CNRS Nantes University US2B US2B
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***  higba  ***

elNémo ID: 2408271406424123040

Job options:

ID        	=	 2408271406424123040
JOBID     	=	 higba
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER higba

HEADER    TOXIN                                   12-APR-16   5JAA              
TITLE     CRYSTAL STRUCTURE OF THE HIGBA2 TOXIN-ANTITOXIN COMPLEX               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTITOXIN IGA-2;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TOXIN HIGB-2;                                              
COMPND   7 CHAIN: C, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE   3 / EL TOR INABA N16961);                                              
SOURCE   4 ORGANISM_TAXID: 243277;                                              
SOURCE   5 STRAIN: ATCC 39315 / EL TOR INABA N16961;                            
SOURCE   6 GENE: HIGA-2, VC_A0469;                                              
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE  11 / EL TOR INABA N16961);                                              
SOURCE  12 ORGANISM_TAXID: 243277;                                              
SOURCE  13 STRAIN: ATCC 39315 / EL TOR INABA N16961;                            
SOURCE  14 GENE: HIGB-2, VC_A0468;                                              
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TOXIN-ANTITOXIN SYSTEM, TOXIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HADZI,R.LORIS                                                       
REVDAT   2   17-MAY-17 5JAA    1       JRNL                                     
REVDAT   1   05-APR-17 5JAA    0                                                
JRNL        AUTH   S.HADZI,A.GARCIA-PINO,S.HAESAERTS,D.JURENAS,K.GERDES,J.LAH,  
JRNL        AUTH 2 R.LORIS                                                      
JRNL        TITL   RIBOSOME-DEPENDENT VIBRIO CHOLERAE MRNASE HIGB2 IS REGULATED 
JRNL        TITL 2 BY A BETA-STRAND SLIDING MECHANISM.                          
JRNL        REF    NUCLEIC ACIDS RES.            V.  45  4972 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28334932                                                     
JRNL        DOI    10.1093/NAR/GKX138                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.47                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 10911                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 546                             
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 40.4756 -  4.7498    0.97     2692   142  0.1803 0.2283        
REMARK   3     2  4.7498 -  3.7709    0.99     2609   137  0.1840 0.2161        
REMARK   3     3  3.7709 -  3.2945    1.00     2574   136  0.2360 0.3017        
REMARK   3     4  3.2945 -  2.9934    0.97     2490   131  0.2872 0.3577        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 84.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 96.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3263                                  
REMARK   3   ANGLE     :  0.640           4405                                  
REMARK   3   CHIRALITY :  0.025            496                                  
REMARK   3   PLANARITY :  0.002            569                                  
REMARK   3   DIHEDRAL  : 12.824           1187                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 104)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6988  47.3825  44.4934              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3795 T22:   0.5735                                     
REMARK   3      T33:   0.5839 T12:  -0.0365                                     
REMARK   3      T13:   0.1683 T23:   0.0481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5401 L22:   9.1268                                     
REMARK   3      L33:   3.0463 L12:   3.3140                                     
REMARK   3      L13:   1.8310 L23:   2.7870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1296 S12:  -0.0486 S13:  -0.2767                       
REMARK   3      S21:  -0.2158 S22:   0.2233 S23:  -0.8510                       
REMARK   3      S31:   0.0067 S32:   0.2593 S33:  -0.1938                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 104 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8834  63.3116  48.1507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5281 T22:   0.7202                                     
REMARK   3      T33:   0.6043 T12:  -0.0197                                     
REMARK   3      T13:  -0.0710 T23:   0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3698 L22:   3.2240                                     
REMARK   3      L33:   1.1132 L12:   1.3245                                     
REMARK   3      L13:   0.4399 L23:   1.6406                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3053 S12:   0.2116 S13:   0.7713                       
REMARK   3      S21:   0.1786 S22:   0.0631 S23:   1.1491                       
REMARK   3      S31:   0.0924 S32:  -0.1429 S33:   0.2674                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 110)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7943  87.6860  53.4582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6955 T22:   0.6538                                     
REMARK   3      T33:   1.5163 T12:   0.0766                                     
REMARK   3      T13:  -0.2192 T23:  -0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0496 L22:   5.6180                                     
REMARK   3      L33:   5.0751 L12:   3.9702                                     
REMARK   3      L13:  -0.2992 L23:   0.1717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3737 S12:  -0.3761 S13:   0.2809                       
REMARK   3      S21:   0.2449 S22:   0.0167 S23:  -1.2570                       
REMARK   3      S31:   0.8945 S32:  -0.1820 S33:   0.2394                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 109 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5225  25.1475  32.3773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3468 T22:   0.2052                                     
REMARK   3      T33:  -0.0108 T12:  -0.1756                                     
REMARK   3      T13:   0.3337 T23:   0.1387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8596 L22:   2.5487                                     
REMARK   3      L33:   0.4290 L12:   1.6338                                     
REMARK   3      L13:   1.1657 L23:   1.0239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1410 S12:   0.8774 S13:  -1.3574                       
REMARK   3      S21:  -1.2293 S22:   0.5212 S23:  -1.5689                       
REMARK   3      S31:   0.0011 S32:   0.2665 S33:   1.5213                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5JAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220191.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979030                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18810                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.854                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 2.190                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.8800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.640                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BICINE/TRIS PH 8.5; 12.5%(W/V)    
REMARK 280  PEG1000; 12.5%(W/V) PEG3350; 12.5%(W/W) MPD; 30 MM NAF; 30 MM       
REMARK 280  NABR; 30 MM NAI, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       64.50000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.50000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
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     2                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     SER C    54                                                      
REMARK 465     LYS C    55                                                      
REMARK 465     GLY C    56                                                      
REMARK 465     LYS C    57                                                      
REMARK 465     GLY C    58                                                      
REMARK 465     LYS C    59                                                      
REMARK 465     ARG C    60                                                      
REMARK 465     GLY C    61                                                      
REMARK 465     GLY C    62                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     LYS D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     LYS D    57                                                      
REMARK 465     GLY D    58                                                      
REMARK 465     LYS D    59                                                      
REMARK 465     ARG D    60                                                      
REMARK 465     SER D   110                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     LYS A  28    CD   CE   NZ                                        
REMARK 470     GLU A  37    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 103    CG   CD   OE1  OE2                                  
REMARK 470     ASP B   5    CG   OD1  OD2                                       
REMARK 470     LEU B   6    CG   CD1  CD2                                       
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     GLU B  37    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     LYS C   2    CG   CD   CE   NZ                                   
REMARK 470     GLU C  17    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  42    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  51    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C  63    OG                                                  
REMARK 470     ARG C  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  73    CG   CD   CE   NZ                                   
REMARK 470     LYS C  84    CG   CD   CE   NZ                                   
REMARK 470     ASN C  85    CG   OD1  ND2                                       
REMARK 470     LYS C  96    CG   CD   CE   NZ                                   
REMARK 470     ARG C 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 108    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 109    CG   CD   OE1  NE2                                  
REMARK 470     SER C 110    OG                                                  
REMARK 470     LYS D   2    CG   CD   CE   NZ                                   
REMARK 470     LYS D  73    CG   CD   CE   NZ                                   
REMARK 470     ASP D  89    CG   OD1  OD2                                       
REMARK 470     ASN D  91    CG   OD1  ND2                                       
REMARK 470     GLU D 103    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 108    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 109    CG   CD   OE1  NE2                                  
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    ARG C  64      -67.20   -130.90                                   
REMARK 500    GLU C  86      -66.64   -131.63                                   
REMARK 500    TYR D  18      -57.78   -123.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5JAA A    2   104  UNP    Q9KMA5   HIGA2_VIBCH      2    104             
DBREF  5JAA B    2   104  UNP    Q9KMA5   HIGA2_VIBCH      2    104             
DBREF  5JAA C    2   110  UNP    Q9KMA6   HIGB2_VIBCH      2    110             
DBREF  5JAA D    2   110  UNP    Q9KMA6   HIGB2_VIBCH      2    110             
SEQADV 5JAA HIS C    0  UNP  Q9KMA6              EXPRESSION TAG                 
SEQADV 5JAA MSE C    1  UNP  Q9KMA6              EXPRESSION TAG                 
SEQADV 5JAA HIS D    0  UNP  Q9KMA6              EXPRESSION TAG                 
SEQADV 5JAA MSE D    1  UNP  Q9KMA6              EXPRESSION TAG                 
SEQRES   1 A  103  SER ASN ARG ASP LEU PHE ALA GLU LEU SER SER ALA LEU          
SEQRES   2 A  103  VAL GLU ALA LYS GLN HIS SER GLU GLY LYS LEU THR LEU          
SEQRES   3 A  103  LYS THR HIS HIS VAL ASN ASP VAL GLY GLU LEU ASN ILE          
SEQRES   4 A  103  SER PRO ASP GLU ILE VAL SER ILE ARG GLU GLN PHE ASN          
SEQRES   5 A  103  MSE SER ARG GLY VAL PHE ALA ARG LEU LEU HIS THR SER          
SEQRES   6 A  103  SER ARG THR LEU GLU ASN TRP GLU GLN GLY ARG SER VAL          
SEQRES   7 A  103  PRO ASN GLY GLN ALA VAL THR LEU LEU LYS LEU VAL GLN          
SEQRES   8 A  103  ARG HIS PRO GLU THR LEU SER HIS ILE ALA GLU LEU              
SEQRES   1 B  103  SER ASN ARG ASP LEU PHE ALA GLU LEU SER SER ALA LEU          
SEQRES   2 B  103  VAL GLU ALA LYS GLN HIS SER GLU GLY LYS LEU THR LEU          
SEQRES   3 B  103  LYS THR HIS HIS VAL ASN ASP VAL GLY GLU LEU ASN ILE          
SEQRES   4 B  103  SER PRO ASP GLU ILE VAL SER ILE ARG GLU GLN PHE ASN          
SEQRES   5 B  103  MSE SER ARG GLY VAL PHE ALA ARG LEU LEU HIS THR SER          
SEQRES   6 B  103  SER ARG THR LEU GLU ASN TRP GLU GLN GLY ARG SER VAL          
SEQRES   7 B  103  PRO ASN GLY GLN ALA VAL THR LEU LEU LYS LEU VAL GLN          
SEQRES   8 B  103  ARG HIS PRO GLU THR LEU SER HIS ILE ALA GLU LEU              
SEQRES   1 C  111  HIS MSE LYS SER VAL PHE VAL GLU SER THR ILE PHE GLU          
SEQRES   2 C  111  LYS TYR ARG ASP GLU TYR LEU SER ASP GLU GLU TYR ARG          
SEQRES   3 C  111  LEU PHE GLN ALA GLU LEU MSE LEU ASN PRO LYS LEU GLY          
SEQRES   4 C  111  ASP VAL ILE GLN GLY THR GLY GLY LEU ARG LYS ILE ARG          
SEQRES   5 C  111  VAL ALA SER LYS GLY LYS GLY LYS ARG GLY GLY SER ARG          
SEQRES   6 C  111  ILE ILE TYR TYR PHE LEU ASP GLU LYS ARG ARG PHE TYR          
SEQRES   7 C  111  LEU LEU THR ILE TYR GLY LYS ASN GLU MSE SER ASP LEU          
SEQRES   8 C  111  ASN ALA ASN GLN ARG LYS GLN LEU MSE ALA PHE MSE GLU          
SEQRES   9 C  111  ALA TRP ARG ASN GLU GLN SER                                  
SEQRES   1 D  111  HIS MSE LYS SER VAL PHE VAL GLU SER THR ILE PHE GLU          
SEQRES   2 D  111  LYS TYR ARG ASP GLU TYR LEU SER ASP GLU GLU TYR ARG          
SEQRES   3 D  111  LEU PHE GLN ALA GLU LEU MSE LEU ASN PRO LYS LEU GLY          
SEQRES   4 D  111  ASP VAL ILE GLN GLY THR GLY GLY LEU ARG LYS ILE ARG          
SEQRES   5 D  111  VAL ALA SER LYS GLY LYS GLY LYS ARG GLY GLY SER ARG          
SEQRES   6 D  111  ILE ILE TYR TYR PHE LEU ASP GLU LYS ARG ARG PHE TYR          
SEQRES   7 D  111  LEU LEU THR ILE TYR GLY LYS ASN GLU MSE SER ASP LEU          
SEQRES   8 D  111  ASN ALA ASN GLN ARG LYS GLN LEU MSE ALA PHE MSE GLU          
SEQRES   9 D  111  ALA TRP ARG ASN GLU GLN SER                                  
MODRES 5JAA MSE A   54  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE B   54  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE C   32  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE C   87  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE C   99  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE C  102  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE D   32  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE D   87  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE D   99  MET  MODIFIED RESIDUE                                   
MODRES 5JAA MSE D  102  MET  MODIFIED RESIDUE                                   
HET    MSE  A  54       8                                                       
HET    MSE  B  54       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C  32       8                                                       
HET    MSE  C  87       8                                                       
HET    MSE  C  99       8                                                       
HET    MSE  C 102       8                                                       
HET    MSE  D  32       8                                                       
HET    MSE  D  87       8                                                       
HET    MSE  D  99       8                                                       
HET    MSE  D 102       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    11(C5 H11 N O2 SE)                                           
HELIX    1 AA1 ASP A    5  GLU A   22  1                                  18    
HELIX    2 AA2 SER A   41  PHE A   52  1                                  12    
HELIX    3 AA3 SER A   55  LEU A   63  1                                   9    
HELIX    4 AA4 SER A   66  GLN A   75  1                                  10    
HELIX    5 AA5 ASN A   81  HIS A   94  1                                  14    
HELIX    6 AA6 PRO A   95  GLU A  103  1                                   9    
HELIX    7 AA7 ASP B    5  GLY B   23  1                                  19    
HELIX    8 AA8 SER B   41  PHE B   52  1                                  12    
HELIX    9 AA9 SER B   55  LEU B   63  1                                   9    
HELIX   10 AB1 SER B   66  GLN B   75  1                                  10    
HELIX   11 AB2 ASN B   81  HIS B   94  1                                  14    
HELIX   12 AB3 GLU B   96  GLU B  103  1                                   8    
HELIX   13 AB4 SER C    8  LEU C   19  1                                  12    
HELIX   14 AB5 SER C   20  ASN C   34  1                                  15    
HELIX   15 AB6 ASN C   91  SER C  110  1                                  20    
HELIX   16 AB7 SER D    8  ARG D   15  1                                   8    
HELIX   17 AB8 SER D   20  ASN D   34  1                                  15    
HELIX   18 AB9 ASN D   91  GLN D  109  1                                  19    
SHEET    1 AA1 6 THR A  29  VAL A  32  0                                        
SHEET    2 AA1 6 SER D   3  GLU D   7 -1  O  PHE D   5   N  HIS A  30           
SHEET    3 AA1 6 ARG D  75  GLY D  83  1  O  LEU D  78   N  VAL D   6           
SHEET    4 AA1 6 ARG D  64  LEU D  70 -1  N  ILE D  65   O  TYR D  82           
SHEET    5 AA1 6 LEU D  47  VAL D  52 -1  N  ILE D  50   O  ILE D  66           
SHEET    6 AA1 6 ASP D  39  VAL D  40 -1  N  ASP D  39   O  LYS D  49           
SHEET    1 AA2 6 LYS B  28  VAL B  32  0                                        
SHEET    2 AA2 6 SER C   3  GLU C   7 -1  O  SER C   3   N  VAL B  32           
SHEET    3 AA2 6 ARG C  75  TYR C  82  1  O  PHE C  76   N  VAL C   4           
SHEET    4 AA2 6 ILE C  65  LEU C  70 -1  N  PHE C  69   O  TYR C  77           
SHEET    5 AA2 6 LEU C  47  ARG C  51 -1  N  ARG C  48   O  TYR C  68           
SHEET    6 AA2 6 ASP C  39  VAL C  40 -1  N  ASP C  39   O  LYS C  49           
LINK         C   ASN A  53                 N   MSE A  54     1555   1555  1.33  
LINK         C   MSE A  54                 N   SER A  55     1555   1555  1.33  
LINK         C   ASN B  53                 N   MSE B  54     1555   1555  1.33  
LINK         C   MSE B  54                 N   SER B  55     1555   1555  1.33  
LINK         C   HIS C   0                 N   MSE C   1     1555   1555  1.33  
LINK         C   MSE C   1                 N   LYS C   2     1555   1555  1.33  
LINK         C   LEU C  31                 N   MSE C  32     1555   1555  1.33  
LINK         C   MSE C  32                 N   LEU C  33     1555   1555  1.33  
LINK         C   GLU C  86                 N   MSE C  87     1555   1555  1.33  
LINK         C   MSE C  87                 N   SER C  88     1555   1555  1.33  
LINK         C   LEU C  98                 N   MSE C  99     1555   1555  1.33  
LINK         C   MSE C  99                 N   ALA C 100     1555   1555  1.33  
LINK         C   PHE C 101                 N   MSE C 102     1555   1555  1.33  
LINK         C   MSE C 102                 N   GLU C 103     1555   1555  1.33  
LINK         C   LEU D  31                 N   MSE D  32     1555   1555  1.33  
LINK         C   MSE D  32                 N   LEU D  33     1555   1555  1.33  
LINK         C   GLU D  86                 N   MSE D  87     1555   1555  1.33  
LINK         C   MSE D  87                 N   SER D  88     1555   1555  1.32  
LINK         C   LEU D  98                 N   MSE D  99     1555   1555  1.33  
LINK         C   MSE D  99                 N   ALA D 100     1555   1555  1.33  
LINK         C   PHE D 101                 N   MSE D 102     1555   1555  1.33  
LINK         C   MSE D 102                 N   GLU D 103     1555   1555  1.33  
CRYST1  129.000  119.800   33.400  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007752  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029940        0.00000                         
ATOM      1  N   ASN A   3      28.562  23.185  13.830  1.00146.69           N  
ANISOU    1  N   ASN A   3    28919  13067  13750  -5069  -4136    664       N  
ATOM      2  CA  ASN A   3      29.914  23.395  13.330  1.00143.05           C  
ANISOU    2  CA  ASN A   3    29014  12667  12671  -5295  -3393    536       C  
ATOM      3  C   ASN A   3      30.957  23.255  14.433  1.00133.04           C  
ANISOU    3  C   ASN A   3    27188  11666  11696  -5111  -2605    282       C  
ATOM      4  O   ASN A   3      32.153  23.159  14.158  1.00137.39           O  
ANISOU    4  O   ASN A   3    28037  12281  11883  -5259  -1858     84       O  
ATOM      5  CB  ASN A   3      30.036  24.771  12.671  1.00149.65           C  
ANISOU    5  CB  ASN A   3    30388  13398  13076  -5484  -3676    754       C  
ATOM      6  CG  ASN A   3      29.901  25.911  13.667  1.00145.72           C  
ANISOU    6  CG  ASN A   3    29277  13047  13044  -5225  -3910    816       C  
ATOM      7  OD1 ASN A   3      30.864  26.630  13.938  1.00131.53           O  
ANISOU    7  OD1 ASN A   3    27501  11397  11077  -5263  -3421    740       O  
ATOM      8  ND2 ASN A   3      28.702  26.086  14.210  1.00144.95           N  
ANISOU    8  ND2 ASN A   3    28608  12893  13573  -4972  -4637    939       N  
ATOM      9  N   ARG A   4      30.502  23.255  15.683  1.00120.81           N  
ANISOU    9  N   ARG A   4    24821  10244  10838  -4802  -2758    294       N  
ATOM     10  CA  ARG A   4      31.408  23.104  16.817  1.00118.55           C  
ANISOU   10  CA  ARG A   4    23999  10160  10884  -4612  -2086    121       C  
ATOM     11  C   ARG A   4      30.825  22.184  17.893  1.00118.15           C  
ANISOU   11  C   ARG A   4    23261  10154  11478  -4377  -2150    119       C  
ATOM     12  O   ARG A   4      29.726  22.422  18.392  1.00123.62           O  
ANISOU   12  O   ARG A   4    23517  10837  12615  -4265  -2720    276       O  
ATOM     13  CB  ARG A   4      31.734  24.475  17.400  1.00 92.59           C  
ANISOU   13  CB  ARG A   4    20466   7002   7710  -4524  -2081    203       C  
ATOM     14  CG  ARG A   4      33.006  24.522  18.211  1.00 96.13           C  
ANISOU   14  CG  ARG A   4    20588   7657   8278  -4398  -1280     29       C  
ATOM     15  CD  ARG A   4      33.502  25.955  18.351  1.00 94.24           C  
ANISOU   15  CD  ARG A   4    20350   7537   7920  -4403  -1224    101       C  
ATOM     16  NE  ARG A   4      34.415  26.104  19.479  1.00 91.16           N  
ANISOU   16  NE  ARG A   4    19227   7533   7875  -4067   -616     30       N  
ATOM     17  CZ  ARG A   4      34.177  26.874  20.535  1.00 97.02           C  
ANISOU   17  CZ  ARG A   4    19296   8522   9044  -3770   -766    179       C  
ATOM     18  NH1 ARG A   4      35.061  26.941  21.521  1.00102.32           N  
ANISOU   18  NH1 ARG A   4    19385   9510   9981  -3498   -229    111       N  
ATOM     19  NH2 ARG A   4      33.062  27.589  20.599  1.00102.78           N  
ANISOU   19  NH2 ARG A   4    19938   9154   9960  -3749  -1471    372       N  
ATOM     20  N   ASP A   5      31.568  21.138  18.248  1.00111.53           N  
ANISOU   20  N   ASP A   5    22322   9344  10710  -4318  -1557    -71       N  
ATOM     21  CA  ASP A   5      31.076  20.108  19.168  1.00109.32           C  
ANISOU   21  CA  ASP A   5    21421   9169  10947  -4083  -1572    -36       C  
ATOM     22  C   ASP A   5      31.838  20.089  20.496  1.00 87.50           C  
ANISOU   22  C   ASP A   5    17907   6767   8571  -3725  -1048    -50       C  
ATOM     23  O   ASP A   5      33.068  20.119  20.513  1.00 91.66           O  
ANISOU   23  O   ASP A   5    18485   7384   8957  -3659   -468   -218       O  
ATOM     24  CB  ASP A   5      31.159  18.732  18.499  1.00126.48           C  
ANISOU   24  CB  ASP A   5    24038  11092  12925  -4242  -1441   -204       C  
ATOM     25  CG  ASP A   5      30.805  17.601  19.443  1.00129.29           C  
ANISOU   25  CG  ASP A   5    23820  11536  13767  -4024  -1399   -172       C  
ATOM     26  OD1 ASP A   5      29.607  17.260  19.541  1.00137.06           O  
ANISOU   26  OD1 ASP A   5    24661  12425  14992  -4084  -1927    -37       O  
ATOM     27  OD2 ASP A   5      31.726  17.046  20.080  1.00127.10           O  
ANISOU   27  OD2 ASP A   5    23247  11396  13648  -3812   -863   -291       O  
ATOM     28  N   LEU A   6      31.104  20.020  21.605  1.00 81.46           N  
ANISOU   28  N   LEU A   6    16462   6186   8303  -3523  -1254    105       N  
ATOM     29  CA  LEU A   6      31.705  20.113  22.938  1.00 77.65           C  
ANISOU   29  CA  LEU A   6    15320   6025   8156  -3223   -859    134       C  
ATOM     30  C   LEU A   6      32.597  18.928  23.316  1.00 93.93           C  
ANISOU   30  C   LEU A   6    17316   8081  10294  -3094   -392      0       C  
ATOM     31  O   LEU A   6      33.758  19.118  23.691  1.00 83.57           O  
ANISOU   31  O   LEU A   6    15858   6898   8998  -2927     59   -104       O  
ATOM     32  CB  LEU A   6      30.613  20.275  23.999  1.00 75.89           C  
ANISOU   32  CB  LEU A   6    14466   5971   8399  -3123  -1172    302       C  
ATOM     33  CG  LEU A   6      31.115  20.434  25.441  1.00 81.15           C  
ANISOU   33  CG  LEU A   6    14517   6955   9361  -2872   -816    355       C  
ATOM     34  CD1 LEU A   6      32.120  21.577  25.560  1.00 70.53           C  
ANISOU   34  CD1 LEU A   6    13132   5785   7881  -2741   -534    328       C  
ATOM     35  CD2 LEU A   6      29.957  20.636  26.405  1.00 71.55           C  
ANISOU   35  CD2 LEU A   6    12740   5889   8555  -2860  -1071    468       C  
ATOM     36  N   PHE A   7      32.052  17.716  23.229  1.00 84.32           N  
ANISOU   36  N   PHE A   7    16187   6682   9166  -3167   -543     -7       N  
ATOM     37  CA  PHE A   7      32.786  16.516  23.616  1.00 79.02           C  
ANISOU   37  CA  PHE A   7    15457   5937   8628  -3037   -209   -125       C  
ATOM     38  C   PHE A   7      34.132  16.402  22.908  1.00 80.63           C  
ANISOU   38  C   PHE A   7    15999   6032   8604  -3012    272   -413       C  
ATOM     39  O   PHE A   7      35.143  16.098  23.539  1.00 79.74           O  
ANISOU   39  O   PHE A   7    15606   5978   8714  -2783    634   -526       O  
ATOM     40  CB  PHE A   7      31.954  15.268  23.337  1.00 98.43           C  
ANISOU   40  CB  PHE A   7    18112   8150  11137  -3185   -488   -110       C  
ATOM     41  CG  PHE A   7      32.699  13.988  23.566  1.00 99.47           C  
ANISOU   41  CG  PHE A   7    18284   8119  11393  -3067   -212   -253       C  
ATOM     42  CD1 PHE A   7      32.873  13.495  24.848  1.00 98.20           C  
ANISOU   42  CD1 PHE A   7    17677   8056  11580  -2878   -150   -138       C  
ATOM     43  CD2 PHE A   7      33.231  13.280  22.501  1.00 91.62           C  
ANISOU   43  CD2 PHE A   7    17806   6839  10168  -3162    -33   -518       C  
ATOM     44  CE1 PHE A   7      33.561  12.317  25.066  1.00 81.97           C  
ANISOU   44  CE1 PHE A   7    15677   5786   9681  -2755      8   -263       C  
ATOM     45  CE2 PHE A   7      33.924  12.106  22.713  1.00 92.02           C  
ANISOU   45  CE2 PHE A   7    17853   6697  10411  -3022    189   -688       C  
ATOM     46  CZ  PHE A   7      34.089  11.623  23.998  1.00 90.54           C  
ANISOU   46  CZ  PHE A   7    17207   6580  10614  -2803    170   -549       C  
ATOM     47  N   ALA A   8      34.134  16.640  21.600  1.00 83.56           N  
ANISOU   47  N   ALA A   8    16982   6218   8547  -3274    266   -553       N  
ATOM     48  CA  ALA A   8      35.364  16.622  20.814  1.00100.20           C  
ANISOU   48  CA  ALA A   8    19457   8220  10394  -3341    801   -888       C  
ATOM     49  C   ALA A   8      36.398  17.586  21.385  1.00 91.05           C  
ANISOU   49  C   ALA A   8    17926   7319   9348  -3155   1192   -941       C  
ATOM     50  O   ALA A   8      37.577  17.248  21.529  1.00 84.45           O  
ANISOU   50  O   ALA A   8    16934   6474   8681  -3006   1689  -1215       O  
ATOM     51  CB  ALA A   8      35.069  16.966  19.361  1.00 89.68           C  
ANISOU   51  CB  ALA A   8    18925   6666   8485  -3744    690   -981       C  
ATOM     52  N   GLU A   9      35.939  18.788  21.718  1.00 86.24           N  
ANISOU   52  N   GLU A   9    17150   6919   8699  -3158    940   -700       N  
ATOM     53  CA  GLU A   9      36.815  19.826  22.241  1.00 85.80           C  
ANISOU   53  CA  GLU A   9    16771   7108   8720  -3011   1252   -719       C  
ATOM     54  C   GLU A   9      37.402  19.441  23.587  1.00 84.38           C  
ANISOU   54  C   GLU A   9    15915   7100   9044  -2645   1431   -698       C  
ATOM     55  O   GLU A   9      38.606  19.560  23.797  1.00 79.57           O  
ANISOU   55  O   GLU A   9    15112   6547   8574  -2504   1870   -907       O  
ATOM     56  CB  GLU A   9      36.063  21.150  22.364  1.00 93.26           C  
ANISOU   56  CB  GLU A   9    17672   8203   9557  -3077    860   -454       C  
ATOM     57  CG  GLU A   9      35.792  21.830  21.037  1.00108.30           C  
ANISOU   57  CG  GLU A   9    20308   9914  10925  -3448    687   -479       C  
ATOM     58  CD  GLU A   9      35.103  23.168  21.205  1.00109.28           C  
ANISOU   58  CD  GLU A   9    20358  10137  11026  -3473    237   -230       C  
ATOM     59  OE1 GLU A   9      33.885  23.179  21.488  1.00 97.49           O  
ANISOU   59  OE1 GLU A   9    18673   8618   9750  -3436   -327    -28       O  
ATOM     60  OE2 GLU A   9      35.780  24.208  21.060  1.00114.88           O1+
ANISOU   60  OE2 GLU A   9    21176  10933  11540  -3532    450   -262       O1+
ATOM     61  N   LEU A  10      36.547  18.986  24.498  1.00 84.64           N  
ANISOU   61  N   LEU A  10    15610   7195   9355  -2524   1077   -456       N  
ATOM     62  CA  LEU A  10      37.001  18.574  25.821  1.00 77.89           C  
ANISOU   62  CA  LEU A  10    14222   6456   8915  -2237   1162   -390       C  
ATOM     63  C   LEU A  10      37.983  17.413  25.723  1.00 83.17           C  
ANISOU   63  C   LEU A  10    14927   6899   9776  -2109   1449   -658       C  
ATOM     64  O   LEU A  10      38.965  17.363  26.457  1.00 79.26           O  
ANISOU   64  O   LEU A  10    14083   6446   9587  -1867   1655   -743       O  
ATOM     65  CB  LEU A  10      35.814  18.188  26.704  1.00 70.92           C  
ANISOU   65  CB  LEU A  10    13093   5636   8217  -2239    764   -109       C  
ATOM     66  CG  LEU A  10      34.927  19.348  27.157  1.00 72.09           C  
ANISOU   66  CG  LEU A  10    12997   6031   8365  -2287    515    109       C  
ATOM     67  CD1 LEU A  10      33.755  18.849  27.982  1.00 69.62           C  
ANISOU   67  CD1 LEU A  10    12427   5760   8267  -2346    218    302       C  
ATOM     68  CD2 LEU A  10      35.742  20.354  27.947  1.00 76.31           C  
ANISOU   68  CD2 LEU A  10    13183   6815   8997  -2098    739    133       C  
ATOM     69  N   SER A  11      37.717  16.492  24.802  1.00 88.36           N  
ANISOU   69  N   SER A  11    16004   7284  10284  -2268   1428   -809       N  
ATOM     70  CA  SER A  11      38.587  15.342  24.586  1.00 86.54           C  
ANISOU   70  CA  SER A  11    15830   6785  10267  -2152   1689  -1120       C  
ATOM     71  C   SER A  11      39.966  15.785  24.116  1.00 86.73           C  
ANISOU   71  C   SER A  11    15824   6803  10326  -2093   2234  -1501       C  
ATOM     72  O   SER A  11      40.990  15.420  24.708  1.00 90.65           O  
ANISOU   72  O   SER A  11    15944   7239  11259  -1822   2436  -1689       O  
ATOM     73  CB  SER A  11      37.967  14.389  23.565  1.00101.09           C  
ANISOU   73  CB  SER A  11    18192   8337  11881  -2382   1576  -1231       C  
ATOM     74  OG  SER A  11      36.662  14.002  23.957  1.00110.03           O  
ANISOU   74  OG  SER A  11    19325   9471  13011  -2470   1083   -904       O  
ATOM     75  N   SER A  12      39.979  16.578  23.047  1.00 85.91           N  
ANISOU   75  N   SER A  12    16132   6735   9774  -2375   2447  -1624       N  
ATOM     76  CA  SER A  12      41.217  17.103  22.487  1.00 86.02           C  
ANISOU   76  CA  SER A  12    16182   6757   9743  -2426   3034  -2011       C  
ATOM     77  C   SER A  12      42.012  17.876  23.529  1.00 83.35           C  
ANISOU   77  C   SER A  12    15238   6662   9767  -2150   3156  -1959       C  
ATOM     78  O   SER A  12      43.231  17.735  23.634  1.00 85.29           O  
ANISOU   78  O   SER A  12    15189   6852  10365  -1992   3576  -2312       O  
ATOM     79  CB  SER A  12      40.917  18.001  21.290  1.00 87.64           C  
ANISOU   79  CB  SER A  12    17016   6978   9307  -2849   3143  -2042       C  
ATOM     80  OG  SER A  12      42.103  18.589  20.787  1.00112.23           O  
ANISOU   80  OG  SER A  12    20180  10119  12342  -2965   3764  -2415       O  
ATOM     81  N   ALA A  13      41.305  18.687  24.307  1.00 82.12           N  
ANISOU   81  N   ALA A  13    14879   6761   9564  -2095   2779  -1544       N  
ATOM     82  CA  ALA A  13      41.934  19.542  25.301  1.00 76.58           C  
ANISOU   82  CA  ALA A  13    13667   6302   9130  -1872   2844  -1451       C  
ATOM     83  C   ALA A  13      42.479  18.736  26.470  1.00 76.09           C  
ANISOU   83  C   ALA A  13    13100   6173   9637  -1515   2746  -1451       C  
ATOM     84  O   ALA A  13      43.462  19.126  27.091  1.00 75.76           O  
ANISOU   84  O   ALA A  13    12651   6209   9923  -1309   2918  -1556       O  
ATOM     85  CB  ALA A  13      40.948  20.586  25.798  1.00 86.24           C  
ANISOU   85  CB  ALA A  13    14835   7783  10148  -1926   2463  -1040       C  
ATOM     86  N   LEU A  14      41.831  17.619  26.780  1.00 91.77           N  
ANISOU   86  N   LEU A  14    15141   7986  11740  -1462   2422  -1320       N  
ATOM     87  CA  LEU A  14      42.265  16.788  27.896  1.00 76.48           C  
ANISOU   87  CA  LEU A  14    12839   5920  10299  -1167   2227  -1275       C  
ATOM     88  C   LEU A  14      43.444  15.892  27.520  1.00 80.71           C  
ANISOU   88  C   LEU A  14    13283   6134  11249   -995   2509  -1735       C  
ATOM     89  O   LEU A  14      44.315  15.633  28.354  1.00 91.32           O  
ANISOU   89  O   LEU A  14    14227   7374  13096   -707   2446  -1816       O  
ATOM     90  CB  LEU A  14      41.103  15.950  28.426  1.00 75.57           C  
ANISOU   90  CB  LEU A  14    12849   5726  10139  -1223   1767   -948       C  
ATOM     91  CG  LEU A  14      40.125  16.711  29.326  1.00 83.16           C  
ANISOU   91  CG  LEU A  14    13674   6987  10937  -1299   1474   -527       C  
ATOM     92  CD1 LEU A  14      38.993  15.803  29.772  1.00 97.58           C  
ANISOU   92  CD1 LEU A  14    15626   8714  12736  -1418   1105   -273       C  
ATOM     93  CD2 LEU A  14      40.843  17.300  30.528  1.00 70.06           C  
ANISOU   93  CD2 LEU A  14    11604   5481   9533  -1084   1459   -425       C  
ATOM     94  N   VAL A  15      43.487  15.415  26.278  1.00 83.96           N  
ANISOU   94  N   VAL A  15    14062   6358  11482  -1174   2801  -2063       N  
ATOM     95  CA  VAL A  15      44.666  14.665  25.854  1.00 96.05           C  
ANISOU   95  CA  VAL A  15    15454   7585  13457  -1022   3165  -2599       C  
ATOM     96  C   VAL A  15      45.832  15.640  25.695  1.00102.31           C  
ANISOU   96  C   VAL A  15    15943   8523  14408   -988   3663  -2921       C  
ATOM     97  O   VAL A  15      46.974  15.314  26.032  1.00110.43           O  
ANISOU   97  O   VAL A  15    16522   9379  16056   -718   3829  -3270       O  
ATOM     98  CB  VAL A  15      44.433  13.862  24.547  1.00 92.51           C  
ANISOU   98  CB  VAL A  15    15512   6878  12760  -1259   3411  -2924       C  
ATOM     99  CG1 VAL A  15      43.844  14.725  23.457  1.00 92.10           C  
ANISOU   99  CG1 VAL A  15    15991   7009  11995  -1679   3633  -2888       C  
ATOM    100  CG2 VAL A  15      45.727  13.216  24.081  1.00 97.90           C  
ANISOU  100  CG2 VAL A  15    15987   7260  13951  -1113   3892  -3573       C  
ATOM    101  N   GLU A  16      45.533  16.845  25.212  1.00102.89           N  
ANISOU  101  N   GLU A  16    16246   8888  13961  -1264   3857  -2802       N  
ATOM    102  CA  GLU A  16      46.521  17.922  25.179  1.00104.25           C  
ANISOU  102  CA  GLU A  16    16147   9242  14223  -1276   4284  -3020       C  
ATOM    103  C   GLU A  16      47.085  18.179  26.570  1.00 85.74           C  
ANISOU  103  C   GLU A  16    13171   6988  12417   -904   4015  -2855       C  
ATOM    104  O   GLU A  16      48.300  18.225  26.760  1.00 91.50           O  
ANISOU  104  O   GLU A  16    13458   7635  13674   -719   4298  -3225       O  
ATOM    105  CB  GLU A  16      45.909  19.216  24.628  1.00117.35           C  
ANISOU  105  CB  GLU A  16    18204  11183  15202  -1627   4354  -2785       C  
ATOM    106  CG  GLU A  16      45.940  19.350  23.112  1.00124.07           C  
ANISOU  106  CG  GLU A  16    19678  11935  15530  -2065   4827  -3109       C  
ATOM    107  CD  GLU A  16      45.266  20.625  22.624  1.00103.84           C  
ANISOU  107  CD  GLU A  16    17573   9584  12297  -2412   4740  -2815       C  
ATOM    108  OE1 GLU A  16      44.698  21.359  23.460  1.00 92.21           O  
ANISOU  108  OE1 GLU A  16    15885   8339  10812  -2280   4310  -2377       O  
ATOM    109  OE2 GLU A  16      45.302  20.891  21.403  1.00 97.99           O  
ANISOU  109  OE2 GLU A  16    17438   8753  11040  -2834   5085  -3035       O  
ATOM    110  N   ALA A  17      46.186  18.342  27.535  1.00 81.45           N  
ANISOU  110  N   ALA A  17    12600   6599  11748   -823   3467  -2321       N  
ATOM    111  CA  ALA A  17      46.556  18.637  28.913  1.00 79.25           C  
ANISOU  111  CA  ALA A  17    11848   6413  11851   -538   3151  -2093       C  
ATOM    112  C   ALA A  17      47.422  17.529  29.485  1.00 82.55           C  
ANISOU  112  C   ALA A  17    11920   6478  12968   -207   2992  -2325       C  
ATOM    113  O   ALA A  17      48.442  17.789  30.133  1.00 83.57           O  
ANISOU  113  O   ALA A  17    11590   6568  13596     31   2988  -2468       O  
ATOM    114  CB  ALA A  17      45.314  18.831  29.763  1.00 74.99           C  
ANISOU  114  CB  ALA A  17    11427   6061  11006   -584   2646  -1532       C  
ATOM    115  N   LYS A  18      47.004  16.291  29.238  1.00104.02           N  
ANISOU  115  N   LYS A  18    14869   8905  15749   -193   2810  -2363       N  
ATOM    116  CA  LYS A  18      47.768  15.128  29.658  1.00104.62           C  
ANISOU  116  CA  LYS A  18    14681   8561  16508    117   2600  -2608       C  
ATOM    117  C   LYS A  18      49.185  15.221  29.109  1.00107.37           C  
ANISOU  117  C   LYS A  18    14633   8757  17407    258   3104  -3246       C  
ATOM    118  O   LYS A  18      50.155  15.090  29.856  1.00 95.03           O  
ANISOU  118  O   LYS A  18    12581   7009  16518    572   2923  -3403       O  
ATOM    119  CB  LYS A  18      47.092  13.836  29.193  1.00 90.44           C  
ANISOU  119  CB  LYS A  18    13262   6465  14634     52   2428  -2623       C  
ATOM    120  CG  LYS A  18      47.747  12.578  29.732  1.00 94.55           C  
ANISOU  120  CG  LYS A  18    13564   6498  15864    380   2074  -2809       C  
ATOM    121  CD  LYS A  18      46.943  11.343  29.386  1.00112.24           C  
ANISOU  121  CD  LYS A  18    16224   8455  17965    290   1835  -2739       C  
ATOM    122  CE  LYS A  18      47.528  10.106  30.044  1.00112.98           C  
ANISOU  122  CE  LYS A  18    16144   8020  18761    617   1361  -2856       C  
ATOM    123  NZ  LYS A  18      46.729   8.886  29.734  1.00120.06           N  
ANISOU  123  NZ  LYS A  18    17478   8624  19517    513   1106  -2771       N  
ATOM    124  N   GLN A  19      49.297  15.485  27.810  1.00109.42           N  
ANISOU  124  N   GLN A  19    15117   9083  17374     -9   3735  -3625       N  
ATOM    125  CA  GLN A  19      50.600  15.569  27.155  1.00 99.88           C  
ANISOU  125  CA  GLN A  19    13559   7739  16650     34   4357  -4314       C  
ATOM    126  C   GLN A  19      51.469  16.698  27.713  1.00106.28           C  
ANISOU  126  C   GLN A  19    13877   8771  17733    130   4502  -4362       C  
ATOM    127  O   GLN A  19      52.687  16.556  27.810  1.00116.65           O  
ANISOU  127  O   GLN A  19    14637   9903  19781    346   4707  -4843       O  
ATOM    128  CB  GLN A  19      50.423  15.741  25.647  1.00102.11           C  
ANISOU  128  CB  GLN A  19    14329   8081  16385   -391   5036  -4659       C  
ATOM    129  CG  GLN A  19      49.820  14.523  24.970  1.00129.87           C  
ANISOU  129  CG  GLN A  19    18281  11304  19759   -473   4978  -4770       C  
ATOM    130  CD  GLN A  19      49.637  14.707  23.480  1.00135.75           C  
ANISOU  130  CD  GLN A  19    19558  12162  19857   -940   5549  -5018       C  
ATOM    131  OE1 GLN A  19      48.574  14.413  22.934  1.00137.12           O  
ANISOU  131  OE1 GLN A  19    20374  12268  19455  -1191   5432  -4831       O  
ATOM    132  NE2 GLN A  19      50.677  15.185  22.809  1.00148.62           N  
ANISOU  132  NE2 GLN A  19    20921  13990  21558  -1099   6096  -5373       N  
ATOM    133  N   HIS A  20      50.846  17.812  28.085  1.00 93.78           N  
ANISOU  133  N   HIS A  20    12461   7580  15592    -29   4362  -3871       N  
ATOM    134  CA  HIS A  20      51.587  18.933  28.652  1.00 92.61           C  
ANISOU  134  CA  HIS A  20    11890   7653  15645     43   4460  -3868       C  
ATOM    135  C   HIS A  20      52.098  18.600  30.050  1.00102.34           C  
ANISOU  135  C   HIS A  20    12619   8715  17552    465   3857  -3711       C  
ATOM    136  O   HIS A  20      53.189  19.020  30.437  1.00118.54           O  
ANISOU  136  O   HIS A  20    14140  10730  20171    643   3954  -3979       O  
ATOM    137  CB  HIS A  20      50.723  20.194  28.697  1.00105.44           C  
ANISOU  137  CB  HIS A  20    13854   9705  16505   -228   4419  -3383       C  
ATOM    138  CG  HIS A  20      51.404  21.367  29.335  1.00100.28           C  
ANISOU  138  CG  HIS A  20    12806   9279  16017   -161   4472  -3335       C  
ATOM    139  ND1 HIS A  20      51.173  21.742  30.641  1.00 95.43           N  
ANISOU  139  ND1 HIS A  20    11989   8789  15480     44   3917  -2880       N  
ATOM    140  CD2 HIS A  20      52.318  22.241  28.849  1.00109.80           C  
ANISOU  140  CD2 HIS A  20    13805  10598  17315   -303   5029  -3698       C  
ATOM    141  CE1 HIS A  20      51.910  22.800  30.931  1.00106.08           C  
ANISOU  141  CE1 HIS A  20    13017  10316  16972     53   4096  -2956       C  
ATOM    142  NE2 HIS A  20      52.613  23.123  29.860  1.00117.85           N  
ANISOU  142  NE2 HIS A  20    14485  11807  18487   -155   4767  -3445       N  
ATOM    143  N   SER A  21      51.308  17.843  30.807  1.00101.51           N  
ANISOU  143  N   SER A  21    12713   8481  17375    590   3218  -3278       N  
ATOM    144  CA  SER A  21      51.726  17.408  32.138  1.00101.49           C  
ANISOU  144  CA  SER A  21    12382   8244  17935    934   2564  -3092       C  
ATOM    145  C   SER A  21      52.911  16.443  32.060  1.00107.64           C  
ANISOU  145  C   SER A  21    12707   8527  19663   1259   2535  -3656       C  
ATOM    146  O   SER A  21      53.780  16.440  32.933  1.00112.41           O  
ANISOU  146  O   SER A  21    12854   8926  20929   1555   2162  -3725       O  
ATOM    147  CB  SER A  21      50.561  16.750  32.876  1.00107.78           C  
ANISOU  147  CB  SER A  21    13595   8988  18368    903   1946  -2526       C  
ATOM    148  OG  SER A  21      50.029  15.673  32.125  1.00112.64           O  
ANISOU  148  OG  SER A  21    14540   9375  18881    824   1995  -2646       O  
ATOM    149  N   GLU A  22      52.936  15.631  31.006  1.00109.29           N  
ANISOU  149  N   GLU A  22    13046   8518  19963   1199   2906  -4081       N  
ATOM    150  CA  GLU A  22      54.028  14.691  30.762  1.00108.11           C  
ANISOU  150  CA  GLU A  22    12454   7997  20628   1455   2914  -4629       C  
ATOM    151  C   GLU A  22      55.308  15.413  30.358  1.00127.20           C  
ANISOU  151  C   GLU A  22    14305  10677  23347   1402   3391  -5041       C  
ATOM    152  O   GLU A  22      56.383  14.813  30.321  1.00121.76           O  
ANISOU  152  O   GLU A  22    13119   9822  23321   1572   3311  -5404       O  
ATOM    153  CB  GLU A  22      53.645  13.691  29.667  1.00132.79           C  
ANISOU  153  CB  GLU A  22    15924  10973  23557   1312   3195  -4888       C  
ATOM    154  CG  GLU A  22      52.444  12.813  29.983  1.00134.29           C  
ANISOU  154  CG  GLU A  22    16661  10854  23509   1324   2711  -4520       C  
ATOM    155  CD  GLU A  22      52.784  11.663  30.905  1.00147.30           C  
ANISOU  155  CD  GLU A  22    18124  12070  25773   1682   1912  -4409       C  
ATOM    156  OE1 GLU A  22      53.974  11.289  30.979  1.00159.26           O  
ANISOU  156  OE1 GLU A  22    19105  13483  27924   1917   1823  -4749       O  
ATOM    157  OE2 GLU A  22      51.859  11.133  31.556  1.00149.61           O  
ANISOU  157  OE2 GLU A  22    18829  12187  25829   1669   1341  -3926       O  
ATOM    158  N   GLY A  23      55.179  16.700  30.043  1.00129.29           N  
ANISOU  158  N   GLY A  23    14661  11332  23130   1128   3878  -4983       N  
ATOM    159  CA  GLY A  23      56.291  17.492  29.551  1.00111.56           C  
ANISOU  159  CA  GLY A  23    11982   9351  21054    958   4390  -5336       C  
ATOM    160  C   GLY A  23      56.530  17.258  28.070  1.00115.99           C  
ANISOU  160  C   GLY A  23    12700   9996  21375    601   5108  -5771       C  
ATOM    161  O   GLY A  23      57.545  17.683  27.519  1.00120.49           O  
ANISOU  161  O   GLY A  23    12916  10697  22166    403   5567  -6140       O  
ATOM    162  N   LYS A  24      55.585  16.581  27.423  1.00115.10           N  
ANISOU  162  N   LYS A  24    13152   9781  20800    479   5193  -5721       N  
ATOM    163  CA  LYS A  24      55.717  16.214  26.017  1.00123.07           C  
ANISOU  163  CA  LYS A  24    14401  10820  21538    132   5810  -6106       C  
ATOM    164  C   LYS A  24      55.080  17.245  25.087  1.00116.90           C  
ANISOU  164  C   LYS A  24    14225  10368  19824   -388   6344  -5973       C  
ATOM    165  O   LYS A  24      55.034  17.051  23.873  1.00120.41           O  
ANISOU  165  O   LYS A  24    15025  10840  19884   -759   6833  -6210       O  
ATOM    166  CB  LYS A  24      55.099  14.835  25.768  1.00121.21           C  
ANISOU  166  CB  LYS A  24    14476  10257  21322    265   5565  -6144       C  
ATOM    167  N   LEU A  25      54.586  18.338  25.658  1.00132.65           N  
ANISOU  167  N   LEU A  25    16366  12586  21447   -427   6211  -5583       N  
ATOM    168  CA  LEU A  25      53.929  19.373  24.867  1.00122.78           C  
ANISOU  168  CA  LEU A  25    15729  11620  19303   -906   6586  -5395       C  
ATOM    169  C   LEU A  25      54.104  20.755  25.491  1.00112.73           C  
ANISOU  169  C   LEU A  25    14289  10623  17921   -937   6559  -5150       C  
ATOM    170  O   LEU A  25      54.287  20.881  26.702  1.00101.92           O  
ANISOU  170  O   LEU A  25    12484   9224  17016   -553   6140  -4986       O  
ATOM    171  CB  LEU A  25      52.441  19.049  24.710  1.00128.87           C  
ANISOU  171  CB  LEU A  25    17225  12313  19426   -989   6343  -5060       C  
ATOM    172  CG  LEU A  25      51.607  19.948  23.796  1.00128.93           C  
ANISOU  172  CG  LEU A  25    17983  12541  18464  -1497   6593  -4842       C  
ATOM    173  CD1 LEU A  25      52.170  19.941  22.385  1.00137.86           C  
ANISOU  173  CD1 LEU A  25    19342  13708  19328  -1954   7165  -5175       C  
ATOM    174  CD2 LEU A  25      50.151  19.516  23.801  1.00127.75           C  
ANISOU  174  CD2 LEU A  25    18472  12258  17810  -1531   6215  -4515       C  
ATOM    175  N   THR A  26      54.060  21.786  24.649  1.00125.71           N  
ANISOU  175  N   THR A  26    16315  12505  18945  -1411   6968  -5112       N  
ATOM    176  CA  THR A  26      54.107  23.172  25.105  1.00126.81           C  
ANISOU  176  CA  THR A  26    16415  12908  18861  -1499   6940  -4850       C  
ATOM    177  C   THR A  26      52.788  23.876  24.800  1.00111.40           C  
ANISOU  177  C   THR A  26    15222  11102  16005  -1765   6845  -4434       C  
ATOM    178  O   THR A  26      52.298  23.833  23.669  1.00106.63           O  
ANISOU  178  O   THR A  26    15246  10472  14799  -2171   7057  -4444       O  
ATOM    179  CB  THR A  26      55.264  23.952  24.448  1.00134.88           C  
ANISOU  179  CB  THR A  26    17244  14036  19967  -1857   7411  -5137       C  
ATOM    180  OG1 THR A  26      56.515  23.374  24.836  1.00147.43           O  
ANISOU  180  OG1 THR A  26    18070  15485  22461  -1600   7444  -5533       O  
ATOM    181  CG2 THR A  26      55.240  25.408  24.875  1.00139.04           C  
ANISOU  181  CG2 THR A  26    17811  14810  20207  -1966   7333  -4840       C  
ATOM    182  N   LEU A  27      52.211  24.513  25.815  1.00 90.67           N  
ANISOU  182  N   LEU A  27    12544   8608  13301  -1542   6492  -4070       N  
ATOM    183  CA  LEU A  27      50.959  25.247  25.655  1.00101.97           C  
ANISOU  183  CA  LEU A  27    14579  10221  13944  -1768   6194  -3564       C  
ATOM    184  C   LEU A  27      51.108  26.669  26.184  1.00102.23           C  
ANISOU  184  C   LEU A  27    14472  10527  13843  -1809   6120  -3308       C  
ATOM    185  O   LEU A  27      51.903  26.912  27.092  1.00 82.92           O  
ANISOU  185  O   LEU A  27    11412   8139  11954  -1528   6074  -3369       O  
ATOM    186  CB  LEU A  27      49.816  24.528  26.376  1.00 99.90           C  
ANISOU  186  CB  LEU A  27    14371   9932  13655  -1503   5477  -3087       C  
ATOM    187  CG  LEU A  27      49.468  23.130  25.861  1.00 97.94           C  
ANISOU  187  CG  LEU A  27    14347   9407  13461  -1483   5453  -3256       C  
ATOM    188  CD1 LEU A  27      48.464  22.440  26.772  1.00 81.23           C  
ANISOU  188  CD1 LEU A  27    12187   7266  11411  -1216   4752  -2791       C  
ATOM    189  CD2 LEU A  27      48.936  23.207  24.440  1.00108.56           C  
ANISOU  189  CD2 LEU A  27    16445  10692  14109  -1959   5760  -3367       C  
ATOM    190  N   LYS A  28      50.348  27.605  25.617  1.00104.52           N  
ANISOU  190  N   LYS A  28    15344  10951  13418  -2156   6060  -3027       N  
ATOM    191  CA  LYS A  28      50.431  29.002  26.037  1.00 97.59           C  
ANISOU  191  CA  LYS A  28    14399  10304  12376  -2221   5974  -2787       C  
ATOM    192  C   LYS A  28      50.062  29.120  27.510  1.00 79.79           C  
ANISOU  192  C   LYS A  28    11657   8197  10463  -1783   5365  -2378       C  
ATOM    193  O   LYS A  28      48.979  28.721  27.930  1.00 83.22           O  
ANISOU  193  O   LYS A  28    12209   8642  10770  -1644   4854  -2015       O  
ATOM    194  CB  LYS A  28      49.530  29.894  25.174  1.00100.97           C  
ANISOU  194  CB  LYS A  28    15593  10774  11996  -2646   5869  -2522       C  
ATOM    195  CG  LYS A  28      48.158  29.311  24.876  1.00110.94           C  
ANISOU  195  CG  LYS A  28    17313  11941  12896  -2669   5376  -2210       C  
ATOM    196  N   THR A  29      50.971  29.692  28.287  1.00 82.61           N  
ANISOU  196  N   THR A  29    11487   8659  11240  -1607   5442  -2456       N  
ATOM    197  CA  THR A  29      50.888  29.597  29.733  1.00 83.04           C  
ANISOU  197  CA  THR A  29    11057   8792  11702  -1197   4929  -2169       C  
ATOM    198  C   THR A  29      51.022  30.955  30.409  1.00 87.04           C  
ANISOU  198  C   THR A  29    11404   9531  12138  -1190   4802  -1944       C  
ATOM    199  O   THR A  29      51.899  31.751  30.067  1.00 90.72           O  
ANISOU  199  O   THR A  29    11775  10047  12646  -1361   5205  -2186       O  
ATOM    200  CB  THR A  29      51.973  28.651  30.272  1.00 83.18           C  
ANISOU  200  CB  THR A  29    10492   8617  12495   -880   4994  -2508       C  
ATOM    201  OG1 THR A  29      51.887  27.392  29.593  1.00103.70           O  
ANISOU  201  OG1 THR A  29    13241  10972  15187   -886   5135  -2762       O  
ATOM    202  CG2 THR A  29      51.804  28.429  31.760  1.00 70.58           C  
ANISOU  202  CG2 THR A  29     8542   7042  11234   -506   4381  -2170       C  
ATOM    203  N   HIS A  30      50.142  31.208  31.371  1.00 83.82           N  
ANISOU  203  N   HIS A  30    10970   9254  11624  -1018   4269  -1505       N  
ATOM    204  CA  HIS A  30      50.164  32.446  32.130  1.00 81.32           C  
ANISOU  204  CA  HIS A  30    10502   9145  11252   -982   4097  -1279       C  
ATOM    205  C   HIS A  30      50.520  32.174  33.585  1.00 88.17           C  
ANISOU  205  C   HIS A  30    10885  10029  12586   -633   3746  -1155       C  
ATOM    206  O   HIS A  30      49.751  31.552  34.320  1.00 91.50           O  
ANISOU  206  O   HIS A  30    11325  10436  13005   -480   3345   -896       O  
ATOM    207  CB  HIS A  30      48.812  33.156  32.035  1.00 80.59           C  
ANISOU  207  CB  HIS A  30    10807   9181  10632  -1119   3787   -910       C  
ATOM    208  CG  HIS A  30      48.429  33.539  30.639  1.00 96.39           C  
ANISOU  208  CG  HIS A  30    13370  11118  12134  -1487   4002   -980       C  
ATOM    209  ND1 HIS A  30      47.222  33.187  30.076  1.00104.59           N  
ANISOU  209  ND1 HIS A  30    14835  12084  12822  -1604   3750   -807       N  
ATOM    210  CD2 HIS A  30      49.095  34.244  29.693  1.00103.39           C  
ANISOU  210  CD2 HIS A  30    14513  11975  12795  -1805   4423  -1202       C  
ATOM    211  CE1 HIS A  30      47.160  33.657  28.842  1.00110.34           C  
ANISOU  211  CE1 HIS A  30    16093  12718  13113  -1967   3951   -901       C  
ATOM    212  NE2 HIS A  30      48.284  34.302  28.585  1.00107.14           N  
ANISOU  212  NE2 HIS A  30    15625  12341  12744  -2117   4383  -1138       N  
ATOM    213  N   HIS A  31      51.698  32.632  33.992  1.00 97.13           N  
ANISOU  213  N   HIS A  31    11620  11172  14114   -545   3890  -1351       N  
ATOM    214  CA  HIS A  31      52.109  32.533  35.383  1.00104.43           C  
ANISOU  214  CA  HIS A  31    12146  12085  15449   -250   3498  -1221       C  
ATOM    215  C   HIS A  31      51.628  33.763  36.142  1.00 93.32           C  
ANISOU  215  C   HIS A  31    10791  10918  13751   -280   3266   -894       C  
ATOM    216  O   HIS A  31      51.918  34.896  35.754  1.00 90.93           O  
ANISOU  216  O   HIS A  31    10522  10743  13285   -448   3504   -952       O  
ATOM    217  CB  HIS A  31      53.627  32.389  35.490  1.00111.38           C  
ANISOU  217  CB  HIS A  31    12520  12813  16985   -119   3694  -1616       C  
ATOM    218  CG  HIS A  31      54.176  31.220  34.736  1.00120.94           C  
ANISOU  218  CG  HIS A  31    13613  13763  18576    -78   3966  -2024       C  
ATOM    219  ND1 HIS A  31      54.316  29.970  35.299  1.00130.98           N  
ANISOU  219  ND1 HIS A  31    14695  14774  20297    203   3609  -2052       N  
ATOM    220  CD2 HIS A  31      54.620  31.110  33.461  1.00134.61           C  
ANISOU  220  CD2 HIS A  31    15417  15430  20300   -306   4568  -2442       C  
ATOM    221  CE1 HIS A  31      54.822  29.140  34.404  1.00135.57           C  
ANISOU  221  CE1 HIS A  31    15184  15140  21185    188   3971  -2487       C  
ATOM    222  NE2 HIS A  31      55.016  29.807  33.281  1.00140.70           N  
ANISOU  222  NE2 HIS A  31    15991  15916  21554   -132   4590  -2745       N  
ATOM    223  N   VAL A  32      50.874  33.539  37.212  1.00 85.67           N  
ANISOU  223  N   VAL A  32     9857   9992  12701   -148   2822   -569       N  
ATOM    224  CA  VAL A  32      50.320  34.639  37.989  1.00 93.80           C  
ANISOU  224  CA  VAL A  32    10936  11238  13466   -178   2618   -294       C  
ATOM    225  C   VAL A  32      50.504  34.423  39.486  1.00116.98           C  
ANISOU  225  C   VAL A  32    13687  14146  16613      7   2213   -118       C  
ATOM    226  O   VAL A  32      50.055  33.419  40.040  1.00122.08           O  
ANISOU  226  O   VAL A  32    14420  14679  17287     80   1945     15       O  
ATOM    227  CB  VAL A  32      48.815  34.841  37.697  1.00 86.29           C  
ANISOU  227  CB  VAL A  32    10342  10406  12038   -320   2528    -65       C  
ATOM    228  CG1 VAL A  32      48.231  35.893  38.623  1.00 70.56           C  
ANISOU  228  CG1 VAL A  32     8336   8607   9867   -321   2317    163       C  
ATOM    229  CG2 VAL A  32      48.594  35.231  36.244  1.00 87.75           C  
ANISOU  229  CG2 VAL A  32    10811  10585  11943   -543   2828   -193       C  
ATOM    230  N   ASN A  33      51.172  35.371  40.134  1.00128.94           N  
ANISOU  230  N   ASN A  33    14999  15745  18246     46   2157   -113       N  
ATOM    231  CA  ASN A  33      51.281  35.373  41.586  1.00132.69           C  
ANISOU  231  CA  ASN A  33    15399  16202  18814    160   1748     82       C  
ATOM    232  C   ASN A  33      50.768  36.691  42.159  1.00131.86           C  
ANISOU  232  C   ASN A  33    15377  16338  18384     65   1712    257       C  
ATOM    233  O   ASN A  33      51.057  37.764  41.630  1.00124.70           O  
ANISOU  233  O   ASN A  33    14408  15551  17419    -12   1944    161       O  
ATOM    234  CB  ASN A  33      52.726  35.114  42.024  1.00137.45           C  
ANISOU  234  CB  ASN A  33    15641  16598  19987    336   1598   -104       C  
ATOM    235  CG  ASN A  33      53.744  35.795  41.127  1.00133.02           C  
ANISOU  235  CG  ASN A  33    14792  16060  19690    299   2001   -432       C  
ATOM    236  OD1 ASN A  33      53.459  36.817  40.503  1.00132.36           O  
ANISOU  236  OD1 ASN A  33    14827  16178  19287    122   2308   -439       O  
ATOM    237  ND2 ASN A  33      54.940  35.224  41.056  1.00123.66           N  
ANISOU  237  ND2 ASN A  33    13230  14639  19116    447   1994   -727       N  
ATOM    238  N   ASP A  34      49.993  36.602  43.234  1.00148.91           N  
ANISOU  238  N   ASP A  34    17702  18552  20325     41   1440    493       N  
ATOM    239  CA  ASP A  34      49.381  37.779  43.837  1.00162.44           C  
ANISOU  239  CA  ASP A  34    19493  20480  21746    -52   1424    620       C  
ATOM    240  C   ASP A  34      50.244  38.325  44.962  1.00173.89           C  
ANISOU  240  C   ASP A  34    20822  21910  23338      7   1194    658       C  
ATOM    241  O   ASP A  34      50.894  37.565  45.680  1.00183.01           O  
ANISOU  241  O   ASP A  34    21948  22870  24719     93    898    693       O  
ATOM    242  CB  ASP A  34      47.985  37.452  44.372  1.00164.77           C  
ANISOU  242  CB  ASP A  34    20027  20857  21721   -167   1343    792       C  
ATOM    243  CG  ASP A  34      48.028  36.568  45.604  1.00170.89           C  
ANISOU  243  CG  ASP A  34    20940  21501  22490   -183   1039    938       C  
ATOM    244  OD1 ASP A  34      48.819  35.600  45.614  1.00171.18           O  
ANISOU  244  OD1 ASP A  34    20939  21304  22798    -75    859    914       O  
ATOM    245  OD2 ASP A  34      47.281  36.850  46.565  1.00170.65           O  
ANISOU  245  OD2 ASP A  34    21075  21574  22190   -324    976   1059       O  
ATOM    246  N   VAL A  35      50.258  39.645  45.112  1.00171.87           N  
ANISOU  246  N   VAL A  35    20520  21820  22962    -42   1277    653       N  
ATOM    247  CA  VAL A  35      50.971  40.244  46.226  1.00163.84           C  
ANISOU  247  CA  VAL A  35    19431  20791  22028    -12   1042    700       C  
ATOM    248  C   VAL A  35      50.226  39.911  47.514  1.00179.39           C  
ANISOU  248  C   VAL A  35    21674  22767  23721   -104    794    895       C  
ATOM    249  O   VAL A  35      49.049  40.237  47.668  1.00175.67           O  
ANISOU  249  O   VAL A  35    21365  22455  22925   -230    926    952       O  
ATOM    250  CB  VAL A  35      51.116  41.777  46.062  1.00142.43           C  
ANISOU  250  CB  VAL A  35    16634  18248  19234    -61   1199    642       C  
ATOM    251  CG1 VAL A  35      49.826  42.394  45.528  1.00114.42           C  
ANISOU  251  CG1 VAL A  35    13248  14870  15358   -164   1399    671       C  
ATOM    252  CG2 VAL A  35      51.536  42.420  47.376  1.00134.71           C  
ANISOU  252  CG2 VAL A  35    15667  17279  18236    -66    933    722       C  
ATOM    253  N   GLY A  36      50.918  39.249  48.434  1.00204.08           N  
ANISOU  253  N   GLY A  36    24862  25688  26993    -66    425    975       N  
ATOM    254  CA  GLY A  36      50.317  38.863  49.696  1.00212.28           C  
ANISOU  254  CA  GLY A  36    26264  26684  27711   -227    180   1166       C  
ATOM    255  C   GLY A  36      50.152  40.091  50.560  1.00203.12           C  
ANISOU  255  C   GLY A  36    25196  25687  26294   -345    190   1195       C  
ATOM    256  O   GLY A  36      49.091  40.337  51.131  1.00208.51           O  
ANISOU  256  O   GLY A  36    26117  26512  26595   -541    325   1246       O  
ATOM    257  N   GLU A  37      51.225  40.864  50.651  1.00156.69           N  
ANISOU  257  N   GLU A  37    19103  19774  20658   -237     68   1127       N  
ATOM    258  CA  GLU A  37      51.194  42.140  51.340  1.00125.10           C  
ANISOU  258  CA  GLU A  37    15155  15919  16460   -326     86   1125       C  
ATOM    259  C   GLU A  37      52.245  43.072  50.753  1.00124.62           C  
ANISOU  259  C   GLU A  37    14732  15878  16738   -185    137    984       C  
ATOM    260  O   GLU A  37      53.296  42.628  50.293  1.00127.70           O  
ANISOU  260  O   GLU A  37    14860  16102  17560    -40     21    897       O  
ATOM    261  CB  GLU A  37      51.424  41.950  52.841  1.00102.65           C  
ANISOU  261  CB  GLU A  37    12667  12926  13409   -472   -320   1276       C  
ATOM    262  N   LEU A  38      51.949  44.366  50.760  1.00106.18           N  
ANISOU  262  N   LEU A  38    12373  13732  14238   -241    327    932       N  
ATOM    263  CA  LEU A  38      52.929  45.370  50.380  1.00 87.00           C  
ANISOU  263  CA  LEU A  38     9670  11317  12068   -172    360    816       C  
ATOM    264  C   LEU A  38      53.634  45.870  51.628  1.00 79.83           C  
ANISOU  264  C   LEU A  38     8842  10324  11165   -209      2    873       C  
ATOM    265  O   LEU A  38      53.026  45.987  52.692  1.00 87.07           O  
ANISOU  265  O   LEU A  38    10089  11270  11724   -344   -123    977       O  
ATOM    266  CB  LEU A  38      52.268  46.534  49.640  1.00 93.17           C  
ANISOU  266  CB  LEU A  38    10421  12297  12683   -219    699    737       C  
ATOM    267  CG  LEU A  38      51.764  46.269  48.223  1.00 92.26           C  
ANISOU  267  CG  LEU A  38    10243  12227  12586   -202   1007    668       C  
ATOM    268  CD1 LEU A  38      51.052  47.497  47.687  1.00 89.06           C  
ANISOU  268  CD1 LEU A  38     9892  11949  11996   -265   1194    623       C  
ATOM    269  CD2 LEU A  38      52.916  45.882  47.316  1.00104.18           C  
ANISOU  269  CD2 LEU A  38    11499  13621  14463   -141   1099    543       C  
ATOM    270  N   ASN A  39      54.924  46.146  51.504  1.00 76.76           N  
ANISOU  270  N   ASN A  39     8160   9815  11190   -117   -155    782       N  
ATOM    271  CA  ASN A  39      55.677  46.700  52.616  1.00 92.03           C  
ANISOU  271  CA  ASN A  39    10147  11643  13175   -150   -543    826       C  
ATOM    272  C   ASN A  39      56.452  47.932  52.183  1.00 94.69           C  
ANISOU  272  C   ASN A  39    10182  12050  13746   -137   -408    680       C  
ATOM    273  O   ASN A  39      56.882  48.041  51.034  1.00101.64           O  
ANISOU  273  O   ASN A  39    10741  12961  14917    -87   -108    523       O  
ATOM    274  CB  ASN A  39      56.624  45.652  53.205  1.00106.05           C  
ANISOU  274  CB  ASN A  39    11879  13099  15315    -60  -1068    871       C  
ATOM    275  CG  ASN A  39      57.399  44.897  52.141  1.00132.04           C  
ANISOU  275  CG  ASN A  39    14719  16258  19190    120   -977    691       C  
ATOM    276  OD1 ASN A  39      57.483  45.327  50.990  1.00138.79           O  
ANISOU  276  OD1 ASN A  39    15289  17261  20186    139   -515    517       O  
ATOM    277  ND2 ASN A  39      57.969  43.761  52.523  1.00141.81           N  
ANISOU  277  ND2 ASN A  39    15925  17187  20770    229  -1426    716       N  
ATOM    278  N   ILE A  40      56.613  48.871  53.105  1.00 82.76           N  
ANISOU  278  N   ILE A  40     8816  10556  12073   -221   -607    724       N  
ATOM    279  CA  ILE A  40      57.374  50.070  52.812  1.00 71.07           C  
ANISOU  279  CA  ILE A  40     7081   9119  10803   -235   -524    600       C  
ATOM    280  C   ILE A  40      58.207  50.463  54.030  1.00 61.99           C  
ANISOU  280  C   ILE A  40     5992   7810   9751   -269  -1021    646       C  
ATOM    281  O   ILE A  40      57.725  50.440  55.166  1.00 60.07           O  
ANISOU  281  O   ILE A  40     6163   7536   9123   -368  -1282    787       O  
ATOM    282  CB  ILE A  40      56.441  51.224  52.363  1.00 62.17           C  
ANISOU  282  CB  ILE A  40     6090   8221   9311   -325   -140    576       C  
ATOM    283  CG1 ILE A  40      57.250  52.427  51.878  1.00 65.84           C  
ANISOU  283  CG1 ILE A  40     6319   8706   9993   -369    -29    453       C  
ATOM    284  CG2 ILE A  40      55.468  51.612  53.464  1.00 68.51           C  
ANISOU  284  CG2 ILE A  40     7293   9101   9636   -423   -231    673       C  
ATOM    285  CD1 ILE A  40      56.427  53.431  51.102  1.00 52.61           C  
ANISOU  285  CD1 ILE A  40     4755   7183   8049   -443    321    420       C  
ATOM    286  N   SER A  41      59.475  50.783  53.786  1.00 68.05           N  
ANISOU  286  N   SER A  41     6356   8458  11044   -216  -1148    507       N  
ATOM    287  CA  SER A  41      60.393  51.178  54.849  1.00 60.95           C  
ANISOU  287  CA  SER A  41     5453   7370  10333   -240  -1676    530       C  
ATOM    288  C   SER A  41      60.203  52.652  55.191  1.00 78.19           C  
ANISOU  288  C   SER A  41     7797   9705  12207   -376  -1568    530       C  
ATOM    289  O   SER A  41      59.680  53.416  54.376  1.00 57.01           O  
ANISOU  289  O   SER A  41     5076   7230   9355   -421  -1093    463       O  
ATOM    290  CB  SER A  41      61.841  50.909  54.433  1.00 64.38           C  
ANISOU  290  CB  SER A  41     5304   7593  11563   -126  -1856    327       C  
ATOM    291  OG  SER A  41      62.254  51.810  53.423  1.00 63.56           O  
ANISOU  291  OG  SER A  41     4839   7638  11675   -185  -1380    123       O  
ATOM    292  N   PRO A  42      60.618  53.057  56.401  1.00 84.97           N  
ANISOU  292  N   PRO A  42     8876  10426  12984   -451  -2051    608       N  
ATOM    293  CA  PRO A  42      60.560  54.477  56.767  1.00 70.55           C  
ANISOU  293  CA  PRO A  42     7183   8707  10917   -575  -1985    581       C  
ATOM    294  C   PRO A  42      61.341  55.348  55.787  1.00 61.27           C  
ANISOU  294  C   PRO A  42     5532   7587  10159   -569  -1711    399       C  
ATOM    295  O   PRO A  42      60.847  56.393  55.349  1.00 82.67           O  
ANISOU  295  O   PRO A  42     8318  10470  12622   -650  -1355    359       O  
ATOM    296  CB  PRO A  42      61.200  54.506  58.156  1.00 73.43           C  
ANISOU  296  CB  PRO A  42     7803   8831  11265   -651  -2650    676       C  
ATOM    297  CG  PRO A  42      60.990  53.136  58.700  1.00 80.66           C  
ANISOU  297  CG  PRO A  42     8987   9567  12092   -628  -2997    824       C  
ATOM    298  CD  PRO A  42      61.080  52.214  57.520  1.00 80.74           C  
ANISOU  298  CD  PRO A  42     8564   9597  12517   -448  -2720    738       C  
ATOM    299  N   ASP A  43      62.545  54.896  55.446  1.00 64.12           N  
ANISOU  299  N   ASP A  43     5413   7776  11173   -493  -1880    269       N  
ATOM    300  CA  ASP A  43      63.415  55.585  54.499  1.00 77.23           C  
ANISOU  300  CA  ASP A  43     6590   9466  13289   -546  -1574     50       C  
ATOM    301  C   ASP A  43      62.699  55.861  53.181  1.00 75.79           C  
ANISOU  301  C   ASP A  43     6416   9508  12872   -610   -900     -8       C  
ATOM    302  O   ASP A  43      62.833  56.941  52.605  1.00 72.00           O  
ANISOU  302  O   ASP A  43     5891   9118  12348   -756   -603    -89       O  
ATOM    303  CB  ASP A  43      64.681  54.761  54.244  1.00101.76           C  
ANISOU  303  CB  ASP A  43     9118  12343  17202   -440  -1777   -149       C  
ATOM    304  CG  ASP A  43      65.351  54.304  55.529  1.00123.59           C  
ANISOU  304  CG  ASP A  43    11908  14808  20244   -353  -2578    -71       C  
ATOM    305  OD1 ASP A  43      64.641  54.125  56.540  1.00131.11           O  
ANISOU  305  OD1 ASP A  43    13423  15730  20662   -370  -2928    176       O  
ATOM    306  OD2 ASP A  43      66.588  54.120  55.526  1.00128.03           O1+
ANISOU  306  OD2 ASP A  43    11940  15139  21566   -291  -2867   -274       O1+
ATOM    307  N   GLU A  44      61.936  54.878  52.711  1.00 67.39           N  
ANISOU  307  N   GLU A  44     5457   8502  11644   -521   -705     46       N  
ATOM    308  CA  GLU A  44      61.153  55.028  51.490  1.00 61.55           C  
ANISOU  308  CA  GLU A  44     4804   7937  10643   -584   -151     18       C  
ATOM    309  C   GLU A  44      60.094  56.114  51.624  1.00 62.47           C  
ANISOU  309  C   GLU A  44     5331   8202  10205   -668    -40    135       C  
ATOM    310  O   GLU A  44      59.847  56.864  50.686  1.00 68.03           O  
ANISOU  310  O   GLU A  44     6082   8983  10785   -786    301     85       O  
ATOM    311  CB  GLU A  44      60.483  53.711  51.112  1.00 76.39           C  
ANISOU  311  CB  GLU A  44     6750   9829  12447   -466    -46     68       C  
ATOM    312  CG  GLU A  44      61.382  52.722  50.402  1.00 97.90           C  
ANISOU  312  CG  GLU A  44     9034  12426  15737   -400     63   -127       C  
ATOM    313  CD  GLU A  44      60.608  51.533  49.868  1.00104.97           C  
ANISOU  313  CD  GLU A  44    10045  13345  16495   -307    229    -82       C  
ATOM    314  OE1 GLU A  44      60.363  51.483  48.644  1.00108.55           O  
ANISOU  314  OE1 GLU A  44    10470  13884  16892   -390    704   -186       O  
ATOM    315  OE2 GLU A  44      60.235  50.653  50.675  1.00100.79           O1+
ANISOU  315  OE2 GLU A  44     9684  12730  15882   -183   -126     65       O1+
ATOM    316  N   ILE A  45      59.466  56.190  52.791  1.00 58.42           N  
ANISOU  316  N   ILE A  45     5135   7698   9365   -629   -336    269       N  
ATOM    317  CA  ILE A  45      58.444  57.199  53.036  1.00 63.39           C  
ANISOU  317  CA  ILE A  45     6101   8439   9545   -687   -240    316       C  
ATOM    318  C   ILE A  45      59.063  58.590  53.001  1.00 65.40           C  
ANISOU  318  C   ILE A  45     6301   8667   9881   -803   -257    244       C  
ATOM    319  O   ILE A  45      58.531  59.519  52.374  1.00 63.26           O  
ANISOU  319  O   ILE A  45     6153   8451   9431   -871    -34    218       O  
ATOM    320  CB  ILE A  45      57.745  56.970  54.386  1.00 57.66           C  
ANISOU  320  CB  ILE A  45     5724   7715   8468   -675   -501    413       C  
ATOM    321  CG1 ILE A  45      57.172  55.553  54.441  1.00 58.60           C  
ANISOU  321  CG1 ILE A  45     5929   7839   8499   -604   -495    495       C  
ATOM    322  CG2 ILE A  45      56.654  58.003  54.601  1.00 62.99           C  
ANISOU  322  CG2 ILE A  45     6674   8495   8766   -725   -343    379       C  
ATOM    323  CD1 ILE A  45      56.463  55.226  55.730  1.00 61.04           C  
ANISOU  323  CD1 ILE A  45     6643   8139   8409   -674   -688    580       C  
ATOM    324  N   VAL A  46      60.202  58.721  53.672  1.00 56.66           N  
ANISOU  324  N   VAL A  46     5017   7441   9070   -831   -570    212       N  
ATOM    325  CA  VAL A  46      60.943  59.973  53.661  1.00 56.65           C  
ANISOU  325  CA  VAL A  46     4922   7395   9207   -962   -607    134       C  
ATOM    326  C   VAL A  46      61.304  60.380  52.235  1.00 65.47           C  
ANISOU  326  C   VAL A  46     5828   8540  10507  -1090   -188     22       C  
ATOM    327  O   VAL A  46      61.062  61.514  51.834  1.00 83.72           O  
ANISOU  327  O   VAL A  46     8306  10870  12635  -1219    -44     13       O  
ATOM    328  CB  VAL A  46      62.228  59.880  54.499  1.00 60.12           C  
ANISOU  328  CB  VAL A  46     5121   7670  10052   -972  -1040     93       C  
ATOM    329  CG1 VAL A  46      63.002  61.185  54.424  1.00 61.67           C  
ANISOU  329  CG1 VAL A  46     5196   7822  10415  -1133  -1049     -2       C  
ATOM    330  CG2 VAL A  46      61.896  59.529  55.937  1.00 60.84           C  
ANISOU  330  CG2 VAL A  46     5554   7690   9873   -918  -1499    224       C  
ATOM    331  N   SER A  47      61.864  59.447  51.469  1.00 61.39           N  
ANISOU  331  N   SER A  47     4988   8002  10336  -1079      8    -74       N  
ATOM    332  CA  SER A  47      62.321  59.748  50.115  1.00 64.78           C  
ANISOU  332  CA  SER A  47     5248   8441  10923  -1275    461   -219       C  
ATOM    333  C   SER A  47      61.156  60.137  49.212  1.00 58.67           C  
ANISOU  333  C   SER A  47     4869   7751   9673  -1347    757   -130       C  
ATOM    334  O   SER A  47      61.273  61.049  48.392  1.00 69.52           O  
ANISOU  334  O   SER A  47     6368   9102  10945  -1578    994   -171       O  
ATOM    335  CB  SER A  47      63.072  58.557  49.519  1.00 80.00           C  
ANISOU  335  CB  SER A  47     6753  10319  13323  -1244    648   -391       C  
ATOM    336  OG  SER A  47      62.195  57.477  49.262  1.00102.79           O  
ANISOU  336  OG  SER A  47     9785  13260  16012  -1087    723   -304       O  
ATOM    337  N   ILE A  48      60.036  59.437  49.368  1.00 58.67           N  
ANISOU  337  N   ILE A  48     5079   7817   9394  -1170    708    -10       N  
ATOM    338  CA  ILE A  48      58.818  59.759  48.634  1.00 56.51           C  
ANISOU  338  CA  ILE A  48     5160   7588   8723  -1195    878     71       C  
ATOM    339  C   ILE A  48      58.397  61.190  48.925  1.00 53.25           C  
ANISOU  339  C   ILE A  48     5014   7138   8079  -1262    736    113       C  
ATOM    340  O   ILE A  48      58.114  61.963  48.010  1.00 59.46           O  
ANISOU  340  O   ILE A  48     6023   7863   8706  -1420    873    120       O  
ATOM    341  CB  ILE A  48      57.657  58.815  49.000  1.00 57.15           C  
ANISOU  341  CB  ILE A  48     5375   7742   8597   -986    799    168       C  
ATOM    342  CG1 ILE A  48      57.864  57.435  48.381  1.00 61.48           C  
ANISOU  342  CG1 ILE A  48     5740   8300   9320   -939    980    132       C  
ATOM    343  CG2 ILE A  48      56.329  59.392  48.533  1.00 47.09           C  
ANISOU  343  CG2 ILE A  48     4430   6480   6984   -982    847    225       C  
ATOM    344  CD1 ILE A  48      56.813  56.429  48.800  1.00 58.31           C  
ANISOU  344  CD1 ILE A  48     5461   7957   8736   -762    891    230       C  
ATOM    345  N   ARG A  49      58.366  61.541  50.206  1.00 53.86           N  
ANISOU  345  N   ARG A  49     5113   7223   8130  -1159    437    136       N  
ATOM    346  CA  ARG A  49      57.968  62.887  50.599  1.00 61.73           C  
ANISOU  346  CA  ARG A  49     6345   8168   8942  -1199    290    138       C  
ATOM    347  C   ARG A  49      58.941  63.927  50.055  1.00 62.59           C  
ANISOU  347  C   ARG A  49     6417   8177   9186  -1437    349     88       C  
ATOM    348  O   ARG A  49      58.550  65.038  49.702  1.00 52.90           O  
ANISOU  348  O   ARG A  49     5446   6860   7793  -1534    324    100       O  
ATOM    349  CB  ARG A  49      57.879  62.993  52.121  1.00 72.46           C  
ANISOU  349  CB  ARG A  49     7753   9545  10233  -1092     -6    139       C  
ATOM    350  CG  ARG A  49      57.426  64.346  52.624  1.00 51.30           C  
ANISOU  350  CG  ARG A  49     5308   6803   7380  -1117   -142     95       C  
ATOM    351  CD  ARG A  49      57.272  64.333  54.125  1.00 51.95           C  
ANISOU  351  CD  ARG A  49     5502   6906   7330  -1054   -375     69       C  
ATOM    352  NE  ARG A  49      58.509  63.949  54.796  1.00 63.81           N  
ANISOU  352  NE  ARG A  49     6843   8370   9030  -1108   -603    102       N  
ATOM    353  CZ  ARG A  49      59.451  64.807  55.170  1.00 82.28           C  
ANISOU  353  CZ  ARG A  49     9134  10616  11513  -1221   -801     69       C  
ATOM    354  NH1 ARG A  49      59.300  66.103  54.934  1.00 83.07           N1+
ANISOU  354  NH1 ARG A  49     9365  10657  11541  -1301   -772     15       N1+
ATOM    355  NH2 ARG A  49      60.546  64.372  55.780  1.00 85.46           N  
ANISOU  355  NH2 ARG A  49     9356  10952  12163  -1253  -1073     86       N  
ATOM    356  N   GLU A  50      60.209  63.545  49.971  1.00 60.03           N  
ANISOU  356  N   GLU A  50     5764   7844   9200  -1541    420     13       N  
ATOM    357  CA  GLU A  50      61.270  64.466  49.591  1.00 71.88           C  
ANISOU  357  CA  GLU A  50     7164   9257  10890  -1807    503    -74       C  
ATOM    358  C   GLU A  50      61.299  64.728  48.084  1.00 84.00           C  
ANISOU  358  C   GLU A  50     8847  10745  12324  -2082    894   -105       C  
ATOM    359  O   GLU A  50      61.644  65.830  47.651  1.00 80.93           O  
ANISOU  359  O   GLU A  50     8630  10253  11866  -2349    954   -121       O  
ATOM    360  CB  GLU A  50      62.622  63.924  50.064  1.00 79.05           C  
ANISOU  360  CB  GLU A  50     7594  10149  12292  -1822    433   -199       C  
ATOM    361  CG  GLU A  50      63.699  64.981  50.258  1.00 97.23           C  
ANISOU  361  CG  GLU A  50     9751  12356  14834  -2048    362   -296       C  
ATOM    362  CD  GLU A  50      64.437  65.314  48.977  1.00122.38           C  
ANISOU  362  CD  GLU A  50    12819  15502  18177  -2402    819   -443       C  
ATOM    363  OE1 GLU A  50      64.354  64.517  48.018  1.00133.98           O  
ANISOU  363  OE1 GLU A  50    14226  17014  19666  -2459   1187   -509       O  
ATOM    364  OE2 GLU A  50      65.102  66.371  48.931  1.00128.89           O1+
ANISOU  364  OE2 GLU A  50    13644  16244  19085  -2658    832   -505       O1+
ATOM    365  N   GLN A  51      60.935  63.729  47.285  1.00 78.15           N  
ANISOU  365  N   GLN A  51     8101  10057  11537  -2055   1148   -110       N  
ATOM    366  CA  GLN A  51      60.975  63.895  45.833  1.00 77.03           C  
ANISOU  366  CA  GLN A  51     8181   9850  11238  -2370   1528   -145       C  
ATOM    367  C   GLN A  51      59.899  64.871  45.353  1.00 84.68           C  
ANISOU  367  C   GLN A  51     9707  10700  11769  -2442   1384      8       C  
ATOM    368  O   GLN A  51      59.969  65.375  44.233  1.00107.73           O  
ANISOU  368  O   GLN A  51    12958  13495  14482  -2780   1588     16       O  
ATOM    369  CB  GLN A  51      60.826  62.547  45.119  1.00 83.35           C  
ANISOU  369  CB  GLN A  51     8867  10718  12084  -2323   1817   -201       C  
ATOM    370  CG  GLN A  51      59.406  62.013  45.044  1.00105.02           C  
ANISOU  370  CG  GLN A  51    11889  13497  14517  -2083   1673    -45       C  
ATOM    371  CD  GLN A  51      59.314  60.720  44.251  1.00124.77           C  
ANISOU  371  CD  GLN A  51    14310  16045  17052  -2076   1969   -105       C  
ATOM    372  OE1 GLN A  51      60.228  60.374  43.500  1.00135.53           O  
ANISOU  372  OE1 GLN A  51    15505  17390  18599  -2314   2351   -280       O  
ATOM    373  NE2 GLN A  51      58.211  59.997  44.418  1.00112.86           N  
ANISOU  373  NE2 GLN A  51    12908  14589  15384  -1821   1821      6       N  
ATOM    374  N   PHE A  52      58.910  65.138  46.201  1.00 77.68           N  
ANISOU  374  N   PHE A  52     8938   9821  10756  -2148   1023    107       N  
ATOM    375  CA  PHE A  52      57.891  66.140  45.894  1.00 73.88           C  
ANISOU  375  CA  PHE A  52     8904   9179   9987  -2159    796    204       C  
ATOM    376  C   PHE A  52      58.232  67.500  46.497  1.00 85.11           C  
ANISOU  376  C   PHE A  52    10424  10486  11429  -2237    560    195       C  
ATOM    377  O   PHE A  52      57.491  68.466  46.311  1.00 92.29           O  
ANISOU  377  O   PHE A  52    11689  11211  12166  -2243    317    250       O  
ATOM    378  CB  PHE A  52      56.518  65.693  46.399  1.00 62.20           C  
ANISOU  378  CB  PHE A  52     7465   7750   8420  -1806    583    245       C  
ATOM    379  CG  PHE A  52      55.901  64.591  45.591  1.00 61.70           C  
ANISOU  379  CG  PHE A  52     7442   7731   8269  -1759    748    282       C  
ATOM    380  CD1 PHE A  52      55.267  64.868  44.392  1.00 61.14           C  
ANISOU  380  CD1 PHE A  52     7768   7485   7980  -1913    728    353       C  
ATOM    381  CD2 PHE A  52      55.944  63.280  46.036  1.00 73.17           C  
ANISOU  381  CD2 PHE A  52     8586   9369   9848  -1576    873    254       C  
ATOM    382  CE1 PHE A  52      54.695  63.856  43.644  1.00 79.65           C  
ANISOU  382  CE1 PHE A  52    10177   9856  10231  -1883    855    385       C  
ATOM    383  CE2 PHE A  52      55.372  62.262  45.293  1.00 84.07           C  
ANISOU  383  CE2 PHE A  52    10013  10781  11150  -1537   1019    283       C  
ATOM    384  CZ  PHE A  52      54.747  62.551  44.095  1.00 84.24           C  
ANISOU  384  CZ  PHE A  52    10410  10646  10952  -1690   1021    343       C  
ATOM    385  N   ASN A  53      59.352  67.563  47.215  1.00 81.86           N  
ANISOU  385  N   ASN A  53     9690  10150  11263  -2290    589    114       N  
ATOM    386  CA  ASN A  53      59.767  68.766  47.936  1.00 81.62           C  
ANISOU  386  CA  ASN A  53     9710  10023  11279  -2354    350     93       C  
ATOM    387  C   ASN A  53      58.682  69.251  48.900  1.00 74.11           C  
ANISOU  387  C   ASN A  53     8912   9042  10206  -2054      2    109       C  
ATOM    388  O   ASN A  53      58.257  70.404  48.848  1.00 77.20           O  
ANISOU  388  O   ASN A  53     9601   9248  10482  -2097   -205    120       O  
ATOM    389  CB  ASN A  53      60.145  69.881  46.955  1.00 95.24           C  
ANISOU  389  CB  ASN A  53    11774  11540  12872  -2748    426    121       C  
ATOM    390  CG  ASN A  53      60.841  71.045  47.636  1.00121.82           C  
ANISOU  390  CG  ASN A  53    15136  14809  16340  -2872    229     83       C  
ATOM    391  OD1 ASN A  53      61.264  70.940  48.788  1.00124.39           O  
ANISOU  391  OD1 ASN A  53    15157  15234  16872  -2701     73     20       O  
ATOM    392  ND2 ASN A  53      60.962  72.162  46.927  1.00130.65           N  
ANISOU  392  ND2 ASN A  53    16645  15704  17294  -3196    201    131       N  
HETATM  393  N   MSE A  54      58.232  68.357  49.775  1.00 66.14           N  
ANISOU  393  N   MSE A  54     7710   8191   9229  -1772    -49     86       N  
HETATM  394  CA  MSE A  54      57.168  68.683  50.718  1.00 58.02           C  
ANISOU  394  CA  MSE A  54     6802   7156   8086  -1527   -273     37       C  
HETATM  395  C   MSE A  54      57.563  68.458  52.169  1.00 66.72           C  
ANISOU  395  C   MSE A  54     7750   8362   9239  -1426   -412    -20       C  
HETATM  396  O   MSE A  54      58.336  67.553  52.488  1.00 70.89           O  
ANISOU  396  O   MSE A  54     8039   8997   9899  -1433   -374      6       O  
HETATM  397  CB  MSE A  54      55.924  67.859  50.421  1.00 69.24           C  
ANISOU  397  CB  MSE A  54     8259   8641   9409  -1328   -195     43       C  
HETATM  398  CG  MSE A  54      55.227  68.215  49.139  1.00 79.34           C  
ANISOU  398  CG  MSE A  54     9787   9754  10603  -1391   -195     94       C  
HETATM  399 SE   MSE A  54      53.608  67.161  48.962  1.00111.09          SE  
ANISOU  399 SE   MSE A  54    13782  13848  14579  -1114   -158     65      SE  
HETATM  400  CE  MSE A  54      52.860  68.033  47.385  1.00179.56           C  
ANISOU  400  CE  MSE A  54    22866  22181  23178  -1231   -365    136       C  
ATOM    401  N   SER A  55      57.014  69.292  53.043  1.00 62.71           N  
ANISOU  401  N   SER A  55     7408   7788   8631  -1341   -599   -112       N  
ATOM    402  CA  SER A  55      57.150  69.104  54.476  1.00 76.87           C  
ANISOU  402  CA  SER A  55     9187   9656  10365  -1276   -736   -177       C  
ATOM    403  C   SER A  55      56.277  67.938  54.928  1.00 84.29           C  
ANISOU  403  C   SER A  55    10110  10743  11175  -1119   -622   -194       C  
ATOM    404  O   SER A  55      55.366  67.519  54.206  1.00 62.99           O  
ANISOU  404  O   SER A  55     7406   8075   8453  -1021   -460   -195       O  
ATOM    405  CB  SER A  55      56.765  70.379  55.227  1.00 73.94           C  
ANISOU  405  CB  SER A  55     9035   9157   9903  -1266   -911   -318       C  
ATOM    406  OG  SER A  55      55.390  70.679  55.054  1.00 56.18           O  
ANISOU  406  OG  SER A  55     6903   6853   7587  -1111   -848   -447       O  
ATOM    407  N   ARG A  56      56.573  67.409  56.112  1.00 85.04           N  
ANISOU  407  N   ARG A  56    10233  10904  11174  -1126   -734   -201       N  
ATOM    408  CA  ARG A  56      55.745  66.373  56.720  1.00 74.57           C  
ANISOU  408  CA  ARG A  56     8979   9695   9658  -1045   -631   -224       C  
ATOM    409  C   ARG A  56      54.284  66.799  56.821  1.00 72.92           C  
ANISOU  409  C   ARG A  56     8899   9491   9317   -950   -459   -413       C  
ATOM    410  O   ARG A  56      53.393  66.007  56.546  1.00 94.35           O  
ANISOU  410  O   ARG A  56    11567  12291  11992   -867   -268   -435       O  
ATOM    411  CB  ARG A  56      56.272  66.004  58.108  1.00 74.14           C  
ANISOU  411  CB  ARG A  56     9087   9642   9443  -1139   -849   -208       C  
ATOM    412  CG  ARG A  56      57.428  65.027  58.089  1.00 72.83           C  
ANISOU  412  CG  ARG A  56     8744   9465   9465  -1171  -1044    -39       C  
ATOM    413  CD  ARG A  56      58.160  65.013  59.418  1.00 88.86           C  
ANISOU  413  CD  ARG A  56    10975  11399  11387  -1291  -1420    -11       C  
ATOM    414  NE  ARG A  56      59.211  64.002  59.435  1.00110.28           N  
ANISOU  414  NE  ARG A  56    13490  14047  14365  -1289  -1689    127       N  
ATOM    415  CZ  ARG A  56      60.103  63.867  60.410  1.00132.84           C  
ANISOU  415  CZ  ARG A  56    16455  16756  17261  -1381  -2142    184       C  
ATOM    416  NH1 ARG A  56      60.079  64.687  61.451  1.00139.06           N1+
ANISOU  416  NH1 ARG A  56    17597  17469  17770  -1515  -2343    128       N1+
ATOM    417  NH2 ARG A  56      61.023  62.913  60.339  1.00142.71           N  
ANISOU  417  NH2 ARG A  56    17463  17905  18857  -1341  -2427    280       N  
ATOM    418  N   GLY A  57      54.044  68.050  57.199  1.00 62.85           N  
ANISOU  418  N   GLY A  57     7751   8102   8027   -960   -534   -578       N  
ATOM    419  CA  GLY A  57      52.690  68.541  57.395  1.00 55.80           C  
ANISOU  419  CA  GLY A  57     6920   7172   7111   -856   -389   -837       C  
ATOM    420  C   GLY A  57      51.811  68.510  56.156  1.00 67.02           C  
ANISOU  420  C   GLY A  57     8194   8541   8731   -708   -303   -851       C  
ATOM    421  O   GLY A  57      50.702  67.962  56.178  1.00 76.94           O  
ANISOU  421  O   GLY A  57     9378   9859   9997   -614   -117   -989       O  
ATOM    422  N   VAL A  58      52.301  69.108  55.074  1.00 56.91           N  
ANISOU  422  N   VAL A  58     6898   7123   7600   -722   -452   -716       N  
ATOM    423  CA  VAL A  58      51.556  69.173  53.821  1.00 56.23           C  
ANISOU  423  CA  VAL A  58     6775   6922   7667   -626   -467   -695       C  
ATOM    424  C   VAL A  58      51.280  67.776  53.278  1.00 67.54           C  
ANISOU  424  C   VAL A  58     8082   8515   9065   -593   -280   -571       C  
ATOM    425  O   VAL A  58      50.131  67.411  52.999  1.00 51.24           O  
ANISOU  425  O   VAL A  58     5948   6445   7078   -464   -207   -679       O  
ATOM    426  CB  VAL A  58      52.317  69.986  52.758  1.00 66.18           C  
ANISOU  426  CB  VAL A  58     8156   7995   8993   -751   -650   -530       C  
ATOM    427  CG1 VAL A  58      51.531  70.029  51.459  1.00 71.63           C  
ANISOU  427  CG1 VAL A  58     8919   8518   9779   -696   -732   -483       C  
ATOM    428  CG2 VAL A  58      52.603  71.394  53.266  1.00 69.72           C  
ANISOU  428  CG2 VAL A  58     8749   8258   9483   -794   -864   -641       C  
ATOM    429  N   PHE A  59      52.349  66.998  53.150  1.00 71.00           N  
ANISOU  429  N   PHE A  59     8467   9077   9434   -706   -218   -371       N  
ATOM    430  CA  PHE A  59      52.266  65.634  52.656  1.00 63.85           C  
ANISOU  430  CA  PHE A  59     7446   8307   8506   -685    -52   -251       C  
ATOM    431  C   PHE A  59      51.295  64.795  53.486  1.00 61.19           C  
ANISOU  431  C   PHE A  59     7072   8104   8073   -592     89   -368       C  
ATOM    432  O   PHE A  59      50.512  64.018  52.938  1.00 49.38           O  
ANISOU  432  O   PHE A  59     5506   6653   6603   -519    209   -362       O  
ATOM    433  CB  PHE A  59      53.652  64.992  52.655  1.00 69.97           C  
ANISOU  433  CB  PHE A  59     8122   9163   9302   -805    -36    -90       C  
ATOM    434  CG  PHE A  59      53.695  63.657  51.985  1.00 68.17           C  
ANISOU  434  CG  PHE A  59     7769   9030   9101   -785    125     18       C  
ATOM    435  CD1 PHE A  59      53.454  63.548  50.628  1.00 63.75           C  
ANISOU  435  CD1 PHE A  59     7231   8411   8580   -812    226     75       C  
ATOM    436  CD2 PHE A  59      53.977  62.512  52.708  1.00 64.58           C  
ANISOU  436  CD2 PHE A  59     7228   8691   8618   -760    142     64       C  
ATOM    437  CE1 PHE A  59      53.492  62.326  50.002  1.00 60.76           C  
ANISOU  437  CE1 PHE A  59     6755   8110   8220   -803    388    151       C  
ATOM    438  CE2 PHE A  59      54.018  61.285  52.088  1.00 59.62           C  
ANISOU  438  CE2 PHE A  59     6485   8123   8043   -730    272    148       C  
ATOM    439  CZ  PHE A  59      53.774  61.191  50.732  1.00 71.16           C  
ANISOU  439  CZ  PHE A  59     7935   9548   9554   -746    419    179       C  
ATOM    440  N   ALA A  60      51.343  64.965  54.807  1.00 58.09           N  
ANISOU  440  N   ALA A  60     6763   7761   7547   -636     83   -482       N  
ATOM    441  CA  ALA A  60      50.457  64.232  55.708  1.00 62.84           C  
ANISOU  441  CA  ALA A  60     7404   8479   7992   -638    267   -619       C  
ATOM    442  C   ALA A  60      49.016  64.656  55.504  1.00 70.58           C  
ANISOU  442  C   ALA A  60     8300   9406   9110   -521    400   -885       C  
ATOM    443  O   ALA A  60      48.100  63.842  55.615  1.00 81.89           O  
ANISOU  443  O   ALA A  60     9661  10930  10524   -504    607   -982       O  
ATOM    444  CB  ALA A  60      50.862  64.436  57.153  1.00 52.39           C  
ANISOU  444  CB  ALA A  60     6289   7182   6435   -779    225   -695       C  
ATOM    445  N   ARG A  61      48.817  65.937  55.213  1.00 78.54           N  
ANISOU  445  N   ARG A  61     9301  10239  10301   -445    256  -1022       N  
ATOM    446  CA  ARG A  61      47.483  66.429  54.908  1.00 81.09           C  
ANISOU  446  CA  ARG A  61     9487  10438  10884   -294    286  -1302       C  
ATOM    447  C   ARG A  61      46.960  65.751  53.648  1.00 72.77           C  
ANISOU  447  C   ARG A  61     8311   9355   9984   -198    251  -1174       C  
ATOM    448  O   ARG A  61      45.803  65.341  53.591  1.00 64.17           O  
ANISOU  448  O   ARG A  61     7054   8274   9055   -110    377  -1369       O  
ATOM    449  CB  ARG A  61      47.483  67.947  54.738  1.00 85.76           C  
ANISOU  449  CB  ARG A  61    10126  10780  11679   -219     34  -1440       C  
ATOM    450  CG  ARG A  61      46.096  68.531  54.569  1.00 90.98           C  
ANISOU  450  CG  ARG A  61    10605  11254  12709    -34      0  -1797       C  
ATOM    451  CD  ARG A  61      45.247  68.232  55.792  1.00109.25           C  
ANISOU  451  CD  ARG A  61    12796  13703  15009    -62    370  -2179       C  
ATOM    452  NE  ARG A  61      45.599  69.087  56.920  1.00114.10           N  
ANISOU  452  NE  ARG A  61    13560  14295  15498   -154    426  -2385       N  
ATOM    453  CZ  ARG A  61      44.807  70.036  57.406  1.00115.36           C  
ANISOU  453  CZ  ARG A  61    13606  14288  15938    -61    474  -2832       C  
ATOM    454  NH1 ARG A  61      43.612  70.242  56.869  1.00120.73           N  
ANISOU  454  NH1 ARG A  61    13975  14796  17100    145    439  -3127       N  
ATOM    455  NH2 ARG A  61      45.204  70.772  58.434  1.00124.50           N  
ANISOU  455  NH2 ARG A  61    14947  15427  16929   -172    537  -3009       N  
ATOM    456  N   LEU A  62      47.826  65.623  52.646  1.00 71.99           N  
ANISOU  456  N   LEU A  62     8299   9217   9837   -246    101   -870       N  
ATOM    457  CA  LEU A  62      47.452  64.965  51.398  1.00 75.36           C  
ANISOU  457  CA  LEU A  62     8692   9602  10340   -204     65   -728       C  
ATOM    458  C   LEU A  62      47.053  63.508  51.605  1.00 73.35           C  
ANISOU  458  C   LEU A  62     8320   9557   9994   -207    317   -700       C  
ATOM    459  O   LEU A  62      46.177  62.995  50.917  1.00 80.41           O  
ANISOU  459  O   LEU A  62     9126  10413  11013   -130    322   -727       O  
ATOM    460  CB  LEU A  62      48.594  65.045  50.385  1.00 76.44           C  
ANISOU  460  CB  LEU A  62     8987   9677  10380   -334    -43   -443       C  
ATOM    461  CG  LEU A  62      48.538  66.225  49.417  1.00 61.32           C  
ANISOU  461  CG  LEU A  62     7265   7465   8569   -357   -342   -413       C  
ATOM    462  CD1 LEU A  62      47.165  66.295  48.792  1.00 67.29           C  
ANISOU  462  CD1 LEU A  62     7994   8032   9542   -202   -526   -537       C  
ATOM    463  CD2 LEU A  62      48.872  67.532  50.114  1.00 66.53           C  
ANISOU  463  CD2 LEU A  62     7997   8005   9278   -366   -495   -531       C  
ATOM    464  N   LEU A  63      47.684  62.847  52.566  1.00 78.51           N  
ANISOU  464  N   LEU A  63     9000  10398  10433   -307    481   -642       N  
ATOM    465  CA  LEU A  63      47.380  61.449  52.844  1.00 73.50           C  
ANISOU  465  CA  LEU A  63     8317   9932   9679   -342    686   -594       C  
ATOM    466  C   LEU A  63      46.255  61.328  53.865  1.00 77.67           C  
ANISOU  466  C   LEU A  63     8794  10530  10188   -360    902   -884       C  
ATOM    467  O   LEU A  63      45.938  60.232  54.326  1.00 71.93           O  
ANISOU  467  O   LEU A  63     8083   9936   9311   -448   1099   -873       O  
ATOM    468  CB  LEU A  63      48.624  60.717  53.338  1.00 72.65           C  
ANISOU  468  CB  LEU A  63     8301   9930   9371   -457    682   -379       C  
ATOM    469  CG  LEU A  63      49.786  60.691  52.346  1.00 81.68           C  
ANISOU  469  CG  LEU A  63     9424  11019  10590   -472    562   -158       C  
ATOM    470  CD1 LEU A  63      50.924  59.864  52.885  1.00 85.79           C  
ANISOU  470  CD1 LEU A  63     9946  11611  11039   -550    527     -8       C  
ATOM    471  CD2 LEU A  63      49.331  60.198  50.985  1.00 77.33           C  
ANISOU  471  CD2 LEU A  63     8821  10426  10134   -421    609    -85       C  
ATOM    472  N   HIS A  64      45.676  62.473  54.223  1.00 94.20           N  
ANISOU  472  N   HIS A  64    10836  12515  12441   -303    881  -1165       N  
ATOM    473  CA  HIS A  64      44.573  62.553  55.179  1.00100.40           C  
ANISOU  473  CA  HIS A  64    11530  13343  13273   -343   1154  -1545       C  
ATOM    474  C   HIS A  64      44.908  61.843  56.486  1.00 86.20           C  
ANISOU  474  C   HIS A  64     9959  11721  11071   -585   1397  -1536       C  
ATOM    475  O   HIS A  64      44.148  61.001  56.967  1.00 67.61           O  
ANISOU  475  O   HIS A  64     7595   9477   8617   -710   1693  -1671       O  
ATOM    476  CB  HIS A  64      43.286  61.990  54.569  1.00115.46           C  
ANISOU  476  CB  HIS A  64    13175  15234  15462   -247   1268  -1709       C  
ATOM    477  CG  HIS A  64      42.695  62.862  53.501  1.00140.09           C  
ANISOU  477  CG  HIS A  64    16107  18105  19018    -24    970  -1814       C  
ATOM    478  ND1 HIS A  64      43.076  62.783  52.178  1.00141.37           N  
ANISOU  478  ND1 HIS A  64    16335  18148  19231     58    662  -1512       N  
ATOM    479  CD2 HIS A  64      41.758  63.838  53.563  1.00145.15           C  
ANISOU  479  CD2 HIS A  64    16527  18551  20071    117    897  -2198       C  
ATOM    480  CE1 HIS A  64      42.396  63.668  51.471  1.00135.29           C  
ANISOU  480  CE1 HIS A  64    15458  17107  18840    223    362  -1664       C  
ATOM    481  NE2 HIS A  64      41.590  64.322  52.288  1.00136.80           N  
ANISOU  481  NE2 HIS A  64    15439  17237  19301    290    472  -2085       N  
ATOM    482  N   THR A  65      46.066  62.197  57.039  1.00 96.88           N  
ANISOU  482  N   THR A  65    11549  13072  12190   -677   1238  -1372       N  
ATOM    483  CA  THR A  65      46.512  61.725  58.346  1.00 91.13           C  
ANISOU  483  CA  THR A  65    11138  12436  11052   -930   1339  -1346       C  
ATOM    484  C   THR A  65      47.280  62.847  59.049  1.00 83.06           C  
ANISOU  484  C   THR A  65    10303  11330   9927   -988   1168  -1396       C  
ATOM    485  O   THR A  65      47.655  63.835  58.419  1.00 87.91           O  
ANISOU  485  O   THR A  65    10793  11828  10782   -830    953  -1376       O  
ATOM    486  CB  THR A  65      47.404  60.476  58.235  1.00 86.04           C  
ANISOU  486  CB  THR A  65    10629  11852  10210  -1002   1188   -966       C  
ATOM    487  OG1 THR A  65      47.685  59.966  59.546  1.00 97.27           O  
ANISOU  487  OG1 THR A  65    12430  13308  11219  -1275   1223   -944       O  
ATOM    488  CG2 THR A  65      48.711  60.816  57.532  1.00 62.47           C  
ANISOU  488  CG2 THR A  65     7579   8789   7368   -884    843   -692       C  
ATOM    489  N   SER A  66      47.508  62.697  60.350  1.00 67.61           N  
ANISOU  489  N   SER A  66     8695   9408   7584  -1245   1247  -1455       N  
ATOM    490  CA  SER A  66      48.225  63.706  61.125  1.00 69.32           C  
ANISOU  490  CA  SER A  66     9142   9536   7661  -1335   1073  -1510       C  
ATOM    491  C   SER A  66      49.731  63.683  60.865  1.00 71.18           C  
ANISOU  491  C   SER A  66     9433   9709   7902  -1301    631  -1134       C  
ATOM    492  O   SER A  66      50.296  62.647  60.520  1.00 84.74           O  
ANISOU  492  O   SER A  66    11130  11461   9606  -1295    489   -846       O  
ATOM    493  CB  SER A  66      47.964  63.516  62.622  1.00 89.04           C  
ANISOU  493  CB  SER A  66    12082  12065   9686  -1680   1291  -1702       C  
ATOM    494  OG  SER A  66      48.659  62.389  63.124  1.00 94.44           O  
ANISOU  494  OG  SER A  66    13101  12768  10013  -1882   1108  -1386       O  
ATOM    495  N   SER A  67      50.373  64.835  61.037  1.00 73.86           N  
ANISOU  495  N   SER A  67     9816   9941   8307  -1282    421  -1171       N  
ATOM    496  CA  SER A  67      51.820  64.950  60.888  1.00 61.87           C  
ANISOU  496  CA  SER A  67     8312   8349   6848  -1283     22   -882       C  
ATOM    497  C   SER A  67      52.536  64.037  61.867  1.00 74.71           C  
ANISOU  497  C   SER A  67    10260   9968   8159  -1493   -187   -697       C  
ATOM    498  O   SER A  67      53.564  63.442  61.543  1.00 75.43           O  
ANISOU  498  O   SER A  67    10253  10019   8389  -1458   -484   -429       O  
ATOM    499  CB  SER A  67      52.270  66.392  61.107  1.00 65.53           C  
ANISOU  499  CB  SER A  67     8822   8686   7391  -1281   -144   -999       C  
ATOM    500  OG  SER A  67      51.492  67.284  60.332  1.00 90.28           O  
ANISOU  500  OG  SER A  67    11736  11767  10800  -1103     -7  -1196       O  
ATOM    501  N   ARG A  68      51.982  63.947  63.072  1.00 87.40           N  
ANISOU  501  N   ARG A  68    12269  11583   9357  -1732    -38   -869       N  
ATOM    502  CA  ARG A  68      52.518  63.091  64.118  1.00 71.44           C  
ANISOU  502  CA  ARG A  68    10698   9502   6943  -1996   -276   -699       C  
ATOM    503  C   ARG A  68      52.573  61.644  63.642  1.00 70.48           C  
ANISOU  503  C   ARG A  68    10486   9422   6873  -1951   -329   -450       C  
ATOM    504  O   ARG A  68      53.582  60.957  63.821  1.00 68.30           O  
ANISOU  504  O   ARG A  68    10308   9031   6613  -1983   -761   -180       O  
ATOM    505  CB  ARG A  68      51.667  63.208  65.385  1.00 75.72           C  
ANISOU  505  CB  ARG A  68    11745  10055   6970  -2326     25   -974       C  
ATOM    506  CG  ARG A  68      52.241  62.487  66.593  1.00109.12           C  
ANISOU  506  CG  ARG A  68    16611  14160  10689  -2681   -289   -794       C  
ATOM    507  CD  ARG A  68      53.562  63.105  67.012  1.00133.15           C  
ANISOU  507  CD  ARG A  68    19804  17020  13766  -2701   -868   -630       C  
ATOM    508  NE  ARG A  68      54.143  62.438  68.172  1.00145.58           N  
ANISOU  508  NE  ARG A  68    22036  18410  14868  -3044  -1291   -440       N  
ATOM    509  CZ  ARG A  68      55.301  62.783  68.725  1.00163.26           C  
ANISOU  509  CZ  ARG A  68    24501  20438  17092  -3121  -1894   -280       C  
ATOM    510  NH1 ARG A  68      55.760  62.123  69.780  1.00169.66           N  
ANISOU  510  NH1 ARG A  68    25971  21032  17458  -3450  -2348    -96       N  
ATOM    511  NH2 ARG A  68      56.003  63.789  68.220  1.00163.87           N  
ANISOU  511  NH2 ARG A  68    24169  20493  17600  -2891  -2076   -301       N  
ATOM    512  N   THR A  69      51.484  61.195  63.023  1.00 63.09           N  
ANISOU  512  N   THR A  69     9337   8621   6013  -1864     81   -563       N  
ATOM    513  CA  THR A  69      51.385  59.831  62.520  1.00 61.67           C  
ANISOU  513  CA  THR A  69     9069   8484   5880  -1820     83   -360       C  
ATOM    514  C   THR A  69      52.426  59.565  61.436  1.00 69.69           C  
ANISOU  514  C   THR A  69     9693   9452   7332  -1564   -224   -109       C  
ATOM    515  O   THR A  69      53.162  58.575  61.500  1.00 66.92           O  
ANISOU  515  O   THR A  69     9399   9015   7012  -1579   -528    124       O  
ATOM    516  CB  THR A  69      49.978  59.534  61.957  1.00 61.21           C  
ANISOU  516  CB  THR A  69     8797   8572   5886  -1761    580   -561       C  
ATOM    517  OG1 THR A  69      48.997  59.714  62.985  1.00 63.59           O  
ANISOU  517  OG1 THR A  69     9418   8918   5823  -2039    945   -860       O  
ATOM    518  CG2 THR A  69      49.902  58.108  61.459  1.00 83.45           C  
ANISOU  518  CG2 THR A  69    11556  11419   8731  -1733    564   -344       C  
ATOM    519  N   LEU A  70      52.486  60.453  60.447  1.00 73.79           N  
ANISOU  519  N   LEU A  70     9836  10002   8200  -1353   -143   -180       N  
ATOM    520  CA  LEU A  70      53.452  60.327  59.361  1.00 69.07           C  
ANISOU  520  CA  LEU A  70     8881   9365   7999  -1173   -330     -4       C  
ATOM    521  C   LEU A  70      54.872  60.267  59.904  1.00 74.82           C  
ANISOU  521  C   LEU A  70     9668   9950   8811  -1237   -783    150       C  
ATOM    522  O   LEU A  70      55.666  59.432  59.480  1.00 81.55           O  
ANISOU  522  O   LEU A  70    10328  10741   9917  -1165   -980    307       O  
ATOM    523  CB  LEU A  70      53.317  61.489  58.374  1.00 66.91           C  
ANISOU  523  CB  LEU A  70     8338   9101   7983  -1033   -199   -113       C  
ATOM    524  CG  LEU A  70      54.357  61.538  57.250  1.00 62.25           C  
ANISOU  524  CG  LEU A  70     7435   8463   7753   -936   -315     24       C  
ATOM    525  CD1 LEU A  70      54.263  60.306  56.360  1.00 61.20           C  
ANISOU  525  CD1 LEU A  70     7118   8382   7753   -849   -195    137       C  
ATOM    526  CD2 LEU A  70      54.202  62.802  56.425  1.00 51.15           C  
ANISOU  526  CD2 LEU A  70     5916   7020   6497   -881   -226    -72       C  
ATOM    527  N   GLU A  71      55.179  61.150  60.849  1.00 79.01           N  
ANISOU  527  N   GLU A  71    10449  10404   9166  -1370   -962     77       N  
ATOM    528  CA  GLU A  71      56.486  61.169  61.497  1.00 79.95           C  
ANISOU  528  CA  GLU A  71    10655  10351   9370  -1451  -1463    205       C  
ATOM    529  C   GLU A  71      56.758  59.844  62.208  1.00 63.53           C  
ANISOU  529  C   GLU A  71     8848   8156   7133  -1557  -1779    381       C  
ATOM    530  O   GLU A  71      57.890  59.361  62.221  1.00 65.00           O  
ANISOU  530  O   GLU A  71     8894   8176   7627  -1512  -2224    523       O  
ATOM    531  CB  GLU A  71      56.578  62.335  62.487  1.00 94.47           C  
ANISOU  531  CB  GLU A  71    12813  12121  10959  -1612  -1587     81       C  
ATOM    532  CG  GLU A  71      57.918  62.446  63.210  1.00113.28           C  
ANISOU  532  CG  GLU A  71    15308  14294  13439  -1711  -2172    205       C  
ATOM    533  CD  GLU A  71      57.914  63.496  64.312  1.00120.16           C  
ANISOU  533  CD  GLU A  71    16603  15084  13967  -1914  -2303     81       C  
ATOM    534  OE1 GLU A  71      57.053  64.401  64.274  1.00125.66           O  
ANISOU  534  OE1 GLU A  71    17354  15886  14503  -1918  -1916   -135       O  
ATOM    535  OE2 GLU A  71      58.771  63.413  65.220  1.00113.11           O  
ANISOU  535  OE2 GLU A  71    15994  13993  12989  -2068  -2824    186       O  
ATOM    536  N   ASN A  72      55.714  59.256  62.789  1.00 73.89           N  
ANISOU  536  N   ASN A  72    10544   9530   8000  -1711  -1559    351       N  
ATOM    537  CA  ASN A  72      55.838  57.960  63.451  1.00 76.27           C  
ANISOU  537  CA  ASN A  72    11201   9696   8081  -1857  -1852    534       C  
ATOM    538  C   ASN A  72      56.147  56.844  62.463  1.00 64.68           C  
ANISOU  538  C   ASN A  72     9340   8215   7021  -1639  -1908    676       C  
ATOM    539  O   ASN A  72      56.902  55.927  62.778  1.00 66.91           O  
ANISOU  539  O   ASN A  72     9716   8286   7421  -1651  -2386    854       O  
ATOM    540  CB  ASN A  72      54.566  57.625  64.233  1.00 76.50           C  
ANISOU  540  CB  ASN A  72    11743   9809   7513  -2133  -1498    434       C  
ATOM    541  CG  ASN A  72      54.544  58.262  65.610  1.00 85.29           C  
ANISOU  541  CG  ASN A  72    13472  10823   8112  -2471  -1620    346       C  
ATOM    542  OD1 ASN A  72      55.010  57.673  66.587  1.00 89.32           O  
ANISOU  542  OD1 ASN A  72    14527  11115   8294  -2727  -2068    514       O  
ATOM    543  ND2 ASN A  72      54.008  59.473  65.692  1.00 98.70           N  
ANISOU  543  ND2 ASN A  72    15122  12645   9736  -2485  -1255     74       N  
ATOM    544  N   TRP A  73      55.561  56.923  61.272  1.00 62.94           N  
ANISOU  544  N   TRP A  73     8701   8187   7027  -1445  -1452    585       N  
ATOM    545  CA  TRP A  73      55.905  55.997  60.195  1.00 59.31           C  
ANISOU  545  CA  TRP A  73     7838   7720   6976  -1238  -1448    677       C  
ATOM    546  C   TRP A  73      57.354  56.186  59.767  1.00 61.90           C  
ANISOU  546  C   TRP A  73     7772   7906   7841  -1100  -1794    713       C  
ATOM    547  O   TRP A  73      58.084  55.219  59.543  1.00 65.65           O  
ANISOU  547  O   TRP A  73     8061   8232   8653  -1006  -2074    802       O  
ATOM    548  CB  TRP A  73      55.004  56.197  58.979  1.00 71.09           C  
ANISOU  548  CB  TRP A  73     9021   9422   8568  -1095   -918    564       C  
ATOM    549  CG  TRP A  73      53.549  55.998  59.224  1.00 55.05           C  
ANISOU  549  CG  TRP A  73     7231   7529   6158  -1198   -543    472       C  
ATOM    550  CD1 TRP A  73      52.971  55.339  60.265  1.00 57.26           C  
ANISOU  550  CD1 TRP A  73     7960   7781   6014  -1426   -553    498       C  
ATOM    551  CD2 TRP A  73      52.479  56.471  58.403  1.00 52.63           C  
ANISOU  551  CD2 TRP A  73     6724   7382   5890  -1105   -108    313       C  
ATOM    552  NE1 TRP A  73      51.603  55.370  60.144  1.00 56.35           N  
ANISOU  552  NE1 TRP A  73     7876   7827   5707  -1484    -84    328       N  
ATOM    553  CE2 TRP A  73      51.276  56.062  59.009  1.00 53.52           C  
ANISOU  553  CE2 TRP A  73     7098   7574   5663  -1263    156    212       C  
ATOM    554  CE3 TRP A  73      52.422  57.202  57.211  1.00 50.31           C  
ANISOU  554  CE3 TRP A  73     6084   7141   5890   -931     54    241       C  
ATOM    555  CZ2 TRP A  73      50.030  56.356  58.464  1.00 52.18           C  
ANISOU  555  CZ2 TRP A  73     6765   7530   5530  -1206    552     15       C  
ATOM    556  CZ3 TRP A  73      51.187  57.495  56.672  1.00 48.98           C  
ANISOU  556  CZ3 TRP A  73     5834   7069   5705   -878    379     89       C  
ATOM    557  CH2 TRP A  73      50.005  57.074  57.298  1.00 49.91           C  
ANISOU  557  CH2 TRP A  73     6130   7262   5573   -992    613    -36       C  
ATOM    558  N   GLU A  74      57.753  57.447  59.643  1.00 59.83           N  
ANISOU  558  N   GLU A  74     7361   7676   7696  -1097  -1759    610       N  
ATOM    559  CA  GLU A  74      59.066  57.805  59.130  1.00 60.71           C  
ANISOU  559  CA  GLU A  74     7041   7682   8344  -1007  -1972    585       C  
ATOM    560  C   GLU A  74      60.190  57.429  60.088  1.00 64.76           C  
ANISOU  560  C   GLU A  74     7634   7926   9048  -1057  -2626    673       C  
ATOM    561  O   GLU A  74      61.313  57.175  59.657  1.00 92.33           O  
ANISOU  561  O   GLU A  74    10686  11279  13118   -953  -2859    642       O  
ATOM    562  CB  GLU A  74      59.128  59.303  58.826  1.00 68.26           C  
ANISOU  562  CB  GLU A  74     7895   8722   9318  -1039  -1777    461       C  
ATOM    563  CG  GLU A  74      58.248  59.755  57.673  1.00 70.95           C  
ANISOU  563  CG  GLU A  74     8097   9249   9613   -970  -1249    375       C  
ATOM    564  CD  GLU A  74      58.632  61.132  57.154  1.00 89.22           C  
ANISOU  564  CD  GLU A  74    10259  11568  12074  -1005  -1148    278       C  
ATOM    565  OE1 GLU A  74      59.646  61.688  57.631  1.00 93.69           O  
ANISOU  565  OE1 GLU A  74    10759  12016  12821  -1077  -1447    266       O  
ATOM    566  OE2 GLU A  74      57.925  61.655  56.265  1.00 92.73           O1+
ANISOU  566  OE2 GLU A  74    10671  12104  12459   -974   -812    220       O1+
ATOM    567  N   GLN A  75      59.906  57.435  61.388  1.00 71.09           N  
ANISOU  567  N   GLN A  75     8999   8627   9385  -1241  -2931    755       N  
ATOM    568  CA  GLN A  75      60.905  57.020  62.373  1.00 79.31           C  
ANISOU  568  CA  GLN A  75    10232   9350  10552  -1317  -3665    871       C  
ATOM    569  C   GLN A  75      60.771  55.546  62.759  1.00 73.45           C  
ANISOU  569  C   GLN A  75     9761   8428   9719  -1335  -3985   1038       C  
ATOM    570  O   GLN A  75      61.628  54.999  63.450  1.00 77.61           O  
ANISOU  570  O   GLN A  75    10426   8624  10439  -1365  -4688   1152       O  
ATOM    571  CB  GLN A  75      60.825  57.898  63.622  1.00 80.26           C  
ANISOU  571  CB  GLN A  75    10911   9397  10187  -1566  -3910    878       C  
ATOM    572  CG  GLN A  75      61.314  59.324  63.404  1.00 93.56           C  
ANISOU  572  CG  GLN A  75    12330  11147  12072  -1551  -3821    735       C  
ATOM    573  CD  GLN A  75      61.716  60.005  64.700  1.00130.94           C  
ANISOU  573  CD  GLN A  75    17555  15691  16506  -1778  -4305    759       C  
ATOM    574  OE1 GLN A  75      62.355  59.399  65.562  1.00139.64           O  
ANISOU  574  OE1 GLN A  75    18955  16498  17602  -1881  -4970    900       O  
ATOM    575  NE2 GLN A  75      61.342  61.271  64.844  1.00134.55           N  
ANISOU  575  NE2 GLN A  75    18129  16279  16713  -1865  -4015    620       N  
ATOM    576  N   GLY A  76      59.695  54.909  62.311  1.00 76.18           N  
ANISOU  576  N   GLY A  76    10195   8957   9792  -1322  -3516   1051       N  
ATOM    577  CA  GLY A  76      59.493  53.495  62.565  1.00 72.36           C  
ANISOU  577  CA  GLY A  76     9969   8310   9215  -1348  -3764   1208       C  
ATOM    578  C   GLY A  76      58.794  53.171  63.873  1.00 81.41           C  
ANISOU  578  C   GLY A  76    11963   9355   9614  -1692  -3945   1341       C  
ATOM    579  O   GLY A  76      58.722  52.007  64.266  1.00 99.49           O  
ANISOU  579  O   GLY A  76    14596  11437  11769  -1781  -4272   1507       O  
ATOM    580  N   ARG A  77      58.274  54.191  64.549  1.00 87.94           N  
ANISOU  580  N   ARG A  77    13161  10310   9943  -1917  -3719   1251       N  
ATOM    581  CA  ARG A  77      57.552  53.978  65.804  1.00 97.57           C  
ANISOU  581  CA  ARG A  77    15232  11454  10384  -2323  -3766   1315       C  
ATOM    582  C   ARG A  77      56.158  53.415  65.545  1.00100.04           C  
ANISOU  582  C   ARG A  77    15690  12003  10316  -2430  -3113   1253       C  
ATOM    583  O   ARG A  77      55.448  53.026  66.472  1.00112.72           O  
ANISOU  583  O   ARG A  77    17986  13562  11279  -2808  -3038   1284       O  
ATOM    584  CB  ARG A  77      57.450  55.280  66.604  1.00 91.30           C  
ANISOU  584  CB  ARG A  77    14768  10715   9208  -2541  -3679   1175       C  
ATOM    585  CG  ARG A  77      58.773  55.773  67.165  1.00 94.33           C  
ANISOU  585  CG  ARG A  77    15198  10808   9834  -2541  -4420   1259       C  
ATOM    586  CD  ARG A  77      58.561  56.894  68.170  1.00109.46           C  
ANISOU  586  CD  ARG A  77    17640  12734  11216  -2844  -4369   1138       C  
ATOM    587  NE  ARG A  77      57.922  58.061  67.568  1.00115.30           N  
ANISOU  587  NE  ARG A  77    17990  13807  12011  -2720  -3667    869       N  
ATOM    588  CZ  ARG A  77      58.572  59.157  67.186  1.00123.33           C  
ANISOU  588  CZ  ARG A  77    18580  14857  13422  -2542  -3721    769       C  
ATOM    589  NH1 ARG A  77      59.887  59.242  67.346  1.00124.37           N1+
ANISOU  589  NH1 ARG A  77    18564  14734  13955  -2472  -4401    890       N1+
ATOM    590  NH2 ARG A  77      57.907  60.171  66.647  1.00120.27           N  
ANISOU  590  NH2 ARG A  77    17912  14727  13059  -2445  -3126    537       N  
ATOM    591  N   SER A  78      55.772  53.384  64.277  1.00 88.92           N  
ANISOU  591  N   SER A  78    13647  10835   9303  -2131  -2636   1151       N  
ATOM    592  CA  SER A  78      54.477  52.861  63.877  1.00 81.69           C  
ANISOU  592  CA  SER A  78    12750  10137   8151  -2186  -2044   1074       C  
ATOM    593  C   SER A  78      54.543  52.341  62.445  1.00 85.53           C  
ANISOU  593  C   SER A  78    12581  10723   9193  -1827  -1865   1082       C  
ATOM    594  O   SER A  78      55.377  52.782  61.653  1.00 77.95           O  
ANISOU  594  O   SER A  78    11098   9761   8757  -1555  -1968   1054       O  
ATOM    595  CB  SER A  78      53.401  53.943  64.013  1.00 74.89           C  
ANISOU  595  CB  SER A  78    11927   9539   6987  -2305  -1419    797       C  
ATOM    596  OG  SER A  78      52.202  53.563  63.361  1.00 85.39           O  
ANISOU  596  OG  SER A  78    13065  11086   8294  -2269   -847    673       O  
ATOM    597  N   VAL A  79      53.681  51.385  62.121  1.00 85.27           N  
ANISOU  597  N   VAL A  79    12606  10764   9028  -1864  -1585   1109       N  
ATOM    598  CA  VAL A  79      53.588  50.896  60.751  1.00 78.23           C  
ANISOU  598  CA  VAL A  79    11160   9977   8586  -1564  -1357   1095       C  
ATOM    599  C   VAL A  79      52.267  51.322  60.123  1.00 67.98           C  
ANISOU  599  C   VAL A  79     9685   8969   7175  -1551   -698    900       C  
ATOM    600  O   VAL A  79      51.198  51.033  60.662  1.00 74.97           O  
ANISOU  600  O   VAL A  79    10901   9934   7652  -1792   -410    836       O  
ATOM    601  CB  VAL A  79      53.721  49.367  60.677  1.00 76.93           C  
ANISOU  601  CB  VAL A  79    11120   9625   8485  -1560  -1626   1280       C  
ATOM    602  CG1 VAL A  79      53.790  48.915  59.223  1.00 59.67           C  
ANISOU  602  CG1 VAL A  79     8351   7524   6797  -1245  -1409   1239       C  
ATOM    603  CG2 VAL A  79      54.956  48.905  61.440  1.00 75.89           C  
ANISOU  603  CG2 VAL A  79    11219   9131   8485  -1588  -2386   1462       C  
ATOM    604  N   PRO A  80      52.338  52.028  58.987  1.00 55.45           N  
ANISOU  604  N   PRO A  80     7589   7515   5965  -1295   -474    790       N  
ATOM    605  CA  PRO A  80      51.130  52.454  58.276  1.00 67.48           C  
ANISOU  605  CA  PRO A  80     8915   9251   7475  -1243     36    610       C  
ATOM    606  C   PRO A  80      50.275  51.262  57.853  1.00 62.93           C  
ANISOU  606  C   PRO A  80     8350   8719   6843  -1264    241    648       C  
ATOM    607  O   PRO A  80      50.805  50.181  57.596  1.00 55.87           O  
ANISOU  607  O   PRO A  80     7447   7703   6078  -1204     14    816       O  
ATOM    608  CB  PRO A  80      51.681  53.201  57.054  1.00 56.15           C  
ANISOU  608  CB  PRO A  80     7016   7852   6465   -987     72    567       C  
ATOM    609  CG  PRO A  80      53.073  52.684  56.886  1.00 57.52           C  
ANISOU  609  CG  PRO A  80     7053   7862   6941   -890   -306    714       C  
ATOM    610  CD  PRO A  80      53.566  52.411  58.272  1.00 54.62           C  
ANISOU  610  CD  PRO A  80     7081   7333   6338  -1069   -705    819       C  
ATOM    611  N   ASN A  81      48.965  51.464  57.782  1.00 59.61           N  
ANISOU  611  N   ASN A  81     7921   8449   6279  -1343    653    467       N  
ATOM    612  CA  ASN A  81      48.052  50.401  57.407  1.00 51.35           C  
ANISOU  612  CA  ASN A  81     6873   7451   5188  -1391    871    475       C  
ATOM    613  C   ASN A  81      48.129  50.074  55.918  1.00 60.19           C  
ANISOU  613  C   ASN A  81     7594   8588   6688  -1117    900    523       C  
ATOM    614  O   ASN A  81      48.904  50.676  55.176  1.00 53.68           O  
ANISOU  614  O   ASN A  81     6517   7740   6140   -922    786    542       O  
ATOM    615  CB  ASN A  81      46.622  50.778  57.788  1.00 52.34           C  
ANISOU  615  CB  ASN A  81     7040   7718   5131  -1569   1314    205       C  
ATOM    616  CG  ASN A  81      46.158  52.042  57.109  1.00 59.00           C  
ANISOU  616  CG  ASN A  81     7511   8649   6258  -1373   1494    -24       C  
ATOM    617  OD1 ASN A  81      45.715  52.018  55.959  1.00 51.89           O  
ANISOU  617  OD1 ASN A  81     6287   7779   5649  -1176   1572    -56       O  
ATOM    618  ND2 ASN A  81      46.265  53.163  57.813  1.00 77.49           N  
ANISOU  618  ND2 ASN A  81     9935  10997   8509  -1436   1517   -181       N  
ATOM    619  N   GLY A  82      47.312  49.117  55.492  1.00 65.07           N  
ANISOU  619  N   GLY A  82     8194   9238   7291  -1147   1072    531       N  
ATOM    620  CA  GLY A  82      47.361  48.600  54.136  1.00 52.99           C  
ANISOU  620  CA  GLY A  82     6384   7697   6052   -939   1088    588       C  
ATOM    621  C   GLY A  82      47.037  49.607  53.056  1.00 45.35           C  
ANISOU  621  C   GLY A  82     5113   6798   5320   -767   1226    455       C  
ATOM    622  O   GLY A  82      47.761  49.712  52.059  1.00 47.09           O  
ANISOU  622  O   GLY A  82     5162   6969   5762   -613   1142    517       O  
ATOM    623  N   GLN A  83      45.951  50.348  53.251  1.00 45.12           N  
ANISOU  623  N   GLN A  83     5035   6854   5255   -817   1434    251       N  
ATOM    624  CA  GLN A  83      45.559  51.383  52.303  1.00 60.07           C  
ANISOU  624  CA  GLN A  83     6693   8750   7382   -663   1472    123       C  
ATOM    625  C   GLN A  83      46.591  52.510  52.273  1.00 67.06           C  
ANISOU  625  C   GLN A  83     7558   9589   8334   -587   1306    149       C  
ATOM    626  O   GLN A  83      46.886  53.071  51.213  1.00 41.33           O  
ANISOU  626  O   GLN A  83     4182   6274   5249   -472   1239    170       O  
ATOM    627  CB  GLN A  83      44.179  51.935  52.647  1.00 44.13           C  
ANISOU  627  CB  GLN A  83     4580   6785   5404   -716   1683   -153       C  
ATOM    628  CG  GLN A  83      43.063  50.921  52.523  1.00 64.38           C  
ANISOU  628  CG  GLN A  83     7093   9389   7978   -802   1873   -223       C  
ATOM    629  CD  GLN A  83      43.038  49.934  53.671  1.00 67.40           C  
ANISOU  629  CD  GLN A  83     7747   9823   8038  -1059   2004   -171       C  
ATOM    630  OE1 GLN A  83      43.186  50.312  54.832  1.00 48.42           O  
ANISOU  630  OE1 GLN A  83     5546   7448   5404  -1235   2077   -249       O  
ATOM    631  NE2 GLN A  83      42.858  48.658  53.350  1.00 71.13           N  
ANISOU  631  NE2 GLN A  83     8282  10281   8464  -1112   2015    -34       N  
ATOM    632  N   ALA A  84      47.141  52.831  53.441  1.00 43.86           N  
ANISOU  632  N   ALA A  84     4781   6657   5229   -691   1233    150       N  
ATOM    633  CA  ALA A  84      48.205  53.822  53.534  1.00 43.86           C  
ANISOU  633  CA  ALA A  84     4767   6604   5294   -645   1053    181       C  
ATOM    634  C   ALA A  84      49.386  53.430  52.654  1.00 57.66           C  
ANISOU  634  C   ALA A  84     6395   8282   7232   -552    908    348       C  
ATOM    635  O   ALA A  84      49.818  54.204  51.791  1.00 64.02           O  
ANISOU  635  O   ALA A  84     7075   9050   8201   -484    894    335       O  
ATOM    636  CB  ALA A  84      48.649  53.990  54.978  1.00 45.93           C  
ANISOU  636  CB  ALA A  84     5274   6857   5320   -801    945    181       C  
ATOM    637  N   VAL A  85      49.898  52.222  52.870  1.00 44.73           N  
ANISOU  637  N   VAL A  85     4807   6604   5586   -572    811    481       N  
ATOM    638  CA  VAL A  85      51.023  51.728  52.088  1.00 56.15           C  
ANISOU  638  CA  VAL A  85     6083   7965   7288   -484    711    570       C  
ATOM    639  C   VAL A  85      50.671  51.722  50.606  1.00 51.05           C  
ANISOU  639  C   VAL A  85     5295   7335   6767   -415    913    534       C  
ATOM    640  O   VAL A  85      51.498  52.059  49.764  1.00 41.45           O  
ANISOU  640  O   VAL A  85     3943   6071   5736   -393    942    519       O  
ATOM    641  CB  VAL A  85      51.451  50.312  52.527  1.00 52.51           C  
ANISOU  641  CB  VAL A  85     5691   7411   6851   -491    540    689       C  
ATOM    642  CG1 VAL A  85      52.627  49.829  51.687  1.00 44.70           C  
ANISOU  642  CG1 VAL A  85     4442   6312   6230   -381    470    700       C  
ATOM    643  CG2 VAL A  85      51.819  50.303  54.005  1.00 46.61           C  
ANISOU  643  CG2 VAL A  85     5194   6591   5924   -608    259    754       C  
ATOM    644  N   THR A  86      49.433  51.356  50.294  1.00 49.13           N  
ANISOU  644  N   THR A  86     5108   7145   6416   -416   1055    504       N  
ATOM    645  CA  THR A  86      48.980  51.357  48.912  1.00 39.60           C  
ANISOU  645  CA  THR A  86     3843   5918   5287   -375   1179    480       C  
ATOM    646  C   THR A  86      49.096  52.743  48.281  1.00 39.44           C  
ANISOU  646  C   THR A  86     3817   5857   5312   -380   1167    419       C  
ATOM    647  O   THR A  86      49.663  52.880  47.206  1.00 44.89           O  
ANISOU  647  O   THR A  86     4504   6480   6074   -410   1218    438       O  
ATOM    648  CB  THR A  86      47.533  50.863  48.801  1.00 60.51           C  
ANISOU  648  CB  THR A  86     6532   8607   7853   -378   1272    435       C  
ATOM    649  OG1 THR A  86      47.477  49.478  49.167  1.00 58.11           O  
ANISOU  649  OG1 THR A  86     6274   8311   7493   -407   1290    514       O  
ATOM    650  CG2 THR A  86      47.025  51.027  47.379  1.00 51.77           C  
ANISOU  650  CG2 THR A  86     5419   7434   6818   -348   1306    415       C  
ATOM    651  N   LEU A  87      48.571  53.765  48.952  1.00 42.98           N  
ANISOU  651  N   LEU A  87     4296   6325   5711   -378   1109    330       N  
ATOM    652  CA  LEU A  87      48.681  55.138  48.457  1.00 40.01           C  
ANISOU  652  CA  LEU A  87     3951   5868   5385   -384   1034    278       C  
ATOM    653  C   LEU A  87      50.135  55.576  48.304  1.00 51.69           C  
ANISOU  653  C   LEU A  87     5406   7309   6923   -450   1006    335       C  
ATOM    654  O   LEU A  87      50.502  56.199  47.311  1.00 40.74           O  
ANISOU  654  O   LEU A  87     4082   5833   5566   -521   1020    346       O  
ATOM    655  CB  LEU A  87      47.956  56.107  49.389  1.00 40.77           C  
ANISOU  655  CB  LEU A  87     4053   5975   5463   -357    975    132       C  
ATOM    656  CG  LEU A  87      46.429  56.115  49.366  1.00 68.48           C  
ANISOU  656  CG  LEU A  87     7511   9475   9035   -298   1010    -23       C  
ATOM    657  CD1 LEU A  87      45.891  57.164  50.328  1.00 58.41           C  
ANISOU  657  CD1 LEU A  87     6199   8192   7801   -281    997   -237       C  
ATOM    658  CD2 LEU A  87      45.915  56.360  47.961  1.00 69.04           C  
ANISOU  658  CD2 LEU A  87     7612   9398   9224   -253    893     -5       C  
ATOM    659  N   LEU A  88      50.957  55.251  49.296  1.00 41.03           N  
ANISOU  659  N   LEU A  88     3988   6005   5596   -455    949    363       N  
ATOM    660  CA  LEU A  88      52.362  55.634  49.277  1.00 41.99           C  
ANISOU  660  CA  LEU A  88     4013   6081   5863   -513    897    378       C  
ATOM    661  C   LEU A  88      53.096  55.029  48.086  1.00 62.28           C  
ANISOU  661  C   LEU A  88     6473   8603   8587   -561   1059    385       C  
ATOM    662  O   LEU A  88      53.824  55.723  47.373  1.00 59.10           O  
ANISOU  662  O   LEU A  88     6047   8142   8266   -677   1146    344       O  
ATOM    663  CB  LEU A  88      53.036  55.215  50.579  1.00 48.20           C  
ANISOU  663  CB  LEU A  88     4755   6877   6682   -499    717    410       C  
ATOM    664  CG  LEU A  88      52.662  56.047  51.804  1.00 58.35           C  
ANISOU  664  CG  LEU A  88     6192   8188   7791   -527    583    369       C  
ATOM    665  CD1 LEU A  88      53.139  55.379  53.080  1.00 74.47           C  
ANISOU  665  CD1 LEU A  88     8319  10207   9771   -560    369    432       C  
ATOM    666  CD2 LEU A  88      53.268  57.430  51.676  1.00 48.54           C  
ANISOU  666  CD2 LEU A  88     4925   6894   6625   -576    522    317       C  
ATOM    667  N   LYS A  89      52.898  53.731  47.877  1.00 62.23           N  
ANISOU  667  N   LYS A  89     6421   8611   8612   -504   1127    415       N  
ATOM    668  CA  LYS A  89      53.506  53.029  46.750  1.00 58.26           C  
ANISOU  668  CA  LYS A  89     5819   8056   8260   -552   1327    374       C  
ATOM    669  C   LYS A  89      52.987  53.610  45.442  1.00 55.33           C  
ANISOU  669  C   LYS A  89     5648   7645   7731   -676   1493    359       C  
ATOM    670  O   LYS A  89      53.738  53.792  44.477  1.00 63.58           O  
ANISOU  670  O   LYS A  89     6696   8628   8836   -834   1696    289       O  
ATOM    671  CB  LYS A  89      53.210  51.529  46.826  1.00 58.69           C  
ANISOU  671  CB  LYS A  89     5830   8112   8357   -454   1333    409       C  
ATOM    672  CG  LYS A  89      54.100  50.749  47.787  1.00 53.62           C  
ANISOU  672  CG  LYS A  89     5007   7415   7952   -369   1135    417       C  
ATOM    673  CD  LYS A  89      55.516  50.641  47.243  1.00 76.23           C  
ANISOU  673  CD  LYS A  89     7576  10184  11205   -397   1232    275       C  
ATOM    674  CE  LYS A  89      56.392  49.765  48.120  1.00 90.26           C  
ANISOU  674  CE  LYS A  89     9138  11835  13322   -278    941    263       C  
ATOM    675  NZ  LYS A  89      57.787  49.696  47.602  1.00 96.36           N1+
ANISOU  675  NZ  LYS A  89     9521  12494  14598   -292   1043     51       N1+
ATOM    676  N   LEU A  90      51.696  53.922  45.441  1.00 61.80           N  
ANISOU  676  N   LEU A  90     6650   8473   8356   -628   1392    406       N  
ATOM    677  CA  LEU A  90      51.021  54.506  44.290  1.00 62.89           C  
ANISOU  677  CA  LEU A  90     7039   8512   8345   -730   1404    416       C  
ATOM    678  C   LEU A  90      51.645  55.832  43.864  1.00 55.48           C  
ANISOU  678  C   LEU A  90     6234   7476   7368   -898   1392    399       C  
ATOM    679  O   LEU A  90      51.910  56.036  42.680  1.00 50.67           O  
ANISOU  679  O   LEU A  90     5844   6758   6652  -1104   1518    399       O  
ATOM    680  CB  LEU A  90      49.539  54.707  44.598  1.00 52.17           C  
ANISOU  680  CB  LEU A  90     5758   7149   6914   -610   1218    423       C  
ATOM    681  CG  LEU A  90      48.600  54.669  43.400  1.00 56.19           C  
ANISOU  681  CG  LEU A  90     6495   7525   7328   -660   1151    445       C  
ATOM    682  CD1 LEU A  90      48.737  53.331  42.698  1.00 68.01           C  
ANISOU  682  CD1 LEU A  90     8008   9041   8791   -701   1336    473       C  
ATOM    683  CD2 LEU A  90      47.168  54.897  43.852  1.00 58.58           C  
ANISOU  683  CD2 LEU A  90     6753   7809   7694   -514    946    388       C  
ATOM    684  N   VAL A  91      51.880  56.730  44.822  1.00 43.06           N  
ANISOU  684  N   VAL A  91     4581   5928   5850   -850   1247    383       N  
ATOM    685  CA  VAL A  91      52.477  58.026  44.502  1.00 47.58           C  
ANISOU  685  CA  VAL A  91     5290   6397   6393  -1019   1211    371       C  
ATOM    686  C   VAL A  91      53.976  57.882  44.251  1.00 52.58           C  
ANISOU  686  C   VAL A  91     5766   7047   7166  -1192   1450    312       C  
ATOM    687  O   VAL A  91      54.586  58.726  43.592  1.00 52.44           O  
ANISOU  687  O   VAL A  91     5899   6930   7096  -1434   1543    288       O  
ATOM    688  CB  VAL A  91      52.239  59.084  45.616  1.00 55.69           C  
ANISOU  688  CB  VAL A  91     6285   7426   7448   -916    975    347       C  
ATOM    689  CG1 VAL A  91      50.753  59.341  45.807  1.00 57.94           C  
ANISOU  689  CG1 VAL A  91     6666   7665   7684   -761    779    323       C  
ATOM    690  CG2 VAL A  91      52.878  58.663  46.926  1.00 69.65           C  
ANISOU  690  CG2 VAL A  91     7790   9330   9343   -813    962    321       C  
ATOM    691  N   GLN A  92      54.569  56.808  44.766  1.00 52.23           N  
ANISOU  691  N   GLN A  92     5417   7101   7328  -1086   1540    268       N  
ATOM    692  CA  GLN A  92      55.970  56.530  44.468  1.00 55.79           C  
ANISOU  692  CA  GLN A  92     5623   7539   8035  -1224   1772    144       C  
ATOM    693  C   GLN A  92      56.128  56.231  42.982  1.00 69.01           C  
ANISOU  693  C   GLN A  92     7464   9143   9612  -1465   2121     71       C  
ATOM    694  O   GLN A  92      56.916  56.878  42.294  1.00 87.20           O  
ANISOU  694  O   GLN A  92     9834  11380  11920  -1752   2352    -25       O  
ATOM    695  CB  GLN A  92      56.493  55.362  45.305  1.00 63.13           C  
ANISOU  695  CB  GLN A  92     6198   8522   9266  -1029   1703    103       C  
ATOM    696  CG  GLN A  92      57.981  55.091  45.132  1.00 64.54           C  
ANISOU  696  CG  GLN A  92     6010   8651   9861  -1124   1880    -84       C  
ATOM    697  CD  GLN A  92      58.478  53.957  46.016  1.00 90.56           C  
ANISOU  697  CD  GLN A  92     8972  11925  13511   -901   1674   -118       C  
ATOM    698  OE1 GLN A  92      57.730  53.037  46.350  1.00 87.14           O  
ANISOU  698  OE1 GLN A  92     8625  11513  12970   -733   1539    -13       O  
ATOM    699  NE2 GLN A  92      59.747  54.022  46.401  1.00100.18           N  
ANISOU  699  NE2 GLN A  92     9817  13069  15177   -915   1611   -267       N  
ATOM    700  N   ARG A  93      55.357  55.265  42.489  1.00 77.81           N  
ANISOU  700  N   ARG A  93     8689  10265  10610  -1388   2172    109       N  
ATOM    701  CA  ARG A  93      55.438  54.867  41.084  1.00 75.32           C  
ANISOU  701  CA  ARG A  93     8596   9871  10152  -1634   2501     33       C  
ATOM    702  C   ARG A  93      54.826  55.909  40.151  1.00 70.26           C  
ANISOU  702  C   ARG A  93     8483   9093   9121  -1889   2448    128       C  
ATOM    703  O   ARG A  93      55.426  56.282  39.143  1.00 79.60           O  
ANISOU  703  O   ARG A  93     9908  10175  10160  -2251   2738     44       O  
ATOM    704  CB  ARG A  93      54.748  53.519  40.873  1.00 86.36           C  
ANISOU  704  CB  ARG A  93     9984  11297  11534  -1472   2519     54       C  
ATOM    705  CG  ARG A  93      55.349  52.386  41.684  1.00121.85           C  
ANISOU  705  CG  ARG A  93    14030  15861  16407  -1244   2523    -31       C  
ATOM    706  CD  ARG A  93      56.679  51.937  41.103  1.00141.56           C  
ANISOU  706  CD  ARG A  93    16255  18308  19222  -1400   2907   -289       C  
ATOM    707  NE  ARG A  93      56.523  51.417  39.749  1.00152.08           N  
ANISOU  707  NE  ARG A  93    17840  19574  20369  -1620   3266   -392       N  
ATOM    708  CZ  ARG A  93      56.138  50.176  39.465  1.00148.34           C  
ANISOU  708  CZ  ARG A  93    17349  19085  19929  -1502   3321   -420       C  
ATOM    709  NH1 ARG A  93      56.023  49.791  38.201  1.00164.71           N1+
ANISOU  709  NH1 ARG A  93    19735  21077  21769  -1699   3565   -515       N1+
ATOM    710  NH2 ARG A  93      55.864  49.322  40.443  1.00117.52           N  
ANISOU  710  NH2 ARG A  93    13198  15220  16233  -1176   3034   -337       N  
ATOM    711  N   HIS A  94      53.637  56.384  40.502  1.00 67.95           N  
ANISOU  711  N   HIS A  94     8377   8766   8674  -1721   2066    284       N  
ATOM    712  CA  HIS A  94      52.900  57.315  39.656  1.00 58.92           C  
ANISOU  712  CA  HIS A  94     7745   7425   7218  -1907   1869    387       C  
ATOM    713  C   HIS A  94      52.668  58.644  40.370  1.00 57.61           C  
ANISOU  713  C   HIS A  94     7614   7199   7075  -1832   1537    446       C  
ATOM    714  O   HIS A  94      51.643  58.827  41.028  1.00 49.09           O  
ANISOU  714  O   HIS A  94     6473   6122   6056  -1566   1213    491       O  
ATOM    715  CB  HIS A  94      51.560  56.706  39.237  1.00 61.32           C  
ANISOU  715  CB  HIS A  94     8243   7663   7393  -1775   1652    473       C  
ATOM    716  CG  HIS A  94      51.678  55.342  38.635  1.00 80.06           C  
ANISOU  716  CG  HIS A  94    10579  10090   9748  -1813   1942    415       C  
ATOM    717  ND1 HIS A  94      51.425  54.189  39.348  1.00 85.96           N  
ANISOU  717  ND1 HIS A  94    10960  10997  10703  -1530   1966    391       N  
ATOM    718  CD2 HIS A  94      52.024  54.944  37.388  1.00 94.06           C  
ANISOU  718  CD2 HIS A  94    12673  11760  11305  -2126   2227    362       C  
ATOM    719  CE1 HIS A  94      51.608  53.141  38.565  1.00 83.05           C  
ANISOU  719  CE1 HIS A  94    10653  10617  10287  -1629   2227    328       C  
ATOM    720  NE2 HIS A  94      51.973  53.570  37.371  1.00 95.02           N  
ANISOU  720  NE2 HIS A  94    12575  11982  11546  -1990   2411    294       N  
ATOM    721  N   PRO A  95      53.625  59.578  40.239  1.00 66.59           N  
ANISOU  721  N   PRO A  95     8839   8274   8187  -2085   1645    413       N  
ATOM    722  CA  PRO A  95      53.586  60.895  40.887  1.00 68.89           C  
ANISOU  722  CA  PRO A  95     9177   8489   8508  -2049   1353    452       C  
ATOM    723  C   PRO A  95      52.368  61.718  40.486  1.00 71.09           C  
ANISOU  723  C   PRO A  95     9872   8523   8615  -2020    914    561       C  
ATOM    724  O   PRO A  95      52.008  62.661  41.190  1.00 66.59           O  
ANISOU  724  O   PRO A  95     9274   7886   8142  -1873    606    564       O  
ATOM    725  CB  PRO A  95      54.872  61.567  40.398  1.00 62.94           C  
ANISOU  725  CB  PRO A  95     8538   7674   7703  -2442   1629    392       C  
ATOM    726  CG  PRO A  95      55.765  60.438  40.009  1.00 80.33           C  
ANISOU  726  CG  PRO A  95    10484  10012  10027  -2562   2110    248       C  
ATOM    727  CD  PRO A  95      54.853  59.395  39.449  1.00 77.64           C  
ANISOU  727  CD  PRO A  95    10275   9670   9555  -2450   2103    295       C  
ATOM    728  N   GLU A  96      51.743  61.354  39.370  1.00 64.55           N  
ANISOU  728  N   GLU A  96     9424   7536   7566  -2157    857    630       N  
ATOM    729  CA  GLU A  96      50.551  62.040  38.891  1.00 79.21           C  
ANISOU  729  CA  GLU A  96    11678   9096   9321  -2121    349    726       C  
ATOM    730  C   GLU A  96      49.395  61.930  39.878  1.00 86.47           C  
ANISOU  730  C   GLU A  96    12232  10080  10542  -1672     42    667       C  
ATOM    731  O   GLU A  96      48.530  62.802  39.932  1.00 86.35           O  
ANISOU  731  O   GLU A  96    12355   9830  10625  -1555   -413    668       O  
ATOM    732  CB  GLU A  96      50.116  61.475  37.538  1.00107.98           C  
ANISOU  732  CB  GLU A  96    15796  12555  12675  -2357    326    809       C  
ATOM    733  CG  GLU A  96      51.263  61.137  36.598  1.00139.43           C  
ANISOU  733  CG  GLU A  96    20058  16555  16362  -2818    829    788       C  
ATOM    734  CD  GLU A  96      51.769  59.721  36.783  1.00139.04           C  
ANISOU  734  CD  GLU A  96    19570  16807  16451  -2720   1323    662       C  
ATOM    735  OE1 GLU A  96      52.953  59.465  36.483  1.00144.62           O  
ANISOU  735  OE1 GLU A  96    20214  17611  17125  -2997   1824    543       O  
ATOM    736  OE2 GLU A  96      50.979  58.863  37.228  1.00139.97           O1+
ANISOU  736  OE2 GLU A  96    19395  17042  16744  -2377   1207    660       O1+
ATOM    737  N   THR A  97      49.383  60.854  40.657  1.00 88.60           N  
ANISOU  737  N   THR A  97    12043  10645  10978  -1442    294    592       N  
ATOM    738  CA  THR A  97      48.235  60.541  41.497  1.00 82.61           C  
ANISOU  738  CA  THR A  97    10972   9961  10456  -1095    109    509       C  
ATOM    739  C   THR A  97      48.109  61.477  42.700  1.00 75.89           C  
ANISOU  739  C   THR A  97     9892   9139   9803   -912    -39    400       C  
ATOM    740  O   THR A  97      47.020  61.634  43.248  1.00 79.09           O  
ANISOU  740  O   THR A  97    10125   9509  10417   -680   -244    280       O  
ATOM    741  CB  THR A  97      48.290  59.077  42.001  1.00 73.01           C  
ANISOU  741  CB  THR A  97     9411   9029   9302   -964    426    475       C  
ATOM    742  OG1 THR A  97      49.387  58.918  42.905  1.00 86.14           O  
ANISOU  742  OG1 THR A  97    10806  10904  11021   -956    684    443       O  
ATOM    743  CG2 THR A  97      48.461  58.114  40.838  1.00 67.78           C  
ANISOU  743  CG2 THR A  97     8958   8336   8459  -1140    605    547       C  
ATOM    744  N   LEU A  98      49.210  62.097  43.111  1.00 58.66           N  
ANISOU  744  N   LEU A  98     7696   7013   7579  -1030     84    409       N  
ATOM    745  CA  LEU A  98      49.177  62.986  44.270  1.00 56.58           C  
ANISOU  745  CA  LEU A  98     7256   6773   7469   -884    -43    301       C  
ATOM    746  C   LEU A  98      48.368  64.243  43.956  1.00 67.36           C  
ANISOU  746  C   LEU A  98     8856   7815   8923   -842   -476    259       C  
ATOM    747  O   LEU A  98      47.688  64.798  44.828  1.00 65.40           O  
ANISOU  747  O   LEU A  98     8419   7536   8892   -627   -639     92       O  
ATOM    748  CB  LEU A  98      50.594  63.355  44.712  1.00 50.21           C  
ANISOU  748  CB  LEU A  98     6391   6071   6615  -1040    145    326       C  
ATOM    749  CG  LEU A  98      50.740  64.118  46.033  1.00 54.21           C  
ANISOU  749  CG  LEU A  98     6720   6636   7241   -914     53    217       C  
ATOM    750  CD1 LEU A  98      50.194  63.320  47.204  1.00 60.88           C  
ANISOU  750  CD1 LEU A  98     7266   7695   8170   -690    151    110       C  
ATOM    751  CD2 LEU A  98      52.193  64.479  46.276  1.00 59.71           C  
ANISOU  751  CD2 LEU A  98     7379   7392   7915  -1104    188    254       C  
ATOM    752  N   SER A  99      48.437  64.680  42.702  1.00 60.94           N  
ANISOU  752  N   SER A  99     8482   6729   7945  -1069   -671    392       N  
ATOM    753  CA  SER A  99      47.617  65.791  42.243  1.00 63.36           C  
ANISOU  753  CA  SER A  99     9082   6641   8350  -1038  -1197    381       C  
ATOM    754  C   SER A  99      46.143  65.393  42.251  1.00 70.69           C  
ANISOU  754  C   SER A  99     9827   7472   9560   -752  -1466    254       C  
ATOM    755  O   SER A  99      45.285  66.175  42.660  1.00 75.03           O  
ANISOU  755  O   SER A  99    10260   7817  10433   -533  -1824     84       O  
ATOM    756  CB  SER A  99      48.042  66.236  40.846  1.00 76.01           C  
ANISOU  756  CB  SER A  99    11308   7940   9634  -1417  -1365    583       C  
ATOM    757  OG  SER A  99      47.862  65.195  39.904  1.00111.65           O  
ANISOU  757  OG  SER A  99    15996  12472  13954  -1546  -1240    679       O  
ATOM    758  N   HIS A 100      45.859  64.173  41.798  1.00 71.75           N  
ANISOU  758  N   HIS A 100     9906   7741   9615   -758  -1286    306       N  
ATOM    759  CA  HIS A 100      44.500  63.635  41.815  1.00 63.54           C  
ANISOU  759  CA  HIS A 100     8636   6643   8862   -512  -1484    173       C  
ATOM    760  C   HIS A 100      43.937  63.658  43.228  1.00 62.89           C  
ANISOU  760  C   HIS A 100     8019   6758   9117   -225  -1343   -100       C  
ATOM    761  O   HIS A 100      42.828  64.143  43.462  1.00 68.04           O  
ANISOU  761  O   HIS A 100     8479   7214  10158    -11  -1652   -321       O  
ATOM    762  CB  HIS A 100      44.477  62.208  41.272  1.00 67.86           C  
ANISOU  762  CB  HIS A 100     9179   7371   9236   -587  -1214    273       C  
ATOM    763  CG  HIS A 100      44.936  62.089  39.852  1.00 85.86           C  
ANISOU  763  CG  HIS A 100    12016   9453  11156   -908  -1295    495       C  
ATOM    764  ND1 HIS A 100      45.264  60.880  39.276  1.00102.62           N  
ANISOU  764  ND1 HIS A 100    14211  11735  13045  -1050   -969    587       N  
ATOM    765  CD2 HIS A 100      45.116  63.025  38.892  1.00 85.49           C  
ANISOU  765  CD2 HIS A 100    12531   9038  10913  -1154  -1653    629       C  
ATOM    766  CE1 HIS A 100      45.628  61.077  38.023  1.00102.72           C  
ANISOU  766  CE1 HIS A 100    14802  11506  12721  -1383  -1075    745       C  
ATOM    767  NE2 HIS A 100      45.548  62.369  37.763  1.00 98.78           N  
ANISOU  767  NE2 HIS A 100    14639  10681  12212  -1473  -1495    789       N  
ATOM    768  N   ILE A 101      44.718  63.125  44.163  1.00 55.15           N  
ANISOU  768  N   ILE A 101     6816   6142   7997   -245   -881   -106       N  
ATOM    769  CA  ILE A 101      44.374  63.135  45.579  1.00 56.49           C  
ANISOU  769  CA  ILE A 101     6595   6512   8357    -69   -682   -347       C  
ATOM    770  C   ILE A 101      44.113  64.553  46.081  1.00 53.34           C  
ANISOU  770  C   ILE A 101     6175   5902   8192     35   -947   -539       C  
ATOM    771  O   ILE A 101      43.151  64.793  46.811  1.00 56.17           O  
ANISOU  771  O   ILE A 101     6234   6234   8875    223   -967   -842       O  
ATOM    772  CB  ILE A 101      45.493  62.494  46.427  1.00 54.73           C  
ANISOU  772  CB  ILE A 101     6281   6630   7883   -166   -262   -262       C  
ATOM    773  CG1 ILE A 101      45.607  61.000  46.114  1.00 61.68           C  
ANISOU  773  CG1 ILE A 101     7111   7706   8619   -218     -6   -135       C  
ATOM    774  CG2 ILE A 101      45.234  62.706  47.902  1.00 47.54           C  
ANISOU  774  CG2 ILE A 101     5117   5873   7073    -62   -101   -494       C  
ATOM    775  CD1 ILE A 101      46.602  60.262  46.985  1.00 43.85           C  
ANISOU  775  CD1 ILE A 101     4744   5724   6193   -280    312    -69       C  
ATOM    776  N   ALA A 102      44.971  65.488  45.680  1.00 53.39           N  
ANISOU  776  N   ALA A 102     6494   5743   8047   -108  -1126   -390       N  
ATOM    777  CA  ALA A 102      44.853  66.879  46.113  1.00 64.26           C  
ANISOU  777  CA  ALA A 102     7903   6888   9624    -28  -1406   -548       C  
ATOM    778  C   ALA A 102      43.522  67.520  45.718  1.00 71.60           C  
ANISOU  778  C   ALA A 102     8781   7434  10990    179  -1891   -756       C  
ATOM    779  O   ALA A 102      42.882  68.183  46.532  1.00 78.20           O  
ANISOU  779  O   ALA A 102     9347   8183  12182    378  -1967  -1079       O  
ATOM    780  CB  ALA A 102      46.004  67.691  45.555  1.00 79.50           C  
ANISOU  780  CB  ALA A 102    10238   8676  11291   -273  -1532   -316       C  
ATOM    781  N   GLU A 103      43.109  67.316  44.471  1.00 76.32           N  
ANISOU  781  N   GLU A 103     9638   7774  11584    125  -2234   -597       N  
ATOM    782  CA  GLU A 103      41.905  67.954  43.942  1.00 92.38           C  
ANISOU  782  CA  GLU A 103    11674   9353  14074    313  -2841   -762       C  
ATOM    783  C   GLU A 103      40.662  67.104  44.173  1.00101.25           C  
ANISOU  783  C   GLU A 103    12325  10554  15593    539  -2774  -1024       C  
ATOM    784  O   GLU A 103      39.574  67.442  43.710  1.00111.63           O  
ANISOU  784  O   GLU A 103    13545  11492  17378    717  -3285  -1197       O  
ATOM    785  CB  GLU A 103      42.065  68.243  42.446  1.00 93.96           C  
ANISOU  785  CB  GLU A 103    12494   9159  14049     95  -3348   -445       C  
ATOM    786  N   LEU A 104      40.838  65.995  44.882  1.00 99.27           N  
ANISOU  786  N   LEU A 104    11786  10763  15170    514  -2174  -1056       N  
ATOM    787  CA  LEU A 104      39.768  65.032  45.117  1.00 97.25           C  
ANISOU  787  CA  LEU A 104    11111  10634  15204    651  -2007  -1278       C  
ATOM    788  C   LEU A 104      38.545  65.660  45.779  1.00 99.43           C  
ANISOU  788  C   LEU A 104    10910  10723  16148    916  -2158  -1772       C  
ATOM    789  O   LEU A 104      37.411  65.260  45.511  1.00107.47           O  
ANISOU  789  O   LEU A 104    11622  11607  17604   1053  -2321  -1987       O  
ATOM    790  CB  LEU A 104      40.291  63.887  45.979  1.00 83.02           C  
ANISOU  790  CB  LEU A 104     9141   9337  13065    544  -1334  -1235       C  
ATOM    791  CG  LEU A 104      39.663  62.509  45.811  1.00 69.16           C  
ANISOU  791  CG  LEU A 104     7191   7762  11324    538  -1111  -1239       C  
ATOM    792  CD1 LEU A 104      39.601  62.129  44.341  1.00 63.34           C  
ANISOU  792  CD1 LEU A 104     6780   6804  10481    465  -1477   -961       C  
ATOM    793  CD2 LEU A 104      40.492  61.506  46.588  1.00 76.36           C  
ANISOU  793  CD2 LEU A 104     8095   9106  11814    390   -545  -1106       C  
TER     794      LEU A 104                                                      
ATOM    795  N   ARG B   4      68.231  98.337  42.827  1.00100.63           N  
ANISOU  795  N   ARG B   4    12047  11288  14901  -3565  -2157   1871       N  
ATOM    796  CA  ARG B   4      67.060  97.785  43.497  1.00113.78           C  
ANISOU  796  CA  ARG B   4    13594  12916  16721  -3186  -2288   1870       C  
ATOM    797  C   ARG B   4      67.292  97.675  45.005  1.00127.01           C  
ANISOU  797  C   ARG B   4    15015  14633  18610  -2794  -2116   1395       C  
ATOM    798  O   ARG B   4      67.963  96.756  45.473  1.00130.44           O  
ANISOU  798  O   ARG B   4    15404  15392  18764  -2681  -1910   1046       O  
ATOM    799  CB  ARG B   4      66.709  96.417  42.906  1.00117.68           C  
ANISOU  799  CB  ARG B   4    14215  13732  16767  -3212  -2297   1956       C  
ATOM    800  CG  ARG B   4      65.425  95.803  43.444  1.00123.05           C  
ANISOU  800  CG  ARG B   4    14800  14372  17583  -2869  -2437   1998       C  
ATOM    801  CD  ARG B   4      65.146  94.451  42.795  1.00125.68           C  
ANISOU  801  CD  ARG B   4    15264  15024  17464  -2924  -2437   2080       C  
ATOM    802  NE  ARG B   4      63.996  93.775  43.393  1.00126.77           N  
ANISOU  802  NE  ARG B   4    15299  15150  17717  -2593  -2526   2065       N  
ATOM    803  CZ  ARG B   4      63.641  92.522  43.123  1.00112.93           C  
ANISOU  803  CZ  ARG B   4    13610  13660  15636  -2549  -2510   2069       C  
ATOM    804  NH1 ARG B   4      64.347  91.801  42.263  1.00113.96           N  
ANISOU  804  NH1 ARG B   4    13900  14090  15310  -2808  -2412   2077       N  
ATOM    805  NH2 ARG B   4      62.583  91.986  43.718  1.00 95.94           N  
ANISOU  805  NH2 ARG B   4    11358  11470  13625  -2257  -2577   2045       N  
ATOM    806  N   ASP B   5      66.732  98.619  45.758  1.00131.50           N  
ANISOU  806  N   ASP B   5    15422  14864  19679  -2594  -2213   1379       N  
ATOM    807  CA  ASP B   5      66.911  98.664  47.209  1.00126.92           C  
ANISOU  807  CA  ASP B   5    14610  14292  19320  -2247  -2059    936       C  
ATOM    808  C   ASP B   5      65.780  97.942  47.936  1.00128.59           C  
ANISOU  808  C   ASP B   5    14727  14528  19603  -1906  -2115    877       C  
ATOM    809  O   ASP B   5      64.625  97.993  47.514  1.00131.62           O  
ANISOU  809  O   ASP B   5    15137  14731  20142  -1889  -2330   1194       O  
ATOM    810  CB  ASP B   5      67.004 100.113  47.694  1.00118.97           C  
ANISOU  810  CB  ASP B   5    13461  12913  18827  -2230  -2095    890       C  
ATOM    811  N   LEU B   6      66.122  97.274  49.034  1.00117.34           N  
ANISOU  811  N   LEU B   6    13196  13321  18066  -1644  -1926    464       N  
ATOM    812  CA  LEU B   6      65.173  96.437  49.762  1.00 99.30           C  
ANISOU  812  CA  LEU B   6    10851  11112  15767  -1347  -1929    369       C  
ATOM    813  C   LEU B   6      64.203  97.232  50.629  1.00 95.60           C  
ANISOU  813  C   LEU B   6    10191  10317  15813  -1121  -1999    318       C  
ATOM    814  O   LEU B   6      63.010  96.926  50.676  1.00 79.56           O  
ANISOU  814  O   LEU B   6     8126   8195  13907   -994  -2110    457       O  
ATOM    815  CB  LEU B   6      65.924  95.429  50.635  1.00 99.51           C  
ANISOU  815  CB  LEU B   6    10865  11478  15465  -1167  -1714    -45       C  
ATOM    816  N   PHE B   7      64.720  98.248  51.315  1.00 99.63           N  
ANISOU  816  N   PHE B   7    10562  10656  16638  -1077  -1926     93       N  
ATOM    817  CA  PHE B   7      63.918  99.027  52.254  1.00 94.78           C  
ANISOU  817  CA  PHE B   7     9738   9745  16527   -860  -1954    -38       C  
ATOM    818  C   PHE B   7      62.805  99.804  51.551  1.00 95.33           C  
ANISOU  818  C   PHE B   7     9769   9436  17017   -935  -2217    352       C  
ATOM    819  O   PHE B   7      61.693  99.926  52.074  1.00 90.80           O  
ANISOU  819  O   PHE B   7     9047   8676  16777   -741  -2282    325       O  
ATOM    820  CB  PHE B   7      64.808  99.984  53.046  1.00 99.11           C  
ANISOU  820  CB  PHE B   7    10149  10192  17315   -828  -1823   -364       C  
ATOM    821  CG  PHE B   7      64.049 100.873  53.987  1.00118.93           C  
ANISOU  821  CG  PHE B   7    12431  12389  20368   -630  -1837   -526       C  
ATOM    822  CD1 PHE B   7      63.442 100.349  55.118  1.00112.66           C  
ANISOU  822  CD1 PHE B   7    11534  11682  19589   -359  -1721   -816       C  
ATOM    823  CD2 PHE B   7      63.944 102.235  53.743  1.00123.79           C  
ANISOU  823  CD2 PHE B   7    12936  12616  21482   -728  -1960   -399       C  
ATOM    824  CE1 PHE B   7      62.742 101.166  55.988  1.00113.75           C  
ANISOU  824  CE1 PHE B   7    11449  11542  20230   -196  -1708  -1002       C  
ATOM    825  CE2 PHE B   7      63.246 103.057  54.608  1.00120.19           C  
ANISOU  825  CE2 PHE B   7    12245  11863  21560   -546  -1969   -580       C  
ATOM    826  CZ  PHE B   7      62.644 102.522  55.732  1.00121.44           C  
ANISOU  826  CZ  PHE B   7    12287  12127  21727   -283  -1833   -895       C  
ATOM    827  N   ALA B   8      63.112 100.323  50.366  1.00 89.08           N  
ANISOU  827  N   ALA B   8     9113   8523  16209  -1227  -2373    705       N  
ATOM    828  CA  ALA B   8      62.126 101.035  49.560  1.00102.46           C  
ANISOU  828  CA  ALA B   8    10813   9851  18265  -1327  -2677   1124       C  
ATOM    829  C   ALA B   8      60.962 100.123  49.197  1.00112.60           C  
ANISOU  829  C   ALA B   8    12141  11203  19438  -1242  -2818   1330       C  
ATOM    830  O   ALA B   8      59.793 100.510  49.296  1.00123.19           O  
ANISOU  830  O   ALA B   8    13345  12252  21211  -1116  -3005   1447       O  
ATOM    831  CB  ALA B   8      62.771 101.589  48.304  1.00106.37           C  
ANISOU  831  CB  ALA B   8    11514  10263  18638  -1696  -2806   1478       C  
ATOM    832  N   GLU B   9      61.295  98.906  48.779  1.00116.65           N  
ANISOU  832  N   GLU B   9    12829  12099  19394  -1311  -2725   1351       N  
ATOM    833  CA  GLU B   9      60.292  97.931  48.380  1.00117.65           C  
ANISOU  833  CA  GLU B   9    13012  12332  19357  -1252  -2838   1534       C  
ATOM    834  C   GLU B   9      59.465  97.467  49.571  1.00102.34           C  
ANISOU  834  C   GLU B   9    10880  10407  17598   -918  -2724   1233       C  
ATOM    835  O   GLU B   9      58.252  97.316  49.459  1.00102.69           O  
ANISOU  835  O   GLU B   9    10849  10304  17865   -821  -2881   1378       O  
ATOM    836  CB  GLU B   9      60.953  96.737  47.689  1.00132.72           C  
ANISOU  836  CB  GLU B   9    15146  14655  20627  -1412  -2739   1585       C  
ATOM    837  CG  GLU B   9      61.632  97.096  46.376  1.00148.61           C  
ANISOU  837  CG  GLU B   9    17373  16672  22419  -1788  -2848   1908       C  
ATOM    838  CD  GLU B   9      62.094  95.879  45.600  1.00152.46           C  
ANISOU  838  CD  GLU B   9    18066  17554  22308  -1957  -2769   1969       C  
ATOM    839  OE1 GLU B   9      63.138  95.299  45.965  1.00160.43           O  
ANISOU  839  OE1 GLU B   9    19093  18863  23000  -1951  -2517   1660       O  
ATOM    840  OE2 GLU B   9      61.411  95.504  44.624  1.00146.81           O1+
ANISOU  840  OE2 GLU B   9    17485  16842  21454  -2095  -2967   2313       O1+
ATOM    841  N   LEU B  10      60.116  97.243  50.708  1.00 75.83           N  
ANISOU  841  N   LEU B  10     7447   7224  14142   -753  -2454    809       N  
ATOM    842  CA  LEU B  10      59.397  96.848  51.913  1.00 74.55           C  
ANISOU  842  CA  LEU B  10     7125   7079  14121   -465  -2317    501       C  
ATOM    843  C   LEU B  10      58.422  97.933  52.353  1.00 90.49           C  
ANISOU  843  C   LEU B  10     8903   8683  16797   -347  -2432    486       C  
ATOM    844  O   LEU B  10      57.270  97.644  52.678  1.00 83.54           O  
ANISOU  844  O   LEU B  10     7904   7714  16124   -197  -2464    461       O  
ATOM    845  CB  LEU B  10      60.368  96.528  53.049  1.00 72.59           C  
ANISOU  845  CB  LEU B  10     6865   7073  13641   -336  -2035     58       C  
ATOM    846  CG  LEU B  10      60.881  95.088  53.089  1.00 87.87           C  
ANISOU  846  CG  LEU B  10     8978   9426  14984   -314  -1894    -46       C  
ATOM    847  CD1 LEU B  10      61.679  94.830  54.358  1.00 81.71           C  
ANISOU  847  CD1 LEU B  10     8170   8833  14044   -147  -1660   -495       C  
ATOM    848  CD2 LEU B  10      59.724  94.102  52.964  1.00 73.25           C  
ANISOU  848  CD2 LEU B  10     7156   7643  13032   -225  -1939     79       C  
ATOM    849  N   SER B  11      58.888  99.179  52.354  1.00100.63           N  
ANISOU  849  N   SER B  11    10103   9706  18426   -423  -2488    485       N  
ATOM    850  CA  SER B  11      58.050 100.314  52.731  1.00 95.68           C  
ANISOU  850  CA  SER B  11     9229   8649  18474   -321  -2612    460       C  
ATOM    851  C   SER B  11      56.853 100.462  51.795  1.00 88.17           C  
ANISOU  851  C   SER B  11     8258   7432  17810   -372  -2938    859       C  
ATOM    852  O   SER B  11      55.709 100.579  52.245  1.00 85.28           O  
ANISOU  852  O   SER B  11     7683   6864  17856   -199  -2994    775       O  
ATOM    853  CB  SER B  11      58.871 101.602  52.737  1.00112.81           C  
ANISOU  853  CB  SER B  11    11346  10585  20932   -430  -2635    431       C  
ATOM    854  OG  SER B  11      59.995 101.477  53.587  1.00123.44           O  
ANISOU  854  OG  SER B  11    12700  12176  22024   -383  -2353     49       O  
ATOM    855  N   SER B  12      57.129 100.455  50.495  1.00 85.15           N  
ANISOU  855  N   SER B  12     8091   7051  17209   -619  -3152   1280       N  
ATOM    856  CA  SER B  12      56.082 100.554  49.487  1.00 87.28           C  
ANISOU  856  CA  SER B  12     8386   7087  17687   -696  -3504   1698       C  
ATOM    857  C   SER B  12      55.046  99.442  49.652  1.00 92.67           C  
ANISOU  857  C   SER B  12     9021   7929  18259   -536  -3486   1654       C  
ATOM    858  O   SER B  12      53.837  99.695  49.668  1.00 97.69           O  
ANISOU  858  O   SER B  12     9474   8289  19356   -418  -3676   1719       O  
ATOM    859  CB  SER B  12      56.692 100.510  48.085  1.00 99.75           C  
ANISOU  859  CB  SER B  12    10268   8743  18889  -1021  -3686   2130       C  
ATOM    860  OG  SER B  12      55.691 100.635  47.090  1.00120.33           O  
ANISOU  860  OG  SER B  12    12922  11116  21682  -1106  -4062   2552       O  
ATOM    861  N   ALA B  13      55.530  98.212  49.786  1.00 82.16           N  
ANISOU  861  N   ALA B  13     7843   7033  16339   -533  -3257   1525       N  
ATOM    862  CA  ALA B  13      54.659  97.057  49.947  1.00 80.30           C  
ANISOU  862  CA  ALA B  13     7592   6983  15936   -402  -3206   1473       C  
ATOM    863  C   ALA B  13      53.813  97.179  51.206  1.00 80.40           C  
ANISOU  863  C   ALA B  13     7326   6860  16363   -134  -3057   1108       C  
ATOM    864  O   ALA B  13      52.644  96.794  51.216  1.00 80.81           O  
ANISOU  864  O   ALA B  13     7260   6829  16613    -31  -3137   1134       O  
ATOM    865  CB  ALA B  13      55.478  95.775  49.982  1.00 76.80           C  
ANISOU  865  CB  ALA B  13     7360   7014  14805   -441  -2968   1359       C  
ATOM    866  N   LEU B  14      54.403  97.727  52.263  1.00 80.24           N  
ANISOU  866  N   LEU B  14     7195   6817  16476    -35  -2833    754       N  
ATOM    867  CA  LEU B  14      53.715  97.829  53.545  1.00 86.11           C  
ANISOU  867  CA  LEU B  14     7692   7470  17556    194  -2639    357       C  
ATOM    868  C   LEU B  14      52.661  98.933  53.579  1.00 88.08           C  
ANISOU  868  C   LEU B  14     7652   7248  18568    267  -2845    385       C  
ATOM    869  O   LEU B  14      51.620  98.773  54.219  1.00 94.63           O  
ANISOU  869  O   LEU B  14     8271   7982  19703    425  -2771    173       O  
ATOM    870  CB  LEU B  14      54.723  98.040  54.672  1.00 85.79           C  
ANISOU  870  CB  LEU B  14     7641   7575  17381    265  -2340    -46       C  
ATOM    871  CG  LEU B  14      55.324  96.748  55.222  1.00 75.77           C  
ANISOU  871  CG  LEU B  14     6562   6754  15475    313  -2072   -255       C  
ATOM    872  CD1 LEU B  14      56.260  97.041  56.379  1.00 97.20           C  
ANISOU  872  CD1 LEU B  14     9252   9577  18104    394  -1818   -660       C  
ATOM    873  CD2 LEU B  14      54.216  95.808  55.656  1.00 74.84           C  
ANISOU  873  CD2 LEU B  14     6397   6724  15317    442  -1975   -357       C  
ATOM    874  N   VAL B  15      52.917 100.051  52.904  1.00 86.60           N  
ANISOU  874  N   VAL B  15     7446   6752  18706    149  -3100    633       N  
ATOM    875  CA  VAL B  15      51.903 101.100  52.847  1.00 97.50           C  
ANISOU  875  CA  VAL B  15     8550   7648  20847    221  -3348    688       C  
ATOM    876  C   VAL B  15      50.780 100.657  51.900  1.00 91.38           C  
ANISOU  876  C   VAL B  15     7778   6766  20175    198  -3658   1030       C  
ATOM    877  O   VAL B  15      49.602 100.939  52.147  1.00 93.48           O  
ANISOU  877  O   VAL B  15     7771   6752  20996    338  -3770    940       O  
ATOM    878  CB  VAL B  15      52.494 102.470  52.421  1.00 93.19           C  
ANISOU  878  CB  VAL B  15     7991   6763  20653     98  -3553    864       C  
ATOM    879  CG1 VAL B  15      53.112 102.408  51.035  1.00101.32           C  
ANISOU  879  CG1 VAL B  15     9336   7851  21308   -167  -3800   1360       C  
ATOM    880  CG2 VAL B  15      51.429 103.552  52.491  1.00 97.21           C  
ANISOU  880  CG2 VAL B  15     8184   6746  22004    204  -3809    869       C  
ATOM    881  N   GLU B  16      51.145  99.930  50.843  1.00 90.00           N  
ANISOU  881  N   GLU B  16     7900   6827  19467     22  -3783   1389       N  
ATOM    882  CA  GLU B  16      50.155  99.286  49.981  1.00 94.71           C  
ANISOU  882  CA  GLU B  16     8533   7411  20040     -4  -4039   1683       C  
ATOM    883  C   GLU B  16      49.267  98.346  50.786  1.00 96.46           C  
ANISOU  883  C   GLU B  16     8595   7791  20266    192  -3813   1367       C  
ATOM    884  O   GLU B  16      48.050  98.323  50.611  1.00106.68           O  
ANISOU  884  O   GLU B  16     9699   8873  21962    278  -4001   1416       O  
ATOM    885  CB  GLU B  16      50.830  98.499  48.855  1.00104.48           C  
ANISOU  885  CB  GLU B  16    10134   8963  20601   -234  -4121   2041       C  
ATOM    886  CG  GLU B  16      51.273  99.326  47.664  1.00132.65           C  
ANISOU  886  CG  GLU B  16    13884  12320  24195   -481  -4463   2489       C  
ATOM    887  CD  GLU B  16      51.780  98.463  46.523  1.00137.07           C  
ANISOU  887  CD  GLU B  16    14789  13204  24087   -724  -4534   2820       C  
ATOM    888  OE1 GLU B  16      51.683  97.222  46.627  1.00130.41           O  
ANISOU  888  OE1 GLU B  16    14016  12718  22818   -678  -4351   2711       O  
ATOM    889  OE2 GLU B  16      52.275  99.024  45.523  1.00151.14           O1+
ANISOU  889  OE2 GLU B  16    16778  14880  25769   -974  -4766   3183       O1+
ATOM    890  N   ALA B  17      49.892  97.565  51.659  1.00104.45           N  
ANISOU  890  N   ALA B  17     9690   9170  20825    251  -3417   1043       N  
ATOM    891  CA  ALA B  17      49.181  96.605  52.492  1.00 83.81           C  
ANISOU  891  CA  ALA B  17     6977   6741  18127    407  -3156    734       C  
ATOM    892  C   ALA B  17      48.236  97.313  53.448  1.00101.92           C  
ANISOU  892  C   ALA B  17     8904   8720  21101    585  -3083    395       C  
ATOM    893  O   ALA B  17      47.089  96.892  53.625  1.00 86.84           O  
ANISOU  893  O   ALA B  17     6820   6744  19431    681  -3077    295       O  
ATOM    894  CB  ALA B  17      50.162  95.748  53.263  1.00 80.28           C  
ANISOU  894  CB  ALA B  17     6720   6715  17066    424  -2777    468       C  
ATOM    895  N   LYS B  18      48.729  98.387  54.063  1.00113.77           N  
ANISOU  895  N   LYS B  18    10277  10028  22921    620  -3014    197       N  
ATOM    896  CA  LYS B  18      47.922  99.188  54.976  1.00 90.18           C  
ANISOU  896  CA  LYS B  18     6924   6722  20619    774  -2937   -156       C  
ATOM    897  C   LYS B  18      46.679  99.698  54.264  1.00 96.89           C  
ANISOU  897  C   LYS B  18     7536   7165  22114    806  -3313     55       C  
ATOM    898  O   LYS B  18      45.563  99.547  54.762  1.00116.21           O  
ANISOU  898  O   LYS B  18     9743   9510  24901    906  -3227   -195       O  
ATOM    899  CB  LYS B  18      48.729 100.360  55.534  1.00 91.46           C  
ANISOU  899  CB  LYS B  18     7002   6712  21038    779  -2867   -338       C  
ATOM    900  N   GLN B  19      46.877 100.279  53.085  1.00110.46           N  
ANISOU  900  N   GLN B  19     9361   8672  23937    682  -3719    509       N  
ATOM    901  CA  GLN B  19      45.760 100.807  52.308  1.00 98.96           C  
ANISOU  901  CA  GLN B  19     7775   6873  22953    633  -4096    736       C  
ATOM    902  C   GLN B  19      44.799  99.714  51.844  1.00 98.18           C  
ANISOU  902  C   GLN B  19     7716   6930  22659    632  -4154    837       C  
ATOM    903  O   GLN B  19      43.597  99.947  51.738  1.00103.46           O  
ANISOU  903  O   GLN B  19     8215   7396  23699    621  -4270    768       O  
ATOM    904  CB  GLN B  19      46.277 101.588  51.105  1.00100.98           C  
ANISOU  904  CB  GLN B  19     8210   6919  23239    457  -4512   1229       C  
ATOM    905  CG  GLN B  19      47.114 102.791  51.480  1.00102.43           C  
ANISOU  905  CG  GLN B  19     8337   6887  23693    438  -4489   1146       C  
ATOM    906  CD  GLN B  19      47.829 103.378  50.288  1.00123.04           C  
ANISOU  906  CD  GLN B  19    11202   9355  26194    234  -4847   1655       C  
ATOM    907  OE1 GLN B  19      49.032 103.633  50.337  1.00121.21           O  
ANISOU  907  OE1 GLN B  19    11144   9194  25716    154  -4736   1695       O  
ATOM    908  NE2 GLN B  19      47.094 103.592  49.203  1.00137.12           N  
ANISOU  908  NE2 GLN B  19    13041  11003  28054     90  -5233   2010       N  
ATOM    909  N   HIS B  20      45.322  98.522  51.570  1.00109.33           N  
ANISOU  909  N   HIS B  20     9342   8706  23493    633  -4072    983       N  
ATOM    910  CA  HIS B  20      44.473  97.404  51.166  1.00103.62           C  
ANISOU  910  CA  HIS B  20     8653   8157  22561    635  -4103   1063       C  
ATOM    911  C   HIS B  20      43.598  96.942  52.327  1.00102.04           C  
ANISOU  911  C   HIS B  20     8220   8015  22534    778  -3739    570       C  
ATOM    912  O   HIS B  20      42.424  96.616  52.140  1.00 94.72           O  
ANISOU  912  O   HIS B  20     7193   7013  21784    776  -3797    531       O  
ATOM    913  CB  HIS B  20      45.313  96.238  50.649  1.00 99.53           C  
ANISOU  913  CB  HIS B  20     8515   8104  21198    502  -3995   1267       C  
ATOM    914  CG  HIS B  20      44.514  95.005  50.357  1.00103.64           C  
ANISOU  914  CG  HIS B  20     9064   8829  21485    518  -3978   1304       C  
ATOM    915  ND1 HIS B  20      44.494  93.914  51.199  1.00 93.10           N  
ANISOU  915  ND1 HIS B  20     7767   7828  19780    588  -3571    987       N  
ATOM    916  CD2 HIS B  20      43.703  94.693  49.319  1.00105.77           C  
ANISOU  916  CD2 HIS B  20     9336   9011  21842    466  -4325   1618       C  
ATOM    917  CE1 HIS B  20      43.707  92.982  50.691  1.00 89.99           C  
ANISOU  917  CE1 HIS B  20     7387   7538  19265    579  -3652   1100       C  
ATOM    918  NE2 HIS B  20      43.215  93.430  49.549  1.00 97.23           N  
ANISOU  918  NE2 HIS B  20     8275   8211  20456    508  -4108   1474       N  
ATOM    919  N   SER B  21      44.176  96.906  53.524  1.00103.56           N  
ANISOU  919  N   SER B  21     8353   8354  22642    878  -3351    183       N  
ATOM    920  CA  SER B  21      43.412  96.588  54.725  1.00111.68           C  
ANISOU  920  CA  SER B  21     9173   9422  23837    987  -2977   -310       C  
ATOM    921  C   SER B  21      42.340  97.650  54.961  1.00128.02           C  
ANISOU  921  C   SER B  21    10986  11104  26551    963  -3053   -505       C  
ATOM    922  O   SER B  21      41.210  97.330  55.332  1.00125.29           O  
ANISOU  922  O   SER B  21    10480  10712  26412    983  -2931   -744       O  
ATOM    923  CB  SER B  21      44.329  96.479  55.943  1.00103.86           C  
ANISOU  923  CB  SER B  21     8252   8673  22538   1035  -2549   -679       C  
ATOM    924  OG  SER B  21      44.914  97.733  56.252  1.00103.91           O  
ANISOU  924  OG  SER B  21     8151   8445  22887   1049  -2591   -769       O  
ATOM    925  N   GLU B  22      42.705  98.912  54.737  1.00141.85           N  
ANISOU  925  N   GLU B  22    12689  12574  28634    910  -3261   -409       N  
ATOM    926  CA  GLU B  22      41.751 100.017  54.823  1.00144.98           C  
ANISOU  926  CA  GLU B  22    12829  12582  29676    868  -3406   -550       C  
ATOM    927  C   GLU B  22      40.653  99.871  53.768  1.00131.83           C  
ANISOU  927  C   GLU B  22    11136  10744  28209    801  -3768   -274       C  
ATOM    928  O   GLU B  22      39.499 100.224  54.008  1.00129.39           O  
ANISOU  928  O   GLU B  22    10586  10207  28370    799  -3792   -499       O  
ATOM    929  CB  GLU B  22      42.463 101.365  54.655  1.00159.24           C  
ANISOU  929  CB  GLU B  22    14605  14135  31765    810  -3600   -440       C  
ATOM    930  CG  GLU B  22      43.497 101.688  55.730  1.00162.02           C  
ANISOU  930  CG  GLU B  22    14951  14609  32000    870  -3257   -754       C  
ATOM    931  CD  GLU B  22      42.944 102.550  56.849  1.00170.03           C  
ANISOU  931  CD  GLU B  22    15674  15440  33490    882  -3038  -1241       C  
ATOM    932  OE1 GLU B  22      41.773 102.975  56.755  1.00186.17           O  
ANISOU  932  OE1 GLU B  22    17498  17230  36007    845  -3175  -1327       O  
ATOM    933  OE2 GLU B  22      43.685 102.807  57.821  1.00159.93           O  
ANISOU  933  OE2 GLU B  22    14382  14273  32110    919  -2735  -1549       O  
ATOM    934  N   GLY B  23      41.019  99.342  52.604  1.00123.88           N  
ANISOU  934  N   GLY B  23    10379   9853  26835    735  -4049    198       N  
ATOM    935  CA  GLY B  23      40.074  99.142  51.520  1.00116.98           C  
ANISOU  935  CA  GLY B  23     9528   8854  26067    655  -4407    486       C  
ATOM    936  C   GLY B  23      40.136 100.227  50.461  1.00125.90           C  
ANISOU  936  C   GLY B  23    10701   9679  27455    516  -4885    867       C  
ATOM    937  O   GLY B  23      39.238 100.344  49.628  1.00140.06           O  
ANISOU  937  O   GLY B  23    12464  11292  29460    441  -5218   1056       O  
ATOM    938  N   LYS B  24      41.199 101.022  50.492  1.00121.46           N  
ANISOU  938  N   LYS B  24    10213   9063  26874    476  -4923    972       N  
ATOM    939  CA  LYS B  24      41.368 102.117  49.544  1.00118.48           C  
ANISOU  939  CA  LYS B  24     9883   8408  26725    330  -5360   1331       C  
ATOM    940  C   LYS B  24      42.181 101.693  48.323  1.00114.87           C  
ANISOU  940  C   LYS B  24     9801   8130  25716    180  -5610   1861       C  
ATOM    941  O   LYS B  24      42.491 102.515  47.460  1.00126.96           O  
ANISOU  941  O   LYS B  24    11441   9487  27311     27  -5960   2204       O  
ATOM    942  CB  LYS B  24      42.038 103.313  50.227  1.00114.01           C  
ANISOU  942  CB  LYS B  24     9176   7658  26484    349  -5274   1151       C  
ATOM    943  N   LEU B  25      42.533 100.413  48.258  1.00109.51           N  
ANISOU  943  N   LEU B  25     9320   7811  24479    208  -5425   1918       N  
ATOM    944  CA  LEU B  25      43.410  99.922  47.202  1.00113.66           C  
ANISOU  944  CA  LEU B  25    10209   8555  24422     49  -5599   2374       C  
ATOM    945  C   LEU B  25      43.132  98.465  46.840  1.00111.60           C  
ANISOU  945  C   LEU B  25    10100   8631  23672     52  -5523   2455       C  
ATOM    946  O   LEU B  25      42.804  97.651  47.703  1.00113.45           O  
ANISOU  946  O   LEU B  25    10204   9043  23861    215  -5198   2121       O  
ATOM    947  CB  LEU B  25      44.872 100.087  47.628  1.00116.54           C  
ANISOU  947  CB  LEU B  25    10705   9046  24528     60  -5403   2372       C  
ATOM    948  CG  LEU B  25      45.988  99.593  46.706  1.00109.84           C  
ANISOU  948  CG  LEU B  25    10239   8438  23058   -116  -5511   2791       C  
ATOM    949  CD1 LEU B  25      45.846 100.180  45.313  1.00120.08           C  
ANISOU  949  CD1 LEU B  25    11736   9581  24309   -376  -5951   3254       C  
ATOM    950  CD2 LEU B  25      47.337  99.955  47.297  1.00 98.79           C  
ANISOU  950  CD2 LEU B  25     8918   7104  21514   -108  -5274   2683       C  
ATOM    951  N   THR B  26      43.267  98.147  45.556  1.00108.55           N  
ANISOU  951  N   THR B  26     9994   8346  22905   -147  -5816   2889       N  
ATOM    952  CA  THR B  26      43.124  96.776  45.078  1.00112.69           C  
ANISOU  952  CA  THR B  26    10694   9214  22910   -181  -5763   3002       C  
ATOM    953  C   THR B  26      44.494  96.158  44.816  1.00107.26           C  
ANISOU  953  C   THR B  26    10305   8870  21578   -277  -5656   3202       C  
ATOM    954  O   THR B  26      45.354  96.781  44.190  1.00104.01           O  
ANISOU  954  O   THR B  26    10101   8408  21010   -456  -5825   3492       O  
ATOM    955  CB  THR B  26      42.275  96.706  43.786  1.00112.05           C  
ANISOU  955  CB  THR B  26    10731   9051  22791   -357  -6143   3314       C  
ATOM    956  OG1 THR B  26      40.904  96.991  44.091  1.00105.86           O  
ANISOU  956  OG1 THR B  26     9651   7994  22575   -243  -6213   3082       O  
ATOM    957  CG2 THR B  26      42.368  95.325  43.150  1.00105.10           C  
ANISOU  957  CG2 THR B  26    10088   8557  21287   -439  -6094   3475       C  
ATOM    958  N   LEU B  27      44.694  94.940  45.310  1.00 92.73           N  
ANISOU  958  N   LEU B  27     8479   7381  19372   -170  -5372   3034       N  
ATOM    959  CA  LEU B  27      45.913  94.186  45.034  1.00 89.42           C  
ANISOU  959  CA  LEU B  27     8380   7379  18215   -319  -5179   3131       C  
ATOM    960  C   LEU B  27      45.559  92.819  44.471  1.00 98.50           C  
ANISOU  960  C   LEU B  27     9670   8858  18898   -376  -5161   3222       C  
ATOM    961  O   LEU B  27      44.428  92.358  44.611  1.00112.17           O  
ANISOU  961  O   LEU B  27    11204  10523  20894   -243  -5215   3128       O  
ATOM    962  CB  LEU B  27      46.762  94.024  46.297  1.00 86.43           C  
ANISOU  962  CB  LEU B  27     7976   7217  17645   -212  -4685   2705       C  
ATOM    963  CG  LEU B  27      47.255  95.284  47.007  1.00 91.59           C  
ANISOU  963  CG  LEU B  27     8494   7606  18700   -152  -4622   2539       C  
ATOM    964  CD1 LEU B  27      48.086  94.910  48.229  1.00 84.70           C  
ANISOU  964  CD1 LEU B  27     7627   7011  17542    -53  -4135   2113       C  
ATOM    965  CD2 LEU B  27      48.049  96.172  46.061  1.00102.14           C  
ANISOU  965  CD2 LEU B  27    10037   8801  19970   -379  -4894   2914       C  
ATOM    966  N   LYS B  28      46.528  92.171  43.836  1.00 86.00           N  
ANISOU  966  N   LYS B  28     8412   7626  16639   -580  -5075   3384       N  
ATOM    967  CA  LYS B  28      46.318  90.822  43.333  1.00 85.64           C  
ANISOU  967  CA  LYS B  28     8507   7920  16111   -642  -5020   3439       C  
ATOM    968  C   LYS B  28      46.322  89.850  44.505  1.00 88.44           C  
ANISOU  968  C   LYS B  28     8768   8534  16301   -454  -4566   3006       C  
ATOM    969  O   LYS B  28      47.265  89.822  45.294  1.00112.42           O  
ANISOU  969  O   LYS B  28    11860  11733  19121   -416  -4239   2760       O  
ATOM    970  CB  LYS B  28      47.391  90.445  42.311  1.00100.18           C  
ANISOU  970  CB  LYS B  28    10712  10055  17298   -929  -5048   3708       C  
ATOM    971  CG  LYS B  28      47.034  89.237  41.450  1.00127.48           C  
ANISOU  971  CG  LYS B  28    14320  13790  20329  -1043  -5124   3865       C  
ATOM    972  CD  LYS B  28      48.052  89.026  40.337  1.00142.19           C  
ANISOU  972  CD  LYS B  28    16529  15902  21596  -1363  -5184   4141       C  
ATOM    973  CE  LYS B  28      47.571  87.989  39.334  1.00140.76           C  
ANISOU  973  CE  LYS B  28    16487  15939  21056  -1500  -5336   4339       C  
ATOM    974  NZ  LYS B  28      47.360  86.665  39.970  1.00126.98           N  
ANISOU  974  NZ  LYS B  28    14667  14484  19095  -1340  -5010   4026       N  
ATOM    975  N   THR B  29      45.266  89.050  44.614  1.00 94.26           N  
ANISOU  975  N   THR B  29     9372   9304  17138   -344  -4555   2914       N  
ATOM    976  CA  THR B  29      45.075  88.205  45.788  1.00107.71           C  
ANISOU  976  CA  THR B  29    10970  11190  18763   -165  -4143   2506       C  
ATOM    977  C   THR B  29      44.549  86.810  45.451  1.00 91.13           C  
ANISOU  977  C   THR B  29     8942   9353  16331   -181  -4080   2513       C  
ATOM    978  O   THR B  29      43.695  86.658  44.579  1.00 86.33           O  
ANISOU  978  O   THR B  29     8290   8650  15861   -235  -4386   2742       O  
ATOM    979  CB  THR B  29      44.100  88.867  46.772  1.00129.26           C  
ANISOU  979  CB  THR B  29    13345  13594  22175     48  -4092   2226       C  
ATOM    980  OG1 THR B  29      44.386  90.269  46.864  1.00142.19           O  
ANISOU  980  OG1 THR B  29    14884  14914  24226     53  -4252   2277       O  
ATOM    981  CG2 THR B  29      44.220  88.237  48.127  1.00125.31           C  
ANISOU  981  CG2 THR B  29    12791  13279  21541    194  -3620   1789       C  
ATOM    982  N   HIS B  30      45.039  85.796  46.161  1.00 95.21           N  
ANISOU  982  N   HIS B  30     9565  10184  16427   -131  -3698   2258       N  
ATOM    983  CA  HIS B  30      44.595  84.423  45.927  1.00 87.76           C  
ANISOU  983  CA  HIS B  30     8694   9490  15162   -143  -3604   2238       C  
ATOM    984  C   HIS B  30      43.850  83.830  47.119  1.00 92.00           C  
ANISOU  984  C   HIS B  30     9059  10031  15866     42  -3286   1868       C  
ATOM    985  O   HIS B  30      44.391  83.738  48.224  1.00 86.20           O  
ANISOU  985  O   HIS B  30     8350   9387  15014    134  -2955   1580       O  
ATOM    986  CB  HIS B  30      45.785  83.530  45.575  1.00 72.85           C  
ANISOU  986  CB  HIS B  30     7113   7985  12581   -275  -3451   2285       C  
ATOM    987  CG  HIS B  30      46.632  84.067  44.465  1.00 81.09           C  
ANISOU  987  CG  HIS B  30     8346   9060  13402   -491  -3694   2605       C  
ATOM    988  ND1 HIS B  30      47.948  84.439  44.642  1.00113.81           N  
ANISOU  988  ND1 HIS B  30    12638  13316  17288   -561  -3561   2560       N  
ATOM    989  CD2 HIS B  30      46.345  84.310  43.165  1.00 89.71           C  
ANISOU  989  CD2 HIS B  30     9512  10085  14490   -671  -4060   2969       C  
ATOM    990  CE1 HIS B  30      48.438  84.876  43.495  1.00105.98           C  
ANISOU  990  CE1 HIS B  30    11803  12328  16136   -787  -3809   2876       C  
ATOM    991  NE2 HIS B  30      47.485  84.807  42.582  1.00 95.10           N  
ANISOU  991  NE2 HIS B  30    10398  10844  14890   -863  -4119   3139       N  
ATOM    992  N   HIS B  31      42.607  83.424  46.877  1.00100.76           N  
ANISOU  992  N   HIS B  31    10001  11042  17240     81  -3392   1877       N  
ATOM    993  CA  HIS B  31      41.826  82.681  47.858  1.00 92.28           C  
ANISOU  993  CA  HIS B  31     8790  10003  16271    211  -3081   1545       C  
ATOM    994  C   HIS B  31      42.158  81.197  47.756  1.00 84.54           C  
ANISOU  994  C   HIS B  31     8044   9383  14696    154  -2877   1526       C  
ATOM    995  O   HIS B  31      41.963  80.583  46.708  1.00 94.66           O  
ANISOU  995  O   HIS B  31     9415  10778  15775     46  -3076   1760       O  
ATOM    996  CB  HIS B  31      40.326  82.895  47.643  1.00 78.01           C  
ANISOU  996  CB  HIS B  31     6671   7921  15050    274  -3278   1532       C  
ATOM    997  CG  HIS B  31      39.886  84.320  47.774  1.00 97.75           C  
ANISOU  997  CG  HIS B  31     8902  10029  18209    348  -3495   1522       C  
ATOM    998  ND1 HIS B  31      40.185  85.097  48.873  1.00101.09           N  
ANISOU  998  ND1 HIS B  31     9213  10323  18874    450  -3270   1248       N  
ATOM    999  CD2 HIS B  31      39.149  85.104  46.949  1.00113.34           C  
ANISOU  999  CD2 HIS B  31    10693  11696  20673    339  -3931   1745       C  
ATOM   1000  CE1 HIS B  31      39.662  86.300  48.715  1.00 97.28           C  
ANISOU 1000  CE1 HIS B  31     8478   9468  19016    501  -3546   1295       C  
ATOM   1001  NE2 HIS B  31      39.028  86.330  47.557  1.00 99.45           N  
ANISOU 1001  NE2 HIS B  31     8708   9620  19458    440  -3961   1602       N  
ATOM   1002  N   VAL B  32      42.660  80.623  48.843  1.00 86.13           N  
ANISOU 1002  N   VAL B  32     8350   9757  14621    224  -2493   1247       N  
ATOM   1003  CA  VAL B  32      43.041  79.215  48.854  1.00 93.56           C  
ANISOU 1003  CA  VAL B  32     9520  11016  15012    184  -2294   1209       C  
ATOM   1004  C   VAL B  32      42.396  78.475  50.028  1.00107.30           C  
ANISOU 1004  C   VAL B  32    11206  12781  16783    287  -1937    881       C  
ATOM   1005  O   VAL B  32      42.409  78.955  51.159  1.00116.26           O  
ANISOU 1005  O   VAL B  32    12264  13817  18092    380  -1714    621       O  
ATOM   1006  CB  VAL B  32      44.577  79.060  48.912  1.00 77.52           C  
ANISOU 1006  CB  VAL B  32     7762   9220  12471    135  -2199   1230       C  
ATOM   1007  CG1 VAL B  32      44.969  77.625  49.222  1.00 60.10           C  
ANISOU 1007  CG1 VAL B  32     5770   7304   9760    134  -1954   1115       C  
ATOM   1008  CG2 VAL B  32      45.204  79.524  47.601  1.00 71.71           C  
ANISOU 1008  CG2 VAL B  32     7124   8516  11608    -21  -2520   1564       C  
ATOM   1009  N   ASN B  33      41.819  77.310  49.746  1.00115.37           N  
ANISOU 1009  N   ASN B  33    12272  13932  17631    253  -1879    891       N  
ATOM   1010  CA  ASN B  33      41.185  76.491  50.776  1.00113.14           C  
ANISOU 1010  CA  ASN B  33    11972  13683  17335    314  -1534    602       C  
ATOM   1011  C   ASN B  33      41.805  75.099  50.855  1.00111.32           C  
ANISOU 1011  C   ASN B  33    12036  13747  16512    275  -1351    591       C  
ATOM   1012  O   ASN B  33      42.485  74.659  49.928  1.00105.28           O  
ANISOU 1012  O   ASN B  33    11436  13159  15407    193  -1517    809       O  
ATOM   1013  CB  ASN B  33      39.680  76.390  50.524  1.00 98.39           C  
ANISOU 1013  CB  ASN B  33     9829  11637  15919    320  -1601    563       C  
ATOM   1014  CG  ASN B  33      39.343  76.356  49.052  1.00 95.81           C  
ANISOU 1014  CG  ASN B  33     9451  11297  15654    235  -1996    884       C  
ATOM   1015  OD1 ASN B  33      40.163  75.956  48.227  1.00107.50           O  
ANISOU 1015  OD1 ASN B  33    11155  12979  16713    144  -2136   1113       O  
ATOM   1016  ND2 ASN B  33      38.135  76.787  48.711  1.00 99.54           N  
ANISOU 1016  ND2 ASN B  33     9628  11533  16660    258  -2183    889       N  
ATOM   1017  N   ASP B  34      41.573  74.416  51.973  1.00130.77           N  
ANISOU 1017  N   ASP B  34    14569  16256  18860    322  -1008    330       N  
ATOM   1018  CA  ASP B  34      42.229  73.142  52.262  1.00150.44           C  
ANISOU 1018  CA  ASP B  34    17359  18993  20807    303   -822    292       C  
ATOM   1019  C   ASP B  34      41.575  71.969  51.534  1.00163.30           C  
ANISOU 1019  C   ASP B  34    19010  20720  22317    232   -856    391       C  
ATOM   1020  O   ASP B  34      40.602  72.143  50.800  1.00171.74           O  
ANISOU 1020  O   ASP B  34    19862  21675  23718    197  -1030    486       O  
ATOM   1021  CB  ASP B  34      42.225  72.884  53.772  1.00154.93           C  
ANISOU 1021  CB  ASP B  34    18029  19557  21280    364   -455    -10       C  
ATOM   1022  CG  ASP B  34      43.349  71.965  54.217  1.00163.17           C  
ANISOU 1022  CG  ASP B  34    19416  20823  21757    373   -327    -39       C  
ATOM   1023  OD1 ASP B  34      43.785  71.112  53.414  1.00155.42           O  
ANISOU 1023  OD1 ASP B  34    18577  20007  20470    326   -444    125       O  
ATOM   1024  OD2 ASP B  34      43.795  72.095  55.377  1.00177.30           O  
ANISOU 1024  OD2 ASP B  34    21332  22616  23417    427   -118   -238       O  
ATOM   1025  N   VAL B  35      42.125  70.775  51.742  1.00175.68           N  
ANISOU 1025  N   VAL B  35    20839  22489  23424    215   -706    361       N  
ATOM   1026  CA  VAL B  35      41.579  69.553  51.167  1.00184.05           C  
ANISOU 1026  CA  VAL B  35    21944  23649  24338    148   -699    423       C  
ATOM   1027  C   VAL B  35      40.364  69.089  51.961  1.00194.88           C  
ANISOU 1027  C   VAL B  35    23217  24907  25923    155   -434    213       C  
ATOM   1028  O   VAL B  35      39.533  68.331  51.459  1.00195.62           O  
ANISOU 1028  O   VAL B  35    23240  25010  26078     98   -441    243       O  
ATOM   1029  CB  VAL B  35      42.622  68.418  51.139  1.00181.49           C  
ANISOU 1029  CB  VAL B  35    21930  23559  23470    131   -633    449       C  
ATOM   1030  CG1 VAL B  35      43.837  68.827  50.323  1.00183.21           C  
ANISOU 1030  CG1 VAL B  35    22230  23903  23479    102   -868    622       C  
ATOM   1031  CG2 VAL B  35      43.028  68.037  52.554  1.00175.58           C  
ANISOU 1031  CG2 VAL B  35    21385  22824  22503    201   -334    228       C  
ATOM   1032  N   GLY B  36      40.273  69.548  53.206  1.00190.26           N  
ANISOU 1032  N   GLY B  36    22627  24218  25446    210   -187    -15       N  
ATOM   1033  CA  GLY B  36      39.188  69.167  54.086  1.00186.81           C  
ANISOU 1033  CA  GLY B  36    22112  23675  25191    191    117   -254       C  
ATOM   1034  C   GLY B  36      39.181  67.683  54.392  1.00173.13           C  
ANISOU 1034  C   GLY B  36    20638  22080  23063    138    328   -295       C  
ATOM   1035  O   GLY B  36      40.228  67.037  54.429  1.00172.22           O  
ANISOU 1035  O   GLY B  36    20813  22129  22493    149    317   -218       O  
ATOM   1036  N   GLU B  37      37.987  67.149  54.619  1.00154.47           N  
ANISOU 1036  N   GLU B  37    18157  19634  20900     77    519   -430       N  
ATOM   1037  CA  GLU B  37      37.812  65.735  54.923  1.00126.53           C  
ANISOU 1037  CA  GLU B  37    14847  16190  17038      8    737   -476       C  
ATOM   1038  C   GLU B  37      36.971  65.057  53.846  1.00122.90           C  
ANISOU 1038  C   GLU B  37    14227  15741  16727    -56    608   -371       C  
ATOM   1039  O   GLU B  37      36.148  65.699  53.193  1.00117.98           O  
ANISOU 1039  O   GLU B  37    13278  15001  16549    -57    439   -348       O  
ATOM   1040  CB  GLU B  37      37.160  65.556  56.296  1.00105.14           C  
ANISOU 1040  CB  GLU B  37    12193  13384  14371    -44   1148   -764       C  
ATOM   1041  N   LEU B  38      37.185  63.759  53.664  1.00111.15           N  
ANISOU 1041  N   LEU B  38    12969  14384  14879   -107    669   -311       N  
ATOM   1042  CA  LEU B  38      36.438  62.993  52.676  1.00 93.53           C  
ANISOU 1042  CA  LEU B  38    10612  12181  12746   -175    565   -226       C  
ATOM   1043  C   LEU B  38      35.497  62.006  53.354  1.00 88.13           C  
ANISOU 1043  C   LEU B  38     9971  11440  12076   -264    906   -415       C  
ATOM   1044  O   LEU B  38      35.757  61.551  54.469  1.00 83.70           O  
ANISOU 1044  O   LEU B  38     9668  10878  11255   -286   1199   -544       O  
ATOM   1045  CB  LEU B  38      37.388  62.246  51.741  1.00 91.55           C  
ANISOU 1045  CB  LEU B  38    10555  12127  12103   -182    345    -10       C  
ATOM   1046  CG  LEU B  38      38.357  63.080  50.905  1.00 90.09           C  
ANISOU 1046  CG  LEU B  38    10347  12025  11857   -135     11    188       C  
ATOM   1047  CD1 LEU B  38      39.269  62.168  50.099  1.00 79.34           C  
ANISOU 1047  CD1 LEU B  38     9189  10869  10087   -166   -131    339       C  
ATOM   1048  CD2 LEU B  38      37.602  64.038  49.993  1.00 94.89           C  
ANISOU 1048  CD2 LEU B  38    10618  12530  12907   -147   -256    286       C  
ATOM   1049  N   ASN B  39      34.395  61.689  52.685  1.00 78.62           N  
ANISOU 1049  N   ASN B  39     8518  10179  11174   -326    864   -434       N  
ATOM   1050  CA  ASN B  39      33.483  60.673  53.187  1.00 95.90           C  
ANISOU 1050  CA  ASN B  39    10736  12319  13382   -431   1183   -607       C  
ATOM   1051  C   ASN B  39      32.759  59.980  52.045  1.00 94.45           C  
ANISOU 1051  C   ASN B  39    10376  12166  13343   -489   1021   -528       C  
ATOM   1052  O   ASN B  39      32.485  60.593  51.015  1.00 93.63           O  
ANISOU 1052  O   ASN B  39    10008  12049  13518   -457    695   -410       O  
ATOM   1053  CB  ASN B  39      32.480  61.283  54.162  1.00103.92           C  
ANISOU 1053  CB  ASN B  39    11547  13148  14788   -469   1478   -892       C  
ATOM   1054  CG  ASN B  39      32.214  60.384  55.354  1.00121.49           C  
ANISOU 1054  CG  ASN B  39    14027  15352  16780   -582   1928  -1089       C  
ATOM   1055  OD1 ASN B  39      32.132  59.161  55.218  1.00123.01           O  
ANISOU 1055  OD1 ASN B  39    14404  15609  16725   -660   2024  -1049       O  
ATOM   1056  ND2 ASN B  39      32.092  60.984  56.532  1.00125.12           N  
ANISOU 1056  ND2 ASN B  39    14514  15720  17307   -605   2207  -1303       N  
ATOM   1057  N   ILE B  40      32.455  58.700  52.229  1.00 86.03           N  
ANISOU 1057  N   ILE B  40     9469  11136  12081   -582   1238   -587       N  
ATOM   1058  CA  ILE B  40      31.837  57.917  51.170  1.00 80.89           C  
ANISOU 1058  CA  ILE B  40     8679  10531  11523   -644   1100   -523       C  
ATOM   1059  C   ILE B  40      30.755  56.994  51.726  1.00 88.81           C  
ANISOU 1059  C   ILE B  40     9656  11442  12645   -768   1457   -740       C  
ATOM   1060  O   ILE B  40      30.925  56.376  52.777  1.00 86.45           O  
ANISOU 1060  O   ILE B  40     9639  11123  12086   -827   1794   -846       O  
ATOM   1061  CB  ILE B  40      32.900  57.093  50.395  1.00 69.47           C  
ANISOU 1061  CB  ILE B  40     7489   9283   9623   -633    899   -304       C  
ATOM   1062  CG1 ILE B  40      32.275  56.393  49.187  1.00 69.34           C  
ANISOU 1062  CG1 ILE B  40     7303   9328   9715   -702    719   -238       C  
ATOM   1063  CG2 ILE B  40      33.602  56.094  51.309  1.00 58.13           C  
ANISOU 1063  CG2 ILE B  40     6458   7890   7737   -655   1166   -341       C  
ATOM   1064  CD1 ILE B  40      33.290  55.889  48.186  1.00 55.55           C  
ANISOU 1064  CD1 ILE B  40     5719   7781   7606   -695    452    -27       C  
ATOM   1065  N   SER B  41      29.631  56.923  51.023  1.00 96.09           N  
ANISOU 1065  N   SER B  41    10243  12301  13968   -816   1375   -807       N  
ATOM   1066  CA  SER B  41      28.537  56.053  51.429  1.00 91.01           C  
ANISOU 1066  CA  SER B  41     9529  11566  13482   -948   1704  -1027       C  
ATOM   1067  C   SER B  41      28.835  54.614  51.034  1.00 85.59           C  
ANISOU 1067  C   SER B  41     9095  11000  12424  -1019   1737   -929       C  
ATOM   1068  O   SER B  41      29.560  54.366  50.068  1.00 75.51           O  
ANISOU 1068  O   SER B  41     7896   9872  10923   -969   1425   -710       O  
ATOM   1069  CB  SER B  41      27.213  56.509  50.808  1.00100.17           C  
ANISOU 1069  CB  SER B  41    10208  12605  15248   -966   1585  -1160       C  
ATOM   1070  OG  SER B  41      27.197  56.295  49.407  1.00 99.04           O  
ANISOU 1070  OG  SER B  41     9932  12561  15139   -942   1186   -968       O  
ATOM   1071  N   PRO B  42      28.286  53.659  51.797  1.00 94.60           N  
ANISOU 1071  N   PRO B  42    10371  12072  13500  -1149   2128  -1101       N  
ATOM   1072  CA  PRO B  42      28.406  52.230  51.495  1.00 96.29           C  
ANISOU 1072  CA  PRO B  42    10804  12358  13423  -1232   2195  -1042       C  
ATOM   1073  C   PRO B  42      27.886  51.874  50.102  1.00 94.79           C  
ANISOU 1073  C   PRO B  42    10338  12236  13442  -1242   1906   -976       C  
ATOM   1074  O   PRO B  42      28.478  51.032  49.423  1.00109.35           O  
ANISOU 1074  O   PRO B  42    12347  14210  14990  -1244   1756   -827       O  
ATOM   1075  CB  PRO B  42      27.551  51.577  52.580  1.00 84.92           C  
ANISOU 1075  CB  PRO B  42     9448  10776  12042  -1394   2682  -1287       C  
ATOM   1076  CG  PRO B  42      27.609  52.531  53.710  1.00 82.18           C  
ANISOU 1076  CG  PRO B  42     9139  10339  11747  -1382   2891  -1414       C  
ATOM   1077  CD  PRO B  42      27.632  53.891  53.096  1.00 89.79           C  
ANISOU 1077  CD  PRO B  42     9763  11309  13043  -1240   2555  -1365       C  
ATOM   1078  N   ASP B  43      26.796  52.510  49.685  1.00 80.34           N  
ANISOU 1078  N   ASP B  43     8085  10315  12124  -1251   1818  -1100       N  
ATOM   1079  CA  ASP B  43      26.215  52.234  48.375  1.00 90.20           C  
ANISOU 1079  CA  ASP B  43     9058  11620  13596  -1266   1520  -1049       C  
ATOM   1080  C   ASP B  43      27.102  52.729  47.240  1.00 88.57           C  
ANISOU 1080  C   ASP B  43     8859  11574  13219  -1164   1042   -770       C  
ATOM   1081  O   ASP B  43      27.121  52.144  46.158  1.00 76.37           O  
ANISOU 1081  O   ASP B  43     7274  10150  11593  -1196    808   -664       O  
ATOM   1082  CB  ASP B  43      24.832  52.866  48.253  1.00113.39           C  
ANISOU 1082  CB  ASP B  43    11529  14397  17157  -1288   1512  -1262       C  
ATOM   1083  CG  ASP B  43      23.913  52.474  49.385  1.00135.23           C  
ANISOU 1083  CG  ASP B  43    14255  17002  20124  -1414   2015  -1576       C  
ATOM   1084  OD1 ASP B  43      24.165  51.433  50.026  1.00142.16           O1+
ANISOU 1084  OD1 ASP B  43    15460  17898  20655  -1516   2344  -1609       O1+
ATOM   1085  OD2 ASP B  43      22.938  53.213  49.634  1.00142.55           O  
ANISOU 1085  OD2 ASP B  43    14823  17773  21565  -1419   2082  -1798       O  
ATOM   1086  N   GLU B  44      27.826  53.817  47.484  1.00 89.34           N  
ANISOU 1086  N   GLU B  44     9008  11676  13264  -1057    909   -664       N  
ATOM   1087  CA  GLU B  44      28.801  54.287  46.514  1.00 91.18           C  
ANISOU 1087  CA  GLU B  44     9302  12064  13278   -984    501   -400       C  
ATOM   1088  C   GLU B  44      29.941  53.285  46.421  1.00 82.56           C  
ANISOU 1088  C   GLU B  44     8586  11144  11640  -1001    540   -278       C  
ATOM   1089  O   GLU B  44      30.464  53.039  45.339  1.00 82.37           O  
ANISOU 1089  O   GLU B  44     8589  11282  11426  -1012    254   -115       O  
ATOM   1090  CB  GLU B  44      29.334  55.672  46.880  1.00100.70           C  
ANISOU 1090  CB  GLU B  44    10486  13217  14558   -875    382   -330       C  
ATOM   1091  CG  GLU B  44      28.432  56.827  46.480  1.00119.09           C  
ANISOU 1091  CG  GLU B  44    12414  15403  17433   -834    149   -363       C  
ATOM   1092  CD  GLU B  44      29.079  58.176  46.731  1.00132.65           C  
ANISOU 1092  CD  GLU B  44    14129  17072  19198   -727     -4   -266       C  
ATOM   1093  OE1 GLU B  44      30.265  58.200  47.122  1.00119.01           O  
ANISOU 1093  OE1 GLU B  44    12707  15448  17063   -689     53   -166       O  
ATOM   1094  OE2 GLU B  44      28.406  59.209  46.535  1.00152.98           O1+
ANISOU 1094  OE2 GLU B  44    16389  19496  22240   -679   -191   -299       O1+
ATOM   1095  N   ILE B  45      30.316  52.703  47.558  1.00 78.77           N  
ANISOU 1095  N   ILE B  45     8393  10622  10914  -1012    887   -369       N  
ATOM   1096  CA  ILE B  45      31.353  51.676  47.580  1.00 72.35           C  
ANISOU 1096  CA  ILE B  45     7933   9932   9624  -1019    930   -281       C  
ATOM   1097  C   ILE B  45      30.931  50.456  46.764  1.00 65.70           C  
ANISOU 1097  C   ILE B  45     7055   9158   8751  -1116    905   -294       C  
ATOM   1098  O   ILE B  45      31.666  50.005  45.873  1.00 67.43           O  
ANISOU 1098  O   ILE B  45     7358   9541   8721  -1115    684   -166       O  
ATOM   1099  CB  ILE B  45      31.695  51.228  49.024  1.00 72.88           C  
ANISOU 1099  CB  ILE B  45     8328   9904   9457  -1024   1301   -379       C  
ATOM   1100  CG1 ILE B  45      32.228  52.402  49.852  1.00 71.22           C  
ANISOU 1100  CG1 ILE B  45     8181   9647   9234   -930   1325   -374       C  
ATOM   1101  CG2 ILE B  45      32.708  50.103  48.999  1.00 68.54           C  
ANISOU 1101  CG2 ILE B  45     8125   9452   8464  -1022   1306   -293       C  
ATOM   1102  CD1 ILE B  45      32.560  52.050  51.296  1.00 57.04           C  
ANISOU 1102  CD1 ILE B  45     6722   7761   7189   -946   1669   -469       C  
ATOM   1103  N   VAL B  46      29.742  49.932  47.047  1.00 64.75           N  
ANISOU 1103  N   VAL B  46     6793   8914   8896  -1210   1138   -470       N  
ATOM   1104  CA  VAL B  46      29.280  48.756  46.323  1.00 69.26           C  
ANISOU 1104  CA  VAL B  46     7317   9535   9462  -1309   1135   -506       C  
ATOM   1105  C   VAL B  46      29.092  49.098  44.845  1.00 68.33           C  
ANISOU 1105  C   VAL B  46     6926   9550   9487  -1309    726   -399       C  
ATOM   1106  O   VAL B  46      29.288  48.241  43.992  1.00 83.94           O  
ANISOU 1106  O   VAL B  46     8937  11655  11302  -1365    605   -353       O  
ATOM   1107  CB  VAL B  46      27.970  48.162  46.925  1.00 65.22           C  
ANISOU 1107  CB  VAL B  46     6684   8854   9243  -1427   1484   -738       C  
ATOM   1108  CG1 VAL B  46      26.790  49.078  46.697  1.00 76.80           C  
ANISOU 1108  CG1 VAL B  46     7726  10222  11234  -1431   1411   -860       C  
ATOM   1109  CG2 VAL B  46      27.690  46.781  46.346  1.00 71.17           C  
ANISOU 1109  CG2 VAL B  46     7472   9654   9917  -1532   1529   -776       C  
ATOM   1110  N   SER B  47      28.754  50.349  44.536  1.00 72.43           N  
ANISOU 1110  N   SER B  47     7190  10036  10293  -1252    500   -356       N  
ATOM   1111  CA  SER B  47      28.605  50.748  43.138  1.00 81.60           C  
ANISOU 1111  CA  SER B  47     8128  11314  11562  -1263     77   -225       C  
ATOM   1112  C   SER B  47      29.966  50.762  42.436  1.00 69.56           C  
ANISOU 1112  C   SER B  47     6826   9999   9603  -1242   -167    -12       C  
ATOM   1113  O   SER B  47      30.074  50.368  41.275  1.00 67.70           O  
ANISOU 1113  O   SER B  47     6547   9922   9256  -1311   -412     72       O  
ATOM   1114  CB  SER B  47      27.916  52.114  43.024  1.00104.35           C  
ANISOU 1114  CB  SER B  47    10697  14074  14878  -1204   -128   -219       C  
ATOM   1115  OG  SER B  47      28.724  53.159  43.535  1.00124.76           O  
ANISOU 1115  OG  SER B  47    13396  16639  17371  -1104   -170   -118       O  
ATOM   1116  N   ILE B  48      31.000  51.204  43.150  1.00 77.53           N  
ANISOU 1116  N   ILE B  48     8070  11016  10372  -1158    -88     53       N  
ATOM   1117  CA  ILE B  48      32.370  51.174  42.634  1.00 70.04           C  
ANISOU 1117  CA  ILE B  48     7341  10257   9014  -1140   -264    212       C  
ATOM   1118  C   ILE B  48      32.809  49.745  42.342  1.00 67.61           C  
ANISOU 1118  C   ILE B  48     7217  10065   8407  -1207   -169    171       C  
ATOM   1119  O   ILE B  48      33.419  49.471  41.307  1.00 53.53           O  
ANISOU 1119  O   ILE B  48     5464   8470   6407  -1260   -388    260       O  
ATOM   1120  CB  ILE B  48      33.379  51.803  43.624  1.00 63.43           C  
ANISOU 1120  CB  ILE B  48     6725   9384   7992  -1032   -154    246       C  
ATOM   1121  CG1 ILE B  48      33.130  53.299  43.779  1.00 68.76           C  
ANISOU 1121  CG1 ILE B  48     7221   9962   8944   -965   -291    302       C  
ATOM   1122  CG2 ILE B  48      34.811  51.569  43.161  1.00 56.20           C  
ANISOU 1122  CG2 ILE B  48     6036   8657   6659  -1021   -289    360       C  
ATOM   1123  CD1 ILE B  48      33.879  53.911  44.941  1.00 76.68           C  
ANISOU 1123  CD1 ILE B  48     8408  10894   9834   -863   -126    283       C  
ATOM   1124  N   ARG B  49      32.498  48.834  43.259  1.00 73.59           N  
ANISOU 1124  N   ARG B  49     8103  10704   9154  -1216    162     29       N  
ATOM   1125  CA  ARG B  49      32.869  47.436  43.059  1.00 68.96           C  
ANISOU 1125  CA  ARG B  49     7692  10188   8321  -1273    259    -19       C  
ATOM   1126  C   ARG B  49      32.079  46.803  41.913  1.00 73.74           C  
ANISOU 1126  C   ARG B  49     8079  10876   9063  -1389    128    -58       C  
ATOM   1127  O   ARG B  49      32.614  45.992  41.152  1.00 64.47           O  
ANISOU 1127  O   ARG B  49     6979   9850   7666  -1444     33    -46       O  
ATOM   1128  CB  ARG B  49      32.664  46.632  44.344  1.00 66.02           C  
ANISOU 1128  CB  ARG B  49     7531   9642   7913  -1272    637   -145       C  
ATOM   1129  CG  ARG B  49      33.122  45.186  44.234  1.00 70.98           C  
ANISOU 1129  CG  ARG B  49     8369  10304   8296  -1318    729   -186       C  
ATOM   1130  CD  ARG B  49      33.010  44.448  45.555  1.00 68.44           C  
ANISOU 1130  CD  ARG B  49     8311   9791   7901  -1324   1079   -274       C  
ATOM   1131  NE  ARG B  49      31.642  44.430  46.058  1.00 75.02           N  
ANISOU 1131  NE  ARG B  49     8994  10464   9047  -1411   1326   -403       N  
ATOM   1132  CZ  ARG B  49      30.672  43.688  45.540  1.00 76.55           C  
ANISOU 1132  CZ  ARG B  49     9011  10634   9440  -1524   1390   -506       C  
ATOM   1133  NH1 ARG B  49      30.928  42.910  44.496  1.00 75.13           N1+
ANISOU 1133  NH1 ARG B  49     8792  10587   9165  -1562   1217   -486       N1+
ATOM   1134  NH2 ARG B  49      29.451  43.729  46.060  1.00 78.62           N  
ANISOU 1134  NH2 ARG B  49     9122  10743  10007  -1607   1633   -650       N  
ATOM   1135  N   GLU B  50      30.810  47.184  41.793  1.00 83.68           N  
ANISOU 1135  N   GLU B  50     9056  12036  10702  -1427    118   -124       N  
ATOM   1136  CA  GLU B  50      29.924  46.638  40.768  1.00 79.98           C  
ANISOU 1136  CA  GLU B  50     8354  11625  10409  -1535    -14   -181       C  
ATOM   1137  C   GLU B  50      30.239  47.172  39.373  1.00 83.44           C  
ANISOU 1137  C   GLU B  50     8672  12265  10767  -1572   -433    -28       C  
ATOM   1138  O   GLU B  50      29.920  46.528  38.373  1.00 84.18           O  
ANISOU 1138  O   GLU B  50     8663  12477  10846  -1675   -574    -51       O  
ATOM   1139  CB  GLU B  50      28.461  46.935  41.112  1.00 93.18           C  
ANISOU 1139  CB  GLU B  50     9739  13113  12551  -1557     94   -322       C  
ATOM   1140  CG  GLU B  50      27.876  46.027  42.184  1.00116.03           C  
ANISOU 1140  CG  GLU B  50    12719  15835  15531  -1602    527   -516       C  
ATOM   1141  CD  GLU B  50      26.462  46.416  42.583  1.00128.61           C  
ANISOU 1141  CD  GLU B  50    14009  17244  17613  -1633    663   -692       C  
ATOM   1142  OE1 GLU B  50      25.982  47.477  42.131  1.00128.79           O  
ANISOU 1142  OE1 GLU B  50    13756  17250  17929  -1590    407   -659       O  
ATOM   1143  OE2 GLU B  50      25.833  45.657  43.353  1.00124.07           O1+
ANISOU 1143  OE2 GLU B  50    13471  16531  17140  -1708   1026   -871       O1+
ATOM   1144  N   GLN B  51      30.857  48.349  39.302  1.00 87.87           N  
ANISOU 1144  N   GLN B  51     9256  12863  11267  -1505   -630    127       N  
ATOM   1145  CA  GLN B  51      31.177  48.937  38.004  1.00 94.82           C  
ANISOU 1145  CA  GLN B  51    10056  13924  12047  -1565  -1027    293       C  
ATOM   1146  C   GLN B  51      32.413  48.286  37.383  1.00 90.81           C  
ANISOU 1146  C   GLN B  51     9769  13643  11090  -1627  -1079    343       C  
ATOM   1147  O   GLN B  51      32.609  48.348  36.170  1.00 97.42           O  
ANISOU 1147  O   GLN B  51    10559  14668  11788  -1737  -1357    432       O  
ATOM   1148  CB  GLN B  51      31.375  50.450  38.125  1.00100.40           C  
ANISOU 1148  CB  GLN B  51    10708  14572  12867  -1487  -1222    445       C  
ATOM   1149  CG  GLN B  51      32.794  50.892  38.417  1.00111.76           C  
ANISOU 1149  CG  GLN B  51    12399  16098  13968  -1431  -1214    553       C  
ATOM   1150  CD  GLN B  51      32.976  52.382  38.218  1.00139.10           C  
ANISOU 1150  CD  GLN B  51    15787  19528  17535  -1389  -1473    724       C  
ATOM   1151  OE1 GLN B  51      32.060  53.072  37.769  1.00151.71           O  
ANISOU 1151  OE1 GLN B  51    17151  21041  19453  -1403  -1699    779       O  
ATOM   1152  NE2 GLN B  51      34.158  52.888  38.549  1.00143.61           N  
ANISOU 1152  NE2 GLN B  51    16553  20154  17858  -1336  -1456    805       N  
ATOM   1153  N   PHE B  52      33.245  47.665  38.212  1.00 82.41           N  
ANISOU 1153  N   PHE B  52     8948  12560   9805  -1565   -819    275       N  
ATOM   1154  CA  PHE B  52      34.391  46.914  37.710  1.00 66.92           C  
ANISOU 1154  CA  PHE B  52     7171  10786   7469  -1615   -838    268       C  
ATOM   1155  C   PHE B  52      34.063  45.427  37.595  1.00 69.26           C  
ANISOU 1155  C   PHE B  52     7488  11087   7741  -1682   -670    107       C  
ATOM   1156  O   PHE B  52      34.912  44.626  37.205  1.00 66.21           O  
ANISOU 1156  O   PHE B  52     7232  10833   7092  -1724   -661     57       O  
ATOM   1157  CB  PHE B  52      35.611  47.121  38.606  1.00 59.36           C  
ANISOU 1157  CB  PHE B  52     6462   9801   6290  -1498   -708    286       C  
ATOM   1158  CG  PHE B  52      36.226  48.484  38.483  1.00 94.30           C  
ANISOU 1158  CG  PHE B  52    10890  14278  10664  -1458   -900    441       C  
ATOM   1159  CD1 PHE B  52      37.069  48.783  37.424  1.00107.96           C  
ANISOU 1159  CD1 PHE B  52    12641  16227  12152  -1549  -1133    531       C  
ATOM   1160  CD2 PHE B  52      35.966  49.466  39.425  1.00113.22           C  
ANISOU 1160  CD2 PHE B  52    13266  16500  13251  -1344   -835    482       C  
ATOM   1161  CE1 PHE B  52      37.641  50.037  37.305  1.00114.11           C  
ANISOU 1161  CE1 PHE B  52    13432  17041  12883  -1530  -1302    678       C  
ATOM   1162  CE2 PHE B  52      36.536  50.724  39.312  1.00120.43           C  
ANISOU 1162  CE2 PHE B  52    14178  17446  14135  -1309  -1012    621       C  
ATOM   1163  CZ  PHE B  52      37.374  51.009  38.250  1.00122.89           C  
ANISOU 1163  CZ  PHE B  52    14522  17967  14206  -1402  -1248    727       C  
ATOM   1164  N   ASN B  53      32.825  45.080  37.940  1.00 79.58           N  
ANISOU 1164  N   ASN B  53     8651  12238   9346  -1696   -533     11       N  
ATOM   1165  CA  ASN B  53      32.310  43.712  37.842  1.00 81.12           C  
ANISOU 1165  CA  ASN B  53     8834  12407   9580  -1773   -365   -147       C  
ATOM   1166  C   ASN B  53      33.196  42.679  38.541  1.00 86.38           C  
ANISOU 1166  C   ASN B  53     9781  13029  10010  -1729   -130   -223       C  
ATOM   1167  O   ASN B  53      33.474  41.611  37.991  1.00 79.15           O  
ANISOU 1167  O   ASN B  53     8906  12203   8965  -1801   -121   -311       O  
ATOM   1168  CB  ASN B  53      32.119  43.324  36.372  1.00 82.36           C  
ANISOU 1168  CB  ASN B  53     8837  12775   9682  -1917   -613   -157       C  
ATOM   1169  CG  ASN B  53      31.169  42.152  36.194  1.00 95.35           C  
ANISOU 1169  CG  ASN B  53    10367  14365  11498  -2005   -476   -328       C  
ATOM   1170  OD1 ASN B  53      30.430  41.792  37.111  1.00 98.73           O  
ANISOU 1170  OD1 ASN B  53    10784  14584  12147  -1972   -213   -428       O  
ATOM   1171  ND2 ASN B  53      31.184  41.551  35.009  1.00105.03           N  
ANISOU 1171  ND2 ASN B  53    11510  15783  12616  -2133   -642   -374       N  
HETATM 1172  N   MSE B  54      33.632  42.997  39.757  1.00 90.38           N  
ANISOU 1172  N   MSE B  54    10481  13388  10469  -1611     47   -196       N  
HETATM 1173  CA  MSE B  54      34.494  42.091  40.507  1.00 75.42           C  
ANISOU 1173  CA  MSE B  54     8877  11423   8358  -1555    233   -249       C  
HETATM 1174  C   MSE B  54      33.946  41.750  41.895  1.00 73.78           C  
ANISOU 1174  C   MSE B  54     8817  10957   8259  -1516    554   -308       C  
HETATM 1175  O   MSE B  54      33.172  42.502  42.490  1.00 60.32           O  
ANISOU 1175  O   MSE B  54     7021   9136   6764  -1502    651   -302       O  
HETATM 1176  CB  MSE B  54      35.905  42.679  40.630  1.00 72.07           C  
ANISOU 1176  CB  MSE B  54     8621  11093   7668  -1457    110   -159       C  
HETATM 1177  CG  MSE B  54      35.961  44.140  41.054  1.00 74.01           C  
ANISOU 1177  CG  MSE B  54     8829  11315   7976  -1377     37    -41       C  
HETATM 1178 SE   MSE B  54      37.789  44.793  41.248  1.00125.75          SE  
ANISOU 1178 SE   MSE B  54    15597  17981  14201  -1261    -96     42      SE  
HETATM 1179  CE  MSE B  54      38.372  44.668  39.394  1.00 78.57           C  
ANISOU 1179  CE  MSE B  54     9471  12324   8058  -1405   -396     55       C  
ATOM   1180  N   SER B  55      34.364  40.590  42.389  1.00 65.38           N  
ANISOU 1180  N   SER B  55     7988   9800   7053  -1512    716   -373       N  
ATOM   1181  CA  SER B  55      33.942  40.065  43.680  1.00 56.08           C  
ANISOU 1181  CA  SER B  55     7016   8377   5914  -1510   1028   -422       C  
ATOM   1182  C   SER B  55      34.548  40.840  44.842  1.00 72.07           C  
ANISOU 1182  C   SER B  55     9264  10308   7812  -1395   1100   -343       C  
ATOM   1183  O   SER B  55      35.544  41.548  44.675  1.00 72.82           O  
ANISOU 1183  O   SER B  55     9398  10521   7749  -1298    908   -259       O  
ATOM   1184  CB  SER B  55      34.333  38.594  43.790  1.00 69.09           C  
ANISOU 1184  CB  SER B  55     8876   9945   7429  -1538   1126   -489       C  
ATOM   1185  OG  SER B  55      35.742  38.445  43.712  1.00 52.77           O  
ANISOU 1185  OG  SER B  55     6994   7957   5102  -1437    967   -446       O  
ATOM   1186  N   ARG B  56      33.946  40.699  46.021  1.00 66.57           N  
ANISOU 1186  N   ARG B  56     8715   9402   7176  -1422   1387   -382       N  
ATOM   1187  CA  ARG B  56      34.487  41.324  47.222  1.00 66.99           C  
ANISOU 1187  CA  ARG B  56     9014   9356   7083  -1332   1483   -325       C  
ATOM   1188  C   ARG B  56      35.919  40.881  47.475  1.00 68.19           C  
ANISOU 1188  C   ARG B  56     9469   9525   6917  -1222   1363   -261       C  
ATOM   1189  O   ARG B  56      36.737  41.667  47.936  1.00 88.53           O  
ANISOU 1189  O   ARG B  56    12156  12128   9352  -1111   1275   -194       O  
ATOM   1190  CB  ARG B  56      33.623  41.007  48.443  1.00 74.16           C  
ANISOU 1190  CB  ARG B  56    10080  10036   8061  -1420   1843   -397       C  
ATOM   1191  CG  ARG B  56      32.432  41.937  48.622  1.00 87.33           C  
ANISOU 1191  CG  ARG B  56    11474  11665  10041  -1483   1979   -474       C  
ATOM   1192  CD  ARG B  56      31.552  41.473  49.768  1.00 93.90           C  
ANISOU 1192  CD  ARG B  56    12460  12280  10937  -1612   2377   -582       C  
ATOM   1193  NE  ARG B  56      30.278  42.183  49.810  1.00 98.25           N  
ANISOU 1193  NE  ARG B  56    12686  12786  11856  -1694   2525   -713       N  
ATOM   1194  CZ  ARG B  56      29.255  41.827  50.579  1.00107.58           C  
ANISOU 1194  CZ  ARG B  56    13890  13800  13187  -1846   2889   -861       C  
ATOM   1195  NH1 ARG B  56      29.358  40.765  51.366  1.00110.45           N1+
ANISOU 1195  NH1 ARG B  56    14615  14020  13329  -1944   3137   -866       N1+
ATOM   1196  NH2 ARG B  56      28.128  42.527  50.559  1.00115.79           N  
ANISOU 1196  NH2 ARG B  56    14589  14801  14605  -1909   3002  -1009       N  
ATOM   1197  N   GLY B  57      36.221  39.627  47.160  1.00 60.84           N  
ANISOU 1197  N   GLY B  57     8651   8566   5898  -1250   1349   -297       N  
ATOM   1198  CA  GLY B  57      37.551  39.095  47.384  1.00 62.65           C  
ANISOU 1198  CA  GLY B  57     9146   8783   5874  -1142   1221   -265       C  
ATOM   1199  C   GLY B  57      38.620  39.840  46.610  1.00 60.00           C  
ANISOU 1199  C   GLY B  57     8686   8667   5443  -1042    933   -230       C  
ATOM   1200  O   GLY B  57      39.583  40.337  47.194  1.00 59.98           O  
ANISOU 1200  O   GLY B  57     8854   8658   5276   -922    852   -181       O  
ATOM   1201  N   VAL B  58      38.445  39.918  45.294  1.00 59.65           N  
ANISOU 1201  N   VAL B  58     8349   8819   5495  -1105    781   -262       N  
ATOM   1202  CA  VAL B  58      39.403  40.586  44.416  1.00 72.25           C  
ANISOU 1202  CA  VAL B  58     9818  10642   6993  -1057    523   -238       C  
ATOM   1203  C   VAL B  58      39.540  42.065  44.760  1.00 65.15           C  
ANISOU 1203  C   VAL B  58     8869   9787   6098   -990    465   -141       C  
ATOM   1204  O   VAL B  58      40.655  42.601  44.871  1.00 55.52           O  
ANISOU 1204  O   VAL B  58     7733   8638   4724   -893    334   -110       O  
ATOM   1205  CB  VAL B  58      38.990  40.453  42.931  1.00 78.09           C  
ANISOU 1205  CB  VAL B  58    10260  11584   7825  -1181    387   -281       C  
ATOM   1206  CG1 VAL B  58      39.950  41.214  42.036  1.00 71.30           C  
ANISOU 1206  CG1 VAL B  58     9290  10962   6839  -1167    142   -250       C  
ATOM   1207  CG2 VAL B  58      38.928  38.991  42.524  1.00 89.18           C  
ANISOU 1207  CG2 VAL B  58    11694  12958   9233  -1247    435   -399       C  
ATOM   1208  N   PHE B  59      38.395  42.717  44.933  1.00 48.60           N  
ANISOU 1208  N   PHE B  59     6622   7638   4205  -1044    566   -112       N  
ATOM   1209  CA  PHE B  59      38.375  44.135  45.244  1.00 55.24           C  
ANISOU 1209  CA  PHE B  59     7385   8498   5107   -989    518    -34       C  
ATOM   1210  C   PHE B  59      39.142  44.391  46.531  1.00 53.54           C  
ANISOU 1210  C   PHE B  59     7456   8162   4727   -868    608    -15       C  
ATOM   1211  O   PHE B  59      40.032  45.242  46.573  1.00 48.39           O  
ANISOU 1211  O   PHE B  59     6825   7591   3972   -780    468     36       O  
ATOM   1212  CB  PHE B  59      36.938  44.647  45.356  1.00 59.02           C  
ANISOU 1212  CB  PHE B  59     7652   8892   5880  -1062    639    -46       C  
ATOM   1213  CG  PHE B  59      36.827  46.149  45.342  1.00 81.51           C  
ANISOU 1213  CG  PHE B  59    10337  11776   8857  -1017    529     28       C  
ATOM   1214  CD1 PHE B  59      37.584  46.904  44.463  1.00 71.26           C  
ANISOU 1214  CD1 PHE B  59     8939  10658   7479   -993    255    119       C  
ATOM   1215  CD2 PHE B  59      35.957  46.804  46.196  1.00 92.62           C  
ANISOU 1215  CD2 PHE B  59    11684  13030  10477  -1014    706     -6       C  
ATOM   1216  CE1 PHE B  59      37.483  48.279  44.442  1.00 61.90           C  
ANISOU 1216  CE1 PHE B  59     7611   9483   6424   -956    142    198       C  
ATOM   1217  CE2 PHE B  59      35.852  48.182  46.180  1.00 77.29           C  
ANISOU 1217  CE2 PHE B  59     9577  11100   8688   -966    594     51       C  
ATOM   1218  CZ  PHE B  59      36.616  48.918  45.300  1.00 66.39           C  
ANISOU 1218  CZ  PHE B  59     8111   9884   7229   -933    302    164       C  
ATOM   1219  N   ALA B  60      38.815  43.624  47.566  1.00 48.76           N  
ANISOU 1219  N   ALA B  60     7082   7362   4083   -877    837    -57       N  
ATOM   1220  CA  ALA B  60      39.486  43.738  48.852  1.00 48.76           C  
ANISOU 1220  CA  ALA B  60     7397   7233   3897   -781    922    -38       C  
ATOM   1221  C   ALA B  60      40.979  43.459  48.728  1.00 47.61           C  
ANISOU 1221  C   ALA B  60     7412   7157   3520   -663    715    -26       C  
ATOM   1222  O   ALA B  60      41.783  44.052  49.446  1.00 60.63           O  
ANISOU 1222  O   ALA B  60     9219   8785   5034   -555    666      1       O  
ATOM   1223  CB  ALA B  60      38.856  42.802  49.864  1.00 50.41           C  
ANISOU 1223  CB  ALA B  60     7856   7221   4075   -848   1193    -75       C  
ATOM   1224  N   ARG B  61      41.351  42.562  47.820  1.00 54.71           N  
ANISOU 1224  N   ARG B  61     8257   8140   4392   -687    595    -70       N  
ATOM   1225  CA  ARG B  61      42.764  42.282  47.592  1.00 55.73           C  
ANISOU 1225  CA  ARG B  61     8485   8341   4347   -584    396   -101       C  
ATOM   1226  C   ARG B  61      43.454  43.534  47.076  1.00 62.05           C  
ANISOU 1226  C   ARG B  61     9118   9332   5126   -535    219    -70       C  
ATOM   1227  O   ARG B  61      44.509  43.920  47.578  1.00 65.03           O  
ANISOU 1227  O   ARG B  61     9630   9708   5371   -417    125    -73       O  
ATOM   1228  CB  ARG B  61      42.955  41.118  46.616  1.00 54.88           C  
ANISOU 1228  CB  ARG B  61     8301   8299   4252   -640    317   -189       C  
ATOM   1229  CG  ARG B  61      42.728  39.748  47.242  1.00 85.81           C  
ANISOU 1229  CG  ARG B  61    12459  11997   8149   -649    443   -225       C  
ATOM   1230  CD  ARG B  61      43.604  39.552  48.473  1.00111.24           C  
ANISOU 1230  CD  ARG B  61    16031  15038  11196   -512    421   -199       C  
ATOM   1231  NE  ARG B  61      43.192  38.400  49.272  1.00125.45           N  
ANISOU 1231  NE  ARG B  61    18112  16586  12968   -543    566   -189       N  
ATOM   1232  CZ  ARG B  61      43.719  37.184  49.165  1.00134.26           C  
ANISOU 1232  CZ  ARG B  61    19360  17596  14058   -512    481   -248       C  
ATOM   1233  NH1 ARG B  61      43.279  36.198  49.937  1.00138.40           N1+
ANISOU 1233  NH1 ARG B  61    20162  17868  14556   -556    617   -214       N1+
ATOM   1234  NH2 ARG B  61      44.688  36.953  48.288  1.00131.02           N  
ANISOU 1234  NH2 ARG B  61    18804  17321  13658   -446    265   -350       N  
ATOM   1235  N   LEU B  62      42.839  44.178  46.088  1.00 70.96           N  
ANISOU 1235  N   LEU B  62     9960  10612   6390   -633    165    -37       N  
ATOM   1236  CA  LEU B  62      43.387  45.414  45.529  1.00 63.40           C  
ANISOU 1236  CA  LEU B  62     8845   9825   5421   -617     -3     15       C  
ATOM   1237  C   LEU B  62      43.457  46.545  46.560  1.00 57.00           C  
ANISOU 1237  C   LEU B  62     8115   8924   4620   -524     48     77       C  
ATOM   1238  O   LEU B  62      44.349  47.390  46.514  1.00 57.15           O  
ANISOU 1238  O   LEU B  62     8122   9029   4563   -460    -80     97       O  
ATOM   1239  CB  LEU B  62      42.557  45.852  44.325  1.00 58.09           C  
ANISOU 1239  CB  LEU B  62     7879   9296   4898   -754    -84     63       C  
ATOM   1240  CG  LEU B  62      42.623  44.860  43.166  1.00 60.37           C  
ANISOU 1240  CG  LEU B  62     8070   9721   5148   -861   -161    -12       C  
ATOM   1241  CD1 LEU B  62      41.709  45.280  42.025  1.00 56.73           C  
ANISOU 1241  CD1 LEU B  62     7341   9393   4823  -1005   -256     45       C  
ATOM   1242  CD2 LEU B  62      44.059  44.727  42.692  1.00 59.65           C  
ANISOU 1242  CD2 LEU B  62     8023   9775   4867   -831   -306    -83       C  
ATOM   1243  N   LEU B  63      42.520  46.543  47.500  1.00 52.88           N  
ANISOU 1243  N   LEU B  63     7673   8227   4192   -530    251     88       N  
ATOM   1244  CA  LEU B  63      42.477  47.556  48.547  1.00 50.88           C  
ANISOU 1244  CA  LEU B  63     7497   7878   3958   -459    335    117       C  
ATOM   1245  C   LEU B  63      43.308  47.122  49.745  1.00 67.65           C  
ANISOU 1245  C   LEU B  63     9962   9879   5865   -351    391     85       C  
ATOM   1246  O   LEU B  63      43.307  47.786  50.787  1.00 60.46           O  
ANISOU 1246  O   LEU B  63     9174   8873   4925   -299    487     90       O  
ATOM   1247  CB  LEU B  63      41.037  47.827  48.977  1.00 58.93           C  
ANISOU 1247  CB  LEU B  63     8417   8775   5200   -539    544    113       C  
ATOM   1248  CG  LEU B  63      40.125  48.392  47.889  1.00 81.56           C  
ANISOU 1248  CG  LEU B  63    10934  11733   8323   -630    459    147       C  
ATOM   1249  CD1 LEU B  63      38.716  48.604  48.424  1.00 84.19           C  
ANISOU 1249  CD1 LEU B  63    11157  11918   8913   -698    676     99       C  
ATOM   1250  CD2 LEU B  63      40.701  49.688  47.330  1.00 78.55           C  
ANISOU 1250  CD2 LEU B  63    10396  11479   7971   -588    240    226       C  
ATOM   1251  N   HIS B  64      43.990  45.991  49.589  1.00 65.63           N  
ANISOU 1251  N   HIS B  64     9855   9616   5467   -323    321     43       N  
ATOM   1252  CA  HIS B  64      44.877  45.461  50.617  1.00 65.49           C  
ANISOU 1252  CA  HIS B  64    10169   9470   5245   -212    308     17       C  
ATOM   1253  C   HIS B  64      44.135  45.261  51.936  1.00 58.88           C  
ANISOU 1253  C   HIS B  64     9585   8423   4365   -240    546     38       C  
ATOM   1254  O   HIS B  64      44.624  45.644  52.998  1.00 60.27           O  
ANISOU 1254  O   HIS B  64     9987   8514   4398   -160    561     46       O  
ATOM   1255  CB  HIS B  64      46.078  46.390  50.813  1.00 73.33           C  
ANISOU 1255  CB  HIS B  64    11177  10545   6138    -86    138      9       C  
ATOM   1256  CG  HIS B  64      47.251  45.733  51.470  1.00 89.71           C  
ANISOU 1256  CG  HIS B  64    13529  12535   8023     43     20    -42       C  
ATOM   1257  ND1 HIS B  64      47.307  45.490  52.826  1.00 85.53           N  
ANISOU 1257  ND1 HIS B  64    13333  11814   7351    101    101    -22       N  
ATOM   1258  CD2 HIS B  64      48.417  45.271  50.956  1.00100.30           C  
ANISOU 1258  CD2 HIS B  64    14860  13947   9303    122   -186   -122       C  
ATOM   1259  CE1 HIS B  64      48.454  44.905  53.119  1.00 96.82           C  
ANISOU 1259  CE1 HIS B  64    14952  13191   8646    224    -80    -72       C  
ATOM   1260  NE2 HIS B  64      49.146  44.761  52.003  1.00110.62           N  
ANISOU 1260  NE2 HIS B  64    16479  15092  10458    245   -251   -146       N  
ATOM   1261  N   THR B  65      42.948  44.665  51.855  1.00 61.55           N  
ANISOU 1261  N   THR B  65     9883   8683   4822   -370    738     35       N  
ATOM   1262  CA  THR B  65      42.129  44.394  53.033  1.00 56.12           C  
ANISOU 1262  CA  THR B  65     9426   7799   4098   -444   1008     36       C  
ATOM   1263  C   THR B  65      41.382  43.067  52.897  1.00 55.25           C  
ANISOU 1263  C   THR B  65     9392   7574   4025   -562   1150     19       C  
ATOM   1264  O   THR B  65      41.342  42.469  51.822  1.00 69.27           O  
ANISOU 1264  O   THR B  65    10987   9436   5896   -589   1048     -3       O  
ATOM   1265  CB  THR B  65      41.108  45.525  53.295  1.00 69.04           C  
ANISOU 1265  CB  THR B  65    10866   9442   5924   -516   1190     19       C  
ATOM   1266  OG1 THR B  65      40.401  45.257  54.513  1.00 66.87           O  
ANISOU 1266  OG1 THR B  65    10838   8984   5587   -608   1479    -10       O  
ATOM   1267  CG2 THR B  65      40.109  45.637  52.147  1.00 49.58           C  
ANISOU 1267  CG2 THR B  65     8022   7071   3745   -614   1199     -1       C  
ATOM   1268  N   SER B  66      40.811  42.600  54.000  1.00 57.90           N  
ANISOU 1268  N   SER B  66    10009   7716   4274   -646   1392     22       N  
ATOM   1269  CA  SER B  66      40.032  41.368  54.002  1.00 61.35           C  
ANISOU 1269  CA  SER B  66    10547   8016   4749   -780   1565      5       C  
ATOM   1270  C   SER B  66      38.647  41.591  53.414  1.00 65.41           C  
ANISOU 1270  C   SER B  66    10725   8574   5555   -925   1755    -61       C  
ATOM   1271  O   SER B  66      38.091  42.683  53.519  1.00 80.83           O  
ANISOU 1271  O   SER B  66    12476  10581   7654   -946   1843    -93       O  
ATOM   1272  CB  SER B  66      39.907  40.816  55.422  1.00 67.08           C  
ANISOU 1272  CB  SER B  66    11723   8510   5256   -849   1769     38       C  
ATOM   1273  OG  SER B  66      39.214  41.730  56.250  1.00 70.55           O  
ANISOU 1273  OG  SER B  66    12168   8921   5715   -930   2012      4       O  
ATOM   1274  N   SER B  67      38.097  40.549  52.800  1.00 68.66           N  
ANISOU 1274  N   SER B  67    11067   8949   6071  -1019   1807    -94       N  
ATOM   1275  CA  SER B  67      36.748  40.597  52.248  1.00 65.88           C  
ANISOU 1275  CA  SER B  67    10403   8619   6009  -1162   1980   -174       C  
ATOM   1276  C   SER B  67      35.717  40.979  53.309  1.00 77.89           C  
ANISOU 1276  C   SER B  67    11994  10000   7600  -1292   2324   -234       C  
ATOM   1277  O   SER B  67      34.780  41.726  53.037  1.00 66.70           O  
ANISOU 1277  O   SER B  67    10258   8632   6453  -1353   2424   -313       O  
ATOM   1278  CB  SER B  67      36.381  39.247  51.635  1.00 56.42           C  
ANISOU 1278  CB  SER B  67     9196   7368   4875  -1253   2010   -211       C  
ATOM   1279  OG  SER B  67      37.515  38.631  51.054  1.00 67.66           O  
ANISOU 1279  OG  SER B  67    10695   8853   6159  -1141   1742   -174       O  
ATOM   1280  N   ARG B  68      35.903  40.460  54.518  1.00 74.73           N  
ANISOU 1280  N   ARG B  68    12016   9419   6960  -1341   2499   -204       N  
ATOM   1281  CA  ARG B  68      34.984  40.710  55.621  1.00 70.58           C  
ANISOU 1281  CA  ARG B  68    11615   8755   6448  -1499   2865   -278       C  
ATOM   1282  C   ARG B  68      34.963  42.182  56.017  1.00 76.10           C  
ANISOU 1282  C   ARG B  68    12164   9535   7214  -1443   2885   -319       C  
ATOM   1283  O   ARG B  68      33.914  42.727  56.367  1.00 62.30           O  
ANISOU 1283  O   ARG B  68    10248   7748   5674  -1566   3151   -443       O  
ATOM   1284  CB  ARG B  68      35.363  39.844  56.824  1.00 63.16           C  
ANISOU 1284  CB  ARG B  68    11220   7612   5168  -1568   3002   -208       C  
ATOM   1285  CG  ARG B  68      34.675  40.230  58.123  1.00 65.55           C  
ANISOU 1285  CG  ARG B  68    11731   7790   5386  -1736   3370   -276       C  
ATOM   1286  CD  ARG B  68      33.170  40.022  58.058  1.00 67.50           C  
ANISOU 1286  CD  ARG B  68    11759   7970   5916  -1961   3733   -433       C  
ATOM   1287  NE  ARG B  68      32.555  40.178  59.373  1.00 70.28           N  
ANISOU 1287  NE  ARG B  68    12373   8184   6145  -2163   4127   -515       N  
ATOM   1288  CZ  ARG B  68      31.244  40.189  59.588  1.00 74.91           C  
ANISOU 1288  CZ  ARG B  68    12792   8704   6968  -2383   4507   -695       C  
ATOM   1289  NH1 ARG B  68      30.773  40.338  60.818  1.00 75.16           N  
ANISOU 1289  NH1 ARG B  68    13066   8615   6876  -2569   4842   -783       N  
ATOM   1290  NH2 ARG B  68      30.404  40.054  58.572  1.00 78.68           N  
ANISOU 1290  NH2 ARG B  68    12832   9232   7829  -2411   4516   -801       N  
ATOM   1291  N   THR B  69      36.127  42.819  55.961  1.00 69.89           N  
ANISOU 1291  N   THR B  69    11427   8854   6275  -1259   2606   -232       N  
ATOM   1292  CA  THR B  69      36.235  44.237  56.275  1.00 69.59           C  
ANISOU 1292  CA  THR B  69    11243   8894   6304  -1189   2588   -265       C  
ATOM   1293  C   THR B  69      35.460  45.052  55.245  1.00 66.38           C  
ANISOU 1293  C   THR B  69    10323   8606   6290  -1188   2530   -332       C  
ATOM   1294  O   THR B  69      34.644  45.910  55.595  1.00 58.81           O  
ANISOU 1294  O   THR B  69     9172   7620   5552  -1250   2710   -440       O  
ATOM   1295  CB  THR B  69      37.701  44.695  56.313  1.00 76.22           C  
ANISOU 1295  CB  THR B  69    12221   9825   6912   -991   2278   -163       C  
ATOM   1296  OG1 THR B  69      38.368  44.080  57.424  1.00 70.55           O  
ANISOU 1296  OG1 THR B  69    11988   8974   5842   -987   2321   -109       O  
ATOM   1297  CG2 THR B  69      37.785  46.203  56.456  1.00 73.49           C  
ANISOU 1297  CG2 THR B  69    11668   9570   6685   -917   2239   -200       C  
ATOM   1298  N   LEU B  70      35.713  44.756  53.975  1.00 56.23           N  
ANISOU 1298  N   LEU B  70     8823   7446   5095  -1126   2270   -276       N  
ATOM   1299  CA  LEU B  70      34.986  45.360  52.865  1.00 55.80           C  
ANISOU 1299  CA  LEU B  70     8311   7501   5388  -1138   2163   -314       C  
ATOM   1300  C   LEU B  70      33.475  45.176  52.996  1.00 57.95           C  
ANISOU 1300  C   LEU B  70     8392   7665   5960  -1305   2454   -457       C  
ATOM   1301  O   LEU B  70      32.700  46.079  52.690  1.00 64.25           O  
ANISOU 1301  O   LEU B  70     8845   8484   7083  -1319   2458   -533       O  
ATOM   1302  CB  LEU B  70      35.469  44.767  51.547  1.00 54.31           C  
ANISOU 1302  CB  LEU B  70     8000   7453   5182  -1092   1879   -241       C  
ATOM   1303  CG  LEU B  70      34.816  45.342  50.297  1.00 69.53           C  
ANISOU 1303  CG  LEU B  70     9490   9509   7421  -1110   1711   -253       C  
ATOM   1304  CD1 LEU B  70      34.953  46.862  50.288  1.00 62.08           C  
ANISOU 1304  CD1 LEU B  70     8359   8626   6604  -1025   1583   -222       C  
ATOM   1305  CD2 LEU B  70      35.438  44.725  49.054  1.00 59.40           C  
ANISOU 1305  CD2 LEU B  70     8140   8382   6046  -1084   1440   -188       C  
ATOM   1306  N   GLU B  71      33.065  43.996  53.445  1.00 66.47           N  
ANISOU 1306  N   GLU B  71     9692   8617   6948  -1433   2690   -501       N  
ATOM   1307  CA  GLU B  71      31.659  43.719  53.682  1.00 61.74           C  
ANISOU 1307  CA  GLU B  71     8943   7900   6616  -1615   3011   -662       C  
ATOM   1308  C   GLU B  71      31.132  44.633  54.778  1.00 72.66           C  
ANISOU 1308  C   GLU B  71    10328   9191   8087  -1678   3286   -784       C  
ATOM   1309  O   GLU B  71      30.052  45.212  54.655  1.00 75.62           O  
ANISOU 1309  O   GLU B  71    10359   9540   8835  -1750   3419   -939       O  
ATOM   1310  CB  GLU B  71      31.456  42.254  54.067  1.00 91.79           C  
ANISOU 1310  CB  GLU B  71    13051  11568  10256  -1754   3225   -671       C  
ATOM   1311  CG  GLU B  71      30.010  41.890  54.373  1.00110.95           C  
ANISOU 1311  CG  GLU B  71    15345  13863  12947  -1969   3599   -857       C  
ATOM   1312  CD  GLU B  71      29.869  40.502  54.970  1.00114.61           C  
ANISOU 1312  CD  GLU B  71    16182  14161  13204  -2128   3849   -853       C  
ATOM   1313  OE1 GLU B  71      28.914  40.285  55.748  1.00114.73           O  
ANISOU 1313  OE1 GLU B  71    16258  14031  13302  -2332   4241   -997       O  
ATOM   1314  OE2 GLU B  71      30.711  39.632  54.662  1.00113.45           O  
ANISOU 1314  OE2 GLU B  71    16265  14018  12823  -2058   3656   -716       O  
ATOM   1315  N   ASN B  72      31.907  44.756  55.851  1.00 66.90           N  
ANISOU 1315  N   ASN B  72     9983   8413   7025  -1650   3360   -728       N  
ATOM   1316  CA  ASN B  72      31.544  45.618  56.965  1.00 70.71           C  
ANISOU 1316  CA  ASN B  72    10511   8820   7534  -1716   3625   -851       C  
ATOM   1317  C   ASN B  72      31.372  47.065  56.518  1.00 79.73           C  
ANISOU 1317  C   ASN B  72    11238  10054   9000  -1604   3468   -907       C  
ATOM   1318  O   ASN B  72      30.522  47.786  57.040  1.00 82.58           O  
ANISOU 1318  O   ASN B  72    11412  10347   9618  -1689   3707  -1089       O  
ATOM   1319  CB  ASN B  72      32.593  45.526  58.075  1.00 86.67           C  
ANISOU 1319  CB  ASN B  72    13030  10799   9100  -1681   3647   -754       C  
ATOM   1320  CG  ASN B  72      32.562  44.189  58.801  1.00 87.25           C  
ANISOU 1320  CG  ASN B  72    13554  10725   8871  -1836   3866   -719       C  
ATOM   1321  OD1 ASN B  72      31.543  43.499  58.812  1.00 94.15           O  
ANISOU 1321  OD1 ASN B  72    14382  11502   9890  -2023   4137   -822       O  
ATOM   1322  ND2 ASN B  72      33.680  43.824  59.417  1.00 79.97           N  
ANISOU 1322  ND2 ASN B  72    13075   9773   7538  -1763   3740   -574       N  
ATOM   1323  N   TRP B  73      32.174  47.481  55.542  1.00 77.46           N  
ANISOU 1323  N   TRP B  73    10806   9912   8713  -1423   3069   -760       N  
ATOM   1324  CA  TRP B  73      32.030  48.811  54.960  1.00 60.99           C  
ANISOU 1324  CA  TRP B  73     8329   7903   6941  -1320   2870   -778       C  
ATOM   1325  C   TRP B  73      30.745  48.915  54.145  1.00 62.20           C  
ANISOU 1325  C   TRP B  73     8037   8036   7561  -1393   2884   -895       C  
ATOM   1326  O   TRP B  73      29.936  49.821  54.351  1.00 85.22           O  
ANISOU 1326  O   TRP B  73    10664  10886  10830  -1418   2987  -1045       O  
ATOM   1327  CB  TRP B  73      33.230  49.152  54.075  1.00 58.27           C  
ANISOU 1327  CB  TRP B  73     7970   7720   6448  -1141   2449   -583       C  
ATOM   1328  CG  TRP B  73      34.529  49.241  54.809  1.00 57.11           C  
ANISOU 1328  CG  TRP B  73     8193   7598   5907  -1041   2387   -490       C  
ATOM   1329  CD1 TRP B  73      34.703  49.310  56.157  1.00 60.95           C  
ANISOU 1329  CD1 TRP B  73     8988   7985   6185  -1080   2629   -552       C  
ATOM   1330  CD2 TRP B  73      35.840  49.261  54.232  1.00 54.81           C  
ANISOU 1330  CD2 TRP B  73     8000   7440   5386   -895   2055   -333       C  
ATOM   1331  NE1 TRP B  73      36.042  49.377  56.459  1.00 69.86           N  
ANISOU 1331  NE1 TRP B  73    10397   9170   6975   -952   2443   -436       N  
ATOM   1332  CE2 TRP B  73      36.761  49.346  55.294  1.00 60.68           C  
ANISOU 1332  CE2 TRP B  73     9099   8147   5808   -834   2098   -311       C  
ATOM   1333  CE3 TRP B  73      36.325  49.218  52.920  1.00 70.93           C  
ANISOU 1333  CE3 TRP B  73     9862   9630   7456   -824   1732   -224       C  
ATOM   1334  CZ2 TRP B  73      38.139  49.391  55.087  1.00 72.16           C  
ANISOU 1334  CZ2 TRP B  73    10707   9701   7010   -690   1825   -199       C  
ATOM   1335  CZ3 TRP B  73      37.694  49.262  52.716  1.00 63.42           C  
ANISOU 1335  CZ3 TRP B  73     9072   8786   6240   -700   1491   -118       C  
ATOM   1336  CH2 TRP B  73      38.585  49.347  53.794  1.00 63.96           C  
ANISOU 1336  CH2 TRP B  73     9468   8806   6028   -627   1536   -113       C  
ATOM   1337  N   GLU B  74      30.563  47.973  53.223  1.00 71.51           N  
ANISOU 1337  N   GLU B  74     9154   9263   8753  -1426   2770   -840       N  
ATOM   1338  CA  GLU B  74      29.440  47.999  52.290  1.00 75.11           C  
ANISOU 1338  CA  GLU B  74     9187   9719   9632  -1482   2711   -932       C  
ATOM   1339  C   GLU B  74      28.082  47.840  52.972  1.00 90.02           C  
ANISOU 1339  C   GLU B  74    10937  11444  11822  -1653   3108  -1183       C  
ATOM   1340  O   GLU B  74      27.093  48.432  52.540  1.00 91.05           O  
ANISOU 1340  O   GLU B  74    10654  11538  12404  -1672   3081  -1318       O  
ATOM   1341  CB  GLU B  74      29.610  46.906  51.232  1.00 61.82           C  
ANISOU 1341  CB  GLU B  74     7513   8129   7846  -1497   2528   -834       C  
ATOM   1342  CG  GLU B  74      30.770  47.140  50.280  1.00 84.50           C  
ANISOU 1342  CG  GLU B  74    10407  11183  10514  -1353   2117   -629       C  
ATOM   1343  CD  GLU B  74      30.783  46.164  49.120  1.00 93.21           C  
ANISOU 1343  CD  GLU B  74    11444  12390  11581  -1387   1938   -575       C  
ATOM   1344  OE1 GLU B  74      29.789  45.429  48.938  1.00 99.29           O  
ANISOU 1344  OE1 GLU B  74    12088  13092  12544  -1509   2094   -695       O  
ATOM   1345  OE2 GLU B  74      31.793  46.134  48.387  1.00 91.91           O1+
ANISOU 1345  OE2 GLU B  74    11345  12378  11199  -1303   1652   -432       O1+
ATOM   1346  N   GLN B  75      28.032  47.037  54.029  1.00 87.00           N  
ANISOU 1346  N   GLN B  75    10901  10956  11197  -1787   3471  -1252       N  
ATOM   1347  CA  GLN B  75      26.781  46.808  54.740  1.00 91.79           C  
ANISOU 1347  CA  GLN B  75    11416  11410  12051  -1987   3900  -1508       C  
ATOM   1348  C   GLN B  75      26.535  47.900  55.780  1.00100.38           C  
ANISOU 1348  C   GLN B  75    12462  12422  13257  -2011   4127  -1669       C  
ATOM   1349  O   GLN B  75      25.516  47.896  56.470  1.00100.83           O  
ANISOU 1349  O   GLN B  75    12422  12354  13536  -2188   4514  -1921       O  
ATOM   1350  CB  GLN B  75      26.786  45.428  55.399  1.00 88.56           C  
ANISOU 1350  CB  GLN B  75    11419  10910  11321  -2155   4203  -1507       C  
ATOM   1351  N   GLY B  76      27.472  48.838  55.880  1.00 98.37           N  
ANISOU 1351  N   GLY B  76    12270  12244  12863  -1844   3897  -1542       N  
ATOM   1352  CA  GLY B  76      27.336  49.963  56.789  1.00100.93           C  
ANISOU 1352  CA  GLY B  76    12534  12509  13306  -1847   4069  -1693       C  
ATOM   1353  C   GLY B  76      27.702  49.646  58.228  1.00 97.50           C  
ANISOU 1353  C   GLY B  76    12572  12009  12467  -1971   4426  -1741       C  
ATOM   1354  O   GLY B  76      27.536  50.483  59.118  1.00 90.25           O  
ANISOU 1354  O   GLY B  76    11640  11038  11614  -2013   4636  -1902       O  
ATOM   1355  N   ARG B  77      28.208  48.439  58.456  1.00102.03           N  
ANISOU 1355  N   ARG B  77    13571  12578  12619  -2036   4483  -1602       N  
ATOM   1356  CA  ARG B  77      28.580  48.005  59.799  1.00103.20           C  
ANISOU 1356  CA  ARG B  77    14229  12651  12333  -2169   4787  -1612       C  
ATOM   1357  C   ARG B  77      29.894  48.622  60.277  1.00112.68           C  
ANISOU 1357  C   ARG B  77    15709  13925  13179  -2006   4575  -1456       C  
ATOM   1358  O   ARG B  77      30.240  48.513  61.453  1.00114.60           O  
ANISOU 1358  O   ARG B  77    16358  14113  13072  -2102   4793  -1474       O  
ATOM   1359  CB  ARG B  77      28.681  46.476  59.857  1.00 98.65           C  
ANISOU 1359  CB  ARG B  77    14022  12015  11447  -2288   4881  -1500       C  
ATOM   1360  CG  ARG B  77      27.339  45.760  59.831  1.00106.27           C  
ANISOU 1360  CG  ARG B  77    14831  12867  12678  -2524   5233  -1699       C  
ATOM   1361  CD  ARG B  77      27.489  44.275  60.135  1.00102.77           C  
ANISOU 1361  CD  ARG B  77    14833  12332  11882  -2669   5375  -1589       C  
ATOM   1362  NE  ARG B  77      28.135  43.549  59.046  1.00107.44           N  
ANISOU 1362  NE  ARG B  77    15424  12997  12401  -2511   4992  -1374       N  
ATOM   1363  CZ  ARG B  77      27.485  43.023  58.011  1.00115.10           C  
ANISOU 1363  CZ  ARG B  77    16077  13983  13671  -2527   4921  -1416       C  
ATOM   1364  NH1 ARG B  77      26.167  43.144  57.921  1.00125.52           N  
ANISOU 1364  NH1 ARG B  77    17046  15242  15403  -2683   5190  -1661       N  
ATOM   1365  NH2 ARG B  77      28.152  42.377  57.064  1.00101.32           N  
ANISOU 1365  NH2 ARG B  77    14354  12316  11828  -2393   4581  -1233       N  
ATOM   1366  N   SER B  78      30.623  49.267  59.369  1.00107.19           N  
ANISOU 1366  N   SER B  78    14808  13354  12566  -1774   4152  -1308       N  
ATOM   1367  CA  SER B  78      31.921  49.847  59.711  1.00 94.74           C  
ANISOU 1367  CA  SER B  78    13463  11854  10680  -1609   3924  -1166       C  
ATOM   1368  C   SER B  78      32.286  51.040  58.825  1.00 90.26           C  
ANISOU 1368  C   SER B  78    12516  11396  10383  -1407   3569  -1110       C  
ATOM   1369  O   SER B  78      31.809  51.162  57.697  1.00 76.10           O  
ANISOU 1369  O   SER B  78    10348   9645   8922  -1362   3384  -1092       O  
ATOM   1370  CB  SER B  78      33.014  48.778  59.622  1.00 83.92           C  
ANISOU 1370  CB  SER B  78    12506  10516   8863  -1542   3727   -942       C  
ATOM   1371  OG  SER B  78      34.279  49.299  59.987  1.00 80.53           O  
ANISOU 1371  OG  SER B  78    12299  10154   8146  -1384   3506   -828       O  
ATOM   1372  N   VAL B  79      33.126  51.924  59.355  1.00 94.80           N  
ANISOU 1372  N   VAL B  79    13201  12011  10809  -1297   3473  -1082       N  
ATOM   1373  CA  VAL B  79      33.629  53.066  58.598  1.00 87.22           C  
ANISOU 1373  CA  VAL B  79    11943  11145  10052  -1112   3133  -1007       C  
ATOM   1374  C   VAL B  79      35.117  52.910  58.289  1.00 69.30           C  
ANISOU 1374  C   VAL B  79     9920   8993   7419   -949   2800   -788       C  
ATOM   1375  O   VAL B  79      35.929  52.726  59.196  1.00 73.14           O  
ANISOU 1375  O   VAL B  79    10785   9472   7534   -931   2848   -761       O  
ATOM   1376  CB  VAL B  79      33.398  54.387  59.350  1.00 82.32           C  
ANISOU 1376  CB  VAL B  79    11172  10473   9633  -1106   3269  -1177       C  
ATOM   1377  CG1 VAL B  79      33.949  55.556  58.552  1.00 70.53           C  
ANISOU 1377  CG1 VAL B  79     9393   9058   8349   -921   2904  -1079       C  
ATOM   1378  CG2 VAL B  79      31.916  54.579  59.624  1.00 85.80           C  
ANISOU 1378  CG2 VAL B  79    11321  10791  10488  -1267   3600  -1435       C  
ATOM   1379  N   PRO B  80      35.478  52.971  57.001  1.00 60.71           N  
ANISOU 1379  N   PRO B  80     8616   8014   6437   -840   2458   -644       N  
ATOM   1380  CA  PRO B  80      36.875  52.816  56.585  1.00 72.79           C  
ANISOU 1380  CA  PRO B  80    10328   9664   7664   -698   2146   -468       C  
ATOM   1381  C   PRO B  80      37.754  53.969  57.068  1.00 71.99           C  
ANISOU 1381  C   PRO B  80    10265   9598   7489   -578   2035   -463       C  
ATOM   1382  O   PRO B  80      37.262  55.077  57.271  1.00 65.69           O  
ANISOU 1382  O   PRO B  80     9229   8759   6972   -577   2098   -560       O  
ATOM   1383  CB  PRO B  80      36.785  52.794  55.054  1.00 57.01           C  
ANISOU 1383  CB  PRO B  80     8019   7773   5870   -659   1859   -361       C  
ATOM   1384  CG  PRO B  80      35.534  53.533  54.741  1.00 55.25           C  
ANISOU 1384  CG  PRO B  80     7402   7487   6105   -718   1932   -464       C  
ATOM   1385  CD  PRO B  80      34.583  53.217  55.857  1.00 67.75           C  
ANISOU 1385  CD  PRO B  80     9075   8922   7746   -857   2340   -653       C  
ATOM   1386  N   ASN B  81      39.046  53.707  57.238  1.00 66.01           N  
ANISOU 1386  N   ASN B  81     9787   8908   6384   -475   1864   -365       N  
ATOM   1387  CA  ASN B  81      39.971  54.730  57.702  1.00 63.63           C  
ANISOU 1387  CA  ASN B  81     9537   8645   5993   -359   1749   -367       C  
ATOM   1388  C   ASN B  81      40.228  55.783  56.633  1.00 67.78           C  
ANISOU 1388  C   ASN B  81     9713   9267   6775   -270   1476   -296       C  
ATOM   1389  O   ASN B  81      39.677  55.716  55.535  1.00 63.72           O  
ANISOU 1389  O   ASN B  81     8930   8791   6490   -302   1364   -237       O  
ATOM   1390  CB  ASN B  81      41.295  54.101  58.136  1.00 71.05           C  
ANISOU 1390  CB  ASN B  81    10858   9625   6514   -270   1615   -296       C  
ATOM   1391  CG  ASN B  81      41.946  53.297  57.031  1.00 74.83           C  
ANISOU 1391  CG  ASN B  81    11324  10204   6904   -213   1355   -171       C  
ATOM   1392  OD1 ASN B  81      42.588  53.851  56.139  1.00 73.89           O  
ANISOU 1392  OD1 ASN B  81    11012  10203   6858   -128   1103   -106       O  
ATOM   1393  ND2 ASN B  81      41.781  51.981  57.083  1.00 82.70           N  
ANISOU 1393  ND2 ASN B  81    12529  11150   7744   -274   1426   -146       N  
ATOM   1394  N   GLY B  82      41.077  56.751  56.961  1.00 70.41           N  
ANISOU 1394  N   GLY B  82    10063   9633   7056   -169   1363   -299       N  
ATOM   1395  CA  GLY B  82      41.337  57.874  56.080  1.00 63.57           C  
ANISOU 1395  CA  GLY B  82     8894   8834   6427   -100   1124   -231       C  
ATOM   1396  C   GLY B  82      41.904  57.478  54.733  1.00 61.48           C  
ANISOU 1396  C   GLY B  82     8546   8706   6109    -75    839    -77       C  
ATOM   1397  O   GLY B  82      41.375  57.856  53.683  1.00 58.15           O  
ANISOU 1397  O   GLY B  82     7835   8313   5945   -111    703     -6       O  
ATOM   1398  N   GLN B  83      42.983  56.705  54.759  1.00 59.41           N  
ANISOU 1398  N   GLN B  83     8538   8522   5511    -21    741    -36       N  
ATOM   1399  CA  GLN B  83      43.649  56.302  53.532  1.00 65.59           C  
ANISOU 1399  CA  GLN B  83     9256   9447   6217     -8    491     73       C  
ATOM   1400  C   GLN B  83      42.741  55.391  52.721  1.00 68.17           C  
ANISOU 1400  C   GLN B  83     9474   9785   6643   -111    518    110       C  
ATOM   1401  O   GLN B  83      42.811  55.363  51.492  1.00 44.78           O  
ANISOU 1401  O   GLN B  83     6335   6935   3746   -146    327    197       O  
ATOM   1402  CB  GLN B  83      44.978  55.612  53.841  1.00 67.43           C  
ANISOU 1402  CB  GLN B  83     9774   9739   6107     77    396     63       C  
ATOM   1403  CG  GLN B  83      46.005  56.515  54.514  1.00 63.89           C  
ANISOU 1403  CG  GLN B  83     9414   9301   5561    185    325     20       C  
ATOM   1404  CD  GLN B  83      45.722  56.733  55.984  1.00 62.41           C  
ANISOU 1404  CD  GLN B  83     9424   8980   5307    202    541    -80       C  
ATOM   1405  OE1 GLN B  83      45.306  55.815  56.690  1.00 58.66           O  
ANISOU 1405  OE1 GLN B  83     9178   8418   4692    158    710   -115       O  
ATOM   1406  NE2 GLN B  83      45.937  57.956  56.454  1.00 73.67           N  
ANISOU 1406  NE2 GLN B  83    10771  10389   6831    249    544   -130       N  
ATOM   1407  N   ALA B  84      41.881  54.658  53.419  1.00 57.02           N  
ANISOU 1407  N   ALA B  84     8174   8256   5235   -175    763     37       N  
ATOM   1408  CA  ALA B  84      40.901  53.807  52.765  1.00 47.30           C  
ANISOU 1408  CA  ALA B  84     6829   7014   4130   -281    823     46       C  
ATOM   1409  C   ALA B  84      39.916  54.640  51.944  1.00 60.18           C  
ANISOU 1409  C   ALA B  84     8081   8646   6139   -334    754     69       C  
ATOM   1410  O   ALA B  84      39.712  54.379  50.756  1.00 47.49           O  
ANISOU 1410  O   ALA B  84     6301   7130   4612   -380    584    147       O  
ATOM   1411  CB  ALA B  84      40.170  52.970  53.793  1.00 48.82           C  
ANISOU 1411  CB  ALA B  84     7225   7063   4262   -355   1129    -50       C  
ATOM   1412  N   VAL B  85      39.310  55.640  52.578  1.00 52.56           N  
ANISOU 1412  N   VAL B  85     6987   7573   5411   -329    872     -6       N  
ATOM   1413  CA  VAL B  85      38.365  56.509  51.883  1.00 58.05           C  
ANISOU 1413  CA  VAL B  85     7313   8232   6512   -362    780      5       C  
ATOM   1414  C   VAL B  85      39.052  57.246  50.742  1.00 57.12           C  
ANISOU 1414  C   VAL B  85     7049   8237   6416   -321    435    164       C  
ATOM   1415  O   VAL B  85      38.484  57.393  49.660  1.00 53.36           O  
ANISOU 1415  O   VAL B  85     6335   7794   6145   -374    256    245       O  
ATOM   1416  CB  VAL B  85      37.721  57.532  52.831  1.00 57.12           C  
ANISOU 1416  CB  VAL B  85     7075   7963   6664   -352    962   -131       C  
ATOM   1417  CG1 VAL B  85      36.642  58.318  52.106  1.00 52.77           C  
ANISOU 1417  CG1 VAL B  85     6124   7340   6585   -381    850   -135       C  
ATOM   1418  CG2 VAL B  85      37.135  56.830  54.043  1.00 71.74           C  
ANISOU 1418  CG2 VAL B  85     9115   9704   8439   -424   1335   -300       C  
ATOM   1419  N   THR B  86      40.277  57.696  50.988  1.00 53.57           N  
ANISOU 1419  N   THR B  86     6753   7855   5746   -238    341    204       N  
ATOM   1420  CA  THR B  86      41.068  58.365  49.963  1.00 46.48           C  
ANISOU 1420  CA  THR B  86     5758   7082   4821   -221     43    345       C  
ATOM   1421  C   THR B  86      41.230  57.481  48.739  1.00 49.47           C  
ANISOU 1421  C   THR B  86     6124   7609   5062   -297   -118    440       C  
ATOM   1422  O   THR B  86      40.968  57.893  47.609  1.00 47.49           O  
ANISOU 1422  O   THR B  86     5676   7421   4946   -361   -333    555       O  
ATOM   1423  CB  THR B  86      42.465  58.734  50.480  1.00 57.21           C  
ANISOU 1423  CB  THR B  86     7316   8500   5921   -129      1    338       C  
ATOM   1424  OG1 THR B  86      42.354  59.409  51.739  1.00 67.86           O  
ANISOU 1424  OG1 THR B  86     8718   9719   7349    -65    179    224       O  
ATOM   1425  CG2 THR B  86      43.189  59.614  49.478  1.00 44.61           C  
ANISOU 1425  CG2 THR B  86     5596   7012   4342   -136   -274    468       C  
ATOM   1426  N   LEU B  87      41.662  56.253  48.990  1.00 53.90           N  
ANISOU 1426  N   LEU B  87     6908   8218   5352   -295    -17    387       N  
ATOM   1427  CA  LEU B  87      41.908  55.282  47.941  1.00 44.51           C  
ANISOU 1427  CA  LEU B  87     5729   7171   4012   -365   -136    436       C  
ATOM   1428  C   LEU B  87      40.629  54.983  47.169  1.00 52.07           C  
ANISOU 1428  C   LEU B  87     6469   8111   5204   -471   -155    462       C  
ATOM   1429  O   LEU B  87      40.627  54.930  45.937  1.00 45.55           O  
ANISOU 1429  O   LEU B  87     5514   7412   4379   -552   -359    553       O  
ATOM   1430  CB  LEU B  87      42.484  54.011  48.553  1.00 43.97           C  
ANISOU 1430  CB  LEU B  87     5938   7101   3666   -329     -3    351       C  
ATOM   1431  CG  LEU B  87      43.002  52.938  47.611  1.00 55.21           C  
ANISOU 1431  CG  LEU B  87     7403   8666   4907   -381   -114    360       C  
ATOM   1432  CD1 LEU B  87      44.002  53.537  46.649  1.00 48.96           C  
ANISOU 1432  CD1 LEU B  87     6533   8050   4022   -396   -350    426       C  
ATOM   1433  CD2 LEU B  87      43.628  51.821  48.427  1.00 59.06           C  
ANISOU 1433  CD2 LEU B  87     8180   9100   5161   -315      3    272       C  
ATOM   1434  N   LEU B  88      39.536  54.814  47.904  1.00 46.85           N  
ANISOU 1434  N   LEU B  88     5764   7293   4742   -481     60    371       N  
ATOM   1435  CA  LEU B  88      38.246  54.528  47.302  1.00 48.16           C  
ANISOU 1435  CA  LEU B  88     5705   7419   5174   -573     61    360       C  
ATOM   1436  C   LEU B  88      37.803  55.651  46.379  1.00 48.90           C  
ANISOU 1436  C   LEU B  88     5512   7527   5542   -599   -197    469       C  
ATOM   1437  O   LEU B  88      37.432  55.401  45.234  1.00 49.29           O  
ANISOU 1437  O   LEU B  88     5419   7664   5646   -683   -385    545       O  
ATOM   1438  CB  LEU B  88      37.197  54.281  48.386  1.00 71.03           C  
ANISOU 1438  CB  LEU B  88     8599  10131   8257   -587    372    209       C  
ATOM   1439  CG  LEU B  88      37.229  52.882  49.007  1.00 65.49           C  
ANISOU 1439  CG  LEU B  88     8156   9400   7329   -621    611    123       C  
ATOM   1440  CD1 LEU B  88      36.279  52.790  50.188  1.00 73.63           C  
ANISOU 1440  CD1 LEU B  88     9217  10247   8512   -659    946    -30       C  
ATOM   1441  CD2 LEU B  88      36.884  51.830  47.964  1.00 49.55           C  
ANISOU 1441  CD2 LEU B  88     6066   7468   5294   -709    528    147       C  
ATOM   1442  N   LYS B  89      37.846  56.884  46.881  1.00 65.64           N  
ANISOU 1442  N   LYS B  89     7555   9551   7833   -530   -219    477       N  
ATOM   1443  CA  LYS B  89      37.518  58.065  46.083  1.00 54.25           C  
ANISOU 1443  CA  LYS B  89     5862   8087   6662   -543   -492    597       C  
ATOM   1444  C   LYS B  89      38.386  58.148  44.833  1.00 58.99           C  
ANISOU 1444  C   LYS B  89     6499   8881   7035   -603   -788    775       C  
ATOM   1445  O   LYS B  89      37.905  58.458  43.736  1.00 69.76           O  
ANISOU 1445  O   LYS B  89     7687  10279   8539   -683  -1041    897       O  
ATOM   1446  CB  LYS B  89      37.687  59.336  46.913  1.00 50.55           C  
ANISOU 1446  CB  LYS B  89     5351   7488   6366   -450   -456    568       C  
ATOM   1447  CG  LYS B  89      36.587  59.586  47.928  1.00 67.18           C  
ANISOU 1447  CG  LYS B  89     7324   9390   8812   -422   -210    386       C  
ATOM   1448  CD  LYS B  89      35.264  59.896  47.250  1.00 74.89           C  
ANISOU 1448  CD  LYS B  89     7965  10261  10230   -470   -347    387       C  
ATOM   1449  CE  LYS B  89      34.188  60.221  48.274  1.00 81.59           C  
ANISOU 1449  CE  LYS B  89     8644  10900  11458   -449    -85    164       C  
ATOM   1450  NZ  LYS B  89      32.862  60.455  47.635  1.00 91.45           N1+
ANISOU 1450  NZ  LYS B  89     9538  12031  13178   -487   -222    130       N1+
ATOM   1451  N   LEU B  90      39.672  57.869  45.014  1.00 49.23           N  
ANISOU 1451  N   LEU B  90     5494   7767   5445   -574   -757    778       N  
ATOM   1452  CA  LEU B  90      40.631  57.890  43.921  1.00 62.75           C  
ANISOU 1452  CA  LEU B  90     7260   9675   6907   -649   -983    903       C  
ATOM   1453  C   LEU B  90      40.233  56.918  42.818  1.00 61.71           C  
ANISOU 1453  C   LEU B  90     7079   9673   6695   -776  -1079    934       C  
ATOM   1454  O   LEU B  90      40.205  57.280  41.643  1.00 69.92           O  
ANISOU 1454  O   LEU B  90     8021  10816   7730   -887  -1331   1071       O  
ATOM   1455  CB  LEU B  90      42.028  57.554  44.436  1.00 69.04           C  
ANISOU 1455  CB  LEU B  90     8299  10565   7369   -587   -890    838       C  
ATOM   1456  CG  LEU B  90      43.169  57.995  43.526  1.00 76.60           C  
ANISOU 1456  CG  LEU B  90     9292  11698   8116   -655  -1097    936       C  
ATOM   1457  CD1 LEU B  90      43.178  59.510  43.418  1.00 77.48           C  
ANISOU 1457  CD1 LEU B  90     9287  11735   8415   -650  -1252   1058       C  
ATOM   1458  CD2 LEU B  90      44.493  57.479  44.052  1.00 89.48           C  
ANISOU 1458  CD2 LEU B  90    11136  13411   9449   -586   -997    825       C  
ATOM   1459  N   VAL B  91      39.925  55.683  43.202  1.00 60.67           N  
ANISOU 1459  N   VAL B  91     7028   9532   6493   -770   -880    808       N  
ATOM   1460  CA  VAL B  91      39.481  54.678  42.242  1.00 59.82           C  
ANISOU 1460  CA  VAL B  91     6866   9534   6330   -887   -942    806       C  
ATOM   1461  C   VAL B  91      38.179  55.116  41.575  1.00 56.99           C  
ANISOU 1461  C   VAL B  91     6247   9109   6296   -956  -1098    875       C  
ATOM   1462  O   VAL B  91      37.984  54.924  40.374  1.00 59.55           O  
ANISOU 1462  O   VAL B  91     6485   9564   6579  -1079  -1309    958       O  
ATOM   1463  CB  VAL B  91      39.289  53.303  42.916  1.00 60.39           C  
ANISOU 1463  CB  VAL B  91     7070   9560   6314   -862   -679    651       C  
ATOM   1464  CG1 VAL B  91      38.680  52.307  41.946  1.00 71.83           C  
ANISOU 1464  CG1 VAL B  91     8428  11100   7762   -984   -734    632       C  
ATOM   1465  CG2 VAL B  91      40.616  52.785  43.436  1.00 58.44           C  
ANISOU 1465  CG2 VAL B  91     7080   9376   5749   -793   -588    589       C  
ATOM   1466  N   GLN B  92      37.298  55.725  42.360  1.00 54.35           N  
ANISOU 1466  N   GLN B  92     5784   8572   6294   -881  -1003    827       N  
ATOM   1467  CA  GLN B  92      36.010  56.180  41.853  1.00 63.43           C  
ANISOU 1467  CA  GLN B  92     6657   9620   7822   -923  -1155    861       C  
ATOM   1468  C   GLN B  92      36.163  57.203  40.728  1.00 81.70           C  
ANISOU 1468  C   GLN B  92     8863  11998  10180   -987  -1535   1069       C  
ATOM   1469  O   GLN B  92      35.698  56.970  39.614  1.00 94.78           O  
ANISOU 1469  O   GLN B  92    10415  13741  11855  -1100  -1761   1152       O  
ATOM   1470  CB  GLN B  92      35.175  56.775  42.988  1.00 58.82           C  
ANISOU 1470  CB  GLN B  92     5945   8798   7606   -826   -967    739       C  
ATOM   1471  CG  GLN B  92      33.761  57.156  42.588  1.00 55.64           C  
ANISOU 1471  CG  GLN B  92     5223   8257   7660   -853  -1098    718       C  
ATOM   1472  CD  GLN B  92      32.918  57.575  43.776  1.00 65.82           C  
ANISOU 1472  CD  GLN B  92     6375   9316   9318   -774   -848    533       C  
ATOM   1473  OE1 GLN B  92      33.329  58.411  44.579  1.00 67.92           O  
ANISOU 1473  OE1 GLN B  92     6686   9494   9627   -689   -765    512       O  
ATOM   1474  NE2 GLN B  92      31.735  56.984  43.900  1.00 76.51           N  
ANISOU 1474  NE2 GLN B  92     7554  10572  10942   -814   -711    376       N  
ATOM   1475  N   ARG B  93      36.833  58.319  41.011  1.00 77.87           N  
ANISOU 1475  N   ARG B  93     8420  11472   9696   -928  -1612   1156       N  
ATOM   1476  CA  ARG B  93      36.978  59.387  40.017  1.00 79.32           C  
ANISOU 1476  CA  ARG B  93     8524  11682   9931   -998  -1972   1371       C  
ATOM   1477  C   ARG B  93      37.934  59.022  38.884  1.00 78.01           C  
ANISOU 1477  C   ARG B  93     8514  11774   9351  -1147  -2136   1495       C  
ATOM   1478  O   ARG B  93      37.764  59.472  37.754  1.00 86.92           O  
ANISOU 1478  O   ARG B  93     9583  12965  10479  -1273  -2449   1672       O  
ATOM   1479  CB  ARG B  93      37.456  60.684  40.673  1.00 87.38           C  
ANISOU 1479  CB  ARG B  93     9550  12574  11077   -900  -1989   1419       C  
ATOM   1480  CG  ARG B  93      36.386  61.439  41.442  1.00108.54           C  
ANISOU 1480  CG  ARG B  93    12003  14986  14250   -790  -1945   1336       C  
ATOM   1481  CD  ARG B  93      36.879  62.829  41.827  1.00119.16           C  
ANISOU 1481  CD  ARG B  93    13333  16212  15731   -717  -2035   1412       C  
ATOM   1482  NE  ARG B  93      35.945  63.524  42.709  1.00128.04           N  
ANISOU 1482  NE  ARG B  93    14240  17077  17331   -604  -1942   1281       N  
ATOM   1483  CZ  ARG B  93      34.894  64.220  42.288  1.00143.56           C  
ANISOU 1483  CZ  ARG B  93    15935  18865  19747   -600  -2181   1330       C  
ATOM   1484  NH1 ARG B  93      34.630  64.314  40.991  1.00139.15           N1+
ANISOU 1484  NH1 ARG B  93    15315  18359  19197   -705  -2549   1535       N1+
ATOM   1485  NH2 ARG B  93      34.101  64.819  43.166  1.00151.26           N  
ANISOU 1485  NH2 ARG B  93    16699  19604  21170   -496  -2059   1163       N  
ATOM   1486  N   HIS B  94      38.944  58.218  39.192  1.00 78.24           N  
ANISOU 1486  N   HIS B  94     8747  11946   9034  -1141  -1932   1394       N  
ATOM   1487  CA  HIS B  94      39.935  57.825  38.196  1.00 78.87           C  
ANISOU 1487  CA  HIS B  94     8964  12275   8727  -1286  -2040   1455       C  
ATOM   1488  C   HIS B  94      40.091  56.310  38.163  1.00 81.31           C  
ANISOU 1488  C   HIS B  94     9362  12711   8822  -1315  -1853   1294       C  
ATOM   1489  O   HIS B  94      40.996  55.765  38.790  1.00 70.62           O  
ANISOU 1489  O   HIS B  94     8168  11402   7263  -1246  -1655   1171       O  
ATOM   1490  CB  HIS B  94      41.283  58.486  38.490  1.00 99.93           C  
ANISOU 1490  CB  HIS B  94    11783  14999  11187  -1259  -2014   1480       C  
ATOM   1491  CG  HIS B  94      41.207  59.971  38.661  1.00102.37           C  
ANISOU 1491  CG  HIS B  94    12017  15160  11719  -1218  -2167   1622       C  
ATOM   1492  ND1 HIS B  94      41.175  60.843  37.594  1.00117.96           N  
ANISOU 1492  ND1 HIS B  94    13948  17171  13702  -1360  -2477   1838       N  
ATOM   1493  CD2 HIS B  94      41.160  60.739  39.776  1.00 94.56           C  
ANISOU 1493  CD2 HIS B  94    10997  13979  10953  -1058  -2056   1576       C  
ATOM   1494  CE1 HIS B  94      41.109  62.084  38.044  1.00111.59           C  
ANISOU 1494  CE1 HIS B  94    13077  16183  13138  -1280  -2558   1924       C  
ATOM   1495  NE2 HIS B  94      41.099  62.048  39.364  1.00 94.58           N  
ANISOU 1495  NE2 HIS B  94    10919  13895  11123  -1095  -2299   1756       N  
ATOM   1496  N   PRO B  95      39.202  55.627  37.427  1.00 86.75           N  
ANISOU 1496  N   PRO B  95     9942  13445   9574  -1413  -1934   1290       N  
ATOM   1497  CA  PRO B  95      39.129  54.161  37.357  1.00 85.78           C  
ANISOU 1497  CA  PRO B  95     9868  13411   9312  -1445  -1765   1131       C  
ATOM   1498  C   PRO B  95      40.452  53.490  36.990  1.00 83.52           C  
ANISOU 1498  C   PRO B  95     9759  13337   8638  -1512  -1710   1060       C  
ATOM   1499  O   PRO B  95      40.753  52.414  37.514  1.00 82.54           O  
ANISOU 1499  O   PRO B  95     9732  13214   8414  -1454  -1496    897       O  
ATOM   1500  CB  PRO B  95      38.083  53.922  36.268  1.00 93.32           C  
ANISOU 1500  CB  PRO B  95    10656  14418  10382  -1583  -1972   1191       C  
ATOM   1501  CG  PRO B  95      37.211  55.125  36.329  1.00 98.35           C  
ANISOU 1501  CG  PRO B  95    11122  14878  11367  -1540  -2160   1325       C  
ATOM   1502  CD  PRO B  95      38.139  56.266  36.633  1.00 90.78           C  
ANISOU 1502  CD  PRO B  95    10261  13899  10334  -1492  -2214   1436       C  
ATOM   1503  N   GLU B  96      41.230  54.124  36.116  1.00 79.56           N  
ANISOU 1503  N   GLU B  96     9298  12998   7933  -1641  -1899   1173       N  
ATOM   1504  CA  GLU B  96      42.515  53.580  35.675  1.00 76.43           C  
ANISOU 1504  CA  GLU B  96     9048  12737   7254  -1694  -1796   1057       C  
ATOM   1505  C   GLU B  96      43.451  53.296  36.850  1.00 81.08           C  
ANISOU 1505  C   GLU B  96     9766  13304   7738  -1542  -1604    924       C  
ATOM   1506  O   GLU B  96      44.322  52.424  36.768  1.00 87.22           O  
ANISOU 1506  O   GLU B  96    10640  14104   8396  -1518  -1451    751       O  
ATOM   1507  CB  GLU B  96      43.190  54.540  34.691  1.00 84.61           C  
ANISOU 1507  CB  GLU B  96    10135  13734   8279  -1772  -1864   1144       C  
ATOM   1508  CG  GLU B  96      43.697  55.844  35.308  1.00112.66           C  
ANISOU 1508  CG  GLU B  96    13723  17186  11898  -1688  -1901   1242       C  
ATOM   1509  CD  GLU B  96      42.593  56.857  35.570  1.00131.70           C  
ANISOU 1509  CD  GLU B  96    16003  19500  14539  -1671  -2119   1445       C  
ATOM   1510  OE1 GLU B  96      41.404  56.519  35.380  1.00133.49           O  
ANISOU 1510  OE1 GLU B  96    16092  19730  14899  -1710  -2244   1497       O  
ATOM   1511  OE2 GLU B  96      42.919  57.998  35.964  1.00135.53           O1+
ANISOU 1511  OE2 GLU B  96    16498  19892  15106  -1616  -2177   1541       O1+
ATOM   1512  N   THR B  97      43.256  54.035  37.940  1.00 65.50           N  
ANISOU 1512  N   THR B  97     7797  11158   5932  -1387  -1551    968       N  
ATOM   1513  CA  THR B  97      44.021  53.852  39.166  1.00 65.88           C  
ANISOU 1513  CA  THR B  97     7986  11114   5932  -1212  -1355    843       C  
ATOM   1514  C   THR B  97      43.972  52.405  39.634  1.00 65.34           C  
ANISOU 1514  C   THR B  97     8003  11017   5805  -1152  -1167    672       C  
ATOM   1515  O   THR B  97      44.978  51.844  40.075  1.00 48.06           O  
ANISOU 1515  O   THR B  97     5954   8856   3452  -1081  -1074    544       O  
ATOM   1516  CB  THR B  97      43.494  54.759  40.289  1.00 60.87           C  
ANISOU 1516  CB  THR B  97     7328  10255   5546  -1060  -1288    893       C  
ATOM   1517  OG1 THR B  97      43.614  56.129  39.891  1.00 70.66           O  
ANISOU 1517  OG1 THR B  97     8492  11496   6859  -1105  -1472   1051       O  
ATOM   1518  CG2 THR B  97      44.266  54.532  41.575  1.00 52.00           C  
ANISOU 1518  CG2 THR B  97     6374   9040   4342   -892  -1096    765       C  
ATOM   1519  N   LEU B  98      42.794  51.802  39.513  1.00 78.93           N  
ANISOU 1519  N   LEU B  98     9636  12673   7681  -1184  -1127    667       N  
ATOM   1520  CA  LEU B  98      42.593  50.430  39.952  1.00 74.16           C  
ANISOU 1520  CA  LEU B  98     9111  12013   7052  -1143   -946    520       C  
ATOM   1521  C   LEU B  98      43.529  49.471  39.223  1.00 76.97           C  
ANISOU 1521  C   LEU B  98     9529  12552   7163  -1223   -970    403       C  
ATOM   1522  O   LEU B  98      43.955  48.459  39.785  1.00 75.41           O  
ANISOU 1522  O   LEU B  98     9459  12300   6893  -1145   -835    266       O  
ATOM   1523  CB  LEU B  98      41.141  50.016  39.741  1.00 61.13           C  
ANISOU 1523  CB  LEU B  98     7320  10284   5622  -1200   -916    530       C  
ATOM   1524  CG  LEU B  98      40.708  48.761  40.494  1.00 63.95           C  
ANISOU 1524  CG  LEU B  98     7769  10512   6019  -1144   -685    394       C  
ATOM   1525  CD1 LEU B  98      40.910  48.931  41.994  1.00 45.10           C  
ANISOU 1525  CD1 LEU B  98     5550   7929   3656   -985   -492    360       C  
ATOM   1526  CD2 LEU B  98      39.265  48.454  40.178  1.00 65.38           C  
ANISOU 1526  CD2 LEU B  98     7774  10627   6439  -1221   -664    391       C  
ATOM   1527  N   SER B  99      43.861  49.793  37.977  1.00 69.11           N  
ANISOU 1527  N   SER B  99     8448  11766   6043  -1388  -1145    451       N  
ATOM   1528  CA  SER B  99      44.819  48.985  37.238  1.00 61.64           C  
ANISOU 1528  CA  SER B  99     7539  10937   4944  -1456  -1124    304       C  
ATOM   1529  C   SER B  99      46.235  49.241  37.741  1.00 70.03           C  
ANISOU 1529  C   SER B  99     8718  11898   5991  -1316  -1045    214       C  
ATOM   1530  O   SER B  99      47.023  48.307  37.894  1.00 58.22           O  
ANISOU 1530  O   SER B  99     7293  10371   4457  -1252   -956     43       O  
ATOM   1531  CB  SER B  99      44.736  49.268  35.741  1.00 67.88           C  
ANISOU 1531  CB  SER B  99     8222  11803   5765  -1625  -1226    359       C  
ATOM   1532  OG  SER B  99      45.697  48.495  35.043  1.00 86.21           O  
ANISOU 1532  OG  SER B  99    10567  14158   8031  -1663  -1139    193       O  
ATOM   1533  N   HIS B 100      46.546  50.512  37.993  1.00 81.11           N  
ANISOU 1533  N   HIS B 100    10129  13251   7439  -1272  -1098    324       N  
ATOM   1534  CA  HIS B 100      47.856  50.901  38.511  1.00 70.66           C  
ANISOU 1534  CA  HIS B 100     8899  11839   6111  -1147  -1044    240       C  
ATOM   1535  C   HIS B 100      48.157  50.145  39.788  1.00 60.03           C  
ANISOU 1535  C   HIS B 100     7693  10397   4718   -973   -943    124       C  
ATOM   1536  O   HIS B 100      49.263  49.640  39.981  1.00 60.85           O  
ANISOU 1536  O   HIS B 100     7871  10442   4808   -885   -899    -27       O  
ATOM   1537  CB  HIS B 100      47.921  52.405  38.780  1.00 84.61           C  
ANISOU 1537  CB  HIS B 100    10652  13566   7931  -1125  -1117    385       C  
ATOM   1538  CG  HIS B 100      47.928  53.246  37.542  1.00 96.02           C  
ANISOU 1538  CG  HIS B 100    12007  15067   9410  -1286  -1219    496       C  
ATOM   1539  ND1 HIS B 100      47.790  54.616  37.575  1.00 95.74           N  
ANISOU 1539  ND1 HIS B 100    11943  14998   9436  -1304  -1319    656       N  
ATOM   1540  CD2 HIS B 100      48.057  52.910  36.237  1.00 99.72           C  
ANISOU 1540  CD2 HIS B 100    12423  15621   9846  -1446  -1235    473       C  
ATOM   1541  CE1 HIS B 100      47.832  55.090  36.343  1.00102.94           C  
ANISOU 1541  CE1 HIS B 100    12806  15959  10348  -1468  -1397    737       C  
ATOM   1542  NE2 HIS B 100      47.994  54.076  35.512  1.00106.55           N  
ANISOU 1542  NE2 HIS B 100    13252  16497  10736  -1561  -1341    628       N  
ATOM   1543  N   ILE B 101      47.151  50.070  40.653  1.00 71.88           N  
ANISOU 1543  N   ILE B 101     9234  11888   6189   -934   -912    199       N  
ATOM   1544  CA  ILE B 101      47.261  49.373  41.926  1.00 76.52           C  
ANISOU 1544  CA  ILE B 101     9995  12347   6731   -779   -790    115       C  
ATOM   1545  C   ILE B 101      47.470  47.880  41.703  1.00 69.64           C  
ANISOU 1545  C   ILE B 101     9179  11491   5792   -792   -743    -37       C  
ATOM   1546  O   ILE B 101      48.182  47.222  42.462  1.00 60.12           O  
ANISOU 1546  O   ILE B 101     8129  10175   4537   -660   -696   -150       O  
ATOM   1547  CB  ILE B 101      46.006  49.600  42.792  1.00 72.92           C  
ANISOU 1547  CB  ILE B 101     9555  11693   6458   -717   -671    210       C  
ATOM   1548  CG1 ILE B 101      45.786  51.096  43.021  1.00 84.09           C  
ANISOU 1548  CG1 ILE B 101    10892  13074   7983   -697   -724    340       C  
ATOM   1549  CG2 ILE B 101      46.123  48.875  44.121  1.00 48.53           C  
ANISOU 1549  CG2 ILE B 101     6685   8410   3343   -568   -518    131       C  
ATOM   1550  CD1 ILE B 101      44.493  51.415  43.729  1.00 96.03           C  
ANISOU 1550  CD1 ILE B 101    12364  14405   9717   -662   -608    403       C  
ATOM   1551  N   ALA B 102      46.854  47.352  40.651  1.00 71.16           N  
ANISOU 1551  N   ALA B 102     9240  11797   6001   -948   -770    -42       N  
ATOM   1552  CA  ALA B 102      46.979  45.934  40.340  1.00 80.61           C  
ANISOU 1552  CA  ALA B 102    10461  13009   7158   -977   -725   -198       C  
ATOM   1553  C   ALA B 102      48.417  45.583  39.970  1.00 79.24           C  
ANISOU 1553  C   ALA B 102    10298  12801   7007   -919   -751   -356       C  
ATOM   1554  O   ALA B 102      48.962  44.578  40.427  1.00 64.60           O  
ANISOU 1554  O   ALA B 102     8551  10872   5123   -829   -720   -500       O  
ATOM   1555  CB  ALA B 102      46.031  45.551  39.211  1.00 81.98           C  
ANISOU 1555  CB  ALA B 102    10470  13301   7377  -1161   -754   -177       C  
ATOM   1556  N   GLU B 103      49.033  46.439  39.163  1.00 89.09           N  
ANISOU 1556  N   GLU B 103    11441  14099   8311   -977   -808   -329       N  
ATOM   1557  CA  GLU B 103      50.351  46.171  38.598  1.00 89.60           C  
ANISOU 1557  CA  GLU B 103    11474  14167   8401   -973   -813   -485       C  
ATOM   1558  C   GLU B 103      51.457  46.642  39.532  1.00 84.70           C  
ANISOU 1558  C   GLU B 103    10965  13421   7795   -801   -826   -533       C  
ATOM   1559  O   GLU B 103      52.639  46.602  39.189  1.00 90.07           O  
ANISOU 1559  O   GLU B 103    11613  14106   8505   -793   -837   -663       O  
ATOM   1560  CB  GLU B 103      50.480  46.842  37.232  1.00 95.37           C  
ANISOU 1560  CB  GLU B 103    12057  15026   9153  -1153   -841   -437       C  
ATOM   1561  CG  GLU B 103      49.376  46.447  36.263  1.00121.75           C  
ANISOU 1561  CG  GLU B 103    15294  18490  12476  -1330   -855   -380       C  
ATOM   1562  CD  GLU B 103      49.363  47.292  35.005  1.00145.43           C  
ANISOU 1562  CD  GLU B 103    18191  21596  15470  -1509   -900   -282       C  
ATOM   1563  OE1 GLU B 103      49.936  48.403  35.024  1.00144.67           O  
ANISOU 1563  OE1 GLU B 103    18110  21473  15386  -1498   -925   -208       O  
ATOM   1564  OE2 GLU B 103      48.778  46.842  33.996  1.00151.90           O  
ANISOU 1564  OE2 GLU B 103    18928  22525  16264  -1669   -912   -280       O  
ATOM   1565  N   LEU B 104      51.056  47.099  40.712  1.00 78.06           N  
ANISOU 1565  N   LEU B 104    10249  12478   6931   -677   -820   -435       N  
ATOM   1566  CA  LEU B 104      51.991  47.585  41.716  1.00 92.43           C  
ANISOU 1566  CA  LEU B 104    12194  14170   8756   -512   -840   -469       C  
ATOM   1567  C   LEU B 104      52.895  46.465  42.225  1.00103.90           C  
ANISOU 1567  C   LEU B 104    13759  15527  10190   -395   -860   -651       C  
ATOM   1568  O   LEU B 104      52.937  46.183  43.424  1.00115.49           O  
ANISOU 1568  O   LEU B 104    15415  16861  11606   -252   -864   -653       O  
ATOM   1569  CB  LEU B 104      51.223  48.214  42.878  1.00 96.05           C  
ANISOU 1569  CB  LEU B 104    12769  14551   9175   -422   -809   -329       C  
ATOM   1570  CG  LEU B 104      51.837  49.429  43.564  1.00 89.35           C  
ANISOU 1570  CG  LEU B 104    11968  13629   8352   -328   -836   -285       C  
ATOM   1571  CD1 LEU B 104      52.168  50.502  42.541  1.00 84.50           C  
ANISOU 1571  CD1 LEU B 104    11187  13115   7806   -446   -882   -236       C  
ATOM   1572  CD2 LEU B 104      50.868  49.962  44.606  1.00 91.14           C  
ANISOU 1572  CD2 LEU B 104    12285  13814   8532   -271   -781   -155       C  
TER    1573      LEU B 104                                                      
ATOM   1574  N   HIS C   0      37.371  72.650  56.498  1.00126.69           N  
ANISOU 1574  N   HIS C   0    19018  16830  12288  -6763    603  -1227       N  
ATOM   1575  CA  HIS C   0      38.237  73.421  55.614  1.00144.93           C  
ANISOU 1575  CA  HIS C   0    21007  18875  15185  -6202    497  -1198       C  
ATOM   1576  C   HIS C   0      38.767  74.674  56.304  1.00156.68           C  
ANISOU 1576  C   HIS C   0    21989  20469  17072  -5627    223  -1260       C  
ATOM   1577  O   HIS C   0      37.995  75.498  56.796  1.00158.69           O  
ANISOU 1577  O   HIS C   0    21757  21283  17253  -5655    165  -1459       O  
ATOM   1578  CB  HIS C   0      37.493  73.806  54.330  1.00153.68           C  
ANISOU 1578  CB  HIS C   0    21746  20357  16290  -6407    605  -1301       C  
ATOM   1579  CG  HIS C   0      37.364  72.685  53.343  1.00167.30           C  
ANISOU 1579  CG  HIS C   0    23983  21826  17756  -6871    869  -1246       C  
ATOM   1580  ND1 HIS C   0      37.983  72.704  52.111  1.00167.21           N  
ANISOU 1580  ND1 HIS C   0    24021  21498  18014  -6736    953  -1205       N  
ATOM   1581  CD2 HIS C   0      36.689  71.513  53.406  1.00169.86           C  
ANISOU 1581  CD2 HIS C   0    24816  22163  17561  -7512   1092  -1253       C  
ATOM   1582  CE1 HIS C   0      37.697  71.591  51.460  1.00167.42           C  
ANISOU 1582  CE1 HIS C   0    24569  21347  17698  -7269   1231  -1218       C  
ATOM   1583  NE2 HIS C   0      36.915  70.850  52.223  1.00164.66           N  
ANISOU 1583  NE2 HIS C   0    24510  21174  16881  -7740   1310  -1239       N  
HETATM 1584  N   MSE C   1      40.089  74.807  56.343  1.00159.50           N  
ANISOU 1584  N   MSE C   1    22448  20278  17875  -5116     72  -1111       N  
HETATM 1585  CA  MSE C   1      40.714  76.038  56.808  1.00164.91           C  
ANISOU 1585  CA  MSE C   1    22654  21012  18994  -4572   -189  -1172       C  
HETATM 1586  C   MSE C   1      41.199  76.842  55.603  1.00153.49           C  
ANISOU 1586  C   MSE C   1    20821  19443  18056  -4209   -211  -1172       C  
HETATM 1587  O   MSE C   1      42.140  76.451  54.915  1.00166.41           O  
ANISOU 1587  O   MSE C   1    22685  20575  19970  -4016   -157  -1027       O  
HETATM 1588  CB  MSE C   1      41.869  75.746  57.777  1.00177.15           C  
ANISOU 1588  CB  MSE C   1    24513  22106  20691  -4274   -399   -991       C  
HETATM 1589  CG  MSE C   1      42.870  74.696  57.307  1.00183.72           C  
ANISOU 1589  CG  MSE C   1    25853  22227  21724  -4158   -339   -730       C  
HETATM 1590 SE   MSE C   1      44.549  74.733  58.315  1.00290.68          SE  
ANISOU 1590 SE   MSE C   1    39510  35213  35724  -3579   -722   -462      SE  
HETATM 1591  CE  MSE C   1      43.887  74.230  60.081  1.00176.21           C  
ANISOU 1591  CE  MSE C   1    25385  21040  20527  -4037   -899   -386       C  
ATOM   1592  N   LYS C   2      40.542  77.966  55.346  1.00129.79           N  
ANISOU 1592  N   LYS C   2    17227  16899  15189  -4129   -280  -1333       N  
ATOM   1593  CA  LYS C   2      40.839  78.762  54.162  1.00106.31           C  
ANISOU 1593  CA  LYS C   2    13889  13869  12635  -3874   -322  -1293       C  
ATOM   1594  C   LYS C   2      41.870  79.845  54.462  1.00 93.17           C  
ANISOU 1594  C   LYS C   2    11897  11977  11527  -3289   -560  -1292       C  
ATOM   1595  O   LYS C   2      41.874  80.433  55.542  1.00 85.33           O  
ANISOU 1595  O   LYS C   2    10705  11123  10592  -3111   -715  -1424       O  
ATOM   1596  CB  LYS C   2      39.559  79.390  53.604  1.00 92.99           C  
ANISOU 1596  CB  LYS C   2    11724  12760  10849  -4105   -313  -1400       C  
ATOM   1597  N   SER C   3      42.749  80.096  53.498  1.00 89.66           N  
ANISOU 1597  N   SER C   3    11410  11193  11465  -3040   -565  -1164       N  
ATOM   1598  CA  SER C   3      43.769  81.126  53.638  1.00 92.84           C  
ANISOU 1598  CA  SER C   3    11494  11367  12412  -2528   -777  -1150       C  
ATOM   1599  C   SER C   3      43.836  81.997  52.391  1.00 95.11           C  
ANISOU 1599  C   SER C   3    11425  11684  13028  -2419   -801  -1085       C  
ATOM   1600  O   SER C   3      43.582  81.538  51.278  1.00 77.49           O  
ANISOU 1600  O   SER C   3     9340   9469  10635  -2701   -627   -992       O  
ATOM   1601  CB  SER C   3      45.134  80.500  53.921  1.00 94.81           C  
ANISOU 1601  CB  SER C   3    12086  11070  12867  -2282   -790  -1018       C  
ATOM   1602  OG  SER C   3      45.159  79.910  55.208  1.00114.68           O  
ANISOU 1602  OG  SER C   3    14881  13562  15131  -2335   -877  -1022       O  
ATOM   1603  N   VAL C   4      44.193  83.259  52.587  1.00 92.96           N  
ANISOU 1603  N   VAL C   4    10712  11411  13198  -2047  -1022  -1128       N  
ATOM   1604  CA  VAL C   4      44.169  84.232  51.506  1.00 83.48           C  
ANISOU 1604  CA  VAL C   4     9144  10256  12319  -1953  -1101  -1031       C  
ATOM   1605  C   VAL C   4      45.521  84.943  51.372  1.00 75.06           C  
ANISOU 1605  C   VAL C   4     7946   8795  11778  -1550  -1221   -961       C  
ATOM   1606  O   VAL C   4      46.097  85.397  52.363  1.00 74.17           O  
ANISOU 1606  O   VAL C   4     7724   8555  11902  -1250  -1380  -1065       O  
ATOM   1607  CB  VAL C   4      43.031  85.250  51.734  1.00 85.67           C  
ANISOU 1607  CB  VAL C   4     8919  10949  12683  -1931  -1262  -1144       C  
ATOM   1608  CG1 VAL C   4      42.996  85.699  53.191  1.00 92.61           C  
ANISOU 1608  CG1 VAL C   4     9649  11890  13648  -1706  -1368  -1400       C  
ATOM   1609  CG2 VAL C   4      43.170  86.430  50.813  1.00 83.55           C  
ANISOU 1609  CG2 VAL C   4     8250  10635  12862  -1741  -1433   -999       C  
ATOM   1610  N   PHE C   5      46.036  85.009  50.146  1.00 73.70           N  
ANISOU 1610  N   PHE C   5     7797   8456  11749  -1596  -1132   -793       N  
ATOM   1611  CA  PHE C   5      47.361  85.575  49.899  1.00 82.01           C  
ANISOU 1611  CA  PHE C   5     8738   9145  13276  -1280  -1191   -723       C  
ATOM   1612  C   PHE C   5      47.336  86.839  49.047  1.00 72.76           C  
ANISOU 1612  C   PHE C   5     7182   8029  12433  -1212  -1343   -598       C  
ATOM   1613  O   PHE C   5      47.063  86.788  47.852  1.00 73.37           O  
ANISOU 1613  O   PHE C   5     7301   8204  12374  -1489  -1246   -438       O  
ATOM   1614  CB  PHE C   5      48.255  84.532  49.234  1.00 85.76           C  
ANISOU 1614  CB  PHE C   5     9592   9296  13695  -1378   -903   -651       C  
ATOM   1615  CG  PHE C   5      48.536  83.347  50.101  1.00 82.37           C  
ANISOU 1615  CG  PHE C   5     9538   8671  13086  -1358   -799   -718       C  
ATOM   1616  CD1 PHE C   5      47.705  82.240  50.076  1.00 89.38           C  
ANISOU 1616  CD1 PHE C   5    10801   9680  13480  -1723   -605   -746       C  
ATOM   1617  CD2 PHE C   5      49.625  83.344  50.955  1.00 78.73           C  
ANISOU 1617  CD2 PHE C   5     9055   7905  12953   -998   -927   -722       C  
ATOM   1618  CE1 PHE C   5      47.960  81.150  50.882  1.00 80.37           C  
ANISOU 1618  CE1 PHE C   5    10037   8310  12189  -1717   -534   -761       C  
ATOM   1619  CE2 PHE C   5      49.885  82.255  51.762  1.00 75.55           C  
ANISOU 1619  CE2 PHE C   5     9001   7302  12403   -979   -891   -713       C  
ATOM   1620  CZ  PHE C   5      49.052  81.159  51.725  1.00 76.65           C  
ANISOU 1620  CZ  PHE C   5     9543   7518  12063  -1333   -692   -724       C  
ATOM   1621  N   VAL C   6      47.662  87.966  49.668  1.00 72.38           N  
ANISOU 1621  N   VAL C   6     6792   7900  12811   -875  -1590   -662       N  
ATOM   1622  CA  VAL C   6      47.620  89.261  49.005  1.00 80.92           C  
ANISOU 1622  CA  VAL C   6     7504   8975  14269   -779  -1779   -530       C  
ATOM   1623  C   VAL C   6      48.999  89.682  48.518  1.00 80.92           C  
ANISOU 1623  C   VAL C   6     7476   8623  14646   -627  -1769   -422       C  
ATOM   1624  O   VAL C   6      49.897  89.938  49.319  1.00 81.25           O  
ANISOU 1624  O   VAL C   6     7453   8441  14980   -346  -1852   -540       O  
ATOM   1625  CB  VAL C   6      47.071  90.353  49.944  1.00 73.91           C  
ANISOU 1625  CB  VAL C   6     6234   8172  13675   -516  -2032   -702       C  
ATOM   1626  CG1 VAL C   6      46.625  91.562  49.140  1.00 74.50           C  
ANISOU 1626  CG1 VAL C   6     5944   8269  14095   -477  -2232   -517       C  
ATOM   1627  CG2 VAL C   6      45.922  89.812  50.784  1.00 73.85           C  
ANISOU 1627  CG2 VAL C   6     6260   8501  13299   -633  -1982   -908       C  
ATOM   1628  N   GLU C   7      49.157  89.766  47.202  1.00 77.09           N  
ANISOU 1628  N   GLU C   7     7032   8127  14133   -857  -1672   -198       N  
ATOM   1629  CA  GLU C   7      50.435  90.136  46.607  1.00 85.87           C  
ANISOU 1629  CA  GLU C   7     8111   8949  15565   -790  -1605    -99       C  
ATOM   1630  C   GLU C   7      50.583  91.647  46.437  1.00 88.58           C  
ANISOU 1630  C   GLU C   7     8087   9197  16372   -633  -1893     28       C  
ATOM   1631  O   GLU C   7      49.732  92.303  45.832  1.00 91.38           O  
ANISOU 1631  O   GLU C   7     8288   9712  16720   -768  -2061    219       O  
ATOM   1632  CB  GLU C   7      50.607  89.453  45.247  1.00 92.19           C  
ANISOU 1632  CB  GLU C   7     9180   9787  16062  -1186  -1300     49       C  
ATOM   1633  CG  GLU C   7      50.571  87.935  45.285  1.00101.28           C  
ANISOU 1633  CG  GLU C   7    10736  10939  16807  -1363   -963    -91       C  
ATOM   1634  CD  GLU C   7      50.746  87.321  43.906  1.00114.77           C  
ANISOU 1634  CD  GLU C   7    12719  12675  18214  -1795   -616    -10       C  
ATOM   1635  OE1 GLU C   7      51.415  86.272  43.798  1.00121.63           O  
ANISOU 1635  OE1 GLU C   7    13873  13331  19008  -1836   -259   -155       O  
ATOM   1636  OE2 GLU C   7      50.213  87.888  42.929  1.00115.17           O  
ANISOU 1636  OE2 GLU C   7    12702  12952  18106  -2108   -701    200       O  
ATOM   1637  N   SER C   8      51.670  92.198  46.968  1.00 83.97           N  
ANISOU 1637  N   SER C   8     7357   8335  16212   -358  -1971    -57       N  
ATOM   1638  CA  SER C   8      52.023  93.579  46.678  1.00 79.43           C  
ANISOU 1638  CA  SER C   8     6491   7592  16098   -261  -2196     74       C  
ATOM   1639  C   SER C   8      52.439  93.668  45.216  1.00 92.34           C  
ANISOU 1639  C   SER C   8     8208   9204  17674   -582  -2051    362       C  
ATOM   1640  O   SER C   8      52.801  92.660  44.611  1.00 98.88           O  
ANISOU 1640  O   SER C   8     9298  10081  18192   -809  -1728    364       O  
ATOM   1641  CB  SER C   8      53.148  94.071  47.588  1.00 82.68           C  
ANISOU 1641  CB  SER C   8     6745   7734  16934     42  -2296   -104       C  
ATOM   1642  OG  SER C   8      54.385  93.477  47.234  1.00 87.89           O  
ANISOU 1642  OG  SER C   8     7509   8247  17638      0  -2065    -88       O  
ATOM   1643  N   THR C   9      52.384  94.870  44.654  1.00103.55           N  
ANISOU 1643  N   THR C   9     9422  10535  19386   -624  -2275    597       N  
ATOM   1644  CA  THR C   9      52.711  95.075  43.247  1.00 97.63           C  
ANISOU 1644  CA  THR C   9     8762   9799  18535  -1000  -2176    914       C  
ATOM   1645  C   THR C   9      54.138  94.631  42.924  1.00 79.79           C  
ANISOU 1645  C   THR C   9     6607   7380  16331  -1079  -1841    825       C  
ATOM   1646  O   THR C   9      54.402  94.110  41.838  1.00 81.12           O  
ANISOU 1646  O   THR C   9     6982   7649  16192  -1458  -1549    938       O  
ATOM   1647  CB  THR C   9      52.532  96.546  42.849  1.00 99.15           C  
ANISOU 1647  CB  THR C   9     8709   9844  19118   -996  -2528   1210       C  
ATOM   1648  OG1 THR C   9      53.236  97.376  43.780  1.00110.67           O  
ANISOU 1648  OG1 THR C   9     9941  10989  21119   -637  -2681   1027       O  
ATOM   1649  CG2 THR C   9      51.054  96.922  42.863  1.00 82.82           C  
ANISOU 1649  CG2 THR C   9     6507   7956  17004   -968  -2831   1365       C  
ATOM   1650  N   ILE C  10      55.048  94.836  43.873  1.00 80.32           N  
ANISOU 1650  N   ILE C  10     6511   7216  16791   -739  -1877    604       N  
ATOM   1651  CA  ILE C  10      56.428  94.375  43.740  1.00 87.09           C  
ANISOU 1651  CA  ILE C  10     7376   7922  17791   -737  -1578    488       C  
ATOM   1652  C   ILE C  10      56.479  92.855  43.615  1.00 90.58           C  
ANISOU 1652  C   ILE C  10     8099   8458  17860   -818  -1195    331       C  
ATOM   1653  O   ILE C  10      57.015  92.307  42.639  1.00 91.42           O  
ANISOU 1653  O   ILE C  10     8349   8573  17812  -1098   -816    349       O  
ATOM   1654  CB  ILE C  10      57.296  94.805  44.946  1.00 91.75           C  
ANISOU 1654  CB  ILE C  10     7713   8294  18856   -347  -1759    284       C  
ATOM   1655  CG1 ILE C  10      57.518  96.319  44.952  1.00107.65           C  
ANISOU 1655  CG1 ILE C  10     9469  10134  21300   -316  -2062    408       C  
ATOM   1656  CG2 ILE C  10      58.633  94.083  44.927  1.00100.76           C  
ANISOU 1656  CG2 ILE C  10     8820   9317  20146   -293  -1456    153       C  
ATOM   1657  CD1 ILE C  10      56.433  97.105  45.665  1.00121.92           C  
ANISOU 1657  CD1 ILE C  10    11180  11936  23208   -130  -2429    383       C  
ATOM   1658  N   PHE C  11      55.909  92.181  44.610  1.00 91.82           N  
ANISOU 1658  N   PHE C  11     8346   8668  17872   -596  -1274    160       N  
ATOM   1659  CA  PHE C  11      55.843  90.728  44.619  1.00 86.23           C  
ANISOU 1659  CA  PHE C  11     7938   7994  16830   -655   -952     21       C  
ATOM   1660  C   PHE C  11      55.109  90.239  43.382  1.00 89.56           C  
ANISOU 1660  C   PHE C  11     8640   8628  16761  -1121   -702    139       C  
ATOM   1661  O   PHE C  11      55.458  89.207  42.812  1.00100.51           O  
ANISOU 1661  O   PHE C  11    10277   9974  17937  -1310   -291     38       O  
ATOM   1662  CB  PHE C  11      55.149  90.220  45.887  1.00 79.65           C  
ANISOU 1662  CB  PHE C  11     7182   7223  15859   -418  -1137   -125       C  
ATOM   1663  CG  PHE C  11      55.157  88.723  46.024  1.00 82.42           C  
ANISOU 1663  CG  PHE C  11     7861   7531  15923   -456   -839   -248       C  
ATOM   1664  CD1 PHE C  11      54.146  87.955  45.469  1.00 80.44           C  
ANISOU 1664  CD1 PHE C  11     7923   7476  15165   -784   -654   -232       C  
ATOM   1665  CD2 PHE C  11      56.180  88.083  46.702  1.00 98.02           C  
ANISOU 1665  CD2 PHE C  11     9828   9254  18161   -175   -764   -360       C  
ATOM   1666  CE1 PHE C  11      54.157  86.580  45.586  1.00 88.89           C  
ANISOU 1666  CE1 PHE C  11     9330   8448  15994   -840   -367   -352       C  
ATOM   1667  CE2 PHE C  11      56.195  86.707  46.825  1.00100.34           C  
ANISOU 1667  CE2 PHE C  11    10436   9432  18255   -188   -505   -444       C  
ATOM   1668  CZ  PHE C  11      55.181  85.956  46.266  1.00 98.12           C  
ANISOU 1668  CZ  PHE C  11    10505   9307  17468   -526   -289   -453       C  
ATOM   1669  N   GLU C  12      54.094  90.993  42.972  1.00 81.09           N  
ANISOU 1669  N   GLU C  12     7511   7771  15527  -1311   -958    348       N  
ATOM   1670  CA  GLU C  12      53.282  90.634  41.817  1.00 94.42           C  
ANISOU 1670  CA  GLU C  12     9440   9729  16708  -1804   -818    512       C  
ATOM   1671  C   GLU C  12      54.110  90.598  40.537  1.00 96.44           C  
ANISOU 1671  C   GLU C  12     9812   9953  16877  -2183   -479    596       C  
ATOM   1672  O   GLU C  12      54.088  89.609  39.801  1.00 98.53           O  
ANISOU 1672  O   GLU C  12    10395  10310  16732  -2539    -83    503       O  
ATOM   1673  CB  GLU C  12      52.119  91.616  41.660  1.00100.30           C  
ANISOU 1673  CB  GLU C  12    10003  10690  17415  -1883  -1244    781       C  
ATOM   1674  CG  GLU C  12      51.131  91.238  40.573  1.00118.80           C  
ANISOU 1674  CG  GLU C  12    12559  13379  19202  -2406  -1198    990       C  
ATOM   1675  CD  GLU C  12      50.053  92.284  40.381  1.00144.39           C  
ANISOU 1675  CD  GLU C  12    15542  16808  22512  -2442  -1671   1315       C  
ATOM   1676  OE1 GLU C  12      50.149  93.357  41.014  1.00151.37           O  
ANISOU 1676  OE1 GLU C  12    16101  17497  23914  -2061  -1987   1359       O  
ATOM   1677  OE2 GLU C  12      49.112  92.033  39.598  1.00151.29           O  
ANISOU 1677  OE2 GLU C  12    16526  18013  22943  -2855  -1732   1525       O  
ATOM   1678  N   LYS C  13      54.845  91.675  40.277  1.00 92.40           N  
ANISOU 1678  N   LYS C  13     9059   9309  16740  -2142   -606    745       N  
ATOM   1679  CA  LYS C  13      55.614  91.778  39.042  1.00 97.39           C  
ANISOU 1679  CA  LYS C  13     9781   9951  17271  -2562   -286    841       C  
ATOM   1680  C   LYS C  13      56.855  90.889  39.049  1.00106.74           C  
ANISOU 1680  C   LYS C  13    11019  10932  18605  -2478    230    515       C  
ATOM   1681  O   LYS C  13      57.296  90.430  37.994  1.00122.77           O  
ANISOU 1681  O   LYS C  13    13241  13024  20381  -2896    680    458       O  
ATOM   1682  CB  LYS C  13      56.020  93.230  38.779  1.00 87.17           C  
ANISOU 1682  CB  LYS C  13     8216   8562  16343  -2576   -587   1122       C  
ATOM   1683  CG  LYS C  13      56.918  93.828  39.844  1.00 85.83           C  
ANISOU 1683  CG  LYS C  13     7715   8087  16808  -2071   -748    974       C  
ATOM   1684  CD  LYS C  13      57.355  95.236  39.485  1.00 95.01           C  
ANISOU 1684  CD  LYS C  13     8659   9124  18318  -2162  -1001   1245       C  
ATOM   1685  CE  LYS C  13      58.239  95.245  38.251  1.00101.02           C  
ANISOU 1685  CE  LYS C  13     9512   9929  18942  -2646   -616   1337       C  
ATOM   1686  NZ  LYS C  13      58.819  96.596  37.999  1.00113.35           N  
ANISOU 1686  NZ  LYS C  13    10862  11326  20881  -2739   -845   1590       N  
ATOM   1687  N   TYR C  14      57.420  90.638  40.227  1.00109.44           N  
ANISOU 1687  N   TYR C  14    11183  11036  19365  -1955    171    299       N  
ATOM   1688  CA  TYR C  14      58.661  89.869  40.295  1.00114.99           C  
ANISOU 1688  CA  TYR C  14    11845  11507  20340  -1800    601     30       C  
ATOM   1689  C   TYR C  14      58.480  88.370  40.566  1.00121.49           C  
ANISOU 1689  C   TYR C  14    12960  12246  20956  -1720    922   -221       C  
ATOM   1690  O   TYR C  14      59.464  87.631  40.627  1.00122.81           O  
ANISOU 1690  O   TYR C  14    13089  12174  21401  -1551   1287   -445       O  
ATOM   1691  CB  TYR C  14      59.584  90.465  41.359  1.00105.61           C  
ANISOU 1691  CB  TYR C  14    10259  10091  19778  -1306    337    -22       C  
ATOM   1692  CG  TYR C  14      60.407  91.636  40.869  1.00118.41           C  
ANISOU 1692  CG  TYR C  14    11590  11676  21725  -1430    285    112       C  
ATOM   1693  CD1 TYR C  14      61.513  91.438  40.051  1.00131.50           C  
ANISOU 1693  CD1 TYR C  14    13165  13275  23523  -1636    754      8       C  
ATOM   1694  CD2 TYR C  14      60.085  92.937  41.232  1.00128.73           C  
ANISOU 1694  CD2 TYR C  14    12704  12987  23221  -1356   -204    322       C  
ATOM   1695  CE1 TYR C  14      62.272  92.506  39.604  1.00141.75           C  
ANISOU 1695  CE1 TYR C  14    14205  14556  25095  -1804    722    136       C  
ATOM   1696  CE2 TYR C  14      60.838  94.011  40.790  1.00131.42           C  
ANISOU 1696  CE2 TYR C  14    12812  13256  23864  -1504   -257    461       C  
ATOM   1697  CZ  TYR C  14      61.930  93.790  39.977  1.00137.26           C  
ANISOU 1697  CZ  TYR C  14    13484  13975  24694  -1746    199    381       C  
ATOM   1698  OH  TYR C  14      62.680  94.856  39.536  1.00138.12           O  
ANISOU 1698  OH  TYR C  14    13370  14031  25080  -1947    160    525       O  
ATOM   1699  N   ARG C  15      57.239  87.917  40.721  1.00116.95           N  
ANISOU 1699  N   ARG C  15    12658  11847  19933  -1843    791   -181       N  
ATOM   1700  CA  ARG C  15      56.991  86.526  41.102  1.00108.96           C  
ANISOU 1700  CA  ARG C  15    11950  10720  18729  -1772   1043   -395       C  
ATOM   1701  C   ARG C  15      57.360  85.541  39.994  1.00106.71           C  
ANISOU 1701  C   ARG C  15    11973  10368  18204  -2153   1681   -597       C  
ATOM   1702  O   ARG C  15      58.005  84.524  40.249  1.00 99.31           O  
ANISOU 1702  O   ARG C  15    11130   9122  17480  -1945   2025   -838       O  
ATOM   1703  CB  ARG C  15      55.526  86.323  41.491  1.00108.81           C  
ANISOU 1703  CB  ARG C  15    12137  10948  18256  -1886    763   -308       C  
ATOM   1704  CG  ARG C  15      55.261  85.021  42.236  1.00 89.10           C  
ANISOU 1704  CG  ARG C  15     9924   8298  15632  -1736    899   -493       C  
ATOM   1705  CD  ARG C  15      53.965  84.374  41.777  1.00 99.79           C  
ANISOU 1705  CD  ARG C  15    11650   9921  16344  -2189    987   -486       C  
ATOM   1706  NE  ARG C  15      54.069  83.858  40.415  1.00115.65           N  
ANISOU 1706  NE  ARG C  15    13945  11982  18017  -2707   1467   -573       N  
ATOM   1707  CZ  ARG C  15      53.082  83.247  39.766  1.00121.05           C  
ANISOU 1707  CZ  ARG C  15    14982  12912  18098  -3221   1618   -590       C  
ATOM   1708  NH1 ARG C  15      51.905  83.075  40.352  1.00119.14           N  
ANISOU 1708  NH1 ARG C  15    14816  12894  17559  -3264   1325   -513       N  
ATOM   1709  NH2 ARG C  15      53.271  82.810  38.528  1.00118.39           N  
ANISOU 1709  NH2 ARG C  15    14919  12625  17440  -3733   2077   -704       N  
ATOM   1710  N   ASP C  16      56.943  85.846  38.769  1.00113.17           N  
ANISOU 1710  N   ASP C  16    12951  11464  18584  -2725   1834   -498       N  
ATOM   1711  CA  ASP C  16      57.153  84.949  37.637  1.00124.22           C  
ANISOU 1711  CA  ASP C  16    14698  12864  19637  -3208   2467   -726       C  
ATOM   1712  C   ASP C  16      58.632  84.721  37.350  1.00124.78           C  
ANISOU 1712  C   ASP C  16    14595  12631  20186  -3058   2962   -983       C  
ATOM   1713  O   ASP C  16      59.039  83.622  36.969  1.00127.52           O  
ANISOU 1713  O   ASP C  16    15173  12765  20513  -3154   3539  -1313       O  
ATOM   1714  CB  ASP C  16      56.466  85.501  36.387  1.00144.86           C  
ANISOU 1714  CB  ASP C  16    17484  15895  21659  -3904   2454   -511       C  
ATOM   1715  CG  ASP C  16      54.962  85.599  36.544  1.00158.03           C  
ANISOU 1715  CG  ASP C  16    19298  17891  22855  -4095   2011   -271       C  
ATOM   1716  OD1 ASP C  16      54.375  84.729  37.222  1.00149.24           O  
ANISOU 1716  OD1 ASP C  16    18367  16709  21626  -3941   2004   -411       O  
ATOM   1717  OD2 ASP C  16      54.366  86.546  35.989  1.00173.57           O  
ANISOU 1717  OD2 ASP C  16    21182  20179  24587  -4405   1663     73       O  
ATOM   1718  N   GLU C  17      59.431  85.765  37.541  1.00137.03           N  
ANISOU 1718  N   GLU C  17    15718  14149  22197  -2827   2750   -848       N  
ATOM   1719  CA  GLU C  17      60.856  85.713  37.238  1.00141.10           C  
ANISOU 1719  CA  GLU C  17    15971  14440  23200  -2712   3192  -1068       C  
ATOM   1720  C   GLU C  17      61.613  84.765  38.164  1.00133.19           C  
ANISOU 1720  C   GLU C  17    14830  13015  22760  -2114   3349  -1321       C  
ATOM   1721  O   GLU C  17      62.700  84.297  37.829  1.00139.57           O  
ANISOU 1721  O   GLU C  17    15481  13591  23956  -2026   3860  -1592       O  
ATOM   1722  CB  GLU C  17      61.463  87.116  37.320  1.00139.72           C  
ANISOU 1722  CB  GLU C  17    15360  14344  23383  -2623   2854   -830       C  
ATOM   1723  N   TYR C  18      61.034  84.480  39.326  1.00125.35           N  
ANISOU 1723  N   TYR C  18    13882  11925  21819  -1717   2909  -1221       N  
ATOM   1724  CA  TYR C  18      61.698  83.652  40.326  1.00126.89           C  
ANISOU 1724  CA  TYR C  18    13948  11724  22540  -1142   2921  -1357       C  
ATOM   1725  C   TYR C  18      61.002  82.310  40.525  1.00123.74           C  
ANISOU 1725  C   TYR C  18    14020  11144  21851  -1162   3113  -1494       C  
ATOM   1726  O   TYR C  18      61.579  81.252  40.267  1.00127.37           O  
ANISOU 1726  O   TYR C  18    14598  11257  22540  -1081   3626  -1764       O  
ATOM   1727  CB  TYR C  18      61.778  84.395  41.662  1.00128.46           C  
ANISOU 1727  CB  TYR C  18    13806  11923  23079   -659   2237  -1126       C  
ATOM   1728  CG  TYR C  18      62.787  85.523  41.682  1.00140.14           C  
ANISOU 1728  CG  TYR C  18    14771  13438  25037   -523   2082  -1048       C  
ATOM   1729  CD1 TYR C  18      64.081  85.314  42.144  1.00147.82           C  
ANISOU 1729  CD1 TYR C  18    15341  14139  26684   -105   2162  -1150       C  
ATOM   1730  CD2 TYR C  18      62.449  86.796  41.239  1.00127.75           C  
ANISOU 1730  CD2 TYR C  18    13105  12161  23273   -823   1839   -855       C  
ATOM   1731  CE1 TYR C  18      65.009  86.340  42.166  1.00145.83           C  
ANISOU 1731  CE1 TYR C  18    14604  13943  26861    -27   2023  -1088       C  
ATOM   1732  CE2 TYR C  18      63.370  87.829  41.256  1.00120.27           C  
ANISOU 1732  CE2 TYR C  18    11719  11219  22759   -743   1704   -784       C  
ATOM   1733  CZ  TYR C  18      64.649  87.595  41.721  1.00127.85           C  
ANISOU 1733  CZ  TYR C  18    12285  11945  24349   -364   1807   -916       C  
ATOM   1734  OH  TYR C  18      65.574  88.614  41.742  1.00123.02           O  
ANISOU 1734  OH  TYR C  18    11220  11361  24161   -327   1677   -855       O  
ATOM   1735  N   LEU C  19      59.762  82.366  40.997  1.00113.63           N  
ANISOU 1735  N   LEU C  19    12993  10082  20101  -1271   2713  -1319       N  
ATOM   1736  CA  LEU C  19      59.019  81.165  41.354  1.00106.90           C  
ANISOU 1736  CA  LEU C  19    12583   9079  18954  -1302   2808  -1406       C  
ATOM   1737  C   LEU C  19      57.985  80.780  40.302  1.00104.04           C  
ANISOU 1737  C   LEU C  19    12685   8977  17868  -1965   3109  -1489       C  
ATOM   1738  O   LEU C  19      57.206  81.618  39.844  1.00 93.48           O  
ANISOU 1738  O   LEU C  19    11340   8072  16107  -2329   2865  -1304       O  
ATOM   1739  CB  LEU C  19      58.330  81.362  42.703  1.00103.94           C  
ANISOU 1739  CB  LEU C  19    12176   8786  18530  -1000   2183  -1185       C  
ATOM   1740  CG  LEU C  19      58.525  80.255  43.734  1.00110.50           C  
ANISOU 1740  CG  LEU C  19    13166   9223  19595   -616   2140  -1217       C  
ATOM   1741  CD1 LEU C  19      60.005  79.960  43.918  1.00123.91           C  
ANISOU 1741  CD1 LEU C  19    14550  10491  22039   -158   2323  -1305       C  
ATOM   1742  CD2 LEU C  19      57.888  80.662  45.051  1.00105.46           C  
ANISOU 1742  CD2 LEU C  19    12458   8758  18852   -394   1511   -998       C  
ATOM   1743  N   SER C  20      57.988  79.505  39.923  1.00113.73           N  
ANISOU 1743  N   SER C  20    14311   9923  18978  -2129   3626  -1761       N  
ATOM   1744  CA  SER C  20      56.986  78.971  39.009  1.00105.69           C  
ANISOU 1744  CA  SER C  20    13786   9133  17237  -2798   3920  -1875       C  
ATOM   1745  C   SER C  20      55.650  78.791  39.718  1.00117.17           C  
ANISOU 1745  C   SER C  20    15468  10811  18239  -2889   3480  -1687       C  
ATOM   1746  O   SER C  20      55.598  78.736  40.946  1.00121.30           O  
ANISOU 1746  O   SER C  20    15872  11190  19025  -2423   3089  -1552       O  
ATOM   1747  CB  SER C  20      57.447  77.644  38.418  1.00105.04           C  
ANISOU 1747  CB  SER C  20    14077   8624  17210  -2950   4653  -2282       C  
ATOM   1748  OG  SER C  20      56.448  77.109  37.571  1.00129.73           O  
ANISOU 1748  OG  SER C  20    17713  11990  19590  -3655   4923  -2410       O  
ATOM   1749  N   ASP C  21      54.576  78.704  38.938  1.00125.97           N  
ANISOU 1749  N   ASP C  21    16897  12310  18655  -3528   3545  -1677       N  
ATOM   1750  CA  ASP C  21      53.225  78.568  39.481  1.00129.10           C  
ANISOU 1750  CA  ASP C  21    17467  12999  18586  -3699   3162  -1514       C  
ATOM   1751  C   ASP C  21      53.094  77.376  40.427  1.00128.02           C  
ANISOU 1751  C   ASP C  21    17632  12468  18541  -3459   3231  -1630       C  
ATOM   1752  O   ASP C  21      52.413  77.459  41.448  1.00123.09           O  
ANISOU 1752  O   ASP C  21    16959  11966  17844  -3275   2796  -1457       O  
ATOM   1753  CB  ASP C  21      52.205  78.441  38.347  1.00133.42           C  
ANISOU 1753  CB  ASP C  21    18332  13988  18374  -4491   3312  -1527       C  
ATOM   1754  CG  ASP C  21      52.188  79.654  37.439  1.00137.70           C  
ANISOU 1754  CG  ASP C  21    18604  14956  18761  -4782   3142  -1313       C  
ATOM   1755  OD1 ASP C  21      52.495  80.764  37.922  1.00127.65           O  
ANISOU 1755  OD1 ASP C  21    16874  13746  17881  -4371   2719  -1074       O  
ATOM   1756  OD2 ASP C  21      51.869  79.498  36.241  1.00141.95           O  
ANISOU 1756  OD2 ASP C  21    19408  15758  18767  -5455   3423  -1375       O  
ATOM   1757  N   GLU C  22      53.746  76.270  40.082  1.00135.03           N  
ANISOU 1757  N   GLU C  22    18838  12869  19599  -3478   3795  -1929       N  
ATOM   1758  CA  GLU C  22      53.701  75.063  40.902  1.00135.28           C  
ANISOU 1758  CA  GLU C  22    19205  12430  19766  -3264   3888  -2015       C  
ATOM   1759  C   GLU C  22      54.402  75.282  42.238  1.00118.53           C  
ANISOU 1759  C   GLU C  22    16743  10019  18274  -2519   3476  -1817       C  
ATOM   1760  O   GLU C  22      53.824  75.044  43.298  1.00127.47           O  
ANISOU 1760  O   GLU C  22    17970  11161  19301  -2376   3103  -1645       O  
ATOM   1761  CB  GLU C  22      54.337  73.881  40.165  1.00156.20           C  
ANISOU 1761  CB  GLU C  22    22240  14543  22565  -3411   4619  -2402       C  
ATOM   1762  CG  GLU C  22      53.696  73.543  38.824  1.00172.00           C  
ANISOU 1762  CG  GLU C  22    24651  16812  23890  -4230   5087  -2657       C  
ATOM   1763  CD  GLU C  22      54.163  74.451  37.699  1.00180.76           C  
ANISOU 1763  CD  GLU C  22    25501  18258  24921  -4497   5277  -2715       C  
ATOM   1764  OE1 GLU C  22      55.045  75.302  37.944  1.00174.40           O  
ANISOU 1764  OE1 GLU C  22    24195  17425  24642  -4025   5092  -2586       O  
ATOM   1765  OE2 GLU C  22      53.647  74.314  36.569  1.00186.30           O  
ANISOU 1765  OE2 GLU C  22    26512  19267  25006  -5226   5599  -2880       O  
ATOM   1766  N   GLU C  23      55.650  75.736  42.172  1.00108.44           N  
ANISOU 1766  N   GLU C  23    15068   8516  17619  -2095   3549  -1844       N  
ATOM   1767  CA  GLU C  23      56.442  76.029  43.361  1.00 98.69           C  
ANISOU 1767  CA  GLU C  23    13453   7045  16998  -1418   3137  -1649       C  
ATOM   1768  C   GLU C  23      55.715  77.016  44.264  1.00103.08           C  
ANISOU 1768  C   GLU C  23    13773   8063  17328  -1337   2468  -1359       C  
ATOM   1769  O   GLU C  23      55.783  76.923  45.489  1.00108.27           O  
ANISOU 1769  O   GLU C  23    14362   8603  18174   -969   2071  -1189       O  
ATOM   1770  CB  GLU C  23      57.809  76.593  42.967  1.00105.08           C  
ANISOU 1770  CB  GLU C  23    13792   7692  18444  -1090   3308  -1726       C  
ATOM   1771  CG  GLU C  23      58.589  75.731  41.984  1.00121.83           C  
ANISOU 1771  CG  GLU C  23    16068   9385  20835  -1177   4051  -2082       C  
ATOM   1772  CD  GLU C  23      59.727  76.486  41.315  1.00142.82           C  
ANISOU 1772  CD  GLU C  23    18246  12076  23944  -1055   4286  -2194       C  
ATOM   1773  OE1 GLU C  23      60.754  75.852  40.990  1.00155.23           O  
ANISOU 1773  OE1 GLU C  23    19724  13188  26069   -825   4780  -2450       O  
ATOM   1774  OE2 GLU C  23      59.591  77.710  41.105  1.00141.51           O  
ANISOU 1774  OE2 GLU C  23    17787  12378  23601  -1197   3992  -2031       O  
ATOM   1775  N   TYR C  24      55.010  77.953  43.641  1.00102.17           N  
ANISOU 1775  N   TYR C  24    13540   8471  16808  -1702   2351  -1307       N  
ATOM   1776  CA  TYR C  24      54.296  79.001  44.359  1.00 96.35           C  
ANISOU 1776  CA  TYR C  24    12531   8166  15910  -1632   1774  -1083       C  
ATOM   1777  C   TYR C  24      53.028  78.462  45.014  1.00 86.26           C  
ANISOU 1777  C   TYR C  24    11567   7080  14127  -1850   1588  -1031       C  
ATOM   1778  O   TYR C  24      52.658  78.878  46.108  1.00 84.08           O  
ANISOU 1778  O   TYR C  24    11133   6962  13853  -1632   1152   -898       O  
ATOM   1779  CB  TYR C  24      53.967  80.151  43.403  1.00 85.94           C  
ANISOU 1779  CB  TYR C  24    10976   7282  14393  -1939   1714  -1015       C  
ATOM   1780  CG  TYR C  24      53.237  81.311  44.036  1.00 82.51           C  
ANISOU 1780  CG  TYR C  24    10225   7245  13882  -1846   1157   -811       C  
ATOM   1781  CD1 TYR C  24      53.711  81.907  45.194  1.00 92.97           C  
ANISOU 1781  CD1 TYR C  24    11225   8480  15619  -1353    767   -730       C  
ATOM   1782  CD2 TYR C  24      52.081  81.823  43.461  1.00 94.90           C  
ANISOU 1782  CD2 TYR C  24    11798   9271  14989  -2261   1024   -710       C  
ATOM   1783  CE1 TYR C  24      53.048  82.974  45.772  1.00 94.93           C  
ANISOU 1783  CE1 TYR C  24    11190   9052  15826  -1273    317   -611       C  
ATOM   1784  CE2 TYR C  24      51.413  82.888  44.028  1.00 91.13           C  
ANISOU 1784  CE2 TYR C  24    10992   9104  14529  -2133    548   -552       C  
ATOM   1785  CZ  TYR C  24      51.900  83.461  45.184  1.00 92.52           C  
ANISOU 1785  CZ  TYR C  24    10874   9151  15127  -1638    225   -532       C  
ATOM   1786  OH  TYR C  24      51.233  84.524  45.751  1.00 88.85           O  
ANISOU 1786  OH  TYR C  24    10093   8960  14707  -1517   -193   -439       O  
ATOM   1787  N   ARG C  25      52.367  77.535  44.333  1.00 88.22           N  
ANISOU 1787  N   ARG C  25    12265   7331  13923  -2327   1948  -1162       N  
ATOM   1788  CA  ARG C  25      51.182  76.872  44.864  1.00 99.65           C  
ANISOU 1788  CA  ARG C  25    14050   8944  14871  -2612   1848  -1139       C  
ATOM   1789  C   ARG C  25      51.567  76.045  46.091  1.00 93.92           C  
ANISOU 1789  C   ARG C  25    13506   7785  14393  -2245   1743  -1090       C  
ATOM   1790  O   ARG C  25      50.888  76.066  47.130  1.00 87.68           O  
ANISOU 1790  O   ARG C  25    12738   7186  13393  -2217   1399   -968       O  
ATOM   1791  CB  ARG C  25      50.552  75.998  43.776  1.00 99.71           C  
ANISOU 1791  CB  ARG C  25    14521   8992  14370  -3241   2304  -1317       C  
ATOM   1792  CG  ARG C  25      49.309  75.230  44.172  1.00105.60           C  
ANISOU 1792  CG  ARG C  25    15642   9919  14561  -3641   2263  -1317       C  
ATOM   1793  CD  ARG C  25      48.846  74.375  42.999  1.00117.72           C  
ANISOU 1793  CD  ARG C  25    17643  11461  15624  -4296   2747  -1528       C  
ATOM   1794  NE  ARG C  25      47.792  73.433  43.363  1.00139.02           N  
ANISOU 1794  NE  ARG C  25    20768  14228  17827  -4709   2785  -1563       N  
ATOM   1795  CZ  ARG C  25      47.300  72.512  42.540  1.00150.56           C  
ANISOU 1795  CZ  ARG C  25    22715  15654  18837  -5323   3196  -1766       C  
ATOM   1796  NH1 ARG C  25      47.770  72.407  41.303  1.00139.91           N  
ANISOU 1796  NH1 ARG C  25    21496  14215  17450  -5601   3620  -1972       N  
ATOM   1797  NH2 ARG C  25      46.339  71.693  42.953  1.00155.08           N  
ANISOU 1797  NH2 ARG C  25    23656  16295  18971  -5708   3201  -1782       N  
ATOM   1798  N   LEU C  26      52.679  75.329  45.952  1.00 92.15           N  
ANISOU 1798  N   LEU C  26    13399   6982  14634  -1974   2045  -1179       N  
ATOM   1799  CA  LEU C  26      53.276  74.580  47.047  1.00 94.12           C  
ANISOU 1799  CA  LEU C  26    13770   6741  15249  -1556   1908  -1068       C  
ATOM   1800  C   LEU C  26      53.610  75.510  48.199  1.00 91.53           C  
ANISOU 1800  C   LEU C  26    13005   6591  15182  -1118   1335   -846       C  
ATOM   1801  O   LEU C  26      53.377  75.178  49.355  1.00100.89           O  
ANISOU 1801  O   LEU C  26    14320   7729  16286  -1001   1016   -684       O  
ATOM   1802  CB  LEU C  26      54.534  73.851  46.571  1.00109.29           C  
ANISOU 1802  CB  LEU C  26    15742   8013  17771  -1265   2325  -1203       C  
ATOM   1803  CG  LEU C  26      55.370  73.101  47.609  1.00108.94           C  
ANISOU 1803  CG  LEU C  26    15742   7383  18269   -748   2156  -1035       C  
ATOM   1804  CD1 LEU C  26      54.586  71.948  48.212  1.00103.49           C  
ANISOU 1804  CD1 LEU C  26    15634   6467  17220   -979   2144   -950       C  
ATOM   1805  CD2 LEU C  26      56.665  72.606  46.985  1.00105.90           C  
ANISOU 1805  CD2 LEU C  26    15241   6407  18589   -414   2592  -1203       C  
ATOM   1806  N   PHE C  27      54.148  76.681  47.871  1.00 89.49           N  
ANISOU 1806  N   PHE C  27    12256   6543  15202   -930   1214   -847       N  
ATOM   1807  CA  PHE C  27      54.483  77.692  48.868  1.00 87.24           C  
ANISOU 1807  CA  PHE C  27    11540   6445  15161   -565    695   -688       C  
ATOM   1808  C   PHE C  27      53.245  78.146  49.636  1.00 84.54           C  
ANISOU 1808  C   PHE C  27    11226   6586  14310   -777    342   -623       C  
ATOM   1809  O   PHE C  27      53.278  78.294  50.859  1.00 84.25           O  
ANISOU 1809  O   PHE C  27    11119   6591  14300   -569    -40   -507       O  
ATOM   1810  CB  PHE C  27      55.162  78.887  48.194  1.00 85.82           C  
ANISOU 1810  CB  PHE C  27    10875   6410  15322   -433    689   -726       C  
ATOM   1811  CG  PHE C  27      55.321  80.085  49.087  1.00 86.38           C  
ANISOU 1811  CG  PHE C  27    10518   6732  15570   -163    178   -611       C  
ATOM   1812  CD1 PHE C  27      56.340  80.138  50.023  1.00 84.65           C  
ANISOU 1812  CD1 PHE C  27    10073   6271  15817    273   -104   -507       C  
ATOM   1813  CD2 PHE C  27      54.459  81.168  48.978  1.00100.20           C  
ANISOU 1813  CD2 PHE C  27    12080   8947  17045   -356    -27   -612       C  
ATOM   1814  CE1 PHE C  27      56.490  81.243  50.842  1.00 95.54           C  
ANISOU 1814  CE1 PHE C  27    11090   7886  17324    462   -556   -442       C  
ATOM   1815  CE2 PHE C  27      54.604  82.276  49.793  1.00 78.75           C  
ANISOU 1815  CE2 PHE C  27     8992   6410  14518   -120   -452   -561       C  
ATOM   1816  CZ  PHE C  27      55.620  82.314  50.726  1.00 79.89           C  
ANISOU 1816  CZ  PHE C  27     8957   6329  15070    264   -704   -495       C  
ATOM   1817  N   GLN C  28      52.156  78.366  48.908  1.00 83.11           N  
ANISOU 1817  N   GLN C  28    11129   6788  13660  -1213    477   -706       N  
ATOM   1818  CA  GLN C  28      50.899  78.770  49.518  1.00 81.18           C  
ANISOU 1818  CA  GLN C  28    10860   7024  12960  -1435    209   -685       C  
ATOM   1819  C   GLN C  28      50.383  77.688  50.454  1.00 92.27           C  
ANISOU 1819  C   GLN C  28    12685   8333  14041  -1566    178   -645       C  
ATOM   1820  O   GLN C  28      49.863  77.989  51.525  1.00 82.02           O  
ANISOU 1820  O   GLN C  28    11316   7295  12554  -1546   -131   -605       O  
ATOM   1821  CB  GLN C  28      49.850  79.081  48.450  1.00 80.29           C  
ANISOU 1821  CB  GLN C  28    10742   7321  12443  -1895    364   -748       C  
ATOM   1822  CG  GLN C  28      50.122  80.343  47.654  1.00101.21           C  
ANISOU 1822  CG  GLN C  28    12961  10159  15335  -1822    283   -718       C  
ATOM   1823  CD  GLN C  28      49.037  80.628  46.635  1.00112.24           C  
ANISOU 1823  CD  GLN C  28    14353  11980  16313  -2299    358   -707       C  
ATOM   1824  OE1 GLN C  28      48.326  79.722  46.202  1.00123.68           O  
ANISOU 1824  OE1 GLN C  28    16165  13514  17312  -2729    595   -764       O  
ATOM   1825  NE2 GLN C  28      48.898  81.892  46.253  1.00108.45           N  
ANISOU 1825  NE2 GLN C  28    13460  11761  15984  -2244    129   -612       N  
ATOM   1826  N   ALA C  29      50.530  76.428  50.053  1.00104.11           N  
ANISOU 1826  N   ALA C  29    14642   9446  15471  -1728    519   -671       N  
ATOM   1827  CA  ALA C  29      50.109  75.319  50.906  1.00 87.85           C  
ANISOU 1827  CA  ALA C  29    13041   7210  13127  -1875    498   -594       C  
ATOM   1828  C   ALA C  29      50.946  75.241  52.187  1.00 89.05           C  
ANISOU 1828  C   ALA C  29    13138   7083  13613  -1437    140   -399       C  
ATOM   1829  O   ALA C  29      50.408  75.180  53.299  1.00 89.21           O  
ANISOU 1829  O   ALA C  29    13262   7310  13323  -1526   -145   -300       O  
ATOM   1830  CB  ALA C  29      50.189  74.010  50.142  1.00 91.19           C  
ANISOU 1830  CB  ALA C  29    13974   7181  13493  -2120    960   -676       C  
ATOM   1831  N   GLU C  30      52.265  75.249  52.011  1.00 91.57           N  
ANISOU 1831  N   GLU C  30    13276   6966  14550   -996    157   -345       N  
ATOM   1832  CA  GLU C  30      53.218  75.162  53.114  1.00 93.43           C  
ANISOU 1832  CA  GLU C  30    13408   6912  15178   -562   -212   -122       C  
ATOM   1833  C   GLU C  30      52.997  76.265  54.131  1.00 89.81           C  
ANISOU 1833  C   GLU C  30    12611   6930  14581   -481   -688    -70       C  
ATOM   1834  O   GLU C  30      52.991  76.022  55.337  1.00101.57           O  
ANISOU 1834  O   GLU C  30    14233   8428  15929   -445  -1030    107       O  
ATOM   1835  CB  GLU C  30      54.653  75.234  52.589  1.00 94.77           C  
ANISOU 1835  CB  GLU C  30    13277   6642  16088   -105   -102   -115       C  
ATOM   1836  CG  GLU C  30      55.076  74.058  51.725  1.00116.20           C  
ANISOU 1836  CG  GLU C  30    16314   8776  19061   -106    396   -198       C  
ATOM   1837  CD  GLU C  30      55.715  72.947  52.526  1.00129.65           C  
ANISOU 1837  CD  GLU C  30    18279   9879  21101    181    259     49       C  
ATOM   1838  OE1 GLU C  30      55.772  73.071  53.768  1.00141.70           O  
ANISOU 1838  OE1 GLU C  30    19772  11500  22567    317   -255    320       O  
ATOM   1839  OE2 GLU C  30      56.167  71.955  51.914  1.00133.50           O  
ANISOU 1839  OE2 GLU C  30    19010   9791  21923    258    663    -25       O  
ATOM   1840  N   LEU C  31      52.815  77.481  53.630  1.00 86.45           N  
ANISOU 1840  N   LEU C  31    11769   6887  14191   -481   -702   -228       N  
ATOM   1841  CA  LEU C  31      52.601  78.634  54.490  1.00 84.41           C  
ANISOU 1841  CA  LEU C  31    11164   7048  13860   -403  -1094   -251       C  
ATOM   1842  C   LEU C  31      51.211  78.577  55.113  1.00 83.78           C  
ANISOU 1842  C   LEU C  31    11286   7408  13138   -795  -1152   -324       C  
ATOM   1843  O   LEU C  31      50.988  79.088  56.210  1.00 83.74           O  
ANISOU 1843  O   LEU C  31    11172   7677  12969   -786  -1464   -336       O  
ATOM   1844  CB  LEU C  31      52.786  79.927  53.697  1.00 85.68           C  
ANISOU 1844  CB  LEU C  31    10845   7413  14296   -294  -1069   -388       C  
ATOM   1845  CG  LEU C  31      53.003  81.228  54.467  1.00 80.22           C  
ANISOU 1845  CG  LEU C  31     9727   6982  13771    -93  -1454   -432       C  
ATOM   1846  CD1 LEU C  31      54.224  81.131  55.363  1.00 82.40           C  
ANISOU 1846  CD1 LEU C  31     9904   6987  14417    249  -1762   -279       C  
ATOM   1847  CD2 LEU C  31      53.156  82.373  53.491  1.00 78.05           C  
ANISOU 1847  CD2 LEU C  31     9053   6817  13785    -29  -1376   -530       C  
HETATM 1848  N   MSE C  32      50.279  77.946  54.406  1.00 88.11           N  
ANISOU 1848  N   MSE C  32    12123   8044  13312  -1176   -829   -399       N  
HETATM 1849  CA  MSE C  32      48.919  77.792  54.906  1.00 86.14           C  
ANISOU 1849  CA  MSE C  32    12044   8228  12456  -1592   -832   -479       C  
HETATM 1850  C   MSE C  32      48.886  76.904  56.140  1.00100.43           C  
ANISOU 1850  C   MSE C  32    14255   9918  13986  -1694   -998   -324       C  
HETATM 1851  O   MSE C  32      48.250  77.241  57.136  1.00115.62           O  
ANISOU 1851  O   MSE C  32    16141  12231  15560  -1855  -1193   -378       O  
HETATM 1852  CB  MSE C  32      48.004  77.217  53.823  1.00 83.63           C  
ANISOU 1852  CB  MSE C  32    11956   8016  11804  -2019   -459   -569       C  
HETATM 1853  CG  MSE C  32      46.542  77.128  54.226  1.00 92.03           C  
ANISOU 1853  CG  MSE C  32    13104   9593  12270  -2475   -442   -670       C  
HETATM 1854 SE   MSE C  32      45.382  76.667  52.727  1.00224.88          SE  
ANISOU 1854 SE   MSE C  32    30077  26669  28698  -3043    -43   -783      SE  
HETATM 1855  CE  MSE C  32      46.034  74.857  52.386  1.00179.83           C  
ANISOU 1855  CE  MSE C  32    25126  20238  22965  -3195    299   -682       C  
ATOM   1856  N   LEU C  33      49.578  75.771  56.076  1.00 89.40           N  
ANISOU 1856  N   LEU C  33    13244   7971  12753  -1613   -911   -131       N  
ATOM   1857  CA  LEU C  33      49.568  74.836  57.197  1.00 92.93           C  
ANISOU 1857  CA  LEU C  33    14129   8239  12943  -1734  -1097     95       C  
ATOM   1858  C   LEU C  33      50.351  75.366  58.394  1.00 93.93           C  
ANISOU 1858  C   LEU C  33    14051   8390  13249  -1429  -1573    257       C  
ATOM   1859  O   LEU C  33      49.976  75.129  59.542  1.00 96.04           O  
ANISOU 1859  O   LEU C  33    14547   8847  13097  -1653  -1813    370       O  
ATOM   1860  CB  LEU C  33      50.118  73.475  56.770  1.00 96.42           C  
ANISOU 1860  CB  LEU C  33    15035   7999  13601  -1693   -885    277       C  
ATOM   1861  CG  LEU C  33      49.044  72.501  56.276  1.00 97.64           C  
ANISOU 1861  CG  LEU C  33    15683   8153  13263  -2230   -513    193       C  
ATOM   1862  CD1 LEU C  33      48.437  72.952  54.954  1.00113.42           C  
ANISOU 1862  CD1 LEU C  33    17480  10439  15175  -2437   -150   -103       C  
ATOM   1863  CD2 LEU C  33      49.605  71.105  56.156  1.00102.78           C  
ANISOU 1863  CD2 LEU C  33    16859   8055  14136  -2186   -355    391       C  
ATOM   1864  N   ASN C  34      51.438  76.080  58.127  1.00 92.84           N  
ANISOU 1864  N   ASN C  34    13490   8086  13698   -972  -1708    265       N  
ATOM   1865  CA  ASN C  34      52.192  76.737  59.190  1.00 93.75           C  
ANISOU 1865  CA  ASN C  34    13345   8288  13987   -715  -2175    382       C  
ATOM   1866  C   ASN C  34      52.367  78.224  58.922  1.00100.96           C  
ANISOU 1866  C   ASN C  34    13680   9525  15153   -523  -2244    134       C  
ATOM   1867  O   ASN C  34      53.306  78.626  58.239  1.00 99.29           O  
ANISOU 1867  O   ASN C  34    13149   9070  15507   -177  -2212    137       O  
ATOM   1868  CB  ASN C  34      53.560  76.085  59.374  1.00 97.31           C  
ANISOU 1868  CB  ASN C  34    13834   8155  14984   -317  -2382    711       C  
ATOM   1869  CG  ASN C  34      54.320  76.660  60.555  1.00 99.10           C  
ANISOU 1869  CG  ASN C  34    13827   8506  15319   -126  -2927    882       C  
ATOM   1870  OD1 ASN C  34      53.749  77.360  61.395  1.00 98.31           O  
ANISOU 1870  OD1 ASN C  34    13670   8906  14779   -363  -3134    754       O  
ATOM   1871  ND2 ASN C  34      55.611  76.361  60.630  1.00102.05           N  
ANISOU 1871  ND2 ASN C  34    14052   8437  16287    285  -3155   1154       N  
ATOM   1872  N   PRO C  35      51.453  79.047  59.456  1.00 98.78           N  
ANISOU 1872  N   PRO C  35    13267   9786  14480   -759  -2314    -95       N  
ATOM   1873  CA  PRO C  35      51.496  80.502  59.269  1.00 97.42           C  
ANISOU 1873  CA  PRO C  35    12571   9893  14550   -598  -2381   -345       C  
ATOM   1874  C   PRO C  35      52.772  81.119  59.835  1.00 87.59           C  
ANISOU 1874  C   PRO C  35    11036   8502  13744   -251  -2751   -251       C  
ATOM   1875  O   PRO C  35      53.290  82.092  59.290  1.00 85.07           O  
ANISOU 1875  O   PRO C  35    10300   8160  13861    -11  -2760   -365       O  
ATOM   1876  CB  PRO C  35      50.266  80.993  60.041  1.00 97.97           C  
ANISOU 1876  CB  PRO C  35    12635  10505  14082   -936  -2396   -595       C  
ATOM   1877  CG  PRO C  35      49.378  79.790  60.159  1.00101.63           C  
ANISOU 1877  CG  PRO C  35    13588  11018  14009  -1331  -2202   -510       C  
ATOM   1878  CD  PRO C  35      50.308  78.631  60.283  1.00 93.89           C  
ANISOU 1878  CD  PRO C  35    12978   9521  13176  -1208  -2306   -147       C  
ATOM   1879  N   LYS C  36      53.280  80.530  60.910  1.00 90.44           N  
ANISOU 1879  N   LYS C  36    11624   8763  13975   -257  -3075    -14       N  
ATOM   1880  CA  LYS C  36      54.439  81.059  61.615  1.00 92.29           C  
ANISOU 1880  CA  LYS C  36    11595   8929  14542     -1  -3498    102       C  
ATOM   1881  C   LYS C  36      55.746  80.509  61.053  1.00100.24           C  
ANISOU 1881  C   LYS C  36    12492   9407  16186    394  -3547    390       C  
ATOM   1882  O   LYS C  36      56.811  80.707  61.639  1.00109.54           O  
ANISOU 1882  O   LYS C  36    13460  10480  17681    617  -3932    570       O  
ATOM   1883  CB  LYS C  36      54.329  80.760  63.109  1.00102.75           C  
ANISOU 1883  CB  LYS C  36    13200  10473  15368   -255  -3881    239       C  
ATOM   1884  CG  LYS C  36      53.151  81.451  63.776  1.00104.76           C  
ANISOU 1884  CG  LYS C  36    13480  11287  15036   -640  -3815   -122       C  
ATOM   1885  CD  LYS C  36      53.177  81.262  65.280  1.00123.43           C  
ANISOU 1885  CD  LYS C  36    16108  13908  16883   -939  -4197    -13       C  
ATOM   1886  CE  LYS C  36      52.061  82.042  65.954  1.00128.13           C  
ANISOU 1886  CE  LYS C  36    16673  15073  16937  -1319  -4068   -461       C  
ATOM   1887  NZ  LYS C  36      52.121  81.913  67.436  1.00135.50           N  
ANISOU 1887  NZ  LYS C  36    17879  16305  17301  -1683  -4421   -391       N  
ATOM   1888  N   LEU C  37      55.646  79.793  59.935  1.00 92.96           N  
ANISOU 1888  N   LEU C  37    11708   8169  15444    454  -3144    415       N  
ATOM   1889  CA  LEU C  37      56.794  79.158  59.284  1.00 94.99           C  
ANISOU 1889  CA  LEU C  37    11873   7891  16329    817  -3064    621       C  
ATOM   1890  C   LEU C  37      57.990  80.089  59.096  1.00 94.86           C  
ANISOU 1890  C   LEU C  37    11290   7822  16931   1170  -3240    599       C  
ATOM   1891  O   LEU C  37      59.121  79.732  59.426  1.00 98.43           O  
ANISOU 1891  O   LEU C  37    11586   7974  17838   1471  -3499    854       O  
ATOM   1892  CB  LEU C  37      56.374  78.595  57.926  1.00 93.39           C  
ANISOU 1892  CB  LEU C  37    11837   7465  16182    750  -2500    491       C  
ATOM   1893  CG  LEU C  37      57.401  77.733  57.192  1.00108.52           C  
ANISOU 1893  CG  LEU C  37    13743   8787  18701   1070  -2280    630       C  
ATOM   1894  CD1 LEU C  37      58.024  76.717  58.137  1.00109.74           C  
ANISOU 1894  CD1 LEU C  37    14121   8563  19013   1250  -2617   1009       C  
ATOM   1895  CD2 LEU C  37      56.745  77.033  56.014  1.00105.87           C  
ANISOU 1895  CD2 LEU C  37    13725   8282  18218    854  -1707    465       C  
ATOM   1896  N   GLY C  38      57.741  81.275  58.555  1.00 94.48           N  
ANISOU 1896  N   GLY C  38    10920   8052  16926   1127  -3110    312       N  
ATOM   1897  CA  GLY C  38      58.786  82.271  58.428  1.00 91.13           C  
ANISOU 1897  CA  GLY C  38     9974   7621  17031   1384  -3281    269       C  
ATOM   1898  C   GLY C  38      59.164  82.805  59.796  1.00106.49           C  
ANISOU 1898  C   GLY C  38    11792   9794  18877   1376  -3830    341       C  
ATOM   1899  O   GLY C  38      58.295  83.052  60.633  1.00 92.80           O  
ANISOU 1899  O   GLY C  38    10266   8402  16592   1094  -3978    232       O  
ATOM   1900  N   ASP C  39      60.460  82.971  60.034  1.00113.59           N  
ANISOU 1900  N   ASP C  39    12338  10527  20295   1654  -4124    509       N  
ATOM   1901  CA  ASP C  39      60.929  83.480  61.317  1.00122.71           C  
ANISOU 1901  CA  ASP C  39    13356  11914  21354   1607  -4685    593       C  
ATOM   1902  C   ASP C  39      60.947  85.004  61.313  1.00111.81           C  
ANISOU 1902  C   ASP C  39    11614  10824  20044   1528  -4742    268       C  
ATOM   1903  O   ASP C  39      61.294  85.625  60.308  1.00106.07           O  
ANISOU 1903  O   ASP C  39    10568   9989  19745   1666  -4485    131       O  
ATOM   1904  CB  ASP C  39      62.319  82.931  61.641  1.00147.77           C  
ANISOU 1904  CB  ASP C  39    16285  14796  25065   1924  -5039    961       C  
ATOM   1905  CG  ASP C  39      62.779  83.300  63.037  1.00168.03           C  
ANISOU 1905  CG  ASP C  39    18769  17633  27442   1807  -5684   1113       C  
ATOM   1906  OD1 ASP C  39      61.911  83.552  63.901  1.00171.89           O  
ANISOU 1906  OD1 ASP C  39    19568  18479  27263   1446  -5830    989       O  
ATOM   1907  OD2 ASP C  39      64.006  83.338  63.272  1.00175.69           O  
ANISOU 1907  OD2 ASP C  39    19351  18483  28920   2047  -6038   1344       O  
ATOM   1908  N   VAL C  40      60.570  85.597  62.442  1.00115.45           N  
ANISOU 1908  N   VAL C  40    12151  11640  20073   1275  -5063    136       N  
ATOM   1909  CA  VAL C  40      60.479  87.049  62.553  1.00107.73           C  
ANISOU 1909  CA  VAL C  40    10888  10905  19140   1170  -5107   -218       C  
ATOM   1910  C   VAL C  40      61.837  87.727  62.423  1.00101.68           C  
ANISOU 1910  C   VAL C  40     9629  10021  18983   1373  -5345   -160       C  
ATOM   1911  O   VAL C  40      62.837  87.265  62.972  1.00101.30           O  
ANISOU 1911  O   VAL C  40     9455   9896  19136   1490  -5723    135       O  
ATOM   1912  CB  VAL C  40      59.836  87.478  63.892  1.00104.45           C  
ANISOU 1912  CB  VAL C  40    10679  10888  18118    821  -5376   -422       C  
ATOM   1913  CG1 VAL C  40      58.357  87.126  63.905  1.00 99.42           C  
ANISOU 1913  CG1 VAL C  40    10428  10435  16912    581  -5051   -600       C  
ATOM   1914  CG2 VAL C  40      60.558  86.837  65.073  1.00112.81           C  
ANISOU 1914  CG2 VAL C  40    11861  12016  18987    743  -5903    -94       C  
ATOM   1915  N   ILE C  41      61.866  88.828  61.682  1.00108.49           N  
ANISOU 1915  N   ILE C  41    10198  10868  20155   1403  -5138   -418       N  
ATOM   1916  CA  ILE C  41      63.072  89.634  61.581  1.00117.39           C  
ANISOU 1916  CA  ILE C  41    10854  11926  21822   1517  -5343   -417       C  
ATOM   1917  C   ILE C  41      63.229  90.434  62.865  1.00118.70           C  
ANISOU 1917  C   ILE C  41    10970  12379  21751   1282  -5791   -584       C  
ATOM   1918  O   ILE C  41      62.299  91.120  63.292  1.00106.48           O  
ANISOU 1918  O   ILE C  41     9595  11038  19825   1048  -5729   -918       O  
ATOM   1919  CB  ILE C  41      63.029  90.574  60.368  1.00 98.96           C  
ANISOU 1919  CB  ILE C  41     8276   9467  19855   1561  -4974   -614       C  
ATOM   1920  CG1 ILE C  41      62.716  89.778  59.105  1.00 91.01           C  
ANISOU 1920  CG1 ILE C  41     7386   8240  18955   1697  -4507   -492       C  
ATOM   1921  CG2 ILE C  41      64.356  91.291  60.207  1.00103.51           C  
ANISOU 1921  CG2 ILE C  41     8606   9993  20732   1538  -4954   -588       C  
ATOM   1922  CD1 ILE C  41      63.719  88.684  58.839  1.00 93.62           C  
ANISOU 1922  CD1 ILE C  41     7698   8359  19515   1881  -4420   -197       C  
ATOM   1923  N   GLN C  42      64.401  90.330  63.486  1.00122.69           N  
ANISOU 1923  N   GLN C  42    11228  12903  22484   1330  -6235   -364       N  
ATOM   1924  CA  GLN C  42      64.637  90.967  64.774  1.00121.31           C  
ANISOU 1924  CA  GLN C  42    11038  13034  22021   1043  -6709   -492       C  
ATOM   1925  C   GLN C  42      64.461  92.478  64.677  1.00138.72           C  
ANISOU 1925  C   GLN C  42    13081  15310  24314    870  -6585   -946       C  
ATOM   1926  O   GLN C  42      65.093  93.137  63.852  1.00151.15           O  
ANISOU 1926  O   GLN C  42    14459  16697  26272    971  -6282   -973       O  
ATOM   1927  CB  GLN C  42      66.038  90.629  65.288  1.00112.62           C  
ANISOU 1927  CB  GLN C  42     9732  11939  21120   1105  -7078   -134       C  
ATOM   1928  N   GLY C  43      63.591  93.018  65.523  1.00128.71           N  
ANISOU 1928  N   GLY C  43    12063  14298  22544    562  -6636  -1302       N  
ATOM   1929  CA  GLY C  43      63.383  94.451  65.584  1.00127.13           C  
ANISOU 1929  CA  GLY C  43    11726  14125  22453    393  -6553  -1769       C  
ATOM   1930  C   GLY C  43      62.365  95.001  64.604  1.00127.39           C  
ANISOU 1930  C   GLY C  43    11796  13978  22630    502  -6044  -2025       C  
ATOM   1931  O   GLY C  43      62.132  96.208  64.570  1.00145.44           O  
ANISOU 1931  O   GLY C  43    13968  16206  25086    405  -5953  -2397       O  
ATOM   1932  N   THR C  44      61.760  94.132  63.800  1.00122.34           N  
ANISOU 1932  N   THR C  44    11311  13232  21939    690  -5730  -1817       N  
ATOM   1933  CA  THR C  44      60.736  94.575  62.856  1.00117.11           C  
ANISOU 1933  CA  THR C  44    10680  12443  21372    767  -5294  -2000       C  
ATOM   1934  C   THR C  44      59.325  94.402  63.407  1.00109.61           C  
ANISOU 1934  C   THR C  44    10054  11725  19866    602  -5122  -2259       C  
ATOM   1935  O   THR C  44      58.352  94.817  62.778  1.00 94.65           O  
ANISOU 1935  O   THR C  44     8160   9777  18025    646  -4804  -2435       O  
ATOM   1936  CB  THR C  44      60.832  93.822  61.524  1.00122.68           C  
ANISOU 1936  CB  THR C  44    11353  12923  22337   1008  -5006  -1667       C  
ATOM   1937  OG1 THR C  44      60.747  92.412  61.766  1.00134.83           O  
ANISOU 1937  OG1 THR C  44    13158  14524  23548   1044  -5026  -1389       O  
ATOM   1938  CG2 THR C  44      62.143  94.141  60.825  1.00128.02           C  
ANISOU 1938  CG2 THR C  44    11749  13375  23519   1130  -4992  -1473       C  
ATOM   1939  N   GLY C  45      59.222  93.794  64.584  1.00119.02           N  
ANISOU 1939  N   GLY C  45    11502  13192  20527    390  -5344  -2265       N  
ATOM   1940  CA  GLY C  45      57.943  93.624  65.249  1.00123.11           C  
ANISOU 1940  CA  GLY C  45    12319  13988  20468    164  -5176  -2544       C  
ATOM   1941  C   GLY C  45      56.900  92.844  64.467  1.00125.58           C  
ANISOU 1941  C   GLY C  45    12808  14284  20623    253  -4807  -2423       C  
ATOM   1942  O   GLY C  45      55.795  93.336  64.242  1.00116.43           O  
ANISOU 1942  O   GLY C  45    11634  13198  19406    218  -4512  -2728       O  
ATOM   1943  N   GLY C  46      57.244  91.628  64.054  1.00120.95           N  
ANISOU 1943  N   GLY C  46    12371  13590  19993    363  -4822  -1988       N  
ATOM   1944  CA  GLY C  46      56.285  90.751  63.404  1.00116.33           C  
ANISOU 1944  CA  GLY C  46    12014  13008  19179    373  -4491  -1870       C  
ATOM   1945  C   GLY C  46      56.445  90.541  61.908  1.00108.76           C  
ANISOU 1945  C   GLY C  46    10920  11750  18653    622  -4232  -1649       C  
ATOM   1946  O   GLY C  46      55.651  89.829  61.293  1.00110.98           O  
ANISOU 1946  O   GLY C  46    11393  12039  18737    592  -3952  -1562       O  
ATOM   1947  N   LEU C  47      57.463  91.154  61.313  1.00106.16           N  
ANISOU 1947  N   LEU C  47    10272  11183  18880    818  -4310  -1570       N  
ATOM   1948  CA  LEU C  47      57.768  90.906  59.908  1.00 94.04           C  
ANISOU 1948  CA  LEU C  47     8624   9383  17722   1002  -4056  -1353       C  
ATOM   1949  C   LEU C  47      58.444  89.550  59.762  1.00101.71           C  
ANISOU 1949  C   LEU C  47     9757  10192  18697   1109  -4064  -1002       C  
ATOM   1950  O   LEU C  47      59.415  89.262  60.461  1.00110.75           O  
ANISOU 1950  O   LEU C  47    10840  11292  19950   1180  -4379   -846       O  
ATOM   1951  CB  LEU C  47      58.664  92.005  59.340  1.00 88.37           C  
ANISOU 1951  CB  LEU C  47     7516   8477  17584   1127  -4114  -1387       C  
ATOM   1952  CG  LEU C  47      58.090  92.832  58.192  1.00 96.39           C  
ANISOU 1952  CG  LEU C  47     8389   9397  18837   1140  -3846  -1470       C  
ATOM   1953  CD1 LEU C  47      56.832  93.555  58.642  1.00102.46           C  
ANISOU 1953  CD1 LEU C  47     9202  10351  19376   1023  -3812  -1785       C  
ATOM   1954  CD2 LEU C  47      59.125  93.819  57.678  1.00 98.47           C  
ANISOU 1954  CD2 LEU C  47     8305   9451  19660   1221  -3925  -1449       C  
ATOM   1955  N   ARG C  48      57.944  88.721  58.851  1.00 99.19           N  
ANISOU 1955  N   ARG C  48     9633   9770  18285   1117  -3728   -877       N  
ATOM   1956  CA  ARG C  48      58.468  87.365  58.714  1.00 90.67           C  
ANISOU 1956  CA  ARG C  48     8752   8475  17222   1219  -3680   -586       C  
ATOM   1957  C   ARG C  48      59.174  87.144  57.382  1.00 83.93           C  
ANISOU 1957  C   ARG C  48     7730   7323  16838   1394  -3381   -467       C  
ATOM   1958  O   ARG C  48      58.905  87.822  56.395  1.00 81.74           O  
ANISOU 1958  O   ARG C  48     7311   7051  16697   1349  -3138   -576       O  
ATOM   1959  CB  ARG C  48      57.347  86.339  58.890  1.00 84.13           C  
ANISOU 1959  CB  ARG C  48     8380   7749  15838   1022  -3510   -554       C  
ATOM   1960  CG  ARG C  48      56.830  86.244  60.315  1.00 86.00           C  
ANISOU 1960  CG  ARG C  48     8839   8268  15569    816  -3797   -617       C  
ATOM   1961  CD  ARG C  48      55.819  85.123  60.477  1.00 90.02           C  
ANISOU 1961  CD  ARG C  48     9811   8858  15537    588  -3620   -547       C  
ATOM   1962  NE  ARG C  48      55.282  85.080  61.834  1.00101.70           N  
ANISOU 1962  NE  ARG C  48    11510  10656  16477    322  -3859   -627       N  
ATOM   1963  CZ  ARG C  48      55.855  84.434  62.844  1.00118.27           C  
ANISOU 1963  CZ  ARG C  48    13809  12724  18404    277  -4208   -379       C  
ATOM   1964  NH1 ARG C  48      56.987  83.772  62.651  1.00134.02           N  
ANISOU 1964  NH1 ARG C  48    15767  14351  20805    543  -4372    -29       N  
ATOM   1965  NH2 ARG C  48      55.297  84.452  64.047  1.00122.05           N  
ANISOU 1965  NH2 ARG C  48    14513  13547  18313    -45  -4395   -476       N  
ATOM   1966  N   LYS C  49      60.091  86.187  57.373  1.00 86.47           N  
ANISOU 1966  N   LYS C  49     8061   7378  17415   1584  -3404   -236       N  
ATOM   1967  CA  LYS C  49      60.914  85.907  56.206  1.00 89.93           C  
ANISOU 1967  CA  LYS C  49     8307   7523  18341   1757  -3089   -165       C  
ATOM   1968  C   LYS C  49      61.146  84.402  56.073  1.00100.74           C  
ANISOU 1968  C   LYS C  49     9944   8583  19751   1879  -2918     28       C  
ATOM   1969  O   LYS C  49      61.411  83.722  57.065  1.00 92.14           O  
ANISOU 1969  O   LYS C  49     8981   7419  18607   1973  -3235    223       O  
ATOM   1970  CB  LYS C  49      62.241  86.655  56.320  1.00 94.36           C  
ANISOU 1970  CB  LYS C  49     8366   8017  19468   1950  -3318   -134       C  
ATOM   1971  CG  LYS C  49      63.268  86.331  55.256  1.00 96.32           C  
ANISOU 1971  CG  LYS C  49     8374   8003  20219   2109  -2976    -77       C  
ATOM   1972  CD  LYS C  49      64.626  86.899  55.640  1.00101.07           C  
ANISOU 1972  CD  LYS C  49     8636   8704  21063   2135  -3161    -31       C  
ATOM   1973  CE  LYS C  49      65.250  86.137  56.799  1.00112.24           C  
ANISOU 1973  CE  LYS C  49    10056  10070  22519   2302  -3554    196       C  
ATOM   1974  NZ  LYS C  49      66.585  86.690  57.170  1.00124.82           N  
ANISOU 1974  NZ  LYS C  49    11292  11763  24370   2318  -3750    248       N  
ATOM   1975  N   ILE C  50      61.046  83.883  54.853  1.00 88.70           N  
ANISOU 1975  N   ILE C  50     8524   6863  18316   1854  -2424    -23       N  
ATOM   1976  CA  ILE C  50      61.194  82.448  54.631  1.00 96.79           C  
ANISOU 1976  CA  ILE C  50     9841   7533  19404   1952  -2185    102       C  
ATOM   1977  C   ILE C  50      62.072  82.153  53.413  1.00109.04           C  
ANISOU 1977  C   ILE C  50    11179   8769  21482   2104  -1727     35       C  
ATOM   1978  O   ILE C  50      62.093  82.921  52.454  1.00 96.98           O  
ANISOU 1978  O   ILE C  50     9459   7365  20022   1974  -1462   -128       O  
ATOM   1979  CB  ILE C  50      59.816  81.765  54.460  1.00 89.46           C  
ANISOU 1979  CB  ILE C  50     9454   6690  17846   1637  -1950     44       C  
ATOM   1980  CG1 ILE C  50      59.942  80.247  54.586  1.00 92.89           C  
ANISOU 1980  CG1 ILE C  50    10260   6721  18314   1726  -1815    204       C  
ATOM   1981  CG2 ILE C  50      59.177  82.149  53.135  1.00 86.60           C  
ANISOU 1981  CG2 ILE C  50     9130   6458  17318   1382  -1501   -161       C  
ATOM   1982  CD1 ILE C  50      58.672  79.512  54.248  1.00 98.24           C  
ANISOU 1982  CD1 ILE C  50    11468   7446  18410   1372  -1514    126       C  
ATOM   1983  N   ARG C  51      62.811  81.046  53.465  1.00113.86           N  
ANISOU 1983  N   ARG C  51    11818   8963  22481   2371  -1632    165       N  
ATOM   1984  CA  ARG C  51      63.693  80.654  52.368  1.00111.96           C  
ANISOU 1984  CA  ARG C  51    11361   8391  22789   2534  -1138     51       C  
ATOM   1985  C   ARG C  51      63.219  79.363  51.709  1.00117.63           C  
ANISOU 1985  C   ARG C  51    12560   8769  23367   2439   -635    -31       C  
ATOM   1986  O   ARG C  51      63.277  78.292  52.311  1.00140.31           O  
ANISOU 1986  O   ARG C  51    15682  11303  26327   2614   -741    144       O  
ATOM   1987  CB  ARG C  51      65.130  80.487  52.867  1.00111.91           C  
ANISOU 1987  CB  ARG C  51    10967   8370  23186   2820  -1336    207       C  
ATOM   1988  N   VAL C  52      62.755  79.468  50.467  1.00 99.71           N  
ANISOU 1988  N   VAL C  52    10436   6579  20869   2130   -100   -284       N  
ATOM   1989  CA  VAL C  52      62.222  78.315  49.752  1.00116.79           C  
ANISOU 1989  CA  VAL C  52    13092   8463  22818   1940    418   -422       C  
ATOM   1990  C   VAL C  52      62.881  78.123  48.386  1.00127.03           C  
ANISOU 1990  C   VAL C  52    14253   9550  24462   1896   1087   -702       C  
ATOM   1991  O   VAL C  52      62.755  78.967  47.500  1.00119.26           O  
ANISOU 1991  O   VAL C  52    13135   8880  23299   1609   1305   -857       O  
ATOM   1992  CB  VAL C  52      60.696  78.435  49.555  1.00111.59           C  
ANISOU 1992  CB  VAL C  52    12895   8171  21331   1445    453   -484       C  
ATOM   1993  CG1 VAL C  52      60.136  77.157  48.947  1.00136.16           C  
ANISOU 1993  CG1 VAL C  52    16555  10986  24193   1209    942   -616       C  
ATOM   1994  CG2 VAL C  52      60.012  78.735  50.879  1.00108.67           C  
ANISOU 1994  CG2 VAL C  52    12621   8073  20594   1441   -146   -273       C  
ATOM   1995  N   ALA C  53      63.585  77.005  48.226  1.00144.77           N  
ANISOU 1995  N   ALA C  53    16542  11250  27213   2169   1419   -764       N  
ATOM   1996  CA  ALA C  53      64.181  76.644  46.944  1.00137.11           C  
ANISOU 1996  CA  ALA C  53    15497  10035  26566   2105   2155  -1102       C  
ATOM   1997  C   ALA C  53      63.317  75.607  46.235  1.00125.39           C  
ANISOU 1997  C   ALA C  53    14664   8347  24633   1730   2682  -1324       C  
ATOM   1998  O   ALA C  53      62.501  74.934  46.866  1.00112.90           O  
ANISOU 1998  O   ALA C  53    13543   6662  22691   1655   2471  -1177       O  
ATOM   1999  CB  ALA C  53      65.597  76.116  47.138  1.00128.76           C  
ANISOU 1999  CB  ALA C  53    14031   8789  26102   2536   2182  -1051       C  
ATOM   2000  N   SER C  63      65.434  81.996  43.072  1.00151.41           N  
ANISOU 2000  N   SER C  63    15877  13553  28098    819   2829  -1549       N  
ATOM   2001  CA  SER C  63      64.215  81.551  43.739  1.00146.94           C  
ANISOU 2001  CA  SER C  63    15785  13024  27022    782   2492  -1405       C  
ATOM   2002  C   SER C  63      64.511  81.046  45.146  1.00147.30           C  
ANISOU 2002  C   SER C  63    15719  12804  27444   1320   2023  -1225       C  
ATOM   2003  O   SER C  63      64.560  79.839  45.381  1.00155.13           O  
ANISOU 2003  O   SER C  63    16947  13413  28584   1514   2205  -1276       O  
ATOM   2004  CB  SER C  63      63.528  80.454  42.921  1.00140.71           C  
ANISOU 2004  CB  SER C  63    15557  12102  25804    435   3046  -1625       C  
ATOM   2005  N   ARG C  64      64.713  81.971  46.081  1.00135.77           N  
ANISOU 2005  N   ARG C  64    13919  11534  26131   1531   1413  -1007       N  
ATOM   2006  CA  ARG C  64      65.084  81.591  47.441  1.00123.78           C  
ANISOU 2006  CA  ARG C  64    12267   9825  24940   1987    913   -804       C  
ATOM   2007  C   ARG C  64      64.249  82.261  48.541  1.00100.04           C  
ANISOU 2007  C   ARG C  64     9367   7128  21514   1949    254   -597       C  
ATOM   2008  O   ARG C  64      63.487  81.595  49.238  1.00 99.44           O  
ANISOU 2008  O   ARG C  64     9676   7008  21100   1954     58   -497       O  
ATOM   2009  CB  ARG C  64      66.569  81.888  47.676  1.00126.06           C  
ANISOU 2009  CB  ARG C  64    11942  10051  25903   2314    815   -766       C  
ATOM   2010  N   ILE C  65      64.389  83.574  48.692  1.00 95.47           N  
ANISOU 2010  N   ILE C  65     8461   6852  20962   1884    -54   -555       N  
ATOM   2011  CA  ILE C  65      63.923  84.255  49.903  1.00105.38           C  
ANISOU 2011  CA  ILE C  65     9694   8343  22002   1936   -684   -407       C  
ATOM   2012  C   ILE C  65      62.694  85.163  49.698  1.00 97.10           C  
ANISOU 2012  C   ILE C  65     8849   7652  20393   1582   -785   -444       C  
ATOM   2013  O   ILE C  65      62.558  85.834  48.673  1.00 97.93           O  
ANISOU 2013  O   ILE C  65     8893   7884  20432   1329   -538   -515       O  
ATOM   2014  CB  ILE C  65      65.085  85.072  50.506  1.00115.16           C  
ANISOU 2014  CB  ILE C  65    10421   9682  23652   2118  -1039   -333       C  
ATOM   2015  CG1 ILE C  65      64.712  85.686  51.855  1.00106.31           C  
ANISOU 2015  CG1 ILE C  65     9334   8821  22240   2115  -1653   -226       C  
ATOM   2016  CG2 ILE C  65      65.547  86.137  49.535  1.00138.64           C  
ANISOU 2016  CG2 ILE C  65    13059  12756  26861   1949   -821   -441       C  
ATOM   2017  CD1 ILE C  65      65.847  86.488  52.454  1.00109.94           C  
ANISOU 2017  CD1 ILE C  65     9434   9460  22879   2133  -1958   -178       C  
ATOM   2018  N   ILE C  66      61.799  85.163  50.685  1.00 86.43           N  
ANISOU 2018  N   ILE C  66     7728   6461  18652   1560  -1151   -383       N  
ATOM   2019  CA  ILE C  66      60.528  85.880  50.604  1.00 82.92           C  
ANISOU 2019  CA  ILE C  66     7459   6335  17714   1275  -1246   -429       C  
ATOM   2020  C   ILE C  66      60.164  86.575  51.916  1.00 81.72           C  
ANISOU 2020  C   ILE C  66     7228   6385  17438   1349  -1764   -416       C  
ATOM   2021  O   ILE C  66      60.175  85.960  52.985  1.00 87.62           O  
ANISOU 2021  O   ILE C  66     8106   7099  18086   1475  -2011   -352       O  
ATOM   2022  CB  ILE C  66      59.377  84.927  50.216  1.00 81.97           C  
ANISOU 2022  CB  ILE C  66     7827   6256  17063   1028   -973   -456       C  
ATOM   2023  CG1 ILE C  66      59.411  84.632  48.719  1.00 82.64           C  
ANISOU 2023  CG1 ILE C  66     8016   6271  17114    787   -446   -529       C  
ATOM   2024  CG2 ILE C  66      58.026  85.516  50.599  1.00 79.09           C  
ANISOU 2024  CG2 ILE C  66     7594   6237  16219    817  -1197   -480       C  
ATOM   2025  CD1 ILE C  66      58.245  83.807  48.240  1.00 81.94           C  
ANISOU 2025  CD1 ILE C  66     8397   6269  16468    462   -185   -572       C  
ATOM   2026  N   TYR C  67      59.840  87.862  51.824  1.00 81.11           N  
ANISOU 2026  N   TYR C  67     6952   6502  17365   1245  -1919   -481       N  
ATOM   2027  CA  TYR C  67      59.365  88.618  52.975  1.00 85.12           C  
ANISOU 2027  CA  TYR C  67     7401   7207  17735   1265  -2331   -554       C  
ATOM   2028  C   TYR C  67      57.843  88.718  52.968  1.00 76.92           C  
ANISOU 2028  C   TYR C  67     6612   6411  16203   1049  -2290   -635       C  
ATOM   2029  O   TYR C  67      57.238  89.138  51.979  1.00 82.25           O  
ANISOU 2029  O   TYR C  67     7288   7161  16804    878  -2101   -632       O  
ATOM   2030  CB  TYR C  67      59.990  90.014  53.001  1.00 96.42           C  
ANISOU 2030  CB  TYR C  67     8436   8643  19556   1310  -2538   -609       C  
ATOM   2031  CG  TYR C  67      61.340  90.065  53.681  1.00110.29           C  
ANISOU 2031  CG  TYR C  67     9903  10278  21726   1518  -2784   -567       C  
ATOM   2032  CD1 TYR C  67      62.504  89.753  52.989  1.00108.27           C  
ANISOU 2032  CD1 TYR C  67     9487   9864  21788   1570  -2551   -478       C  
ATOM   2033  CD2 TYR C  67      61.450  90.425  55.019  1.00122.93           C  
ANISOU 2033  CD2 TYR C  67    11476  12009  23222   1546  -3186   -630       C  
ATOM   2034  CE1 TYR C  67      63.741  89.799  53.611  1.00116.16           C  
ANISOU 2034  CE1 TYR C  67    10310  10861  22965   1644  -2721   -427       C  
ATOM   2035  CE2 TYR C  67      62.681  90.474  55.649  1.00126.47           C  
ANISOU 2035  CE2 TYR C  67    11776  12442  23834   1601  -3378   -565       C  
ATOM   2036  CZ  TYR C  67      63.823  90.162  54.942  1.00125.82           C  
ANISOU 2036  CZ  TYR C  67    11532  12221  24053   1656  -3151   -451       C  
ATOM   2037  OH  TYR C  67      65.050  90.210  55.570  1.00129.26           O  
ANISOU 2037  OH  TYR C  67    11769  12661  24681   1719  -3360   -376       O  
ATOM   2038  N   TYR C  68      57.229  88.323  54.078  1.00 77.02           N  
ANISOU 2038  N   TYR C  68     6821   6569  15876   1033  -2480   -691       N  
ATOM   2039  CA  TYR C  68      55.779  88.353  54.199  1.00 75.54           C  
ANISOU 2039  CA  TYR C  68     6826   6646  15230    828  -2432   -796       C  
ATOM   2040  C   TYR C  68      55.362  88.760  55.603  1.00 76.18           C  
ANISOU 2040  C   TYR C  68     6897   6933  15115    827  -2736   -960       C  
ATOM   2041  O   TYR C  68      56.170  88.765  56.533  1.00 80.18           O  
ANISOU 2041  O   TYR C  68     7344   7384  15735    945  -2998   -953       O  
ATOM   2042  CB  TYR C  68      55.172  86.992  53.844  1.00 75.48           C  
ANISOU 2042  CB  TYR C  68     7215   6636  14827    664  -2160   -715       C  
ATOM   2043  CG  TYR C  68      55.296  85.947  54.933  1.00 77.19           C  
ANISOU 2043  CG  TYR C  68     7711   6806  14813    695  -2288   -656       C  
ATOM   2044  CD1 TYR C  68      56.468  85.220  55.098  1.00 79.37           C  
ANISOU 2044  CD1 TYR C  68     8009   6769  15377    902  -2329   -495       C  
ATOM   2045  CD2 TYR C  68      54.235  85.682  55.789  1.00 77.21           C  
ANISOU 2045  CD2 TYR C  68     7940   7074  14322    506  -2370   -743       C  
ATOM   2046  CE1 TYR C  68      56.582  84.265  56.089  1.00 92.92           C  
ANISOU 2046  CE1 TYR C  68     9994   8411  16902    927  -2501   -370       C  
ATOM   2047  CE2 TYR C  68      54.340  84.731  56.784  1.00 94.81           C  
ANISOU 2047  CE2 TYR C  68    10465   9263  16297    478  -2508   -644       C  
ATOM   2048  CZ  TYR C  68      55.515  84.024  56.929  1.00 97.02           C  
ANISOU 2048  CZ  TYR C  68    10789   9200  16873    692  -2599   -431       C  
ATOM   2049  OH  TYR C  68      55.620  83.071  57.918  1.00 97.08           O  
ANISOU 2049  OH  TYR C  68    11105   9137  16644    661  -2790   -263       O  
ATOM   2050  N   PHE C  69      54.091  89.103  55.749  1.00 75.29           N  
ANISOU 2050  N   PHE C  69     6826   7081  14700    670  -2696  -1119       N  
ATOM   2051  CA  PHE C  69      53.571  89.538  57.032  1.00 76.35           C  
ANISOU 2051  CA  PHE C  69     6947   7446  14617    620  -2900  -1352       C  
ATOM   2052  C   PHE C  69      52.227  88.865  57.298  1.00 76.21           C  
ANISOU 2052  C   PHE C  69     7184   7712  14059    383  -2744  -1435       C  
ATOM   2053  O   PHE C  69      51.391  88.744  56.400  1.00 74.95           O  
ANISOU 2053  O   PHE C  69     7038   7640  13800    270  -2526  -1401       O  
ATOM   2054  CB  PHE C  69      53.464  91.072  57.062  1.00 91.45           C  
ANISOU 2054  CB  PHE C  69     8499   9374  16874    704  -3017  -1565       C  
ATOM   2055  CG  PHE C  69      52.337  91.593  57.902  1.00 77.31           C  
ANISOU 2055  CG  PHE C  69     6671   7862  14842    599  -3038  -1885       C  
ATOM   2056  CD1 PHE C  69      52.373  91.491  59.284  1.00113.96           C  
ANISOU 2056  CD1 PHE C  69    11428  12672  19198    509  -3193  -2088       C  
ATOM   2057  CD2 PHE C  69      51.245  92.201  57.309  1.00 76.73           C  
ANISOU 2057  CD2 PHE C  69     6425   7894  14836    574  -2900  -1986       C  
ATOM   2058  CE1 PHE C  69      51.331  91.971  60.057  1.00113.84           C  
ANISOU 2058  CE1 PHE C  69    11368  12932  18954    382  -3142  -2446       C  
ATOM   2059  CE2 PHE C  69      50.203  92.684  58.076  1.00105.78           C  
ANISOU 2059  CE2 PHE C  69    10008  11821  18363    506  -2874  -2321       C  
ATOM   2060  CZ  PHE C  69      50.247  92.570  59.452  1.00112.69           C  
ANISOU 2060  CZ  PHE C  69    11008  12867  18943    403  -2962  -2583       C  
ATOM   2061  N   LEU C  70      52.038  88.410  58.532  1.00 86.92           N  
ANISOU 2061  N   LEU C  70     8745   9238  15041    265  -2867  -1528       N  
ATOM   2062  CA  LEU C  70      50.851  87.647  58.895  1.00100.00           C  
ANISOU 2062  CA  LEU C  70    10677  11178  16143    -11  -2711  -1597       C  
ATOM   2063  C   LEU C  70      49.791  88.509  59.569  1.00 85.04           C  
ANISOU 2063  C   LEU C  70     8594   9630  14089   -128  -2694  -1967       C  
ATOM   2064  O   LEU C  70      50.023  89.084  60.630  1.00 93.70           O  
ANISOU 2064  O   LEU C  70     9621  10823  15158   -130  -2870  -2187       O  
ATOM   2065  CB  LEU C  70      51.233  86.483  59.812  1.00120.02           C  
ANISOU 2065  CB  LEU C  70    13608  13688  18307   -133  -2830  -1435       C  
ATOM   2066  CG  LEU C  70      50.080  85.682  60.420  1.00117.74           C  
ANISOU 2066  CG  LEU C  70    13648  13706  17381   -487  -2698  -1507       C  
ATOM   2067  CD1 LEU C  70      49.194  85.081  59.335  1.00100.60           C  
ANISOU 2067  CD1 LEU C  70    11585  11571  15069   -637  -2373  -1440       C  
ATOM   2068  CD2 LEU C  70      50.619  84.601  61.345  1.00125.19           C  
ANISOU 2068  CD2 LEU C  70    15000  14559  18009   -601  -2886  -1271       C  
ATOM   2069  N   ASP C  71      48.622  88.581  58.945  1.00 88.76           N  
ANISOU 2069  N   ASP C  71     8970  10295  14457   -242  -2473  -2047       N  
ATOM   2070  CA  ASP C  71      47.507  89.344  59.486  1.00100.93           C  
ANISOU 2070  CA  ASP C  71    10272  12162  15914   -327  -2400  -2414       C  
ATOM   2071  C   ASP C  71      46.529  88.419  60.208  1.00113.24           C  
ANISOU 2071  C   ASP C  71    12106  14085  16833   -681  -2243  -2521       C  
ATOM   2072  O   ASP C  71      46.706  87.202  60.220  1.00119.12           O  
ANISOU 2072  O   ASP C  71    13253  14790  17219   -858  -2211  -2275       O  
ATOM   2073  CB  ASP C  71      46.800  90.106  58.360  1.00101.30           C  
ANISOU 2073  CB  ASP C  71     9956  12214  16321   -216  -2300  -2413       C  
ATOM   2074  CG  ASP C  71      45.904  91.217  58.872  1.00115.18           C  
ANISOU 2074  CG  ASP C  71    11331  14173  18260   -157  -2267  -2809       C  
ATOM   2075  OD1 ASP C  71      46.171  91.737  59.976  1.00125.31           O  
ANISOU 2075  OD1 ASP C  71    12580  15485  19548   -132  -2340  -3121       O  
ATOM   2076  OD2 ASP C  71      44.933  91.566  58.167  1.00106.66           O  
ANISOU 2076  OD2 ASP C  71     9975  13222  17330   -146  -2168  -2815       O  
ATOM   2077  N   GLU C  72      45.497  89.003  60.807  1.00131.68           N  
ANISOU 2077  N   GLU C  72    14219  16759  19055   -791  -2125  -2901       N  
ATOM   2078  CA  GLU C  72      44.444  88.232  61.453  1.00144.26           C  
ANISOU 2078  CA  GLU C  72    16009  18760  20044  -1173  -1928  -3047       C  
ATOM   2079  C   GLU C  72      43.544  87.588  60.406  1.00145.50           C  
ANISOU 2079  C   GLU C  72    16165  19042  20077  -1323  -1731  -2864       C  
ATOM   2080  O   GLU C  72      43.530  88.012  59.250  1.00144.76           O  
ANISOU 2080  O   GLU C  72    15823  18792  20387  -1127  -1743  -2708       O  
ATOM   2081  CB  GLU C  72      43.626  89.121  62.393  1.00154.00           C  
ANISOU 2081  CB  GLU C  72    16940  20330  21243  -1244  -1807  -3573       C  
ATOM   2082  CG  GLU C  72      43.037  90.356  61.731  1.00163.44           C  
ANISOU 2082  CG  GLU C  72    17562  21495  23044   -954  -1740  -3782       C  
ATOM   2083  CD  GLU C  72      42.471  91.343  62.735  1.00172.83           C  
ANISOU 2083  CD  GLU C  72    18441  22898  24330   -949  -1612  -4360       C  
ATOM   2084  OE1 GLU C  72      42.507  91.047  63.948  1.00180.13           O  
ANISOU 2084  OE1 GLU C  72    19617  24056  24766  -1233  -1555  -4617       O  
ATOM   2085  OE2 GLU C  72      41.994  92.417  62.313  1.00170.98           O  
ANISOU 2085  OE2 GLU C  72    17719  22584  24663   -676  -1564  -4560       O  
ATOM   2086  N   LYS C  73      42.810  86.559  60.822  1.00151.76           N  
ANISOU 2086  N   LYS C  73    17258  20127  20276  -1720  -1564  -2869       N  
ATOM   2087  CA  LYS C  73      41.882  85.826  59.957  1.00152.46           C  
ANISOU 2087  CA  LYS C  73    17394  20395  20141  -1970  -1368  -2724       C  
ATOM   2088  C   LYS C  73      42.594  85.118  58.806  1.00146.59           C  
ANISOU 2088  C   LYS C  73    16921  19272  19504  -1907  -1408  -2306       C  
ATOM   2089  O   LYS C  73      42.098  85.101  57.678  1.00144.48           O  
ANISOU 2089  O   LYS C  73    16506  19049  19341  -1950  -1321  -2185       O  
ATOM   2090  CB  LYS C  73      40.801  86.764  59.403  1.00146.79           C  
ANISOU 2090  CB  LYS C  73    16088  19948  19736  -1882  -1271  -2934       C  
ATOM   2091  N   ARG C  74      43.755  84.537  59.104  1.00143.27           N  
ANISOU 2091  N   ARG C  74    16882  18492  19062  -1820  -1537  -2096       N  
ATOM   2092  CA  ARG C  74      44.496  83.708  58.153  1.00137.14           C  
ANISOU 2092  CA  ARG C  74    16409  17324  18374  -1777  -1512  -1751       C  
ATOM   2093  C   ARG C  74      44.836  84.448  56.858  1.00119.28           C  
ANISOU 2093  C   ARG C  74    13823  14877  16622  -1514  -1524  -1654       C  
ATOM   2094  O   ARG C  74      44.837  83.851  55.778  1.00100.70           O  
ANISOU 2094  O   ARG C  74    11628  12396  14238  -1628  -1381  -1463       O  
ATOM   2095  CB  ARG C  74      43.703  82.436  57.828  1.00147.68           C  
ANISOU 2095  CB  ARG C  74    18129  18780  19202  -2210  -1279  -1644       C  
ATOM   2096  CG  ARG C  74      43.277  81.620  59.046  1.00153.96           C  
ANISOU 2096  CG  ARG C  74    19297  19769  19431  -2558  -1249  -1697       C  
ATOM   2097  CD  ARG C  74      44.441  80.846  59.655  1.00156.99           C  
ANISOU 2097  CD  ARG C  74    20132  19732  19787  -2465  -1419  -1443       C  
ATOM   2098  NE  ARG C  74      45.012  79.887  58.714  1.00150.62           N  
ANISOU 2098  NE  ARG C  74    19654  18474  19102  -2434  -1316  -1159       N  
ATOM   2099  CZ  ARG C  74      45.852  78.914  59.053  1.00141.80           C  
ANISOU 2099  CZ  ARG C  74    18975  16934  17967  -2395  -1401   -894       C  
ATOM   2100  NH1 ARG C  74      46.220  78.758  60.317  1.00136.87           N  
ANISOU 2100  NH1 ARG C  74    18532  16313  17159  -2414  -1648   -816       N  
ATOM   2101  NH2 ARG C  74      46.319  78.091  58.125  1.00142.88           N  
ANISOU 2101  NH2 ARG C  74    19371  16640  18277  -2352  -1240   -707       N  
ATOM   2102  N   ARG C  75      45.119  85.744  56.969  1.00108.60           N  
ANISOU 2102  N   ARG C  75    12044  13504  15714  -1206  -1685  -1791       N  
ATOM   2103  CA  ARG C  75      45.468  86.559  55.806  1.00 88.92           C  
ANISOU 2103  CA  ARG C  75     9245  10829  13710   -979  -1732  -1671       C  
ATOM   2104  C   ARG C  75      46.969  86.820  55.741  1.00 82.71           C  
ANISOU 2104  C   ARG C  75     8481   9619  13325   -674  -1879  -1540       C  
ATOM   2105  O   ARG C  75      47.571  87.263  56.717  1.00 92.48           O  
ANISOU 2105  O   ARG C  75     9657  10786  14696   -505  -2057  -1664       O  
ATOM   2106  CB  ARG C  75      44.717  87.891  55.831  1.00104.49           C  
ANISOU 2106  CB  ARG C  75    10700  13016  15988   -843  -1811  -1882       C  
ATOM   2107  CG  ARG C  75      44.770  88.654  54.512  1.00122.98           C  
ANISOU 2107  CG  ARG C  75    12749  15229  18750   -708  -1869  -1689       C  
ATOM   2108  CD  ARG C  75      44.507  90.147  54.703  1.00134.87           C  
ANISOU 2108  CD  ARG C  75    13752  16733  20758   -433  -2028  -1866       C  
ATOM   2109  NE  ARG C  75      43.459  90.417  55.683  1.00139.55           N  
ANISOU 2109  NE  ARG C  75    14138  17659  21226   -481  -1969  -2220       N  
ATOM   2110  CZ  ARG C  75      42.172  90.556  55.386  1.00146.50           C  
ANISOU 2110  CZ  ARG C  75    14731  18868  22063   -598  -1895  -2279       C  
ATOM   2111  NH1 ARG C  75      41.295  90.801  56.351  1.00157.43           N  
ANISOU 2111  NH1 ARG C  75    15900  20553  23362   -635  -1792  -2655       N  
ATOM   2112  NH2 ARG C  75      41.760  90.451  54.129  1.00139.81           N  
ANISOU 2112  NH2 ARG C  75    13796  18076  21250   -704  -1922  -1969       N  
ATOM   2113  N   PHE C  76      47.567  86.547  54.586  1.00 76.76           N  
ANISOU 2113  N   PHE C  76     7803   8614  12750   -642  -1793  -1307       N  
ATOM   2114  CA  PHE C  76      49.007  86.709  54.407  1.00 75.61           C  
ANISOU 2114  CA  PHE C  76     7642   8080  13005   -376  -1882  -1182       C  
ATOM   2115  C   PHE C  76      49.332  87.791  53.386  1.00 78.02           C  
ANISOU 2115  C   PHE C  76     7607   8277  13760   -234  -1922  -1108       C  
ATOM   2116  O   PHE C  76      48.875  87.729  52.250  1.00 85.08           O  
ANISOU 2116  O   PHE C  76     8498   9236  14593   -404  -1780   -983       O  
ATOM   2117  CB  PHE C  76      49.644  85.390  53.963  1.00 83.27           C  
ANISOU 2117  CB  PHE C  76     9007   8784  13847   -455  -1696   -994       C  
ATOM   2118  CG  PHE C  76      49.433  84.258  54.924  1.00 88.83           C  
ANISOU 2118  CG  PHE C  76    10099   9508  14143   -600  -1683   -992       C  
ATOM   2119  CD1 PHE C  76      48.277  83.498  54.878  1.00 91.78           C  
ANISOU 2119  CD1 PHE C  76    10729  10127  14017   -955  -1505  -1025       C  
ATOM   2120  CD2 PHE C  76      50.397  83.948  55.866  1.00 93.17           C  
ANISOU 2120  CD2 PHE C  76    10760   9838  14804   -412  -1876   -924       C  
ATOM   2121  CE1 PHE C  76      48.084  82.456  55.759  1.00101.54           C  
ANISOU 2121  CE1 PHE C  76    12358  11362  14861  -1133  -1496   -994       C  
ATOM   2122  CE2 PHE C  76      50.211  82.905  56.748  1.00102.75           C  
ANISOU 2122  CE2 PHE C  76    12360  11049  15630   -572  -1906   -858       C  
ATOM   2123  CZ  PHE C  76      49.053  82.158  56.695  1.00109.45           C  
ANISOU 2123  CZ  PHE C  76    13497  12116  15972   -940  -1704   -894       C  
ATOM   2124  N   TYR C  77      50.128  88.777  53.781  1.00 72.64           N  
ANISOU 2124  N   TYR C  77     6662   7435  13505     31  -2126  -1170       N  
ATOM   2125  CA  TYR C  77      50.580  89.785  52.830  1.00 72.20           C  
ANISOU 2125  CA  TYR C  77     6322   7220  13892    143  -2173  -1063       C  
ATOM   2126  C   TYR C  77      51.974  89.453  52.327  1.00 75.90           C  
ANISOU 2126  C   TYR C  77     6858   7369  14610    241  -2105   -906       C  
ATOM   2127  O   TYR C  77      52.940  89.476  53.091  1.00 82.18           O  
ANISOU 2127  O   TYR C  77     7616   8000  15607    430  -2243   -950       O  
ATOM   2128  CB  TYR C  77      50.571  91.179  53.455  1.00 73.84           C  
ANISOU 2128  CB  TYR C  77     6175   7414  14469    343  -2412  -1242       C  
ATOM   2129  CG  TYR C  77      49.206  91.806  53.537  1.00 73.60           C  
ANISOU 2129  CG  TYR C  77     5937   7637  14388    292  -2439  -1382       C  
ATOM   2130  CD1 TYR C  77      48.658  92.463  52.447  1.00 73.82           C  
ANISOU 2130  CD1 TYR C  77     5752   7678  14617    257  -2453  -1213       C  
ATOM   2131  CD2 TYR C  77      48.465  91.746  54.706  1.00 74.66           C  
ANISOU 2131  CD2 TYR C  77     6070   8010  14288    267  -2453  -1674       C  
ATOM   2132  CE1 TYR C  77      47.406  93.043  52.517  1.00 75.16           C  
ANISOU 2132  CE1 TYR C  77     5666   8066  14828    255  -2503  -1317       C  
ATOM   2133  CE2 TYR C  77      47.215  92.324  54.788  1.00 83.75           C  
ANISOU 2133  CE2 TYR C  77     6965   9396  15461    246  -2440  -1839       C  
ATOM   2134  CZ  TYR C  77      46.689  92.971  53.691  1.00 76.23           C  
ANISOU 2134  CZ  TYR C  77     5756   8426  14784    269  -2476  -1653       C  
ATOM   2135  OH  TYR C  77      45.442  93.547  53.771  1.00 78.17           O  
ANISOU 2135  OH  TYR C  77     5682   8889  15130    290  -2488  -1794       O  
ATOM   2136  N   LEU C  78      52.076  89.150  51.039  1.00 74.72           N  
ANISOU 2136  N   LEU C  78     6790   7157  14445     88  -1887   -732       N  
ATOM   2137  CA  LEU C  78      53.364  88.841  50.436  1.00 82.37           C  
ANISOU 2137  CA  LEU C  78     7786   7838  15673    157  -1741   -625       C  
ATOM   2138  C   LEU C  78      53.985  90.130  49.928  1.00 80.61           C  
ANISOU 2138  C   LEU C  78     7224   7501  15902    249  -1862   -562       C  
ATOM   2139  O   LEU C  78      53.462  90.759  49.009  1.00 90.90           O  
ANISOU 2139  O   LEU C  78     8438   8895  17206     85  -1846   -447       O  
ATOM   2140  CB  LEU C  78      53.206  87.824  49.305  1.00 72.68           C  
ANISOU 2140  CB  LEU C  78     6852   6598  14165   -114  -1379   -528       C  
ATOM   2141  CG  LEU C  78      52.436  86.555  49.678  1.00 72.81           C  
ANISOU 2141  CG  LEU C  78     7245   6716  13704   -281  -1237   -580       C  
ATOM   2142  CD1 LEU C  78      52.473  85.558  48.542  1.00 73.74           C  
ANISOU 2142  CD1 LEU C  78     7672   6749  13599   -558   -845   -530       C  
ATOM   2143  CD2 LEU C  78      52.980  85.932  50.954  1.00 73.45           C  
ANISOU 2143  CD2 LEU C  78     7439   6639  13829    -52  -1361   -639       C  
ATOM   2144  N   LEU C  79      55.104  90.515  50.532  1.00 73.19           N  
ANISOU 2144  N   LEU C  79     6100   6367  15340    483  -2010   -611       N  
ATOM   2145  CA  LEU C  79      55.682  91.836  50.303  1.00 97.74           C  
ANISOU 2145  CA  LEU C  79     8883   9359  18893    564  -2173   -584       C  
ATOM   2146  C   LEU C  79      56.623  91.869  49.101  1.00 88.64           C  
ANISOU 2146  C   LEU C  79     7669   8046  17965    462  -1946   -429       C  
ATOM   2147  O   LEU C  79      56.374  92.584  48.132  1.00 97.27           O  
ANISOU 2147  O   LEU C  79     8688   9159  19112    284  -1912   -291       O  
ATOM   2148  CB  LEU C  79      56.412  92.310  51.560  1.00 93.69           C  
ANISOU 2148  CB  LEU C  79     8186   8756  18655    799  -2457   -735       C  
ATOM   2149  CG  LEU C  79      55.555  92.329  52.830  1.00 86.78           C  
ANISOU 2149  CG  LEU C  79     7381   8066  17525    848  -2655   -938       C  
ATOM   2150  CD1 LEU C  79      56.377  92.773  54.030  1.00 97.72           C  
ANISOU 2150  CD1 LEU C  79     8616   9386  19126   1005  -2936  -1086       C  
ATOM   2151  CD2 LEU C  79      54.331  93.221  52.657  1.00 75.03           C  
ANISOU 2151  CD2 LEU C  79     5789   6715  16003    781  -2710  -1015       C  
ATOM   2152  N   THR C  80      57.710  91.111  49.174  1.00 75.60           N  
ANISOU 2152  N   THR C  80     6030   6234  16460    567  -1794   -444       N  
ATOM   2153  CA  THR C  80      58.666  91.061  48.076  1.00 77.07           C  
ANISOU 2153  CA  THR C  80     6132   6282  16871    463  -1504   -358       C  
ATOM   2154  C   THR C  80      59.387  89.717  48.012  1.00 85.45           C  
ANISOU 2154  C   THR C  80     7326   7193  17947    548  -1201   -405       C  
ATOM   2155  O   THR C  80      59.347  88.933  48.958  1.00 88.04           O  
ANISOU 2155  O   THR C  80     7775   7479  18199    737  -1306   -457       O  
ATOM   2156  CB  THR C  80      59.703  92.191  48.184  1.00 80.83           C  
ANISOU 2156  CB  THR C  80     6232   6629  17850    562  -1683   -346       C  
ATOM   2157  OG1 THR C  80      60.747  91.976  47.224  1.00 80.29           O  
ANISOU 2157  OG1 THR C  80     6060   6444  18002    460  -1350   -300       O  
ATOM   2158  CG2 THR C  80      60.298  92.233  49.582  1.00 80.51           C  
ANISOU 2158  CG2 THR C  80     6023   6526  18042    858  -1999   -462       C  
ATOM   2159  N   ILE C  81      60.036  89.457  46.880  1.00 88.55           N  
ANISOU 2159  N   ILE C  81     7704   7494  18445    392   -813   -387       N  
ATOM   2160  CA  ILE C  81      60.710  88.187  46.641  1.00 82.23           C  
ANISOU 2160  CA  ILE C  81     7018   6500  17728    470   -437   -470       C  
ATOM   2161  C   ILE C  81      61.995  88.392  45.838  1.00107.33           C  
ANISOU 2161  C   ILE C  81     9907   9540  21332    447   -129   -507       C  
ATOM   2162  O   ILE C  81      62.035  89.214  44.923  1.00127.42           O  
ANISOU 2162  O   ILE C  81    12368  12192  23854    162    -20   -450       O  
ATOM   2163  CB  ILE C  81      59.775  87.207  45.903  1.00 93.47           C  
ANISOU 2163  CB  ILE C  81     8888   7989  18638    177    -86   -505       C  
ATOM   2164  CG1 ILE C  81      60.520  85.930  45.504  1.00101.09           C  
ANISOU 2164  CG1 ILE C  81     9983   8680  19748    236    386   -636       C  
ATOM   2165  CG2 ILE C  81      59.153  87.880  44.687  1.00 82.47           C  
ANISOU 2165  CG2 ILE C  81     7572   6820  16942   -256     48   -421       C  
ATOM   2166  CD1 ILE C  81      59.654  84.908  44.798  1.00 88.60           C  
ANISOU 2166  CD1 ILE C  81     8879   7127  17660    -91    762   -715       C  
ATOM   2167  N   TYR C  82      63.047  87.658  46.194  1.00109.28           N  
ANISOU 2167  N   TYR C  82     9983   9551  21986    739     -1   -585       N  
ATOM   2168  CA  TYR C  82      64.321  87.740  45.482  1.00121.97           C  
ANISOU 2168  CA  TYR C  82    11256  11033  24054    743    346   -665       C  
ATOM   2169  C   TYR C  82      65.206  86.522  45.760  1.00133.62           C  
ANISOU 2169  C   TYR C  82    12633  12206  25932   1080    587   -771       C  
ATOM   2170  O   TYR C  82      64.770  85.561  46.393  1.00126.41           O  
ANISOU 2170  O   TYR C  82    11989  11157  24883   1262    506   -755       O  
ATOM   2171  CB  TYR C  82      65.059  89.036  45.845  1.00125.87           C  
ANISOU 2171  CB  TYR C  82    11291  11595  24939    814      1   -591       C  
ATOM   2172  CG  TYR C  82      65.377  89.214  47.318  1.00126.15           C  
ANISOU 2172  CG  TYR C  82    11103  11590  25238   1187   -546   -536       C  
ATOM   2173  CD1 TYR C  82      64.382  89.525  48.238  1.00113.92           C  
ANISOU 2173  CD1 TYR C  82     9762  10167  23353   1221   -986   -479       C  
ATOM   2174  CD2 TYR C  82      66.680  89.097  47.782  1.00137.99           C  
ANISOU 2174  CD2 TYR C  82    12161  12956  27312   1471   -622   -549       C  
ATOM   2175  CE1 TYR C  82      64.677  89.692  49.582  1.00110.97           C  
ANISOU 2175  CE1 TYR C  82     9249   9813  23103   1462  -1462   -450       C  
ATOM   2176  CE2 TYR C  82      66.987  89.266  49.121  1.00136.29           C  
ANISOU 2176  CE2 TYR C  82    11963  12862  26958   1589  -1125   -469       C  
ATOM   2177  CZ  TYR C  82      65.982  89.562  50.017  1.00118.56           C  
ANISOU 2177  CZ  TYR C  82     9988  10756  24303   1567  -1524   -430       C  
ATOM   2178  OH  TYR C  82      66.286  89.727  51.349  1.00101.06           O  
ANISOU 2178  OH  TYR C  82     7789   8660  21948   1647  -1970   -383       O  
ATOM   2179  N   GLY C  83      66.444  86.562  45.271  1.00154.53           N  
ANISOU 2179  N   GLY C  83    14882  14735  29098   1155    891   -871       N  
ATOM   2180  CA  GLY C  83      67.371  85.451  45.423  1.00164.97           C  
ANISOU 2180  CA  GLY C  83    16021  15732  30927   1509   1161   -980       C  
ATOM   2181  C   GLY C  83      68.146  85.469  46.728  1.00163.56           C  
ANISOU 2181  C   GLY C  83    15472  15477  31197   1951    628   -826       C  
ATOM   2182  O   GLY C  83      67.983  86.381  47.536  1.00159.46           O  
ANISOU 2182  O   GLY C  83    14897  15207  30483   1909     71   -673       O  
ATOM   2183  N   LYS C  84      68.994  84.462  46.925  1.00167.56           N  
ANISOU 2183  N   LYS C  84    15906  15807  31954   2181    776   -842       N  
ATOM   2184  CA  LYS C  84      69.748  84.301  48.170  1.00162.19           C  
ANISOU 2184  CA  LYS C  84    15077  15210  31337   2422    243   -629       C  
ATOM   2185  C   LYS C  84      70.508  85.566  48.561  1.00151.01           C  
ANISOU 2185  C   LYS C  84    13273  14065  30040   2332   -128   -556       C  
ATOM   2186  O   LYS C  84      70.169  86.223  49.544  1.00143.11           O  
ANISOU 2186  O   LYS C  84    12359  13271  28745   2291   -679   -414       O  
ATOM   2187  CB  LYS C  84      70.725  83.129  48.052  1.00164.63           C  
ANISOU 2187  CB  LYS C  84    15246  15252  32052   2686    539   -669       C  
ATOM   2188  N   ASN C  85      71.535  85.907  47.791  1.00148.04           N  
ANISOU 2188  N   ASN C  85    12485  13672  30092   2277    211   -685       N  
ATOM   2189  CA  ASN C  85      72.219  87.177  47.983  1.00147.86           C  
ANISOU 2189  CA  ASN C  85    12123  13869  30188   2130    -65   -645       C  
ATOM   2190  C   ASN C  85      71.883  88.138  46.850  1.00156.68           C  
ANISOU 2190  C   ASN C  85    13142  15048  31340   1808    270   -780       C  
ATOM   2191  O   ASN C  85      72.353  87.973  45.725  1.00166.93           O  
ANISOU 2191  O   ASN C  85    14208  16253  32965   1713    870   -967       O  
ATOM   2192  CB  ASN C  85      73.732  86.968  48.073  1.00141.66           C  
ANISOU 2192  CB  ASN C  85    10884  13051  29891   2291     -6   -653       C  
ATOM   2193  N   GLU C  86      71.064  89.141  47.156  1.00148.25           N  
ANISOU 2193  N   GLU C  86    12242  14141  29945   1625   -100   -690       N  
ATOM   2194  CA  GLU C  86      70.679  90.149  46.174  1.00145.23           C  
ANISOU 2194  CA  GLU C  86    11751  13831  29599   1309    112   -740       C  
ATOM   2195  C   GLU C  86      70.838  91.554  46.738  1.00154.72           C  
ANISOU 2195  C   GLU C  86    12873  15194  30719   1146   -381   -634       C  
ATOM   2196  O   GLU C  86      71.681  92.324  46.283  1.00157.92           O  
ANISOU 2196  O   GLU C  86    12951  15645  31407    971   -272   -659       O  
ATOM   2197  CB  GLU C  86      69.236  89.936  45.711  1.00141.69           C  
ANISOU 2197  CB  GLU C  86    11717  13381  28740   1176    238   -736       C  
ATOM   2198  CG  GLU C  86      68.999  88.646  44.943  1.00157.51           C  
ANISOU 2198  CG  GLU C  86    14025  15243  30580   1153    822   -879       C  
ATOM   2199  CD  GLU C  86      69.422  88.733  43.489  1.00161.52           C  
ANISOU 2199  CD  GLU C  86    14487  15802  31082    763   1486  -1037       C  
ATOM   2200  OE1 GLU C  86      70.640  88.680  43.216  1.00161.33           O  
ANISOU 2200  OE1 GLU C  86    13986  15710  31604    850   1782  -1167       O  
ATOM   2201  OE2 GLU C  86      68.533  88.854  42.619  1.00158.35           O  
ANISOU 2201  OE2 GLU C  86    14514  15534  30115    341   1711  -1030       O  
HETATM 2202  N   MSE C  87      70.020  91.877  47.735  1.00158.29           N  
ANISOU 2202  N   MSE C  87    13642  15723  30776   1185   -882   -543       N  
HETATM 2203  CA  MSE C  87      70.019  93.212  48.326  1.00170.96           C  
ANISOU 2203  CA  MSE C  87    15249  17427  32278   1033  -1310   -498       C  
HETATM 2204  C   MSE C  87      70.484  93.176  49.777  1.00167.96           C  
ANISOU 2204  C   MSE C  87    14914  17127  31775   1192  -1768   -472       C  
HETATM 2205  O   MSE C  87      70.366  92.152  50.451  1.00168.72           O  
ANISOU 2205  O   MSE C  87    15152  17231  31724   1403  -1864   -435       O  
HETATM 2206  CB  MSE C  87      68.627  93.840  48.245  1.00176.55           C  
ANISOU 2206  CB  MSE C  87    16253  18169  32661    893  -1470   -462       C  
HETATM 2207  CG  MSE C  87      67.674  93.123  47.308  1.00180.95           C  
ANISOU 2207  CG  MSE C  87    16925  18689  33140    870  -1123   -454       C  
HETATM 2208 SE   MSE C  87      65.923  93.973  47.264  1.00257.38          SE  
ANISOU 2208 SE   MSE C  87    26969  28458  42365    679  -1396   -366      SE  
HETATM 2209  CE  MSE C  87      64.930  92.574  46.347  1.00119.17           C  
ANISOU 2209  CE  MSE C  87     9965  11001  24312    558   -909   -365       C  
ATOM   2210  N   SER C  88      71.011  94.301  50.249  1.00166.57           N  
ANISOU 2210  N   SER C  88    14607  17004  31679   1069  -2049   -482       N  
ATOM   2211  CA  SER C  88      71.574  94.384  51.592  1.00165.73           C  
ANISOU 2211  CA  SER C  88    14463  16995  31512   1171  -2475   -465       C  
ATOM   2212  C   SER C  88      70.497  94.296  52.666  1.00156.93           C  
ANISOU 2212  C   SER C  88    13714  15957  29956   1221  -2816   -478       C  
ATOM   2213  O   SER C  88      69.361  94.724  52.461  1.00146.53           O  
ANISOU 2213  O   SER C  88    12650  14624  28400   1121  -2806   -531       O  
ATOM   2214  CB  SER C  88      72.370  95.680  51.757  1.00166.80           C  
ANISOU 2214  CB  SER C  88    14359  17152  31866    993  -2654   -505       C  
ATOM   2215  OG  SER C  88      73.027  95.720  53.012  1.00167.49           O  
ANISOU 2215  OG  SER C  88    14346  17356  31938   1073  -3053   -487       O  
ATOM   2216  N   ASP C  89      70.869  93.736  53.812  1.00153.17           N  
ANISOU 2216  N   ASP C  89    13229  15572  29396   1373  -3125   -419       N  
ATOM   2217  CA  ASP C  89      69.944  93.555  54.924  1.00149.07           C  
ANISOU 2217  CA  ASP C  89    13007  15149  28485   1415  -3455   -434       C  
ATOM   2218  C   ASP C  89      69.588  94.890  55.568  1.00135.82           C  
ANISOU 2218  C   ASP C  89    11391  13529  26688   1234  -3740   -585       C  
ATOM   2219  O   ASP C  89      70.342  95.856  55.473  1.00149.17           O  
ANISOU 2219  O   ASP C  89    12862  15194  28620   1108  -3795   -636       O  
ATOM   2220  CB  ASP C  89      70.545  92.607  55.964  1.00163.98           C  
ANISOU 2220  CB  ASP C  89    14824  17112  30371   1606  -3745   -284       C  
ATOM   2221  CG  ASP C  89      69.555  92.225  57.048  1.00173.73           C  
ANISOU 2221  CG  ASP C  89    16359  18442  31209   1643  -4065   -274       C  
ATOM   2222  OD1 ASP C  89      68.333  92.314  56.799  1.00166.37           O  
ANISOU 2222  OD1 ASP C  89    15699  17500  30014   1584  -3946   -380       O  
ATOM   2223  OD2 ASP C  89      70.000  91.833  58.147  1.00185.79           O  
ANISOU 2223  OD2 ASP C  89    17827  20068  32698   1721  -4452   -148       O  
ATOM   2224  N   LEU C  90      68.429  94.938  56.214  1.00116.41           N  
ANISOU 2224  N   LEU C  90     9214  11132  23886   1223  -3905   -679       N  
ATOM   2225  CA  LEU C  90      67.943  96.168  56.821  1.00105.41           C  
ANISOU 2225  CA  LEU C  90     7886   9758  22406   1075  -4132   -882       C  
ATOM   2226  C   LEU C  90      68.719  96.523  58.084  1.00110.26           C  
ANISOU 2226  C   LEU C  90     8344  10503  23047   1035  -4554   -926       C  
ATOM   2227  O   LEU C  90      68.794  95.724  59.018  1.00115.18           O  
ANISOU 2227  O   LEU C  90     8996  11275  23491   1122  -4822   -837       O  
ATOM   2228  CB  LEU C  90      66.450  96.053  57.145  1.00105.83           C  
ANISOU 2228  CB  LEU C  90     8235   9862  22115   1087  -4158  -1006       C  
ATOM   2229  CG  LEU C  90      65.444  95.916  55.993  1.00109.46           C  
ANISOU 2229  CG  LEU C  90     8858  10235  22496   1079  -3806   -983       C  
ATOM   2230  CD1 LEU C  90      65.758  96.892  54.864  1.00114.31           C  
ANISOU 2230  CD1 LEU C  90     9349  10681  23404    945  -3594   -966       C  
ATOM   2231  CD2 LEU C  90      65.354  94.481  55.473  1.00 97.90           C  
ANISOU 2231  CD2 LEU C  90     7469   8786  20942   1213  -3586   -803       C  
ATOM   2232  N   ASN C  91      69.295  97.723  58.108  1.00116.80           N  
ANISOU 2232  N   ASN C  91     9003  11277  24099    881  -4639  -1044       N  
ATOM   2233  CA  ASN C  91      69.984  98.223  59.295  1.00110.74           C  
ANISOU 2233  CA  ASN C  91     8081  10661  23336    778  -5052  -1123       C  
ATOM   2234  C   ASN C  91      68.995  98.656  60.376  1.00113.92           C  
ANISOU 2234  C   ASN C  91     8685  11167  23434    687  -5323  -1380       C  
ATOM   2235  O   ASN C  91      67.812  98.860  60.100  1.00121.04           O  
ANISOU 2235  O   ASN C  91     9801  11976  24214    705  -5162  -1534       O  
ATOM   2236  CB  ASN C  91      70.931  99.374  58.939  1.00110.50           C  
ANISOU 2236  CB  ASN C  91     7793  10536  23657    614  -5041  -1184       C  
ATOM   2237  CG  ASN C  91      70.257 100.466  58.135  1.00111.11           C  
ANISOU 2237  CG  ASN C  91     7976  10361  23879    510  -4818  -1343       C  
ATOM   2238  OD1 ASN C  91      69.563 101.322  58.684  1.00107.90           O  
ANISOU 2238  OD1 ASN C  91     7692   9898  23408    417  -4963  -1591       O  
ATOM   2239  ND2 ASN C  91      70.474 100.452  56.824  1.00115.47           N  
ANISOU 2239  ND2 ASN C  91     8459  10757  24657    515  -4473  -1203       N  
ATOM   2240  N   ALA C  92      69.492  98.773  61.605  1.00111.22           N  
ANISOU 2240  N   ALA C  92     8251  11048  22960    567  -5739  -1433       N  
ATOM   2241  CA  ALA C  92      68.661  99.013  62.785  1.00111.84           C  
ANISOU 2241  CA  ALA C  92     8505  11309  22681    423  -6030  -1699       C  
ATOM   2242  C   ALA C  92      67.698 100.197  62.656  1.00135.85           C  
ANISOU 2242  C   ALA C  92    11666  14183  25767    316  -5882  -2093       C  
ATOM   2243  O   ALA C  92      66.601 100.161  63.209  1.00124.13           O  
ANISOU 2243  O   ALA C  92    10372  12788  24003    277  -5924  -2337       O  
ATOM   2244  CB  ALA C  92      69.548  99.204  64.002  1.00117.25           C  
ANISOU 2244  CB  ALA C  92     9044  12274  23231    204  -6493  -1707       C  
ATOM   2245  N   ASN C  93      68.109 101.244  61.944  1.00127.99           N  
ANISOU 2245  N   ASN C  93    10545  12940  25145    261  -5717  -2161       N  
ATOM   2246  CA  ASN C  93      67.231 102.387  61.690  1.00126.95           C  
ANISOU 2246  CA  ASN C  93    10503  12561  25171    206  -5571  -2486       C  
ATOM   2247  C   ASN C  93      65.974 101.951  60.954  1.00123.99           C  
ANISOU 2247  C   ASN C  93    10312  12067  24730    397  -5283  -2456       C  
ATOM   2248  O   ASN C  93      64.844 102.223  61.383  1.00134.76           O  
ANISOU 2248  O   ASN C  93    11802  13438  25963    392  -5279  -2754       O  
ATOM   2249  CB  ASN C  93      67.955 103.460  60.875  1.00121.12           C  
ANISOU 2249  CB  ASN C  93     9596  11535  24887    126  -5449  -2456       C  
ATOM   2250  CG  ASN C  93      69.049 104.148  61.658  1.00127.86           C  
ANISOU 2250  CG  ASN C  93    10268  12502  25811   -123  -5731  -2571       C  
ATOM   2251  OD1 ASN C  93      69.319 103.802  62.807  1.00134.55           O  
ANISOU 2251  OD1 ASN C  93    11114  13666  26345   -251  -6036  -2649       O  
ATOM   2252  ND2 ASN C  93      69.693 105.128  61.034  1.00132.24           N  
ANISOU 2252  ND2 ASN C  93    10672  12822  26751   -235  -5649  -2564       N  
ATOM   2253  N   GLN C  94      66.197 101.268  59.837  1.00112.78           N  
ANISOU 2253  N   GLN C  94     8894  10566  23391    532  -5026  -2115       N  
ATOM   2254  CA  GLN C  94      65.124 100.736  59.014  1.00113.76           C  
ANISOU 2254  CA  GLN C  94     9197  10624  23403    664  -4742  -2021       C  
ATOM   2255  C   GLN C  94      64.234  99.798  59.819  1.00107.84           C  
ANISOU 2255  C   GLN C  94     8606  10127  22243    736  -4844  -2101       C  
ATOM   2256  O   GLN C  94      63.013  99.814  59.673  1.00120.11           O  
ANISOU 2256  O   GLN C  94    10287  11671  23679    785  -4718  -2234       O  
ATOM   2257  CB  GLN C  94      65.710 100.020  57.796  1.00 98.03           C  
ANISOU 2257  CB  GLN C  94     7171   8575  21499    722  -4467  -1666       C  
ATOM   2258  CG  GLN C  94      66.447 100.958  56.854  1.00104.05           C  
ANISOU 2258  CG  GLN C  94     7770   9103  22662    613  -4339  -1586       C  
ATOM   2259  CD  GLN C  94      67.443 100.242  55.970  1.00 98.30           C  
ANISOU 2259  CD  GLN C  94     6897   8400  22054    628  -4132  -1308       C  
ATOM   2260  OE1 GLN C  94      68.071  99.274  56.387  1.00 99.40           O  
ANISOU 2260  OE1 GLN C  94     6966   8712  22092    717  -4194  -1203       O  
ATOM   2261  NE2 GLN C  94      67.597 100.720  54.742  1.00 97.94           N  
ANISOU 2261  NE2 GLN C  94     6776   8175  22262    540  -3895  -1187       N  
ATOM   2262  N   ARG C  95      64.851  99.000  60.684  1.00103.10           N  
ANISOU 2262  N   ARG C  95     7974   9761  21438    726  -5100  -2007       N  
ATOM   2263  CA  ARG C  95      64.111  98.081  61.541  1.00113.21           C  
ANISOU 2263  CA  ARG C  95     9400  11295  22319    744  -5272  -2053       C  
ATOM   2264  C   ARG C  95      63.192  98.835  62.499  1.00125.39           C  
ANISOU 2264  C   ARG C  95    11005  12957  23680    579  -5421  -2510       C  
ATOM   2265  O   ARG C  95      62.020  98.484  62.655  1.00135.00           O  
ANISOU 2265  O   ARG C  95    12353  14281  24659    591  -5348  -2665       O  
ATOM   2266  CB  ARG C  95      65.076  97.189  62.320  1.00112.81           C  
ANISOU 2266  CB  ARG C  95     9291  11444  22127    734  -5597  -1812       C  
ATOM   2267  CG  ARG C  95      65.878  96.258  61.430  1.00124.64           C  
ANISOU 2267  CG  ARG C  95    10717  12822  23816    923  -5406  -1413       C  
ATOM   2268  CD  ARG C  95      67.010  95.588  62.186  1.00145.41           C  
ANISOU 2268  CD  ARG C  95    13209  15598  26441    937  -5749  -1162       C  
ATOM   2269  NE  ARG C  95      67.723  94.640  61.335  1.00148.64           N  
ANISOU 2269  NE  ARG C  95    13529  15869  27080   1141  -5518   -836       N  
ATOM   2270  CZ  ARG C  95      67.478  93.335  61.306  1.00155.64           C  
ANISOU 2270  CZ  ARG C  95    14539  16739  27858   1312  -5499   -607       C  
ATOM   2271  NH1 ARG C  95      66.544  92.818  62.091  1.00155.72           N  
ANISOU 2271  NH1 ARG C  95    14771  16883  27514   1288  -5738   -630       N  
ATOM   2272  NH2 ARG C  95      68.171  92.545  60.499  1.00165.88           N  
ANISOU 2272  NH2 ARG C  95    15732  17882  29412   1488  -5242   -376       N  
ATOM   2273  N   LYS C  96      63.731  99.876  63.128  1.00132.25           N  
ANISOU 2273  N   LYS C  96    11775  13814  24660    393  -5601  -2760       N  
ATOM   2274  CA  LYS C  96      62.955 100.721  64.028  1.00123.85           C  
ANISOU 2274  CA  LYS C  96    10783  12824  23452    189  -5674  -3283       C  
ATOM   2275  C   LYS C  96      61.762 101.330  63.298  1.00124.72           C  
ANISOU 2275  C   LYS C  96    10905  12687  23795    321  -5349  -3502       C  
ATOM   2276  O   LYS C  96      60.644 101.340  63.820  1.00102.75           O  
ANISOU 2276  O   LYS C  96     8219  10027  20793    258  -5291  -3855       O  
ATOM   2277  CB  LYS C  96      63.833 101.824  64.624  1.00109.55           C  
ANISOU 2277  CB  LYS C  96     8869  10970  21784    -42  -5856  -3504       C  
ATOM   2278  N   GLN C  97      62.004 101.826  62.085  1.00123.27           N  
ANISOU 2278  N   GLN C  97    10623  12168  24044    478  -5138  -3282       N  
ATOM   2279  CA  GLN C  97      60.930 102.386  61.266  1.00128.49           C  
ANISOU 2279  CA  GLN C  97    11279  12577  24966    614  -4877  -3374       C  
ATOM   2280  C   GLN C  97      59.839 101.358  60.988  1.00119.84           C  
ANISOU 2280  C   GLN C  97    10300  11670  23564    737  -4718  -3267       C  
ATOM   2281  O   GLN C  97      58.650 101.627  61.191  1.00112.87           O  
ANISOU 2281  O   GLN C  97     9406  10813  22667    761  -4627  -3572       O  
ATOM   2282  CB  GLN C  97      61.476 102.919  59.940  1.00130.71           C  
ANISOU 2282  CB  GLN C  97    11496  12508  25660    688  -4713  -3048       C  
ATOM   2283  CG  GLN C  97      62.369 104.136  60.068  1.00136.81           C  
ANISOU 2283  CG  GLN C  97    12125  13030  26826    560  -4840  -3180       C  
ATOM   2284  CD  GLN C  97      62.399 104.958  58.795  1.00135.19           C  
ANISOU 2284  CD  GLN C  97    11860  12420  27086    600  -4682  -2975       C  
ATOM   2285  OE1 GLN C  97      61.387 105.531  58.390  1.00124.00           O  
ANISOU 2285  OE1 GLN C  97    10441  10770  25902    684  -4590  -3073       O  
ATOM   2286  NE2 GLN C  97      63.559 105.012  58.152  1.00136.86           N  
ANISOU 2286  NE2 GLN C  97    11998  12554  27448    519  -4665  -2676       N  
ATOM   2287  N   LEU C  98      60.256 100.185  60.521  1.00118.58           N  
ANISOU 2287  N   LEU C  98    10233  11635  23189    806  -4670  -2857       N  
ATOM   2288  CA  LEU C  98      59.328  99.112  60.184  1.00123.26           C  
ANISOU 2288  CA  LEU C  98    10952  12398  23484    897  -4516  -2714       C  
ATOM   2289  C   LEU C  98      58.471  98.714  61.380  1.00129.40           C  
ANISOU 2289  C   LEU C  98    11828  13491  23846    790  -4631  -3043       C  
ATOM   2290  O   LEU C  98      57.253  98.602  61.261  1.00139.40           O  
ANISOU 2290  O   LEU C  98    13206  14843  24918    818  -4406  -3166       O  
ATOM   2291  CB  LEU C  98      60.088  97.893  59.654  1.00121.27           C  
ANISOU 2291  CB  LEU C  98    10783  12191  23104    962  -4467  -2280       C  
ATOM   2292  CG  LEU C  98      60.746  98.050  58.280  1.00115.17           C  
ANISOU 2292  CG  LEU C  98    10000  11177  22584    989  -4210  -1967       C  
ATOM   2293  CD1 LEU C  98      61.545  96.810  57.918  1.00100.36           C  
ANISOU 2293  CD1 LEU C  98     8154   9353  20626   1049  -4149  -1643       C  
ATOM   2294  CD2 LEU C  98      59.706  98.349  57.213  1.00115.52           C  
ANISOU 2294  CD2 LEU C  98    10117  11120  22656   1001  -3939  -1914       C  
HETATM 2295  N   MSE C  99      59.108  98.511  62.529  1.00119.74           N  
ANISOU 2295  N   MSE C  99    10671  12463  22362    621  -4905  -3149       N  
HETATM 2296  CA  MSE C  99      58.379  98.153  63.742  1.00114.68           C  
ANISOU 2296  CA  MSE C  99    10287  12154  21132    421  -4933  -3434       C  
HETATM 2297  C   MSE C  99      57.395  99.245  64.149  1.00133.89           C  
ANISOU 2297  C   MSE C  99    12700  14565  23606    339  -4747  -3982       C  
HETATM 2298  O   MSE C  99      56.237  98.960  64.473  1.00141.42           O  
ANISOU 2298  O   MSE C  99    13806  15722  24206    288  -4528  -4194       O  
HETATM 2299  CB  MSE C  99      59.347  97.879  64.890  1.00108.36           C  
ANISOU 2299  CB  MSE C  99     9548  11569  20054    198  -5324  -3420       C  
HETATM 2300  CG  MSE C  99      58.664  97.744  66.238  1.00109.46           C  
ANISOU 2300  CG  MSE C  99     9967  12073  19551   -115  -5367  -3778       C  
HETATM 2301 SE   MSE C  99      59.921  97.404  67.685  1.00193.28          SE  
ANISOU 2301 SE   MSE C  99    20679  23007  29751   -475  -5955  -3679      SE  
HETATM 2302  CE  MSE C  99      60.310  95.529  67.313  1.00182.01           C  
ANISOU 2302  CE  MSE C  99    19401  21625  28128   -271  -6107  -2921       C  
ATOM   2303  N   ALA C 100      57.865 100.491  64.131  1.00145.01           N  
ANISOU 2303  N   ALA C 100    13908  15711  25479    322  -4817  -4224       N  
ATOM   2304  CA  ALA C 100      57.026 101.640  64.462  1.00145.66           C  
ANISOU 2304  CA  ALA C 100    13937  15661  25747    288  -4627  -4770       C  
ATOM   2305  C   ALA C 100      55.782 101.671  63.582  1.00145.97           C  
ANISOU 2305  C   ALA C 100    13912  15585  25965    532  -4303  -4731       C  
ATOM   2306  O   ALA C 100      54.682 101.966  64.051  1.00149.37           O  
ANISOU 2306  O   ALA C 100    14361  16110  26283    512  -4081  -5145       O  
ATOM   2307  CB  ALA C 100      57.812 102.934  64.315  1.00135.94           C  
ANISOU 2307  CB  ALA C 100    12502  14052  25096    264  -4749  -4935       C  
ATOM   2308  N   PHE C 101      55.966 101.356  62.305  1.00142.58           N  
ANISOU 2308  N   PHE C 101    13388  14977  25809    737  -4276  -4239       N  
ATOM   2309  CA  PHE C 101      54.850 101.263  61.377  1.00144.41           C  
ANISOU 2309  CA  PHE C 101    13560  15150  26159    927  -4031  -4102       C  
ATOM   2310  C   PHE C 101      53.924 100.113  61.762  1.00132.53           C  
ANISOU 2310  C   PHE C 101    12257  14057  24042    857  -3876  -4110       C  
ATOM   2311  O   PHE C 101      52.702 100.249  61.736  1.00146.14           O  
ANISOU 2311  O   PHE C 101    13926  15867  25732    910  -3659  -4316       O  
ATOM   2312  CB  PHE C 101      55.361 101.079  59.947  1.00150.75           C  
ANISOU 2312  CB  PHE C 101    14270  15731  27275   1065  -4046  -3559       C  
ATOM   2313  CG  PHE C 101      54.270 100.947  58.926  1.00152.57           C  
ANISOU 2313  CG  PHE C 101    14478  15939  27555   1195  -3834  -3348       C  
ATOM   2314  CD1 PHE C 101      53.671 102.072  58.384  1.00147.02           C  
ANISOU 2314  CD1 PHE C 101    13685  14934  27241   1283  -3738  -3393       C  
ATOM   2315  CD2 PHE C 101      53.846  99.698  58.502  1.00152.73           C  
ANISOU 2315  CD2 PHE C 101    14633  16228  27171   1180  -3727  -3073       C  
ATOM   2316  CE1 PHE C 101      52.668 101.956  57.443  1.00143.85           C  
ANISOU 2316  CE1 PHE C 101    13329  14558  26768   1324  -3565  -3130       C  
ATOM   2317  CE2 PHE C 101      52.844  99.574  57.561  1.00149.01           C  
ANISOU 2317  CE2 PHE C 101    14190  15779  26648   1224  -3533  -2863       C  
ATOM   2318  CZ  PHE C 101      52.254 100.704  57.030  1.00148.02           C  
ANISOU 2318  CZ  PHE C 101    13975  15406  26860   1288  -3465  -2873       C  
HETATM 2319  N   MSE C 102      54.521  98.984  62.126  1.00118.00           N  
ANISOU 2319  N   MSE C 102    10632  12454  21748    735  -3998  -3874       N  
HETATM 2320  CA  MSE C 102      53.778  97.783  62.490  1.00118.73           C  
ANISOU 2320  CA  MSE C 102    10973  12907  21231    623  -3878  -3815       C  
HETATM 2321  C   MSE C 102      52.917  97.976  63.733  1.00126.77           C  
ANISOU 2321  C   MSE C 102    12088  14224  21854    413  -3770  -4339       C  
HETATM 2322  O   MSE C 102      51.918  97.278  63.925  1.00128.33           O  
ANISOU 2322  O   MSE C 102    12421  14710  21629    316  -3573  -4393       O  
HETATM 2323  CB  MSE C 102      54.744  96.619  62.711  1.00131.34           C  
ANISOU 2323  CB  MSE C 102    12783  14611  22509    545  -4082  -3441       C  
HETATM 2324  CG  MSE C 102      55.349  96.079  61.432  1.00138.95           C  
ANISOU 2324  CG  MSE C 102    13692  15351  23752    732  -4060  -2947       C  
HETATM 2325 SE   MSE C 102      54.065  95.020  60.432  1.00234.34          SE  
ANISOU 2325 SE   MSE C 102    25942  27554  35543    759  -3716  -2710      SE  
HETATM 2326  CE  MSE C 102      53.842  93.580  61.728  1.00171.52           C  
ANISOU 2326  CE  MSE C 102    18407  19967  26798    510  -3783  -2699       C  
ATOM   2327  N   GLU C 103      53.309  98.921  64.580  1.00132.50           N  
ANISOU 2327  N   GLU C 103    12750  14896  22696    300  -3874  -4751       N  
ATOM   2328  CA  GLU C 103      52.557  99.184  65.800  1.00134.63           C  
ANISOU 2328  CA  GLU C 103    13117  15455  22581     49  -3727  -5328       C  
ATOM   2329  C   GLU C 103      51.203  99.817  65.502  1.00131.52           C  
ANISOU 2329  C   GLU C 103    12502  15010  22458    200  -3367  -5687       C  
ATOM   2330  O   GLU C 103      50.298  99.771  66.332  1.00140.06           O  
ANISOU 2330  O   GLU C 103    13640  16396  23178     12  -3132  -6135       O  
ATOM   2331  CB  GLU C 103      53.366 100.068  66.744  1.00146.72           C  
ANISOU 2331  CB  GLU C 103    14649  16927  24171   -152  -3916  -5712       C  
ATOM   2332  CG  GLU C 103      54.599  99.370  67.280  1.00157.99           C  
ANISOU 2332  CG  GLU C 103    16275  18517  25238   -358  -4310  -5385       C  
ATOM   2333  CD  GLU C 103      54.316  97.929  67.662  1.00164.69           C  
ANISOU 2333  CD  GLU C 103    17431  19748  25394   -521  -4345  -5085       C  
ATOM   2334  OE1 GLU C 103      53.526  97.706  68.604  1.00173.24           O  
ANISOU 2334  OE1 GLU C 103    18717  21192  25915   -817  -4193  -5435       O  
ATOM   2335  OE2 GLU C 103      54.873  97.020  67.011  1.00160.46           O  
ANISOU 2335  OE2 GLU C 103    16943  19137  24888   -368  -4498  -4512       O  
ATOM   2336  N   ALA C 104      51.065 100.399  64.315  1.00127.87           N  
ANISOU 2336  N   ALA C 104    11773  14176  22637    522  -3329  -5475       N  
ATOM   2337  CA  ALA C 104      49.773 100.895  63.861  1.00122.84           C  
ANISOU 2337  CA  ALA C 104    10874  13476  22325    717  -3050  -5677       C  
ATOM   2338  C   ALA C 104      48.840  99.719  63.599  1.00122.87           C  
ANISOU 2338  C   ALA C 104    10973  13863  21849    655  -2883  -5456       C  
ATOM   2339  O   ALA C 104      47.646  99.785  63.880  1.00126.54           O  
ANISOU 2339  O   ALA C 104    11302  14542  22237    639  -2613  -5790       O  
ATOM   2340  CB  ALA C 104      49.929 101.744  62.612  1.00118.46           C  
ANISOU 2340  CB  ALA C 104    10044  12432  22534   1036  -3130  -5389       C  
ATOM   2341  N   TRP C 105      49.403  98.642  63.061  1.00127.20           N  
ANISOU 2341  N   TRP C 105    11742  14487  22101    610  -3027  -4914       N  
ATOM   2342  CA  TRP C 105      48.660  97.409  62.823  1.00141.86           C  
ANISOU 2342  CA  TRP C 105    13765  16680  23455    493  -2887  -4676       C  
ATOM   2343  C   TRP C 105      48.302  96.710  64.124  1.00141.95           C  
ANISOU 2343  C   TRP C 105    14051  17130  22754    149  -2792  -4974       C  
ATOM   2344  O   TRP C 105      47.166  96.275  64.314  1.00140.48           O  
ANISOU 2344  O   TRP C 105    13863  17265  22247     17  -2541  -5137       O  
ATOM   2345  CB  TRP C 105      49.469  96.458  61.945  1.00153.13           C  
ANISOU 2345  CB  TRP C 105    15387  18003  24794    526  -3042  -4065       C  
ATOM   2346  CG  TRP C 105      49.355  96.743  60.492  1.00153.18           C  
ANISOU 2346  CG  TRP C 105    15185  17750  25266    749  -3025  -3718       C  
ATOM   2347  CD1 TRP C 105      49.972  97.743  59.800  1.00161.36           C  
ANISOU 2347  CD1 TRP C 105    16000  18396  26912    950  -3152  -3609       C  
ATOM   2348  CD2 TRP C 105      48.579  96.012  59.541  1.00127.65           C  
ANISOU 2348  CD2 TRP C 105    11973  14647  21881    730  -2885  -3416       C  
ATOM   2349  NE1 TRP C 105      49.624  97.681  58.473  1.00153.79           N  
ANISOU 2349  NE1 TRP C 105    14933  17332  26168   1049  -3109  -3236       N  
ATOM   2350  CE2 TRP C 105      48.770  96.626  58.288  1.00130.35           C  
ANISOU 2350  CE2 TRP C 105    12106  14689  22734    914  -2949  -3121       C  
ATOM   2351  CE3 TRP C 105      47.740  94.899  59.627  1.00118.16           C  
ANISOU 2351  CE3 TRP C 105    10963  13797  20135    529  -2715  -3362       C  
ATOM   2352  CZ2 TRP C 105      48.153  96.164  57.130  1.00122.36           C  
ANISOU 2352  CZ2 TRP C 105    11071  13746  21673    888  -2864  -2781       C  
ATOM   2353  CZ3 TRP C 105      47.129  94.442  58.478  1.00124.78           C  
ANISOU 2353  CZ3 TRP C 105    11767  14685  20957    516  -2619  -3047       C  
ATOM   2354  CH2 TRP C 105      47.338  95.074  57.245  1.00125.86           C  
ANISOU 2354  CH2 TRP C 105    11695  14547  21580    688  -2700  -2762       C  
ATOM   2355  N   ARG C 106      49.287  96.588  65.007  1.00148.72           N  
ANISOU 2355  N   ARG C 106    15141  18022  23345    -31  -3011  -5016       N  
ATOM   2356  CA  ARG C 106      49.070  95.963  66.304  1.00160.45           C  
ANISOU 2356  CA  ARG C 106    16935  19928  24101   -423  -2981  -5255       C  
ATOM   2357  C   ARG C 106      48.021  96.732  67.100  1.00173.16           C  
ANISOU 2357  C   ARG C 106    18385  21760  25650   -562  -2661  -5954       C  
ATOM   2358  O   ARG C 106      47.218  96.140  67.820  1.00180.24           O  
ANISOU 2358  O   ARG C 106    19448  23079  25956   -875  -2451  -6173       O  
ATOM   2359  CB  ARG C 106      50.381  95.883  67.089  1.00169.78           C  
ANISOU 2359  CB  ARG C 106    18338  21090  25080   -592  -3344  -5160       C  
ATOM   2360  N   ASN C 107      48.031  98.055  66.958  1.00171.20           N  
ANISOU 2360  N   ASN C 107    17808  21205  26035   -339  -2602  -6314       N  
ATOM   2361  CA  ASN C 107      47.072  98.909  67.650  1.00164.46           C  
ANISOU 2361  CA  ASN C 107    16742  20468  25278   -405  -2256  -7039       C  
ATOM   2362  C   ASN C 107      45.682  98.862  67.023  1.00167.61           C  
ANISOU 2362  C   ASN C 107    16829  20966  25890   -222  -1925  -7108       C  
ATOM   2363  O   ASN C 107      44.674  98.923  67.726  1.00173.88           O  
ANISOU 2363  O   ASN C 107    17531  22088  26448   -401  -1576  -7628       O  
ATOM   2364  CB  ASN C 107      47.572 100.354  67.678  1.00153.51           C  
ANISOU 2364  CB  ASN C 107    15116  18633  24579   -207  -2304  -7397       C  
ATOM   2365  CG  ASN C 107      46.548 101.312  68.241  1.00155.99           C  
ANISOU 2365  CG  ASN C 107    15153  18955  25163   -188  -1899  -8169       C  
ATOM   2366  OD1 ASN C 107      45.740 101.879  67.505  1.00158.49           O  
ANISOU 2366  OD1 ASN C 107    15077  19033  26108    168  -1717  -8228       O  
ATOM   2367  ND2 ASN C 107      46.573 101.499  69.556  1.00160.82           N  
ANISOU 2367  ND2 ASN C 107    15955  19842  25309   -583  -1754  -8771       N  
ATOM   2368  N   GLU C 108      45.633  98.760  65.698  1.00169.85           N  
ANISOU 2368  N   GLU C 108    16933  20993  26611    104  -2035  -6590       N  
ATOM   2369  CA  GLU C 108      44.362  98.729  64.982  1.00168.24           C  
ANISOU 2369  CA  GLU C 108    16394  20882  26645    278  -1801  -6566       C  
ATOM   2370  C   GLU C 108      43.648  97.391  65.157  1.00173.23           C  
ANISOU 2370  C   GLU C 108    17247  22032  26540    -36  -1648  -6418       C  
ATOM   2371  O   GLU C 108      42.419  97.336  65.197  1.00177.51           O  
ANISOU 2371  O   GLU C 108    17535  22858  27051    -73  -1352  -6671       O  
ATOM   2372  CB  GLU C 108      44.576  99.015  63.495  1.00156.39           C  
ANISOU 2372  CB  GLU C 108    14681  18981  25760    642  -2007  -6015       C  
ATOM   2373  N   GLN C 109      44.422  96.316  65.262  1.00175.71           N  
ANISOU 2373  N   GLN C 109    18016  22450  26297   -262  -1850  -6005       N  
ATOM   2374  CA  GLN C 109      43.855  94.977  65.396  1.00171.63           C  
ANISOU 2374  CA  GLN C 109    17784  22349  25080   -585  -1736  -5802       C  
ATOM   2375  C   GLN C 109      43.411  94.683  66.828  1.00175.95           C  
ANISOU 2375  C   GLN C 109    18544  23356  24951  -1028  -1524  -6284       C  
ATOM   2376  O   GLN C 109      42.622  93.769  67.064  1.00187.90           O  
ANISOU 2376  O   GLN C 109    20214  25270  25911  -1340  -1330  -6265       O  
ATOM   2377  CB  GLN C 109      44.866  93.924  64.936  1.00162.63           C  
ANISOU 2377  CB  GLN C 109    17053  21067  23672   -631  -2026  -5164       C  
ATOM   2378  N   SER C 110      43.921  95.462  67.779  1.00162.90           N  
ANISOU 2378  N   SER C 110    16919  21661  23316  -1108  -1554  -6721       N  
ATOM   2379  CA  SER C 110      43.610  95.259  69.191  1.00141.90           C  
ANISOU 2379  CA  SER C 110    14503  19454  19959  -1600  -1363  -7205       C  
ATOM   2380  C   SER C 110      42.132  95.491  69.485  1.00132.84           C  
ANISOU 2380  C   SER C 110    13035  18670  18770  -1714   -860  -7769       C  
ATOM   2381  O   SER C 110      41.655  95.187  70.578  1.00121.80           O  
ANISOU 2381  O   SER C 110    11828  17734  16718  -2186   -608  -8179       O  
ATOM   2382  CB  SER C 110      44.465  96.182  70.063  1.00142.29           C  
ANISOU 2382  CB  SER C 110    14613  19365  20085  -1675  -1493  -7605       C  
TER    2383      SER C 110                                                      
ATOM   2384  N   LYS D   2      51.817  31.117  44.462  1.00123.39           N  
ANISOU 2384  N   LYS D   2    14649  14751  17484    398    761   1038       N  
ATOM   2385  CA  LYS D   2      51.829  31.314  43.017  1.00125.01           C  
ANISOU 2385  CA  LYS D   2    14900  14762  17836    409   1110    983       C  
ATOM   2386  C   LYS D   2      51.020  30.233  42.303  1.00133.44           C  
ANISOU 2386  C   LYS D   2    15974  15764  18963    393   1216    948       C  
ATOM   2387  O   LYS D   2      51.058  29.065  42.692  1.00146.08           O  
ANISOU 2387  O   LYS D   2    17465  17319  20720    369   1109    944       O  
ATOM   2388  CB  LYS D   2      53.267  31.327  42.494  1.00115.66           C  
ANISOU 2388  CB  LYS D   2    13654  13261  17032    375   1396    851       C  
ATOM   2389  N   SER D   3      50.290  30.624  41.261  1.00117.99           N  
ANISOU 2389  N   SER D   3    14165  13788  16878    406   1431    910       N  
ATOM   2390  CA  SER D   3      49.510  29.670  40.473  1.00 94.48           C  
ANISOU 2390  CA  SER D   3    11255  10774  13870    338   1553    826       C  
ATOM   2391  C   SER D   3      49.704  29.872  38.968  1.00 86.68           C  
ANISOU 2391  C   SER D   3    10475   9748  12712    107   1882    570       C  
ATOM   2392  O   SER D   3      50.220  30.899  38.527  1.00 88.25           O  
ANISOU 2392  O   SER D   3    10774   9964  12793     37   2006    502       O  
ATOM   2393  CB  SER D   3      48.024  29.763  40.832  1.00 86.33           C  
ANISOU 2393  CB  SER D   3    10271  10067  12462    361   1266    967       C  
ATOM   2394  OG  SER D   3      47.564  31.101  40.807  1.00 72.19           O  
ANISOU 2394  OG  SER D   3     8601   8499  10329    339   1163    991       O  
ATOM   2395  N   VAL D   4      49.278  28.883  38.188  1.00 93.45           N  
ANISOU 2395  N   VAL D   4    11377  10569  13563     -8   2009    433       N  
ATOM   2396  CA  VAL D   4      49.566  28.834  36.754  1.00 96.14           C  
ANISOU 2396  CA  VAL D   4    11860  10850  13820   -220   2334    161       C  
ATOM   2397  C   VAL D   4      48.312  28.581  35.914  1.00 78.68           C  
ANISOU 2397  C   VAL D   4     9841   8837  11216   -341   2308    137       C  
ATOM   2398  O   VAL D   4      47.481  27.755  36.274  1.00 63.08           O  
ANISOU 2398  O   VAL D   4     7822   6915   9231   -287   2150    229       O  
ATOM   2399  CB  VAL D   4      50.610  27.733  36.450  1.00 97.91           C  
ANISOU 2399  CB  VAL D   4    11899  10737  14566   -264   2590    -90       C  
ATOM   2400  CG1 VAL D   4      50.695  27.451  34.962  1.00 81.25           C  
ANISOU 2400  CG1 VAL D   4     9913   8603  12354   -499   2908   -400       C  
ATOM   2401  CG2 VAL D   4      51.971  28.121  37.006  1.00115.29           C  
ANISOU 2401  CG2 VAL D   4    13938  12701  17166   -189   2658   -127       C  
ATOM   2402  N   PHE D   5      48.168  29.300  34.804  1.00 71.02           N  
ANISOU 2402  N   PHE D   5     9079   7967   9937   -503   2447     22       N  
ATOM   2403  CA  PHE D   5      47.047  29.071  33.897  1.00 51.73           C  
ANISOU 2403  CA  PHE D   5     6827   5668   7162   -621   2431    -19       C  
ATOM   2404  C   PHE D   5      47.515  28.542  32.551  1.00 76.51           C  
ANISOU 2404  C   PHE D   5    10043   8682  10345   -826   2779   -321       C  
ATOM   2405  O   PHE D   5      48.133  29.265  31.771  1.00 86.65           O  
ANISOU 2405  O   PHE D   5    11422   9955  11545   -963   2974   -455       O  
ATOM   2406  CB  PHE D   5      46.243  30.353  33.697  1.00 50.19           C  
ANISOU 2406  CB  PHE D   5     6803   5700   6565   -643   2238    112       C  
ATOM   2407  CG  PHE D   5      45.534  30.818  34.932  1.00 60.57           C  
ANISOU 2407  CG  PHE D   5     8027   7177   7810   -482   1877    356       C  
ATOM   2408  CD1 PHE D   5      44.273  30.340  35.242  1.00 55.66           C  
ANISOU 2408  CD1 PHE D   5     7407   6689   7053   -447   1641    455       C  
ATOM   2409  CD2 PHE D   5      46.130  31.727  35.788  1.00 71.16           C  
ANISOU 2409  CD2 PHE D   5     9270   8536   9232   -383   1779    459       C  
ATOM   2410  CE1 PHE D   5      43.619  30.764  36.380  1.00 68.10           C  
ANISOU 2410  CE1 PHE D   5     8877   8417   8579   -346   1322    619       C  
ATOM   2411  CE2 PHE D   5      45.480  32.155  36.930  1.00 70.51           C  
ANISOU 2411  CE2 PHE D   5     9092   8602   9096   -263   1459    628       C  
ATOM   2412  CZ  PHE D   5      44.224  31.671  37.226  1.00 68.20           C  
ANISOU 2412  CZ  PHE D   5     8797   8443   8675   -257   1237    687       C  
ATOM   2413  N   VAL D   6      47.207  27.278  32.278  1.00 82.51           N  
ANISOU 2413  N   VAL D   6    10750   9360  11240   -860   2856   -438       N  
ATOM   2414  CA  VAL D   6      47.586  26.655  31.017  1.00 70.34           C  
ANISOU 2414  CA  VAL D   6     9250   7714   9760  -1070   3180   -760       C  
ATOM   2415  C   VAL D   6      46.400  26.591  30.072  1.00 68.06           C  
ANISOU 2415  C   VAL D   6     9201   7589   9068  -1194   3138   -770       C  
ATOM   2416  O   VAL D   6      45.332  26.135  30.451  1.00 84.07           O  
ANISOU 2416  O   VAL D   6    11256   9703  10983  -1102   2917   -616       O  
ATOM   2417  CB  VAL D   6      48.123  25.238  31.229  1.00 66.47           C  
ANISOU 2417  CB  VAL D   6     8503   6990   9763  -1047   3314   -948       C  
ATOM   2418  CG1 VAL D   6      48.633  24.668  29.908  1.00 52.21           C  
ANISOU 2418  CG1 VAL D   6     6699   5085   8053  -1289   3665  -1333       C  
ATOM   2419  CG2 VAL D   6      49.217  25.245  32.282  1.00 80.40           C  
ANISOU 2419  CG2 VAL D   6    10010   8550  11989   -899   3290   -913       C  
ATOM   2420  N   GLU D   7      46.588  27.045  28.841  1.00 69.37           N  
ANISOU 2420  N   GLU D   7     9536   7792   9029  -1410   3345   -949       N  
ATOM   2421  CA  GLU D   7      45.500  27.053  27.874  1.00 76.33           C  
ANISOU 2421  CA  GLU D   7    10651   8808   9543  -1544   3300   -958       C  
ATOM   2422  C   GLU D   7      45.640  25.936  26.847  1.00 73.24           C  
ANISOU 2422  C   GLU D   7    10245   8341   9242  -1734   3579  -1262       C  
ATOM   2423  O   GLU D   7      46.741  25.632  26.383  1.00 69.01           O  
ANISOU 2423  O   GLU D   7     9586   7684   8949  -1863   3885  -1535       O  
ATOM   2424  CB  GLU D   7      45.427  28.408  27.162  1.00 82.14           C  
ANISOU 2424  CB  GLU D   7    11600   9664   9946  -1670   3293   -916       C  
ATOM   2425  CG  GLU D   7      45.096  29.578  28.081  1.00102.45           C  
ANISOU 2425  CG  GLU D   7    14180  12336  12410  -1494   2991   -631       C  
ATOM   2426  CD  GLU D   7      45.095  30.917  27.361  1.00111.84           C  
ANISOU 2426  CD  GLU D   7    15548  13620  13326  -1624   2996   -606       C  
ATOM   2427  OE1 GLU D   7      45.833  31.061  26.363  1.00120.92           O  
ANISOU 2427  OE1 GLU D   7    16773  14736  14434  -1837   3285   -807       O  
ATOM   2428  OE2 GLU D   7      44.355  31.828  27.792  1.00106.66           O1+
ANISOU 2428  OE2 GLU D   7    14940  13073  12514  -1525   2716   -398       O1+
ATOM   2429  N   SER D   8      44.511  25.318  26.515  1.00 75.27           N  
ANISOU 2429  N   SER D   8    10606   8668   9323  -1751   3467  -1227       N  
ATOM   2430  CA  SER D   8      44.434  24.387  25.400  1.00 74.72           C  
ANISOU 2430  CA  SER D   8    10561   8575   9252  -1951   3705  -1502       C  
ATOM   2431  C   SER D   8      44.356  25.185  24.113  1.00 82.26           C  
ANISOU 2431  C   SER D   8    11759   9642   9854  -2195   3833  -1593       C  
ATOM   2432  O   SER D   8      43.906  26.332  24.123  1.00106.45           O  
ANISOU 2432  O   SER D   8    14998  12809  12639  -2179   3646  -1389       O  
ATOM   2433  CB  SER D   8      43.216  23.478  25.525  1.00 82.08           C  
ANISOU 2433  CB  SER D   8    11526   9548  10114  -1876   3525  -1414       C  
ATOM   2434  OG  SER D   8      42.028  24.210  25.283  1.00 87.14           O  
ANISOU 2434  OG  SER D   8    12416  10335  10357  -1879   3273  -1203       O  
ATOM   2435  N   THR D   9      44.782  24.582  23.009  1.00 77.95           N  
ANISOU 2435  N   THR D   9    11203   9078   9336  -2426   4145  -1907       N  
ATOM   2436  CA  THR D   9      44.780  25.268  21.721  1.00 84.78           C  
ANISOU 2436  CA  THR D   9    12293  10056   9865  -2691   4299  -2014       C  
ATOM   2437  C   THR D   9      43.378  25.756  21.366  1.00 84.59           C  
ANISOU 2437  C   THR D   9    12536  10164   9439  -2701   4026  -1783       C  
ATOM   2438  O   THR D   9      43.213  26.829  20.788  1.00111.33           O  
ANISOU 2438  O   THR D   9    16124  13639  12536  -2824   3989  -1706       O  
ATOM   2439  CB  THR D   9      45.310  24.360  20.594  1.00 88.95           C  
ANISOU 2439  CB  THR D   9    12749  10565  10481  -2942   4669  -2408       C  
ATOM   2440  OG1 THR D   9      44.404  23.270  20.384  1.00 92.77           O  
ANISOU 2440  OG1 THR D   9    13227  11067  10953  -2923   4609  -2444       O  
ATOM   2441  CG2 THR D   9      46.687  23.816  20.956  1.00 75.89           C  
ANISOU 2441  CG2 THR D   9    10780   8746   9309  -2932   4929  -2677       C  
ATOM   2442  N   ILE D  10      42.374  24.968  21.734  1.00 56.02           N  
ANISOU 2442  N   ILE D  10     8906   6546   5834  -2572   3831  -1679       N  
ATOM   2443  CA  ILE D  10      40.977  25.330  21.518  1.00 85.75           C  
ANISOU 2443  CA  ILE D  10    12884  10405   9291  -2556   3546  -1467       C  
ATOM   2444  C   ILE D  10      40.629  26.616  22.271  1.00 84.27           C  
ANISOU 2444  C   ILE D  10    12758  10255   9005  -2406   3246  -1182       C  
ATOM   2445  O   ILE D  10      40.129  27.591  21.684  1.00 97.66           O  
ANISOU 2445  O   ILE D  10    14647  12025  10436  -2512   3147  -1095       O  
ATOM   2446  CB  ILE D  10      40.025  24.195  21.967  1.00 78.34           C  
ANISOU 2446  CB  ILE D  10    11882   9445   8439  -2416   3385  -1406       C  
ATOM   2447  CG1 ILE D  10      40.198  22.956  21.084  1.00 77.73           C  
ANISOU 2447  CG1 ILE D  10    11750   9352   8432  -2576   3667  -1700       C  
ATOM   2448  CG2 ILE D  10      38.580  24.665  21.944  1.00 82.22           C  
ANISOU 2448  CG2 ILE D  10    12558  10009   8673  -2367   3055  -1173       C  
ATOM   2449  CD1 ILE D  10      41.277  21.992  21.558  1.00 87.28           C  
ANISOU 2449  CD1 ILE D  10    12659  10439  10064  -2519   3896  -1920       C  
ATOM   2450  N   PHE D  11      40.905  26.605  23.572  1.00 61.90           N  
ANISOU 2450  N   PHE D  11     9744   7371   6404  -2166   3106  -1050       N  
ATOM   2451  CA  PHE D  11      40.686  27.766  24.420  1.00 65.18           C  
ANISOU 2451  CA  PHE D  11    10157   7830   6777  -2006   2837   -808       C  
ATOM   2452  C   PHE D  11      41.447  28.971  23.878  1.00 72.36           C  
ANISOU 2452  C   PHE D  11    11156   8771   7566  -2143   2966   -845       C  
ATOM   2453  O   PHE D  11      40.899  30.068  23.798  1.00 77.80           O  
ANISOU 2453  O   PHE D  11    11961   9530   8070  -2148   2778   -700       O  
ATOM   2454  CB  PHE D  11      41.111  27.475  25.866  1.00 64.42           C  
ANISOU 2454  CB  PHE D  11     9829   7684   6965  -1754   2730   -697       C  
ATOM   2455  CG  PHE D  11      40.752  28.571  26.836  1.00 67.12           C  
ANISOU 2455  CG  PHE D  11    10134   8099   7272  -1576   2429   -454       C  
ATOM   2456  CD1 PHE D  11      39.560  28.528  27.539  1.00 66.83           C  
ANISOU 2456  CD1 PHE D  11    10069   8124   7198  -1426   2111   -279       C  
ATOM   2457  CD2 PHE D  11      41.607  29.646  27.042  1.00 64.59           C  
ANISOU 2457  CD2 PHE D  11     9785   7788   6970  -1568   2476   -421       C  
ATOM   2458  CE1 PHE D  11      39.227  29.537  28.427  1.00 75.21           C  
ANISOU 2458  CE1 PHE D  11    11055   9265   8258  -1280   1854    -98       C  
ATOM   2459  CE2 PHE D  11      41.278  30.656  27.926  1.00 45.26           C  
ANISOU 2459  CE2 PHE D  11     7275   5417   4504  -1412   2210   -218       C  
ATOM   2460  CZ  PHE D  11      40.088  30.602  28.620  1.00 59.01           C  
ANISOU 2460  CZ  PHE D  11     8969   7227   6224  -1271   1904    -67       C  
ATOM   2461  N   GLU D  12      42.708  28.761  23.509  1.00 64.88           N  
ANISOU 2461  N   GLU D  12    10138   7764   6749  -2262   3292  -1053       N  
ATOM   2462  CA  GLU D  12      43.542  29.835  22.980  1.00 78.24           C  
ANISOU 2462  CA  GLU D  12    11906   9484   8338  -2409   3450  -1109       C  
ATOM   2463  C   GLU D  12      42.913  30.461  21.742  1.00 88.93           C  
ANISOU 2463  C   GLU D  12    13520  10935   9335  -2644   3455  -1122       C  
ATOM   2464  O   GLU D  12      42.915  31.683  21.577  1.00104.96           O  
ANISOU 2464  O   GLU D  12    15657  13022  11199  -2692   3373  -1013       O  
ATOM   2465  CB  GLU D  12      44.941  29.318  22.644  1.00 90.54           C  
ANISOU 2465  CB  GLU D  12    13331  10952  10117  -2536   3836  -1392       C  
ATOM   2466  CG  GLU D  12      45.860  30.383  22.065  1.00121.74           C  
ANISOU 2466  CG  GLU D  12    17357  14934  13965  -2708   4027  -1470       C  
ATOM   2467  CD  GLU D  12      46.934  29.809  21.161  1.00139.63           C  
ANISOU 2467  CD  GLU D  12    19562  17149  16341  -2954   4451  -1828       C  
ATOM   2468  OE1 GLU D  12      47.011  28.568  21.041  1.00150.27           O  
ANISOU 2468  OE1 GLU D  12    20779  18427  17888  -2975   4594  -2025       O  
ATOM   2469  OE2 GLU D  12      47.696  30.600  20.565  1.00136.29           O  
ANISOU 2469  OE2 GLU D  12    19208  16760  15817  -3133   4643  -1925       O  
ATOM   2470  N   LYS D  13      42.367  29.611  20.880  1.00 86.72           N  
ANISOU 2470  N   LYS D  13    13333  10671   8945  -2794   3548  -1253       N  
ATOM   2471  CA  LYS D  13      41.737  30.064  19.648  1.00 81.66           C  
ANISOU 2471  CA  LYS D  13    12944  10118   7966  -3037   3561  -1273       C  
ATOM   2472  C   LYS D  13      40.487  30.889  19.923  1.00 85.29           C  
ANISOU 2472  C   LYS D  13    13521  10621   8265  -2935   3186  -1007       C  
ATOM   2473  O   LYS D  13      40.325  31.982  19.380  1.00 98.13           O  
ANISOU 2473  O   LYS D  13    15307  12302   9675  -3065   3132   -938       O  
ATOM   2474  CB  LYS D  13      41.389  28.871  18.752  1.00 85.13           C  
ANISOU 2474  CB  LYS D  13    13433  10569   8344  -3200   3733  -1471       C  
ATOM   2475  CG  LYS D  13      42.589  28.270  18.035  1.00 99.89           C  
ANISOU 2475  CG  LYS D  13    15224  12425  10306  -3410   4158  -1804       C  
ATOM   2476  CD  LYS D  13      42.176  27.179  17.051  1.00115.65           C  
ANISOU 2476  CD  LYS D  13    17271  14459  12211  -3591   4327  -2015       C  
ATOM   2477  CE  LYS D  13      43.380  26.658  16.270  1.00129.90           C  
ANISOU 2477  CE  LYS D  13    18976  16263  14117  -3829   4767  -2392       C  
ATOM   2478  NZ  LYS D  13      43.006  25.647  15.241  1.00131.57           N  
ANISOU 2478  NZ  LYS D  13    19230  16535  14226  -4024   4949  -2627       N  
ATOM   2479  N   TYR D  14      39.609  30.375  20.778  1.00 81.68           N  
ANISOU 2479  N   TYR D  14    12970  10134   7931  -2711   2930   -872       N  
ATOM   2480  CA  TYR D  14      38.312  31.023  20.969  1.00 82.83           C  
ANISOU 2480  CA  TYR D  14    13201  10309   7960  -2635   2592   -670       C  
ATOM   2481  C   TYR D  14      38.250  32.038  22.116  1.00 78.77           C  
ANISOU 2481  C   TYR D  14    12566   9804   7559  -2418   2343   -478       C  
ATOM   2482  O   TYR D  14      37.191  32.605  22.382  1.00 72.98           O  
ANISOU 2482  O   TYR D  14    11858   9090   6781  -2347   2069   -337       O  
ATOM   2483  CB  TYR D  14      37.233  29.958  21.172  1.00 86.25           C  
ANISOU 2483  CB  TYR D  14    13609  10718   8445  -2540   2446   -642       C  
ATOM   2484  CG  TYR D  14      36.780  29.329  19.878  1.00101.88           C  
ANISOU 2484  CG  TYR D  14    15768  12718  10225  -2773   2589   -774       C  
ATOM   2485  CD1 TYR D  14      37.602  28.447  19.187  1.00113.23           C  
ANISOU 2485  CD1 TYR D  14    17197  14155  11670  -2930   2924  -1007       C  
ATOM   2486  CD2 TYR D  14      35.536  29.629  19.338  1.00103.38           C  
ANISOU 2486  CD2 TYR D  14    16121  12927  10232  -2845   2397   -683       C  
ATOM   2487  CE1 TYR D  14      37.196  27.875  17.996  1.00122.55           C  
ANISOU 2487  CE1 TYR D  14    18530  15375  12657  -3150   3064  -1142       C  
ATOM   2488  CE2 TYR D  14      35.120  29.062  18.148  1.00125.18           C  
ANISOU 2488  CE2 TYR D  14    19053  15714  12797  -3061   2524   -796       C  
ATOM   2489  CZ  TYR D  14      35.953  28.185  17.481  1.00132.03           C  
ANISOU 2489  CZ  TYR D  14    19911  16601  13651  -3213   2857  -1024       C  
ATOM   2490  OH  TYR D  14      35.544  27.616  16.296  1.00134.71           O  
ANISOU 2490  OH  TYR D  14    20410  16987  13787  -3433   2991  -1152       O  
ATOM   2491  N   ARG D  15      39.373  32.287  22.780  1.00 65.93           N  
ANISOU 2491  N   ARG D  15    10798   8163   6092  -2323   2445   -487       N  
ATOM   2492  CA  ARG D  15      39.359  33.151  23.957  1.00 70.08           C  
ANISOU 2492  CA  ARG D  15    11178   8708   6741  -2104   2217   -313       C  
ATOM   2493  C   ARG D  15      39.035  34.612  23.635  1.00 83.24           C  
ANISOU 2493  C   ARG D  15    12956  10430   8243  -2181   2090   -215       C  
ATOM   2494  O   ARG D  15      38.261  35.251  24.348  1.00 65.83           O  
ANISOU 2494  O   ARG D  15    10676   8253   6083  -2040   1818    -74       O  
ATOM   2495  CB  ARG D  15      40.698  33.086  24.690  1.00 71.05           C  
ANISOU 2495  CB  ARG D  15    11129   8797   7071  -1997   2372   -344       C  
ATOM   2496  CG  ARG D  15      40.642  33.719  26.069  1.00 84.85           C  
ANISOU 2496  CG  ARG D  15    12690  10575   8974  -1745   2128   -162       C  
ATOM   2497  CD  ARG D  15      42.000  34.226  26.521  1.00106.23           C  
ANISOU 2497  CD  ARG D  15    15287  13262  11812  -1699   2276   -171       C  
ATOM   2498  NE  ARG D  15      42.481  35.336  25.698  1.00107.33           N  
ANISOU 2498  NE  ARG D  15    15566  13432  11783  -1875   2396   -203       N  
ATOM   2499  CZ  ARG D  15      42.073  36.595  25.828  1.00 93.91           C  
ANISOU 2499  CZ  ARG D  15    13899  11800   9984  -1854   2210    -71       C  
ATOM   2500  NH1 ARG D  15      41.167  36.912  26.741  1.00111.94           N1+
ANISOU 2500  NH1 ARG D  15    16070  14129  12333  -1669   1909     79       N1+
ATOM   2501  NH2 ARG D  15      42.567  37.539  25.041  1.00 75.68           N  
ANISOU 2501  NH2 ARG D  15    11722   9516   7517  -2030   2336   -100       N  
ATOM   2502  N   ASP D  16      39.631  35.132  22.564  1.00105.55           N  
ANISOU 2502  N   ASP D  16    15948  13273  10883  -2418   2296   -304       N  
ATOM   2503  CA  ASP D  16      39.513  36.548  22.216  1.00 97.04           C  
ANISOU 2503  CA  ASP D  16    14979  12244   9646  -2514   2206   -216       C  
ATOM   2504  C   ASP D  16      38.083  36.961  21.888  1.00 74.61           C  
ANISOU 2504  C   ASP D  16    12256   9419   6673  -2559   1952   -122       C  
ATOM   2505  O   ASP D  16      37.715  38.122  22.043  1.00 76.83           O  
ANISOU 2505  O   ASP D  16    12553   9728   6912  -2550   1778    -10       O  
ATOM   2506  CB  ASP D  16      40.413  36.883  21.022  1.00110.87           C  
ANISOU 2506  CB  ASP D  16    16907  14020  11199  -2800   2500   -345       C  
ATOM   2507  CG  ASP D  16      41.764  36.201  21.097  1.00131.66           C  
ANISOU 2507  CG  ASP D  16    19434  16617  13973  -2813   2814   -508       C  
ATOM   2508  OD1 ASP D  16      42.108  35.674  22.176  1.00138.82           O1+
ANISOU 2508  OD1 ASP D  16    20130  17477  15140  -2582   2781   -485       O1+
ATOM   2509  OD2 ASP D  16      42.483  36.197  20.073  1.00140.98           O  
ANISOU 2509  OD2 ASP D  16    20737  17816  15011  -3069   3101   -669       O  
ATOM   2510  N   GLU D  17      37.285  36.005  21.429  1.00 66.57           N  
ANISOU 2510  N   GLU D  17    11314   8376   5605  -2614   1938   -174       N  
ATOM   2511  CA  GLU D  17      35.949  36.296  20.926  1.00 69.75           C  
ANISOU 2511  CA  GLU D  17    11853   8776   5873  -2699   1736   -109       C  
ATOM   2512  C   GLU D  17      34.905  36.277  22.036  1.00 55.42           C  
ANISOU 2512  C   GLU D  17     9864   6940   4251  -2461   1442      2       C  
ATOM   2513  O   GLU D  17      33.737  36.593  21.816  1.00 63.18           O  
ANISOU 2513  O   GLU D  17    10919   7908   5179  -2502   1254     59       O  
ATOM   2514  CB  GLU D  17      35.579  35.296  19.828  1.00 96.07           C  
ANISOU 2514  CB  GLU D  17    15360  12097   9047  -2891   1874   -223       C  
ATOM   2515  CG  GLU D  17      36.565  35.286  18.665  1.00132.67           C  
ANISOU 2515  CG  GLU D  17    20162  16769  13476  -3166   2191   -367       C  
ATOM   2516  CD  GLU D  17      36.058  34.505  17.465  1.00162.39           C  
ANISOU 2516  CD  GLU D  17    24120  20544  17037  -3395   2307   -475       C  
ATOM   2517  OE1 GLU D  17      35.274  33.550  17.664  1.00160.50           O  
ANISOU 2517  OE1 GLU D  17    23834  20269  16880  -3296   2220   -477       O  
ATOM   2518  OE2 GLU D  17      36.440  34.851  16.323  1.00169.66           O  
ANISOU 2518  OE2 GLU D  17    25239  21516  17707  -3681   2488   -558       O  
ATOM   2519  N   TYR D  18      35.344  35.916  23.233  1.00 51.00           N  
ANISOU 2519  N   TYR D  18     9073   6382   3921  -2227   1413     27       N  
ATOM   2520  CA  TYR D  18      34.467  35.798  24.389  1.00 38.88           C  
ANISOU 2520  CA  TYR D  18     7346   4847   2581  -2009   1165    111       C  
ATOM   2521  C   TYR D  18      34.964  36.682  25.529  1.00 55.53           C  
ANISOU 2521  C   TYR D  18     9253   7000   4844  -1835   1070    195       C  
ATOM   2522  O   TYR D  18      34.224  37.500  26.063  1.00 57.90           O  
ANISOU 2522  O   TYR D  18     9472   7324   5204  -1772    867    269       O  
ATOM   2523  CB  TYR D  18      34.361  34.342  24.830  1.00 73.50           C  
ANISOU 2523  CB  TYR D  18    11632   9204   7092  -1894   1196     68       C  
ATOM   2524  CG  TYR D  18      33.585  33.479  23.859  1.00 58.69           C  
ANISOU 2524  CG  TYR D  18     9922   7288   5088  -2037   1235      1       C  
ATOM   2525  CD1 TYR D  18      32.202  33.375  23.947  1.00 37.70           C  
ANISOU 2525  CD1 TYR D  18     7270   4610   2446  -2013   1029     48       C  
ATOM   2526  CD2 TYR D  18      34.233  32.774  22.852  1.00 50.06           C  
ANISOU 2526  CD2 TYR D  18     8973   6180   3866  -2206   1494   -122       C  
ATOM   2527  CE1 TYR D  18      31.488  32.593  23.061  1.00 71.34           C  
ANISOU 2527  CE1 TYR D  18    11684   8833   6589  -2139   1062     -3       C  
ATOM   2528  CE2 TYR D  18      33.528  31.982  21.964  1.00 64.29           C  
ANISOU 2528  CE2 TYR D  18    10923   7959   5546  -2339   1535   -185       C  
ATOM   2529  CZ  TYR D  18      32.155  31.893  22.074  1.00 84.06           C  
ANISOU 2529  CZ  TYR D  18    13438  10439   8060  -2297   1310   -114       C  
ATOM   2530  OH  TYR D  18      31.446  31.108  21.194  1.00 98.78           O  
ANISOU 2530  OH  TYR D  18    15450  12280   9803  -2423   1348   -168       O  
ATOM   2531  N   LEU D  19      36.200  36.450  25.951  1.00 67.27           N  
ANISOU 2531  N   LEU D  19    10647   8496   6416  -1756   1225    176       N  
ATOM   2532  CA  LEU D  19      36.837  37.284  26.962  1.00 65.16           C  
ANISOU 2532  CA  LEU D  19    10200   8274   6282  -1602   1166    256       C  
ATOM   2533  C   LEU D  19      37.814  38.280  26.360  1.00 64.31           C  
ANISOU 2533  C   LEU D  19    10197   8180   6058  -1728   1315    249       C  
ATOM   2534  O   LEU D  19      38.740  37.901  25.642  1.00 76.69           O  
ANISOU 2534  O   LEU D  19    11869   9720   7547  -1855   1566    156       O  
ATOM   2535  CB  LEU D  19      37.578  36.416  27.978  1.00 70.27           C  
ANISOU 2535  CB  LEU D  19    10652   8920   7127  -1416   1218    262       C  
ATOM   2536  CG  LEU D  19      36.894  36.096  29.301  1.00 51.73           C  
ANISOU 2536  CG  LEU D  19     8078   6612   4964  -1206    999    341       C  
ATOM   2537  CD1 LEU D  19      35.409  35.856  29.103  1.00 49.28           C  
ANISOU 2537  CD1 LEU D  19     7813   6295   4616  -1246    831    332       C  
ATOM   2538  CD2 LEU D  19      37.567  34.877  29.897  1.00 49.36           C  
ANISOU 2538  CD2 LEU D  19     7661   6292   4800  -1094   1091    329       C  
ATOM   2539  N   SER D  20      37.608  39.556  26.663  1.00 67.51           N  
ANISOU 2539  N   SER D  20    10563   8627   6460  -1705   1175    334       N  
ATOM   2540  CA  SER D  20      38.625  40.562  26.399  1.00 53.30           C  
ANISOU 2540  CA  SER D  20     8808   6851   4594  -1775   1294    354       C  
ATOM   2541  C   SER D  20      39.734  40.402  27.429  1.00 59.66           C  
ANISOU 2541  C   SER D  20     9408   7668   5593  -1588   1370    381       C  
ATOM   2542  O   SER D  20      39.523  39.797  28.478  1.00 71.27           O  
ANISOU 2542  O   SER D  20    10688   9147   7244  -1395   1262    417       O  
ATOM   2543  CB  SER D  20      38.040  41.969  26.450  1.00 54.97           C  
ANISOU 2543  CB  SER D  20     9030   7100   4756  -1805   1110    441       C  
ATOM   2544  OG  SER D  20      37.778  42.370  27.782  1.00 62.47           O  
ANISOU 2544  OG  SER D  20     9735   8089   5912  -1586    927    518       O  
ATOM   2545  N   ASP D  21      40.910  40.942  27.125  1.00 65.53           N  
ANISOU 2545  N   ASP D  21    10190   8410   6298  -1659   1556    366       N  
ATOM   2546  CA  ASP D  21      42.087  40.778  27.974  1.00 73.83           C  
ANISOU 2546  CA  ASP D  21    11063   9453   7535  -1514   1661    381       C  
ATOM   2547  C   ASP D  21      41.871  41.263  29.403  1.00 71.63           C  
ANISOU 2547  C   ASP D  21    10539   9232   7444  -1270   1433    515       C  
ATOM   2548  O   ASP D  21      42.425  40.700  30.353  1.00 69.29           O  
ANISOU 2548  O   ASP D  21    10062   8933   7332  -1112   1439    544       O  
ATOM   2549  CB  ASP D  21      43.276  41.507  27.353  1.00 81.74           C  
ANISOU 2549  CB  ASP D  21    12153  10446   8458  -1654   1888    344       C  
ATOM   2550  CG  ASP D  21      43.614  40.987  25.971  1.00115.37           C  
ANISOU 2550  CG  ASP D  21    16634  14663  12538  -1918   2155    184       C  
ATOM   2551  OD1 ASP D  21      43.246  39.831  25.672  1.00133.60           O  
ANISOU 2551  OD1 ASP D  21    18984  16932  14847  -1953   2209     90       O  
ATOM   2552  OD2 ASP D  21      44.247  41.726  25.187  1.00121.98           O1+
ANISOU 2552  OD2 ASP D  21    17599  15514  13233  -2102   2316    147       O1+
ATOM   2553  N   GLU D  22      41.061  42.306  29.548  1.00 71.74           N  
ANISOU 2553  N   GLU D  22    10546   9298   7415  -1260   1239    588       N  
ATOM   2554  CA  GLU D  22      40.755  42.864  30.859  1.00 77.23           C  
ANISOU 2554  CA  GLU D  22    11009  10054   8283  -1058   1037    687       C  
ATOM   2555  C   GLU D  22      39.885  41.906  31.672  1.00 64.50           C  
ANISOU 2555  C   GLU D  22     9259   8451   6797   -924    891    684       C  
ATOM   2556  O   GLU D  22      40.243  41.524  32.792  1.00 54.74           O  
ANISOU 2556  O   GLU D  22     7819   7244   5734   -749    851    736       O  
ATOM   2557  CB  GLU D  22      40.058  44.221  30.718  1.00 87.10           C  
ANISOU 2557  CB  GLU D  22    12295  11335   9462  -1116    889    727       C  
ATOM   2558  CG  GLU D  22      40.825  45.246  29.890  1.00106.91           C  
ANISOU 2558  CG  GLU D  22    14950  13844  11827  -1264   1014    746       C  
ATOM   2559  CD  GLU D  22      40.656  45.047  28.391  1.00127.32           C  
ANISOU 2559  CD  GLU D  22    17816  16387  14171  -1521   1135    670       C  
ATOM   2560  OE1 GLU D  22      39.716  44.329  27.987  1.00144.40           O  
ANISOU 2560  OE1 GLU D  22    20064  18525  16278  -1582   1075    617       O  
ATOM   2561  OE2 GLU D  22      41.466  45.603  27.618  1.00118.21           O  
ANISOU 2561  OE2 GLU D  22    16800  15232  12884  -1672   1298    663       O  
ATOM   2562  N   GLU D  23      38.755  41.502  31.101  1.00 47.07           N  
ANISOU 2562  N   GLU D  23     7164   6220   4501  -1020    814    627       N  
ATOM   2563  CA  GLU D  23      37.858  40.593  31.798  1.00 60.14           C  
ANISOU 2563  CA  GLU D  23     8702   7883   6268   -919    684    615       C  
ATOM   2564  C   GLU D  23      38.473  39.196  31.907  1.00 58.56           C  
ANISOU 2564  C   GLU D  23     8475   7652   6121   -864    809    593       C  
ATOM   2565  O   GLU D  23      38.073  38.402  32.760  1.00 47.89           O  
ANISOU 2565  O   GLU D  23     6979   6321   4897   -741    716    611       O  
ATOM   2566  CB  GLU D  23      36.490  40.544  31.107  1.00 47.09           C  
ANISOU 2566  CB  GLU D  23     7175   6202   4512  -1051    576    564       C  
ATOM   2567  CG  GLU D  23      36.523  40.273  29.622  1.00 66.94           C  
ANISOU 2567  CG  GLU D  23     9959   8657   6816  -1256    713    503       C  
ATOM   2568  CD  GLU D  23      35.245  40.713  28.917  1.00 84.38           C  
ANISOU 2568  CD  GLU D  23    12304  10844   8915  -1404    587    487       C  
ATOM   2569  OE1 GLU D  23      34.298  41.152  29.606  1.00 80.64           O  
ANISOU 2569  OE1 GLU D  23    11701  10393   8547  -1347    400    510       O  
ATOM   2570  OE2 GLU D  23      35.188  40.626  27.673  1.00 79.27           O1+
ANISOU 2570  OE2 GLU D  23    11890  10153   8074  -1594    682    445       O1+
ATOM   2571  N   TYR D  24      39.459  38.908  31.060  1.00 44.30           N  
ANISOU 2571  N   TYR D  24     6809   5793   4228   -972   1030    540       N  
ATOM   2572  CA  TYR D  24      40.201  37.658  31.170  1.00 48.71           C  
ANISOU 2572  CA  TYR D  24     7336   6303   4868   -940   1180    496       C  
ATOM   2573  C   TYR D  24      41.146  37.690  32.363  1.00 53.71           C  
ANISOU 2573  C   TYR D  24     7747   6969   5691   -777   1169    581       C  
ATOM   2574  O   TYR D  24      41.214  36.732  33.139  1.00 54.66           O  
ANISOU 2574  O   TYR D  24     7729   7094   5945   -673   1127    610       O  
ATOM   2575  CB  TYR D  24      40.985  37.367  29.888  1.00 47.86           C  
ANISOU 2575  CB  TYR D  24     7437   6113   4634  -1137   1461    370       C  
ATOM   2576  CG  TYR D  24      41.757  36.065  29.939  1.00 75.77           C  
ANISOU 2576  CG  TYR D  24    10936   9568   8286  -1126   1652    284       C  
ATOM   2577  CD1 TYR D  24      41.118  34.867  30.233  1.00 81.50           C  
ANISOU 2577  CD1 TYR D  24    11615  10277   9075  -1063   1583    273       C  
ATOM   2578  CD2 TYR D  24      43.121  36.033  29.692  1.00 78.60           C  
ANISOU 2578  CD2 TYR D  24    11295   9855   8712  -1189   1913    200       C  
ATOM   2579  CE1 TYR D  24      41.816  33.678  30.287  1.00 83.12           C  
ANISOU 2579  CE1 TYR D  24    11776  10395   9411  -1058   1763    188       C  
ATOM   2580  CE2 TYR D  24      43.827  34.846  29.741  1.00 76.08           C  
ANISOU 2580  CE2 TYR D  24    10921   9435   8550  -1189   2108     91       C  
ATOM   2581  CZ  TYR D  24      43.169  33.673  30.039  1.00 70.98           C  
ANISOU 2581  CZ  TYR D  24    10229   8772   7969  -1122   2030     89       C  
ATOM   2582  OH  TYR D  24      43.869  32.491  30.091  1.00 66.62           O  
ANISOU 2582  OH  TYR D  24     9605   8103   7605  -1126   2230    -27       O  
ATOM   2583  N   ARG D  25      41.881  38.790  32.493  1.00 63.16           N  
ANISOU 2583  N   ARG D  25     8913   8192   6895   -773   1202    627       N  
ATOM   2584  CA  ARG D  25      42.779  38.983  33.626  1.00 63.85           C  
ANISOU 2584  CA  ARG D  25     8788   8316   7154   -644   1169    714       C  
ATOM   2585  C   ARG D  25      41.981  38.921  34.928  1.00 60.65           C  
ANISOU 2585  C   ARG D  25     8152   8026   6866   -488    907    824       C  
ATOM   2586  O   ARG D  25      42.364  38.239  35.893  1.00 49.98           O  
ANISOU 2586  O   ARG D  25     6653   6702   5635   -459    819    835       O  
ATOM   2587  CB  ARG D  25      43.518  40.315  33.496  1.00 47.67           C  
ANISOU 2587  CB  ARG D  25     6751   6286   5076   -676   1223    750       C  
ATOM   2588  CG  ARG D  25      44.692  40.488  34.442  1.00 83.53           C  
ANISOU 2588  CG  ARG D  25    11128  10829   9780   -604   1238    796       C  
ATOM   2589  CD  ARG D  25      45.375  41.834  34.215  1.00111.88           C  
ANISOU 2589  CD  ARG D  25    14742  14436  13330   -645   1299    829       C  
ATOM   2590  NE  ARG D  25      46.431  42.093  35.190  1.00128.26           N  
ANISOU 2590  NE  ARG D  25    16679  16489  15564   -584   1289    851       N  
ATOM   2591  CZ  ARG D  25      47.059  43.258  35.326  1.00131.01           C  
ANISOU 2591  CZ  ARG D  25    17002  16861  15915   -597   1298    892       C  
ATOM   2592  NH1 ARG D  25      46.737  44.285  34.548  1.00127.89           N  
ANISOU 2592  NH1 ARG D  25    16690  16530  15374   -662   1314    941       N  
ATOM   2593  NH2 ARG D  25      48.007  43.400  36.243  1.00130.31           N  
ANISOU 2593  NH2 ARG D  25    16824  16688  15999   -516   1307    878       N  
ATOM   2594  N   LEU D  26      40.851  39.620  34.929  1.00 53.87           N  
ANISOU 2594  N   LEU D  26     7318   7183   5966   -439    790    833       N  
ATOM   2595  CA  LEU D  26      39.926  39.584  36.049  1.00 48.80           C  
ANISOU 2595  CA  LEU D  26     6614   6473   5455   -288    645    788       C  
ATOM   2596  C   LEU D  26      39.471  38.158  36.349  1.00 53.00           C  
ANISOU 2596  C   LEU D  26     7127   6970   6042   -255    618    750       C  
ATOM   2597  O   LEU D  26      39.453  37.739  37.505  1.00 25.94           O  
ANISOU 2597  O   LEU D  26     3663   3501   2691   -287    505    674       O  
ATOM   2598  CB  LEU D  26      38.723  40.476  35.761  1.00 42.68           C  
ANISOU 2598  CB  LEU D  26     5893   5736   4587   -401    499    736       C  
ATOM   2599  CG  LEU D  26      37.547  40.347  36.725  1.00 56.85           C  
ANISOU 2599  CG  LEU D  26     7530   7585   6486   -425    264    662       C  
ATOM   2600  CD1 LEU D  26      37.216  41.693  37.337  1.00 41.36           C  
ANISOU 2600  CD1 LEU D  26     5403   5716   4597   -466    106    650       C  
ATOM   2601  CD2 LEU D  26      36.337  39.761  36.007  1.00 79.87           C  
ANISOU 2601  CD2 LEU D  26    10524  10499   9322   -517    220    625       C  
ATOM   2602  N   PHE D  27      39.113  37.417  35.302  1.00 61.44           N  
ANISOU 2602  N   PHE D  27     8261   8103   6979   -379    659    763       N  
ATOM   2603  CA  PHE D  27      38.693  36.029  35.457  1.00 47.50           C  
ANISOU 2603  CA  PHE D  27     6469   6326   5254   -358    642    749       C  
ATOM   2604  C   PHE D  27      39.765  35.196  36.145  1.00 42.97           C  
ANISOU 2604  C   PHE D  27     5723   5791   4814   -329    639    793       C  
ATOM   2605  O   PHE D  27      39.459  34.390  37.027  1.00 36.04           O  
ANISOU 2605  O   PHE D  27     5067   4663   3963   -417    595    563       O  
ATOM   2606  CB  PHE D  27      38.355  35.402  34.103  1.00 44.28           C  
ANISOU 2606  CB  PHE D  27     6279   5860   4686   -532    733    645       C  
ATOM   2607  CG  PHE D  27      38.207  33.912  34.160  1.00 50.48           C  
ANISOU 2607  CG  PHE D  27     7050   6617   5514   -521    759    626       C  
ATOM   2608  CD1 PHE D  27      37.052  33.340  34.663  1.00 57.48           C  
ANISOU 2608  CD1 PHE D  27     7871   7525   6442   -464    611    631       C  
ATOM   2609  CD2 PHE D  27      39.230  33.081  33.732  1.00 59.97           C  
ANISOU 2609  CD2 PHE D  27     8312   7740   6733   -575    957    575       C  
ATOM   2610  CE1 PHE D  27      36.916  31.966  34.733  1.00 65.88           C  
ANISOU 2610  CE1 PHE D  27     8916   8570   7545   -451    630    629       C  
ATOM   2611  CE2 PHE D  27      39.101  31.706  33.799  1.00 56.07           C  
ANISOU 2611  CE2 PHE D  27     7803   7204   6296   -566    990    551       C  
ATOM   2612  CZ  PHE D  27      37.941  31.147  34.300  1.00 58.48           C  
ANISOU 2612  CZ  PHE D  27     8030   7569   6620   -503    809    599       C  
ATOM   2613  N   GLN D  28      41.014  35.386  35.725  1.00 47.03           N  
ANISOU 2613  N   GLN D  28     6314   6270   5286   -437    806    780       N  
ATOM   2614  CA  GLN D  28      42.142  34.696  36.341  1.00 40.42           C  
ANISOU 2614  CA  GLN D  28     5434   5337   4585   -436    884    746       C  
ATOM   2615  C   GLN D  28      42.289  35.064  37.809  1.00 61.64           C  
ANISOU 2615  C   GLN D  28     8037   7985   7397   -349    725    736       C  
ATOM   2616  O   GLN D  28      42.594  34.210  38.633  1.00 66.62           O  
ANISOU 2616  O   GLN D  28     8540   8554   8219   -195    706    772       O  
ATOM   2617  CB  GLN D  28      43.443  35.016  35.614  1.00 34.01           C  
ANISOU 2617  CB  GLN D  28     4716   4391   3814   -460   1166    684       C  
ATOM   2618  CG  GLN D  28      43.558  34.419  34.240  1.00 62.04           C  
ANISOU 2618  CG  GLN D  28     8458   7825   7289   -575   1427    548       C  
ATOM   2619  CD  GLN D  28      44.869  34.782  33.586  1.00 84.22           C  
ANISOU 2619  CD  GLN D  28    11342  10508  10150   -662   1718    438       C  
ATOM   2620  OE1 GLN D  28      45.427  35.849  33.845  1.00 84.43           O  
ANISOU 2620  OE1 GLN D  28    11332  10564  10184   -643   1704    488       O  
ATOM   2621  NE2 GLN D  28      45.376  33.894  32.738  1.00 97.06           N  
ANISOU 2621  NE2 GLN D  28    13055  11993  11829   -772   1995    268       N  
ATOM   2622  N   ALA D  29      42.094  36.339  38.134  1.00 65.18           N  
ANISOU 2622  N   ALA D  29     8493   8455   7819   -326    642    724       N  
ATOM   2623  CA  ALA D  29      42.197  36.773  39.524  1.00 64.87           C  
ANISOU 2623  CA  ALA D  29     8168   8482   7997    -84    468    796       C  
ATOM   2624  C   ALA D  29      41.134  36.093  40.385  1.00 56.07           C  
ANISOU 2624  C   ALA D  29     6812   7508   6985     -1    247    818       C  
ATOM   2625  O   ALA D  29      41.440  35.495  41.429  1.00 54.93           O  
ANISOU 2625  O   ALA D  29     6397   7448   7025    124    135    892       O  
ATOM   2626  CB  ALA D  29      42.072  38.278  39.615  1.00 78.95           C  
ANISOU 2626  CB  ALA D  29     9917  10331   9749    -84    396    793       C  
ATOM   2627  N   GLU D  30      39.888  36.190  39.927  1.00 53.30           N  
ANISOU 2627  N   GLU D  30     6539   7189   6522   -101    190    754       N  
ATOM   2628  CA  GLU D  30      38.755  35.538  40.575  1.00 57.98           C  
ANISOU 2628  CA  GLU D  30     6912   7920   7197   -108      7    745       C  
ATOM   2629  C   GLU D  30      39.042  34.067  40.820  1.00 53.64           C  
ANISOU 2629  C   GLU D  30     6329   7338   6713    -57     30    787       C  
ATOM   2630  O   GLU D  30      38.898  33.576  41.937  1.00 42.79           O  
ANISOU 2630  O   GLU D  30     4890   5933   5434    -41    -53    696       O  
ATOM   2631  CB  GLU D  30      37.495  35.673  39.721  1.00 56.54           C  
ANISOU 2631  CB  GLU D  30     6905   7701   6876   -231     10    672       C  
ATOM   2632  CG  GLU D  30      36.994  37.090  39.556  1.00 86.50           C  
ANISOU 2632  CG  GLU D  30    10686  11540  10639   -293    -45    643       C  
ATOM   2633  CD  GLU D  30      36.069  37.508  40.679  1.00 99.97           C  
ANISOU 2633  CD  GLU D  30    12231  13263  12489   -277   -157    543       C  
ATOM   2634  OE1 GLU D  30      35.598  36.618  41.420  1.00 95.03           O  
ANISOU 2634  OE1 GLU D  30    11732  12529  11845   -222   -119    516       O  
ATOM   2635  OE2 GLU D  30      35.813  38.724  40.817  1.00110.40           O1+
ANISOU 2635  OE2 GLU D  30    13575  14549  13824   -276   -159    490       O1+
ATOM   2636  N   LEU D  31      39.468  33.380  39.765  1.00 61.08           N  
ANISOU 2636  N   LEU D  31     7589   8089   7530   -109    248    761       N  
ATOM   2637  CA  LEU D  31      39.731  31.949  39.824  1.00 61.73           C  
ANISOU 2637  CA  LEU D  31     7666   8110   7677    -86    302    795       C  
ATOM   2638  C   LEU D  31      40.900  31.643  40.753  1.00 60.81           C  
ANISOU 2638  C   LEU D  31     7319   7997   7790     63    285    906       C  
ATOM   2639  O   LEU D  31      40.975  30.566  41.340  1.00 56.35           O  
ANISOU 2639  O   LEU D  31     6587   7448   7377    128    220    980       O  
ATOM   2640  CB  LEU D  31      40.007  31.403  38.420  1.00 63.04           C  
ANISOU 2640  CB  LEU D  31     8163   8125   7665   -275    546    719       C  
ATOM   2641  CG  LEU D  31      39.900  29.891  38.226  1.00 61.60           C  
ANISOU 2641  CG  LEU D  31     7980   7901   7526   -301    594    732       C  
ATOM   2642  CD1 LEU D  31      38.534  29.401  38.666  1.00 61.95           C  
ANISOU 2642  CD1 LEU D  31     7975   7997   7566   -244    427    728       C  
ATOM   2643  CD2 LEU D  31      40.158  29.524  36.776  1.00 65.37           C  
ANISOU 2643  CD2 LEU D  31     8539   8389   7909   -413    787    723       C  
HETATM 2644  N   MSE D  32      41.806  32.605  40.890  1.00 67.56           N  
ANISOU 2644  N   MSE D  32     8156   8824   8688    115    338    926       N  
HETATM 2645  CA  MSE D  32      42.972  32.443  41.748  1.00 62.49           C  
ANISOU 2645  CA  MSE D  32     7305   8147   8290    271    331   1038       C  
HETATM 2646  C   MSE D  32      42.591  32.524  43.218  1.00 64.88           C  
ANISOU 2646  C   MSE D  32     7615   8514   8523    162     96    837       C  
HETATM 2647  O   MSE D  32      43.115  31.781  44.047  1.00 68.97           O  
ANISOU 2647  O   MSE D  32     8225   8920   9060    100    107    932       O  
HETATM 2648  CB  MSE D  32      44.028  33.497  41.425  1.00 78.08           C  
ANISOU 2648  CB  MSE D  32     9386  10015  10267    281    484   1023       C  
HETATM 2649  CG  MSE D  32      45.254  33.412  42.305  1.00 89.34           C  
ANISOU 2649  CG  MSE D  32    10674  11356  11916    383    474   1080       C  
HETATM 2650 SE   MSE D  32      46.773  34.333  41.532  1.00214.05          SE  
ANISOU 2650 SE   MSE D  32    26595  26915  27819    405    795   1077      SE  
HETATM 2651  CE  MSE D  32      48.132  33.777  42.816  1.00225.61           C  
ANISOU 2651  CE  MSE D  32    27899  28272  29550    449    702   1096       C  
ATOM   2652  N   LEU D  33      41.677  33.429  43.545  1.00 76.26           N  
ANISOU 2652  N   LEU D  33     9072  10041   9863     58     52    742       N  
ATOM   2653  CA  LEU D  33      41.200  33.507  44.919  1.00 61.87           C  
ANISOU 2653  CA  LEU D  33     7374   8189   7947    -17    -15    824       C  
ATOM   2654  C   LEU D  33      40.377  32.281  45.278  1.00 56.02           C  
ANISOU 2654  C   LEU D  33     6486   7512   7287    -69    -60    768       C  
ATOM   2655  O   LEU D  33      40.537  31.717  46.356  1.00 66.71           O  
ANISOU 2655  O   LEU D  33     7952   8789   8606    -96    -87    903       O  
ATOM   2656  CB  LEU D  33      40.385  34.774  45.145  1.00 75.09           C  
ANISOU 2656  CB  LEU D  33     9076   9911   9544    -54    -42    764       C  
ATOM   2657  CG  LEU D  33      41.222  35.878  45.786  1.00 90.80           C  
ANISOU 2657  CG  LEU D  33    11054  11896  11551    -39    -32    786       C  
ATOM   2658  CD1 LEU D  33      42.233  36.445  44.794  1.00 77.25           C  
ANISOU 2658  CD1 LEU D  33     9203  10209   9937     28     23    725       C  
ATOM   2659  CD2 LEU D  33      40.330  36.960  46.349  1.00106.23           C  
ANISOU 2659  CD2 LEU D  33    13029  13883  13451    -80    -60    744       C  
ATOM   2660  N   ASN D  34      39.499  31.867  44.370  1.00 61.91           N  
ANISOU 2660  N   ASN D  34     7400   8217   7906    -71    -58    786       N  
ATOM   2661  CA  ASN D  34      38.710  30.659  44.578  1.00 72.19           C  
ANISOU 2661  CA  ASN D  34     8565   9572   9290   -122   -101    732       C  
ATOM   2662  C   ASN D  34      38.828  29.684  43.406  1.00 54.48           C  
ANISOU 2662  C   ASN D  34     6323   7307   7070    -81    -69    728       C  
ATOM   2663  O   ASN D  34      38.076  29.774  42.439  1.00 47.22           O  
ANISOU 2663  O   ASN D  34     5441   6422   6079    -73    -95    706       O  
ATOM   2664  CB  ASN D  34      37.243  31.016  44.818  1.00 84.67           C  
ANISOU 2664  CB  ASN D  34    10317  11138  10716   -170   -128    744       C  
ATOM   2665  CG  ASN D  34      36.450  29.858  45.399  1.00 99.29           C  
ANISOU 2665  CG  ASN D  34    12165  12985  12574   -218   -168    777       C  
ATOM   2666  OD1 ASN D  34      37.020  28.881  45.891  1.00 90.75           O  
ANISOU 2666  OD1 ASN D  34    10905  11932  11644   -243   -202    778       O  
ATOM   2667  ND2 ASN D  34      35.126  29.964  45.348  1.00 96.66           N  
ANISOU 2667  ND2 ASN D  34    11866  12673  12190   -255   -185    732       N  
ATOM   2668  N   PRO D  35      39.789  28.749  43.492  1.00 63.05           N  
ANISOU 2668  N   PRO D  35     7501   8264   8190    -33    -32    872       N  
ATOM   2669  CA  PRO D  35      40.053  27.754  42.443  1.00 68.99           C  
ANISOU 2669  CA  PRO D  35     8061   9043   9111     54     22    965       C  
ATOM   2670  C   PRO D  35      38.865  26.839  42.151  1.00 70.66           C  
ANISOU 2670  C   PRO D  35     8283   9302   9264    -17    -41    956       C  
ATOM   2671  O   PRO D  35      38.688  26.400  41.015  1.00 75.93           O  
ANISOU 2671  O   PRO D  35     9062   9905   9883    -22     93   1010       O  
ATOM   2672  CB  PRO D  35      41.223  26.946  43.018  1.00 54.84           C  
ANISOU 2672  CB  PRO D  35     6208   7115   7516     96     53   1014       C  
ATOM   2673  CG  PRO D  35      41.880  27.868  43.980  1.00 63.85           C  
ANISOU 2673  CG  PRO D  35     7514   8184   8561     35     43   1014       C  
ATOM   2674  CD  PRO D  35      40.762  28.655  44.591  1.00 62.16           C  
ANISOU 2674  CD  PRO D  35     7339   8097   8180    -39    -40    961       C  
ATOM   2675  N   LYS D  36      38.062  26.561  43.170  1.00 63.17           N  
ANISOU 2675  N   LYS D  36     7383   8357   8263   -122   -115    796       N  
ATOM   2676  CA  LYS D  36      36.933  25.649  43.037  1.00 69.78           C  
ANISOU 2676  CA  LYS D  36     8154   9276   9082   -228   -208   1065       C  
ATOM   2677  C   LYS D  36      35.650  26.382  42.643  1.00 72.74           C  
ANISOU 2677  C   LYS D  36     8820   9580   9238   -211   -169    755       C  
ATOM   2678  O   LYS D  36      34.567  25.799  42.677  1.00 85.58           O  
ANISOU 2678  O   LYS D  36    10278  11358  10882   -358   -277    919       O  
ATOM   2679  CB  LYS D  36      36.728  24.861  44.332  1.00 77.10           C  
ANISOU 2679  CB  LYS D  36     9284  10039   9972   -229   -221    942       C  
ATOM   2680  CG  LYS D  36      37.853  23.879  44.638  1.00 88.78           C  
ANISOU 2680  CG  LYS D  36    10409  11527  11795   -283   -313   1313       C  
ATOM   2681  CD  LYS D  36      37.597  23.131  45.941  1.00107.38           C  
ANISOU 2681  CD  LYS D  36    12824  13842  14131   -311   -357   1048       C  
ATOM   2682  CE  LYS D  36      38.720  22.155  46.264  1.00107.29           C  
ANISOU 2682  CE  LYS D  36    12702  13713  14349   -301   -396   1154       C  
ATOM   2683  NZ  LYS D  36      38.465  21.427  47.539  1.00102.56           N  
ANISOU 2683  NZ  LYS D  36    12293  12930  13747   -362   -484   1376       N  
ATOM   2684  N   LEU D  37      35.781  27.663  42.303  1.00 70.59           N  
ANISOU 2684  N   LEU D  37     8566   9336   8921   -194   -145    702       N  
ATOM   2685  CA  LEU D  37      34.642  28.522  41.968  1.00 73.93           C  
ANISOU 2685  CA  LEU D  37     8922   9820   9348   -261   -174    569       C  
ATOM   2686  C   LEU D  37      33.653  27.878  40.999  1.00 72.42           C  
ANISOU 2686  C   LEU D  37     8763   9674   9081   -334   -223    595       C  
ATOM   2687  O   LEU D  37      32.441  27.954  41.197  1.00 66.87           O  
ANISOU 2687  O   LEU D  37     8115   8909   8384   -370   -198    501       O  
ATOM   2688  CB  LEU D  37      35.139  29.841  41.375  1.00 80.84           C  
ANISOU 2688  CB  LEU D  37     9792  10750  10174   -245   -174    598       C  
ATOM   2689  CG  LEU D  37      34.046  30.834  40.977  1.00 88.82           C  
ANISOU 2689  CG  LEU D  37    10857  11763  11127   -308   -192    527       C  
ATOM   2690  CD1 LEU D  37      33.238  31.251  42.196  1.00 77.67           C  
ANISOU 2690  CD1 LEU D  37     9554  10293   9664   -276   -179    540       C  
ATOM   2691  CD2 LEU D  37      34.636  32.047  40.265  1.00 79.54           C  
ANISOU 2691  CD2 LEU D  37     9657  10682   9882   -355   -194    604       C  
ATOM   2692  N   GLY D  38      34.164  27.263  39.940  1.00 80.71           N  
ANISOU 2692  N   GLY D  38     9886  10734  10046   -359   -171    703       N  
ATOM   2693  CA  GLY D  38      33.324  26.449  39.083  1.00 81.42           C  
ANISOU 2693  CA  GLY D  38    10178  10733  10024   -404   -116    658       C  
ATOM   2694  C   GLY D  38      33.015  25.133  39.772  1.00 77.64           C  
ANISOU 2694  C   GLY D  38     9516  10319   9664   -434   -238    715       C  
ATOM   2695  O   GLY D  38      33.909  24.490  40.321  1.00 61.79           O  
ANISOU 2695  O   GLY D  38     7381   8317   7781   -372   -248    812       O  
ATOM   2696  N   ASP D  39      31.754  24.720  39.745  1.00 76.80           N  
ANISOU 2696  N   ASP D  39     9398  10238   9546   -531   -323    664       N  
ATOM   2697  CA  ASP D  39      31.371  23.475  40.396  1.00 89.88           C  
ANISOU 2697  CA  ASP D  39    11036  11830  11284   -488   -336    649       C  
ATOM   2698  C   ASP D  39      31.643  22.283  39.483  1.00 72.76           C  
ANISOU 2698  C   ASP D  39     8938   9640   9067   -527   -330    752       C  
ATOM   2699  O   ASP D  39      31.531  22.395  38.262  1.00 65.12           O  
ANISOU 2699  O   ASP D  39     8272   8541   7928   -489   -151    686       O  
ATOM   2700  CB  ASP D  39      29.898  23.509  40.803  1.00126.90           C  
ANISOU 2700  CB  ASP D  39    15785  16442  15989   -500   -288    534       C  
ATOM   2701  CG  ASP D  39      29.535  22.389  41.759  1.00164.09           C  
ANISOU 2701  CG  ASP D  39    20560  21143  20645   -449   -359    662       C  
ATOM   2702  OD1 ASP D  39      30.411  21.967  42.545  1.00168.76           O  
ANISOU 2702  OD1 ASP D  39    20988  21730  21405   -510   -348    683       O  
ATOM   2703  OD2 ASP D  39      28.373  21.932  41.726  1.00176.58           O  
ANISOU 2703  OD2 ASP D  39    22175  22718  22198   -487   -382    651       O  
ATOM   2704  N   VAL D  40      32.003  21.145  40.076  1.00 61.63           N  
ANISOU 2704  N   VAL D  40     7380   8231   7806   -517   -405    853       N  
ATOM   2705  CA  VAL D  40      32.245  19.926  39.304  1.00 67.13           C  
ANISOU 2705  CA  VAL D  40     8250   8766   8489   -466   -289    902       C  
ATOM   2706  C   VAL D  40      30.994  19.451  38.570  1.00 76.22           C  
ANISOU 2706  C   VAL D  40     9573   9892   9497   -532   -289    817       C  
ATOM   2707  O   VAL D  40      29.883  19.514  39.099  1.00 73.46           O  
ANISOU 2707  O   VAL D  40     9080   9659   9175   -657   -471    775       O  
ATOM   2708  CB  VAL D  40      32.748  18.764  40.194  1.00 47.34           C  
ANISOU 2708  CB  VAL D  40     5464   6257   6266   -466   -449   1058       C  
ATOM   2709  CG1 VAL D  40      34.164  19.030  40.692  1.00 37.68           C  
ANISOU 2709  CG1 VAL D  40     4088   4983   5247   -368   -409   1158       C  
ATOM   2710  CG2 VAL D  40      31.795  18.528  41.361  1.00 79.77           C  
ANISOU 2710  CG2 VAL D  40     9598  10369  10343   -484   -498    901       C  
ATOM   2711  N   ILE D  41      31.184  18.982  37.343  1.00 79.38           N  
ANISOU 2711  N   ILE D  41    10263  10117   9782   -475    -38    790       N  
ATOM   2712  CA  ILE D  41      30.112  18.330  36.610  1.00 75.06           C  
ANISOU 2712  CA  ILE D  41     9839   9548   9130   -520    -45    735       C  
ATOM   2713  C   ILE D  41      30.111  16.862  37.001  1.00 96.95           C  
ANISOU 2713  C   ILE D  41    12516  12254  12066   -532   -136    837       C  
ATOM   2714  O   ILE D  41      31.105  16.164  36.794  1.00 91.15           O  
ANISOU 2714  O   ILE D  41    11817  11319  11496   -495     46    905       O  
ATOM   2715  CB  ILE D  41      30.285  18.468  35.092  1.00 73.98           C  
ANISOU 2715  CB  ILE D  41     9923   9338   8849   -511    212    676       C  
ATOM   2716  CG1 ILE D  41      30.551  19.924  34.714  1.00 69.84           C  
ANISOU 2716  CG1 ILE D  41     9462   8861   8212   -529    257    593       C  
ATOM   2717  CG2 ILE D  41      29.060  17.941  34.368  1.00 92.24           C  
ANISOU 2717  CG2 ILE D  41    12370  11645  11033   -600    139    573       C  
ATOM   2718  CD1 ILE D  41      30.654  20.146  33.223  1.00 76.92           C  
ANISOU 2718  CD1 ILE D  41    10593   9690   8942   -634    429    447       C  
ATOM   2719  N   GLN D  42      29.005  16.397  37.575  1.00117.97           N  
ANISOU 2719  N   GLN D  42    15033  15029  14762   -633   -398    830       N  
ATOM   2720  CA  GLN D  42      28.959  15.055  38.146  1.00128.38           C  
ANISOU 2720  CA  GLN D  42    16174  16312  16293   -665   -574    947       C  
ATOM   2721  C   GLN D  42      29.169  13.984  37.082  1.00119.91           C  
ANISOU 2721  C   GLN D  42    15321  14998  15242   -595   -375    969       C  
ATOM   2722  O   GLN D  42      28.517  13.987  36.039  1.00116.72           O  
ANISOU 2722  O   GLN D  42    15153  14562  14635   -601   -223    875       O  
ATOM   2723  CB  GLN D  42      27.632  14.822  38.882  1.00148.99           C  
ANISOU 2723  CB  GLN D  42    18678  19014  18916   -769   -731    878       C  
ATOM   2724  CG  GLN D  42      26.382  15.043  38.044  1.00167.01           C  
ANISOU 2724  CG  GLN D  42    21142  21300  21016   -846   -704    757       C  
ATOM   2725  CD  GLN D  42      25.114  14.627  38.768  1.00175.44           C  
ANISOU 2725  CD  GLN D  42    22174  22352  22135   -798   -681    688       C  
ATOM   2726  OE1 GLN D  42      25.135  14.344  39.966  1.00177.34           O  
ANISOU 2726  OE1 GLN D  42    22301  22595  22485   -743   -672    694       O  
ATOM   2727  NE2 GLN D  42      24.003  14.586  38.041  1.00173.80           N  
ANISOU 2727  NE2 GLN D  42    22089  22117  21831   -843   -667    618       N  
ATOM   2728  N   GLY D  43      30.106  13.080  37.349  1.00115.81           N  
ANISOU 2728  N   GLY D  43    14665  14274  15062   -559   -374   1071       N  
ATOM   2729  CA  GLY D  43      30.375  11.974  36.451  1.00110.84           C  
ANISOU 2729  CA  GLY D  43    14167  13310  14638   -587   -166   1009       C  
ATOM   2730  C   GLY D  43      31.441  12.261  35.411  1.00 94.01           C  
ANISOU 2730  C   GLY D  43    12262  10936  12521   -730    244    817       C  
ATOM   2731  O   GLY D  43      31.694  11.435  34.537  1.00100.76           O  
ANISOU 2731  O   GLY D  43    13114  11560  13611   -884    304    697       O  
ATOM   2732  N   THR D  44      32.056  13.435  35.489  1.00 86.53           N  
ANISOU 2732  N   THR D  44    11374  10110  11393   -741    351    811       N  
ATOM   2733  CA  THR D  44      33.126  13.785  34.560  1.00 75.82           C  
ANISOU 2733  CA  THR D  44     9921   8742  10145   -900    459    761       C  
ATOM   2734  C   THR D  44      34.513  13.526  35.143  1.00 76.83           C  
ANISOU 2734  C   THR D  44     9760   8640  10793   -791    571    681       C  
ATOM   2735  O   THR D  44      35.522  13.678  34.452  1.00 73.76           O  
ANISOU 2735  O   THR D  44     9209   8085  10732   -785    936    478       O  
ATOM   2736  CB  THR D  44      33.036  15.259  34.141  1.00 79.94           C  
ANISOU 2736  CB  THR D  44    10445   9566  10363   -800    587    822       C  
ATOM   2737  OG1 THR D  44      32.898  16.082  35.308  1.00 84.09           O  
ANISOU 2737  OG1 THR D  44    11038  10259  10654   -758    323    837       O  
ATOM   2738  CG2 THR D  44      31.843  15.478  33.227  1.00 77.43           C  
ANISOU 2738  CG2 THR D  44    10353   9385   9684   -727    697    700       C  
ATOM   2739  N   GLY D  45      34.559  13.132  36.411  1.00 62.64           N  
ANISOU 2739  N   GLY D  45     7752   6826   9221   -624    316    825       N  
ATOM   2740  CA  GLY D  45      35.818  12.842  37.070  1.00 59.11           C  
ANISOU 2740  CA  GLY D  45     6932   6217   9310   -499    267    831       C  
ATOM   2741  C   GLY D  45      36.672  14.062  37.373  1.00 78.39           C  
ANISOU 2741  C   GLY D  45     9355   8763  11666   -457    378    861       C  
ATOM   2742  O   GLY D  45      37.894  14.011  37.239  1.00 85.09           O  
ANISOU 2742  O   GLY D  45    10002   9428  12899   -420    536    728       O  
ATOM   2743  N   GLY D  46      36.037  15.153  37.798  1.00 76.44           N  
ANISOU 2743  N   GLY D  46     9278   8805  10960   -438    289    992       N  
ATOM   2744  CA  GLY D  46      36.768  16.343  38.199  1.00 85.05           C  
ANISOU 2744  CA  GLY D  46    10336  10007  11975   -376    339   1023       C  
ATOM   2745  C   GLY D  46      36.716  17.545  37.271  1.00 92.19           C  
ANISOU 2745  C   GLY D  46    11553  11038  12438   -494    574    900       C  
ATOM   2746  O   GLY D  46      37.372  18.559  37.529  1.00 93.11           O  
ANISOU 2746  O   GLY D  46    11644  11223  12512   -441    621    905       O  
ATOM   2747  N   LEU D  47      35.946  17.448  36.193  1.00 80.08           N  
ANISOU 2747  N   LEU D  47    10245   9572  10610   -644    658    820       N  
ATOM   2748  CA  LEU D  47      35.802  18.580  35.279  1.00 71.88           C  
ANISOU 2748  CA  LEU D  47     9328   8728   9257   -659    788    769       C  
ATOM   2749  C   LEU D  47      34.916  19.670  35.871  1.00 66.43           C  
ANISOU 2749  C   LEU D  47     8682   8286   8273   -614    500    842       C  
ATOM   2750  O   LEU D  47      33.808  19.400  36.330  1.00 72.73           O  
ANISOU 2750  O   LEU D  47     9671   8937   9027   -431    550    724       O  
ATOM   2751  CB  LEU D  47      35.237  18.120  33.938  1.00 50.73           C  
ANISOU 2751  CB  LEU D  47     6799   6019   6458   -689   1010    604       C  
ATOM   2752  CG  LEU D  47      36.277  17.882  32.843  1.00 56.76           C  
ANISOU 2752  CG  LEU D  47     7590   6607   7371   -763   1437    298       C  
ATOM   2753  CD1 LEU D  47      37.457  17.062  33.365  1.00 47.03           C  
ANISOU 2753  CD1 LEU D  47     6059   5093   6719   -763   1568    233       C  
ATOM   2754  CD2 LEU D  47      35.636  17.210  31.633  1.00 47.02           C  
ANISOU 2754  CD2 LEU D  47     6537   5334   5995   -861   1632     76       C  
ATOM   2755  N   ARG D  48      35.408  20.904  35.850  1.00 68.98           N  
ANISOU 2755  N   ARG D  48     8997   8686   8528   -563    562    830       N  
ATOM   2756  CA  ARG D  48      34.671  22.033  36.413  1.00 60.20           C  
ANISOU 2756  CA  ARG D  48     7906   7564   7401   -265    565    795       C  
ATOM   2757  C   ARG D  48      34.171  22.992  35.339  1.00 52.43           C  
ANISOU 2757  C   ARG D  48     7056   6718   6145   -406    541    730       C  
ATOM   2758  O   ARG D  48      34.776  23.134  34.275  1.00 59.23           O  
ANISOU 2758  O   ARG D  48     8086   7506   6914   -514    726    593       O  
ATOM   2759  CB  ARG D  48      35.536  22.788  37.419  1.00 42.14           C  
ANISOU 2759  CB  ARG D  48     5687   5256   5068   -410    466    731       C  
ATOM   2760  CG  ARG D  48      35.879  21.971  38.648  1.00 52.11           C  
ANISOU 2760  CG  ARG D  48     6591   6582   6626   -306    267    897       C  
ATOM   2761  CD  ARG D  48      36.737  22.756  39.614  1.00 49.63           C  
ANISOU 2761  CD  ARG D  48     6024   6360   6473   -208    165    979       C  
ATOM   2762  NE  ARG D  48      37.071  21.979  40.804  1.00 66.97           N  
ANISOU 2762  NE  ARG D  48     7842   8620   8981   -143    -53   1138       N  
ATOM   2763  CZ  ARG D  48      36.229  21.753  41.808  1.00 72.23           C  
ANISOU 2763  CZ  ARG D  48     8437   9408   9600   -214   -257   1063       C  
ATOM   2764  NH1 ARG D  48      34.993  22.232  41.762  1.00 77.13           N1+
ANISOU 2764  NH1 ARG D  48     9162  10117  10026   -286   -296    925       N1+
ATOM   2765  NH2 ARG D  48      36.621  21.039  42.853  1.00 76.97           N  
ANISOU 2765  NH2 ARG D  48     9007   9931  10308   -217   -313   1028       N  
ATOM   2766  N   LYS D  49      33.047  23.636  35.632  1.00 38.14           N  
ANISOU 2766  N   LYS D  49     5295   4938   4258   -393    386    653       N  
ATOM   2767  CA  LYS D  49      32.425  24.578  34.716  1.00 43.57           C  
ANISOU 2767  CA  LYS D  49     6134   5632   4788   -499    363    535       C  
ATOM   2768  C   LYS D  49      32.053  25.864  35.442  1.00 43.47           C  
ANISOU 2768  C   LYS D  49     6028   5680   4810   -490    223    527       C  
ATOM   2769  O   LYS D  49      31.341  25.837  36.446  1.00 51.38           O  
ANISOU 2769  O   LYS D  49     6871   6745   5907   -512     44    521       O  
ATOM   2770  CB  LYS D  49      31.182  23.961  34.077  1.00 50.42           C  
ANISOU 2770  CB  LYS D  49     7119   6466   5573   -592    298    453       C  
ATOM   2771  CG  LYS D  49      30.417  24.925  33.198  1.00 64.54           C  
ANISOU 2771  CG  LYS D  49     9058   8220   7243   -705    273    364       C  
ATOM   2772  CD  LYS D  49      29.124  24.316  32.679  1.00 79.80           C  
ANISOU 2772  CD  LYS D  49    11084  10107   9129   -790    201    310       C  
ATOM   2773  CE  LYS D  49      28.155  24.057  33.814  1.00 99.22           C  
ANISOU 2773  CE  LYS D  49    13352  12631  11717   -771     13    342       C  
ATOM   2774  NZ  LYS D  49      27.825  25.311  34.545  1.00115.81           N1+
ANISOU 2774  NZ  LYS D  49    15315  14793  13893   -790    -91    349       N1+
ATOM   2775  N   ILE D  50      32.534  26.991  34.935  1.00 42.10           N  
ANISOU 2775  N   ILE D  50     5926   5501   4570   -512    292    509       N  
ATOM   2776  CA  ILE D  50      32.253  28.274  35.566  1.00 43.62           C  
ANISOU 2776  CA  ILE D  50     6023   5746   4805   -516    175    501       C  
ATOM   2777  C   ILE D  50      31.580  29.228  34.587  1.00 42.29           C  
ANISOU 2777  C   ILE D  50     5998   5549   4520   -630    167    438       C  
ATOM   2778  O   ILE D  50      31.936  29.277  33.414  1.00 49.57           O  
ANISOU 2778  O   ILE D  50     7113   6409   5311   -700    297    403       O  
ATOM   2779  CB  ILE D  50      33.546  28.916  36.139  1.00 48.61           C  
ANISOU 2779  CB  ILE D  50     6582   6389   5499   -419    247    561       C  
ATOM   2780  CG1 ILE D  50      33.253  30.290  36.740  1.00 52.74           C  
ANISOU 2780  CG1 ILE D  50     6998   6978   6064   -453    116    535       C  
ATOM   2781  CG2 ILE D  50      34.626  29.018  35.083  1.00 56.63           C  
ANISOU 2781  CG2 ILE D  50     7722   7369   6427   -436    450    582       C  
ATOM   2782  CD1 ILE D  50      32.244  30.262  37.864  1.00 73.46           C  
ANISOU 2782  CD1 ILE D  50     9366   9719   8826   -524   -103    511       C  
ATOM   2783  N   ARG D  51      30.578  29.955  35.072  1.00 53.35           N  
ANISOU 2783  N   ARG D  51     7303   6990   5978   -685     19    415       N  
ATOM   2784  CA  ARG D  51      29.899  30.970  34.275  1.00 59.40           C  
ANISOU 2784  CA  ARG D  51     8189   7721   6659   -791      1    378       C  
ATOM   2785  C   ARG D  51      30.434  32.364  34.612  1.00 67.44           C  
ANISOU 2785  C   ARG D  51     9143   8783   7701   -774    -10    400       C  
ATOM   2786  O   ARG D  51      30.630  32.702  35.782  1.00 60.58           O  
ANISOU 2786  O   ARG D  51     8061   7990   6965   -723    -88    421       O  
ATOM   2787  CB  ARG D  51      28.389  30.901  34.506  1.00 64.69           C  
ANISOU 2787  CB  ARG D  51     8799   8392   7388   -876   -129    347       C  
ATOM   2788  CG  ARG D  51      27.592  32.023  33.869  1.00 78.79           C  
ANISOU 2788  CG  ARG D  51    10681  10139   9117   -983   -165    326       C  
ATOM   2789  CD  ARG D  51      26.106  31.861  34.157  1.00 96.95           C  
ANISOU 2789  CD  ARG D  51    12915  12426  11494  -1063   -271    304       C  
ATOM   2790  NE  ARG D  51      25.332  33.018  33.716  1.00117.23           N  
ANISOU 2790  NE  ARG D  51    15552  14958  14033  -1159   -314    296       N  
ATOM   2791  CZ  ARG D  51      25.050  34.063  34.485  1.00127.54           C  
ANISOU 2791  CZ  ARG D  51    16693  16321  15446  -1152   -366    308       C  
ATOM   2792  NH1 ARG D  51      25.476  34.098  35.741  1.00127.78           N1+
ANISOU 2792  NH1 ARG D  51    16485  16443  15623   -988   -347    323       N1+
ATOM   2793  NH2 ARG D  51      24.340  35.074  34.000  1.00126.21           N  
ANISOU 2793  NH2 ARG D  51    16601  16111  15244  -1204   -389    311       N  
ATOM   2794  N   VAL D  52      30.672  33.161  33.573  1.00 71.63           N  
ANISOU 2794  N   VAL D  52     9851   9266   8098   -843     62    391       N  
ATOM   2795  CA  VAL D  52      31.234  34.501  33.704  1.00 65.98           C  
ANISOU 2795  CA  VAL D  52     9108   8582   7379   -838     66    416       C  
ATOM   2796  C   VAL D  52      30.299  35.545  33.104  1.00 73.77           C  
ANISOU 2796  C   VAL D  52    10183   9541   8303   -967     -4    395       C  
ATOM   2797  O   VAL D  52      29.871  35.407  31.959  1.00 66.39           O  
ANISOU 2797  O   VAL D  52     9456   8537   7232  -1078     34    369       O  
ATOM   2798  CB  VAL D  52      32.601  34.597  33.010  1.00 58.63           C  
ANISOU 2798  CB  VAL D  52     8309   7624   6342   -825    238    435       C  
ATOM   2799  CG1 VAL D  52      33.144  36.016  33.093  1.00 64.00           C  
ANISOU 2799  CG1 VAL D  52     8972   8334   7011   -828    239    465       C  
ATOM   2800  CG2 VAL D  52      33.574  33.602  33.622  1.00 62.79           C  
ANISOU 2800  CG2 VAL D  52     8742   8166   6950   -698    320    471       C  
ATOM   2801  N   ALA D  53      30.002  36.599  33.859  1.00 86.10           N  
ANISOU 2801  N   ALA D  53    11593  11156   9964   -967   -103    406       N  
ATOM   2802  CA  ALA D  53      29.027  37.587  33.404  1.00 96.44           C  
ANISOU 2802  CA  ALA D  53    12966  12437  11238  -1090   -178    394       C  
ATOM   2803  C   ALA D  53      29.675  38.926  33.065  1.00115.99           C  
ANISOU 2803  C   ALA D  53    15504  14923  13646  -1121   -156    423       C  
ATOM   2804  O   ALA D  53      30.884  39.101  33.227  1.00109.18           O  
ANISOU 2804  O   ALA D  53    14623  14091  12770  -1041    -75    450       O  
ATOM   2805  CB  ALA D  53      27.949  37.779  34.457  1.00 81.31           C  
ANISOU 2805  CB  ALA D  53    10831  10567   9494  -1110   -303    379       C  
ATOM   2806  N   SER D  54      28.857  39.867  32.599  1.00136.13           N  
ANISOU 2806  N   SER D  54    18129  17442  16154  -1241   -227    422       N  
ATOM   2807  CA  SER D  54      29.341  41.172  32.153  1.00141.06           C  
ANISOU 2807  CA  SER D  54    18835  18068  16694  -1300   -220    453       C  
ATOM   2808  C   SER D  54      28.402  42.299  32.575  1.00129.56           C  
ANISOU 2808  C   SER D  54    17280  16620  15326  -1371   -348    458       C  
ATOM   2809  O   SER D  54      27.846  42.279  33.673  1.00119.28           O  
ANISOU 2809  O   SER D  54    15752  15367  14201  -1331   -416    442       O  
ATOM   2810  CB  SER D  54      29.517  41.186  30.631  1.00137.45           C  
ANISOU 2810  CB  SER D  54    18678  17537  16009  -1433   -142    457       C  
ATOM   2811  OG  SER D  54      28.279  40.984  29.968  1.00123.53           O  
ANISOU 2811  OG  SER D  54    17044  15701  14190  -1555   -211    438       O  
ATOM   2812  N   GLY D  61      24.611  42.112  28.483  1.00115.10           N  
ANISOU 2812  N   GLY D  61    16294  14412  13028  -1938   -520    450       N  
ATOM   2813  CA  GLY D  61      24.863  41.144  27.431  1.00132.14           C  
ANISOU 2813  CA  GLY D  61    18665  16528  15015  -1992   -427    433       C  
ATOM   2814  C   GLY D  61      24.820  39.710  27.920  1.00146.32           C  
ANISOU 2814  C   GLY D  61    20354  18339  16902  -1869   -369    391       C  
ATOM   2815  O   GLY D  61      24.518  39.449  29.084  1.00153.74           O  
ANISOU 2815  O   GLY D  61    21058  19323  18033  -1752   -410    378       O  
ATOM   2816  N   GLY D  62      25.131  38.775  27.029  1.00139.95           N  
ANISOU 2816  N   GLY D  62    19722  17500  15951  -1913   -269    371       N  
ATOM   2817  CA  GLY D  62      25.120  37.364  27.371  1.00133.47           C  
ANISOU 2817  CA  GLY D  62    18826  16685  15200  -1810   -214    334       C  
ATOM   2818  C   GLY D  62      26.315  36.954  28.210  1.00127.73           C  
ANISOU 2818  C   GLY D  62    17927  16042  14564  -1657   -128    328       C  
ATOM   2819  O   GLY D  62      27.364  37.598  28.176  1.00134.60           O  
ANISOU 2819  O   GLY D  62    18803  16954  15387  -1647    -62    346       O  
ATOM   2820  N   SER D  63      26.153  35.881  28.978  1.00114.85           N  
ANISOU 2820  N   SER D  63    16145  14432  13063  -1541   -132    309       N  
ATOM   2821  CA  SER D  63      27.242  35.359  29.797  1.00 95.62           C  
ANISOU 2821  CA  SER D  63    13552  12066  10714  -1397    -63    311       C  
ATOM   2822  C   SER D  63      28.123  34.422  28.980  1.00 79.23           C  
ANISOU 2822  C   SER D  63    11633   9963   8509  -1413     95    287       C  
ATOM   2823  O   SER D  63      27.875  34.199  27.797  1.00 83.44           O  
ANISOU 2823  O   SER D  63    12388  10432   8881  -1547    154    261       O  
ATOM   2824  CB  SER D  63      26.700  34.629  31.028  1.00 91.24           C  
ANISOU 2824  CB  SER D  63    12764  11553  10349  -1289   -143    307       C  
ATOM   2825  OG  SER D  63      25.792  35.441  31.752  1.00 96.88           O  
ANISOU 2825  OG  SER D  63    13334  12292  11184  -1311   -262    315       O  
ATOM   2826  N   ARG D  64      29.152  33.879  29.618  1.00 72.72           N  
ANISOU 2826  N   ARG D  64    10691   9184   7755  -1290    170    292       N  
ATOM   2827  CA  ARG D  64      30.096  32.989  28.952  1.00 66.37           C  
ANISOU 2827  CA  ARG D  64    10011   8352   6855  -1308    346    260       C  
ATOM   2828  C   ARG D  64      30.391  31.783  29.829  1.00 48.28           C  
ANISOU 2828  C   ARG D  64     7562   6085   4695  -1166    353    264       C  
ATOM   2829  O   ARG D  64      30.275  31.854  31.047  1.00 38.79           O  
ANISOU 2829  O   ARG D  64     6144   4946   3649  -1044    245    305       O  
ATOM   2830  CB  ARG D  64      31.384  33.742  28.613  1.00 67.46           C  
ANISOU 2830  CB  ARG D  64    10210   8508   6914  -1337    482    265       C  
ATOM   2831  CG  ARG D  64      31.209  34.755  27.490  1.00 89.07           C  
ANISOU 2831  CG  ARG D  64    13155  11217   9471  -1519    507    255       C  
ATOM   2832  CD  ARG D  64      31.976  36.030  27.759  1.00 96.03           C  
ANISOU 2832  CD  ARG D  64    13989  12144  10353  -1504    515    298       C  
ATOM   2833  NE  ARG D  64      31.513  36.701  28.968  1.00105.26           N  
ANISOU 2833  NE  ARG D  64    14934  13364  11694  -1375    340    350       N  
ATOM   2834  CZ  ARG D  64      31.978  37.870  29.394  1.00117.61           C  
ANISOU 2834  CZ  ARG D  64    16420  14975  13292  -1344    309    393       C  
ATOM   2835  NH1 ARG D  64      32.918  38.503  28.705  1.00121.93           N  
ANISOU 2835  NH1 ARG D  64    17097  15520  13710  -1427    433    399       N  
ATOM   2836  NH2 ARG D  64      31.503  38.410  30.506  1.00117.00           N  
ANISOU 2836  NH2 ARG D  64    16132  14947  13376  -1247    164    422       N  
ATOM   2837  N   ILE D  65      30.761  30.668  29.214  1.00 55.83           N  
ANISOU 2837  N   ILE D  65     8628   6996   5588  -1200    487    219       N  
ATOM   2838  CA  ILE D  65      31.008  29.456  29.980  1.00 56.52           C  
ANISOU 2838  CA  ILE D  65     8582   7100   5794  -1078    492    229       C  
ATOM   2839  C   ILE D  65      32.422  28.934  29.761  1.00 60.74           C  
ANISOU 2839  C   ILE D  65     9148   7615   6317  -1065    701    202       C  
ATOM   2840  O   ILE D  65      32.842  28.706  28.628  1.00 68.70           O  
ANISOU 2840  O   ILE D  65    10340   8564   7198  -1202    885    119       O  
ATOM   2841  CB  ILE D  65      30.008  28.351  29.619  1.00 51.08           C  
ANISOU 2841  CB  ILE D  65     7958   6364   5086  -1119    454    195       C  
ATOM   2842  CG1 ILE D  65      28.570  28.877  29.674  1.00 55.93           C  
ANISOU 2842  CG1 ILE D  65     8563   6973   5715  -1165    280    207       C  
ATOM   2843  CG2 ILE D  65      30.175  27.185  30.556  1.00 45.52           C  
ANISOU 2843  CG2 ILE D  65     7093   5690   4513   -991    426    223       C  
ATOM   2844  CD1 ILE D  65      28.090  29.216  31.071  1.00 54.96           C  
ANISOU 2844  CD1 ILE D  65     8191   6924   5767  -1062    118    254       C  
ATOM   2845  N   ILE D  66      33.154  28.752  30.854  1.00 45.77           N  
ANISOU 2845  N   ILE D  66     7061   5767   4561   -918    688    265       N  
ATOM   2846  CA  ILE D  66      34.505  28.217  30.782  1.00 45.37           C  
ANISOU 2846  CA  ILE D  66     7006   5682   4549   -903    895    241       C  
ATOM   2847  C   ILE D  66      34.580  26.842  31.433  1.00 45.00           C  
ANISOU 2847  C   ILE D  66     6841   5632   4626   -809    894    271       C  
ATOM   2848  O   ILE D  66      34.167  26.657  32.576  1.00 49.06           O  
ANISOU 2848  O   ILE D  66     7166   6222   5251   -683    716    376       O  
ATOM   2849  CB  ILE D  66      35.535  29.151  31.455  1.00 40.54           C  
ANISOU 2849  CB  ILE D  66     6275   5116   4014   -823    914    308       C  
ATOM   2850  CG1 ILE D  66      35.812  30.378  30.581  1.00 49.03           C  
ANISOU 2850  CG1 ILE D  66     7501   6174   4955   -946    994    261       C  
ATOM   2851  CG2 ILE D  66      36.833  28.412  31.710  1.00 48.57           C  
ANISOU 2851  CG2 ILE D  66     7219   6084   5149   -783   1103    297       C  
ATOM   2852  CD1 ILE D  66      34.877  31.540  30.825  1.00 48.84           C  
ANISOU 2852  CD1 ILE D  66     7450   6209   4899   -939    790    315       C  
ATOM   2853  N   TYR D  67      35.094  25.874  30.686  1.00 48.81           N  
ANISOU 2853  N   TYR D  67     7423   6026   5098   -891   1111    167       N  
ATOM   2854  CA  TYR D  67      35.344  24.547  31.220  1.00 45.30           C  
ANISOU 2854  CA  TYR D  67     6860   5555   4796   -819   1156    189       C  
ATOM   2855  C   TYR D  67      36.811  24.422  31.555  1.00 44.49           C  
ANISOU 2855  C   TYR D  67     6644   5395   4866   -790   1355    176       C  
ATOM   2856  O   TYR D  67      37.671  24.612  30.695  1.00 61.04           O  
ANISOU 2856  O   TYR D  67     8834   7402   6955   -908   1613     23       O  
ATOM   2857  CB  TYR D  67      34.939  23.461  30.225  1.00 57.17           C  
ANISOU 2857  CB  TYR D  67     8505   6978   6237   -936   1293     54       C  
ATOM   2858  CG  TYR D  67      33.451  23.311  30.058  1.00 71.50           C  
ANISOU 2858  CG  TYR D  67    10397   8829   7941   -950   1084     83       C  
ATOM   2859  CD1 TYR D  67      32.706  24.291  29.419  1.00 80.21           C  
ANISOU 2859  CD1 TYR D  67    11634   9945   8898  -1039    996     64       C  
ATOM   2860  CD2 TYR D  67      32.788  22.188  30.532  1.00 79.01           C  
ANISOU 2860  CD2 TYR D  67    11274   9790   8956   -885    983    130       C  
ATOM   2861  CE1 TYR D  67      31.346  24.161  29.262  1.00 88.08           C  
ANISOU 2861  CE1 TYR D  67    12680  10946   9840  -1064    826     79       C  
ATOM   2862  CE2 TYR D  67      31.422  22.047  30.376  1.00 93.40           C  
ANISOU 2862  CE2 TYR D  67    13156  11628  10703   -909    804    138       C  
ATOM   2863  CZ  TYR D  67      30.707  23.039  29.739  1.00100.04           C  
ANISOU 2863  CZ  TYR D  67    14122  12465  11426  -1000    734    107       C  
ATOM   2864  OH  TYR D  67      29.347  22.915  29.577  1.00111.10           O  
ANISOU 2864  OH  TYR D  67    15565  13857  12790  -1035    579    111       O  
ATOM   2865  N   TYR D  68      37.100  24.100  32.805  1.00 40.74           N  
ANISOU 2865  N   TYR D  68     5944   4964   4571   -659   1236    333       N  
ATOM   2866  CA  TYR D  68      38.480  23.943  33.225  1.00 46.29           C  
ANISOU 2866  CA  TYR D  68     6505   5573   5508   -634   1406    327       C  
ATOM   2867  C   TYR D  68      38.642  22.730  34.126  1.00 55.26           C  
ANISOU 2867  C   TYR D  68     7427   6659   6912   -577   1349    434       C  
ATOM   2868  O   TYR D  68      37.667  22.130  34.570  1.00 53.31           O  
ANISOU 2868  O   TYR D  68     7137   6495   6622   -558   1134    557       O  
ATOM   2869  CB  TYR D  68      38.974  25.204  33.937  1.00 46.85           C  
ANISOU 2869  CB  TYR D  68     6499   5725   5578   -568   1291    433       C  
ATOM   2870  CG  TYR D  68      38.376  25.430  35.310  1.00 47.13           C  
ANISOU 2870  CG  TYR D  68     6351   5927   5630   -479    951    643       C  
ATOM   2871  CD1 TYR D  68      37.091  25.953  35.460  1.00 32.07           C  
ANISOU 2871  CD1 TYR D  68     4439   4168   3579   -448    731    706       C  
ATOM   2872  CD2 TYR D  68      39.105  25.138  36.457  1.00 43.95           C  
ANISOU 2872  CD2 TYR D  68     5789   5478   5431   -437    883    720       C  
ATOM   2873  CE1 TYR D  68      36.548  26.171  36.714  1.00 38.72           C  
ANISOU 2873  CE1 TYR D  68     5082   5134   4495   -397    431    775       C  
ATOM   2874  CE2 TYR D  68      38.572  25.353  37.716  1.00 48.99           C  
ANISOU 2874  CE2 TYR D  68     6373   6171   6071   -381    634    774       C  
ATOM   2875  CZ  TYR D  68      37.295  25.869  37.840  1.00 51.60           C  
ANISOU 2875  CZ  TYR D  68     6815   6560   6230   -382    498    716       C  
ATOM   2876  OH  TYR D  68      36.769  26.079  39.097  1.00 46.77           O  
ANISOU 2876  OH  TYR D  68     5892   6109   5770   -230    240    799       O  
ATOM   2877  N   PHE D  69      39.889  22.364  34.372  1.00 58.56           N  
ANISOU 2877  N   PHE D  69     7689   6905   7657   -562   1536    373       N  
ATOM   2878  CA  PHE D  69      40.208  21.263  35.255  1.00 63.39           C  
ANISOU 2878  CA  PHE D  69     8053   7385   8646   -507   1463    460       C  
ATOM   2879  C   PHE D  69      41.308  21.709  36.210  1.00 64.48           C  
ANISOU 2879  C   PHE D  69     8003   7432   9064   -397   1431    529       C  
ATOM   2880  O   PHE D  69      42.376  22.151  35.784  1.00 70.26           O  
ANISOU 2880  O   PHE D  69     8716   8041   9938   -405   1675    374       O  
ATOM   2881  CB  PHE D  69      40.625  20.030  34.447  1.00 70.33           C  
ANISOU 2881  CB  PHE D  69     8838   8042   9842   -578   1742    224       C  
ATOM   2882  CG  PHE D  69      41.538  19.103  35.186  1.00 74.52           C  
ANISOU 2882  CG  PHE D  69     9030   8318  10967   -497   1727    207       C  
ATOM   2883  CD1 PHE D  69      41.090  18.402  36.294  1.00 84.69           C  
ANISOU 2883  CD1 PHE D  69    10159   9583  12436   -411   1392    436       C  
ATOM   2884  CD2 PHE D  69      42.844  18.926  34.770  1.00 80.02           C  
ANISOU 2884  CD2 PHE D  69     9552   8735  12115   -486   2056    -83       C  
ATOM   2885  CE1 PHE D  69      41.931  17.551  36.979  1.00 80.75           C  
ANISOU 2885  CE1 PHE D  69     9317   8831  12533   -291   1310    421       C  
ATOM   2886  CE2 PHE D  69      43.689  18.076  35.446  1.00 88.57           C  
ANISOU 2886  CE2 PHE D  69    10260   9504  13891   -353   2036   -139       C  
ATOM   2887  CZ  PHE D  69      43.232  17.385  36.553  1.00 92.20           C  
ANISOU 2887  CZ  PHE D  69    10541   9984  14507   -243   1626    142       C  
ATOM   2888  N   LEU D  70      41.034  21.608  37.505  1.00 62.00           N  
ANISOU 2888  N   LEU D  70     7552   7174   8833   -286   1125    742       N  
ATOM   2889  CA  LEU D  70      41.984  22.041  38.518  1.00 67.90           C  
ANISOU 2889  CA  LEU D  70     8091   7855   9852   -134   1046    839       C  
ATOM   2890  C   LEU D  70      42.933  20.913  38.891  1.00 78.20           C  
ANISOU 2890  C   LEU D  70     9082   8870  11760    -46   1080    815       C  
ATOM   2891  O   LEU D  70      42.515  19.887  39.428  1.00 83.87           O  
ANISOU 2891  O   LEU D  70     9628   9551  12688      0    870    919       O  
ATOM   2892  CB  LEU D  70      41.244  22.541  39.758  1.00 71.49           C  
ANISOU 2892  CB  LEU D  70     8462   8553  10148    -22    680   1046       C  
ATOM   2893  CG  LEU D  70      42.119  22.883  40.961  1.00 69.18           C  
ANISOU 2893  CG  LEU D  70     7871   8261  10153    149    520   1191       C  
ATOM   2894  CD1 LEU D  70      43.029  24.065  40.643  1.00 69.91           C  
ANISOU 2894  CD1 LEU D  70     8073   8297  10191    163    717   1109       C  
ATOM   2895  CD2 LEU D  70      41.254  23.162  42.183  1.00 62.08           C  
ANISOU 2895  CD2 LEU D  70     6913   7676   8999    114    152   1241       C  
ATOM   2896  N   ASP D  71      44.215  21.118  38.614  1.00 97.79           N  
ANISOU 2896  N   ASP D  71    11467  11136  14555    -20   1316    656       N  
ATOM   2897  CA  ASP D  71      45.223  20.088  38.825  1.00112.64           C  
ANISOU 2897  CA  ASP D  71    13023  12688  17087     69   1361    542       C  
ATOM   2898  C   ASP D  71      45.905  20.261  40.179  1.00132.75           C  
ANISOU 2898  C   ASP D  71    15375  15255  19810    188   1056    740       C  
ATOM   2899  O   ASP D  71      45.626  21.211  40.912  1.00132.83           O  
ANISOU 2899  O   ASP D  71    15478  15509  19484    221    871    930       O  
ATOM   2900  CB  ASP D  71      46.257  20.134  37.694  1.00115.82           C  
ANISOU 2900  CB  ASP D  71    13447  12859  17699    -26   1775    168       C  
ATOM   2901  CG  ASP D  71      47.114  18.884  37.622  1.00135.40           C  
ANISOU 2901  CG  ASP D  71    15605  15022  20819     -1   1824    -53       C  
ATOM   2902  OD1 ASP D  71      46.648  17.810  38.057  1.00154.65           O  
ANISOU 2902  OD1 ASP D  71    17866  17444  23452     37   1581     45       O  
ATOM   2903  OD2 ASP D  71      48.258  18.978  37.130  1.00136.56           O  
ANISOU 2903  OD2 ASP D  71    15681  14985  21220    -73   2057   -320       O  
ATOM   2904  N   GLU D  72      46.798  19.335  40.505  1.00164.78           N  
ANISOU 2904  N   GLU D  72    19225  19131  24254    173    966    647       N  
ATOM   2905  CA  GLU D  72      47.634  19.449  41.688  1.00175.60           C  
ANISOU 2905  CA  GLU D  72    20504  20538  25676    197    711    758       C  
ATOM   2906  C   GLU D  72      48.649  20.561  41.471  1.00174.70           C  
ANISOU 2906  C   GLU D  72    20447  20359  25571    210    920    667       C  
ATOM   2907  O   GLU D  72      48.900  20.963  40.334  1.00179.01           O  
ANISOU 2907  O   GLU D  72    21068  20774  26172    174   1280    457       O  
ATOM   2908  CB  GLU D  72      48.333  18.122  41.988  1.00187.62           C  
ANISOU 2908  CB  GLU D  72    21791  21853  27642    192    583    669       C  
ATOM   2909  CG  GLU D  72      49.133  17.566  40.820  1.00200.70           C  
ANISOU 2909  CG  GLU D  72    23313  23214  29731    166    897    330       C  
ATOM   2910  CD  GLU D  72      49.637  16.158  41.074  1.00213.86           C  
ANISOU 2910  CD  GLU D  72    24698  24680  31880    177    739    242       C  
ATOM   2911  OE1 GLU D  72      49.352  15.610  42.159  1.00221.04           O  
ANISOU 2911  OE1 GLU D  72    25566  25696  32723    190    383    460       O  
ATOM   2912  OE2 GLU D  72      50.316  15.599  40.188  1.00215.45           O  
ANISOU 2912  OE2 GLU D  72    24709  24616  32535    156    983    -75       O  
ATOM   2913  N   LYS D  73      49.211  21.064  42.567  1.00165.83           N  
ANISOU 2913  N   LYS D  73    19316  19339  24354    237    708    798       N  
ATOM   2914  CA  LYS D  73      50.175  22.161  42.531  1.00167.63           C  
ANISOU 2914  CA  LYS D  73    19591  19519  24580    251    851    746       C  
ATOM   2915  C   LYS D  73      49.563  23.429  41.936  1.00172.56           C  
ANISOU 2915  C   LYS D  73    20421  20289  24853    260   1025    777       C  
ATOM   2916  O   LYS D  73      50.262  24.236  41.322  1.00181.10           O  
ANISOU 2916  O   LYS D  73    21563  21256  25990    248   1283    653       O  
ATOM   2917  CB  LYS D  73      51.432  21.759  41.748  1.00164.44           C  
ANISOU 2917  CB  LYS D  73    19051  18785  24645    216   1117    473       C  
ATOM   2918  N   ARG D  74      48.252  23.582  42.115  1.00158.85           N  
ANISOU 2918  N   ARG D  74    18793  18803  22760    273    877    924       N  
ATOM   2919  CA  ARG D  74      47.540  24.825  41.809  1.00150.69           C  
ANISOU 2919  CA  ARG D  74    17941  17963  21352    303    936    989       C  
ATOM   2920  C   ARG D  74      47.635  25.294  40.356  1.00126.69           C  
ANISOU 2920  C   ARG D  74    15050  14724  18362    297   1377    813       C  
ATOM   2921  O   ARG D  74      47.712  26.495  40.101  1.00119.49           O  
ANISOU 2921  O   ARG D  74    14305  13925  17171    264   1446    800       O  
ATOM   2922  CB  ARG D  74      48.047  25.949  42.719  1.00156.43           C  
ANISOU 2922  CB  ARG D  74    18701  18852  21884    320    772   1054       C  
ATOM   2923  CG  ARG D  74      47.623  25.831  44.174  1.00155.77           C  
ANISOU 2923  CG  ARG D  74    18613  19031  21541    280    404   1118       C  
ATOM   2924  CD  ARG D  74      46.443  26.740  44.472  1.00149.39           C  
ANISOU 2924  CD  ARG D  74    17942  18527  20293    252    264   1106       C  
ATOM   2925  NE  ARG D  74      46.701  28.114  44.047  1.00145.52           N  
ANISOU 2925  NE  ARG D  74    17526  18066  19701    293    369   1097       N  
ATOM   2926  CZ  ARG D  74      45.905  29.143  44.316  1.00142.44           C  
ANISOU 2926  CZ  ARG D  74    17042  17818  19261    234    386   1386       C  
ATOM   2927  NH1 ARG D  74      44.797  28.962  45.020  1.00138.61           N  
ANISOU 2927  NH1 ARG D  74    16694  17592  18379    107    155   1032       N  
ATOM   2928  NH2 ARG D  74      46.221  30.357  43.887  1.00137.65           N  
ANISOU 2928  NH2 ARG D  74    16665  17288  18347    305    342   1042       N  
ATOM   2929  N   ARG D  75      47.624  24.369  39.403  1.00110.27           N  
ANISOU 2929  N   ARG D  75    12991  12484  16425    182   1602    601       N  
ATOM   2930  CA  ARG D  75      47.636  24.781  38.004  1.00 97.21           C  
ANISOU 2930  CA  ARG D  75    11579  10857  14498    -21   1917    351       C  
ATOM   2931  C   ARG D  75      46.302  24.487  37.319  1.00 86.82           C  
ANISOU 2931  C   ARG D  75    10460   9759  12768   -140   1883    352       C  
ATOM   2932  O   ARG D  75      45.810  23.360  37.322  1.00 92.71           O  
ANISOU 2932  O   ARG D  75    11116  10456  13653   -142   1833    347       O  
ATOM   2933  CB  ARG D  75      48.797  24.125  37.246  1.00108.69           C  
ANISOU 2933  CB  ARG D  75    12914  11977  16407   -103   2245     19       C  
ATOM   2934  CG  ARG D  75      48.933  22.622  37.409  1.00128.44           C  
ANISOU 2934  CG  ARG D  75    15159  14230  19411    -48   2219    -82       C  
ATOM   2935  CD  ARG D  75      50.368  22.192  37.128  1.00141.18           C  
ANISOU 2935  CD  ARG D  75    16572  15603  21466   -125   2367   -353       C  
ATOM   2936  NE  ARG D  75      50.488  20.757  36.888  1.00155.21           N  
ANISOU 2936  NE  ARG D  75    18123  17229  23619   -162   2358   -531       N  
ATOM   2937  CZ  ARG D  75      50.734  20.219  35.698  1.00161.50           C  
ANISOU 2937  CZ  ARG D  75    18896  17863  24603   -332   2696   -913       C  
ATOM   2938  NH1 ARG D  75      50.895  20.999  34.638  1.00160.80           N  
ANISOU 2938  NH1 ARG D  75    19040  17793  24264   -508   3035  -1138       N  
ATOM   2939  NH2 ARG D  75      50.827  18.902  35.568  1.00160.70           N  
ANISOU 2939  NH2 ARG D  75    18542  17599  24918   -344   2669  -1079       N  
ATOM   2940  N   PHE D  76      45.728  25.535  36.741  1.00 77.11           N  
ANISOU 2940  N   PHE D  76     9485   8753  11060   -232   1884    360       N  
ATOM   2941  CA  PHE D  76      44.439  25.478  36.070  1.00 56.34           C  
ANISOU 2941  CA  PHE D  76     7059   6323   8025   -334   1812    367       C  
ATOM   2942  C   PHE D  76      44.586  25.105  34.601  1.00 63.00           C  
ANISOU 2942  C   PHE D  76     8039   7075   8822   -504   2131     92       C  
ATOM   2943  O   PHE D  76      45.234  25.815  33.830  1.00 69.82           O  
ANISOU 2943  O   PHE D  76     9009   7901   9618   -605   2339    -63       O  
ATOM   2944  CB  PHE D  76      43.723  26.828  36.176  1.00 56.03           C  
ANISOU 2944  CB  PHE D  76     7177   6533   7578   -338   1604    488       C  
ATOM   2945  CG  PHE D  76      43.534  27.313  37.583  1.00 68.36           C  
ANISOU 2945  CG  PHE D  76     8605   8204   9163   -195   1301    687       C  
ATOM   2946  CD1 PHE D  76      44.540  28.005  38.234  1.00 72.17           C  
ANISOU 2946  CD1 PHE D  76     8977   8617   9828    -91   1313    732       C  
ATOM   2947  CD2 PHE D  76      42.342  27.090  38.248  1.00 68.95           C  
ANISOU 2947  CD2 PHE D  76     8658   8443   9097   -164   1016    795       C  
ATOM   2948  CE1 PHE D  76      44.362  28.456  39.527  1.00 73.77           C  
ANISOU 2948  CE1 PHE D  76     9025   8930  10072     68   1038    896       C  
ATOM   2949  CE2 PHE D  76      42.159  27.537  39.538  1.00 69.59           C  
ANISOU 2949  CE2 PHE D  76     8567   8633   9242    -13    759    923       C  
ATOM   2950  CZ  PHE D  76      43.169  28.223  40.179  1.00 65.85           C  
ANISOU 2950  CZ  PHE D  76     7954   8119   8947    109    760    984       C  
ATOM   2951  N   TYR D  77      43.977  23.996  34.206  1.00 63.02           N  
ANISOU 2951  N   TYR D  77     8038   7048   8859   -552   2166     21       N  
ATOM   2952  CA  TYR D  77      43.945  23.650  32.796  1.00 65.97           C  
ANISOU 2952  CA  TYR D  77     8560   7369   9137   -729   2441   -254       C  
ATOM   2953  C   TYR D  77      42.663  24.183  32.186  1.00 65.07           C  
ANISOU 2953  C   TYR D  77     8718   7469   8535   -794   2295   -178       C  
ATOM   2954  O   TYR D  77      41.580  23.693  32.478  1.00 76.29           O  
ANISOU 2954  O   TYR D  77    10160   8988   9838   -745   2090    -48       O  
ATOM   2955  CB  TYR D  77      44.053  22.139  32.597  1.00 73.59           C  
ANISOU 2955  CB  TYR D  77     9347   8156  10460   -753   2578   -430       C  
ATOM   2956  CG  TYR D  77      45.472  21.623  32.647  1.00 80.27           C  
ANISOU 2956  CG  TYR D  77     9927   8712  11861   -753   2804   -670       C  
ATOM   2957  CD1 TYR D  77      46.325  21.789  31.565  1.00 93.30           C  
ANISOU 2957  CD1 TYR D  77    11618  10258  13574   -933   3132  -1000       C  
ATOM   2958  CD2 TYR D  77      45.958  20.969  33.770  1.00 83.02           C  
ANISOU 2958  CD2 TYR D  77     9967   8873  12702   -584   2662   -576       C  
ATOM   2959  CE1 TYR D  77      47.623  21.323  31.598  1.00100.16           C  
ANISOU 2959  CE1 TYR D  77    12232  10808  15017   -959   3352  -1275       C  
ATOM   2960  CE2 TYR D  77      47.255  20.498  33.813  1.00102.22           C  
ANISOU 2960  CE2 TYR D  77    12141  10916  15780   -569   2888   -853       C  
ATOM   2961  CZ  TYR D  77      48.084  20.679  32.724  1.00110.44           C  
ANISOU 2961  CZ  TYR D  77    13235  11833  16896   -773   3240  -1221       C  
ATOM   2962  OH  TYR D  77      49.378  20.213  32.758  1.00118.68           O  
ANISOU 2962  OH  TYR D  77    13999  12524  18571   -799   3408  -1503       O  
ATOM   2963  N   LEU D  78      42.792  25.189  31.330  1.00 55.56           N  
ANISOU 2963  N   LEU D  78     7705   6316   7087   -912   2388   -263       N  
ATOM   2964  CA  LEU D  78      41.631  25.816  30.717  1.00 58.86           C  
ANISOU 2964  CA  LEU D  78     8354   6888   7123   -975   2228   -204       C  
ATOM   2965  C   LEU D  78      41.341  25.134  29.387  1.00 60.21           C  
ANISOU 2965  C   LEU D  78     8675   7012   7191  -1167   2435   -425       C  
ATOM   2966  O   LEU D  78      42.108  25.257  28.433  1.00 63.01           O  
ANISOU 2966  O   LEU D  78     9086   7300   7553  -1339   2716   -639       O  
ATOM   2967  CB  LEU D  78      41.866  27.318  30.527  1.00 53.12           C  
ANISOU 2967  CB  LEU D  78     7727   6236   6220  -1007   2185   -154       C  
ATOM   2968  CG  LEU D  78      42.356  28.074  31.770  1.00 41.48           C  
ANISOU 2968  CG  LEU D  78     6089   4806   4865   -841   2023     27       C  
ATOM   2969  CD1 LEU D  78      42.533  29.553  31.482  1.00 45.66           C  
ANISOU 2969  CD1 LEU D  78     6714   5409   5226   -885   1992     59       C  
ATOM   2970  CD2 LEU D  78      41.401  27.873  32.934  1.00 48.67           C  
ANISOU 2970  CD2 LEU D  78     6877   5843   5774   -681   1688    243       C  
ATOM   2971  N   LEU D  79      40.221  24.421  29.333  1.00 50.62           N  
ANISOU 2971  N   LEU D  79     7512   5843   5878  -1148   2293   -378       N  
ATOM   2972  CA  LEU D  79      39.922  23.537  28.214  1.00 63.22           C  
ANISOU 2972  CA  LEU D  79     9208   7393   7421  -1313   2480   -583       C  
ATOM   2973  C   LEU D  79      39.267  24.258  27.044  1.00 69.06           C  
ANISOU 2973  C   LEU D  79    10203   8210   7827  -1485   2469   -624       C  
ATOM   2974  O   LEU D  79      39.848  24.354  25.966  1.00 75.61           O  
ANISOU 2974  O   LEU D  79    11115   9013   8598  -1685   2733   -825       O  
ATOM   2975  CB  LEU D  79      39.029  22.391  28.688  1.00 65.14           C  
ANISOU 2975  CB  LEU D  79     9382   7640   7727  -1216   2338   -509       C  
ATOM   2976  CG  LEU D  79      39.538  21.631  29.918  1.00 50.75           C  
ANISOU 2976  CG  LEU D  79     7281   5745   6255  -1049   2306   -419       C  
ATOM   2977  CD1 LEU D  79      38.525  20.589  30.356  1.00 52.82           C  
ANISOU 2977  CD1 LEU D  79     7490   6040   6540   -975   2136   -308       C  
ATOM   2978  CD2 LEU D  79      40.891  20.991  29.652  1.00 39.65           C  
ANISOU 2978  CD2 LEU D  79     5678   4148   5240  -1115   2642   -678       C  
ATOM   2979  N   THR D  80      38.055  24.758  27.255  1.00 68.08           N  
ANISOU 2979  N   THR D  80    10179   8178   7511  -1421   2168   -446       N  
ATOM   2980  CA  THR D  80      37.327  25.456  26.201  1.00 65.45           C  
ANISOU 2980  CA  THR D  80    10063   7895   6908  -1578   2127   -465       C  
ATOM   2981  C   THR D  80      36.440  26.559  26.779  1.00 50.79           C  
ANISOU 2981  C   THR D  80     8222   6116   4958  -1472   1803   -269       C  
ATOM   2982  O   THR D  80      36.169  26.580  27.975  1.00 46.94           O  
ANISOU 2982  O   THR D  80     7578   5665   4593  -1282   1594   -129       O  
ATOM   2983  CB  THR D  80      36.466  24.481  25.379  1.00 66.01           C  
ANISOU 2983  CB  THR D  80    10243   7957   6880  -1686   2161   -555       C  
ATOM   2984  OG1 THR D  80      35.739  25.206  24.382  1.00 80.68           O  
ANISOU 2984  OG1 THR D  80    12309   9859   8486  -1841   2109   -551       O  
ATOM   2985  CG2 THR D  80      35.481  23.748  26.279  1.00 63.97           C  
ANISOU 2985  CG2 THR D  80     9895   7709   6703  -1512   1911   -421       C  
ATOM   2986  N   ILE D  81      36.001  27.479  25.927  1.00 60.44           N  
ANISOU 2986  N   ILE D  81     9614   7368   5983  -1611   1775   -274       N  
ATOM   2987  CA  ILE D  81      35.154  28.589  26.355  1.00 69.09           C  
ANISOU 2987  CA  ILE D  81    10705   8519   7028  -1542   1503   -131       C  
ATOM   2988  C   ILE D  81      34.119  28.955  25.284  1.00 69.75           C  
ANISOU 2988  C   ILE D  81    10988   8603   6909  -1708   1444   -148       C  
ATOM   2989  O   ILE D  81      34.444  29.037  24.096  1.00 70.04           O  
ANISOU 2989  O   ILE D  81    11201   8631   6782  -1913   1638   -252       O  
ATOM   2990  CB  ILE D  81      36.013  29.835  26.710  1.00 75.04           C  
ANISOU 2990  CB  ILE D  81    11407   9306   7800  -1511   1518    -82       C  
ATOM   2991  CG1 ILE D  81      35.134  31.072  26.927  1.00 85.85           C  
ANISOU 2991  CG1 ILE D  81    12782  10727   9110  -1487   1278     26       C  
ATOM   2992  CG2 ILE D  81      37.053  30.096  25.633  1.00 67.77           C  
ANISOU 2992  CG2 ILE D  81    10624   8358   6767  -1709   1811   -214       C  
ATOM   2993  CD1 ILE D  81      35.900  32.309  27.348  1.00 87.76           C  
ANISOU 2993  CD1 ILE D  81    12958  11009   9377  -1443   1273     84       C  
ATOM   2994  N   TYR D  82      32.872  29.166  25.705  1.00 56.30           N  
ANISOU 2994  N   TYR D  82     9250   6913   5227  -1634   1190    -56       N  
ATOM   2995  CA  TYR D  82      31.818  29.578  24.777  1.00 71.89           C  
ANISOU 2995  CA  TYR D  82    11402   8874   7039  -1782   1114    -57       C  
ATOM   2996  C   TYR D  82      30.662  30.289  25.496  1.00 74.49           C  
ANISOU 2996  C   TYR D  82    11636   9217   7449  -1689    839     44       C  
ATOM   2997  O   TYR D  82      30.713  30.502  26.710  1.00 70.25           O  
ANISOU 2997  O   TYR D  82    10890   8719   7081  -1519    718    106       O  
ATOM   2998  CB  TYR D  82      31.300  28.373  23.990  1.00 88.74           C  
ANISOU 2998  CB  TYR D  82    13651  10969   9097  -1877   1197   -133       C  
ATOM   2999  CG  TYR D  82      30.725  27.271  24.844  1.00 79.86           C  
ANISOU 2999  CG  TYR D  82    12381   9830   8133  -1717   1082   -103       C  
ATOM   3000  CD1 TYR D  82      29.397  27.301  25.237  1.00 90.51           C  
ANISOU 3000  CD1 TYR D  82    13689  11170   9532  -1657    853    -32       C  
ATOM   3001  CD2 TYR D  82      31.506  26.197  25.245  1.00 88.92           C  
ANISOU 3001  CD2 TYR D  82    13429  10969   9389  -1641   1214   -153       C  
ATOM   3002  CE1 TYR D  82      28.860  26.301  26.013  1.00125.55           C  
ANISOU 3002  CE1 TYR D  82    17995  15603  14107  -1529    752     -8       C  
ATOM   3003  CE2 TYR D  82      30.977  25.184  26.024  1.00114.21           C  
ANISOU 3003  CE2 TYR D  82    16508  14164  12724  -1506   1101   -116       C  
ATOM   3004  CZ  TYR D  82      29.650  25.241  26.406  1.00130.96           C  
ANISOU 3004  CZ  TYR D  82    18595  16289  14875  -1453    866    -41       C  
ATOM   3005  OH  TYR D  82      29.104  24.242  27.183  1.00123.41           O  
ANISOU 3005  OH  TYR D  82    17515  15334  14042  -1336    755     -7       O  
ATOM   3006  N   GLY D  83      29.620  30.643  24.745  1.00 64.95           N  
ANISOU 3006  N   GLY D  83    10574   7980   6125  -1813    756     51       N  
ATOM   3007  CA  GLY D  83      28.588  31.537  25.246  1.00 84.98           C  
ANISOU 3007  CA  GLY D  83    13040  10519   8730  -1775    538    121       C  
ATOM   3008  C   GLY D  83      27.524  30.960  26.158  1.00103.20           C  
ANISOU 3008  C   GLY D  83    15185  12819  11208  -1649    371    149       C  
ATOM   3009  O   GLY D  83      27.330  29.746  26.214  1.00101.37           O  
ANISOU 3009  O   GLY D  83    14937  12567  11012  -1608    398    123       O  
ATOM   3010  N   LYS D  84      26.819  31.848  26.863  1.00126.02           N  
ANISOU 3010  N   LYS D  84    17954  15727  14203  -1605    208    195       N  
ATOM   3011  CA  LYS D  84      25.733  31.446  27.758  1.00131.46           C  
ANISOU 3011  CA  LYS D  84    18478  16416  15055  -1521     63    209       C  
ATOM   3012  C   LYS D  84      24.593  30.820  26.977  1.00125.51           C  
ANISOU 3012  C   LYS D  84    17875  15584  14232  -1614     31    191       C  
ATOM   3013  O   LYS D  84      23.696  30.208  27.550  1.00117.01           O  
ANISOU 3013  O   LYS D  84    16693  14494  13271  -1562    -57    193       O  
ATOM   3014  CB  LYS D  84      25.212  32.634  28.577  1.00137.34           C  
ANISOU 3014  CB  LYS D  84    19071  17195  15916  -1497    -70    243       C  
ATOM   3015  CG  LYS D  84      24.173  32.265  29.644  1.00129.58           C  
ANISOU 3015  CG  LYS D  84    17890  16230  15116  -1433   -190    246       C  
ATOM   3016  CD  LYS D  84      24.594  31.027  30.426  1.00120.80           C  
ANISOU 3016  CD  LYS D  84    16633  15163  14101  -1316   -164    239       C  
ATOM   3017  CE  LYS D  84      23.404  30.380  31.120  1.00119.17           C  
ANISOU 3017  CE  LYS D  84    16301  14953  14023  -1309   -260    234       C  
ATOM   3018  NZ  LYS D  84      22.789  31.279  32.133  1.00112.38           N  
ANISOU 3018  NZ  LYS D  84    15248  14146  13307  -1318   -355    248       N  
ATOM   3019  N   ASN D  85      24.624  30.953  25.659  1.00134.40           N  
ANISOU 3019  N   ASN D  85    19248  16660  15159  -1765    108    174       N  
ATOM   3020  CA  ASN D  85      23.699  30.170  24.880  1.00128.18           C  
ANISOU 3020  CA  ASN D  85    18609  15803  14291  -1845    100    157       C  
ATOM   3021  C   ASN D  85      24.440  28.883  24.650  1.00116.51           C  
ANISOU 3021  C   ASN D  85    17155  14336  12778  -1816    246    111       C  
ATOM   3022  O   ASN D  85      25.341  28.790  23.816  1.00102.40           O  
ANISOU 3022  O   ASN D  85    15509  12560  10840  -1910    411     70       O  
ATOM   3023  CB  ASN D  85      23.341  30.849  23.573  1.00144.41           C  
ANISOU 3023  CB  ASN D  85    20924  17809  16137  -2038    112    162       C  
ATOM   3024  CG  ASN D  85      22.455  29.996  22.718  1.00156.91           C  
ANISOU 3024  CG  ASN D  85    22671  19326  17621  -2123    112    146       C  
ATOM   3025  OD1 ASN D  85      21.241  29.959  22.913  1.00161.49           O  
ANISOU 3025  OD1 ASN D  85    23233  19851  18276  -2109    -21    171       O  
ATOM   3026  ND2 ASN D  85      23.057  29.271  21.782  1.00159.90           N  
ANISOU 3026  ND2 ASN D  85    23206  19715  17835  -2216    276     97       N  
ATOM   3027  N   GLU D  86      24.010  27.872  25.381  1.00127.20           N  
ANISOU 3027  N   GLU D  86    18372  15687  14271  -1702    192    110       N  
ATOM   3028  CA  GLU D  86      24.909  26.799  25.742  1.00151.78           C  
ANISOU 3028  CA  GLU D  86    21405  18831  17432  -1614    298     81       C  
ATOM   3029  C   GLU D  86      24.934  25.697  24.708  1.00184.17           C  
ANISOU 3029  C   GLU D  86    25678  22894  21404  -1702    431     26       C  
ATOM   3030  O   GLU D  86      23.923  25.382  24.083  1.00192.87           O  
ANISOU 3030  O   GLU D  86    26897  23946  22438  -1774    385     25       O  
ATOM   3031  CB  GLU D  86      24.536  26.244  27.123  1.00144.41           C  
ANISOU 3031  CB  GLU D  86    20229  17931  16708  -1458    174    112       C  
ATOM   3032  CG  GLU D  86      25.706  26.285  28.116  1.00133.26           C  
ANISOU 3032  CG  GLU D  86    18638  16595  15400  -1334    208    128       C  
ATOM   3033  CD  GLU D  86      25.280  26.267  29.579  1.00125.86           C  
ANISOU 3033  CD  GLU D  86    17444  15721  14655  -1218     59    171       C  
ATOM   3034  OE1 GLU D  86      26.060  25.766  30.416  1.00118.74           O  
ANISOU 3034  OE1 GLU D  86    16397  14878  13839  -1112     75    191       O  
ATOM   3035  OE2 GLU D  86      24.186  26.774  29.901  1.00129.85           O  
ANISOU 3035  OE2 GLU D  86    17892  16221  15223  -1248    -63    183       O  
HETATM 3036  N   MSE D  87      26.115  25.119  24.531  1.00195.36           N  
ANISOU 3036  N   MSE D  87    27103  24336  22788  -1702    611    -28       N  
HETATM 3037  CA  MSE D  87      26.261  23.970  23.661  1.00190.38           C  
ANISOU 3037  CA  MSE D  87    26594  23685  22054  -1786    772   -105       C  
HETATM 3038  C   MSE D  87      25.591  22.781  24.309  1.00163.49           C  
ANISOU 3038  C   MSE D  87    23081  20260  18778  -1670    676    -85       C  
HETATM 3039  O   MSE D  87      25.039  22.883  25.407  1.00154.96           O  
ANISOU 3039  O   MSE D  87    21836  19186  17856  -1543    494    -17       O  
HETATM 3040  CB  MSE D  87      27.731  23.657  23.391  1.00200.50           C  
ANISOU 3040  CB  MSE D  87    27879  24997  23304  -1826   1020   -195       C  
HETATM 3041  CG  MSE D  87      28.423  24.650  22.494  1.00205.49           C  
ANISOU 3041  CG  MSE D  87    28655  25653  23770  -1990   1165   -244       C  
HETATM 3042 SE   MSE D  87      30.277  24.143  22.162  1.00148.36          SE  
ANISOU 3042 SE   MSE D  87    21391  18445  16534  -2063   1529   -405      SE  
HETATM 3043  CE  MSE D  87      30.662  25.440  20.763  1.00250.56           C  
ANISOU 3043  CE  MSE D  87    34574  31427  29202  -2334   1675   -464       C  
ATOM   3044  N   SER D  88      25.641  21.652  23.620  1.00143.28           N  
ANISOU 3044  N   SER D  88    20607  17686  16146  -1729    810   -155       N  
ATOM   3045  CA  SER D  88      24.965  20.464  24.094  1.00145.16           C  
ANISOU 3045  CA  SER D  88    20770  17902  16483  -1637    725   -136       C  
ATOM   3046  C   SER D  88      25.487  20.057  25.467  1.00144.02           C  
ANISOU 3046  C   SER D  88    20407  17783  16533  -1470    659    -95       C  
ATOM   3047  O   SER D  88      26.693  19.885  25.659  1.00152.27           O  
ANISOU 3047  O   SER D  88    21395  18852  17609  -1446    807   -136       O  
ATOM   3048  CB  SER D  88      25.141  19.332  23.087  1.00150.38           C  
ANISOU 3048  CB  SER D  88    21547  18563  17027  -1734    920   -241       C  
ATOM   3049  OG  SER D  88      24.891  19.804  21.776  1.00147.59           O  
ANISOU 3049  OG  SER D  88    21398  18218  16461  -1910   1011   -293       O  
ATOM   3050  N   ASP D  89      24.573  19.934  26.424  1.00129.55           N  
ANISOU 3050  N   ASP D  89    18444  15950  14829  -1370    446    -20       N  
ATOM   3051  CA  ASP D  89      24.897  19.334  27.708  1.00116.14           C  
ANISOU 3051  CA  ASP D  89    16542  14296  13290  -1231    366     23       C  
ATOM   3052  C   ASP D  89      25.250  17.881  27.434  1.00120.60           C  
ANISOU 3052  C   ASP D  89    17141  14837  13846  -1225    485    -23       C  
ATOM   3053  O   ASP D  89      24.495  17.168  26.772  1.00129.43           O  
ANISOU 3053  O   ASP D  89    18366  15910  14901  -1281    490    -51       O  
ATOM   3054  CB  ASP D  89      23.731  19.451  28.689  1.00102.00           C  
ANISOU 3054  CB  ASP D  89    14605  12525  11625  -1178    139     85       C  
ATOM   3055  N   LEU D  90      26.404  17.452  27.934  1.00110.02           N  
ANISOU 3055  N   LEU D  90    15704  13526  12573  -1159    593    -30       N  
ATOM   3056  CA  LEU D  90      27.005  16.186  27.525  1.00106.71           C  
ANISOU 3056  CA  LEU D  90    15311  13076  12157  -1182    794   -112       C  
ATOM   3057  C   LEU D  90      26.117  14.962  27.770  1.00110.20           C  
ANISOU 3057  C   LEU D  90    15738  13500  12633  -1144    677    -79       C  
ATOM   3058  O   LEU D  90      25.498  14.833  28.828  1.00105.25           O  
ANISOU 3058  O   LEU D  90    14983  12909  12099  -1051    437     35       O  
ATOM   3059  CB  LEU D  90      28.345  16.002  28.242  1.00100.35           C  
ANISOU 3059  CB  LEU D  90    14353  12292  11484  -1104    928   -102       C  
ATOM   3060  CG  LEU D  90      29.330  17.172  28.158  1.00 96.36           C  
ANISOU 3060  CG  LEU D  90    13840  11800  10973  -1125   1038   -128       C  
ATOM   3061  CD1 LEU D  90      29.312  17.985  29.445  1.00116.98           C  
ANISOU 3061  CD1 LEU D  90    16290  14490  13666   -988    808     34       C  
ATOM   3062  CD2 LEU D  90      30.731  16.678  27.851  1.00 77.04           C  
ANISOU 3062  CD2 LEU D  90    11326   9306   8641  -1170   1376   -267       C  
ATOM   3063  N   ASN D  91      26.056  14.071  26.781  1.00114.18           N  
ANISOU 3063  N   ASN D  91    16351  13969  13063  -1230    856   -196       N  
ATOM   3064  CA  ASN D  91      25.364  12.796  26.942  1.00 92.31           C  
ANISOU 3064  CA  ASN D  91    13573  11180  10321  -1194    779   -181       C  
ATOM   3065  C   ASN D  91      26.044  11.998  28.041  1.00 90.22           C  
ANISOU 3065  C   ASN D  91    13268  10838  10173  -1191    817   -139       C  
ATOM   3066  O   ASN D  91      27.244  12.151  28.260  1.00103.35           O  
ANISOU 3066  O   ASN D  91    14914  12432  11922  -1255   1075   -207       O  
ATOM   3067  CB  ASN D  91      25.353  12.004  25.633  1.00 79.81           C  
ANISOU 3067  CB  ASN D  91    12111   9591   8621  -1305   1027   -383       C  
ATOM   3068  N   ALA D  92      25.281  11.166  28.742  1.00 75.33           N  
ANISOU 3068  N   ALA D  92    11374   8920   8327  -1160    580     -2       N  
ATOM   3069  CA  ALA D  92      25.830  10.398  29.856  1.00 77.28           C  
ANISOU 3069  CA  ALA D  92    11433   9015   8914  -1149    494    226       C  
ATOM   3070  C   ALA D  92      27.022   9.548  29.417  1.00 84.97           C  
ANISOU 3070  C   ALA D  92    12352   9529  10405  -1351    869    -64       C  
ATOM   3071  O   ALA D  92      27.994   9.406  30.161  1.00 75.05           O  
ANISOU 3071  O   ALA D  92    10729   8097   9691  -1272    815      0       O  
ATOM   3072  CB  ALA D  92      24.755   9.525  30.478  1.00 70.51           C  
ANISOU 3072  CB  ALA D  92    10436   8148   8207  -1054    111    408       C  
ATOM   3073  N   ASN D  93      26.949   9.001  28.203  1.00 89.21           N  
ANISOU 3073  N   ASN D  93    13005  10014  10875  -1422   1137   -521       N  
ATOM   3074  CA  ASN D  93      28.044   8.214  27.643  1.00103.93           C  
ANISOU 3074  CA  ASN D  93    14554  11613  13322  -1414   1426  -1022       C  
ATOM   3075  C   ASN D  93      29.325   9.027  27.564  1.00103.08           C  
ANISOU 3075  C   ASN D  93    14345  11542  13280  -1453   1792  -1152       C  
ATOM   3076  O   ASN D  93      30.402   8.549  27.917  1.00 95.57           O  
ANISOU 3076  O   ASN D  93    12983  10311  13017  -1392   1850  -1317       O  
ATOM   3077  CB  ASN D  93      27.682   7.686  26.252  1.00133.85           C  
ANISOU 3077  CB  ASN D  93    18532  15444  16881  -1497   1691  -1514       C  
ATOM   3078  CG  ASN D  93      26.743   6.493  26.304  1.00165.95           C  
ANISOU 3078  CG  ASN D  93    22536  19337  21179  -1432   1355  -1522       C  
ATOM   3079  OD1 ASN D  93      26.705   5.760  27.292  1.00174.46           O  
ANISOU 3079  OD1 ASN D  93    23306  20162  22821  -1325    982  -1290       O  
ATOM   3080  ND2 ASN D  93      25.984   6.290  25.232  1.00175.51           N  
ANISOU 3080  ND2 ASN D  93    23966  20758  21962  -1455   1433  -1698       N  
ATOM   3081  N   GLN D  94      29.191  10.268  27.109  1.00114.33           N  
ANISOU 3081  N   GLN D  94    16139  13299  14002  -1559   2020  -1070       N  
ATOM   3082  CA  GLN D  94      30.326  11.169  26.963  1.00104.24           C  
ANISOU 3082  CA  GLN D  94    14819  12098  12689  -1620   2386  -1174       C  
ATOM   3083  C   GLN D  94      30.966  11.495  28.313  1.00 96.73           C  
ANISOU 3083  C   GLN D  94    13569  11023  12162  -1511   2160   -802       C  
ATOM   3084  O   GLN D  94      32.193  11.492  28.445  1.00107.65           O  
ANISOU 3084  O   GLN D  94    14645  12238  14019  -1492   2369   -991       O  
ATOM   3085  CB  GLN D  94      29.880  12.441  26.251  1.00102.93           C  
ANISOU 3085  CB  GLN D  94    14822  12222  12064  -1582   2079   -916       C  
ATOM   3086  CG  GLN D  94      29.193  12.155  24.927  1.00110.18           C  
ANISOU 3086  CG  GLN D  94    15837  13253  12773  -1636   2070  -1037       C  
ATOM   3087  CD  GLN D  94      28.737  13.407  24.213  1.00106.46           C  
ANISOU 3087  CD  GLN D  94    15400  12995  12053  -1536   1800   -830       C  
ATOM   3088  OE1 GLN D  94      28.023  14.235  24.779  1.00 98.05           O  
ANISOU 3088  OE1 GLN D  94    14386  11947  10922  -1461   1497   -579       O  
ATOM   3089  NE2 GLN D  94      29.146  13.552  22.959  1.00107.09           N  
ANISOU 3089  NE2 GLN D  94    15527  13131  12031  -1659   2020  -1033       N  
ATOM   3090  N   ARG D  95      30.132  11.761  29.313  1.00 68.59           N  
ANISOU 3090  N   ARG D  95    10035   7600   8425  -1365   1657   -308       N  
ATOM   3091  CA  ARG D  95      30.610  11.965  30.678  1.00 77.20           C  
ANISOU 3091  CA  ARG D  95    10776   8677   9880  -1180   1292     52       C  
ATOM   3092  C   ARG D  95      31.362  10.727  31.182  1.00 93.23           C  
ANISOU 3092  C   ARG D  95    12385  10279  12759  -1152   1197    -50       C  
ATOM   3093  O   ARG D  95      32.423  10.841  31.803  1.00 74.98           O  
ANISOU 3093  O   ARG D  95     9781   7877  10832  -1066   1161    -16       O  
ATOM   3094  CB  ARG D  95      29.440  12.295  31.609  1.00 70.02           C  
ANISOU 3094  CB  ARG D  95     9803   8069   8732   -978    741    468       C  
ATOM   3095  CG  ARG D  95      28.521  13.386  31.081  1.00 70.78           C  
ANISOU 3095  CG  ARG D  95    10054   8521   8319   -854    645    389       C  
ATOM   3096  CD  ARG D  95      27.168  13.370  31.778  1.00 72.04           C  
ANISOU 3096  CD  ARG D  95    10208   8780   8384   -785    298    467       C  
ATOM   3097  NE  ARG D  95      27.255  13.818  33.163  1.00 95.81           N  
ANISOU 3097  NE  ARG D  95    12999  11870  11536   -697     93    613       N  
ATOM   3098  CZ  ARG D  95      26.983  15.056  33.566  1.00126.46           C  
ANISOU 3098  CZ  ARG D  95    16855  15866  15330   -704    -12    544       C  
ATOM   3099  NH1 ARG D  95      26.604  15.974  32.688  1.00133.26           N  
ANISOU 3099  NH1 ARG D  95    17883  16721  16029   -771     51    395       N  
ATOM   3100  NH2 ARG D  95      27.086  15.378  34.849  1.00127.42           N  
ANISOU 3100  NH2 ARG D  95    16763  16065  15586   -684   -182    624       N  
ATOM   3101  N   LYS D  96      30.811   9.547  30.901  1.00120.72           N  
ANISOU 3101  N   LYS D  96    15816  13544  16508  -1165   1080   -202       N  
ATOM   3102  CA  LYS D  96      31.448   8.285  31.275  1.00121.45           C  
ANISOU 3102  CA  LYS D  96    15472  13325  17348  -1041    882   -342       C  
ATOM   3103  C   LYS D  96      32.837   8.144  30.650  1.00101.27           C  
ANISOU 3103  C   LYS D  96    12631  10605  15242  -1026   1295   -816       C  
ATOM   3104  O   LYS D  96      33.798   7.778  31.332  1.00 99.18           O  
ANISOU 3104  O   LYS D  96    11986  10206  15492   -890   1155   -780       O  
ATOM   3105  CB  LYS D  96      30.569   7.097  30.867  1.00138.07           C  
ANISOU 3105  CB  LYS D  96    17591  15290  19579  -1038    713   -480       C  
ATOM   3106  CG  LYS D  96      29.249   7.003  31.617  1.00146.71           C  
ANISOU 3106  CG  LYS D  96    18893  16528  20322  -1036    270    -26       C  
ATOM   3107  CD  LYS D  96      29.362   6.155  32.872  1.00150.30           C  
ANISOU 3107  CD  LYS D  96    19034  16979  21093   -863   -112    218       C  
ATOM   3108  CE  LYS D  96      29.499   4.679  32.529  1.00148.43           C  
ANISOU 3108  CE  LYS D  96    18506  16470  21422   -788   -205    -36       C  
ATOM   3109  NZ  LYS D  96      29.456   3.820  33.743  1.00149.18           N  
ANISOU 3109  NZ  LYS D  96    18291  16593  21797   -636   -607    242       N  
ATOM   3110  N   GLN D  97      32.936   8.431  29.353  1.00 78.52           N  
ANISOU 3110  N   GLN D  97     9949   7785  12098  -1173   1808  -1271       N  
ATOM   3111  CA  GLN D  97      34.212   8.350  28.642  1.00 83.33           C  
ANISOU 3111  CA  GLN D  97    10300   8320  13041  -1190   2248  -1758       C  
ATOM   3112  C   GLN D  97      35.220   9.340  29.215  1.00 87.92           C  
ANISOU 3112  C   GLN D  97    10774   8947  13685  -1171   2374  -1608       C  
ATOM   3113  O   GLN D  97      36.413   9.031  29.362  1.00100.24           O  
ANISOU 3113  O   GLN D  97    11921  10357  15808  -1083   2468  -1803       O  
ATOM   3114  CB  GLN D  97      34.013   8.607  27.144  1.00 78.44           C  
ANISOU 3114  CB  GLN D  97     9987   7915  11903  -1377   2740  -2195       C  
ATOM   3115  CG  GLN D  97      33.062   7.635  26.469  1.00 90.66           C  
ANISOU 3115  CG  GLN D  97    11632   9465  13350  -1377   2623  -2364       C  
ATOM   3116  CD  GLN D  97      32.783   7.992  25.024  1.00 98.71           C  
ANISOU 3116  CD  GLN D  97    12964  10814  13728  -1557   2978  -2615       C  
ATOM   3117  OE1 GLN D  97      33.682   8.401  24.287  1.00 97.58           O  
ANISOU 3117  OE1 GLN D  97    12746  10795  13536  -1683   3309  -2819       O  
ATOM   3118  NE2 GLN D  97      31.529   7.841  24.609  1.00 98.90           N  
ANISOU 3118  NE2 GLN D  97    13320  10983  13273  -1583   2817  -2514       N  
ATOM   3119  N   LEU D  98      34.729  10.530  29.547  1.00 81.76           N  
ANISOU 3119  N   LEU D  98    10354   8404  12309  -1243   2350  -1243       N  
ATOM   3120  CA  LEU D  98      35.576  11.558  30.133  1.00 87.10           C  
ANISOU 3120  CA  LEU D  98    10965   9184  12947  -1189   2403  -1048       C  
ATOM   3121  C   LEU D  98      36.147  11.091  31.464  1.00 77.17           C  
ANISOU 3121  C   LEU D  98     9300   7766  12256   -969   1936   -755       C  
ATOM   3122  O   LEU D  98      37.358  11.163  31.682  1.00 72.11           O  
ANISOU 3122  O   LEU D  98     8356   7007  12036   -888   2060   -896       O  
ATOM   3123  CB  LEU D  98      34.800  12.866  30.311  1.00 85.13           C  
ANISOU 3123  CB  LEU D  98    11153   9318  11875  -1210   2286   -657       C  
ATOM   3124  CG  LEU D  98      34.521  13.645  29.022  1.00 75.61           C  
ANISOU 3124  CG  LEU D  98    10385   8349   9994  -1353   2609   -911       C  
ATOM   3125  CD1 LEU D  98      33.745  14.918  29.319  1.00 76.36           C  
ANISOU 3125  CD1 LEU D  98    10735   8796   9483  -1210   2125   -507       C  
ATOM   3126  CD2 LEU D  98      35.817  13.955  28.275  1.00 50.06           C  
ANISOU 3126  CD2 LEU D  98     7060   5006   6956  -1451   2984  -1305       C  
HETATM 3127  N   MSE D  99      35.280  10.595  32.344  1.00 75.34           N  
ANISOU 3127  N   MSE D  99     9083   7557  11986   -888   1408   -367       N  
HETATM 3128  CA  MSE D  99      35.722  10.113  33.650  1.00 75.94           C  
ANISOU 3128  CA  MSE D  99     8856   7563  12434   -714    966    -95       C  
HETATM 3129  C   MSE D  99      36.678   8.934  33.503  1.00 82.11           C  
ANISOU 3129  C   MSE D  99     9174   8029  13995   -608   1010   -421       C  
HETATM 3130  O   MSE D  99      37.591   8.764  34.309  1.00 79.20           O  
ANISOU 3130  O   MSE D  99     8486   7579  14030   -471    849   -337       O  
HETATM 3131  CB  MSE D  99      34.525   9.719  34.518  1.00 79.05           C  
ANISOU 3131  CB  MSE D  99     9397   8108  12529   -683    487    281       C  
HETATM 3132  CG  MSE D  99      34.891   9.354  35.952  1.00 85.91           C  
ANISOU 3132  CG  MSE D  99     9997   9023  13624   -517    103    536       C  
HETATM 3133 SE   MSE D  99      33.341   9.139  37.120  1.00175.39          SE  
ANISOU 3133 SE   MSE D  99    21468  20697  24476   -471   -350    896      SE  
HETATM 3134  CE  MSE D  99      32.343   7.827  36.074  1.00115.42           C  
ANISOU 3134  CE  MSE D  99    13963  12884  17008   -547   -348    731       C  
ATOM   3135  N   ALA D 100      36.464   8.123  32.470  1.00 84.22           N  
ANISOU 3135  N   ALA D 100     9396   8148  14456   -669   1219   -808       N  
ATOM   3136  CA  ALA D 100      37.378   7.030  32.159  1.00 89.68           C  
ANISOU 3136  CA  ALA D 100     9625   8589  15862   -583   1300  -1187       C  
ATOM   3137  C   ALA D 100      38.773   7.564  31.856  1.00 98.77           C  
ANISOU 3137  C   ALA D 100    10527   9695  17307   -585   1698  -1488       C  
ATOM   3138  O   ALA D 100      39.766   7.062  32.387  1.00108.02           O  
ANISOU 3138  O   ALA D 100    11261  10711  19071   -455   1573  -1526       O  
ATOM   3139  CB  ALA D 100      36.857   6.214  30.990  1.00103.76           C  
ANISOU 3139  CB  ALA D 100    11447  10300  17675   -671   1502  -1595       C  
ATOM   3140  N   PHE D 101      38.844   8.586  31.006  1.00105.36           N  
ANISOU 3140  N   PHE D 101    11637  10682  17712   -749   2183  -1699       N  
ATOM   3141  CA  PHE D 101      40.129   9.201  30.674  1.00104.59           C  
ANISOU 3141  CA  PHE D 101    11337  10585  17816   -789   2611  -1984       C  
ATOM   3142  C   PHE D 101      40.780   9.839  31.904  1.00 89.51           C  
ANISOU 3142  C   PHE D 101     9318   8662  16028   -618   2343  -1607       C  
ATOM   3143  O   PHE D 101      41.997   9.752  32.095  1.00 81.08           O  
ANISOU 3143  O   PHE D 101     7858   7474  15473   -538   2447  -1775       O  
ATOM   3144  CB  PHE D 101      39.955  10.248  29.571  1.00109.85           C  
ANISOU 3144  CB  PHE D 101    12395  11481  17860  -1042   3172  -2219       C  
ATOM   3145  CG  PHE D 101      41.252  10.802  29.052  1.00118.75           C  
ANISOU 3145  CG  PHE D 101    13421  12629  19068  -1191   3507  -2474       C  
ATOM   3146  CD1 PHE D 101      41.931  10.163  28.028  1.00131.28           C  
ANISOU 3146  CD1 PHE D 101    14800  14137  20942  -1411   3759  -2930       C  
ATOM   3147  CD2 PHE D 101      41.794  11.961  29.588  1.00116.26           C  
ANISOU 3147  CD2 PHE D 101    13297  12374  18502  -1100   3468  -2249       C  
ATOM   3148  CE1 PHE D 101      43.125  10.667  27.549  1.00140.74           C  
ANISOU 3148  CE1 PHE D 101    15985  15289  22199  -1573   3972  -3150       C  
ATOM   3149  CE2 PHE D 101      42.988  12.469  29.114  1.00122.20           C  
ANISOU 3149  CE2 PHE D 101    14081  13010  19338  -1305   3629  -2458       C  
ATOM   3150  CZ  PHE D 101      43.654  11.822  28.092  1.00135.98           C  
ANISOU 3150  CZ  PHE D 101    15592  14698  21374  -1520   3912  -2909       C  
HETATM 3151  N   MSE D 102      39.960  10.475  32.735  1.00 82.69           N  
ANISOU 3151  N   MSE D 102     8786   7963  14670   -585   1986  -1097       N  
HETATM 3152  CA  MSE D 102      40.443  11.157  33.929  1.00 82.18           C  
ANISOU 3152  CA  MSE D 102     8679   7970  14576   -454   1700   -715       C  
HETATM 3153  C   MSE D 102      41.022  10.184  34.949  1.00 98.13           C  
ANISOU 3153  C   MSE D 102    10261   9816  17209   -268   1292   -585       C  
HETATM 3154  O   MSE D 102      42.072  10.443  35.535  1.00104.77           O  
ANISOU 3154  O   MSE D 102    10850  10589  18368   -153   1263   -559       O  
HETATM 3155  CB  MSE D 102      39.315  11.971  34.568  1.00 98.44           C  
ANISOU 3155  CB  MSE D 102    11160  10337  15907   -498   1391   -234       C  
HETATM 3156  CG  MSE D 102      38.994  13.275  33.844  1.00111.98           C  
ANISOU 3156  CG  MSE D 102    13280  12295  16972   -641   1716   -257       C  
HETATM 3157 SE   MSE D 102      40.483  14.540  33.865  1.00135.32          SE  
ANISOU 3157 SE   MSE D 102    16184  15264  19967   -590   2025   -382      SE  
HETATM 3158  CE  MSE D 102      40.896  14.463  35.770  1.00176.77           C  
ANISOU 3158  CE  MSE D 102    21167  20531  25466   -374   1420     70       C  
ATOM   3159  N   GLU D 103      40.332   9.068  35.161  1.00113.18           N  
ANISOU 3159  N   GLU D 103    12082  11655  19267   -242    972   -501       N  
ATOM   3160  CA  GLU D 103      40.797   8.042  36.089  1.00107.59           C  
ANISOU 3160  CA  GLU D 103    10956  10802  19121    -87    570   -376       C  
ATOM   3161  C   GLU D 103      42.034   7.335  35.540  1.00103.45           C  
ANISOU 3161  C   GLU D 103    10000  10020  19286    -62    785   -811       C  
ATOM   3162  O   GLU D 103      42.978   7.049  36.281  1.00103.33           O  
ANISOU 3162  O   GLU D 103     9831   9922  19507    -16    560   -728       O  
ATOM   3163  CB  GLU D 103      39.687   7.028  36.371  1.00104.32           C  
ANISOU 3163  CB  GLU D 103    10596  10400  18642    -88    197   -193       C  
ATOM   3164  N   ALA D 104      42.027   7.060  34.238  1.00107.93           N  
ANISOU 3164  N   ALA D 104    10491  10510  20007   -161   1215  -1283       N  
ATOM   3165  CA  ALA D 104      43.176   6.443  33.580  1.00122.17           C  
ANISOU 3165  CA  ALA D 104    12000  12142  22279   -225   1437  -1729       C  
ATOM   3166  C   ALA D 104      44.401   7.354  33.645  1.00121.83           C  
ANISOU 3166  C   ALA D 104    11970  12120  22201   -261   1656  -1801       C  
ATOM   3167  O   ALA D 104      45.539   6.886  33.602  1.00122.79           O  
ANISOU 3167  O   ALA D 104    11812  12092  22750   -274   1668  -2015       O  
ATOM   3168  CB  ALA D 104      42.842   6.103  32.135  1.00133.70           C  
ANISOU 3168  CB  ALA D 104    13444  13608  23746   -390   1885  -2226       C  
ATOM   3169  N   TRP D 105      44.161   8.657  33.737  1.00123.53           N  
ANISOU 3169  N   TRP D 105    12511  12517  21909   -280   1822  -1624       N  
ATOM   3170  CA  TRP D 105      45.238   9.616  33.946  1.00120.30           C  
ANISOU 3170  CA  TRP D 105    12155  12139  21415   -288   1963  -1618       C  
ATOM   3171  C   TRP D 105      45.690   9.590  35.406  1.00112.19           C  
ANISOU 3171  C   TRP D 105    11033  11082  20512   -130   1475  -1210       C  
ATOM   3172  O   TRP D 105      46.886   9.560  35.695  1.00114.64           O  
ANISOU 3172  O   TRP D 105    11158  11293  21106   -114   1452  -1289       O  
ATOM   3173  CB  TRP D 105      44.782  11.023  33.543  1.00121.27           C  
ANISOU 3173  CB  TRP D 105    12707  12463  20908   -363   2281  -1563       C  
ATOM   3174  CG  TRP D 105      45.834  12.093  33.659  1.00114.77           C  
ANISOU 3174  CG  TRP D 105    11993  11662  19952   -371   2431  -1575       C  
ATOM   3175  CD1 TRP D 105      47.164  11.920  33.915  1.00111.92           C  
ANISOU 3175  CD1 TRP D 105    11370  11169  19986   -338   2395  -1692       C  
ATOM   3176  CD2 TRP D 105      45.635  13.504  33.519  1.00108.93           C  
ANISOU 3176  CD2 TRP D 105    11671  11068  18649   -423   2618  -1466       C  
ATOM   3177  NE1 TRP D 105      47.802  13.135  33.947  1.00105.76           N  
ANISOU 3177  NE1 TRP D 105    10839  10406  18941   -356   2544  -1671       N  
ATOM   3178  CE2 TRP D 105      46.887  14.124  33.706  1.00106.88           C  
ANISOU 3178  CE2 TRP D 105    11384  10726  18501   -423   2671  -1525       C  
ATOM   3179  CE3 TRP D 105      44.520  14.304  33.255  1.00106.80           C  
ANISOU 3179  CE3 TRP D 105    11806  10986  17788   -482   2727  -1322       C  
ATOM   3180  CZ2 TRP D 105      47.054  15.506  33.637  1.00103.08           C  
ANISOU 3180  CZ2 TRP D 105    11227  10353  17587   -487   2814  -1434       C  
ATOM   3181  CZ3 TRP D 105      44.689  15.676  33.185  1.00103.68           C  
ANISOU 3181  CZ3 TRP D 105    11751  10709  16934   -533   2856  -1234       C  
ATOM   3182  CH2 TRP D 105      45.946  16.263  33.377  1.00 96.76           C  
ANISOU 3182  CH2 TRP D 105    10800   9754  16209   -533   2893  -1287       C  
ATOM   3183  N   ARG D 106      44.724   9.582  36.319  1.00113.65           N  
ANISOU 3183  N   ARG D 106    11360  11385  20437    -49   1087   -781       N  
ATOM   3184  CA  ARG D 106      45.003   9.698  37.748  1.00130.32           C  
ANISOU 3184  CA  ARG D 106    13493  13574  22448     31    646   -379       C  
ATOM   3185  C   ARG D 106      45.755   8.495  38.318  1.00154.29           C  
ANISOU 3185  C   ARG D 106    16238  16424  25963     59    352   -408       C  
ATOM   3186  O   ARG D 106      46.640   8.660  39.158  1.00158.67           O  
ANISOU 3186  O   ARG D 106    16736  16972  26579     86    190   -288       O  
ATOM   3187  CB  ARG D 106      43.694   9.903  38.518  1.00122.19           C  
ANISOU 3187  CB  ARG D 106    12717  12786  20925     46    322     38       C  
ATOM   3188  CG  ARG D 106      43.869  10.117  40.014  1.00125.78           C  
ANISOU 3188  CG  ARG D 106    13277  13422  21090     60    -66    394       C  
ATOM   3189  CD  ARG D 106      42.533  10.356  40.705  1.00137.85           C  
ANISOU 3189  CD  ARG D 106    15077  15254  22044     23   -319    713       C  
ATOM   3190  NE  ARG D 106      41.911  11.615  40.296  1.00148.83           N  
ANISOU 3190  NE  ARG D 106    16687  16844  23017     19   -123    780       N  
ATOM   3191  CZ  ARG D 106      40.921  11.713  39.413  1.00144.93           C  
ANISOU 3191  CZ  ARG D 106    16289  16386  22394      8     32    740       C  
ATOM   3192  NH1 ARG D 106      40.430  10.624  38.837  1.00152.04           N  
ANISOU 3192  NH1 ARG D 106    17088  17122  23560    -12     16    617       N  
ATOM   3193  NH2 ARG D 106      40.420  12.903  39.105  1.00121.68           N  
ANISOU 3193  NH2 ARG D 106    13682  13656  18896    -61    207    794       N  
ATOM   3194  N   ASN D 107      45.406   7.293  37.865  1.00174.99           N  
ANISOU 3194  N   ASN D 107    18678  18893  28919     50    285   -575       N  
ATOM   3195  CA  ASN D 107      46.002   6.077  38.416  1.00191.20           C  
ANISOU 3195  CA  ASN D 107    20468  20761  31420     76    -22   -583       C  
ATOM   3196  C   ASN D 107      47.506   5.986  38.163  1.00196.20           C  
ANISOU 3196  C   ASN D 107    20814  21208  32524     65    148   -883       C  
ATOM   3197  O   ASN D 107      48.257   5.505  39.013  1.00203.93           O  
ANISOU 3197  O   ASN D 107    21647  22094  33745     90   -126   -773       O  
ATOM   3198  CB  ASN D 107      45.296   4.831  37.860  1.00202.62           C  
ANISOU 3198  CB  ASN D 107    21776  22073  33138     71   -105   -733       C  
ATOM   3199  CG  ASN D 107      45.322   4.759  36.341  1.00209.21           C  
ANISOU 3199  CG  ASN D 107    22478  22815  34198     12    357  -1227       C  
ATOM   3200  OD1 ASN D 107      46.250   5.242  35.692  1.00212.97           O  
ANISOU 3200  OD1 ASN D 107    22851  23250  34817    -48    721  -1544       O  
ATOM   3201  ND2 ASN D 107      44.295   4.144  35.767  1.00208.11           N  
ANISOU 3201  ND2 ASN D 107    22356  22667  34051     -1    358  -1312       N  
ATOM   3202  N   GLU D 108      47.939   6.449  36.995  1.00166.71           N  
ANISOU 3202  N   GLU D 108    17013  17437  28891     -1    615  -1274       N  
ATOM   3203  CA  GLU D 108      49.358   6.470  36.660  1.00147.61           C  
ANISOU 3203  CA  GLU D 108    14337  14878  26871    -53    821  -1587       C  
ATOM   3204  C   GLU D 108      50.102   7.467  37.545  1.00141.27           C  
ANISOU 3204  C   GLU D 108    13644  14167  25865    -13    744  -1340       C  
ATOM   3205  O   GLU D 108      51.269   7.258  37.882  1.00127.39           O  
ANISOU 3205  O   GLU D 108    11658  12279  24465    -25    678  -1423       O  
ATOM   3206  CB  GLU D 108      49.558   6.815  35.182  1.00120.30           C  
ANISOU 3206  CB  GLU D 108    10847  11424  23435   -204   1373  -2065       C  
ATOM   3207  N   GLN D 109      49.409   8.544  37.914  1.00152.53           N  
ANISOU 3207  N   GLN D 109    15417  15815  26723     25    746  -1047       N  
ATOM   3208  CA  GLN D 109      49.951   9.594  38.779  1.00153.75           C  
ANISOU 3208  CA  GLN D 109    15726  16091  26600     70    666   -796       C  
ATOM   3209  C   GLN D 109      51.246  10.185  38.227  1.00148.94           C  
ANISOU 3209  C   GLN D 109    14986  15403  26201     24   1002  -1094       C  
ATOM   3210  O   GLN D 109      51.277  10.702  37.110  1.00139.26           O  
ANISOU 3210  O   GLN D 109    13825  14199  24888    -57   1429  -1385       O  
ATOM   3211  CB  GLN D 109      50.180   9.057  40.195  1.00159.47           C  
ANISOU 3211  CB  GLN D 109    16394  16818  27378    114    188   -475       C  
TER    3212      GLN D 109                                                      
CONECT  387  393                                                                
CONECT  393  387  394                                                           
CONECT  394  393  395  397                                                      
CONECT  395  394  396  401                                                      
CONECT  396  395                                                                
CONECT  397  394  398                                                           
CONECT  398  397  399                                                           
CONECT  399  398  400                                                           
CONECT  400  399                                                                
CONECT  401  395                                                                
CONECT 1166 1172                                                                
CONECT 1172 1166 1173                                                           
CONECT 1173 1172 1174 1176                                                      
CONECT 1174 1173 1175 1180                                                      
CONECT 1175 1174                                                                
CONECT 1176 1173 1177                                                           
CONECT 1177 1176 1178                                                           
CONECT 1178 1177 1179                                                           
CONECT 1179 1178                                                                
CONECT 1180 1174                                                                
CONECT 1576 1584                                                                
CONECT 1584 1576 1585                                                           
CONECT 1585 1584 1586 1588                                                      
CONECT 1586 1585 1587 1592                                                      
CONECT 1587 1586                                                                
CONECT 1588 1585 1589                                                           
CONECT 1589 1588 1590                                                           
CONECT 1590 1589 1591                                                           
CONECT 1591 1590                                                                
CONECT 1592 1586                                                                
CONECT 1842 1848                                                                
CONECT 1848 1842 1849                                                           
CONECT 1849 1848 1850 1852                                                      
CONECT 1850 1849 1851 1856                                                      
CONECT 1851 1850                                                                
CONECT 1852 1849 1853                                                           
CONECT 1853 1852 1854                                                           
CONECT 1854 1853 1855                                                           
CONECT 1855 1854                                                                
CONECT 1856 1850                                                                
CONECT 2195 2202                                                                
CONECT 2202 2195 2203                                                           
CONECT 2203 2202 2204 2206                                                      
CONECT 2204 2203 2205 2210                                                      
CONECT 2205 2204                                                                
CONECT 2206 2203 2207                                                           
CONECT 2207 2206 2208                                                           
CONECT 2208 2207 2209                                                           
CONECT 2209 2208                                                                
CONECT 2210 2204                                                                
CONECT 2289 2295                                                                
CONECT 2295 2289 2296                                                           
CONECT 2296 2295 2297 2299                                                      
CONECT 2297 2296 2298 2303                                                      
CONECT 2298 2297                                                                
CONECT 2299 2296 2300                                                           
CONECT 2300 2299 2301                                                           
CONECT 2301 2300 2302                                                           
CONECT 2302 2301                                                                
CONECT 2303 2297                                                                
CONECT 2310 2319                                                                
CONECT 2319 2310 2320                                                           
CONECT 2320 2319 2321 2323                                                      
CONECT 2321 2320 2322 2327                                                      
CONECT 2322 2321                                                                
CONECT 2323 2320 2324                                                           
CONECT 2324 2323 2325                                                           
CONECT 2325 2324 2326                                                           
CONECT 2326 2325                                                                
CONECT 2327 2321                                                                
CONECT 2638 2644                                                                
CONECT 2644 2638 2645                                                           
CONECT 2645 2644 2646 2648                                                      
CONECT 2646 2645 2647 2652                                                      
CONECT 2647 2646                                                                
CONECT 2648 2645 2649                                                           
CONECT 2649 2648 2650                                                           
CONECT 2650 2649 2651                                                           
CONECT 2651 2650                                                                
CONECT 2652 2646                                                                
CONECT 3029 3036                                                                
CONECT 3036 3029 3037                                                           
CONECT 3037 3036 3038 3040                                                      
CONECT 3038 3037 3039 3044                                                      
CONECT 3039 3038                                                                
CONECT 3040 3037 3041                                                           
CONECT 3041 3040 3042                                                           
CONECT 3042 3041 3043                                                           
CONECT 3043 3042                                                                
CONECT 3044 3038                                                                
CONECT 3121 3127                                                                
CONECT 3127 3121 3128                                                           
CONECT 3128 3127 3129 3131                                                      
CONECT 3129 3128 3130 3135                                                      
CONECT 3130 3129                                                                
CONECT 3131 3128 3132                                                           
CONECT 3132 3131 3133                                                           
CONECT 3133 3132 3134                                                           
CONECT 3134 3133                                                                
CONECT 3135 3129                                                                
CONECT 3142 3151                                                                
CONECT 3151 3142 3152                                                           
CONECT 3152 3151 3153 3155                                                      
CONECT 3153 3152 3154 3159                                                      
CONECT 3154 3153                                                                
CONECT 3155 3152 3156                                                           
CONECT 3156 3155 3157                                                           
CONECT 3157 3156 3158                                                           
CONECT 3158 3157                                                                
CONECT 3159 3153                                                                
MASTER      341    0   11   18   12    0    0    6 3208    4  110   34          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.