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***  METAL TRANSPORT, MEMBRANE PROTEIN 02-AUG-07 2QTO  ***

elNémo ID: 21111012221567437

Job options:

ID        	=	 21111012221567437
JOBID     	=	 METAL TRANSPORT, MEMBRANE PROTEIN 02-AUG-07 2QTO
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    METAL TRANSPORT, MEMBRANE PROTEIN       02-AUG-07   2QTO              
TITLE     AN ANISOTROPIC MODEL FOR POTASSIUM CHANNEL KCSA                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: POTASSIUM CHANNEL KCSA;                                     
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;                          
SOURCE   3 ORGANISM_TAXID: 1916;                                                
SOURCE   4 GENE: KCSA, SKC1;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    POTASSIUM CHANNEL, MEMBRANE PROTEINS, NORMAL-MODE REFINEMENT,         
KEYWDS   2 ANISOTROPIC THERMAL FACTORS, METAL TRANSPORT, MEMBRANE PROTEIN       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.CHEN,B.K.POON,A.DOUSIS,Q.WANG,J.MA                                  
REVDAT   3   20-OCT-21 2QTO    1       SEQADV LINK                              
REVDAT   2   24-FEB-09 2QTO    1       VERSN                                    
REVDAT   1   25-SEP-07 2QTO    0                                                
JRNL        AUTH   X.CHEN,B.K.POON,A.DOUSIS,Q.WANG,J.MA                         
JRNL        TITL   NORMAL-MODE REFINEMENT OF ANISOTROPIC THERMAL PARAMETERS FOR 
JRNL        TITL 2 POTASSIUM CHANNEL KCSA AT 3.2 A CRYSTALLOGRAPHIC RESOLUTION  
JRNL        REF    STRUCTURE                     V.  15   955 2007              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   17698000                                                     
JRNL        DOI    10.1016/J.STR.2007.06.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.99                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 10912                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.272                           
REMARK   3   R VALUE            (WORKING SET) : 0.272                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.400                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1265                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 520                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2849                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 121.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.06000                                             
REMARK   3    B22 (A**2) : 0.68000                                              
REMARK   3    B33 (A**2) : -1.49000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.64000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.993         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.461         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2925 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4040 ; 0.989 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   384 ; 5.493 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    83 ;47.921 ;21.566       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   376 ;20.400 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ; 8.627 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   504 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2143 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1537 ; 0.285 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2103 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   103 ; 0.173 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    11 ; 0.108 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    24 ; 0.469 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     23       A     119      1                      
REMARK   3           1     B     23       B     119      1                      
REMARK   3           1     C     23       C     119      1                      
REMARK   3           1     D     23       D     119      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    710 ;  0.09 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    710 ;  0.15 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    710 ;  0.09 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    710 ;  0.10 ;  0.05           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QTO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044041.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.908                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12603                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.201                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: 1BL8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM CACL2, 100 MM HEPES PH 7.5, 48%   
REMARK 280  PEG 400                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       64.39000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.46500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       64.39000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.46500            
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 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 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     ARG A  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 117    CZ   NH1  NH2                                       
REMARK 470     ARG B  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  64    CG   CD   NE   CZ   NH1  NH2                        
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    PRO A  55       61.03    -68.63                                   
REMARK 500    ALA A  57      164.61    -46.20                                   
REMARK 500    GLN A  58       21.67    -62.73                                   
REMARK 500    PRO A  63       -6.46    -57.83                                   
REMARK 500    PRO B  55       61.26    -68.72                                   
REMARK 500    ALA B  57      163.46    -46.46                                   
REMARK 500    GLN B  58       22.06    -62.17                                   
REMARK 500    PRO B  63       -6.44    -57.43                                   
REMARK 500    PRO C  55       61.00    -68.89                                   
REMARK 500    ALA C  57      164.18    -47.49                                   
REMARK 500    GLN C  58       23.49    -62.37                                   
REMARK 500    PRO C  63       -6.26    -57.79                                   
REMARK 500    PRO D  55       60.31    -69.31                                   
REMARK 500    ALA D  57      164.49    -48.57                                   
REMARK 500    GLN D  58       21.88    -61.54                                   
REMARK 500    PRO D  63       -6.64    -57.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A   1   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  75   OG1                                                    
REMARK 620 2 THR B  75   O   108.8                                              
REMARK 620 3 THR B  75   OG1  89.3  51.3                                        
REMARK 620 4 THR C  75   OG1 163.9  82.4  89.0                                  
REMARK 620 5 THR D  75   OG1  89.6 144.1 163.0  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A   2   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  75   O                                                      
REMARK 620 2 THR B  75   O    72.3                                              
REMARK 620 3 THR C  75   O   116.8  71.6                                        
REMARK 620 4 THR D  75   O    75.6 113.9  74.1                                  
REMARK 620 5 VAL D  76   O    89.6 152.9 135.5  79.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A   3   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  78   O                                                      
REMARK 620 2 TYR B  78   O    82.8                                              
REMARK 620 3 TYR C  78   O   138.5  80.0                                        
REMARK 620 4 TYR D  78   O    84.9 138.6  83.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BL8   RELATED DB: PDB                                   
REMARK 900 THIS IS THE NEWLY REFINED MODEL OF 1BL8 THAT WAS IMPROVED BY USING   
REMARK 900 A NEW NORMAL-MODE BASED REFINEMENT METHOD                            
DBREF  2QTO A   23   119  UNP    P0A334   KCSA_STRLI      23    119             
DBREF  2QTO B   23   119  UNP    P0A334   KCSA_STRLI      23    119             
DBREF  2QTO C   23   119  UNP    P0A334   KCSA_STRLI      23    119             
DBREF  2QTO D   23   119  UNP    P0A334   KCSA_STRLI      23    119             
SEQADV 2QTO CYS A   90  UNP  P0A334    LEU    90 ENGINEERED MUTATION            
SEQADV 2QTO CYS B   90  UNP  P0A334    LEU    90 ENGINEERED MUTATION            
SEQADV 2QTO CYS C   90  UNP  P0A334    LEU    90 ENGINEERED MUTATION            
SEQADV 2QTO CYS D   90  UNP  P0A334    LEU    90 ENGINEERED MUTATION            
SEQRES   1 A   97  ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU          
SEQRES   2 A   97  LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL          
SEQRES   3 A   97  LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR          
SEQRES   4 A   97  TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR          
SEQRES   5 A   97  THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP          
SEQRES   6 A   97  GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE          
SEQRES   7 A   97  THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP          
SEQRES   8 A   97  PHE VAL GLY ARG GLU GLN                                      
SEQRES   1 B   97  ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU          
SEQRES   2 B   97  LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL          
SEQRES   3 B   97  LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR          
SEQRES   4 B   97  TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR          
SEQRES   5 B   97  THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP          
SEQRES   6 B   97  GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE          
SEQRES   7 B   97  THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP          
SEQRES   8 B   97  PHE VAL GLY ARG GLU GLN                                      
SEQRES   1 C   97  ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU          
SEQRES   2 C   97  LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL          
SEQRES   3 C   97  LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR          
SEQRES   4 C   97  TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR          
SEQRES   5 C   97  THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP          
SEQRES   6 C   97  GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE          
SEQRES   7 C   97  THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP          
SEQRES   8 C   97  PHE VAL GLY ARG GLU GLN                                      
SEQRES   1 D   97  ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU          
SEQRES   2 D   97  LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL          
SEQRES   3 D   97  LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR          
SEQRES   4 D   97  TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR          
SEQRES   5 D   97  THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP          
SEQRES   6 D   97  GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE          
SEQRES   7 D   97  THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP          
SEQRES   8 D   97  PHE VAL GLY ARG GLU GLN                                      
HET      K  A   1       1                                                       
HET      K  A   2       1                                                       
HET      K  A   3       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL   5    K    3(K 1+)                                                      
FORMUL   8  HOH   *(H2 O)                                                       
HELIX    1   1 LEU A   24  ARG A   52  1                                  29    
HELIX    2   2 THR A   61  THR A   74  1                                  14    
HELIX    3   3 THR A   85  GLY A  116  1                                  32    
HELIX    4   4 LEU B   24  ARG B   52  1                                  29    
HELIX    5   5 THR B   61  THR B   74  1                                  14    
HELIX    6   6 THR B   85  GLY B  116  1                                  32    
HELIX    7   7 LEU C   24  ARG C   52  1                                  29    
HELIX    8   8 THR C   61  THR C   74  1                                  14    
HELIX    9   9 THR C   85  GLY C  116  1                                  32    
HELIX   10  10 LEU D   24  ARG D   52  1                                  29    
HELIX   11  11 THR D   61  THR D   74  1                                  14    
HELIX   12  12 THR D   85  GLY D  116  1                                  32    
LINK         K     K A   1                 OG1 THR A  75     1555   1555  2.71  
LINK         K     K A   1                 O   THR B  75     1555   1555  3.00  
LINK         K     K A   1                 OG1 THR B  75     1555   1555  2.74  
LINK         K     K A   1                 OG1 THR C  75     1555   1555  2.72  
LINK         K     K A   1                 OG1 THR D  75     1555   1555  2.70  
LINK         K     K A   2                 O   THR A  75     1555   1555  2.70  
LINK         K     K A   2                 O   THR B  75     1555   1555  2.85  
LINK         K     K A   2                 O   THR C  75     1555   1555  2.76  
LINK         K     K A   2                 O   THR D  75     1555   1555  2.68  
LINK         K     K A   2                 O   VAL D  76     1555   1555  2.99  
LINK         K     K A   3                 O   TYR A  78     1555   1555  2.67  
LINK         K     K A   3                 O   TYR B  78     1555   1555  2.69  
LINK         K     K A   3                 O   TYR C  78     1555   1555  2.76  
LINK         K     K A   3                 O   TYR D  78     1555   1555  2.55  
CRYST1  128.780   68.930  112.040  90.00 124.63  90.00 C 1 2 1      16          
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      0.007765  0.000000  0.005363        0.00000                         
SCALE2      0.000000  0.014507  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010847        0.00000                         
ATOM      1  N   ALA A  23      65.970  21.141  48.213  1.00230.64           N  
ANISOU    1  N   ALA A  23    23715  51669  12247  -9463    717   8011       N  
ATOM      2  CA  ALA A  23      66.882  22.321  48.219  1.00228.69           C  
ANISOU    2  CA  ALA A  23    23683  51169  12041  -9045    520   7378       C  
ATOM      3  C   ALA A  23      66.288  23.477  47.413  1.00226.58           C  
ANISOU    3  C   ALA A  23    23288  50868  11935  -8602    732   6631       C  
ATOM      4  O   ALA A  23      65.065  23.600  47.314  1.00229.70           O  
ANISOU    4  O   ALA A  23    23388  51902  11986  -8508   1087   6475       O  
ATOM      5  CB  ALA A  23      68.254  21.928  47.681  1.00223.81           C  
ANISOU    5  CB  ALA A  23    23347  49650  12042  -9072    111   7537       C  
ATOM      6  N   LEU A  24      67.151  24.332  46.861  1.00198.31           N  
ANISOU    6  N   LEU A  24    20090  45521   9739  -4707   1188   2198       N  
ATOM      7  CA  LEU A  24      66.719  25.388  45.947  1.00195.45           C  
ANISOU    7  CA  LEU A  24    19674  44884   9704  -4325   1320   1587       C  
ATOM      8  C   LEU A  24      67.113  25.042  44.518  1.00188.84           C  
ANISOU    8  C   LEU A  24    18907  43147   9695  -4394   1156   1729       C  
ATOM      9  O   LEU A  24      66.254  24.942  43.644  1.00186.48           O  
ANISOU    9  O   LEU A  24    18421  42694   9740  -4388   1338   1778       O  
ATOM     10  CB  LEU A  24      67.305  26.752  46.336  1.00196.61           C  
ANISOU   10  CB  LEU A  24    20065  44983   9656  -3944   1182    871       C  
ATOM     11  CG  LEU A  24      66.981  27.921  45.392  1.00193.62           C  
ANISOU   11  CG  LEU A  24    19735  44142   9690  -3550   1231    262       C  
ATOM     12  CD1 LEU A  24      65.651  28.577  45.746  1.00198.38           C  
ANISOU   12  CD1 LEU A  24    20188  45399   9789  -3149   1543   -234       C  
ATOM     13  CD2 LEU A  24      68.098  28.952  45.389  1.00191.30           C  
ANISOU   13  CD2 LEU A  24    19808  43189   9689  -3429    870   -145       C  
ATOM     14  N   HIS A  25      68.415  24.858  44.295  1.00167.27           N  
ANISOU   14  N   HIS A  25    18349  35669   9538  -3209    167   2454       N  
ATOM     15  CA  HIS A  25      68.965  24.587  42.966  1.00161.47           C  
ANISOU   15  CA  HIS A  25    17678  34129   9544  -3253     -4   2584       C  
ATOM     16  C   HIS A  25      68.242  23.446  42.250  1.00159.92           C  
ANISOU   16  C   HIS A  25    17302  33826   9633  -3476    159   3058       C  
ATOM     17  O   HIS A  25      67.910  23.551  41.070  1.00156.80           O  
ANISOU   17  O   HIS A  25    16799  33148   9629  -3370    295   2896       O  
ATOM     18  CB  HIS A  25      70.480  24.334  43.048  1.00160.44           C  
ANISOU   18  CB  HIS A  25    17754  33643   9562  -3350   -391   2759       C  
ATOM     19  CG  HIS A  25      70.857  23.009  43.637  1.00162.09           C  
ANISOU   19  CG  HIS A  25    17986  33919   9681  -3639   -526   3436       C  
ATOM     20  ND1 HIS A  25      72.114  22.748  44.134  1.00160.58           N  
ANISOU   20  ND1 HIS A  25    17925  33312   9775  -3687   -867   3690       N  
ATOM     21  CD2 HIS A  25      70.143  21.872  43.812  1.00165.71           C  
ANISOU   21  CD2 HIS A  25    18367  34812   9782  -3890   -390   3923       C  
ATOM     22  CE1 HIS A  25      72.161  21.510  44.590  1.00163.10           C  
ANISOU   22  CE1 HIS A  25    18290  33744   9938  -3911   -954   4292       C  
ATOM     23  NE2 HIS A  25      70.978  20.956  44.403  1.00166.22           N  
ANISOU   23  NE2 HIS A  25    18578  34631   9948  -4077   -674   4463       N  
ATOM     24  N   TRP A  26      67.974  22.378  42.994  1.00174.52           N  
ANISOU   24  N   TRP A  26    18968  35081  12260  -5385   -623   5430       N  
ATOM     25  CA  TRP A  26      67.359  21.171  42.468  1.00174.14           C  
ANISOU   25  CA  TRP A  26    18823  34905  12436  -5696   -546   5963       C  
ATOM     26  C   TRP A  26      65.867  21.382  42.206  1.00175.26           C  
ANISOU   26  C   TRP A  26    18652  35461  12479  -5718   -183   5866       C  
ATOM     27  O   TRP A  26      65.288  20.736  41.331  1.00173.76           O  
ANISOU   27  O   TRP A  26    18370  35025  12625  -5932   -130   6161       O  
ATOM     28  CB  TRP A  26      67.564  20.044  43.482  1.00178.91           C  
ANISOU   28  CB  TRP A  26    19513  35855  12609  -6049   -649   6575       C  
ATOM     29  CG  TRP A  26      68.324  18.820  43.003  1.00177.66           C  
ANISOU   29  CG  TRP A  26    19578  35090  12836  -6276   -942   7131       C  
ATOM     30  CD1 TRP A  26      68.497  17.659  43.700  1.00181.96           C  
ANISOU   30  CD1 TRP A  26    20262  35774  13099  -6624  -1082   7778       C  
ATOM     31  CD2 TRP A  26      69.001  18.635  41.746  1.00172.45           C  
ANISOU   31  CD2 TRP A  26    19051  33593  12878  -6147  -1145   7101       C  
ATOM     32  NE1 TRP A  26      69.240  16.767  42.969  1.00179.84           N  
ANISOU   32  NE1 TRP A  26    20240  34758  13333  -6679  -1382   8126       N  
ATOM     33  CE2 TRP A  26      69.562  17.337  41.766  1.00174.01           C  
ANISOU   33  CE2 TRP A  26    19480  33443  13192  -6379  -1412   7707       C  
ATOM     34  CE3 TRP A  26      69.190  19.434  40.609  1.00167.05           C  
ANISOU   34  CE3 TRP A  26    18328  32430  12715  -5853  -1135   6628       C  
ATOM     35  CZ2 TRP A  26      70.297  16.818  40.694  1.00170.45           C  
ANISOU   35  CZ2 TRP A  26    19207  32210  13348  -6271  -1654   7807       C  
ATOM     36  CZ3 TRP A  26      69.923  18.917  39.542  1.00163.40           C  
ANISOU   36  CZ3 TRP A  26    18009  31242  12833  -5797  -1356   6759       C  
ATOM     37  CH2 TRP A  26      70.466  17.620  39.595  1.00165.16           C  
ANISOU   37  CH2 TRP A  26    18447  31159  13148  -5980  -1606   7323       C  
ATOM     38  N   ARG A  27      65.262  22.300  42.962  1.00186.03           N  
ANISOU   38  N   ARG A  27    17999  42273  10410  -5773    375   4805       N  
ATOM     39  CA  ARG A  27      63.817  22.542  42.924  1.00188.83           C  
ANISOU   39  CA  ARG A  27    17981  43258  10506  -5763    743   4730       C  
ATOM     40  C   ARG A  27      63.412  23.731  42.053  1.00186.40           C  
ANISOU   40  C   ARG A  27    17576  42822  10427  -5284    875   4066       C  
ATOM     41  O   ARG A  27      62.323  23.732  41.477  1.00187.05           O  
ANISOU   41  O   ARG A  27    17342  43185  10542  -5249   1122   4026       O  
ATOM     42  CB  ARG A  27      63.271  22.730  44.341  1.00195.81           C  
ANISOU   42  CB  ARG A  27    18695  45151  10553  -5829    951   4793       C  
ATOM     43  N   ALA A  28      64.282  24.739  41.974  1.00169.52           N  
ANISOU   43  N   ALA A  28    16519  39677   8215  -2340    876    853       N  
ATOM     44  CA  ALA A  28      64.056  25.911  41.122  1.00166.84           C  
ANISOU   44  CA  ALA A  28    16206  38996   8191  -1899    910    250       C  
ATOM     45  C   ALA A  28      64.085  25.524  39.648  1.00161.46           C  
ANISOU   45  C   ALA A  28    15492  37649   8206  -1999    854    425       C  
ATOM     46  O   ALA A  28      63.323  26.061  38.839  1.00160.44           O  
ANISOU   46  O   ALA A  28    15201  37491   8269  -1761   1005    159       O  
ATOM     47  CB  ALA A  28      65.089  26.997  41.409  1.00165.88           C  
ANISOU   47  CB  ALA A  28    16448  38476   8101  -1632    651   -231       C  
ATOM     48  N   ALA A  29      64.968  24.582  39.318  1.00147.25           N  
ANISOU   48  N   ALA A  29    15195  31695   9059  -2660    685   1603       N  
ATOM     49  CA  ALA A  29      65.098  24.063  37.962  1.00142.42           C  
ANISOU   49  CA  ALA A  29    14596  30431   9086  -2769    601   1791       C  
ATOM     50  C   ALA A  29      63.851  23.285  37.550  1.00143.71           C  
ANISOU   50  C   ALA A  29    14454  30895   9253  -3001    820   2108       C  
ATOM     51  O   ALA A  29      63.254  23.569  36.513  1.00142.74           O  
ANISOU   51  O   ALA A  29    14141  30804   9290  -2807    974   1849       O  
ATOM     52  CB  ALA A  29      66.344  23.198  37.839  1.00140.01           C  
ANISOU   52  CB  ALA A  29    14536  29582   9078  -2991    303   2157       C  
ATOM     53  N   GLY A  30      63.453  22.315  38.369  1.00159.95           N  
ANISOU   53  N   GLY A  30    15836  33727  11209  -5206    625   4545       N  
ATOM     54  CA  GLY A  30      62.239  21.544  38.119  1.00162.12           C  
ANISOU   54  CA  GLY A  30    15810  34350  11438  -5520    816   4879       C  
ATOM     55  C   GLY A  30      61.010  22.413  37.912  1.00163.90           C  
ANISOU   55  C   GLY A  30    15642  35152  11480  -5256   1127   4500       C  
ATOM     56  O   GLY A  30      60.107  22.048  37.157  1.00163.49           O  
ANISOU   56  O   GLY A  30    15347  35124  11646  -5395   1227   4619       O  
ATOM     57  N   ALA A  31      60.983  23.564  38.583  1.00165.51           N  
ANISOU   57  N   ALA A  31    14682  39756   8448  -3462   1223   3082       N  
ATOM     58  CA  ALA A  31      59.880  24.517  38.472  1.00168.17           C  
ANISOU   58  CA  ALA A  31    14654  40696   8548  -3101   1509   2672       C  
ATOM     59  C   ALA A  31      59.984  25.358  37.203  1.00163.89           C  
ANISOU   59  C   ALA A  31    14189  39586   8495  -2653   1450   2183       C  
ATOM     60  O   ALA A  31      58.968  25.774  36.640  1.00165.49           O  
ANISOU   60  O   ALA A  31    14052  40168   8658  -2381   1656   1936       O  
ATOM     61  CB  ALA A  31      59.821  25.409  39.697  1.00173.36           C  
ANISOU   61  CB  ALA A  31    15245  42095   8528  -2799   1669   2337       C  
ATOM     62  N   ALA A  32      61.213  25.607  36.759  1.00142.86           N  
ANISOU   62  N   ALA A  32    13834  32795   7651  -1435   1289    140       N  
ATOM     63  CA  ALA A  32      61.451  26.356  35.528  1.00138.89           C  
ANISOU   63  CA  ALA A  32    13414  31722   7634  -1105   1218   -222       C  
ATOM     64  C   ALA A  32      60.982  25.587  34.296  1.00136.28           C  
ANISOU   64  C   ALA A  32    12915  31142   7723  -1393   1222    130       C  
ATOM     65  O   ALA A  32      60.541  26.194  33.318  1.00135.85           O  
ANISOU   65  O   ALA A  32    12653  31129   7834  -1181   1322    -61       O  
ATOM     66  CB  ALA A  32      62.921  26.727  35.396  1.00134.95           C  
ANISOU   66  CB  ALA A  32    13352  30460   7463   -987    935   -431       C  
ATOM     67  N   THR A  33      61.081  24.257  34.346  1.00132.81           N  
ANISOU   67  N   THR A  33    13543  28096   8823  -3049   1537   2094       N  
ATOM     68  CA  THR A  33      60.627  23.400  33.242  1.00131.05           C  
ANISOU   68  CA  THR A  33    13195  27632   8965  -3339   1518   2407       C  
ATOM     69  C   THR A  33      59.100  23.344  33.180  1.00134.98           C  
ANISOU   69  C   THR A  33    13196  28884   9206  -3369   1793   2420       C  
ATOM     70  O   THR A  33      58.520  23.186  32.104  1.00133.44           O  
ANISOU   70  O   THR A  33    12838  28541   9323  -3378   1803   2412       O  
ATOM     71  CB  THR A  33      61.202  21.966  33.318  1.00130.43           C  
ANISOU   71  CB  THR A  33    13327  27195   9034  -3827   1326   2957       C  
ATOM     72  OG1 THR A  33      60.678  21.295  34.469  1.00135.62           O  
ANISOU   72  OG1 THR A  33    13800  28500   9229  -4214   1444   3364       O  
ATOM     73  CG2 THR A  33      62.730  21.992  33.378  1.00127.90           C  
ANISOU   73  CG2 THR A  33    13398  26363   8834  -3709   1090   2896       C  
ATOM     74  N   VAL A  34      58.459  23.478  34.336  1.00147.08           N  
ANISOU   74  N   VAL A  34    13203  33800   8880  -3291   1533   3323       N  
ATOM     75  CA  VAL A  34      57.008  23.631  34.391  1.00151.15           C  
ANISOU   75  CA  VAL A  34    13195  35109   9125  -3182   1808   3222       C  
ATOM     76  C   VAL A  34      56.624  24.992  33.808  1.00149.99           C  
ANISOU   76  C   VAL A  34    12993  34890   9106  -2513   1860   2606       C  
ATOM     77  O   VAL A  34      55.558  25.139  33.208  1.00151.16           O  
ANISOU   77  O   VAL A  34    12773  35341   9319  -2392   1982   2528       O  
ATOM     78  CB  VAL A  34      56.481  23.502  35.832  1.00157.77           C  
ANISOU   78  CB  VAL A  34    13710  36975   9262  -3277   2061   3334       C  
ATOM     79  CG1 VAL A  34      54.988  23.787  35.881  1.00162.24           C  
ANISOU   79  CG1 VAL A  34    13653  38416   9574  -3160   2350   3246       C  
ATOM     80  CG2 VAL A  34      56.786  22.120  36.389  1.00159.51           C  
ANISOU   80  CG2 VAL A  34    14017  37247   9343  -3978   1983   4004       C  
ATOM     81  N   LEU A  35      57.502  25.977  33.981  1.00140.78           N  
ANISOU   81  N   LEU A  35    13091  32627   7771  -1071   1593   -140       N  
ATOM     82  CA  LEU A  35      57.275  27.309  33.433  1.00138.96           C  
ANISOU   82  CA  LEU A  35    12963  32042   7792   -491   1544   -673       C  
ATOM     83  C   LEU A  35      57.502  27.350  31.913  1.00133.54           C  
ANISOU   83  C   LEU A  35    12398  30590   7753   -588   1365   -573       C  
ATOM     84  O   LEU A  35      56.813  28.090  31.200  1.00133.92           O  
ANISOU   84  O   LEU A  35    12194  30756   7934   -351   1432   -723       O  
ATOM     85  CB  LEU A  35      58.149  28.340  34.151  1.00138.73           C  
ANISOU   85  CB  LEU A  35    13365  31690   7657    -92   1412  -1133       C  
ATOM     86  CG  LEU A  35      57.585  29.758  34.273  1.00143.40           C  
ANISOU   86  CG  LEU A  35    13803  32791   7892    557   1573  -1688       C  
ATOM     87  CD1 LEU A  35      57.947  30.350  35.629  1.00146.45           C  
ANISOU   87  CD1 LEU A  35    14474  33327   7842    797   1539  -2028       C  
ATOM     88  CD2 LEU A  35      58.055  30.662  33.134  1.00140.83           C  
ANISOU   88  CD2 LEU A  35    13633  31867   8009    996   1439  -2046       C  
ATOM     89  N   LEU A  36      58.456  26.553  31.423  1.00121.21           N  
ANISOU   89  N   LEU A  36    13022  25318   7715  -1580   1524    -27       N  
ATOM     90  CA  LEU A  36      58.762  26.503  29.989  1.00116.51           C  
ANISOU   90  CA  LEU A  36    12555  24037   7675  -1656   1363     48       C  
ATOM     91  C   LEU A  36      57.595  25.950  29.174  1.00117.63           C  
ANISOU   91  C   LEU A  36    12294  24499   7902  -1791   1474    219       C  
ATOM     92  O   LEU A  36      57.287  26.469  28.102  1.00116.20           O  
ANISOU   92  O   LEU A  36    12064  24117   7970  -1509   1445     -5       O  
ATOM     93  CB  LEU A  36      60.048  25.709  29.712  1.00112.90           C  
ANISOU   93  CB  LEU A  36    12417  22973   7507  -2046   1152    390       C  
ATOM     94  CG  LEU A  36      60.510  25.618  28.245  1.00108.06           C  
ANISOU   94  CG  LEU A  36    12009  21618   7429  -1988    976    333       C  
ATOM     95  CD1 LEU A  36      60.792  26.992  27.622  1.00107.16           C  
ANISOU   95  CD1 LEU A  36    11986  21309   7421  -1492    959   -147       C  
ATOM     96  CD2 LEU A  36      61.726  24.710  28.102  1.00104.82           C  
ANISOU   96  CD2 LEU A  36    11950  20611   7264  -2186    759    519       C  
ATOM     97  N   VAL A  37      56.952  24.904  29.690  1.00126.27           N  
ANISOU   97  N   VAL A  37    13357  26133   8487  -3351   1649    968       N  
ATOM     98  CA  VAL A  37      55.763  24.328  29.058  1.00128.32           C  
ANISOU   98  CA  VAL A  37    13186  26798   8771  -3568   1746   1164       C  
ATOM     99  C   VAL A  37      54.653  25.376  28.936  1.00131.34           C  
ANISOU   99  C   VAL A  37    13173  27768   8961  -3048   1929    769       C  
ATOM    100  O   VAL A  37      54.001  25.470  27.895  1.00130.32           O  
ANISOU  100  O   VAL A  37    12886  27534   9094  -2946   1888    702       O  
ATOM    101  CB  VAL A  37      55.284  23.052  29.805  1.00132.21           C  
ANISOU  101  CB  VAL A  37    13449  27802   8983  -4206   1824   1698       C  
ATOM    102  CG1 VAL A  37      53.804  22.777  29.569  1.00137.10           C  
ANISOU  102  CG1 VAL A  37    13451  29289   9353  -4339   2030   1803       C  
ATOM    103  CG2 VAL A  37      56.118  21.856  29.380  1.00129.13           C  
ANISOU  103  CG2 VAL A  37    13398  26687   8978  -4707   1575   2102       C  
ATOM    104  N   ILE A  38      54.466  26.170  29.990  1.00135.79           N  
ANISOU  104  N   ILE A  38    12848  30256   8491  -1958   1776    583       N  
ATOM    105  CA  ILE A  38      53.515  27.286  29.979  1.00139.09           C  
ANISOU  105  CA  ILE A  38    12954  31174   8718  -1317   1923    126       C  
ATOM    106  C   ILE A  38      53.792  28.252  28.821  1.00135.10           C  
ANISOU  106  C   ILE A  38    12747  29914   8669   -863   1729   -225       C  
ATOM    107  O   ILE A  38      52.888  28.569  28.045  1.00135.99           O  
ANISOU  107  O   ILE A  38    12561  30205   8905   -653   1747   -310       O  
ATOM    108  CB  ILE A  38      53.568  28.087  31.293  1.00143.18           C  
ANISOU  108  CB  ILE A  38    13494  32177   8731   -844   2072   -262       C  
ATOM    109  CG1 ILE A  38      53.225  27.186  32.481  1.00148.41           C  
ANISOU  109  CG1 ILE A  38    13805  33769   8815  -1217   2310     47       C  
ATOM    110  CG2 ILE A  38      52.629  29.280  31.229  1.00146.10           C  
ANISOU  110  CG2 ILE A  38    13708  32803   9002    -35   2140   -829       C  
ATOM    111  CD1 ILE A  38      53.485  27.825  33.828  1.00151.39           C  
ANISOU  111  CD1 ILE A  38    13580  34831   9110  -1801   2456    571       C  
ATOM    112  N   VAL A  39      55.045  28.697  28.706  1.00128.09           N  
ANISOU  112  N   VAL A  39    13170  26938   8561   -176   1929   -895       N  
ATOM    113  CA  VAL A  39      55.462  29.645  27.660  1.00124.65           C  
ANISOU  113  CA  VAL A  39    13089  25747   8527    212   1725  -1205       C  
ATOM    114  C   VAL A  39      55.283  29.082  26.241  1.00121.11           C  
ANISOU  114  C   VAL A  39    12587  24902   8528    -26   1606   -969       C  
ATOM    115  O   VAL A  39      54.885  29.811  25.327  1.00120.86           O  
ANISOU  115  O   VAL A  39    12542  24695   8683    355   1536  -1194       O  
ATOM    116  CB  VAL A  39      56.915  30.157  27.893  1.00121.64           C  
ANISOU  116  CB  VAL A  39    13299  24646   8273    257   1531  -1367       C  
ATOM    117  CG1 VAL A  39      57.446  30.906  26.679  1.00116.71           C  
ANISOU  117  CG1 VAL A  39    13031  23153   8162    256   1295  -1383       C  
ATOM    118  CG2 VAL A  39      56.971  31.054  29.119  1.00125.44           C  
ANISOU  118  CG2 VAL A  39    13937  25307   8418    817   1558  -1867       C  
ATOM    119  N   LEU A  40      55.562  27.791  26.066  1.00120.52           N  
ANISOU  119  N   LEU A  40    13059  24277   8455  -1543   1627   -436       N  
ATOM    120  CA  LEU A  40      55.355  27.128  24.778  1.00118.09           C  
ANISOU  120  CA  LEU A  40    12671  23695   8504  -1814   1523   -204       C  
ATOM    121  C   LEU A  40      53.892  27.175  24.342  1.00121.87           C  
ANISOU  121  C   LEU A  40    12615  24838   8851  -1650   1647   -255       C  
ATOM    122  O   LEU A  40      53.584  27.711  23.282  1.00121.38           O  
ANISOU  122  O   LEU A  40    12548  24614   8958  -1241   1576   -504       O  
ATOM    123  CB  LEU A  40      55.858  25.681  24.805  1.00116.80           C  
ANISOU  123  CB  LEU A  40    12561  23386   8431  -2479   1464    270       C  
ATOM    124  CG  LEU A  40      57.356  25.419  24.983  1.00113.33           C  
ANISOU  124  CG  LEU A  40    12605  22316   8139  -2642   1317    364       C  
ATOM    125  CD1 LEU A  40      57.676  23.988  24.591  1.00111.97           C  
ANISOU  125  CD1 LEU A  40    12530  21847   8165  -3197   1195    797       C  
ATOM    126  CD2 LEU A  40      58.213  26.394  24.186  1.00109.47           C  
ANISOU  126  CD2 LEU A  40    12499  21154   7940  -2286   1166     63       C  
ATOM    127  N   LEU A  41      53.000  26.630  25.168  1.00135.51           N  
ANISOU  127  N   LEU A  41    12877  29065   9544  -2766   1967    251       N  
ATOM    128  CA  LEU A  41      51.567  26.590  24.859  1.00139.86           C  
ANISOU  128  CA  LEU A  41    12817  30392   9933  -2689   2095    258       C  
ATOM    129  C   LEU A  41      50.984  27.991  24.654  1.00141.80           C  
ANISOU  129  C   LEU A  41    12943  30824  10112  -1879   2131   -237       C  
ATOM    130  O   LEU A  41      50.216  28.220  23.715  1.00142.47           O  
ANISOU  130  O   LEU A  41    12774  31012  10346  -1697   2073   -295       O  
ATOM    131  CB  LEU A  41      50.788  25.830  25.943  1.00145.35           C  
ANISOU  131  CB  LEU A  41    13013  32046  10167  -3089   2325    553       C  
ATOM    132  CG  LEU A  41      51.199  24.397  26.313  1.00144.57           C  
ANISOU  132  CG  LEU A  41    13063  31770  10098  -3906   2262   1085       C  
ATOM    133  CD1 LEU A  41      50.289  23.852  27.400  1.00150.85           C  
ANISOU  133  CD1 LEU A  41    13272  33577  10468  -4370   2462   1434       C  
ATOM    134  CD2 LEU A  41      51.208  23.459  25.116  1.00140.25           C  
ANISOU  134  CD2 LEU A  41    12812  30432  10044  -4315   1998   1323       C  
ATOM    135  N   ALA A  42      51.370  28.922  25.525  1.00143.51           N  
ANISOU  135  N   ALA A  42    12893  31631  10005    627   2648   -785       N  
ATOM    136  CA  ALA A  42      50.920  30.311  25.438  1.00146.10           C  
ANISOU  136  CA  ALA A  42    13207  32058  10247   1445   2648  -1284       C  
ATOM    137  C   ALA A  42      51.492  31.009  24.215  1.00141.83           C  
ANISOU  137  C   ALA A  42    13117  30608  10165   1694   2382  -1441       C  
ATOM    138  O   ALA A  42      50.800  31.784  23.562  1.00143.64           O  
ANISOU  138  O   ALA A  42    13177  30940  10460   2150   2329  -1635       O  
ATOM    139  CB  ALA A  42      51.291  31.072  26.702  1.00148.51           C  
ANISOU  139  CB  ALA A  42    13748  32467  10213   1854   2728  -1635       C  
ATOM    140  N   GLY A  43      52.758  30.727  23.921  1.00127.73           N  
ANISOU  140  N   GLY A  43    12869  25936   9725   1632   2106  -1750       N  
ATOM    141  CA  GLY A  43      53.437  31.276  22.750  1.00123.40           C  
ANISOU  141  CA  GLY A  43    12766  24508   9613   1735   1856  -1816       C  
ATOM    142  C   GLY A  43      52.892  30.753  21.431  1.00121.70           C  
ANISOU  142  C   GLY A  43    12333  24227   9682   1509   1768  -1578       C  
ATOM    143  O   GLY A  43      52.675  31.526  20.494  1.00121.67           O  
ANISOU  143  O   GLY A  43    12408  23969   9851   1899   1632  -1750       O  
ATOM    144  N   SER A  44      52.675  29.437  21.363  1.00124.15           N  
ANISOU  144  N   SER A  44    11984  25190   9999   -401   1844  -1119       N  
ATOM    145  CA  SER A  44      52.060  28.787  20.202  1.00124.36           C  
ANISOU  145  CA  SER A  44    11669  25412  10172   -675   1795   -889       C  
ATOM    146  C   SER A  44      50.708  29.402  19.884  1.00128.84           C  
ANISOU  146  C   SER A  44    11778  26587  10589   -170   1844  -1101       C  
ATOM    147  O   SER A  44      50.450  29.808  18.756  1.00128.02           O  
ANISOU  147  O   SER A  44    11773  26177  10690    161   1687  -1240       O  
ATOM    148  CB  SER A  44      51.862  27.290  20.454  1.00125.98           C  
ANISOU  148  CB  SER A  44    11538  26097  10230  -1347   1902   -490       C  
ATOM    149  OG  SER A  44      53.086  26.642  20.730  1.00122.12           O  
ANISOU  149  OG  SER A  44    11452  25016   9932  -1843   1804   -236       O  
ATOM    150  N   TYR A  45      49.855  29.476  20.898  1.00146.22           N  
ANISOU  150  N   TYR A  45    11751  32253  11553    247   2448   -958       N  
ATOM    151  CA  TYR A  45      48.493  29.942  20.719  1.00151.31           C  
ANISOU  151  CA  TYR A  45    11842  33635  12014    706   2515  -1126       C  
ATOM    152  C   TYR A  45      48.409  31.458  20.534  1.00152.98           C  
ANISOU  152  C   TYR A  45    12282  33658  12186   1609   2455  -1613       C  
ATOM    153  O   TYR A  45      47.411  31.964  20.026  1.00157.55           O  
ANISOU  153  O   TYR A  45    12447  34796  12618   2134   2481  -1806       O  
ATOM    154  CB  TYR A  45      47.616  29.462  21.881  1.00157.08           C  
ANISOU  154  CB  TYR A  45    11904  35489  12289    512   2791   -991       C  
ATOM    155  CG  TYR A  45      47.265  27.979  21.832  1.00157.04           C  
ANISOU  155  CG  TYR A  45    11612  35761  12295   -410   2819   -471       C  
ATOM    156  CD1 TYR A  45      48.188  27.026  21.357  1.00151.46           C  
ANISOU  156  CD1 TYR A  45    11415  34196  11938  -1028   2638   -179       C  
ATOM    157  CD2 TYR A  45      46.013  27.524  22.280  1.00163.35           C  
ANISOU  157  CD2 TYR A  45    11631  37707  12726   -673   3016   -266       C  
ATOM    158  CE1 TYR A  45      47.870  25.666  21.313  1.00152.07           C  
ANISOU  158  CE1 TYR A  45    11318  34432  12029  -1859   2615    283       C  
ATOM    159  CE2 TYR A  45      45.681  26.164  22.248  1.00164.13           C  
ANISOU  159  CE2 TYR A  45    11509  38029  12823  -1592   3005    243       C  
ATOM    160  CZ  TYR A  45      46.614  25.242  21.763  1.00158.42           C  
ANISOU  160  CZ  TYR A  45    11393  36319  12481  -2174   2785    507       C  
ATOM    161  OH  TYR A  45      46.285  23.901  21.732  1.00159.88           O  
ANISOU  161  OH  TYR A  45    11434  36650  12664  -3059   2731    993       O  
ATOM    162  N   LEU A  46      49.458  32.176  20.930  1.00146.64           N  
ANISOU  162  N   LEU A  46    13000  31108  11607   3986   2304  -2376       N  
ATOM    163  CA  LEU A  46      49.513  33.618  20.710  1.00148.32           C  
ANISOU  163  CA  LEU A  46    13545  30969  11839   4787   2170  -2815       C  
ATOM    164  C   LEU A  46      50.081  33.938  19.329  1.00144.22           C  
ANISOU  164  C   LEU A  46    13437  29609  11751   4778   1890  -2752       C  
ATOM    165  O   LEU A  46      49.642  34.887  18.678  1.00146.51           O  
ANISOU  165  O   LEU A  46    13739  29831  12099   5343   1750  -2955       O  
ATOM    166  CB  LEU A  46      50.320  34.323  21.810  1.00148.61           C  
ANISOU  166  CB  LEU A  46    14075  30670  11719   5047   2182  -3114       C  
ATOM    167  CG  LEU A  46      50.004  35.796  22.112  1.00153.99           C  
ANISOU  167  CG  LEU A  46    14880  31446  12182   5978   2139  -3641       C  
ATOM    168  CD1 LEU A  46      48.630  35.950  22.757  1.00160.42           C  
ANISOU  168  CD1 LEU A  46    15042  33410  12500   6284   2427  -3785       C  
ATOM    169  CD2 LEU A  46      51.074  36.415  22.997  1.00153.09           C  
ANISOU  169  CD2 LEU A  46    15513  30566  12090   6197   1985  -3946       C  
ATOM    170  N   ALA A  47      51.047  33.132  18.889  1.00128.35           N  
ANISOU  170  N   ALA A  47    12250  25422  11094   3226   1428  -2596       N  
ATOM    171  CA  ALA A  47      51.687  33.298  17.577  1.00124.23           C  
ANISOU  171  CA  ALA A  47    12110  24137  10954   3113   1186  -2487       C  
ATOM    172  C   ALA A  47      50.731  33.064  16.407  1.00125.54           C  
ANISOU  172  C   ALA A  47    11920  24561  11219   3204   1092  -2392       C  
ATOM    173  O   ALA A  47      50.826  33.741  15.383  1.00126.15           O  
ANISOU  173  O   ALA A  47    12218  24288  11424   3649    902  -2538       O  
ATOM    174  CB  ALA A  47      52.907  32.389  17.453  1.00118.85           C  
ANISOU  174  CB  ALA A  47    11700  22974  10484   2416   1163  -2183       C  
ATOM    175  N   VAL A  48      49.824  32.100  16.563  1.00135.36           N  
ANISOU  175  N   VAL A  48    11137  28276  12018   1794   1260  -2107       N  
ATOM    176  CA  VAL A  48      48.813  31.808  15.550  1.00137.95           C  
ANISOU  176  CA  VAL A  48    10991  29066  12356   1865   1190  -2030       C  
ATOM    177  C   VAL A  48      47.961  33.044  15.280  1.00142.54           C  
ANISOU  177  C   VAL A  48    11457  29887  12814   2723   1129  -2364       C  
ATOM    178  O   VAL A  48      47.923  33.510  14.147  1.00141.74           O  
ANISOU  178  O   VAL A  48    11623  29322  12908   3010    905  -2420       O  
ATOM    179  CB  VAL A  48      47.942  30.577  15.916  1.00140.68           C  
ANISOU  179  CB  VAL A  48    10680  30265  12508   1366   1355  -1777       C  
ATOM    180  CG1 VAL A  48      46.689  30.517  15.067  1.00144.46           C  
ANISOU  180  CG1 VAL A  48    10611  31334  12945   1518   1278  -1747       C  
ATOM    181  CG2 VAL A  48      48.733  29.303  15.736  1.00136.50           C  
ANISOU  181  CG2 VAL A  48    10348  29355  12162    557   1318  -1437       C  
ATOM    182  N   LEU A  49      47.320  33.596  16.313  1.00159.70           N  
ANISOU  182  N   LEU A  49    12338  34842  13499   5672   1539  -2728       N  
ATOM    183  CA  LEU A  49      46.433  34.756  16.127  1.00164.96           C  
ANISOU  183  CA  LEU A  49    12865  35774  14037   6570   1455  -3067       C  
ATOM    184  C   LEU A  49      47.170  36.011  15.646  1.00163.67           C  
ANISOU  184  C   LEU A  49    13466  34648  14074   7103   1201  -3319       C  
ATOM    185  O   LEU A  49      46.549  36.938  15.122  1.00167.73           O  
ANISOU  185  O   LEU A  49    13990  35186  14554   7838   1049  -3560       O  
ATOM    186  CB  LEU A  49      45.579  35.042  17.378  1.00171.44           C  
ANISOU  186  CB  LEU A  49    13141  37581  14418   7022   1710  -3307       C  
ATOM    187  CG  LEU A  49      46.025  35.922  18.555  1.00174.52           C  
ANISOU  187  CG  LEU A  49    13820  37938  14552   7653   1799  -3730       C  
ATOM    188  CD1 LEU A  49      46.829  37.145  18.114  1.00175.38           C  
ANISOU  188  CD1 LEU A  49    14602  37229  14807   8423   1521  -4097       C  
ATOM    189  CD2 LEU A  49      44.797  36.366  19.344  1.00181.96           C  
ANISOU  189  CD2 LEU A  49    13980  40138  15020   8072   2067  -3905       C  
ATOM    190  N   ALA A  50      48.489  36.026  15.822  1.00148.81           N  
ANISOU  190  N   ALA A  50    14471  29096  12974   7377    407  -3680       N  
ATOM    191  CA  ALA A  50      49.326  37.132  15.371  1.00147.68           C  
ANISOU  191  CA  ALA A  50    15075  28016  13019   7727    155  -3858       C  
ATOM    192  C   ALA A  50      49.625  37.042  13.880  1.00144.85           C  
ANISOU  192  C   ALA A  50    14936  27139  12962   7564    -87  -3635       C  
ATOM    193  O   ALA A  50      49.733  38.066  13.204  1.00146.66           O  
ANISOU  193  O   ALA A  50    15548  26893  13283   8064   -333  -3772       O  
ATOM    194  CB  ALA A  50      50.625  37.169  16.165  1.00143.90           C  
ANISOU  194  CB  ALA A  50    15132  26946  12596   7349    187  -3862       C  
ATOM    195  N   GLU A  51      49.735  35.809  13.384  1.00134.80           N  
ANISOU  195  N   GLU A  51    12769  25916  12532   5529   -103  -3318       N  
ATOM    196  CA  GLU A  51      50.251  35.511  12.044  1.00130.87           C  
ANISOU  196  CA  GLU A  51    12522  24897  12305   5163   -285  -3064       C  
ATOM    197  C   GLU A  51      49.186  35.087  11.034  1.00132.54           C  
ANISOU  197  C   GLU A  51    12236  25604  12521   5133   -356  -2915       C  
ATOM    198  O   GLU A  51      49.342  35.318   9.835  1.00131.77           O  
ANISOU  198  O   GLU A  51    12351  25141  12574   5198   -575  -2825       O  
ATOM    199  CB  GLU A  51      51.293  34.397  12.137  1.00125.55           C  
ANISOU  199  CB  GLU A  51    11991  23961  11751   4399   -179  -2821       C  
ATOM    200  CG  GLU A  51      52.617  34.809  12.758  1.00122.90           C  
ANISOU  200  CG  GLU A  51    12228  22988  11479   4306   -179  -2896       C  
ATOM    201  CD  GLU A  51      53.682  35.149  11.724  1.00119.01           C  
ANISOU  201  CD  GLU A  51    12251  21733  11233   4048   -359  -2741       C  
ATOM    202  OE1 GLU A  51      53.973  34.308  10.836  1.00115.72           O  
ANISOU  202  OE1 GLU A  51    11768  21259  10940   3556   -352  -2496       O  
ATOM    203  OE2 GLU A  51      54.245  36.256  11.817  1.00119.74           O  
ANISOU  203  OE2 GLU A  51    12826  21295  11374   4333   -512  -2870       O  
ATOM    204  N   ARG A  52      48.114  34.470  11.527  1.00150.36           N  
ANISOU  204  N   ARG A  52    11574  31573  13982   3877   -185  -3397       N  
ATOM    205  CA  ARG A  52      47.119  33.776  10.701  1.00152.49           C  
ANISOU  205  CA  ARG A  52    11282  32432  14226   3737   -248  -3238       C  
ATOM    206  C   ARG A  52      46.603  34.557   9.491  1.00154.47           C  
ANISOU  206  C   ARG A  52    11605  32527  14558   4219   -522  -3283       C  
ATOM    207  O   ARG A  52      46.435  33.988   8.407  1.00153.63           O  
ANISOU  207  O   ARG A  52    11353  32476  14543   3905   -662  -3083       O  
ATOM    208  CB  ARG A  52      45.941  33.339  11.570  1.00157.70           C  
ANISOU  208  CB  ARG A  52    11187  34140  14593   3851    -46  -3291       C  
ATOM    209  CG  ARG A  52      45.291  32.033  11.158  1.00159.27           C  
ANISOU  209  CG  ARG A  52    10790  34963  14764   3395    -77  -3045       C  
ATOM    210  CD  ARG A  52      44.395  31.540  12.282  1.00160.28           C  
ANISOU  210  CD  ARG A  52    10463  35722  14714   2795    171  -2870       C  
ATOM    211  NE  ARG A  52      43.616  30.357  11.926  1.00162.96           N  
ANISOU  211  NE  ARG A  52    10187  36735  14996   2311    122  -2627       N  
ATOM    212  CZ  ARG A  52      42.807  29.709  12.763  1.00167.15           C  
ANISOU  212  CZ  ARG A  52    10046  38187  15275   1953    306  -2482       C  
ATOM    213  NH1 ARG A  52      42.660  30.119  14.020  1.00169.27           N  
ANISOU  213  NH1 ARG A  52    10132  38893  15289   2049    584  -2556       N  
ATOM    214  NH2 ARG A  52      42.141  28.644  12.340  1.00169.66           N  
ANISOU  214  NH2 ARG A  52     9870  39019  15575   1460    195  -2249       N  
ATOM    215  N   GLY A  53      46.357  35.852   9.674  1.00165.25           N  
ANISOU  215  N   GLY A  53    12961  35157  14669   7927  -1140  -3714       N  
ATOM    216  CA  GLY A  53      45.746  36.673   8.622  1.00168.41           C  
ANISOU  216  CA  GLY A  53    13398  35482  15107   8487  -1423  -3756       C  
ATOM    217  C   GLY A  53      46.713  37.414   7.714  1.00165.76           C  
ANISOU  217  C   GLY A  53    13805  34185  14991   8544  -1697  -3678       C  
ATOM    218  O   GLY A  53      46.303  38.303   6.962  1.00169.17           O  
ANISOU  218  O   GLY A  53    14334  34515  15427   9097  -1954  -3721       O  
ATOM    219  N   ALA A  54      47.990  37.046   7.778  1.00147.76           N  
ANISOU  219  N   ALA A  54    14198  28246  13698   8285  -1884  -3169       N  
ATOM    220  CA  ALA A  54      49.032  37.738   7.035  1.00145.85           C  
ANISOU  220  CA  ALA A  54    14663  27133  13621   8322  -2113  -3093       C  
ATOM    221  C   ALA A  54      49.538  36.873   5.887  1.00141.48           C  
ANISOU  221  C   ALA A  54    14168  26397  13192   7670  -2149  -2801       C  
ATOM    222  O   ALA A  54      49.287  35.669   5.874  1.00140.17           O  
ANISOU  222  O   ALA A  54    13544  26717  12999   7227  -2016  -2694       O  
ATOM    223  CB  ALA A  54      50.176  38.113   7.967  1.00144.06           C  
ANISOU  223  CB  ALA A  54    15000  26294  13444   8293  -2058  -3212       C  
ATOM    224  N   PRO A  55      50.217  37.491   4.898  1.00136.04           N  
ANISOU  224  N   PRO A  55    14531  24262  12895   7416  -2270  -2032       N  
ATOM    225  CA  PRO A  55      50.955  36.793   3.833  1.00131.64           C  
ANISOU  225  CA  PRO A  55    14279  23292  12446   6838  -2299  -1791       C  
ATOM    226  C   PRO A  55      52.216  36.044   4.311  1.00126.69           C  
ANISOU  226  C   PRO A  55    13717  22532  11889   6204  -2068  -1722       C  
ATOM    227  O   PRO A  55      53.316  36.338   3.847  1.00123.92           O  
ANISOU  227  O   PRO A  55    13784  21683  11616   5915  -2095  -1597       O  
ATOM    228  CB  PRO A  55      51.343  37.936   2.876  1.00132.64           C  
ANISOU  228  CB  PRO A  55    15068  22699  12629   7088  -2522  -1746       C  
ATOM    229  CG  PRO A  55      50.424  39.075   3.222  1.00138.32           C  
ANISOU  229  CG  PRO A  55    15729  23554  13272   7835  -2736  -1882       C  
ATOM    230  CD  PRO A  55      50.246  38.952   4.693  1.00140.40           C  
ANISOU  230  CD  PRO A  55    15427  24487  13432   8096  -2542  -2122       C  
ATOM    231  N   GLY A  56      52.055  35.066   5.203  1.00117.64           N  
ANISOU  231  N   GLY A  56    12473  20779  11446   4344  -1540  -1848       N  
ATOM    232  CA  GLY A  56      53.206  34.398   5.812  1.00113.53           C  
ANISOU  232  CA  GLY A  56    12085  20063  10990   3829  -1360  -1785       C  
ATOM    233  C   GLY A  56      53.069  32.937   6.189  1.00112.19           C  
ANISOU  233  C   GLY A  56    11519  20316  10793   3389  -1176  -1731       C  
ATOM    234  O   GLY A  56      51.962  32.408   6.306  1.00114.86           O  
ANISOU  234  O   GLY A  56    11370  21248  11023   3450  -1108  -1773       O  
ATOM    235  N   ALA A  57      54.231  32.317   6.416  1.00107.20           N  
ANISOU  235  N   ALA A  57    11906  18583  10244   1976   -920  -1893       N  
ATOM    236  CA  ALA A  57      54.405  30.871   6.691  1.00105.22           C  
ANISOU  236  CA  ALA A  57    11483  18489  10006   1476   -776  -1801       C  
ATOM    237  C   ALA A  57      53.446  30.245   7.721  1.00107.39           C  
ANISOU  237  C   ALA A  57    11316  19324  10163   1411   -629  -1829       C  
ATOM    238  O   ALA A  57      52.802  30.951   8.511  1.00109.70           O  
ANISOU  238  O   ALA A  57    11481  19853  10347   1760   -550  -1971       O  
ATOM    239  CB  ALA A  57      55.892  30.549   7.041  1.00101.42           C  
ANISOU  239  CB  ALA A  57    11404  17512   9618   1194   -703  -1746       C  
ATOM    240  N   GLN A  58      53.403  28.914   7.716  1.00112.73           N  
ANISOU  240  N   GLN A  58    11979  19927  10927   -617  -1052  -2163       N  
ATOM    241  CA  GLN A  58      52.283  28.136   8.262  1.00115.82           C  
ANISOU  241  CA  GLN A  58    11862  20951  11195   -806   -986  -2103       C  
ATOM    242  C   GLN A  58      52.002  28.275   9.764  1.00118.07           C  
ANISOU  242  C   GLN A  58    11883  21665  11312   -653   -790  -2175       C  
ATOM    243  O   GLN A  58      51.360  27.402  10.359  1.00120.94           O  
ANISOU  243  O   GLN A  58    11797  22616  11539   -891   -707  -2081       O  
ATOM    244  CB  GLN A  58      52.424  26.653   7.878  1.00114.72           C  
ANISOU  244  CB  GLN A  58    11733  20739  11116  -1423  -1018  -1917       C  
ATOM    245  CG  GLN A  58      51.102  25.977   7.516  1.00117.62           C  
ANISOU  245  CG  GLN A  58    11739  21508  11443  -1688  -1156  -1825       C  
ATOM    246  CD  GLN A  58      51.072  24.497   7.847  1.00118.42           C  
ANISOU  246  CD  GLN A  58    11756  21699  11538  -2317  -1159  -1636       C  
ATOM    247  OE1 GLN A  58      50.941  23.653   6.957  1.00118.78           O  
ANISOU  247  OE1 GLN A  58    11873  21612  11645  -2676  -1337  -1559       O  
ATOM    248  NE2 GLN A  58      51.184  24.174   9.133  1.00119.15           N  
ANISOU  248  NE2 GLN A  58    11732  22000  11538  -2466   -981  -1557       N  
ATOM    249  N   LEU A  59      52.460  29.371  10.369  1.00110.23           N  
ANISOU  249  N   LEU A  59    10443  20687  10754     20   -254  -1696       N  
ATOM    250  CA  LEU A  59      52.060  29.709  11.735  1.00112.81           C  
ANISOU  250  CA  LEU A  59    10555  21426  10880    242    -76  -1817       C  
ATOM    251  C   LEU A  59      50.601  30.162  11.698  1.00117.67           C  
ANISOU  251  C   LEU A  59    10667  22710  11334    630    -76  -1923       C  
ATOM    252  O   LEU A  59      50.245  31.259  12.132  1.00120.29           O  
ANISOU  252  O   LEU A  59    10994  23148  11564   1230    -74  -2160       O  
ATOM    253  CB  LEU A  59      52.984  30.770  12.347  1.00111.37           C  
ANISOU  253  CB  LEU A  59    10829  20774  10714    560    -58  -2002       C  
ATOM    254  CG  LEU A  59      54.429  30.369  12.674  1.00107.15           C  
ANISOU  254  CG  LEU A  59    10711  19697  10305    181    -44  -1894       C  
ATOM    255  CD1 LEU A  59      55.105  31.452  13.496  1.00106.90           C  
ANISOU  255  CD1 LEU A  59    11042  19341  10235    468    -32  -2087       C  
ATOM    256  CD2 LEU A  59      54.492  29.036  13.399  1.00106.65           C  
ANISOU  256  CD2 LEU A  59    10451  19888  10184   -333     77  -1691       C  
ATOM    257  N   ILE A  60      49.771  29.278  11.159  1.00132.91           N  
ANISOU  257  N   ILE A  60    10685  27145  12668   -563   -573  -1384       N  
ATOM    258  CA  ILE A  60      48.390  29.573  10.849  1.00137.24           C  
ANISOU  258  CA  ILE A  60    10725  28311  13109   -315   -636  -1418       C  
ATOM    259  C   ILE A  60      47.479  28.483  11.413  1.00140.15           C  
ANISOU  259  C   ILE A  60    10523  29401  13328   -854   -539  -1205       C  
ATOM    260  O   ILE A  60      46.258  28.639  11.442  1.00144.93           O  
ANISOU  260  O   ILE A  60    10542  30764  13760   -693   -524  -1220       O  
ATOM    261  CB  ILE A  60      48.178  29.762   9.316  1.00136.16           C  
ANISOU  261  CB  ILE A  60    10763  27825  13146   -223   -898  -1395       C  
ATOM    262  CG1 ILE A  60      48.470  28.469   8.544  1.00134.19           C  
ANISOU  262  CG1 ILE A  60    10535  27437  13013   -910  -1005  -1161       C  
ATOM    263  CG2 ILE A  60      49.036  30.922   8.787  1.00133.18           C  
ANISOU  263  CG2 ILE A  60    11023  26659  12919    166  -1007  -1529       C  
ATOM    264  CD1 ILE A  60      47.874  28.432   7.142  1.00135.46           C  
ANISOU  264  CD1 ILE A  60    10584  27661  13224   -864  -1247  -1129       C  
ATOM    265  N   THR A  61      48.085  27.381  11.852  1.00145.06           N  
ANISOU  265  N   THR A  61    11289  29326  14503  -2945   -479   -971       N  
ATOM    266  CA  THR A  61      47.392  26.368  12.651  1.00148.51           C  
ANISOU  266  CA  THR A  61    11248  30440  14739  -3441   -341   -760       C  
ATOM    267  C   THR A  61      48.122  26.153  13.974  1.00147.73           C  
ANISOU  267  C   THR A  61    11307  30311  14512  -3498   -127   -752       C  
ATOM    268  O   THR A  61      49.339  26.357  14.055  1.00143.46           O  
ANISOU  268  O   THR A  61    11325  29066  14116  -3406   -137   -827       O  
ATOM    269  CB  THR A  61      47.255  25.020  11.913  1.00148.22           C  
ANISOU  269  CB  THR A  61    11217  30292  14808  -4226   -486   -464       C  
ATOM    270  OG1 THR A  61      48.499  24.672  11.300  1.00143.85           O  
ANISOU  270  OG1 THR A  61    11206  28927  14525  -4272   -688   -493       O  
ATOM    271  CG2 THR A  61      46.183  25.100  10.850  1.00153.27           C  
ANISOU  271  CG2 THR A  61    11222  31692  15322  -4431   -563   -357       C  
ATOM    272  N   TYR A  62      47.379  25.752  15.007  1.00144.70           N  
ANISOU  272  N   TYR A  62    10695  29475  14808  -2323   1085   -290       N  
ATOM    273  CA  TYR A  62      47.962  25.479  16.328  1.00144.71           C  
ANISOU  273  CA  TYR A  62    10796  29554  14632  -2485   1286   -222       C  
ATOM    274  C   TYR A  62      48.950  24.298  16.334  1.00141.11           C  
ANISOU  274  C   TYR A  62    10802  28453  14362  -3154   1190     62       C  
ATOM    275  O   TYR A  62      50.087  24.466  16.788  1.00137.44           O  
ANISOU  275  O   TYR A  62    10832  27405  13985  -3049   1206     -8       O  
ATOM    276  CB  TYR A  62      46.882  25.292  17.411  1.00151.02           C  
ANISOU  276  CB  TYR A  62    10898  31460  15023  -2574   1521   -130       C  
ATOM    277  CG  TYR A  62      46.018  26.510  17.675  1.00155.20           C  
ANISOU  277  CG  TYR A  62    10997  32668  15304  -1776   1658   -469       C  
ATOM    278  CD1 TYR A  62      46.565  27.681  18.201  1.00153.95           C  
ANISOU  278  CD1 TYR A  62    11188  32200  15105  -1073   1723   -835       C  
ATOM    279  CD2 TYR A  62      44.645  26.481  17.418  1.00161.07           C  
ANISOU  279  CD2 TYR A  62    10978  34386  15835  -1719   1706   -433       C  
ATOM    280  CE1 TYR A  62      45.769  28.801  18.446  1.00158.47           C  
ANISOU  280  CE1 TYR A  62    11426  33346  15441   -272   1817  -1184       C  
ATOM    281  CE2 TYR A  62      43.840  27.594  17.664  1.00165.59           C  
ANISOU  281  CE2 TYR A  62    11138  35616  16161   -900   1824   -771       C  
ATOM    282  CZ  TYR A  62      44.409  28.748  18.178  1.00164.30           C  
ANISOU  282  CZ  TYR A  62    11397  35062  15968   -155   1876  -1157       C  
ATOM    283  OH  TYR A  62      43.619  29.849  18.423  1.00169.30           O  
ANISOU  283  OH  TYR A  62    11696  36275  16356    714   1962  -1524       O  
ATOM    284  N   PRO A  63      48.535  23.110  15.822  1.00145.79           N  
ANISOU  284  N   PRO A  63    12743  27613  15039  -4997   1005   -183       N  
ATOM    285  CA  PRO A  63      49.417  21.928  15.843  1.00143.46           C  
ANISOU  285  CA  PRO A  63    12902  26707  14899  -5603    886     84       C  
ATOM    286  C   PRO A  63      50.761  22.120  15.129  1.00137.60           C  
ANISOU  286  C   PRO A  63    12840  24970  14471  -5428    737    -44       C  
ATOM    287  O   PRO A  63      51.625  21.242  15.187  1.00135.97           O  
ANISOU  287  O   PRO A  63    13018  24238  14408  -5849    607    142       O  
ATOM    288  CB  PRO A  63      48.587  20.859  15.125  1.00146.57           C  
ANISOU  288  CB  PRO A  63    13053  27308  15330  -6230    705    343       C  
ATOM    289  CG  PRO A  63      47.181  21.297  15.304  1.00151.84           C  
ANISOU  289  CG  PRO A  63    12970  28991  15733  -6106    832    321       C  
ATOM    290  CD  PRO A  63      47.233  22.785  15.208  1.00150.21           C  
ANISOU  290  CD  PRO A  63    12733  28819  15520  -5231    930    -72       C  
ATOM    291  N   ARG A  64      50.925  23.261  14.467  1.00121.56           N  
ANISOU  291  N   ARG A  64    11641  22383  12165  -3156    292   -626       N  
ATOM    292  CA  ARG A  64      52.166  23.598  13.788  1.00116.69           C  
ANISOU  292  CA  ARG A  64    11586  20941  11809  -2998    164   -735       C  
ATOM    293  C   ARG A  64      52.914  24.648  14.582  1.00115.09           C  
ANISOU  293  C   ARG A  64    11553  20628  11549  -2498    294   -958       C  
ATOM    294  O   ARG A  64      54.141  24.713  14.532  1.00111.60           O  
ANISOU  294  O   ARG A  64    11550  19614  11239  -2442    259   -998       O  
ATOM    295  CB  ARG A  64      51.884  24.112  12.374  1.00115.80           C  
ANISOU  295  CB  ARG A  64    11499  20644  11857  -2801     -6   -859       C  
ATOM    296  N   ALA A  65      52.166  25.473  15.306  1.00110.87           N  
ANISOU  296  N   ALA A  65    10430  21056  10638  -1364    603   -513       N  
ATOM    297  CA  ALA A  65      52.756  26.470  16.188  1.00110.53           C  
ANISOU  297  CA  ALA A  65    10545  20980  10472   -952    731   -723       C  
ATOM    298  C   ALA A  65      53.423  25.824  17.412  1.00110.14           C  
ANISOU  298  C   ALA A  65    10632  20916  10299  -1284    839   -563       C  
ATOM    299  O   ALA A  65      54.440  26.326  17.902  1.00107.71           O  
ANISOU  299  O   ALA A  65    10700  20195  10029  -1105    841   -684       O  
ATOM    300  CB  ALA A  65      51.719  27.482  16.612  1.00114.72           C  
ANISOU  300  CB  ALA A  65    10675  22152  10763   -445    849   -949       C  
ATOM    301  N   LEU A  66      52.851  24.714  17.891  1.00115.48           N  
ANISOU  301  N   LEU A  66    12112  21071  10694  -2042   1444   -114       N  
ATOM    302  CA  LEU A  66      53.444  23.924  18.980  1.00115.27           C  
ANISOU  302  CA  LEU A  66    12269  20958  10570  -2429   1493    114       C  
ATOM    303  C   LEU A  66      54.807  23.384  18.568  1.00110.66           C  
ANISOU  303  C   LEU A  66    12241  19530  10274  -2552   1326    167       C  
ATOM    304  O   LEU A  66      55.778  23.469  19.325  1.00108.64           O  
ANISOU  304  O   LEU A  66    12287  18980  10013  -2394   1347     85       O  
ATOM    305  CB  LEU A  66      52.508  22.783  19.385  1.00119.04           C  
ANISOU  305  CB  LEU A  66    12435  21903  10892  -3051   1518    486       C  
ATOM    306  CG  LEU A  66      51.122  23.190  19.889  1.00124.57           C  
ANISOU  306  CG  LEU A  66    12478  23587  11267  -3062   1693    516       C  
ATOM    307  CD1 LEU A  66      50.301  21.963  20.254  1.00128.28           C  
ANISOU  307  CD1 LEU A  66    12726  24409  11607  -3824   1676    961       C  
ATOM    308  CD2 LEU A  66      51.236  24.131  21.078  1.00126.95           C  
ANISOU  308  CD2 LEU A  66    12561  24447  11226  -2581   1936    279       C  
ATOM    309  N   TRP A  67      54.869  22.841  17.358  1.00107.48           N  
ANISOU  309  N   TRP A  67    12484  18466   9887  -2111    508    316       N  
ATOM    310  CA  TRP A  67      56.109  22.341  16.791  1.00103.69           C  
ANISOU  310  CA  TRP A  67    12485  17247   9664  -2167    351    336       C  
ATOM    311  C   TRP A  67      57.113  23.467  16.577  1.00100.43           C  
ANISOU  311  C   TRP A  67    12335  16480   9344  -1700    364     72       C  
ATOM    312  O   TRP A  67      58.311  23.250  16.716  1.00 97.97           O  
ANISOU  312  O   TRP A  67    12361  15723   9141  -1718    302     95       O  
ATOM    313  CB  TRP A  67      55.826  21.584  15.488  1.00103.30           C  
ANISOU  313  CB  TRP A  67    12495  16935   9819  -2377    166    395       C  
ATOM    314  CG  TRP A  67      57.028  21.319  14.624  1.00 99.80           C  
ANISOU  314  CG  TRP A  67    12496  15807   9615  -2314     18    341       C  
ATOM    315  CD1 TRP A  67      57.267  21.829  13.378  1.00 97.57           C  
ANISOU  315  CD1 TRP A  67    12341  15240   9490  -2055    -64    158       C  
ATOM    316  CD2 TRP A  67      58.152  20.487  14.938  1.00 98.58           C  
ANISOU  316  CD2 TRP A  67    12701  15214   9542  -2477    -62    469       C  
ATOM    317  NE1 TRP A  67      58.465  21.365  12.893  1.00 95.12           N  
ANISOU  317  NE1 TRP A  67    12416  14391   9335  -2055   -166    156       N  
ATOM    318  CE2 TRP A  67      59.032  20.540  13.830  1.00 95.69           C  
ANISOU  318  CE2 TRP A  67    12634  14349   9375  -2282   -173    332       C  
ATOM    319  CE3 TRP A  67      58.503  19.700  16.044  1.00100.04           C  
ANISOU  319  CE3 TRP A  67    12983  15396   9632  -2751    -60    697       C  
ATOM    320  CZ2 TRP A  67      60.242  19.837  13.797  1.00 94.35           C  
ANISOU  320  CZ2 TRP A  67    12819  13719   9312  -2305   -271    386       C  
ATOM    321  CZ3 TRP A  67      59.708  19.001  16.010  1.00 98.63           C  
ANISOU  321  CZ3 TRP A  67    13196  14699   9581  -2777   -187    769       C  
ATOM    322  CH2 TRP A  67      60.563  19.077  14.892  1.00 95.85           C  
ANISOU  322  CH2 TRP A  67    13102  13888   9428  -2530   -286    597       C  
ATOM    323  N   TRP A  68      56.625  24.665  16.252  1.00 95.01           N  
ANISOU  323  N   TRP A  68    10994  16682   8423   -903     48     23       N  
ATOM    324  CA  TRP A  68      57.506  25.817  16.050  1.00 92.55           C  
ANISOU  324  CA  TRP A  68    10971  15989   8203   -508     19   -211       C  
ATOM    325  C   TRP A  68      58.133  26.263  17.350  1.00 92.69           C  
ANISOU  325  C   TRP A  68    11112  16037   8069   -398    108   -288       C  
ATOM    326  O   TRP A  68      59.303  26.644  17.374  1.00 90.20           O  
ANISOU  326  O   TRP A  68    11124  15288   7860   -354     43   -332       O  
ATOM    327  CB  TRP A  68      56.773  27.004  15.429  1.00 93.73           C  
ANISOU  327  CB  TRP A  68    10994  16282   8336    -76     13   -442       C  
ATOM    328  CG  TRP A  68      57.561  28.294  15.534  1.00 92.37           C  
ANISOU  328  CG  TRP A  68    11152  15741   8205    301    -24   -672       C  
ATOM    329  CD1 TRP A  68      58.700  28.617  14.851  1.00 89.37           C  
ANISOU  329  CD1 TRP A  68    11138  14799   8020    307   -142   -685       C  
ATOM    330  CD2 TRP A  68      57.274  29.413  16.384  1.00 94.66           C  
ANISOU  330  CD2 TRP A  68    11438  16210   8317    701     39   -917       C  
ATOM    331  NE1 TRP A  68      59.135  29.871  15.216  1.00 89.71           N  
ANISOU  331  NE1 TRP A  68    11414  14642   8031    622   -174   -891       N  
ATOM    332  CE2 TRP A  68      58.278  30.383  16.152  1.00 92.92           C  
ANISOU  332  CE2 TRP A  68    11636  15452   8219    889    -79  -1058       C  
ATOM    333  CE3 TRP A  68      56.263  29.693  17.310  1.00 98.50           C  
ANISOU  333  CE3 TRP A  68    11612  17279   8533    921    177  -1042       C  
ATOM    334  CZ2 TRP A  68      58.300  31.611  16.812  1.00 94.93           C  
ANISOU  334  CZ2 TRP A  68    12065  15650   8354   1272    -97  -1324       C  
ATOM    335  CZ3 TRP A  68      56.284  30.916  17.965  1.00100.44           C  
ANISOU  335  CZ3 TRP A  68    12010  17509   8645   1376    182  -1342       C  
ATOM    336  CH2 TRP A  68      57.297  31.860  17.711  1.00 98.66           C  
ANISOU  336  CH2 TRP A  68    12266  16654   8568   1544     27  -1487       C  
ATOM    337  N   SER A  69      57.339  26.235  18.417  1.00 95.42           N  
ANISOU  337  N   SER A  69    11463  16737   8056   -451    395    -20       N  
ATOM    338  CA  SER A  69      57.800  26.594  19.754  1.00 96.34           C  
ANISOU  338  CA  SER A  69    11666  16984   7954   -392    487    -80       C  
ATOM    339  C   SER A  69      58.991  25.736  20.164  1.00 94.28           C  
ANISOU  339  C   SER A  69    11661  16392   7769   -739    419    147       C  
ATOM    340  O   SER A  69      60.045  26.263  20.521  1.00 92.59           O  
ANISOU  340  O   SER A  69    11730  15863   7586   -632    367     49       O  
ATOM    341  CB  SER A  69      56.661  26.452  20.759  1.00100.66           C  
ANISOU  341  CB  SER A  69    11819  18273   8154   -430    669    -38       C  
ATOM    342  OG  SER A  69      55.569  27.275  20.388  1.00103.20           O  
ANISOU  342  OG  SER A  69    11745  19040   8427   -345    722    -59       O  
ATOM    343  N   VAL A  70      58.822  24.419  20.078  1.00 95.94           N  
ANISOU  343  N   VAL A  70    12038  16530   7884  -1127    117    521       N  
ATOM    344  CA  VAL A  70      59.886  23.480  20.414  1.00 94.70           C  
ANISOU  344  CA  VAL A  70    12143  16054   7786  -1406     27    744       C  
ATOM    345  C   VAL A  70      61.113  23.723  19.537  1.00 91.01           C  
ANISOU  345  C   VAL A  70    12010  14996   7575  -1240   -103    628       C  
ATOM    346  O   VAL A  70      62.228  23.780  20.034  1.00 90.10           O  
ANISOU  346  O   VAL A  70    12078  14734   7422  -1155   -125    578       O  
ATOM    347  CB  VAL A  70      59.421  22.015  20.294  1.00 95.98           C  
ANISOU  347  CB  VAL A  70    12272  16192   8004  -1854    -51   1072       C  
ATOM    348  CG1 VAL A  70      60.521  21.066  20.753  1.00 95.27           C  
ANISOU  348  CG1 VAL A  70    12499  15735   7964  -2057   -171   1291       C  
ATOM    349  CG2 VAL A  70      58.155  21.794  21.105  1.00100.21           C  
ANISOU  349  CG2 VAL A  70    12417  17395   8265  -2081     85   1219       C  
ATOM    350  N   GLU A  71      60.889  23.887  18.236  1.00 86.95           N  
ANISOU  350  N   GLU A  71    11048  14559   7429   -983   -532    542       N  
ATOM    351  CA  GLU A  71      61.951  24.212  17.273  1.00 83.92           C  
ANISOU  351  CA  GLU A  71    10924  13700   7262   -825   -635    432       C  
ATOM    352  C   GLU A  71      62.736  25.465  17.710  1.00 83.20           C  
ANISOU  352  C   GLU A  71    10944  13552   7117   -548   -610    212       C  
ATOM    353  O   GLU A  71      63.965  25.509  17.606  1.00 81.76           O  
ANISOU  353  O   GLU A  71    10961  13114   6991   -551   -675    218       O  
ATOM    354  CB  GLU A  71      61.340  24.405  15.878  1.00 83.11           C  
ANISOU  354  CB  GLU A  71    10786  13470   7323   -763   -693    369       C  
ATOM    355  CG  GLU A  71      62.299  24.318  14.703  1.00 80.76           C  
ANISOU  355  CG  GLU A  71    10719  12739   7228   -749   -807    367       C  
ATOM    356  CD  GLU A  71      61.559  24.341  13.350  1.00 80.65           C  
ANISOU  356  CD  GLU A  71    10641  12687   7314   -702   -864    307       C  
ATOM    357  OE1 GLU A  71      60.642  23.498  13.168  1.00 82.68           O  
ANISOU  357  OE1 GLU A  71    10662  13246   7506   -809   -848    350       O  
ATOM    358  OE2 GLU A  71      61.883  25.195  12.471  1.00 78.98           O  
ANISOU  358  OE2 GLU A  71    10581  12211   7218   -572   -927    227       O  
ATOM    359  N   THR A  72      62.019  26.453  18.242  1.00 84.00           N  
ANISOU  359  N   THR A  72    10991  13995   6931   -465   -418    103       N  
ATOM    360  CA  THR A  72      62.592  27.753  18.565  1.00 83.99           C  
ANISOU  360  CA  THR A  72    11166  13862   6883   -214   -441   -125       C  
ATOM    361  C   THR A  72      63.195  27.818  19.964  1.00 84.89           C  
ANISOU  361  C   THR A  72    11359  14085   6811   -273   -419   -132       C  
ATOM    362  O   THR A  72      64.252  28.431  20.148  1.00 84.13           O  
ANISOU  362  O   THR A  72    11490  13731   6743   -222   -506   -234       O  
ATOM    363  CB  THR A  72      61.540  28.862  18.498  1.00 86.22           C  
ANISOU  363  CB  THR A  72    11350  14352   7059    124   -397   -362       C  
ATOM    364  OG1 THR A  72      60.992  28.925  17.176  1.00 85.39           O  
ANISOU  364  OG1 THR A  72    11257  14055   7134    251   -469   -396       O  
ATOM    365  CG2 THR A  72      62.162  30.207  18.839  1.00 87.40           C  
ANISOU  365  CG2 THR A  72    11743  14376   7090    365   -440   -619       C  
ATOM    366  N   ALA A  73      62.516  27.205  20.938  1.00 87.94           N  
ANISOU  366  N   ALA A  73    11734  14805   6875   -419   -332     40       N  
ATOM    367  CA  ALA A  73      62.958  27.206  22.343  1.00 89.77           C  
ANISOU  367  CA  ALA A  73    11983  15286   6838   -460   -285     37       C  
ATOM    368  C   ALA A  73      64.243  26.402  22.536  1.00 88.25           C  
ANISOU  368  C   ALA A  73    11969  14850   6712   -686   -392    232       C  
ATOM    369  O   ALA A  73      65.066  26.713  23.395  1.00 89.33           O  
ANISOU  369  O   ALA A  73    12184  15093   6663   -706   -410    214       O  
ATOM    370  CB  ALA A  73      61.859  26.673  23.249  1.00 92.83           C  
ANISOU  370  CB  ALA A  73    12072  16237   6963   -581   -133    171       C  
ATOM    371  N   THR A  74      64.395  25.364  21.725  1.00 86.49           N  
ANISOU  371  N   THR A  74    11651  14473   6740   -762   -704    419       N  
ATOM    372  CA  THR A  74      65.607  24.562  21.670  1.00 85.52           C  
ANISOU  372  CA  THR A  74    11665  14136   6692   -912   -815    607       C  
ATOM    373  C   THR A  74      66.700  25.331  20.932  1.00 83.29           C  
ANISOU  373  C   THR A  74    11533  13507   6608   -793   -914    478       C  
ATOM    374  O   THR A  74      67.895  25.033  21.054  1.00 82.62           O  
ANISOU  374  O   THR A  74    11540  13276   6577   -840  -1014    559       O  
ATOM    375  CB  THR A  74      65.359  23.218  20.981  1.00 85.39           C  
ANISOU  375  CB  THR A  74    11622  14015   6806  -1104   -848    850       C  
ATOM    376  OG1 THR A  74      64.364  22.484  21.704  1.00 87.96           O  
ANISOU  376  OG1 THR A  74    11768  14714   6939  -1265   -748    974       O  
ATOM    377  CG2 THR A  74      66.640  22.399  20.936  1.00 85.17           C  
ANISOU  377  CG2 THR A  74    11753  13767   6842  -1205   -980   1056       C  
ATOM    378  N   THR A  75      66.257  26.327  20.166  1.00 82.19           N  
ANISOU  378  N   THR A  75    11272  13336   6621   -920   -994    196       N  
ATOM    379  CA  THR A  75      67.086  27.082  19.222  1.00 80.72           C  
ANISOU  379  CA  THR A  75    11222  12859   6588   -835  -1074     78       C  
ATOM    380  C   THR A  75      67.685  26.166  18.139  1.00 78.94           C  
ANISOU  380  C   THR A  75    11014  12421   6560   -920  -1132    238       C  
ATOM    381  O   THR A  75      68.810  26.383  17.677  1.00 78.13           O  
ANISOU  381  O   THR A  75    10986  12160   6538   -928  -1208    232       O  
ATOM    382  CB  THR A  75      68.201  27.938  19.913  1.00 81.56           C  
ANISOU  382  CB  THR A  75    11463  12943   6582   -835  -1151    -39       C  
ATOM    383  OG1 THR A  75      69.398  27.162  20.019  1.00 80.70           O  
ANISOU  383  OG1 THR A  75    11370  12746   6547   -964  -1237    110       O  
ATOM    384  CG2 THR A  75      67.775  28.456  21.297  1.00 83.98           C  
ANISOU  384  CG2 THR A  75    11747  13555   6606   -797  -1100   -134       C  
ATOM    385  N   VAL A  76      66.936  25.137  17.748  1.00 78.90           N  
ANISOU  385  N   VAL A  76    10743  12397   6840  -1160  -1294    477       N  
ATOM    386  CA  VAL A  76      67.320  24.287  16.620  1.00 77.71           C  
ANISOU  386  CA  VAL A  76    10630  12027   6870  -1155  -1342    532       C  
ATOM    387  C   VAL A  76      67.073  25.052  15.324  1.00 76.66           C  
ANISOU  387  C   VAL A  76    10503  11785   6839  -1050  -1331    402       C  
ATOM    388  O   VAL A  76      67.953  25.107  14.458  1.00 75.68           O  
ANISOU  388  O   VAL A  76    10438  11499   6817  -1010  -1374    403       O  
ATOM    389  CB  VAL A  76      66.554  22.951  16.634  1.00 78.73           C  
ANISOU  389  CB  VAL A  76    10714  12198   7003  -1291  -1342    666       C  
ATOM    390  CG1 VAL A  76      66.877  22.139  15.389  1.00 78.09           C  
ANISOU  390  CG1 VAL A  76    10705  11887   7079  -1287  -1411    686       C  
ATOM    391  CG2 VAL A  76      66.880  22.163  17.893  1.00 80.29           C  
ANISOU  391  CG2 VAL A  76    10942  12470   7095  -1435  -1376    856       C  
ATOM    392  N   GLY A  77      65.882  25.652  15.221  1.00 76.29           N  
ANISOU  392  N   GLY A  77    10337  11841   6810   -952  -1163    212       N  
ATOM    393  CA  GLY A  77      65.493  26.529  14.115  1.00 75.86           C  
ANISOU  393  CA  GLY A  77    10290  11702   6830   -826  -1175    107       C  
ATOM    394  C   GLY A  77      65.708  25.923  12.742  1.00 74.81           C  
ANISOU  394  C   GLY A  77    10202  11397   6824   -848  -1227    157       C  
ATOM    395  O   GLY A  77      66.646  26.319  12.028  1.00 73.99           O  
ANISOU  395  O   GLY A  77    10197  11150   6765   -811  -1257    143       O  
ATOM    396  N   TYR A  78      64.848  24.962  12.380  1.00 74.81           N  
ANISOU  396  N   TYR A  78    10016  11354   7056   -725  -1283    150       N  
ATOM    397  CA  TYR A  78      64.950  24.251  11.106  1.00 74.35           C  
ANISOU  397  CA  TYR A  78    10030  11134   7087   -752  -1354    173       C  
ATOM    398  C   TYR A  78      64.801  25.198   9.931  1.00 73.87           C  
ANISOU  398  C   TYR A  78     9993  11030   7044   -615  -1368     84       C  
ATOM    399  O   TYR A  78      65.630  25.183   9.024  1.00 73.19           O  
ANISOU  399  O   TYR A  78    10006  10821   6983   -573  -1389     79       O  
ATOM    400  CB  TYR A  78      63.918  23.130  10.996  1.00 75.63           C  
ANISOU  400  CB  TYR A  78    10135  11339   7263   -917  -1408    240       C  
ATOM    401  CG  TYR A  78      64.263  21.893  11.771  1.00 76.54           C  
ANISOU  401  CG  TYR A  78    10321  11385   7375  -1085  -1449    374       C  
ATOM    402  CD1 TYR A  78      65.458  21.213  11.545  1.00 76.19           C  
ANISOU  402  CD1 TYR A  78    10457  11108   7384  -1029  -1511    398       C  
ATOM    403  CD2 TYR A  78      63.383  21.388  12.719  1.00 78.30           C  
ANISOU  403  CD2 TYR A  78    10427  11799   7526  -1294  -1435    493       C  
ATOM    404  CE1 TYR A  78      65.773  20.061  12.266  1.00 77.56           C  
ANISOU  404  CE1 TYR A  78    10745  11167   7559  -1152  -1588    538       C  
ATOM    405  CE2 TYR A  78      63.683  20.239  13.445  1.00 79.69           C  
ANISOU  405  CE2 TYR A  78    10709  11882   7686  -1489  -1500    666       C  
ATOM    406  CZ  TYR A  78      64.876  19.579  13.215  1.00 79.29           C  
ANISOU  406  CZ  TYR A  78    10894  11521   7712  -1404  -1594    688       C  
ATOM    407  OH  TYR A  78      65.152  18.438  13.934  1.00 81.16           O  
ANISOU  407  OH  TYR A  78    11294  11604   7940  -1560  -1702    871       O  
ATOM    408  N   GLY A  79      63.765  26.036   9.966  1.00 73.83           N  
ANISOU  408  N   GLY A  79     9875  11243   6933   -331  -1171   -104       N  
ATOM    409  CA  GLY A  79      63.462  26.949   8.860  1.00 73.95           C  
ANISOU  409  CA  GLY A  79     9936  11201   6960   -186  -1224   -160       C  
ATOM    410  C   GLY A  79      62.177  26.637   8.114  1.00 75.06           C  
ANISOU  410  C   GLY A  79     9940  11483   7095   -168  -1283   -173       C  
ATOM    411  O   GLY A  79      61.713  27.440   7.298  1.00 75.85           O  
ANISOU  411  O   GLY A  79    10031  11609   7179     -1  -1338   -219       O  
ATOM    412  N   ASP A  80      61.606  25.469   8.404  1.00 76.70           N  
ANISOU  412  N   ASP A  80     9892  11766   7483   -381  -1213   -359       N  
ATOM    413  CA  ASP A  80      60.311  25.067   7.859  1.00 78.38           C  
ANISOU  413  CA  ASP A  80     9915  12190   7677   -473  -1274   -348       C  
ATOM    414  C   ASP A  80      59.142  25.931   8.358  1.00 80.23           C  
ANISOU  414  C   ASP A  80     9885  12765   7835   -328  -1236   -392       C  
ATOM    415  O   ASP A  80      58.062  25.910   7.768  1.00 82.00           O  
ANISOU  415  O   ASP A  80     9901  13225   8031   -374  -1301   -384       O  
ATOM    416  CB  ASP A  80      60.044  23.583   8.147  1.00 79.06           C  
ANISOU  416  CB  ASP A  80    10001  12257   7783   -772  -1302   -245       C  
ATOM    417  CG  ASP A  80      59.841  23.283   9.630  1.00 80.52           C  
ANISOU  417  CG  ASP A  80     9985  12716   7893   -908  -1217   -161       C  
ATOM    418  OD1 ASP A  80      60.445  23.959  10.487  1.00 80.08           O  
ANISOU  418  OD1 ASP A  80     9911  12736   7779   -784  -1105   -184       O  
ATOM    419  OD2 ASP A  80      59.072  22.348   9.936  1.00 82.57           O  
ANISOU  419  OD2 ASP A  80    10107  13135   8130  -1180  -1277    -64       O  
ATOM    420  N   LEU A  81      59.367  26.675   9.441  1.00 80.63           N  
ANISOU  420  N   LEU A  81    10079  12865   7693   -283   -746   -346       N  
ATOM    421  CA  LEU A  81      58.360  27.556  10.035  1.00 82.90           C  
ANISOU  421  CA  LEU A  81    10144  13476   7878    -35   -704   -443       C  
ATOM    422  C   LEU A  81      59.029  28.710  10.770  1.00 82.71           C  
ANISOU  422  C   LEU A  81    10301  13308   7816    209   -657   -561       C  
ATOM    423  O   LEU A  81      60.096  28.527  11.371  1.00 81.12           O  
ANISOU  423  O   LEU A  81    10280  12905   7636     79   -619   -528       O  
ATOM    424  CB  LEU A  81      57.496  26.774  11.021  1.00 84.87           C  
ANISOU  424  CB  LEU A  81    10082  14146   8020   -221   -613   -376       C  
ATOM    425  CG  LEU A  81      56.460  25.791  10.468  1.00 86.39           C  
ANISOU  425  CG  LEU A  81    10038  14571   8215   -518   -681   -253       C  
ATOM    426  CD1 LEU A  81      56.453  24.508  11.269  1.00 87.00           C  
ANISOU  426  CD1 LEU A  81    10066  14737   8253   -910   -632    -85       C  
ATOM    427  CD2 LEU A  81      55.081  26.414  10.433  1.00 89.56           C  
ANISOU  427  CD2 LEU A  81    10048  15469   8511   -350   -684   -306       C  
ATOM    428  N   TYR A  82      58.400  29.887  10.713  1.00 83.07           N  
ANISOU  428  N   TYR A  82    10096  13500   7968    253   -357   -480       N  
ATOM    429  CA  TYR A  82      58.833  31.093  11.441  1.00 84.08           C  
ANISOU  429  CA  TYR A  82    10418  13499   8031    532   -348   -644       C  
ATOM    430  C   TYR A  82      57.839  32.253  11.274  1.00 87.15           C  
ANISOU  430  C   TYR A  82    10788  13964   8360   1003   -431   -817       C  
ATOM    431  O   TYR A  82      57.005  32.230  10.366  1.00 88.25           O  
ANISOU  431  O   TYR A  82    10773  14236   8521   1127   -509   -789       O  
ATOM    432  CB  TYR A  82      60.239  31.535  11.007  1.00 82.02           C  
ANISOU  432  CB  TYR A  82    10547  12750   7865    431   -419   -615       C  
ATOM    433  CG  TYR A  82      60.379  31.803   9.534  1.00 81.24           C  
ANISOU  433  CG  TYR A  82    10604  12393   7870    428   -543   -531       C  
ATOM    434  CD1 TYR A  82      60.821  30.802   8.669  1.00 79.21           C  
ANISOU  434  CD1 TYR A  82    10303  12112   7683    149   -537   -381       C  
ATOM    435  CD2 TYR A  82      60.071  33.058   9.000  1.00 83.03           C  
ANISOU  435  CD2 TYR A  82    11047  12400   8102    721   -682   -602       C  
ATOM    436  CE1 TYR A  82      60.951  31.035   7.309  1.00 78.83           C  
ANISOU  436  CE1 TYR A  82    10380  11890   7680    146   -638   -306       C  
ATOM    437  CE2 TYR A  82      60.195  33.307   7.642  1.00 82.69           C  
ANISOU  437  CE2 TYR A  82    11149  12153   8118    696   -801   -486       C  
ATOM    438  CZ  TYR A  82      60.638  32.290   6.800  1.00 80.49           C  
ANISOU  438  CZ  TYR A  82    10785  11918   7881    400   -763   -339       C  
ATOM    439  OH  TYR A  82      60.768  32.529   5.447  1.00 80.47           O  
ANISOU  439  OH  TYR A  82    10921  11766   7889    377   -872   -230       O  
ATOM    440  N   PRO A  83      57.923  33.275  12.142  1.00 89.63           N  
ANISOU  440  N   PRO A  83    10907  14098   9049   1206   -345  -1064       N  
ATOM    441  CA  PRO A  83      57.017  34.404  11.983  1.00 93.07           C  
ANISOU  441  CA  PRO A  83    11370  14560   9432   1714   -454  -1242       C  
ATOM    442  C   PRO A  83      57.479  35.435  10.949  1.00 93.20           C  
ANISOU  442  C   PRO A  83    11837  14002   9571   1858   -677  -1228       C  
ATOM    443  O   PRO A  83      58.681  35.590  10.708  1.00 90.99           O  
ANISOU  443  O   PRO A  83    11897  13286   9388   1573   -735  -1123       O  
ATOM    444  CB  PRO A  83      56.995  35.024  13.376  1.00 95.67           C  
ANISOU  444  CB  PRO A  83    11734  15030   9586   1992   -381  -1488       C  
ATOM    445  CG  PRO A  83      58.338  34.735  13.924  1.00 93.08           C  
ANISOU  445  CG  PRO A  83    11713  14347   9306   1648   -372  -1434       C  
ATOM    446  CD  PRO A  83      58.814  33.449  13.302  1.00 89.33           C  
ANISOU  446  CD  PRO A  83    11068  13930   8944   1137   -290  -1154       C  
ATOM    447  N   VAL A  84      56.509  36.121  10.343  1.00100.18           N  
ANISOU  447  N   VAL A  84    12266  14977  10822   2415  -1341   -707       N  
ATOM    448  CA  VAL A  84      56.777  37.217   9.399  1.00101.68           C  
ANISOU  448  CA  VAL A  84    12881  14658  11093   2646  -1591   -686       C  
ATOM    449  C   VAL A  84      56.084  38.519   9.838  1.00106.67           C  
ANISOU  449  C   VAL A  84    13681  15218  11632   3298  -1731   -961       C  
ATOM    450  O   VAL A  84      56.301  39.581   9.246  1.00108.80           O  
ANISOU  450  O   VAL A  84    14413  14970  11957   3527  -1976   -969       O  
ATOM    451  CB  VAL A  84      56.392  36.863   7.930  1.00101.15           C  
ANISOU  451  CB  VAL A  84    12681  14658  11092   2591  -1689   -485       C  
ATOM    452  CG1 VAL A  84      57.194  37.720   6.961  1.00101.84           C  
ANISOU  452  CG1 VAL A  84    13288  14151  11256   2624  -1926   -370       C  
ATOM    453  CG2 VAL A  84      56.662  35.398   7.628  1.00 97.16           C  
ANISOU  453  CG2 VAL A  84    11945  14333  10640   2046  -1548   -285       C  
ATOM    454  N   THR A  85      55.262  38.426  10.882  1.00115.59           N  
ANISOU  454  N   THR A  85    14904  16299  12715   4359  -1936  -1954       N  
ATOM    455  CA  THR A  85      54.647  39.597  11.507  1.00120.73           C  
ANISOU  455  CA  THR A  85    15732  16903  13238   5026  -2044  -2282       C  
ATOM    456  C   THR A  85      55.562  40.158  12.598  1.00121.15           C  
ANISOU  456  C   THR A  85    16262  16521  13250   4986  -2074  -2470       C  
ATOM    457  O   THR A  85      56.323  39.418  13.225  1.00117.79           O  
ANISOU  457  O   THR A  85    15806  16123  12825   4490  -1919  -2386       O  
ATOM    458  CB  THR A  85      53.279  39.251  12.145  1.00123.89           C  
ANISOU  458  CB  THR A  85    15513  18137  13424   5403  -1854  -2467       C  
ATOM    459  OG1 THR A  85      52.623  38.240  11.371  1.00121.95           O  
ANISOU  459  OG1 THR A  85    14709  18423  13203   5083  -1731  -2224       O  
ATOM    460  CG2 THR A  85      52.384  40.496  12.251  1.00130.31           C  
ANISOU  460  CG2 THR A  85    16412  18981  14119   6281  -2034  -2777       C  
ATOM    461  N   LEU A  86      55.477  41.468  12.821  1.00133.11           N  
ANISOU  461  N   LEU A  86    19235  16363  14977   5503  -3380  -2811       N  
ATOM    462  CA  LEU A  86      56.219  42.134  13.890  1.00134.64           C  
ANISOU  462  CA  LEU A  86    19879  16188  15089   5524  -3439  -3057       C  
ATOM    463  C   LEU A  86      55.826  41.574  15.259  1.00134.86           C  
ANISOU  463  C   LEU A  86    19449  16907  14884   5563  -3140  -3245       C  
ATOM    464  O   LEU A  86      56.689  41.273  16.081  1.00131.65           O  
ANISOU  464  O   LEU A  86    19017  16544  14461   5059  -2999  -3157       O  
ATOM    465  CB  LEU A  86      55.988  43.646  13.841  1.00140.74           C  
ANISOU  465  CB  LEU A  86    21219  16438  15819   6194  -3754  -3370       C  
ATOM    466  CG  LEU A  86      56.882  44.498  14.745  1.00141.71           C  
ANISOU  466  CG  LEU A  86    22114  15719  16009   5960  -4013  -3433       C  
ATOM    467  CD1 LEU A  86      58.315  44.499  14.236  1.00136.52           C  
ANISOU  467  CD1 LEU A  86    21603  14710  15560   5128  -4032  -3008       C  
ATOM    468  CD2 LEU A  86      56.347  45.917  14.844  1.00147.72           C  
ANISOU  468  CD2 LEU A  86    23506  15822  16800   6557  -4406  -3621       C  
ATOM    469  N   TRP A  87      54.523  41.428  15.483  1.00139.50           N  
ANISOU  469  N   TRP A  87    19359  19124  14520   7140  -2343  -4467       N  
ATOM    470  CA  TRP A  87      53.997  40.839  16.712  1.00140.17           C  
ANISOU  470  CA  TRP A  87    18911  20007  14341   7147  -2028  -4588       C  
ATOM    471  C   TRP A  87      54.374  39.370  16.873  1.00134.63           C  
ANISOU  471  C   TRP A  87    17828  19628  13698   6373  -1788  -4232       C  
ATOM    472  O   TRP A  87      54.831  38.952  17.932  1.00132.68           O  
ANISOU  472  O   TRP A  87    17695  19324  13393   6007  -1696  -4218       O  
ATOM    473  CB  TRP A  87      52.481  41.020  16.778  1.00145.04           C  
ANISOU  473  CB  TRP A  87    18993  21361  14756   7795  -1934  -4774       C  
ATOM    474  CG  TRP A  87      52.024  42.294  17.447  1.00151.74           C  
ANISOU  474  CG  TRP A  87    20153  22100  15402   8650  -2078  -5260       C  
ATOM    475  CD1 TRP A  87      50.732  42.661  17.696  1.00157.74           C  
ANISOU  475  CD1 TRP A  87    20502  23520  15913   9419  -2011  -5547       C  
ATOM    476  CD2 TRP A  87      52.848  43.352  17.976  1.00153.82           C  
ANISOU  476  CD2 TRP A  87    21213  21561  15671   8847  -2328  -5543       C  
ATOM    477  NE1 TRP A  87      50.696  43.882  18.326  1.00163.42           N  
ANISOU  477  NE1 TRP A  87    21743  23861  16488  10142  -2209  -6014       N  
ATOM    478  CE2 TRP A  87      51.979  44.328  18.513  1.00161.17           C  
ANISOU  478  CE2 TRP A  87    22228  22651  16359   9782  -2416  -6021       C  
ATOM    479  CE3 TRP A  87      54.234  43.573  18.042  1.00150.66           C  
ANISOU  479  CE3 TRP A  87    21453  20342  15448   8314  -2500  -5440       C  
ATOM    480  CZ2 TRP A  87      52.448  45.506  19.109  1.00165.46           C  
ANISOU  480  CZ2 TRP A  87    23544  22482  16841  10196  -2696  -6413       C  
ATOM    481  CZ3 TRP A  87      54.700  44.746  18.637  1.00154.89           C  
ANISOU  481  CZ3 TRP A  87    22716  20213  15922   8659  -2773  -5801       C  
ATOM    482  CH2 TRP A  87      53.807  45.695  19.161  1.00162.20           C  
ANISOU  482  CH2 TRP A  87    23778  21237  16615   9589  -2881  -6287       C  
ATOM    483  N   GLY A  88      54.191  38.589  15.816  1.00121.74           N  
ANISOU  483  N   GLY A  88    14946  19208  12100   4999   -605  -3272       N  
ATOM    484  CA  GLY A  88      54.594  37.187  15.814  1.00116.77           C  
ANISOU  484  CA  GLY A  88    14060  18746  11560   4272   -438  -2930       C  
ATOM    485  C   GLY A  88      56.078  37.009  16.064  1.00112.78           C  
ANISOU  485  C   GLY A  88    13965  17710  11176   3765   -469  -2808       C  
ATOM    486  O   GLY A  88      56.501  35.982  16.590  1.00110.10           O  
ANISOU  486  O   GLY A  88    13414  17610  10809   3298   -303  -2626       O  
ATOM    487  N   ARG A  89      56.862  38.016  15.684  1.00110.17           N  
ANISOU  487  N   ARG A  89    14881  15887  11091   3143   -961  -2197       N  
ATOM    488  CA  ARG A  89      58.311  38.003  15.896  1.00107.13           C  
ANISOU  488  CA  ARG A  89    14868  15035  10801   2667  -1014  -2092       C  
ATOM    489  C   ARG A  89      58.705  38.393  17.321  1.00108.91           C  
ANISOU  489  C   ARG A  89    15224  15340  10815   2718   -959  -2329       C  
ATOM    490  O   ARG A  89      59.780  38.014  17.792  1.00106.17           O  
ANISOU  490  O   ARG A  89    14902  14962  10475   2259   -893  -2195       O  
ATOM    491  CB  ARG A  89      59.032  38.868  14.852  1.00106.83           C  
ANISOU  491  CB  ARG A  89    15374  14254  10964   2608  -1289  -2022       C  
ATOM    492  CG  ARG A  89      59.204  38.143  13.524  1.00104.19           C  
ANISOU  492  CG  ARG A  89    14898  13878  10813   2402  -1313  -1723       C  
ATOM    493  CD  ARG A  89      59.707  39.019  12.389  1.00103.78           C  
ANISOU  493  CD  ARG A  89    15316  13185  10932   2248  -1553  -1564       C  
ATOM    494  NE  ARG A  89      59.761  38.243  11.147  1.00100.67           N  
ANISOU  494  NE  ARG A  89    14680  12913  10656   1965  -1499  -1270       N  
ATOM    495  CZ  ARG A  89      60.306  38.655  10.006  1.00 99.91           C  
ANISOU  495  CZ  ARG A  89    14835  12452  10676   1781  -1646  -1058       C  
ATOM    496  NH1 ARG A  89      60.866  39.851   9.912  1.00102.05           N  
ANISOU  496  NH1 ARG A  89    15621  12171  10983   1790  -1874  -1054       N  
ATOM    497  NH2 ARG A  89      60.296  37.857   8.954  1.00 97.39           N  
ANISOU  497  NH2 ARG A  89    14260  12330  10413   1561  -1573   -844       N  
ATOM    498  N   CYS A  90      57.835  39.143  17.999  1.00117.82           N  
ANISOU  498  N   CYS A  90    16905  16252  11610   3659  -1038  -3222       N  
ATOM    499  CA  CYS A  90      57.991  39.411  19.429  1.00120.42           C  
ANISOU  499  CA  CYS A  90    17262  16842  11651   3796   -944  -3501       C  
ATOM    500  C   CYS A  90      57.809  38.122  20.207  1.00118.58           C  
ANISOU  500  C   CYS A  90    16473  17320  11262   3473   -641  -3318       C  
ATOM    501  O   CYS A  90      58.713  37.705  20.927  1.00115.97           O  
ANISOU  501  O   CYS A  90    16207  16932  10926   3010   -595  -3176       O  
ATOM    502  CB  CYS A  90      56.997  40.459  19.916  1.00126.62           C  
ANISOU  502  CB  CYS A  90    18120  17788  12201   4568   -995  -3939       C  
ATOM    503  SG  CYS A  90      57.486  42.142  19.547  1.00129.95           S  
ANISOU  503  SG  CYS A  90    19348  17241  12786   4962  -1421  -4176       S  
ATOM    504  N   VAL A  91      56.645  37.491  20.042  1.00116.79           N  
ANISOU  504  N   VAL A  91    15035  18770  10571   3669    250  -3437       N  
ATOM    505  CA  VAL A  91      56.379  36.171  20.618  1.00115.23           C  
ANISOU  505  CA  VAL A  91    14316  19218  10247   3254    512  -3177       C  
ATOM    506  C   VAL A  91      57.617  35.275  20.484  1.00110.01           C  
ANISOU  506  C   VAL A  91    13811  18200   9787   2578    490  -2845       C  
ATOM    507  O   VAL A  91      58.016  34.625  21.449  1.00109.47           O  
ANISOU  507  O   VAL A  91    13652  18381   9561   2281    613  -2754       O  
ATOM    508  CB  VAL A  91      55.173  35.493  19.941  1.00115.82           C  
ANISOU  508  CB  VAL A  91    13824  19844  10340   3272    632  -2999       C  
ATOM    509  CG1 VAL A  91      54.993  34.078  20.469  1.00114.61           C  
ANISOU  509  CG1 VAL A  91    13219  20258  10071   2746    856  -2689       C  
ATOM    510  CG2 VAL A  91      53.911  36.314  20.155  1.00121.50           C  
ANISOU  510  CG2 VAL A  91    14286  21059  10821   3958    678  -3314       C  
ATOM    511  N   ALA A  92      58.233  35.282  19.300  1.00101.26           N  
ANISOU  511  N   ALA A  92    13034  16424   9017   1984    105  -2045       N  
ATOM    512  CA  ALA A  92      59.444  34.505  19.034  1.00 96.80           C  
ANISOU  512  CA  ALA A  92    12596  15542   8640   1424     77  -1754       C  
ATOM    513  C   ALA A  92      60.524  34.734  20.096  1.00 96.65           C  
ANISOU  513  C   ALA A  92    12854  15357   8511   1250     44  -1829       C  
ATOM    514  O   ALA A  92      60.892  33.803  20.824  1.00 95.51           O  
ANISOU  514  O   ALA A  92    12538  15484   8267    929    164  -1662       O  
ATOM    515  CB  ALA A  92      59.971  34.804  17.641  1.00 94.38           C  
ANISOU  515  CB  ALA A  92    12538  14692   8629   1335    -98  -1631       C  
ATOM    516  N   VAL A  93      61.005  35.976  20.189  1.00 99.97           N  
ANISOU  516  N   VAL A  93    14052  15151   8781   1233   -290  -2121       N  
ATOM    517  CA  VAL A  93      62.020  36.370  21.173  1.00100.94           C  
ANISOU  517  CA  VAL A  93    14475  15107   8769   1122   -372  -2263       C  
ATOM    518  C   VAL A  93      61.711  35.773  22.551  1.00102.71           C  
ANISOU  518  C   VAL A  93    14425  15942   8660   1134   -174  -2329       C  
ATOM    519  O   VAL A  93      62.580  35.153  23.170  1.00100.95           O  
ANISOU  519  O   VAL A  93    14159  15807   8391    754   -136  -2148       O  
ATOM    520  CB  VAL A  93      62.149  37.915  21.274  1.00104.52           C  
ANISOU  520  CB  VAL A  93    15436  15081   9197   1477   -612  -2611       C  
ATOM    521  CG1 VAL A  93      63.084  38.318  22.409  1.00107.36           C  
ANISOU  521  CG1 VAL A  93    16023  15480   9289   1520   -663  -2882       C  
ATOM    522  CG2 VAL A  93      62.631  38.499  19.966  1.00102.68           C  
ANISOU  522  CG2 VAL A  93    15563  14203   9248   1211   -839  -2460       C  
ATOM    523  N   VAL A  94      60.472  35.953  23.009  1.00107.93           N  
ANISOU  523  N   VAL A  94    15057  17122   8831   1743    157  -2808       N  
ATOM    524  CA  VAL A  94      60.030  35.421  24.297  1.00110.24           C  
ANISOU  524  CA  VAL A  94    15042  18087   8756   1753    370  -2846       C  
ATOM    525  C   VAL A  94      60.283  33.915  24.378  1.00106.80           C  
ANISOU  525  C   VAL A  94    14287  17900   8392   1210    506  -2402       C  
ATOM    526  O   VAL A  94      60.977  33.463  25.288  1.00106.06           O  
ANISOU  526  O   VAL A  94    14259  17850   8189    908    511  -2289       O  
ATOM    527  CB  VAL A  94      58.547  35.769  24.603  1.00114.69           C  
ANISOU  527  CB  VAL A  94    15262  19260   9055   2260    537  -3071       C  
ATOM    528  CG1 VAL A  94      58.069  35.063  25.863  1.00116.92           C  
ANISOU  528  CG1 VAL A  94    15134  20346   8943   2140    798  -2994       C  
ATOM    529  CG2 VAL A  94      58.371  37.273  24.733  1.00118.92           C  
ANISOU  529  CG2 VAL A  94    16176  19519   9488   2875    376  -3555       C  
ATOM    530  N   VAL A  95      59.759  33.145  23.424  1.00102.14           N  
ANISOU  530  N   VAL A  95    13217  17672   7918   1053    396  -1879       N  
ATOM    531  CA  VAL A  95      59.982  31.687  23.431  1.00 99.56           C  
ANISOU  531  CA  VAL A  95    12656  17522   7652    541    488  -1470       C  
ATOM    532  C   VAL A  95      61.465  31.298  23.248  1.00 95.79           C  
ANISOU  532  C   VAL A  95    12476  16530   7390    161    344  -1276       C  
ATOM    533  O   VAL A  95      61.920  30.277  23.783  1.00 95.12           O  
ANISOU  533  O   VAL A  95    12316  16605   7222   -171    391  -1035       O  
ATOM    534  CB  VAL A  95      59.205  30.992  22.297  1.00 99.04           C  
ANISOU  534  CB  VAL A  95    12206  17717   7706    417    577  -1237       C  
ATOM    535  CG1 VAL A  95      58.064  31.874  21.815  1.00100.21           C  
ANISOU  535  CG1 VAL A  95    12327  17793   7955    836    522  -1451       C  
ATOM    536  CG2 VAL A  95      60.139  30.642  21.149  1.00 94.94           C  
ANISOU  536  CG2 VAL A  95    11733  16866   7475    -77    506   -864       C  
ATOM    537  N   MET A  96      62.212  32.129  22.523  1.00 93.46           N  
ANISOU  537  N   MET A  96    12407  15718   7386    137   -174  -1237       N  
ATOM    538  CA  MET A  96      63.661  31.951  22.389  1.00 91.07           C  
ANISOU  538  CA  MET A  96    12354  15039   7210   -165   -308  -1115       C  
ATOM    539  C   MET A  96      64.387  32.007  23.740  1.00 92.81           C  
ANISOU  539  C   MET A  96    12676  15423   7163   -245   -322  -1192       C  
ATOM    540  O   MET A  96      65.004  31.023  24.152  1.00 91.78           O  
ANISOU  540  O   MET A  96    12438  15445   6988   -535   -289   -942       O  
ATOM    541  CB  MET A  96      64.252  32.996  21.444  1.00 89.90           C  
ANISOU  541  CB  MET A  96    12527  14331   7300   -120   -497  -1206       C  
ATOM    542  CG  MET A  96      64.269  32.612  19.984  1.00 87.06           C  
ANISOU  542  CG  MET A  96    12078  13781   7221   -234   -504   -991       C  
ATOM    543  SD  MET A  96      64.271  34.123  18.988  1.00 87.51           S  
ANISOU  543  SD  MET A  96    12457  13329   7465    -16   -688  -1145       S  
ATOM    544  CE  MET A  96      65.281  33.671  17.580  1.00 85.18           C  
ANISOU  544  CE  MET A  96    12388  12632   7345   -421   -836   -959       C  
ATOM    545  N   VAL A  97      64.310  33.149  24.423  1.00 95.85           N  
ANISOU  545  N   VAL A  97    13149  15697   7574     55   -450  -1758       N  
ATOM    546  CA  VAL A  97      65.018  33.318  25.701  1.00 97.80           C  
ANISOU  546  CA  VAL A  97    13503  16120   7535    -36   -484  -1845       C  
ATOM    547  C   VAL A  97      64.473  32.395  26.797  1.00 99.15           C  
ANISOU  547  C   VAL A  97    13347  16919   7407   -125   -278  -1680       C  
ATOM    548  O   VAL A  97      65.233  31.917  27.633  1.00 98.19           O  
ANISOU  548  O   VAL A  97    13188  16881   7237   -432   -296  -1434       O  
ATOM    549  CB  VAL A  97      65.093  34.811  26.190  1.00101.49           C  
ANISOU  549  CB  VAL A  97    14342  16407   7813    254   -636  -2290       C  
ATOM    550  CG1 VAL A  97      65.685  35.710  25.107  1.00100.65           C  
ANISOU  550  CG1 VAL A  97    14585  15664   7993    248   -864  -2379       C  
ATOM    551  CG2 VAL A  97      63.732  35.336  26.652  1.00105.30           C  
ANISOU  551  CG2 VAL A  97    14750  17216   8044    732   -515  -2604       C  
ATOM    552  N   ALA A  98      63.167  32.129  26.765  1.00100.52           N  
ANISOU  552  N   ALA A  98    13099  17710   7383    302   -214  -1725       N  
ATOM    553  CA  ALA A  98      62.535  31.191  27.688  1.00101.93           C  
ANISOU  553  CA  ALA A  98    12907  18511   7309    137     -4  -1479       C  
ATOM    554  C   ALA A  98      63.219  29.836  27.632  1.00 99.13           C  
ANISOU  554  C   ALA A  98    12508  18065   7092   -340    -40  -1033       C  
ATOM    555  O   ALA A  98      63.423  29.197  28.662  1.00100.70           O  
ANISOU  555  O   ALA A  98    12654  18588   7021   -532      1   -873       O  
ATOM    556  CB  ALA A  98      61.069  31.044  27.366  1.00102.81           C  
ANISOU  556  CB  ALA A  98    12674  18938   7450    285    157  -1444       C  
ATOM    557  N   GLY A  99      63.570  29.409  26.421  1.00 94.35           N  
ANISOU  557  N   GLY A  99    11924  16986   6939   -675   -109   -790       N  
ATOM    558  CA  GLY A  99      64.300  28.166  26.208  1.00 91.97           C  
ANISOU  558  CA  GLY A  99    11612  16528   6804  -1048   -168   -401       C  
ATOM    559  C   GLY A  99      65.731  28.260  26.697  1.00 91.01           C  
ANISOU  559  C   GLY A  99    11740  16136   6705  -1152   -341   -394       C  
ATOM    560  O   GLY A  99      66.162  27.438  27.507  1.00 91.88           O  
ANISOU  560  O   GLY A  99    11837  16422   6653  -1351   -363   -176       O  
ATOM    561  N   ILE A 100      66.461  29.267  26.213  1.00 89.64           N  
ANISOU  561  N   ILE A 100    11804  15278   6976  -1007   -436   -660       N  
ATOM    562  CA  ILE A 100      67.863  29.475  26.588  1.00 89.26           C  
ANISOU  562  CA  ILE A 100    11954  15019   6940  -1131   -619   -672       C  
ATOM    563  C   ILE A 100      68.009  29.536  28.113  1.00 92.50           C  
ANISOU  563  C   ILE A 100    12392  15810   6945  -1133   -613   -754       C  
ATOM    564  O   ILE A 100      68.759  28.751  28.702  1.00 92.72           O  
ANISOU  564  O   ILE A 100    12416  15932   6880  -1331   -695   -546       O  
ATOM    565  CB  ILE A 100      68.428  30.766  25.967  1.00 89.03           C  
ANISOU  565  CB  ILE A 100    12177  14595   7055  -1024   -769   -950       C  
ATOM    566  CG1 ILE A 100      68.352  30.701  24.440  1.00 86.16           C  
ANISOU  566  CG1 ILE A 100    11809  13875   7052  -1035   -787   -859       C  
ATOM    567  CG2 ILE A 100      69.858  30.998  26.429  1.00 89.63           C  
ANISOU  567  CG2 ILE A 100    12419  14556   7080  -1206   -967   -969       C  
ATOM    568  CD1 ILE A 100      68.662  32.015  23.757  1.00 86.83           C  
ANISOU  568  CD1 ILE A 100    12160  13595   7238   -913   -919  -1120       C  
ATOM    569  N   THR A 101      67.267  30.452  28.737  1.00 95.40           N  
ANISOU  569  N   THR A 101    12305  16775   7167   -591   -688  -1302       N  
ATOM    570  CA  THR A 101      67.317  30.673  30.177  1.00 98.96           C  
ANISOU  570  CA  THR A 101    12819  17588   7195   -543   -688  -1460       C  
ATOM    571  C   THR A 101      66.961  29.428  30.975  1.00100.18           C  
ANISOU  571  C   THR A 101    12744  18226   7095   -732   -560  -1133       C  
ATOM    572  O   THR A 101      67.753  28.993  31.813  1.00101.07           O  
ANISOU  572  O   THR A 101    12921  18445   7037   -908   -662  -1003       O  
ATOM    573  CB  THR A 101      66.358  31.785  30.607  1.00102.32           C  
ANISOU  573  CB  THR A 101    13336  18154   7386   -153   -628  -1911       C  
ATOM    574  OG1 THR A 101      66.713  33.007  29.950  1.00103.66           O  
ANISOU  574  OG1 THR A 101    13877  17983   7525    -94   -861  -2232       O  
ATOM    575  CG2 THR A 101      66.428  31.996  32.112  1.00106.29           C  
ANISOU  575  CG2 THR A 101    13631  19354   7401    -35   -422  -1957       C  
ATOM    576  N   SER A 102      65.797  28.839  30.719  1.00100.14           N  
ANISOU  576  N   SER A 102    12120  18720   7209   -627   -220   -879       N  
ATOM    577  CA  SER A 102      65.372  27.688  31.520  1.00102.17           C  
ANISOU  577  CA  SER A 102    12204  19443   7174   -872   -122   -534       C  
ATOM    578  C   SER A 102      66.277  26.462  31.322  1.00 99.69           C  
ANISOU  578  C   SER A 102    11945  18827   7106  -1199   -271   -100       C  
ATOM    579  O   SER A 102      66.463  25.669  32.254  1.00101.56           O  
ANISOU  579  O   SER A 102    12156  19321   7111  -1418   -286    207       O  
ATOM    580  CB  SER A 102      63.894  27.343  31.297  1.00104.33           C  
ANISOU  580  CB  SER A 102    12146  20217   7279   -868    128   -428       C  
ATOM    581  OG  SER A 102      63.697  26.676  30.064  1.00101.45           O  
ANISOU  581  OG  SER A 102    11674  19567   7304  -1028    128   -179       O  
ATOM    582  N   PHE A 103      66.847  26.315  30.126  1.00 95.64           N  
ANISOU  582  N   PHE A 103    11499  17597   7244  -1394    -83    128       N  
ATOM    583  CA  PHE A 103      67.837  25.265  29.892  1.00 94.05           C  
ANISOU  583  CA  PHE A 103    11355  17144   7235  -1615   -228    488       C  
ATOM    584  C   PHE A 103      69.175  25.589  30.549  1.00 94.62           C  
ANISOU  584  C   PHE A 103    11580  17169   7202  -1631   -417    451       C  
ATOM    585  O   PHE A 103      69.978  24.692  30.798  1.00 95.03           O  
ANISOU  585  O   PHE A 103    11663  17207   7238  -1778   -540    759       O  
ATOM    586  CB  PHE A 103      68.033  25.006  28.401  1.00 90.51           C  
ANISOU  586  CB  PHE A 103    10927  16223   7240  -1611   -285    547       C  
ATOM    587  CG  PHE A 103      67.135  23.933  27.846  1.00 90.38           C  
ANISOU  587  CG  PHE A 103    10792  16212   7335  -1764   -201    825       C  
ATOM    588  CD1 PHE A 103      67.298  22.598  28.227  1.00 91.80           C  
ANISOU  588  CD1 PHE A 103    11005  16420   7453  -2006   -273   1222       C  
ATOM    589  CD2 PHE A 103      66.128  24.251  26.937  1.00 89.37           C  
ANISOU  589  CD2 PHE A 103    10542  16049   7364  -1689    -85    703       C  
ATOM    590  CE1 PHE A 103      66.471  21.595  27.712  1.00 92.31           C  
ANISOU  590  CE1 PHE A 103    11012  16442   7621  -2215   -239   1493       C  
ATOM    591  CE2 PHE A 103      65.296  23.260  26.417  1.00 89.65           C  
ANISOU  591  CE2 PHE A 103    10468  16097   7497  -1885    -40    957       C  
ATOM    592  CZ  PHE A 103      65.468  21.928  26.806  1.00 91.20           C  
ANISOU  592  CZ  PHE A 103    10726  16286   7638  -2173   -122   1351       C  
ATOM    593  N   GLY A 104      69.407  26.873  30.820  1.00 97.32           N  
ANISOU  593  N   GLY A 104    11747  17495   7734  -1439   -798     88       N  
ATOM    594  CA  GLY A 104      70.598  27.327  31.535  1.00 98.66           C  
ANISOU  594  CA  GLY A 104    12060  17683   7745  -1480   -996    -13       C  
ATOM    595  C   GLY A 104      70.515  26.955  32.999  1.00102.22           C  
ANISOU  595  C   GLY A 104    12488  18612   7738  -1555   -980    103       C  
ATOM    596  O   GLY A 104      71.501  26.497  33.583  1.00102.97           O  
ANISOU  596  O   GLY A 104    12616  18753   7756  -1687  -1148    317       O  
ATOM    597  N   LEU A 105      69.335  27.145  33.588  1.00106.73           N  
ANISOU  597  N   LEU A 105    12739  20039   7774  -1393   -688    -21       N  
ATOM    598  CA  LEU A 105      69.084  26.742  34.970  1.00110.55           C  
ANISOU  598  CA  LEU A 105    13171  21060   7773  -1490   -635    137       C  
ATOM    599  C   LEU A 105      69.406  25.278  35.219  1.00110.35           C  
ANISOU  599  C   LEU A 105    13106  21024   7797  -1750   -721    666       C  
ATOM    600  O   LEU A 105      69.986  24.941  36.255  1.00111.94           O  
ANISOU  600  O   LEU A 105    13398  21322   7812  -1841   -900    803       O  
ATOM    601  CB  LEU A 105      67.633  27.005  35.378  1.00113.49           C  
ANISOU  601  CB  LEU A 105    13363  21953   7804  -1386   -353     43       C  
ATOM    602  CG  LEU A 105      67.400  28.124  36.394  1.00117.21           C  
ANISOU  602  CG  LEU A 105    13939  22765   7832  -1139   -330   -425       C  
ATOM    603  CD1 LEU A 105      66.868  29.367  35.695  1.00115.87           C  
ANISOU  603  CD1 LEU A 105    13891  22226   7910   -818   -340   -914       C  
ATOM    604  CD2 LEU A 105      66.427  27.657  37.464  1.00121.91           C  
ANISOU  604  CD2 LEU A 105    14324  24124   7871  -1103    -76   -392       C  
ATOM    605  N   VAL A 106      69.027  24.417  34.275  1.00110.40           N  
ANISOU  605  N   VAL A 106    13039  20668   8239  -2001   -346    965       N  
ATOM    606  CA  VAL A 106      69.251  22.980  34.414  1.00111.04           C  
ANISOU  606  CA  VAL A 106    13147  20692   8353  -2242   -447   1479       C  
ATOM    607  C   VAL A 106      70.742  22.647  34.363  1.00109.74           C  
ANISOU  607  C   VAL A 106    13127  20179   8390  -2223   -731   1590       C  
ATOM    608  O   VAL A 106      71.198  21.729  35.049  1.00111.59           O  
ANISOU  608  O   VAL A 106    13436  20444   8520  -2351   -879   1967       O  
ATOM    609  CB  VAL A 106      68.441  22.166  33.389  1.00109.48           C  
ANISOU  609  CB  VAL A 106    12875  20265   8459  -2364   -364   1714       C  
ATOM    610  CG1 VAL A 106      68.707  20.672  33.542  1.00111.61           C  
ANISOU  610  CG1 VAL A 106    13232  20502   8672  -2643   -480   2258       C  
ATOM    611  CG2 VAL A 106      66.956  22.442  33.568  1.00110.83           C  
ANISOU  611  CG2 VAL A 106    12831  20829   8451  -2351    -89   1559       C  
ATOM    612  N   THR A 107      71.500  23.409  33.579  1.00107.45           N  
ANISOU  612  N   THR A 107    12785  19603   8439  -1965   -848   1366       N  
ATOM    613  CA  THR A 107      72.960  23.318  33.608  1.00107.05           C  
ANISOU  613  CA  THR A 107    12799  19374   8500  -1941  -1107   1425       C  
ATOM    614  C   THR A 107      73.512  23.803  34.954  1.00110.41           C  
ANISOU  614  C   THR A 107    13274  20177   8498  -1979  -1233   1364       C  
ATOM    615  O   THR A 107      74.380  23.153  35.543  1.00112.06           O  
ANISOU  615  O   THR A 107    13511  20452   8614  -2030  -1432   1650       O  
ATOM    616  CB  THR A 107      73.607  24.086  32.431  1.00103.89           C  
ANISOU  616  CB  THR A 107    12387  18611   8474  -1830  -1167   1152       C  
ATOM    617  OG1 THR A 107      73.587  23.255  31.266  1.00101.29           O  
ANISOU  617  OG1 THR A 107    12025  17926   8535  -1797  -1150   1338       O  
ATOM    618  CG2 THR A 107      75.055  24.464  32.741  1.00104.81           C  
ANISOU  618  CG2 THR A 107    12510  18756   8556  -1839  -1424   1114       C  
ATOM    619  N   ALA A 108      72.987  24.932  35.430  1.00112.58           N  
ANISOU  619  N   ALA A 108    13577  20887   8310  -1897  -1211    971       N  
ATOM    620  CA  ALA A 108      73.371  25.509  36.721  1.00116.36           C  
ANISOU  620  CA  ALA A 108    14134  21768   8311  -1926  -1321    842       C  
ATOM    621  C   ALA A 108      73.069  24.577  37.891  1.00119.80           C  
ANISOU  621  C   ALA A 108    14551  22624   8343  -2054  -1302   1231       C  
ATOM    622  O   ALA A 108      73.883  24.443  38.806  1.00121.83           O  
ANISOU  622  O   ALA A 108    14854  23011   8423  -2125  -1525   1432       O  
ATOM    623  CB  ALA A 108      72.687  26.849  36.926  1.00117.80           C  
ANISOU  623  CB  ALA A 108    14389  22111   8257  -1791  -1194    345       C  
ATOM    624  N   ALA A 109      71.900  23.938  37.848  1.00125.02           N  
ANISOU  624  N   ALA A 109    15085  23680   8738  -2509   -917   1646       N  
ATOM    625  CA  ALA A 109      71.493  22.965  38.859  1.00128.44           C  
ANISOU  625  CA  ALA A 109    15495  24487   8820  -2705   -878   2098       C  
ATOM    626  C   ALA A 109      72.502  21.826  38.959  1.00128.45           C  
ANISOU  626  C   ALA A 109    15596  24230   8980  -2800  -1164   2536       C  
ATOM    627  O   ALA A 109      72.921  21.456  40.056  1.00131.84           O  
ANISOU  627  O   ALA A 109    16097  24949   9048  -2874  -1326   2742       O  
ATOM    628  CB  ALA A 109      70.109  22.423  38.544  1.00128.21           C  
ANISOU  628  CB  ALA A 109    15336  24513   8865  -2818   -626   2299       C  
ATOM    629  N   LEU A 110      72.899  21.288  37.806  1.00125.13           N  
ANISOU  629  N   LEU A 110    15773  22848   8924  -2751  -1363   2513       N  
ATOM    630  CA  LEU A 110      73.880  20.199  37.742  1.00125.47           C  
ANISOU  630  CA  LEU A 110    15915  22610   9149  -2749  -1646   2901       C  
ATOM    631  C   LEU A 110      75.295  20.648  38.119  1.00126.08           C  
ANISOU  631  C   LEU A 110    15994  22730   9181  -2624  -1923   2780       C  
ATOM    632  O   LEU A 110      76.086  19.852  38.628  1.00128.61           O  
ANISOU  632  O   LEU A 110    16386  23093   9388  -2623  -2165   3124       O  
ATOM    633  CB  LEU A 110      73.915  19.592  36.338  1.00122.13           C  
ANISOU  633  CB  LEU A 110    15511  21624   9270  -2683  -1657   3010       C  
ATOM    634  CG  LEU A 110      72.607  18.988  35.828  1.00121.82           C  
ANISOU  634  CG  LEU A 110    15474  21494   9319  -2852  -1449   3177       C  
ATOM    635  CD1 LEU A 110      72.785  18.423  34.427  1.00118.79           C  
ANISOU  635  CD1 LEU A 110    15142  20545   9449  -2748  -1520   3219       C  
ATOM    636  CD2 LEU A 110      72.104  17.911  36.778  1.00126.01           C  
ANISOU  636  CD2 LEU A 110    16118  22216   9543  -3109  -1490   3671       C  
ATOM    637  N   ALA A 111      75.607  21.917  37.855  1.00121.88           N  
ANISOU  637  N   ALA A 111    15285  22315   8709  -2184  -1808   2162       N  
ATOM    638  CA  ALA A 111      76.919  22.483  38.163  1.00122.74           C  
ANISOU  638  CA  ALA A 111    15358  22495   8781  -2133  -2076   2023       C  
ATOM    639  C   ALA A 111      77.148  22.598  39.670  1.00127.32           C  
ANISOU  639  C   ALA A 111    16002  23578   8794  -2225  -2200   2087       C  
ATOM    640  O   ALA A 111      78.277  22.454  40.137  1.00129.44           O  
ANISOU  640  O   ALA A 111    16252  23966   8964  -2211  -2484   2265       O  
ATOM    641  CB  ALA A 111      77.090  23.835  37.491  1.00120.46           C  
ANISOU  641  CB  ALA A 111    15030  22068   8673  -2103  -2036   1531       C  
ATOM    642  N   THR A 112      76.084  22.849  40.428  1.00130.69           N  
ANISOU  642  N   THR A 112    16538  24398   8722  -2415  -1708   1979       N  
ATOM    643  CA  THR A 112      76.201  22.946  41.883  1.00135.49           C  
ANISOU  643  CA  THR A 112    17213  25534   8734  -2500  -1810   2052       C  
ATOM    644  C   THR A 112      76.052  21.585  42.554  1.00138.12           C  
ANISOU  644  C   THR A 112    17594  25983   8901  -2599  -1893   2666       C  
ATOM    645  O   THR A 112      76.552  21.380  43.656  1.00141.43           O  
ANISOU  645  O   THR A 112    18061  26642   9033  -2626  -2150   2885       O  
ATOM    646  CB  THR A 112      75.205  23.956  42.499  1.00137.77           C  
ANISOU  646  CB  THR A 112    17541  26247   8560  -2505  -1565   1689       C  
ATOM    647  OG1 THR A 112      73.881  23.416  42.474  1.00137.35           O  
ANISOU  647  OG1 THR A 112    17424  26260   8503  -2543  -1250   1852       O  
ATOM    648  CG2 THR A 112      75.230  25.267  41.742  1.00136.03           C  
ANISOU  648  CG2 THR A 112    17359  25841   8486  -2386  -1543   1082       C  
ATOM    649  N   TRP A 113      75.363  20.661  41.890  1.00141.86           N  
ANISOU  649  N   TRP A 113    18669  25826   9405  -3154  -1692   3016       N  
ATOM    650  CA  TRP A 113      75.280  19.276  42.354  1.00144.90           C  
ANISOU  650  CA  TRP A 113    19171  26238   9648  -3294  -1802   3632       C  
ATOM    651  C   TRP A 113      76.658  18.621  42.272  1.00145.53           C  
ANISOU  651  C   TRP A 113    19321  26046   9926  -3157  -2188   3916       C  
ATOM    652  O   TRP A 113      77.016  17.791  43.108  1.00149.50           O  
ANISOU  652  O   TRP A 113    19959  26681  10164  -3222  -2392   4374       O  
ATOM    653  CB  TRP A 113      74.238  18.496  41.538  1.00143.48           C  
ANISOU  653  CB  TRP A 113    19011  25775   9731  -3425  -1597   3888       C  
ATOM    654  CG  TRP A 113      74.225  17.002  41.780  1.00146.58           C  
ANISOU  654  CG  TRP A 113    19599  26006  10089  -3580  -1786   4535       C  
ATOM    655  CD1 TRP A 113      74.288  16.358  42.988  1.00151.89           C  
ANISOU  655  CD1 TRP A 113    20402  27046  10262  -3749  -1932   4960       C  
ATOM    656  CD2 TRP A 113      74.117  15.974  40.785  1.00145.19           C  
ANISOU  656  CD2 TRP A 113    19562  25224  10380  -3585  -1882   4843       C  
ATOM    657  NE1 TRP A 113      74.244  14.996  42.802  1.00153.91           N  
ANISOU  657  NE1 TRP A 113    20894  26913  10671  -3862  -2129   5535       N  
ATOM    658  CE2 TRP A 113      74.136  14.733  41.462  1.00149.94           C  
ANISOU  658  CE2 TRP A 113    20412  25797  10762  -3757  -2108   5452       C  
ATOM    659  CE3 TRP A 113      74.011  15.980  39.389  1.00140.82           C  
ANISOU  659  CE3 TRP A 113    18978  24142  10384  -3463  -1814   4661       C  
ATOM    660  CZ2 TRP A 113      74.052  13.509  40.786  1.00150.54           C  
ANISOU  660  CZ2 TRP A 113    20741  25271  11186  -3795  -2288   5856       C  
ATOM    661  CZ3 TRP A 113      73.928  14.762  38.718  1.00141.28           C  
ANISOU  661  CZ3 TRP A 113    19258  23657  10764  -3493  -1975   5039       C  
ATOM    662  CH2 TRP A 113      73.949  13.546  39.418  1.00146.14           C  
ANISOU  662  CH2 TRP A 113    20153  24195  11178  -3650  -2218   5614       C  
ATOM    663  N   PHE A 114      77.428  19.017  41.263  1.00141.26           N  
ANISOU  663  N   PHE A 114    19032  24987   9653  -2404  -2467   3400       N  
ATOM    664  CA  PHE A 114      78.797  18.545  41.111  1.00142.05           C  
ANISOU  664  CA  PHE A 114    19119  24905   9947  -2209  -2815   3604       C  
ATOM    665  C   PHE A 114      79.744  19.291  42.052  1.00144.86           C  
ANISOU  665  C   PHE A 114    19389  25717   9935  -2205  -3040   3444       C  
ATOM    666  O   PHE A 114      80.718  18.718  42.539  1.00148.13           O  
ANISOU  666  O   PHE A 114    19822  26253  10209  -2113  -3355   3747       O  
ATOM    667  CB  PHE A 114      79.263  18.666  39.653  1.00137.59           C  
ANISOU  667  CB  PHE A 114    18427  23867   9983  -2007  -2802   3389       C  
ATOM    668  CG  PHE A 114      78.670  17.636  38.721  1.00136.03           C  
ANISOU  668  CG  PHE A 114    18362  23164  10161  -1943  -2735   3661       C  
ATOM    669  CD1 PHE A 114      77.931  16.555  39.208  1.00137.38           C  
ANISOU  669  CD1 PHE A 114    18719  23324  10157  -2194  -2554   3944       C  
ATOM    670  CD2 PHE A 114      78.884  17.728  37.350  1.00133.76           C  
ANISOU  670  CD2 PHE A 114    18001  22449  10372  -1653  -2855   3625       C  
ATOM    671  CE1 PHE A 114      77.392  15.600  38.339  1.00136.50           C  
ANISOU  671  CE1 PHE A 114    18766  22706  10390  -2190  -2539   4196       C  
ATOM    672  CE2 PHE A 114      78.354  16.775  36.478  1.00132.90           C  
ANISOU  672  CE2 PHE A 114    18067  21851  10578  -1584  -2825   3842       C  
ATOM    673  CZ  PHE A 114      77.606  15.708  36.976  1.00134.19           C  
ANISOU  673  CZ  PHE A 114    18462  21930  10595  -1870  -2685   4123       C  
ATOM    674  N   VAL A 115      79.453  20.568  42.297  1.00141.82           N  
ANISOU  674  N   VAL A 115    18629  25853   9404  -2102  -2617   2874       N  
ATOM    675  CA  VAL A 115      80.193  21.376  43.272  1.00144.88           C  
ANISOU  675  CA  VAL A 115    18976  26675   9395  -2157  -2825   2651       C  
ATOM    676  C   VAL A 115      79.874  20.926  44.709  1.00150.12           C  
ANISOU  676  C   VAL A 115    19781  27852   9404  -2282  -2885   2919       C  
ATOM    677  O   VAL A 115      80.745  20.958  45.586  1.00153.75           O  
ANISOU  677  O   VAL A 115    20228  28643   9547  -2286  -3188   2996       O  
ATOM    678  CB  VAL A 115      79.925  22.901  43.070  1.00142.83           C  
ANISOU  678  CB  VAL A 115    18681  26415   9173  -2219  -2687   2025       C  
ATOM    679  CG1 VAL A 115      80.017  23.673  44.380  1.00146.85           C  
ANISOU  679  CG1 VAL A 115    19282  27414   9099  -2333  -2767   1751       C  
ATOM    680  CG2 VAL A 115      80.883  23.480  42.048  1.00140.40           C  
ANISOU  680  CG2 VAL A 115    18205  25839   9302  -2163  -2850   1835       C  
ATOM    681  N   GLY A 116      78.632  20.491  44.929  1.00156.53           N  
ANISOU  681  N   GLY A 116    21143  28671   9660  -3086  -2258   3246       N  
ATOM    682  CA  GLY A 116      78.190  19.948  46.214  1.00161.75           C  
ANISOU  682  CA  GLY A 116    21930  29820   9706  -3238  -2278   3609       C  
ATOM    683  C   GLY A 116      78.822  18.608  46.547  1.00164.11           C  
ANISOU  683  C   GLY A 116    22341  29949  10065  -3218  -2556   4268       C  
ATOM    684  O   GLY A 116      78.306  17.861  47.377  1.00167.03           O  
ANISOU  684  O   GLY A 116    22857  30431  10177  -3385  -2490   4729       O  
ATOM    685  N   ARG A 117      79.929  18.299  45.874  1.00166.86           N  
ANISOU  685  N   ARG A 117    23220  29543  10638  -2511  -3383   4499       N  
ATOM    686  CA  ARG A 117      80.789  17.177  46.233  1.00170.15           C  
ANISOU  686  CA  ARG A 117    23739  29855  11057  -2381  -3749   5042       C  
ATOM    687  C   ARG A 117      82.238  17.659  46.309  1.00170.49           C  
ANISOU  687  C   ARG A 117    23569  30020  11188  -2177  -4074   4818       C  
ATOM    688  O   ARG A 117      83.104  17.249  45.527  1.00169.27           O  
ANISOU  688  O   ARG A 117    23304  29540  11471  -1913  -4274   4901       O  
ATOM    689  CB  ARG A 117      80.618  16.001  45.268  1.00168.38           C  
ANISOU  689  CB  ARG A 117    23648  28998  11332  -2268  -3744   5401       C  
ATOM    690  CG  ARG A 117      79.296  15.265  45.439  1.00169.86           C  
ANISOU  690  CG  ARG A 117    24064  29131  11344  -2552  -3521   5769       C  
ATOM    691  CD  ARG A 117      79.412  13.800  45.064  1.00171.91           C  
ANISOU  691  CD  ARG A 117    24605  28864  11849  -2482  -3752   6358       C  
ATOM    692  NE  ARG A 117      78.162  13.082  45.296  1.00173.84           N  
ANISOU  692  NE  ARG A 117    25067  29066  11920  -2851  -3556   6741       N  
ATOM    693  N   GLU A 118      82.463  18.564  47.259  1.00174.50           N  
ANISOU  693  N   GLU A 118    23668  32017  10618  -2415  -4139   3996       N  
ATOM    694  CA  GLU A 118      83.785  19.088  47.589  1.00176.73           C  
ANISOU  694  CA  GLU A 118    23767  32609  10772  -2346  -4494   3829       C  
ATOM    695  C   GLU A 118      84.394  18.287  48.744  1.00182.86           C  
ANISOU  695  C   GLU A 118    24643  33761  11073  -2306  -4854   4325       C  
ATOM    696  O   GLU A 118      85.602  18.350  48.991  1.00185.20           O  
ANISOU  696  O   GLU A 118    24768  34209  11389  -2141  -5235   4416       O  
ATOM    697  CB  GLU A 118      83.681  20.572  47.965  1.00176.63           C  
ANISOU  697  CB  GLU A 118    23712  32929  10470  -2550  -4392   3226       C  
ATOM    698  CG  GLU A 118      82.860  20.850  49.235  1.00180.77           C  
ANISOU  698  CG  GLU A 118    24440  33974  10272  -2737  -4289   3211       C  
ATOM    699  CD  GLU A 118      82.388  22.290  49.345  1.00179.91           C  
ANISOU  699  CD  GLU A 118    24370  34020   9968  -2866  -4071   2555       C  
ATOM    700  OE1 GLU A 118      83.090  23.201  48.854  1.00178.16           O  
ANISOU  700  OE1 GLU A 118    24039  33655   9997  -2879  -4186   2117       O  
ATOM    701  OE2 GLU A 118      81.307  22.511  49.933  1.00181.45           O  
ANISOU  701  OE2 GLU A 118    24709  34483   9749  -2947  -3790   2481       O  
ATOM    702  N   GLN A 119      83.539  17.541  49.441  1.00201.11           N  
ANISOU  702  N   GLN A 119    27704  36910  11797  -2834  -5466   6143       N  
ATOM    703  CA  GLN A 119      83.920  16.715  50.584  1.00207.13           C  
ANISOU  703  CA  GLN A 119    28626  37972  12103  -2824  -5784   6703       C  
ATOM    704  C   GLN A 119      84.896  15.607  50.196  1.00208.16           C  
ANISOU  704  C   GLN A 119    28764  37705  12623  -2494  -6136   7165       C  
ATOM    705  O   GLN A 119      86.108  15.757  50.345  1.00209.95           O  
ANISOU  705  O   GLN A 119    28790  38092  12891  -2274  -6497   7139       O  
ATOM    706  CB  GLN A 119      82.665  16.117  51.222  1.00209.33           C  
ANISOU  706  CB  GLN A 119    29175  38362  11997  -3077  -5528   7062       C  
ATOM    707  CG  GLN A 119      81.814  15.287  50.256  1.00206.64           C  
ANISOU  707  CG  GLN A 119    28983  37386  12146  -3061  -5353   7396       C  
ATOM    708  CD  GLN A 119      80.337  15.660  50.275  1.00204.76           C  
ANISOU  708  CD  GLN A 119    28790  37208  11802  -3353  -4865   7264       C  
ATOM    709  OE1 GLN A 119      79.474  14.830  49.989  1.00204.75           O  
ANISOU  709  OE1 GLN A 119    28960  36880  11956  -3486  -4735   7661       O  
ATOM    710  NE2 GLN A 119      80.042  16.916  50.597  1.00203.60           N  
ANISOU  710  NE2 GLN A 119    28493  37479  11388  -3448  -4611   6698       N  
TER     711      GLN A 119                                                      
ATOM    712  N   ALA B  23      86.113  10.235  40.196  1.00196.54           N  
ANISOU  712  N   ALA B  23    31017  26407  17252   3791 -10168   3928       N  
ATOM    713  CA  ALA B  23      85.138  11.071  40.954  1.00195.07           C  
ANISOU  713  CA  ALA B  23    30834  26602  16681   3181  -9922   3896       C  
ATOM    714  C   ALA B  23      83.708  10.814  40.474  1.00192.96           C  
ANISOU  714  C   ALA B  23    30925  25907  16485   2791  -9639   4004       C  
ATOM    715  O   ALA B  23      83.399   9.719  39.996  1.00195.44           O  
ANISOU  715  O   ALA B  23    31659  25668  16933   2876  -9793   4366       O  
ATOM    716  CB  ALA B  23      85.502  12.547  40.828  1.00191.03           C  
ANISOU  716  CB  ALA B  23    29837  26589  16157   3014  -9684   3369       C  
ATOM    717  N   LEU B  24      82.838  11.813  40.621  1.00179.83           N  
ANISOU  717  N   LEU B  24    28871  24972  14485   -649  -7747   5536       N  
ATOM    718  CA  LEU B  24      81.486  11.750  40.068  1.00177.04           C  
ANISOU  718  CA  LEU B  24    28714  24281  14273   -978  -7429   5524       C  
ATOM    719  C   LEU B  24      81.371  12.656  38.853  1.00171.13           C  
ANISOU  719  C   LEU B  24    27658  23500  13864   -952  -7119   4978       C  
ATOM    720  O   LEU B  24      81.052  12.189  37.762  1.00168.79           O  
ANISOU  720  O   LEU B  24    27442  22718  13971   -822  -7040   4895       O  
ATOM    721  CB  LEU B  24      80.428  12.142  41.105  1.00178.24           C  
ANISOU  721  CB  LEU B  24    28949  24819  13954  -1491  -7221   5661       C  
ATOM    722  CG  LEU B  24      78.977  12.190  40.606  1.00175.35           C  
ANISOU  722  CG  LEU B  24    28662  24257  13707  -1847  -6855   5589       C  
ATOM    723  CD1 LEU B  24      78.314  10.822  40.688  1.00179.41           C  
ANISOU  723  CD1 LEU B  24    29599  24435  14134  -2099  -6969   6165       C  
ATOM    724  CD2 LEU B  24      78.168  13.218  41.376  1.00173.70           C  
ANISOU  724  CD2 LEU B  24    28218  24629  13152  -2168  -6511   5281       C  
ATOM    725  N   HIS B  25      81.635  13.948  39.050  1.00152.18           N  
ANISOU  725  N   HIS B  25    21777  23827  12218   -792  -4985   4338       N  
ATOM    726  CA  HIS B  25      81.504  14.955  37.992  1.00147.03           C  
ANISOU  726  CA  HIS B  25    20857  23149  11860   -796  -4718   3837       C  
ATOM    727  C   HIS B  25      82.221  14.556  36.701  1.00145.29           C  
ANISOU  727  C   HIS B  25    20563  22514  12128   -413  -4791   3749       C  
ATOM    728  O   HIS B  25      81.674  14.689  35.612  1.00142.20           O  
ANISOU  728  O   HIS B  25    20241  21743  12046   -423  -4594   3626       O  
ATOM    729  CB  HIS B  25      81.970  16.334  38.489  1.00146.46           C  
ANISOU  729  CB  HIS B  25    20488  23612  11550   -915  -4687   3476       C  
ATOM    730  CG  HIS B  25      83.451  16.448  38.709  1.00148.25           C  
ANISOU  730  CG  HIS B  25    20445  24075  11808   -649  -4982   3425       C  
ATOM    731  ND1 HIS B  25      84.359  15.626  38.077  1.00147.39           N  
ANISOU  731  ND1 HIS B  25    20041  24339  11621   -763  -4979   3057       N  
ATOM    732  CD2 HIS B  25      84.180  17.288  39.482  1.00151.43           C  
ANISOU  732  CD2 HIS B  25    20814  24429  12292   -279  -5305   3696       C  
ATOM    733  CE1 HIS B  25      85.584  15.953  38.449  1.00149.85           C  
ANISOU  733  CE1 HIS B  25    20100  24874  11962   -519  -5272   3116       C  
ATOM    734  NE2 HIS B  25      85.503  16.956  39.304  1.00152.30           N  
ANISOU  734  NE2 HIS B  25    20546  24952  12369   -182  -5466   3491       N  
ATOM    735  N   TRP B  26      83.433  14.035  36.850  1.00152.75           N  
ANISOU  735  N   TRP B  26    20477  23662  13898    963  -5887   2102       N  
ATOM    736  CA  TRP B  26      84.295  13.665  35.736  1.00152.20           C  
ANISOU  736  CA  TRP B  26    20264  23353  14213   1410  -5981   1996       C  
ATOM    737  C   TRP B  26      83.813  12.374  35.074  1.00152.98           C  
ANISOU  737  C   TRP B  26    20739  22807  14579   1632  -6042   2214       C  
ATOM    738  O   TRP B  26      84.056  12.152  33.890  1.00151.82           O  
ANISOU  738  O   TRP B  26    20523  22397  14766   1971  -6031   2048       O  
ATOM    739  CB  TRP B  26      85.722  13.478  36.264  1.00156.62           C  
ANISOU  739  CB  TRP B  26    20610  24260  14638   1773  -6346   2135       C  
ATOM    740  CG  TRP B  26      86.799  14.365  35.664  1.00155.69           C  
ANISOU  740  CG  TRP B  26    19981  24522  14653   1961  -6352   1815       C  
ATOM    741  CD1 TRP B  26      88.138  14.301  35.935  1.00159.61           C  
ANISOU  741  CD1 TRP B  26    20165  25400  15081   2325  -6656   1887       C  
ATOM    742  CD2 TRP B  26      86.638  15.431  34.712  1.00151.16           C  
ANISOU  742  CD2 TRP B  26    19128  24031  14276   1766  -6057   1406       C  
ATOM    743  NE1 TRP B  26      88.816  15.256  35.221  1.00157.88           N  
ANISOU  743  NE1 TRP B  26    19460  25533  14996   2327  -6554   1556       N  
ATOM    744  CE2 TRP B  26      87.923  15.963  34.461  1.00152.72           C  
ANISOU  744  CE2 TRP B  26    18845  24675  14505   1974  -6195   1270       C  
ATOM    745  CE3 TRP B  26      85.536  15.986  34.046  1.00146.37           C  
ANISOU  745  CE3 TRP B  26    18624  23182  13807   1436  -5708   1163       C  
ATOM    746  CZ2 TRP B  26      88.139  17.021  33.574  1.00149.74           C  
ANISOU  746  CZ2 TRP B  26    18120  24485  14289   1810  -5993    926       C  
ATOM    747  CZ3 TRP B  26      85.752  17.041  33.162  1.00143.29           C  
ANISOU  747  CZ3 TRP B  26    17920  22937  13588   1326  -5524    810       C  
ATOM    748  CH2 TRP B  26      87.046  17.546  32.936  1.00145.02           C  
ANISOU  748  CH2 TRP B  26    17691  23579  13831   1487  -5667    707       C  
ATOM    749  N   ARG B  27      83.127  11.536  35.849  1.00161.27           N  
ANISOU  749  N   ARG B  27    24058  22534  14683   1196  -7474   3341       N  
ATOM    750  CA  ARG B  27      82.704  10.208  35.401  1.00163.62           C  
ANISOU  750  CA  ARG B  27    24802  22176  15190   1384  -7645   3626       C  
ATOM    751  C   ARG B  27      81.245  10.161  34.943  1.00161.19           C  
ANISOU  751  C   ARG B  27    24751  21526  14966    938  -7381   3650       C  
ATOM    752  O   ARG B  27      80.900   9.374  34.057  1.00161.35           O  
ANISOU  752  O   ARG B  27    25061  20965  15278   1054  -7429   3694       O  
ATOM    753  CB  ARG B  27      82.946   9.169  36.502  1.00169.97           C  
ANISOU  753  CB  ARG B  27    25941  22894  15747   1520  -8050   4139       C  
ATOM    754  N   ALA B  28      80.399  10.992  35.552  1.00150.45           N  
ANISOU  754  N   ALA B  28    23780  21096  12288   -991  -5360   5206       N  
ATOM    755  CA  ALA B  28      78.985  11.089  35.177  1.00148.09           C  
ANISOU  755  CA  ALA B  28    23599  20632  12038  -1421  -5068   5182       C  
ATOM    756  C   ALA B  28      78.846  11.663  33.775  1.00143.20           C  
ANISOU  756  C   ALA B  28    22795  19798  11815  -1280  -4849   4747       C  
ATOM    757  O   ALA B  28      77.973  11.247  33.011  1.00142.21           O  
ANISOU  757  O   ALA B  28    22869  19254  11909  -1402  -4766   4765       O  
ATOM    758  CB  ALA B  28      78.213  11.938  36.180  1.00147.44           C  
ANISOU  758  CB  ALA B  28    23344  21124  11554  -1863  -4809   5134       C  
ATOM    759  N   ALA B  29      79.719  12.617  33.452  1.00131.58           N  
ANISOU  759  N   ALA B  29    18913  19578  11503   -862  -3767   3732       N  
ATOM    760  CA  ALA B  29      79.763  13.244  32.136  1.00127.29           C  
ANISOU  760  CA  ALA B  29    18160  18910  11296   -717  -3573   3332       C  
ATOM    761  C   ALA B  29      80.179  12.242  31.063  1.00128.36           C  
ANISOU  761  C   ALA B  29    18486  18521  11763   -313  -3748   3368       C  
ATOM    762  O   ALA B  29      79.475  12.076  30.067  1.00127.33           O  
ANISOU  762  O   ALA B  29    18588  17965  11828   -414  -3668   3369       O  
ATOM    763  CB  ALA B  29      80.701  14.441  32.149  1.00125.47           C  
ANISOU  763  CB  ALA B  29    17509  19137  11026   -614  -3514   3007       C  
ATOM    764  N   GLY B  30      81.310  11.572  31.274  1.00136.27           N  
ANISOU  764  N   GLY B  30    18901  19292  13585    681  -4693   2389       N  
ATOM    765  CA  GLY B  30      81.783  10.540  30.351  1.00138.11           C  
ANISOU  765  CA  GLY B  30    19336  19039  14101   1162  -4877   2386       C  
ATOM    766  C   GLY B  30      80.742   9.469  30.057  1.00139.67           C  
ANISOU  766  C   GLY B  30    20077  18563  14428   1035  -4964   2606       C  
ATOM    767  O   GLY B  30      80.702   8.919  28.954  1.00139.26           O  
ANISOU  767  O   GLY B  30    20179  18083  14650   1277  -4975   2443       O  
ATOM    768  N   ALA B  31      79.897   9.184  31.049  1.00138.99           N  
ANISOU  768  N   ALA B  31    21491  18037  13283    640  -5746   4219       N  
ATOM    769  CA  ALA B  31      78.822   8.201  30.915  1.00141.40           C  
ANISOU  769  CA  ALA B  31    22324  17735  13667    396  -5865   4507       C  
ATOM    770  C   ALA B  31      77.616   8.768  30.170  1.00137.53           C  
ANISOU  770  C   ALA B  31    21798  17180  13277    -76  -5540   4346       C  
ATOM    771  O   ALA B  31      76.896   8.032  29.491  1.00139.11           O  
ANISOU  771  O   ALA B  31    22386  16854  13616   -261  -5630   4491       O  
ATOM    772  CB  ALA B  31      78.407   7.686  32.280  1.00146.04           C  
ANISOU  772  CB  ALA B  31    23211  18329  13947    113  -6078   5019       C  
ATOM    773  N   ALA B  32      77.400  10.076  30.303  1.00124.88           N  
ANISOU  773  N   ALA B  32    19555  16417  11477   -748  -3525   4617       N  
ATOM    774  CA  ALA B  32      76.312  10.763  29.604  1.00121.19           C  
ANISOU  774  CA  ALA B  32    19000  15921  11127  -1087  -3224   4410       C  
ATOM    775  C   ALA B  32      76.544  10.804  28.101  1.00118.82           C  
ANISOU  775  C   ALA B  32    18651  15332  11162   -725  -3195   4064       C  
ATOM    776  O   ALA B  32      75.588  10.767  27.329  1.00118.33           O  
ANISOU  776  O   ALA B  32    18791  14881  11289   -842  -3172   4017       O  
ATOM    777  CB  ALA B  32      76.120  12.170  30.148  1.00117.66           C  
ANISOU  777  CB  ALA B  32    18141  16076  10489  -1346  -2894   4186       C  
ATOM    778  N   THR B  33      77.809  10.883  27.693  1.00116.03           N  
ANISOU  778  N   THR B  33    17136  15606  11346    195  -3130   3521       N  
ATOM    779  CA  THR B  33      78.163  10.881  26.270  1.00114.25           C  
ANISOU  779  CA  THR B  33    16853  15154  11401    534  -3085   3203       C  
ATOM    780  C   THR B  33      77.981   9.490  25.652  1.00117.75           C  
ANISOU  780  C   THR B  33    17814  14897  12027    712  -3351   3340       C  
ATOM    781  O   THR B  33      77.660   9.365  24.462  1.00116.22           O  
ANISOU  781  O   THR B  33    17715  14402  12042    745  -3273   3118       O  
ATOM    782  CB  THR B  33      79.598  11.393  26.015  1.00113.69           C  
ANISOU  782  CB  THR B  33    16397  15457  11344    967  -3086   2974       C  
ATOM    783  OG1 THR B  33      80.542  10.483  26.591  1.00118.39           O  
ANISOU  783  OG1 THR B  33    17147  15924  11910   1414  -3419   3162       O  
ATOM    784  CG2 THR B  33      79.795  12.784  26.609  1.00111.54           C  
ANISOU  784  CG2 THR B  33    15741  15783  10857    700  -2915   2912       C  
ATOM    785  N   VAL B  34      78.187   8.453  26.467  1.00122.98           N  
ANISOU  785  N   VAL B  34    18939  15178  12608   1067  -4392   3615       N  
ATOM    786  CA  VAL B  34      77.867   7.083  26.066  1.00126.89           C  
ANISOU  786  CA  VAL B  34    20028  14931  13252   1094  -4674   3793       C  
ATOM    787  C   VAL B  34      76.351   6.935  25.932  1.00125.87           C  
ANISOU  787  C   VAL B  34    20083  14607  13135    434  -4544   3915       C  
ATOM    788  O   VAL B  34      75.866   6.179  25.086  1.00126.90           O  
ANISOU  788  O   VAL B  34    20551  14202  13465    408  -4647   3842       O  
ATOM    789  CB  VAL B  34      78.412   6.057  27.077  1.00132.94           C  
ANISOU  789  CB  VAL B  34    21224  15373  13916   1262  -5080   4205       C  
ATOM    790  CG1 VAL B  34      77.962   4.652  26.706  1.00137.26           C  
ANISOU  790  CG1 VAL B  34    22447  15060  14644   1269  -5396   4347       C  
ATOM    791  CG2 VAL B  34      79.929   6.137  27.152  1.00134.61           C  
ANISOU  791  CG2 VAL B  34    21221  15812  14112   1965  -5236   4084       C  
ATOM    792  N   LEU B  35      75.610   7.672  26.760  1.00121.52           N  
ANISOU  792  N   LEU B  35    19833  14404  11935   -234  -3491   4556       N  
ATOM    793  CA  LEU B  35      74.152   7.672  26.695  1.00119.61           C  
ANISOU  793  CA  LEU B  35    19553  14198  11695   -807  -3267   4558       C  
ATOM    794  C   LEU B  35      73.626   8.460  25.486  1.00114.80           C  
ANISOU  794  C   LEU B  35    18670  13648  11299   -713  -3007   4095       C  
ATOM    795  O   LEU B  35      72.599   8.092  24.913  1.00115.32           O  
ANISOU  795  O   LEU B  35    18973  13309  11533   -864  -3060   4053       O  
ATOM    796  CB  LEU B  35      73.559   8.263  27.975  1.00119.47           C  
ANISOU  796  CB  LEU B  35    19307  14739  11349  -1317  -3068   4797       C  
ATOM    797  CG  LEU B  35      72.047   8.113  28.154  1.00123.92           C  
ANISOU  797  CG  LEU B  35    20249  15023  11811  -1875  -3218   5255       C  
ATOM    798  CD1 LEU B  35      71.631   6.656  28.018  1.00126.63           C  
ANISOU  798  CD1 LEU B  35    20537  15812  11763  -2191  -3204   5641       C  
ATOM    799  CD2 LEU B  35      71.606   8.671  29.499  1.00121.67           C  
ANISOU  799  CD2 LEU B  35    19810  14808  11611  -2310  -2974   5116       C  
ATOM    800  N   LEU B  36      74.330   9.527  25.099  1.00110.14           N  
ANISOU  800  N   LEU B  36    16701  13947  11202   -348  -2370   4161       N  
ATOM    801  CA  LEU B  36      73.925  10.349  23.952  1.00105.86           C  
ANISOU  801  CA  LEU B  36    15907  13484  10832   -288  -2127   3763       C  
ATOM    802  C   LEU B  36      74.005   9.582  22.631  1.00106.88           C  
ANISOU  802  C   LEU B  36    16336  13062  11213    -47  -2281   3612       C  
ATOM    803  O   LEU B  36      73.109   9.699  21.789  1.00105.52           O  
ANISOU  803  O   LEU B  36    16197  12754  11141   -297  -2183   3500       O  
ATOM    804  CB  LEU B  36      74.738  11.647  23.867  1.00102.52           C  
ANISOU  804  CB  LEU B  36    15048  13516  10388      3  -1943   3464       C  
ATOM    805  CG  LEU B  36      74.381  12.631  22.735  1.00 98.17           C  
ANISOU  805  CG  LEU B  36    14230  13126   9946    -85  -1659   3129       C  
ATOM    806  CD1 LEU B  36      72.927  13.116  22.798  1.00 97.37           C  
ANISOU  806  CD1 LEU B  36    14155  13035   9806   -567  -1515   3200       C  
ATOM    807  CD2 LEU B  36      75.327  13.819  22.713  1.00 95.20           C  
ANISOU  807  CD2 LEU B  36    13440  13241   9490     -3  -1463   2906       C  
ATOM    808  N   VAL B  37      75.074   8.801  22.461  1.00109.74           N  
ANISOU  808  N   VAL B  37    16870  13527  11301    546  -2676   3562       N  
ATOM    809  CA  VAL B  37      75.225   7.919  21.298  1.00111.97           C  
ANISOU  809  CA  VAL B  37    17524  13233  11785    848  -2879   3409       C  
ATOM    810  C   VAL B  37      74.055   6.928  21.191  1.00114.98           C  
ANISOU  810  C   VAL B  37    18408  13049  12229    406  -3077   3633       C  
ATOM    811  O   VAL B  37      73.517   6.717  20.103  1.00114.29           O  
ANISOU  811  O   VAL B  37    18438  12708  12279    329  -3058   3427       O  
ATOM    812  CB  VAL B  37      76.600   7.198  21.308  1.00115.61           C  
ANISOU  812  CB  VAL B  37    18139  13510  12276   1523  -3146   3376       C  
ATOM    813  CG1 VAL B  37      76.578   5.921  20.469  1.00120.26           C  
ANISOU  813  CG1 VAL B  37    19338  13336  13020   1782  -3489   3353       C  
ATOM    814  CG2 VAL B  37      77.683   8.140  20.815  1.00112.72           C  
ANISOU  814  CG2 VAL B  37    17280  13624  11924   1966  -2933   3013       C  
ATOM    815  N   ILE B  38      73.661   6.344  22.324  1.00120.30           N  
ANISOU  815  N   ILE B  38    19458  13314  12938    -19  -3357   4365       N  
ATOM    816  CA  ILE B  38      72.486   5.468  22.398  1.00123.53           C  
ANISOU  816  CA  ILE B  38    20291  13278  13365   -593  -3529   4649       C  
ATOM    817  C   ILE B  38      71.227   6.157  21.855  1.00119.85           C  
ANISOU  817  C   ILE B  38    19519  13099  12919  -1079  -3230   4499       C  
ATOM    818  O   ILE B  38      70.542   5.607  20.996  1.00120.98           O  
ANISOU  818  O   ILE B  38    19918  12842  13207  -1239  -3340   4403       O  
ATOM    819  CB  ILE B  38      72.201   5.028  23.846  1.00127.19           C  
ANISOU  819  CB  ILE B  38    20921  13803  13601  -1054  -3659   5198       C  
ATOM    820  CG1 ILE B  38      73.396   4.262  24.416  1.00132.28           C  
ANISOU  820  CG1 ILE B  38    21988  14061  14211   -646  -4049   5460       C  
ATOM    821  CG2 ILE B  38      70.938   4.182  23.906  1.00130.05           C  
ANISOU  821  CG2 ILE B  38    21558  13914  13940  -1800  -3745   5505       C  
ATOM    822  CD1 ILE B  38      73.301   4.001  25.903  1.00135.32           C  
ANISOU  822  CD1 ILE B  38    22835  13737  14842     10  -4385   5212       C  
ATOM    823  N   VAL B  39      70.943   7.361  22.350  1.00118.92           N  
ANISOU  823  N   VAL B  39    18158  13513  13512  -1389  -2602   5091       N  
ATOM    824  CA  VAL B  39      69.755   8.122  21.949  1.00115.96           C  
ANISOU  824  CA  VAL B  39    17457  13484  13118  -1808  -2320   4978       C  
ATOM    825  C   VAL B  39      69.778   8.488  20.457  1.00112.80           C  
ANISOU  825  C   VAL B  39    16956  12976  12927  -1537  -2223   4535       C  
ATOM    826  O   VAL B  39      68.737   8.457  19.790  1.00112.67           O  
ANISOU  826  O   VAL B  39    16951  12884  12976  -1870  -2194   4480       O  
ATOM    827  CB  VAL B  39      69.625   9.429  22.752  1.00113.03           C  
ANISOU  827  CB  VAL B  39    16574  13861  12512  -1970  -1987   4999       C  
ATOM    828  CG1 VAL B  39      69.979  10.626  21.883  1.00108.26           C  
ANISOU  828  CG1 VAL B  39    15533  13647  11954  -1955  -1661   4635       C  
ATOM    829  CG2 VAL B  39      68.219   9.569  23.318  1.00116.28           C  
ANISOU  829  CG2 VAL B  39    17016  14478  12689  -2558  -1987   5421       C  
ATOM    830  N   LEU B  40      70.957   8.818  19.934  1.00110.18           N  
ANISOU  830  N   LEU B  40    16686  12687  12490   -878  -2387   4144       N  
ATOM    831  CA  LEU B  40      71.096   9.123  18.510  1.00107.99           C  
ANISOU  831  CA  LEU B  40    16353  12307  12371   -593  -2319   3755       C  
ATOM    832  C   LEU B  40      70.707   7.935  17.637  1.00111.68           C  
ANISOU  832  C   LEU B  40    17331  12127  12976   -664  -2613   3752       C  
ATOM    833  O   LEU B  40      69.799   8.045  16.816  1.00111.24           O  
ANISOU  833  O   LEU B  40    17275  12029  12962  -1034  -2575   3705       O  
ATOM    834  CB  LEU B  40      72.514   9.594  18.170  1.00106.75           C  
ANISOU  834  CB  LEU B  40    16042  12273  12244     33  -2283   3504       C  
ATOM    835  CG  LEU B  40      73.018  10.911  18.761  1.00103.43           C  
ANISOU  835  CG  LEU B  40    15140  12462  11698     91  -2028   3468       C  
ATOM    836  CD1 LEU B  40      74.264  11.360  18.013  1.00102.27           C  
ANISOU  836  CD1 LEU B  40    14786  12474  11597    627  -1971   3181       C  
ATOM    837  CD2 LEU B  40      71.954  11.998  18.732  1.00 99.87           C  
ANISOU  837  CD2 LEU B  40    14358  12405  11184   -311  -1742   3420       C  
ATOM    838  N   LEU B  41      71.376   6.800  17.832  1.00122.93           N  
ANISOU  838  N   LEU B  41    19865  12004  14837    -73  -3813   3700       N  
ATOM    839  CA  LEU B  41      71.113   5.589  17.050  1.00127.35           C  
ANISOU  839  CA  LEU B  41    21018  11842  15527    -72  -4159   3660       C  
ATOM    840  C   LEU B  41      69.664   5.113  17.191  1.00129.41           C  
ANISOU  840  C   LEU B  41    21487  11895  15789   -837  -4264   3922       C  
ATOM    841  O   LEU B  41      69.030   4.751  16.198  1.00130.30           O  
ANISOU  841  O   LEU B  41    21798  11711  16000   -974  -4364   3735       O  
ATOM    842  CB  LEU B  41      72.053   4.460  17.476  1.00132.53           C  
ANISOU  842  CB  LEU B  41    22181  11957  16217    388  -4534   3764       C  
ATOM    843  CG  LEU B  41      73.550   4.718  17.286  1.00131.61           C  
ANISOU  843  CG  LEU B  41    21829  12097  16080   1171  -4466   3529       C  
ATOM    844  CD1 LEU B  41      74.300   3.409  17.097  1.00137.67           C  
ANISOU  844  CD1 LEU B  41    23167  12235  16907   1724  -4886   3535       C  
ATOM    845  CD2 LEU B  41      73.791   5.648  16.107  1.00127.45           C  
ANISOU  845  CD2 LEU B  41    20883  11963  15581   1507  -4171   3067       C  
ATOM    846  N   ALA B  42      69.145   5.131  18.419  1.00136.94           N  
ANISOU  846  N   ALA B  42    21608  12798  17624  -2489  -4587   5757       N  
ATOM    847  CA  ALA B  42      67.760   4.742  18.692  1.00139.29           C  
ANISOU  847  CA  ALA B  42    21993  13054  17875  -3272  -4648   6050       C  
ATOM    848  C   ALA B  42      66.775   5.737  18.097  1.00135.12           C  
ANISOU  848  C   ALA B  42    20953  13053  17335  -3538  -4322   5838       C  
ATOM    849  O   ALA B  42      65.735   5.346  17.572  1.00136.82           O  
ANISOU  849  O   ALA B  42    21296  13075  17614  -3932  -4433   5818       O  
ATOM    850  CB  ALA B  42      67.530   4.601  20.183  1.00141.37           C  
ANISOU  850  CB  ALA B  42    22201  13573  17939  -3701  -4636   6537       C  
ATOM    851  N   GLY B  43      67.111   7.020  18.186  1.00123.12           N  
ANISOU  851  N   GLY B  43    18356  13051  15374  -3168  -2992   5225       N  
ATOM    852  CA  GLY B  43      66.294   8.089  17.613  1.00118.95           C  
ANISOU  852  CA  GLY B  43    17337  13020  14838  -3267  -2680   4975       C  
ATOM    853  C   GLY B  43      66.251   8.065  16.095  1.00117.87           C  
ANISOU  853  C   GLY B  43    17306  12613  14868  -3034  -2739   4597       C  
ATOM    854  O   GLY B  43      65.179   8.195  15.500  1.00118.20           O  
ANISOU  854  O   GLY B  43    17267  12715  14929  -3402  -2735   4558       O  
ATOM    855  N   SER B  44      67.422   7.901  15.478  1.00116.87           N  
ANISOU  855  N   SER B  44    17984  11331  15092  -1669  -2744   3409       N  
ATOM    856  CA  SER B  44      67.548   7.776  14.027  1.00117.31           C  
ANISOU  856  CA  SER B  44    18274  11030  15268  -1362  -2870   3059       C  
ATOM    857  C   SER B  44      66.684   6.645  13.502  1.00121.74           C  
ANISOU  857  C   SER B  44    19285  11073  15896  -1787  -3189   3141       C  
ATOM    858  O   SER B  44      65.887   6.834  12.585  1.00121.04           O  
ANISOU  858  O   SER B  44    19069  11099  15822  -2072  -3147   3021       O  
ATOM    859  CB  SER B  44      69.001   7.505  13.632  1.00118.76           C  
ANISOU  859  CB  SER B  44    18731  10894  15498   -699  -3017   2895       C  
ATOM    860  OG  SER B  44      69.858   8.546  14.055  1.00114.84           O  
ANISOU  860  OG  SER B  44    17792  10898  14944   -293  -2733   2752       O  
ATOM    861  N   TYR B  45      66.841   5.472  14.103  1.00140.97           N  
ANISOU  861  N   TYR B  45    22690  10985  19887  -2108  -4956   3612       N  
ATOM    862  CA  TYR B  45      66.162   4.276  13.637  1.00146.06           C  
ANISOU  862  CA  TYR B  45    23871  11020  20607  -2500  -5331   3675       C  
ATOM    863  C   TYR B  45      64.681   4.259  14.013  1.00147.55           C  
ANISOU  863  C   TYR B  45    23900  11437  20727  -3370  -5324   4034       C  
ATOM    864  O   TYR B  45      63.900   3.522  13.418  1.00151.94           O  
ANISOU  864  O   TYR B  45    24833  11567  21331  -3838  -5629   4119       O  
ATOM    865  CB  TYR B  45      66.893   3.029  14.147  1.00151.66           C  
ANISOU  865  CB  TYR B  45    25281  10965  21378  -2260  -5748   3802       C  
ATOM    866  CG  TYR B  45      68.211   2.731  13.433  1.00151.78           C  
ANISOU  866  CG  TYR B  45    25509  10707  21454  -1347  -5823   3394       C  
ATOM    867  CD1 TYR B  45      69.053   3.773  12.986  1.00146.25           C  
ANISOU  867  CD1 TYR B  45    24245  10615  20709   -796  -5436   3067       C  
ATOM    868  CD2 TYR B  45      68.627   1.401  13.223  1.00158.20           C  
ANISOU  868  CD2 TYR B  45    27102  10656  22349  -1027  -6298   3347       C  
ATOM    869  CE1 TYR B  45      70.259   3.502  12.334  1.00146.98           C  
ANISOU  869  CE1 TYR B  45    24459  10573  20814     15  -5481   2714       C  
ATOM    870  CE2 TYR B  45      69.836   1.115  12.575  1.00159.05           C  
ANISOU  870  CE2 TYR B  45    27366  10587  22477   -122  -6357   2952       C  
ATOM    871  CZ  TYR B  45      70.645   2.171  12.134  1.00153.35           C  
ANISOU  871  CZ  TYR B  45    25985  10594  21687    381  -5926   2644       C  
ATOM    872  OH  TYR B  45      71.835   1.891  11.496  1.00154.74           O  
ANISOU  872  OH  TYR B  45    26242  10706  21845   1246  -5963   2276       O  
ATOM    873  N   LEU B  46      64.294   5.078  14.988  1.00144.00           N  
ANISOU  873  N   LEU B  46    21993  12997  19725  -4991  -4649   5703       N  
ATOM    874  CA  LEU B  46      62.887   5.202  15.349  1.00145.50           C  
ANISOU  874  CA  LEU B  46    21916  13554  19812  -5755  -4590   5994       C  
ATOM    875  C   LEU B  46      62.191   6.236  14.470  1.00141.85           C  
ANISOU  875  C   LEU B  46    20980  13559  19359  -5763  -4351   5687       C  
ATOM    876  O   LEU B  46      61.031   6.055  14.097  1.00144.33           O  
ANISOU  876  O   LEU B  46    21282  13882  19675  -6278  -4472   5743       O  
ATOM    877  CB  LEU B  46      62.720   5.544  16.835  1.00145.23           C  
ANISOU  877  CB  LEU B  46    21532  14069  19581  -6028  -4369   6383       C  
ATOM    878  CG  LEU B  46      61.416   5.116  17.534  1.00150.45           C  
ANISOU  878  CG  LEU B  46    22214  14847  20104  -6911  -4497   6875       C  
ATOM    879  CD1 LEU B  46      61.296   3.596  17.655  1.00156.82           C  
ANISOU  879  CD1 LEU B  46    23759  14867  20958  -7183  -4958   7216       C  
ATOM    880  CD2 LEU B  46      61.289   5.764  18.908  1.00149.50           C  
ANISOU  880  CD2 LEU B  46    21520  15566  19719  -7188  -4151   7158       C  
ATOM    881  N   ALA B  47      62.911   7.308  14.135  1.00123.25           N  
ANISOU  881  N   ALA B  47    18584  12262  15985  -4387  -2830   3713       N  
ATOM    882  CA  ALA B  47      62.391   8.392  13.287  1.00119.43           C  
ANISOU  882  CA  ALA B  47    17653  12222  15502  -4276  -2590   3409       C  
ATOM    883  C   ALA B  47      62.088   7.948  11.857  1.00120.94           C  
ANISOU  883  C   ALA B  47    18099  12060  15793  -4305  -2810   3148       C  
ATOM    884  O   ALA B  47      61.122   8.414  11.257  1.00121.51           O  
ANISOU  884  O   ALA B  47    17929  12408  15833  -4696  -2796   3155       O  
ATOM    885  CB  ALA B  47      63.350   9.578  13.279  1.00114.18           C  
ANISOU  885  CB  ALA B  47    16689  11864  14829  -3651  -2291   3146       C  
ATOM    886  N   VAL B  48      62.921   7.057  11.320  1.00130.29           N  
ANISOU  886  N   VAL B  48    20570  10983  17953  -3122  -3268   1311       N  
ATOM    887  CA  VAL B  48      62.709   6.491   9.990  1.00133.19           C  
ANISOU  887  CA  VAL B  48    21328  10893  18387  -3166  -3559   1071       C  
ATOM    888  C   VAL B  48      61.352   5.798   9.907  1.00137.71           C  
ANISOU  888  C   VAL B  48    22015  11356  18951  -3965  -3809   1326       C  
ATOM    889  O   VAL B  48      60.527   6.183   9.086  1.00137.07           O  
ANISOU  889  O   VAL B  48    21636  11607  18837  -4219  -3754   1227       O  
ATOM    890  CB  VAL B  48      63.865   5.547   9.564  1.00136.12           C  
ANISOU  890  CB  VAL B  48    22327  10559  18832  -2697  -3842    893       C  
ATOM    891  CG1 VAL B  48      63.464   4.685   8.380  1.00140.37           C  
ANISOU  891  CG1 VAL B  48    23362  10556  19417  -2828  -4206    666       C  
ATOM    892  CG2 VAL B  48      65.098   6.352   9.219  1.00132.07           C  
ANISOU  892  CG2 VAL B  48    21608  10273  18300  -1938  -3588    591       C  
ATOM    893  N   LEU B  49      61.103   4.812  10.773  1.00158.08           N  
ANISOU  893  N   LEU B  49    24789  11905  23369  -5928  -5562   3046       N  
ATOM    894  CA  LEU B  49      59.843   4.060  10.731  1.00163.16           C  
ANISOU  894  CA  LEU B  49    25556  12445  23994  -6763  -5830   3314       C  
ATOM    895  C   LEU B  49      58.612   4.921  11.036  1.00161.68           C  
ANISOU  895  C   LEU B  49    24635  13117  23678  -7273  -5547   3518       C  
ATOM    896  O   LEU B  49      57.491   4.550  10.695  1.00165.54           O  
ANISOU  896  O   LEU B  49    25079  13684  24136  -7940  -5728   3674       O  
ATOM    897  CB  LEU B  49      59.894   2.806  11.624  1.00169.16           C  
ANISOU  897  CB  LEU B  49    26910  12585  24777  -7161  -6194   3710       C  
ATOM    898  CG  LEU B  49      59.698   2.798  13.147  1.00171.72           C  
ANISOU  898  CG  LEU B  49    27099  13164  24983  -7756  -6157   4291       C  
ATOM    899  CD1 LEU B  49      58.358   3.398  13.579  1.00172.14           C  
ANISOU  899  CD1 LEU B  49    26491  14033  24882  -8484  -5950   4562       C  
ATOM    900  CD2 LEU B  49      59.813   1.361  13.662  1.00179.23           C  
ANISOU  900  CD2 LEU B  49    28893  13209  25997  -8146  -6687   4602       C  
ATOM    901  N   ALA B  50      58.835   6.068  11.670  1.00142.96           N  
ANISOU  901  N   ALA B  50    20996  14531  18790  -7501  -4058   3855       N  
ATOM    902  CA  ALA B  50      57.763   7.014  11.975  1.00141.58           C  
ANISOU  902  CA  ALA B  50    20104  15211  18478  -7828  -3766   3980       C  
ATOM    903  C   ALA B  50      57.378   7.850  10.760  1.00139.00           C  
ANISOU  903  C   ALA B  50    19455  15188  18171  -7638  -3671   3626       C  
ATOM    904  O   ALA B  50      56.208   8.201  10.592  1.00140.61           O  
ANISOU  904  O   ALA B  50    19244  15892  18291  -8078  -3641   3723       O  
ATOM    905  CB  ALA B  50      58.175   7.926  13.125  1.00137.63           C  
ANISOU  905  CB  ALA B  50    19169  15262  17863  -7508  -3369   4068       C  
ATOM    906  N   GLU B  51      58.369   8.147   9.917  1.00125.76           N  
ANISOU  906  N   GLU B  51    18978  13020  15786  -6097  -2977   1183       N  
ATOM    907  CA  GLU B  51      58.249   9.122   8.830  1.00122.19           C  
ANISOU  907  CA  GLU B  51    18224  12873  15331  -5732  -2819    834       C  
ATOM    908  C   GLU B  51      58.159   8.513   7.432  1.00124.25           C  
ANISOU  908  C   GLU B  51    18891  12667  15652  -5692  -3122    543       C  
ATOM    909  O   GLU B  51      57.563   9.111   6.536  1.00123.56           O  
ANISOU  909  O   GLU B  51    18545  12880  15524  -5710  -3100    369       O  
ATOM    910  CB  GLU B  51      59.449  10.064   8.862  1.00116.96           C  
ANISOU  910  CB  GLU B  51    17450  12311  14680  -5030  -2530    632       C  
ATOM    911  CG  GLU B  51      59.452  11.051  10.011  1.00114.21           C  
ANISOU  911  CG  GLU B  51    16626  12523  14244  -4971  -2195    801       C  
ATOM    912  CD  GLU B  51      58.941  12.423   9.616  1.00110.39           C  
ANISOU  912  CD  GLU B  51    15651  12582  13709  -4678  -1919    606       C  
ATOM    913  OE1 GLU B  51      59.478  13.024   8.652  1.00107.25           O  
ANISOU  913  OE1 GLU B  51    15306  12094  13351  -4187  -1835    330       O  
ATOM    914  OE2 GLU B  51      58.017  12.916  10.291  1.00110.97           O  
ANISOU  914  OE2 GLU B  51    15283  13197  13685  -4933  -1785    747       O  
ATOM    915  N   ARG B  52      58.750   7.333   7.258  1.00147.68           N  
ANISOU  915  N   ARG B  52    23299  13189  19624  -5358  -2996  -1934       N  
ATOM    916  CA  ARG B  52      58.982   6.721   5.944  1.00150.10           C  
ANISOU  916  CA  ARG B  52    24085  12983  19963  -5213  -3297  -2269       C  
ATOM    917  C   ARG B  52      57.771   6.687   5.003  1.00152.43           C  
ANISOU  917  C   ARG B  52    24247  13463  20207  -5666  -3471  -2354       C  
ATOM    918  O   ARG B  52      57.910   6.919   3.798  1.00152.23           O  
ANISOU  918  O   ARG B  52    24360  13335  20146  -5382  -3556  -2716       O  
ATOM    919  CB  ARG B  52      59.540   5.312   6.124  1.00155.14           C  
ANISOU  919  CB  ARG B  52    25462  12802  20684  -5305  -3684  -2208       C  
ATOM    920  CG  ARG B  52      60.528   4.875   5.063  1.00157.38           C  
ANISOU  920  CG  ARG B  52    26301  12516  20981  -4911  -3953  -2633       C  
ATOM    921  CD  ARG B  52      61.259   3.633   5.536  1.00158.22           C  
ANISOU  921  CD  ARG B  52    26885  12088  21144  -4330  -4031  -2728       C  
ATOM    922  NE  ARG B  52      62.127   3.054   4.515  1.00161.38           N  
ANISOU  922  NE  ARG B  52    27857  11932  21527  -3899  -4310  -3171       N  
ATOM    923  CZ  ARG B  52      62.903   1.988   4.705  1.00165.53           C  
ANISOU  923  CZ  ARG B  52    29050  11738  22107  -3543  -4606  -3285       C  
ATOM    924  NH1 ARG B  52      62.935   1.374   5.883  1.00167.04           N  
ANISOU  924  NH1 ARG B  52    29444  11641  22382  -3585  -4684  -2953       N  
ATOM    925  NH2 ARG B  52      63.655   1.532   3.712  1.00168.68           N  
ANISOU  925  NH2 ARG B  52    29933  11705  22452  -3109  -4841  -3743       N  
ATOM    926  N   GLY B  53      56.593   6.399   5.551  1.00161.76           N  
ANISOU  926  N   GLY B  53    25478  15512  20470  -8331  -4751  -2495       N  
ATOM    927  CA  GLY B  53      55.391   6.225   4.733  1.00165.01           C  
ANISOU  927  CA  GLY B  53    25761  16107  20828  -8837  -4974  -2542       C  
ATOM    928  C   GLY B  53      54.524   7.460   4.569  1.00162.19           C  
ANISOU  928  C   GLY B  53    24640  16612  20371  -8839  -4702  -2557       C  
ATOM    929  O   GLY B  53      53.385   7.366   4.106  1.00165.46           O  
ANISOU  929  O   GLY B  53    24856  17285  20725  -9329  -4889  -2525       O  
ATOM    930  N   ALA B  54      55.061   8.618   4.941  1.00140.96           N  
ANISOU  930  N   ALA B  54    20546  16723  16291  -8459  -4517   -955       N  
ATOM    931  CA  ALA B  54      54.307   9.863   4.913  1.00138.88           C  
ANISOU  931  CA  ALA B  54    19590  17244  15934  -8429  -4274   -939       C  
ATOM    932  C   ALA B  54      54.785  10.772   3.786  1.00134.76           C  
ANISOU  932  C   ALA B  54    19020  16791  15391  -7781  -4130  -1288       C  
ATOM    933  O   ALA B  54      55.866  10.554   3.238  1.00133.54           O  
ANISOU  933  O   ALA B  54    19322  16141  15276  -7381  -4185  -1525       O  
ATOM    934  CB  ALA B  54      54.417  10.573   6.254  1.00136.80           C  
ANISOU  934  CB  ALA B  54    18851  17498  15628  -8403  -3931   -675       C  
ATOM    935  N   PRO B  55      53.958  11.766   3.404  1.00136.51           N  
ANISOU  935  N   PRO B  55    17888  19071  14909  -8176  -5050     30       N  
ATOM    936  CA  PRO B  55      54.338  12.846   2.488  1.00132.33           C  
ANISOU  936  CA  PRO B  55    17113  18835  14333  -7595  -4820   -171       C  
ATOM    937  C   PRO B  55      55.366  13.836   3.062  1.00127.49           C  
ANISOU  937  C   PRO B  55    16546  18137  13758  -7020  -4514   -234       C  
ATOM    938  O   PRO B  55      55.080  15.027   3.157  1.00124.74           O  
ANISOU  938  O   PRO B  55    15853  18176  13368  -6696  -4292   -265       O  
ATOM    939  CB  PRO B  55      52.998  13.557   2.225  1.00133.14           C  
ANISOU  939  CB  PRO B  55    16556  19678  14354  -7760  -4706    -17       C  
ATOM    940  CG  PRO B  55      51.941  12.573   2.611  1.00138.75           C  
ANISOU  940  CG  PRO B  55    17220  20470  15030  -8464  -5023    120       C  
ATOM    941  CD  PRO B  55      52.534  11.862   3.774  1.00140.85           C  
ANISOU  941  CD  PRO B  55    18053  20078  15386  -8790  -5211    214       C  
ATOM    942  N   GLY B  56      56.560  13.358   3.409  1.00114.15           N  
ANISOU  942  N   GLY B  56    15547  15185  12639  -5365  -3480   -285       N  
ATOM    943  CA  GLY B  56      57.544  14.199   4.093  1.00109.96           C  
ANISOU  943  CA  GLY B  56    14963  14686  12132  -4895  -3186   -301       C  
ATOM    944  C   GLY B  56      59.012  13.943   3.821  1.00108.71           C  
ANISOU  944  C   GLY B  56    15220  14069  12016  -4528  -3183   -444       C  
ATOM    945  O   GLY B  56      59.395  12.885   3.324  1.00111.37           O  
ANISOU  945  O   GLY B  56    15992  13933  12390  -4614  -3412   -500       O  
ATOM    946  N   ALA B  57      59.823  14.935   4.204  1.00102.28           N  
ANISOU  946  N   ALA B  57    14320  13494  11046  -3467  -2289     30       N  
ATOM    947  CA  ALA B  57      61.294  15.011   3.981  1.00100.21           C  
ANISOU  947  CA  ALA B  57    14262  13013  10799  -3033  -2168    -68       C  
ATOM    948  C   ALA B  57      62.106  13.746   4.305  1.00102.15           C  
ANISOU  948  C   ALA B  57    14902  12801  11109  -3010  -2310    -44       C  
ATOM    949  O   ALA B  57      61.644  12.852   5.028  1.00104.16           O  
ANISOU  949  O   ALA B  57    15246  12908  11421  -3340  -2419    163       O  
ATOM    950  CB  ALA B  57      61.904  16.257   4.692  1.00 96.48           C  
ANISOU  950  CB  ALA B  57    13468  12873  10316  -2787  -1865      6       C  
ATOM    951  N   GLN B  58      63.333  13.715   3.785  1.00107.48           N  
ANISOU  951  N   GLN B  58    15739  13810  11287  -1918   -898  -1229       N  
ATOM    952  CA  GLN B  58      64.084  12.469   3.570  1.00110.69           C  
ANISOU  952  CA  GLN B  58    16620  13721  11715  -1777  -1128  -1354       C  
ATOM    953  C   GLN B  58      64.419  11.642   4.823  1.00112.77           C  
ANISOU  953  C   GLN B  58    17115  13650  12082  -1962  -1268  -1132       C  
ATOM    954  O   GLN B  58      65.345  10.824   4.799  1.00115.82           O  
ANISOU  954  O   GLN B  58    17939  13571  12496  -1785  -1482  -1224       O  
ATOM    955  CB  GLN B  58      65.349  12.742   2.732  1.00109.79           C  
ANISOU  955  CB  GLN B  58    16558  13645  11514  -1208  -1007  -1588       C  
ATOM    956  CG  GLN B  58      65.686  11.642   1.731  1.00112.92           C  
ANISOU  956  CG  GLN B  58    17311  13782  11811   -970  -1197  -1907       C  
ATOM    957  CD  GLN B  58      67.109  11.719   1.214  1.00113.76           C  
ANISOU  957  CD  GLN B  58    17544  13838  11841   -399  -1133  -2094       C  
ATOM    958  OE1 GLN B  58      67.373  12.339   0.185  1.00114.31           O  
ANISOU  958  OE1 GLN B  58    17613  14075  11745    -66  -1068  -2346       O  
ATOM    959  NE2 GLN B  58      68.034  11.083   1.925  1.00114.28           N  
ANISOU  959  NE2 GLN B  58    17699  13720  12002   -271  -1154  -1965       N  
ATOM    960  N   LEU B  59      63.663  11.835   5.903  1.00103.39           N  
ANISOU  960  N   LEU B  59    15720  11091  12473  -1884  -1386   -638       N  
ATOM    961  CA  LEU B  59      63.765  10.952   7.062  1.00105.69           C  
ANISOU  961  CA  LEU B  59    16220  11114  12823  -2109  -1518   -380       C  
ATOM    962  C   LEU B  59      63.151   9.603   6.690  1.00110.66           C  
ANISOU  962  C   LEU B  59    17312  11237  13497  -2452  -1894   -369       C  
ATOM    963  O   LEU B  59      62.243   9.094   7.350  1.00113.17           O  
ANISOU  963  O   LEU B  59    17641  11528  13829  -3007  -2024   -103       O  
ATOM    964  CB  LEU B  59      63.122  11.601   8.288  1.00104.08           C  
ANISOU  964  CB  LEU B  59    15611  11344  12591  -2428  -1321    -89       C  
ATOM    965  CG  LEU B  59      63.719  12.934   8.741  1.00 99.93           C  
ANISOU  965  CG  LEU B  59    14734  11212  12022  -2094  -1007   -106       C  
ATOM    966  CD1 LEU B  59      62.986  13.463   9.964  1.00 99.48           C  
ANISOU  966  CD1 LEU B  59    14378  11513  11908  -2387   -861    163       C  
ATOM    967  CD2 LEU B  59      65.205  12.787   9.029  1.00 99.54           C  
ANISOU  967  CD2 LEU B  59    14892  10933  11995  -1646  -1010   -188       C  
ATOM    968  N   ILE B  60      63.675   9.042   5.606  1.00128.34           N  
ANISOU  968  N   ILE B  60    20282  12330  16152  -1641  -2371  -2540       N  
ATOM    969  CA  ILE B  60      63.111   7.874   4.967  1.00132.94           C  
ANISOU  969  CA  ILE B  60    21322  12440  16748  -1873  -2735  -2667       C  
ATOM    970  C   ILE B  60      64.195   6.819   4.737  1.00136.03           C  
ANISOU  970  C   ILE B  60    22280  12250  17155  -1375  -2955  -2906       C  
ATOM    971  O   ILE B  60      63.899   5.671   4.400  1.00141.01           O  
ANISOU  971  O   ILE B  60    23460  12300  17818  -1526  -3332  -2991       O  
ATOM    972  CB  ILE B  60      62.383   8.251   3.645  1.00132.13           C  
ANISOU  972  CB  ILE B  60    21020  12623  16561  -1947  -2710  -2900       C  
ATOM    973  CG1 ILE B  60      63.360   8.833   2.613  1.00130.19           C  
ANISOU  973  CG1 ILE B  60    20766  12489  16212  -1301  -2564  -3267       C  
ATOM    974  CG2 ILE B  60      61.234   9.234   3.918  1.00129.05           C  
ANISOU  974  CG2 ILE B  60    20017  12873  16145  -2296  -2467  -2688       C  
ATOM    975  CD1 ILE B  60      62.839   8.803   1.177  1.00131.79           C  
ANISOU  975  CD1 ILE B  60    21063  12711  16299  -1332  -2703  -3558       C  
ATOM    976  N   THR B  61      65.449   7.225   4.918  1.00142.83           N  
ANISOU  976  N   THR B  61    22576  13034  18658    198  -2184  -3598       N  
ATOM    977  CA  THR B  61      66.571   6.292   4.990  1.00146.21           C  
ANISOU  977  CA  THR B  61    23478  12963  19114    665  -2385  -3709       C  
ATOM    978  C   THR B  61      67.326   6.482   6.307  1.00144.91           C  
ANISOU  978  C   THR B  61    23167  12886  19006    731  -2270  -3397       C  
ATOM    979  O   THR B  61      67.327   7.580   6.879  1.00140.40           O  
ANISOU  979  O   THR B  61    22058  12873  18413    634  -1942  -3219       O  
ATOM    980  CB  THR B  61      67.530   6.478   3.813  1.00146.16           C  
ANISOU  980  CB  THR B  61    23491  13056  18988   1398  -2287  -4121       C  
ATOM    981  OG1 THR B  61      68.068   7.804   3.837  1.00141.76           O  
ANISOU  981  OG1 THR B  61    22412  13128  18323   1432  -1954  -4222       O  
ATOM    982  CG2 THR B  61      66.802   6.265   2.495  1.00151.71           C  
ANISOU  982  CG2 THR B  61    24823  13170  19650   1588  -2657  -4465       C  
ATOM    983  N   TYR B  62      67.955   5.408   6.786  1.00144.58           N  
ANISOU  983  N   TYR B  62    22907  10800  21227    361  -2401  -1238       N  
ATOM    984  CA  TYR B  62      68.734   5.458   8.026  1.00144.14           C  
ANISOU  984  CA  TYR B  62    22776  10791  21201    513  -2344   -964       C  
ATOM    985  C   TYR B  62      69.967   6.373   7.936  1.00140.49           C  
ANISOU  985  C   TYR B  62    21863  10858  20659   1132  -2014  -1132       C  
ATOM    986  O   TYR B  62      70.112   7.268   8.773  1.00136.47           O  
ANISOU  986  O   TYR B  62    20869  10856  20126    999  -1729   -930       O  
ATOM    987  CB  TYR B  62      69.132   4.053   8.503  1.00150.29           C  
ANISOU  987  CB  TYR B  62    24249  10801  22053    635  -2778   -872       C  
ATOM    988  CG  TYR B  62      67.974   3.145   8.877  1.00154.42           C  
ANISOU  988  CG  TYR B  62    25212  10810  22651   -110  -3120   -569       C  
ATOM    989  CD1 TYR B  62      67.137   3.449   9.955  1.00152.86           C  
ANISOU  989  CD1 TYR B  62    24710  10920  22448   -794  -3001   -120       C  
ATOM    990  CD2 TYR B  62      67.737   1.962   8.168  1.00160.69           C  
ANISOU  990  CD2 TYR B  62    26752  10801  23502   -130  -3588   -725       C  
ATOM    991  CE1 TYR B  62      66.076   2.606  10.305  1.00157.41           C  
ANISOU  991  CE1 TYR B  62    25657  11088  23065  -1544  -3318    208       C  
ATOM    992  CE2 TYR B  62      66.682   1.108   8.512  1.00165.34           C  
ANISOU  992  CE2 TYR B  62    27782  10883  24156   -901  -3948   -402       C  
ATOM    993  CZ  TYR B  62      65.856   1.436   9.580  1.00163.67           C  
ANISOU  993  CZ  TYR B  62    27200  11059  23929  -1629  -3801     86       C  
ATOM    994  OH  TYR B  62      64.815   0.597   9.922  1.00168.74           O  
ANISOU  994  OH  TYR B  62    28217  11292  24604  -2442  -4140    442       O  
ATOM    995  N   PRO B  63      70.844   6.175   6.920  1.00140.74           N  
ANISOU  995  N   PRO B  63    21992  12378  19104   2615  -1500   -939       N  
ATOM    996  CA  PRO B  63      72.067   6.993   6.813  1.00138.29           C  
ANISOU  996  CA  PRO B  63    21239  12611  18695   3175  -1208  -1070       C  
ATOM    997  C   PRO B  63      71.823   8.504   6.733  1.00132.52           C  
ANISOU  997  C   PRO B  63    19859  12593  17899   2975   -802  -1024       C  
ATOM    998  O   PRO B  63      72.774   9.286   6.762  1.00130.85           O  
ANISOU  998  O   PRO B  63    19281  12844  17592   3357   -571  -1128       O  
ATOM    999  CB  PRO B  63      72.712   6.491   5.517  1.00141.74           C  
ANISOU  999  CB  PRO B  63    21926  12904  19026   3796  -1307  -1515       C  
ATOM   1000  CG  PRO B  63      72.180   5.117   5.344  1.00147.12           C  
ANISOU 1000  CG  PRO B  63    23328  12781  19789   3708  -1747  -1577       C  
ATOM   1001  CD  PRO B  63      70.770   5.187   5.826  1.00145.63           C  
ANISOU 1001  CD  PRO B  63    23175  12452  19706   2864  -1814  -1275       C  
ATOM   1002  N   ARG B  64      70.558   8.898   6.635  1.00115.07           N  
ANISOU 1002  N   ARG B  64    17805  11854  14061   1377  -1372   -293       N  
ATOM   1003  CA  ARG B  64      70.175  10.303   6.610  1.00110.23           C  
ANISOU 1003  CA  ARG B  64    16660  11827  13394   1196  -1039   -260       C  
ATOM   1004  C   ARG B  64      69.586  10.699   7.951  1.00108.37           C  
ANISOU 1004  C   ARG B  64    16251  11702  13221    722   -979     84       C  
ATOM   1005  O   ARG B  64      69.675  11.856   8.360  1.00104.85           O  
ANISOU 1005  O   ARG B  64    15393  11702  12744    646   -725    181       O  
ATOM   1006  CB  ARG B  64      69.161  10.568   5.494  1.00109.66           C  
ANISOU 1006  CB  ARG B  64    16581  11804  13279    992  -1029   -436       C  
ATOM   1007  N   ALA B  65      68.974   9.730   8.626  1.00105.42           N  
ANISOU 1007  N   ALA B  65    16300  10336  13419   -216  -1841    750       N  
ATOM   1008  CA  ALA B  65      68.418   9.945   9.953  1.00104.79           C  
ANISOU 1008  CA  ALA B  65    16092  10366  13357   -638  -1805   1101       C  
ATOM   1009  C   ALA B  65      69.526  10.111  10.996  1.00104.12           C  
ANISOU 1009  C   ALA B  65    15883  10434  13242   -344  -1722   1232       C  
ATOM   1010  O   ALA B  65      69.365  10.877  11.948  1.00101.59           O  
ANISOU 1010  O   ALA B  65    15227  10498  12874   -548  -1527   1411       O  
ATOM   1011  CB  ALA B  65      67.486   8.813  10.329  1.00108.99           C  
ANISOU 1011  CB  ALA B  65    17044  10422  13946  -1090  -2117   1309       C  
ATOM   1012  N   LEU B  66      70.643   9.401  10.807  1.00109.21           N  
ANISOU 1012  N   LEU B  66    16229  11262  14003    402  -1646   2453       N  
ATOM   1013  CA  LEU B  66      71.826   9.541  11.666  1.00108.88           C  
ANISOU 1013  CA  LEU B  66    16016  11436  13918    724  -1581   2557       C  
ATOM   1014  C   LEU B  66      72.365  10.958  11.585  1.00104.46           C  
ANISOU 1014  C   LEU B  66    14914  11490  13286    792  -1242   2467       C  
ATOM   1015  O   LEU B  66      72.687  11.565  12.606  1.00102.41           O  
ANISOU 1015  O   LEU B  66    14382  11545  12983    599  -1104   2653       O  
ATOM   1016  CB  LEU B  66      72.888   8.507  11.288  1.00112.56           C  
ANISOU 1016  CB  LEU B  66    16751  11632  14385   1351  -1776   2394       C  
ATOM   1017  CG  LEU B  66      72.475   7.038  11.403  1.00118.06           C  
ANISOU 1017  CG  LEU B  66    18108  11593  15158   1442  -2179   2398       C  
ATOM   1018  CD1 LEU B  66      73.621   6.124  10.999  1.00121.81           C  
ANISOU 1018  CD1 LEU B  66    18781  11894  15607   2216  -2335   2158       C  
ATOM   1019  CD2 LEU B  66      72.010   6.720  12.816  1.00120.43           C  
ANISOU 1019  CD2 LEU B  66    18708  11548  15501   1002  -2401   2814       C  
ATOM   1020  N   TRP B  67      72.447  11.479  10.364  1.00100.01           N  
ANISOU 1020  N   TRP B  67    14148  11817  12035    656  -1658   2090       N  
ATOM   1021  CA  TRP B  67      72.890  12.844  10.122  1.00 96.37           C  
ANISOU 1021  CA  TRP B  67    13219  11895  11501    678  -1364   2022       C  
ATOM   1022  C   TRP B  67      71.904  13.859  10.698  1.00 93.17           C  
ANISOU 1022  C   TRP B  67    12586  11713  11101    201  -1209   2184       C  
ATOM   1023  O   TRP B  67      72.312  14.925  11.149  1.00 90.81           O  
ANISOU 1023  O   TRP B  67    11964  11789  10749    175  -1024   2219       O  
ATOM   1024  CB  TRP B  67      73.120  13.072   8.622  1.00 96.21           C  
ANISOU 1024  CB  TRP B  67    13148  11986  11422    911  -1280   1734       C  
ATOM   1025  CG  TRP B  67      73.230  14.512   8.205  1.00 92.85           C  
ANISOU 1025  CG  TRP B  67    12319  12034  10926    811  -1013   1703       C  
ATOM   1026  CD1 TRP B  67      72.355  15.199   7.421  1.00 90.76           C  
ANISOU 1026  CD1 TRP B  67    11973  11859  10652    553   -913   1656       C  
ATOM   1027  CD2 TRP B  67      74.267  15.439   8.550  1.00 91.63           C  
ANISOU 1027  CD2 TRP B  67    11810  12309  10697    933   -844   1745       C  
ATOM   1028  NE1 TRP B  67      72.777  16.494   7.249  1.00 88.42           N  
ANISOU 1028  NE1 TRP B  67    11339  11971  10285    529   -701   1666       N  
ATOM   1029  CE2 TRP B  67      73.949  16.669   7.933  1.00 88.94           C  
ANISOU 1029  CE2 TRP B  67    11233  12251  10310    724   -655   1724       C  
ATOM   1030  CE3 TRP B  67      75.433  15.352   9.318  1.00 92.97           C  
ANISOU 1030  CE3 TRP B  67    11835  12664  10826   1187   -855   1804       C  
ATOM   1031  CZ2 TRP B  67      74.758  17.804   8.058  1.00 87.73           C  
ANISOU 1031  CZ2 TRP B  67    10746  12509  10079    715   -491   1771       C  
ATOM   1032  CZ3 TRP B  67      76.236  16.486   9.444  1.00 91.65           C  
ANISOU 1032  CZ3 TRP B  67    11279  12970  10573   1170   -679   1840       C  
ATOM   1033  CH2 TRP B  67      75.892  17.693   8.817  1.00 89.13           C  
ANISOU 1033  CH2 TRP B  67    10773  12877  10216    911   -504   1828       C  
ATOM   1034  N   TRP B  68      70.616  13.524  10.692  1.00 88.88           N  
ANISOU 1034  N   TRP B  68    12582  10914  10273   -613  -1752   1580       N  
ATOM   1035  CA  TRP B  68      69.600  14.409  11.254  1.00 86.49           C  
ANISOU 1035  CA  TRP B  68    12034  10879   9949   -999  -1599   1696       C  
ATOM   1036  C   TRP B  68      69.728  14.494  12.764  1.00 86.55           C  
ANISOU 1036  C   TRP B  68    11961  11014   9909  -1145  -1576   1934       C  
ATOM   1037  O   TRP B  68      69.562  15.567  13.345  1.00 84.24           O  
ANISOU 1037  O   TRP B  68    11378  11077   9551  -1223  -1391   1957       O  
ATOM   1038  CB  TRP B  68      68.190  13.947  10.905  1.00 87.72           C  
ANISOU 1038  CB  TRP B  68    12328  10858  10142  -1365  -1703   1742       C  
ATOM   1039  CG  TRP B  68      67.136  14.625  11.742  1.00 86.48           C  
ANISOU 1039  CG  TRP B  68    11914  11008   9938  -1737  -1573   1904       C  
ATOM   1040  CD1 TRP B  68      66.753  15.932  11.674  1.00 83.76           C  
ANISOU 1040  CD1 TRP B  68    11243  11036   9547  -1754  -1364   1828       C  
ATOM   1041  CD2 TRP B  68      66.350  14.032  12.782  1.00 88.56           C  
ANISOU 1041  CD2 TRP B  68    12230  11253  10167  -2122  -1650   2168       C  
ATOM   1042  NE1 TRP B  68      65.769  16.189  12.597  1.00 84.04           N  
ANISOU 1042  NE1 TRP B  68    11104  11310   9519  -2066  -1295   1987       N  
ATOM   1043  CE2 TRP B  68      65.501  15.041  13.290  1.00 86.97           C  
ANISOU 1043  CE2 TRP B  68    11673  11489   9881  -2322  -1451   2209       C  
ATOM   1044  CE3 TRP B  68      66.272  12.742  13.326  1.00 92.16           C  
ANISOU 1044  CE3 TRP B  68    13013  11365  10639  -2323  -1881   2387       C  
ATOM   1045  CZ2 TRP B  68      64.585  14.805  14.316  1.00 88.79           C  
ANISOU 1045  CZ2 TRP B  68    11803  11917  10016  -2706  -1438   2449       C  
ATOM   1046  CZ3 TRP B  68      65.357  12.504  14.345  1.00 93.98           C  
ANISOU 1046  CZ3 TRP B  68    13176  11749  10785  -2779  -1885   2671       C  
ATOM   1047  CH2 TRP B  68      64.526  13.533  14.830  1.00 92.28           C  
ANISOU 1047  CH2 TRP B  68    12539  12064  10458  -2963  -1647   2696       C  
ATOM   1048  N   SER B  69      70.006  13.352  13.389  1.00 90.82           N  
ANISOU 1048  N   SER B  69    12533  11511  10463  -1129  -1860   2390       N  
ATOM   1049  CA  SER B  69      70.197  13.272  14.831  1.00 91.52           C  
ANISOU 1049  CA  SER B  69    12582  11720  10473  -1233  -1869   2640       C  
ATOM   1050  C   SER B  69      71.291  14.228  15.274  1.00 89.42           C  
ANISOU 1050  C   SER B  69    12031  11801  10145   -964  -1718   2556       C  
ATOM   1051  O   SER B  69      71.068  15.074  16.135  1.00 87.58           O  
ANISOU 1051  O   SER B  69    11548  11905   9824  -1123  -1558   2599       O  
ATOM   1052  CB  SER B  69      70.526  11.838  15.249  1.00 95.48           C  
ANISOU 1052  CB  SER B  69    13471  11808  10998  -1141  -2148   2816       C  
ATOM   1053  OG  SER B  69      69.451  10.962  14.955  1.00 98.19           O  
ANISOU 1053  OG  SER B  69    14194  11672  11440  -1163  -2369   2763       O  
ATOM   1054  N   VAL B  70      72.460  14.111  14.657  1.00 90.82           N  
ANISOU 1054  N   VAL B  70    12144  12247  10118   -630  -2002   2561       N  
ATOM   1055  CA  VAL B  70      73.586  14.976  14.972  1.00 89.54           C  
ANISOU 1055  CA  VAL B  70    11684  12450   9887   -423  -1887   2511       C  
ATOM   1056  C   VAL B  70      73.213  16.437  14.737  1.00 86.18           C  
ANISOU 1056  C   VAL B  70    10961  12363   9422   -633  -1655   2422       C  
ATOM   1057  O   VAL B  70      73.482  17.292  15.572  1.00 85.24           O  
ANISOU 1057  O   VAL B  70    10678  12492   9217   -782  -1577   2500       O  
ATOM   1058  CB  VAL B  70      74.825  14.620  14.132  1.00 90.81           C  
ANISOU 1058  CB  VAL B  70    11813  12627  10063     41  -1927   2334       C  
ATOM   1059  CG1 VAL B  70      76.034  15.413  14.601  1.00 90.08           C  
ANISOU 1059  CG1 VAL B  70    11362  12986   9879    173  -1824   2334       C  
ATOM   1060  CG2 VAL B  70      75.101  13.125  14.199  1.00 94.77           C  
ANISOU 1060  CG2 VAL B  70    12683  12714  10610    319  -2194   2381       C  
ATOM   1061  N   GLU B  71      72.574  16.713  13.606  1.00 82.87           N  
ANISOU 1061  N   GLU B  71    10863  11670   8954   -827  -1919   1693       N  
ATOM   1062  CA  GLU B  71      72.105  18.061  13.267  1.00 80.19           C  
ANISOU 1062  CA  GLU B  71    10303  11579   8587   -993  -1736   1609       C  
ATOM   1063  C   GLU B  71      71.193  18.631  14.371  1.00 79.46           C  
ANISOU 1063  C   GLU B  71    10152  11598   8440  -1296  -1675   1719       C  
ATOM   1064  O   GLU B  71      71.269  19.822  14.697  1.00 78.12           O  
ANISOU 1064  O   GLU B  71     9812  11666   8204  -1353  -1565   1682       O  
ATOM   1065  CB  GLU B  71      71.375  18.033  11.913  1.00 79.51           C  
ANISOU 1065  CB  GLU B  71    10260  11396   8554   -979  -1702   1456       C  
ATOM   1066  CG  GLU B  71      71.184  19.369  11.216  1.00 77.48           C  
ANISOU 1066  CG  GLU B  71     9810  11362   8267   -996  -1551   1346       C  
ATOM   1067  CD  GLU B  71      70.611  19.197   9.801  1.00 77.46           C  
ANISOU 1067  CD  GLU B  71     9891  11249   8292   -957  -1559   1215       C  
ATOM   1068  OE1 GLU B  71      71.231  18.447   9.003  1.00 79.31           O  
ANISOU 1068  OE1 GLU B  71    10321  11260   8554   -820  -1683   1164       O  
ATOM   1069  OE2 GLU B  71      69.547  19.801   9.477  1.00 76.10           O  
ANISOU 1069  OE2 GLU B  71     9631  11179   8105  -1044  -1474   1156       O  
ATOM   1070  N   THR B  72      70.365  17.766  14.956  1.00 80.62           N  
ANISOU 1070  N   THR B  72    10602  11677   8353  -1267  -1797   1689       N  
ATOM   1071  CA  THR B  72      69.347  18.173  15.922  1.00 80.65           C  
ANISOU 1071  CA  THR B  72    10506  11878   8258  -1537  -1720   1797       C  
ATOM   1072  C   THR B  72      69.858  18.205  17.367  1.00 81.50           C  
ANISOU 1072  C   THR B  72    10576  12161   8230  -1571  -1723   1939       C  
ATOM   1073  O   THR B  72      69.521  19.121  18.123  1.00 80.93           O  
ANISOU 1073  O   THR B  72    10347  12369   8032  -1667  -1605   1916       O  
ATOM   1074  CB  THR B  72      68.150  17.221  15.909  1.00 82.67           C  
ANISOU 1074  CB  THR B  72    10901  11981   8530  -1797  -1814   1944       C  
ATOM   1075  OG1 THR B  72      67.557  17.211  14.605  1.00 82.01           O  
ANISOU 1075  OG1 THR B  72    10807  11820   8534  -1826  -1805   1805       O  
ATOM   1076  CG2 THR B  72      67.105  17.665  16.922  1.00 83.80           C  
ANISOU 1076  CG2 THR B  72    10911  12419   8510  -2092  -1733   2117       C  
ATOM   1077  N   ALA B  73      70.654  17.204  17.743  1.00 85.09           N  
ANISOU 1077  N   ALA B  73    11023  12671   8637  -1517  -1952   2330       N  
ATOM   1078  CA  ALA B  73      71.194  17.088  19.100  1.00 86.63           C  
ANISOU 1078  CA  ALA B  73    11233  12989   8695  -1546  -2013   2509       C  
ATOM   1079  C   ALA B  73      72.194  18.200  19.409  1.00 85.37           C  
ANISOU 1079  C   ALA B  73    10872  13105   8460  -1402  -1945   2395       C  
ATOM   1080  O   ALA B  73      72.336  18.628  20.556  1.00 86.44           O  
ANISOU 1080  O   ALA B  73    10971  13430   8443  -1445  -1976   2502       O  
ATOM   1081  CB  ALA B  73      71.838  15.731  19.290  1.00 89.27           C  
ANISOU 1081  CB  ALA B  73    11826  13006   9087  -1404  -2237   2665       C  
ATOM   1082  N   THR B  74      72.884  18.653  18.370  1.00 84.64           N  
ANISOU 1082  N   THR B  74    10912  12992   8257  -1535  -2183   2157       N  
ATOM   1083  CA  THR B  74      73.774  19.797  18.446  1.00 83.87           C  
ANISOU 1083  CA  THR B  74    10637  13132   8099  -1471  -2141   2060       C  
ATOM   1084  C   THR B  74      72.948  21.077  18.482  1.00 82.18           C  
ANISOU 1084  C   THR B  74    10337  13040   7847  -1619  -1997   1912       C  
ATOM   1085  O   THR B  74      73.427  22.142  18.888  1.00 81.83           O  
ANISOU 1085  O   THR B  74    10200  13167   7725  -1659  -1967   1820       O  
ATOM   1086  CB  THR B  74      74.667  19.844  17.197  1.00 83.64           C  
ANISOU 1086  CB  THR B  74    10541  13063   8174  -1245  -2158   1962       C  
ATOM   1087  OG1 THR B  74      75.273  18.563  16.992  1.00 85.72           O  
ANISOU 1087  OG1 THR B  74    10940  13148   8482  -1033  -2306   2062       O  
ATOM   1088  CG2 THR B  74      75.756  20.878  17.352  1.00 83.72           C  
ANISOU 1088  CG2 THR B  74    10340  13356   8112  -1220  -2153   1914       C  
ATOM   1089  N   THR B  75      71.695  20.949  18.054  1.00 81.40           N  
ANISOU 1089  N   THR B  75    10689  12715   7526  -1379  -1910   1342       N  
ATOM   1090  CA  THR B  75      70.794  22.078  17.808  1.00 80.30           C  
ANISOU 1090  CA  THR B  75    10479  12670   7360  -1454  -1789   1203       C  
ATOM   1091  C   THR B  75      71.372  23.048  16.761  1.00 78.94           C  
ANISOU 1091  C   THR B  75    10258  12478   7256  -1366  -1760   1044       C  
ATOM   1092  O   THR B  75      71.173  24.267  16.859  1.00 78.67           O  
ANISOU 1092  O   THR B  75    10204  12525   7162  -1398  -1717    927       O  
ATOM   1093  CB  THR B  75      70.394  22.849  19.103  1.00 81.28           C  
ANISOU 1093  CB  THR B  75    10559  13037   7286  -1555  -1738   1199       C  
ATOM   1094  OG1 THR B  75      71.318  23.924  19.323  1.00 80.86           O  
ANISOU 1094  OG1 THR B  75    10479  13059   7184  -1509  -1735   1043       O  
ATOM   1095  CG2 THR B  75      70.339  21.927  20.336  1.00 83.29           C  
ANISOU 1095  CG2 THR B  75    10861  13377   7408  -1640  -1817   1419       C  
ATOM   1096  N   VAL B  76      72.095  22.509  15.775  1.00 77.78           N  
ANISOU 1096  N   VAL B  76    10174  11992   7386  -1341  -1845   1022       N  
ATOM   1097  CA  VAL B  76      72.533  23.288  14.611  1.00 76.87           C  
ANISOU 1097  CA  VAL B  76    10010  11871   7327  -1292  -1806    919       C  
ATOM   1098  C   VAL B  76      71.338  23.543  13.694  1.00 75.95           C  
ANISOU 1098  C   VAL B  76     9946  11635   7277  -1296  -1752    845       C  
ATOM   1099  O   VAL B  76      71.115  24.683  13.271  1.00 75.32           O  
ANISOU 1099  O   VAL B  76     9863  11556   7201  -1316  -1713    761       O  
ATOM   1100  CB  VAL B  76      73.650  22.565  13.836  1.00 77.51           C  
ANISOU 1100  CB  VAL B  76    10066  11928   7458  -1123  -1847    947       C  
ATOM   1101  CG1 VAL B  76      74.001  23.330  12.569  1.00 77.05           C  
ANISOU 1101  CG1 VAL B  76     9939  11920   7417  -1087  -1789    869       C  
ATOM   1102  CG2 VAL B  76      74.878  22.384  14.716  1.00 78.99           C  
ANISOU 1102  CG2 VAL B  76    10168  12258   7586  -1048  -1927   1035       C  
ATOM   1103  N   GLY B  77      70.572  22.478  13.426  1.00 75.21           N  
ANISOU 1103  N   GLY B  77     9941  11371   7264   -972  -1544    664       N  
ATOM   1104  CA  GLY B  77      69.334  22.523  12.634  1.00 74.80           C  
ANISOU 1104  CA  GLY B  77     9920  11224   7276  -1007  -1527    598       C  
ATOM   1105  C   GLY B  77      69.471  23.245  11.304  1.00 73.91           C  
ANISOU 1105  C   GLY B  77     9791  11106   7187   -913  -1494    494       C  
ATOM   1106  O   GLY B  77      69.032  24.398  11.176  1.00 73.40           O  
ANISOU 1106  O   GLY B  77     9690  11102   7095   -932  -1451    445       O  
ATOM   1107  N   TYR B  78      70.094  22.575  10.325  1.00 72.75           N  
ANISOU 1107  N   TYR B  78     9486  10817   7337   -925  -1518    453       N  
ATOM   1108  CA  TYR B  78      70.358  23.153   9.003  1.00 72.46           C  
ANISOU 1108  CA  TYR B  78     9424  10835   7271   -845  -1478    389       C  
ATOM   1109  C   TYR B  78      69.068  23.446   8.281  1.00 72.12           C  
ANISOU 1109  C   TYR B  78     9415  10743   7246   -889  -1488    341       C  
ATOM   1110  O   TYR B  78      68.890  24.553   7.784  1.00 71.74           O  
ANISOU 1110  O   TYR B  78     9346  10743   7170   -897  -1456    329       O  
ATOM   1111  CB  TYR B  78      71.227  22.243   8.131  1.00 73.53           C  
ANISOU 1111  CB  TYR B  78     9589  10968   7380   -669  -1500    339       C  
ATOM   1112  CG  TYR B  78      72.692  22.276   8.471  1.00 74.33           C  
ANISOU 1112  CG  TYR B  78     9581  11228   7433   -567  -1476    376       C  
ATOM   1113  CD1 TYR B  78      73.410  23.478   8.453  1.00 74.14           C  
ANISOU 1113  CD1 TYR B  78     9415  11407   7348   -661  -1410    427       C  
ATOM   1114  CD2 TYR B  78      73.367  21.106   8.798  1.00 75.81           C  
ANISOU 1114  CD2 TYR B  78     9813  11365   7628   -377  -1546    367       C  
ATOM   1115  CE1 TYR B  78      74.762  23.506   8.775  1.00 75.33           C  
ANISOU 1115  CE1 TYR B  78     9405  11778   7439   -606  -1399    477       C  
ATOM   1116  CE2 TYR B  78      74.718  21.121   9.120  1.00 76.99           C  
ANISOU 1116  CE2 TYR B  78     9812  11722   7720   -244  -1536    402       C  
ATOM   1117  CZ  TYR B  78      75.413  22.318   9.108  1.00 76.74           C  
ANISOU 1117  CZ  TYR B  78     9571  11968   7618   -370  -1454    460       C  
ATOM   1118  OH  TYR B  78      76.758  22.309   9.424  1.00 78.44           O  
ANISOU 1118  OH  TYR B  78     9576  12469   7759   -260  -1454    505       O  
ATOM   1119  N   GLY B  79      68.163  22.466   8.252  1.00 71.58           N  
ANISOU 1119  N   GLY B  79     9421  10501   7274   -921  -1390    290       N  
ATOM   1120  CA  GLY B  79      66.890  22.604   7.547  1.00 71.78           C  
ANISOU 1120  CA  GLY B  79     9435  10532   7305   -974  -1426    244       C  
ATOM   1121  C   GLY B  79      66.755  21.669   6.363  1.00 72.83           C  
ANISOU 1121  C   GLY B  79     9688  10547   7437   -944  -1521    173       C  
ATOM   1122  O   GLY B  79      65.665  21.499   5.815  1.00 73.71           O  
ANISOU 1122  O   GLY B  79     9813  10632   7561  -1052  -1606    150       O  
ATOM   1123  N   ASP B  80      67.866  21.051   5.976  1.00 72.61           N  
ANISOU 1123  N   ASP B  80     9486  10460   7644   -847  -1293    182       N  
ATOM   1124  CA  ASP B  80      67.873  20.062   4.904  1.00 74.19           C  
ANISOU 1124  CA  ASP B  80     9846  10527   7814   -743  -1389     68       C  
ATOM   1125  C   ASP B  80      67.080  18.792   5.245  1.00 75.86           C  
ANISOU 1125  C   ASP B  80    10236  10489   8099   -872  -1555     66       C  
ATOM   1126  O   ASP B  80      66.761  18.007   4.363  1.00 77.64           O  
ANISOU 1126  O   ASP B  80    10653  10545   8300   -793  -1675    -54       O  
ATOM   1127  CB  ASP B  80      69.315  19.719   4.496  1.00 74.78           C  
ANISOU 1127  CB  ASP B  80     9921  10671   7820   -498  -1331     20       C  
ATOM   1128  CG  ASP B  80      70.086  18.978   5.582  1.00 76.01           C  
ANISOU 1128  CG  ASP B  80    10179  10667   8033   -400  -1407     43       C  
ATOM   1129  OD1 ASP B  80      69.845  19.229   6.786  1.00 75.44           O  
ANISOU 1129  OD1 ASP B  80    10081  10548   8036   -544  -1418    179       O  
ATOM   1130  OD2 ASP B  80      70.947  18.143   5.223  1.00 78.00           O  
ANISOU 1130  OD2 ASP B  80    10555  10851   8229   -141  -1464    -87       O  
ATOM   1131  N   LEU B  81      66.772  18.599   6.524  1.00 76.27           N  
ANISOU 1131  N   LEU B  81    10121  10387   8473   -949  -1409    270       N  
ATOM   1132  CA  LEU B  81      66.024  17.434   7.005  1.00 78.40           C  
ANISOU 1132  CA  LEU B  81    10556  10434   8800  -1172  -1576    343       C  
ATOM   1133  C   LEU B  81      65.292  17.769   8.299  1.00 78.16           C  
ANISOU 1133  C   LEU B  81    10358  10560   8781  -1424  -1518    531       C  
ATOM   1134  O   LEU B  81      65.820  18.514   9.143  1.00 76.66           O  
ANISOU 1134  O   LEU B  81    10025  10536   8565  -1348  -1382    589       O  
ATOM   1135  CB  LEU B  81      66.975  16.266   7.263  1.00 80.15           C  
ANISOU 1135  CB  LEU B  81    11037  10365   9050  -1026  -1691    341       C  
ATOM   1136  CG  LEU B  81      67.557  15.519   6.069  1.00 81.77           C  
ANISOU 1136  CG  LEU B  81    11469  10376   9222   -741  -1791    134       C  
ATOM   1137  CD1 LEU B  81      69.015  15.242   6.300  1.00 81.87           C  
ANISOU 1137  CD1 LEU B  81    11486  10405   9217   -425  -1737    127       C  
ATOM   1138  CD2 LEU B  81      66.802  14.239   5.806  1.00 85.04           C  
ANISOU 1138  CD2 LEU B  81    12239  10394   9680   -872  -2054     89       C  
ATOM   1139  N   TYR B  82      64.087  17.215   8.447  1.00 79.50           N  
ANISOU 1139  N   TYR B  82    10509  10601   9095  -1474  -1586    389       N  
ATOM   1140  CA  TYR B  82      63.281  17.324   9.675  1.00 80.36           C  
ANISOU 1140  CA  TYR B  82    10458  10905   9172  -1758  -1544    591       C  
ATOM   1141  C   TYR B  82      62.012  16.461   9.624  1.00 83.27           C  
ANISOU 1141  C   TYR B  82    10807  11299   9533  -2167  -1685    708       C  
ATOM   1142  O   TYR B  82      61.596  16.026   8.546  1.00 84.50           O  
ANISOU 1142  O   TYR B  82    11059  11329   9718  -2250  -1830    610       O  
ATOM   1143  CB  TYR B  82      62.907  18.782   9.967  1.00 78.47           C  
ANISOU 1143  CB  TYR B  82     9896  11054   8865  -1663  -1340    570       C  
ATOM   1144  CG  TYR B  82      62.180  19.464   8.842  1.00 77.85           C  
ANISOU 1144  CG  TYR B  82     9675  11125   8781  -1580  -1323    434       C  
ATOM   1145  CD1 TYR B  82      62.878  20.209   7.887  1.00 76.01           C  
ANISOU 1145  CD1 TYR B  82     9504  10817   8559  -1294  -1284    283       C  
ATOM   1146  CD2 TYR B  82      60.794  19.369   8.729  1.00 79.59           C  
ANISOU 1146  CD2 TYR B  82     9683  11594   8962  -1798  -1358    477       C  
ATOM   1147  CE1 TYR B  82      62.214  20.838   6.852  1.00 75.78           C  
ANISOU 1147  CE1 TYR B  82     9376  10912   8506  -1215  -1292    187       C  
ATOM   1148  CE2 TYR B  82      60.123  19.990   7.697  1.00 79.37           C  
ANISOU 1148  CE2 TYR B  82     9524  11713   8920  -1689  -1372    361       C  
ATOM   1149  CZ  TYR B  82      60.839  20.721   6.761  1.00 77.40           C  
ANISOU 1149  CZ  TYR B  82     9388  11336   8685  -1390  -1345    219       C  
ATOM   1150  OH  TYR B  82      60.177  21.348   5.734  1.00 77.48           O  
ANISOU 1150  OH  TYR B  82     9291  11485   8662  -1276  -1374    133       O  
ATOM   1151  N   PRO B  83      61.380  16.208  10.788  1.00 85.20           N  
ANISOU 1151  N   PRO B  83    10817  11684   9871  -2361  -1349    593       N  
ATOM   1152  CA  PRO B  83      60.150  15.417  10.756  1.00 88.58           C  
ANISOU 1152  CA  PRO B  83    11199  12180  10278  -2816  -1495    735       C  
ATOM   1153  C   PRO B  83      58.901  16.222  10.414  1.00 88.81           C  
ANISOU 1153  C   PRO B  83    10800  12711  10231  -2899  -1394    697       C  
ATOM   1154  O   PRO B  83      58.834  17.421  10.694  1.00 86.74           O  
ANISOU 1154  O   PRO B  83    10260  12788   9908  -2625  -1188    609       O  
ATOM   1155  CB  PRO B  83      60.053  14.876  12.177  1.00 90.81           C  
ANISOU 1155  CB  PRO B  83    11502  12517  10486  -3123  -1497   1027       C  
ATOM   1156  CG  PRO B  83      60.694  15.915  13.004  1.00 88.22           C  
ANISOU 1156  CG  PRO B  83    10955  12491  10075  -2833  -1251    994       C  
ATOM   1157  CD  PRO B  83      61.744  16.591  12.163  1.00 84.77           C  
ANISOU 1157  CD  PRO B  83    10637  11841   9729  -2355  -1201    738       C  
ATOM   1158  N   VAL B  84      57.928  15.554   9.800  1.00 95.60           N  
ANISOU 1158  N   VAL B  84    11296  13599  11430  -3109  -2027    -64       N  
ATOM   1159  CA  VAL B  84      56.631  16.162   9.479  1.00 96.86           C  
ANISOU 1159  CA  VAL B  84    11022  14270  11509  -3228  -1986    -79       C  
ATOM   1160  C   VAL B  84      55.481  15.354  10.093  1.00101.38           C  
ANISOU 1160  C   VAL B  84    11420  15102  11998  -3824  -2088    193       C  
ATOM   1161  O   VAL B  84      54.325  15.779  10.056  1.00103.28           O  
ANISOU 1161  O   VAL B  84    11205  15903  12133  -3968  -2030    234       O  
ATOM   1162  CB  VAL B  84      56.409  16.248   7.958  1.00 96.64           C  
ANISOU 1162  CB  VAL B  84    11051  14132  11536  -3121  -2137   -292       C  
ATOM   1163  CG1 VAL B  84      55.012  16.766   7.652  1.00 97.69           C  
ANISOU 1163  CG1 VAL B  84    10675  14870  11571  -3116  -2064   -312       C  
ATOM   1164  CG2 VAL B  84      57.466  17.132   7.315  1.00 92.81           C  
ANISOU 1164  CG2 VAL B  84    10786  13365  11113  -2599  -2061   -525       C  
ATOM   1165  N   THR B  85      55.814  14.195  10.659  1.00106.85           N  
ANISOU 1165  N   THR B  85    12061  16165  12373  -4642  -1648    533       N  
ATOM   1166  CA  THR B  85      54.861  13.378  11.413  1.00111.68           C  
ANISOU 1166  CA  THR B  85    12535  17021  12877  -5290  -1736    876       C  
ATOM   1167  C   THR B  85      54.838  13.814  12.881  1.00111.76           C  
ANISOU 1167  C   THR B  85    12219  17534  12710  -5286  -1461   1071       C  
ATOM   1168  O   THR B  85      55.851  14.274  13.414  1.00108.50           O  
ANISOU 1168  O   THR B  85    11911  17012  12301  -4866  -1298    983       O  
ATOM   1169  CB  THR B  85      55.221  11.874  11.354  1.00114.79           C  
ANISOU 1169  CB  THR B  85    13515  16735  13365  -5685  -2059   1050       C  
ATOM   1170  OG1 THR B  85      55.807  11.564  10.083  1.00113.22           O  
ANISOU 1170  OG1 THR B  85    13771  15919  13329  -5377  -2251    763       O  
ATOM   1171  CG2 THR B  85      53.978  10.997  11.593  1.00120.91           C  
ANISOU 1171  CG2 THR B  85    14175  17709  14057  -6498  -2273   1368       C  
ATOM   1172  N   LEU B  86      53.683  13.657  13.526  1.00124.24           N  
ANISOU 1172  N   LEU B  86    12250  21621  13334  -5730  -1248    719       N  
ATOM   1173  CA  LEU B  86      53.528  13.945  14.950  1.00125.46           C  
ANISOU 1173  CA  LEU B  86    12107  22298  13263  -5798  -1003    930       C  
ATOM   1174  C   LEU B  86      54.460  13.064  15.780  1.00125.67           C  
ANISOU 1174  C   LEU B  86    12643  21780  13325  -5924  -1109   1135       C  
ATOM   1175  O   LEU B  86      55.139  13.555  16.677  1.00122.61           O  
ANISOU 1175  O   LEU B  86    12349  21319  12917  -5506   -952   1044       O  
ATOM   1176  CB  LEU B  86      52.073  13.750  15.381  1.00131.16           C  
ANISOU 1176  CB  LEU B  86    12328  23749  13759  -6412   -978   1234       C  
ATOM   1177  CG  LEU B  86      51.710  14.241  16.784  1.00132.21           C  
ANISOU 1177  CG  LEU B  86    11835  24802  13595  -6235   -624   1254       C  
ATOM   1178  CD1 LEU B  86      51.733  15.760  16.845  1.00127.38           C  
ANISOU 1178  CD1 LEU B  86    11073  24294  13031  -5414   -416    820       C  
ATOM   1179  CD2 LEU B  86      50.347  13.709  17.203  1.00138.07           C  
ANISOU 1179  CD2 LEU B  86    11959  26379  14122  -6770   -605   1477       C  
ATOM   1180  N   TRP B  87      54.499  11.774  15.461  1.00130.28           N  
ANISOU 1180  N   TRP B  87    13980  21742  13780  -7490  -1276   3163       N  
ATOM   1181  CA  TRP B  87      55.396  10.827  16.121  1.00130.84           C  
ANISOU 1181  CA  TRP B  87    14624  21175  13915  -7543  -1443   3343       C  
ATOM   1182  C   TRP B  87      56.870  11.120  15.849  1.00125.58           C  
ANISOU 1182  C   TRP B  87    14290  20007  13417  -6827  -1406   3022       C  
ATOM   1183  O   TRP B  87      57.684  11.152  16.772  1.00123.52           O  
ANISOU 1183  O   TRP B  87    14002  19856  13074  -6523  -1228   3033       O  
ATOM   1184  CB  TRP B  87      55.047   9.394  15.716  1.00135.64           C  
ANISOU 1184  CB  TRP B  87    15706  21202  14629  -8137  -1850   3574       C  
ATOM   1185  CG  TRP B  87      54.029   8.718  16.600  1.00141.77           C  
ANISOU 1185  CG  TRP B  87    16281  22391  15195  -8943  -1905   4052       C  
ATOM   1186  CD1 TRP B  87      53.598   7.427  16.497  1.00147.56           C  
ANISOU 1186  CD1 TRP B  87    17401  22702  15964  -9659  -2280   4375       C  
ATOM   1187  CD2 TRP B  87      53.337   9.280  17.731  1.00143.43           C  
ANISOU 1187  CD2 TRP B  87    15858  23543  15096  -9146  -1586   4277       C  
ATOM   1188  NE1 TRP B  87      52.672   7.155  17.472  1.00152.73           N  
ANISOU 1188  NE1 TRP B  87    17671  24008  16351 -10352  -2207   4824       N  
ATOM   1189  CE2 TRP B  87      52.494   8.270  18.246  1.00150.34           C  
ANISOU 1189  CE2 TRP B  87    16719  24584  15820 -10031  -1767   4766       C  
ATOM   1190  CE3 TRP B  87      53.343  10.539  18.353  1.00140.27           C  
ANISOU 1190  CE3 TRP B  87    14919  23862  14515  -8662  -1177   4102       C  
ATOM   1191  CZ2 TRP B  87      51.665   8.478  19.357  1.00154.16           C  
ANISOU 1191  CZ2 TRP B  87    16608  26017  15950 -10443  -1517   5098       C  
ATOM   1192  CZ3 TRP B  87      52.518  10.745  19.456  1.00144.05           C  
ANISOU 1192  CZ3 TRP B  87    14844  25239  14649  -9009   -939   4383       C  
ATOM   1193  CH2 TRP B  87      51.690   9.718  19.945  1.00150.92           C  
ANISOU 1193  CH2 TRP B  87    15652  26342  15348  -9890  -1094   4882       C  
ATOM   1194  N   GLY B  88      57.207  11.339  14.582  1.00114.19           N  
ANISOU 1194  N   GLY B  88    14097  16359  12932  -5658  -1699   2796       N  
ATOM   1195  CA  GLY B  88      58.563  11.728  14.211  1.00109.58           C  
ANISOU 1195  CA  GLY B  88    13726  15436  12473  -4993  -1631   2494       C  
ATOM   1196  C   GLY B  88      59.008  13.006  14.897  1.00105.79           C  
ANISOU 1196  C   GLY B  88    12909  15398  11890  -4566  -1300   2386       C  
ATOM   1197  O   GLY B  88      60.201  13.203  15.134  1.00103.30           O  
ANISOU 1197  O   GLY B  88    12804  14816  11631  -4167  -1270   2285       O  
ATOM   1198  N   ARG B  89      58.045  13.869  15.213  1.00105.39           N  
ANISOU 1198  N   ARG B  89    12162  16767  11116  -3841  -1363   1963       N  
ATOM   1199  CA  ARG B  89      58.323  15.134  15.894  1.00102.52           C  
ANISOU 1199  CA  ARG B  89    11504  16818  10632  -3439  -1071   1826       C  
ATOM   1200  C   ARG B  89      58.506  14.970  17.400  1.00104.01           C  
ANISOU 1200  C   ARG B  89    11689  17198  10632  -3561   -980   2073       C  
ATOM   1201  O   ARG B  89      59.177  15.786  18.035  1.00101.42           O  
ANISOU 1201  O   ARG B  89    11392  16874  10268  -3186   -856   1952       O  
ATOM   1202  CB  ARG B  89      57.259  16.190  15.564  1.00102.31           C  
ANISOU 1202  CB  ARG B  89    10964  17409  10500  -3332   -876   1673       C  
ATOM   1203  CG  ARG B  89      57.492  16.844  14.210  1.00 99.87           C  
ANISOU 1203  CG  ARG B  89    10686  16896  10364  -3048   -941   1386       C  
ATOM   1204  CD  ARG B  89      56.359  17.737  13.734  1.00 99.66           C  
ANISOU 1204  CD  ARG B  89    10210  17394  10263  -2841   -797   1209       C  
ATOM   1205  NE  ARG B  89      56.668  18.258  12.400  1.00 96.92           N  
ANISOU 1205  NE  ARG B  89    10017  16724  10084  -2525   -882    955       N  
ATOM   1206  CZ  ARG B  89      55.972  19.192  11.757  1.00 96.44           C  
ANISOU 1206  CZ  ARG B  89     9697  16931  10015  -2283   -839    778       C  
ATOM   1207  NH1 ARG B  89      54.901  19.739  12.319  1.00 98.64           N  
ANISOU 1207  NH1 ARG B  89     9516  17829  10132  -2268   -708    794       N  
ATOM   1208  NH2 ARG B  89      56.355  19.585  10.545  1.00 94.19           N  
ANISOU 1208  NH2 ARG B  89     9608  16321   9859  -2030   -930    587       N  
ATOM   1209  N   CYS B  90      57.913  13.915  17.962  1.00113.71           N  
ANISOU 1209  N   CYS B  90    12290  19636  11277  -4672   -809   3044       N  
ATOM   1210  CA  CYS B  90      58.190  13.521  19.342  1.00115.87           C  
ANISOU 1210  CA  CYS B  90    12701  19943  11380  -4861   -807   3349       C  
ATOM   1211  C   CYS B  90      59.635  13.072  19.456  1.00113.89           C  
ANISOU 1211  C   CYS B  90    12956  19016  11300  -4562   -978   3308       C  
ATOM   1212  O   CYS B  90      60.403  13.655  20.221  1.00111.20           O  
ANISOU 1212  O   CYS B  90    12595  18744  10911  -4163   -846   3172       O  
ATOM   1213  CB  CYS B  90      57.259  12.407  19.806  1.00121.54           C  
ANISOU 1213  CB  CYS B  90    13456  20749  11973  -5570   -958   3789       C  
ATOM   1214  SG  CYS B  90      55.646  12.996  20.328  1.00124.93           S  
ANISOU 1214  SG  CYS B  90    13163  22205  12100  -5930   -703   3899       S  
ATOM   1215  N   VAL B  91      60.002  12.054  18.678  1.00110.69           N  
ANISOU 1215  N   VAL B  91    13696  16521  11842  -5080  -1372   4137       N  
ATOM   1216  CA  VAL B  91      61.389  11.590  18.604  1.00109.30           C  
ANISOU 1216  CA  VAL B  91    13976  15732  11822  -4703  -1541   4062       C  
ATOM   1217  C   VAL B  91      62.334  12.786  18.601  1.00104.53           C  
ANISOU 1217  C   VAL B  91    13175  15321  11220  -4124  -1315   3753       C  
ATOM   1218  O   VAL B  91      63.311  12.797  19.338  1.00104.09           O  
ANISOU 1218  O   VAL B  91    13226  15220  11102  -3920  -1310   3817       O  
ATOM   1219  CB  VAL B  91      61.640  10.680  17.370  1.00110.03           C  
ANISOU 1219  CB  VAL B  91    14499  15148  12161  -4651  -1834   3930       C  
ATOM   1220  CG1 VAL B  91      63.117  10.323  17.235  1.00108.72           C  
ANISOU 1220  CG1 VAL B  91    14715  14469  12125  -4141  -1964   3795       C  
ATOM   1221  CG2 VAL B  91      60.803   9.414  17.462  1.00115.50           C  
ANISOU 1221  CG2 VAL B  91    15487  15549  12848  -5264  -2119   4264       C  
ATOM   1222  N   ALA B  92      62.006  13.804  17.805  1.00 97.37           N  
ANISOU 1222  N   ALA B  92    12335  14421  10242  -3295  -1441   2892       N  
ATOM   1223  CA  ALA B  92      62.810  15.025  17.720  1.00 93.26           C  
ANISOU 1223  CA  ALA B  92    11663  14037   9734  -2798  -1258   2605       C  
ATOM   1224  C   ALA B  92      63.102  15.625  19.100  1.00 93.08           C  
ANISOU 1224  C   ALA B  92    11478  14392   9498  -2726  -1094   2683       C  
ATOM   1225  O   ALA B  92      64.258  15.691  19.520  1.00 92.00           O  
ANISOU 1225  O   ALA B  92    11490  14100   9366  -2477  -1128   2663       O  
ATOM   1226  CB  ALA B  92      62.138  16.052  16.803  1.00 91.00           C  
ANISOU 1226  CB  ALA B  92    11086  13997   9493  -2651  -1114   2330       C  
ATOM   1227  N   VAL B  93      62.041  16.033  19.801  1.00 97.54           N  
ANISOU 1227  N   VAL B  93    11711  15986   9364  -2512  -1032   2694       N  
ATOM   1228  CA  VAL B  93      62.147  16.608  21.142  1.00 98.43           C  
ANISOU 1228  CA  VAL B  93    11655  16535   9208  -2499   -876   2770       C  
ATOM   1229  C   VAL B  93      63.133  15.809  21.990  1.00 99.93           C  
ANISOU 1229  C   VAL B  93    12158  16459   9351  -2570  -1033   3028       C  
ATOM   1230  O   VAL B  93      64.044  16.383  22.587  1.00 98.33           O  
ANISOU 1230  O   VAL B  93    12000  16260   9101  -2283  -1005   2925       O  
ATOM   1231  CB  VAL B  93      60.780  16.650  21.847  1.00101.86           C  
ANISOU 1231  CB  VAL B  93    11739  17584   9378  -2847   -726   2936       C  
ATOM   1232  CG1 VAL B  93      60.904  16.150  23.279  1.00104.25           C  
ANISOU 1232  CG1 VAL B  93    12000  18238   9374  -2966   -644   3143       C  
ATOM   1233  CG2 VAL B  93      60.206  18.058  21.814  1.00100.50           C  
ANISOU 1233  CG2 VAL B  93    11199  17835   9152  -2586   -517   2626       C  
ATOM   1234  N   VAL B  94      62.955  14.489  22.022  1.00103.18           N  
ANISOU 1234  N   VAL B  94    12582  16746   9875  -3342  -1024   3894       N  
ATOM   1235  CA  VAL B  94      63.838  13.599  22.776  1.00105.11           C  
ANISOU 1235  CA  VAL B  94    13180  16671  10086  -3366  -1222   4159       C  
ATOM   1236  C   VAL B  94      65.306  13.813  22.385  1.00101.92           C  
ANISOU 1236  C   VAL B  94    12954  15901   9869  -2850  -1301   3912       C  
ATOM   1237  O   VAL B  94      66.124  14.126  23.249  1.00101.25           O  
ANISOU 1237  O   VAL B  94    12826  15987   9656  -2647  -1254   3896       O  
ATOM   1238  CB  VAL B  94      63.420  12.107  22.650  1.00109.26           C  
ANISOU 1238  CB  VAL B  94    14069  16758  10687  -3783  -1505   4512       C  
ATOM   1239  CG1 VAL B  94      64.444  11.189  23.313  1.00111.25           C  
ANISOU 1239  CG1 VAL B  94    14754  16567  10949  -3675  -1759   4744       C  
ATOM   1240  CG2 VAL B  94      62.047  11.892  23.257  1.00113.22           C  
ANISOU 1240  CG2 VAL B  94    14354  17722  10944  -4367  -1425   4831       C  
ATOM   1241  N   VAL B  95      65.636  13.682  21.100  1.00 95.83           N  
ANISOU 1241  N   VAL B  95    12756  13963   9691  -2850  -1610   3486       N  
ATOM   1242  CA  VAL B  95      67.024  13.890  20.656  1.00 93.51           C  
ANISOU 1242  CA  VAL B  95    12578  13414   9537  -2374  -1671   3277       C  
ATOM   1243  C   VAL B  95      67.513  15.340  20.861  1.00 90.07           C  
ANISOU 1243  C   VAL B  95    11822  13371   9028  -2100  -1442   3010       C  
ATOM   1244  O   VAL B  95      68.710  15.573  21.061  1.00 89.17           O  
ANISOU 1244  O   VAL B  95    11737  13221   8921  -1811  -1483   2943       O  
ATOM   1245  CB  VAL B  95      67.321  13.329  19.208  1.00 93.11           C  
ANISOU 1245  CB  VAL B  95    12775  12857   9744  -2170  -1837   3106       C  
ATOM   1246  CG1 VAL B  95      66.078  12.770  18.549  1.00 94.13           C  
ANISOU 1246  CG1 VAL B  95    12920  12905   9940  -2502  -1864   3115       C  
ATOM   1247  CG2 VAL B  95      68.010  14.376  18.300  1.00 89.33           C  
ANISOU 1247  CG2 VAL B  95    12138  12429   9374  -1707  -1720   2746       C  
ATOM   1248  N   MET B  96      66.587  16.298  20.831  1.00 89.94           N  
ANISOU 1248  N   MET B  96    11875  13659   8641  -1811  -1565   2523       N  
ATOM   1249  CA  MET B  96      66.905  17.695  21.131  1.00 87.74           C  
ANISOU 1249  CA  MET B  96    11375  13704   8260  -1595  -1394   2301       C  
ATOM   1250  C   MET B  96      67.409  17.863  22.567  1.00 89.36           C  
ANISOU 1250  C   MET B  96    11572  14165   8216  -1627  -1391   2446       C  
ATOM   1251  O   MET B  96      68.555  18.277  22.781  1.00 88.52           O  
ANISOU 1251  O   MET B  96    11518  13997   8120  -1405  -1458   2382       O  
ATOM   1252  CB  MET B  96      65.693  18.592  20.907  1.00 86.85           C  
ANISOU 1252  CB  MET B  96    10996  13915   8087  -1628  -1200   2119       C  
ATOM   1253  CG  MET B  96      65.563  19.169  19.522  1.00 84.30           C  
ANISOU 1253  CG  MET B  96    10650  13406   7974  -1438  -1184   1875       C  
ATOM   1254  SD  MET B  96      63.827  19.529  19.214  1.00 84.92           S  
ANISOU 1254  SD  MET B  96    10459  13802   8006  -1573  -1046   1793       S  
ATOM   1255  CE  MET B  96      63.911  21.009  18.207  1.00 82.73           C  
ANISOU 1255  CE  MET B  96    10032  13717   7683  -1219   -895   1452       C  
ATOM   1256  N   VAL B  97      66.565  17.539  23.547  1.00 91.04           N  
ANISOU 1256  N   VAL B  97    11909  14388   8293  -1766  -1141   2406       N  
ATOM   1257  CA  VAL B  97      66.943  17.714  24.954  1.00 92.82           C  
ANISOU 1257  CA  VAL B  97    12138  14887   8244  -1787  -1143   2535       C  
ATOM   1258  C   VAL B  97      68.111  16.814  25.357  1.00 93.78           C  
ANISOU 1258  C   VAL B  97    12527  14673   8431  -1694  -1382   2731       C  
ATOM   1259  O   VAL B  97      68.954  17.223  26.151  1.00 92.79           O  
ANISOU 1259  O   VAL B  97    12387  14595   8275  -1462  -1419   2611       O  
ATOM   1260  CB  VAL B  97      65.741  17.590  25.953  1.00 96.22           C  
ANISOU 1260  CB  VAL B  97    12420  15808   8332  -2106  -1017   2748       C  
ATOM   1261  CG1 VAL B  97      64.613  18.545  25.561  1.00 95.64           C  
ANISOU 1261  CG1 VAL B  97    12048  16095   8197  -2097   -792   2518       C  
ATOM   1262  CG2 VAL B  97      65.237  16.149  26.071  1.00 99.52           C  
ANISOU 1262  CG2 VAL B  97    12996  16086   8732  -2484  -1148   3156       C  
ATOM   1263  N   ALA B  98      68.166  15.607  24.789  1.00 93.30           N  
ANISOU 1263  N   ALA B  98    12569  14298   8581  -2250  -1538   2966       N  
ATOM   1264  CA  ALA B  98      69.275  14.680  25.016  1.00 94.39           C  
ANISOU 1264  CA  ALA B  98    12996  14023   8844  -2048  -1800   3100       C  
ATOM   1265  C   ALA B  98      70.606  15.340  24.701  1.00 91.85           C  
ANISOU 1265  C   ALA B  98    12579  13707   8612  -1636  -1808   2832       C  
ATOM   1266  O   ALA B  98      71.581  15.145  25.414  1.00 93.19           O  
ANISOU 1266  O   ALA B  98    12797  13933   8677  -1498  -1932   2938       O  
ATOM   1267  CB  ALA B  98      69.104  13.430  24.185  1.00 95.28           C  
ANISOU 1267  CB  ALA B  98    13382  13607   9214  -2074  -1976   3164       C  
ATOM   1268  N   GLY B  99      70.629  16.129  23.633  1.00 88.76           N  
ANISOU 1268  N   GLY B  99    12306  13125   8292  -1603  -1807   2561       N  
ATOM   1269  CA  GLY B  99      71.812  16.888  23.249  1.00 86.74           C  
ANISOU 1269  CA  GLY B  99    11930  12912   8114  -1284  -1808   2332       C  
ATOM   1270  C   GLY B  99      72.083  18.039  24.199  1.00 85.95           C  
ANISOU 1270  C   GLY B  99    11622  13228   7808  -1317  -1684   2203       C  
ATOM   1271  O   GLY B  99      73.186  18.156  24.733  1.00 86.60           O  
ANISOU 1271  O   GLY B  99    11663  13437   7805  -1192  -1776   2209       O  
ATOM   1272  N   ILE B 100      71.073  18.882  24.415  1.00 86.10           N  
ANISOU 1272  N   ILE B 100    11698  13173   7844  -1414  -1416   2164       N  
ATOM   1273  CA  ILE B 100      71.201  20.039  25.302  1.00 86.05           C  
ANISOU 1273  CA  ILE B 100    11558  13523   7614  -1424  -1317   2005       C  
ATOM   1274  C   ILE B 100      71.680  19.604  26.686  1.00 88.94           C  
ANISOU 1274  C   ILE B 100    11987  14089   7719  -1505  -1427   2240       C  
ATOM   1275  O   ILE B 100      72.714  20.073  27.157  1.00 89.22           O  
ANISOU 1275  O   ILE B 100    11989  14242   7668  -1401  -1515   2173       O  
ATOM   1276  CB  ILE B 100      69.875  20.834  25.432  1.00 86.06           C  
ANISOU 1276  CB  ILE B 100    11438  13786   7476  -1540  -1114   1872       C  
ATOM   1277  CG1 ILE B 100      69.339  21.226  24.047  1.00 83.62           C  
ANISOU 1277  CG1 ILE B 100    11065  13307   7398  -1459  -1018   1659       C  
ATOM   1278  CG2 ILE B 100      70.072  22.068  26.310  1.00 87.03           C  
ANISOU 1278  CG2 ILE B 100    11490  14265   7314  -1507  -1051   1693       C  
ATOM   1279  CD1 ILE B 100      67.876  21.654  24.028  1.00 84.35           C  
ANISOU 1279  CD1 ILE B 100    11021  13645   7382  -1553   -849   1599       C  
ATOM   1280  N   THR B 101      70.932  18.691  27.311  1.00 89.80           N  
ANISOU 1280  N   THR B 101    12172  14272   7676  -2000  -1298   2288       N  
ATOM   1281  CA  THR B 101      71.241  18.181  28.646  1.00 93.08           C  
ANISOU 1281  CA  THR B 101    12672  14891   7805  -2112  -1408   2569       C  
ATOM   1282  C   THR B 101      72.632  17.567  28.751  1.00 94.05           C  
ANISOU 1282  C   THR B 101    12917  14836   7983  -1923  -1656   2702       C  
ATOM   1283  O   THR B 101      73.429  18.016  29.566  1.00 94.90           O  
ANISOU 1283  O   THR B 101    12959  15211   7889  -1866  -1707   2658       O  
ATOM   1284  CB  THR B 101      70.162  17.191  29.130  1.00 95.95           C  
ANISOU 1284  CB  THR B 101    13137  15267   8051  -2420  -1407   2919       C  
ATOM   1285  OG1 THR B 101      68.995  17.930  29.500  1.00 97.49           O  
ANISOU 1285  OG1 THR B 101    13156  15987   7899  -2604  -1203   2891       O  
ATOM   1286  CG2 THR B 101      70.633  16.381  30.338  1.00 99.39           C  
ANISOU 1286  CG2 THR B 101    13831  15531   8402  -2482  -1665   3330       C  
ATOM   1287  N   SER B 102      72.937  16.567  27.932  1.00 93.92           N  
ANISOU 1287  N   SER B 102    12831  14662   8193  -1942  -1764   2947       N  
ATOM   1288  CA  SER B 102      74.230  15.887  28.049  1.00 95.56           C  
ANISOU 1288  CA  SER B 102    13120  14776   8414  -1696  -2008   3068       C  
ATOM   1289  C   SER B 102      75.421  16.804  27.735  1.00 93.45           C  
ANISOU 1289  C   SER B 102    12625  14649   8234  -1439  -2002   2768       C  
ATOM   1290  O   SER B 102      76.499  16.631  28.311  1.00 95.17           O  
ANISOU 1290  O   SER B 102    12798  14994   8368  -1271  -2180   2839       O  
ATOM   1291  CB  SER B 102      74.282  14.606  27.214  1.00 97.44           C  
ANISOU 1291  CB  SER B 102    13643  14513   8865  -1560  -2228   3287       C  
ATOM   1292  OG  SER B 102      74.471  14.897  25.844  1.00 94.98           O  
ANISOU 1292  OG  SER B 102    13281  13953   8855  -1307  -2199   3026       O  
ATOM   1293  N   PHE B 103      75.229  17.776  26.842  1.00 92.00           N  
ANISOU 1293  N   PHE B 103    12326  14490   8138  -1669  -1841   2552       N  
ATOM   1294  CA  PHE B 103      76.256  18.790  26.594  1.00 90.71           C  
ANISOU 1294  CA  PHE B 103    11954  14497   8015  -1524  -1850   2318       C  
ATOM   1295  C   PHE B 103      76.351  19.779  27.749  1.00 91.55           C  
ANISOU 1295  C   PHE B 103    11968  14984   7833  -1675  -1833   2236       C  
ATOM   1296  O   PHE B 103      77.378  20.432  27.921  1.00 91.97           O  
ANISOU 1296  O   PHE B 103    11877  15222   7845  -1611  -1932   2137       O  
ATOM   1297  CB  PHE B 103      76.014  19.535  25.283  1.00 87.60           C  
ANISOU 1297  CB  PHE B 103    11457  13983   7843  -1487  -1694   2046       C  
ATOM   1298  CG  PHE B 103      76.699  18.916  24.092  1.00 87.25           C  
ANISOU 1298  CG  PHE B 103    11395  13717   8040  -1224  -1767   2032       C  
ATOM   1299  CD1 PHE B 103      78.089  18.945  23.975  1.00 88.55           C  
ANISOU 1299  CD1 PHE B 103    11397  14039   8210  -1009  -1903   2033       C  
ATOM   1300  CD2 PHE B 103      75.958  18.316  23.078  1.00 86.09           C  
ANISOU 1300  CD2 PHE B 103    11370  13252   8090  -1179  -1703   2004       C  
ATOM   1301  CE1 PHE B 103      78.733  18.381  22.870  1.00 88.83           C  
ANISOU 1301  CE1 PHE B 103    11377  13947   8428   -704  -1951   1992       C  
ATOM   1302  CE2 PHE B 103      76.591  17.749  21.967  1.00 86.18           C  
ANISOU 1302  CE2 PHE B 103    11378  13079   8289   -891  -1766   1944       C  
ATOM   1303  CZ  PHE B 103      77.983  17.781  21.868  1.00 87.64           C  
ANISOU 1303  CZ  PHE B 103    11385  13454   8459   -631  -1878   1932       C  
ATOM   1304  N   GLY B 104      75.277  19.886  28.532  1.00 93.87           N  
ANISOU 1304  N   GLY B 104    12157  15472   8036  -2034  -1559   1965       N  
ATOM   1305  CA  GLY B 104      75.255  20.723  29.730  1.00 95.49           C  
ANISOU 1305  CA  GLY B 104    12325  16059   7896  -2158  -1544   1881       C  
ATOM   1306  C   GLY B 104      76.110  20.111  30.815  1.00 98.55           C  
ANISOU 1306  C   GLY B 104    12744  16619   8083  -2125  -1773   2122       C  
ATOM   1307  O   GLY B 104      76.878  20.814  31.468  1.00 99.41           O  
ANISOU 1307  O   GLY B 104    12756  16957   8057  -2110  -1881   1995       O  
ATOM   1308  N   LEU B 105      75.977  18.796  30.996  1.00101.67           N  
ANISOU 1308  N   LEU B 105    13282  17133   8216  -1980  -1936   2556       N  
ATOM   1309  CA  LEU B 105      76.791  18.044  31.951  1.00105.05           C  
ANISOU 1309  CA  LEU B 105    13778  17668   8470  -1905  -2191   2841       C  
ATOM   1310  C   LEU B 105      78.284  18.237  31.740  1.00105.02           C  
ANISOU 1310  C   LEU B 105    13602  17725   8574  -1670  -2369   2726       C  
ATOM   1311  O   LEU B 105      79.035  18.353  32.710  1.00106.97           O  
ANISOU 1311  O   LEU B 105    13760  18310   8572  -1697  -2496   2715       O  
ATOM   1312  CB  LEU B 105      76.480  16.551  31.891  1.00107.15           C  
ANISOU 1312  CB  LEU B 105    14286  17598   8829  -1864  -2334   3228       C  
ATOM   1313  CG  LEU B 105      75.722  15.970  33.081  1.00110.56           C  
ANISOU 1313  CG  LEU B 105    14877  18237   8895  -2138  -2345   3555       C  
ATOM   1314  CD1 LEU B 105      74.335  15.520  32.655  1.00109.46           C  
ANISOU 1314  CD1 LEU B 105    14755  18083   8752  -2419  -2082   3535       C  
ATOM   1315  CD2 LEU B 105      76.503  14.803  33.667  1.00114.50           C  
ANISOU 1315  CD2 LEU B 105    15650  18481   9372  -2063  -2643   4011       C  
ATOM   1316  N   VAL B 106      78.709  18.260  30.478  1.00105.10           N  
ANISOU 1316  N   VAL B 106    13345  17676   8911  -1568  -2278   2494       N  
ATOM   1317  CA  VAL B 106      80.122  18.421  30.144  1.00105.74           C  
ANISOU 1317  CA  VAL B 106    13199  17898   9078  -1338  -2440   2417       C  
ATOM   1318  C   VAL B 106      80.608  19.825  30.496  1.00105.07           C  
ANISOU 1318  C   VAL B 106    12901  18163   8857  -1518  -2402   2146       C  
ATOM   1319  O   VAL B 106      81.762  19.999  30.887  1.00106.83           O  
ANISOU 1319  O   VAL B 106    12912  18659   9018  -1447  -2578   2134       O  
ATOM   1320  CB  VAL B 106      80.419  18.062  28.668  1.00104.02           C  
ANISOU 1320  CB  VAL B 106    12908  17407   9209  -1081  -2402   2318       C  
ATOM   1321  CG1 VAL B 106      81.894  18.264  28.337  1.00105.74           C  
ANISOU 1321  CG1 VAL B 106    12836  17872   9468   -811  -2574   2288       C  
ATOM   1322  CG2 VAL B 106      80.019  16.615  28.393  1.00104.95           C  
ANISOU 1322  CG2 VAL B 106    13322  17089   9465   -933  -2457   2541       C  
ATOM   1323  N   THR B 107      79.725  20.815  30.380  1.00103.22           N  
ANISOU 1323  N   THR B 107    12562  17904   8751  -1698  -2198   1927       N  
ATOM   1324  CA  THR B 107      80.019  22.162  30.879  1.00103.43           C  
ANISOU 1324  CA  THR B 107    12493  18200   8607  -1886  -2206   1665       C  
ATOM   1325  C   THR B 107      80.092  22.170  32.409  1.00106.70           C  
ANISOU 1325  C   THR B 107    12969  18952   8622  -1997  -2343   1753       C  
ATOM   1326  O   THR B 107      81.014  22.745  32.991  1.00108.72           O  
ANISOU 1326  O   THR B 107    13095  19484   8728  -2054  -2533   1688       O  
ATOM   1327  CB  THR B 107      78.969  23.172  30.417  1.00100.86           C  
ANISOU 1327  CB  THR B 107    12246  17737   8341  -2031  -1976   1365       C  
ATOM   1328  OG1 THR B 107      79.253  23.580  29.074  1.00 98.50           O  
ANISOU 1328  OG1 THR B 107    11830  17238   8356  -1982  -1920   1229       O  
ATOM   1329  CG2 THR B 107      78.977  24.399  31.316  1.00102.47           C  
ANISOU 1329  CG2 THR B 107    12492  18191   8250  -2223  -2023   1109       C  
ATOM   1330  N   ALA B 108      79.124  21.512  33.043  1.00108.33           N  
ANISOU 1330  N   ALA B 108    13420  19223   8518  -1801  -2222   1908       N  
ATOM   1331  CA  ALA B 108      79.090  21.372  34.495  1.00111.96           C  
ANISOU 1331  CA  ALA B 108    13954  20024   8562  -1886  -2352   2070       C  
ATOM   1332  C   ALA B 108      80.326  20.663  35.042  1.00114.70           C  
ANISOU 1332  C   ALA B 108    14203  20513   8866  -1741  -2663   2310       C  
ATOM   1333  O   ALA B 108      80.886  21.084  36.054  1.00116.70           O  
ANISOU 1333  O   ALA B 108    14341  21090   8909  -1808  -2834   2198       O  
ATOM   1334  CB  ALA B 108      77.831  20.644  34.923  1.00113.02           C  
ANISOU 1334  CB  ALA B 108    14269  20139   8535  -1964  -2228   2333       C  
ATOM   1335  N   ALA B 109      80.746  19.593  34.366  1.00117.97           N  
ANISOU 1335  N   ALA B 109    14663  20682   9480  -1160  -2751   2408       N  
ATOM   1336  CA  ALA B 109      81.945  18.845  34.738  1.00120.96           C  
ANISOU 1336  CA  ALA B 109    14938  21167   9853   -916  -3061   2638       C  
ATOM   1337  C   ALA B 109      83.176  19.750  34.769  1.00121.60           C  
ANISOU 1337  C   ALA B 109    14712  21604   9887   -937  -3197   2405       C  
ATOM   1338  O   ALA B 109      83.951  19.723  35.731  1.00125.05           O  
ANISOU 1338  O   ALA B 109    15068  22414  10031   -961  -3434   2498       O  
ATOM   1339  CB  ALA B 109      82.164  17.679  33.783  1.00120.30           C  
ANISOU 1339  CB  ALA B 109    14884  20687  10137   -594  -3104   2782       C  
ATOM   1340  N   LEU B 110      83.335  20.558  33.720  1.00118.69           N  
ANISOU 1340  N   LEU B 110    13894  21501   9702  -1015  -3084   2220       N  
ATOM   1341  CA  LEU B 110      84.462  21.487  33.599  1.00119.41           C  
ANISOU 1341  CA  LEU B 110    13680  21898   9794  -1108  -3204   2016       C  
ATOM   1342  C   LEU B 110      84.362  22.652  34.583  1.00120.76           C  
ANISOU 1342  C   LEU B 110    13894  22351   9637  -1452  -3261   1795       C  
ATOM   1343  O   LEU B 110      85.382  23.196  35.007  1.00123.50           O  
ANISOU 1343  O   LEU B 110    14030  23060   9834  -1556  -3495   1751       O  
ATOM   1344  CB  LEU B 110      84.567  22.030  32.168  1.00116.15           C  
ANISOU 1344  CB  LEU B 110    13120  21274   9737  -1103  -3025   1806       C  
ATOM   1345  CG  LEU B 110      84.832  21.085  31.024  1.00115.21           C  
ANISOU 1345  CG  LEU B 110    12905  20933   9935   -743  -2983   1935       C  
ATOM   1346  CD1 LEU B 110      84.448  21.737  29.712  1.00112.66           C  
ANISOU 1346  CD1 LEU B 110    12417  20537   9851   -828  -2819   1708       C  
ATOM   1347  CD2 LEU B 110      86.286  20.646  31.010  1.00118.89           C  
ANISOU 1347  CD2 LEU B 110    13117  21682  10375   -414  -3247   2143       C  
ATOM   1348  N   ALA B 111      83.133  23.029  34.932  1.00117.79           N  
ANISOU 1348  N   ALA B 111    13813  21727   9216  -1573  -3131   1867       N  
ATOM   1349  CA  ALA B 111      82.888  24.125  35.865  1.00119.35           C  
ANISOU 1349  CA  ALA B 111    14125  22139   9083  -1835  -3163   1597       C  
ATOM   1350  C   ALA B 111      83.326  23.781  37.293  1.00123.73           C  
ANISOU 1350  C   ALA B 111    14701  23108   9202  -1861  -3407   1772       C  
ATOM   1351  O   ALA B 111      83.767  24.657  38.039  1.00126.36           O  
ANISOU 1351  O   ALA B 111    14996  23735   9280  -2054  -3602   1587       O  
ATOM   1352  CB  ALA B 111      81.425  24.536  35.835  1.00117.30           C  
ANISOU 1352  CB  ALA B 111    14117  21675   8776  -1895  -2874   1400       C  
ATOM   1353  N   THR B 112      83.211  22.510  37.671  1.00126.18           N  
ANISOU 1353  N   THR B 112    15180  23304   9458  -1249  -3355   2244       N  
ATOM   1354  CA  THR B 112      83.639  22.077  39.002  1.00130.65           C  
ANISOU 1354  CA  THR B 112    15767  24262   9611  -1254  -3612   2468       C  
ATOM   1355  C   THR B 112      85.112  21.685  39.023  1.00132.98           C  
ANISOU 1355  C   THR B 112    15770  24777   9981  -1122  -3938   2606       C  
ATOM   1356  O   THR B 112      85.744  21.730  40.071  1.00136.56           O  
ANISOU 1356  O   THR B 112    16140  25637  10110  -1233  -4192   2588       O  
ATOM   1357  CB  THR B 112      82.824  20.879  39.490  1.00132.11           C  
ANISOU 1357  CB  THR B 112    16167  24396   9633  -1154  -3574   2877       C  
ATOM   1358  OG1 THR B 112      83.010  19.776  38.596  1.00130.58           O  
ANISOU 1358  OG1 THR B 112    15961  23822   9833   -902  -3570   3139       O  
ATOM   1359  CG2 THR B 112      81.345  21.227  39.543  1.00130.89           C  
ANISOU 1359  CG2 THR B 112    16224  24193   9314  -1318  -3265   2758       C  
ATOM   1360  N   TRP B 113      85.651  21.297  37.868  1.00137.61           N  
ANISOU 1360  N   TRP B 113    15641  25528  11117   -468  -3567   2845       N  
ATOM   1361  CA  TRP B 113      87.088  21.056  37.725  1.00140.27           C  
ANISOU 1361  CA  TRP B 113    15621  26152  11523   -284  -3858   2960       C  
ATOM   1362  C   TRP B 113      87.852  22.369  37.886  1.00141.45           C  
ANISOU 1362  C   TRP B 113    15506  26661  11576   -593  -3990   2661       C  
ATOM   1363  O   TRP B 113      88.962  22.391  38.416  1.00145.13           O  
ANISOU 1363  O   TRP B 113    15676  27555  11913   -564  -4288   2753       O  
ATOM   1364  CB  TRP B 113      87.396  20.398  36.372  1.00138.42           C  
ANISOU 1364  CB  TRP B 113    15225  25644  11726     63  -3785   3053       C  
ATOM   1365  CG  TRP B 113      88.869  20.306  36.021  1.00141.26           C  
ANISOU 1365  CG  TRP B 113    15117  26399  12156    254  -4032   3091       C  
ATOM   1366  CD1 TRP B 113      89.889  19.919  36.843  1.00146.09           C  
ANISOU 1366  CD1 TRP B 113    15522  27468  12519    383  -4379   3286       C  
ATOM   1367  CD2 TRP B 113      89.467  20.581  34.746  1.00139.91           C  
ANISOU 1367  CD2 TRP B 113    14592  26271  12296    335  -3947   2944       C  
ATOM   1368  NE1 TRP B 113      91.084  19.954  36.166  1.00147.93           N  
ANISOU 1368  NE1 TRP B 113    15259  28053  12893    548  -4511   3259       N  
ATOM   1369  CE2 TRP B 113      90.855  20.353  34.877  1.00144.29           C  
ANISOU 1369  CE2 TRP B 113    14694  27363  12765    513  -4241   3057       C  
ATOM   1370  CE3 TRP B 113      88.964  21.004  33.504  1.00135.77           C  
ANISOU 1370  CE3 TRP B 113    14071  25423  12093    280  -3652   2743       C  
ATOM   1371  CZ2 TRP B 113      91.749  20.531  33.817  1.00144.84           C  
ANISOU 1371  CZ2 TRP B 113    14291  27702  13039    622  -4227   2977       C  
ATOM   1372  CZ3 TRP B 113      89.856  21.183  32.446  1.00136.17           C  
ANISOU 1372  CZ3 TRP B 113    13688  25707  12342    376  -3642   2669       C  
ATOM   1373  CH2 TRP B 113      91.230  20.946  32.611  1.00140.73           C  
ANISOU 1373  CH2 TRP B 113    13796  26864  12812    538  -3916   2785       C  
ATOM   1374  N   PHE B 114      87.238  23.460  37.434  1.00137.31           N  
ANISOU 1374  N   PHE B 114    14935  26478  10757  -1590  -4212   2347       N  
ATOM   1375  CA  PHE B 114      87.800  24.793  37.611  1.00138.86           C  
ANISOU 1375  CA  PHE B 114    14999  26916  10846  -1961  -4359   2052       C  
ATOM   1376  C   PHE B 114      87.551  25.315  39.026  1.00142.18           C  
ANISOU 1376  C   PHE B 114    15642  27604  10776  -2181  -4526   1938       C  
ATOM   1377  O   PHE B 114      88.383  26.038  39.578  1.00145.93           O  
ANISOU 1377  O   PHE B 114    15958  28468  11022  -2408  -4829   1855       O  
ATOM   1378  CB  PHE B 114      87.246  25.767  36.566  1.00135.17           C  
ANISOU 1378  CB  PHE B 114    14630  26072  10657  -2158  -4113   1743       C  
ATOM   1379  CG  PHE B 114      87.809  25.571  35.174  1.00133.38           C  
ANISOU 1379  CG  PHE B 114    14072  25773  10835  -2058  -4041   1808       C  
ATOM   1380  CD1 PHE B 114      88.892  24.717  34.942  1.00133.86           C  
ANISOU 1380  CD1 PHE B 114    13868  25941  11051  -1657  -4079   2113       C  
ATOM   1381  CD2 PHE B 114      87.274  26.271  34.098  1.00131.73           C  
ANISOU 1381  CD2 PHE B 114    13835  25388  10828  -2340  -3946   1569       C  
ATOM   1382  CE1 PHE B 114      89.414  24.547  33.656  1.00132.78           C  
ANISOU 1382  CE1 PHE B 114    13403  25811  11236  -1523  -3998   2142       C  
ATOM   1383  CE2 PHE B 114      87.793  26.112  32.817  1.00130.62           C  
ANISOU 1383  CE2 PHE B 114    13365  25265  11000  -2263  -3870   1648       C  
ATOM   1384  CZ  PHE B 114      88.868  25.246  32.597  1.00131.17           C  
ANISOU 1384  CZ  PHE B 114    13134  25513  11192  -1841  -3884   1921       C  
ATOM   1385  N   VAL B 115      86.410  24.945  39.606  1.00140.18           N  
ANISOU 1385  N   VAL B 115    16095  27035  10131  -2306  -4591   2046       N  
ATOM   1386  CA  VAL B 115      86.102  25.251  41.009  1.00143.66           C  
ANISOU 1386  CA  VAL B 115    16763  27779  10044  -2447  -4708   1965       C  
ATOM   1387  C   VAL B 115      86.971  24.421  41.971  1.00148.22           C  
ANISOU 1387  C   VAL B 115    17208  28807  10301  -2336  -5033   2319       C  
ATOM   1388  O   VAL B 115      87.351  24.895  43.042  1.00152.16           O  
ANISOU 1388  O   VAL B 115    17751  29687  10374  -2524  -5268   2207       O  
ATOM   1389  CB  VAL B 115      84.584  25.075  41.311  1.00141.84           C  
ANISOU 1389  CB  VAL B 115    16882  27339   9672  -2400  -4373   1891       C  
ATOM   1390  CG1 VAL B 115      84.334  24.672  42.765  1.00145.78           C  
ANISOU 1390  CG1 VAL B 115    17553  28221   9616  -2400  -4455   2052       C  
ATOM   1391  CG2 VAL B 115      83.824  26.348  40.974  1.00140.09           C  
ANISOU 1391  CG2 VAL B 115    16848  26886   9495  -2578  -4199   1395       C  
ATOM   1392  N   GLY B 116      87.288  23.192  41.565  1.00160.66           N  
ANISOU 1392  N   GLY B 116    17176  31215  12651   -889  -5022   4330       N  
ATOM   1393  CA  GLY B 116      88.176  22.306  42.316  1.00165.14           C  
ANISOU 1393  CA  GLY B 116    17581  32161  13002   -705  -5371   4693       C  
ATOM   1394  C   GLY B 116      89.619  22.775  42.320  1.00167.56           C  
ANISOU 1394  C   GLY B 116    17449  32834  13383   -762  -5678   4619       C  
ATOM   1395  O   GLY B 116      90.533  21.990  42.572  1.00169.88           O  
ANISOU 1395  O   GLY B 116    17458  33325  13764   -461  -5901   4915       O  
ATOM   1396  N   ARG B 117      89.823  24.055  42.014  1.00184.19           N  
ANISOU 1396  N   ARG B 117    17796  38102  14086  -3558  -6657   5304       N  
ATOM   1397  CA  ARG B 117      91.102  24.725  42.215  1.00187.77           C  
ANISOU 1397  CA  ARG B 117    17873  39008  14464  -3792  -6996   5201       C  
ATOM   1398  C   ARG B 117      90.874  26.036  42.967  1.00189.21           C  
ANISOU 1398  C   ARG B 117    18315  39246  14332  -4266  -7065   4779       C  
ATOM   1399  O   ARG B 117      91.096  27.132  42.442  1.00188.61           O  
ANISOU 1399  O   ARG B 117    18188  39062  14412  -4609  -7073   4467       O  
ATOM   1400  CB  ARG B 117      91.843  24.938  40.892  1.00185.93           C  
ANISOU 1400  CB  ARG B 117    17232  38718  14694  -3763  -6937   5184       C  
ATOM   1401  CG  ARG B 117      92.407  23.654  40.307  1.00186.61           C  
ANISOU 1401  CG  ARG B 117    17003  38912  14988  -3242  -6993   5572       C  
ATOM   1402  CD  ARG B 117      93.660  23.907  39.495  1.00188.40           C  
ANISOU 1402  CD  ARG B 117    16638  39517  15429  -3253  -7134   5580       C  
ATOM   1403  NE  ARG B 117      94.247  22.661  39.007  1.00189.62           N  
ANISOU 1403  NE  ARG B 117    16483  39795  15769  -2661  -7188   5902       N  
ATOM   1404  CZ  ARG B 117      95.525  22.506  38.663  1.00192.71           C  
ANISOU 1404  CZ  ARG B 117    16267  40689  16264  -2515  -7355   5983       C  
ATOM   1405  NH1 ARG B 117      96.378  23.520  38.751  1.00194.91           N  
ANISOU 1405  NH1 ARG B 117    16156  41416  16485  -2997  -7492   5809       N  
ATOM   1406  NH2 ARG B 117      95.955  21.328  38.233  1.00194.15           N  
ANISOU 1406  NH2 ARG B 117    16226  40944  16599  -1881  -7399   6239       N  
ATOM   1407  N   GLU B 118      90.395  25.888  44.201  1.00200.99           N  
ANISOU 1407  N   GLU B 118    22768  41220  12380  -8561  -7673   3088       N  
ATOM   1408  CA  GLU B 118      90.194  26.989  45.141  1.00204.12           C  
ANISOU 1408  CA  GLU B 118    23446  41795  12315  -8909  -7816   2715       C  
ATOM   1409  C   GLU B 118      91.411  27.125  46.056  1.00210.08           C  
ANISOU 1409  C   GLU B 118    23951  43158  12713  -9076  -8299   2795       C  
ATOM   1410  O   GLU B 118      91.591  28.151  46.715  1.00213.26           O  
ANISOU 1410  O   GLU B 118    24460  43724  12845  -9465  -8528   2439       O  
ATOM   1411  CB  GLU B 118      88.933  26.747  45.979  1.00204.19           C  
ANISOU 1411  CB  GLU B 118    23880  41765  11937  -8780  -7604   2706       C  
ATOM   1412  CG  GLU B 118      88.992  25.501  46.868  1.00206.97           C  
ANISOU 1412  CG  GLU B 118    24202  42453  11984  -8519  -7726   3194       C  
ATOM   1413  CD  GLU B 118      87.622  24.944  47.216  1.00205.59           C  
ANISOU 1413  CD  GLU B 118    24372  42127  11616  -8363  -7391   3322       C  
ATOM   1414  OE1 GLU B 118      86.671  25.737  47.376  1.00204.63           O  
ANISOU 1414  OE1 GLU B 118    24531  41887  11332  -8491  -7154   2940       O  
ATOM   1415  OE2 GLU B 118      87.501  23.706  47.334  1.00205.93           O  
ANISOU 1415  OE2 GLU B 118    24408  42177  11660  -8113  -7376   3811       O  
ATOM   1416  N   GLN B 119      92.233  26.076  46.081  1.00258.16           N  
ANISOU 1416  N   GLN B 119    23655  57389  17044 -10513 -11346   8635       N  
ATOM   1417  CA  GLN B 119      93.447  26.002  46.896  1.00260.31           C  
ANISOU 1417  CA  GLN B 119    23927  57570  17409 -10201 -11724   8457       C  
ATOM   1418  C   GLN B 119      94.479  27.057  46.507  1.00260.75           C  
ANISOU 1418  C   GLN B 119    23734  57567  17771 -10427 -11927   8101       C  
ATOM   1419  O   GLN B 119      94.556  28.116  47.126  1.00261.97           O  
ANISOU 1419  O   GLN B 119    24155  57557  17823 -10663 -12074   7652       O  
ATOM   1420  CB  GLN B 119      94.056  24.600  46.791  1.00260.74           C  
ANISOU 1420  CB  GLN B 119    23777  57666  17626  -9687 -11816   8877       C  
ATOM   1421  CG  GLN B 119      94.397  24.164  45.366  1.00259.53           C  
ANISOU 1421  CG  GLN B 119    23096  57636  17877  -9633 -11753   9105       C  
ATOM   1422  CD  GLN B 119      93.866  22.781  45.015  1.00258.86           C  
ANISOU 1422  CD  GLN B 119    22950  57579  17827  -9328 -11587   9627       C  
ATOM   1423  OE1 GLN B 119      94.437  22.081  44.180  1.00258.87           O  
ANISOU 1423  OE1 GLN B 119    22591  57638  18129  -9047 -11615   9830       O  
ATOM   1424  NE2 GLN B 119      92.760  22.388  45.640  1.00258.52           N  
ANISOU 1424  NE2 GLN B 119    23279  57464  17482  -9371 -11414   9826       N  
TER    1425      GLN B 119                                                      
ATOM   1426  N   ALA C  23      95.900  32.012  36.449  1.00237.76           N  
ANISOU 1426  N   ALA C  23    21446  56042  12851 -17159  -6430    898       N  
ATOM   1427  CA  ALA C  23      95.251  30.828  37.082  1.00237.57           C  
ANISOU 1427  CA  ALA C  23    21487  56320  12457 -16804  -6348   1018       C  
ATOM   1428  C   ALA C  23      95.145  29.675  36.084  1.00236.53           C  
ANISOU 1428  C   ALA C  23    20905  56637  12327 -16495  -6080   1342       C  
ATOM   1429  O   ALA C  23      95.980  29.558  35.184  1.00236.97           O  
ANISOU 1429  O   ALA C  23    20508  56835  12696 -16291  -6098   1488       O  
ATOM   1430  CB  ALA C  23      93.880  31.211  37.630  1.00236.79           C  
ANISOU 1430  CB  ALA C  23    21915  56085  11971 -17043  -6205    814       C  
ATOM   1431  N   LEU C  24      94.138  28.819  36.258  1.00207.80           N  
ANISOU 1431  N   LEU C  24    15152  51615  12187  -6901  -6212   2784       N  
ATOM   1432  CA  LEU C  24      93.838  27.763  35.293  1.00204.40           C  
ANISOU 1432  CA  LEU C  24    14556  51058  12048  -6337  -5922   2989       C  
ATOM   1433  C   LEU C  24      92.575  28.106  34.525  1.00198.91           C  
ANISOU 1433  C   LEU C  24    14357  49643  11576  -6311  -5565   2808       C  
ATOM   1434  O   LEU C  24      92.604  28.207  33.301  1.00196.41           O  
ANISOU 1434  O   LEU C  24    13932  49140  11554  -6310  -5342   2801       O  
ATOM   1435  CB  LEU C  24      93.674  26.398  35.971  1.00204.89           C  
ANISOU 1435  CB  LEU C  24    14626  51233  11991  -5754  -5968   3231       C  
ATOM   1436  CG  LEU C  24      93.275  25.230  35.059  1.00201.52           C  
ANISOU 1436  CG  LEU C  24    14182  50524  11862  -5158  -5689   3407       C  
ATOM   1437  CD1 LEU C  24      94.491  24.582  34.418  1.00204.79           C  
ANISOU 1437  CD1 LEU C  24    13996  51471  12345  -4774  -5819   3641       C  
ATOM   1438  CD2 LEU C  24      92.462  24.196  35.815  1.00199.56           C  
ANISOU 1438  CD2 LEU C  24    14403  49888  11533  -4800  -5598   3512       C  
ATOM   1439  N   HIS C  25      91.471  28.288  35.248  1.00159.19           N  
ANISOU 1439  N   HIS C  25    15210  34397  10879  -5687  -4956    915       N  
ATOM   1440  CA  HIS C  25      90.159  28.554  34.640  1.00154.41           C  
ANISOU 1440  CA  HIS C  25    15057  33156  10457  -5642  -4625    730       C  
ATOM   1441  C   HIS C  25      90.200  29.699  33.626  1.00153.39           C  
ANISOU 1441  C   HIS C  25    14907  32810  10566  -6014  -4549    566       C  
ATOM   1442  O   HIS C  25      89.644  29.596  32.538  1.00150.27           O  
ANISOU 1442  O   HIS C  25    14426  32203  10468  -5850  -4303    631       O  
ATOM   1443  CB  HIS C  25      89.095  28.805  35.724  1.00154.30           C  
ANISOU 1443  CB  HIS C  25    15559  32916  10153  -5675  -4611    527       C  
ATOM   1444  CG  HIS C  25      89.233  30.118  36.437  1.00157.28           C  
ANISOU 1444  CG  HIS C  25    16181  33283  10295  -6159  -4832    196       C  
ATOM   1445  ND1 HIS C  25      88.748  30.321  37.709  1.00156.93           N  
ANISOU 1445  ND1 HIS C  25    16644  32941  10041  -6185  -4757   -102       N  
ATOM   1446  CD2 HIS C  25      89.802  31.285  36.059  1.00161.20           C  
ANISOU 1446  CD2 HIS C  25    16505  34027  10718  -6634  -5144    102       C  
ATOM   1447  CE1 HIS C  25      89.011  31.559  38.086  1.00160.45           C  
ANISOU 1447  CE1 HIS C  25    17271  33390  10303  -6615  -5022   -392       C  
ATOM   1448  NE2 HIS C  25      89.647  32.166  37.102  1.00163.08           N  
ANISOU 1448  NE2 HIS C  25    17210  34031  10721  -6935  -5271   -264       N  
ATOM   1449  N   TRP C  26      90.903  30.766  33.991  1.00170.08           N  
ANISOU 1449  N   TRP C  26    19794  33040  11790 -10052  -2552  -1773       N  
ATOM   1450  CA  TRP C  26      90.996  31.979  33.194  1.00170.36           C  
ANISOU 1450  CA  TRP C  26    19911  32833  11986 -10522  -2568  -1926       C  
ATOM   1451  C   TRP C  26      91.921  31.778  31.991  1.00170.70           C  
ANISOU 1451  C   TRP C  26    19415  33174  12268 -10605  -2509  -1693       C  
ATOM   1452  O   TRP C  26      91.767  32.442  30.965  1.00169.95           O  
ANISOU 1452  O   TRP C  26    19393  32819  12361 -10908  -2424  -1747       O  
ATOM   1453  CB  TRP C  26      91.529  33.102  34.085  1.00175.51           C  
ANISOU 1453  CB  TRP C  26    20689  33636  12359 -11085  -2958  -2117       C  
ATOM   1454  CG  TRP C  26      90.643  34.323  34.254  1.00175.69           C  
ANISOU 1454  CG  TRP C  26    21338  33076  12342 -11394  -3006  -2483       C  
ATOM   1455  CD1 TRP C  26      90.967  35.463  34.931  1.00180.50           C  
ANISOU 1455  CD1 TRP C  26    22197  33645  12739 -11943  -3371  -2719       C  
ATOM   1456  CD2 TRP C  26      89.311  34.527  33.747  1.00171.54           C  
ANISOU 1456  CD2 TRP C  26    21285  31916  11978 -11154  -2712  -2676       C  
ATOM   1457  NE1 TRP C  26      89.929  36.359  34.886  1.00179.73           N  
ANISOU 1457  NE1 TRP C  26    22739  32888  12664 -12015  -3328  -3064       N  
ATOM   1458  CE2 TRP C  26      88.901  35.813  34.166  1.00174.25           C  
ANISOU 1458  CE2 TRP C  26    22164  31848  12194 -11523  -2919  -3037       C  
ATOM   1459  CE3 TRP C  26      88.427  33.752  32.980  1.00166.21           C  
ANISOU 1459  CE3 TRP C  26    20638  30979  11537 -10661  -2316  -2584       C  
ATOM   1460  CZ2 TRP C  26      87.646  36.344  33.845  1.00171.87           C  
ANISOU 1460  CZ2 TRP C  26    22397  30915  11990 -11354  -2734  -3310       C  
ATOM   1461  CZ3 TRP C  26      87.178  34.280  32.662  1.00163.69           C  
ANISOU 1461  CZ3 TRP C  26    20811  30072  11310 -10549  -2127  -2837       C  
ATOM   1462  CH2 TRP C  26      86.801  35.566  33.095  1.00166.55           C  
ANISOU 1462  CH2 TRP C  26    21678  30065  11540 -10865  -2334  -3197       C  
ATOM   1463  N   ARG C  27      92.869  30.853  32.126  1.00171.27           N  
ANISOU 1463  N   ARG C  27    16273  37435  11367  -9396  -4388   -307       N  
ATOM   1464  CA  ARG C  27      93.905  30.620  31.113  1.00173.02           C  
ANISOU 1464  CA  ARG C  27    15880  38127  11732  -9460  -4365    -94       C  
ATOM   1465  C   ARG C  27      93.611  29.432  30.199  1.00169.87           C  
ANISOU 1465  C   ARG C  27    15260  37737  11544  -8803  -4068     77       C  
ATOM   1466  O   ARG C  27      94.018  29.434  29.037  1.00169.91           O  
ANISOU 1466  O   ARG C  27    14903  37941  11713  -8797  -3924    179       O  
ATOM   1467  CB  ARG C  27      95.269  30.436  31.779  1.00179.03           C  
ANISOU 1467  CB  ARG C  27    16090  39672  12260  -9682  -4721     50       C  
ATOM   1468  N   ALA C  28      92.921  28.421  30.729  1.00149.72           N  
ANISOU 1468  N   ALA C  28    12593  32828  11464  -3686  -5057   3054       N  
ATOM   1469  CA  ALA C  28      92.523  27.246  29.952  1.00146.74           C  
ANISOU 1469  CA  ALA C  28    12163  32297  11293  -3064  -4802   3182       C  
ATOM   1470  C   ALA C  28      91.501  27.632  28.888  1.00142.20           C  
ANISOU 1470  C   ALA C  28    11887  31171  10973  -3124  -4486   3050       C  
ATOM   1471  O   ALA C  28      91.513  27.098  27.774  1.00140.72           O  
ANISOU 1471  O   ALA C  28    11502  30985  10982  -2830  -4281   3125       O  
ATOM   1472  CB  ALA C  28      91.960  26.161  30.864  1.00145.70           C  
ANISOU 1472  CB  ALA C  28    12345  31954  11059  -2618  -4823   3255       C  
ATOM   1473  N   ALA C  29      90.628  28.572  29.247  1.00126.32           N  
ANISOU 1473  N   ALA C  29    12563  24876  10556  -3560  -3854   1098       N  
ATOM   1474  CA  ALA C  29      89.609  29.097  28.348  1.00122.37           C  
ANISOU 1474  CA  ALA C  29    12409  23820  10265  -3631  -3597    955       C  
ATOM   1475  C   ALA C  29      90.238  29.880  27.197  1.00123.35           C  
ANISOU 1475  C   ALA C  29    12271  24077  10520  -3983  -3558    983       C  
ATOM   1476  O   ALA C  29      89.977  29.593  26.029  1.00121.76           O  
ANISOU 1476  O   ALA C  29    11855  23912  10495  -3731  -3345   1084       O  
ATOM   1477  CB  ALA C  29      88.621  29.963  29.119  1.00121.42           C  
ANISOU 1477  CB  ALA C  29    12846  23253  10035  -3869  -3633    706       C  
ATOM   1478  N   GLY C  30      91.074  30.857  27.528  1.00130.82           N  
ANISOU 1478  N   GLY C  30    13128  23965  12613  -4432  -2632    685       N  
ATOM   1479  CA  GLY C  30      91.791  31.626  26.515  1.00132.67           C  
ANISOU 1479  CA  GLY C  30    13088  24384  12937  -4852  -2624    776       C  
ATOM   1480  C   GLY C  30      92.551  30.755  25.525  1.00133.37           C  
ANISOU 1480  C   GLY C  30    12551  25018  13104  -4554  -2467   1005       C  
ATOM   1481  O   GLY C  30      92.699  31.119  24.357  1.00133.03           O  
ANISOU 1481  O   GLY C  30    12374  24990  13180  -4700  -2302   1076       O  
ATOM   1482  N   ALA C  31      93.028  29.603  25.996  1.00127.94           N  
ANISOU 1482  N   ALA C  31    11550  25862  11201  -3845  -3996   1197       N  
ATOM   1483  CA  ALA C  31      93.773  28.658  25.166  1.00129.63           C  
ANISOU 1483  CA  ALA C  31    11152  26652  11449  -3474  -3883   1377       C  
ATOM   1484  C   ALA C  31      92.842  27.811  24.314  1.00125.37           C  
ANISOU 1484  C   ALA C  31    10791  25742  11102  -2858  -3579   1351       C  
ATOM   1485  O   ALA C  31      93.212  27.385  23.223  1.00126.15           O  
ANISOU 1485  O   ALA C  31    10506  26169  11255  -2559  -3422   1434       O  
ATOM   1486  CB  ALA C  31      94.656  27.769  26.029  1.00133.73           C  
ANISOU 1486  CB  ALA C  31    11212  27812  11788  -3201  -4115   1504       C  
ATOM   1487  N   ALA C  32      91.638  27.568  24.821  1.00121.65           N  
ANISOU 1487  N   ALA C  32    10730  24736  10756  -2694  -3484   1302       N  
ATOM   1488  CA  ALA C  32      90.624  26.819  24.082  1.00117.77           C  
ANISOU 1488  CA  ALA C  32    10439  23850  10457  -2224  -3209   1271       C  
ATOM   1489  C   ALA C  32      90.120  27.589  22.859  1.00115.87           C  
ANISOU 1489  C   ALA C  32    10307  23372  10346  -2544  -3013   1208       C  
ATOM   1490  O   ALA C  32      89.772  26.978  21.842  1.00115.30           O  
ANISOU 1490  O   ALA C  32    10033  23408  10368  -2301  -2809   1247       O  
ATOM   1491  CB  ALA C  32      89.462  26.438  24.992  1.00114.31           C  
ANISOU 1491  CB  ALA C  32    10542  22830  10061  -1967  -3173   1189       C  
ATOM   1492  N   THR C  33      90.078  28.918  22.961  1.00120.03           N  
ANISOU 1492  N   THR C  33    10789  23929  10887  -4106  -3271   2573       N  
ATOM   1493  CA  THR C  33      89.668  29.777  21.838  1.00118.89           C  
ANISOU 1493  CA  THR C  33    10769  23550  10853  -4417  -3128   2550       C  
ATOM   1494  C   THR C  33      90.749  29.834  20.757  1.00122.13           C  
ANISOU 1494  C   THR C  33    10574  24607  11224  -4515  -3059   2733       C  
ATOM   1495  O   THR C  33      90.447  29.983  19.575  1.00120.78           O  
ANISOU 1495  O   THR C  33    10393  24353  11143  -4465  -2846   2758       O  
ATOM   1496  CB  THR C  33      89.378  31.204  22.301  1.00119.19           C  
ANISOU 1496  CB  THR C  33    11253  23171  10863  -4976  -3281   2421       C  
ATOM   1497  OG1 THR C  33      90.562  31.774  22.870  1.00124.03           O  
ANISOU 1497  OG1 THR C  33    11592  24204  11331  -5540  -3528   2511       O  
ATOM   1498  CG2 THR C  33      88.275  31.211  23.349  1.00117.45           C  
ANISOU 1498  CG2 THR C  33    11468  22572  10587  -4806  -3365   2244       C  
ATOM   1499  N   VAL C  34      92.006  29.708  21.171  1.00132.80           N  
ANISOU 1499  N   VAL C  34    10939  28320  11198  -5437  -2804   1698       N  
ATOM   1500  CA  VAL C  34      93.110  29.554  20.228  1.00136.07           C  
ANISOU 1500  CA  VAL C  34    10707  29450  11545  -5352  -2698   1859       C  
ATOM   1501  C   VAL C  34      92.996  28.193  19.545  1.00134.30           C  
ANISOU 1501  C   VAL C  34    10362  29269  11395  -4555  -2481   1828       C  
ATOM   1502  O   VAL C  34      93.367  28.043  18.381  1.00134.93           O  
ANISOU 1502  O   VAL C  34    10175  29617  11477  -4409  -2274   1870       O  
ATOM   1503  CB  VAL C  34      94.473  29.710  20.925  1.00141.88           C  
ANISOU 1503  CB  VAL C  34    10825  31006  12078  -5597  -2925   2007       C  
ATOM   1504  CG1 VAL C  34      95.565  29.022  20.121  1.00145.71           C  
ANISOU 1504  CG1 VAL C  34    10592  32306  12464  -5514  -2770   2170       C  
ATOM   1505  CG2 VAL C  34      94.800  31.182  21.131  1.00144.21           C  
ANISOU 1505  CG2 VAL C  34    11288  31212  12293  -6445  -3180   2026       C  
ATOM   1506  N   LEU C  35      92.469  27.210  20.264  1.00129.28           N  
ANISOU 1506  N   LEU C  35    10114  28378  10628  -3376  -2560   1819       N  
ATOM   1507  CA  LEU C  35      92.275  25.883  19.701  1.00126.99           C  
ANISOU 1507  CA  LEU C  35     9930  27866  10456  -2683  -2364   1755       C  
ATOM   1508  C   LEU C  35      91.081  25.838  18.747  1.00122.60           C  
ANISOU 1508  C   LEU C  35     9807  26715  10062  -2716  -2125   1649       C  
ATOM   1509  O   LEU C  35      91.106  25.090  17.767  1.00122.92           O  
ANISOU 1509  O   LEU C  35     9656  26932  10116  -2468  -1932   1641       O  
ATOM   1510  CB  LEU C  35      92.096  24.849  20.815  1.00126.13           C  
ANISOU 1510  CB  LEU C  35    10062  27487  10375  -2165  -2487   1733       C  
ATOM   1511  CG  LEU C  35      92.119  23.381  20.387  1.00129.87           C  
ANISOU 1511  CG  LEU C  35    10070  28489  10784  -1518  -2506   1789       C  
ATOM   1512  CD1 LEU C  35      93.518  22.968  19.957  1.00132.47           C  
ANISOU 1512  CD1 LEU C  35    10333  28986  11014  -1247  -2785   1878       C  
ATOM   1513  CD2 LEU C  35      91.619  22.486  21.510  1.00127.43           C  
ANISOU 1513  CD2 LEU C  35    10038  27753  10625   -952  -2304   1678       C  
ATOM   1514  N   LEU C  36      90.046  26.634  19.031  1.00116.36           N  
ANISOU 1514  N   LEU C  36    10329  23674  10207  -3572  -2617   2841       N  
ATOM   1515  CA  LEU C  36      88.842  26.676  18.188  1.00112.41           C  
ANISOU 1515  CA  LEU C  36    10230  22623   9857  -3561  -2414   2742       C  
ATOM   1516  C   LEU C  36      89.134  27.236  16.791  1.00113.55           C  
ANISOU 1516  C   LEU C  36    10120  23042   9981  -3738  -2247   2798       C  
ATOM   1517  O   LEU C  36      88.629  26.714  15.791  1.00112.03           O  
ANISOU 1517  O   LEU C  36     9972  22743   9853  -3387  -2056   2746       O  
ATOM   1518  CB  LEU C  36      87.702  27.455  18.864  1.00109.68           C  
ANISOU 1518  CB  LEU C  36    10408  21697   9570  -3924  -2472   2643       C  
ATOM   1519  CG  LEU C  36      86.368  27.560  18.097  1.00105.62           C  
ANISOU 1519  CG  LEU C  36    10304  20614   9213  -3786  -2282   2536       C  
ATOM   1520  CD1 LEU C  36      85.728  26.193  17.830  1.00104.12           C  
ANISOU 1520  CD1 LEU C  36    10128  20329   9105  -3201  -2162   2513       C  
ATOM   1521  CD2 LEU C  36      85.378  28.473  18.812  1.00103.19           C  
ANISOU 1521  CD2 LEU C  36    10492  19769   8947  -3966  -2329   2408       C  
ATOM   1522  N   VAL C  37      89.950  28.290  16.733  1.00123.46           N  
ANISOU 1522  N   VAL C  37    11291  24974  10644  -5410  -2564   3364       N  
ATOM   1523  CA  VAL C  37      90.400  28.867  15.464  1.00125.55           C  
ANISOU 1523  CA  VAL C  37    11260  25610  10835  -5665  -2420   3481       C  
ATOM   1524  C   VAL C  37      91.128  27.816  14.620  1.00127.68           C  
ANISOU 1524  C   VAL C  37    11029  26470  11013  -5120  -2249   3503       C  
ATOM   1525  O   VAL C  37      90.875  27.702  13.421  1.00126.42           O  
ANISOU 1525  O   VAL C  37    10932  26229  10872  -4911  -2040   3461       O  
ATOM   1526  CB  VAL C  37      91.263  30.139  15.691  1.00129.58           C  
ANISOU 1526  CB  VAL C  37    11553  26466  11217  -6426  -2588   3647       C  
ATOM   1527  CG1 VAL C  37      92.175  30.425  14.505  1.00133.84           C  
ANISOU 1527  CG1 VAL C  37    11506  27761  11588  -6618  -2464   3842       C  
ATOM   1528  CG2 VAL C  37      90.368  31.333  15.969  1.00127.54           C  
ANISOU 1528  CG2 VAL C  37    11892  25509  11059  -6921  -2671   3603       C  
ATOM   1529  N   ILE C  38      92.005  27.041  15.260  1.00131.48           N  
ANISOU 1529  N   ILE C  38    10203  28750  11004  -4348  -2208   3747       N  
ATOM   1530  CA  ILE C  38      92.689  25.914  14.616  1.00133.80           C  
ANISOU 1530  CA  ILE C  38    10082  29542  11215  -3655  -2078   3705       C  
ATOM   1531  C   ILE C  38      91.695  24.948  13.958  1.00129.92           C  
ANISOU 1531  C   ILE C  38    10038  28455  10871  -3092  -1916   3522       C  
ATOM   1532  O   ILE C  38      91.836  24.621  12.782  1.00130.72           O  
ANISOU 1532  O   ILE C  38     9994  28769  10906  -2852  -1713   3475       O  
ATOM   1533  CB  ILE C  38      93.533  25.115  15.626  1.00136.91           C  
ANISOU 1533  CB  ILE C  38    10145  30336  11538  -3227  -2273   3721       C  
ATOM   1534  CG1 ILE C  38      94.598  26.013  16.260  1.00141.77           C  
ANISOU 1534  CG1 ILE C  38    10202  31695  11971  -3727  -2449   3901       C  
ATOM   1535  CG2 ILE C  38      94.172  23.911  14.951  1.00139.27           C  
ANISOU 1535  CG2 ILE C  38    10158  30978  11779  -2380  -2168   3625       C  
ATOM   1536  CD1 ILE C  38      95.313  25.377  17.432  1.00144.88           C  
ANISOU 1536  CD1 ILE C  38    10189  32643  12215  -4355  -2342   4061       C  
ATOM   1537  N   VAL C  39      90.691  24.514  14.719  1.00120.69           N  
ANISOU 1537  N   VAL C  39     9377  24815  11664  -1524  -1955   3462       N  
ATOM   1538  CA  VAL C  39      89.688  23.557  14.235  1.00117.65           C  
ANISOU 1538  CA  VAL C  39     9409  23874  11418  -1018  -1855   3305       C  
ATOM   1539  C   VAL C  39      88.862  24.114  13.066  1.00114.92           C  
ANISOU 1539  C   VAL C  39     9319  23220  11127  -1206  -1653   3242       C  
ATOM   1540  O   VAL C  39      88.545  23.384  12.117  1.00114.72           O  
ANISOU 1540  O   VAL C  39     9358  23124  11106   -773  -1517   3121       O  
ATOM   1541  CB  VAL C  39      88.780  23.041  15.392  1.00114.79           C  
ANISOU 1541  CB  VAL C  39     9534  22879  11201   -897  -2013   3267       C  
ATOM   1542  CG1 VAL C  39      87.557  22.305  14.860  1.00110.42           C  
ANISOU 1542  CG1 VAL C  39     9534  21606  10815   -829  -1907   3149       C  
ATOM   1543  CG2 VAL C  39      89.571  22.127  16.317  1.00117.65           C  
ANISOU 1543  CG2 VAL C  39     9756  23418  11528   -303  -2163   3276       C  
ATOM   1544  N   LEU C  40      88.532  25.404  13.128  1.00112.13           N  
ANISOU 1544  N   LEU C  40     9991  22031  10583  -2206  -1949   3042       N  
ATOM   1545  CA  LEU C  40      87.804  26.060  12.041  1.00110.43           C  
ANISOU 1545  CA  LEU C  40     9963  21612  10385  -2442  -1787   3033       C  
ATOM   1546  C   LEU C  40      88.589  26.020  10.731  1.00114.01           C  
ANISOU 1546  C   LEU C  40     9943  22734  10642  -2317  -1614   3084       C  
ATOM   1547  O   LEU C  40      88.105  25.478   9.743  1.00113.71           O  
ANISOU 1547  O   LEU C  40     9946  22671  10588  -1852  -1477   2954       O  
ATOM   1548  CB  LEU C  40      87.435  27.505  12.400  1.00109.62           C  
ANISOU 1548  CB  LEU C  40    10071  21270  10309  -3134  -1870   3134       C  
ATOM   1549  CG  LEU C  40      86.768  27.793  13.746  1.00106.87           C  
ANISOU 1549  CG  LEU C  40    10158  20351  10095  -3277  -2035   3060       C  
ATOM   1550  CD1 LEU C  40      85.932  29.058  13.650  1.00106.28           C  
ANISOU 1550  CD1 LEU C  40    10391  19939  10051  -3855  -2108   3098       C  
ATOM   1551  CD2 LEU C  40      85.914  26.626  14.206  1.00103.28           C  
ANISOU 1551  CD2 LEU C  40    10070  19385   9785  -2834  -1982   2910       C  
ATOM   1552  N   LEU C  41      89.800  26.575  10.736  1.00127.14           N  
ANISOU 1552  N   LEU C  41    10247  26828  11233  -3542  -1507   3411       N  
ATOM   1553  CA  LEU C  41      90.640  26.615   9.538  1.00131.22           C  
ANISOU 1553  CA  LEU C  41    10249  28097  11510  -3479  -1320   3488       C  
ATOM   1554  C   LEU C  41      90.939  25.219   8.993  1.00132.69           C  
ANISOU 1554  C   LEU C  41    10235  28561  11621  -2645  -1199   3297       C  
ATOM   1555  O   LEU C  41      90.889  24.999   7.779  1.00133.94           O  
ANISOU 1555  O   LEU C  41    10282  28975  11635  -2435   -996   3240       O  
ATOM   1556  CB  LEU C  41      91.960  27.329   9.833  1.00136.36           C  
ANISOU 1556  CB  LEU C  41    10304  29546  11960  -3992  -1383   3729       C  
ATOM   1557  CG  LEU C  41      91.855  28.782  10.303  1.00135.98           C  
ANISOU 1557  CG  LEU C  41    10488  29207  11973  -4846  -1564   3908       C  
ATOM   1558  CD1 LEU C  41      93.236  29.366  10.558  1.00141.82           C  
ANISOU 1558  CD1 LEU C  41    10630  30774  12480  -5425  -1605   4173       C  
ATOM   1559  CD2 LEU C  41      91.099  29.622   9.285  1.00132.47           C  
ANISOU 1559  CD2 LEU C  41    10635  28051  11645  -5169  -1515   3913       C  
ATOM   1560  N   ALA C  42      91.233  24.283   9.894  1.00137.41           N  
ANISOU 1560  N   ALA C  42     9166  29298  13746   -323  -1141   2240       N  
ATOM   1561  CA  ALA C  42      91.522  22.900   9.518  1.00139.64           C  
ANISOU 1561  CA  ALA C  42     9312  29784  13961    511  -1085   2046       C  
ATOM   1562  C   ALA C  42      90.276  22.199   9.009  1.00135.93           C  
ANISOU 1562  C   ALA C  42     9429  28579  13641    844  -1029   1841       C  
ATOM   1563  O   ALA C  42      90.346  21.419   8.060  1.00137.80           O  
ANISOU 1563  O   ALA C  42     9601  29001  13756   1326   -891   1675       O  
ATOM   1564  CB  ALA C  42      92.112  22.138  10.690  1.00141.24           C  
ANISOU 1564  CB  ALA C  42     9417  30031  14217    907  -1296   2027       C  
ATOM   1565  N   GLY C  43      89.143  22.484   9.650  1.00121.81           N  
ANISOU 1565  N   GLY C  43     9309  23788  13184   1135  -1009   1812       N  
ATOM   1566  CA  GLY C  43      87.847  21.935   9.248  1.00117.98           C  
ANISOU 1566  CA  GLY C  43     9406  22560  12861   1305   -981   1650       C  
ATOM   1567  C   GLY C  43      87.370  22.458   7.904  1.00117.22           C  
ANISOU 1567  C   GLY C  43     9363  22499  12675   1117   -783   1623       C  
ATOM   1568  O   GLY C  43      86.920  21.683   7.058  1.00117.61           O  
ANISOU 1568  O   GLY C  43     9558  22447  12682   1544   -701   1436       O  
ATOM   1569  N   SER C  44      87.471  23.775   7.714  1.00117.04           N  
ANISOU 1569  N   SER C  44     9615  23227  11626   -580   -515   1899       N  
ATOM   1570  CA  SER C  44      87.129  24.427   6.448  1.00117.69           C  
ANISOU 1570  CA  SER C  44     9633  23529  11554   -837   -337   1958       C  
ATOM   1571  C   SER C  44      87.901  23.809   5.302  1.00121.80           C  
ANISOU 1571  C   SER C  44     9773  24687  11817   -350   -168   1848       C  
ATOM   1572  O   SER C  44      87.324  23.390   4.311  1.00121.29           O  
ANISOU 1572  O   SER C  44     9931  24427  11726     43    -92   1652       O  
ATOM   1573  CB  SER C  44      87.443  25.925   6.497  1.00119.39           C  
ANISOU 1573  CB  SER C  44     9591  24105  11667  -1550   -341   2235       C  
ATOM   1574  OG  SER C  44      86.725  26.574   7.528  1.00116.00           O  
ANISOU 1574  OG  SER C  44     9581  23056  11438  -2025   -485   2310       O  
ATOM   1575  N   TYR C  45      89.214  23.743   5.461  1.00140.70           N  
ANISOU 1575  N   TYR C  45     9593  30356  13512   -678    428    761       N  
ATOM   1576  CA  TYR C  45      90.089  23.279   4.403  1.00145.48           C  
ANISOU 1576  CA  TYR C  45     9749  31715  13813   -233    615    666       C  
ATOM   1577  C   TYR C  45      90.025  21.764   4.206  1.00146.65           C  
ANISOU 1577  C   TYR C  45    10008  31734  13978    670    581    340       C  
ATOM   1578  O   TYR C  45      90.432  21.258   3.158  1.00151.14           O  
ANISOU 1578  O   TYR C  45    10235  32917  14275   1183    729    188       O  
ATOM   1579  CB  TYR C  45      91.525  23.763   4.657  1.00150.76           C  
ANISOU 1579  CB  TYR C  45     9669  33376  14236   -500    664    894       C  
ATOM   1580  CG  TYR C  45      91.743  25.250   4.384  1.00151.16           C  
ANISOU 1580  CG  TYR C  45     9597  33633  14205  -1430    697   1236       C  
ATOM   1581  CD1 TYR C  45      90.740  26.200   4.668  1.00146.23           C  
ANISOU 1581  CD1 TYR C  45     9570  32165  13827  -1997    577   1336       C  
ATOM   1582  CD2 TYR C  45      92.959  25.709   3.855  1.00157.13           C  
ANISOU 1582  CD2 TYR C  45     9640  35442  14621  -1743    832   1467       C  
ATOM   1583  CE1 TYR C  45      90.939  27.562   4.418  1.00147.26           C  
ANISOU 1583  CE1 TYR C  45     9670  32396  13886  -2825    561   1645       C  
ATOM   1584  CE2 TYR C  45      93.172  27.071   3.607  1.00158.25           C  
ANISOU 1584  CE2 TYR C  45     9714  35732  14682  -2662    823   1817       C  
ATOM   1585  CZ  TYR C  45      92.158  27.989   3.891  1.00153.31           C  
ANISOU 1585  CZ  TYR C  45     9770  34155  14324  -3188    671   1900       C  
ATOM   1586  OH  TYR C  45      92.372  29.330   3.644  1.00155.19           O  
ANISOU 1586  OH  TYR C  45     9998  34488  14479  -4066    621   2245       O  
ATOM   1587  N   LEU C  46      89.510  21.046   5.199  1.00143.63           N  
ANISOU 1587  N   LEU C  46     9857  29110  15604   3192    -35   -544       N  
ATOM   1588  CA  LEU C  46      89.345  19.601   5.072  1.00145.21           C  
ANISOU 1588  CA  LEU C  46    10262  29083  15827   4005   -109   -836       C  
ATOM   1589  C   LEU C  46      87.994  19.278   4.444  1.00141.85           C  
ANISOU 1589  C   LEU C  46    10436  27948  15511   4050    -96  -1011       C  
ATOM   1590  O   LEU C  46      87.877  18.329   3.669  1.00144.09           O  
ANISOU 1590  O   LEU C  46    10846  28224  15678   4609    -54  -1278       O  
ATOM   1591  CB  LEU C  46      89.513  18.894   6.426  1.00144.99           C  
ANISOU 1591  CB  LEU C  46    10376  28706  16006   4276   -365   -832       C  
ATOM   1592  CG  LEU C  46      89.956  17.423   6.433  1.00149.64           C  
ANISOU 1592  CG  LEU C  46    10911  29426  16521   5189   -467  -1067       C  
ATOM   1593  CD1 LEU C  46      91.394  17.279   5.969  1.00155.19           C  
ANISOU 1593  CD1 LEU C  46    10848  31159  16959   5399   -388  -1001       C  
ATOM   1594  CD2 LEU C  46      89.781  16.798   7.809  1.00148.48           C  
ANISOU 1594  CD2 LEU C  46    11227  28558  16631   5468   -761  -1086       C  
ATOM   1595  N   ALA C  47      86.986  20.084   4.774  1.00124.48           N  
ANISOU 1595  N   ALA C  47    10034  23579  13683   2892    239    127       N  
ATOM   1596  CA  ALA C  47      85.627  19.909   4.250  1.00121.01           C  
ANISOU 1596  CA  ALA C  47    10141  22473  13365   2830    231      3       C  
ATOM   1597  C   ALA C  47      85.531  20.145   2.739  1.00122.72           C  
ANISOU 1597  C   ALA C  47    10293  23006  13329   2917    425   -111       C  
ATOM   1598  O   ALA C  47      84.775  19.461   2.049  1.00123.57           O  
ANISOU 1598  O   ALA C  47    10686  22864  13400   3364    403   -376       O  
ATOM   1599  CB  ALA C  47      84.641  20.810   4.997  1.00116.03           C  
ANISOU 1599  CB  ALA C  47     9802  21320  12965   2175    162    197       C  
ATOM   1600  N   VAL C  48      86.294  21.118   2.240  1.00131.08           N  
ANISOU 1600  N   VAL C  48    10552  26319  12932    891   1137   -182       N  
ATOM   1601  CA  VAL C  48      86.350  21.415   0.812  1.00134.04           C  
ANISOU 1601  CA  VAL C  48    10725  27229  12975    961   1348   -230       C  
ATOM   1602  C   VAL C  48      86.793  20.180   0.035  1.00138.27           C  
ANISOU 1602  C   VAL C  48    11167  28059  13312   1768   1393   -565       C  
ATOM   1603  O   VAL C  48      86.047  19.704  -0.814  1.00137.80           O  
ANISOU 1603  O   VAL C  48    11497  27625  13237   2061   1371   -813       O  
ATOM   1604  CB  VAL C  48      87.243  22.646   0.502  1.00136.84           C  
ANISOU 1604  CB  VAL C  48    10532  28373  13087    469   1505     80       C  
ATOM   1605  CG1 VAL C  48      87.608  22.709  -0.965  1.00140.95           C  
ANISOU 1605  CG1 VAL C  48    10774  29575  13205    618   1736     34       C  
ATOM   1606  CG2 VAL C  48      86.534  23.920   0.902  1.00133.16           C  
ANISOU 1606  CG2 VAL C  48    10303  27500  12790   -293   1439    363       C  
ATOM   1607  N   LEU C  49      87.971  19.637   0.352  1.00157.35           N  
ANISOU 1607  N   LEU C  49    10874  33181  15729   3738   1362  -2994       N  
ATOM   1608  CA  LEU C  49      88.498  18.477  -0.385  1.00162.35           C  
ANISOU 1608  CA  LEU C  49    11414  34142  16128   4596   1408  -3353       C  
ATOM   1609  C   LEU C  49      87.630  17.223  -0.243  1.00161.07           C  
ANISOU 1609  C   LEU C  49    11909  33098  16191   5125   1181  -3682       C  
ATOM   1610  O   LEU C  49      87.729  16.303  -1.056  1.00165.11           O  
ANISOU 1610  O   LEU C  49    12510  33711  16513   5820   1186  -4030       O  
ATOM   1611  CB  LEU C  49      89.973  18.187  -0.041  1.00168.04           C  
ANISOU 1611  CB  LEU C  49    11457  35758  16634   5001   1474  -3343       C  
ATOM   1612  CG  LEU C  49      90.447  17.332   1.144  1.00170.24           C  
ANISOU 1612  CG  LEU C  49    11687  35941  17056   5602   1264  -3463       C  
ATOM   1613  CD1 LEU C  49      89.978  15.878   1.057  1.00170.97           C  
ANISOU 1613  CD1 LEU C  49    12384  35297  17279   6371   1058  -3851       C  
ATOM   1614  CD2 LEU C  49      91.973  17.382   1.226  1.00177.06           C  
ANISOU 1614  CD2 LEU C  49    11713  37989  17571   5966   1414  -3441       C  
ATOM   1615  N   ALA C  50      86.784  17.202   0.784  1.00147.10           N  
ANISOU 1615  N   ALA C  50    12551  27283  16058   6267     73  -2549       N  
ATOM   1616  CA  ALA C  50      85.871  16.089   1.018  1.00146.00           C  
ANISOU 1616  CA  ALA C  50    13049  26278  16145   6621   -167  -2789       C  
ATOM   1617  C   ALA C  50      84.641  16.178   0.127  1.00143.90           C  
ANISOU 1617  C   ALA C  50    13223  25584  15870   6460   -155  -2930       C  
ATOM   1618  O   ALA C  50      84.107  15.156  -0.296  1.00145.80           O  
ANISOU 1618  O   ALA C  50    13875  25421  16101   6927   -286  -3244       O  
ATOM   1619  CB  ALA C  50      85.458  16.044   2.484  1.00142.06           C  
ANISOU 1619  CB  ALA C  50    12812  25148  16016   6297   -384  -2579       C  
ATOM   1620  N   GLU C  51      84.220  17.410  -0.163  1.00131.42           N  
ANISOU 1620  N   GLU C  51    11988  23769  14176   4428    744  -1551       N  
ATOM   1621  CA  GLU C  51      82.927  17.702  -0.792  1.00128.13           C  
ANISOU 1621  CA  GLU C  51    11980  22879  13825   4084    721  -1571       C  
ATOM   1622  C   GLU C  51      83.015  18.134  -2.254  1.00130.25           C  
ANISOU 1622  C   GLU C  51    12068  23685  13735   4054    934  -1621       C  
ATOM   1623  O   GLU C  51      82.079  17.911  -3.021  1.00129.76           O  
ANISOU 1623  O   GLU C  51    12361  23316  13624   4086    890  -1791       O  
ATOM   1624  CB  GLU C  51      82.218  18.810  -0.011  1.00123.03           C  
ANISOU 1624  CB  GLU C  51    11393  21916  13436   3383    687  -1245       C  
ATOM   1625  CG  GLU C  51      81.670  18.393   1.344  1.00120.19           C  
ANISOU 1625  CG  GLU C  51    11335  20908  13424   3308    471  -1194       C  
ATOM   1626  CD  GLU C  51      80.188  18.060   1.312  1.00116.71           C  
ANISOU 1626  CD  GLU C  51    11387  19765  13192   3058    335  -1228       C  
ATOM   1627  OE1 GLU C  51      79.379  18.907   0.859  1.00113.91           O  
ANISOU 1627  OE1 GLU C  51    11058  19362  12861   2601    397  -1082       O  
ATOM   1628  OE2 GLU C  51      79.829  16.956   1.770  1.00117.19           O  
ANISOU 1628  OE2 GLU C  51    11806  19325  13397   3314    144  -1383       O  
ATOM   1629  N   ARG C  52      84.141  18.744  -2.624  1.00144.28           N  
ANISOU 1629  N   ARG C  52    12715  28592  13513   2143   1638  -1646       N  
ATOM   1630  CA  ARG C  52      84.313  19.444  -3.906  1.00146.79           C  
ANISOU 1630  CA  ARG C  52    12783  29550  13439   2010   1867  -1597       C  
ATOM   1631  C   ARG C  52      83.879  18.669  -5.151  1.00149.24           C  
ANISOU 1631  C   ARG C  52    13372  29830  13504   2459   1883  -1958       C  
ATOM   1632  O   ARG C  52      83.271  19.241  -6.060  1.00149.02           O  
ANISOU 1632  O   ARG C  52    13415  29926  13278   2183   1974  -1893       O  
ATOM   1633  CB  ARG C  52      85.765  19.893  -4.062  1.00151.54           C  
ANISOU 1633  CB  ARG C  52    12699  31160  13720   2084   2086  -1467       C  
ATOM   1634  CG  ARG C  52      85.957  21.199  -4.809  1.00153.59           C  
ANISOU 1634  CG  ARG C  52    12666  32080  13611   1682   2317  -1246       C  
ATOM   1635  CD  ARG C  52      87.374  21.703  -4.592  1.00154.31           C  
ANISOU 1635  CD  ARG C  52    12256  32704  13672   1101   2410   -820       C  
ATOM   1636  NE  ARG C  52      87.699  22.894  -5.374  1.00157.32           N  
ANISOU 1636  NE  ARG C  52    12322  33788  13663    661   2627   -546       N  
ATOM   1637  CZ  ARG C  52      88.861  23.540  -5.317  1.00161.25           C  
ANISOU 1637  CZ  ARG C  52    12210  35143  13914    304   2784   -233       C  
ATOM   1638  NH1 ARG C  52      89.833  23.123  -4.511  1.00162.83           N  
ANISOU 1638  NH1 ARG C  52    11990  35678  14201    359   2755   -170       N  
ATOM   1639  NH2 ARG C  52      89.060  24.612  -6.070  1.00164.12           N  
ANISOU 1639  NH2 ARG C  52    12371  36071  13917   -139   2960     40       N  
ATOM   1640  N   GLY C  53      84.185  17.375  -5.188  1.00156.84           N  
ANISOU 1640  N   GLY C  53    13562  31396  14635   4480   1414  -3757       N  
ATOM   1641  CA  GLY C  53      83.915  16.554  -6.371  1.00160.29           C  
ANISOU 1641  CA  GLY C  53    14273  31837  14791   4978   1409  -4163       C  
ATOM   1642  C   GLY C  53      82.588  15.816  -6.378  1.00157.83           C  
ANISOU 1642  C   GLY C  53    14665  30604  14701   4981   1144  -4391       C  
ATOM   1643  O   GLY C  53      82.369  14.932  -7.208  1.00161.28           O  
ANISOU 1643  O   GLY C  53    15385  30978  14917   5441   1085  -4779       O  
ATOM   1644  N   ALA C  54      81.699  16.183  -5.462  1.00141.05           N  
ANISOU 1644  N   ALA C  54    14186  25124  14282   5134    551  -3259       N  
ATOM   1645  CA  ALA C  54      80.426  15.493  -5.303  1.00139.38           C  
ANISOU 1645  CA  ALA C  54    14589  24077  14291   5131    278  -3459       C  
ATOM   1646  C   ALA C  54      79.265  16.352  -5.802  1.00135.49           C  
ANISOU 1646  C   ALA C  54    14230  23394  13855   4525    277  -3259       C  
ATOM   1647  O   ALA C  54      79.428  17.558  -5.988  1.00134.22           O  
ANISOU 1647  O   ALA C  54    13732  23691  13573   4142    472  -2966       O  
ATOM   1648  CB  ALA C  54      80.222  15.108  -3.840  1.00137.22           C  
ANISOU 1648  CB  ALA C  54    14562  23139  14435   5115     46  -3400       C  
ATOM   1649  N   PRO C  55      78.099  15.726  -6.057  1.00133.41           N  
ANISOU 1649  N   PRO C  55    14602  22207  13880   4319   -168  -3568       N  
ATOM   1650  CA  PRO C  55      76.836  16.422  -6.337  1.00129.39           C  
ANISOU 1650  CA  PRO C  55    14320  21276  13566   3777   -286  -3401       C  
ATOM   1651  C   PRO C  55      76.235  17.175  -5.133  1.00124.36           C  
ANISOU 1651  C   PRO C  55    13545  20455  13252   3231   -273  -3001       C  
ATOM   1652  O   PRO C  55      75.112  16.881  -4.727  1.00121.73           O  
ANISOU 1652  O   PRO C  55    13468  19618  13164   2944   -446  -2949       O  
ATOM   1653  CB  PRO C  55      75.903  15.275  -6.763  1.00130.34           C  
ANISOU 1653  CB  PRO C  55    14971  20686  13865   3930   -599  -3682       C  
ATOM   1654  CG  PRO C  55      76.807  14.137  -7.122  1.00135.99           C  
ANISOU 1654  CG  PRO C  55    15818  21566  14285   4590   -620  -4102       C  
ATOM   1655  CD  PRO C  55      77.940  14.266  -6.177  1.00137.74           C  
ANISOU 1655  CD  PRO C  55    15542  22465  14329   4891   -355  -4021       C  
ATOM   1656  N   GLY C  56      76.956  18.154  -4.590  1.00119.02           N  
ANISOU 1656  N   GLY C  56    13012  19750  12460   3231   -181  -1903       N  
ATOM   1657  CA  GLY C  56      76.532  18.810  -3.352  1.00114.87           C  
ANISOU 1657  CA  GLY C  56    12435  18964  12246   2795   -214  -1601       C  
ATOM   1658  C   GLY C  56      76.873  20.276  -3.169  1.00113.46           C  
ANISOU 1658  C   GLY C  56    11918  19155  12038   2426    -49  -1268       C  
ATOM   1659  O   GLY C  56      77.745  20.817  -3.850  1.00115.95           O  
ANISOU 1659  O   GLY C  56    11902  20052  12101   2485    129  -1196       O  
ATOM   1660  N   ALA C  57      76.178  20.886  -2.202  1.00110.66           N  
ANISOU 1660  N   ALA C  57    12790  18009  11246   2649   -828   -562       N  
ATOM   1661  CA  ALA C  57      76.225  22.332  -1.884  1.00108.74           C  
ANISOU 1661  CA  ALA C  57    12371  17870  11076   2226   -762   -245       C  
ATOM   1662  C   ALA C  57      77.626  22.961  -1.770  1.00110.58           C  
ANISOU 1662  C   ALA C  57    12222  18612  11180   2163   -615    -80       C  
ATOM   1663  O   ALA C  57      78.636  22.259  -1.610  1.00112.42           O  
ANISOU 1663  O   ALA C  57    12272  19060  11381   2455   -583   -177       O  
ATOM   1664  CB  ALA C  57      75.365  22.649  -0.623  1.00105.03           C  
ANISOU 1664  CB  ALA C  57    12088  16873  10947   1971   -903   -153       C  
ATOM   1665  N   GLN C  58      77.652  24.295  -1.814  1.00113.50           N  
ANISOU 1665  N   GLN C  58    14750  18270  10105    631   -687   1095       N  
ATOM   1666  CA  GLN C  58      78.848  25.075  -2.165  1.00116.50           C  
ANISOU 1666  CA  GLN C  58    14772  19260  10233    458   -533   1294       C  
ATOM   1667  C   GLN C  58      80.063  24.935  -1.234  1.00118.01           C  
ANISOU 1667  C   GLN C  58    14621  19781  10437    542   -486   1321       C  
ATOM   1668  O   GLN C  58      80.921  25.825  -1.194  1.00120.45           O  
ANISOU 1668  O   GLN C  58    14598  20588  10578    274   -388   1541       O  
ATOM   1669  CB  GLN C  58      78.483  26.558  -2.367  1.00115.86           C  
ANISOU 1669  CB  GLN C  58    14763  19097  10163    -72   -563   1608       C  
ATOM   1670  CG  GLN C  58      79.209  27.233  -3.533  1.00119.11           C  
ANISOU 1670  CG  GLN C  58    15051  19977  10228   -272   -444   1800       C  
ATOM   1671  CD  GLN C  58      79.451  28.713  -3.307  1.00119.97           C  
ANISOU 1671  CD  GLN C  58    15132  20117  10335   -836   -482   2168       C  
ATOM   1672  OE1 GLN C  58      78.948  29.554  -4.050  1.00120.79           O  
ANISOU 1672  OE1 GLN C  58    15419  20145  10331  -1105   -520   2368       O  
ATOM   1673  NE2 GLN C  58      80.229  29.039  -2.277  1.00120.16           N  
ANISOU 1673  NE2 GLN C  58    14963  20216  10477  -1029   -502   2264       N  
ATOM   1674  N   LEU C  59      80.147  23.825  -0.504  1.00108.18           N  
ANISOU 1674  N   LEU C  59    11775  19044  10283    414    502    898       N  
ATOM   1675  CA  LEU C  59      81.369  23.492   0.227  1.00110.16           C  
ANISOU 1675  CA  LEU C  59    11691  19644  10519    577    527    908       C  
ATOM   1676  C   LEU C  59      82.432  23.050  -0.779  1.00114.90           C  
ANISOU 1676  C   LEU C  59    11926  20962  10767    919    699    815       C  
ATOM   1677  O   LEU C  59      83.004  21.964  -0.687  1.00117.12           O  
ANISOU 1677  O   LEU C  59    12124  21378  10997   1448    694    588       O  
ATOM   1678  CB  LEU C  59      81.105  22.427   1.299  1.00108.45           C  
ANISOU 1678  CB  LEU C  59    11695  18951  10560    873    369    743       C  
ATOM   1679  CG  LEU C  59      80.273  22.829   2.525  1.00104.52           C  
ANISOU 1679  CG  LEU C  59    11447  17905  10359    528    229    861       C  
ATOM   1680  CD1 LEU C  59      80.334  21.741   3.582  1.00103.96           C  
ANISOU 1680  CD1 LEU C  59    11507  17519  10473    806     89    757       C  
ATOM   1681  CD2 LEU C  59      80.728  24.159   3.111  1.00104.28           C  
ANISOU 1681  CD2 LEU C  59    11214  18077  10330     47    248   1122       C  
ATOM   1682  N   ILE C  60      82.671  23.933  -1.743  1.00131.09           N  
ANISOU 1682  N   ILE C  60    14167  24712  10928  -1476   1643    294       N  
ATOM   1683  CA  ILE C  60      83.477  23.647  -2.917  1.00135.53           C  
ANISOU 1683  CA  ILE C  60    14449  25961  11085  -1238   1837    225       C  
ATOM   1684  C   ILE C  60      84.524  24.742  -3.118  1.00138.41           C  
ANISOU 1684  C   ILE C  60    14387  26992  11212  -1747   1978    585       C  
ATOM   1685  O   ILE C  60      85.440  24.593  -3.924  1.00143.05           O  
ANISOU 1685  O   ILE C  60    14572  28355  11424  -1609   2169    595       O  
ATOM   1686  CB  ILE C  60      82.609  23.525  -4.181  1.00135.03           C  
ANISOU 1686  CB  ILE C  60    14743  25667  10897  -1114   1846     65       C  
ATOM   1687  CG1 ILE C  60      82.047  24.891  -4.577  1.00133.47           C  
ANISOU 1687  CG1 ILE C  60    14701  25330  10682  -1713   1835    373       C  
ATOM   1688  CG2 ILE C  60      81.488  22.521  -3.961  1.00132.19           C  
ANISOU 1688  CG2 ILE C  60    14856  24563  10807   -748   1657   -254       C  
ATOM   1689  CD1 ILE C  60      81.382  24.907  -5.936  1.00134.85           C  
ANISOU 1689  CD1 ILE C  60    15042  25614  10580  -1643   1895    304       C  
ATOM   1690  N   THR C  61      84.372  25.841  -2.384  1.00142.12           N  
ANISOU 1690  N   THR C  61    16013  27031  10955  -3568   2053   1337       N  
ATOM   1691  CA  THR C  61      85.421  26.855  -2.263  1.00145.38           C  
ANISOU 1691  CA  THR C  61    15991  28038  11208  -4063   2120   1673       C  
ATOM   1692  C   THR C  61      85.773  27.069  -0.791  1.00144.02           C  
ANISOU 1692  C   THR C  61    15727  27688  11305  -4178   1974   1713       C  
ATOM   1693  O   THR C  61      84.935  26.857   0.094  1.00139.76           O  
ANISOU 1693  O   THR C  61    15568  26431  11105  -4081   1804   1581       O  
ATOM   1694  CB  THR C  61      84.993  28.182  -2.890  1.00145.70           C  
ANISOU 1694  CB  THR C  61    16186  27991  11181  -4768   2090   2042       C  
ATOM   1695  OG1 THR C  61      83.831  28.679  -2.217  1.00141.79           O  
ANISOU 1695  OG1 THR C  61    16252  26747  10875  -4763   1971   1967       O  
ATOM   1696  CG2 THR C  61      84.665  27.993  -4.364  1.00150.94           C  
ANISOU 1696  CG2 THR C  61    16479  29487  11384  -4932   2302   2239       C  
ATOM   1697  N   TYR C  62      87.016  27.478  -0.536  1.00138.42           N  
ANISOU 1697  N   TYR C  62    13039  27288  12266  -2733   2466   1261       N  
ATOM   1698  CA  TYR C  62      87.486  27.744   0.827  1.00138.06           C  
ANISOU 1698  CA  TYR C  62    12848  27195  12414  -2952   2315   1354       C  
ATOM   1699  C   TYR C  62      86.763  28.920   1.503  1.00134.88           C  
ANISOU 1699  C   TYR C  62    12885  26096  12266  -3578   2116   1547       C  
ATOM   1700  O   TYR C  62      86.232  28.746   2.598  1.00131.16           O  
ANISOU 1700  O   TYR C  62    12732  25011  12093  -3479   1956   1415       O  
ATOM   1701  CB  TYR C  62      89.014  27.936   0.881  1.00143.91           C  
ANISOU 1701  CB  TYR C  62    12862  28951  12865  -3111   2420   1542       C  
ATOM   1702  CG  TYR C  62      89.831  26.721   0.482  1.00147.54           C  
ANISOU 1702  CG  TYR C  62    12848  30114  13095  -2364   2584   1298       C  
ATOM   1703  CD1 TYR C  62      89.790  25.547   1.238  1.00145.86           C  
ANISOU 1703  CD1 TYR C  62    12747  29592  13082  -1701   2482    991       C  
ATOM   1704  CD2 TYR C  62      90.664  26.756  -0.639  1.00153.29           C  
ANISOU 1704  CD2 TYR C  62    13023  31835  13384  -2313   2828   1383       C  
ATOM   1705  CE1 TYR C  62      90.543  24.432   0.877  1.00149.78           C  
ANISOU 1705  CE1 TYR C  62    12869  30667  13374   -952   2591    748       C  
ATOM   1706  CE2 TYR C  62      91.425  25.648  -1.008  1.00157.28           C  
ANISOU 1706  CE2 TYR C  62    13092  33013  13655  -1543   2973   1116       C  
ATOM   1707  CZ  TYR C  62      91.359  24.490  -0.244  1.00155.48           C  
ANISOU 1707  CZ  TYR C  62    13038  32377  13662   -842   2838    787       C  
ATOM   1708  OH  TYR C  62      92.105  23.391  -0.600  1.00159.84           O  
ANISOU 1708  OH  TYR C  62    13231  33502  13999    -16   2937    500       O  
ATOM   1709  N   PRO C  63      86.725  30.111   0.854  1.00135.96           N  
ANISOU 1709  N   PRO C  63    14693  25463  11501  -4264    831   3252       N  
ATOM   1710  CA  PRO C  63      86.088  31.287   1.475  1.00134.00           C  
ANISOU 1710  CA  PRO C  63    14881  24554  11477  -4833    609   3424       C  
ATOM   1711  C   PRO C  63      84.612  31.088   1.854  1.00128.58           C  
ANISOU 1711  C   PRO C  63    14815  22938  11101  -4605    480   3216       C  
ATOM   1712  O   PRO C  63      84.008  31.959   2.486  1.00127.29           O  
ANISOU 1712  O   PRO C  63    15056  22215  11095  -4984    305   3322       O  
ATOM   1713  CB  PRO C  63      86.214  32.365   0.392  1.00137.55           C  
ANISOU 1713  CB  PRO C  63    15334  25246  11681  -5404    648   3773       C  
ATOM   1714  CG  PRO C  63      87.369  31.932  -0.436  1.00142.43           C  
ANISOU 1714  CG  PRO C  63    15311  26884  11921  -5314    888   3860       C  
ATOM   1715  CD  PRO C  63      87.268  30.444  -0.477  1.00140.54           C  
ANISOU 1715  CD  PRO C  63    14956  26747  11694  -4471   1024   3465       C  
ATOM   1716  N   ARG C  64      84.049  29.949   1.470  1.00116.08           N  
ANISOU 1716  N   ARG C  64    13104  20872  10129  -2257   -323   2793       N  
ATOM   1717  CA  ARG C  64      82.679  29.605   1.809  1.00111.61           C  
ANISOU 1717  CA  ARG C  64    13040  19552   9815  -2051   -423   2611       C  
ATOM   1718  C   ARG C  64      82.671  28.561   2.912  1.00109.54           C  
ANISOU 1718  C   ARG C  64    12747  19148   9726  -1618   -460   2369       C  
ATOM   1719  O   ARG C  64      81.740  28.500   3.715  1.00106.27           O  
ANISOU 1719  O   ARG C  64    12654  18171   9551  -1565   -584   2261       O  
ATOM   1720  CB  ARG C  64      81.940  29.083   0.571  1.00111.21           C  
ANISOU 1720  CB  ARG C  64    13141  19472   9642  -1785   -316   2518       C  
ATOM   1721  N   ALA C  65      83.713  27.737   2.937  1.00106.00           N  
ANISOU 1721  N   ALA C  65    10782  19640   9855   -993     95   1773       N  
ATOM   1722  CA  ALA C  65      83.884  26.739   3.983  1.00105.25           C  
ANISOU 1722  CA  ALA C  65    10608  19488   9896   -641     23   1615       C  
ATOM   1723  C   ALA C  65      84.219  27.383   5.336  1.00104.77           C  
ANISOU 1723  C   ALA C  65    10530  19304   9974  -1013   -137   1743       C  
ATOM   1724  O   ALA C  65      83.795  26.882   6.384  1.00102.20           O  
ANISOU 1724  O   ALA C  65    10427  18557   9848   -846   -252   1623       O  
ATOM   1725  CB  ALA C  65      84.942  25.730   3.585  1.00108.94           C  
ANISOU 1725  CB  ALA C  65    10633  20606  10154   -182    143   1517       C  
ATOM   1726  N   LEU C  66      84.971  28.489   5.304  1.00107.37           N  
ANISOU 1726  N   LEU C  66    10755  19599  10441  -1629   -740   2373       N  
ATOM   1727  CA  LEU C  66      85.268  29.280   6.505  1.00107.15           C  
ANISOU 1727  CA  LEU C  66    10812  19367  10533  -2059   -930   2476       C  
ATOM   1728  C   LEU C  66      83.983  29.814   7.127  1.00103.10           C  
ANISOU 1728  C   LEU C  66    10867  18053  10255  -2126  -1055   2378       C  
ATOM   1729  O   LEU C  66      83.786  29.727   8.343  1.00101.01           O  
ANISOU 1729  O   LEU C  66    10757  17482  10142  -1972  -1157   2251       O  
ATOM   1730  CB  LEU C  66      86.224  30.426   6.169  1.00110.88           C  
ANISOU 1730  CB  LEU C  66    11091  20188  10852  -2713   -974   2760       C  
ATOM   1731  CG  LEU C  66      87.587  30.027   5.599  1.00115.78           C  
ANISOU 1731  CG  LEU C  66    11081  21723  11187  -2761   -834   2912       C  
ATOM   1732  CD1 LEU C  66      88.432  31.259   5.312  1.00119.71           C  
ANISOU 1732  CD1 LEU C  66    11459  22481  11543  -3552   -914   3245       C  
ATOM   1733  CD2 LEU C  66      88.314  29.090   6.552  1.00117.33           C  
ANISOU 1733  CD2 LEU C  66    10835  22392  11354  -2385   -842   2811       C  
ATOM   1734  N   TRP C  67      83.111  30.356   6.281  1.00101.50           N  
ANISOU 1734  N   TRP C  67    11698  17247   9621  -1752  -1480   1901       N  
ATOM   1735  CA  TRP C  67      81.812  30.853   6.709  1.00 98.25           C  
ANISOU 1735  CA  TRP C  67    11784  16142   9403  -1745  -1584   1795       C  
ATOM   1736  C   TRP C  67      80.919  29.726   7.218  1.00 94.92           C  
ANISOU 1736  C   TRP C  67    11493  15441   9130  -1260  -1560   1560       C  
ATOM   1737  O   TRP C  67      80.106  29.943   8.111  1.00 92.72           O  
ANISOU 1737  O   TRP C  67    11514  14716   9000  -1252  -1656   1464       O  
ATOM   1738  CB  TRP C  67      81.140  31.614   5.562  1.00 98.31           C  
ANISOU 1738  CB  TRP C  67    12033  15958   9363  -1866  -1550   1884       C  
ATOM   1739  CG  TRP C  67      79.674  31.873   5.741  1.00 95.33           C  
ANISOU 1739  CG  TRP C  67    12098  14963   9160  -1734  -1631   1754       C  
ATOM   1740  CD1 TRP C  67      78.660  31.361   4.989  1.00 93.27           C  
ANISOU 1740  CD1 TRP C  67    11980  14522   8935  -1412  -1560   1637       C  
ATOM   1741  CD2 TRP C  67      79.057  32.701   6.734  1.00 94.54           C  
ANISOU 1741  CD2 TRP C  67    12331  14389   9202  -1894  -1804   1706       C  
ATOM   1742  NE1 TRP C  67      77.451  31.820   5.445  1.00 91.26           N  
ANISOU 1742  NE1 TRP C  67    12079  13757   8840  -1365  -1671   1541       N  
ATOM   1743  CE2 TRP C  67      77.664  32.644   6.517  1.00 92.04           C  
ANISOU 1743  CE2 TRP C  67    12308  13665   8998  -1624  -1813   1568       C  
ATOM   1744  CE3 TRP C  67      79.548  33.488   7.785  1.00 96.14           C  
ANISOU 1744  CE3 TRP C  67    12610  14492   9425  -2227  -1966   1750       C  
ATOM   1745  CZ2 TRP C  67      76.748  33.345   7.311  1.00 91.20           C  
ANISOU 1745  CZ2 TRP C  67    12541  13096   9015  -1624  -1952   1464       C  
ATOM   1746  CZ3 TRP C  67      78.638  34.185   8.575  1.00 95.28           C  
ANISOU 1746  CZ3 TRP C  67    12898  13867   9437  -2234  -2119   1627       C  
ATOM   1747  CH2 TRP C  67      77.251  34.107   8.331  1.00 92.86           C  
ANISOU 1747  CH2 TRP C  67    12854  13196   9233  -1905  -2099   1481       C  
ATOM   1748  N   TRP C  68      81.073  28.526   6.658  1.00 91.78           N  
ANISOU 1748  N   TRP C  68    10431  15704   8738   -743  -1259   1111       N  
ATOM   1749  CA  TRP C  68      80.294  27.373   7.108  1.00 89.26           C  
ANISOU 1749  CA  TRP C  68    10279  15082   8554   -333  -1267    917       C  
ATOM   1750  C   TRP C  68      80.724  26.931   8.484  1.00 89.13           C  
ANISOU 1750  C   TRP C  68    10194  15061   8609   -260  -1361    890       C  
ATOM   1751  O   TRP C  68      79.889  26.564   9.305  1.00 86.89           O  
ANISOU 1751  O   TRP C  68    10161  14392   8460   -195  -1430    809       O  
ATOM   1752  CB  TRP C  68      80.428  26.189   6.159  1.00 90.17           C  
ANISOU 1752  CB  TRP C  68    10262  15417   8583     89  -1160    807       C  
ATOM   1753  CG  TRP C  68      79.926  24.896   6.765  1.00 88.67           C  
ANISOU 1753  CG  TRP C  68    10236  14929   8526    473  -1219    641       C  
ATOM   1754  CD1 TRP C  68      78.624  24.563   7.032  1.00 86.06           C  
ANISOU 1754  CD1 TRP C  68    10242  14110   8346    529  -1273    547       C  
ATOM   1755  CD2 TRP C  68      80.719  23.779   7.188  1.00 90.38           C  
ANISOU 1755  CD2 TRP C  68    10290  15329   8722    841  -1248    572       C  
ATOM   1756  NE1 TRP C  68      78.560  23.306   7.587  1.00 86.11           N  
ANISOU 1756  NE1 TRP C  68    10328  13965   8423    845  -1338    447       N  
ATOM   1757  CE2 TRP C  68      79.829  22.801   7.692  1.00 88.71           C  
ANISOU 1757  CE2 TRP C  68    10388  14660   8659   1067  -1336    456       C  
ATOM   1758  CE3 TRP C  68      82.093  23.503   7.181  1.00 93.65           C  
ANISOU 1758  CE3 TRP C  68    10319  16267   8995   1012  -1222    605       C  
ATOM   1759  CZ2 TRP C  68      80.269  21.571   8.184  1.00 90.23           C  
ANISOU 1759  CZ2 TRP C  68    10587  14822   8874   1449  -1421    387       C  
ATOM   1760  CZ3 TRP C  68      82.529  22.279   7.667  1.00 95.10           C  
ANISOU 1760  CZ3 TRP C  68    10474  16461   9198   1465  -1295    506       C  
ATOM   1761  CH2 TRP C  68      81.620  21.328   8.161  1.00 93.41           C  
ANISOU 1761  CH2 TRP C  68    10641  15705   9145   1676  -1405    403       C  
ATOM   1762  N   SER C  69      82.032  26.948   8.716  1.00 91.02           N  
ANISOU 1762  N   SER C  69     9991  15603   8989   -762  -1430   1193       N  
ATOM   1763  CA  SER C  69      82.602  26.597  10.009  1.00 91.56           C  
ANISOU 1763  CA  SER C  69     9957  15742   9090   -744  -1553   1205       C  
ATOM   1764  C   SER C  69      82.001  27.450  11.114  1.00 89.96           C  
ANISOU 1764  C   SER C  69    10030  15172   8977  -1077  -1672   1215       C  
ATOM   1765  O   SER C  69      81.467  26.918  12.083  1.00 88.17           O  
ANISOU 1765  O   SER C  69    10003  14654   8845   -932  -1732   1134       O  
ATOM   1766  CB  SER C  69      84.120  26.749   9.977  1.00 95.31           C  
ANISOU 1766  CB  SER C  69     9967  16840   9407   -863  -1567   1331       C  
ATOM   1767  OG  SER C  69      84.679  25.938   8.960  1.00 97.75           O  
ANISOU 1767  OG  SER C  69     9977  17610   9554   -791  -1419   1376       O  
ATOM   1768  N   VAL C  70      82.064  28.769  10.946  1.00 91.26           N  
ANISOU 1768  N   VAL C  70    10635  15369   8671  -1718  -1756   1214       N  
ATOM   1769  CA  VAL C  70      81.500  29.703  11.915  1.00 90.43           C  
ANISOU 1769  CA  VAL C  70    10834  14895   8630  -1992  -1894   1179       C  
ATOM   1770  C   VAL C  70      80.001  29.458  12.100  1.00 87.19           C  
ANISOU 1770  C   VAL C  70    10779  14001   8350  -1754  -1872   1026       C  
ATOM   1771  O   VAL C  70      79.501  29.421  13.218  1.00 86.22           O  
ANISOU 1771  O   VAL C  70    10774  13723   8262  -1667  -1935    943       O  
ATOM   1772  CB  VAL C  70      81.765  31.167  11.518  1.00 92.23           C  
ANISOU 1772  CB  VAL C  70    11174  15055   8813  -2458  -1966   1289       C  
ATOM   1773  CG1 VAL C  70      81.272  32.118  12.602  1.00 92.21           C  
ANISOU 1773  CG1 VAL C  70    11513  14663   8858  -2693  -2146   1206       C  
ATOM   1774  CG2 VAL C  70      83.249  31.382  11.263  1.00 95.89           C  
ANISOU 1774  CG2 VAL C  70    11227  16081   9125  -2735  -1972   1473       C  
ATOM   1775  N   GLU C  71      79.296  29.269  10.996  1.00 84.76           N  
ANISOU 1775  N   GLU C  71    10628  13636   7940  -1366  -1629    582       N  
ATOM   1776  CA  GLU C  71      77.867  28.956  11.020  1.00 82.18           C  
ANISOU 1776  CA  GLU C  71    10563  12941   7720  -1148  -1604    454       C  
ATOM   1777  C   GLU C  71      77.583  27.703  11.872  1.00 81.07           C  
ANISOU 1777  C   GLU C  71    10385  12794   7623   -856  -1590    389       C  
ATOM   1778  O   GLU C  71      76.590  27.646  12.606  1.00 79.80           O  
ANISOU 1778  O   GLU C  71    10401  12406   7512   -809  -1618    315       O  
ATOM   1779  CB  GLU C  71      77.365  28.769   9.579  1.00 81.47           C  
ANISOU 1779  CB  GLU C  71    10538  12773   7644  -1046  -1512    452       C  
ATOM   1780  CG  GLU C  71      75.860  28.846   9.368  1.00 79.75           C  
ANISOU 1780  CG  GLU C  71    10601  12187   7512   -981  -1523    362       C  
ATOM   1781  CD  GLU C  71      75.488  28.831   7.879  1.00 79.61           C  
ANISOU 1781  CD  GLU C  71    10606  12172   7469   -895  -1452    384       C  
ATOM   1782  OE1 GLU C  71      76.015  29.696   7.140  1.00 81.37           O  
ANISOU 1782  OE1 GLU C  71    10671  12667   7580  -1013  -1409    499       O  
ATOM   1783  OE2 GLU C  71      74.681  27.961   7.445  1.00 78.17           O  
ANISOU 1783  OE2 GLU C  71    10561  11790   7350   -728  -1439    296       O  
ATOM   1784  N   THR C  72      78.482  26.724  11.789  1.00 81.65           N  
ANISOU 1784  N   THR C  72     9904  13199   7920   -961  -1764    568       N  
ATOM   1785  CA  THR C  72      78.282  25.418  12.407  1.00 81.26           C  
ANISOU 1785  CA  THR C  72     9881  13081   7913   -686  -1791    535       C  
ATOM   1786  C   THR C  72      78.801  25.344  13.845  1.00 82.05           C  
ANISOU 1786  C   THR C  72     9936  13265   7975   -747  -1897    582       C  
ATOM   1787  O   THR C  72      78.159  24.736  14.706  1.00 81.41           O  
ANISOU 1787  O   THR C  72     9994  13012   7925   -644  -1940    578       O  
ATOM   1788  CB  THR C  72      78.934  24.310  11.554  1.00 82.80           C  
ANISOU 1788  CB  THR C  72     9900  13487   8072   -370  -1756    529       C  
ATOM   1789  OG1 THR C  72      78.338  24.304  10.249  1.00 82.08           O  
ANISOU 1789  OG1 THR C  72     9917  13265   8003   -245  -1674    449       O  
ATOM   1790  CG2 THR C  72      78.766  22.932  12.199  1.00 83.58           C  
ANISOU 1790  CG2 THR C  72    10038  13518   8201    -94  -1857    538       C  
ATOM   1791  N   ALA C  73      79.960  25.952  14.093  1.00 84.65           N  
ANISOU 1791  N   ALA C  73    10170  13810   8183  -1244  -2064    851       N  
ATOM   1792  CA  ALA C  73      80.582  25.954  15.419  1.00 86.10           C  
ANISOU 1792  CA  ALA C  73    10251  14169   8293  -1306  -2188    904       C  
ATOM   1793  C   ALA C  73      79.767  26.764  16.426  1.00 85.21           C  
ANISOU 1793  C   ALA C  73    10383  13828   8164  -1521  -2253    844       C  
ATOM   1794  O   ALA C  73      79.771  26.469  17.619  1.00 86.25           O  
ANISOU 1794  O   ALA C  73    10497  14060   8213  -1565  -2360    866       O  
ATOM   1795  CB  ALA C  73      81.994  26.486  15.334  1.00 88.75           C  
ANISOU 1795  CB  ALA C  73    10269  14926   8527  -1504  -2235    988       C  
ATOM   1796  N   THR C  74      79.084  27.790  15.931  1.00 84.35           N  
ANISOU 1796  N   THR C  74    10642  13622   7786  -1622  -2140    525       N  
ATOM   1797  CA  THR C  74      78.170  28.591  16.725  1.00 84.15           C  
ANISOU 1797  CA  THR C  74    10842  13413   7720  -1768  -2197    427       C  
ATOM   1798  C   THR C  74      76.880  27.809  16.928  1.00 82.31           C  
ANISOU 1798  C   THR C  74    10761  12975   7539  -1562  -2109    373       C  
ATOM   1799  O   THR C  74      76.081  28.100  17.820  1.00 82.15           O  
ANISOU 1799  O   THR C  74    10894  12860   7461  -1571  -2114    288       O  
ATOM   1800  CB  THR C  74      77.834  29.877  15.970  1.00 84.55           C  
ANISOU 1800  CB  THR C  74    11026  13308   7791  -1990  -2217    379       C  
ATOM   1801  OG1 THR C  74      79.046  30.495  15.525  1.00 86.64           O  
ANISOU 1801  OG1 THR C  74    11081  13832   8007  -2218  -2280    493       O  
ATOM   1802  CG2 THR C  74      77.083  30.844  16.861  1.00 85.28           C  
ANISOU 1802  CG2 THR C  74    11385  13200   7819  -2114  -2315    233       C  
ATOM   1803  N   THR C  75      76.700  26.808  16.078  1.00 81.47           N  
ANISOU 1803  N   THR C  75    10595  12887   7471  -1450  -2016    509       N  
ATOM   1804  CA  THR C  75      75.440  26.071  15.945  1.00 80.13           C  
ANISOU 1804  CA  THR C  75    10542  12538   7364  -1300  -1951    490       C  
ATOM   1805  C   THR C  75      74.258  26.984  15.548  1.00 79.11           C  
ANISOU 1805  C   THR C  75    10568  12230   7261  -1356  -1896    376       C  
ATOM   1806  O   THR C  75      73.117  26.754  15.971  1.00 78.70           O  
ANISOU 1806  O   THR C  75    10594  12115   7195  -1314  -1858    337       O  
ATOM   1807  CB  THR C  75      75.088  25.225  17.205  1.00 80.78           C  
ANISOU 1807  CB  THR C  75    10650  12664   7377  -1254  -1999    560       C  
ATOM   1808  OG1 THR C  75      74.285  26.011  18.091  1.00 80.60           O  
ANISOU 1808  OG1 THR C  75    10743  12604   7279  -1346  -1970    483       O  
ATOM   1809  CG2 THR C  75      76.343  24.711  17.924  1.00 82.58           C  
ANISOU 1809  CG2 THR C  75    10734  13126   7516  -1261  -2111    647       C  
ATOM   1810  N   VAL C  76      74.538  28.013  14.744  1.00 78.41           N  
ANISOU 1810  N   VAL C  76    10488  12162   7144  -1294  -1701    145       N  
ATOM   1811  CA  VAL C  76      73.492  28.871  14.179  1.00 77.96           C  
ANISOU 1811  CA  VAL C  76    10585  11917   7119  -1292  -1681     51       C  
ATOM   1812  C   VAL C  76      72.794  28.120  13.055  1.00 76.80           C  
ANISOU 1812  C   VAL C  76    10426  11697   7058  -1168  -1610     68       C  
ATOM   1813  O   VAL C  76      71.559  28.084  13.003  1.00 76.24           O  
ANISOU 1813  O   VAL C  76    10427  11526   7016  -1079  -1580     -1       O  
ATOM   1814  CB  VAL C  76      74.045  30.212  13.661  1.00 79.36           C  
ANISOU 1814  CB  VAL C  76    10862  12027   7264  -1488  -1772     35       C  
ATOM   1815  CG1 VAL C  76      73.014  30.931  12.784  1.00 79.56           C  
ANISOU 1815  CG1 VAL C  76    10797  12115   7318  -1565  -1753    144       C  
ATOM   1816  CG2 VAL C  76      74.461  31.092  14.825  1.00 79.57           C  
ANISOU 1816  CG2 VAL C  76    11086  11832   7316  -1463  -1797    -50       C  
ATOM   1817  N   GLY C  77      73.599  27.510  12.180  1.00 75.84           N  
ANISOU 1817  N   GLY C  77    10193  11523   7098  -1074  -1588    228       N  
ATOM   1818  CA  GLY C  77      73.128  26.632  11.098  1.00 75.17           C  
ANISOU 1818  CA  GLY C  77    10086  11411   7063   -916  -1538    229       C  
ATOM   1819  C   GLY C  77      72.028  27.231  10.247  1.00 74.52           C  
ANISOU 1819  C   GLY C  77    10113  11184   7016   -895  -1520    175       C  
ATOM   1820  O   GLY C  77      70.860  26.828  10.373  1.00 73.91           O  
ANISOU 1820  O   GLY C  77    10072  11027   6984   -819  -1514    130       O  
ATOM   1821  N   TYR C  78      72.403  28.197   9.396  1.00 74.20           N  
ANISOU 1821  N   TYR C  78    10215  11085   6892   -728  -1268    149       N  
ATOM   1822  CA  TYR C  78      71.459  28.911   8.530  1.00 74.20           C  
ANISOU 1822  CA  TYR C  78    10353  10935   6903   -713  -1292    127       C  
ATOM   1823  C   TYR C  78      70.783  27.969   7.557  1.00 73.60           C  
ANISOU 1823  C   TYR C  78    10240  10881   6843   -574  -1259     96       C  
ATOM   1824  O   TYR C  78      69.562  27.973   7.446  1.00 73.18           O  
ANISOU 1824  O   TYR C  78    10223  10750   6831   -499  -1279     35       O  
ATOM   1825  CB  TYR C  78      72.140  30.037   7.756  1.00 75.56           C  
ANISOU 1825  CB  TYR C  78    10592  11107   7012   -872  -1326    233       C  
ATOM   1826  CG  TYR C  78      72.413  31.267   8.564  1.00 76.70           C  
ANISOU 1826  CG  TYR C  78    10870  11121   7152  -1035  -1417    244       C  
ATOM   1827  CD1 TYR C  78      71.381  31.947   9.206  1.00 76.85           C  
ANISOU 1827  CD1 TYR C  78    11072  10917   7212   -941  -1489    133       C  
ATOM   1828  CD2 TYR C  78      73.704  31.770   8.669  1.00 78.21           C  
ANISOU 1828  CD2 TYR C  78    11005  11432   7280  -1286  -1449    356       C  
ATOM   1829  CE1 TYR C  78      71.636  33.097   9.960  1.00 78.51           C  
ANISOU 1829  CE1 TYR C  78    11475  10953   7403  -1070  -1609     98       C  
ATOM   1830  CE2 TYR C  78      73.974  32.916   9.410  1.00 79.84           C  
ANISOU 1830  CE2 TYR C  78    11384  11477   7476  -1494  -1578    358       C  
ATOM   1831  CZ  TYR C  78      72.938  33.577  10.055  1.00 79.99           C  
ANISOU 1831  CZ  TYR C  78    11655  11197   7540  -1371  -1668    210       C  
ATOM   1832  OH  TYR C  78      73.207  34.714  10.784  1.00 82.15           O  
ANISOU 1832  OH  TYR C  78    12174  11248   7790  -1538  -1829    164       O  
ATOM   1833  N   GLY C  79      71.572  27.142   6.877  1.00 74.08           N  
ANISOU 1833  N   GLY C  79     9955  11141   7052   -165  -1384    -47       N  
ATOM   1834  CA  GLY C  79      71.036  26.227   5.869  1.00 74.08           C  
ANISOU 1834  CA  GLY C  79     9975  11130   7041    -31  -1381   -113       C  
ATOM   1835  C   GLY C  79      71.485  26.541   4.454  1.00 75.12           C  
ANISOU 1835  C   GLY C  79    10095  11398   7049    -15  -1347    -82       C  
ATOM   1836  O   GLY C  79      71.305  25.729   3.547  1.00 75.79           O  
ANISOU 1836  O   GLY C  79    10174  11557   7067    122  -1331   -156       O  
ATOM   1837  N   ASP C  80      72.077  27.721   4.279  1.00 76.65           N  
ANISOU 1837  N   ASP C  80    10319  11720   7084    234  -1110    209       N  
ATOM   1838  CA  ASP C  80      72.662  28.120   3.007  1.00 78.24           C  
ANISOU 1838  CA  ASP C  80    10483  12115   7131    152  -1067    316       C  
ATOM   1839  C   ASP C  80      73.855  27.248   2.571  1.00 79.65           C  
ANISOU 1839  C   ASP C  80    10457  12636   7170    243   -961    308       C  
ATOM   1840  O   ASP C  80      74.249  27.277   1.411  1.00 81.36           O  
ANISOU 1840  O   ASP C  80    10608  13092   7213    195   -903    388       O  
ATOM   1841  CB  ASP C  80      73.044  29.606   3.040  1.00 79.09           C  
ANISOU 1841  CB  ASP C  80    10675  12135   7239    -99  -1125    465       C  
ATOM   1842  CG  ASP C  80      74.202  29.908   3.978  1.00 80.36           C  
ANISOU 1842  CG  ASP C  80    10675  12516   7343   -286  -1088    566       C  
ATOM   1843  OD1 ASP C  80      74.328  29.248   5.028  1.00 79.69           O  
ANISOU 1843  OD1 ASP C  80    10474  12483   7322   -228  -1073    497       O  
ATOM   1844  OD2 ASP C  80      74.988  30.825   3.662  1.00 82.46           O  
ANISOU 1844  OD2 ASP C  80    10922  12929   7479   -520  -1085    741       O  
ATOM   1845  N   LEU C  81      74.416  26.484   3.506  1.00 80.66           N  
ANISOU 1845  N   LEU C  81    10034  12649   7966    247  -1135    211       N  
ATOM   1846  CA  LEU C  81      75.574  25.616   3.259  1.00 82.50           C  
ANISOU 1846  CA  LEU C  81    10060  13211   8077    431  -1055    170       C  
ATOM   1847  C   LEU C  81      75.592  24.462   4.260  1.00 82.00           C  
ANISOU 1847  C   LEU C  81    10002  13017   8137    632  -1109     66       C  
ATOM   1848  O   LEU C  81      75.222  24.642   5.435  1.00 80.48           O  
ANISOU 1848  O   LEU C  81     9883  12607   8090    517  -1176    100       O  
ATOM   1849  CB  LEU C  81      76.879  26.408   3.390  1.00 84.32           C  
ANISOU 1849  CB  LEU C  81    10046  13800   8190    234   -992    333       C  
ATOM   1850  CG  LEU C  81      77.269  27.390   2.281  1.00 86.12           C  
ANISOU 1850  CG  LEU C  81    10215  14267   8240    -20   -935    507       C  
ATOM   1851  CD1 LEU C  81      77.812  28.671   2.885  1.00 86.62           C  
ANISOU 1851  CD1 LEU C  81    10250  14318   8345   -400   -995    692       C  
ATOM   1852  CD2 LEU C  81      78.260  26.771   1.317  1.00 89.08           C  
ANISOU 1852  CD2 LEU C  81    10323  15167   8355    121   -795    509       C  
ATOM   1853  N   TYR C  82      76.019  23.289   3.783  1.00 82.95           N  
ANISOU 1853  N   TYR C  82     9453  13182   8882    351   -771    250       N  
ATOM   1854  CA  TYR C  82      76.205  22.086   4.609  1.00 83.52           C  
ANISOU 1854  CA  TYR C  82     9558  13137   9040    597   -849    168       C  
ATOM   1855  C   TYR C  82      76.827  20.929   3.814  1.00 86.27           C  
ANISOU 1855  C   TYR C  82     9909  13600   9271   1018   -851    -13       C  
ATOM   1856  O   TYR C  82      76.834  20.949   2.583  1.00 87.67           O  
ANISOU 1856  O   TYR C  82    10066  13961   9282   1136   -778   -110       O  
ATOM   1857  CB  TYR C  82      74.882  21.642   5.241  1.00 81.64           C  
ANISOU 1857  CB  TYR C  82     9576  12457   8986    515   -967    151       C  
ATOM   1858  CG  TYR C  82      73.778  21.378   4.248  1.00 81.18           C  
ANISOU 1858  CG  TYR C  82     9717  12191   8936    504  -1005     51       C  
ATOM   1859  CD1 TYR C  82      72.854  22.372   3.931  1.00 79.57           C  
ANISOU 1859  CD1 TYR C  82     9541  11942   8749    263   -983    114       C  
ATOM   1860  CD2 TYR C  82      73.651  20.130   3.632  1.00 82.84           C  
ANISOU 1860  CD2 TYR C  82    10108  12243   9125    752  -1090   -119       C  
ATOM   1861  CE1 TYR C  82      71.835  22.134   3.027  1.00 79.45           C  
ANISOU 1861  CE1 TYR C  82     9673  11785   8728    254  -1037     31       C  
ATOM   1862  CE2 TYR C  82      72.641  19.881   2.726  1.00 82.80           C  
ANISOU 1862  CE2 TYR C  82    10281  12068   9110    708  -1152   -218       C  
ATOM   1863  CZ  TYR C  82      71.736  20.888   2.426  1.00 81.00           C  
ANISOU 1863  CZ  TYR C  82    10022  11857   8898    451  -1120   -132       C  
ATOM   1864  OH  TYR C  82      70.724  20.645   1.521  1.00 81.24           O  
ANISOU 1864  OH  TYR C  82    10199  11763   8906    407  -1200   -222       O  
ATOM   1865  N   PRO C  83      77.358  19.911   4.510  1.00 89.62           N  
ANISOU 1865  N   PRO C  83    10096  13413  10541   1068   -267    212       N  
ATOM   1866  CA  PRO C  83      77.927  18.795   3.768  1.00 92.85           C  
ANISOU 1866  CA  PRO C  83    10544  13911  10822   1527   -285      4       C  
ATOM   1867  C   PRO C  83      76.888  17.773   3.316  1.00 93.10           C  
ANISOU 1867  C   PRO C  83    10990  13448  10935   1646   -439   -171       C  
ATOM   1868  O   PRO C  83      75.839  17.628   3.957  1.00 91.00           O  
ANISOU 1868  O   PRO C  83    10948  12776  10852   1380   -550    -92       O  
ATOM   1869  CB  PRO C  83      78.893  18.168   4.774  1.00 94.88           C  
ANISOU 1869  CB  PRO C  83    10663  14288  11098   1807   -348     31       C  
ATOM   1870  CG  PRO C  83      78.291  18.457   6.097  1.00 92.36           C  
ANISOU 1870  CG  PRO C  83    10481  13624  10986   1509   -458    200       C  
ATOM   1871  CD  PRO C  83      77.492  19.730   5.967  1.00 88.99           C  
ANISOU 1871  CD  PRO C  83    10042  13164  10607   1022   -370    320       C  
ATOM   1872  N   VAL C  84      77.187  17.083   2.214  1.00100.97           N  
ANISOU 1872  N   VAL C  84    12471  14485  11407   1333    439  -1049       N  
ATOM   1873  CA  VAL C  84      76.344  15.991   1.707  1.00102.41           C  
ANISOU 1873  CA  VAL C  84    13082  14209  11622   1491    257  -1270       C  
ATOM   1874  C   VAL C  84      77.146  14.694   1.561  1.00106.84           C  
ANISOU 1874  C   VAL C  84    13787  14706  12100   2074    144  -1507       C  
ATOM   1875  O   VAL C  84      76.582  13.638   1.269  1.00108.88           O  
ANISOU 1875  O   VAL C  84    14471  14497  12400   2239    -64  -1703       O  
ATOM   1876  CB  VAL C  84      75.734  16.339   0.338  1.00102.45           C  
ANISOU 1876  CB  VAL C  84    13154  14306  11467   1412    315  -1404       C  
ATOM   1877  CG1 VAL C  84      74.968  15.151  -0.222  1.00103.46           C  
ANISOU 1877  CG1 VAL C  84    13745  13881  11684   1411     75  -1582       C  
ATOM   1878  CG2 VAL C  84      74.831  17.558   0.451  1.00 98.85           C  
ANISOU 1878  CG2 VAL C  84    12513  14005  11042    927    441  -1174       C  
ATOM   1879  N   THR C  85      78.457  14.785   1.778  1.00116.11           N  
ANISOU 1879  N   THR C  85    15168  15204  13746   3288    416  -1253       N  
ATOM   1880  CA  THR C  85      79.337  13.613   1.797  1.00120.80           C  
ANISOU 1880  CA  THR C  85    15858  15773  14269   3926    294  -1465       C  
ATOM   1881  C   THR C  85      79.414  13.041   3.215  1.00120.83           C  
ANISOU 1881  C   THR C  85    16059  15338  14511   3946     76  -1315       C  
ATOM   1882  O   THR C  85      79.282  13.775   4.192  1.00117.53           O  
ANISOU 1882  O   THR C  85    15495  14924  14238   3526    106  -1030       O  
ATOM   1883  CB  THR C  85      80.742  13.959   1.301  1.00123.64           C  
ANISOU 1883  CB  THR C  85    15684  16931  14361   4287    513  -1507       C  
ATOM   1884  OG1 THR C  85      80.731  15.256   0.695  1.00122.33           O  
ANISOU 1884  OG1 THR C  85    15214  17269  13995   3994    763  -1451       O  
ATOM   1885  CG2 THR C  85      81.210  12.940   0.275  1.00129.67           C  
ANISOU 1885  CG2 THR C  85    16572  17751  14945   5095    417  -1867       C  
ATOM   1886  N   LEU C  86      79.627  11.732   3.315  1.00134.27           N  
ANISOU 1886  N   LEU C  86    19915  15404  15699   4575   -368  -1220       N  
ATOM   1887  CA  LEU C  86      79.812  11.065   4.600  1.00135.22           C  
ANISOU 1887  CA  LEU C  86    20215  15161  16001   4655   -587  -1052       C  
ATOM   1888  C   LEU C  86      81.029  11.629   5.336  1.00134.92           C  
ANISOU 1888  C   LEU C  86    19619  15746  15898   4727   -432   -863       C  
ATOM   1889  O   LEU C  86      80.955  11.928   6.529  1.00131.67           O  
ANISOU 1889  O   LEU C  86    19069  15348  15613   4281   -410   -569       O  
ATOM   1890  CB  LEU C  86      79.953   9.554   4.404  1.00140.91           C  
ANISOU 1890  CB  LEU C  86    21419  15400  16719   5292   -888  -1306       C  
ATOM   1891  CG  LEU C  86      79.916   8.700   5.672  1.00141.70           C  
ANISOU 1891  CG  LEU C  86    22063  14716  17061   5132  -1230  -1131       C  
ATOM   1892  CD1 LEU C  86      78.519   8.691   6.274  1.00137.16           C  
ANISOU 1892  CD1 LEU C  86    21648  13814  16651   4336  -1229   -908       C  
ATOM   1893  CD2 LEU C  86      80.381   7.281   5.379  1.00147.54           C  
ANISOU 1893  CD2 LEU C  86    23425  14838  17797   5669  -1562  -1430       C  
ATOM   1894  N   TRP C  87      82.136  11.784   4.612  1.00140.20           N  
ANISOU 1894  N   TRP C  87    18490  17830  16948   6942   -811  -1070       N  
ATOM   1895  CA  TRP C  87      83.359  12.367   5.161  1.00140.45           C  
ANISOU 1895  CA  TRP C  87    17914  18568  16882   6967   -656   -893       C  
ATOM   1896  C   TRP C  87      83.188  13.834   5.541  1.00135.26           C  
ANISOU 1896  C   TRP C  87    16945  18172  16276   6217   -460   -605       C  
ATOM   1897  O   TRP C  87      83.570  14.242   6.639  1.00133.08           O  
ANISOU 1897  O   TRP C  87    16627  17795  16144   5892   -527   -354       O  
ATOM   1898  CB  TRP C  87      84.518  12.191   4.181  1.00145.09           C  
ANISOU 1898  CB  TRP C  87    18083  19880  17165   7550   -491  -1128       C  
ATOM   1899  CG  TRP C  87      85.309  10.916   4.359  1.00151.01           C  
ANISOU 1899  CG  TRP C  87    18986  20527  17865   8384   -706  -1348       C  
ATOM   1900  CD1 TRP C  87      86.423  10.552   3.662  1.00156.59           C  
ANISOU 1900  CD1 TRP C  87    19341  21865  18291   9095   -615  -1597       C  
ATOM   1901  CD2 TRP C  87      85.062   9.856   5.305  1.00152.58           C  
ANISOU 1901  CD2 TRP C  87    19735  19956  18284   8622  -1064  -1327       C  
ATOM   1902  NE1 TRP C  87      86.877   9.331   4.095  1.00161.55           N  
ANISOU 1902  NE1 TRP C  87    20292  22126  18964   9819   -905  -1771       N  
ATOM   1903  CE2 TRP C  87      86.064   8.882   5.104  1.00159.24           C  
ANISOU 1903  CE2 TRP C  87    20578  20945  18982   9526  -1198  -1591       C  
ATOM   1904  CE3 TRP C  87      84.092   9.633   6.297  1.00149.50           C  
ANISOU 1904  CE3 TRP C  87    19835  18792  18175   8156  -1287  -1100       C  
ATOM   1905  CZ2 TRP C  87      86.126   7.701   5.857  1.00162.94           C  
ANISOU 1905  CZ2 TRP C  87    21582  20728  19601   9986  -1582  -1624       C  
ATOM   1906  CZ3 TRP C  87      84.155   8.459   7.046  1.00153.14           C  
ANISOU 1906  CZ3 TRP C  87    20799  18619  18769   8548  -1649  -1101       C  
ATOM   1907  CH2 TRP C  87      85.166   7.510   6.819  1.00159.77           C  
ANISOU 1907  CH2 TRP C  87    21686  19539  19481   9452  -1807  -1357       C  
ATOM   1908  N   GLY C  88      82.612  14.620   4.638  1.00120.06           N  
ANISOU 1908  N   GLY C  88    13446  17808  14363   4650   -201   -555       N  
ATOM   1909  CA  GLY C  88      82.302  16.020   4.918  1.00115.65           C  
ANISOU 1909  CA  GLY C  88    12685  17397  13860   3965    -55   -299       C  
ATOM   1910  C   GLY C  88      81.382  16.189   6.117  1.00111.87           C  
ANISOU 1910  C   GLY C  88    12471  16396  13638   3522   -190    -93       C  
ATOM   1911  O   GLY C  88      81.425  17.213   6.799  1.00109.42           O  
ANISOU 1911  O   GLY C  88    11937  16274  13365   3088   -117    119       O  
ATOM   1912  N   ARG C  89      80.549  15.181   6.370  1.00109.25           N  
ANISOU 1912  N   ARG C  89    13279  14942  13289   2705   -835     13       N  
ATOM   1913  CA  ARG C  89      79.633  15.192   7.510  1.00106.37           C  
ANISOU 1913  CA  ARG C  89    13156  14132  13128   2296   -957    220       C  
ATOM   1914  C   ARG C  89      80.316  14.794   8.820  1.00107.63           C  
ANISOU 1914  C   ARG C  89    13229  14334  13332   2399  -1084    391       C  
ATOM   1915  O   ARG C  89      79.849  15.163   9.901  1.00105.13           O  
ANISOU 1915  O   ARG C  89    12885  13964  13095   1996  -1091    599       O  
ATOM   1916  CB  ARG C  89      78.393  14.330   7.233  1.00106.27           C  
ANISOU 1916  CB  ARG C  89    13667  13464  13246   2234  -1132    142       C  
ATOM   1917  CG  ARG C  89      77.374  15.049   6.364  1.00104.46           C  
ANISOU 1917  CG  ARG C  89    13491  13221  12977   2016  -1018     22       C  
ATOM   1918  CD  ARG C  89      76.230  14.170   5.875  1.00104.32           C  
ANISOU 1918  CD  ARG C  89    13930  12629  13076   1842  -1189    -40       C  
ATOM   1919  NE  ARG C  89      75.273  14.974   5.109  1.00101.77           N  
ANISOU 1919  NE  ARG C  89    13534  12419  12714   1527  -1053    -78       N  
ATOM   1920  CZ  ARG C  89      74.160  14.517   4.543  1.00101.50           C  
ANISOU 1920  CZ  ARG C  89    13779  12056  12729   1329  -1154   -152       C  
ATOM   1921  NH1 ARG C  89      73.825  13.238   4.643  1.00103.69           N  
ANISOU 1921  NH1 ARG C  89    14463  11828  13107   1346  -1401   -194       N  
ATOM   1922  NH2 ARG C  89      73.370  15.347   3.875  1.00 99.43           N  
ANISOU 1922  NH2 ARG C  89    13399  11967  12412   1089  -1033   -167       N  
ATOM   1923  N   CYS C  90      81.415  14.046   8.721  1.00117.64           N  
ANISOU 1923  N   CYS C  90    14558  15154  14986   3592  -1665    719       N  
ATOM   1924  CA  CYS C  90      82.266  13.777   9.877  1.00119.44           C  
ANISOU 1924  CA  CYS C  90    14596  15581  15206   3750  -1773    880       C  
ATOM   1925  C   CYS C  90      82.920  15.070  10.326  1.00117.63           C  
ANISOU 1925  C   CYS C  90    13845  15961  14887   3406  -1590   1024       C  
ATOM   1926  O   CYS C  90      82.742  15.489  11.467  1.00115.17           O  
ANISOU 1926  O   CYS C  90    13530  15584  14644   2985  -1613   1221       O  
ATOM   1927  CB  CYS C  90      83.332  12.735   9.554  1.00124.84           C  
ANISOU 1927  CB  CYS C  90    15225  16424  15786   4495  -1892    716       C  
ATOM   1928  SG  CYS C  90      82.732  11.044   9.605  1.00128.11           S  
ANISOU 1928  SG  CYS C  90    16373  15984  16319   4920  -2208    557       S  
ATOM   1929  N   VAL C  91      83.658  15.703   9.415  1.00113.99           N  
ANISOU 1929  N   VAL C  91    11953  17298  14059   3680  -1324   1022       N  
ATOM   1930  CA  VAL C  91      84.251  17.016   9.663  1.00112.68           C  
ANISOU 1930  CA  VAL C  91    11323  17685  13805   3251  -1170   1180       C  
ATOM   1931  C   VAL C  91      83.257  17.905  10.415  1.00108.13           C  
ANISOU 1931  C   VAL C  91    10953  16762  13371   2623  -1173   1342       C  
ATOM   1932  O   VAL C  91      83.623  18.544  11.401  1.00107.60           O  
ANISOU 1932  O   VAL C  91    10712  16869  13302   2346  -1217   1506       O  
ATOM   1933  CB  VAL C  91      84.673  17.702   8.350  1.00113.57           C  
ANISOU 1933  CB  VAL C  91    11094  18329  13729   3213   -930   1091       C  
ATOM   1934  CG1 VAL C  91      85.172  19.112   8.623  1.00112.59           C  
ANISOU 1934  CG1 VAL C  91    10567  18684  13529   2667   -815   1296       C  
ATOM   1935  CG2 VAL C  91      85.737  16.880   7.639  1.00118.66           C  
ANISOU 1935  CG2 VAL C  91    11449  19454  14182   3851   -904    927       C  
ATOM   1936  N   ALA C  92      81.999  17.908   9.964  1.00 97.67           N  
ANISOU 1936  N   ALA C  92    10522  15201  11387   1668  -1304    979       N  
ATOM   1937  CA  ALA C  92      80.930  18.685  10.600  1.00 93.84           C  
ANISOU 1937  CA  ALA C  92    10215  14425  11014   1145  -1293   1098       C  
ATOM   1938  C   ALA C  92      80.865  18.440  12.113  1.00 93.62           C  
ANISOU 1938  C   ALA C  92    10283  14239  11051   1039  -1446   1254       C  
ATOM   1939  O   ALA C  92      81.117  19.352  12.906  1.00 92.93           O  
ANISOU 1939  O   ALA C  92    10002  14387  10922    746  -1436   1371       O  
ATOM   1940  CB  ALA C  92      79.586  18.395   9.937  1.00 91.78           C  
ANISOU 1940  CB  ALA C  92    10316  13707  10848   1051  -1276   1000       C  
ATOM   1941  N   VAL C  93      80.561  17.200  12.498  1.00 97.24           N  
ANISOU 1941  N   VAL C  93    11140  14138  11668    900  -1999   1715       N  
ATOM   1942  CA  VAL C  93      80.489  16.798  13.903  1.00 97.91           C  
ANISOU 1942  CA  VAL C  93    11346  14079  11778    859  -2163   1885       C  
ATOM   1943  C   VAL C  93      81.649  17.401  14.699  1.00 99.20           C  
ANISOU 1943  C   VAL C  93    11118  14746  11827    844  -2176   1983       C  
ATOM   1944  O   VAL C  93      81.427  18.029  15.739  1.00 97.54           O  
ANISOU 1944  O   VAL C  93    10854  14617  11591    465  -2163   2088       O  
ATOM   1945  CB  VAL C  93      80.509  15.267  14.054  1.00100.97           C  
ANISOU 1945  CB  VAL C  93    12077  14067  12221   1262  -2380   1887       C  
ATOM   1946  CG1 VAL C  93      81.264  14.864  15.312  1.00103.26           C  
ANISOU 1946  CG1 VAL C  93    12373  14389  12472   1377  -2573   2082       C  
ATOM   1947  CG2 VAL C  93      79.091  14.715  14.076  1.00 99.63           C  
ANISOU 1947  CG2 VAL C  93    12333  13358  12164   1039  -2429   1898       C  
ATOM   1948  N   VAL C  94      82.872  17.219  14.198  1.00103.74           N  
ANISOU 1948  N   VAL C  94    11163  15923  12329   1448  -2382   2426       N  
ATOM   1949  CA  VAL C  94      84.068  17.755  14.848  1.00105.51           C  
ANISOU 1949  CA  VAL C  94    10951  16708  12430   1407  -2407   2525       C  
ATOM   1950  C   VAL C  94      83.930  19.264  15.081  1.00102.69           C  
ANISOU 1950  C   VAL C  94    10437  16537  12043    817  -2273   2568       C  
ATOM   1951  O   VAL C  94      84.039  19.714  16.219  1.00101.98           O  
ANISOU 1951  O   VAL C  94    10367  16449  11931    525  -2353   2680       O  
ATOM   1952  CB  VAL C  94      85.372  17.405  14.073  1.00109.43           C  
ANISOU 1952  CB  VAL C  94    11040  17733  12805   1865  -2379   2434       C  
ATOM   1953  CG1 VAL C  94      86.572  18.120  14.669  1.00111.22           C  
ANISOU 1953  CG1 VAL C  94    10745  18621  12891   1676  -2384   2552       C  
ATOM   1954  CG2 VAL C  94      85.599  15.902  14.063  1.00112.98           C  
ANISOU 1954  CG2 VAL C  94    11689  17962  13276   2512  -2565   2378       C  
ATOM   1955  N   VAL C  95      83.657  20.036  14.030  1.00 95.96           N  
ANISOU 1955  N   VAL C  95     9885  16248  10328    456  -2046   1940       N  
ATOM   1956  CA  VAL C  95      83.512  21.491  14.193  1.00 94.07           C  
ANISOU 1956  CA  VAL C  95     9553  16126  10063    -84  -1970   1993       C  
ATOM   1957  C   VAL C  95      82.307  21.878  15.064  1.00 91.04           C  
ANISOU 1957  C   VAL C  95     9522  15306   9764   -408  -2009   2018       C  
ATOM   1958  O   VAL C  95      82.338  22.902  15.755  1.00 90.70           O  
ANISOU 1958  O   VAL C  95     9425  15367   9669   -766  -2045   2070       O  
ATOM   1959  CB  VAL C  95      83.319  22.194  12.837  1.00 93.86           C  
ANISOU 1959  CB  VAL C  95     9356  16323   9983   -257  -1793   1944       C  
ATOM   1960  CG1 VAL C  95      83.927  21.366  11.716  1.00 94.87           C  
ANISOU 1960  CG1 VAL C  95     9499  16452  10096    165  -1708   1819       C  
ATOM   1961  CG2 VAL C  95      81.843  22.454  12.577  1.00 90.72           C  
ANISOU 1961  CG2 VAL C  95     9199  15619   9651   -732  -1733   1949       C  
ATOM   1962  N   MET C  96      81.267  21.045  15.046  1.00 88.53           N  
ANISOU 1962  N   MET C  96     9831  14746   9059   -578  -2034   1639       N  
ATOM   1963  CA  MET C  96      80.102  21.232  15.920  1.00 86.58           C  
ANISOU 1963  CA  MET C  96     9855  14193   8848   -829  -2071   1683       C  
ATOM   1964  C   MET C  96      80.484  21.168  17.402  1.00 88.01           C  
ANISOU 1964  C   MET C  96    10001  14502   8935   -883  -2218   1806       C  
ATOM   1965  O   MET C  96      80.308  22.149  18.125  1.00 87.41           O  
ANISOU 1965  O   MET C  96     9895  14529   8788  -1193  -2219   1806       O  
ATOM   1966  CB  MET C  96      79.027  20.189  15.610  1.00 85.47           C  
ANISOU 1966  CB  MET C  96    10039  13625   8812   -727  -2070   1661       C  
ATOM   1967  CG  MET C  96      78.508  20.237  14.183  1.00 83.33           C  
ANISOU 1967  CG  MET C  96     9858  13195   8609   -846  -1935   1547       C  
ATOM   1968  SD  MET C  96      77.055  19.200  13.935  1.00 83.89           S  
ANISOU 1968  SD  MET C  96    10221  12871   8783   -586  -1993   1500       S  
ATOM   1969  CE  MET C  96      75.825  20.112  14.865  1.00 82.25           C  
ANISOU 1969  CE  MET C  96    10269  12362   8621   -906  -2004   1581       C  
ATOM   1970  N   VAL C  97      81.008  20.025  17.847  1.00 90.14           N  
ANISOU 1970  N   VAL C  97    10168  14840   9241   -621  -2120   2189       N  
ATOM   1971  CA  VAL C  97      81.353  19.849  19.260  1.00 91.83           C  
ANISOU 1971  CA  VAL C  97    10347  15208   9336   -673  -2276   2328       C  
ATOM   1972  C   VAL C  97      82.489  20.773  19.701  1.00 92.91           C  
ANISOU 1972  C   VAL C  97    10139  15811   9352   -875  -2301   2321       C  
ATOM   1973  O   VAL C  97      82.490  21.251  20.828  1.00 92.37           O  
ANISOU 1973  O   VAL C  97    10105  15800   9192  -1196  -2325   2322       O  
ATOM   1974  CB  VAL C  97      81.635  18.357  19.650  1.00 95.16           C  
ANISOU 1974  CB  VAL C  97    10782  15638   9738   -249  -2468   2451       C  
ATOM   1975  CG1 VAL C  97      80.464  17.460  19.244  1.00 95.43           C  
ANISOU 1975  CG1 VAL C  97    11181  15304   9775   -267  -2574   2596       C  
ATOM   1976  CG2 VAL C  97      82.949  17.845  19.055  1.00 95.53           C  
ANISOU 1976  CG2 VAL C  97    10947  15432   9919    118  -2425   2341       C  
ATOM   1977  N   ALA C  98      83.429  21.045  18.797  1.00 93.46           N  
ANISOU 1977  N   ALA C  98    10069  16435   9008   -701  -2242   2101       N  
ATOM   1978  CA  ALA C  98      84.520  21.982  19.060  1.00 94.80           C  
ANISOU 1978  CA  ALA C  98     9880  17069   9072   -973  -2253   2102       C  
ATOM   1979  C   ALA C  98      83.978  23.339  19.473  1.00 92.92           C  
ANISOU 1979  C   ALA C  98     9788  16716   8802  -1474  -2228   2054       C  
ATOM   1980  O   ALA C  98      84.524  23.989  20.355  1.00 94.38           O  
ANISOU 1980  O   ALA C  98     9884  17113   8863  -1712  -2359   2090       O  
ATOM   1981  CB  ALA C  98      85.400  22.122  17.845  1.00 95.57           C  
ANISOU 1981  CB  ALA C  98     9697  17430   9185   -890  -2120   2044       C  
ATOM   1982  N   GLY C  99      82.897  23.757  18.828  1.00 89.73           N  
ANISOU 1982  N   GLY C  99     9871  15860   8361  -1654  -2201   1768       N  
ATOM   1983  CA  GLY C  99      82.216  24.995  19.180  1.00 88.33           C  
ANISOU 1983  CA  GLY C  99     9884  15517   8159  -2046  -2188   1688       C  
ATOM   1984  C   GLY C  99      81.491  24.891  20.508  1.00 87.66           C  
ANISOU 1984  C   GLY C  99    10065  15232   8009  -2075  -2247   1678       C  
ATOM   1985  O   GLY C  99      81.708  25.710  21.399  1.00 88.69           O  
ANISOU 1985  O   GLY C  99    10230  15458   8011  -2313  -2347   1643       O  
ATOM   1986  N   ILE C 100      80.636  23.879  20.642  1.00 85.46           N  
ANISOU 1986  N   ILE C 100     9859  14558   8054  -1679  -2135   1632       N  
ATOM   1987  CA  ILE C 100      79.860  23.677  21.864  1.00 85.38           C  
ANISOU 1987  CA  ILE C 100    10059  14433   7948  -1720  -2170   1665       C  
ATOM   1988  C   ILE C 100      80.792  23.618  23.083  1.00 88.15           C  
ANISOU 1988  C   ILE C 100    10269  15105   8119  -1753  -2357   1761       C  
ATOM   1989  O   ILE C 100      80.638  24.398  24.030  1.00 88.88           O  
ANISOU 1989  O   ILE C 100    10431  15295   8046  -1978  -2420   1701       O  
ATOM   1990  CB  ILE C 100      79.021  22.388  21.793  1.00 84.99           C  
ANISOU 1990  CB  ILE C 100    10180  14139   7973  -1492  -2149   1777       C  
ATOM   1991  CG1 ILE C 100      78.042  22.452  20.618  1.00 82.63           C  
ANISOU 1991  CG1 ILE C 100    10010  13554   7831  -1482  -1993   1684       C  
ATOM   1992  CG2 ILE C 100      78.280  22.161  23.102  1.00 85.87           C  
ANISOU 1992  CG2 ILE C 100    10466  14234   7927  -1576  -2203   1887       C  
ATOM   1993  CD1 ILE C 100      77.349  21.139  20.328  1.00 82.89           C  
ANISOU 1993  CD1 ILE C 100    10204  13329   7960  -1282  -2016   1789       C  
ATOM   1994  N   THR C 101      81.766  22.706  23.034  1.00 89.26           N  
ANISOU 1994  N   THR C 101    10165  15660   8089  -1208  -2132   1808       N  
ATOM   1995  CA  THR C 101      82.703  22.480  24.129  1.00 92.25           C  
ANISOU 1995  CA  THR C 101    10411  16343   8295  -1165  -2335   1936       C  
ATOM   1996  C   THR C 101      83.487  23.732  24.474  1.00 93.57           C  
ANISOU 1996  C   THR C 101    10389  16832   8330  -1489  -2422   1855       C  
ATOM   1997  O   THR C 101      83.432  24.184  25.607  1.00 94.42           O  
ANISOU 1997  O   THR C 101    10609  17005   8263  -1681  -2513   1835       O  
ATOM   1998  CB  THR C 101      83.642  21.286  23.832  1.00 94.53           C  
ANISOU 1998  CB  THR C 101    10520  16762   8635   -754  -2441   2070       C  
ATOM   1999  OG1 THR C 101      82.920  20.066  24.021  1.00 95.58           O  
ANISOU 1999  OG1 THR C 101    10905  16685   8725   -559  -2548   2237       O  
ATOM   2000  CG2 THR C 101      84.843  21.275  24.756  1.00 97.77           C  
ANISOU 2000  CG2 THR C 101    10534  17696   8920   -750  -2605   2117       C  
ATOM   2001  N   SER C 102      84.194  24.311  23.510  1.00 93.39           N  
ANISOU 2001  N   SER C 102    10095  17035   8355  -1497  -2452   1600       N  
ATOM   2002  CA  SER C 102      85.032  25.469  23.820  1.00 95.44           C  
ANISOU 2002  CA  SER C 102    10204  17587   8473  -1875  -2588   1553       C  
ATOM   2003  C   SER C 102      84.218  26.680  24.293  1.00 94.00           C  
ANISOU 2003  C   SER C 102    10359  17114   8244  -2216  -2558   1373       C  
ATOM   2004  O   SER C 102      84.702  27.473  25.098  1.00 96.00           O  
ANISOU 2004  O   SER C 102    10632  17507   8338  -2515  -2716   1303       O  
ATOM   2005  CB  SER C 102      85.961  25.837  22.654  1.00 97.15           C  
ANISOU 2005  CB  SER C 102    10029  18153   8732  -1998  -2588   1580       C  
ATOM   2006  OG  SER C 102      85.256  26.487  21.608  1.00 94.99           O  
ANISOU 2006  OG  SER C 102     9877  17625   8590  -2179  -2418   1483       O  
ATOM   2007  N   PHE C 103      82.990  26.819  23.803  1.00 91.80           N  
ANISOU 2007  N   PHE C 103    10253  16421   8207  -2109  -2463   1301       N  
ATOM   2008  CA  PHE C 103      82.107  27.875  24.293  1.00 91.23           C  
ANISOU 2008  CA  PHE C 103    10479  16118   8067  -2356  -2456   1109       C  
ATOM   2009  C   PHE C 103      81.586  27.552  25.689  1.00 92.20           C  
ANISOU 2009  C   PHE C 103    10765  16293   7975  -2315  -2527   1090       C  
ATOM   2010  O   PHE C 103      81.180  28.449  26.424  1.00 93.44           O  
ANISOU 2010  O   PHE C 103    11106  16425   7971  -2518  -2609    919       O  
ATOM   2011  CB  PHE C 103      80.942  28.138  23.331  1.00 88.33           C  
ANISOU 2011  CB  PHE C 103    10328  15369   7864  -2297  -2259   1002       C  
ATOM   2012  CG  PHE C 103      81.224  29.217  22.312  1.00 88.40           C  
ANISOU 2012  CG  PHE C 103    10336  15276   7975  -2535  -2255    934       C  
ATOM   2013  CD1 PHE C 103      81.370  30.549  22.706  1.00 90.51           C  
ANISOU 2013  CD1 PHE C 103    10752  15495   8141  -2881  -2413    803       C  
ATOM   2014  CD2 PHE C 103      81.342  28.903  20.960  1.00 86.92           C  
ANISOU 2014  CD2 PHE C 103    10031  15035   7960  -2437  -2119   1005       C  
ATOM   2015  CE1 PHE C 103      81.629  31.555  21.769  1.00 91.23           C  
ANISOU 2015  CE1 PHE C 103    10896  15447   8321  -3164  -2448    784       C  
ATOM   2016  CE2 PHE C 103      81.602  29.899  20.017  1.00 87.43           C  
ANISOU 2016  CE2 PHE C 103    10108  15025   8088  -2697  -2123    988       C  
ATOM   2017  CZ  PHE C 103      81.746  31.229  20.425  1.00 89.65           C  
ANISOU 2017  CZ  PHE C 103    10558  15221   8283  -3078  -2293    895       C  
ATOM   2018  N   GLY C 104      81.601  26.267  26.045  1.00 92.85           N  
ANISOU 2018  N   GLY C 104    10731  16526   8021  -1902  -2317   1332       N  
ATOM   2019  CA  GLY C 104      81.213  25.817  27.380  1.00 94.33           C  
ANISOU 2019  CA  GLY C 104    11046  16828   7968  -1866  -2392   1395       C  
ATOM   2020  C   GLY C 104      82.270  26.191  28.402  1.00 97.61           C  
ANISOU 2020  C   GLY C 104    11339  17590   8157  -2040  -2632   1392       C  
ATOM   2021  O   GLY C 104      81.948  26.652  29.501  1.00 99.01           O  
ANISOU 2021  O   GLY C 104    11690  17835   8095  -2192  -2697   1261       O  
ATOM   2022  N   LEU C 105      83.536  25.997  28.037  1.00100.20           N  
ANISOU 2022  N   LEU C 105    11315  18458   8299  -1958  -2843   1361       N  
ATOM   2023  CA  LEU C 105      84.659  26.400  28.874  1.00103.72           C  
ANISOU 2023  CA  LEU C 105    11589  19287   8534  -2168  -3097   1362       C  
ATOM   2024  C   LEU C 105      84.591  27.865  29.264  1.00104.45           C  
ANISOU 2024  C   LEU C 105    11882  19297   8509  -2547  -3157   1100       C  
ATOM   2025  O   LEU C 105      84.863  28.209  30.413  1.00106.30           O  
ANISOU 2025  O   LEU C 105    12288  19625   8478  -2647  -3274   1008       O  
ATOM   2026  CB  LEU C 105      85.994  26.139  28.183  1.00105.58           C  
ANISOU 2026  CB  LEU C 105    11391  19862   8863  -2160  -3206   1481       C  
ATOM   2027  CG  LEU C 105      86.862  25.031  28.772  1.00108.27           C  
ANISOU 2027  CG  LEU C 105    11497  20544   9095  -1857  -3378   1716       C  
ATOM   2028  CD1 LEU C 105      86.432  23.679  28.235  1.00106.57           C  
ANISOU 2028  CD1 LEU C 105    11306  20112   9075  -1401  -3238   1859       C  
ATOM   2029  CD2 LEU C 105      88.318  25.294  28.435  1.00111.86           C  
ANISOU 2029  CD2 LEU C 105    11480  21529   9493  -1966  -3578   1785       C  
ATOM   2030  N   VAL C 106      84.237  28.725  28.312  1.00104.58           N  
ANISOU 2030  N   VAL C 106    11959  19001   8777  -2640  -3023   1022       N  
ATOM   2031  CA  VAL C 106      84.153  30.163  28.571  1.00105.93           C  
ANISOU 2031  CA  VAL C 106    12395  19002   8853  -3004  -3129    763       C  
ATOM   2032  C   VAL C 106      83.018  30.493  29.552  1.00105.67           C  
ANISOU 2032  C   VAL C 106    12763  18759   8626  -2918  -3077    545       C  
ATOM   2033  O   VAL C 106      83.138  31.421  30.355  1.00108.18           O  
ANISOU 2033  O   VAL C 106    13321  19035   8747  -3148  -3240    307       O  
ATOM   2034  CB  VAL C 106      84.051  30.978  27.261  1.00104.51           C  
ANISOU 2034  CB  VAL C 106    12273  18524   8913  -3174  -3032    694       C  
ATOM   2035  CG1 VAL C 106      83.937  32.474  27.546  1.00107.10           C  
ANISOU 2035  CG1 VAL C 106    12890  18654   9149  -3594  -3229    461       C  
ATOM   2036  CG2 VAL C 106      85.270  30.715  26.394  1.00104.99           C  
ANISOU 2036  CG2 VAL C 106    11894  18881   9118  -3212  -3031    920       C  
ATOM   2037  N   THR C 107      81.936  29.717  29.498  1.00104.44           N  
ANISOU 2037  N   THR C 107    12495  18505   8684  -2532  -2782    794       N  
ATOM   2038  CA  THR C 107      80.879  29.813  30.505  1.00104.89           C  
ANISOU 2038  CA  THR C 107    12832  18524   8498  -2434  -2713    635       C  
ATOM   2039  C   THR C 107      81.388  29.315  31.859  1.00107.92           C  
ANISOU 2039  C   THR C 107    13168  19288   8548  -2451  -2886    723       C  
ATOM   2040  O   THR C 107      81.162  29.961  32.890  1.00110.50           O  
ANISOU 2040  O   THR C 107    13709  19701   8574  -2561  -2991    491       O  
ATOM   2041  CB  THR C 107      79.598  29.060  30.076  1.00101.93           C  
ANISOU 2041  CB  THR C 107    12530  17971   8229  -2159  -2431    701       C  
ATOM   2042  OG1 THR C 107      78.787  29.930  29.280  1.00100.15           O  
ANISOU 2042  OG1 THR C 107    12485  17385   8184  -2160  -2301    473       O  
ATOM   2043  CG2 THR C 107      78.786  28.599  31.292  1.00103.47           C  
ANISOU 2043  CG2 THR C 107    12862  18372   8080  -2052  -2370    687       C  
ATOM   2044  N   ALA C 108      82.088  28.181  31.842  1.00108.07           N  
ANISOU 2044  N   ALA C 108    12967  19668   8428  -2319  -2978    969       N  
ATOM   2045  CA  ALA C 108      82.690  27.609  33.050  1.00111.46           C  
ANISOU 2045  CA  ALA C 108    13313  20490   8547  -2336  -3197   1108       C  
ATOM   2046  C   ALA C 108      83.695  28.552  33.707  1.00114.94           C  
ANISOU 2046  C   ALA C 108    13734  21150   8789  -2657  -3481    920       C  
ATOM   2047  O   ALA C 108      83.701  28.694  34.930  1.00117.55           O  
ANISOU 2047  O   ALA C 108    14265  21625   8772  -2754  -3589    754       O  
ATOM   2048  CB  ALA C 108      83.342  26.274  32.735  1.00111.61           C  
ANISOU 2048  CB  ALA C 108    13051  20666   8688  -2117  -3263   1463       C  
ATOM   2049  N   ALA C 109      84.529  29.191  32.886  1.00117.86           N  
ANISOU 2049  N   ALA C 109    14026  21896   8860  -3393  -3543    736       N  
ATOM   2050  CA  ALA C 109      85.509  30.169  33.353  1.00121.42           C  
ANISOU 2050  CA  ALA C 109    14452  22514   9167  -3793  -3829    570       C  
ATOM   2051  C   ALA C 109      84.836  31.310  34.117  1.00122.98           C  
ANISOU 2051  C   ALA C 109    15099  22514   9113  -3955  -3884    201       C  
ATOM   2052  O   ALA C 109      85.282  31.689  35.201  1.00126.70           O  
ANISOU 2052  O   ALA C 109    15661  23234   9245  -4113  -4123     85       O  
ATOM   2053  CB  ALA C 109      86.319  30.713  32.184  1.00120.95           C  
ANISOU 2053  CB  ALA C 109    14201  22356   9397  -4034  -3843    579       C  
ATOM   2054  N   LEU C 110      83.756  31.838  33.550  1.00121.83           N  
ANISOU 2054  N   LEU C 110    15641  21324   9325  -3736  -3585    321       N  
ATOM   2055  CA  LEU C 110      82.997  32.930  34.166  1.00123.58           C  
ANISOU 2055  CA  LEU C 110    16311  21309   9333  -3801  -3623    -76       C  
ATOM   2056  C   LEU C 110      82.225  32.474  35.405  1.00124.76           C  
ANISOU 2056  C   LEU C 110    16616  21685   9102  -3560  -3546   -155       C  
ATOM   2057  O   LEU C 110      81.991  33.267  36.318  1.00128.07           O  
ANISOU 2057  O   LEU C 110    17336  22125   9200  -3635  -3683   -480       O  
ATOM   2058  CB  LEU C 110      82.016  33.534  33.160  1.00120.78           C  
ANISOU 2058  CB  LEU C 110    16190  20449   9253  -3704  -3414   -245       C  
ATOM   2059  CG  LEU C 110      82.627  34.131  31.891  1.00120.02           C  
ANISOU 2059  CG  LEU C 110    16019  20088   9494  -3971  -3476   -185       C  
ATOM   2060  CD1 LEU C 110      81.542  34.693  30.985  1.00117.76           C  
ANISOU 2060  CD1 LEU C 110    16013  19340   9390  -3801  -3282   -354       C  
ATOM   2061  CD2 LEU C 110      83.644  35.207  32.238  1.00124.38           C  
ANISOU 2061  CD2 LEU C 110    16701  20610   9946  -4451  -3838   -337       C  
ATOM   2062  N   ALA C 111      81.829  31.203  35.421  1.00121.07           N  
ANISOU 2062  N   ALA C 111    15524  21364   9114  -2943  -3388    296       N  
ATOM   2063  CA  ALA C 111      81.069  30.632  36.532  1.00122.28           C  
ANISOU 2063  CA  ALA C 111    15790  21766   8903  -2745  -3274    302       C  
ATOM   2064  C   ALA C 111      81.914  30.510  37.797  1.00126.52           C  
ANISOU 2064  C   ALA C 111    16289  22737   9044  -2884  -3558    345       C  
ATOM   2065  O   ALA C 111      81.395  30.644  38.904  1.00129.37           O  
ANISOU 2065  O   ALA C 111    16863  23307   8984  -2849  -3572    149       O  
ATOM   2066  CB  ALA C 111      80.486  29.284  36.146  1.00119.32           C  
ANISOU 2066  CB  ALA C 111    15244  21412   8679  -2500  -3025    665       C  
ATOM   2067  N   THR C 112      83.213  30.263  37.634  1.00128.15           N  
ANISOU 2067  N   THR C 112    16069  23653   8970  -3398  -3768    509       N  
ATOM   2068  CA  THR C 112      84.117  30.167  38.786  1.00132.68           C  
ANISOU 2068  CA  THR C 112    16579  24672   9163  -3555  -4092    547       C  
ATOM   2069  C   THR C 112      84.677  31.530  39.182  1.00136.16           C  
ANISOU 2069  C   THR C 112    17248  25066   9420  -3890  -4356    128       C  
ATOM   2070  O   THR C 112      85.044  31.735  40.330  1.00139.98           O  
ANISOU 2070  O   THR C 112    17923  25797   9465  -3958  -4519    -62       O  
ATOM   2071  CB  THR C 112      85.277  29.159  38.567  1.00133.43           C  
ANISOU 2071  CB  THR C 112    16246  25071   9382  -3555  -4292    948       C  
ATOM   2072  OG1 THR C 112      86.280  29.738  37.727  1.00132.42           O  
ANISOU 2072  OG1 THR C 112    15891  24808   9615  -3736  -4362    939       O  
ATOM   2073  CG2 THR C 112      84.769  27.883  37.933  1.00131.06           C  
ANISOU 2073  CG2 THR C 112    15811  24763   9221  -3207  -4101   1344       C  
ATOM   2074  N   TRP C 113      84.743  32.454  38.226  1.00140.59           N  
ANISOU 2074  N   TRP C 113    18539  24949   9929  -4900  -4022    -91       N  
ATOM   2075  CA  TRP C 113      85.109  33.843  38.510  1.00144.24           C  
ANISOU 2075  CA  TRP C 113    19296  25246  10263  -5267  -4305   -484       C  
ATOM   2076  C   TRP C 113      84.034  34.492  39.382  1.00146.19           C  
ANISOU 2076  C   TRP C 113    20044  25337  10165  -5123  -4252   -926       C  
ATOM   2077  O   TRP C 113      84.333  35.324  40.237  1.00150.69           O  
ANISOU 2077  O   TRP C 113    20904  25907  10446  -5359  -4545  -1263       O  
ATOM   2078  CB  TRP C 113      85.315  34.628  37.205  1.00142.73           C  
ANISOU 2078  CB  TRP C 113    19111  24626  10492  -5517  -4318   -532       C  
ATOM   2079  CG  TRP C 113      85.482  36.121  37.375  1.00146.71           C  
ANISOU 2079  CG  TRP C 113    20047  24815  10881  -5887  -4607   -947       C  
ATOM   2080  CD1 TRP C 113      86.250  36.767  38.307  1.00152.16           C  
ANISOU 2080  CD1 TRP C 113    20875  25708  11231  -6233  -5003  -1144       C  
ATOM   2081  CD2 TRP C 113      84.886  37.148  36.568  1.00146.13           C  
ANISOU 2081  CD2 TRP C 113    20370  24128  11023  -5952  -4566  -1218       C  
ATOM   2082  NE1 TRP C 113      86.153  38.128  38.141  1.00155.13           N  
ANISOU 2082  NE1 TRP C 113    21743  25593  11605  -6522  -5219  -1535       N  
ATOM   2083  CE2 TRP C 113      85.327  38.390  37.080  1.00151.57           C  
ANISOU 2083  CE2 TRP C 113    21468  24624  11497  -6341  -4960  -1578       C  
ATOM   2084  CE3 TRP C 113      84.019  37.140  35.466  1.00141.92           C  
ANISOU 2084  CE3 TRP C 113    19907  23175  10842  -5722  -4264  -1187       C  
ATOM   2085  CZ2 TRP C 113      84.930  39.615  36.524  1.00153.07           C  
ANISOU 2085  CZ2 TRP C 113    22171  24163  11824  -6487  -5069  -1898       C  
ATOM   2086  CZ3 TRP C 113      83.623  38.361  34.915  1.00143.24           C  
ANISOU 2086  CZ3 TRP C 113    20549  22744  11133  -5852  -4359  -1495       C  
ATOM   2087  CH2 TRP C 113      84.079  39.579  35.445  1.00148.80           C  
ANISOU 2087  CH2 TRP C 113    21685  23220  11631  -6220  -4761  -1837       C  
ATOM   2088  N   PHE C 114      82.786  34.093  39.162  1.00144.38           N  
ANISOU 2088  N   PHE C 114    20165  24054  10640  -4148  -3571   -653       N  
ATOM   2089  CA  PHE C 114      81.676  34.560  39.980  1.00146.63           C  
ANISOU 2089  CA  PHE C 114    20843  24317  10554  -3931  -3477  -1057       C  
ATOM   2090  C   PHE C 114      81.623  33.808  41.310  1.00149.47           C  
ANISOU 2090  C   PHE C 114    21131  25260  10401  -3834  -3504   -950       C  
ATOM   2091  O   PHE C 114      81.236  34.378  42.330  1.00153.83           O  
ANISOU 2091  O   PHE C 114    21982  25979  10486  -3815  -3624  -1315       O  
ATOM   2092  CB  PHE C 114      80.345  34.437  39.226  1.00142.90           C  
ANISOU 2092  CB  PHE C 114    20440  23562  10292  -3574  -3079  -1106       C  
ATOM   2093  CG  PHE C 114      80.147  35.472  38.143  1.00141.82           C  
ANISOU 2093  CG  PHE C 114    20556  22825  10506  -3628  -3100  -1371       C  
ATOM   2094  CD1 PHE C 114      81.013  36.562  38.010  1.00142.51           C  
ANISOU 2094  CD1 PHE C 114    20653  22635  10858  -4035  -3392  -1351       C  
ATOM   2095  CD2 PHE C 114      79.064  35.376  37.273  1.00140.52           C  
ANISOU 2095  CD2 PHE C 114    20598  22392  10401  -3283  -2836  -1606       C  
ATOM   2096  CE1 PHE C 114      80.817  37.522  37.011  1.00141.97           C  
ANISOU 2096  CE1 PHE C 114    20862  21980  11101  -4117  -3429  -1552       C  
ATOM   2097  CE2 PHE C 114      78.857  36.334  36.275  1.00139.95           C  
ANISOU 2097  CE2 PHE C 114    20797  21731  10647  -3308  -2888  -1832       C  
ATOM   2098  CZ  PHE C 114      79.737  37.409  36.146  1.00140.70           C  
ANISOU 2098  CZ  PHE C 114    20957  21508  10996  -3738  -3190  -1791       C  
ATOM   2099  N   VAL C 115      82.011  32.533  41.287  1.00144.91           N  
ANISOU 2099  N   VAL C 115    19380  25913   9766  -3768  -3709   -370       N  
ATOM   2100  CA  VAL C 115      82.130  31.722  42.503  1.00147.73           C  
ANISOU 2100  CA  VAL C 115    19653  26817   9660  -3704  -3765   -160       C  
ATOM   2101  C   VAL C 115      83.336  32.173  43.344  1.00152.62           C  
ANISOU 2101  C   VAL C 115    20269  27751   9968  -4005  -4213   -242       C  
ATOM   2102  O   VAL C 115      83.293  32.132  44.579  1.00156.67           O  
ANISOU 2102  O   VAL C 115    20904  28678   9944  -3987  -4319   -320       O  
ATOM   2103  CB  VAL C 115      82.196  30.199  42.175  1.00144.61           C  
ANISOU 2103  CB  VAL C 115    18925  26554   9465  -3536  -3585    420       C  
ATOM   2104  CG1 VAL C 115      83.011  29.425  43.216  1.00148.00           C  
ANISOU 2104  CG1 VAL C 115    19192  27490   9550  -3583  -3829    757       C  
ATOM   2105  CG2 VAL C 115      80.801  29.616  42.060  1.00142.49           C  
ANISOU 2105  CG2 VAL C 115    18730  26245   9163  -3271  -3185    480       C  
ATOM   2106  N   GLY C 116      84.393  32.618  42.662  1.00161.48           N  
ANISOU 2106  N   GLY C 116    20917  30380  10057  -5845  -4241   -824       N  
ATOM   2107  CA  GLY C 116      85.587  33.168  43.301  1.00166.39           C  
ANISOU 2107  CA  GLY C 116    21528  31254  10440  -6218  -4698   -949       C  
ATOM   2108  C   GLY C 116      85.347  34.503  43.986  1.00170.39           C  
ANISOU 2108  C   GLY C 116    22532  31549  10661  -6401  -4887  -1546       C  
ATOM   2109  O   GLY C 116      86.286  35.255  44.243  1.00173.42           O  
ANISOU 2109  O   GLY C 116    22994  31817  11081  -6810  -5246  -1738       O  
ATOM   2110  N   ARG C 117      84.079  34.803  44.257  1.00181.72           N  
ANISOU 2110  N   ARG C 117    24934  31884  12228  -6590  -3356  -3055       N  
ATOM   2111  CA  ARG C 117      83.693  35.922  45.110  1.00186.52           C  
ANISOU 2111  CA  ARG C 117    26056  32395  12417  -6607  -3512  -3655       C  
ATOM   2112  C   ARG C 117      82.682  35.434  46.145  1.00187.65           C  
ANISOU 2112  C   ARG C 117    26287  32946  12064  -6205  -3226  -3709       C  
ATOM   2113  O   ARG C 117      81.517  35.847  46.166  1.00187.89           O  
ANISOU 2113  O   ARG C 117    26607  32823  11960  -5890  -2974  -4066       O  
ATOM   2114  CB  ARG C 117      83.160  37.102  44.293  1.00185.68           C  
ANISOU 2114  CB  ARG C 117    26325  31593  12632  -6616  -3484  -4064       C  
ATOM   2115  CG  ARG C 117      84.244  37.852  43.535  1.00186.50           C  
ANISOU 2115  CG  ARG C 117    26419  31346  13095  -7131  -3847  -4054       C  
ATOM   2116  CD  ARG C 117      84.013  39.346  43.556  1.00189.88           C  
ANISOU 2116  CD  ARG C 117    27453  31171  13523  -7258  -4061  -4622       C  
ATOM   2117  NE  ARG C 117      85.152  40.072  42.998  1.00189.84           N  
ANISOU 2117  NE  ARG C 117    27397  30778  13954  -7783  -4333  -4498       N  
ATOM   2118  CZ  ARG C 117      85.213  41.393  42.860  1.00194.40           C  
ANISOU 2118  CZ  ARG C 117    28465  30865  14533  -8162  -4720  -4880       C  
ATOM   2119  NH1 ARG C 117      84.199  42.162  43.247  1.00199.75           N  
ANISOU 2119  NH1 ARG C 117    29774  31345  14778  -8028  -4916  -5483       N  
ATOM   2120  NH2 ARG C 117      86.295  41.952  42.335  1.00194.39           N  
ANISOU 2120  NH2 ARG C 117    28340  30602  14919  -8689  -4937  -4668       N  
ATOM   2121  N   GLU C 118      83.159  34.519  46.983  1.00195.44           N  
ANISOU 2121  N   GLU C 118    25151  38077  11030  -5877  -3717  -1962       N  
ATOM   2122  CA  GLU C 118      82.414  33.994  48.122  1.00198.39           C  
ANISOU 2122  CA  GLU C 118    25584  39006  10789  -5644  -3574  -1939       C  
ATOM   2123  C   GLU C 118      82.744  34.796  49.384  1.00205.32           C  
ANISOU 2123  C   GLU C 118    26798  40171  11043  -5784  -3928  -2406       C  
ATOM   2124  O   GLU C 118      82.023  34.728  50.383  1.00208.78           O  
ANISOU 2124  O   GLU C 118    27461  40952  10913  -5546  -3786  -2673       O  
ATOM   2125  CB  GLU C 118      82.750  32.513  48.328  1.00197.09           C  
ANISOU 2125  CB  GLU C 118    25013  39269  10605  -5629  -3538  -1263       C  
ATOM   2126  CG  GLU C 118      84.217  32.239  48.682  1.00199.78           C  
ANISOU 2126  CG  GLU C 118    25139  39880  10887  -5933  -3998  -1030       C  
ATOM   2127  CD  GLU C 118      84.639  30.802  48.433  1.00197.12           C  
ANISOU 2127  CD  GLU C 118    24379  39709  10807  -5856  -3962   -348       C  
ATOM   2128  OE1 GLU C 118      83.795  29.889  48.558  1.00195.51           O  
ANISOU 2128  OE1 GLU C 118    24129  39629  10527  -5612  -3659    -20       O  
ATOM   2129  OE2 GLU C 118      85.826  30.585  48.113  1.00197.07           O  
ANISOU 2129  OE2 GLU C 118    24090  39712  11075  -6042  -4250   -139       O  
ATOM   2130  N   GLN C 119      83.842  35.547  49.315  1.00243.36           N  
ANISOU 2130  N   GLN C 119    30246  49569  12652  -9377  -3145  -7300       N  
ATOM   2131  CA  GLN C 119      84.340  36.370  50.415  1.00250.17           C  
ANISOU 2131  CA  GLN C 119    31459  50605  12989  -9596  -3561  -7776       C  
ATOM   2132  C   GLN C 119      83.358  37.473  50.803  1.00253.04           C  
ANISOU 2132  C   GLN C 119    32391  50668  13085  -9359  -3471  -8483       C  
ATOM   2133  O   GLN C 119      82.584  37.321  51.749  1.00256.04           O  
ANISOU 2133  O   GLN C 119    32940  51455  12890  -9036  -3287  -8696       O  
ATOM   2134  CB  GLN C 119      85.696  36.973  50.035  1.00251.65           C  
ANISOU 2134  CB  GLN C 119    31572  50573  13470 -10123  -4044  -7780       C  
ATOM   2135  CG  GLN C 119      85.671  37.814  48.759  1.00249.77           C  
ANISOU 2135  CG  GLN C 119    31573  49579  13750 -10285  -4072  -8069       C  
ATOM   2136  CD  GLN C 119      86.774  37.449  47.776  1.00246.54           C  
ANISOU 2136  CD  GLN C 119    30718  49024  13932 -10642  -4197  -7628       C  
ATOM   2137  OE1 GLN C 119      87.212  38.286  46.983  1.00246.52           O  
ANISOU 2137  OE1 GLN C 119    30867  48503  14296 -10958  -4362  -7799       O  
ATOM   2138  NE2 GLN C 119      87.217  36.198  47.813  1.00244.20           N  
ANISOU 2138  NE2 GLN C 119    29872  49192  13719 -10577  -4119  -7047       N  
TER    2139      GLN C 119                                                      
ATOM   2140  N   ALA D  23      75.809  42.792  44.273  1.00230.87           N  
ANISOU 2140  N   ALA D  23    45883  29485  12352   4224  -2626  -5461       N  
ATOM   2141  CA  ALA D  23      77.038  41.954  44.173  1.00228.11           C  
ANISOU 2141  CA  ALA D  23    45141  29405  12125   3601  -2772  -4909       C  
ATOM   2142  C   ALA D  23      77.760  42.212  42.849  1.00224.94           C  
ANISOU 2142  C   ALA D  23    44754  28350  12363   3100  -3019  -4629       C  
ATOM   2143  O   ALA D  23      77.668  43.310  42.296  1.00227.93           O  
ANISOU 2143  O   ALA D  23    45665  28039  12900   3005  -3335  -4989       O  
ATOM   2144  CB  ALA D  23      76.683  40.479  44.327  1.00223.37           C  
ANISOU 2144  CB  ALA D  23    43878  29499  11493   3701  -2330  -4342       C  
ATOM   2145  N   LEU D  24      78.490  41.211  42.357  1.00199.91           N  
ANISOU 2145  N   LEU D  24    38983  25354  11619  -1433  -4138  -4472       N  
ATOM   2146  CA  LEU D  24      79.105  41.275  41.030  1.00196.18           C  
ANISOU 2146  CA  LEU D  24    38401  24380  11759  -1812  -4241  -4145       C  
ATOM   2147  C   LEU D  24      78.358  40.376  40.054  1.00189.58           C  
ANISOU 2147  C   LEU D  24    37100  23651  11281  -1551  -3778  -3716       C  
ATOM   2148  O   LEU D  24      77.858  40.848  39.034  1.00187.30           O  
ANISOU 2148  O   LEU D  24    36925  22881  11359  -1398  -3665  -3747       O  
ATOM   2149  CB  LEU D  24      80.587  40.880  41.071  1.00196.27           C  
ANISOU 2149  CB  LEU D  24    38130  24580  11863  -2442  -4548  -3780       C  
ATOM   2150  CG  LEU D  24      81.316  40.833  39.719  1.00192.28           C  
ANISOU 2150  CG  LEU D  24    37363  23743  11950  -2823  -4581  -3360       C  
ATOM   2151  CD1 LEU D  24      81.864  42.201  39.333  1.00196.50           C  
ANISOU 2151  CD1 LEU D  24    38341  23701  12618  -3327  -5048  -3586       C  
ATOM   2152  CD2 LEU D  24      82.430  39.799  39.731  1.00189.23           C  
ANISOU 2152  CD2 LEU D  24    36329  23895  11676  -3076  -4530  -2785       C  
ATOM   2153  N   HIS D  25      78.284  39.086  40.381  1.00166.38           N  
ANISOU 2153  N   HIS D  25    27988  24142  11087  -1104  -3301  -2585       N  
ATOM   2154  CA  HIS D  25      77.664  38.079  39.513  1.00160.59           C  
ANISOU 2154  CA  HIS D  25    26824  23530  10661   -893  -2892  -2160       C  
ATOM   2155  C   HIS D  25      76.259  38.480  39.054  1.00159.76           C  
ANISOU 2155  C   HIS D  25    26909  23138  10654   -428  -2623  -2437       C  
ATOM   2156  O   HIS D  25      75.917  38.346  37.878  1.00156.45           O  
ANISOU 2156  O   HIS D  25    26471  22284  10688   -418  -2547  -2326       O  
ATOM   2157  CB  HIS D  25      77.663  36.698  40.195  1.00159.49           C  
ANISOU 2157  CB  HIS D  25    26263  24079  10256   -838  -2693  -1769       C  
ATOM   2158  CG  HIS D  25      76.654  36.550  41.293  1.00162.33           C  
ANISOU 2158  CG  HIS D  25    26689  24900  10088   -457  -2463  -1991       C  
ATOM   2159  ND1 HIS D  25      76.702  35.521  42.209  1.00161.02           N  
ANISOU 2159  ND1 HIS D  25    26168  25287   9727   -354  -2189  -1604       N  
ATOM   2160  CD2 HIS D  25      75.577  37.299  41.624  1.00166.97           C  
ANISOU 2160  CD2 HIS D  25    27653  25516  10273   -155  -2469  -2552       C  
ATOM   2161  CE1 HIS D  25      75.698  35.643  43.058  1.00164.65           C  
ANISOU 2161  CE1 HIS D  25    26734  26150   9675    -42  -2011  -1888       C  
ATOM   2162  NE2 HIS D  25      74.998  36.711  42.724  1.00168.29           N  
ANISOU 2162  NE2 HIS D  25    27626  26322   9994    122  -2166  -2488       N  
ATOM   2163  N   TRP D  26      75.474  39.002  39.991  1.00178.29           N  
ANISOU 2163  N   TRP D  26    29539  26370  11832   3148   -732  -1083       N  
ATOM   2164  CA  TRP D  26      74.088  39.380  39.761  1.00178.74           C  
ANISOU 2164  CA  TRP D  26    29723  26331  11859   3678   -468  -1388       C  
ATOM   2165  C   TRP D  26      73.998  40.670  38.947  1.00179.91           C  
ANISOU 2165  C   TRP D  26    30339  25708  12312   3762   -677  -1742       C  
ATOM   2166  O   TRP D  26      73.017  40.894  38.238  1.00179.16           O  
ANISOU 2166  O   TRP D  26    30284  25441  12349   4181   -469  -1885       O  
ATOM   2167  CB  TRP D  26      73.406  39.569  41.118  1.00184.43           C  
ANISOU 2167  CB  TRP D  26    30622  27535  11918   4038   -412  -1831       C  
ATOM   2168  CG  TRP D  26      72.181  38.716  41.392  1.00183.92           C  
ANISOU 2168  CG  TRP D  26    30193  28100  11589   4441     47  -1729       C  
ATOM   2169  CD1 TRP D  26      71.351  38.823  42.473  1.00189.05           C  
ANISOU 2169  CD1 TRP D  26    30905  29305  11622   4846    204  -2099       C  
ATOM   2170  CD2 TRP D  26      71.655  37.642  40.591  1.00178.66           C  
ANISOU 2170  CD2 TRP D  26    29033  27624  11224   4452    402  -1221       C  
ATOM   2171  NE1 TRP D  26      70.349  37.887  42.401  1.00187.34           N  
ANISOU 2171  NE1 TRP D  26    30224  29652  11306   5070    646  -1819       N  
ATOM   2172  CE2 TRP D  26      70.508  37.150  41.258  1.00180.98           C  
ANISOU 2172  CE2 TRP D  26    29094  28602  11070   4819    759  -1280       C  
ATOM   2173  CE3 TRP D  26      72.037  37.049  39.381  1.00172.67           C  
ANISOU 2173  CE3 TRP D  26    28011  26552  11043   4181    447   -732       C  
ATOM   2174  CZ2 TRP D  26      69.740  36.096  40.753  1.00177.57           C  
ANISOU 2174  CZ2 TRP D  26    28189  28506  10773   4863   1128   -849       C  
ATOM   2175  CZ3 TRP D  26      71.272  35.999  38.881  1.00169.22           C  
ANISOU 2175  CZ3 TRP D  26    27149  26410  10737   4273    805   -347       C  
ATOM   2176  CH2 TRP D  26      70.137  35.535  39.568  1.00171.69           C  
ANISOU 2176  CH2 TRP D  26    27250  27368  10618   4583   1130   -396       C  
ATOM   2177  N   ARG D  27      75.032  41.505  39.050  1.00183.39           N  
ANISOU 2177  N   ARG D  27    34108  24346  11227   2985  -2349  -3301       N  
ATOM   2178  CA  ARG D  27      75.041  42.836  38.436  1.00186.41           C  
ANISOU 2178  CA  ARG D  27    35081  23955  11792   3033  -2636  -3699       C  
ATOM   2179  C   ARG D  27      75.801  42.890  37.112  1.00183.19           C  
ANISOU 2179  C   ARG D  27    34640  23027  11936   2535  -2813  -3335       C  
ATOM   2180  O   ARG D  27      75.459  43.684  36.233  1.00183.76           O  
ANISOU 2180  O   ARG D  27    35068  22460  12291   2615  -2924  -3475       O  
ATOM   2181  CB  ARG D  27      75.614  43.871  39.411  1.00193.71           C  
ANISOU 2181  CB  ARG D  27    36598  24701  12302   2962  -3058  -4250       C  
ATOM   2182  N   ALA D  28      76.833  42.057  36.984  1.00160.91           N  
ANISOU 2182  N   ALA D  28    28894  21229  11016  -1118  -5274  -4005       N  
ATOM   2183  CA  ALA D  28      77.613  41.960  35.749  1.00157.51           C  
ANISOU 2183  CA  ALA D  28    28276  20492  11079  -1571  -5358  -3585       C  
ATOM   2184  C   ALA D  28      76.762  41.384  34.623  1.00152.21           C  
ANISOU 2184  C   ALA D  28    27342  19735  10757  -1244  -4977  -3342       C  
ATOM   2185  O   ALA D  28      76.887  41.792  33.464  1.00150.78           O  
ANISOU 2185  O   ALA D  28    27270  19063  10957  -1390  -5040  -3220       O  
ATOM   2186  CB  ALA D  28      78.861  41.109  35.963  1.00155.73           C  
ANISOU 2186  CB  ALA D  28    27552  20755  10865  -2032  -5414  -3139       C  
ATOM   2187  N   ALA D  29      75.894  40.439  34.984  1.00144.32           N  
ANISOU 2187  N   ALA D  29    23168  20272  11394   -731  -3151  -2186       N  
ATOM   2188  CA  ALA D  29      74.966  39.814  34.049  1.00139.78           C  
ANISOU 2188  CA  ALA D  29    22317  19706  11088   -409  -2786  -1976       C  
ATOM   2189  C   ALA D  29      73.936  40.820  33.539  1.00141.70           C  
ANISOU 2189  C   ALA D  29    22981  19445  11413    -15  -2800  -2355       C  
ATOM   2190  O   ALA D  29      73.778  40.987  32.329  1.00140.38           O  
ANISOU 2190  O   ALA D  29    22957  18762  11618   -150  -2900  -2252       O  
ATOM   2191  CB  ALA D  29      74.279  38.618  34.697  1.00138.02           C  
ANISOU 2191  CB  ALA D  29    21678  20145  10619   -126  -2427  -1817       C  
ATOM   2192  N   GLY D  30      73.253  41.496  34.461  1.00151.87           N  
ANISOU 2192  N   GLY D  30    24493  20289  12923   1102  -1468  -1829       N  
ATOM   2193  CA  GLY D  30      72.281  42.531  34.103  1.00154.45           C  
ANISOU 2193  CA  GLY D  30    25224  20158  13302   1578  -1499  -2224       C  
ATOM   2194  C   GLY D  30      72.849  43.600  33.182  1.00155.77           C  
ANISOU 2194  C   GLY D  30    25886  19483  13816   1320  -1865  -2280       C  
ATOM   2195  O   GLY D  30      72.130  44.158  32.351  1.00155.45           O  
ANISOU 2195  O   GLY D  30    26015  19035  14015   1617  -1835  -2339       O  
ATOM   2196  N   ALA D  31      74.144  43.877  33.335  1.00146.90           N  
ANISOU 2196  N   ALA D  31    25635  18825  11356   -230  -4051  -4081       N  
ATOM   2197  CA  ALA D  31      74.845  44.865  32.516  1.00149.38           C  
ANISOU 2197  CA  ALA D  31    26460  18358  11938   -595  -4452  -4117       C  
ATOM   2198  C   ALA D  31      75.227  44.300  31.152  1.00144.45           C  
ANISOU 2198  C   ALA D  31    25511  17599  11774  -1007  -4380  -3565       C  
ATOM   2199  O   ALA D  31      75.293  45.038  30.166  1.00145.93           O  
ANISOU 2199  O   ALA D  31    26075  17154  12219  -1217  -4622  -3529       O  
ATOM   2200  CB  ALA D  31      76.077  45.376  33.243  1.00154.29           C  
ANISOU 2200  CB  ALA D  31    27442  18832  12349  -1091  -4887  -4303       C  
ATOM   2201  N   ALA D  32      75.482  42.994  31.102  1.00132.43           N  
ANISOU 2201  N   ALA D  32    22162  16729  11428  -2110  -4676  -3489       N  
ATOM   2202  CA  ALA D  32      75.795  42.315  29.845  1.00127.77           C  
ANISOU 2202  CA  ALA D  32    21239  16063  11243  -2362  -4548  -3010       C  
ATOM   2203  C   ALA D  32      74.596  42.284  28.900  1.00125.61           C  
ANISOU 2203  C   ALA D  32    20973  15616  11138  -1849  -4304  -3044       C  
ATOM   2204  O   ALA D  32      74.770  42.332  27.685  1.00125.16           O  
ANISOU 2204  O   ALA D  32    21092  15096  11366  -1944  -4389  -2915       O  
ATOM   2205  CB  ALA D  32      76.304  40.906  30.106  1.00123.26           C  
ANISOU 2205  CB  ALA D  32    20006  16115  10714  -2570  -4313  -2577       C  
ATOM   2206  N   THR D  33      73.389  42.203  29.459  1.00125.81           N  
ANISOU 2206  N   THR D  33    20357  15549  11896  -1060  -3725  -3517       N  
ATOM   2207  CA  THR D  33      72.163  42.215  28.657  1.00124.36           C  
ANISOU 2207  CA  THR D  33    20155  15236  11862   -578  -3520  -3558       C  
ATOM   2208  C   THR D  33      71.882  43.607  28.087  1.00128.41           C  
ANISOU 2208  C   THR D  33    21317  14972  12500   -461  -3837  -3829       C  
ATOM   2209  O   THR D  33      71.300  43.737  27.003  1.00126.75           O  
ANISOU 2209  O   THR D  33    21120  14482  12557   -303  -3778  -3690       O  
ATOM   2210  CB  THR D  33      70.949  41.782  29.482  1.00124.39           C  
ANISOU 2210  CB  THR D  33    19891  15791  11579    -32  -3200  -3746       C  
ATOM   2211  OG1 THR D  33      70.761  42.691  30.574  1.00130.19           O  
ANISOU 2211  OG1 THR D  33    21069  16427  11971    337  -3355  -4289       O  
ATOM   2212  CG2 THR D  33      71.155  40.382  30.038  1.00121.62           C  
ANISOU 2212  CG2 THR D  33    19035  16097  11077   -264  -2992  -3459       C  
ATOM   2213  N   VAL D  34      72.304  44.637  28.820  1.00132.28           N  
ANISOU 2213  N   VAL D  34    23092  15276  11891   -603  -4298  -4336       N  
ATOM   2214  CA  VAL D  34      72.267  46.010  28.319  1.00136.59           C  
ANISOU 2214  CA  VAL D  34    24327  14983  12589   -651  -4685  -4512       C  
ATOM   2215  C   VAL D  34      73.295  46.163  27.200  1.00134.87           C  
ANISOU 2215  C   VAL D  34    24101  14436  12708  -1350  -4860  -4048       C  
ATOM   2216  O   VAL D  34      73.090  46.936  26.262  1.00136.23           O  
ANISOU 2216  O   VAL D  34    24638  14018  13107  -1360  -5032  -3981       O  
ATOM   2217  CB  VAL D  34      72.547  47.051  29.423  1.00143.58           C  
ANISOU 2217  CB  VAL D  34    25883  15470  13202   -640  -5087  -5013       C  
ATOM   2218  CG1 VAL D  34      72.466  48.468  28.857  1.00148.27           C  
ANISOU 2218  CG1 VAL D  34    27238  15105  13992   -672  -5506  -5149       C  
ATOM   2219  CG2 VAL D  34      71.571  46.888  30.584  1.00146.11           C  
ANISOU 2219  CG2 VAL D  34    26212  16179  13126     86  -4909  -5510       C  
ATOM   2220  N   LEU D  35      74.393  45.417  27.299  1.00131.86           N  
ANISOU 2220  N   LEU D  35    23087  14574  12441  -1873  -5055  -3783       N  
ATOM   2221  CA  LEU D  35      75.410  45.414  26.254  1.00128.98           C  
ANISOU 2221  CA  LEU D  35    22469  14154  12385  -2420  -5058  -3270       C  
ATOM   2222  C   LEU D  35      74.970  44.633  24.999  1.00123.54           C  
ANISOU 2222  C   LEU D  35    21364  13628  11949  -2146  -4695  -2956       C  
ATOM   2223  O   LEU D  35      75.336  44.999  23.877  1.00123.77           O  
ANISOU 2223  O   LEU D  35    21592  13230  12205  -2267  -4791  -2773       O  
ATOM   2224  CB  LEU D  35      76.732  44.877  26.801  1.00128.04           C  
ANISOU 2224  CB  LEU D  35    21946  14493  12210  -3022  -5098  -2998       C  
ATOM   2225  CG  LEU D  35      78.014  45.450  26.191  1.00132.29           C  
ANISOU 2225  CG  LEU D  35    22851  14571  12844  -3722  -5520  -2870       C  
ATOM   2226  CD1 LEU D  35      79.072  45.596  27.272  1.00134.57           C  
ANISOU 2226  CD1 LEU D  35    22995  15207  12927  -4202  -5715  -2875       C  
ATOM   2227  CD2 LEU D  35      78.534  44.604  25.033  1.00129.33           C  
ANISOU 2227  CD2 LEU D  35    22157  14218  12766  -4080  -5411  -2359       C  
ATOM   2228  N   LEU D  36      74.183  43.571  25.189  1.00120.02           N  
ANISOU 2228  N   LEU D  36    19619  13963  12019  -1445  -4122  -3589       N  
ATOM   2229  CA  LEU D  36      73.700  42.754  24.072  1.00115.30           C  
ANISOU 2229  CA  LEU D  36    18640  13532  11635  -1222  -3810  -3316       C  
ATOM   2230  C   LEU D  36      72.746  43.528  23.163  1.00116.71           C  
ANISOU 2230  C   LEU D  36    19195  13186  11964   -899  -3887  -3414       C  
ATOM   2231  O   LEU D  36      72.826  43.414  21.938  1.00114.86           O  
ANISOU 2231  O   LEU D  36    18890  12789  11961  -1082  -3868  -3107       O  
ATOM   2232  CB  LEU D  36      72.992  41.501  24.592  1.00112.01           C  
ANISOU 2232  CB  LEU D  36    17749  13717  11093   -827  -3444  -3330       C  
ATOM   2233  CG  LEU D  36      72.644  40.438  23.548  1.00107.01           C  
ANISOU 2233  CG  LEU D  36    16669  13301  10690   -765  -3155  -2980       C  
ATOM   2234  CD1 LEU D  36      73.902  39.755  23.035  1.00105.23           C  
ANISOU 2234  CD1 LEU D  36    16299  12996  10688  -1280  -3225  -2593       C  
ATOM   2235  CD2 LEU D  36      71.678  39.414  24.126  1.00103.93           C  
ANISOU 2235  CD2 LEU D  36    15782  13525  10183   -580  -2839  -2887       C  
ATOM   2236  N   VAL D  37      71.854  44.313  23.767  1.00124.01           N  
ANISOU 2236  N   VAL D  37    20616  14132  12370    316  -4296  -4356       N  
ATOM   2237  CA  VAL D  37      70.952  45.191  23.016  1.00126.49           C  
ANISOU 2237  CA  VAL D  37    21364  13888  12810    675  -4441  -4483       C  
ATOM   2238  C   VAL D  37      71.739  46.184  22.151  1.00129.38           C  
ANISOU 2238  C   VAL D  37    22235  13558  13364    183  -4819  -4301       C  
ATOM   2239  O   VAL D  37      71.394  46.404  20.990  1.00128.48           O  
ANISOU 2239  O   VAL D  37    22174  13188  13454    214  -4823  -4073       O  
ATOM   2240  CB  VAL D  37      70.031  45.991  23.956  1.00131.07           C  
ANISOU 2240  CB  VAL D  37    22309  14342  13151   1345  -4514  -5028       C  
ATOM   2241  CG1 VAL D  37      69.193  46.982  23.164  1.00136.16           C  
ANISOU 2241  CG1 VAL D  37    23669  14171  13896   1602  -4871  -5227       C  
ATOM   2242  CG2 VAL D  37      69.143  45.052  24.758  1.00128.14           C  
ANISOU 2242  CG2 VAL D  37    21399  14604  12686   1901  -4102  -5079       C  
ATOM   2243  N   ILE D  38      72.802  46.759  22.717  1.00135.69           N  
ANISOU 2243  N   ILE D  38    24268  13414  13874   -717  -5211  -4079       N  
ATOM   2244  CA  ILE D  38      73.716  47.636  21.975  1.00138.66           C  
ANISOU 2244  CA  ILE D  38    25056  13214  14414  -1347  -5569  -3818       C  
ATOM   2245  C   ILE D  38      74.264  46.947  20.719  1.00134.04           C  
ANISOU 2245  C   ILE D  38    23970  12914  14046  -1741  -5358  -3262       C  
ATOM   2246  O   ILE D  38      74.176  47.497  19.622  1.00134.87           O  
ANISOU 2246  O   ILE D  38    24309  12618  14319  -1805  -5459  -3046       O  
ATOM   2247  CB  ILE D  38      74.912  48.069  22.843  1.00142.45           C  
ANISOU 2247  CB  ILE D  38    25763  13597  14765  -2002  -5895  -3864       C  
ATOM   2248  CG1 ILE D  38      74.494  49.178  23.811  1.00148.42           C  
ANISOU 2248  CG1 ILE D  38    27160  13953  15280  -1703  -6205  -4446       C  
ATOM   2249  CG2 ILE D  38      76.070  48.523  21.968  1.00144.90           C  
ANISOU 2249  CG2 ILE D  38    26302  13508  15245  -2790  -6193  -3459       C  
ATOM   2250  CD1 ILE D  38      75.536  49.496  24.862  1.00152.46           C  
ANISOU 2250  CD1 ILE D  38    28313  13820  15793  -1009  -6371  -4827       C  
ATOM   2251  N   VAL D  39      74.808  45.742  20.889  1.00129.08           N  
ANISOU 2251  N   VAL D  39    21679  13227  14138  -2725  -4380  -3310       N  
ATOM   2252  CA  VAL D  39      75.398  44.977  19.784  1.00125.03           C  
ANISOU 2252  CA  VAL D  39    20656  13063  13788  -3059  -4166  -2827       C  
ATOM   2253  C   VAL D  39      74.368  44.628  18.697  1.00121.85           C  
ANISOU 2253  C   VAL D  39    20116  12644  13538  -2626  -3931  -2701       C  
ATOM   2254  O   VAL D  39      74.684  44.674  17.504  1.00121.53           O  
ANISOU 2254  O   VAL D  39    20059  12482  13633  -2907  -3951  -2363       O  
ATOM   2255  CB  VAL D  39      76.152  43.712  20.299  1.00121.39           C  
ANISOU 2255  CB  VAL D  39    19528  13344  13252  -3253  -3921  -2674       C  
ATOM   2256  CG1 VAL D  39      76.511  42.766  19.158  1.00115.94           C  
ANISOU 2256  CG1 VAL D  39    18243  13116  12693  -3132  -3549  -2355       C  
ATOM   2257  CG2 VAL D  39      77.412  44.117  21.049  1.00124.40           C  
ANISOU 2257  CG2 VAL D  39    19902  13785  13581  -3978  -4174  -2499       C  
ATOM   2258  N   LEU D  40      73.144  44.293  19.105  1.00120.26           N  
ANISOU 2258  N   LEU D  40    19556  12884  13252  -1503  -3757  -3211       N  
ATOM   2259  CA  LEU D  40      72.072  43.997  18.151  1.00118.03           C  
ANISOU 2259  CA  LEU D  40    19169  12586  13091  -1071  -3580  -3140       C  
ATOM   2260  C   LEU D  40      71.767  45.194  17.258  1.00122.01           C  
ANISOU 2260  C   LEU D  40    20262  12398  13697  -1090  -3889  -3100       C  
ATOM   2261  O   LEU D  40      71.874  45.096  16.042  1.00121.22           O  
ANISOU 2261  O   LEU D  40    20114  12220  13723  -1403  -3899  -2741       O  
ATOM   2262  CB  LEU D  40      70.798  43.522  18.859  1.00117.22           C  
ANISOU 2262  CB  LEU D  40    18934  12726  12877   -388  -3383  -3476       C  
ATOM   2263  CG  LEU D  40      70.814  42.199  19.628  1.00113.64           C  
ANISOU 2263  CG  LEU D  40    17925  12947  12306   -335  -3075  -3486       C  
ATOM   2264  CD1 LEU D  40      69.392  41.756  19.914  1.00112.86           C  
ANISOU 2264  CD1 LEU D  40    17630  13130  12122    289  -2849  -3703       C  
ATOM   2265  CD2 LEU D  40      71.571  41.111  18.891  1.00109.21           C  
ANISOU 2265  CD2 LEU D  40    16863  12772  11860   -712  -2875  -3089       C  
ATOM   2266  N   LEU D  41      71.405  46.322  17.865  1.00136.91           N  
ANISOU 2266  N   LEU D  41    24303  12520  15197   -232  -4711  -3565       N  
ATOM   2267  CA  LEU D  41      71.082  47.541  17.119  1.00141.60           C  
ANISOU 2267  CA  LEU D  41    25559  12359  15884   -197  -5065  -3545       C  
ATOM   2268  C   LEU D  41      72.241  48.013  16.233  1.00143.08           C  
ANISOU 2268  C   LEU D  41    25929  12255  16181   -987  -5281  -3092       C  
ATOM   2269  O   LEU D  41      72.030  48.379  15.073  1.00143.71           O  
ANISOU 2269  O   LEU D  41    26169  12056  16377  -1008  -5353  -2823       O  
ATOM   2270  CB  LEU D  41      70.698  48.670  18.078  1.00147.78           C  
ANISOU 2270  CB  LEU D  41    27036  12572  16540    181  -5404  -4041       C  
ATOM   2271  CG  LEU D  41      69.488  48.413  18.979  1.00147.60           C  
ANISOU 2271  CG  LEU D  41    26851  12883  16348    993  -5201  -4520       C  
ATOM   2272  CD1 LEU D  41      69.222  49.612  19.876  1.00154.50           C  
ANISOU 2272  CD1 LEU D  41    28477  13108  17118   1493  -5560  -4989       C  
ATOM   2273  CD2 LEU D  41      68.259  48.084  18.147  1.00143.30           C  
ANISOU 2273  CD2 LEU D  41    25755  12831  15863   1502  -4832  -4427       C  
ATOM   2274  N   ALA D  42      73.456  47.991  16.783  1.00149.04           N  
ANISOU 2274  N   ALA D  42    27272  12579  16778  -3935  -4843  -2931       N  
ATOM   2275  CA  ALA D  42      74.660  48.379  16.046  1.00150.95           C  
ANISOU 2275  CA  ALA D  42    27586  12686  17082  -4754  -5025  -2480       C  
ATOM   2276  C   ALA D  42      74.979  47.390  14.933  1.00146.03           C  
ANISOU 2276  C   ALA D  42    26318  12632  16535  -4926  -4679  -2046       C  
ATOM   2277  O   ALA D  42      75.393  47.787  13.846  1.00147.55           O  
ANISOU 2277  O   ALA D  42    26647  12624  16792  -5259  -4775  -1683       O  
ATOM   2278  CB  ALA D  42      75.840  48.506  16.985  1.00152.95           C  
ANISOU 2278  CB  ALA D  42    27799  13085  17231  -5353  -5176  -2491       C  
ATOM   2279  N   GLY D  43      74.781  46.104  15.220  1.00131.26           N  
ANISOU 2279  N   GLY D  43    21830  12681  15360  -4620  -3697  -1896       N  
ATOM   2280  CA  GLY D  43      74.986  45.034  14.246  1.00126.33           C  
ANISOU 2280  CA  GLY D  43    20581  12625  14793  -4628  -3339  -1579       C  
ATOM   2281  C   GLY D  43      73.984  45.064  13.108  1.00125.31           C  
ANISOU 2281  C   GLY D  43    20550  12307  14754  -4239  -3268  -1489       C  
ATOM   2282  O   GLY D  43      74.366  44.936  11.946  1.00125.32           O  
ANISOU 2282  O   GLY D  43    20467  12361  14788  -4546  -3244  -1123       O  
ATOM   2283  N   SER D  44      72.706  45.235  13.448  1.00126.55           N  
ANISOU 2283  N   SER D  44    21220  11490  15372  -2352  -3605  -1741       N  
ATOM   2284  CA  SER D  44      71.631  45.370  12.462  1.00127.20           C  
ANISOU 2284  CA  SER D  44    21532  11272  15526  -1918  -3648  -1725       C  
ATOM   2285  C   SER D  44      71.911  46.509  11.493  1.00131.67           C  
ANISOU 2285  C   SER D  44    22623  11270  16134  -2303  -3974  -1430       C  
ATOM   2286  O   SER D  44      71.869  46.329  10.279  1.00130.64           O  
ANISOU 2286  O   SER D  44    22335  11272  16032  -2521  -3895  -1068       O  
ATOM   2287  CB  SER D  44      70.292  45.638  13.151  1.00129.37           C  
ANISOU 2287  CB  SER D  44    22133  11255  15766  -1240  -3752  -2175       C  
ATOM   2288  OG  SER D  44      69.934  44.583  14.017  1.00125.35           O  
ANISOU 2288  OG  SER D  44    21106  11308  15214   -794  -3416  -2377       O  
ATOM   2289  N   TYR D  45      72.207  47.677  12.045  1.00152.56           N  
ANISOU 2289  N   TYR D  45    28523  11160  18283  -2867  -4375  -1483       N  
ATOM   2290  CA  TYR D  45      72.393  48.873  11.247  1.00157.62           C  
ANISOU 2290  CA  TYR D  45    29760  11165  18962  -3204  -4735  -1206       C  
ATOM   2291  C   TYR D  45      73.735  48.886  10.513  1.00158.59           C  
ANISOU 2291  C   TYR D  45    29743  11460  19054  -4117  -4773   -730       C  
ATOM   2292  O   TYR D  45      73.905  49.630   9.549  1.00163.10           O  
ANISOU 2292  O   TYR D  45    30771  11567  19631  -4538  -5062   -406       O  
ATOM   2293  CB  TYR D  45      72.214  50.116  12.125  1.00163.91           C  
ANISOU 2293  CB  TYR D  45    31375  11153  19749  -3028  -5181  -1542       C  
ATOM   2294  CG  TYR D  45      70.766  50.417  12.503  1.00164.51           C  
ANISOU 2294  CG  TYR D  45    31652  11029  19827  -2054  -5188  -2008       C  
ATOM   2295  CD1 TYR D  45      69.841  49.379  12.752  1.00158.90           C  
ANISOU 2295  CD1 TYR D  45    30267  11014  19094  -1461  -4752  -2207       C  
ATOM   2296  CD2 TYR D  45      70.324  51.748  12.632  1.00171.47           C  
ANISOU 2296  CD2 TYR D  45    33412  11023  20715  -1722  -5653  -2258       C  
ATOM   2297  CE1 TYR D  45      68.516  49.654  13.099  1.00160.06           C  
ANISOU 2297  CE1 TYR D  45    30517  11090  19210   -593  -4743  -2615       C  
ATOM   2298  CE2 TYR D  45      69.000  52.040  12.984  1.00172.80           C  
ANISOU 2298  CE2 TYR D  45    33725  11075  20855   -761  -5659  -2711       C  
ATOM   2299  CZ  TYR D  45      68.103  50.989  13.216  1.00166.99           C  
ANISOU 2299  CZ  TYR D  45    32216  11155  20079   -211  -5182  -2879       C  
ATOM   2300  OH  TYR D  45      66.800  51.282  13.563  1.00168.91           O  
ANISOU 2300  OH  TYR D  45    32533  11382  20262    710  -5177  -3309       O  
ATOM   2301  N   LEU D  46      74.678  48.060  10.958  1.00153.75           N  
ANISOU 2301  N   LEU D  46    27476  12746  18196  -6775  -4066   -672       N  
ATOM   2302  CA  LEU D  46      75.958  47.933  10.266  1.00154.77           C  
ANISOU 2302  CA  LEU D  46    27349  13190  18268  -7574  -4052   -211       C  
ATOM   2303  C   LEU D  46      75.867  46.902   9.145  1.00150.59           C  
ANISOU 2303  C   LEU D  46    26274  13216  17727  -7462  -3696     69       C  
ATOM   2304  O   LEU D  46      76.472  47.077   8.087  1.00152.72           O  
ANISOU 2304  O   LEU D  46    26564  13521  17943  -7911  -3740    488       O  
ATOM   2305  CB  LEU D  46      77.066  47.561  11.253  1.00154.38           C  
ANISOU 2305  CB  LEU D  46    26921  13593  18142  -8027  -3999   -250       C  
ATOM   2306  CG  LEU D  46      78.503  47.777  10.773  1.00159.39           C  
ANISOU 2306  CG  LEU D  46    27632  14231  18697  -8988  -4238    151       C  
ATOM   2307  CD1 LEU D  46      78.814  49.261  10.660  1.00166.21           C  
ANISOU 2307  CD1 LEU D  46    29342  14240  19571  -9319  -4765     55       C  
ATOM   2308  CD2 LEU D  46      79.490  47.093  11.706  1.00157.96           C  
ANISOU 2308  CD2 LEU D  46    26783  14814  18421  -9410  -4062    233       C  
ATOM   2309  N   ALA D  47      75.098  45.839   9.384  1.00131.91           N  
ANISOU 2309  N   ALA D  47    21772  12120  16227  -5376  -3658    355       N  
ATOM   2310  CA  ALA D  47      74.904  44.755   8.412  1.00127.57           C  
ANISOU 2310  CA  ALA D  47    20690  12118  15664  -5179  -3308    528       C  
ATOM   2311  C   ALA D  47      74.154  45.201   7.159  1.00128.97           C  
ANISOU 2311  C   ALA D  47    21135  12021  15846  -5047  -3387    752       C  
ATOM   2312  O   ALA D  47      74.442  44.726   6.059  1.00128.99           O  
ANISOU 2312  O   ALA D  47    20908  12342  15762  -5363  -3274   1107       O  
ATOM   2313  CB  ALA D  47      74.192  43.573   9.062  1.00122.35           C  
ANISOU 2313  CB  ALA D  47    19619  11821  15048  -4566  -3013    193       C  
ATOM   2314  N   VAL D  48      73.190  46.104   7.334  1.00139.92           N  
ANISOU 2314  N   VAL D  48    24291  11178  17693  -3031  -3906   1045       N  
ATOM   2315  CA  VAL D  48      72.440  46.673   6.216  1.00142.91           C  
ANISOU 2315  CA  VAL D  48    25089  11135  18074  -2929  -4108   1261       C  
ATOM   2316  C   VAL D  48      73.388  47.360   5.237  1.00147.13           C  
ANISOU 2316  C   VAL D  48    25840  11547  18514  -3699  -4288   1745       C  
ATOM   2317  O   VAL D  48      73.441  46.969   4.076  1.00146.05           O  
ANISOU 2317  O   VAL D  48    25395  11817  18280  -3890  -4110   2065       O  
ATOM   2318  CB  VAL D  48      71.303  47.623   6.686  1.00146.39           C  
ANISOU 2318  CB  VAL D  48    26167  10858  18597  -2415  -4430    965       C  
ATOM   2319  CG1 VAL D  48      70.796  48.484   5.547  1.00150.66           C  
ANISOU 2319  CG1 VAL D  48    27227  10885  19132  -2401  -4718   1242       C  
ATOM   2320  CG2 VAL D  48      70.157  46.821   7.263  1.00142.54           C  
ANISOU 2320  CG2 VAL D  48    25362  10641  18156  -1645  -4206    566       C  
ATOM   2321  N   LEU D  49      74.160  48.341   5.708  1.00167.66           N  
ANISOU 2321  N   LEU D  49    31261  12058  20384  -6402  -3838   2046       N  
ATOM   2322  CA  LEU D  49      75.056  49.097   4.822  1.00172.58           C  
ANISOU 2322  CA  LEU D  49    32124  12549  20901  -7189  -4041   2565       C  
ATOM   2323  C   LEU D  49      76.162  48.235   4.203  1.00170.59           C  
ANISOU 2323  C   LEU D  49    31164  13157  20497  -7728  -3711   2902       C  
ATOM   2324  O   LEU D  49      76.753  48.610   3.190  1.00174.26           O  
ANISOU 2324  O   LEU D  49    31682  13705  20822  -8326  -3787   3373       O  
ATOM   2325  CB  LEU D  49      75.708  50.255   5.581  1.00179.09           C  
ANISOU 2325  CB  LEU D  49    33650  12645  21752  -7684  -4515   2579       C  
ATOM   2326  CG  LEU D  49      77.106  49.993   6.145  1.00181.63           C  
ANISOU 2326  CG  LEU D  49    33887  13104  22019  -8452  -4622   2651       C  
ATOM   2327  CD1 LEU D  49      77.898  49.083   5.219  1.00181.57           C  
ANISOU 2327  CD1 LEU D  49    33256  13887  21847  -9198  -4389   3130       C  
ATOM   2328  CD2 LEU D  49      77.847  51.301   6.373  1.00189.49           C  
ANISOU 2328  CD2 LEU D  49    35824  13121  23051  -8865  -5208   2694       C  
ATOM   2329  N   ALA D  50      76.427  47.086   4.815  1.00152.01           N  
ANISOU 2329  N   ALA D  50    25532  14434  17789  -8268  -3924   2856       N  
ATOM   2330  CA  ALA D  50      77.416  46.143   4.303  1.00150.24           C  
ANISOU 2330  CA  ALA D  50    24610  15059  17416  -8635  -3600   3109       C  
ATOM   2331  C   ALA D  50      76.865  45.304   3.151  1.00147.30           C  
ANISOU 2331  C   ALA D  50    23904  15106  16956  -8306  -3313   3239       C  
ATOM   2332  O   ALA D  50      77.606  44.937   2.237  1.00148.45           O  
ANISOU 2332  O   ALA D  50    23699  15793  16911  -8700  -3151   3586       O  
ATOM   2333  CB  ALA D  50      77.905  45.236   5.423  1.00146.27           C  
ANISOU 2333  CB  ALA D  50    23572  15053  16951  -8487  -3366   2804       C  
ATOM   2334  N   GLU D  51      75.562  45.023   3.204  1.00134.79           N  
ANISOU 2334  N   GLU D  51    21685  13234  16296  -5454  -4120   3576       N  
ATOM   2335  CA  GLU D  51      74.911  44.045   2.329  1.00130.95           C  
ANISOU 2335  CA  GLU D  51    20833  13160  15761  -5008  -3837   3551       C  
ATOM   2336  C   GLU D  51      74.027  44.653   1.244  1.00133.03           C  
ANISOU 2336  C   GLU D  51    21512  13037  15997  -4796  -4010   3712       C  
ATOM   2337  O   GLU D  51      73.849  44.055   0.188  1.00132.07           O  
ANISOU 2337  O   GLU D  51    21151  13290  15740  -4727  -3842   3881       O  
ATOM   2338  CB  GLU D  51      74.050  43.105   3.172  1.00125.81           C  
ANISOU 2338  CB  GLU D  51    19927  12618  15258  -4373  -3653   3093       C  
ATOM   2339  CG  GLU D  51      74.823  42.112   4.021  1.00122.78           C  
ANISOU 2339  CG  GLU D  51    19021  12755  14876  -4444  -3412   2940       C  
ATOM   2340  CD  GLU D  51      74.933  40.746   3.376  1.00118.69           C  
ANISOU 2340  CD  GLU D  51    17952  12846  14299  -4162  -3069   2889       C  
ATOM   2341  OE1 GLU D  51      73.887  40.153   3.009  1.00115.79           O  
ANISOU 2341  OE1 GLU D  51    17548  12445  14003  -3647  -2983   2685       O  
ATOM   2342  OE2 GLU D  51      76.071  40.253   3.258  1.00118.83           O  
ANISOU 2342  OE2 GLU D  51    17570  13390  14191  -4459  -2900   3042       O  
ATOM   2343  N   ARG D  52      73.481  45.836   1.518  1.00156.04           N  
ANISOU 2343  N   ARG D  52    25941  13640  19706  -2538  -4415   4769       N  
ATOM   2344  CA  ARG D  52      72.419  46.455   0.714  1.00158.63           C  
ANISOU 2344  CA  ARG D  52    26738  13502  20034  -2239  -4648   4884       C  
ATOM   2345  C   ARG D  52      72.664  46.501  -0.798  1.00160.69           C  
ANISOU 2345  C   ARG D  52    26960  14017  20079  -2552  -4617   5353       C  
ATOM   2346  O   ARG D  52      71.739  46.279  -1.586  1.00160.50           O  
ANISOU 2346  O   ARG D  52    27020  13942  20019  -2147  -4647   5388       O  
ATOM   2347  CB  ARG D  52      72.139  47.866   1.232  1.00164.16           C  
ANISOU 2347  CB  ARG D  52    28215  13329  20829  -2334  -5105   4891       C  
ATOM   2348  CG  ARG D  52      70.696  48.317   1.121  1.00166.70           C  
ANISOU 2348  CG  ARG D  52    29045  13092  21203  -1796  -5378   4863       C  
ATOM   2349  CD  ARG D  52      70.488  49.561   1.969  1.00167.55           C  
ANISOU 2349  CD  ARG D  52    29519  12656  21485  -1221  -5586   4391       C  
ATOM   2350  NE  ARG D  52      69.159  50.148   1.813  1.00170.95           N  
ANISOU 2350  NE  ARG D  52    30452  12546  21956   -653  -5885   4368       N  
ATOM   2351  CZ  ARG D  52      68.724  51.213   2.484  1.00175.58           C  
ANISOU 2351  CZ  ARG D  52    31702  12367  22642   -295  -6268   4140       C  
ATOM   2352  NH1 ARG D  52      69.505  51.821   3.371  1.00177.46           N  
ANISOU 2352  NH1 ARG D  52    32229  12251  22945   -474  -6416   3901       N  
ATOM   2353  NH2 ARG D  52      67.500  51.674   2.268  1.00178.83           N  
ANISOU 2353  NH2 ARG D  52    32510  12365  23073    277  -6529   4143       N  
ATOM   2354  N   GLY D  53      73.899  46.788  -1.200  1.00169.29           N  
ANISOU 2354  N   GLY D  53    28784  15898  19641  -3731  -4956   7195       N  
ATOM   2355  CA  GLY D  53      74.225  46.967  -2.619  1.00172.43           C  
ANISOU 2355  CA  GLY D  53    29194  16542  19779  -4091  -4948   7687       C  
ATOM   2356  C   GLY D  53      74.746  45.734  -3.337  1.00169.45           C  
ANISOU 2356  C   GLY D  53    28120  17089  19173  -4117  -4526   7770       C  
ATOM   2357  O   GLY D  53      75.267  45.833  -4.448  1.00172.70           O  
ANISOU 2357  O   GLY D  53    28491  17815  19311  -4516  -4493   8194       O  
ATOM   2358  N   ALA D  54      74.601  44.574  -2.707  1.00147.64           N  
ANISOU 2358  N   ALA D  54    23270  17097  15730  -4829  -4735   6606       N  
ATOM   2359  CA  ALA D  54      75.128  43.329  -3.245  1.00145.35           C  
ANISOU 2359  CA  ALA D  54    22353  17645  15229  -4837  -4358   6631       C  
ATOM   2360  C   ALA D  54      74.004  42.427  -3.754  1.00141.21           C  
ANISOU 2360  C   ALA D  54    21665  17249  14739  -4166  -4217   6342       C  
ATOM   2361  O   ALA D  54      72.837  42.656  -3.433  1.00140.39           O  
ANISOU 2361  O   ALA D  54    21889  16641  14813  -3740  -4405   6161       O  
ATOM   2362  CB  ALA D  54      75.951  42.610  -2.184  1.00143.08           C  
ANISOU 2362  CB  ALA D  54    21575  17801  14986  -4977  -4132   6445       C  
ATOM   2363  N   PRO D  55      74.348  41.425  -4.586  1.00139.68           N  
ANISOU 2363  N   PRO D  55    20378  19457  13237  -4859  -3905   5462       N  
ATOM   2364  CA  PRO D  55      73.445  40.345  -4.998  1.00135.37           C  
ANISOU 2364  CA  PRO D  55    19492  19248  12696  -4321  -3683   5129       C  
ATOM   2365  C   PRO D  55      73.075  39.348  -3.881  1.00130.45           C  
ANISOU 2365  C   PRO D  55    18707  18495  12363  -3859  -3609   4663       C  
ATOM   2366  O   PRO D  55      73.332  38.152  -4.017  1.00127.52           O  
ANISOU 2366  O   PRO D  55    17963  18526  11963  -3603  -3383   4435       O  
ATOM   2367  CB  PRO D  55      74.252  39.631  -6.097  1.00135.95           C  
ANISOU 2367  CB  PRO D  55    19071  20098  12485  -4533  -3379   5220       C  
ATOM   2368  CG  PRO D  55      75.299  40.610  -6.525  1.00141.50           C  
ANISOU 2368  CG  PRO D  55    19923  20926  12915  -5128  -3464   5726       C  
ATOM   2369  CD  PRO D  55      75.648  41.322  -5.273  1.00143.68           C  
ANISOU 2369  CD  PRO D  55    20691  20494  13406  -5420  -3792   5871       C  
ATOM   2370  N   GLY D  56      72.450  39.825  -2.804  1.00120.81           N  
ANISOU 2370  N   GLY D  56    17226  15937  12740  -3398  -3462   3571       N  
ATOM   2371  CA  GLY D  56      72.196  38.981  -1.633  1.00116.75           C  
ANISOU 2371  CA  GLY D  56    16502  15415  12443  -3062  -3358   3182       C  
ATOM   2372  C   GLY D  56      70.940  39.243  -0.825  1.00115.78           C  
ANISOU 2372  C   GLY D  56    16642  14800  12550  -2697  -3529   2935       C  
ATOM   2373  O   GLY D  56      70.321  40.304  -0.934  1.00118.69           O  
ANISOU 2373  O   GLY D  56    17453  14671  12974  -2712  -3795   3024       O  
ATOM   2374  N   ALA D  57      70.609  38.259   0.018  1.00110.57           N  
ANISOU 2374  N   ALA D  57    15088  14176  12747  -2270  -3336   1901       N  
ATOM   2375  CA  ALA D  57      69.363  38.189   0.822  1.00108.88           C  
ANISOU 2375  CA  ALA D  57    14927  13717  12724  -1858  -3396   1593       C  
ATOM   2376  C   ALA D  57      68.989  39.454   1.608  1.00111.22           C  
ANISOU 2376  C   ALA D  57    15623  13504  13133  -1822  -3629   1527       C  
ATOM   2377  O   ALA D  57      69.824  40.344   1.824  1.00113.31           O  
ANISOU 2377  O   ALA D  57    16084  13578  13389  -2183  -3727   1644       O  
ATOM   2378  CB  ALA D  57      69.375  36.943   1.746  1.00105.01           C  
ANISOU 2378  CB  ALA D  57    14030  13555  12313  -1711  -3166   1333       C  
ATOM   2379  N   GLN D  58      67.732  39.494   2.054  1.00116.07           N  
ANISOU 2379  N   GLN D  58    15561  14039  14500   -287  -3871   1766       N  
ATOM   2380  CA  GLN D  58      67.038  40.738   2.422  1.00119.56           C  
ANISOU 2380  CA  GLN D  58    16466  13961  15002    -66  -4154   1715       C  
ATOM   2381  C   GLN D  58      67.643  41.555   3.574  1.00121.83           C  
ANISOU 2381  C   GLN D  58    17088  13866  15337   -295  -4305   1670       C  
ATOM   2382  O   GLN D  58      66.943  42.367   4.190  1.00125.08           O  
ANISOU 2382  O   GLN D  58    17925  13801  15799    -51  -4557   1557       O  
ATOM   2383  CB  GLN D  58      65.543  40.466   2.678  1.00118.84           C  
ANISOU 2383  CB  GLN D  58    16253  13918  14983    517  -4153   1419       C  
ATOM   2384  CG  GLN D  58      64.625  41.609   2.257  1.00121.98           C  
ANISOU 2384  CG  GLN D  58    16917  14067  15364    880  -4387   1470       C  
ATOM   2385  CD  GLN D  58      63.282  41.593   2.963  1.00123.15           C  
ANISOU 2385  CD  GLN D  58    17059  14153  15578   1459  -4457   1146       C  
ATOM   2386  OE1 GLN D  58      62.227  41.598   2.323  1.00123.76           O  
ANISOU 2386  OE1 GLN D  58    16983  14400  15639   1861  -4495   1089       O  
ATOM   2387  NE2 GLN D  58      63.314  41.581   4.291  1.00123.92           N  
ANISOU 2387  NE2 GLN D  58    17305  14056  15724   1515  -4481    925       N  
ATOM   2388  N   LEU D  59      68.932  41.360   3.855  1.00113.20           N  
ANISOU 2388  N   LEU D  59    16883  11625  14502   -983  -3422   1613       N  
ATOM   2389  CA  LEU D  59      69.647  42.234   4.783  1.00115.68           C  
ANISOU 2389  CA  LEU D  59    17503  11607  14845  -1263  -3590   1576       C  
ATOM   2390  C   LEU D  59      69.853  43.583   4.096  1.00120.73           C  
ANISOU 2390  C   LEU D  59    18703  11722  15448  -1518  -3914   1846       C  
ATOM   2391  O   LEU D  59      70.970  44.087   3.969  1.00123.08           O  
ANISOU 2391  O   LEU D  59    19126  11960  15680  -2092  -4000   2113       O  
ATOM   2392  CB  LEU D  59      70.968  41.603   5.242  1.00113.81           C  
ANISOU 2392  CB  LEU D  59    16909  11766  14567  -1694  -3405   1636       C  
ATOM   2393  CG  LEU D  59      70.894  40.382   6.165  1.00109.55           C  
ANISOU 2393  CG  LEU D  59    15914  11641  14069  -1439  -3143   1375       C  
ATOM   2394  CD1 LEU D  59      72.270  40.061   6.715  1.00108.78           C  
ANISOU 2394  CD1 LEU D  59    15544  11858  13930  -1839  -3034   1441       C  
ATOM   2395  CD2 LEU D  59      69.910  40.597   7.303  1.00109.67           C  
ANISOU 2395  CD2 LEU D  59    16084  11430  14155  -1012  -3213   1031       C  
ATOM   2396  N   ILE D  60      68.736  44.150   3.656  1.00138.60           N  
ANISOU 2396  N   ILE D  60    22345  12749  17566    323  -4301   2722       N  
ATOM   2397  CA  ILE D  60      68.720  45.323   2.804  1.00143.21           C  
ANISOU 2397  CA  ILE D  60    23441  12867  18107    217  -4603   3014       C  
ATOM   2398  C   ILE D  60      67.770  46.377   3.375  1.00146.73           C  
ANISOU 2398  C   ILE D  60    24396  12713  18640    772  -4910   2763       C  
ATOM   2399  O   ILE D  60      67.756  47.526   2.926  1.00151.77           O  
ANISOU 2399  O   ILE D  60    25628  12767  19271    727  -5259   2949       O  
ATOM   2400  CB  ILE D  60      68.298  44.970   1.366  1.00142.02           C  
ANISOU 2400  CB  ILE D  60    23046  13069  17847    255  -4481   3279       C  
ATOM   2401  CG1 ILE D  60      66.815  44.595   1.322  1.00140.22           C  
ANISOU 2401  CG1 ILE D  60    22639  12970  17669    954  -4432   3027       C  
ATOM   2402  CG2 ILE D  60      69.158  43.842   0.820  1.00138.50           C  
ANISOU 2402  CG2 ILE D  60    22037  13297  17291   -160  -4138   3434       C  
ATOM   2403  CD1 ILE D  60      66.259  44.468  -0.079  1.00141.17           C  
ANISOU 2403  CD1 ILE D  60    22758  13204  17677   1062  -4482   3281       C  
ATOM   2404  N   THR D  61      66.978  45.970   4.365  1.00152.31           N  
ANISOU 2404  N   THR D  61    24596  13216  20058   2459  -4482   2031       N  
ATOM   2405  CA  THR D  61      66.208  46.903   5.187  1.00156.16           C  
ANISOU 2405  CA  THR D  61    25553  13178  20602   2930  -4749   1706       C  
ATOM   2406  C   THR D  61      66.554  46.708   6.664  1.00155.22           C  
ANISOU 2406  C   THR D  61    25372  13108  20497   2836  -4668   1395       C  
ATOM   2407  O   THR D  61      66.937  45.606   7.081  1.00150.58           O  
ANISOU 2407  O   THR D  61    24233  13085  19894   2649  -4342   1345       O  
ATOM   2408  CB  THR D  61      64.703  46.722   4.981  1.00156.23           C  
ANISOU 2408  CB  THR D  61    25416  13318  20627   3737  -4732   1436       C  
ATOM   2409  OG1 THR D  61      64.322  45.394   5.361  1.00151.50           O  
ANISOU 2409  OG1 THR D  61    24172  13390  20002   3783  -4412   1513       O  
ATOM   2410  CG2 THR D  61      64.335  46.940   3.521  1.00161.75           C  
ANISOU 2410  CG2 THR D  61    26699  13428  21331   4065  -5121   1549       C  
ATOM   2411  N   TYR D  62      66.427  47.780   7.447  1.00154.92           N  
ANISOU 2411  N   TYR D  62    26215  11260  21387   1376  -3789    339       N  
ATOM   2412  CA  TYR D  62      66.695  47.722   8.886  1.00154.87           C  
ANISOU 2412  CA  TYR D  62    26210  11275  21357   1395  -3752    -21       C  
ATOM   2413  C   TYR D  62      65.724  46.807   9.655  1.00151.38           C  
ANISOU 2413  C   TYR D  62    25221  11417  20881   1988  -3434   -387       C  
ATOM   2414  O   TYR D  62      66.182  45.907  10.363  1.00147.23           O  
ANISOU 2414  O   TYR D  62    24205  11410  20326   1764  -3141   -429       O  
ATOM   2415  CB  TYR D  62      66.731  49.123   9.513  1.00161.52           C  
ANISOU 2415  CB  TYR D  62    27871  11299  22201   1493  -4199   -221       C  
ATOM   2416  CG  TYR D  62      67.897  49.992   9.082  1.00165.57           C  
ANISOU 2416  CG  TYR D  62    28943  11232  22733    746  -4536    146       C  
ATOM   2417  CD1 TYR D  62      69.214  49.537   9.194  1.00163.82           C  
ANISOU 2417  CD1 TYR D  62    28496  11267  22483    -48  -4433    364       C  
ATOM   2418  CD2 TYR D  62      67.686  51.285   8.588  1.00171.92           C  
ANISOU 2418  CD2 TYR D  62    30527  11224  23572    829  -4989    279       C  
ATOM   2419  CE1 TYR D  62      70.291  50.342   8.805  1.00168.28           C  
ANISOU 2419  CE1 TYR D  62    29536  11362  23039   -810  -4751    729       C  
ATOM   2420  CE2 TYR D  62      68.756  52.101   8.200  1.00176.48           C  
ANISOU 2420  CE2 TYR D  62    31661  11242  24152     51  -5333    661       C  
ATOM   2421  CZ  TYR D  62      70.055  51.623   8.312  1.00174.63           C  
ANISOU 2421  CZ  TYR D  62    31130  11345  23876   -793  -5200    886       C  
ATOM   2422  OH  TYR D  62      71.115  52.421   7.933  1.00179.49           O  
ANISOU 2422  OH  TYR D  62    32216  11511  24471  -1622  -5524   1286       O  
ATOM   2423  N   PRO D  63      64.391  47.013   9.508  1.00152.23           N  
ANISOU 2423  N   PRO D  63    23859  12953  21029   3382  -4102  -1415       N  
ATOM   2424  CA  PRO D  63      63.418  46.200  10.263  1.00150.09           C  
ANISOU 2424  CA  PRO D  63    23073  13264  20690   3920  -3820  -1760       C  
ATOM   2425  C   PRO D  63      63.538  44.690  10.033  1.00143.89           C  
ANISOU 2425  C   PRO D  63    21529  13235  19907   3696  -3413  -1609       C  
ATOM   2426  O   PRO D  63      62.863  43.906  10.704  1.00142.33           O  
ANISOU 2426  O   PRO D  63    20880  13549  19650   4073  -3186  -1816       O  
ATOM   2427  CB  PRO D  63      62.066  46.709   9.754  1.00153.68           C  
ANISOU 2427  CB  PRO D  63    23661  13592  21139   4664  -3978  -1899       C  
ATOM   2428  CG  PRO D  63      62.341  48.075   9.262  1.00159.00           C  
ANISOU 2428  CG  PRO D  63    25117  13433  21863   4629  -4415  -1789       C  
ATOM   2429  CD  PRO D  63      63.701  47.999   8.653  1.00157.01           C  
ANISOU 2429  CD  PRO D  63    24965  13023  21669   3764  -4436  -1347       C  
ATOM   2430  N   ARG D  64      64.394  44.297   9.094  1.00125.83           N  
ANISOU 2430  N   ARG D  64    18842  12429  16537   1741  -3740   -995       N  
ATOM   2431  CA  ARG D  64      64.651  42.892   8.809  1.00120.56           C  
ANISOU 2431  CA  ARG D  64    17543  12390  15876   1543  -3401   -851       C  
ATOM   2432  C   ARG D  64      65.995  42.486   9.390  1.00118.50           C  
ANISOU 2432  C   ARG D  64    17200  12215  15608    963  -3307   -740       C  
ATOM   2433  O   ARG D  64      66.201  41.329   9.761  1.00114.79           O  
ANISOU 2433  O   ARG D  64    16275  12219  15122    834  -3044   -752       O  
ATOM   2434  CB  ARG D  64      64.619  42.635   7.301  1.00119.57           C  
ANISOU 2434  CB  ARG D  64    17320  12328  15782   1452  -3402   -535       C  
ATOM   2435  N   ALA D  65      66.907  43.449   9.461  1.00114.93           N  
ANISOU 2435  N   ALA D  65    18077  10872  14719   -164  -3129   -640       N  
ATOM   2436  CA  ALA D  65      68.212  43.224  10.064  1.00114.18           C  
ANISOU 2436  CA  ALA D  65    17940  10844  14601   -688  -3098   -576       C  
ATOM   2437  C   ALA D  65      68.111  43.051  11.588  1.00113.95           C  
ANISOU 2437  C   ALA D  65    17824  10967  14506   -494  -3026   -941       C  
ATOM   2438  O   ALA D  65      68.872  42.272  12.176  1.00111.15           O  
ANISOU 2438  O   ALA D  65    17115  10997  14119   -779  -2840   -906       O  
ATOM   2439  CB  ALA D  65      69.159  44.355   9.707  1.00118.42           C  
ANISOU 2439  CB  ALA D  65    19014  10835  15144  -1156  -3421   -365       C  
ATOM   2440  N   LEU D  66      67.172  43.773  12.214  1.00118.78           N  
ANISOU 2440  N   LEU D  66    18112  11710  15309   -136  -2840  -2448       N  
ATOM   2441  CA  LEU D  66      66.885  43.624  13.647  1.00118.88           C  
ANISOU 2441  CA  LEU D  66    18002  11964  15203    120  -2737  -2808       C  
ATOM   2442  C   LEU D  66      66.426  42.200  13.946  1.00114.07           C  
ANISOU 2442  C   LEU D  66    16721  12053  14569    190  -2363  -2770       C  
ATOM   2443  O   LEU D  66      66.889  41.575  14.905  1.00111.76           O  
ANISOU 2443  O   LEU D  66    16156  12082  14226    -95  -2211  -2745       O  
ATOM   2444  CB  LEU D  66      65.852  44.659  14.097  1.00123.30           C  
ANISOU 2444  CB  LEU D  66    18904  12266  15680    776  -2896  -3204       C  
ATOM   2445  CG  LEU D  66      66.240  46.128  13.912  1.00129.11           C  
ANISOU 2445  CG  LEU D  66    20407  12207  16443    854  -3322  -3292       C  
ATOM   2446  CD1 LEU D  66      65.127  47.042  14.399  1.00133.49           C  
ANISOU 2446  CD1 LEU D  66    21213  12614  16894   1644  -3436  -3732       C  
ATOM   2447  CD2 LEU D  66      67.541  46.435  14.637  1.00131.44           C  
ANISOU 2447  CD2 LEU D  66    21123  12101  16717    298  -3561  -3280       C  
ATOM   2448  N   TRP D  67      65.526  41.693  13.108  1.00108.56           N  
ANISOU 2448  N   TRP D  67    15797  12611  12840    217  -2139  -2495       N  
ATOM   2449  CA  TRP D  67      65.034  40.328  13.227  1.00104.63           C  
ANISOU 2449  CA  TRP D  67    14706  12721  12326    252  -1826  -2438       C  
ATOM   2450  C   TRP D  67      66.144  39.307  12.979  1.00100.80           C  
ANISOU 2450  C   TRP D  67    13950  12456  11892   -275  -1680  -2168       C  
ATOM   2451  O   TRP D  67      66.133  38.226  13.567  1.00 98.10           O  
ANISOU 2451  O   TRP D  67    13209  12546  11519   -320  -1459  -2151       O  
ATOM   2452  CB  TRP D  67      63.847  40.108  12.281  1.00104.34           C  
ANISOU 2452  CB  TRP D  67    14478  12826  12341    582  -1782  -2377       C  
ATOM   2453  CG  TRP D  67      63.477  38.672  12.048  1.00100.63           C  
ANISOU 2453  CG  TRP D  67    13469  12884  11882    489  -1520  -2251       C  
ATOM   2454  CD1 TRP D  67      63.584  37.988  10.874  1.00 97.97           C  
ANISOU 2454  CD1 TRP D  67    12948  12641  11635    253  -1456  -1988       C  
ATOM   2455  CD2 TRP D  67      62.947  37.744  13.005  1.00 99.59           C  
ANISOU 2455  CD2 TRP D  67    12941  13245  11653    593  -1304  -2371       C  
ATOM   2456  NE1 TRP D  67      63.150  36.693  11.032  1.00 95.43           N  
ANISOU 2456  NE1 TRP D  67    12179  12783  11298    212  -1241  -1956       N  
ATOM   2457  CE2 TRP D  67      62.755  36.515  12.332  1.00 96.37           C  
ANISOU 2457  CE2 TRP D  67    12155  13154  11306    389  -1143  -2161       C  
ATOM   2458  CE3 TRP D  67      62.615  37.830  14.362  1.00101.50           C  
ANISOU 2458  CE3 TRP D  67    13123  13708  11736    832  -1236  -2630       C  
ATOM   2459  CZ2 TRP D  67      62.240  35.377  12.972  1.00 95.14           C  
ANISOU 2459  CZ2 TRP D  67    11588  13480  11080    369   -939  -2171       C  
ATOM   2460  CZ3 TRP D  67      62.104  36.694  14.999  1.00100.19           C  
ANISOU 2460  CZ3 TRP D  67    12499  14095  11473    819  -1001  -2624       C  
ATOM   2461  CH2 TRP D  67      61.924  35.486  14.299  1.00 97.08           C  
ANISOU 2461  CH2 TRP D  67    11760  13961  11166    564   -867  -2379       C  
ATOM   2462  N   TRP D  68      67.100  39.656  12.117  1.00 95.42           N  
ANISOU 2462  N   TRP D  68    14181  11466  10610   -776  -1884  -1253       N  
ATOM   2463  CA  TRP D  68      68.220  38.763  11.817  1.00 92.44           C  
ANISOU 2463  CA  TRP D  68    13520  11338  10266  -1206  -1750   -996       C  
ATOM   2464  C   TRP D  68      69.156  38.666  12.995  1.00 92.44           C  
ANISOU 2464  C   TRP D  68    13486  11436  10201  -1456  -1744  -1058       C  
ATOM   2465  O   TRP D  68      69.672  37.590  13.288  1.00 89.75           O  
ANISOU 2465  O   TRP D  68    12783  11471   9847  -1566  -1560   -991       O  
ATOM   2466  CB  TRP D  68      69.011  39.225  10.591  1.00 93.34           C  
ANISOU 2466  CB  TRP D  68    13815  11224  10427  -1548  -1873   -719       C  
ATOM   2467  CG  TRP D  68      70.357  38.540  10.471  1.00 91.53           C  
ANISOU 2467  CG  TRP D  68    13313  11277  10186  -1998  -1761   -496       C  
ATOM   2468  CD1 TRP D  68      70.588  37.233  10.145  1.00 88.30           C  
ANISOU 2468  CD1 TRP D  68    12482  11283   9785  -2020  -1536   -392       C  
ATOM   2469  CD2 TRP D  68      71.644  39.127  10.694  1.00 93.51           C  
ANISOU 2469  CD2 TRP D  68    13698  11429  10404  -2458  -1892   -362       C  
ATOM   2470  NE1 TRP D  68      71.936  36.973  10.143  1.00 88.22           N  
ANISOU 2470  NE1 TRP D  68    12319  11460   9741  -2398  -1506   -219       N  
ATOM   2471  CE2 TRP D  68      72.608  38.118  10.473  1.00 91.35           C  
ANISOU 2471  CE2 TRP D  68    13015  11587  10108  -2699  -1714   -179       C  
ATOM   2472  CE3 TRP D  68      72.077  40.412  11.047  1.00 97.44           C  
ANISOU 2472  CE3 TRP D  68    14635  11509  10879  -2701  -2166   -376       C  
ATOM   2473  CZ2 TRP D  68      73.977  38.349  10.596  1.00 92.93           C  
ANISOU 2473  CZ2 TRP D  68    13152  11904  10254  -3161  -1775     -5       C  
ATOM   2474  CZ3 TRP D  68      73.438  40.645  11.164  1.00 99.02           C  
ANISOU 2474  CZ3 TRP D  68    14808  11779  11035  -3240  -2247   -181       C  
ATOM   2475  CH2 TRP D  68      74.373  39.616  10.941  1.00 96.73           C  
ANISOU 2475  CH2 TRP D  68    14024  12016  10712  -3463  -2039      8       C  
ATOM   2476  N   SER D  69      69.381  39.802  13.648  1.00 95.64           N  
ANISOU 2476  N   SER D  69    14274  11672  10391  -1487  -1687  -1544       N  
ATOM   2477  CA  SER D  69      70.217  39.871  14.843  1.00 96.39           C  
ANISOU 2477  CA  SER D  69    14376  11861  10388  -1682  -1722  -1668       C  
ATOM   2478  C   SER D  69      69.716  38.917  15.923  1.00 94.61           C  
ANISOU 2478  C   SER D  69    13838  12045  10066  -1401  -1514  -1846       C  
ATOM   2479  O   SER D  69      70.468  38.073  16.408  1.00 92.43           O  
ANISOU 2479  O   SER D  69    13246  12113   9760  -1596  -1380  -1738       O  
ATOM   2480  CB  SER D  69      70.264  41.302  15.369  1.00101.02           C  
ANISOU 2480  CB  SER D  69    15504  11967  10912  -1729  -2028  -1870       C  
ATOM   2481  OG  SER D  69      70.756  42.175  14.372  1.00103.82           O  
ANISOU 2481  OG  SER D  69    16276  11842  11329  -1512  -2220  -1905       O  
ATOM   2482  N   VAL D  70      68.438  39.040  16.268  1.00 96.32           N  
ANISOU 2482  N   VAL D  70    14176  12663   9757  -1033  -1509  -2252       N  
ATOM   2483  CA  VAL D  70      67.816  38.166  17.252  1.00 95.15           C  
ANISOU 2483  CA  VAL D  70    13703  12967   9484   -813  -1298  -2379       C  
ATOM   2484  C   VAL D  70      67.916  36.704  16.822  1.00 91.12           C  
ANISOU 2484  C   VAL D  70    12738  12841   9044   -996  -1077  -2114       C  
ATOM   2485  O   VAL D  70      68.280  35.843  17.612  1.00 89.91           O  
ANISOU 2485  O   VAL D  70    12394  12943   8826  -1191   -996  -2046       O  
ATOM   2486  CB  VAL D  70      66.346  38.551  17.505  1.00 96.99           C  
ANISOU 2486  CB  VAL D  70    13935  13277   9640   -285  -1249  -2618       C  
ATOM   2487  CG1 VAL D  70      65.757  37.693  18.619  1.00 96.51           C  
ANISOU 2487  CG1 VAL D  70    13516  13757   9396   -132  -1024  -2722       C  
ATOM   2488  CG2 VAL D  70      66.238  40.030  17.854  1.00101.57           C  
ANISOU 2488  CG2 VAL D  70    15034  13398  10161    -34  -1508  -2901       C  
ATOM   2489  N   GLU D  71      67.610  36.437  15.560  1.00 87.29           N  
ANISOU 2489  N   GLU D  71    12792  12186   8187   -964  -1085  -1363       N  
ATOM   2490  CA  GLU D  71      67.728  35.094  14.982  1.00 84.01           C  
ANISOU 2490  CA  GLU D  71    12024  12049   7848  -1122   -917  -1135       C  
ATOM   2491  C   GLU D  71      69.138  34.513  15.175  1.00 82.70           C  
ANISOU 2491  C   GLU D  71    11775  11944   7702  -1487   -920   -958       C  
ATOM   2492  O   GLU D  71      69.295  33.321  15.453  1.00 80.95           O  
ANISOU 2492  O   GLU D  71    11292  11999   7467  -1551   -796   -863       O  
ATOM   2493  CB  GLU D  71      67.357  35.140  13.489  1.00 83.11           C  
ANISOU 2493  CB  GLU D  71    11892  11828   7859  -1066   -922  -1007       C  
ATOM   2494  CG  GLU D  71      66.991  33.802  12.845  1.00 80.76           C  
ANISOU 2494  CG  GLU D  71    11257  11822   7605  -1033   -758   -895       C  
ATOM   2495  CD  GLU D  71      66.454  33.972  11.415  1.00 80.47           C  
ANISOU 2495  CD  GLU D  71    11248  11669   7658   -963   -800   -798       C  
ATOM   2496  OE1 GLU D  71      65.470  34.731  11.241  1.00 82.57           O  
ANISOU 2496  OE1 GLU D  71    11783  11660   7930   -823   -946   -857       O  
ATOM   2497  OE2 GLU D  71      67.009  33.353  10.464  1.00 78.62           O  
ANISOU 2497  OE2 GLU D  71    10815  11582   7474  -1044   -717   -671       O  
ATOM   2498  N   THR D  72      70.146  35.376  15.056  1.00 83.53           N  
ANISOU 2498  N   THR D  72    12157  11769   7810  -1450  -1224  -1025       N  
ATOM   2499  CA  THR D  72      71.547  34.966  15.053  1.00 82.98           C  
ANISOU 2499  CA  THR D  72    11959  11826   7744  -1791  -1237   -850       C  
ATOM   2500  C   THR D  72      72.175  34.927  16.445  1.00 83.87           C  
ANISOU 2500  C   THR D  72    12038  12091   7736  -1898  -1276   -933       C  
ATOM   2501  O   THR D  72      72.956  34.019  16.745  1.00 82.76           O  
ANISOU 2501  O   THR D  72    11645  12217   7582  -2035  -1216   -798       O  
ATOM   2502  CB  THR D  72      72.408  35.919  14.221  1.00 84.86           C  
ANISOU 2502  CB  THR D  72    12405  11819   8019  -2087  -1401   -726       C  
ATOM   2503  OG1 THR D  72      71.939  35.933  12.867  1.00 83.81           O  
ANISOU 2503  OG1 THR D  72    12220  11657   7967  -2051  -1338   -572       O  
ATOM   2504  CG2 THR D  72      73.862  35.471  14.234  1.00 85.61           C  
ANISOU 2504  CG2 THR D  72    12347  12114   8065  -2481  -1452   -579       C  
ATOM   2505  N   ALA D  73      71.840  35.918  17.276  1.00 87.93           N  
ANISOU 2505  N   ALA D  73    12811  12591   8006  -1891  -1348  -1358       N  
ATOM   2506  CA  ALA D  73      72.369  36.030  18.647  1.00 89.72           C  
ANISOU 2506  CA  ALA D  73    13106  12911   8074  -1996  -1439  -1490       C  
ATOM   2507  C   ALA D  73      71.851  34.918  19.556  1.00 88.51           C  
ANISOU 2507  C   ALA D  73    12696  13134   7798  -1830  -1275  -1522       C  
ATOM   2508  O   ALA D  73      72.538  34.481  20.484  1.00 89.56           O  
ANISOU 2508  O   ALA D  73    12798  13444   7785  -1944  -1326  -1558       O  
ATOM   2509  CB  ALA D  73      72.040  37.391  19.238  1.00 93.27           C  
ANISOU 2509  CB  ALA D  73    13988  13017   8432  -1882  -1631  -1776       C  
ATOM   2510  N   THR D  74      70.631  34.475  19.268  1.00 88.20           N  
ANISOU 2510  N   THR D  74    12851  13298   7363  -1856  -1319  -1201       N  
ATOM   2511  CA  THR D  74      70.023  33.326  19.913  1.00 87.37           C  
ANISOU 2511  CA  THR D  74    12513  13533   7152  -1743  -1162  -1175       C  
ATOM   2512  C   THR D  74      70.636  32.042  19.371  1.00 84.82           C  
ANISOU 2512  C   THR D  74    11934  13340   6954  -1868  -1077   -904       C  
ATOM   2513  O   THR D  74      70.549  30.979  19.991  1.00 84.22           O  
ANISOU 2513  O   THR D  74    11680  13504   6814  -1863   -987   -797       O  
ATOM   2514  CB  THR D  74      68.526  33.293  19.600  1.00 87.58           C  
ANISOU 2514  CB  THR D  74    12510  13601   7167  -1447  -1053  -1289       C  
ATOM   2515  OG1 THR D  74      67.957  34.580  19.871  1.00 90.39           O  
ANISOU 2515  OG1 THR D  74    13157  13749   7439  -1256  -1168  -1566       O  
ATOM   2516  CG2 THR D  74      67.822  32.256  20.444  1.00 87.67           C  
ANISOU 2516  CG2 THR D  74    12287  14002   7023  -1367   -895  -1262       C  
ATOM   2517  N   THR D  75      71.264  32.170  18.203  1.00 83.32           N  
ANISOU 2517  N   THR D  75    11949  12715   6993  -1577  -1403   -660       N  
ATOM   2518  CA  THR D  75      71.758  31.051  17.395  1.00 81.47           C  
ANISOU 2518  CA  THR D  75    11512  12571   6870  -1648  -1342   -450       C  
ATOM   2519  C   THR D  75      70.622  30.101  17.005  1.00 80.09           C  
ANISOU 2519  C   THR D  75    11214  12479   6738  -1486  -1211   -407       C  
ATOM   2520  O   THR D  75      70.822  28.885  16.930  1.00 79.29           O  
ANISOU 2520  O   THR D  75    10972  12499   6655  -1500  -1167   -269       O  
ATOM   2521  CB  THR D  75      72.930  30.265  18.057  1.00 81.86           C  
ANISOU 2521  CB  THR D  75    11427  12822   6855  -1789  -1390   -336       C  
ATOM   2522  OG1 THR D  75      72.406  29.168  18.813  1.00 81.11           O  
ANISOU 2522  OG1 THR D  75    11200  12888   6732  -1690  -1307   -244       O  
ATOM   2523  CG2 THR D  75      73.809  31.167  18.952  1.00 84.22           C  
ANISOU 2523  CG2 THR D  75    11859  13142   6998  -1940  -1536   -455       C  
ATOM   2524  N   VAL D  76      69.430  30.653  16.769  1.00 80.04           N  
ANISOU 2524  N   VAL D  76    11410  12237   6764  -1481  -1147   -350       N  
ATOM   2525  CA  VAL D  76      68.302  29.879  16.235  1.00 79.21           C  
ANISOU 2525  CA  VAL D  76    11170  12222   6703  -1368  -1046   -310       C  
ATOM   2526  C   VAL D  76      68.527  29.624  14.750  1.00 77.82           C  
ANISOU 2526  C   VAL D  76    10984  11904   6681  -1384  -1054   -218       C  
ATOM   2527  O   VAL D  76      68.379  28.482  14.284  1.00 76.85           O  
ANISOU 2527  O   VAL D  76    10748  11832   6621  -1394  -1008   -118       O  
ATOM   2528  CB  VAL D  76      66.964  30.609  16.452  1.00 80.56           C  
ANISOU 2528  CB  VAL D  76    11384  12410   6817  -1161  -1026   -484       C  
ATOM   2529  CG1 VAL D  76      65.828  29.850  15.784  1.00 80.04           C  
ANISOU 2529  CG1 VAL D  76    11151  12455   6804  -1089   -951   -430       C  
ATOM   2530  CG2 VAL D  76      66.691  30.792  17.937  1.00 82.50           C  
ANISOU 2530  CG2 VAL D  76    11624  12859   6863  -1081   -991   -620       C  
ATOM   2531  N   GLY D  77      68.899  30.694  14.034  1.00 76.46           N  
ANISOU 2531  N   GLY D  77    10743  11531   6776  -1074  -1102   -294       N  
ATOM   2532  CA  GLY D  77      69.298  30.652  12.617  1.00 75.78           C  
ANISOU 2532  CA  GLY D  77    10681  11330   6781  -1118  -1123   -199       C  
ATOM   2533  C   GLY D  77      68.311  29.935  11.719  1.00 74.81           C  
ANISOU 2533  C   GLY D  77    10457  11249   6717  -1011  -1066   -171       C  
ATOM   2534  O   GLY D  77      68.564  28.795  11.304  1.00 73.89           O  
ANISOU 2534  O   GLY D  77    10225  11217   6631  -1046  -1022    -92       O  
ATOM   2535  N   TYR D  78      67.186  30.603  11.439  1.00 74.88           N  
ANISOU 2535  N   TYR D  78    10565  11071   6814   -942  -1044   -181       N  
ATOM   2536  CA  TYR D  78      66.093  30.023  10.651  1.00 74.65           C  
ANISOU 2536  CA  TYR D  78    10405  11147   6812   -820  -1011   -192       C  
ATOM   2537  C   TYR D  78      66.541  29.725   9.235  1.00 73.97           C  
ANISOU 2537  C   TYR D  78    10305  11029   6772   -848  -1028   -115       C  
ATOM   2538  O   TYR D  78      66.328  28.623   8.745  1.00 73.10           O  
ANISOU 2538  O   TYR D  78    10145  10946   6682   -937  -1002    -46       O  
ATOM   2539  CB  TYR D  78      64.862  30.932  10.616  1.00 76.21           C  
ANISOU 2539  CB  TYR D  78    10639  11334   6985   -598  -1059   -305       C  
ATOM   2540  CG  TYR D  78      64.024  30.896  11.863  1.00 77.44           C  
ANISOU 2540  CG  TYR D  78    10674  11696   7055   -474  -1001   -423       C  
ATOM   2541  CD1 TYR D  78      63.479  29.694  12.334  1.00 77.20           C  
ANISOU 2541  CD1 TYR D  78    10404  11938   6989   -569   -906   -370       C  
ATOM   2542  CD2 TYR D  78      63.762  32.066  12.573  1.00 79.44           C  
ANISOU 2542  CD2 TYR D  78    11068  11882   7235   -265  -1050   -586       C  
ATOM   2543  CE1 TYR D  78      62.709  29.661  13.495  1.00 78.84           C  
ANISOU 2543  CE1 TYR D  78    10463  12427   7067   -484   -829   -453       C  
ATOM   2544  CE2 TYR D  78      62.991  32.047  13.729  1.00 81.09           C  
ANISOU 2544  CE2 TYR D  78    11144  12352   7314   -111   -977   -721       C  
ATOM   2545  CZ  TYR D  78      62.466  30.844  14.185  1.00 80.77           C  
ANISOU 2545  CZ  TYR D  78    10808  12666   7214   -232   -850   -642       C  
ATOM   2546  OH  TYR D  78      61.693  30.842  15.326  1.00 82.97           O  
ANISOU 2546  OH  TYR D  78    10912  13298   7316    -93   -754   -754       O  
ATOM   2547  N   GLY D  79      67.193  30.696   8.595  1.00 73.53           N  
ANISOU 2547  N   GLY D  79    10106  10905   6926   -669  -1009    -50       N  
ATOM   2548  CA  GLY D  79      67.624  30.556   7.203  1.00 73.52           C  
ANISOU 2548  CA  GLY D  79    10157  10868   6910   -737  -1032     64       C  
ATOM   2549  C   GLY D  79      66.918  31.496   6.249  1.00 74.75           C  
ANISOU 2549  C   GLY D  79    10454  10901   7047   -641  -1127     89       C  
ATOM   2550  O   GLY D  79      67.333  31.653   5.104  1.00 75.39           O  
ANISOU 2550  O   GLY D  79    10619  10951   7075   -722  -1159    204       O  
ATOM   2551  N   ASP D  80      65.853  32.123   6.733  1.00 75.68           N  
ANISOU 2551  N   ASP D  80    10223  10941   7590   -588  -1055     92       N  
ATOM   2552  CA  ASP D  80      65.130  33.131   5.972  1.00 77.50           C  
ANISOU 2552  CA  ASP D  80    10617  11022   7808   -414  -1182     88       C  
ATOM   2553  C   ASP D  80      65.949  34.396   5.698  1.00 79.26           C  
ANISOU 2553  C   ASP D  80    11155  10949   8010   -508  -1307    183       C  
ATOM   2554  O   ASP D  80      65.580  35.197   4.845  1.00 81.21           O  
ANISOU 2554  O   ASP D  80    11598  11013   8246   -359  -1448    209       O  
ATOM   2555  CB  ASP D  80      63.797  33.473   6.659  1.00 78.49           C  
ANISOU 2555  CB  ASP D  80    10645  11239   7940   -146  -1190    -81       C  
ATOM   2556  CG  ASP D  80      63.974  34.216   7.983  1.00 80.20           C  
ANISOU 2556  CG  ASP D  80    11062  11270   8140    -29  -1252   -204       C  
ATOM   2557  OD1 ASP D  80      64.972  33.970   8.696  1.00 79.74           O  
ANISOU 2557  OD1 ASP D  80    11090  11133   8076   -217  -1225   -206       O  
ATOM   2558  OD2 ASP D  80      63.100  35.048   8.319  1.00 82.48           O  
ANISOU 2558  OD2 ASP D  80    11431  11501   8408    288  -1348   -319       O  
ATOM   2559  N   LEU D  81      67.049  34.575   6.426  1.00 79.90           N  
ANISOU 2559  N   LEU D  81    11122  10802   8434   -697  -1155    111       N  
ATOM   2560  CA  LEU D  81      67.928  35.736   6.276  1.00 82.08           C  
ANISOU 2560  CA  LEU D  81    11693  10809   8683   -903  -1292    231       C  
ATOM   2561  C   LEU D  81      69.344  35.395   6.723  1.00 81.54           C  
ANISOU 2561  C   LEU D  81    11528  10864   8590  -1225  -1222    308       C  
ATOM   2562  O   LEU D  81      69.527  34.643   7.695  1.00 79.93           O  
ANISOU 2562  O   LEU D  81    11123  10839   8407  -1206  -1115    200       O  
ATOM   2563  CB  LEU D  81      67.415  36.904   7.118  1.00 84.33           C  
ANISOU 2563  CB  LEU D  81    12269  10779   8994   -744  -1451     87       C  
ATOM   2564  CG  LEU D  81      66.188  37.672   6.637  1.00 86.26           C  
ANISOU 2564  CG  LEU D  81    12687  10836   9250   -381  -1586      9       C  
ATOM   2565  CD1 LEU D  81      65.277  37.954   7.803  1.00 86.87           C  
ANISOU 2565  CD1 LEU D  81    12745  10930   9332    -89  -1577   -263       C  
ATOM   2566  CD2 LEU D  81      66.576  38.953   5.921  1.00 89.61           C  
ANISOU 2566  CD2 LEU D  81    13552  10836   9661   -452  -1828    154       C  
ATOM   2567  N   TYR D  82      70.330  35.953   6.013  1.00 82.87           N  
ANISOU 2567  N   TYR D  82    11834  10834   8819  -1289  -1192    408       N  
ATOM   2568  CA  TYR D  82      71.758  35.833   6.357  1.00 83.49           C  
ANISOU 2568  CA  TYR D  82    11815  11059   8849  -1646  -1166    519       C  
ATOM   2569  C   TYR D  82      72.653  36.707   5.459  1.00 86.32           C  
ANISOU 2569  C   TYR D  82    12297  11393   9106  -2027  -1253    796       C  
ATOM   2570  O   TYR D  82      72.213  37.169   4.404  1.00 87.61           O  
ANISOU 2570  O   TYR D  82    12627  11435   9224  -2017  -1318    930       O  
ATOM   2571  CB  TYR D  82      72.220  34.369   6.308  1.00 81.14           C  
ANISOU 2571  CB  TYR D  82    11127  11171   8533  -1608   -966    494       C  
ATOM   2572  CG  TYR D  82      71.986  33.701   4.981  1.00 80.34           C  
ANISOU 2572  CG  TYR D  82    10884  11267   8376  -1498   -860    559       C  
ATOM   2573  CD1 TYR D  82      70.815  32.979   4.744  1.00 78.69           C  
ANISOU 2573  CD1 TYR D  82    10650  11030   8220  -1192   -826    425       C  
ATOM   2574  CD2 TYR D  82      72.932  33.791   3.955  1.00 81.80           C  
ANISOU 2574  CD2 TYR D  82    10957  11700   8422  -1713   -804    756       C  
ATOM   2575  CE1 TYR D  82      70.588  32.364   3.527  1.00 78.33           C  
ANISOU 2575  CE1 TYR D  82    10511  11143   8106  -1098   -763    458       C  
ATOM   2576  CE2 TYR D  82      72.714  33.183   2.729  1.00 81.49           C  
ANISOU 2576  CE2 TYR D  82    10817  11857   8290  -1583   -713    785       C  
ATOM   2577  CZ  TYR D  82      71.536  32.468   2.524  1.00 79.65           C  
ANISOU 2577  CZ  TYR D  82    10603  11535   8126  -1269   -705    621       C  
ATOM   2578  OH  TYR D  82      71.307  31.847   1.315  1.00 79.61           O  
ANISOU 2578  OH  TYR D  82    10520  11711   8016  -1142   -644    616       O  
ATOM   2579  N   PRO D  83      73.911  36.945   5.873  1.00 88.34           N  
ANISOU 2579  N   PRO D  83    12288  11663   9613  -2212  -1226   1183       N  
ATOM   2580  CA  PRO D  83      74.782  37.730   5.018  1.00 91.52           C  
ANISOU 2580  CA  PRO D  83    12776  12099   9897  -2623  -1303   1478       C  
ATOM   2581  C   PRO D  83      75.454  36.921   3.910  1.00 91.26           C  
ANISOU 2581  C   PRO D  83    12357  12606   9713  -2697  -1094   1641       C  
ATOM   2582  O   PRO D  83      75.677  35.717   4.064  1.00 88.87           O  
ANISOU 2582  O   PRO D  83    11704  12652   9409  -2472   -906   1509       O  
ATOM   2583  CB  PRO D  83      75.827  38.263   5.993  1.00 93.76           C  
ANISOU 2583  CB  PRO D  83    13108  12341  10176  -3016  -1432   1520       C  
ATOM   2584  CG  PRO D  83      75.931  37.217   7.020  1.00 91.05           C  
ANISOU 2584  CG  PRO D  83    12413  12313   9868  -2830  -1278   1331       C  
ATOM   2585  CD  PRO D  83      74.593  36.547   7.118  1.00 87.79           C  
ANISOU 2585  CD  PRO D  83    12029  11766   9560  -2315  -1195   1086       C  
ATOM   2586  N   VAL D  84      75.762  37.592   2.799  1.00 95.82           N  
ANISOU 2586  N   VAL D  84    13396  13314   9697  -2504  -1085   2492       N  
ATOM   2587  CA  VAL D  84      76.502  36.986   1.689  1.00 96.79           C  
ANISOU 2587  CA  VAL D  84    13178  13993   9606  -2614   -894   2676       C  
ATOM   2588  C   VAL D  84      77.769  37.789   1.370  1.00101.21           C  
ANISOU 2588  C   VAL D  84    13694  14762   9999  -3212   -959   3014       C  
ATOM   2589  O   VAL D  84      78.593  37.363   0.562  1.00102.83           O  
ANISOU 2589  O   VAL D  84    13538  15546   9987  -3359   -785   3177       O  
ATOM   2590  CB  VAL D  84      75.643  36.907   0.415  1.00 96.68           C  
ANISOU 2590  CB  VAL D  84    13278  13963   9492  -2400   -861   2736       C  
ATOM   2591  CG1 VAL D  84      76.468  36.390  -0.753  1.00 97.43           C  
ANISOU 2591  CG1 VAL D  84    12970  14708   9340  -2405   -625   2825       C  
ATOM   2592  CG2 VAL D  84      74.425  36.026   0.648  1.00 93.01           C  
ANISOU 2592  CG2 VAL D  84    12887  13256   9195  -1877   -850   2429       C  
ATOM   2593  N   THR D  85      77.916  38.947   2.015  1.00108.17           N  
ANISOU 2593  N   THR D  85    14148  15779  11174  -4148  -1329   3421       N  
ATOM   2594  CA  THR D  85      79.128  39.765   1.911  1.00112.95           C  
ANISOU 2594  CA  THR D  85    14725  16553  11637  -4824  -1438   3754       C  
ATOM   2595  C   THR D  85      80.144  39.328   2.968  1.00112.78           C  
ANISOU 2595  C   THR D  85    14291  16938  11623  -4972  -1366   3662       C  
ATOM   2596  O   THR D  85      79.768  38.859   4.042  1.00109.55           O  
ANISOU 2596  O   THR D  85    13843  16402  11378  -4625  -1349   3350       O  
ATOM   2597  CB  THR D  85      78.826  41.279   2.103  1.00116.56           C  
ANISOU 2597  CB  THR D  85    15829  16278  12179  -5187  -1808   3898       C  
ATOM   2598  OG1 THR D  85      77.546  41.598   1.539  1.00115.52           O  
ANISOU 2598  OG1 THR D  85    16133  15620  12138  -4794  -1917   3818       O  
ATOM   2599  CG2 THR D  85      79.916  42.156   1.456  1.00122.59           C  
ANISOU 2599  CG2 THR D  85    16636  17213  12729  -5970  -1932   4381       C  
ATOM   2600  N   LEU D  86      81.428  39.485   2.655  1.00123.28           N  
ANISOU 2600  N   LEU D  86    14309  20655  11878  -5386  -1150   4283       N  
ATOM   2601  CA  LEU D  86      82.509  39.186   3.593  1.00124.21           C  
ANISOU 2601  CA  LEU D  86    14018  21199  11976  -5595  -1129   4247       C  
ATOM   2602  C   LEU D  86      82.393  40.060   4.839  1.00124.71           C  
ANISOU 2602  C   LEU D  86    14518  20639  12227  -5784  -1434   4119       C  
ATOM   2603  O   LEU D  86      82.505  39.568   5.962  1.00121.73           O  
ANISOU 2603  O   LEU D  86    14090  20171  11989  -5450  -1429   3811       O  
ATOM   2604  CB  LEU D  86      83.870  39.378   2.920  1.00129.60           C  
ANISOU 2604  CB  LEU D  86    14302  22552  12388  -6233  -1090   4640       C  
ATOM   2605  CG  LEU D  86      85.088  38.877   3.700  1.00129.96           C  
ANISOU 2605  CG  LEU D  86    13616  23455  12306  -6148   -873   4592       C  
ATOM   2606  CD1 LEU D  86      85.105  37.358   3.753  1.00125.07           C  
ANISOU 2606  CD1 LEU D  86    12733  23046  11743  -5335   -608   4252       C  
ATOM   2607  CD2 LEU D  86      86.374  39.407   3.084  1.00135.58           C  
ANISOU 2607  CD2 LEU D  86    13867  24969  12678  -6680   -754   5004       C  
ATOM   2608  N   TRP D  87      82.149  41.352   4.630  1.00132.02           N  
ANISOU 2608  N   TRP D  87    16022  20603  13536  -8122  -2055   3574       N  
ATOM   2609  CA  TRP D  87      81.944  42.298   5.725  1.00133.01           C  
ANISOU 2609  CA  TRP D  87    16690  20018  13831  -8239  -2383   3404       C  
ATOM   2610  C   TRP D  87      80.677  42.013   6.525  1.00128.06           C  
ANISOU 2610  C   TRP D  87    16306  18944  13408  -7508  -2355   2966       C  
ATOM   2611  O   TRP D  87      80.709  41.983   7.752  1.00125.96           O  
ANISOU 2611  O   TRP D  87    15891  18753  13216  -7302  -2330   2699       O  
ATOM   2612  CB  TRP D  87      81.937  43.732   5.191  1.00138.16           C  
ANISOU 2612  CB  TRP D  87    17953  20086  14457  -8767  -2712   3692       C  
ATOM   2613  CG  TRP D  87      83.287  44.401   5.149  1.00144.08           C  
ANISOU 2613  CG  TRP D  87    18556  21147  15039  -9641  -2860   4074       C  
ATOM   2614  CD1 TRP D  87      83.537  45.690   4.783  1.00150.06           C  
ANISOU 2614  CD1 TRP D  87    19824  21449  15743 -10318  -3198   4408       C  
ATOM   2615  CD2 TRP D  87      84.558  43.831   5.510  1.00145.21           C  
ANISOU 2615  CD2 TRP D  87    17993  22144  15036  -9959  -2703   4176       C  
ATOM   2616  NE1 TRP D  87      84.881  45.957   4.872  1.00154.92           N  
ANISOU 2616  NE1 TRP D  87    20070  22612  16179 -11104  -3251   4736       N  
ATOM   2617  CE2 TRP D  87      85.530  44.837   5.318  1.00152.06           C  
ANISOU 2617  CE2 TRP D  87    18932  23091  15753 -10880  -2944   4591       C  
ATOM   2618  CE3 TRP D  87      84.970  42.570   5.971  1.00141.59           C  
ANISOU 2618  CE3 TRP D  87    16855  22389  14552  -9550  -2402   3968       C  
ATOM   2619  CZ2 TRP D  87      86.893  44.624   5.571  1.00155.41           C  
ANISOU 2619  CZ2 TRP D  87    18699  24356  15992 -11410  -2876   4801       C  
ATOM   2620  CZ3 TRP D  87      86.325  42.357   6.223  1.00144.86           C  
ANISOU 2620  CZ3 TRP D  87    16648  23601  14791 -10006  -2344   4159       C  
ATOM   2621  CH2 TRP D  87      87.269  43.381   6.021  1.00151.68           C  
ANISOU 2621  CH2 TRP D  87    17531  24604  15497 -10927  -2570   4568       C  
ATOM   2622  N   GLY D  88      79.570  41.796   5.828  1.00117.55           N  
ANISOU 2622  N   GLY D  88    16154  15617  12893  -6258  -2311   2234       N  
ATOM   2623  CA  GLY D  88      78.320  41.409   6.477  1.00113.14           C  
ANISOU 2623  CA  GLY D  88    15711  14783  12495  -5572  -2242   1847       C  
ATOM   2624  C   GLY D  88      78.449  40.123   7.275  1.00109.11           C  
ANISOU 2624  C   GLY D  88    14728  14709  12021  -5231  -2011   1592       C  
ATOM   2625  O   GLY D  88      77.728  39.923   8.252  1.00106.92           O  
ANISOU 2625  O   GLY D  88    14594  14174  11857  -4860  -2040   1283       O  
ATOM   2626  N   ARG D  89      79.368  39.255   6.852  1.00106.23           N  
ANISOU 2626  N   ARG D  89    13623  16007  10733  -4437  -1587   1482       N  
ATOM   2627  CA  ARG D  89      79.629  37.990   7.538  1.00103.05           C  
ANISOU 2627  CA  ARG D  89    12785  16016  10354  -4111  -1395   1280       C  
ATOM   2628  C   ARG D  89      80.529  38.151   8.769  1.00104.50           C  
ANISOU 2628  C   ARG D  89    12890  16279  10538  -4363  -1532   1208       C  
ATOM   2629  O   ARG D  89      80.476  37.334   9.693  1.00101.95           O  
ANISOU 2629  O   ARG D  89    12485  15969  10282  -4036  -1488    965       O  
ATOM   2630  CB  ARG D  89      80.182  36.939   6.566  1.00102.34           C  
ANISOU 2630  CB  ARG D  89    12162  16586  10136  -3998  -1125   1400       C  
ATOM   2631  CG  ARG D  89      79.093  36.280   5.744  1.00100.11           C  
ANISOU 2631  CG  ARG D  89    11950  16228   9860  -3623   -983   1364       C  
ATOM   2632  CD  ARG D  89      79.595  35.397   4.611  1.00 99.33           C  
ANISOU 2632  CD  ARG D  89    11404  16709   9626  -3382   -721   1392       C  
ATOM   2633  NE  ARG D  89      78.457  34.892   3.832  1.00 96.90           N  
ANISOU 2633  NE  ARG D  89    11283  16176   9360  -2998   -651   1286       N  
ATOM   2634  CZ  ARG D  89      78.525  33.962   2.883  1.00 96.14           C  
ANISOU 2634  CZ  ARG D  89    10965  16410   9153  -2721   -465   1254       C  
ATOM   2635  NH1 ARG D  89      79.685  33.399   2.569  1.00 97.64           N  
ANISOU 2635  NH1 ARG D  89    10726  17195   9177  -2717   -305   1305       N  
ATOM   2636  NH2 ARG D  89      77.423  33.586   2.246  1.00 94.27           N  
ANISOU 2636  NH2 ARG D  89    10930  15933   8956  -2425   -450   1154       N  
ATOM   2637  N   CYS D  90      81.348  39.203   8.780  1.00113.93           N  
ANISOU 2637  N   CYS D  90    13472  18528  11287  -5615  -1664   1242       N  
ATOM   2638  CA  CYS D  90      82.088  39.588   9.979  1.00116.10           C  
ANISOU 2638  CA  CYS D  90    13819  18734  11561  -5922  -1883   1157       C  
ATOM   2639  C   CYS D  90      81.110  40.037  11.048  1.00114.73           C  
ANISOU 2639  C   CYS D  90    14169  17907  11515  -5618  -2041    836       C  
ATOM   2640  O   CYS D  90      81.076  39.460  12.129  1.00112.03           O  
ANISOU 2640  O   CYS D  90    13709  17649  11209  -5255  -1964    590       O  
ATOM   2641  CB  CYS D  90      83.084  40.708   9.688  1.00121.85           C  
ANISOU 2641  CB  CYS D  90    14672  19439  12185  -6694  -2132   1452       C  
ATOM   2642  SG  CYS D  90      84.633  40.158   8.957  1.00124.91           S  
ANISOU 2642  SG  CYS D  90    14330  20776  12354  -7145  -1956   1847       S  
ATOM   2643  N   VAL D  91      80.309  41.056  10.735  1.00113.59           N  
ANISOU 2643  N   VAL D  91    15355  15576  12227  -6200  -2283    636       N  
ATOM   2644  CA  VAL D  91      79.244  41.519  11.625  1.00112.78           C  
ANISOU 2644  CA  VAL D  91    15736  14895  12220  -5811  -2419    291       C  
ATOM   2645  C   VAL D  91      78.530  40.329  12.255  1.00107.89           C  
ANISOU 2645  C   VAL D  91    14823  14527  11644  -5206  -2164     27       C  
ATOM   2646  O   VAL D  91      78.298  40.324  13.456  1.00107.65           O  
ANISOU 2646  O   VAL D  91    14894  14405  11604  -5047  -2231   -230       O  
ATOM   2647  CB  VAL D  91      78.224  42.397  10.876  1.00114.07           C  
ANISOU 2647  CB  VAL D  91    16443  14446  12454  -5660  -2557    300       C  
ATOM   2648  CG1 VAL D  91      77.065  42.764  11.789  1.00113.24           C  
ANISOU 2648  CG1 VAL D  91    16729  13875  12422  -5123  -2643    -98       C  
ATOM   2649  CG2 VAL D  91      78.898  43.647  10.329  1.00119.79           C  
ANISOU 2649  CG2 VAL D  91    17582  14798  13134  -6301  -2882    560       C  
ATOM   2650  N   ALA D  92      78.226  39.311  11.449  1.00 99.64           N  
ANISOU 2650  N   ALA D  92    13766  13665  10427  -4032  -1814     88       N  
ATOM   2651  CA  ALA D  92      77.573  38.091  11.931  1.00 95.47           C  
ANISOU 2651  CA  ALA D  92    12984  13346   9943  -3517  -1595   -118       C  
ATOM   2652  C   ALA D  92      78.297  37.477  13.132  1.00 95.02           C  
ANISOU 2652  C   ALA D  92    12651  13624   9830  -3542  -1576   -214       C  
ATOM   2653  O   ALA D  92      77.732  37.399  14.229  1.00 94.31           O  
ANISOU 2653  O   ALA D  92    12696  13404   9735  -3312  -1613   -457       O  
ATOM   2654  CB  ALA D  92      77.437  37.075  10.810  1.00 92.85           C  
ANISOU 2654  CB  ALA D  92    12326  13327   9625  -3300  -1348      5       C  
ATOM   2655  N   VAL D  93      79.547  37.063  12.922  1.00 98.23           N  
ANISOU 2655  N   VAL D  93    12588  14985   9751  -3388  -1643   -256       N  
ATOM   2656  CA  VAL D  93      80.393  36.500  13.985  1.00 98.96           C  
ANISOU 2656  CA  VAL D  93    12405  15429   9766  -3494  -1685   -286       C  
ATOM   2657  C   VAL D  93      80.250  37.298  15.279  1.00101.03           C  
ANISOU 2657  C   VAL D  93    13030  15369   9989  -3643  -1931   -485       C  
ATOM   2658  O   VAL D  93      79.985  36.726  16.336  1.00 99.63           O  
ANISOU 2658  O   VAL D  93    12841  15230   9782  -3371  -1907   -679       O  
ATOM   2659  CB  VAL D  93      81.879  36.493  13.580  1.00101.75           C  
ANISOU 2659  CB  VAL D  93    12335  16307  10017  -3910  -1693    -16       C  
ATOM   2660  CG1 VAL D  93      82.765  36.697  14.799  1.00104.09           C  
ANISOU 2660  CG1 VAL D  93    12483  16843  10222  -4168  -1860    -39       C  
ATOM   2661  CG2 VAL D  93      82.230  35.196  12.867  1.00 99.67           C  
ANISOU 2661  CG2 VAL D  93    11610  16518   9743  -3590  -1430     75       C  
ATOM   2662  N   VAL D  94      80.408  38.616  15.181  1.00104.69           N  
ANISOU 2662  N   VAL D  94    13528  15567  10681  -4572  -2232   -569       N  
ATOM   2663  CA  VAL D  94      80.268  39.501  16.332  1.00107.14           C  
ANISOU 2663  CA  VAL D  94    14267  15500  10943  -4670  -2492   -810       C  
ATOM   2664  C   VAL D  94      78.926  39.291  17.042  1.00104.46           C  
ANISOU 2664  C   VAL D  94    14143  14915  10631  -4084  -2393  -1123       C  
ATOM   2665  O   VAL D  94      78.910  38.969  18.225  1.00103.65           O  
ANISOU 2665  O   VAL D  94    13936  15002  10446  -3903  -2363  -1291       O  
ATOM   2666  CB  VAL D  94      80.492  40.993  15.960  1.00111.73           C  
ANISOU 2666  CB  VAL D  94    15360  15563  11529  -5125  -2803   -754       C  
ATOM   2667  CG1 VAL D  94      80.186  41.903  17.142  1.00114.41           C  
ANISOU 2667  CG1 VAL D  94    16237  15422  11813  -5087  -3080  -1096       C  
ATOM   2668  CG2 VAL D  94      81.918  41.212  15.479  1.00115.26           C  
ANISOU 2668  CG2 VAL D  94    15549  16339  11906  -5809  -2921   -422       C  
ATOM   2669  N   VAL D  95      77.813  39.435  16.328  1.00 99.31           N  
ANISOU 2669  N   VAL D  95    14252  13303  10177  -3732  -2375   -914       N  
ATOM   2670  CA  VAL D  95      76.495  39.231  16.948  1.00 97.49           C  
ANISOU 2670  CA  VAL D  95    14173  12926   9944  -3194  -2282  -1209       C  
ATOM   2671  C   VAL D  95      76.287  37.788  17.448  1.00 93.82           C  
ANISOU 2671  C   VAL D  95    13261  12939   9447  -2890  -2019  -1229       C  
ATOM   2672  O   VAL D  95      75.590  37.569  18.450  1.00 93.76           O  
ANISOU 2672  O   VAL D  95    13317  12968   9339  -2638  -2002  -1464       O  
ATOM   2673  CB  VAL D  95      75.355  39.524  15.957  1.00 97.28           C  
ANISOU 2673  CB  VAL D  95    14461  12485  10017  -2867  -2272  -1275       C  
ATOM   2674  CG1 VAL D  95      75.874  40.313  14.764  1.00 97.95           C  
ANISOU 2674  CG1 VAL D  95    14571  12459  10185  -3147  -2305   -974       C  
ATOM   2675  CG2 VAL D  95      74.698  38.229  15.503  1.00 93.55           C  
ANISOU 2675  CG2 VAL D  95    13756  12216   9574  -2318  -2000  -1392       C  
ATOM   2676  N   MET D  96      76.912  36.821  16.770  1.00 92.26           N  
ANISOU 2676  N   MET D  96    13078  13071   8904  -2540  -2049   -908       N  
ATOM   2677  CA  MET D  96      76.889  35.420  17.206  1.00 89.74           C  
ANISOU 2677  CA  MET D  96    12391  13155   8552  -2321  -1870   -894       C  
ATOM   2678  C   MET D  96      77.494  35.244  18.603  1.00 91.35           C  
ANISOU 2678  C   MET D  96    12548  13555   8606  -2436  -1986   -982       C  
ATOM   2679  O   MET D  96      76.793  34.843  19.533  1.00 90.98           O  
ANISOU 2679  O   MET D  96    12593  13506   8468  -2191  -1954  -1167       O  
ATOM   2680  CB  MET D  96      77.649  34.537  16.213  1.00 88.19           C  
ANISOU 2680  CB  MET D  96    11804  13290   8414  -2350  -1726   -653       C  
ATOM   2681  CG  MET D  96      77.084  34.561  14.803  1.00 85.85           C  
ANISOU 2681  CG  MET D  96    11490  12903   8226  -2099  -1560   -613       C  
ATOM   2682  SD  MET D  96      77.815  33.303  13.739  1.00 85.75           S  
ANISOU 2682  SD  MET D  96    11092  13261   8227  -2224  -1446   -347       S  
ATOM   2683  CE  MET D  96      77.122  31.813  14.449  1.00 82.70           C  
ANISOU 2683  CE  MET D  96    10448  13092   7884  -1785  -1253   -376       C  
ATOM   2684  N   VAL D  97      78.784  35.550  18.750  1.00 93.46           N  
ANISOU 2684  N   VAL D  97    12764  13620   9127  -2611  -2340   -710       N  
ATOM   2685  CA  VAL D  97      79.466  35.368  20.039  1.00 95.26           C  
ANISOU 2685  CA  VAL D  97    12936  14066   9191  -2720  -2476   -791       C  
ATOM   2686  C   VAL D  97      78.899  36.272  21.144  1.00 97.24           C  
ANISOU 2686  C   VAL D  97    13620  14014   9312  -2665  -2627  -1101       C  
ATOM   2687  O   VAL D  97      78.839  35.868  22.304  1.00 96.60           O  
ANISOU 2687  O   VAL D  97    13523  14071   9108  -2410  -2561  -1233       O  
ATOM   2688  CB  VAL D  97      81.022  35.486  19.941  1.00 97.97           C  
ANISOU 2688  CB  VAL D  97    13001  14751   9473  -3153  -2632   -604       C  
ATOM   2689  CG1 VAL D  97      81.569  34.539  18.872  1.00 96.51           C  
ANISOU 2689  CG1 VAL D  97    12380  14916   9373  -3098  -2459   -353       C  
ATOM   2690  CG2 VAL D  97      81.474  36.930  19.688  1.00101.61           C  
ANISOU 2690  CG2 VAL D  97    13732  14952   9922  -3633  -2874   -599       C  
ATOM   2691  N   ALA D  98      78.469  37.478  20.770  1.00 97.71           N  
ANISOU 2691  N   ALA D  98    14110  13757   9257  -3039  -2776   -964       N  
ATOM   2692  CA  ALA D  98      77.817  38.404  21.696  1.00 99.69           C  
ANISOU 2692  CA  ALA D  98    14842  13625   9412  -2848  -2897  -1306       C  
ATOM   2693  C   ALA D  98      76.616  37.744  22.358  1.00 97.46           C  
ANISOU 2693  C   ALA D  98    14497  13490   9045  -2334  -2676  -1481       C  
ATOM   2694  O   ALA D  98      76.378  37.920  23.551  1.00 99.19           O  
ANISOU 2694  O   ALA D  98    14845  13787   9057  -2216  -2736  -1713       O  
ATOM   2695  CB  ALA D  98      77.388  39.663  20.972  1.00100.88           C  
ANISOU 2695  CB  ALA D  98    15382  13252   9696  -2849  -2989  -1342       C  
ATOM   2696  N   GLY D  99      75.866  36.981  21.573  1.00 93.98           N  
ANISOU 2696  N   GLY D  99    14023  13019   8667  -2144  -2604  -1292       N  
ATOM   2697  CA  GLY D  99      74.742  36.218  22.092  1.00 92.13           C  
ANISOU 2697  CA  GLY D  99    13674  12975   8357  -1728  -2387  -1397       C  
ATOM   2698  C   GLY D  99      75.193  35.078  22.988  1.00 90.99           C  
ANISOU 2698  C   GLY D  99    13193  13284   8096  -1742  -2292  -1266       C  
ATOM   2699  O   GLY D  99      74.746  34.975  24.137  1.00 92.18           O  
ANISOU 2699  O   GLY D  99    13382  13614   8027  -1597  -2273  -1421       O  
ATOM   2700  N   ILE D 100      76.083  34.230  22.462  1.00 90.41           N  
ANISOU 2700  N   ILE D 100    12753  13157   8442  -1956  -2404   -964       N  
ATOM   2701  CA  ILE D 100      76.576  33.057  23.189  1.00 89.79           C  
ANISOU 2701  CA  ILE D 100    12381  13461   8274  -1948  -2358   -807       C  
ATOM   2702  C   ILE D 100      77.171  33.480  24.532  1.00 92.97           C  
ANISOU 2702  C   ILE D 100    12891  13997   8437  -2124  -2561   -938       C  
ATOM   2703  O   ILE D 100      76.743  33.006  25.587  1.00 93.63           O  
ANISOU 2703  O   ILE D 100    12966  14295   8315  -1991  -2530  -1000       O  
ATOM   2704  CB  ILE D 100      77.633  32.291  22.373  1.00 88.74           C  
ANISOU 2704  CB  ILE D 100    11932  13503   8282  -2080  -2348   -534       C  
ATOM   2705  CG1 ILE D 100      77.038  31.810  21.048  1.00 85.94           C  
ANISOU 2705  CG1 ILE D 100    11482  13042   8129  -1901  -2163   -423       C  
ATOM   2706  CG2 ILE D 100      78.182  31.122  23.177  1.00 88.88           C  
ANISOU 2706  CG2 ILE D 100    11696  13878   8198  -2020  -2354   -385       C  
ATOM   2707  CD1 ILE D 100      78.064  31.259  20.082  1.00 85.78           C  
ANISOU 2707  CD1 ILE D 100    11210  13162   8220  -2029  -2163   -223       C  
ATOM   2708  N   THR D 101      78.135  34.396  24.480  1.00 93.88           N  
ANISOU 2708  N   THR D 101    13200  13937   8532  -2546  -2825   -547       N  
ATOM   2709  CA  THR D 101      78.818  34.883  25.668  1.00 97.24           C  
ANISOU 2709  CA  THR D 101    13730  14484   8734  -2764  -3055   -671       C  
ATOM   2710  C   THR D 101      77.862  35.487  26.693  1.00 99.04           C  
ANISOU 2710  C   THR D 101    14286  14615   8731  -2560  -3080   -999       C  
ATOM   2711  O   THR D 101      77.836  35.039  27.835  1.00 99.95           O  
ANISOU 2711  O   THR D 101    14320  15038   8617  -2491  -3083  -1026       O  
ATOM   2712  CB  THR D 101      79.953  35.869  25.296  1.00 99.97           C  
ANISOU 2712  CB  THR D 101    14171  14678   9136  -3216  -3305   -644       C  
ATOM   2713  OG1 THR D 101      81.057  35.127  24.766  1.00100.40           O  
ANISOU 2713  OG1 THR D 101    13806  15159   9181  -3436  -3360   -386       O  
ATOM   2714  CG2 THR D 101      80.434  36.674  26.510  1.00104.33           C  
ANISOU 2714  CG2 THR D 101    15166  14986   9488  -3416  -3596   -959       C  
ATOM   2715  N   SER D 102      77.073  36.482  26.295  1.00 99.39           N  
ANISOU 2715  N   SER D 102    14554  14520   8688  -2548  -2955  -1079       N  
ATOM   2716  CA  SER D 102      76.220  37.180  27.263  1.00102.28           C  
ANISOU 2716  CA  SER D 102    15235  14851   8775  -2335  -3015  -1444       C  
ATOM   2717  C   SER D 102      75.131  36.277  27.846  1.00100.46           C  
ANISOU 2717  C   SER D 102    14814  14938   8417  -1934  -2725  -1450       C  
ATOM   2718  O   SER D 102      74.722  36.460  28.994  1.00102.84           O  
ANISOU 2718  O   SER D 102    15240  15421   8415  -1747  -2716  -1693       O  
ATOM   2719  CB  SER D 102      75.559  38.397  26.614  1.00104.95           C  
ANISOU 2719  CB  SER D 102    16073  14656   9147  -2249  -3170  -1759       C  
ATOM   2720  OG  SER D 102      74.701  38.008  25.557  1.00102.56           O  
ANISOU 2720  OG  SER D 102    15754  14196   9019  -1902  -2955  -1749       O  
ATOM   2721  N   PHE D 103      74.674  35.303  27.062  1.00 98.21           N  
ANISOU 2721  N   PHE D 103    13928  14681   8705  -1845  -2694  -1054       N  
ATOM   2722  CA  PHE D 103      73.745  34.296  27.573  1.00 97.08           C  
ANISOU 2722  CA  PHE D 103    13591  14870   8426  -1569  -2451  -1008       C  
ATOM   2723  C   PHE D 103      74.456  33.293  28.478  1.00 97.42           C  
ANISOU 2723  C   PHE D 103    13415  15317   8282  -1701  -2467   -807       C  
ATOM   2724  O   PHE D 103      73.817  32.631  29.296  1.00 98.24           O  
ANISOU 2724  O   PHE D 103    13443  15747   8137  -1551  -2341   -807       O  
ATOM   2725  CB  PHE D 103      73.032  33.564  26.435  1.00 93.60           C  
ANISOU 2725  CB  PHE D 103    12948  14378   8239  -1423  -2231   -810       C  
ATOM   2726  CG  PHE D 103      71.722  34.187  26.035  1.00 94.03           C  
ANISOU 2726  CG  PHE D 103    13139  14286   8303  -1110  -2120  -1037       C  
ATOM   2727  CD1 PHE D 103      70.625  34.160  26.901  1.00 96.09           C  
ANISOU 2727  CD1 PHE D 103    13396  14832   8280   -833  -1991  -1237       C  
ATOM   2728  CD2 PHE D 103      71.575  34.785  24.788  1.00 92.81           C  
ANISOU 2728  CD2 PHE D 103    13088  13760   8415  -1072  -2143  -1041       C  
ATOM   2729  CE1 PHE D 103      69.401  34.726  26.531  1.00 97.01           C  
ANISOU 2729  CE1 PHE D 103    13581  14888   8391   -482  -1884  -1458       C  
ATOM   2730  CE2 PHE D 103      70.355  35.355  24.408  1.00 93.53           C  
ANISOU 2730  CE2 PHE D 103    13284  13738   8514   -732  -2058  -1242       C  
ATOM   2731  CZ  PHE D 103      69.267  35.327  25.285  1.00 95.72           C  
ANISOU 2731  CZ  PHE D 103    13529  14323   8517   -418  -1932  -1462       C  
ATOM   2732  N   GLY D 104      75.775  33.187  28.321  1.00 98.76           N  
ANISOU 2732  N   GLY D 104    13085  15657   8783  -2159  -2588   -144       N  
ATOM   2733  CA  GLY D 104      76.603  32.349  29.185  1.00 99.84           C  
ANISOU 2733  CA  GLY D 104    13036  16161   8737  -2282  -2678     40       C  
ATOM   2734  C   GLY D 104      76.724  32.957  30.566  1.00103.67           C  
ANISOU 2734  C   GLY D 104    13726  16819   8845  -2320  -2827   -215       C  
ATOM   2735  O   GLY D 104      76.608  32.253  31.568  1.00104.73           O  
ANISOU 2735  O   GLY D 104    13780  17303   8709  -2233  -2770   -147       O  
ATOM   2736  N   LEU D 105      76.950  34.270  30.609  1.00106.94           N  
ANISOU 2736  N   LEU D 105    14668  17198   8765  -2359  -2956   -509       N  
ATOM   2737  CA  LEU D 105      77.003  35.016  31.864  1.00111.13           C  
ANISOU 2737  CA  LEU D 105    15468  17836   8921  -2370  -3123   -829       C  
ATOM   2738  C   LEU D 105      75.765  34.819  32.724  1.00111.90           C  
ANISOU 2738  C   LEU D 105    15596  18198   8722  -2018  -2902   -973       C  
ATOM   2739  O   LEU D 105      75.875  34.690  33.945  1.00113.96           O  
ANISOU 2739  O   LEU D 105    15798  18860   8641  -2022  -2924   -952       O  
ATOM   2740  CB  LEU D 105      77.192  36.512  31.615  1.00114.04           C  
ANISOU 2740  CB  LEU D 105    16267  17755   9308  -2481  -3357  -1192       C  
ATOM   2741  CG  LEU D 105      78.544  37.101  32.011  1.00117.04           C  
ANISOU 2741  CG  LEU D 105    16701  18155   9614  -2935  -3711  -1184       C  
ATOM   2742  CD1 LEU D 105      79.392  37.330  30.771  1.00114.80           C  
ANISOU 2742  CD1 LEU D 105    16202  17703   9715  -3236  -3754   -873       C  
ATOM   2743  CD2 LEU D 105      78.343  38.402  32.767  1.00122.04           C  
ANISOU 2743  CD2 LEU D 105    17863  18462  10043  -3035  -4009  -1637       C  
ATOM   2744  N   VAL D 106      74.596  34.805  32.086  1.00114.27           N  
ANISOU 2744  N   VAL D 106    15469  18476   9474  -1518  -2604   -700       N  
ATOM   2745  CA  VAL D 106      73.329  34.651  32.798  1.00115.77           C  
ANISOU 2745  CA  VAL D 106    15650  18984   9354  -1176  -2380   -866       C  
ATOM   2746  C   VAL D 106      73.208  33.247  33.390  1.00114.64           C  
ANISOU 2746  C   VAL D 106    15166  19330   9063  -1213  -2206   -498       C  
ATOM   2747  O   VAL D 106      72.631  33.073  34.467  1.00117.10           O  
ANISOU 2747  O   VAL D 106    15440  20069   8985  -1058  -2072   -572       O  
ATOM   2748  CB  VAL D 106      72.113  35.013  31.912  1.00114.49           C  
ANISOU 2748  CB  VAL D 106    15513  18621   9367   -856  -2179   -996       C  
ATOM   2749  CG1 VAL D 106      70.805  34.826  32.673  1.00117.41           C  
ANISOU 2749  CG1 VAL D 106    15865  19399   9345   -487  -1973  -1244       C  
ATOM   2750  CG2 VAL D 106      72.228  36.454  31.426  1.00115.47           C  
ANISOU 2750  CG2 VAL D 106    16007  18163   9703   -847  -2389  -1274       C  
ATOM   2751  N   THR D 107      73.773  32.257  32.701  1.00111.65           N  
ANISOU 2751  N   THR D 107    14213  18852   9356  -1500  -2179    -66       N  
ATOM   2752  CA  THR D 107      73.885  30.907  33.259  1.00111.25           C  
ANISOU 2752  CA  THR D 107    13917  19179   9175  -1559  -2095    308       C  
ATOM   2753  C   THR D 107      74.869  30.888  34.431  1.00114.37           C  
ANISOU 2753  C   THR D 107    14349  19867   9239  -1718  -2310    326       C  
ATOM   2754  O   THR D 107      74.582  30.300  35.474  1.00116.55           O  
ANISOU 2754  O   THR D 107    14579  20556   9149  -1676  -2237    414       O  
ATOM   2755  CB  THR D 107      74.283  29.864  32.189  1.00107.57           C  
ANISOU 2755  CB  THR D 107    13226  18552   9094  -1644  -2058    705       C  
ATOM   2756  OG1 THR D 107      73.110  29.449  31.474  1.00105.35           O  
ANISOU 2756  OG1 THR D 107    12859  18185   8985  -1490  -1810    770       O  
ATOM   2757  CG2 THR D 107      74.938  28.634  32.832  1.00108.42           C  
ANISOU 2757  CG2 THR D 107    13176  18968   9050  -1745  -2126   1081       C  
ATOM   2758  N   ALA D 108      76.014  31.547  34.248  1.00113.75           N  
ANISOU 2758  N   ALA D 108    14709  19682   8827  -1905  -2508    117       N  
ATOM   2759  CA  ALA D 108      77.038  31.674  35.289  1.00117.29           C  
ANISOU 2759  CA  ALA D 108    15209  20400   8954  -2085  -2771     74       C  
ATOM   2760  C   ALA D 108      76.506  32.378  36.537  1.00121.29           C  
ANISOU 2760  C   ALA D 108    15960  21151   8975  -1958  -2761   -288       C  
ATOM   2761  O   ALA D 108      76.779  31.949  37.660  1.00123.48           O  
ANISOU 2761  O   ALA D 108    16171  21871   8874  -1934  -2735   -168       O  
ATOM   2762  CB  ALA D 108      78.261  32.398  34.746  1.00117.96           C  
ANISOU 2762  CB  ALA D 108    15357  20237   9226  -2361  -3064    -27       C  
ATOM   2763  N   ALA D 109      75.746  33.452  36.330  1.00127.29           N  
ANISOU 2763  N   ALA D 109    17271  21538   9555  -1162  -2429   -595       N  
ATOM   2764  CA  ALA D 109      75.119  34.200  37.420  1.00131.48           C  
ANISOU 2764  CA  ALA D 109    18061  22268   9628   -934  -2396  -1024       C  
ATOM   2765  C   ALA D 109      74.227  33.299  38.273  1.00132.40           C  
ANISOU 2765  C   ALA D 109    17970  22964   9373   -758  -2128   -847       C  
ATOM   2766  O   ALA D 109      74.307  33.324  39.500  1.00136.21           O  
ANISOU 2766  O   ALA D 109    18509  23871   9374   -772  -2198   -928       O  
ATOM   2767  CB  ALA D 109      74.321  35.378  36.867  1.00131.67           C  
ANISOU 2767  CB  ALA D 109    18349  21884   9797   -663  -2321  -1421       C  
ATOM   2768  N   LEU D 110      73.393  32.498  37.611  1.00131.05           N  
ANISOU 2768  N   LEU D 110    16758  23309   9726   -757  -1786   -637       N  
ATOM   2769  CA  LEU D 110      72.483  31.569  38.286  1.00132.09           C  
ANISOU 2769  CA  LEU D 110    16671  23978   9538   -656  -1516   -407       C  
ATOM   2770  C   LEU D 110      73.219  30.395  38.936  1.00132.34           C  
ANISOU 2770  C   LEU D 110    16529  24327   9428   -900  -1595     77       C  
ATOM   2771  O   LEU D 110      72.747  29.834  39.925  1.00135.06           O  
ANISOU 2771  O   LEU D 110    16787  25184   9347   -888  -1465    225       O  
ATOM   2772  CB  LEU D 110      71.432  31.035  37.303  1.00128.85           C  
ANISOU 2772  CB  LEU D 110    16055  23464   9437   -523  -1225   -241       C  
ATOM   2773  CG  LEU D 110      70.452  31.992  36.621  1.00128.57           C  
ANISOU 2773  CG  LEU D 110    16135  23157   9558   -223  -1116   -643       C  
ATOM   2774  CD1 LEU D 110      69.886  31.332  35.379  1.00125.32           C  
ANISOU 2774  CD1 LEU D 110    15462  22703   9452   -171   -871   -378       C  
ATOM   2775  CD2 LEU D 110      69.332  32.429  37.559  1.00133.58           C  
ANISOU 2775  CD2 LEU D 110    16890  24187   9676     93  -1016  -1087       C  
ATOM   2776  N   ALA D 111      74.364  30.026  38.365  1.00125.97           N  
ANISOU 2776  N   ALA D 111    15858  23060   8943  -1562  -1823    114       N  
ATOM   2777  CA  ALA D 111      75.166  28.917  38.869  1.00126.37           C  
ANISOU 2777  CA  ALA D 111    15762  23339   8913  -1732  -1943    576       C  
ATOM   2778  C   ALA D 111      75.811  29.251  40.210  1.00130.92           C  
ANISOU 2778  C   ALA D 111    16460  24292   8992  -1817  -2166    442       C  
ATOM   2779  O   ALA D 111      75.983  28.370  41.050  1.00133.25           O  
ANISOU 2779  O   ALA D 111    16686  24996   8946  -1873  -2176    744       O  
ATOM   2780  CB  ALA D 111      76.223  28.509  37.853  1.00123.09           C  
ANISOU 2780  CB  ALA D 111    15225  22554   8989  -1847  -2112    828       C  
ATOM   2781  N   THR D 112      76.161  30.521  40.411  1.00132.29           N  
ANISOU 2781  N   THR D 112    17389  24012   8862  -1699  -2079   -128       N  
ATOM   2782  CA  THR D 112      76.759  30.954  41.679  1.00137.23           C  
ANISOU 2782  CA  THR D 112    18169  25005   8967  -1784  -2310   -326       C  
ATOM   2783  C   THR D 112      75.697  31.339  42.708  1.00141.00           C  
ANISOU 2783  C   THR D 112    18765  25927   8881  -1573  -2098   -580       C  
ATOM   2784  O   THR D 112      75.945  31.268  43.908  1.00144.68           O  
ANISOU 2784  O   THR D 112    19222  26905   8843  -1621  -2147   -465       O  
ATOM   2785  CB  THR D 112      77.772  32.110  41.502  1.00138.89           C  
ANISOU 2785  CB  THR D 112    18611  24921   9241  -1941  -2644   -734       C  
ATOM   2786  OG1 THR D 112      77.082  33.330  41.207  1.00138.47           O  
ANISOU 2786  OG1 THR D 112    18800  24475   9336  -1779  -2549  -1181       O  
ATOM   2787  CG2 THR D 112      78.741  31.800  40.383  1.00136.23           C  
ANISOU 2787  CG2 THR D 112    18083  24317   9362  -2183  -2856   -451       C  
ATOM   2788  N   TRP D 113      74.522  31.746  42.233  1.00148.42           N  
ANISOU 2788  N   TRP D 113    19130  26769  10495   -807  -1384   -960       N  
ATOM   2789  CA  TRP D 113      73.371  31.987  43.103  1.00152.32           C  
ANISOU 2789  CA  TRP D 113    19671  27751  10452   -542  -1139  -1225       C  
ATOM   2790  C   TRP D 113      72.919  30.671  43.732  1.00153.18           C  
ANISOU 2790  C   TRP D 113    19502  28440  10258   -607   -910   -727       C  
ATOM   2791  O   TRP D 113      72.465  30.645  44.874  1.00157.70           O  
ANISOU 2791  O   TRP D 113    20079  29605  10233   -499   -778   -840       O  
ATOM   2792  CB  TRP D 113      72.228  32.653  42.321  1.00151.36           C  
ANISOU 2792  CB  TRP D 113    19607  27389  10513   -212   -904  -1591       C  
ATOM   2793  CG  TRP D 113      70.911  32.750  43.060  1.00155.34           C  
ANISOU 2793  CG  TRP D 113    20031  28512  10481    100   -586  -1789       C  
ATOM   2794  CD1 TRP D 113      70.722  33.135  44.356  1.00161.14           C  
ANISOU 2794  CD1 TRP D 113    20889  29798  10537    225   -595  -2076       C  
ATOM   2795  CD2 TRP D 113      69.604  32.480  42.529  1.00154.33           C  
ANISOU 2795  CD2 TRP D 113    19644  28578  10418    325   -212  -1717       C  
ATOM   2796  NE1 TRP D 113      69.385  33.105  44.670  1.00163.90           N  
ANISOU 2796  NE1 TRP D 113    21047  30716  10512    526   -226  -2177       N  
ATOM   2797  CE2 TRP D 113      68.676  32.710  43.568  1.00159.87           C  
ANISOU 2797  CE2 TRP D 113    20285  30006  10451    582      8  -1954       C  
ATOM   2798  CE3 TRP D 113      69.129  32.062  41.276  1.00149.65           C  
ANISOU 2798  CE3 TRP D 113    18849  27653  10360    330    -49  -1482       C  
ATOM   2799  CZ2 TRP D 113      67.298  32.536  43.396  1.00161.01           C  
ANISOU 2799  CZ2 TRP D 113    20128  30598  10450    829    390  -1945       C  
ATOM   2800  CZ3 TRP D 113      67.756  31.888  41.105  1.00150.62           C  
ANISOU 2800  CZ3 TRP D 113    18700  28176  10354    559    306  -1474       C  
ATOM   2801  CH2 TRP D 113      66.859  32.126  42.161  1.00156.31           C  
ANISOU 2801  CH2 TRP D 113    19321  29658  10410    798    525  -1694       C  
ATOM   2802  N   PHE D 114      73.058  29.583  42.981  1.00148.63           N  
ANISOU 2802  N   PHE D 114    18493  28044   9937  -1494   -680   -317       N  
ATOM   2803  CA  PHE D 114      72.751  28.252  43.484  1.00149.78           C  
ANISOU 2803  CA  PHE D 114    18438  28634   9837  -1624   -531    219       C  
ATOM   2804  C   PHE D 114      73.891  27.716  44.349  1.00152.27           C  
ANISOU 2804  C   PHE D 114    18806  29173   9878  -1828   -829    498       C  
ATOM   2805  O   PHE D 114      73.651  26.978  45.307  1.00156.05           O  
ANISOU 2805  O   PHE D 114    19240  30202   9848  -1910   -773    771       O  
ATOM   2806  CB  PHE D 114      72.444  27.287  42.333  1.00145.15           C  
ANISOU 2806  CB  PHE D 114    17664  27693   9792  -1707   -400    653       C  
ATOM   2807  CG  PHE D 114      71.084  27.490  41.697  1.00144.10           C  
ANISOU 2807  CG  PHE D 114    17397  27602   9753  -1544    -49    525       C  
ATOM   2808  CD1 PHE D 114      70.133  28.338  42.271  1.00145.85           C  
ANISOU 2808  CD1 PHE D 114    17693  27933   9789  -1251     86    -51       C  
ATOM   2809  CD2 PHE D 114      70.743  26.795  40.539  1.00141.79           C  
ANISOU 2809  CD2 PHE D 114    16911  27227   9734  -1670    119    970       C  
ATOM   2810  CE1 PHE D 114      68.877  28.513  41.682  1.00145.30           C  
ANISOU 2810  CE1 PHE D 114    17451  27960   9798  -1057    399   -164       C  
ATOM   2811  CE2 PHE D 114      69.487  26.958  39.950  1.00141.26           C  
ANISOU 2811  CE2 PHE D 114    16673  27266   9733  -1544    425    864       C  
ATOM   2812  CZ  PHE D 114      68.554  27.820  40.524  1.00142.99           C  
ANISOU 2812  CZ  PHE D 114    16913  27658   9759  -1224    571    301       C  
ATOM   2813  N   VAL D 115      75.124  28.091  44.005  1.00144.28           N  
ANISOU 2813  N   VAL D 115    18964  27463   8391  -1989  -1221    403       N  
ATOM   2814  CA  VAL D 115      76.304  27.766  44.813  1.00146.91           C  
ANISOU 2814  CA  VAL D 115    19324  28009   8487  -2154  -1557    609       C  
ATOM   2815  C   VAL D 115      76.318  28.590  46.113  1.00152.55           C  
ANISOU 2815  C   VAL D 115    20234  29199   8528  -2134  -1675    201       C  
ATOM   2816  O   VAL D 115      76.756  28.107  47.168  1.00156.38           O  
ANISOU 2816  O   VAL D 115    20723  30147   8549  -2242  -1829    441       O  
ATOM   2817  CB  VAL D 115      77.619  27.941  44.000  1.00143.86           C  
ANISOU 2817  CB  VAL D 115    18881  27147   8632  -2259  -1854    672       C  
ATOM   2818  CG1 VAL D 115      78.784  28.341  44.892  1.00147.42           C  
ANISOU 2818  CG1 VAL D 115    19406  27802   8803  -2400  -2235    536       C  
ATOM   2819  CG2 VAL D 115      77.951  26.669  43.247  1.00141.15           C  
ANISOU 2819  CG2 VAL D 115    18346  26636   8650  -2289  -1857   1260       C  
ATOM   2820  N   GLY D 116      75.815  29.823  46.029  1.00161.16           N  
ANISOU 2820  N   GLY D 116    21532  29535  10166  -1941   -445  -1056       N  
ATOM   2821  CA  GLY D 116      75.675  30.707  47.189  1.00166.95           C  
ANISOU 2821  CA  GLY D 116    22500  30697  10235  -1841   -508  -1537       C  
ATOM   2822  C   GLY D 116      74.628  30.236  48.183  1.00170.45           C  
ANISOU 2822  C   GLY D 116    22854  31820  10089  -1692   -168  -1449       C  
ATOM   2823  O   GLY D 116      74.138  31.019  48.995  1.00174.20           O  
ANISOU 2823  O   GLY D 116    23473  32589  10127  -1445    -26  -1949       O  
ATOM   2824  N   ARG D 117      74.271  28.958  48.094  1.00180.09           N  
ANISOU 2824  N   ARG D 117    24301  33489  10635  -3143   1371  -1384       N  
ATOM   2825  CA  ARG D 117      73.466  28.290  49.106  1.00184.19           C  
ANISOU 2825  CA  ARG D 117    24705  34738  10542  -3148   1627  -1118       C  
ATOM   2826  C   ARG D 117      74.139  26.976  49.495  1.00184.19           C  
ANISOU 2826  C   ARG D 117    24605  34828  10551  -3434   1452   -386       C  
ATOM   2827  O   ARG D 117      73.611  25.882  49.266  1.00183.15           O  
ANISOU 2827  O   ARG D 117    24310  34755  10524  -3558   1635    164       O  
ATOM   2828  CB  ARG D 117      72.022  28.087  48.641  1.00183.10           C  
ANISOU 2828  CB  ARG D 117    24373  34727  10469  -2994   2075  -1116       C  
ATOM   2829  CG  ARG D 117      71.217  29.375  48.602  1.00185.20           C  
ANISOU 2829  CG  ARG D 117    24751  35091  10524  -2623   2240  -1859       C  
ATOM   2830  CD  ARG D 117      69.742  29.131  48.849  1.00188.01           C  
ANISOU 2830  CD  ARG D 117    24863  36083  10491  -2452   2691  -1854       C  
ATOM   2831  NE  ARG D 117      69.001  30.391  48.867  1.00190.33           N  
ANISOU 2831  NE  ARG D 117    25278  36429  10609  -2000   2818  -2611       N  
ATOM   2832  CZ  ARG D 117      67.708  30.511  49.156  1.00192.64           C  
ANISOU 2832  CZ  ARG D 117    25347  37195  10654  -1708   3207  -2795       C  
ATOM   2833  NH1 ARG D 117      66.979  29.444  49.463  1.00192.97           N  
ANISOU 2833  NH1 ARG D 117    25003  37737  10581  -1895   3524  -2254       N  
ATOM   2834  NH2 ARG D 117      67.140  31.710  49.141  1.00195.14           N  
ANISOU 2834  NH2 ARG D 117    25831  37484  10828  -1225   3260  -3529       N  
ATOM   2835  N   GLU D 118      75.332  27.119  50.067  1.00185.23           N  
ANISOU 2835  N   GLU D 118    27768  34782   7829  -3759   -463    710       N  
ATOM   2836  CA  GLU D 118      76.109  26.014  50.619  1.00187.21           C  
ANISOU 2836  CA  GLU D 118    27984  35243   7906  -3961   -721   1298       C  
ATOM   2837  C   GLU D 118      75.837  25.871  52.115  1.00193.98           C  
ANISOU 2837  C   GLU D 118    28915  36912   7878  -4009   -701   1351       C  
ATOM   2838  O   GLU D 118      76.150  24.841  52.713  1.00196.39           O  
ANISOU 2838  O   GLU D 118    29180  37510   7930  -4174   -776   1960       O  
ATOM   2839  CB  GLU D 118      77.606  26.249  50.377  1.00186.19           C  
ANISOU 2839  CB  GLU D 118    27898  34775   8069  -4032  -1176   1225       C  
ATOM   2840  CG  GLU D 118      78.184  27.483  51.088  1.00190.24           C  
ANISOU 2840  CG  GLU D 118    28606  35523   8153  -4032  -1438    638       C  
ATOM   2841  CD  GLU D 118      79.491  27.976  50.478  1.00187.94           C  
ANISOU 2841  CD  GLU D 118    28318  34740   8350  -4128  -1806    421       C  
ATOM   2842  OE1 GLU D 118      80.274  27.146  49.964  1.00185.36           O  
ANISOU 2842  OE1 GLU D 118    27804  34169   8455  -4206  -1985    863       O  
ATOM   2843  OE2 GLU D 118      79.739  29.202  50.517  1.00189.14           O  
ANISOU 2843  OE2 GLU D 118    28664  34753   8447  -4125  -1923   -192       O  
ATOM   2844  N   GLN D 119      75.252  26.916  52.698  1.00233.18           N  
ANISOU 2844  N   GLN D 119    36247  43145   9204  -7494   2780  -1121       N  
ATOM   2845  CA  GLN D 119      74.917  26.985  54.125  1.00240.22           C  
ANISOU 2845  CA  GLN D 119    37210  44892   9169  -7482   2856  -1194       C  
ATOM   2846  C   GLN D 119      73.892  25.934  54.544  1.00242.53           C  
ANISOU 2846  C   GLN D 119    37314  45749   9089  -7580   3225   -650       C  
ATOM   2847  O   GLN D 119      74.252  24.872  55.051  1.00244.67           O  
ANISOU 2847  O   GLN D 119    37553  46272   9139  -7817   3105      6       O  
ATOM   2848  CB  GLN D 119      74.405  28.389  54.467  1.00243.03           C  
ANISOU 2848  CB  GLN D 119    37747  45419   9176  -7195   2962  -2054       C  
ATOM   2849  CG  GLN D 119      73.191  28.829  53.643  1.00241.12           C  
ANISOU 2849  CG  GLN D 119    37385  45119   9111  -6937   3415  -2326       C  
ATOM   2850  CD  GLN D 119      73.347  30.213  53.028  1.00239.14           C  
ANISOU 2850  CD  GLN D 119    37347  44294   9223  -6669   3342  -3086       C  
ATOM   2851  OE1 GLN D 119      72.361  30.910  52.790  1.00239.67           O  
ANISOU 2851  OE1 GLN D 119    37398  44428   9239  -6352   3651  -3501       O  
ATOM   2852  NE2 GLN D 119      74.585  30.609  52.753  1.00237.27           N  
ANISOU 2852  NE2 GLN D 119    37304  43498   9351  -6801   2918  -3248       N  
TER    2853      GLN D 119                                                      
HETATM 2854  K     K A   1      71.690  26.567  18.706  1.00 79.42           K  
ANISOU 2854  K     K A   1    10998  12453   6724  -1245  -1612    366       K  
HETATM 2855  K     K A   2      70.401  26.656  15.511  1.00 77.09           K  
ANISOU 2855  K     K A   2    10563  11875   6852  -1278  -1544    285       K  
HETATM 2856  K     K A   3      67.866  26.630   9.156  1.00 72.91           K  
ANISOU 2856  K     K A   3    10089  10946   6668   -827  -1215     80       K  
HETATM 2857  O   HOH B   4      69.203  26.571  12.420  1.00 74.58           O  
ANISOU 2857  O   HOH B   4    10187  11310   6839  -1001  -1356     44       O  
CONECT  381 2855                                                                
CONECT  383 2854                                                                
CONECT  399 2856                                                                
CONECT 1092 2854 2855                                                           
CONECT 1094 2854                                                                
CONECT 1110 2856                                                                
CONECT 1806 2855                                                                
CONECT 1808 2854                                                                
CONECT 1824 2856                                                                
CONECT 2520 2855                                                                
CONECT 2522 2854                                                                
CONECT 2527 2855                                                                
CONECT 2538 2856                                                                
CONECT 2854  383 1092 1094 1808                                                 
CONECT 2854 2522                                                                
CONECT 2855  381 1092 1806 2520                                                 
CONECT 2855 2527                                                                
CONECT 2856  399 1110 1824 2538                                                 
MASTER      333    0    3   12    0    0    0    6 2853    4   18   32          
END                                                                             



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