU 3495  CD  GLU C 460     8697   8996   9199    818    481   -279       C
ATOM   3496  OE1 GLU C 460      90.737  18.036 -38.561  0.00 71.68           O
ANISOU 3496  OE1 GLU C 460     8757   9146   9331    812    460   -253       O
ATOM   3497  OE2 GLU C 460      89.659  19.592 -39.675  0.00 70.55           O
ANISOU 3497  OE2 GLU C 460     8667   8961   9176    792    509   -299       O
ATOM   3498  N   GLU C 461      87.346  13.440 -38.145  1.00 84.23           N
ANISOU 3498  N   GLU C 461    10546  10638  10818    904    359   -258       N
ATOM   3499  CA  GLU C 461      87.279  12.414 -37.102  1.00 84.73           C
ANISOU 3499  CA  GLU C 461    10599  10717  10878    901    314   -236       C
ATOM   3500  C   GLU C 461      85.867  11.995 -36.689  1.00 84.25           C
ANISOU 3500  C   GLU C 461    10594  10637  10781    882    281   -260       C
ATOM   3501  O   GLU C 461      85.694  11.279 -35.704  1.00 85.10           O
ANISOU 3501  O   GLU C 461    10692  10760  10881    871    240   -244       O
ATOM   3502  CB  GLU C 461      88.095  12.826 -35.870  1.00 86.10           C
ANISOU 3502  CB  GLU C 461    10699  10950  11065    858    283   -214       C
ATOM   3503  CG  GLU C 461      89.548  12.370 -35.900  0.00 86.68           C
ANISOU 3503  CG  GLU C 461    10712  11045  11177    893    295   -168       C
ATOM   3504  CD  GLU C 461      90.345  13.011 -37.018  0.00 86.39           C
ANISOU 3504  CD  GLU C 461    10661  10997  11166    919    349   -168       C
ATOM   3505  OE1 GLU C 461      90.760  14.179 -36.860  0.00 86.88           O
ANISOU 3505  OE1 GLU C 461    10686  11087  11237    880    357   -178       O
ATOM   3506  OE2 GLU C 461      90.558  12.348 -38.055  0.00 85.69           O
ANISOU 3506  OE2 GLU C 461    10598  10870  11088    978    385   -159       O
ATOM   3507  N   ARG C 462      84.862  12.432 -37.441  1.00 62.41           N
ANISOU 3507  N   ARG C 462     7884   7838   7991    880    298   -297       N
ATOM   3508  CA  ARG C 462      83.486  12.036 -37.162  1.00 61.40           C
ANISOU 3508  CA  ARG C 462     7811   7689   7829    864    271   -321       C
ATOM   3509  C   ARG C 462      83.039  10.911 -38.090  1.00 60.21           C
ANISOU 3509  C   ARG C 462     7716   7490   7670    918    287   -323       C
ATOM   3510  O   ARG C 462      81.907  10.435 -38.009  1.00 59.48           O
ANISOU 3510  O   ARG C 462     7673   7375   7550    912    268   -343       O
ATOM   3511  CB  ARG C 462      82.542  13.234 -37.267  1.00 60.28           C
ANISOU 3511  CB  ARG C 462     7694   7544   7665    821    274   -359       C
ATOM   3512  CG  ARG C 462      82.670  14.212 -36.111  1.00 60.86           C
ANISOU 3512  CG  ARG C 462     7723   7662   7741    758    249   -365       C
ATOM   3513  CD  ARG C 462      81.893  15.487 -36.375  1.00 60.19           C
ANISOU 3513  CD  ARG C 462     7657   7568   7643    721    265   -401       C
ATOM   3514  NE  ARG C 462      80.454  15.263 -36.467  1.00 59.12           N
ANISOU 3514  NE  ARG C 462     7582   7403   7475    714    250   -426       N
ATOM   3515  CZ  ARG C 462      79.606  16.111 -37.040  1.00 58.27           C
ANISOU 3515  CZ  ARG C 462     7508   7276   7356    700    270   -453       C
ATOM   3516  NH1 ARG C 462      80.054  17.235 -37.582  1.00 58.26           N
ANISOU 3516  NH1 ARG C 462     7485   7277   7374    693    307   -458       N
ATOM   3517  NH2 ARG C 462      78.310  15.833 -37.077  1.00 57.63           N
ANISOU 3517  NH2 ARG C 462     7479   7172   7245    695    254   -474       N
ATOM   3518  N   LEU C 463      83.942  10.490 -38.970  1.00 50.26           N
ANISOU 3518  N   LEU C 463     6447   6216   6434    969    325   -305       N
ATOM   3519  CA  LEU C 463      83.680   9.370 -39.863  1.00 48.66           C
ANISOU 3519  CA  LEU C 463     6292   5969   6227   1021    346   -309       C
ATOM   3520  C   LEU C 463      84.506   8.157 -39.457  1.00 49.01           C
ANISOU 3520  C   LEU C 463     6309   6012   6301   1057    339   -270       C
ATOM   3521  O   LEU C 463      85.714   8.258 -39.248  1.00 50.05           O
ANISOU 3521  O   LEU C 463     6383   6169   6465   1068    349   -238       O
ATOM   3522  CB  LEU C 463      83.987   9.750 -41.313  1.00 46.87           C
ANISOU 3522  CB  LEU C 463     6084   5722   6002   1056    400   -321       C
ATOM   3523  CG  LEU C 463      83.114  10.838 -41.940  1.00 46.19           C
ANISOU 3523  CG  LEU C 463     6032   5630   5887   1031    413   -355       C
ATOM   3524  CD1 LEU C 463      83.511  11.070 -43.391  1.00 45.82           C
ANISOU 3524  CD1 LEU C 463     6001   5566   5842   1071    468   -361       C
ATOM   3525  CD2 LEU C 463      81.643  10.473 -41.836  1.00 45.33           C
ANISOU 3525  CD2 LEU C 463     5982   5500   5741   1014    387   -384       C
ATOM   3526  N   ASP C 464      83.846   7.012 -39.344  1.00 59.29           N
ANISOU 3526  N   ASP C 464     7650   7284   7594   1074    324   -272       N
ATOM   3527  CA  ASP C 464      84.522   5.768 -39.008  1.00 60.18           C
ANISOU 3527  CA  ASP C 464     7741   7386   7737   1112    322   -235       C
ATOM   3528  C   ASP C 464      84.102   4.698 -40.008  1.00 59.05           C
ANISOU 3528  C   ASP C 464     7656   7187   7592   1160    351   -252       C
ATOM   3529  O   ASP C 464      83.430   3.729 -39.655  1.00 58.40           O
ANISOU 3529  O   ASP C 464     7605   7081   7505   1165    331   -253       O
ATOM   3530  CB  ASP C 464      84.167   5.337 -37.585  1.00 61.54           C
ANISOU 3530  CB  ASP C 464     7895   7581   7905   1080    267   -215       C
ATOM   3531  CG  ASP C 464      85.319   4.653 -36.877  1.00 62.77           C
ANISOU 3531  CG  ASP C 464     7991   7760   8100   1102    258   -160       C
ATOM   3532  OD1 ASP C 464      85.645   3.502 -37.237  1.00 63.00           O
ANISOU 3532  OD1 ASP C 464     8029   7754   8154   1152    278   -139       O
ATOM   3533  OD2 ASP C 464      85.894   5.265 -35.953  1.00 63.61           O
ANISOU 3533  OD2 ASP C 464     8039   7919   8212   1068    232   -137       O
ATOM   3534  N   ILE C 465      84.503   4.889 -41.261  1.00 43.62           N
ANISOU 3534  N   ILE C 465     5716   5214   5642   1194    401   -266       N
ATOM   3535  CA  ILE C 465      84.054   4.037 -42.355  1.00 42.50           C
ANISOU 3535  CA  ILE C 465     5634   5023   5492   1234    434   -291       C
ATOM   3536  C   ILE C 465      85.199   3.237 -42.968  1.00 43.28           C
ANISOU 3536  C   ILE C 465     5713   5100   5631   1292    478   -267       C
ATOM   3537  O   ILE C 465      86.029   3.780 -43.699  1.00 43.28           O
ANISOU 3537  O   ILE C 465     5691   5110   5643   1312    516   -262       O
ATOM   3538  CB  ILE C 465      83.381   4.874 -43.458  1.00 41.26           C
ANISOU 3538  CB  ILE C 465     5522   4859   5298   1225    459   -334       C
ATOM   3539  CG1 ILE C 465      82.261   5.730 -42.863  1.00 41.17           C
ANISOU 3539  CG1 ILE C 465     5526   4867   5250   1168    419   -356       C
ATOM   3540  CG2 ILE C 465      82.854   3.974 -44.567  1.00 40.60           C
ANISOU 3540  CG2 ILE C 465     5500   4728   5198   1262    490   -364       C
ATOM   3541  CD1 ILE C 465      81.681   6.737 -43.827  1.00 40.42           C
ANISOU 3541  CD1 ILE C 465     5462   4772   5122   1156    441   -389       C
ATOM   3542  N   LYS C 466      85.235   1.943 -42.666  1.00 53.83           N
ANISOU 3542  N   LYS C 466     7057   6406   6989   1320    475   -250       N
ATOM   3543  CA  LYS C 466      86.250   1.051 -43.215  1.00 53.57           C
ANISOU 3543  CA  LYS C 466     7008   6346   6999   1378    519   -227       C
ATOM   3544  C   LYS C 466      85.814  -0.406 -43.107  1.00 53.68           C
ANISOU 3544  C   LYS C 466     7056   6311   7027   1405    519   -228       C
ATOM   3545  O   LYS C 466      84.748  -0.704 -42.568  1.00 53.54           O
ANISOU 3545  O   LYS C 466     7073   6285   6986   1377    482   -243       O
ATOM   3546  CB  LYS C 466      87.591   1.252 -42.503  1.00 54.32           C
ANISOU 3546  CB  LYS C 466     7022   6479   7137   1386    514   -172       C
ATOM   3547  CG  LYS C 466      87.556   0.969 -41.010  1.00 55.04           C
ANISOU 3547  CG  LYS C 466     7075   6598   7240   1359    459   -134       C
ATOM   3548  CD  LYS C 466      88.930   1.157 -40.388  1.00 56.15           C
ANISOU 3548  CD  LYS C 466     7132   6780   7421   1368    457    -78       C
ATOM   3549  CE  LYS C 466      88.908   0.878 -38.895  0.00 56.92           C
ANISOU 3549  CE  LYS C 466     7189   6912   7526   1339    401    -37       C
ATOM   3550  NZ  LYS C 466      90.259   1.029 -38.286  0.00 57.69           N
ANISOU 3550  NZ  LYS C 466     7203   7055   7661   1347    396     20       N
ATOM   3551  N   HIS C 467      86.647  -1.303 -43.630  1.00 67.52           N
ANISOU 3551  N   HIS C 467     8801   8032   8821   1459    563   -210       N
ATOM   3552  CA  HIS C 467      86.404  -2.744 -43.575  1.00 67.33           C
ANISOU 3552  CA  HIS C 467     8805   7957   8822   1491    573   -207       C
ATOM   3553  C   HIS C 467      85.108  -3.174 -44.263  1.00 65.87           C
ANISOU 3553  C   HIS C 467     8700   7729   8597   1483    579   -266       C
ATOM   3554  O   HIS C 467      84.475  -4.151 -43.863  1.00 65.69           O
ANISOU 3554  O   HIS C 467     8705   7672   8582   1485    564   -268       O
ATOM   3555  CB  HIS C 467      86.447  -3.253 -42.130  1.00 68.72           C
ANISOU 3555  CB  HIS C 467     8941   8147   9022   1477    525   -158       C
ATOM   3556  CG  HIS C 467      87.801  -3.110 -41.488  1.00 70.18           C
ANISOU 3556  CG  HIS C 467     9044   8369   9251   1493    523    -95       C
ATOM   3557  ND1 HIS C 467      87.976  -2.441 -40.284  1.00 71.27           N
ANISOU 3557  ND1 HIS C 467     9129   8566   9383   1452    471    -61       N
ATOM   3558  CD2 HIS C 467      89.007  -3.538 -41.871  1.00 70.39           C
ANISOU 3558  CD2 HIS C 467     9033   8385   9327   1543    565    -62       C
ATOM   3559  CE1 HIS C 467      89.254  -2.478 -39.974  1.00 71.70           C
ANISOU 3559  CE1 HIS C 467     9116   8646   9481   1476    481     -8       C
ATOM   3560  NE2 HIS C 467      89.916  -3.127 -40.897  1.00 71.11           N
ANISOU 3560  NE2 HIS C 467     9046   8531   9442   1532    537     -5       N
ATOM   3561  N   ASN C 468      84.721  -2.436 -45.298  1.00 57.45           N
ANISOU 3561  N   ASN C 468     7670   6667   7491   1474    600   -311       N
ATOM   3562  CA  ASN C 468      83.612  -2.836 -46.154  1.00 57.11           C
ANISOU 3562  CA  ASN C 468     7703   6588   7410   1471    614   -368       C
ATOM   3563  C   ASN C 468      84.162  -3.526 -47.394  1.00 57.10           C
ANISOU 3563  C   ASN C 468     7724   6546   7425   1523    680   -388       C
ATOM   3564  O   ASN C 468      85.300  -3.996 -47.389  1.00 57.56           O
ANISOU 3564  O   ASN C 468     7743   6594   7534   1563    711   -354       O
ATOM   3565  CB  ASN C 468      82.772  -1.623 -46.554  1.00 56.75           C
ANISOU 3565  CB  ASN C 468     7683   6573   7305   1430    597   -404       C
ATOM   3566  CG  ASN C 468      82.123  -0.944 -45.365  1.00 57.42           C
ANISOU 3566  CG  ASN C 468     7751   6693   7372   1377    535   -391       C
ATOM   3567  OD1 ASN C 468      81.012  -1.294 -44.967  1.00 57.40           O
ANISOU 3567  OD1 ASN C 468     7786   6677   7347   1351    503   -411       O
ATOM   3568  ND2 ASN C 468      82.813   0.034 -44.791  1.00 58.13           N
ANISOU 3568  ND2 ASN C 468     7785   6830   7473   1359    520   -360       N
ATOM   3569  N   ARG C 469      83.366  -3.593 -48.455  1.00 58.18           N
ANISOU 3569  N   ARG C 469     7924   6663   7520   1520    702   -444       N
ATOM   3570  CA  ARG C 469      83.868  -4.123 -49.716  1.00 57.73           C
ANISOU 3570  CA  ARG C 469     7891   6574   7471   1564    768   -470       C
ATOM   3571  C   ARG C 469      84.829  -3.109 -50.322  1.00 57.27           C
ANISOU 3571  C   ARG C 469     7796   6551   7411   1577    798   -456       C
ATOM   3572  O   ARG C 469      84.473  -1.944 -50.491  1.00 56.81           O
ANISOU 3572  O   ARG C 469     7738   6533   7313   1546    780   -466       O
ATOM   3573  CB  ARG C 469      82.726  -4.435 -50.687  1.00 57.59           C
ANISOU 3573  CB  ARG C 469     7948   6531   7401   1554    781   -535       C
ATOM   3574  CG  ARG C 469      83.174  -5.206 -51.925  1.00 57.93           C
ANISOU 3574  CG  ARG C 469     8022   6536   7454   1598    849   -567       C
ATOM   3575  CD  ARG C 469      82.136  -6.233 -52.354  1.00 58.02           C
ANISOU 3575  CD  ARG C 469     8099   6501   7443   1593    856   -620       C
ATOM   3576  NE  ARG C 469      82.682  -7.213 -53.290  1.00 58.22           N
ANISOU 3576  NE  ARG C 469     8147   6480   7493   1638    923   -645       N
ATOM   3577  CZ  ARG C 469      82.506  -7.177 -54.607  1.00 58.02           C
ANISOU 3577  CZ  ARG C 469     8165   6453   7428   1646    966   -697       C
ATOM   3578  NH1 ARG C 469      81.790  -6.207 -55.159  1.00 57.59           N
ANISOU 3578  NH1 ARG C 469     8135   6441   7307   1614    948   -724       N
ATOM   3579  NH2 ARG C 469      83.043  -8.117 -55.374  1.00 58.38           N
ANISOU 3579  NH2 ARG C 469     8228   6454   7499   1687   1028   -720       N
ATOM   3580  N   PRO C 470      86.057  -3.551 -50.637  1.00 58.52           N
ANISOU 3580  N   PRO C 470     7922   6696   7619   1625    845   -431       N
ATOM   3581  CA  PRO C 470      87.111  -2.680 -51.172  1.00 59.01           C
ANISOU 3581  CA  PRO C 470     7943   6789   7688   1642    877   -411       C
ATOM   3582  C   PRO C 470      86.692  -1.965 -52.452  1.00 58.66           C
ANISOU 3582  C   PRO C 470     7940   6758   7588   1635    906   -457       C
ATOM   3583  O   PRO C 470      85.976  -2.539 -53.272  1.00 58.21           O
ANISOU 3583  O   PRO C 470     7945   6673   7501   1640    928   -506       O
ATOM   3584  CB  PRO C 470      88.263  -3.653 -51.456  1.00 59.63           C
ANISOU 3584  CB  PRO C 470     7997   6833   7826   1699    931   -389       C
ATOM   3585  CG  PRO C 470      87.631  -5.007 -51.507  1.00 59.42           C
ANISOU 3585  CG  PRO C 470     8019   6750   7810   1713    940   -416       C
ATOM   3586  CD  PRO C 470      86.507  -4.948 -50.528  1.00 58.78           C
ANISOU 3586  CD  PRO C 470     7954   6676   7703   1667    873   -418       C
ATOM   3587  N   ARG C 471      87.146  -0.725 -52.609  1.00 65.03           N
ANISOU 3587  N   ARG C 471     8713   7610   8384   1622    907   -441       N
ATOM   3588  CA  ARG C 471      86.767   0.116 -53.739  1.00 64.83           C
ANISOU 3588  CA  ARG C 471     8721   7606   8307   1613    931   -475       C
ATOM   3589  C   ARG C 471      87.188  -0.488 -55.078  1.00 64.99           C
ANISOU 3589  C   ARG C 471     8772   7600   8323   1657    999   -504       C
ATOM   3590  O   ARG C 471      86.556  -0.242 -56.105  1.00 64.81           O
ANISOU 3590  O   ARG C 471     8797   7582   8247   1651   1018   -546       O
ATOM   3591  CB  ARG C 471      87.377   1.511 -53.574  1.00 65.27           C
ANISOU 3591  CB  ARG C 471     8724   7710   8364   1596    924   -444       C
ATOM   3592  CG  ARG C 471      86.733   2.593 -54.424  1.00 65.41           C
ANISOU 3592  CG  ARG C 471     8771   7755   8325   1573    930   -471       C
ATOM   3593  CD  ARG C 471      87.250   3.964 -54.021  1.00 66.44           C
ANISOU 3593  CD  ARG C 471     8847   7930   8466   1549    917   -437       C
ATOM   3594  NE  ARG C 471      86.485   5.048 -54.629  1.00 66.99           N
ANISOU 3594  NE  ARG C 471     8943   8026   8485   1521    914   -458       N
ATOM   3595  CZ  ARG C 471      86.597   6.325 -54.279  1.00 67.88           C
ANISOU 3595  CZ  ARG C 471     9020   8174   8599   1491    898   -438       C
ATOM   3596  NH1 ARG C 471      87.444   6.679 -53.321  1.00 68.65           N
ANISOU 3596  NH1 ARG C 471     9054   8287   8741   1483    881   -399       N
ATOM   3597  NH2 ARG C 471      85.862   7.249 -54.883  1.00 67.75           N
ANISOU 3597  NH2 ARG C 471     9028   8177   8538   1469    899   -455       N
ATOM   3598  N   ARG C 472      88.253  -1.283 -55.059  1.00 55.78           N
ANISOU 3598  N   ARG C 472     7576   6407   7212   1702   1036   -481       N
ATOM   3599  CA  ARG C 472      88.755  -1.923 -56.270  1.00 55.92           C
ANISOU 3599  CA  ARG C 472     7619   6397   7233   1746   1105   -507       C
ATOM   3600  C   ARG C 472      87.796  -2.992 -56.788  1.00 55.82           C
ANISOU 3600  C   ARG C 472     7677   6341   7192   1748   1117   -563       C
ATOM   3601  O   ARG C 472      87.614  -3.140 -57.997  1.00 55.41           O
ANISOU 3601  O   ARG C 472     7669   6282   7104   1761   1161   -607       O
ATOM   3602  CB  ARG C 472      90.138  -2.531 -56.023  1.00 56.43           C
ANISOU 3602  CB  ARG C 472     7630   6441   7370   1794   1142   -464       C
ATOM   3603  CG  ARG C 472      91.220  -1.510 -55.701  0.00 56.75           C
ANISOU 3603  CG  ARG C 472     7600   6525   7438   1796   1141   -413       C
ATOM   3604  CD  ARG C 472      92.547  -2.188 -55.399  0.00 57.17           C
ANISOU 3604  CD  ARG C 472     7598   6559   7565   1843   1174   -368       C
ATOM   3605  NE  ARG C 472      93.607  -1.221 -55.126  0.00 57.48           N
ANISOU 3605  NE  ARG C 472     7568   6641   7632   1844   1175   -319       N
ATOM   3606  CZ  ARG C 472      94.844  -1.550 -54.768  0.00 57.88           C
ANISOU 3606  CZ  ARG C 472     7557   6688   7746   1879   1196   -270       C
ATOM   3607  NH1 ARG C 472      95.180  -2.826 -54.635  0.00 58.00           N
ANISOU 3607  NH1 ARG C 472     7573   6658   7808   1918   1221   -261       N
ATOM   3608  NH2 ARG C 472      95.744  -0.604 -54.540  0.00 58.15           N
ANISOU 3608  NH2 ARG C 472     7529   6766   7801   1875   1195   -230       N
ATOM   3609  N   ASP C 473      87.184  -3.734 -55.870  1.00 69.13           N
ANISOU 3609  N   ASP C 473     9372   7999   8893   1733   1077   -561       N
ATOM   3610  CA  ASP C 473      86.264  -4.805 -56.243  1.00 69.08           C
ANISOU 3610  CA  ASP C 473     9431   7948   8868   1732   1085   -613       C
ATOM   3611  C   ASP C 473      84.927  -4.264 -56.743  1.00 68.89           C
ANISOU 3611  C   ASP C 473     9462   7947   8766   1689   1058   -661       C
ATOM   3612  O   ASP C 473      84.277  -4.880 -57.590  1.00 68.99           O
ANISOU 3612  O   ASP C 473     9532   7936   8744   1690   1082   -715       O
ATOM   3613  CB  ASP C 473      86.039  -5.761 -55.070  1.00 69.51           C
ANISOU 3613  CB  ASP C 473     9477   7967   8968   1730   1051   -591       C
ATOM   3614  CG  ASP C 473      87.274  -6.579 -54.738  1.00 70.51           C
ANISOU 3614  CG  ASP C 473     9558   8060   9171   1779   1087   -549       C
ATOM   3615  OD1 ASP C 473      88.393  -6.027 -54.802  1.00 70.87           O
ANISOU 3615  OD1 ASP C 473     9552   8131   9245   1802   1109   -511       O
ATOM   3616  OD2 ASP C 473      87.124  -7.777 -54.415  1.00 71.10           O
ANISOU 3616  OD2 ASP C 473     9649   8084   9283   1796   1095   -553       O
ATOM   3617  N   CYS C 474      84.523  -3.113 -56.214  1.00 68.41           N
ANISOU 3617  N   CYS C 474     9382   7933   8680   1651   1009   -640       N
ATOM   3618  CA  CYS C 474      83.251  -2.502 -56.588  1.00 68.01           C
ANISOU 3618  CA  CYS C 474     9375   7906   8558   1609    979   -677       C
ATOM   3619  C   CYS C 474      83.294  -1.960 -58.014  1.00 68.18           C
ANISOU 3619  C   CYS C 474     9422   7951   8531   1619   1024   -708       C
ATOM   3620  O   CYS C 474      82.385  -2.200 -58.809  1.00 67.83           O
ANISOU 3620  O   CYS C 474     9434   7905   8434   1606   1031   -758       O
ATOM   3621  CB  CYS C 474      82.898  -1.370 -55.623  1.00 67.91           C
ANISOU 3621  CB  CYS C 474     9330   7935   8538   1568    920   -644       C
ATOM   3622  SG  CYS C 474      82.987  -1.813 -53.880  1.00 69.17           S
ANISOU 3622  SG  CYS C 474     9448   8080   8752   1555    866   -600       S
ATOM   3623  N   VAL C 475      84.361  -1.231 -58.330  1.00 58.96           N
ANISOU 3623  N   VAL C 475     8212   6810   7381   1640   1055   -677       N
ATOM   3624  CA  VAL C 475      84.535  -0.635 -59.653  1.00 58.74           C
ANISOU 3624  CA  VAL C 475     8200   6808   7309   1651   1100   -698       C
ATOM   3625  C   VAL C 475      84.690  -1.706 -60.730  1.00 58.68           C
ANISOU 3625  C   VAL C 475     8236   6767   7292   1685   1159   -743       C
ATOM   3626  O   VAL C 475      84.106  -1.604 -61.809  1.00 58.06           O
ANISOU 3626  O   VAL C 475     8203   6704   7154   1678   1179   -786       O
ATOM   3627  CB  VAL C 475      85.756   0.309 -59.684  1.00 58.26           C
ANISOU 3627  CB  VAL C 475     8080   6778   7279   1670   1123   -651       C
ATOM   3628  CG1 VAL C 475      85.985   0.848 -61.086  1.00 57.13           C
ANISOU 3628  CG1 VAL C 475     7954   6661   7094   1685   1174   -670       C
ATOM   3629  CG2 VAL C 475      85.563   1.450 -58.696  1.00 58.29           C
ANISOU 3629  CG2 VAL C 475     8043   6817   7288   1632   1068   -612       C
ATOM   3630  N   ALA C 476      85.472  -2.737 -60.424  1.00 66.69           N
ANISOU 3630  N   ALA C 476     9234   7737   8366   1720   1186   -733       N
ATOM   3631  CA  ALA C 476      85.705  -3.834 -61.358  1.00 67.08           C
ANISOU 3631  CA  ALA C 476     9322   7749   8418   1754   1247   -777       C
ATOM   3632  C   ALA C 476      84.420  -4.600 -61.664  1.00 67.06           C
ANISOU 3632  C   ALA C 476     9387   7722   8370   1729   1234   -837       C
ATOM   3633  O   ALA C 476      84.295  -5.223 -62.718  1.00 67.15           O
ANISOU 3633  O   ALA C 476     9443   7718   8353   1743   1281   -888       O
ATOM   3634  CB  ALA C 476      86.769  -4.775 -60.813  1.00 67.48           C
ANISOU 3634  CB  ALA C 476     9336   7751   8550   1796   1276   -747       C
ATOM   3635  N   GLU C 477      83.467  -4.549 -60.739  1.00 75.05           N
ANISOU 3635  N   GLU C 477    10407   8735   9375   1691   1170   -832       N
ATOM   3636  CA  GLU C 477      82.198  -5.245 -60.912  1.00 74.56           C
ANISOU 3636  CA  GLU C 477    10405   8652   9272   1664   1151   -886       C
ATOM   3637  C   GLU C 477      81.148  -4.314 -61.516  1.00 73.88           C
ANISOU 3637  C   GLU C 477    10351   8617   9104   1624   1124   -912       C
ATOM   3638  O   GLU C 477      80.024  -4.729 -61.801  1.00 73.52           O
ANISOU 3638  O   GLU C 477    10355   8565   9013   1597   1107   -959       O
ATOM   3639  CB  GLU C 477      81.718  -5.815 -59.575  1.00 74.69           C
ANISOU 3639  CB  GLU C 477    10414   8637   9328   1646   1099   -867       C
ATOM   3640  CG  GLU C 477      80.852  -7.057 -59.702  1.00 74.97           C
ANISOU 3640  CG  GLU C 477    10505   8624   9356   1637   1101   -920       C
ATOM   3641  CD  GLU C 477      80.871  -7.909 -58.447  1.00 75.47           C
ANISOU 3641  CD  GLU C 477    10550   8642   9484   1641   1074   -892       C
ATOM   3642  OE1 GLU C 477      81.581  -8.936 -58.438  1.00 75.84           O
ANISOU 3642  OE1 GLU C 477    10591   8638   9587   1678   1117   -890       O
ATOM   3643  OE2 GLU C 477      80.179  -7.552 -57.471  1.00 75.52           O
ANISOU 3643  OE2 GLU C 477    10547   8663   9485   1606   1012   -870       O
ATOM   3644  N   GLY C 478      81.526  -3.054 -61.711  1.00 49.30           N
ANISOU 3644  N   GLY C 478     7204   5553   5973   1621   1121   -879       N
ATOM   3645  CA  GLY C 478      80.659  -2.082 -62.351  1.00 48.91           C
ANISOU 3645  CA  GLY C 478     7179   5555   5851   1590   1102   -895       C
ATOM   3646  C   GLY C 478      79.750  -1.336 -61.392  1.00 49.03           C
ANISOU 3646  C   GLY C 478     7183   5592   5853   1546   1032   -873       C
ATOM   3647  O   GLY C 478      78.910  -0.541 -61.814  1.00 48.91           O
ANISOU 3647  O   GLY C 478     7187   5617   5781   1517   1012   -883       O
ATOM   3648  N   LYS C 479      79.918  -1.588 -60.098  1.00 61.87           N
ANISOU 3648  N   LYS C 479     8778   7194   7535   1541    997   -841       N
ATOM   3649  CA  LYS C 479      79.077  -0.960 -59.085  1.00 61.41           C
ANISOU 3649  CA  LYS C 479     8710   7154   7470   1499    931   -821       C
ATOM   3650  C   LYS C 479      79.535   0.460 -58.765  1.00 61.83           C
ANISOU 3650  C   LYS C 479     8713   7250   7529   1490    917   -774       C
ATOM   3651  O   LYS C 479      80.088   0.722 -57.696  1.00 62.32           O
ANISOU 3651  O   LYS C 479     8727   7311   7639   1487    894   -732       O
ATOM   3652  CB  LYS C 479      79.039  -1.815 -57.818  1.00 61.17           C
ANISOU 3652  CB  LYS C 479     8667   7082   7491   1496    898   -805       C
ATOM   3653  CG  LYS C 479      78.405  -3.181 -58.028  1.00 61.49           C
ANISOU 3653  CG  LYS C 479     8759   7077   7527   1498    906   -852       C
ATOM   3654  CD  LYS C 479      78.520  -4.048 -56.788  1.00 62.55           C
ANISOU 3654  CD  LYS C 479     8876   7170   7721   1501    881   -830       C
ATOM   3655  CE  LYS C 479      77.808  -5.377 -56.981  1.00 63.28           C
ANISOU 3655  CE  LYS C 479     9020   7213   7810   1500    888   -877       C
ATOM   3656  NZ  LYS C 479      76.346  -5.197 -57.198  1.00 63.40           N
ANISOU 3656  NZ  LYS C 479     9083   7245   7763   1456    852   -917       N
ATOM   3657  N   VAL C 480      79.297   1.372 -59.704  1.00 40.34           N
ANISOU 3657  N   VAL C 480     6002   4568   4758   1483    933   -781       N
ATOM   3658  CA  VAL C 480      79.669   2.771 -59.537  1.00 40.09           C
ANISOU 3658  CA  VAL C 480     5926   4576   4729   1472    925   -740       C
ATOM   3659  C   VAL C 480      78.440   3.669 -59.648  1.00 39.72           C
ANISOU 3659  C   VAL C 480     5901   4564   4629   1432    889   -748       C
ATOM   3660  O   VAL C 480      77.327   3.188 -59.855  1.00 39.51           O
ANISOU 3660  O   VAL C 480     5920   4531   4561   1412    869   -784       O
ATOM   3661  CB  VAL C 480      80.715   3.205 -60.582  1.00 40.37           C
ANISOU 3661  CB  VAL C 480     5944   4631   4763   1507    985   -730       C
ATOM   3662  CG1 VAL C 480      81.994   2.397 -60.419  1.00 40.72           C
ANISOU 3662  CG1 VAL C 480     5962   4643   4867   1548   1022   -717       C
ATOM   3663  CG2 VAL C 480      80.156   3.051 -61.988  1.00 40.37           C
ANISOU 3663  CG2 VAL C 480     5996   4647   4697   1512   1017   -773       C
ATOM   3664  N   CYS C 481      78.647   4.975 -59.514  1.00 68.59           N
ANISOU 3664  N   CYS C 481     9520   8253   8286   1419    883   -713       N
ATOM   3665  CA  CYS C 481      77.541   5.927 -59.538  1.00 68.58           C
ANISOU 3665  CA  CYS C 481     9531   8283   8244   1382    851   -713       C
ATOM   3666  C   CYS C 481      77.073   6.255 -60.954  1.00 69.24           C
ANISOU 3666  C   CYS C 481     9649   8397   8263   1387    880   -734       C
ATOM   3667  O   CYS C 481      77.850   6.199 -61.908  1.00 70.03           O
ANISOU 3667  O   CYS C 481     9747   8504   8356   1419    931   -736       O
ATOM   3668  CB  CYS C 481      77.915   7.208 -58.789  1.00 68.79           C
ANISOU 3668  CB  CYS C 481     9505   8331   8302   1364    834   -668       C
ATOM   3669  SG  CYS C 481      78.099   6.992 -57.002  1.00 74.66           S
ANISOU 3669  SG  CYS C 481    10211   9052   9105   1343    785   -646       S
ATOM   3670  N   ASP C 482      75.794   6.597 -61.072  1.00 59.52           N
ANISOU 3670  N   ASP C 482     8446   7184   6984   1355    848   -748       N
ATOM   3671  CA  ASP C 482      75.182   6.928 -62.354  1.00 59.37           C
ANISOU 3671  CA  ASP C 482     8459   7200   6899   1354    868   -765       C
ATOM   3672  C   ASP C 482      75.813   8.189 -62.940  1.00 60.02           C
ANISOU 3672  C   ASP C 482     8507   7317   6979   1366    900   -728       C
ATOM   3673  O   ASP C 482      76.135   9.121 -62.204  1.00 59.88           O
ANISOU 3673  O   ASP C 482     8447   7305   7001   1355    887   -690       O
ATOM   3674  CB  ASP C 482      73.675   7.126 -62.169  1.00 59.24           C
ANISOU 3674  CB  ASP C 482     8471   7197   6840   1315    821   -779       C
ATOM   3675  CG  ASP C 482      72.921   7.157 -63.484  1.00 59.81           C
ANISOU 3675  CG  ASP C 482     8584   7305   6838   1313    836   -804       C
ATOM   3676  OD1 ASP C 482      72.431   6.091 -63.913  1.00 60.26           O
ANISOU 3676  OD1 ASP C 482     8684   7351   6862   1312    836   -849       O
ATOM   3677  OD2 ASP C 482      72.817   8.245 -64.088  1.00 59.99           O
ANISOU 3677  OD2 ASP C 482     8592   7367   6833   1311    849   -778       O
ATOM   3678  N   PRO C 483      76.005   8.214 -64.271  1.00 43.29           N
ANISOU 3678  N   PRO C 483     6407   5225   4817   1388    944   -739       N
ATOM   3679  CA  PRO C 483      76.579   9.362 -64.986  1.00 43.19           C
ANISOU 3679  CA  PRO C 483     6366   5248   4797   1401    980   -703       C
ATOM   3680  C   PRO C 483      75.868  10.684 -64.696  1.00 42.98           C
ANISOU 3680  C   PRO C 483     6319   5248   4763   1372    953   -669       C
ATOM   3681  O   PRO C 483      76.494  11.741 -64.774  1.00 43.30           O
ANISOU 3681  O   PRO C 483     6320   5304   4826   1378    975   -630       O
ATOM   3682  CB  PRO C 483      76.389   8.978 -66.454  1.00 43.90           C
ANISOU 3682  CB  PRO C 483     6495   5365   4819   1418   1018   -732       C
ATOM   3683  CG  PRO C 483      76.457   7.496 -66.450  1.00 43.88           C
ANISOU 3683  CG  PRO C 483     6528   5327   4818   1430   1023   -780       C
ATOM   3684  CD  PRO C 483      75.803   7.060 -65.166  1.00 43.35           C
ANISOU 3684  CD  PRO C 483     6464   5227   4782   1402    967   -788       C
ATOM   3685  N   LEU C 484      74.583  10.621 -64.364  1.00 49.76           N
ANISOU 3685  N   LEU C 484     7204   6109   5592   1339    907   -684       N
ATOM   3686  CA  LEU C 484      73.805  11.822 -64.070  1.00 49.77           C
ANISOU 3686  CA  LEU C 484     7190   6134   5588   1310    881   -654       C
ATOM   3687  C   LEU C 484      74.052  12.362 -62.660  1.00 49.84           C
ANISOU 3687  C   LEU C 484     7157   6119   5662   1291    852   -628       C
ATOM   3688  O   LEU C 484      73.597  13.454 -62.320  1.00 49.85           O
ANISOU 3688  O   LEU C 484     7137   6134   5671   1268    837   -601       O
ATOM   3689  CB  LEU C 484      72.313  11.561 -64.286  1.00 49.14           C
ANISOU 3689  CB  LEU C 484     7151   6069   5451   1284    845   -679       C
ATOM   3690  CG  LEU C 484      71.788  11.833 -65.697  1.00 49.29           C
ANISOU 3690  CG  LEU C 484     7196   6136   5398   1290    868   -682       C
ATOM   3691  CD1 LEU C 484      70.469  11.117 -65.931  0.00 49.09           C
ANISOU 3691  CD1 LEU C 484     7217   6119   5316   1267    834   -721       C
ATOM   3692  CD2 LEU C 484      71.628  13.330 -65.913  0.00 49.51           C
ANISOU 3692  CD2 LEU C 484     7191   6196   5426   1283    876   -632       C
ATOM   3693  N   CYS C 485      74.770  11.597 -61.844  1.00 59.17           N
ANISOU 3693  N   CYS C 485     8326   7265   6889   1299    846   -637       N
ATOM   3694  CA  CYS C 485      75.111  12.039 -60.496  1.00 59.60           C
ANISOU 3694  CA  CYS C 485     8340   7301   7004   1280    819   -614       C
ATOM   3695  C   CYS C 485      76.262  13.035 -60.542  1.00 60.17           C
ANISOU 3695  C   CYS C 485     8361   7384   7117   1293    854   -576       C
ATOM   3696  O   CYS C 485      77.126  12.956 -61.415  1.00 60.49           O
ANISOU 3696  O   CYS C 485     8396   7434   7155   1326    900   -571       O
ATOM   3697  CB  CYS C 485      75.497  10.852 -59.612  1.00 59.29           C
ANISOU 3697  CB  CYS C 485     8303   7226   7000   1285    800   -633       C
ATOM   3698  SG  CYS C 485      74.231   9.577 -59.455  1.00 60.71           S
ANISOU 3698  SG  CYS C 485     8540   7385   7141   1268    760   -679       S
ATOM   3699  N   SER C 486      76.271  13.969 -59.598  1.00 60.04           N
ANISOU 3699  N   SER C 486     8308   7367   7139   1267    834   -550       N
ATOM   3700  CA  SER C 486      77.356  14.936 -59.499  1.00 60.52           C
ANISOU 3700  CA  SER C 486     8317   7436   7244   1274    864   -515       C
ATOM   3701  C   SER C 486      78.541  14.323 -58.761  1.00 60.82           C
ANISOU 3701  C   SER C 486     8323   7452   7334   1288    866   -512       C
ATOM   3702  O   SER C 486      78.588  13.112 -58.543  1.00 60.80           O
ANISOU 3702  O   SER C 486     8341   7429   7330   1300    854   -535       O
ATOM   3703  CB  SER C 486      76.885  16.204 -58.785  1.00 60.68           C
ANISOU 3703  CB  SER C 486     8308   7462   7285   1236    844   -492       C
ATOM   3704  OG  SER C 486      76.487  15.922 -57.455  1.00 60.96           O
ANISOU 3704  OG  SER C 486     8338   7479   7344   1206    795   -503       O
ATOM   3705  N   SER C 487      79.493  15.163 -58.371  1.00 69.00           N
ANISOU 3705  N   SER C 487     9307   8494   8418   1286    883   -481       N
ATOM   3706  CA  SER C 487      80.686  14.697 -57.673  1.00 69.78           C
ANISOU 3706  CA  SER C 487     9368   8579   8568   1298    886   -472       C
ATOM   3707  C   SER C 487      80.392  14.318 -56.222  1.00 70.22           C
ANISOU 3707  C   SER C 487     9413   8618   8649   1267    833   -478       C
ATOM   3708  O   SER C 487      81.269  13.826 -55.512  1.00 70.91           O
ANISOU 3708  O   SER C 487     9471   8696   8778   1275    828   -469       O
ATOM   3709  CB  SER C 487      81.785  15.761 -57.729  1.00 70.38           C
ANISOU 3709  CB  SER C 487     9389   8668   8685   1302    921   -438       C
ATOM   3710  OG  SER C 487      81.323  16.999 -57.218  1.00 70.72           O
ANISOU 3710  OG  SER C 487     9410   8721   8740   1264    906   -423       O
ATOM   3711  N   GLY C 488      79.155  14.545 -55.791  1.00 56.43           N
ANISOU 3711  N   GLY C 488     7691   6872   6879   1233    795   -491       N
ATOM   3712  CA  GLY C 488      78.749  14.248 -54.429  1.00 56.15           C
ANISOU 3712  CA  GLY C 488     7648   6824   6861   1201    744   -498       C
ATOM   3713  C   GLY C 488      78.731  12.765 -54.110  1.00 55.85           C
ANISOU 3713  C   GLY C 488     7636   6764   6822   1217    725   -517       C
ATOM   3714  O   GLY C 488      79.029  12.362 -52.986  1.00 56.12           O
ANISOU 3714  O   GLY C 488     7647   6789   6888   1204    695   -512       O
ATOM   3715  N   GLY C 489      78.377  11.951 -55.100  1.00 44.94           N
ANISOU 3715  N   GLY C 489     6300   5374   5402   1243    742   -540       N
ATOM   3716  CA  GLY C 489      78.326  10.512 -54.920  1.00 43.72           C
ANISOU 3716  CA  GLY C 489     6172   5193   5246   1260    730   -561       C
ATOM   3717  C   GLY C 489      76.919   9.960 -55.040  1.00 42.92           C
ANISOU 3717  C   GLY C 489     6126   5084   5100   1243    700   -594       C
ATOM   3718  O   GLY C 489      76.050  10.582 -55.650  1.00 42.55           O
ANISOU 3718  O   GLY C 489     6102   5053   5012   1229    700   -602       O
ATOM   3719  N   CYS C 490      76.696   8.788 -54.453  1.00 46.43           N
ANISOU 3719  N   CYS C 490     6588   5501   5551   1244    675   -610       N
ATOM   3720  CA  CYS C 490      75.393   8.135 -54.514  1.00 46.12           C
ANISOU 3720  CA  CYS C 490     6601   5451   5473   1228    647   -642       C
ATOM   3721  C   CYS C 490      75.249   7.072 -53.430  1.00 46.05           C
ANISOU 3721  C   CYS C 490     6596   5412   5488   1220    612   -648       C
ATOM   3722  O   CYS C 490      76.234   6.653 -52.823  1.00 46.46           O
ANISOU 3722  O   CYS C 490     6615   5452   5585   1236    616   -629       O
ATOM   3723  CB  CYS C 490      75.180   7.499 -55.888  1.00 45.16           C
ANISOU 3723  CB  CYS C 490     6525   5325   5308   1254    681   -672       C
ATOM   3724  SG  CYS C 490      76.370   6.201 -56.286  1.00 47.26           S
ANISOU 3724  SG  CYS C 490     6793   5562   5603   1303    722   -681       S
ATOM   3725  N   TRP C 491      74.015   6.637 -53.198  1.00 38.18           N
ANISOU 3725  N   TRP C 491     5638   4406   4463   1196    577   -673       N
ATOM   3726  CA  TRP C 491      73.737   5.608 -52.204  1.00 38.17           C
ANISOU 3726  CA  TRP C 491     5644   4377   4482   1187    544   -679       C
ATOM   3727  C   TRP C 491      73.561   4.246 -52.868  1.00 38.19           C
ANISOU 3727  C   TRP C 491     5692   4349   4471   1212    561   -712       C
ATOM   3728  O   TRP C 491      73.551   3.214 -52.199  1.00 38.43           O
ANISOU 3728  O   TRP C 491     5728   4349   4525   1215    545   -715       O
ATOM   3729  CB  TRP C 491      72.485   5.967 -51.401  1.00 38.13           C
ANISOU 3729  CB  TRP C 491     5651   4378   4459   1142    494   -684       C
ATOM   3730  CG  TRP C 491      72.525   7.348 -50.821  1.00 37.99           C
ANISOU 3730  CG  TRP C 491     5594   4388   4451   1114    480   -659       C
ATOM   3731  CD1 TRP C 491      72.052   8.491 -51.396  1.00 37.67           C
ANISOU 3731  CD1 TRP C 491     5555   4373   4384   1100    489   -657       C
ATOM   3732  CD2 TRP C 491      73.072   7.733 -49.554  1.00 38.05           C
ANISOU 3732  CD2 TRP C 491     5554   4402   4499   1096    457   -631       C
ATOM   3733  NE1 TRP C 491      72.269   9.563 -50.565  1.00 37.63           N
ANISOU 3733  NE1 TRP C 491     5509   4386   4405   1074    475   -633       N
ATOM   3734  CE2 TRP C 491      72.893   9.124 -49.428  1.00 38.02           C
ANISOU 3734  CE2 TRP C 491     5527   4425   4492   1069    455   -619       C
ATOM   3735  CE3 TRP C 491      73.693   7.035 -48.513  1.00 38.65           C
ANISOU 3735  CE3 TRP C 491     5605   4466   4613   1099    439   -615       C
ATOM   3736  CZ2 TRP C 491      73.314   9.832 -48.304  1.00 38.55           C
ANISOU 3736  CZ2 TRP C 491     5548   4506   4592   1043    436   -596       C
ATOM   3737  CZ3 TRP C 491      74.110   7.740 -47.398  1.00 39.23           C
ANISOU 3737  CZ3 TRP C 491     5631   4558   4716   1073    418   -589       C
ATOM   3738  CH2 TRP C 491      73.919   9.124 -47.303  1.00 39.28           C
ANISOU 3738  CH2 TRP C 491     5616   4591   4717   1044    417   -583       C
ATOM   3739  N   GLY C 492      73.422   4.253 -54.190  1.00 50.38           N
ANISOU 3739  N   GLY C 492     7265   5900   5975   1229    595   -735       N
ATOM   3740  CA  GLY C 492      73.254   3.028 -54.949  1.00 50.22           C
ANISOU 3740  CA  GLY C 492     7290   5852   5938   1250    618   -773       C
ATOM   3741  C   GLY C 492      73.247   3.268 -56.446  1.00 50.18           C
ANISOU 3741  C   GLY C 492     7311   5868   5888   1267    659   -795       C
ATOM   3742  O   GLY C 492      73.521   4.379 -56.900  1.00 50.07           O
ANISOU 3742  O   GLY C 492     7275   5887   5860   1268    675   -775       O
ATOM   3743  N   PRO C 493      72.929   2.222 -57.226  1.00 54.92           N
ANISOU 3743  N   PRO C 493     7957   6449   6462   1280    679   -837       N
ATOM   3744  CA  PRO C 493      72.917   2.304 -58.690  1.00 54.80           C
ANISOU 3744  CA  PRO C 493     7969   6454   6397   1296    720   -863       C
ATOM   3745  C   PRO C 493      71.659   2.981 -59.223  1.00 54.65           C
ANISOU 3745  C   PRO C 493     7977   6472   6315   1264    698   -877       C
ATOM   3746  O   PRO C 493      70.573   2.801 -58.670  1.00 54.63           O
ANISOU 3746  O   PRO C 493     7993   6464   6299   1232    654   -889       O
ATOM   3747  CB  PRO C 493      72.941   0.836 -59.113  1.00 54.45           C
ANISOU 3747  CB  PRO C 493     7964   6371   6354   1314    744   -906       C
ATOM   3748  CG  PRO C 493      72.237   0.129 -58.010  1.00 54.27           C
ANISOU 3748  CG  PRO C 493     7952   6316   6353   1291    699   -912       C
ATOM   3749  CD  PRO C 493      72.583   0.872 -56.745  1.00 54.74           C
ANISOU 3749  CD  PRO C 493     7961   6382   6457   1279    665   -862       C
ATOM   3750  N   GLY C 494      71.810   3.755 -60.292  1.00 62.20           N
ANISOU 3750  N   GLY C 494     8933   7467   7234   1273    728   -873       N
ATOM   3751  CA  GLY C 494      70.681   4.423 -60.912  1.00 62.41           C
ANISOU 3751  CA  GLY C 494     8981   7532   7198   1247    711   -881       C
ATOM   3752  C   GLY C 494      70.684   5.924 -60.705  1.00 62.57           C
ANISOU 3752  C   GLY C 494     8964   7588   7223   1235    701   -836       C
ATOM   3753  O   GLY C 494      71.367   6.431 -59.816  1.00 62.62           O
ANISOU 3753  O   GLY C 494     8927   7584   7281   1237    695   -801       O
ATOM   3754  N   PRO C 495      69.913   6.645 -61.532  1.00 50.58           N
ANISOU 3754  N   PRO C 495     7459   6110   5649   1222    701   -835       N
ATOM   3755  CA  PRO C 495      69.817   8.106 -61.462  1.00 50.16           C
ANISOU 3755  CA  PRO C 495     7372   6089   5597   1211    697   -792       C
ATOM   3756  C   PRO C 495      68.951   8.573 -60.296  1.00 49.12           C
ANISOU 3756  C   PRO C 495     7229   5951   5484   1174    645   -778       C
ATOM   3757  O   PRO C 495      68.917   9.766 -59.998  1.00 49.08           O
ANISOU 3757  O   PRO C 495     7192   5964   5494   1163    640   -742       O
ATOM   3758  CB  PRO C 495      69.149   8.468 -62.789  1.00 50.37           C
ANISOU 3758  CB  PRO C 495     7424   6161   5553   1210    712   -801       C
ATOM   3759  CG  PRO C 495      68.315   7.280 -63.111  1.00 50.45           C
ANISOU 3759  CG  PRO C 495     7484   6163   5522   1199    696   -852       C
ATOM   3760  CD  PRO C 495      69.098   6.090 -62.627  1.00 50.39           C
ANISOU 3760  CD  PRO C 495     7482   6106   5557   1218    707   -876       C
ATOM   3761  N   GLY C 496      68.260   7.642 -59.646  1.00 44.03           N
ANISOU 3761  N   GLY C 496     6609   5279   4840   1156    610   -806       N
ATOM   3762  CA  GLY C 496      67.394   7.981 -58.531  1.00 44.03           C
ANISOU 3762  CA  GLY C 496     6601   5272   4856   1120    561   -795       C
ATOM   3763  C   GLY C 496      68.051   7.760 -57.182  1.00 43.81           C
ANISOU 3763  C   GLY C 496     6543   5210   4891   1118    544   -781       C
ATOM   3764  O   GLY C 496      67.394   7.840 -56.144  1.00 43.70           O
ANISOU 3764  O   GLY C 496     6525   5186   4892   1089    504   -777       O
ATOM   3765  N   GLN C 497      69.352   7.489 -57.197  1.00 46.62           N
ANISOU 3765  N   GLN C 497     6878   5552   5283   1148    576   -772       N
ATOM   3766  CA  GLN C 497      70.092   7.202 -55.972  1.00 46.37           C
ANISOU 3766  CA  GLN C 497     6814   5493   5310   1149    562   -755       C
ATOM   3767  C   GLN C 497      71.227   8.198 -55.745  1.00 47.37           C
ANISOU 3767  C   GLN C 497     6889   5633   5476   1161    585   -717       C
ATOM   3768  O   GLN C 497      72.100   7.973 -54.908  1.00 48.07           O
ANISOU 3768  O   GLN C 497     6946   5705   5614   1168    582   -700       O
ATOM   3769  CB  GLN C 497      70.655   5.779 -56.018  1.00 47.18           C
ANISOU 3769  CB  GLN C 497     6935   5561   5430   1176    577   -778       C
ATOM   3770  CG  GLN C 497      69.596   4.687 -56.039  1.00 47.71           C
ANISOU 3770  CG  GLN C 497     7051   5607   5469   1162    553   -818       C
ATOM   3771  CD  GLN C 497      69.088   4.341 -54.653  1.00 48.60           C
ANISOU 3771  CD  GLN C 497     7158   5698   5611   1135    505   -812       C
ATOM   3772  OE1 GLN C 497      69.870   4.058 -53.746  1.00 49.09           O
ANISOU 3772  OE1 GLN C 497     7190   5740   5723   1143    500   -792       O
ATOM   3773  NE2 GLN C 497      67.771   4.365 -54.482  1.00 48.71           N
ANISOU 3773  NE2 GLN C 497     7198   5717   5592   1102    469   -829       N
ATOM   3774  N   CYS C 498      71.208   9.297 -56.492  1.00 45.40           N
ANISOU 3774  N   CYS C 498     6630   5415   5206   1161    607   -700       N
ATOM   3775  CA  CYS C 498      72.269  10.297 -56.414  1.00 45.48           C
ANISOU 3775  CA  CYS C 498     6591   5438   5252   1172    633   -665       C
ATOM   3776  C   CYS C 498      72.091  11.218 -55.214  1.00 45.78           C
ANISOU 3776  C   CYS C 498     6593   5479   5324   1138    602   -641       C
ATOM   3777  O   CYS C 498      70.972  11.445 -54.754  1.00 45.71           O
ANISOU 3777  O   CYS C 498     6599   5472   5298   1106    567   -648       O
ATOM   3778  CB  CYS C 498      72.306  11.132 -57.695  1.00 45.23           C
ANISOU 3778  CB  CYS C 498     6561   5437   5186   1186    671   -655       C
ATOM   3779  SG  CYS C 498      72.305  10.171 -59.226  1.00 46.26           S
ANISOU 3779  SG  CYS C 498     6739   5574   5263   1219    708   -688       S
ATOM   3780  N   LEU C 499      73.201  11.749 -54.711  1.00 46.94           N
ANISOU 3780  N   LEU C 499     6692   5626   5517   1143    617   -615       N
ATOM   3781  CA  LEU C 499      73.155  12.739 -53.643  1.00 47.29           C
ANISOU 3781  CA  LEU C 499     6698   5676   5593   1109    594   -594       C
ATOM   3782  C   LEU C 499      72.661  14.056 -54.230  1.00 47.25           C
ANISOU 3782  C   LEU C 499     6688   5694   5571   1097    610   -579       C
ATOM   3783  O   LEU C 499      71.801  14.724 -53.657  1.00 47.54           O
ANISOU 3783  O   LEU C 499     6722   5735   5606   1063    584   -576       O
ATOM   3784  CB  LEU C 499      74.538  12.910 -53.008  1.00 48.03           C
ANISOU 3784  CB  LEU C 499     6741   5768   5741   1118    607   -571       C
ATOM   3785  CG  LEU C 499      74.625  13.493 -51.593  1.00 48.74           C
ANISOU 3785  CG  LEU C 499     6792   5859   5868   1081    575   -557       C
ATOM   3786  CD1 LEU C 499      75.932  13.079 -50.937  1.00 49.26           C
ANISOU 3786  CD1 LEU C 499     6817   5921   5979   1094    579   -541       C
ATOM   3787  CD2 LEU C 499      74.498  15.010 -51.598  1.00 49.11           C
ANISOU 3787  CD2 LEU C 499     6811   5923   5924   1057    588   -540       C
ATOM   3788  N   SER C 500      73.216  14.419 -55.382  1.00 45.79           N
ANISOU 3788  N   SER C 500     6500   5524   5374   1126    655   -568       N
ATOM   3789  CA  SER C 500      72.769  15.591 -56.125  1.00 45.97           C
ANISOU 3789  CA  SER C 500     6519   5570   5377   1120    676   -550       C
ATOM   3790  C   SER C 500      72.908  15.335 -57.622  1.00 46.17           C
ANISOU 3790  C   SER C 500     6570   5612   5360   1155    714   -554       C
ATOM   3791  O   SER C 500      73.766  14.562 -58.049  1.00 46.25           O
ANISOU 3791  O   SER C 500     6584   5615   5372   1186    737   -562       O
ATOM   3792  CB  SER C 500      73.565  16.833 -55.720  1.00 46.53           C
ANISOU 3792  CB  SER C 500     6537   5646   5496   1111    696   -519       C
ATOM   3793  OG  SER C 500      74.948  16.665 -55.978  1.00 47.39           O
ANISOU 3793  OG  SER C 500     6619   5754   5632   1140    730   -507       O
ATOM   3794  N   CYS C 501      72.059  15.983 -58.412  1.00 54.26           N
ANISOU 3794  N   CYS C 501     7611   6660   6345   1150    721   -546       N
ATOM   3795  CA  CYS C 501      72.054  15.786 -59.857  1.00 54.47           C
ANISOU 3795  CA  CYS C 501     7663   6709   6322   1179    755   -549       C
ATOM   3796  C   CYS C 501      72.988  16.761 -60.563  1.00 55.07           C
ANISOU 3796  C   CYS C 501     7705   6803   6414   1200    805   -515       C
ATOM   3797  O   CYS C 501      73.268  17.847 -60.055  1.00 55.55           O
ANISOU 3797  O   CYS C 501     7726   6863   6516   1186    811   -486       O
ATOM   3798  CB  CYS C 501      70.636  15.933 -60.410  1.00 52.90           C
ANISOU 3798  CB  CYS C 501     7498   6532   6068   1163    736   -556       C
ATOM   3799  SG  CYS C 501      69.437  14.772 -59.719  1.00 57.17           S
ANISOU 3799  SG  CYS C 501     8082   7054   6584   1138    679   -598       S
ATOM   3800  N   ARG C 502      73.467  16.365 -61.737  1.00 63.29           N
ANISOU 3800  N   ARG C 502     8762   7861   7423   1234    842   -519       N
ATOM   3801  CA  ARG C 502      74.306  17.233 -62.554  1.00 63.68           C
ANISOU 3801  CA  ARG C 502     8784   7931   7481   1257    892   -486       C
ATOM   3802  C   ARG C 502      73.477  18.335 -63.200  1.00 63.79           C
ANISOU 3802  C   ARG C 502     8797   7975   7465   1247    900   -458       C
ATOM   3803  O   ARG C 502      73.897  19.491 -63.254  1.00 64.24           O
ANISOU 3803  O   ARG C 502     8816   8039   7553   1246    927   -420       O
ATOM   3804  CB  ARG C 502      75.031  16.425 -63.633  1.00 63.97           C
ANISOU 3804  CB  ARG C 502     8839   7977   7488   1295    931   -501       C
ATOM   3805  CG  ARG C 502      76.207  15.616 -63.119  1.00 63.98           C
ANISOU 3805  CG  ARG C 502     8826   7951   7534   1314    941   -514       C
ATOM   3806  CD  ARG C 502      76.952  14.940 -64.258  1.00 64.27           C
ANISOU 3806  CD  ARG C 502     8879   7997   7544   1353    987   -527       C
ATOM   3807  NE  ARG C 502      78.346  14.682 -63.911  1.00 64.47           N
ANISOU 3807  NE  ARG C 502     8870   8001   7624   1376   1013   -518       N
ATOM   3808  CZ  ARG C 502      79.341  15.531 -64.146  1.00 64.76           C
ANISOU 3808  CZ  ARG C 502     8864   8048   7693   1391   1051   -483       C
ATOM   3809  NH1 ARG C 502      79.095  16.694 -64.734  0.00 64.92           N
ANISOU 3809  NH1 ARG C 502     8873   8097   7698   1386   1070   -453       N
ATOM   3810  NH2 ARG C 502      80.581  15.219 -63.795  0.00 64.90           N
ANISOU 3810  NH2 ARG C 502     8851   8048   7761   1411   1071   -476       N
ATOM   3811  N   ASN C 503      72.295  17.969 -63.688  1.00 61.43           N
ANISOU 3811  N   ASN C 503     8538   7695   7108   1238    878   -475       N
ATOM   3812  CA  ASN C 503      71.420  18.920 -64.363  1.00 62.10           C
ANISOU 3812  CA  ASN C 503     8624   7812   7158   1230    884   -446       C
ATOM   3813  C   ASN C 503      70.113  19.169 -63.614  1.00 61.97           C
ANISOU 3813  C   ASN C 503     8616   7789   7139   1194    837   -448       C
ATOM   3814  O   ASN C 503      69.983  20.159 -62.894  1.00 62.31           O
ANISOU 3814  O   ASN C 503     8627   7820   7226   1174    831   -422       O
ATOM   3815  CB  ASN C 503      71.134  18.459 -65.794  1.00 62.95           C
ANISOU 3815  CB  ASN C 503     8767   7960   7192   1252    904   -455       C
ATOM   3816  CG  ASN C 503      72.393  18.341 -66.629  1.00 63.51           C
ANISOU 3816  CG  ASN C 503     8827   8041   7263   1289    957   -448       C
ATOM   3817  OD1 ASN C 503      72.854  19.318 -67.220  1.00 64.25           O
ANISOU 3817  OD1 ASN C 503     8893   8154   7363   1303    995   -408       O
ATOM   3818  ND2 ASN C 503      72.959  17.141 -66.681  1.00 63.11           N
ANISOU 3818  ND2 ASN C 503     8798   7974   7207   1305    961   -488       N
ATOM   3819  N   TYR C 504      69.150  18.269 -63.783  1.00 54.85           N
ANISOU 3819  N   TYR C 504     7757   6896   6188   1185    804   -481       N
ATOM   3820  CA  TYR C 504      67.836  18.437 -63.171  1.00 54.64           C
ANISOU 3820  CA  TYR C 504     7742   6866   6153   1151    760   -485       C
ATOM   3821  C   TYR C 504      67.381  17.195 -62.410  1.00 54.15           C
ANISOU 3821  C   TYR C 504     7711   6778   6086   1135    716   -531       C
ATOM   3822  O   TYR C 504      67.979  16.125 -62.529  1.00 54.14           O
ANISOU 3822  O   TYR C 504     7729   6764   6078   1151    721   -563       O
ATOM   3823  CB  TYR C 504      66.795  18.799 -64.232  1.00 55.69           C
ANISOU 3823  CB  TYR C 504     7893   7044   6224   1151    761   -469       C
ATOM   3824  CG  TYR C 504      67.060  20.111 -64.934  1.00 56.44           C
ANISOU 3824  CG  TYR C 504     7955   7164   6324   1165    801   -415       C
ATOM   3825  CD1 TYR C 504      67.718  20.147 -66.156  1.00 56.31           C
ANISOU 3825  CD1 TYR C 504     7940   7180   6274   1196    845   -402       C
ATOM   3826  CD2 TYR C 504      66.651  21.314 -64.373  1.00 56.64           C
ANISOU 3826  CD2 TYR C 504     7949   7182   6389   1146    799   -378       C
ATOM   3827  CE1 TYR C 504      67.961  21.345 -66.801  1.00 56.82           C
ANISOU 3827  CE1 TYR C 504     7975   7269   6346   1209    883   -350       C
ATOM   3828  CE2 TYR C 504      66.890  22.517 -65.010  1.00 57.01           C
ANISOU 3828  CE2 TYR C 504     7966   7250   6447   1159    839   -327       C
ATOM   3829  CZ  TYR C 504      67.545  22.526 -66.223  1.00 57.02           C
ANISOU 3829  CZ  TYR C 504     7968   7283   6415   1191    880   -311       C
ATOM   3830  OH  TYR C 504      67.785  23.721 -66.862  1.00 57.51           O
ANISOU 3830  OH  TYR C 504     7998   7365   6488   1205    921   -257       O
ATOM   3831  N   SER C 505      66.315  17.348 -61.632  1.00 45.83           N
ANISOU 3831  N   SER C 505     6662   5715   5036   1103    675   -534       N
ATOM   3832  CA  SER C 505      65.738  16.238 -60.883  1.00 45.24           C
ANISOU 3832  CA  SER C 505     6617   5617   4956   1085    631   -575       C
ATOM   3833  C   SER C 505      64.221  16.216 -61.038  1.00 45.08           C
ANISOU 3833  C   SER C 505     6622   5615   4891   1061    597   -581       C
ATOM   3834  O   SER C 505      63.572  17.263 -61.039  1.00 44.39           O
ANISOU 3834  O   SER C 505     6518   5544   4806   1047    595   -549       O
ATOM   3835  CB  SER C 505      66.116  16.330 -59.403  1.00 45.16           C
ANISOU 3835  CB  SER C 505     6581   5568   5010   1066    610   -575       C
ATOM   3836  OG  SER C 505      65.625  17.526 -58.824  1.00 45.98           O
ANISOU 3836  OG  SER C 505     6657   5673   5142   1042    603   -546       O
ATOM   3837  N   ARG C 506      63.662  15.018 -61.170  1.00 63.68           N
ANISOU 3837  N   ARG C 506     9018   7968   7209   1055    572   -622       N
ATOM   3838  CA  ARG C 506      62.224  14.856 -61.343  1.00 63.94           C
ANISOU 3838  CA  ARG C 506     9078   8020   7197   1032    538   -633       C
ATOM   3839  C   ARG C 506      61.685  13.789 -60.395  1.00 63.57           C
ANISOU 3839  C   ARG C 506     9055   7941   7158   1009    495   -672       C
ATOM   3840  O   ARG C 506      61.696  12.600 -60.714  1.00 63.74           O
ANISOU 3840  O   ARG C 506     9110   7955   7152   1015    490   -711       O
ATOM   3841  CB  ARG C 506      61.900  14.487 -62.793  1.00 64.80           C
ANISOU 3841  CB  ARG C 506     9215   8173   7233   1046    554   -644       C
ATOM   3842  CG  ARG C 506      60.414  14.352 -63.094  1.00 64.85           C
ANISOU 3842  CG  ARG C 506     9245   8206   7187   1022    519   -652       C
ATOM   3843  CD  ARG C 506      60.188  13.782 -64.487  1.00 65.47           C
ANISOU 3843  CD  ARG C 506     9356   8329   7190   1033    533   -673       C
ATOM   3844  NE  ARG C 506      60.713  14.657 -65.531  1.00 66.36           N
ANISOU 3844  NE  ARG C 506     9449   8482   7283   1058    575   -634       N
ATOM   3845  CZ  ARG C 506      60.827  14.310 -66.809  1.00 67.05           C
ANISOU 3845  CZ  ARG C 506     9557   8612   7309   1074    598   -646       C
ATOM   3846  NH1 ARG C 506      60.462  13.098 -67.204  1.00 67.10           N
ANISOU 3846  NH1 ARG C 506     9603   8623   7267   1066    584   -699       N
ATOM   3847  NH2 ARG C 506      61.314  15.172 -67.692  1.00 67.73           N
ANISOU 3847  NH2 ARG C 506     9621   8734   7380   1096    637   -606       N
ATOM   3848  N   GLY C 507      61.222  14.222 -59.227  1.00 71.87           N
ANISOU 3848  N   GLY C 507    10090   8971   8248    983    467   -661       N
ATOM   3849  CA  GLY C 507      60.668  13.313 -58.241  1.00 71.13           C
ANISOU 3849  CA  GLY C 507    10015   8847   8165    960    425   -692       C
ATOM   3850  C   GLY C 507      61.705  12.395 -57.624  1.00 71.51           C
ANISOU 3850  C   GLY C 507    10064   8859   8249    973    429   -714       C
ATOM   3851  O   GLY C 507      61.482  11.191 -57.496  1.00 71.82           O
ANISOU 3851  O   GLY C 507    10134   8880   8275    970    411   -750       O
ATOM   3852  N   GLY C 508      62.845  12.964 -57.244  1.00 67.11           N
ANISOU 3852  N   GLY C 508     9470   8289   7738    986    453   -691       N
ATOM   3853  CA  GLY C 508      63.907  12.201 -56.613  1.00 67.06           C
ANISOU 3853  CA  GLY C 508     9458   8252   7771    999    458   -704       C
ATOM   3854  C   GLY C 508      64.785  11.462 -57.605  1.00 66.99           C
ANISOU 3854  C   GLY C 508     9463   8245   7744   1035    493   -720       C
ATOM   3855  O   GLY C 508      65.737  10.782 -57.219  1.00 67.00           O
ANISOU 3855  O   GLY C 508     9458   8221   7778   1051    502   -729       O
ATOM   3856  N   VAL C 509      64.464  11.595 -58.888  1.00 50.34           N
ANISOU 3856  N   VAL C 509     7374   6168   5583   1047    514   -723       N
ATOM   3857  CA  VAL C 509      65.231  10.943 -59.943  1.00 50.14           C
ANISOU 3857  CA  VAL C 509     7365   6150   5535   1080    551   -741       C
ATOM   3858  C   VAL C 509      65.939  11.981 -60.807  1.00 49.95           C
ANISOU 3858  C   VAL C 509     7315   6157   5507   1102    595   -707       C
ATOM   3859  O   VAL C 509      65.320  12.937 -61.273  1.00 49.93           O
ANISOU 3859  O   VAL C 509     7305   6186   5480   1093    596   -682       O
ATOM   3860  CB  VAL C 509      64.329  10.070 -60.836  1.00 49.84           C
ANISOU 3860  CB  VAL C 509     7375   6128   5432   1075    543   -779       C
ATOM   3861  CG1 VAL C 509      65.160   9.337 -61.879  1.00 49.43           C
ANISOU 3861  CG1 VAL C 509     7342   6081   5358   1107    585   -803       C
ATOM   3862  CG2 VAL C 509      63.539   9.084 -59.988  1.00 49.76           C
ANISOU 3862  CG2 VAL C 509     7391   6088   5427   1050    500   -811       C
ATOM   3863  N   CYS C 510      67.238  11.791 -61.015  1.00 49.87           N
ANISOU 3863  N   CYS C 510     7290   6136   5523   1132    631   -703       N
ATOM   3864  CA  CYS C 510      68.022  12.714 -61.829  1.00 50.37           C
ANISOU 3864  CA  CYS C 510     7328   6226   5586   1155    676   -671       C
ATOM   3865  C   CYS C 510      67.674  12.592 -63.307  1.00 51.24           C
ANISOU 3865  C   CYS C 510     7466   6376   5627   1169    700   -681       C
ATOM   3866  O   CYS C 510      67.697  11.499 -63.873  1.00 51.70           O
ANISOU 3866  O   CYS C 510     7559   6431   5652   1181    708   -720       O
ATOM   3867  CB  CYS C 510      69.520  12.479 -61.625  1.00 50.38           C
ANISOU 3867  CB  CYS C 510     7303   6204   5634   1183    708   -666       C
ATOM   3868  SG  CYS C 510      70.120  12.876 -59.970  1.00 51.41           S
ANISOU 3868  SG  CYS C 510     7388   6300   5845   1167    686   -644       S
ATOM   3869  N   VAL C 511      67.350  13.723 -63.924  1.00 51.06           N
ANISOU 3869  N   VAL C 511     7428   6390   5582   1168    714   -646       N
ATOM   3870  CA  VAL C 511      67.058  13.764 -65.351  1.00 51.00           C
ANISOU 3870  CA  VAL C 511     7441   6429   5506   1181    738   -647       C
ATOM   3871  C   VAL C 511      67.953  14.781 -66.048  1.00 51.62           C
ANISOU 3871  C   VAL C 511     7487   6531   5594   1207    787   -604       C
ATOM   3872  O   VAL C 511      68.496  15.685 -65.412  1.00 51.64           O
ANISOU 3872  O   VAL C 511     7450   6519   5654   1207    795   -569       O
ATOM   3873  CB  VAL C 511      65.581  14.112 -65.622  1.00 50.83           C
ANISOU 3873  CB  VAL C 511     7437   6441   5436   1155    706   -641       C
ATOM   3874  CG1 VAL C 511      64.676  12.972 -65.180  1.00 50.15           C
ANISOU 3874  CG1 VAL C 511     7389   6336   5329   1131    663   -689       C
ATOM   3875  CG2 VAL C 511      65.203  15.409 -64.922  1.00 51.09           C
ANISOU 3875  CG2 VAL C 511     7433   6472   5508   1138    693   -595       C
ATOM   3876  N   THR C 512      68.105  14.625 -67.359  1.00 53.22           N
ANISOU 3876  N   THR C 512     7707   6772   5741   1228    819   -609       N
ATOM   3877  CA  THR C 512      68.940  15.519 -68.149  1.00 53.33           C
ANISOU 3877  CA  THR C 512     7693   6814   5757   1254    868   -568       C
ATOM   3878  C   THR C 512      68.221  16.833 -68.429  1.00 53.49           C
ANISOU 3878  C   THR C 512     7691   6868   5764   1243    866   -518       C
ATOM   3879  O   THR C 512      68.841  17.896 -68.466  1.00 53.79           O
ANISOU 3879  O   THR C 512     7690   6909   5838   1254    896   -472       O
ATOM   3880  CB  THR C 512      69.322  14.876 -69.485  1.00 53.93           C
ANISOU 3880  CB  THR C 512     7796   6923   5773   1279    906   -592       C
ATOM   3881  OG1 THR C 512      68.131  14.592 -70.229  1.00 55.15           O
ANISOU 3881  OG1 THR C 512     7986   7119   5851   1263    885   -609       O
ATOM   3882  CG2 THR C 512      70.083  13.583 -69.251  1.00 53.02           C
ANISOU 3882  CG2 THR C 512     7701   6769   5675   1293    915   -640       C
ATOM   3883  N   HIS C 513      66.910  16.748 -68.629  1.00 61.08           N
ANISOU 3883  N   HIS C 513     8676   7855   6676   1220    832   -525       N
ATOM   3884  CA  HIS C 513      66.092  17.924 -68.896  1.00 62.05           C
ANISOU 3884  CA  HIS C 513     8779   8011   6785   1209    828   -475       C
ATOM   3885  C   HIS C 513      64.628  17.638 -68.586  1.00 62.12           C
ANISOU 3885  C   HIS C 513     8811   8028   6762   1178    776   -491       C
ATOM   3886  O   HIS C 513      64.190  16.489 -68.628  1.00 62.28           O
ANISOU 3886  O   HIS C 513     8870   8047   6746   1167    751   -542       O
ATOM   3887  CB  HIS C 513      66.237  18.355 -70.356  1.00 63.22           C
ANISOU 3887  CB  HIS C 513     8927   8219   6876   1232    867   -447       C
ATOM   3888  CG  HIS C 513      65.729  17.343 -71.336  1.00 63.76           C
ANISOU 3888  CG  HIS C 513     9039   8326   6859   1232    861   -489       C
ATOM   3889  ND1 HIS C 513      66.490  16.278 -71.765  1.00 63.73           N
ANISOU 3889  ND1 HIS C 513     9062   8316   6837   1249    882   -536       N
ATOM   3890  CD2 HIS C 513      64.537  17.233 -71.967  1.00 64.17           C
ANISOU 3890  CD2 HIS C 513     9114   8426   6841   1216    836   -492       C
ATOM   3891  CE1 HIS C 513      65.788  15.554 -72.620  1.00 64.05           C
ANISOU 3891  CE1 HIS C 513     9141   8398   6799   1242    872   -569       C
ATOM   3892  NE2 HIS C 513      64.599  16.113 -72.760  1.00 64.37           N
ANISOU 3892  NE2 HIS C 513     9178   8473   6805   1220    843   -543       N
ATOM   3893  N   CYS C 514      63.877  18.688 -68.273  1.00 70.77           N
ANISOU 3893  N   CYS C 514     9882   9132   7874   1162    762   -448       N
ATOM   3894  CA  CYS C 514      62.450  18.554 -68.009  1.00 70.81           C
ANISOU 3894  CA  CYS C 514     9905   9149   7851   1132    716   -456       C
ATOM   3895  C   CYS C 514      61.687  18.473 -69.325  1.00 71.68           C
ANISOU 3895  C   CYS C 514    10035   9325   7875   1135    717   -449       C
ATOM   3896  O   CYS C 514      62.273  18.608 -70.399  1.00 72.18           O
ANISOU 3896  O   CYS C 514    10097   9425   7902   1160    755   -435       O
ATOM   3897  CB  CYS C 514      61.946  19.741 -67.186  1.00 70.71           C
ANISOU 3897  CB  CYS C 514     9856   9118   7891   1116    704   -411       C
ATOM   3898  SG  CYS C 514      62.898  20.072 -65.685  1.00 72.28           S
ANISOU 3898  SG  CYS C 514    10024   9249   8190   1110    708   -413       S
ATOM   3899  N   ASN C 515      60.379  18.255 -69.241  1.00 56.40           N
ANISOU 3899  N   ASN C 515     8117   7408   5904   1109    675   -458       N
ATOM   3900  CA  ASN C 515      59.538  18.230 -70.431  1.00 56.38           C
ANISOU 3900  CA  ASN C 515     8130   7475   5818   1107    670   -448       C
ATOM   3901  C   ASN C 515      59.258  19.638 -70.947  1.00 57.57           C
ANISOU 3901  C   ASN C 515     8242   7663   5968   1117    691   -373       C
ATOM   3902  O   ASN C 515      58.107  20.072 -70.998  1.00 58.54           O
ANISOU 3902  O   ASN C 515     8359   7813   6069   1100    665   -345       O
ATOM   3903  CB  ASN C 515      58.224  17.501 -70.146  1.00 56.10           C
ANISOU 3903  CB  ASN C 515     8123   7446   5746   1074    617   -482       C
ATOM   3904  CG  ASN C 515      58.426  16.027 -69.855  1.00 55.74           C
ANISOU 3904  CG  ASN C 515     8119   7370   5691   1066    600   -557       C
ATOM   3905  OD1 ASN C 515      59.264  15.370 -70.472  1.00 55.44           O
ANISOU 3905  OD1 ASN C 515     8099   7336   5630   1084    628   -588       O
ATOM   3906  ND2 ASN C 515      57.657  15.500 -68.909  1.00 55.87           N
ANISOU 3906  ND2 ASN C 515     8149   7353   5726   1037    556   -586       N
ATOM   3907  N   PHE C 516      60.316  20.349 -71.326  1.00 55.85           N
ANISOU 3907  N   PHE C 516     7998   7446   5776   1145    739   -337       N
ATOM   3908  CA  PHE C 516      60.189  21.721 -71.803  1.00 56.59           C
ANISOU 3908  CA  PHE C 516     8053   7571   5879   1158    766   -262       C
ATOM   3909  C   PHE C 516      59.484  21.790 -73.151  1.00 57.23           C
ANISOU 3909  C   PHE C 516     8142   7732   5869   1163    768   -237       C
ATOM   3910  O   PHE C 516      58.433  22.414 -73.281  1.00 57.21           O
ANISOU 3910  O   PHE C 516     8125   7760   5851   1151    750   -196       O
ATOM   3911  CB  PHE C 516      61.563  22.385 -71.923  1.00 56.61           C
ANISOU 3911  CB  PHE C 516     8025   7553   5929   1186    820   -233       C
ATOM   3912  CG  PHE C 516      62.304  22.497 -70.623  1.00 55.78           C
ANISOU 3912  CG  PHE C 516     7904   7375   5915   1181    821   -248       C
ATOM   3913  CD1 PHE C 516      63.460  21.766 -70.406  1.00 55.08           C
ANISOU 3913  CD1 PHE C 516     7826   7255   5847   1194    837   -289       C
ATOM   3914  CD2 PHE C 516      61.849  23.337 -69.621  1.00 56.05           C
ANISOU 3914  CD2 PHE C 516     7910   7374   6012   1163    807   -221       C
ATOM   3915  CE1 PHE C 516      64.148  21.869 -69.213  1.00 54.87           C
ANISOU 3915  CE1 PHE C 516     7781   7167   5900   1188    836   -300       C
ATOM   3916  CE2 PHE C 516      62.532  23.444 -68.424  1.00 55.48           C
ANISOU 3916  CE2 PHE C 516     7822   7240   6018   1155    807   -236       C
ATOM   3917  CZ  PHE C 516      63.683  22.709 -68.220  1.00 55.00           C
ANISOU 3917  CZ  PHE C 516     7770   7152   5974   1167    820   -275       C
ATOM   3918  N   LEU C 517      60.074  21.145 -74.152  1.00 73.45           N
ANISOU 3918  N   LEU C 517    10218   9823   7865   1179    791   -263       N
ATOM   3919  CA  LEU C 517      59.594  21.254 -75.524  1.00 73.85           C
ANISOU 3919  CA  LEU C 517    10275   9958   7827   1186    800   -237       C
ATOM   3920  C   LEU C 517      58.694  20.088 -75.931  1.00 74.36           C
ANISOU 3920  C   LEU C 517    10383  10060   7810   1162    760   -294       C
ATOM   3921  O   LEU C 517      57.877  20.218 -76.843  1.00 74.98           O
ANISOU 3921  O   LEU C 517    10464  10211   7815   1156    749   -272       O
ATOM   3922  CB  LEU C 517      60.778  21.378 -76.485  1.00 73.52           C
ANISOU 3922  CB  LEU C 517    10228   9942   7765   1219    855   -225       C
ATOM   3923  CG  LEU C 517      61.734  22.536 -76.183  1.00 73.27           C
ANISOU 3923  CG  LEU C 517    10152   9876   7812   1243    900   -169       C
ATOM   3924  CD1 LEU C 517      62.991  22.442 -77.033  1.00 73.01           C
ANISOU 3924  CD1 LEU C 517    10118   9860   7762   1275    953   -169       C
ATOM   3925  CD2 LEU C 517      61.041  23.875 -76.394  1.00 73.55           C
ANISOU 3925  CD2 LEU C 517    10147   9940   7857   1245    905    -86       C
ATOM   3926  N   ASN C 518      58.845  18.954 -75.255  1.00 85.43           N
ANISOU 3926  N   ASN C 518    11818  11414   9227   1148    738   -366       N
ATOM   3927  CA  ASN C 518      58.014  17.787 -75.536  1.00 85.26           C
ANISOU 3927  CA  ASN C 518    11839  11419   9138   1122    700   -427       C
ATOM   3928  C   ASN C 518      57.891  16.853 -74.335  1.00 84.12           C
ANISOU 3928  C   ASN C 518    11719  11205   9040   1101    666   -488       C
ATOM   3929  O   ASN C 518      58.781  16.797 -73.486  1.00 83.66           O
ANISOU 3929  O   ASN C 518    11653  11081   9053   1112    680   -499       O
ATOM   3930  CB  ASN C 518      58.550  17.017 -76.747  1.00 85.69           C
ANISOU 3930  CB  ASN C 518    11922  11520   9115   1134    729   -466       C
ATOM   3931  CG  ASN C 518      57.550  16.011 -77.286  1.00 86.04           C
ANISOU 3931  CG  ASN C 518    12006  11610   9075   1105    693   -519       C
ATOM   3932  OD1 ASN C 518      56.342  16.156 -77.095  1.00 86.51           O
ANISOU 3932  OD1 ASN C 518    12063  11692   9115   1079    651   -505       O
ATOM   3933  ND2 ASN C 518      58.049  14.984 -77.963  1.00 85.79           N
ANISOU 3933  ND2 ASN C 518    12010  11592   8994   1108    712   -580       N
ATOM   3934  N   GLY C 519      56.782  16.124 -74.273  1.00 66.60           N
ANISOU 3934  N   GLY C 519     9527   9001   6777   1070    621   -525       N
ATOM   3935  CA  GLY C 519      56.540  15.188 -73.191  1.00 66.17           C
ANISOU 3935  CA  GLY C 519     9497   8885   6761   1048    587   -581       C
ATOM   3936  C   GLY C 519      55.277  15.516 -72.421  1.00 66.53           C
ANISOU 3936  C   GLY C 519     9532   8923   6822   1019    539   -562       C
ATOM   3937  O   GLY C 519      54.840  16.666 -72.388  1.00 67.39           O
ANISOU 3937  O   GLY C 519     9606   9052   6947   1021    538   -498       O
ATOM   3938  N   GLU C 520      54.685  14.501 -71.802  1.00 53.19           N
ANISOU 3938  N   GLU C 520     7872   7204   5132    991    500   -618       N
ATOM   3939  CA  GLU C 520      53.481  14.692 -71.004  1.00 52.63           C
ANISOU 3939  CA  GLU C 520     7795   7123   5080    962    453   -606       C
ATOM   3940  C   GLU C 520      53.664  14.149 -69.588  1.00 51.83           C
ANISOU 3940  C   GLU C 520     7702   6941   5051    950    433   -641       C
ATOM   3941  O   GLU C 520      54.041  12.991 -69.407  0.00 51.40           O
ANISOU 3941  O   GLU C 520     7680   6855   4995    947    430   -701       O
ATOM   3942  CB  GLU C 520      52.269  14.046 -71.686  1.00 52.60           C
ANISOU 3942  CB  GLU C 520     7817   7176   4993    934    418   -634       C
ATOM   3943  CG  GLU C 520      52.488  12.607 -72.130  0.00 52.18           C
ANISOU 3943  CG  GLU C 520     7810   7121   4894    924    418   -714       C
ATOM   3944  CD  GLU C 520      51.284  12.027 -72.848  0.00 52.11           C
ANISOU 3944  CD  GLU C 520     7825   7174   4801    893    384   -741       C
ATOM   3945  OE1 GLU C 520      50.531  11.254 -72.220  0.00 51.62           O
ANISOU 3945  OE1 GLU C 520     7784   7085   4745    863    345   -783       O
ATOM   3946  OE2 GLU C 520      51.093  12.343 -74.042  0.00 52.55           O
ANISOU 3946  OE2 GLU C 520     7876   7306   4784    897    396   -721       O
ATOM   3947  N   PRO C 521      53.400  14.990 -68.576  1.00 67.21           N
ANISOU 3947  N   PRO C 521     9620   8856   7062    945    421   -601       N
ATOM   3948  CA  PRO C 521      52.967  16.385 -68.720  1.00 67.74           C
ANISOU 3948  CA  PRO C 521     9646   8951   7140    950    428   -529       C
ATOM   3949  C   PRO C 521      54.127  17.341 -68.998  1.00 67.96           C
ANISOU 3949  C   PRO C 521     9643   8976   7203    983    478   -484       C
ATOM   3950  O   PRO C 521      55.285  16.994 -68.758  1.00 67.25           O
ANISOU 3950  O   PRO C 521     9558   8849   7146   1000    504   -508       O
ATOM   3951  CB  PRO C 521      52.359  16.709 -67.346  1.00 67.48           C
ANISOU 3951  CB  PRO C 521     9599   8869   7172    928    397   -519       C
ATOM   3952  CG  PRO C 521      52.249  15.391 -66.622  1.00 66.88           C
ANISOU 3952  CG  PRO C 521     9559   8751   7102    908    366   -587       C
ATOM   3953  CD  PRO C 521      53.347  14.552 -67.173  1.00 66.70           C
ANISOU 3953  CD  PRO C 521     9561   8723   7061    928    394   -629       C
ATOM   3954  N   ARG C 522      53.811  18.531 -69.502  1.00 74.66           N
ANISOU 3954  N   ARG C 522    10458   9863   8046    993    494   -417       N
ATOM   3955  CA  ARG C 522      54.817  19.567 -69.716  1.00 74.94           C
ANISOU 3955  CA  ARG C 522    10460   9894   8121   1023    543   -368       C
ATOM   3956  C   ARG C 522      55.315  20.110 -68.382  1.00 74.72           C
ANISOU 3956  C   ARG C 522    10408   9795   8188   1021    548   -359       C
ATOM   3957  O   ARG C 522      54.566  20.151 -67.408  1.00 74.07           O
ANISOU 3957  O   ARG C 522    10323   9682   8139    996    515   -364       O
ATOM   3958  CB  ARG C 522      54.246  20.703 -70.564  1.00 75.86           C
ANISOU 3958  CB  ARG C 522    10546  10069   8210   1033    558   -296       C
ATOM   3959  CG  ARG C 522      54.059  20.356 -72.029  1.00 76.56           C
ANISOU 3959  CG  ARG C 522    10650  10236   8203   1042    565   -295       C
ATOM   3960  CD  ARG C 522      55.367  19.902 -72.648  1.00 76.98           C
ANISOU 3960  CD  ARG C 522    10718  10291   8241   1067    605   -321       C
ATOM   3961  NE  ARG C 522      55.421  20.211 -74.070  1.00 78.03           N
ANISOU 3961  NE  ARG C 522    10846  10501   8302   1085    631   -288       N
ATOM   3962  CZ  ARG C 522      55.830  21.377 -74.557  1.00 78.71           C
ANISOU 3962  CZ  ARG C 522    10894  10608   8403   1110    670   -218       C
ATOM   3963  NH1 ARG C 522      56.218  22.341 -73.733  1.00 78.93           N
ANISOU 3963  NH1 ARG C 522    10888  10585   8519   1118    688   -178       N
ATOM   3964  NH2 ARG C 522      55.854  21.582 -75.866  1.00 78.82           N
ANISOU 3964  NH2 ARG C 522    10906  10697   8346   1125    692   -189       N
ATOM   3965  N   GLU C 523      56.576  20.530 -68.340  1.00 84.04           N
ANISOU 3965  N   GLU C 523    11569  10950   9411   1045    590   -346       N
ATOM   3966  CA  GLU C 523      57.191  20.959 -67.085  1.00 83.80           C
ANISOU 3966  CA  GLU C 523    11516  10855   9469   1041    596   -344       C
ATOM   3967  C   GLU C 523      58.039  22.226 -67.214  1.00 83.76           C
ANISOU 3967  C   GLU C 523    11469  10844   9514   1063    645   -289       C
ATOM   3968  O   GLU C 523      58.441  22.610 -68.312  1.00 84.47           O
ANISOU 3968  O   GLU C 523    11549  10974   9570   1087    679   -258       O
ATOM   3969  CB  GLU C 523      58.038  19.823 -66.501  1.00 83.79           C
ANISOU 3969  CB  GLU C 523    11540  10811   9486   1041    590   -405       C
ATOM   3970  CG  GLU C 523      57.229  18.618 -66.042  1.00 84.05           C
ANISOU 3970  CG  GLU C 523    11611  10833   9492   1015    541   -460       C
ATOM   3971  CD  GLU C 523      58.037  17.337 -66.032  1.00 84.18           C
ANISOU 3971  CD  GLU C 523    11658  10827   9499   1023    543   -518       C
ATOM   3972  OE1 GLU C 523      57.422  16.250 -66.073  1.00 84.17           O
ANISOU 3972  OE1 GLU C 523    11693  10829   9459   1007    513   -565       O
ATOM   3973  OE2 GLU C 523      59.282  17.413 -65.986  1.00 84.26           O
ANISOU 3973  OE2 GLU C 523    11655  10815   9543   1045    577   -517       O
ATOM   3974  N   PHE C 524      58.303  22.867 -66.078  1.00 56.77           N
ANISOU 3974  N   PHE C 524     8024   7373   6173   1052    648   -278       N
ATOM   3975  CA  PHE C 524      59.173  24.039 -66.031  1.00 57.11           C
ANISOU 3975  CA  PHE C 524     8026   7400   6274   1069    694   -233       C
ATOM   3976  C   PHE C 524      60.272  23.846 -64.988  1.00 56.57           C
ANISOU 3976  C   PHE C 524     7948   7275   6270   1066    701   -263       C
ATOM   3977  O   PHE C 524      60.150  23.006 -64.096  1.00 56.06           O
ANISOU 3977  O   PHE C 524     7904   7180   6217   1046    666   -310       O
ATOM   3978  CB  PHE C 524      58.368  25.310 -65.730  1.00 57.46           C
ANISOU 3978  CB  PHE C 524     8036   7440   6354   1058    699   -179       C
ATOM   3979  CG  PHE C 524      57.812  25.366 -64.333  1.00 56.63           C
ANISOU 3979  CG  PHE C 524     7928   7288   6302   1026    667   -199       C
ATOM   3980  CD1 PHE C 524      58.491  26.035 -63.326  1.00 55.99           C
ANISOU 3980  CD1 PHE C 524     7817   7156   6299   1018    685   -196       C
ATOM   3981  CD2 PHE C 524      56.606  24.757 -64.028  1.00 56.62           C
ANISOU 3981  CD2 PHE C 524     7951   7294   6268   1003    619   -222       C
ATOM   3982  CE1 PHE C 524      57.981  26.089 -62.042  1.00 55.97           C
ANISOU 3982  CE1 PHE C 524     7812   7113   6341    987    657   -216       C
ATOM   3983  CE2 PHE C 524      56.091  24.807 -62.746  1.00 56.20           C
ANISOU 3983  CE2 PHE C 524     7894   7198   6261    974    592   -240       C
ATOM   3984  CZ  PHE C 524      56.779  25.475 -61.752  1.00 55.99           C
ANISOU 3984  CZ  PHE C 524     7840   7123   6311    966    611   -237       C
ATOM   3985  N   ALA C 525      61.340  24.629 -65.099  1.00 62.66           N
ANISOU 3985  N   ALA C 525     8688   8035   7085   1084    746   -234       N
ATOM   3986  CA  ALA C 525      62.480  24.493 -64.198  1.00 62.52           C
ANISOU 3986  CA  ALA C 525     8657   7970   7127   1082    756   -258       C
ATOM   3987  C   ALA C 525      62.419  25.468 -63.024  1.00 62.38           C
ANISOU 3987  C   ALA C 525     8605   7911   7186   1059    757   -241       C
ATOM   3988  O   ALA C 525      62.132  26.652 -63.199  1.00 62.78           O
ANISOU 3988  O   ALA C 525     8626   7965   7262   1059    782   -194       O
ATOM   3989  CB  ALA C 525      63.785  24.667 -64.964  1.00 62.91           C
ANISOU 3989  CB  ALA C 525     8692   8030   7180   1114    804   -243       C
ATOM   3990  N   HIS C 526      62.691  24.957 -61.828  1.00 69.43           N
ANISOU 3990  N   HIS C 526     9501   8764   8115   1038    731   -281       N
ATOM   3991  CA  HIS C 526      62.736  25.783 -60.626  1.00 69.79           C
ANISOU 3991  CA  HIS C 526     9515   8770   8232   1012    732   -274       C
ATOM   3992  C   HIS C 526      63.824  25.283 -59.682  1.00 69.30           C
ANISOU 3992  C   HIS C 526     9446   8675   8212   1005    727   -309       C
ATOM   3993  O   HIS C 526      63.622  24.311 -58.953  1.00 68.74           O
ANISOU 3993  O   HIS C 526     9398   8589   8132    990    687   -350       O
ATOM   3994  CB  HIS C 526      61.382  25.780 -59.916  1.00 69.92           C
ANISOU 3994  CB  HIS C 526     9543   8777   8246    982    691   -283       C
ATOM   3995  CG  HIS C 526      61.361  26.589 -58.651  1.00 69.94           C
ANISOU 3995  CG  HIS C 526     9516   8739   8318    952    692   -282       C
ATOM   3996  ND1 HIS C 526      61.551  27.953 -58.645  1.00 70.37           N
ANISOU 3996  ND1 HIS C 526     9532   8783   8423    951    732   -241       N
ATOM   3997  CD2 HIS C 526      61.176  26.220 -57.368  1.00 69.57           C
ANISOU 3997  CD2 HIS C 526     9473   8662   8298    922    658   -317       C
ATOM   3998  CE1 HIS C 526      61.481  28.392 -57.397  1.00 70.00           C
ANISOU 3998  CE1 HIS C 526     9466   8699   8431    919    724   -255       C
ATOM   3999  NE2 HIS C 526      61.256  27.368 -56.604  1.00 69.63           N
ANISOU 3999  NE2 HIS C 526     9444   8642   8369    901    679   -300       N
ATOM   4000  N   GLU C 527      64.971  25.958 -59.705  1.00 60.40           N
ANISOU 4000  N   GLU C 527     8284   7536   7128   1016    767   -290       N
ATOM   4001  CA  GLU C 527      66.134  25.568 -58.909  1.00 60.16           C
ANISOU 4001  CA  GLU C 527     8240   7479   7137   1012    767   -317       C
ATOM   4002  C   GLU C 527      66.540  24.118 -59.169  1.00 59.46           C
ANISOU 4002  C   GLU C 527     8185   7398   7007   1030    748   -353       C
ATOM   4003  O   GLU C 527      66.618  23.308 -58.245  1.00 58.63           O
ANISOU 4003  O   GLU C 527     8091   7273   6913   1015    714   -389       O
ATOM   4004  CB  GLU C 527      65.886  25.809 -57.415  1.00 60.41           C
ANISOU 4004  CB  GLU C 527     8257   7477   7218    973    740   -336       C
ATOM   4005  CG  GLU C 527      65.756  27.279 -57.042  0.00 61.51           C
ANISOU 4005  CG  GLU C 527     8358   7601   7412    954    768   -304       C
ATOM   4006  CD  GLU C 527      65.464  27.487 -55.568  0.00 61.95           C
ANISOU 4006  CD  GLU C 527     8401   7626   7511    913    742   -328       C
ATOM   4007  OE1 GLU C 527      65.163  26.494 -54.874  0.00 61.84           O
ANISOU 4007  OE1 GLU C 527     8412   7607   7479    899    698   -364       O
ATOM   4008  OE2 GLU C 527      65.537  28.645 -55.105  0.00 62.18           O
ANISOU 4008  OE2 GLU C 527     8397   7637   7593    894    767   -310       O
ATOM   4009  N   ALA C 528      66.783  23.810 -60.441  1.00 59.35           N
ANISOU 4009  N   ALA C 528     8187   7415   6948   1063    771   -344       N
ATOM   4010  CA  ALA C 528      67.212  22.481 -60.882  1.00 59.18           C
ANISOU 4010  CA  ALA C 528     8198   7402   6887   1083    763   -378       C
ATOM   4011  C   ALA C 528      66.212  21.370 -60.559  1.00 58.43           C
ANISOU 4011  C   ALA C 528     8144   7304   6752   1067    713   -417       C
ATOM   4012  O   ALA C 528      66.590  20.207 -60.426  1.00 58.05           O
ANISOU 4012  O   ALA C 528     8119   7247   6691   1075    699   -453       O
ATOM   4013  CB  ALA C 528      68.595  22.144 -60.324  1.00 59.21           C
ANISOU 4013  CB  ALA C 528     8181   7382   6935   1092    776   -391       C
ATOM   4014  N   GLU C 529      64.938  21.731 -60.442  1.00 69.73           N
ANISOU 4014  N   GLU C 529     9585   8744   8166   1046    689   -409       N
ATOM   4015  CA  GLU C 529      63.888  20.750 -60.184  1.00 69.91           C
ANISOU 4015  CA  GLU C 529     9646   8767   8150   1029    642   -443       C
ATOM   4016  C   GLU C 529      62.751  20.883 -61.194  1.00 70.16           C
ANISOU 4016  C   GLU C 529     9699   8838   8122   1031    637   -429       C
ATOM   4017  O   GLU C 529      62.400  21.989 -61.607  1.00 70.97           O
ANISOU 4017  O   GLU C 529     9779   8958   8228   1033    657   -386       O
ATOM   4018  CB  GLU C 529      63.354  20.891 -58.757  1.00 70.08           C
ANISOU 4018  CB  GLU C 529     9658   8756   8213    993    607   -455       C
ATOM   4019  CG  GLU C 529      64.400  20.666 -57.676  1.00 70.43           C
ANISOU 4019  CG  GLU C 529     9683   8767   8312    987    605   -471       C
ATOM   4020  CD  GLU C 529      63.836  20.813 -56.276  0.00 70.14           C
ANISOU 4020  CD  GLU C 529     9637   8703   8309    950    570   -482       C
ATOM   4021  OE1 GLU C 529      62.897  20.067 -55.929  0.00 69.80           O
ANISOU 4021  OE1 GLU C 529     9624   8657   8241    933    530   -507       O
ATOM   4022  OE2 GLU C 529      64.331  21.679 -55.524  0.00 70.22           O
ANISOU 4022  OE2 GLU C 529     9611   8697   8374    935    582   -468       O
ATOM   4023  N   CYS C 530      62.179  19.748 -61.587  1.00 55.65           N
ANISOU 4023  N   CYS C 530     7902   7015   6229   1031    611   -463       N
ATOM   4024  CA  CYS C 530      61.111  19.730 -62.580  1.00 55.54           C
ANISOU 4024  CA  CYS C 530     7909   7043   6150   1031    602   -454       C
ATOM   4025  C   CYS C 530      59.727  19.726 -61.937  1.00 55.38           C
ANISOU 4025  C   CYS C 530     7899   7020   6124    999    558   -460       C
ATOM   4026  O   CYS C 530      59.385  18.819 -61.178  1.00 55.36           O
ANISOU 4026  O   CYS C 530     7919   6993   6124    980    522   -499       O
ATOM   4027  CB  CYS C 530      61.257  18.517 -63.504  1.00 55.89           C
ANISOU 4027  CB  CYS C 530     7993   7111   6133   1047    602   -492       C
ATOM   4028  SG  CYS C 530      62.800  18.465 -64.447  1.00 58.42           S
ANISOU 4028  SG  CYS C 530     8305   7443   6450   1087    658   -486       S
ATOM   4029  N   PHE C 531      58.940  20.749 -62.248  1.00 53.17           N
ANISOU 4029  N   PHE C 531     7600   6762   5838    993    563   -417       N
ATOM   4030  CA  PHE C 531      57.558  20.832 -61.793  1.00 53.25           C
ANISOU 4030  CA  PHE C 531     7618   6775   5840    965    525   -416       C
ATOM   4031  C   PHE C 531      56.659  20.960 -63.014  1.00 53.98           C
ANISOU 4031  C   PHE C 531     7721   6924   5866    972    524   -393       C
ATOM   4032  O   PHE C 531      57.004  21.652 -63.969  1.00 54.75           O
ANISOU 4032  O   PHE C 531     7801   7053   5948    995    560   -354       O
ATOM   4033  CB  PHE C 531      57.364  22.032 -60.864  1.00 53.21           C
ANISOU 4033  CB  PHE C 531     7575   6741   5900    949    531   -383       C
ATOM   4034  CG  PHE C 531      58.239  22.001 -59.643  1.00 52.82           C
ANISOU 4034  CG  PHE C 531     7511   6643   5914    939    532   -404       C
ATOM   4035  CD1 PHE C 531      59.464  22.648 -59.634  1.00 52.81           C
ANISOU 4035  CD1 PHE C 531     7480   6629   5956    955    573   -385       C
ATOM   4036  CD2 PHE C 531      57.836  21.325 -58.504  1.00 52.53           C
ANISOU 4036  CD2 PHE C 531     7489   6577   5894    912    492   -440       C
ATOM   4037  CE1 PHE C 531      60.271  22.621 -58.511  1.00 52.59           C
ANISOU 4037  CE1 PHE C 531     7436   6561   5985    943    572   -404       C
ATOM   4038  CE2 PHE C 531      58.638  21.294 -57.377  1.00 51.93           C
ANISOU 4038  CE2 PHE C 531     7397   6461   5872    902    491   -457       C
ATOM   4039  CZ  PHE C 531      59.857  21.943 -57.381  1.00 51.91           C
ANISOU 4039  CZ  PHE C 531     7364   6449   5911    917    530   -439       C
ATOM   4040  N   SER C 532      55.508  20.297 -62.989  1.00 57.06           N
ANISOU 4040  N   SER C 532     8138   7329   6215    952    482   -415       N
ATOM   4041  CA  SER C 532      54.630  20.288 -64.153  1.00 57.75           C
ANISOU 4041  CA  SER C 532     8237   7475   6232    955    476   -397       C
ATOM   4042  C   SER C 532      53.853  21.590 -64.312  1.00 58.28           C
ANISOU 4042  C   SER C 532     8270   7563   6311    953    485   -335       C
ATOM   4043  O   SER C 532      53.619  22.314 -63.341  1.00 58.82           O
ANISOU 4043  O   SER C 532     8314   7595   6440    939    483   -317       O
ATOM   4044  CB  SER C 532      53.662  19.106 -64.097  1.00 57.53           C
ANISOU 4044  CB  SER C 532     8247   7456   6155    932    429   -444       C
ATOM   4045  OG  SER C 532      52.509  19.426 -63.340  1.00 57.77           O
ANISOU 4045  OG  SER C 532     8269   7476   6204    905    397   -433       O
ATOM   4046  N   CYS C 533      53.459  21.888 -65.546  1.00 49.79           N
ANISOU 4046  N   CYS C 533     7192   6547   5179    967    496   -301       N
ATOM   4047  CA  CYS C 533      52.676  23.085 -65.819  1.00 50.11           C
ANISOU 4047  CA  CYS C 533     7200   6613   5228    968    506   -236       C
ATOM   4048  C   CYS C 533      51.238  22.881 -65.365  1.00 50.11           C
ANISOU 4048  C   CYS C 533     7207   6618   5214    939    460   -241       C
ATOM   4049  O   CYS C 533      50.786  21.745 -65.176  1.00 49.89           O
ANISOU 4049  O   CYS C 533     7214   6591   5151    920    421   -293       O
ATOM   4050  CB  CYS C 533      52.698  23.409 -67.309  1.00 50.73           C
ANISOU 4050  CB  CYS C 533     7271   6759   5244    992    531   -195       C
ATOM   4051  SG  CYS C 533      54.290  24.023 -67.905  1.00 51.74           S
ANISOU 4051  SG  CYS C 533     7379   6884   5397   1029    593   -169       S
ATOM   4052  N   HIS C 534      50.525  23.985 -65.167  1.00 49.05           N
ANISOU 4052  N   HIS C 534     7040   6485   5112    935    466   -186       N
ATOM   4053  CA  HIS C 534      49.116  23.922 -64.806  1.00 49.22           C
ANISOU 4053  CA  HIS C 534     7064   6517   5123    910    427   -182       C
ATOM   4054  C   HIS C 534      48.398  23.113 -65.866  1.00 49.73           C
ANISOU 4054  C   HIS C 534     7154   6647   5095    907    399   -194       C
ATOM   4055  O   HIS C 534      48.665  23.277 -67.059  1.00 50.14           O
ANISOU 4055  O   HIS C 534     7201   6752   5097    928    420   -167       O
ATOM   4056  CB  HIS C 534      48.519  25.333 -64.763  1.00 50.04           C
ANISOU 4056  CB  HIS C 534     7122   6622   5267    915    448   -110       C
ATOM   4057  CG  HIS C 534      47.182  25.415 -64.092  1.00 50.31           C
ANISOU 4057  CG  HIS C 534     7152   6649   5314    888    413   -104       C
ATOM   4058  ND1 HIS C 534      45.996  25.446 -64.788  1.00 50.74           N
ANISOU 4058  ND1 HIS C 534     7203   6760   5316    884    391    -73       N
ATOM   4059  CD2 HIS C 534      46.850  25.492 -62.779  1.00 50.09           C
ANISOU 4059  CD2 HIS C 534     7121   6566   5344    865    398   -125       C
ATOM   4060  CE1 HIS C 534      44.987  25.528 -63.937  1.00 50.84           C
ANISOU 4060  CE1 HIS C 534     7210   6750   5357    860    364    -74       C
ATOM   4061  NE2 HIS C 534      45.481  25.556 -62.713  1.00 50.40           N
ANISOU 4061  NE2 HIS C 534     7157   6627   5368    848    368   -106       N
ATOM   4062  N   PRO C 535      47.496  22.221 -65.443  1.00 68.94           N
ANISOU 4062  N   PRO C 535     9612   9079   7502    878    351   -236       N
ATOM   4063  CA  PRO C 535      46.608  21.665 -66.464  1.00 69.17           C
ANISOU 4063  CA  PRO C 535     9659   9178   7446    871    324   -237       C
ATOM   4064  C   PRO C 535      45.815  22.843 -67.016  1.00 70.32           C
ANISOU 4064  C   PRO C 535     9765   9367   7587    880    335   -158       C
ATOM   4065  O   PRO C 535      45.685  23.813 -66.271  1.00 71.14           O
ANISOU 4065  O   PRO C 535     9837   9433   7761    881    350   -120       O
ATOM   4066  CB  PRO C 535      45.708  20.725 -65.664  1.00 68.49           C
ANISOU 4066  CB  PRO C 535     9598   9070   7355    837    274   -288       C
ATOM   4067  CG  PRO C 535      45.686  21.306 -64.286  1.00 68.80           C
ANISOU 4067  CG  PRO C 535     9619   9042   7481    827    276   -280       C
ATOM   4068  CD  PRO C 535      47.069  21.873 -64.075  1.00 68.97           C
ANISOU 4068  CD  PRO C 535     9624   9026   7554    851    321   -271       C
ATOM   4069  N   GLU C 536      45.331  22.769 -68.256  1.00 70.80           N
ANISOU 4069  N   GLU C 536     9825   9505   7570    886    330   -134       N
ATOM   4070  CA  GLU C 536      44.750  23.910 -68.983  1.00 72.49           C
ANISOU 4070  CA  GLU C 536     9998   9770   7774    901    347    -49       C
ATOM   4071  C   GLU C 536      45.779  24.809 -69.622  1.00 72.74           C
ANISOU 4071  C   GLU C 536    10005   9811   7823    937    401      0       C
ATOM   4072  O   GLU C 536      45.458  25.932 -70.022  1.00 73.24           O
ANISOU 4072  O   GLU C 536    10028   9899   7901    953    425     77       O
ATOM   4073  CB  GLU C 536      43.853  24.799 -68.128  1.00 73.74           C
ANISOU 4073  CB  GLU C 536    10124   9898   7997    891    340     -5       C
ATOM   4074  CG  GLU C 536      42.429  24.791 -68.565  1.00 74.74           C
ANISOU 4074  CG  GLU C 536    10240  10083   8075    876    305     26       C
ATOM   4075  CD  GLU C 536      41.645  23.767 -67.788  1.00 75.31           C
ANISOU 4075  CD  GLU C 536    10343  10135   8138    840    254    -36       C
ATOM   4076  OE1 GLU C 536      41.562  22.611 -68.247  0.00 75.69           O
ANISOU 4076  OE1 GLU C 536    10427  10214   8117    825    224    -91       O
ATOM   4077  OE2 GLU C 536      41.158  24.129 -66.702  0.00 75.38           O
ANISOU 4077  OE2 GLU C 536    10338  10092   8211    827    246    -32       O
ATOM   4078  N   CYS C 537      47.021  24.362 -69.682  1.00 69.74           N
ANISOU 4078  N   CYS C 537     9644   9406   7446    949    424    -40       N
ATOM   4079  CA  CYS C 537      47.983  25.081 -70.492  1.00 69.51           C
ANISOU 4079  CA  CYS C 537     9595   9398   7418    983    475      4       C
ATOM   4080  C   CYS C 537      48.044  24.294 -71.780  1.00 69.52           C
ANISOU 4080  C   CYS C 537     9622   9474   7318    988    468    -16       C
ATOM   4081  O   CYS C 537      48.231  23.077 -71.753  1.00 68.94           O
ANISOU 4081  O   CYS C 537     9590   9397   7207    973    445    -89       O
ATOM   4082  CB  CYS C 537      49.350  25.130 -69.815  1.00 69.02           C
ANISOU 4082  CB  CYS C 537     9536   9267   7422    995    508    -25       C
ATOM   4083  SG  CYS C 537      49.373  26.195 -68.346  1.00 70.58           S
ANISOU 4083  SG  CYS C 537     9699   9381   7738    988    523      0       S
ATOM   4084  N   GLN C 538      47.820  24.960 -72.906  1.00 85.00           N
ANISOU 4084  N   GLN C 538    11558  11506   9234   1006    487     49       N
ATOM   4085  CA  GLN C 538      47.928  24.289 -74.195  1.00 84.82           C
ANISOU 4085  CA  GLN C 538    11557  11561   9110   1011    484     33       C
ATOM   4086  C   GLN C 538      49.399  23.994 -74.449  1.00 84.50           C
ANISOU 4086  C   GLN C 538    11533  11497   9075   1032    524      0       C
ATOM   4087  O   GLN C 538      50.226  24.909 -74.445  1.00 84.88           O
ANISOU 4087  O   GLN C 538    11553  11523   9176   1059    570     45       O
ATOM   4088  CB  GLN C 538      47.367  25.165 -75.319  1.00 85.43           C
ANISOU 4088  CB  GLN C 538    11599  11721   9139   1027    497    118       C
ATOM   4089  CG  GLN C 538      47.237  24.449 -76.651  1.00 85.70           C
ANISOU 4089  CG  GLN C 538    11655  11849   9058   1024    487    101       C
ATOM   4090  CD  GLN C 538      46.138  23.403 -76.642  1.00 85.70           C
ANISOU 4090  CD  GLN C 538    11685  11881   8995    987    428     48       C
ATOM   4091  OE1 GLN C 538      44.986  23.702 -76.331  1.00 85.76           O
ANISOU 4091  OE1 GLN C 538    11674  11902   9010    970    396     80       O
ATOM   4092  NE2 GLN C 538      46.490  22.166 -76.975  1.00 85.65           N
ANISOU 4092  NE2 GLN C 538    11725  11888   8931    973    416    -33       N
ATOM   4093  N   PRO C 539      49.738  22.710 -74.631  1.00 64.55           N
ANISOU 4093  N   PRO C 539     9052   8975   6501   1021    508    -79       N
ATOM   4094  CA  PRO C 539      51.123  22.318 -74.905  1.00 64.05           C
ANISOU 4094  CA  PRO C 539     9006   8892   6440   1041    546   -114       C
ATOM   4095  C   PRO C 539      51.619  22.917 -76.216  1.00 64.41           C
ANISOU 4095  C   PRO C 539     9033   9005   6436   1070    587    -61       C
ATOM   4096  O   PRO C 539      51.016  22.682 -77.261  1.00 64.64           O
ANISOU 4096  O   PRO C 539     9069   9116   6376   1065    575    -52       O
ATOM   4097  CB  PRO C 539      51.038  20.793 -75.021  1.00 63.47           C
ANISOU 4097  CB  PRO C 539     8984   8824   6308   1019    516   -204       C
ATOM   4098  CG  PRO C 539      49.807  20.418 -74.266  1.00 63.42           C
ANISOU 4098  CG  PRO C 539     8986   8803   6307    985    462   -225       C
ATOM   4099  CD  PRO C 539      48.847  21.545 -74.496  1.00 64.03           C
ANISOU 4099  CD  PRO C 539     9022   8922   6383    986    456   -142       C
ATOM   4100  N   MET C 540      52.704  23.682 -76.153  1.00 65.96           N
ANISOU 4100  N   MET C 540     9205   9168   6688   1099    636    -27       N
ATOM   4101  CA  MET C 540      53.244  24.353 -77.331  1.00 66.92           C
ANISOU 4101  CA  MET C 540     9305   9348   6773   1129    681     30       C
ATOM   4102  C   MET C 540      54.201  23.448 -78.101  1.00 67.25           C
ANISOU 4102  C   MET C 540     9381   9413   6759   1140    702    -25       C
ATOM   4103  O   MET C 540      55.070  22.811 -77.512  1.00 66.89           O
ANISOU 4103  O   MET C 540     9357   9307   6751   1142    711    -83       O
ATOM   4104  CB  MET C 540      53.968  25.637 -76.920  1.00 67.41           C
ANISOU 4104  CB  MET C 540     9323   9363   6925   1155    727     94       C
ATOM   4105  CG  MET C 540      53.142  26.565 -76.044  1.00 67.71           C
ANISOU 4105  CG  MET C 540     9328   9365   7033   1145    713    142       C
ATOM   4106  SD  MET C 540      51.724  27.268 -76.905  1.00 67.89           S
ANISOU 4106  SD  MET C 540     9323   9476   6999   1143    696    224       S
ATOM   4107  CE  MET C 540      52.543  28.332 -78.090  1.00 68.42           C
ANISOU 4107  CE  MET C 540     9353   9591   7054   1185    760    309       C
ATOM   4108  N   GLU C 541      54.044  23.399 -79.420  1.00 98.11           N
ANISOU 4108  N   GLU C 541    13292  13411  10576   1148    712     -4       N
ATOM   4109  CA  GLU C 541      54.931  22.599 -80.257  1.00 98.28           C
ANISOU 4109  CA  GLU C 541    13344  13461  10539   1159    738    -53       C
ATOM   4110  C   GLU C 541      56.231  23.339 -80.559  1.00 98.92           C
ANISOU 4110  C   GLU C 541    13400  13525  10659   1196    799    -12       C
ATOM   4111  O   GLU C 541      56.235  24.337 -81.280  1.00 99.62           O
ANISOU 4111  O   GLU C 541    13455  13663  10735   1217    828     66       O
ATOM   4112  CB  GLU C 541      54.236  22.195 -81.559  1.00 98.25           C
ANISOU 4112  CB  GLU C 541    13354  13562  10413   1148    723    -53       C
ATOM   4113  CG  GLU C 541      53.139  21.157 -81.383  0.00 97.92           C
ANISOU 4113  CG  GLU C 541    13347  13539  10321   1108    665   -115       C
ATOM   4114  CD  GLU C 541      52.555  20.697 -82.705  0.00 98.08           C
ANISOU 4114  CD  GLU C 541    13383  13667  10217   1095    653   -123       C
ATOM   4115  OE1 GLU C 541      52.011  21.543 -83.444  0.00 98.46           O
ANISOU 4115  OE1 GLU C 541    13397  13789  10224   1103    656    -46       O
ATOM   4116  OE2 GLU C 541      52.646  19.488 -83.007  0.00 97.83           O
ANISOU 4116  OE2 GLU C 541    13395  13646  10129   1077    642   -207       O
ATOM   4117  N   GLY C 542      57.330  22.846 -79.997  1.00 86.66           N
ANISOU 4117  N   GLY C 542    11864  11905   9158   1205    820    -63       N
ATOM   4118  CA  GLY C 542      58.639  23.432 -80.227  1.00 86.61           C
ANISOU 4118  CA  GLY C 542    11837  11879   9193   1239    878    -34       C
ATOM   4119  C   GLY C 542      58.888  24.693 -79.423  1.00 86.78           C
ANISOU 4119  C   GLY C 542    11812  11845   9315   1251    898     30       C
ATOM   4120  O   GLY C 542      59.824  25.442 -79.703  1.00 86.79           O
ANISOU 4120  O   GLY C 542    11786  11839   9351   1279    948     74       O
ATOM   4121  N   THR C 543      58.048  24.931 -78.420  1.00100.01           N
ANISOU 4121  N   THR C 543    13478  13480  11039   1229    861     35       N
ATOM   4122  CA  THR C 543      58.179  26.116 -77.579  1.00100.15           C
ANISOU 4122  CA  THR C 543    13455  13443  11156   1235    878     90       C
ATOM   4123  C   THR C 543      57.811  25.790 -76.133  1.00 99.32           C
ANISOU 4123  C   THR C 543    13358  13263  11116   1208    839     46       C
ATOM   4124  O   THR C 543      57.097  24.822 -75.870  1.00 98.76           O
ANISOU 4124  O   THR C 543    13320  13195  11008   1183    793     -8       O
ATOM   4125  CB  THR C 543      57.286  27.267 -78.088  1.00100.98           C
ANISOU 4125  CB  THR C 543    13521  13596  11250   1241    883    181       C
ATOM   4126  OG1 THR C 543      57.190  27.209 -79.517  1.00101.75           O
ANISOU 4126  OG1 THR C 543    13622  13786  11252   1256    897    209       O
ATOM   4127  CG2 THR C 543      57.857  28.617 -77.675  1.00101.05           C
ANISOU 4127  CG2 THR C 543    13482  13559  11353   1261    928    247       C
ATOM   4128  N   ALA C 544      58.306  26.600 -75.201  1.00 74.03           N
ANISOU 4128  N   ALA C 544    10124   9992   8010   1212    860     70       N
ATOM   4129  CA  ALA C 544      58.020  26.410 -73.782  1.00 73.36           C
ANISOU 4129  CA  ALA C 544    10045   9838   7993   1187    827     33       C
ATOM   4130  C   ALA C 544      56.538  26.617 -73.484  1.00 73.12           C
ANISOU 4130  C   ALA C 544    10010   9822   7951   1163    785     53       C
ATOM   4131  O   ALA C 544      55.910  27.533 -74.014  1.00 73.93           O
ANISOU 4131  O   ALA C 544    10083   9963   8043   1171    796    122       O
ATOM   4132  CB  ALA C 544      58.870  27.351 -72.941  1.00 73.23           C
ANISOU 4132  CB  ALA C 544     9991   9754   8077   1195    862     59       C
ATOM   4133  N   THR C 545      55.986  25.760 -72.631  1.00 55.33           N
ANISOU 4133  N   THR C 545     7785   7539   5701   1135    738     -6       N
ATOM   4134  CA  THR C 545      54.566  25.817 -72.298  1.00 55.41           C
ANISOU 4134  CA  THR C 545     7795   7561   5699   1110    695      4       C
ATOM   4135  C   THR C 545      54.281  26.822 -71.184  1.00 55.98           C
ANISOU 4135  C   THR C 545     7832   7575   5863   1101    699     38       C
ATOM   4136  O   THR C 545      53.335  27.605 -71.270  1.00 56.09           O
ANISOU 4136  O   THR C 545     7822   7609   5882   1098    694     93       O
ATOM   4137  CB  THR C 545      54.033  24.433 -71.880  1.00 54.71           C
ANISOU 4137  CB  THR C 545     7751   7465   5571   1082    643    -74       C
ATOM   4138  OG1 THR C 545      54.301  23.482 -72.918  1.00 54.99           O
ANISOU 4138  OG1 THR C 545     7819   7552   5522   1089    643   -111       O
ATOM   4139  CG2 THR C 545      52.534  24.490 -71.628  1.00 54.46           C
ANISOU 4139  CG2 THR C 545     7718   7453   5522   1057    599    -60       C
ATOM   4140  N   CYS C 546      55.104  26.795 -70.141  1.00 82.63           N
ANISOU 4140  N   CYS C 546    11206  10879   9310   1096    708      6       N
ATOM   4141  CA  CYS C 546      54.921  27.687 -69.003  1.00 82.64           C
ANISOU 4141  CA  CYS C 546    11177  10822   9400   1084    714     28       C
ATOM   4142  C   CYS C 546      56.260  28.121 -68.410  1.00 82.89           C
ANISOU 4142  C   CYS C 546    11190  10798   9506   1093    753     22       C
ATOM   4143  O   CYS C 546      57.276  27.448 -68.584  1.00 83.16           O
ANISOU 4143  O   CYS C 546    11242  10828   9528   1104    763    -16       O
ATOM   4144  CB  CYS C 546      54.073  27.004 -67.925  1.00 81.82           C
ANISOU 4144  CB  CYS C 546    11095  10686   9306   1050    661    -21       C
ATOM   4145  SG  CYS C 546      54.935  25.705 -67.010  1.00 82.17           S
ANISOU 4145  SG  CYS C 546    11176  10680   9366   1036    639   -111       S
ATOM   4146  N   ASN C 547      56.252  29.252 -67.712  1.00 71.60           N
ANISOU 4146  N   ASN C 547     9724   9327   8155   1089    775     59       N
ATOM   4147  CA  ASN C 547      57.445  29.736 -67.028  1.00 71.45           C
ANISOU 4147  CA  ASN C 547     9684   9253   8212   1092    810     52       C
ATOM   4148  C   ASN C 547      57.383  29.430 -65.536  1.00 70.38           C
ANISOU 4148  C   ASN C 547     9555   9057   8131   1061    781      2       C
ATOM   4149  O   ASN C 547      58.370  29.581 -64.818  1.00 69.83           O
ANISOU 4149  O   ASN C 547     9473   8943   8118   1057    799    -18       O
ATOM   4150  CB  ASN C 547      57.629  31.237 -67.259  1.00 72.40           C
ANISOU 4150  CB  ASN C 547     9757   9365   8388   1106    862    124       C
ATOM   4151  CG  ASN C 547      56.438  32.049 -66.792  1.00 73.56           C
ANISOU 4151  CG  ASN C 547     9882   9498   8569   1090    854    162       C
ATOM   4152  OD1 ASN C 547      55.478  32.249 -67.537  1.00 74.40           O
ANISOU 4152  OD1 ASN C 547     9985   9651   8630   1098    846    204       O
ATOM   4153  ND2 ASN C 547      56.495  32.524 -65.553  1.00 73.54           N
ANISOU 4153  ND2 ASN C 547     9863   9433   8644   1068    857    146       N
ATOM   4154  N   GLY C 548      56.213  28.995 -65.078  1.00 51.97           N
ANISOU 4154  N   GLY C 548     7240   6727   5778   1037    736    -17       N
ATOM   4155  CA  GLY C 548      56.017  28.634 -63.686  1.00 51.26           C
ANISOU 4155  CA  GLY C 548     7160   6586   5732   1006    704    -64       C
ATOM   4156  C   GLY C 548      54.699  27.913 -63.473  1.00 51.38           C
ANISOU 4156  C   GLY C 548     7202   6617   5704    984    651    -87       C
ATOM   4157  O   GLY C 548      53.983  27.621 -64.431  1.00 52.03           O
ANISOU 4157  O   GLY C 548     7298   6753   5720    993    637    -71       O
ATOM   4158  N   SER C 549      54.378  27.623 -62.217  1.00 60.53           N
ANISOU 4158  N   SER C 549     8368   7733   6899    955    621   -125       N
ATOM   4159  CA  SER C 549      53.114  26.976 -61.887  1.00 60.56           C
ANISOU 4159  CA  SER C 549     8395   7746   6869    932    572   -147       C
ATOM   4160  C   SER C 549      52.016  28.019 -61.716  1.00 60.84           C
ANISOU 4160  C   SER C 549     8402   7781   6932    923    577    -98       C
ATOM   4161  O   SER C 549      52.247  29.090 -61.155  1.00 61.69           O
ANISOU 4161  O   SER C 549     8477   7852   7109    920    609    -71       O
ATOM   4162  CB  SER C 549      53.250  26.135 -60.615  1.00 60.20           C
ANISOU 4162  CB  SER C 549     8370   7656   6847    906    538   -209       C
ATOM   4163  OG  SER C 549      53.593  26.942 -59.503  1.00 60.54           O
ANISOU 4163  OG  SER C 549     8386   7649   6969    890    555   -206       O
ATOM   4164  N   GLY C 550      50.823  27.701 -62.206  1.00 41.87           N
ANISOU 4164  N   GLY C 550     6013   5419   4477    918    546    -87       N
ATOM   4165  CA  GLY C 550      49.707  28.626 -62.145  1.00 42.69           C
ANISOU 4165  CA  GLY C 550     6090   5528   4602    912    549    -36       C
ATOM   4166  C   GLY C 550      49.087  28.851 -63.510  1.00 44.05           C
ANISOU 4166  C   GLY C 550     6256   5768   4714    932    553     17       C
ATOM   4167  O   GLY C 550      49.763  28.752 -64.534  1.00 44.01           O
ANISOU 4167  O   GLY C 550     6254   5800   4669    957    574     30       O
ATOM   4168  N   SER C 551      47.795  29.162 -63.521  1.00 68.88           N
ANISOU 4168  N   SER C 551     9389   8931   7851    922    534     49       N
ATOM   4169  CA  SER C 551      47.054  29.336 -64.766  1.00 69.60           C
ANISOU 4169  CA  SER C 551     9471   9093   7879    938    532    101       C
ATOM   4170  C   SER C 551      47.432  30.615 -65.509  1.00 70.43           C
ANISOU 4170  C   SER C 551     9535   9213   8012    969    587    179       C
ATOM   4171  O   SER C 551      47.095  30.781 -66.682  1.00 71.10           O
ANISOU 4171  O   SER C 551     9611   9363   8042    988    592    227       O
ATOM   4172  CB  SER C 551      45.549  29.315 -64.490  1.00 69.75           C
ANISOU 4172  CB  SER C 551     9487   9127   7888    918    495    115       C
ATOM   4173  OG  SER C 551      45.201  30.264 -63.497  1.00 70.51           O
ANISOU 4173  OG  SER C 551     9553   9169   8068    908    513    138       O
ATOM   4174  N   ASP C 552      48.134  31.514 -64.828  1.00 63.83           N
ANISOU 4174  N   ASP C 552     8674   8319   7261    972    629    191       N
ATOM   4175  CA  ASP C 552      48.508  32.795 -65.420  1.00 64.26           C
ANISOU 4175  CA  ASP C 552     8686   8376   7353   1000    686    265       C
ATOM   4176  C   ASP C 552      49.897  32.774 -66.057  1.00 64.44           C
ANISOU 4176  C   ASP C 552     8712   8407   7367   1023    721    263       C
ATOM   4177  O   ASP C 552      50.317  33.753 -66.671  1.00 65.05           O
ANISOU 4177  O   ASP C 552     8755   8491   7468   1048    769    323       O
ATOM   4178  CB  ASP C 552      48.422  33.912 -64.377  1.00 64.78           C
ANISOU 4178  CB  ASP C 552     8719   8375   7521    989    718    286       C
ATOM   4179  CG  ASP C 552      49.151  33.568 -63.093  1.00 64.33           C
ANISOU 4179  CG  ASP C 552     8676   8251   7514    964    712    216       C
ATOM   4180  OD1 ASP C 552      48.511  33.013 -62.176  1.00 64.30           O
ANISOU 4180  OD1 ASP C 552     8692   8225   7515    936    673    171       O
ATOM   4181  OD2 ASP C 552      50.364  33.852 -63.000  1.00 63.83           O
ANISOU 4181  OD2 ASP C 552     8605   8160   7486    973    747    206       O
ATOM   4182  N   THR C 553      50.601  31.657 -65.914  1.00 66.29           N
ANISOU 4182  N   THR C 553     8982   8637   7566   1017    697    194       N
ATOM   4183  CA  THR C 553      51.950  31.533 -66.456  1.00 65.77           C
ANISOU 4183  CA  THR C 553     8920   8576   7492   1038    729    185       C
ATOM   4184  C   THR C 553      51.984  30.694 -67.730  1.00 65.88           C
ANISOU 4184  C   THR C 553     8960   8662   7408   1055    714    180       C
ATOM   4185  O   THR C 553      53.057  30.319 -68.205  1.00 65.98           O
ANISOU 4185  O   THR C 553     8985   8684   7401   1071    733    160       O
ATOM   4186  CB  THR C 553      52.921  30.926 -65.425  1.00 64.54           C
ANISOU 4186  CB  THR C 553     8783   8364   7375   1023    722    114       C
ATOM   4187  OG1 THR C 553      52.347  29.737 -64.868  1.00 64.49           O
ANISOU 4187  OG1 THR C 553     8815   8356   7333    998    666     52       O
ATOM   4188  CG2 THR C 553      53.195  31.918 -64.304  1.00 63.49           C
ANISOU 4188  CG2 THR C 553     8619   8163   7341   1009    750    123       C
ATOM   4189  N   CYS C 554      50.810  30.405 -68.283  1.00 69.16           N
ANISOU 4189  N   CYS C 554     9384   9132   7762   1049    681    197       N
ATOM   4190  CA  CYS C 554      50.715  29.589 -69.488  1.00 68.74           C
ANISOU 4190  CA  CYS C 554     9357   9153   7609   1060    664    189       C
ATOM   4191  C   CYS C 554      50.997  30.421 -70.739  1.00 68.93           C
ANISOU 4191  C   CYS C 554     9351   9230   7608   1092    707    264       C
ATOM   4192  O   CYS C 554      50.712  31.620 -70.779  1.00 69.39           O
ANISOU 4192  O   CYS C 554     9368   9282   7713   1104    738    335       O
ATOM   4193  CB  CYS C 554      49.323  28.964 -69.593  1.00 68.46           C
ANISOU 4193  CB  CYS C 554     9339   9159   7515   1038    610    178       C
ATOM   4194  SG  CYS C 554      48.772  28.103 -68.100  1.00 70.05           S
ANISOU 4194  SG  CYS C 554     9568   9299   7748    998    559    102       S
ATOM   4195  N   ALA C 555      51.567  29.782 -71.756  1.00 67.51           N
ANISOU 4195  N   ALA C 555     9192   9101   7356   1107    712    248       N
ATOM   4196  CA  ALA C 555      51.819  30.445 -73.031  1.00 68.07           C
ANISOU 4196  CA  ALA C 555     9239   9233   7389   1138    750    317       C
ATOM   4197  C   ALA C 555      50.537  30.505 -73.852  1.00 68.30           C
ANISOU 4197  C   ALA C 555     9261   9341   7348   1135    723    363       C
ATOM   4198  O   ALA C 555      50.354  31.404 -74.673  1.00 68.76           O
ANISOU 4198  O   ALA C 555     9285   9444   7396   1158    752    443       O
ATOM   4199  CB  ALA C 555      52.911  29.720 -73.805  1.00 67.74           C
ANISOU 4199  CB  ALA C 555     9224   9219   7295   1153    767    280       C
ATOM   4200  N   GLN C 556      49.649  29.545 -73.616  1.00 69.94           N
ANISOU 4200  N   GLN C 556     9500   9566   7509   1107    668    313       N
ATOM   4201  CA  GLN C 556      48.373  29.481 -74.315  1.00 70.26           C
ANISOU 4201  CA  GLN C 556     9534   9682   7480   1099    635    348       C
ATOM   4202  C   GLN C 556      47.399  28.588 -73.548  1.00 70.37           C
ANISOU 4202  C   GLN C 556     9576   9680   7481   1063    576    289       C
ATOM   4203  O   GLN C 556      47.786  27.547 -73.017  1.00 70.54           O
ANISOU 4203  O   GLN C 556     9637   9667   7497   1046    554    207       O
ATOM   4204  CB  GLN C 556      48.576  28.958 -75.738  1.00 70.49           C
ANISOU 4204  CB  GLN C 556     9579   9800   7402   1112    636    350       C
ATOM   4205  CG  GLN C 556      47.426  29.255 -76.682  1.00 71.13           C
ANISOU 4205  CG  GLN C 556     9639   9973   7414   1112    617    414       C
ATOM   4206  CD  GLN C 556      47.716  28.814 -78.104  1.00 71.48           C
ANISOU 4206  CD  GLN C 556     9697  10111   7353   1123    623    418       C
ATOM   4207  OE1 GLN C 556      48.678  29.268 -78.724  1.00 71.65           O
ANISOU 4207  OE1 GLN C 556     9706  10143   7375   1152    670    448       O
ATOM   4208  NE2 GLN C 556      46.887  27.917 -78.624  1.00 71.49           N
ANISOU 4208  NE2 GLN C 556     9722  10179   7262   1100    576    385       N
ATOM   4209  N   CYS C 557      46.138  29.002 -73.489  1.00 78.74           N
ANISOU 4209  N   CYS C 557    10614  10765   8538   1053    552    334       N
ATOM   4210  CA  CYS C 557      45.130  28.282 -72.715  1.00 78.64           C
ANISOU 4210  CA  CYS C 557    10621  10736   8521   1018    498    287       C
ATOM   4211  C   CYS C 557      44.525  27.114 -73.489  1.00 78.49           C
ANISOU 4211  C   CYS C 557    10637  10792   8395    999    452    244       C
ATOM   4212  O   CYS C 557      44.257  27.221 -74.686  1.00 79.00           O
ANISOU 4212  O   CYS C 557    10691  10941   8385   1010    453    286       O
ATOM   4213  CB  CYS C 557      44.026  29.237 -72.256  1.00 79.20           C
ANISOU 4213  CB  CYS C 557    10652  10797   8642   1014    494    352       C
ATOM   4214  SG  CYS C 557      44.612  30.624 -71.256  1.00 82.60           S
ANISOU 4214  SG  CYS C 557    11043  11136   9205   1031    549    396       S
ATOM   4215  N   ALA C 558      44.307  26.002 -72.795  1.00 76.69           N
ANISOU 4215  N   ALA C 558    10448  10532   8158    969    411    162       N
ATOM   4216  CA  ALA C 558      43.736  24.810 -73.412  1.00 76.50           C
ANISOU 4216  CA  ALA C 558    10459  10568   8038    946    367    111       C
ATOM   4217  C   ALA C 558      42.240  24.972 -73.658  1.00 77.11           C
ANISOU 4217  C   ALA C 558    10516  10703   8078    928    329    151       C
ATOM   4218  O   ALA C 558      41.738  24.630 -74.728  1.00 77.28           O
ANISOU 4218  O   ALA C 558    10542  10813   8009    922    310    161       O
ATOM   4219  CB  ALA C 558      44.004  23.586 -72.551  1.00 75.65           C
ANISOU 4219  CB  ALA C 558    10398  10402   7942    921    340     13       C
ATOM   4220  N   HIS C 559      41.532  25.492 -72.661  1.00 95.20           N
ANISOU 4220  N   HIS C 559    12787  12946  10439    918    317    174       N
ATOM   4221  CA  HIS C 559      40.091  25.684 -72.774  1.00 95.46           C
ANISOU 4221  CA  HIS C 559    12797  13026  10447    901    282    215       C
ATOM   4222  C   HIS C 559      39.724  27.154 -72.975  1.00 95.79           C
ANISOU 4222  C   HIS C 559    12782  13082  10533    927    313    322       C
ATOM   4223  O   HIS C 559      39.539  27.603 -74.106  1.00 95.83           O
ANISOU 4223  O   HIS C 559    12762  13166  10484    945    324    385       O
ATOM   4224  CB  HIS C 559      39.370  25.102 -71.555  1.00 95.66           C
ANISOU 4224  CB  HIS C 559    12840  12994  10511    868    241    163       C
ATOM   4225  CG  HIS C 559      39.483  23.613 -71.445  1.00 95.63           C
ANISOU 4225  CG  HIS C 559    12891  12988  10458    840    205     65       C
ATOM   4226  ND1 HIS C 559      40.222  22.990 -70.454  1.00 95.51           N
ANISOU 4226  ND1 HIS C 559    12908  12891  10492    832    207     -6       N
ATOM   4227  CD2 HIS C 559      38.964  22.620 -72.197  1.00 95.39           C
ANISOU 4227  CD2 HIS C 559    12886  13023  10334    818    168     26       C
ATOM   4228  CE1 HIS C 559      40.144  21.688 -70.604  1.00 94.89           C
ANISOU 4228  CE1 HIS C 559    12873  12826  10356    808    174    -81       C
ATOM   4229  NE2 HIS C 559      39.384  21.427 -71.660  1.00 94.90           N
ANISOU 4229  NE2 HIS C 559    12872  12916  10270    798    150    -67       N
ATOM   4230  N   PHE C 560      39.623  27.901 -71.879  1.00 73.05           N
ANISOU 4230  N   PHE C 560     9879  10124   7751    929    330    342       N
ATOM   4231  CA  PHE C 560      39.252  29.311 -71.956  1.00 73.39           C
ANISOU 4231  CA  PHE C 560     9867  10168   7849    953    364    442       C
ATOM   4232  C   PHE C 560      40.229  30.206 -71.198  1.00 73.63           C
ANISOU 4232  C   PHE C 560     9882  10113   7983    973    419    455       C
ATOM   4233  O   PHE C 560      41.084  29.723 -70.456  1.00 73.30           O
ANISOU 4233  O   PHE C 560     9870  10007   7974    964    423    386       O
ATOM   4234  CB  PHE C 560      37.834  29.524 -71.421  1.00 73.20           C
ANISOU 4234  CB  PHE C 560     9821  10146   7846    934    332    469       C
ATOM   4235  CG  PHE C 560      36.817  28.586 -72.003  1.00 72.88           C
ANISOU 4235  CG  PHE C 560     9798  10184   7711    908    275    448       C
ATOM   4236  CD1 PHE C 560      36.288  27.559 -71.240  1.00 72.66           C
ANISOU 4236  CD1 PHE C 560     9804  10130   7674    872    227    372       C
ATOM   4237  CD2 PHE C 560      36.391  28.728 -73.313  1.00 72.84           C
ANISOU 4237  CD2 PHE C 560     9772  10281   7624    919    268    505       C
ATOM   4238  CE1 PHE C 560      35.351  26.692 -71.771  1.00 72.45           C
ANISOU 4238  CE1 PHE C 560     9792  10174   7563    845    175    349       C
ATOM   4239  CE2 PHE C 560      35.455  27.863 -73.850  1.00 72.45           C
ANISOU 4239  CE2 PHE C 560     9736  10307   7485    892    214    482       C
ATOM   4240  CZ  PHE C 560      34.935  26.844 -73.077  1.00 72.45           C
ANISOU 4240  CZ  PHE C 560     9771  10277   7480    854    168    403       C
ATOM   4241  N   ARG C 561      40.092  31.514 -71.392  1.00 66.97           N
ANISOU 4241  N   ARG C 561     8989   9267   7190    998    460    545       N
ATOM   4242  CA  ARG C 561      40.921  32.487 -70.690  1.00 66.65           C
ANISOU 4242  CA  ARG C 561     8927   9145   7251   1015    515    564       C
ATOM   4243  C   ARG C 561      40.057  33.527 -69.983  1.00 67.03           C
ANISOU 4243  C   ARG C 561     8933   9153   7382   1015    530    621       C
ATOM   4244  O   ARG C 561      39.204  34.163 -70.601  1.00 67.43           O
ANISOU 4244  O   ARG C 561     8947   9254   7420   1029    533    702       O
ATOM   4245  CB  ARG C 561      41.875  33.186 -71.661  1.00 65.88           C
ANISOU 4245  CB  ARG C 561     8808   9075   7148   1051    567    619       C
ATOM   4246  CG  ARG C 561      42.901  34.078 -70.979  1.00 65.94           C
ANISOU 4246  CG  ARG C 561     8799   8999   7257   1066    624    627       C
ATOM   4247  CD  ARG C 561      43.384  35.188 -71.901  1.00 66.80           C
ANISOU 4247  CD  ARG C 561     8867   9135   7381   1104    681    717       C
ATOM   4248  NE  ARG C 561      44.023  34.674 -73.109  1.00 67.24           N
ANISOU 4248  NE  ARG C 561     8938   9261   7347   1120    682    715       N
ATOM   4249  CZ  ARG C 561      45.334  34.511 -73.250  0.00 67.18           C
ANISOU 4249  CZ  ARG C 561     8948   9232   7344   1132    711    682       C
ATOM   4250  NH1 ARG C 561      46.154  34.819 -72.254  0.00 67.22           N
ANISOU 4250  NH1 ARG C 561     8954   9149   7437   1128    740    649       N
ATOM   4251  NH2 ARG C 561      45.827  34.039 -74.387  0.00 67.08           N
ANISOU 4251  NH2 ARG C 561     8950   9290   7247   1146    712    682       N
ATOM   4252  N   ASP C 562      40.282  33.693 -68.684  1.00 57.27           N
ANISOU 4252  N   ASP C 562     7702   7827   6229   1000    540    580       N
ATOM   4253  CA  ASP C 562      39.565  34.695 -67.904  1.00 57.15           C
ANISOU 4253  CA  ASP C 562     7650   7763   6303    998    561    626       C
ATOM   4254  C   ASP C 562      40.551  35.676 -67.280  1.00 56.57           C
ANISOU 4254  C   ASP C 562     7557   7610   6328   1011    623    636       C
ATOM   4255  O   ASP C 562      41.159  35.389 -66.249  1.00 55.65           O
ANISOU 4255  O   ASP C 562     7463   7425   6255    992    624    567       O
ATOM   4256  CB  ASP C 562      38.718  34.030 -66.818  1.00 57.18           C
ANISOU 4256  CB  ASP C 562     7675   7733   6317    962    515    568       C
ATOM   4257  CG  ASP C 562      37.914  35.031 -66.011  1.00 57.91           C
ANISOU 4257  CG  ASP C 562     7729   7775   6498    959    537    613       C
ATOM   4258  OD1 ASP C 562      37.547  36.088 -66.566  1.00 57.97           O
ANISOU 4258  OD1 ASP C 562     7691   7802   6532    985    573    702       O
ATOM   4259  OD2 ASP C 562      37.649  34.760 -64.821  1.00 58.25           O
ANISOU 4259  OD2 ASP C 562     7788   7761   6584    931    521    559       O
ATOM   4260  N   GLY C 563      40.706  36.835 -67.913  1.00 49.22           N
ANISOU 4260  N   GLY C 563     6582   6688   5431   1042    675    722       N
ATOM   4261  CA  GLY C 563      41.684  37.814 -67.479  1.00 49.01           C
ANISOU 4261  CA  GLY C 563     6535   6592   5496   1056    738    737       C
ATOM   4262  C   GLY C 563      43.082  37.372 -67.864  1.00 49.14           C
ANISOU 4262  C   GLY C 563     6576   6611   5483   1065    752    696       C
ATOM   4263  O   GLY C 563      43.380  37.211 -69.048  1.00 48.82           O
ANISOU 4263  O   GLY C 563     6536   6638   5375   1087    754    727       O
ATOM   4264  N   PRO C 564      43.952  37.172 -66.863  1.00 44.39           N
ANISOU 4264  N   PRO C 564     5994   5938   4932   1047    760    626       N
ATOM   4265  CA  PRO C 564      45.302  36.660 -67.106  1.00 43.94           C
ANISOU 4265  CA  PRO C 564     5964   5880   4852   1054    770    579       C
ATOM   4266  C   PRO C 564      45.403  35.148 -66.901  1.00 43.85           C
ANISOU 4266  C   PRO C 564     6005   5886   4770   1031    711    490       C
ATOM   4267  O   PRO C 564      46.427  34.557 -67.241  1.00 43.51           O
ANISOU 4267  O   PRO C 564     5987   5853   4694   1038    713    452       O
ATOM   4268  CB  PRO C 564      46.137  37.390 -66.052  1.00 43.62           C
ANISOU 4268  CB  PRO C 564     5909   5750   4915   1046    814    559       C
ATOM   4269  CG  PRO C 564      45.157  37.751 -64.945  1.00 43.85           C
ANISOU 4269  CG  PRO C 564     5926   5730   5005   1021    805    553       C
ATOM   4270  CD  PRO C 564      43.750  37.526 -65.448  1.00 44.23           C
ANISOU 4270  CD  PRO C 564     5970   5837   5000   1022    767    592       C
ATOM   4271  N   HIS C 565      44.350  34.537 -66.364  1.00 63.53           N
ANISOU 4271  N   HIS C 565     8514   8381   7243   1005    662    460       N
ATOM   4272  CA  HIS C 565      44.368  33.114 -66.036  1.00 63.16           C
ANISOU 4272  CA  HIS C 565     8517   8342   7140    980    607    374       C
ATOM   4273  C   HIS C 565      43.685  32.257 -67.101  1.00 63.17           C
ANISOU 4273  C   HIS C 565     8538   8429   7035    982    564    377       C
ATOM   4274  O   HIS C 565      42.863  32.748 -67.876  1.00 63.61           O
ANISOU 4274  O   HIS C 565     8567   8539   7063    994    565    445       O
ATOM   4275  CB  HIS C 565      43.684  32.871 -64.687  1.00 62.56           C
ANISOU 4275  CB  HIS C 565     8451   8212   7109    947    578    329       C
ATOM   4276  CG  HIS C 565      44.207  33.726 -63.576  1.00 63.02           C
ANISOU 4276  CG  HIS C 565     8489   8188   7269    940    617    324       C
ATOM   4277  ND1 HIS C 565      43.596  34.913 -63.196  1.00 63.79           N
ANISOU 4277  ND1 HIS C 565     8545   8254   7437    942    650    379       N
ATOM   4278  CD2 HIS C 565      45.265  33.577 -62.756  1.00 62.63           C
ANISOU 4278  CD2 HIS C 565     8452   8082   7262    930    631    270       C
ATOM   4279  CE1 HIS C 565      44.263  35.442 -62.200  1.00 63.81           C
ANISOU 4279  CE1 HIS C 565     8539   8186   7520    931    682    355       C
ATOM   4280  NE2 HIS C 565      45.288  34.659 -61.902  1.00 63.03           N
ANISOU 4280  NE2 HIS C 565     8471   8072   7406    923    670    289       N
ATOM   4281  N   CYS C 566      44.033  30.972 -67.125  1.00 49.84           N
ANISOU 4281  N   CYS C 566     6895   6754   5289    967    528    302       N
ATOM   4282  CA  CYS C 566      43.356  29.987 -67.966  1.00 49.65           C
ANISOU 4282  CA  CYS C 566     6896   6805   5164    959    481    286       C
ATOM   4283  C   CYS C 566      42.391  29.166 -67.109  1.00 50.01           C
ANISOU 4283  C   CYS C 566     6965   6832   5203    924    428    233       C
ATOM   4284  O   CYS C 566      42.758  28.699 -66.030  1.00 49.66           O
ANISOU 4284  O   CYS C 566     6944   6726   5200    905    417    172       O
ATOM   4285  CB  CYS C 566      44.372  29.061 -68.639  1.00 48.72           C
ANISOU 4285  CB  CYS C 566     6814   6713   4984    967    480    236       C
ATOM   4286  SG  CYS C 566      45.620  29.893 -69.652  1.00 49.41           S
ANISOU 4286  SG  CYS C 566     6877   6821   5074   1008    543    289       S
ATOM   4287  N   VAL C 567      41.158  29.001 -67.586  1.00 61.05           N
ANISOU 4287  N   VAL C 567     8357   8288   6550    914    394    260       N
ATOM   4288  CA  VAL C 567      40.115  28.313 -66.821  1.00 60.85           C
ANISOU 4288  CA  VAL C 567     8349   8250   6520    881    344    220       C
ATOM   4289  C   VAL C 567      39.398  27.257 -67.663  1.00 60.43           C
ANISOU 4289  C   VAL C 567     8322   8274   6365    866    295    196       C
ATOM   4290  O   VAL C 567      39.231  27.420 -68.874  1.00 60.50           O
ANISOU 4290  O   VAL C 567     8317   8358   6310    881    298    240       O
ATOM   4291  CB  VAL C 567      39.065  29.311 -66.254  1.00 61.22           C
ANISOU 4291  CB  VAL C 567     8356   8277   6628    878    350    279       C
ATOM   4292  CG1 VAL C 567      38.269  28.678 -65.116  1.00 61.60           C
ANISOU 4292  CG1 VAL C 567     8423   8286   6696    842    308    227       C
ATOM   4293  CG2 VAL C 567      39.733  30.588 -65.771  1.00 60.96           C
ANISOU 4293  CG2 VAL C 567     8288   8185   6689    898    409    321       C
ATOM   4294  N   SER C 568      38.975  26.174 -67.020  1.00 73.21           N
ANISOU 4294  N   SER C 568     9976   9874   7967    834    249    126       N
ATOM   4295  CA  SER C 568      38.272  25.101 -67.713  1.00 73.04           C
ANISOU 4295  CA  SER C 568     9980   9918   7853    814    202     93       C
ATOM   4296  C   SER C 568      36.882  25.541 -68.149  1.00 73.52           C
ANISOU 4296  C   SER C 568    10008  10038   7886    808    179    155       C
ATOM   4297  O   SER C 568      36.443  25.237 -69.259  1.00 73.64           O
ANISOU 4297  O   SER C 568    10024  10138   7819    807    160    172       O
ATOM   4298  CB  SER C 568      38.141  23.890 -66.785  1.00 72.27           C
ANISOU 4298  CB  SER C 568     9926   9776   7757    781    162      5       C
ATOM   4299  OG  SER C 568      37.597  24.280 -65.535  1.00 72.12           O
ANISOU 4299  OG  SER C 568     9893   9697   7813    767    157      9       O
ATOM   4300  N   SER C 569      36.195  26.256 -67.264  1.00 73.35           N
ANISOU 4300  N   SER C 569     9959   9975   7935    803    182    188       N
ATOM   4301  CA  SER C 569      34.821  26.668 -67.505  1.00 73.55           C
ANISOU 4301  CA  SER C 569     9952  10047   7947    796    160    246       C
ATOM   4302  C   SER C 569      34.671  28.150 -67.208  1.00 74.21           C
ANISOU 4302  C   SER C 569     9984  10101   8112    820    205    330       C
ATOM   4303  O   SER C 569      35.202  28.652 -66.219  1.00 74.61           O
ANISOU 4303  O   SER C 569    10030  10071   8246    823    235    319       O
ATOM   4304  CB  SER C 569      33.871  25.860 -66.623  1.00 73.15           C
ANISOU 4304  CB  SER C 569     9921   9973   7898    758    111    195       C
ATOM   4305  OG  SER C 569      34.255  25.954 -65.264  1.00 72.83           O
ANISOU 4305  OG  SER C 569     9890   9840   7942    750    124    158       O
ATOM   4306  N   CYS C 570      33.948  28.846 -68.075  1.00 93.52           N
ANISOU 4306  N   CYS C 570    12388  12612  10532    836    209    413       N
ATOM   4307  CA  CYS C 570      33.698  30.264 -67.896  1.00 93.59           C
ANISOU 4307  CA  CYS C 570    12345  12598  10617    860    253    500       C
ATOM   4308  C   CYS C 570      32.823  30.452 -66.663  1.00 93.33           C
ANISOU 4308  C   CYS C 570    12302  12505  10653    839    241    492       C
ATOM   4309  O   CYS C 570      31.939  29.633 -66.405  1.00 93.38           O
ANISOU 4309  O   CYS C 570    12325  12530  10624    810    191    455       O
ATOM   4310  CB  CYS C 570      33.006  30.831 -69.136  1.00 93.71           C
ANISOU 4310  CB  CYS C 570    12319  12706  10581    880    254    592       C
ATOM   4311  SG  CYS C 570      33.604  32.455 -69.649  1.00103.08           S
ANISOU 4311  SG  CYS C 570    13452  13884  11829    928    328    697       S
ATOM   4312  N   PRO C 571      33.085  31.516 -65.886  1.00 55.64           N
ANISOU 4312  N   PRO C 571     7501   7660   5979    853    289    522       N
ATOM   4313  CA  PRO C 571      32.358  31.843 -64.654  1.00 55.79           C
ANISOU 4313  CA  PRO C 571     7509   7616   6075    835    289    517       C
ATOM   4314  C   PRO C 571      30.848  31.823 -64.855  1.00 56.80           C
ANISOU 4314  C   PRO C 571     7612   7793   6178    824    254    560       C
ATOM   4315  O   PRO C 571      30.316  32.640 -65.607  1.00 57.31           O
ANISOU 4315  O   PRO C 571     7631   7904   6239    847    271    648       O
ATOM   4316  CB  PRO C 571      32.830  33.263 -64.348  1.00 55.51           C
ANISOU 4316  CB  PRO C 571     7434   7524   6135    861    357    575       C
ATOM   4317  CG  PRO C 571      34.209  33.307 -64.895  1.00 55.43           C
ANISOU 4317  CG  PRO C 571     7436   7513   6110    882    387    563       C
ATOM   4318  CD  PRO C 571      34.176  32.473 -66.145  1.00 55.55           C
ANISOU 4318  CD  PRO C 571     7470   7621   6015    885    351    561       C
ATOM   4319  N   HIS C 572      30.170  30.890 -64.194  1.00 72.14           N
ANISOU 4319  N   HIS C 572     9582   9728   8101    789    205    500       N
ATOM   4320  CA  HIS C 572      28.734  30.733 -64.376  1.00 72.08           C
ANISOU 4320  CA  HIS C 572     9553   9770   8064    775    166    533       C
ATOM   4321  C   HIS C 572      27.967  30.825 -63.059  1.00 72.30           C
ANISOU 4321  C   HIS C 572     9577   9734   8161    752    159    513       C
ATOM   4322  O   HIS C 572      27.264  29.894 -62.666  1.00 72.39           O
ANISOU 4322  O   HIS C 572     9612   9753   8141    721    110    465       O
ATOM   4323  CB  HIS C 572      28.409  29.432 -65.129  1.00 71.52           C
ANISOU 4323  CB  HIS C 572     9515   9776   7883    753    106    489       C
ATOM   4324  CG  HIS C 572      29.009  28.194 -64.512  0.00 71.03           C
ANISOU 4324  CG  HIS C 572     9512   9675   7800    725     77    381       C
ATOM   4325  ND1 HIS C 572      30.296  27.785 -64.780  0.00 70.81           N
ANISOU 4325  ND1 HIS C 572     9518   9636   7751    733     92    335       N
ATOM   4326  CD2 HIS C 572      28.477  27.286 -63.674  0.00 70.65           C
ANISOU 4326  CD2 HIS C 572     9493   9600   7750    689     36    316       C
ATOM   4327  CE1 HIS C 572      30.537  26.673 -64.112  0.00 70.27           C
ANISOU 4327  CE1 HIS C 572     9496   9532   7669    705     61    246       C
ATOM   4328  NE2 HIS C 572      29.463  26.339 -63.433  0.00 70.13           N
ANISOU 4328  NE2 HIS C 572     9478   9504   7663    678     27    233       N
ATOM   4329  N   GLY C 573      28.108  31.961 -62.384  1.00 66.10           N
ANISOU 4329  N   GLY C 573     8761   8882   7471    768    212    550       N
ATOM   4330  CA  GLY C 573      27.366  32.222 -61.165  1.00 66.40           C
ANISOU 4330  CA  GLY C 573     8789   8860   7581    749    215    540       C
ATOM   4331  C   GLY C 573      28.202  32.348 -59.913  1.00 66.88           C
ANISOU 4331  C   GLY C 573     8873   8826   7714    738    244    480       C
ATOM   4332  O   GLY C 573      27.685  32.209 -58.805  1.00 67.28           O
ANISOU 4332  O   GLY C 573     8929   8827   7806    713    234    445       O
ATOM   4333  N   VAL C 574      29.492  32.611 -60.083  1.00 78.81           N
ANISOU 4333  N   VAL C 574    10393  10312   9238    755    278    467       N
ATOM   4334  CA  VAL C 574      30.382  32.770 -58.942  1.00 78.97           C
ANISOU 4334  CA  VAL C 574    10432  10248   9325    744    307    411       C
ATOM   4335  C   VAL C 574      30.081  34.064 -58.189  1.00 79.36           C
ANISOU 4335  C   VAL C 574    10441  10236   9476    751    361    454       C
ATOM   4336  O   VAL C 574      30.159  35.158 -58.747  1.00 79.80           O
ANISOU 4336  O   VAL C 574    10456  10296   9569    781    409    528       O
ATOM   4337  CB  VAL C 574      31.866  32.714 -59.358  1.00 79.07           C
ANISOU 4337  CB  VAL C 574    10464  10255   9325    760    331    388       C
ATOM   4338  CG1 VAL C 574      32.300  31.270 -59.564  1.00 78.64           C
ANISOU 4338  CG1 VAL C 574    10462  10230   9190    743    280    313       C
ATOM   4339  CG2 VAL C 574      32.103  33.534 -60.619  1.00 79.28           C
ANISOU 4339  CG2 VAL C 574    10457  10329   9339    798    365    469       C
ATOM   4340  N   LEU C 575      29.725  33.924 -56.916  1.00 68.50           N
ANISOU 4340  N   LEU C 575     9076   8804   8148    722    355    408       N
ATOM   4341  CA  LEU C 575      29.304  35.060 -56.104  1.00 68.58           C
ANISOU 4341  CA  LEU C 575     9050   8753   8253    723    404    439       C
ATOM   4342  C   LEU C 575      30.453  35.999 -55.755  1.00 68.51           C
ANISOU 4342  C   LEU C 575     9030   8684   8316    735    468    439       C
ATOM   4343  O   LEU C 575      31.508  35.566 -55.292  1.00 68.29           O
ANISOU 4343  O   LEU C 575     9034   8626   8286    723    466    374       O
ATOM   4344  CB  LEU C 575      28.617  34.571 -54.829  1.00 68.55           C
ANISOU 4344  CB  LEU C 575     9064   8710   8272    686    378    384       C
ATOM   4345  CG  LEU C 575      27.246  33.936 -55.053  1.00 68.70           C
ANISOU 4345  CG  LEU C 575     9081   8779   8243    674    326    399       C
ATOM   4346  CD1 LEU C 575      27.002  32.830 -54.047  1.00 68.58           C
ANISOU 4346  CD1 LEU C 575     9106   8742   8208    635    279    317       C
ATOM   4347  CD2 LEU C 575      26.157  34.993 -54.965  1.00 68.87           C
ANISOU 4347  CD2 LEU C 575     9051   8791   8326    686    358    474       C
ATOM   4348  N   GLY C 576      30.230  37.290 -55.979  1.00 86.35           N
ANISOU 4348  N   GLY C 576    11243  10925  10642    759    524    513       N
ATOM   4349  CA  GLY C 576      31.221  38.303 -55.674  1.00 86.01           C
ANISOU 4349  CA  GLY C 576    11184  10823  10675    771    591    518       C
ATOM   4350  C   GLY C 576      30.841  39.132 -54.463  1.00 85.48           C
ANISOU 4350  C   GLY C 576    11097  10679  10705    754    634    510       C
ATOM   4351  O   GLY C 576      30.261  38.621 -53.505  1.00 85.65           O
ANISOU 4351  O   GLY C 576    11136  10679  10730    723    605    461       O
ATOM   4352  N   ALA C 577      31.167  40.419 -54.508  1.00 74.65           N
ANISOU 4352  N   ALA C 577     9686   9265   9412    774    704    559       N
ATOM   4353  CA  ALA C 577      30.889  41.319 -53.395  1.00 73.80           C
ANISOU 4353  CA  ALA C 577     9557   9079   9403    758    755    551       C
ATOM   4354  C   ALA C 577      29.428  41.756 -53.375  1.00 74.44           C
ANISOU 4354  C   ALA C 577     9604   9166   9513    764    760    610       C
ATOM   4355  O   ALA C 577      28.810  41.833 -52.313  1.00 74.43           O
ANISOU 4355  O   ALA C 577     9603   9121   9555    738    765    578       O
ATOM   4356  CB  ALA C 577      31.806  42.531 -53.452  1.00 72.99           C
ANISOU 4356  CB  ALA C 577     9427   8926   9379    775    832    578       C
ATOM   4357  N   LYS C 578      28.880  42.043 -54.552  1.00 72.65           N
ANISOU 4357  N   LYS C 578     9347   8996   9262    799    760    697       N
ATOM   4358  CA  LYS C 578      27.497  42.494 -54.660  1.00 72.95           C
ANISOU 4358  CA  LYS C 578     9345   9046   9325    810    766    765       C
ATOM   4359  C   LYS C 578      26.711  41.690 -55.691  1.00 73.67           C
ANISOU 4359  C   LYS C 578     9437   9232   9321    821    702    805       C
ATOM   4360  O   LYS C 578      26.254  42.234 -56.696  1.00 73.93           O
ANISOU 4360  O   LYS C 578     9431   9311   9350    855    716    897       O
ATOM   4361  CB  LYS C 578      27.442  43.986 -55.003  1.00 72.77           C
ANISOU 4361  CB  LYS C 578     9267   8988   9393    843    847    853       C
ATOM   4362  CG  LYS C 578      27.971  44.897 -53.907  0.00 71.99           C
ANISOU 4362  CG  LYS C 578     9161   8791   9401    828    916    817       C
ATOM   4363  CD  LYS C 578      27.891  46.359 -54.316  0.00 71.75           C
ANISOU 4363  CD  LYS C 578     9075   8726   9462    863    999    907       C
ATOM   4364  CE  LYS C 578      28.391  47.272 -53.208  0.00 70.92           C
ANISOU 4364  CE  LYS C 578     8962   8520   9464    844   1071    867       C
ATOM   4365  NZ  LYS C 578      28.345  48.706 -53.605  0.00 70.69           N
ANISOU 4365  NZ  LYS C 578     8878   8450   9530    878   1156    954       N
ATOM   4366  N   GLY C 579      26.555  40.395 -55.435  1.00 68.84           N
ANISOU 4366  N   GLY C 579     8870   8653   8635    792    632    736       N
ATOM   4367  CA  GLY C 579      25.783  39.534 -56.312  1.00 69.24           C
ANISOU 4367  CA  GLY C 579     8925   8791   8591    795    567    760       C
ATOM   4368  C   GLY C 579      26.630  38.546 -57.090  1.00 69.55           C
ANISOU 4368  C   GLY C 579     9004   8887   8536    795    523    723       C
ATOM   4369  O   GLY C 579      27.858  38.624 -57.068  1.00 69.51           O
ANISOU 4369  O   GLY C 579     9018   8855   8539    799    546    690       O
ATOM   4370  N   PRO C 580      25.972  37.602 -57.781  1.00 92.85           N
ANISOU 4370  N   PRO C 580    11967  11916  11396    790    459    726       N
ATOM   4371  CA  PRO C 580      26.643  36.588 -58.602  1.00 92.85           C
ANISOU 4371  CA  PRO C 580    12004  11976  11298    788    415    691       C
ATOM   4372  C   PRO C 580      27.266  37.199 -59.853  1.00 92.98           C
ANISOU 4372  C   PRO C 580    11996  12036  11296    827    445    759       C
ATOM   4373  O   PRO C 580      26.912  38.314 -60.234  1.00 93.34           O
ANISOU 4373  O   PRO C 580    11992  12082  11391    855    491    846       O
ATOM   4374  CB  PRO C 580      25.501  35.643 -59.000  1.00 92.59           C
ANISOU 4374  CB  PRO C 580    11978  12015  11188    772    347    691       C
ATOM   4375  CG  PRO C 580      24.385  35.944 -58.049  1.00 92.90           C
ANISOU 4375  CG  PRO C 580    11996  12015  11286    755    349    700       C
ATOM   4376  CD  PRO C 580      24.516  37.397 -57.742  1.00 92.98           C
ANISOU 4376  CD  PRO C 580    11963  11966  11399    780    425    758       C
ATOM   4377  N   ILE C 581      28.182  36.469 -60.482  1.00 66.01           N
ANISOU 4377  N   ILE C 581     8615   8657   7809    828    423    721       N
ATOM   4378  CA  ILE C 581      28.866  36.962 -61.672  1.00 65.47           C
ANISOU 4378  CA  ILE C 581     8529   8632   7716    863    451    779       C
ATOM   4379  C   ILE C 581      28.873  35.927 -62.791  1.00 65.06           C
ANISOU 4379  C   ILE C 581     8501   8674   7547    862    397    769       C
ATOM   4380  O   ILE C 581      29.379  34.816 -62.625  1.00 64.79           O
ANISOU 4380  O   ILE C 581     8516   8643   7459    840    358    686       O
ATOM   4381  CB  ILE C 581      30.309  37.389 -61.355  1.00 65.34           C
ANISOU 4381  CB  ILE C 581     8525   8553   7748    872    500    748       C
ATOM   4382  CG1 ILE C 581      30.301  38.617 -60.444  1.00 65.13           C
ANISOU 4382  CG1 ILE C 581     8466   8441   7840    877    565    772       C
ATOM   4383  CG2 ILE C 581      31.070  37.682 -62.637  1.00 65.20           C
ANISOU 4383  CG2 ILE C 581     8496   8588   7690    905    522    798       C
ATOM   4384  CD1 ILE C 581      31.643  38.948 -59.850  1.00 64.89           C
ANISOU 4384  CD1 ILE C 581     8451   8341   7863    874    608    725       C
ATOM   4385  N   TYR C 582      28.308  36.308 -63.932  1.00 71.59           N
ANISOU 4385  N   TYR C 582     9291   9577   8333    886    395    855       N
ATOM   4386  CA  TYR C 582      28.174  35.411 -65.072  1.00 70.70           C
ANISOU 4386  CA  TYR C 582     9194   9562   8105    884    345    853       C
ATOM   4387  C   TYR C 582      28.993  35.905 -66.260  1.00 70.20           C
ANISOU 4387  C   TYR C 582     9115   9545   8011    919    377    908       C
ATOM   4388  O   TYR C 582      29.088  37.108 -66.500  1.00 70.44           O
ANISOU 4388  O   TYR C 582     9100   9561   8102    951    432    989       O
ATOM   4389  CB  TYR C 582      26.700  35.272 -65.464  1.00 70.25           C
ANISOU 4389  CB  TYR C 582     9109   9574   8010    877    304    904       C
ATOM   4390  CG  TYR C 582      25.868  34.529 -64.443  1.00 70.01           C
ANISOU 4390  CG  TYR C 582     9101   9514   7987    839    261    841       C
ATOM   4391  CD1 TYR C 582      25.868  33.139 -64.401  1.00 69.79           C
ANISOU 4391  CD1 TYR C 582     9123   9512   7881    805    201    755       C
ATOM   4392  CD2 TYR C 582      25.083  35.217 -63.520  1.00 69.94           C
ANISOU 4392  CD2 TYR C 582     9061   9448   8064    836    282    868       C
ATOM   4393  CE1 TYR C 582      25.106  32.452 -63.472  1.00 69.60           C
ANISOU 4393  CE1 TYR C 582     9119   9461   7866    770    162    701       C
ATOM   4394  CE2 TYR C 582      24.323  34.541 -62.584  1.00 69.99           C
ANISOU 4394  CE2 TYR C 582     9088   9429   8078    801    244    813       C
ATOM   4395  CZ  TYR C 582      24.340  33.160 -62.562  1.00 69.89           C
ANISOU 4395  CZ  TYR C 582     9125   9444   7986    768    183    730       C
ATOM   4396  OH  TYR C 582      23.580  32.491 -61.630  1.00 69.87           O
ANISOU 4396  OH  TYR C 582     9140   9415   7992    734    146    677       O
ATOM   4397  N   LYS C 583      29.588  34.972 -66.998  1.00 56.98           N
ANISOU 4397  N   LYS C 583     7478   7926   6246    913    345    863       N
ATOM   4398  CA  LYS C 583      30.385  35.312 -68.175  1.00 56.95           C
ANISOU 4398  CA  LYS C 583     7464   7974   6201    944    372    909       C
ATOM   4399  C   LYS C 583      30.196  34.308 -69.310  1.00 56.79           C
ANISOU 4399  C   LYS C 583     7464   8059   6054    935    320    895       C
ATOM   4400  O   LYS C 583      29.750  33.181 -69.089  1.00 56.40           O
ANISOU 4400  O   LYS C 583     7450   8029   5949    901    264    826       O
ATOM   4401  CB  LYS C 583      31.871  35.416 -67.815  1.00 56.99           C
ANISOU 4401  CB  LYS C 583     7495   7912   6246    952    413    860       C
ATOM   4402  CG  LYS C 583      32.254  36.690 -67.078  1.00 57.27           C
ANISOU 4402  CG  LYS C 583     7499   7861   6402    971    480    897       C
ATOM   4403  CD  LYS C 583      33.757  36.774 -66.868  1.00 57.21           C
ANISOU 4403  CD  LYS C 583     7514   7799   6423    978    518    852       C
ATOM   4404  CE  LYS C 583      34.157  38.113 -66.271  1.00 57.30           C
ANISOU 4404  CE  LYS C 583     7490   7730   6551    997    589    895       C
ATOM   4405  NZ  LYS C 583      35.631  38.225 -66.097  1.00 57.36           N
ANISOU 4405  NZ  LYS C 583     7518   7690   6588   1003    626    854       N
ATOM   4406  N   TYR C 584      30.542  34.725 -70.524  1.00 66.05           N
ANISOU 4406  N   TYR C 584     8614   9300   7181    964    340    960       N
ATOM   4407  CA  TYR C 584      30.434  33.864 -71.697  1.00 66.17           C
ANISOU 4407  CA  TYR C 584     8647   9422   7073    956    296    950       C
ATOM   4408  C   TYR C 584      31.759  33.816 -72.452  1.00 66.37           C
ANISOU 4408  C   TYR C 584     8691   9463   7062    977    325    939       C
ATOM   4409  O   TYR C 584      32.527  34.778 -72.423  1.00 66.24           O
ANISOU 4409  O   TYR C 584     8653   9403   7111   1007    384    982       O
ATOM   4410  CB  TYR C 584      29.326  34.364 -72.630  1.00 66.03           C
ANISOU 4410  CB  TYR C 584     8577   9499   7013    970    283   1053       C
ATOM   4411  CG  TYR C 584      29.705  35.594 -73.426  1.00 66.32           C
ANISOU 4411  CG  TYR C 584     8564   9559   7075   1015    340   1161       C
ATOM   4412  CD1 TYR C 584      30.120  35.489 -74.748  1.00 66.29           C
ANISOU 4412  CD1 TYR C 584     8557   9649   6982   1031    339   1195       C
ATOM   4413  CD2 TYR C 584      29.655  36.858 -72.853  1.00 66.52           C
ANISOU 4413  CD2 TYR C 584     8547   9515   7215   1041    396   1229       C
ATOM   4414  CE1 TYR C 584      30.472  36.609 -75.478  1.00 66.40           C
ANISOU 4414  CE1 TYR C 584     8525   9686   7020   1073    392   1297       C
ATOM   4415  CE2 TYR C 584      30.004  37.984 -73.576  1.00 66.67           C
ANISOU 4415  CE2 TYR C 584     8519   9551   7261   1083    451   1329       C
ATOM   4416  CZ  TYR C 584      30.412  37.853 -74.887  1.00 66.72           C
ANISOU 4416  CZ  TYR C 584     8522   9652   7177   1099    448   1365       C
ATOM   4417  OH  TYR C 584      30.762  38.969 -75.611  1.00 67.04           O
ANISOU 4417  OH  TYR C 584     8516   9711   7245   1142    503   1468       O
ATOM   4418  N   PRO C 585      32.034  32.692 -73.132  1.00 79.58           N
ANISOU 4418  N   PRO C 585    10406  11200   8633    959    287    878       N
ATOM   4419  CA  PRO C 585      33.236  32.575 -73.962  1.00 79.74           C
ANISOU 4419  CA  PRO C 585    10444  11246   8607    978    313    867       C
ATOM   4420  C   PRO C 585      32.986  33.087 -75.378  1.00 80.13           C
ANISOU 4420  C   PRO C 585    10455  11404   8589   1003    321    961       C
ATOM   4421  O   PRO C 585      32.097  32.578 -76.061  1.00 80.21           O
ANISOU 4421  O   PRO C 585    10460  11505   8512    987    274    973       O
ATOM   4422  CB  PRO C 585      33.502  31.061 -73.987  1.00 79.34           C
ANISOU 4422  CB  PRO C 585    10455  11212   8478    944    265    755       C
ATOM   4423  CG  PRO C 585      32.349  30.410 -73.225  1.00 79.20           C
ANISOU 4423  CG  PRO C 585    10449  11183   8461    907    211    714       C
ATOM   4424  CD  PRO C 585      31.273  31.435 -73.102  1.00 79.38           C
ANISOU 4424  CD  PRO C 585    10414  11216   8532    919    219    810       C
ATOM   4425  N   ASP C 586      33.757  34.080 -75.813  1.00 79.58           N
ANISOU 4425  N   ASP C 586    10356  11325   8555   1042    379   1028       N
ATOM   4426  CA  ASP C 586      33.577  34.640 -77.149  1.00 80.10           C
ANISOU 4426  CA  ASP C 586    10382  11492   8560   1069    392   1125       C
ATOM   4427  C   ASP C 586      34.267  33.791 -78.215  1.00 80.50           C
ANISOU 4427  C   ASP C 586    10468  11621   8498   1064    377   1082       C
ATOM   4428  O   ASP C 586      34.683  32.662 -77.950  1.00 80.25           O
ANISOU 4428  O   ASP C 586    10491  11572   8428   1037    348    976       O
ATOM   4429  CB  ASP C 586      34.054  36.098 -77.216  1.00 80.40           C
ANISOU 4429  CB  ASP C 586    10371  11491   8686   1112    464   1223       C
ATOM   4430  CG  ASP C 586      35.567  36.227 -77.204  1.00 80.59           C
ANISOU 4430  CG  ASP C 586    10419  11463   8740   1130    512   1188       C
ATOM   4431  OD1 ASP C 586      36.190  36.068 -78.274  1.00 80.89           O
ANISOU 4431  OD1 ASP C 586    10462  11568   8703   1145    521   1202       O
ATOM   4432  OD2 ASP C 586      36.135  36.509 -76.129  1.00 80.60           O
ANISOU 4432  OD2 ASP C 586    10430  11356   8838   1129    542   1149       O
ATOM   4433  N   VAL C 587      34.386  34.343 -79.419  1.00108.71           N
ANISOU 4433  N   VAL C 587    14008  15279  12019   1092    399   1166       N
ATOM   4434  CA  VAL C 587      34.963  33.621 -80.549  0.00108.63           C
ANISOU 4434  CA  VAL C 587    14026  15356  11894   1089    387   1136       C
ATOM   4435  C   VAL C 587      36.443  33.293 -80.355  1.00108.47           C
ANISOU 4435  C   VAL C 587    14048  15272  11893   1096    422   1062       C
ATOM   4436  O   VAL C 587      36.960  32.353 -80.957  1.00108.60           O
ANISOU 4436  O   VAL C 587    14106  15334  11823   1083    405    996       O
ATOM   4437  CB  VAL C 587      34.779  34.400 -81.869  0.00108.81           C
ANISOU 4437  CB  VAL C 587    13998  15485  11861   1120    407   1252       C
ATOM   4438  CG1 VAL C 587      33.310  34.439 -82.260  0.00108.74           C
ANISOU 4438  CG1 VAL C 587    13952  15564  11801   1106    361   1313       C
ATOM   4439  CG2 VAL C 587      35.342  35.807 -81.740  0.00109.10           C
ANISOU 4439  CG2 VAL C 587    13990  15464  12000   1165    479   1344       C
ATOM   4440  N   GLN C 588      37.119  34.069 -79.514  1.00 76.49           N
ANISOU 4440  N   GLN C 588     9988  11117   7957   1117    471   1073       N
ATOM   4441  CA  GLN C 588      38.529  33.830 -79.222  1.00 75.91           C
ANISOU 4441  CA  GLN C 588     9951  10978   7915   1124    505   1008       C
ATOM   4442  C   GLN C 588      38.703  33.100 -77.893  1.00 75.30           C
ANISOU 4442  C   GLN C 588     9917  10803   7892   1094    484    902       C
ATOM   4443  O   GLN C 588      39.768  33.158 -77.277  1.00 75.37           O
ANISOU 4443  O   GLN C 588     9945  10730   7963   1101    517    859       O
ATOM   4444  CB  GLN C 588      39.311  35.146 -79.219  1.00 76.17           C
ANISOU 4444  CB  GLN C 588     9944  10961   8035   1164    577   1085       C
ATOM   4445  CG  GLN C 588      39.431  35.798 -80.589  1.00 76.36           C
ANISOU 4445  CG  GLN C 588     9931  11079   8003   1197    606   1183       C
ATOM   4446  CD  GLN C 588      40.180  37.116 -80.547  0.00 76.59           C
ANISOU 4446  CD  GLN C 588     9920  11055   8126   1237    680   1261       C
ATOM   4447  OE1 GLN C 588      39.680  38.111 -80.021  0.00 76.70           O
ANISOU 4447  OE1 GLN C 588     9891  11021   8229   1250    704   1328       O
ATOM   4448  NE2 GLN C 588      41.387  37.129 -81.100  0.00 76.65           N
ANISOU 4448  NE2 GLN C 588     9941  11067   8116   1256    717   1252       N
ATOM   4449  N   ASN C 589      37.642  32.421 -77.460  1.00 64.54           N
ANISOU 4449  N   ASN C 589     8567   9450   6505   1061    428    865       N
ATOM   4450  CA  ASN C 589      37.647  31.629 -76.228  1.00 64.21           C
ANISOU 4450  CA  ASN C 589     8567   9327   6505   1030    401    766       C
ATOM   4451  C   ASN C 589      37.964  32.410 -74.951  1.00 64.10           C
ANISOU 4451  C   ASN C 589     8538   9197   6620   1038    437    770       C
ATOM   4452  O   ASN C 589      38.246  31.817 -73.909  1.00 63.78           O
ANISOU 4452  O   ASN C 589     8532   9081   6619   1016    424    688       O
ATOM   4453  CB  ASN C 589      38.581  30.420 -76.355  1.00 64.01           C
ANISOU 4453  CB  ASN C 589     8600   9297   6424   1015    388    663       C
ATOM   4454  CG  ASN C 589      38.000  29.323 -77.226  1.00 63.60           C
ANISOU 4454  CG  ASN C 589     8574   9341   6250    990    336    624       C
ATOM   4455  OD1 ASN C 589      38.585  28.944 -78.240  1.00 63.47           O
ANISOU 4455  OD1 ASN C 589     8574   9387   6156    997    344    613       O
ATOM   4456  ND2 ASN C 589      36.843  28.805 -76.830  1.00 63.34           N
ANISOU 4456  ND2 ASN C 589     8546   9321   6199    958    285    602       N
ATOM   4457  N   GLU C 590      37.911  33.734 -75.032  1.00 56.39           N
ANISOU 4457  N   GLU C 590     7510   8206   5709   1068    484    865       N
ATOM   4458  CA  GLU C 590      38.157  34.576 -73.868  1.00 56.20           C
ANISOU 4458  CA  GLU C 590     7468   8076   5809   1074    523    874       C
ATOM   4459  C   GLU C 590      36.837  34.897 -73.170  1.00 56.03           C
ANISOU 4459  C   GLU C 590     7421   8036   5831   1059    500    903       C
ATOM   4460  O   GLU C 590      35.815  35.101 -73.823  1.00 55.74           O
ANISOU 4460  O   GLU C 590     7354   8072   5751   1063    480    968       O
ATOM   4461  CB  GLU C 590      38.885  35.857 -74.281  1.00 56.23           C
ANISOU 4461  CB  GLU C 590     7431   8064   5871   1114    592    957       C
ATOM   4462  CG  GLU C 590      39.430  36.670 -73.118  1.00 56.96           C
ANISOU 4462  CG  GLU C 590     7510   8042   6089   1118    639    951       C
ATOM   4463  CD  GLU C 590      40.362  37.778 -73.567  0.00 57.16           C
ANISOU 4463  CD  GLU C 590     7503   8050   6166   1155    709   1018       C
ATOM   4464  OE1 GLU C 590      41.186  37.535 -74.474  0.00 57.12           O
ANISOU 4464  OE1 GLU C 590     7510   8091   6103   1171    721   1018       O
ATOM   4465  OE2 GLU C 590      40.269  38.895 -73.014  0.00 57.35           O
ANISOU 4465  OE2 GLU C 590     7489   8011   6290   1167    754   1069       O
ATOM   4466  N   CYS C 591      36.857  34.928 -71.841  1.00 71.92           N
ANISOU 4466  N   CYS C 591     9445   9954   7928   1041    503    854       N
ATOM   4467  CA  CYS C 591      35.636  35.149 -71.071  1.00 72.17           C
ANISOU 4467  CA  CYS C 591     9457   9961   8003   1024    483    870       C
ATOM   4468  C   CYS C 591      35.287  36.629 -70.928  1.00 72.06           C
ANISOU 4468  C   CYS C 591     9385   9916   8080   1051    536    969       C
ATOM   4469  O   CYS C 591      36.035  37.403 -70.332  1.00 72.26           O
ANISOU 4469  O   CYS C 591     9399   9863   8195   1064    588    973       O
ATOM   4470  CB  CYS C 591      35.735  34.486 -69.695  1.00 72.58           C
ANISOU 4470  CB  CYS C 591     9548   9931   8100    991    461    773       C
ATOM   4471  SG  CYS C 591      35.623  32.679 -69.730  1.00 73.83           S
ANISOU 4471  SG  CYS C 591     9770  10127   8156    954    387    664       S
ATOM   4472  N   ARG C 592      34.139  37.008 -71.483  1.00 55.25           N
ANISOU 4472  N   ARG C 592     7216   7849   5928   1060    522   1048       N
ATOM   4473  CA  ARG C 592      33.647  38.380 -71.414  1.00 55.02           C
ANISOU 4473  CA  ARG C 592     7127   7795   5982   1086    570   1150       C
ATOM   4474  C   ARG C 592      32.406  38.462 -70.522  1.00 54.66           C
ANISOU 4474  C   ARG C 592     7066   7719   5983   1066    548   1153       C
ATOM   4475  O   ARG C 592      31.655  37.493 -70.412  1.00 54.31           O
ANISOU 4475  O   ARG C 592     7046   7712   5878   1037    487   1107       O
ATOM   4476  CB  ARG C 592      33.323  38.898 -72.818  1.00 55.13           C
ANISOU 4476  CB  ARG C 592     7098   7908   5939   1118    580   1257       C
ATOM   4477  CG  ARG C 592      34.348  39.868 -73.389  1.00 55.52           C
ANISOU 4477  CG  ARG C 592     7123   7946   6027   1157    648   1318       C
ATOM   4478  CD  ARG C 592      35.642  39.169 -73.773  1.00 55.66           C
ANISOU 4478  CD  ARG C 592     7186   7972   5989   1155    648   1249       C
ATOM   4479  NE  ARG C 592      36.604  40.099 -74.359  1.00 56.19           N
ANISOU 4479  NE  ARG C 592     7227   8032   6092   1191    713   1311       N
ATOM   4480  CZ  ARG C 592      37.603  40.664 -73.689  0.00 56.35           C
ANISOU 4480  CZ  ARG C 592     7249   7959   6202   1199    766   1290       C
ATOM   4481  NH1 ARG C 592      37.779  40.391 -72.403  0.00 56.39           N
ANISOU 4481  NH1 ARG C 592     7282   7875   6269   1172    760   1207       N
ATOM   4482  NH2 ARG C 592      38.428  41.499 -74.304  0.00 56.47           N
ANISOU 4482  NH2 ARG C 592     7239   7974   6245   1232    824   1351       N
ATOM   4483  N   PRO C 593      32.188  39.623 -69.879  1.00 52.67           N
ANISOU 4483  N   PRO C 593     6774   7397   5842   1081    600   1206       N
ATOM   4484  CA  PRO C 593      31.037  39.804 -68.985  1.00 52.54           C
ANISOU 4484  CA  PRO C 593     6741   7343   5880   1065    587   1212       C
ATOM   4485  C   PRO C 593      29.704  39.841 -69.729  1.00 52.74           C
ANISOU 4485  C   PRO C 593     6728   7457   5854   1071    554   1291       C
ATOM   4486  O   PRO C 593      29.668  40.128 -70.926  1.00 53.19           O
ANISOU 4486  O   PRO C 593     6757   7596   5858   1097    559   1368       O
ATOM   4487  CB  PRO C 593      31.313  41.162 -68.334  1.00 52.25           C
ANISOU 4487  CB  PRO C 593     6666   7214   5973   1085    663   1258       C
ATOM   4488  CG  PRO C 593      32.172  41.879 -69.313  1.00 52.50           C
ANISOU 4488  CG  PRO C 593     6674   7271   6004   1123    712   1325       C
ATOM   4489  CD  PRO C 593      33.044  40.822 -69.920  1.00 52.53           C
ANISOU 4489  CD  PRO C 593     6727   7326   5908   1113    677   1259       C
ATOM   4490  N   CYS C 594      28.620  39.556 -69.014  1.00 68.87           N
ANISOU 4490  N   CYS C 594     8769   9487   7913   1047    520   1273       N
ATOM   4491  CA  CYS C 594      27.286  39.542 -69.604  1.00 68.67           C
ANISOU 4491  CA  CYS C 594     8707   9543   7843   1049    485   1343       C
ATOM   4492  C   CYS C 594      26.608  40.902 -69.479  1.00 68.68           C
ANISOU 4492  C   CYS C 594     8641   9515   7939   1079    537   1452       C
ATOM   4493  O   CYS C 594      27.179  41.842 -68.926  1.00 68.92           O
ANISOU 4493  O   CYS C 594     8657   9459   8071   1096    603   1468       O
ATOM   4494  CB  CYS C 594      26.421  38.466 -68.942  1.00 68.25           C
ANISOU 4494  CB  CYS C 594     8684   9495   7752   1006    418   1269       C
ATOM   4495  SG  CYS C 594      27.108  36.797 -69.025  1.00 79.51           S
ANISOU 4495  SG  CYS C 594    10188  10950   9072    969    356   1139       S
ATOM   4496  N   HIS C 595      25.387  40.997 -69.997  1.00 66.80           N
ANISOU 4496  N   HIS C 595     8363   9350   7669   1084    510   1526       N
ATOM   4497  CA  HIS C 595      24.614  42.232 -69.937  1.00 67.52           C
ANISOU 4497  CA  HIS C 595     8387   9421   7847   1114    557   1636       C
ATOM   4498  C   HIS C 595      24.170  42.492 -68.499  1.00 68.28           C
ANISOU 4498  C   HIS C 595     8485   9411   8047   1096    575   1595       C
ATOM   4499  O   HIS C 595      23.914  41.556 -67.742  1.00 68.44           O
ANISOU 4499  O   HIS C 595     8547   9412   8043   1057    529   1503       O
ATOM   4500  CB  HIS C 595      23.405  42.142 -70.872  1.00 67.74           C
ANISOU 4500  CB  HIS C 595     8372   9563   7805   1122    514   1723       C
ATOM   4501  CG  HIS C 595      22.823  43.474 -71.248  1.00 67.69           C
ANISOU 4501  CG  HIS C 595     8289   9560   7869   1164    568   1861       C
ATOM   4502  ND1 HIS C 595      21.920  44.141 -70.448  1.00 67.63           N
ANISOU 4502  ND1 HIS C 595     8244   9494   7959   1168    593   1900       N
ATOM   4503  CD2 HIS C 595      23.010  44.245 -72.338  1.00 67.70           C
ANISOU 4503  CD2 HIS C 595     8245   9619   7859   1205    601   1969       C
ATOM   4504  CE1 HIS C 595      21.581  45.274 -71.032  1.00 67.66           C
ANISOU 4504  CE1 HIS C 595     8181   9515   8011   1211    642   2028       C
ATOM   4505  NE2 HIS C 595      22.223  45.368 -72.180  1.00 67.91           N
ANISOU 4505  NE2 HIS C 595     8206   9618   7978   1234    647   2075       N
ATOM   4506  N   GLU C 596      24.082  43.766 -68.129  1.00 85.48           N
ANISOU 4506  N   GLU C 596    10618  11522  10340   1123    646   1665       N
ATOM   4507  CA  GLU C 596      23.791  44.153 -66.751  1.00 86.01           C
ANISOU 4507  CA  GLU C 596    10685  11480  10514   1108    677   1626       C
ATOM   4508  C   GLU C 596      22.377  43.782 -66.302  1.00 86.40           C
ANISOU 4508  C   GLU C 596    10721  11549  10558   1087    633   1630       C
ATOM   4509  O   GLU C 596      22.107  43.686 -65.105  1.00 86.92           O
ANISOU 4509  O   GLU C 596    10805  11538  10684   1062    637   1568       O
ATOM   4510  CB  GLU C 596      24.031  45.654 -66.557  1.00 86.27           C
ANISOU 4510  CB  GLU C 596    10670  11438  10672   1143    769   1704       C
ATOM   4511  CG  GLU C 596      23.235  46.537 -67.503  1.00 86.70           C
ANISOU 4511  CG  GLU C 596    10652  11550  10739   1185    794   1847       C
ATOM   4512  CD  GLU C 596      23.491  48.015 -67.279  1.00 87.07           C
ANISOU 4512  CD  GLU C 596    10651  11514  10916   1220    890   1922       C
ATOM   4513  OE1 GLU C 596      24.653  48.450 -67.426  1.00 87.03           O
ANISOU 4513  OE1 GLU C 596    10656  11471  10939   1234    936   1913       O
ATOM   4514  OE2 GLU C 596      22.529  48.742 -66.953  1.00 87.27           O
ANISOU 4514  OE2 GLU C 596    10628  11511  11018   1234    920   1988       O
ATOM   4515  N   ASN C 597      21.482  43.569 -67.262  1.00 96.35           N
ANISOU 4515  N   ASN C 597    11950  12914  11746   1097    592   1702       N
ATOM   4516  CA  ASN C 597      20.093  43.245 -66.949  1.00 96.55           C
ANISOU 4516  CA  ASN C 597    11955  12967  11763   1079    549   1716       C
ATOM   4517  C   ASN C 597      19.764  41.752 -67.055  1.00 96.98           C
ANISOU 4517  C   ASN C 597    12056  13090  11701   1037    459   1633       C
ATOM   4518  O   ASN C 597      18.598  41.362 -66.980  1.00 97.29           O
ANISOU 4518  O   ASN C 597    12079  13171  11714   1021    415   1646       O
ATOM   4519  CB  ASN C 597      19.139  44.068 -67.825  1.00 96.28           C
ANISOU 4519  CB  ASN C 597    11844  13000  11736   1116    564   1858       C
ATOM   4520  CG  ASN C 597      19.209  45.557 -67.528  1.00 96.12           C
ANISOU 4520  CG  ASN C 597    11773  12900  11850   1155    656   1942       C
ATOM   4521  OD1 ASN C 597      20.129  46.025 -66.859  1.00 95.89           O
ANISOU 4521  OD1 ASN C 597    11764  12774  11897   1157    711   1898       O
ATOM   4522  ND2 ASN C 597      18.234  46.308 -68.029  1.00 96.20           N
ANISOU 4522  ND2 ASN C 597    11714  12950  11888   1186    673   2064       N
ATOM   4523  N   CYS C 598      20.792  40.922 -67.222  1.00 89.85           N
ANISOU 4523  N   CYS C 598    11211  12196  10731   1020    435   1547       N
ATOM   4524  CA  CYS C 598      20.604  39.473 -67.316  1.00 89.79           C
ANISOU 4524  CA  CYS C 598    11254  12245  10617    979    354   1460       C
ATOM   4525  C   CYS C 598      20.443  38.828 -65.941  1.00 90.24           C
ANISOU 4525  C   CYS C 598    11354  12222  10711    940    335   1356       C
ATOM   4526  O   CYS C 598      21.085  39.236 -64.972  1.00 90.21           O
ANISOU 4526  O   CYS C 598    11367  12118  10792    939    380   1313       O
ATOM   4527  CB  CYS C 598      21.758  38.818 -68.079  1.00 89.37           C
ANISOU 4527  CB  CYS C 598    11245  12234  10478    977    338   1411       C
ATOM   4528  SG  CYS C 598      21.828  39.232 -69.835  1.00 92.81           S
ANISOU 4528  SG  CYS C 598    11638  12793  10834   1014    341   1521       S
ATOM   4529  N   THR C 599      19.593  37.807 -65.874  1.00101.47           N
ANISOU 4529  N   THR C 599    12793  13693  12067    906    266   1315       N
ATOM   4530  CA  THR C 599      19.211  37.200 -64.603  1.00101.95           C
ANISOU 4530  CA  THR C 599    12887  13688  12161    868    244   1230       C
ATOM   4531  C   THR C 599      20.056  35.986 -64.226  1.00102.09           C
ANISOU 4531  C   THR C 599    12978  13686  12125    835    207   1106       C
ATOM   4532  O   THR C 599      20.629  35.938 -63.137  1.00102.16           O
ANISOU 4532  O   THR C 599    13019  13604  12193    821    229   1036       O
ATOM   4533  CB  THR C 599      17.730  36.780 -64.617  1.00101.93           C
ANISOU 4533  CB  THR C 599    12860  13742  12128    849    192   1255       C
ATOM   4534  OG1 THR C 599      17.482  35.947 -65.757  1.00101.83           O
ANISOU 4534  OG1 THR C 599    12854  13844  11994    838    132   1259       O
ATOM   4535  CG2 THR C 599      16.833  38.004 -64.687  1.00101.93           C
ANISOU 4535  CG2 THR C 599    12787  13739  12202    880    234   1371       C
ATOM   4536  N   GLN C 600      20.122  35.006 -65.123  1.00105.86           N
ANISOU 4536  N   GLN C 600    13480  14250  12490    820    152   1079       N
ATOM   4537  CA  GLN C 600      20.752  33.728 -64.807  1.00105.63           C
ANISOU 4537  CA  GLN C 600    13520  14210  12406    786    112    963       C
ATOM   4538  C   GLN C 600      21.840  33.305 -65.796  1.00105.43           C
ANISOU 4538  C   GLN C 600    13524  14232  12304    796    107    941       C
ATOM   4539  O   GLN C 600      22.974  33.046 -65.400  1.00105.50           O
ANISOU 4539  O   GLN C 600    13574  14185  12327    793    125    873       O
ATOM   4540  CB  GLN C 600      19.690  32.630 -64.696  1.00105.40           C
ANISOU 4540  CB  GLN C 600    13506  14226  12315    746     41    921       C
ATOM   4541  CG  GLN C 600      18.825  32.715 -63.448  0.00105.72           C
ANISOU 4541  CG  GLN C 600    13539  14202  12428    727     40    906       C
ATOM   4542  CD  GLN C 600      17.794  31.609 -63.397  0.00105.94           C
ANISOU 4542  CD  GLN C 600    13581  14279  12393    687    -30    866       C
ATOM   4543  OE1 GLN C 600      17.479  30.996 -64.417  0.00106.00           O
ANISOU 4543  OE1 GLN C 600    13588  14380  12306    678    -75    875       O
ATOM   4544  NE2 GLN C 600      17.266  31.340 -62.208  0.00106.05           N
ANISOU 4544  NE2 GLN C 600    13608  14230  12457    662    -39    821       N
ATOM   4545  N   GLY C 601      21.492  33.236 -67.079  1.00115.54           N
ANISOU 4545  N   GLY C 601    14780  15617  13502    806     84    998       N
ATOM   4546  CA  GLY C 601      22.410  32.746 -68.096  1.00115.27           C
ANISOU 4546  CA  GLY C 601    14774  15641  13383    812     75    975       C
ATOM   4547  C   GLY C 601      23.038  33.825 -68.956  1.00115.16           C
ANISOU 4547  C   GLY C 601    14723  15650  13383    857    128   1063       C
ATOM   4548  O   GLY C 601      22.725  35.003 -68.807  1.00115.62           O
ANISOU 4548  O   GLY C 601    14730  15681  13519    886    173   1148       O
ATOM   4549  N   CYS C 602      23.921  33.423 -69.865  1.00 82.47           N
ANISOU 4549  N   CYS C 602    10607  11560   9169    863    125   1043       N
ATOM   4550  CA  CYS C 602      24.597  34.385 -70.728  1.00 82.36           C
ANISOU 4550  CA  CYS C 602    10561  11570   9162    906    175   1124       C
ATOM   4551  C   CYS C 602      24.475  34.106 -72.232  1.00 81.96           C
ANISOU 4551  C   CYS C 602    10498  11648   8996    913    148   1168       C
ATOM   4552  O   CYS C 602      23.793  34.843 -72.946  1.00 82.32           O
ANISOU 4552  O   CYS C 602    10486  11758   9032    936    155   1274       O
ATOM   4553  CB  CYS C 602      26.068  34.516 -70.342  1.00 82.63           C
ANISOU 4553  CB  CYS C 602    10630  11526   9239    918    221   1072       C
ATOM   4554  SG  CYS C 602      26.802  36.062 -70.892  1.00 83.56           S
ANISOU 4554  SG  CYS C 602    10697  11628   9422    972    302   1179       S
ATOM   4555  N   LYS C 603      25.151  33.057 -72.701  1.00 76.15           N
ANISOU 4555  N   LYS C 603     9814  10948   8174    894    119   1089       N
ATOM   4556  CA  LYS C 603      25.273  32.738 -74.133  1.00 75.56           C
ANISOU 4556  CA  LYS C 603     9735  10990   7985    898     98   1116       C
ATOM   4557  C   LYS C 603      26.077  33.773 -74.928  1.00 75.29           C
ANISOU 4557  C   LYS C 603     9668  10973   7964    945    156   1199       C
ATOM   4558  O   LYS C 603      27.042  33.426 -75.608  1.00 75.11           O
ANISOU 4558  O   LYS C 603     9675  10981   7884    951    165   1169       O
ATOM   4559  CB  LYS C 603      23.908  32.499 -74.796  1.00 75.71           C
ANISOU 4559  CB  LYS C 603     9720  11117   7931    882     46   1166       C
ATOM   4560  CG  LYS C 603      23.326  31.113 -74.575  0.00 75.35           C
ANISOU 4560  CG  LYS C 603     9717  11097   7816    830    -23   1069       C
ATOM   4561  CD  LYS C 603      22.072  30.920 -75.413  0.00 75.22           C
ANISOU 4561  CD  LYS C 603     9662  11200   7716    814    -73   1124       C
ATOM   4562  CE  LYS C 603      21.525  29.509 -75.288  0.00 74.84           C
ANISOU 4562  CE  LYS C 603     9659  11184   7595    761   -141   1025       C
ATOM   4563  NZ  LYS C 603      20.317  29.312 -76.138  0.00 74.74           N
ANISOU 4563  NZ  LYS C 603     9607  11293   7496    742   -191   1077       N
ATOM   4564  N   GLY C 604      25.674  35.038 -74.847  1.00 75.99           N
ANISOU 4564  N   GLY C 604     9698  11045   8130    978    198   1305       N
ATOM   4565  CA  GLY C 604      26.347  36.101 -75.574  1.00 75.52           C
ANISOU 4565  CA  GLY C 604     9602  10999   8092   1023    256   1394       C
ATOM   4566  C   GLY C 604      26.357  37.419 -74.823  1.00 75.56           C
ANISOU 4566  C   GLY C 604     9565  10910   8233   1054    321   1462       C
ATOM   4567  O   GLY C 604      25.929  37.480 -73.671  1.00 75.97           O
ANISOU 4567  O   GLY C 604     9621  10881   8363   1039    321   1429       O
ATOM   4568  N   PRO C 605      26.849  38.485 -75.473  1.00 55.24           N
ANISOU 4568  N   PRO C 605     6952   8349   5690   1097    377   1555       N
ATOM   4569  CA  PRO C 605      26.942  39.818 -74.865  1.00 55.32           C
ANISOU 4569  CA  PRO C 605     6919   8269   5831   1129    447   1625       C
ATOM   4570  C   PRO C 605      25.625  40.590 -74.896  1.00 55.50           C
ANISOU 4570  C   PRO C 605     6876   8317   5894   1144    450   1731       C
ATOM   4571  O   PRO C 605      25.386  41.425 -74.022  1.00 55.64           O
ANISOU 4571  O   PRO C 605     6868   8245   6028   1156    493   1759       O
ATOM   4572  CB  PRO C 605      27.974  40.523 -75.746  1.00 55.47           C
ANISOU 4572  CB  PRO C 605     6921   8307   5848   1168    501   1684       C
ATOM   4573  CG  PRO C 605      27.806  39.891 -77.082  1.00 55.55           C
ANISOU 4573  CG  PRO C 605     6932   8454   5720   1165    456   1706       C
ATOM   4574  CD  PRO C 605      27.444  38.451 -76.821  1.00 55.36           C
ANISOU 4574  CD  PRO C 605     6962   8457   5614   1116    381   1594       C
ATOM   4575  N   GLU C 606      24.785  40.317 -75.889  1.00 60.44           N
ANISOU 4575  N   GLU C 606     7474   9064   6426   1143    405   1789       N
ATOM   4576  CA  GLU C 606      23.535  41.051 -76.053  1.00 60.30           C
ANISOU 4576  CA  GLU C 606     7389   9084   6440   1160    406   1901       C
ATOM   4577  C   GLU C 606      22.455  40.563 -75.091  1.00 60.58           C
ANISOU 4577  C   GLU C 606     7430   9088   6500   1126    364   1855       C
ATOM   4578  O   GLU C 606      22.530  39.452 -74.567  1.00 60.49           O
ANISOU 4578  O   GLU C 606     7475   9059   6447   1085    317   1740       O
ATOM   4579  CB  GLU C 606      23.045  40.954 -77.500  1.00 60.02           C
ANISOU 4579  CB  GLU C 606     7317   9197   6289   1171    373   1985       C
ATOM   4580  CG  GLU C 606      24.092  41.347 -78.532  1.00 60.01           C
ANISOU 4580  CG  GLU C 606     7312   9241   6250   1203    410   2029       C
ATOM   4581  CD  GLU C 606      24.616  42.755 -78.328  0.00 60.11           C
ANISOU 4581  CD  GLU C 606     7283   9172   6384   1250    497   2114       C
ATOM   4582  OE1 GLU C 606      23.797  43.671 -78.103  0.00 60.08           O
ANISOU 4582  OE1 GLU C 606     7221   9149   6460   1273    525   2209       O
ATOM   4583  OE2 GLU C 606      25.850  42.945 -78.388  0.00 60.19           O
ANISOU 4583  OE2 GLU C 606     7318   9136   6414   1264    540   2085       O
ATOM   4584  N   LEU C 607      21.452  41.407 -74.868  1.00 65.38           N
ANISOU 4584  N   LEU C 607     7977   9686   7177   1145    383   1948       N
ATOM   4585  CA  LEU C 607      20.362  41.106 -73.945  1.00 65.68           C
ANISOU 4585  CA  LEU C 607     8013   9692   7252   1118    351   1920       C
ATOM   4586  C   LEU C 607      19.540  39.907 -74.410  1.00 65.94           C
ANISOU 4586  C   LEU C 607     8061   9830   7162   1079    264   1881       C
ATOM   4587  O   LEU C 607      18.978  39.172 -73.598  1.00 65.84           O
ANISOU 4587  O   LEU C 607     8077   9788   7151   1042    223   1805       O
ATOM   4588  CB  LEU C 607      19.451  42.327 -73.797  1.00 65.69           C
ANISOU 4588  CB  LEU C 607     7937   9673   7347   1152    394   2043       C
ATOM   4589  CG  LEU C 607      18.312  42.245 -72.778  1.00 65.82           C
ANISOU 4589  CG  LEU C 607     7941   9643   7423   1130    376   2028       C
ATOM   4590  CD1 LEU C 607      18.847  42.364 -71.358  1.00 66.14           C
ANISOU 4590  CD1 LEU C 607     8021   9541   7569   1117    415   1940       C
ATOM   4591  CD2 LEU C 607      17.263  43.311 -73.055  1.00 65.66           C
ANISOU 4591  CD2 LEU C 607     7837   9649   7460   1165    404   2170       C
ATOM   4592  N   GLN C 608      19.481  39.714 -75.724  1.00 88.15           N
ANISOU 4592  N   GLN C 608    10857  12769   9868   1086    236   1933       N
ATOM   4593  CA  GLN C 608      18.655  38.669 -76.320  1.00 88.05           C
ANISOU 4593  CA  GLN C 608    10850  12870   9734   1049    155   1909       C
ATOM   4594  C   GLN C 608      19.187  37.261 -76.058  1.00 88.46           C
ANISOU 4594  C   GLN C 608    10984  12914   9713   1002    107   1761       C
ATOM   4595  O   GLN C 608      18.471  36.277 -76.242  1.00 88.47           O
ANISOU 4595  O   GLN C 608    11000  12983   9630    963     39   1715       O
ATOM   4596  CB  GLN C 608      18.519  38.905 -77.826  1.00 87.28           C
ANISOU 4596  CB  GLN C 608    10711  12911   9540   1070    143   2007       C
ATOM   4597  CG  GLN C 608      19.847  38.981 -78.563  1.00 87.05           C
ANISOU 4597  CG  GLN C 608    10707  12897   9470   1090    175   1997       C
ATOM   4598  CD  GLN C 608      19.689  39.388 -80.015  1.00 86.83           C
ANISOU 4598  CD  GLN C 608    10629  13003   9358   1116    172   2109       C
ATOM   4599  OE1 GLN C 608      19.155  40.456 -80.318  1.00 86.49           O
ANISOU 4599  OE1 GLN C 608    10516  12982   9365   1153    205   2239       O
ATOM   4600  NE2 GLN C 608      20.150  38.536 -80.923  1.00 87.05           N
ANISOU 4600  NE2 GLN C 608    10693  13123   9260   1095    135   2059       N
ATOM   4601  N   ASP C 609      20.440  37.168 -75.622  1.00 94.51           N
ANISOU 4601  N   ASP C 609    11800  13597  10513   1006    142   1686       N
ATOM   4602  CA  ASP C 609      21.081  35.871 -75.427  1.00 94.38           C
ANISOU 4602  CA  ASP C 609    11859  13569  10430    966    103   1551       C
ATOM   4603  C   ASP C 609      20.876  35.299 -74.024  1.00 94.05           C
ANISOU 4603  C   ASP C 609    11858  13427  10451    933     87   1453       C
ATOM   4604  O   ASP C 609      21.231  34.150 -73.764  1.00 93.91           O
ANISOU 4604  O   ASP C 609    11901  13399  10382    897     49   1341       O
ATOM   4605  CB  ASP C 609      22.579  35.966 -75.733  1.00 94.58           C
ANISOU 4605  CB  ASP C 609    11918  13564  10452    986    145   1519       C
ATOM   4606  CG  ASP C 609      22.858  36.501 -77.123  1.00 95.14           C
ANISOU 4606  CG  ASP C 609    11953  13735  10460   1018    163   1612       C
ATOM   4607  OD1 ASP C 609      22.702  35.738 -78.099  1.00 95.42           O
ANISOU 4607  OD1 ASP C 609    12001  13882  10373    999    116   1598       O
ATOM   4608  OD2 ASP C 609      23.242  37.684 -77.238  1.00 95.42           O
ANISOU 4608  OD2 ASP C 609    11949  13739  10568   1062    226   1699       O
ATOM   4609  N   CYS C 610      20.298  36.102 -73.134  1.00 89.42           N
ANISOU 4609  N   CYS C 610    11236  12767   9972    946    117   1497       N
ATOM   4610  CA  CYS C 610      20.145  35.741 -71.722  1.00 89.39           C
ANISOU 4610  CA  CYS C 610    11265  12658  10040    919    113   1413       C
ATOM   4611  C   CYS C 610      19.514  34.372 -71.473  1.00 89.09           C
ANISOU 4611  C   CYS C 610    11269  12653   9930    868     39   1322       C
ATOM   4612  O   CYS C 610      18.609  33.953 -72.194  1.00 89.25           O
ANISOU 4612  O   CYS C 610    11268  12774   9870    852    -11   1352       O
ATOM   4613  CB  CYS C 610      19.357  36.819 -70.973  1.00 89.47           C
ANISOU 4613  CB  CYS C 610    11223  12607  10165    939    152   1488       C
ATOM   4614  SG  CYS C 610      20.242  38.378 -70.771  1.00 89.35           S
ANISOU 4614  SG  CYS C 610    11174  12505  10271    991    251   1562       S
ATOM   4615  N   LEU C 611      20.009  33.698 -70.435  1.00 68.02           N
ANISOU 4615  N   LEU C 611     8657   9897   7292    842     33   1213       N
ATOM   4616  CA  LEU C 611      19.569  32.357 -70.040  1.00 67.17           C
ANISOU 4616  CA  LEU C 611     8595   9799   7128    792    -31   1114       C
ATOM   4617  C   LEU C 611      19.441  31.388 -71.213  1.00 66.65           C
ANISOU 4617  C   LEU C 611     8546   9851   6928    770    -86   1092       C
ATOM   4618  O   LEU C 611      20.420  31.114 -71.907  1.00 66.10           O
ANISOU 4618  O   LEU C 611     8504   9807   6802    778    -79   1065       O
ATOM   4619  CB  LEU C 611      18.282  32.412 -69.204  1.00 66.95           C
ANISOU 4619  CB  LEU C 611     8542   9747   7150    774    -51   1129       C
ATOM   4620  CG  LEU C 611      16.926  32.618 -69.882  1.00 66.92           C
ANISOU 4620  CG  LEU C 611     8479   9840   7106    773    -84   1217       C
ATOM   4621  CD1 LEU C 611      16.230  31.286 -70.132  0.00 66.62           C
ANISOU 4621  CD1 LEU C 611     8468   9873   6970    725   -161   1151       C
ATOM   4622  CD2 LEU C 611      16.049  33.540 -69.050  0.00 67.15           C
ANISOU 4622  CD2 LEU C 611     8459   9813   7241    788    -55   1282       C
CONECT   18   17  211
CONECT  211   18  210
CONECT 1005 1004 1228
CONECT 1228 1005 1227
CONECT 1248 1247 1310
CONECT 1280 1279 1368
CONECT 1310 1248 1309
CONECT 1368 1280 1367
CONECT 1429 1428 1484
CONECT 1456 1455 1544
CONECT 1484 1429 1483
CONECT 1544 1456 1543
CONECT 1550 1602 1549
CONECT 1583 1582 1657
CONECT 1602 1601 1550
CONECT 1657 1583 1656
CONECT 1679 1678 1748
CONECT 1748 1679 1747
CONECT 1779 2000 1778
CONECT 2000 1999 1779
CONECT 2024 2023 2110
CONECT 2110 2024 2109
CONECT 2139 2138 2254
CONECT 2254 2139 2253
CONECT 2276 2298 2275
CONECT 2298 2276 2297
CONECT 2325 2490 2324
CONECT 2490 2489 2325
CONECT 3360 3359 3622
CONECT 3622 3360 3621
CONECT 3669 3668 3724
CONECT 3698 3697 3779
CONECT 3724 3669 3723
CONECT 3779 3698 3778
CONECT 3799 3798 3868
CONECT 3868 3799 3867
CONECT 3898 3897 4028
CONECT 4028 3898 4027
CONECT 4051 4050 4145
CONECT 4083 4082 4194
CONECT 4145 4051 4144
CONECT 4194 4083 4193
CONECT 4214 4213 4286
CONECT 4286 4214 4285
CONECT 4311 4310 4471
CONECT 4471 4311 4470
CONECT 4495 4494 4554
CONECT 4528 4527 4614
CONECT 4554 4495 4553
CONECT 4614 4528 4613
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.