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***  METAL BINDING PROTEIN 30-APR-15 5A1J  ***

elNémo ID: 200123133304125577

Job options:

ID        	=	 200123133304125577
JOBID     	=	 METAL BINDING PROTEIN 30-APR-15 5A1J
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 BINDING PROTEIN                   30-APR-15   5A1J              
TITLE     PERIPLASMIC BINDING PROTEIN CEUE IN COMPLEX WITH FERRIC 4-LICAM       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENTEROCHELIN UPTAKE PERIPLASMIC BINDING PROTEIN;           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL TRUNCATION, RESIDUES 44-330;                    
COMPND   5 SYNONYM: CEUE;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAMPYLOBACTER JEJUNI;                           
SOURCE   3 ORGANISM_TAXID: 197;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-YSBLIC                                
KEYWDS    METAL BINDING PROTEIN, METAL-BINDING PROTEIN, ENTEROBACTIN UPTAKE,    
KEYWDS   2 IRON, SIDEROPHORE, BINDING PROTEIN, TETRADENTATE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.RAINES,O.V.MOROZ,K.S.WILSON,A.K.DUHME-KLAIR                       
REVDAT   1   13-MAY-15 5A1J    0                                                
SPRSDE     13-MAY-15 5A1J      3ZK3                                             
JRNL        AUTH   D.J.RAINES,O.V.MOROZ,K.S.WILSON,A.DUHME-KLAIR                
JRNL        TITL   INTERACTIONS OF A PERIPLASMIC BINDING PROTEIN WITH A         
JRNL        TITL 2 TETRADENTATE SIDEROPHORE MIMIC.                              
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  52  4595 2013              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   23512642                                                     
JRNL        DOI    10.1002/ANIE.201300751                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.75                          
REMARK   3   NUMBER OF REFLECTIONS             : 34006                          
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) : 0.26660                         
REMARK   3   R VALUE            (WORKING SET) : 0.26422                         
REMARK   3   FREE R VALUE                     : 0.31242                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1773                            
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) : 1.601                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.643                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1910                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.290                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.399                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2264                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 78                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.566                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.83                                                
REMARK   3    B22 (A**2) : 1.39                                                 
REMARK   3    B33 (A**2) : 6.44                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.029         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.029         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.144         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.866                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2328 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2351 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3145 ; 2.370 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5443 ; 1.070 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   295 ; 7.343 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    97 ;37.219 ;26.907       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   451 ;19.736 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ; 8.236 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   363 ; 0.132 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2610 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   472 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
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):  1159 ; 1.549 ; 1.586       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1158 ; 1.549 ; 1.586       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1449 ; 2.157 ; 2.381       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1169 ; 1.459 ; 1.672       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.854                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H, L, K                                        
REMARK   3      TWIN FRACTION : 0.146                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :  1                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    23        A   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3942   2.3768   2.4774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0664 T22:   0.0605                                     
REMARK   3      T33:   0.0030 T12:   0.0009                                     
REMARK   3      T13:   0.0030 T23:  -0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1684 L22:   0.1675                                     
REMARK   3      L33:   0.1035 L12:   0.1017                                     
REMARK   3      L13:   0.0889 L23:   0.1292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0071 S12:  -0.0674 S13:  -0.0058                       
REMARK   3      S21:  -0.0110 S22:  -0.0130 S23:   0.0054                       
REMARK   3      S31:  -0.0006 S32:  -0.0196 S33:   0.0060                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. POOR REFINEMENT STATISTICS BECAUSE OF            
REMARK   3   SPLIT SPOTS AND TWINNING                                           
REMARK   4                                                                      
REMARK   4 5A1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-APR-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-63683.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97840                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 204289                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.61                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.96                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.7                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3                                  
REMARK 200  R MERGE FOR SHELL          (I) : 0.42                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2CHU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM NITRATE, 0.1M BIS            
REMARK 280  TRIS PROPANE PH 7.5, 20% PEG 3350                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       30.21000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.65000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.44500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.65000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.21000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.44500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS A   166     OD1  ASP A   169              2.07            
REMARK 500   OH   TYR A   243     O    HOH A  2037              2.08            
REMARK 500   O    HOH A  2017     O    HOH A  2051              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  58   CB  -  CG  -  CD1 ANGL. DEV. =  12.3 DEGREES          
REMARK 500    LEU A 112   CB  -  CG  -  CD1 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    LEU A 188   CB  -  CG  -  CD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A 205   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  77       87.44    -64.87                                   
REMARK 500    ASN A  80       55.64   -117.62                                   
REMARK 500    SER A 116     -156.06   -139.41                                   
REMARK 500    SER A 194     -134.79     62.53                                   
REMARK 500    ASN A 240       58.21     37.25                                   
REMARK 500    LYS A 277       44.65     39.61                                   
REMARK 500    LEU A 289      -74.17    -74.66                                   
REMARK 500    ASN A 293       38.80    -93.59                                   
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                              FE A1311  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 227   NE2                                                    
REMARK 620 2 TYR A 288   OH   77.9                                              
REMARK 620 3 LCM A1312   O24  94.4  97.4                                        
REMARK 620 4 LCM A1312   O26 167.7  90.3  90.8                                  
REMARK 620 5 LCM A1312   O23  93.0 170.7  85.0  98.7                            
REMARK 620 6 LCM A1312   O25 100.2 102.1 157.7  78.4  77.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A1311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LCM A1312                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL TRUNCATION.  FIRST MET FROM CLONING                       
DBREF  5A1J A   24   310  UNP    Q0P8Q4   Q0P8Q4_CAMJE    44    330             
SEQADV 5A1J MET A   23  UNP  Q0P8Q4              EXPRESSION TAG                 
SEQRES   1 A  288  MET LEU PRO ILE SER MET SER ASP GLU GLY ASP SER PHE          
SEQRES   2 A  288  LEU VAL LYS ASP SER LEU GLY GLU ASN LYS ILE PRO LYS          
SEQRES   3 A  288  ASN PRO SER LYS VAL VAL ILE LEU ASP LEU GLY ILE LEU          
SEQRES   4 A  288  ASP THR PHE ASP ALA LEU LYS LEU ASN ASP LYS VAL VAL          
SEQRES   5 A  288  GLY VAL PRO ALA LYS ASN LEU PRO LYS TYR LEU GLN GLN          
SEQRES   6 A  288  PHE LYS ASN LYS PRO SER VAL GLY GLY VAL GLN GLN VAL          
SEQRES   7 A  288  ASP PHE GLU ALA ILE ASN ALA LEU LYS PRO ASP LEU ILE          
SEQRES   8 A  288  ILE ILE SER GLY ARG GLN SER LYS PHE TYR ASP LYS LEU          
SEQRES   9 A  288  LYS GLU ILE ALA PRO THR LEU PHE VAL GLY LEU ASP ASN          
SEQRES  10 A  288  ALA ASN PHE LEU SER SER PHE GLU ASN ASN VAL LEU SER          
SEQRES  11 A  288  VAL ALA LYS LEU TYR GLY LEU GLU LYS GLU ALA LEU GLU          
SEQRES  12 A  288  LYS ILE SER ASP ILE LYS ASN GLU ILE GLU LYS ALA LYS          
SEQRES  13 A  288  SER ILE VAL ASP GLU ASP LYS LYS ALA LEU ILE ILE LEU          
SEQRES  14 A  288  THR ASN SER ASN LYS ILE SER ALA PHE GLY PRO GLN SER          
SEQRES  15 A  288  ARG PHE GLY ILE ILE HIS ASP VAL LEU GLY ILE ASN ALA          
SEQRES  16 A  288  VAL ASP GLU ASN ILE LYS VAL GLY THR HIS GLY LYS SER          
SEQRES  17 A  288  ILE ASN SER GLU PHE ILE LEU GLU LYS ASN PRO ASP TYR          
SEQRES  18 A  288  ILE PHE VAL VAL ASP ARG ASN VAL ILE LEU GLY ASN LYS          
SEQRES  19 A  288  GLU ARG ALA GLN GLY ILE LEU ASP ASN ALA LEU VAL ALA          
SEQRES  20 A  288  LYS THR LYS ALA ALA GLN ASN LYS LYS ILE ILE TYR LEU          
SEQRES  21 A  288  ASP PRO GLU TYR TRP TYR LEU ALA SER GLY ASN GLY LEU          
SEQRES  22 A  288  GLU SER LEU LYS THR MET ILE LEU GLU ILE LYS ASN ALA          
SEQRES  23 A  288  VAL LYS                                                      
HET     FE  A1311       1                                                       
HET    LCM  A1312      26                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     LCM N,N'-BUTANE-1,4-DIYLBIS(2,3-                                     
HETNAM   2 LCM  DIHYDROXYBENZAMIDE)                                             
HETSYN     LCM 4-LICAM                                                          
FORMUL   2   FE    FE 3+                                                        
FORMUL   3  LCM    C18 H20 N2 O6                                                
FORMUL   4  HOH   *78(H2 O)                                                     
HELIX    1   1 ASP A   57  LEU A   67  1                                  11    
HELIX    2   2 LEU A   69  ASP A   71  5                                   3    
HELIX    3   3 PRO A   77  LEU A   81  5                                   5    
HELIX    4   4 PRO A   82  GLN A   86  5                                   5    
HELIX    5   5 ASP A  101  LYS A  109  1                                   9    
HELIX    6   6 SER A  116  LYS A  121  5                                   6    
HELIX    7   7 PHE A  122  ALA A  130  1                                   9    
HELIX    8   8 ASN A  141  TYR A  157  1                                  17    
HELIX    9   9 LEU A  159  ILE A  180  1                                  22    
HELIX   10  10 GLY A  207  VAL A  212  1                                   6    
HELIX   11  11 ASN A  232  ASN A  240  1                                   9    
HELIX   12  12 ARG A  249  GLY A  254  1                                   6    
HELIX   13  13 ARG A  258  ASP A  264  1                                   7    
HELIX   14  14 ASN A  265  LYS A  270  1                                   6    
HELIX   15  15 THR A  271  ASN A  276  1                                   6    
HELIX   16  16 ASP A  283  TYR A  288  1                                   6    
HELIX   17  17 GLY A  294  LYS A  310  1                                  17    
SHEET    1  AA 3 SER A  27  ASP A  30  0                                        
SHEET    2  AA 3 SER A  34  LYS A  38 -1  O  LEU A  36   N  SER A  29           
SHEET    3  AA 3 GLU A  43  PRO A  47 -1  O  ASN A  44   N  VAL A  37           
SHEET    1  AB 4 VAL A  73  GLY A  75  0                                        
SHEET    2  AB 4 VAL A  53  ILE A  55  1  O  VAL A  53   N  GLY A  75           
SHEET    3  AB 4 LEU A 112  ILE A 115  1  O  LEU A 112   N  VAL A  54           
SHEET    4  AB 4 THR A 132  PHE A 134  1  O  LEU A 133   N  ILE A 115           
SHEET    1  AC 2 ASN A 216  ALA A 217  0                                        
SHEET    2  AC 2 LYS A 186  ASN A 193  1  N  ALA A 187   O  ASN A 216           
SHEET    1  AD 5 LYS A 229  ILE A 231  0                                        
SHEET    2  AD 5 LYS A 196  PHE A 200 -1  O  ILE A 197   N  ILE A 231           
SHEET    3  AD 5 LYS A 186  ASN A 193 -1  O  ILE A 189   N  PHE A 200           
SHEET    4  AD 5 TYR A 243  ASP A 248  1  O  TYR A 243   N  LEU A 188           
SHEET    5  AD 5 ILE A 279  LEU A 282  1  O  ILE A 280   N  VAL A 246           
SHEET    1  AE 4 LYS A 229  ILE A 231  0                                        
SHEET    2  AE 4 LYS A 196  PHE A 200 -1  O  ILE A 197   N  ILE A 231           
SHEET    3  AE 4 LYS A 186  ASN A 193 -1  O  ILE A 189   N  PHE A 200           
SHEET    4  AE 4 ASN A 216  ALA A 217  1  O  ASN A 216   N  ALA A 187           
LINK        FE    FE A1311                 NE2 HIS A 227     1555   1555  2.21  
LINK        FE    FE A1311                 OH  TYR A 288     1555   1555  1.84  
LINK        FE    FE A1311                 O24 LCM A1312     1555   1555  1.86  
LINK        FE    FE A1311                 O26 LCM A1312     1555   1555  2.17  
LINK        FE    FE A1311                 O23 LCM A1312     1555   1555  1.94  
LINK        FE    FE A1311                 O25 LCM A1312     1555   1555  2.13  
SITE     1 AC1  3 HIS A 227  TYR A 288  LCM A1312                               
SITE     1 AC2 10 MET A  28  LYS A  38  GLN A  98  ARG A 118                    
SITE     2 AC2 10 ARG A 205  HIS A 227  ARG A 249  LEU A 253                    
SITE     3 AC2 10 TYR A 288   FE A1311                                          
CRYST1   60.420   66.890   67.300  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016551  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014950  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014859        0.00000                         
ATOM      1  N   MET A  23       9.804  12.030  -8.188  1.00 30.32           N  
ANISOU    1  N   MET A  23     4272   3823   3425    -45     59    -85       N  
ATOM      2  CA  MET A  23       9.487  12.915  -7.027  1.00 29.46           C  
ANISOU    2  CA  MET A  23     4151   3723   3319    -35     50    -90       C  
ATOM      3  C   MET A  23      10.764  13.436  -6.370  1.00 27.58           C  
ANISOU    3  C   MET A  23     3904   3494   3082    -39     61    -98       C  
ATOM      4  O   MET A  23      11.722  12.689  -6.160  1.00 29.72           O  
ANISOU    4  O   MET A  23     4163   3773   3355    -42     75    -99       O  
ATOM      5  CB  MET A  23       8.672  12.136  -5.979  1.00 28.55           C  
ANISOU    5  CB  MET A  23     4011   3624   3210    -20     46    -86       C  
ATOM      6  CG  MET A  23       8.640  12.837  -4.631  1.00 31.51           C  
ANISOU    6  CG  MET A  23     4369   4015   3587    -11     43    -92       C  
ATOM      7  SD  MET A  23       7.306  12.336  -3.539  1.00 31.96           S  
ANISOU    7  SD  MET A  23     4405   4090   3649      4     33    -90       S  
ATOM      8  CE  MET A  23       7.949  10.809  -2.880  1.00 32.94           C  
ANISOU    8  CE  MET A  23     4509   4232   3775      4     46    -81       C  
ATOM      9  N   LEU A  24      10.779  14.722  -6.037  1.00 27.07           N  
ANISOU    9  N   LEU A  24     3845   3426   3016    -39     55   -105       N  
ATOM     10  CA  LEU A  24      11.900  15.266  -5.290  1.00 23.44           C  
ANISOU   10  CA  LEU A  24     3374   2976   2557    -41     64   -113       C  
ATOM     11  C   LEU A  24      12.011  14.582  -3.930  1.00 21.56           C  
ANISOU   11  C   LEU A  24     3107   2761   2325    -29     68   -113       C  
ATOM     12  O   LEU A  24      11.025  14.392  -3.261  1.00 22.26           O  
ANISOU   12  O   LEU A  24     3184   2859   2416    -18     59   -110       O  
ATOM     13  CB  LEU A  24      11.755  16.783  -5.134  1.00 23.11           C  
ANISOU   13  CB  LEU A  24     3341   2925   2513    -42     54   -121       C  
ATOM     14  CG  LEU A  24      12.960  17.662  -5.508  0.50 22.56           C  
ANISOU   14  CG  LEU A  24     3285   2848   2441    -57     63   -128       C  
ATOM     15  CD1 LEU A  24      13.967  17.067  -6.503  0.50 21.78           C  
ANISOU   15  CD1 LEU A  24     3197   2742   2336    -74     79   -128       C  
ATOM     16  CD2 LEU A  24      12.394  18.966  -6.059  0.50 22.24           C  
ANISOU   16  CD2 LEU A  24     3267   2787   2397    -61     48   -130       C  
ATOM     17  N   PRO A  25      13.227  14.169  -3.571  1.00 22.91           N  
ANISOU   17  N   PRO A  25     3265   2940   2497    -33     81   -117       N  
ATOM     18  CA  PRO A  25      13.483  13.599  -2.267  1.00 20.53           C  
ANISOU   18  CA  PRO A  25     2938   2660   2200    -24     83   -116       C  
ATOM     19  C   PRO A  25      13.484  14.688  -1.206  1.00 18.38           C  
ANISOU   19  C   PRO A  25     2657   2399   1928    -18     78   -124       C  
ATOM     20  O   PRO A  25      13.357  15.873  -1.484  1.00 16.67           O  
ANISOU   20  O   PRO A  25     2452   2172   1709    -21     74   -131       O  
ATOM     21  CB  PRO A  25      14.867  12.964  -2.429  1.00 21.67           C  
ANISOU   21  CB  PRO A  25     3077   2807   2349    -31     97   -119       C  
ATOM     22  CG  PRO A  25      15.527  13.718  -3.512  1.00 22.19           C  
ANISOU   22  CG  PRO A  25     3164   2857   2411    -46    104   -127       C  
ATOM     23  CD  PRO A  25      14.473  14.417  -4.317  1.00 22.13           C  
ANISOU   23  CD  PRO A  25     3178   2833   2397    -48     94   -123       C  
ATOM     24  N   ILE A  26      13.581  14.289   0.053  1.00 17.37           N  
ANISOU   24  N   ILE A  26     2507   2291   1802    -10     78   -124       N  
ATOM     25  CA  ILE A  26      13.729  15.268   1.105  1.00 16.19           C  
ANISOU   25  CA  ILE A  26     2346   2154   1652     -6     76   -133       C  
ATOM     26  C   ILE A  26      15.234  15.563   1.270  1.00 15.73           C  
ANISOU   26  C   ILE A  26     2285   2097   1596    -12     86   -141       C  
ATOM     27  O   ILE A  26      16.028  14.641   1.244  1.00 15.71           O  
ANISOU   27  O   ILE A  26     2275   2098   1597    -15     94   -139       O  
ATOM     28  CB  ILE A  26      13.166  14.701   2.409  1.00 14.96           C  
ANISOU   28  CB  ILE A  26     2169   2021   1496      4     71   -129       C  
ATOM     29  CG1 ILE A  26      11.690  14.303   2.297  1.00 16.63           C  
ANISOU   29  CG1 ILE A  26     2382   2233   1705      9     62   -122       C  
ATOM     30  CG2 ILE A  26      13.280  15.741   3.525  1.00 16.07           C  
ANISOU   30  CG2 ILE A  26     2297   2175   1634      8     69   -141       C  
ATOM     31  CD1 ILE A  26      11.245  13.297   3.345  1.00 16.35           C  
ANISOU   31  CD1 ILE A  26     2327   2218   1667     14     60   -114       C  
ATOM     32  N   SER A  27      15.620  16.810   1.463  1.00 16.76           N  
ANISOU   32  N   SER A  27     2418   2225   1726    -14     86   -153       N  
ATOM     33  CA  SER A  27      17.052  17.133   1.638  1.00 18.31           C  
ANISOU   33  CA  SER A  27     2610   2423   1925    -21     97   -162       C  
ATOM     34  C   SER A  27      17.130  17.904   2.986  1.00 17.23           C  
ANISOU   34  C   SER A  27     2455   2303   1787    -13     93   -171       C  
ATOM     35  O   SER A  27      16.211  18.686   3.337  1.00 15.71           O  
ANISOU   35  O   SER A  27     2263   2113   1594     -7     83   -174       O  
ATOM     36  CB  SER A  27      17.599  18.013   0.489  1.00 19.85           C  
ANISOU   36  CB  SER A  27     2826   2598   2118    -34    103   -169       C  
ATOM     37  OG  SER A  27      17.299  17.546  -0.823  1.00 24.71           O  
ANISOU   37  OG  SER A  27     3461   3196   2730    -43    104   -162       O  
ATOM     38  N   MET A  28      18.163  17.635   3.788  1.00 15.18           N  
ANISOU   38  N   MET A  28     2180   2058   1531    -12     99   -175       N  
ATOM     39  CA  MET A  28      18.222  18.281   5.120  1.00 15.01           C  
ANISOU   39  CA  MET A  28     2141   2055   1508     -5     95   -183       C  
ATOM     40  C   MET A  28      19.590  18.900   5.363  1.00 14.46           C  
ANISOU   40  C   MET A  28     2067   1986   1443    -10    103   -196       C  
ATOM     41  O   MET A  28      20.565  18.369   4.918  1.00 15.93           O  
ANISOU   41  O   MET A  28     2254   2167   1633    -16    112   -197       O  
ATOM     42  CB  MET A  28      17.915  17.284   6.317  1.00 16.18           C  
ANISOU   42  CB  MET A  28     2269   2226   1654      3     90   -175       C  
ATOM     43  CG  MET A  28      16.654  16.409   6.170  1.00 16.79           C  
ANISOU   43  CG  MET A  28     2348   2304   1727      7     84   -162       C  
ATOM     44  SD  MET A  28      16.423  15.059   7.297  1.00 21.08           S  
ANISOU   44  SD  MET A  28     2873   2870   2266     12     79   -149       S  
ATOM     45  CE  MET A  28      16.427  16.005   8.824  1.00 19.28           C  
ANISOU   45  CE  MET A  28     2628   2666   2032     16     76   -160       C  
ATOM     46  N   SER A  29      19.649  20.036   6.100  1.00 12.98           N  
ANISOU   46  N   SER A  29     1872   1805   1254     -8    100   -208       N  
ATOM     47  CA  SER A  29      20.896  20.632   6.411  1.00 13.74           C  
ANISOU   47  CA  SER A  29     1963   1904   1355    -12    108   -220       C  
ATOM     48  C   SER A  29      20.851  20.835   7.884  1.00 14.83           C  
ANISOU   48  C   SER A  29     2079   2065   1489     -3    102   -225       C  
ATOM     49  O   SER A  29      19.897  21.402   8.328  1.00 15.53           O  
ANISOU   49  O   SER A  29     2166   2160   1576      3     94   -227       O  
ATOM     50  CB  SER A  29      21.045  22.020   5.761  1.00 14.31           C  
ANISOU   50  CB  SER A  29     2050   1959   1427    -20    109   -231       C  
ATOM     51  OG  SER A  29      22.321  22.508   6.104  1.00 14.54           O  
ANISOU   51  OG  SER A  29     2073   1992   1461    -24    117   -244       O  
ATOM     52  N   ASP A  30      21.880  20.333   8.568  1.00 14.87           N  
ANISOU   52  N   ASP A  30     2069   2083   1497     -2    106   -228       N  
ATOM     53  CA  ASP A  30      22.006  20.381  10.042  1.00 17.26           C  
ANISOU   53  CA  ASP A  30     2351   2409   1796      5    101   -232       C  
ATOM     54  C   ASP A  30      22.408  21.819  10.396  1.00 17.49           C  
ANISOU   54  C   ASP A  30     2379   2440   1828      4    103   -250       C  
ATOM     55  O   ASP A  30      23.401  22.349   9.922  1.00 16.56           O  
ANISOU   55  O   ASP A  30     2265   2310   1716     -2    111   -260       O  
ATOM     56  CB  ASP A  30      23.050  19.372  10.513  1.00 18.53           C  
ANISOU   56  CB  ASP A  30     2500   2579   1961      6    103   -229       C  
ATOM     57  CG  ASP A  30      23.596  19.700  11.872  1.00 18.99           C  
ANISOU   57  CG  ASP A  30     2540   2659   2017     11     99   -237       C  
ATOM     58  OD1 ASP A  30      22.789  20.072  12.773  1.00 21.12           O  
ANISOU   58  OD1 ASP A  30     2802   2945   2278     15     92   -238       O  
ATOM     59  OD2 ASP A  30      24.843  19.637  11.987  1.00 22.40           O  
ANISOU   59  OD2 ASP A  30     2965   3090   2456      9    103   -246       O  
ATOM     60  N   GLU A  31      21.603  22.439  11.235  1.00 15.27           N  
ANISOU   60  N   GLU A  31     2088   2171   1541     10     96   -254       N  
ATOM     61  CA  GLU A  31      21.732  23.810  11.700  1.00 15.49           C  
ANISOU   61  CA  GLU A  31     2112   2202   1571     11     95   -271       C  
ATOM     62  C   GLU A  31      21.802  23.875  13.234  1.00 15.19           C  
ANISOU   62  C   GLU A  31     2052   2192   1528     18     91   -278       C  
ATOM     63  O   GLU A  31      21.394  24.877  13.794  1.00 15.95           O  
ANISOU   63  O   GLU A  31     2142   2296   1624     21     87   -291       O  
ATOM     64  CB  GLU A  31      20.500  24.629  11.318  1.00 15.49           C  
ANISOU   64  CB  GLU A  31     2122   2192   1572     14     87   -275       C  
ATOM     65  CG  GLU A  31      20.161  24.651   9.851  1.00 15.95           C  
ANISOU   65  CG  GLU A  31     2204   2222   1633      8     88   -267       C  
ATOM     66  CD  GLU A  31      21.305  25.253   9.057  1.00 15.24           C  
ANISOU   66  CD  GLU A  31     2127   2115   1549     -3     96   -274       C  
ATOM     67  OE1 GLU A  31      21.971  26.242   9.483  1.00 14.16           O  
ANISOU   67  OE1 GLU A  31     1984   1979   1416     -4     98   -288       O  
ATOM     68  OE2 GLU A  31      21.509  24.708   7.995  1.00 17.65           O  
ANISOU   68  OE2 GLU A  31     2447   2404   1855    -10    101   -265       O  
ATOM     69  N   GLY A  32      22.286  22.810  13.852  1.00 17.04           N  
ANISOU   69  N   GLY A  32     2276   2441   1758     19     90   -269       N  
ATOM     70  CA  GLY A  32      22.678  22.856  15.250  1.00 16.29           C  
ANISOU   70  CA  GLY A  32     2161   2372   1657     22     87   -276       C  
ATOM     71  C   GLY A  32      21.513  22.486  16.150  1.00 17.82           C  
ANISOU   71  C   GLY A  32     2346   2587   1838     25     80   -270       C  
ATOM     72  O   GLY A  32      21.494  21.351  16.671  1.00 15.82           O  
ANISOU   72  O   GLY A  32     2087   2347   1577     25     76   -256       O  
ATOM     73  N   ASP A  33      20.560  23.414  16.334  1.00 17.10           N  
ANISOU   73  N   ASP A  33     2252   2499   1745     27     78   -281       N  
ATOM     74  CA  ASP A  33      19.342  23.163  17.134  1.00 18.31           C  
ANISOU   74  CA  ASP A  33     2396   2675   1887     29     72   -279       C  
ATOM     75  C   ASP A  33      18.165  22.626  16.284  1.00 17.85           C  
ANISOU   75  C   ASP A  33     2349   2604   1828     29     70   -267       C  
ATOM     76  O   ASP A  33      17.061  22.348  16.806  1.00 15.80           O  
ANISOU   76  O   ASP A  33     2083   2360   1560     29     67   -266       O  
ATOM     77  CB  ASP A  33      18.900  24.430  17.825  1.00 20.70           C  
ANISOU   77  CB  ASP A  33     2688   2989   2190     31     70   -300       C  
ATOM     78  CG  ASP A  33      18.312  25.425  16.885  1.00 21.61           C  
ANISOU   78  CG  ASP A  33     2814   3081   2317     34     69   -310       C  
ATOM     79  OD1 ASP A  33      18.614  25.360  15.659  1.00 24.32           O  
ANISOU   79  OD1 ASP A  33     3176   3398   2669     32     71   -303       O  
ATOM     80  OD2 ASP A  33      17.578  26.320  17.389  1.00 28.26           O  
ANISOU   80  OD2 ASP A  33     3646   3932   3159     38     64   -327       O  
ATOM     81  N   SER A  34      18.391  22.561  14.978  1.00 17.46           N  
ANISOU   81  N   SER A  34     2318   2527   1789     28     73   -261       N  
ATOM     82  CA  SER A  34      17.352  22.201  14.037  1.00 18.08           C  
ANISOU   82  CA  SER A  34     2410   2591   1870     28     70   -252       C  
ATOM     83  C   SER A  34      17.975  21.750  12.729  1.00 15.66           C  
ANISOU   83  C   SER A  34     2121   2258   1570     24     75   -241       C  
ATOM     84  O   SER A  34      19.191  21.807  12.498  1.00 14.73           O  
ANISOU   84  O   SER A  34     2006   2133   1457     21     81   -243       O  
ATOM     85  CB  SER A  34      16.461  23.397  13.722  1.00 17.33           C  
ANISOU   85  CB  SER A  34     2319   2487   1781     32     65   -266       C  
ATOM     86  OG  SER A  34      17.192  24.572  13.540  1.00 21.04           O  
ANISOU   86  OG  SER A  34     2791   2944   2258     31     67   -281       O  
ATOM     87  N   PHE A  35      17.067  21.413  11.828  1.00 15.75           N  
ANISOU   87  N   PHE A  35     2145   2255   1583     24     72   -232       N  
ATOM     88  CA  PHE A  35      17.395  21.147  10.476  1.00 16.22           C  
ANISOU   88  CA  PHE A  35     2224   2290   1649     20     76   -224       C  
ATOM     89  C   PHE A  35      16.683  22.121   9.505  1.00 15.49           C  
ANISOU   89  C   PHE A  35     2148   2174   1561     20     71   -231       C  
ATOM     90  O   PHE A  35      15.515  22.466   9.685  1.00 16.06           O  
ANISOU   90  O   PHE A  35     2218   2250   1633     25     63   -235       O  
ATOM     91  CB  PHE A  35      16.937  19.733  10.154  1.00 15.11           C  
ANISOU   91  CB  PHE A  35     2087   2150   1505     20     75   -206       C  
ATOM     92  CG  PHE A  35      17.808  18.612  10.733  1.00 17.03           C  
ANISOU   92  CG  PHE A  35     2320   2405   1746     18     78   -197       C  
ATOM     93  CD1 PHE A  35      19.029  18.243  10.126  1.00 17.17           C  
ANISOU   93  CD1 PHE A  35     2342   2410   1770     14     85   -196       C  
ATOM     94  CD2 PHE A  35      17.435  17.944  11.902  1.00 17.35           C  
ANISOU   94  CD2 PHE A  35     2346   2470   1778     20     74   -190       C  
ATOM     95  CE1 PHE A  35      19.840  17.230  10.657  1.00 17.89           C  
ANISOU   95  CE1 PHE A  35     2424   2512   1863     14     85   -189       C  
ATOM     96  CE2 PHE A  35      18.236  16.924  12.420  1.00 18.51           C  
ANISOU   96  CE2 PHE A  35     2485   2626   1923     19     73   -181       C  
ATOM     97  CZ  PHE A  35      19.437  16.571  11.809  1.00 17.82           C  
ANISOU   97  CZ  PHE A  35     2402   2524   1845     17     78   -180       C  
ATOM     98  N   LEU A  36      17.342  22.478   8.400  1.00 14.20           N  
ANISOU   98  N   LEU A  36     2003   1988   1403     13     75   -231       N  
ATOM     99  CA  LEU A  36      16.668  23.149   7.350  1.00 15.07           C  
ANISOU   99  CA  LEU A  36     2133   2075   1518     11     69   -232       C  
ATOM    100  C   LEU A  36      16.317  22.053   6.348  1.00 14.72           C  
ANISOU  100  C   LEU A  36     2102   2020   1472      7     71   -215       C  
ATOM    101  O   LEU A  36      17.210  21.436   5.805  1.00 14.65           O  
ANISOU  101  O   LEU A  36     2100   2005   1463      0     80   -209       O  
ATOM    102  CB  LEU A  36      17.541  24.201   6.695  1.00 16.19           C  
ANISOU  102  CB  LEU A  36     2289   2198   1665      2     73   -240       C  
ATOM    103  CG  LEU A  36      16.900  25.056   5.591  1.00 16.32           C  
ANISOU  103  CG  LEU A  36     2329   2187   1684     -2     63   -241       C  
ATOM    104  CD1 LEU A  36      15.610  25.666   6.067  1.00 15.62           C  
ANISOU  104  CD1 LEU A  36     2233   2102   1599      9     48   -248       C  
ATOM    105  CD2 LEU A  36      17.869  26.004   4.897  1.00 17.89           C  
ANISOU  105  CD2 LEU A  36     2544   2367   1885    -14     68   -247       C  
ATOM    106  N   VAL A  37      15.043  21.914   6.054  1.00 15.36           N  
ANISOU  106  N   VAL A  37     2188   2096   1552     12     62   -211       N  
ATOM    107  CA  VAL A  37      14.547  20.696   5.364  1.00 15.53           C  
ANISOU  107  CA  VAL A  37     2217   2113   1571     11     62   -195       C  
ATOM    108  C   VAL A  37      13.739  21.073   4.087  1.00 16.75           C  
ANISOU  108  C   VAL A  37     2395   2242   1728      8     54   -192       C  
ATOM    109  O   VAL A  37      12.815  21.896   4.094  1.00 16.31           O  
ANISOU  109  O   VAL A  37     2342   2181   1676     14     42   -200       O  
ATOM    110  CB  VAL A  37      13.732  19.825   6.367  1.00 16.16           C  
ANISOU  110  CB  VAL A  37     2277   2216   1646     18     60   -190       C  
ATOM    111  CG1 VAL A  37      13.147  18.536   5.808  1.00 15.50           C  
ANISOU  111  CG1 VAL A  37     2198   2129   1560     18     60   -174       C  
ATOM    112  CG2 VAL A  37      14.611  19.394   7.527  1.00 15.86           C  
ANISOU  112  CG2 VAL A  37     2220   2200   1604     19     66   -190       C  
ATOM    113  N   LYS A  38      14.154  20.521   2.946  1.00 16.28           N  
ANISOU  113  N   LYS A  38     2353   2166   1667      0     60   -183       N  
ATOM    114  CA  LYS A  38      13.430  20.668   1.674  1.00 17.62           C  
ANISOU  114  CA  LYS A  38     2546   2313   1837     -4     52   -177       C  
ATOM    115  C   LYS A  38      12.776  19.396   1.214  1.00 16.88           C  
ANISOU  115  C   LYS A  38     2453   2219   1741     -3     52   -164       C  
ATOM    116  O   LYS A  38      13.425  18.406   1.216  1.00 14.43           O  
ANISOU  116  O   LYS A  38     2138   1916   1429     -6     63   -157       O  
ATOM    117  CB  LYS A  38      14.384  21.090   0.560  1.00 18.32           C  
ANISOU  117  CB  LYS A  38     2656   2380   1923    -19     59   -177       C  
ATOM    118  CG  LYS A  38      13.891  20.865  -0.846  1.00 19.74           C  
ANISOU  118  CG  LYS A  38     2861   2538   2100    -27     55   -168       C  
ATOM    119  CD  LYS A  38      14.631  21.639  -1.898  1.00 21.90           C  
ANISOU  119  CD  LYS A  38     3160   2790   2370    -43     58   -170       C  
ATOM    120  CE  LYS A  38      13.982  21.381  -3.254  1.00 21.40           C  
ANISOU  120  CE  LYS A  38     3123   2706   2302    -51     52   -160       C  
ATOM    121  NZ  LYS A  38      14.574  20.238  -4.035  1.00 22.29           N  
ANISOU  121  NZ  LYS A  38     3241   2819   2410    -61     67   -153       N  
ATOM    122  N   ASP A  39      11.497  19.492   0.843  1.00 19.66           N  
ANISOU  122  N   ASP A  39     2812   2563   2094      3     40   -162       N  
ATOM    123  CA  ASP A  39      10.713  18.365   0.313  1.00 21.16           C  
ANISOU  123  CA  ASP A  39     3006   2751   2283      5     38   -150       C  
ATOM    124  C   ASP A  39       9.975  18.829  -0.977  1.00 21.18           C  
ANISOU  124  C   ASP A  39     3033   2727   2286      1     26   -147       C  
ATOM    125  O   ASP A  39      10.240  19.943  -1.469  1.00 24.58           O  
ANISOU  125  O   ASP A  39     3481   3141   2718     -4     21   -153       O  
ATOM    126  CB  ASP A  39       9.829  17.668   1.416  1.00 20.91           C  
ANISOU  126  CB  ASP A  39     2951   2743   2252     15     35   -149       C  
ATOM    127  CG  ASP A  39       9.028  18.645   2.297  1.00 23.88           C  
ANISOU  127  CG  ASP A  39     3313   3127   2631     24     25   -162       C  
ATOM    128  OD1 ASP A  39       9.632  19.307   3.175  1.00 29.63           O  
ANISOU  128  OD1 ASP A  39     4030   3868   3360     25     28   -172       O  
ATOM    129  OD2 ASP A  39       7.786  18.740   2.177  1.00 28.32           O  
ANISOU  129  OD2 ASP A  39     3876   3688   3198     30     13   -165       O  
ATOM    130  N   SER A  40       9.113  17.974  -1.530  1.00 23.49           N  
ANISOU  130  N   SER A  40     3331   3016   2579      4     22   -138       N  
ATOM    131  CA  SER A  40       8.497  18.152  -2.836  1.00 25.84           C  
ANISOU  131  CA  SER A  40     3653   3289   2875     -1     12   -134       C  
ATOM    132  C   SER A  40       7.601  19.375  -2.886  1.00 25.44           C  
ANISOU  132  C   SER A  40     3610   3226   2831      5     -8   -143       C  
ATOM    133  O   SER A  40       7.406  19.941  -3.956  1.00 27.59           O  
ANISOU  133  O   SER A  40     3908   3474   3102     -1    -18   -141       O  
ATOM    134  CB  SER A  40       7.692  16.883  -3.248  1.00 25.20           C  
ANISOU  134  CB  SER A  40     3571   3209   2793      2     11   -123       C  
ATOM    135  OG  SER A  40       8.110  15.751  -2.479  1.00 31.27           O  
ANISOU  135  OG  SER A  40     4319   3999   3561      4     24   -118       O  
ATOM    136  N   LEU A  41       7.051  19.746  -1.727  1.00 24.76           N  
ANISOU  136  N   LEU A  41     3501   3155   2750     17    -13   -154       N  
ATOM    137  CA  LEU A  41       6.070  20.814  -1.565  1.00 22.72           C  
ANISOU  137  CA  LEU A  41     3242   2888   2501     26    -33   -166       C  
ATOM    138  C   LEU A  41       6.694  22.085  -0.979  1.00 22.75           C  
ANISOU  138  C   LEU A  41     3243   2892   2509     26    -35   -179       C  
ATOM    139  O   LEU A  41       6.230  23.193  -1.270  1.00 22.00           O  
ANISOU  139  O   LEU A  41     3159   2779   2421     29    -53   -188       O  
ATOM    140  CB  LEU A  41       4.951  20.334  -0.616  1.00 23.16           C  
ANISOU  140  CB  LEU A  41     3273   2966   2562     38    -36   -173       C  
ATOM    141  CG  LEU A  41       4.221  19.058  -1.051  1.00 24.01           C  
ANISOU  141  CG  LEU A  41     3380   3075   2667     40    -35   -162       C  
ATOM    142  CD1 LEU A  41       3.170  18.638  -0.058  1.00 24.49           C  
ANISOU  142  CD1 LEU A  41     3415   3159   2732     49    -37   -170       C  
ATOM    143  CD2 LEU A  41       3.563  19.233  -2.405  1.00 22.89           C  
ANISOU  143  CD2 LEU A  41     3263   2905   2527     38    -50   -157       C  
ATOM    144  N   GLY A  42       7.683  21.951  -0.084  1.00 22.44           N  
ANISOU  144  N   GLY A  42     3188   2873   2466     24    -19   -182       N  
ATOM    145  CA  GLY A  42       8.181  23.181   0.521  1.00 21.89           C  
ANISOU  145  CA  GLY A  42     3113   2803   2400     24    -22   -195       C  
ATOM    146  C   GLY A  42       9.505  23.090   1.182  1.00 21.76           C  
ANISOU  146  C   GLY A  42     3086   2802   2378     19     -5   -196       C  
ATOM    147  O   GLY A  42      10.207  22.106   1.092  1.00 22.86           O  
ANISOU  147  O   GLY A  42     3225   2951   2511     13     10   -186       O  
ATOM    148  N   GLU A  43       9.875  24.178   1.834  1.00 20.67           N  
ANISOU  148  N   GLU A  43     2941   2666   2245     21     -8   -210       N  
ATOM    149  CA  GLU A  43      11.081  24.195   2.616  1.00 20.42           C  
ANISOU  149  CA  GLU A  43     2897   2652   2210     17      7   -213       C  
ATOM    150  C   GLU A  43      10.584  24.502   4.037  1.00 20.93           C  
ANISOU  150  C   GLU A  43     2933   2741   2278     28      4   -228       C  
ATOM    151  O   GLU A  43       9.827  25.472   4.215  1.00 27.46           O  
ANISOU  151  O   GLU A  43     3758   3562   3114     35    -11   -241       O  
ATOM    152  CB  GLU A  43      12.014  25.328   2.146  1.00 19.70           C  
ANISOU  152  CB  GLU A  43     2823   2543   2121      7      7   -219       C  
ATOM    153  CG  GLU A  43      13.165  25.637   3.108  1.00 20.13           C  
ANISOU  153  CG  GLU A  43     2861   2614   2175      6     20   -228       C  
ATOM    154  CD  GLU A  43      14.000  26.762   2.642  1.00 20.60           C  
ANISOU  154  CD  GLU A  43     2936   2655   2236     -4     19   -234       C  
ATOM    155  OE1 GLU A  43      14.640  26.601   1.547  1.00 20.51           O  
ANISOU  155  OE1 GLU A  43     2948   2627   2220    -19     26   -224       O  
ATOM    156  OE2 GLU A  43      14.020  27.819   3.366  1.00 22.35           O  
ANISOU  156  OE2 GLU A  43     3148   2879   2464      1     12   -248       O  
ATOM    157  N   ASN A  44      10.945  23.700   5.043  1.00 21.49           N  
ANISOU  157  N   ASN A  44     2982   2839   2343     30     16   -226       N  
ATOM    158  CA  ASN A  44      10.705  24.102   6.470  1.00 21.13           C  
ANISOU  158  CA  ASN A  44     2910   2819   2298     38     16   -241       C  
ATOM    159  C   ASN A  44      11.984  24.123   7.283  1.00 20.59           C  
ANISOU  159  C   ASN A  44     2831   2768   2226     34     28   -243       C  
ATOM    160  O   ASN A  44      12.855  23.220   7.180  1.00 18.87           O  
ANISOU  160  O   ASN A  44     2615   2554   2002     28     40   -231       O  
ATOM    161  CB  ASN A  44       9.817  23.107   7.313  1.00 22.76           C  
ANISOU  161  CB  ASN A  44     3097   3052   2499     43     17   -238       C  
ATOM    162  CG  ASN A  44       8.425  22.894   6.759  1.00 24.18           C  
ANISOU  162  CG  ASN A  44     3281   3222   2683     48      6   -238       C  
ATOM    163  OD1 ASN A  44       7.458  23.405   7.309  1.00 22.29           O  
ANISOU  163  OD1 ASN A  44     3028   2991   2449     55     -3   -253       O  
ATOM    164  ND2 ASN A  44       8.303  22.056   5.706  1.00 23.18           N  
ANISOU  164  ND2 ASN A  44     3172   3081   2555     44      7   -221       N  
ATOM    165  N   LYS A  45      12.022  25.030   8.255  1.00 19.60           N  
ANISOU  165  N   LYS A  45     2689   2655   2103     38     25   -261       N  
ATOM    166  CA  LYS A  45      12.861  24.813   9.428  1.00 22.73           C  
ANISOU  166  CA  LYS A  45     3066   3076   2492     38     35   -264       C  
ATOM    167  C   LYS A  45      12.190  23.867  10.424  1.00 21.41           C  
ANISOU  167  C   LYS A  45     2879   2938   2316     41     38   -261       C  
ATOM    168  O   LYS A  45      11.027  24.095  10.810  1.00 26.08           O  
ANISOU  168  O   LYS A  45     3461   3539   2910     46     30   -271       O  
ATOM    169  CB  LYS A  45      13.101  26.165  10.099  1.00 23.35           C  
ANISOU  169  CB  LYS A  45     3135   3159   2578     41     31   -285       C  
ATOM    170  CG  LYS A  45      14.443  26.276  10.785  1.00 24.64           C  
ANISOU  170  CG  LYS A  45     3290   3335   2737     37     42   -288       C  
ATOM    171  CD  LYS A  45      14.361  26.187  12.293  1.00 24.89           C  
ANISOU  171  CD  LYS A  45     3294   3400   2762     41     44   -298       C  
ATOM    172  CE  LYS A  45      13.754  27.436  12.914  0.50 24.53           C  
ANISOU  172  CE  LYS A  45     3236   3360   2724     47     35   -322       C  
ATOM    173  NZ  LYS A  45      13.027  27.055  14.148  0.50 24.14           N  
ANISOU  173  NZ  LYS A  45     3163   3343   2666     50     36   -329       N  
ATOM    174  N   ILE A  46      12.869  22.783  10.826  1.00 21.34           N  
ANISOU  174  N   ILE A  46     2865   2944   2299     37     47   -248       N  
ATOM    175  CA  ILE A  46      12.396  21.801  11.830  1.00 19.79           C  
ANISOU  175  CA  ILE A  46     2651   2776   2091     37     49   -242       C  
ATOM    176  C   ILE A  46      13.266  21.599  13.094  1.00 19.25           C  
ANISOU  176  C   ILE A  46     2566   2733   2014     34     55   -243       C  
ATOM    177  O   ILE A  46      14.353  21.016  13.061  1.00 15.31           O  
ANISOU  177  O   ILE A  46     2070   2233   1513     31     61   -233       O  
ATOM    178  CB  ILE A  46      12.233  20.358  11.241  1.00 20.47           C  
ANISOU  178  CB  ILE A  46     2746   2857   2173     33     52   -220       C  
ATOM    179  CG1 ILE A  46      11.332  20.338  10.021  1.00 20.53           C  
ANISOU  179  CG1 ILE A  46     2770   2842   2188     35     46   -216       C  
ATOM    180  CG2 ILE A  46      11.720  19.418  12.324  1.00 20.59           C  
ANISOU  180  CG2 ILE A  46     2745   2901   2177     32     53   -213       C  
ATOM    181  CD1 ILE A  46      10.977  18.919   9.560  1.00 20.42           C  
ANISOU  181  CD1 ILE A  46     2762   2826   2170     33     48   -196       C  
ATOM    182  N   PRO A  47      12.754  21.965  14.269  1.00 19.15           N  
ANISOU  182  N   PRO A  47     2535   2746   1996     35     54   -256       N  
ATOM    183  CA  PRO A  47      13.626  21.757  15.407  1.00 20.52           C  
ANISOU  183  CA  PRO A  47     2694   2942   2159     32     58   -257       C  
ATOM    184  C   PRO A  47      14.089  20.300  15.673  1.00 19.72           C  
ANISOU  184  C   PRO A  47     2594   2851   2049     27     61   -235       C  
ATOM    185  O   PRO A  47      13.373  19.325  15.400  1.00 22.15           O  
ANISOU  185  O   PRO A  47     2906   3159   2353     25     59   -220       O  
ATOM    186  CB  PRO A  47      12.751  22.223  16.568  1.00 18.94           C  
ANISOU  186  CB  PRO A  47     2475   2770   1952     32     56   -273       C  
ATOM    187  CG  PRO A  47      11.711  23.129  15.951  1.00 19.18           C  
ANISOU  187  CG  PRO A  47     2508   2786   1994     38     50   -289       C  
ATOM    188  CD  PRO A  47      11.414  22.373  14.672  1.00 18.92           C  
ANISOU  188  CD  PRO A  47     2494   2728   1966     38     48   -270       C  
ATOM    189  N   LYS A  48      15.303  20.127  16.194  1.00 17.72           N  
ANISOU  189  N   LYS A  48     2336   2604   1793     25     63   -232       N  
ATOM    190  CA  LYS A  48      15.778  18.768  16.432  1.00 18.07           C  
ANISOU  190  CA  LYS A  48     2381   2654   1830     21     62   -212       C  
ATOM    191  C   LYS A  48      14.850  18.134  17.495  1.00 19.53           C  
ANISOU  191  C   LYS A  48     2554   2867   1999     16     59   -206       C  
ATOM    192  O   LYS A  48      14.262  18.857  18.301  1.00 21.17           O  
ANISOU  192  O   LYS A  48     2750   3095   2200     15     60   -222       O  
ATOM    193  CB  LYS A  48      17.238  18.712  16.878  1.00 17.00           C  
ANISOU  193  CB  LYS A  48     2242   2522   1697     20     63   -212       C  
ATOM    194  CG  LYS A  48      18.257  18.651  15.754  1.00 17.43           C  
ANISOU  194  CG  LYS A  48     2308   2549   1764     22     67   -209       C  
ATOM    195  CD  LYS A  48      19.702  18.795  16.202  1.00 16.22           C  
ANISOU  195  CD  LYS A  48     2148   2399   1615     22     68   -215       C  
ATOM    196  CE  LYS A  48      20.578  19.168  15.033  1.00 15.31           C  
ANISOU  196  CE  LYS A  48     2045   2258   1515     22     75   -220       C  
ATOM    197  NZ  LYS A  48      21.989  18.804  15.252  1.00 16.09           N  
ANISOU  197  NZ  LYS A  48     2138   2356   1619     21     76   -221       N  
ATOM    198  N   ASN A  49      14.736  16.812  17.476  1.00 18.15           N  
ANISOU  198  N   ASN A  49     2384   2694   1818     11     57   -185       N  
ATOM    199  CA  ASN A  49      14.027  16.068  18.514  1.00 19.11           C  
ANISOU  199  CA  ASN A  49     2496   2842   1922      3     54   -177       C  
ATOM    200  C   ASN A  49      12.621  16.627  18.821  1.00 18.88           C  
ANISOU  200  C   ASN A  49     2459   2828   1887      1     56   -191       C  
ATOM    201  O   ASN A  49      12.187  16.853  20.017  1.00 19.31           O  
ANISOU  201  O   ASN A  49     2499   2912   1926     -5     57   -200       O  
ATOM    202  CB  ASN A  49      14.939  15.978  19.743  1.00 21.10           C  
ANISOU  202  CB  ASN A  49     2739   3115   2164     -1     51   -176       C  
ATOM    203  CG  ASN A  49      14.449  14.994  20.821  1.00 24.24           C  
ANISOU  203  CG  ASN A  49     3131   3539   2541    -13     46   -162       C  
ATOM    204  OD1 ASN A  49      15.044  14.929  21.897  1.00 27.12           O  
ANISOU  204  OD1 ASN A  49     3488   3923   2894    -18     42   -161       O  
ATOM    205  ND2 ASN A  49      13.408  14.259  20.560  1.00 26.55           N  
ANISOU  205  ND2 ASN A  49     3427   3831   2829    -18     46   -151       N  
ATOM    206  N   PRO A  50      11.814  16.820  17.772  1.00 18.94           N  
ANISOU  206  N   PRO A  50     2475   2817   1906      6     57   -194       N  
ATOM    207  CA  PRO A  50      10.474  17.362  18.044  1.00 20.68           C  
ANISOU  207  CA  PRO A  50     2685   3050   2122      6     58   -210       C  
ATOM    208  C   PRO A  50       9.652  16.478  19.022  1.00 20.99           C  
ANISOU  208  C   PRO A  50     2714   3118   2143     -6     59   -202       C  
ATOM    209  O   PRO A  50       9.578  15.240  18.895  1.00 19.29           O  
ANISOU  209  O   PRO A  50     2507   2901   1922    -12     57   -180       O  
ATOM    210  CB  PRO A  50       9.860  17.507  16.653  1.00 21.06           C  
ANISOU  210  CB  PRO A  50     2746   3069   2186     13     56   -210       C  
ATOM    211  CG  PRO A  50      10.549  16.514  15.870  1.00 19.15           C  
ANISOU  211  CG  PRO A  50     2520   2808   1948     13     56   -187       C  
ATOM    212  CD  PRO A  50      11.942  16.328  16.391  1.00 19.29           C  
ANISOU  212  CD  PRO A  50     2536   2830   1962     11     57   -181       C  
ATOM    213  N   SER A  51       9.096  17.102  20.064  1.00 24.91           N  
ANISOU  213  N   SER A  51     3194   3642   2629    -11     61   -221       N  
ATOM    214  CA  SER A  51       8.498  16.364  21.189  1.00 24.04           C  
ANISOU  214  CA  SER A  51     3074   3565   2497    -26     63   -216       C  
ATOM    215  C   SER A  51       6.986  16.120  21.121  1.00 23.54           C  
ANISOU  215  C   SER A  51     3004   3511   2430    -31     66   -223       C  
ATOM    216  O   SER A  51       6.461  15.324  21.878  1.00 20.90           O  
ANISOU  216  O   SER A  51     2665   3200   2078    -46     69   -215       O  
ATOM    217  CB  SER A  51       8.711  17.184  22.453  1.00 24.61           C  
ANISOU  217  CB  SER A  51     3128   3665   2556    -31     66   -236       C  
ATOM    218  OG  SER A  51       8.298  18.498  22.174  1.00 25.04           O  
ANISOU  218  OG  SER A  51     3174   3714   2625    -21     67   -264       O  
ATOM    219  N   LYS A  52       6.292  16.908  20.300  1.00 23.35           N  
ANISOU  219  N   LYS A  52     2979   3470   2424    -21     66   -241       N  
ATOM    220  CA  LYS A  52       4.839  16.734  20.038  1.00 24.27           C  
ANISOU  220  CA  LYS A  52     3089   3590   2541    -23     67   -250       C  
ATOM    221  C   LYS A  52       4.491  16.609  18.509  1.00 21.25           C  
ANISOU  221  C   LYS A  52     2723   3171   2179    -11     62   -242       C  
ATOM    222  O   LYS A  52       4.092  17.563  17.820  1.00 20.61           O  
ANISOU  222  O   LYS A  52     2643   3073   2116      0     57   -261       O  
ATOM    223  CB  LYS A  52       4.122  17.923  20.704  1.00 23.96           C  
ANISOU  223  CB  LYS A  52     3029   3570   2504    -22     69   -285       C  
ATOM    224  CG  LYS A  52       4.434  18.040  22.205  0.50 24.26           C  
ANISOU  224  CG  LYS A  52     3051   3645   2520    -35     75   -293       C  
ATOM    225  CD  LYS A  52       3.376  18.803  22.992  0.50 24.39           C  
ANISOU  225  CD  LYS A  52     3044   3690   2534    -40     80   -327       C  
ATOM    226  CE  LYS A  52       3.682  20.289  23.052  0.50 24.17           C  
ANISOU  226  CE  LYS A  52     3006   3657   2521    -28     77   -356       C  
ATOM    227  NZ  LYS A  52       2.454  21.134  23.131  0.50 24.13           N  
ANISOU  227  NZ  LYS A  52     2981   3659   2527    -24     76   -391       N  
ATOM    228  N   VAL A  53       4.624  15.410  17.973  1.00 20.76           N  
ANISOU  228  N   VAL A  53     2675   3097   2114    -14     61   -216       N  
ATOM    229  CA  VAL A  53       4.407  15.267  16.533  1.00 20.93           C  
ANISOU  229  CA  VAL A  53     2713   3086   2154     -4     56   -208       C  
ATOM    230  C   VAL A  53       3.006  14.758  16.265  1.00 20.61           C  
ANISOU  230  C   VAL A  53     2669   3049   2114     -7     56   -211       C  
ATOM    231  O   VAL A  53       2.617  13.668  16.737  1.00 19.91           O  
ANISOU  231  O   VAL A  53     2578   2977   2012    -19     60   -196       O  
ATOM    232  CB  VAL A  53       5.452  14.332  15.911  1.00 20.96           C  
ANISOU  232  CB  VAL A  53     2734   3070   2159     -4     55   -180       C  
ATOM    233  CG1 VAL A  53       5.213  14.190  14.379  1.00 21.83           C  
ANISOU  233  CG1 VAL A  53     2862   3147   2285      5     51   -174       C  
ATOM    234  CG2 VAL A  53       6.846  14.878  16.178  1.00 21.57           C  
ANISOU  234  CG2 VAL A  53     2814   3145   2237     -1     55   -181       C  
ATOM    235  N   VAL A  54       2.282  15.529  15.473  1.00 18.52           N  
ANISOU  235  N   VAL A  54     2405   2767   1866      3     51   -228       N  
ATOM    236  CA  VAL A  54       1.114  15.012  14.756  1.00 19.05           C  
ANISOU  236  CA  VAL A  54     2475   2825   1939      4     49   -227       C  
ATOM    237  C   VAL A  54       1.474  14.278  13.450  1.00 19.74           C  
ANISOU  237  C   VAL A  54     2584   2881   2035      9     45   -203       C  
ATOM    238  O   VAL A  54       2.053  14.883  12.514  1.00 19.34           O  
ANISOU  238  O   VAL A  54     2549   2804   1998     19     40   -203       O  
ATOM    239  CB  VAL A  54       0.104  16.138  14.453  1.00 18.36           C  
ANISOU  239  CB  VAL A  54     2377   2731   1866     14     42   -257       C  
ATOM    240  CG1 VAL A  54      -1.040  15.618  13.537  1.00 17.63           C  
ANISOU  240  CG1 VAL A  54     2290   2624   1784     17     37   -255       C  
ATOM    241  CG2 VAL A  54      -0.470  16.582  15.800  1.00 19.17           C  
ANISOU  241  CG2 VAL A  54     2454   2869   1959      6     48   -281       C  
ATOM    242  N   ILE A  55       1.069  13.006  13.384  1.00 20.38           N  
ANISOU  242  N   ILE A  55     2669   2966   2108      1     47   -185       N  
ATOM    243  CA  ILE A  55       1.448  12.169  12.259  1.00 18.51           C  
ANISOU  243  CA  ILE A  55     2452   2704   1879      5     45   -162       C  
ATOM    244  C   ILE A  55       0.132  11.851  11.514  1.00 18.53           C  
ANISOU  244  C   ILE A  55     2455   2696   1889      7     41   -166       C  
ATOM    245  O   ILE A  55      -0.737  11.198  12.098  1.00 18.50           O  
ANISOU  245  O   ILE A  55     2440   2712   1876     -2     45   -166       O  
ATOM    246  CB  ILE A  55       2.212  10.912  12.776  1.00 17.68           C  
ANISOU  246  CB  ILE A  55     2350   2608   1761     -6     49   -136       C  
ATOM    247  CG1 ILE A  55       3.512  11.292  13.518  1.00 15.63           C  
ANISOU  247  CG1 ILE A  55     2088   2357   1495     -7     51   -135       C  
ATOM    248  CG2 ILE A  55       2.555   9.978  11.623  1.00 16.59           C  
ANISOU  248  CG2 ILE A  55     2230   2443   1631     -3     46   -115       C  
ATOM    249  CD1 ILE A  55       4.394  10.153  14.104  1.00 16.25           C  
ANISOU  249  CD1 ILE A  55     2169   2443   1561    -17     51   -111       C  
ATOM    250  N   LEU A  56      -0.029  12.279  10.238  1.00 19.02           N  
ANISOU  250  N   LEU A  56     2531   2728   1966     18     34   -169       N  
ATOM    251  CA  LEU A  56      -1.245  12.010   9.408  1.00 19.75           C  
ANISOU  251  CA  LEU A  56     2627   2809   2068     22     28   -173       C  
ATOM    252  C   LEU A  56      -0.974  11.015   8.257  1.00 19.56           C  
ANISOU  252  C   LEU A  56     2622   2761   2048     23     27   -149       C  
ATOM    253  O   LEU A  56      -1.834  10.824   7.343  1.00 20.69           O  
ANISOU  253  O   LEU A  56     2772   2888   2200     27     21   -151       O  
ATOM    254  CB  LEU A  56      -1.743  13.266   8.774  1.00 19.91           C  
ANISOU  254  CB  LEU A  56     2649   2812   2105     34     18   -195       C  
ATOM    255  CG  LEU A  56      -2.714  14.094   9.618  1.00 21.01           C  
ANISOU  255  CG  LEU A  56     2765   2971   2246     35     16   -224       C  
ATOM    256  CD1 LEU A  56      -2.571  15.583   9.399  1.00 21.09           C  
ANISOU  256  CD1 LEU A  56     2777   2968   2270     46      6   -245       C  
ATOM    257  CD2 LEU A  56      -4.153  13.625   9.341  1.00 21.03           C  
ANISOU  257  CD2 LEU A  56     2761   2977   2255     35     13   -232       C  
ATOM    258  N   ASP A  57       0.223  10.456   8.282  1.00 19.90           N  
ANISOU  258  N   ASP A  57     2674   2801   2086     19     31   -130       N  
ATOM    259  CA  ASP A  57       0.548   9.222   7.553  1.00 19.78           C  
ANISOU  259  CA  ASP A  57     2672   2771   2071     16     32   -107       C  
ATOM    260  C   ASP A  57       0.724   7.989   8.518  1.00 21.25           C  
ANISOU  260  C   ASP A  57     2850   2979   2245      5     38    -90       C  
ATOM    261  O   ASP A  57       1.654   7.948   9.358  1.00 16.75           O  
ANISOU  261  O   ASP A  57     2276   2422   1667      0     41    -84       O  
ATOM    262  CB  ASP A  57       1.806   9.450   6.657  1.00 19.59           C  
ANISOU  262  CB  ASP A  57     2666   2724   2054     21     32   -100       C  
ATOM    263  CG  ASP A  57       2.212   8.196   5.889  1.00 20.46           C  
ANISOU  263  CG  ASP A  57     2788   2820   2167     18     33    -79       C  
ATOM    264  OD1 ASP A  57       2.420   7.148   6.534  1.00 20.13           O  
ANISOU  264  OD1 ASP A  57     2741   2791   2119     11     36    -64       O  
ATOM    265  OD2 ASP A  57       2.359   8.217   4.636  1.00 19.76           O  
ANISOU  265  OD2 ASP A  57     2716   2706   2086     22     31    -76       O  
ATOM    266  N   LEU A  58      -0.146   6.984   8.375  1.00 19.72           N  
ANISOU  266  N   LEU A  58     2655   2788   2050     -1     38    -81       N  
ATOM    267  CA  LEU A  58      -0.140   5.833   9.296  1.00 18.77           C  
ANISOU  267  CA  LEU A  58     2528   2687   1917    -13     41    -65       C  
ATOM    268  C   LEU A  58       1.131   5.022   9.147  1.00 19.13           C  
ANISOU  268  C   LEU A  58     2584   2721   1963    -15     40    -43       C  
ATOM    269  O   LEU A  58       1.589   4.316  10.055  1.00 19.65           O  
ANISOU  269  O   LEU A  58     2645   2802   2018    -24     41    -29       O  
ATOM    270  CB  LEU A  58      -1.466   5.042   9.197  1.00 18.43           C  
ANISOU  270  CB  LEU A  58     2480   2649   1873    -19     42    -62       C  
ATOM    271  CG  LEU A  58      -2.608   5.935   9.767  1.00 20.07           C  
ANISOU  271  CG  LEU A  58     2671   2876   2078    -20     44    -88       C  
ATOM    272  CD1 LEU A  58      -4.026   5.953   9.192  1.00 19.61           C  
ANISOU  272  CD1 LEU A  58     2609   2814   2028    -17     42   -102       C  
ATOM    273  CD2 LEU A  58      -2.728   5.660  11.252  1.00 19.03           C  
ANISOU  273  CD2 LEU A  58     2525   2779   1928    -36     50    -88       C  
ATOM    274  N   GLY A  59       1.798   5.111   8.000  1.00 18.44           N  
ANISOU  274  N   GLY A  59     2510   2607   1887     -6     38    -40       N  
ATOM    275  CA  GLY A  59       3.035   4.358   7.887  1.00 17.91           C  
ANISOU  275  CA  GLY A  59     2450   2531   1823     -7     38    -23       C  
ATOM    276  C   GLY A  59       4.119   4.975   8.768  1.00 17.76           C  
ANISOU  276  C   GLY A  59     2425   2523   1798     -8     39    -27       C  
ATOM    277  O   GLY A  59       4.886   4.272   9.428  1.00 15.93           O  
ANISOU  277  O   GLY A  59     2192   2299   1562    -13     37    -14       O  
ATOM    278  N   ILE A  60       4.120   6.306   8.837  1.00 19.44           N  
ANISOU  278  N   ILE A  60     2636   2739   2012     -2     41    -46       N  
ATOM    279  CA  ILE A  60       5.133   7.047   9.595  1.00 19.81           C  
ANISOU  279  CA  ILE A  60     2677   2796   2054     -2     42    -53       C  
ATOM    280  C   ILE A  60       4.877   6.798  11.104  1.00 18.87           C  
ANISOU  280  C   ILE A  60     2543   2707   1918    -12     43    -51       C  
ATOM    281  O   ILE A  60       5.823   6.794  11.916  1.00 19.05           O  
ANISOU  281  O   ILE A  60     2562   2741   1936    -15     42    -47       O  
ATOM    282  CB  ILE A  60       5.124   8.581   9.368  1.00 20.23           C  
ANISOU  282  CB  ILE A  60     2730   2845   2111      5     44    -75       C  
ATOM    283  CG1 ILE A  60       5.646   8.990   7.993  1.00 22.89           C  
ANISOU  283  CG1 ILE A  60     3083   3152   2461     13     43    -77       C  
ATOM    284  CG2 ILE A  60       6.074   9.222  10.389  1.00 22.68           C  
ANISOU  284  CG2 ILE A  60     3032   3171   2415      4     46    -81       C  
ATOM    285  CD1 ILE A  60       7.127   8.746   7.832  1.00 22.08           C  
ANISOU  285  CD1 ILE A  60     2986   3041   2362     12     46    -70       C  
ATOM    286  N   LEU A  61       3.618   6.498  11.438  1.00 20.62           N  
ANISOU  286  N   LEU A  61     2758   2943   2133    -18     44    -52       N  
ATOM    287  CA  LEU A  61       3.203   6.292  12.830  1.00 18.45           C  
ANISOU  287  CA  LEU A  61     2470   2700   1841    -31     46    -52       C  
ATOM    288  C   LEU A  61       3.750   4.948  13.339  1.00 19.33           C  
ANISOU  288  C   LEU A  61     2584   2814   1944    -41     41    -26       C  
ATOM    289  O   LEU A  61       4.158   4.808  14.526  1.00 20.90           O  
ANISOU  289  O   LEU A  61     2777   3035   2129    -51     40    -21       O  
ATOM    290  CB  LEU A  61       1.692   6.383  12.978  1.00 18.49           C  
ANISOU  290  CB  LEU A  61     2465   2717   1841    -36     49    -64       C  
ATOM    291  CG  LEU A  61       1.159   6.695  14.420  1.00 17.90           C  
ANISOU  291  CG  LEU A  61     2373   2678   1748    -49     54    -75       C  
ATOM    292  CD1 LEU A  61       1.432   8.123  14.974  1.00 17.14           C  
ANISOU  292  CD1 LEU A  61     2267   2595   1651    -44     56    -99       C  
ATOM    293  CD2 LEU A  61      -0.326   6.549  14.411  1.00 18.67           C  
ANISOU  293  CD2 LEU A  61     2463   2787   1844    -55     57    -86       C  
ATOM    294  N   ASP A  62       3.831   3.949  12.477  1.00 16.76           N  
ANISOU  294  N   ASP A  62     2270   2468   1629    -39     38    -10       N  
ATOM    295  CA  ASP A  62       4.493   2.735  12.894  1.00 19.92           C  
ANISOU  295  CA  ASP A  62     2675   2869   2026    -47     31     13       C  
ATOM    296  C   ASP A  62       6.034   2.938  12.912  1.00 18.70           C  
ANISOU  296  C   ASP A  62     2523   2703   1877    -40     27     16       C  
ATOM    297  O   ASP A  62       6.739   2.312  13.710  1.00 21.50           O  
ANISOU  297  O   ASP A  62     2877   3065   2226    -47     20     29       O  
ATOM    298  CB  ASP A  62       4.033   1.480  12.128  1.00 19.59           C  
ANISOU  298  CB  ASP A  62     2641   2809   1992    -49     27     30       C  
ATOM    299  CG  ASP A  62       4.462   1.477  10.697  1.00 20.33           C  
ANISOU  299  CG  ASP A  62     2745   2873   2105    -35     27     28       C  
ATOM    300  OD1 ASP A  62       5.655   1.214  10.481  1.00 21.89           O  
ANISOU  300  OD1 ASP A  62     2948   3059   2312    -31     23     35       O  
ATOM    301  OD2 ASP A  62       3.568   1.707   9.832  1.00 21.40           O  
ANISOU  301  OD2 ASP A  62     2884   3000   2247    -31     31     20       O  
ATOM    302  N   THR A  63       6.594   3.839  12.070  1.00 18.73           N  
ANISOU  302  N   THR A  63     2531   2691   1894    -28     31      1       N  
ATOM    303  CA  THR A  63       8.010   4.156  12.195  1.00 17.34           C  
ANISOU  303  CA  THR A  63     2356   2509   1724    -23     29      0       C  
ATOM    304  C   THR A  63       8.378   4.747  13.503  1.00 18.82           C  
ANISOU  304  C   THR A  63     2534   2721   1898    -28     28     -6       C  
ATOM    305  O   THR A  63       9.334   4.303  14.151  1.00 16.35           O  
ANISOU  305  O   THR A  63     2219   2411   1582    -31     21      4       O  
ATOM    306  CB  THR A  63       8.470   5.037  11.048  1.00 18.61           C  
ANISOU  306  CB  THR A  63     2523   2648   1898    -11     34    -15       C  
ATOM    307  OG1 THR A  63       8.626   4.138   9.984  1.00 18.44           O  
ANISOU  307  OG1 THR A  63     2512   2605   1890     -9     32     -4       O  
ATOM    308  CG2 THR A  63       9.877   5.730  11.278  1.00 17.79           C  
ANISOU  308  CG2 THR A  63     2418   2543   1799     -7     34    -23       C  
ATOM    309  N   PHE A  64       7.602   5.723  13.916  1.00 18.55           N  
ANISOU  309  N   PHE A  64     2491   2703   1854    -29     34    -22       N  
ATOM    310  CA  PHE A  64       7.771   6.172  15.323  1.00 19.29           C  
ANISOU  310  CA  PHE A  64     2573   2824   1931    -37     34    -28       C  
ATOM    311  C   PHE A  64       7.719   5.044  16.371  1.00 21.33           C  
ANISOU  311  C   PHE A  64     2831   3101   2174    -52     27     -7       C  
ATOM    312  O   PHE A  64       8.627   4.969  17.207  1.00 21.41           O  
ANISOU  312  O   PHE A  64     2839   3120   2178    -55     21     -2       O  
ATOM    313  CB  PHE A  64       6.780   7.252  15.662  1.00 18.98           C  
ANISOU  313  CB  PHE A  64     2524   2803   1885    -38     41    -49       C  
ATOM    314  CG  PHE A  64       7.209   8.626  15.254  1.00 18.16           C  
ANISOU  314  CG  PHE A  64     2418   2689   1790    -26     45    -71       C  
ATOM    315  CD1 PHE A  64       7.386   8.967  13.882  1.00 18.46           C  
ANISOU  315  CD1 PHE A  64     2468   2698   1847    -15     46    -75       C  
ATOM    316  CD2 PHE A  64       7.388   9.634  16.201  1.00 19.10           C  
ANISOU  316  CD2 PHE A  64     2527   2830   1902    -28     48    -88       C  
ATOM    317  CE1 PHE A  64       7.786  10.236  13.495  1.00 18.07           C  
ANISOU  317  CE1 PHE A  64     2420   2641   1807     -6     48    -93       C  
ATOM    318  CE2 PHE A  64       7.781  10.928  15.789  1.00 19.40           C  
ANISOU  318  CE2 PHE A  64     2564   2857   1950    -17     50   -107       C  
ATOM    319  CZ  PHE A  64       7.989  11.227  14.454  1.00 19.54           C  
ANISOU  319  CZ  PHE A  64     2594   2845   1985     -6     50   -109       C  
ATOM    320  N   ASP A  65       6.745   4.132  16.297  1.00 23.48           N  
ANISOU  320  N   ASP A  65     3105   3374   2441    -60     26      5       N  
ATOM    321  CA  ASP A  65       6.753   2.967  17.168  1.00 21.54           C  
ANISOU  321  CA  ASP A  65     2862   3142   2182    -76     18     27       C  
ATOM    322  C   ASP A  65       8.073   2.186  17.067  1.00 21.93           C  
ANISOU  322  C   ASP A  65     2919   3173   2241    -71      5     45       C  
ATOM    323  O   ASP A  65       8.676   1.837  18.062  1.00 21.60           O  
ANISOU  323  O   ASP A  65     2876   3143   2189    -80     -4     56       O  
ATOM    324  CB  ASP A  65       5.569   2.035  16.827  1.00 23.03           C  
ANISOU  324  CB  ASP A  65     3053   3328   2368    -84     19     38       C  
ATOM    325  CG  ASP A  65       5.398   0.918  17.830  1.00 23.44           C  
ANISOU  325  CG  ASP A  65     3108   3396   2403   -103     11     61       C  
ATOM    326  OD1 ASP A  65       5.117   1.215  19.016  1.00 28.19           O  
ANISOU  326  OD1 ASP A  65     3703   4027   2983   -118     13     57       O  
ATOM    327  OD2 ASP A  65       5.522  -0.251  17.438  1.00 24.37           O  
ANISOU  327  OD2 ASP A  65     3234   3497   2528   -105      2     81       O  
ATOM    328  N   ALA A  66       8.545   1.956  15.835  1.00 18.76           N  
ANISOU  328  N   ALA A  66     2524   2742   1862    -58      5     46       N  
ATOM    329  CA  ALA A  66       9.688   1.071  15.585  1.00 19.73           C  
ANISOU  329  CA  ALA A  66     2653   2845   1997    -54     -7     61       C  
ATOM    330  C   ALA A  66      10.952   1.642  16.234  1.00 21.34           C  
ANISOU  330  C   ALA A  66     2852   3055   2201    -50    -12     54       C  
ATOM    331  O   ALA A  66      11.833   0.941  16.805  1.00 24.94           O  
ANISOU  331  O   ALA A  66     3309   3508   2658    -53    -26     68       O  
ATOM    332  CB  ALA A  66       9.868   0.933  14.053  1.00 18.80           C  
ANISOU  332  CB  ALA A  66     2542   2698   1902    -41     -4     56       C  
ATOM    333  N   LEU A  67      11.026   2.965  16.181  1.00 20.58           N  
ANISOU  333  N   LEU A  67     2750   2965   2104    -44     -1     33       N  
ATOM    334  CA  LEU A  67      12.140   3.681  16.720  1.00 21.75           C  
ANISOU  334  CA  LEU A  67     2893   3118   2252    -40     -3     23       C  
ATOM    335  C   LEU A  67      11.974   3.947  18.210  1.00 21.74           C  
ANISOU  335  C   LEU A  67     2885   3148   2228    -52     -6     24       C  
ATOM    336  O   LEU A  67      12.843   4.524  18.808  1.00 19.96           O  
ANISOU  336  O   LEU A  67     2653   2929   2000    -49     -8     16       O  
ATOM    337  CB  LEU A  67      12.310   4.990  15.936  1.00 22.49           C  
ANISOU  337  CB  LEU A  67     2985   3203   2356    -28      9     -1       C  
ATOM    338  CG  LEU A  67      12.482   4.684  14.446  1.00 22.88           C  
ANISOU  338  CG  LEU A  67     3044   3223   2426    -19     12     -1       C  
ATOM    339  CD1 LEU A  67      12.706   5.979  13.692  1.00 24.89           C  
ANISOU  339  CD1 LEU A  67     3299   3468   2689    -10     23    -22       C  
ATOM    340  CD2 LEU A  67      13.558   3.646  14.146  1.00 25.27           C  
ANISOU  340  CD2 LEU A  67     3350   3508   2744    -16      2     12       C  
ATOM    341  N   LYS A  68      10.930   3.432  18.842  1.00 23.38           N  
ANISOU  341  N   LYS A  68     3092   3373   2418    -66     -7     34       N  
ATOM    342  CA  LYS A  68      10.715   3.701  20.263  1.00 26.00           C  
ANISOU  342  CA  LYS A  68     3417   3737   2725    -80     -8     34       C  
ATOM    343  C   LYS A  68      10.557   5.219  20.487  1.00 24.07           C  
ANISOU  343  C   LYS A  68     3161   3508   2476    -75      5      6       C  
ATOM    344  O   LYS A  68      11.184   5.799  21.364  1.00 24.23           O  
ANISOU  344  O   LYS A  68     3175   3544   2487    -77      3     -1       O  
ATOM    345  CB  LYS A  68      11.833   3.085  21.135  1.00 27.38           C  
ANISOU  345  CB  LYS A  68     3594   3914   2895    -85    -25     50       C  
ATOM    346  CG  LYS A  68      11.575   1.629  21.521  1.00 29.54           C  
ANISOU  346  CG  LYS A  68     3877   4187   3161    -99    -39     78       C  
ATOM    347  CD  LYS A  68      12.842   0.759  21.590  1.00 30.87           C  
ANISOU  347  CD  LYS A  68     4052   4336   3341    -94    -60     95       C  
ATOM    348  CE  LYS A  68      12.565  -0.623  20.977  1.00 31.20           C  
ANISOU  348  CE  LYS A  68     4104   4357   3394    -96    -70    117       C  
ATOM    349  NZ  LYS A  68      13.774  -1.363  20.518  1.00 33.66           N  
ANISOU  349  NZ  LYS A  68     4420   4641   3730    -85    -87    126       N  
ATOM    350  N   LEU A  69       9.711   5.828  19.678  1.00 24.27           N  
ANISOU  350  N   LEU A  69     3185   3527   2510    -69     16     -9       N  
ATOM    351  CA  LEU A  69       9.414   7.282  19.737  1.00 21.95           C  
ANISOU  351  CA  LEU A  69     2882   3244   2216    -63     27    -37       C  
ATOM    352  C   LEU A  69       7.954   7.479  20.063  1.00 21.68           C  
ANISOU  352  C   LEU A  69     2840   3230   2169    -73     35    -47       C  
ATOM    353  O   LEU A  69       7.373   8.609  19.956  1.00 18.90           O  
ANISOU  353  O   LEU A  69     2478   2884   1818    -67     44    -71       O  
ATOM    354  CB  LEU A  69       9.747   7.949  18.391  1.00 22.67           C  
ANISOU  354  CB  LEU A  69     2977   3306   2329    -45     32    -49       C  
ATOM    355  CG  LEU A  69      11.255   7.991  18.131  1.00 21.38           C  
ANISOU  355  CG  LEU A  69     2819   3127   2180    -37     26    -46       C  
ATOM    356  CD1 LEU A  69      11.444   8.361  16.660  1.00 22.63           C  
ANISOU  356  CD1 LEU A  69     2985   3254   2358    -24     31    -54       C  
ATOM    357  CD2 LEU A  69      12.048   8.887  19.102  1.00 22.42           C  
ANISOU  357  CD2 LEU A  69     2940   3274   2303    -37     26    -59       C  
ATOM    358  N   ASN A  70       7.366   6.431  20.634  1.00 20.20           N  
ANISOU  358  N   ASN A  70     2653   3056   1965    -89     32    -29       N  
ATOM    359  CA  ASN A  70       5.917   6.498  20.938  1.00 21.95           C  
ANISOU  359  CA  ASN A  70     2868   3299   2175   -100     41    -39       C  
ATOM    360  C   ASN A  70       5.604   7.795  21.708  1.00 22.59           C  
ANISOU  360  C   ASN A  70     2933   3405   2246   -102     49    -67       C  
ATOM    361  O   ASN A  70       4.661   8.473  21.350  1.00 21.37           O  
ANISOU  361  O   ASN A  70     2769   3253   2097    -98     57    -88       O  
ATOM    362  CB  ASN A  70       5.359   5.256  21.634  1.00 22.67           C  
ANISOU  362  CB  ASN A  70     2961   3405   2246   -121     37    -17       C  
ATOM    363  CG  ASN A  70       5.697   3.940  20.896  1.00 24.06           C  
ANISOU  363  CG  ASN A  70     3154   3555   2434   -119     26     11       C  
ATOM    364  OD1 ASN A  70       6.859   3.497  20.907  1.00 26.27           O  
ANISOU  364  OD1 ASN A  70     3441   3820   2720   -114     15     26       O  
ATOM    365  ND2 ASN A  70       4.683   3.304  20.273  1.00 26.60           N  
ANISOU  365  ND2 ASN A  70     3478   3868   2759   -122     29     16       N  
ATOM    366  N   ASP A  71       6.396   8.125  22.731  1.00 23.44           N  
ANISOU  366  N   ASP A  71     3036   3531   2341   -108     47    -69       N  
ATOM    367  CA  ASP A  71       6.172   9.335  23.538  1.00 23.38           C  
ANISOU  367  CA  ASP A  71     3011   3548   2323   -110     54    -97       C  
ATOM    368  C   ASP A  71       6.124  10.621  22.742  1.00 23.06           C  
ANISOU  368  C   ASP A  71     2965   3492   2304    -91     60   -123       C  
ATOM    369  O   ASP A  71       5.507  11.556  23.162  1.00 21.61           O  
ANISOU  369  O   ASP A  71     2767   3327   2117    -92     67   -149       O  
ATOM    370  CB  ASP A  71       7.210   9.514  24.662  1.00 24.71           C  
ANISOU  370  CB  ASP A  71     3177   3735   2477   -117     49    -94       C  
ATOM    371  CG  ASP A  71       6.988   8.560  25.827  0.50 24.09           C  
ANISOU  371  CG  ASP A  71     3100   3683   2369   -142     45    -75       C  
ATOM    372  OD1 ASP A  71       5.973   7.805  25.818  0.50 25.37           O  
ANISOU  372  OD1 ASP A  71     3264   3852   2522   -155     48    -66       O  
ATOM    373  OD2 ASP A  71       7.825   8.584  26.774  0.50 23.26           O  
ANISOU  373  OD2 ASP A  71     2996   3593   2251   -149     39    -70       O  
ATOM    374  N   LYS A  72       6.805  10.709  21.591  1.00 22.01           N  
ANISOU  374  N   LYS A  72     2844   3327   2194    -74     56   -118       N  
ATOM    375  CA  LYS A  72       6.882  12.021  20.932  1.00 20.33           C  
ANISOU  375  CA  LYS A  72     2626   3099   1999    -57     59   -142       C  
ATOM    376  C   LYS A  72       5.632  12.320  20.147  1.00 23.07           C  
ANISOU  376  C   LYS A  72     2971   3437   2356    -52     63   -156       C  
ATOM    377  O   LYS A  72       5.429  13.448  19.692  1.00 20.34           O  
ANISOU  377  O   LYS A  72     2621   3083   2024    -41     64   -178       O  
ATOM    378  CB  LYS A  72       8.070  12.143  19.940  1.00 19.35           C  
ANISOU  378  CB  LYS A  72     2516   2943   1894    -43     54   -134       C  
ATOM    379  CG  LYS A  72       9.444  11.648  20.377  1.00 19.96           C  
ANISOU  379  CG  LYS A  72     2597   3018   1967    -44     48   -118       C  
ATOM    380  CD  LYS A  72       9.806  12.073  21.792  1.00 20.33           C  
ANISOU  380  CD  LYS A  72     2633   3096   1996    -53     48   -126       C  
ATOM    381  CE  LYS A  72      11.310  12.157  21.990  1.00 21.19           C  
ANISOU  381  CE  LYS A  72     2745   3197   2110    -48     42   -121       C  
ATOM    382  NZ  LYS A  72      11.621  13.195  23.019  1.00 22.31           N  
ANISOU  382  NZ  LYS A  72     2872   3362   2241    -50     45   -141       N  
ATOM    383  N   VAL A  73       4.781  11.316  19.960  1.00 22.77           N  
ANISOU  383  N   VAL A  73     2937   3401   2313    -61     63   -142       N  
ATOM    384  CA  VAL A  73       3.542  11.594  19.309  1.00 23.37           C  
ANISOU  384  CA  VAL A  73     3009   3472   2399    -57     66   -157       C  
ATOM    385  C   VAL A  73       2.468  12.087  20.258  1.00 24.57           C  
ANISOU  385  C   VAL A  73     3140   3656   2538    -67     73   -181       C  
ATOM    386  O   VAL A  73       2.092  11.392  21.191  1.00 24.18           O  
ANISOU  386  O   VAL A  73     3086   3634   2469    -86     77   -174       O  
ATOM    387  CB  VAL A  73       2.953  10.383  18.638  1.00 22.27           C  
ANISOU  387  CB  VAL A  73     2879   3320   2261    -60     65   -137       C  
ATOM    388  CG1 VAL A  73       1.546  10.700  18.179  1.00 20.77           C  
ANISOU  388  CG1 VAL A  73     2682   3130   2079    -58     68   -155       C  
ATOM    389  CG2 VAL A  73       3.780  10.089  17.415  1.00 22.13           C  
ANISOU  389  CG2 VAL A  73     2881   3267   2262    -47     59   -121       C  
ATOM    390  N   VAL A  74       1.911  13.236  19.905  1.00 25.15           N  
ANISOU  390  N   VAL A  74     3205   3725   2626    -56     74   -209       N  
ATOM    391  CA  VAL A  74       0.784  13.772  20.578  1.00 24.91           C  
ANISOU  391  CA  VAL A  74     3154   3721   2591    -63     80   -237       C  
ATOM    392  C   VAL A  74      -0.578  13.558  19.911  1.00 25.41           C  
ANISOU  392  C   VAL A  74     3214   3778   2664    -62     80   -247       C  
ATOM    393  O   VAL A  74      -1.580  13.673  20.609  1.00 27.34           O  
ANISOU  393  O   VAL A  74     3440   4049   2900    -73     87   -267       O  
ATOM    394  CB  VAL A  74       0.986  15.288  20.832  1.00 25.04           C  
ANISOU  394  CB  VAL A  74     3157   3739   2616    -53     79   -268       C  
ATOM    395  CG1 VAL A  74       2.263  15.488  21.665  1.00 28.06           C  
ANISOU  395  CG1 VAL A  74     3541   4135   2987    -57     80   -261       C  
ATOM    396  CG2 VAL A  74       0.943  16.102  19.535  1.00 22.49           C  
ANISOU  396  CG2 VAL A  74     2843   3381   2321    -32     71   -278       C  
ATOM    397  N   GLY A  75      -0.626  13.271  18.610  1.00 26.25           N  
ANISOU  397  N   GLY A  75     3335   3850   2787    -49     74   -234       N  
ATOM    398  CA  GLY A  75      -1.910  13.131  17.884  1.00 27.00           C  
ANISOU  398  CA  GLY A  75     3428   3937   2895    -45     72   -245       C  
ATOM    399  C   GLY A  75      -1.908  12.123  16.754  1.00 27.52           C  
ANISOU  399  C   GLY A  75     3513   3975   2968    -41     68   -218       C  
ATOM    400  O   GLY A  75      -0.990  12.129  15.928  1.00 29.37           O  
ANISOU  400  O   GLY A  75     3766   4182   3213    -30     62   -203       O  
ATOM    401  N   VAL A  76      -2.922  11.262  16.730  1.00 25.58           N  
ANISOU  401  N   VAL A  76     3264   3737   2718    -51     71   -214       N  
ATOM    402  CA  VAL A  76      -3.074  10.263  15.671  1.00 23.54           C  
ANISOU  402  CA  VAL A  76     3023   3455   2467    -48     67   -191       C  
ATOM    403  C   VAL A  76      -4.457  10.382  15.005  1.00 23.91           C  
ANISOU  403  C   VAL A  76     3063   3495   2528    -42     65   -209       C  
ATOM    404  O   VAL A  76      -5.409  10.829  15.655  1.00 23.71           O  
ANISOU  404  O   VAL A  76     3017   3492   2500    -48     69   -235       O  
ATOM    405  CB  VAL A  76      -2.855   8.824  16.193  0.10 23.34           C  
ANISOU  405  CB  VAL A  76     3003   3441   2423    -65     71   -162       C  
ATOM    406  CG1 VAL A  76      -1.543   8.733  16.959  0.10 23.03           C  
ANISOU  406  CG1 VAL A  76     2968   3411   2371    -71     71   -147       C  
ATOM    407  CG2 VAL A  76      -4.017   8.363  17.061  0.10 23.22           C  
ANISOU  407  CG2 VAL A  76     2972   3458   2393    -84     79   -171       C  
ATOM    408  N   PRO A  77      -4.579  10.051  13.685  1.00 23.09           N  
ANISOU  408  N   PRO A  77     2974   3358   2439    -31     57   -198       N  
ATOM    409  CA  PRO A  77      -5.905   9.765  13.067  1.00 22.19           C  
ANISOU  409  CA  PRO A  77     2857   3239   2336    -29     55   -208       C  
ATOM    410  C   PRO A  77      -6.644   8.528  13.590  1.00 22.25           C  
ANISOU  410  C   PRO A  77     2858   3267   2330    -47     63   -197       C  
ATOM    411  O   PRO A  77      -6.444   7.438  13.110  1.00 22.57           O  
ANISOU  411  O   PRO A  77     2912   3296   2368    -51     63   -171       O  
ATOM    412  CB  PRO A  77      -5.581   9.670  11.563  1.00 23.80           C  
ANISOU  412  CB  PRO A  77     3083   3404   2558    -14     45   -194       C  
ATOM    413  CG  PRO A  77      -4.481  10.642  11.420  1.00 24.25           C  
ANISOU  413  CG  PRO A  77     3147   3447   2619     -4     41   -197       C  
ATOM    414  CD  PRO A  77      -3.618  10.482  12.638  1.00 24.12           C  
ANISOU  414  CD  PRO A  77     3124   3456   2583    -15     49   -189       C  
ATOM    415  N   ALA A  78      -7.429   8.717  14.670  1.00 20.74           N  
ANISOU  415  N   ALA A  78     2645   3110   2127    -61     72   -218       N  
ATOM    416  CA  ALA A  78      -8.112   7.587  15.287  1.00 21.23           C  
ANISOU  416  CA  ALA A  78     2700   3194   2172    -82     81   -209       C  
ATOM    417  C   ALA A  78      -9.273   6.987  14.462  1.00 20.47           C  
ANISOU  417  C   ALA A  78     2603   3087   2088    -81     79   -212       C  
ATOM    418  O   ALA A  78      -9.562   5.814  14.607  1.00 20.86           O  
ANISOU  418  O   ALA A  78     2656   3143   2127    -95     84   -192       O  
ATOM    419  CB  ALA A  78      -8.570   7.903  16.716  1.00 21.62           C  
ANISOU  419  CB  ALA A  78     2726   3285   2202   -101     92   -230       C  
ATOM    420  N   LYS A  79      -9.939   7.785  13.642  1.00 19.68           N  
ANISOU  420  N   LYS A  79     2498   2969   2009    -63     71   -235       N  
ATOM    421  CA  LYS A  79     -10.967   7.272  12.686  1.00 22.49           C  
ANISOU  421  CA  LYS A  79     2856   3309   2380    -58     66   -237       C  
ATOM    422  C   LYS A  79     -10.462   6.083  11.879  1.00 22.85           C  
ANISOU  422  C   LYS A  79     2925   3332   2425    -58     63   -201       C  
ATOM    423  O   LYS A  79     -11.207   5.172  11.558  1.00 21.95           O  
ANISOU  423  O   LYS A  79     2811   3216   2312    -65     65   -194       O  
ATOM    424  CB  LYS A  79     -11.308   8.349  11.678  1.00 20.61           C  
ANISOU  424  CB  LYS A  79     2619   3044   2168    -35     53   -259       C  
ATOM    425  CG  LYS A  79     -12.223   7.840  10.529  1.00 20.82           C  
ANISOU  425  CG  LYS A  79     2652   3049   2211    -27     45   -259       C  
ATOM    426  CD  LYS A  79     -13.050   9.004  10.016  1.00 20.82           C  
ANISOU  426  CD  LYS A  79     2641   3036   2233    -10     32   -294       C  
ATOM    427  CE  LYS A  79     -14.052   8.594   8.938  1.00 23.35           C  
ANISOU  427  CE  LYS A  79     2965   3336   2570     -2     23   -297       C  
ATOM    428  NZ  LYS A  79     -13.568   8.765   7.535  1.00 25.06           N  
ANISOU  428  NZ  LYS A  79     3207   3512   2801     16      7   -282       N  
ATOM    429  N   ASN A  80      -9.205   6.223  11.474  1.00 26.86           N  
ANISOU  429  N   ASN A  80     3451   3819   2934    -49     58   -182       N  
ATOM    430  CA  ASN A  80      -8.490   5.283  10.684  1.00 28.66           C  
ANISOU  430  CA  ASN A  80     3701   4025   3164    -46     55   -150       C  
ATOM    431  C   ASN A  80      -7.290   4.770  11.492  1.00 26.30           C  
ANISOU  431  C   ASN A  80     3408   3737   2848    -57     59   -126       C  
ATOM    432  O   ASN A  80      -6.157   4.905  11.015  1.00 28.35           O  
ANISOU  432  O   ASN A  80     3682   3976   3112    -48     54   -113       O  
ATOM    433  CB  ASN A  80      -7.990   5.966   9.370  1.00 29.28           C  
ANISOU  433  CB  ASN A  80     3796   4067   3261    -25     43   -151       C  
ATOM    434  CG  ASN A  80      -9.111   6.575   8.530  1.00 27.86           C  
ANISOU  434  CG  ASN A  80     3612   3873   3100    -12     35   -174       C  
ATOM    435  OD1 ASN A  80      -9.143   7.792   8.252  1.00 27.35           O  
ANISOU  435  OD1 ASN A  80     3546   3800   3048      1     27   -195       O  
ATOM    436  ND2 ASN A  80     -10.056   5.741   8.139  1.00 27.29           N  
ANISOU  436  ND2 ASN A  80     3538   3800   3032    -16     35   -172       N  
ATOM    437  N   LEU A  81      -7.487   4.222  12.700  1.00 26.40           N  
ANISOU  437  N   LEU A  81     3410   3780   2841    -77     68   -122       N  
ATOM    438  CA  LEU A  81      -6.351   3.603  13.413  1.00 24.02           C  
ANISOU  438  CA  LEU A  81     3118   3486   2524    -88     69    -96       C  
ATOM    439  C   LEU A  81      -6.389   2.078  13.236  1.00 24.12           C  
ANISOU  439  C   LEU A  81     3141   3492   2532    -99     68    -67       C  
ATOM    440  O   LEU A  81      -7.254   1.400  13.779  1.00 23.85           O  
ANISOU  440  O   LEU A  81     3100   3477   2487   -117     73    -66       O  
ATOM    441  CB  LEU A  81      -6.265   4.029  14.896  1.00 23.94           C  
ANISOU  441  CB  LEU A  81     3093   3511   2493   -104     76   -107       C  
ATOM    442  CG  LEU A  81      -4.846   3.795  15.450  1.00 22.94           C  
ANISOU  442  CG  LEU A  81     2976   3385   2355   -107     73    -84       C  
ATOM    443  CD1 LEU A  81      -3.830   4.836  14.987  1.00 24.21           C  
ANISOU  443  CD1 LEU A  81     3142   3528   2528    -88     68    -92       C  
ATOM    444  CD2 LEU A  81      -4.895   3.736  16.972  1.00 21.80           C  
ANISOU  444  CD2 LEU A  81     2820   3278   2184   -129     81    -86       C  
ATOM    445  N   PRO A  82      -5.441   1.534  12.462  1.00 23.42           N  
ANISOU  445  N   PRO A  82     3071   3377   2453    -90     60    -44       N  
ATOM    446  CA  PRO A  82      -5.566   0.106  12.221  1.00 23.76           C  
ANISOU  446  CA  PRO A  82     3123   3412   2494    -99     58    -19       C  
ATOM    447  C   PRO A  82      -5.417  -0.727  13.482  1.00 26.11           C  
ANISOU  447  C   PRO A  82     3418   3733   2770   -122     60     -1       C  
ATOM    448  O   PRO A  82      -4.658  -0.357  14.409  1.00 22.99           O  
ANISOU  448  O   PRO A  82     3021   3353   2362   -128     60      1       O  
ATOM    449  CB  PRO A  82      -4.395  -0.198  11.273  1.00 23.67           C  
ANISOU  449  CB  PRO A  82     3128   3369   2497    -85     50     -1       C  
ATOM    450  CG  PRO A  82      -3.863   1.131  10.840  1.00 22.46           C  
ANISOU  450  CG  PRO A  82     2976   3206   2353    -68     49    -20       C  
ATOM    451  CD  PRO A  82      -4.186   2.076  11.917  1.00 22.20           C  
ANISOU  451  CD  PRO A  82     2927   3201   2308    -74     55    -40       C  
ATOM    452  N   LYS A  83      -6.094  -1.870  13.475  1.00 25.71           N  
ANISOU  452  N   LYS A  83     3370   3684   2715   -136     60     13       N  
ATOM    453  CA  LYS A  83      -5.935  -2.882  14.497  1.00 23.95           C  
ANISOU  453  CA  LYS A  83     3150   3478   2473   -159     59     36       C  
ATOM    454  C   LYS A  83      -4.414  -3.057  14.786  1.00 24.23           C  
ANISOU  454  C   LYS A  83     3197   3503   2507   -155     50     57       C  
ATOM    455  O   LYS A  83      -4.033  -3.193  15.941  1.00 21.39           O  
ANISOU  455  O   LYS A  83     2836   3164   2127   -171     49     66       O  
ATOM    456  CB  LYS A  83      -6.589  -4.184  14.027  1.00 23.22           C  
ANISOU  456  CB  LYS A  83     3063   3374   2384   -168     57     54       C  
ATOM    457  CG  LYS A  83      -8.111  -4.156  14.035  1.00 22.26           C  
ANISOU  457  CG  LYS A  83     2929   3268   2260   -178     67     35       C  
ATOM    458  CD  LYS A  83      -8.671  -4.890  12.824  0.50 22.23           C  
ANISOU  458  CD  LYS A  83     2932   3239   2276   -169     63     41       C  
ATOM    459  CE  LYS A  83     -10.142  -5.214  12.976  0.50 21.96           C  
ANISOU  459  CE  LYS A  83     2886   3222   2237   -184     72     28       C  
ATOM    460  NZ  LYS A  83     -10.402  -6.508  12.319  0.50 21.64           N  
ANISOU  460  NZ  LYS A  83     2856   3162   2205   -187     67     50       N  
ATOM    461  N   TYR A  84      -3.535  -2.926  13.773  1.00 23.47           N  
ANISOU  461  N   TYR A  84     3110   3377   2430   -134     43     60       N  
ATOM    462  CA  TYR A  84      -2.056  -3.046  13.978  1.00 26.17           C  
ANISOU  462  CA  TYR A  84     3461   3709   2774   -129     33     76       C  
ATOM    463  C   TYR A  84      -1.253  -1.917  14.704  1.00 25.61           C  
ANISOU  463  C   TYR A  84     3384   3652   2694   -125     35     63       C  
ATOM    464  O   TYR A  84      -0.001  -2.025  14.914  1.00 26.52           O  
ANISOU  464  O   TYR A  84     3506   3759   2811   -121     27     75       O  
ATOM    465  CB  TYR A  84      -1.366  -3.489  12.677  1.00 27.51           C  
ANISOU  465  CB  TYR A  84     3643   3843   2967   -111     26     86       C  
ATOM    466  CG  TYR A  84      -0.830  -2.367  11.806  1.00 29.80           C  
ANISOU  466  CG  TYR A  84     3934   4118   3272    -90     29     67       C  
ATOM    467  CD1 TYR A  84       0.407  -1.780  12.106  1.00 27.18           C  
ANISOU  467  CD1 TYR A  84     3603   3784   2940    -83     26     66       C  
ATOM    468  CD2 TYR A  84      -1.549  -1.880  10.690  1.00 30.31           C  
ANISOU  468  CD2 TYR A  84     3998   4168   3349    -78     33     51       C  
ATOM    469  CE1 TYR A  84       0.919  -0.754  11.357  1.00 30.65           C  
ANISOU  469  CE1 TYR A  84     4044   4210   3391    -67     28     50       C  
ATOM    470  CE2 TYR A  84      -1.027  -0.845   9.929  1.00 29.18           C  
ANISOU  470  CE2 TYR A  84     3859   4011   3218    -61     34     36       C  
ATOM    471  CZ  TYR A  84       0.205  -0.281  10.273  1.00 30.53           C  
ANISOU  471  CZ  TYR A  84     4030   4181   3387    -56     32     35       C  
ATOM    472  OH  TYR A  84       0.771   0.763   9.550  1.00 29.67           O  
ANISOU  472  OH  TYR A  84     3926   4058   3289    -42     34     21       O  
ATOM    473  N   LEU A  85      -1.958  -0.882  15.134  1.00 22.29           N  
ANISOU  473  N   LEU A  85     2951   3253   2266   -127     45     39       N  
ATOM    474  CA  LEU A  85      -1.374   0.245  15.770  1.00 22.78           C  
ANISOU  474  CA  LEU A  85     3005   3328   2321   -123     48     23       C  
ATOM    475  C   LEU A  85      -2.205   0.474  17.030  1.00 23.51           C  
ANISOU  475  C   LEU A  85     3084   3459   2390   -144     56     12       C  
ATOM    476  O   LEU A  85      -2.336   1.583  17.450  1.00 21.06           O  
ANISOU  476  O   LEU A  85     2762   3164   2076   -141     63    -12       O  
ATOM    477  CB  LEU A  85      -1.415   1.507  14.846  1.00 21.98           C  
ANISOU  477  CB  LEU A  85     2900   3212   2237   -102     51     -2       C  
ATOM    478  CG  LEU A  85      -0.243   1.761  13.855  1.00 21.17           C  
ANISOU  478  CG  LEU A  85     2811   3080   2154    -83     45      2       C  
ATOM    479  CD1 LEU A  85      -0.508   2.844  12.785  1.00 20.49           C  
ANISOU  479  CD1 LEU A  85     2724   2976   2084    -64     47    -20       C  
ATOM    480  CD2 LEU A  85       0.953   2.150  14.689  1.00 21.41           C  
ANISOU  480  CD2 LEU A  85     2840   3119   2176    -84     43      5       C  
ATOM    481  N   GLN A  86      -2.745  -0.579  17.654  1.00 24.07           N  
ANISOU  481  N   GLN A  86     3157   3544   2446   -166     56     29       N  
ATOM    482  CA  GLN A  86      -3.701  -0.357  18.762  1.00 27.75           C  
ANISOU  482  CA  GLN A  86     3608   4047   2888   -188     67     14       C  
ATOM    483  C   GLN A  86      -2.978  -0.121  20.099  1.00 27.48           C  
ANISOU  483  C   GLN A  86     3572   4038   2831   -203     66     19       C  
ATOM    484  O   GLN A  86      -3.572  -0.159  21.209  1.00 30.98           O  
ANISOU  484  O   GLN A  86     4007   4515   3249   -227     74     14       O  
ATOM    485  CB  GLN A  86      -4.821  -1.409  18.799  1.00 29.04           C  
ANISOU  485  CB  GLN A  86     3772   4218   3045   -207     71     24       C  
ATOM    486  CG  GLN A  86      -6.023  -1.103  17.889  1.00 28.92           C  
ANISOU  486  CG  GLN A  86     3748   4196   3046   -197     78      1       C  
ATOM    487  CD  GLN A  86      -6.505   0.342  17.956  1.00 30.38           C  
ANISOU  487  CD  GLN A  86     3914   4393   3234   -187     87    -37       C  
ATOM    488  OE1 GLN A  86      -6.509   0.942  19.022  1.00 32.39           O  
ANISOU  488  OE1 GLN A  86     4157   4677   3472   -199     93    -50       O  
ATOM    489  NE2 GLN A  86      -6.920   0.902  16.817  1.00 29.21           N  
ANISOU  489  NE2 GLN A  86     3764   4224   3111   -166     86    -54       N  
ATOM    490  N   GLN A  87      -1.671   0.106  19.980  1.00 25.10           N  
ANISOU  490  N   GLN A  87     3279   3721   2537   -189     57     28       N  
ATOM    491  CA  GLN A  87      -0.893   0.737  21.026  1.00 24.70           C  
ANISOU  491  CA  GLN A  87     3224   3690   2471   -194     56     24       C  
ATOM    492  C   GLN A  87      -0.971   2.245  20.952  1.00 23.18           C  
ANISOU  492  C   GLN A  87     3017   3504   2285   -180     65    -10       C  
ATOM    493  O   GLN A  87      -0.436   2.934  21.830  1.00 22.24           O  
ANISOU  493  O   GLN A  87     2891   3404   2154   -184     66    -19       O  
ATOM    494  CB  GLN A  87       0.591   0.329  20.983  1.00 26.15           C  
ANISOU  494  CB  GLN A  87     3421   3853   2660   -186     41     47       C  
ATOM    495  CG  GLN A  87       1.370   0.829  19.778  1.00 24.25           C  
ANISOU  495  CG  GLN A  87     3186   3580   2448   -157     37     41       C  
ATOM    496  CD  GLN A  87       1.311  -0.139  18.603  1.00 23.69           C  
ANISOU  496  CD  GLN A  87     3126   3477   2397   -148     31     58       C  
ATOM    497  OE1 GLN A  87       0.250  -0.704  18.275  1.00 22.35           O  
ANISOU  497  OE1 GLN A  87     2957   3309   2228   -156     35     60       O  
ATOM    498  NE2 GLN A  87       2.456  -0.319  17.940  1.00 24.22           N  
ANISOU  498  NE2 GLN A  87     3203   3517   2481   -133     22     68       N  
ATOM    499  N   PHE A  88      -1.590   2.769  19.893  1.00 22.21           N  
ANISOU  499  N   PHE A  88     2890   3365   2183   -163     69    -28       N  
ATOM    500  CA  PHE A  88      -1.739   4.243  19.751  1.00 22.77           C  
ANISOU  500  CA  PHE A  88     2948   3440   2264   -148     75    -62       C  
ATOM    501  C   PHE A  88      -3.120   4.684  20.140  1.00 22.66           C  
ANISOU  501  C   PHE A  88     2915   3451   2243   -158     86    -89       C  
ATOM    502  O   PHE A  88      -3.503   5.884  19.934  1.00 21.65           O  
ANISOU  502  O   PHE A  88     2775   3325   2127   -146     90   -120       O  
ATOM    503  CB  PHE A  88      -1.376   4.729  18.315  1.00 23.27           C  
ANISOU  503  CB  PHE A  88     3019   3467   2356   -121     70    -66       C  
ATOM    504  CG  PHE A  88       0.107   5.053  18.153  1.00 25.25           C  
ANISOU  504  CG  PHE A  88     3279   3700   2614   -108     63    -57       C  
ATOM    505  CD1 PHE A  88       0.643   6.294  18.567  1.00 26.13           C  
ANISOU  505  CD1 PHE A  88     3383   3821   2726   -101     65    -77       C  
ATOM    506  CD2 PHE A  88       0.976   4.096  17.650  1.00 25.09           C  
ANISOU  506  CD2 PHE A  88     3275   3657   2600   -105     54    -30       C  
ATOM    507  CE1 PHE A  88       2.010   6.559  18.462  1.00 24.90           C  
ANISOU  507  CE1 PHE A  88     3235   3651   2576    -91     59    -70       C  
ATOM    508  CE2 PHE A  88       2.341   4.346  17.564  1.00 24.84           C  
ANISOU  508  CE2 PHE A  88     3250   3612   2575    -95     48    -23       C  
ATOM    509  CZ  PHE A  88       2.864   5.574  17.977  1.00 26.41           C  
ANISOU  509  CZ  PHE A  88     3442   3821   2774    -88     51    -43       C  
ATOM    510  N   LYS A  89      -3.827   3.702  20.740  1.00 21.93           N  
ANISOU  510  N   LYS A  89     2822   3378   2132   -182     90    -77       N  
ATOM    511  CA  LYS A  89      -5.223   3.722  21.063  1.00 24.33           C  
ANISOU  511  CA  LYS A  89     3111   3706   2429   -197    102    -98       C  
ATOM    512  C   LYS A  89      -5.629   4.750  22.145  1.00 25.41           C  
ANISOU  512  C   LYS A  89     3225   3878   2550   -207    112   -130       C  
ATOM    513  O   LYS A  89      -6.818   5.137  22.234  1.00 24.27           O  
ANISOU  513  O   LYS A  89     3063   3751   2407   -213    122   -159       O  
ATOM    514  CB  LYS A  89      -5.652   2.325  21.527  1.00 26.61           C  
ANISOU  514  CB  LYS A  89     3406   4005   2698   -223    103    -72       C  
ATOM    515  CG  LYS A  89      -5.525   1.952  23.019  1.00 27.43           C  
ANISOU  515  CG  LYS A  89     3509   4146   2768   -254    107    -63       C  
ATOM    516  CD  LYS A  89      -6.594   0.904  23.404  1.00 26.79           C  
ANISOU  516  CD  LYS A  89     3427   4082   2670   -282    114    -54       C  
ATOM    517  CE  LYS A  89      -7.881   1.073  22.579  1.00 27.91           C  
ANISOU  517  CE  LYS A  89     3556   4219   2829   -274    122    -78       C  
ATOM    518  NZ  LYS A  89      -9.124   0.459  23.095  1.00 27.22           N  
ANISOU  518  NZ  LYS A  89     3459   4158   2725   -303    134    -84       N  
ATOM    519  N   ASN A  90      -4.660   5.186  22.945  1.00 28.40           N  
ANISOU  519  N   ASN A  90     3604   4269   2916   -210    110   -127       N  
ATOM    520  CA  ASN A  90      -4.924   6.196  23.947  1.00 29.06           C  
ANISOU  520  CA  ASN A  90     3668   4386   2987   -219    120   -158       C  
ATOM    521  C   ASN A  90      -4.546   7.587  23.506  1.00 27.68           C  
ANISOU  521  C   ASN A  90     3484   4198   2834   -193    118   -185       C  
ATOM    522  O   ASN A  90      -4.696   8.541  24.260  1.00 25.24           O  
ANISOU  522  O   ASN A  90     3158   3914   2519   -197    124   -213       O  
ATOM    523  CB  ASN A  90      -4.163   5.888  25.237  1.00 29.80           C  
ANISOU  523  CB  ASN A  90     3767   4506   3051   -241    120   -142       C  
ATOM    524  CG  ASN A  90      -4.690   4.677  25.975  1.00 32.47           C  
ANISOU  524  CG  ASN A  90     4109   4866   3361   -273    124   -122       C  
ATOM    525  OD1 ASN A  90      -4.027   4.183  26.895  1.00 36.63           O  
ANISOU  525  OD1 ASN A  90     4646   5408   3864   -292    119   -100       O  
ATOM    526  ND2 ASN A  90      -5.858   4.174  25.580  1.00 32.72           N  
ANISOU  526  ND2 ASN A  90     4136   4899   3396   -281    131   -127       N  
ATOM    527  N   LYS A  91      -4.068   7.749  22.274  1.00 25.17           N  
ANISOU  527  N   LYS A  91     3179   3842   2542   -167    108   -177       N  
ATOM    528  CA  LYS A  91      -3.657   9.055  21.864  1.00 22.82           C  
ANISOU  528  CA  LYS A  91     2876   3530   2264   -145    105   -200       C  
ATOM    529  C   LYS A  91      -4.825   9.901  21.412  1.00 21.91           C  
ANISOU  529  C   LYS A  91     2743   3415   2166   -135    108   -235       C  
ATOM    530  O   LYS A  91      -5.762   9.381  20.817  1.00 22.29           O  
ANISOU  530  O   LYS A  91     2791   3455   2222   -136    109   -236       O  
ATOM    531  CB  LYS A  91      -2.636   9.002  20.713  1.00 22.00           C  
ANISOU  531  CB  LYS A  91     2793   3386   2180   -123     93   -179       C  
ATOM    532  CG  LYS A  91      -1.304   8.334  21.089  1.00 23.31           C  
ANISOU  532  CG  LYS A  91     2974   3548   2335   -128     88   -148       C  
ATOM    533  CD  LYS A  91      -0.348   9.240  21.846  1.00 24.84           C  
ANISOU  533  CD  LYS A  91     3162   3754   2522   -125     87   -158       C  
ATOM    534  CE  LYS A  91       1.037   8.588  21.852  1.00 25.60           C  
ANISOU  534  CE  LYS A  91     3276   3836   2615   -123     78   -127       C  
ATOM    535  NZ  LYS A  91       1.933   9.039  22.958  1.00 25.00           N  
ANISOU  535  NZ  LYS A  91     3195   3780   2524   -130     78   -130       N  
ATOM    536  N   PRO A  92      -4.717  11.219  21.580  1.00 19.78           N  
ANISOU  536  N   PRO A  92     2460   3148   1906   -123    107   -265       N  
ATOM    537  CA  PRO A  92      -5.778  12.031  21.016  1.00 19.82           C  
ANISOU  537  CA  PRO A  92     2451   3147   1933   -111    106   -299       C  
ATOM    538  C   PRO A  92      -5.948  11.806  19.574  1.00 18.47           C  
ANISOU  538  C   PRO A  92     2296   2938   1786    -92     96   -288       C  
ATOM    539  O   PRO A  92      -4.937  11.527  18.864  1.00 18.05           O  
ANISOU  539  O   PRO A  92     2264   2857   1739    -82     89   -261       O  
ATOM    540  CB  PRO A  92      -5.258  13.436  21.159  1.00 19.55           C  
ANISOU  540  CB  PRO A  92     2408   3110   1910    -96    102   -323       C  
ATOM    541  CG  PRO A  92      -4.461  13.383  22.404  1.00 20.06           C  
ANISOU  541  CG  PRO A  92     2469   3203   1949   -112    109   -316       C  
ATOM    542  CD  PRO A  92      -3.840  12.025  22.446  1.00 20.92           C  
ANISOU  542  CD  PRO A  92     2598   3308   2041   -124    109   -274       C  
ATOM    543  N   SER A  93      -7.151  12.099  19.138  1.00 17.84           N  
ANISOU  543  N   SER A  93     2203   2855   1720    -87     96   -312       N  
ATOM    544  CA  SER A  93      -7.444  11.968  17.658  1.00 17.23           C  
ANISOU  544  CA  SER A  93     2141   2739   1668    -69     84   -305       C  
ATOM    545  C   SER A  93      -7.427  13.314  16.943  1.00 18.01           C  
ANISOU  545  C   SER A  93     2238   2814   1793    -45     73   -329       C  
ATOM    546  O   SER A  93      -7.893  14.282  17.492  1.00 17.27           O  
ANISOU  546  O   SER A  93     2122   2735   1703    -43     73   -362       O  
ATOM    547  CB  SER A  93      -8.790  11.340  17.431  1.00 16.23           C  
ANISOU  547  CB  SER A  93     2004   2618   1543    -76     88   -314       C  
ATOM    548  OG  SER A  93      -8.925  10.827  16.054  1.00 16.73           O  
ANISOU  548  OG  SER A  93     2086   2645   1624    -62     78   -296       O  
ATOM    549  N   VAL A  94      -6.934  13.343  15.689  1.00 18.63           N  
ANISOU  549  N   VAL A  94     2338   2854   1887    -28     61   -312       N  
ATOM    550  CA  VAL A  94      -6.926  14.560  14.818  1.00 19.93           C  
ANISOU  550  CA  VAL A  94     2506   2989   2076     -7     47   -330       C  
ATOM    551  C   VAL A  94      -7.890  14.318  13.616  1.00 23.14           C  
ANISOU  551  C   VAL A  94     2920   3370   2502      4     37   -332       C  
ATOM    552  O   VAL A  94      -8.017  15.171  12.730  1.00 24.16           O  
ANISOU  552  O   VAL A  94     3056   3471   2652     21     22   -344       O  
ATOM    553  CB  VAL A  94      -5.487  14.956  14.371  1.00 20.00           C  
ANISOU  553  CB  VAL A  94     2536   2975   2088      3     42   -311       C  
ATOM    554  CG1 VAL A  94      -4.656  15.272  15.583  1.00 20.30           C  
ANISOU  554  CG1 VAL A  94     2565   3039   2109     -6     50   -313       C  
ATOM    555  CG2 VAL A  94      -4.783  13.856  13.588  1.00 20.02           C  
ANISOU  555  CG2 VAL A  94     2564   2958   2086      2     42   -273       C  
ATOM    556  N   GLY A  95      -8.587  13.174  13.676  1.00 23.46           N  
ANISOU  556  N   GLY A  95     2958   3422   2533     -8     44   -322       N  
ATOM    557  CA  GLY A  95      -9.611  12.768  12.699  1.00 24.23           C  
ANISOU  557  CA  GLY A  95     3059   3501   2646     -2     37   -324       C  
ATOM    558  C   GLY A  95      -9.285  11.524  11.924  1.00 24.85           C  
ANISOU  558  C   GLY A  95     3160   3563   2720     -5     37   -288       C  
ATOM    559  O   GLY A  95      -9.019  10.461  12.471  1.00 23.12           O  
ANISOU  559  O   GLY A  95     2943   3361   2482    -21     48   -267       O  
ATOM    560  N   GLY A  96      -9.396  11.671  10.611  1.00 24.60           N  
ANISOU  560  N   GLY A  96     3144   3496   2705     10     24   -284       N  
ATOM    561  CA  GLY A  96      -9.081  10.653   9.589  1.00 26.10           C  
ANISOU  561  CA  GLY A  96     3357   3663   2896     12     22   -253       C  
ATOM    562  C   GLY A  96      -8.232  11.349   8.509  1.00 25.22           C  
ANISOU  562  C   GLY A  96     3268   3516   2796     27     10   -245       C  
ATOM    563  O   GLY A  96      -7.892  12.503   8.650  1.00 26.28           O  
ANISOU  563  O   GLY A  96     3401   3647   2938     35      4   -261       O  
ATOM    564  N   VAL A  97      -7.921  10.690   7.390  1.00 27.49           N  
ANISOU  564  N   VAL A  97     3578   3778   3088     31      5   -222       N  
ATOM    565  CA  VAL A  97      -6.886  11.165   6.452  1.00 28.37           C  
ANISOU  565  CA  VAL A  97     3713   3860   3205     41     -2   -210       C  
ATOM    566  C   VAL A  97      -7.327  12.131   5.283  1.00 30.04           C  
ANISOU  566  C   VAL A  97     3937   4041   3436     56    -21   -223       C  
ATOM    567  O   VAL A  97      -6.492  12.792   4.630  1.00 29.52           O  
ANISOU  567  O   VAL A  97     3889   3953   3374     62    -27   -218       O  
ATOM    568  CB  VAL A  97      -6.145   9.943   5.881  1.00 26.61           C  
ANISOU  568  CB  VAL A  97     3508   3627   2975     35      3   -178       C  
ATOM    569  CG1 VAL A  97      -5.531   9.079   6.990  1.00 24.79           C  
ANISOU  569  CG1 VAL A  97     3271   3423   2727     21     17   -162       C  
ATOM    570  CG2 VAL A  97      -7.109   9.139   5.016  1.00 26.79           C  
ANISOU  570  CG2 VAL A  97     3536   3637   3005     36     -1   -173       C  
ATOM    571  N   GLN A  98      -8.624  12.167   4.954  1.00 34.02           N  
ANISOU  571  N   GLN A  98     4432   4542   3952     61    -29   -240       N  
ATOM    572  CA  GLN A  98      -9.172  13.328   4.194  1.00 34.33           C  
ANISOU  572  CA  GLN A  98     4476   4556   4010     75    -49   -261       C  
ATOM    573  C   GLN A  98     -10.382  13.891   4.917  1.00 34.54           C  
ANISOU  573  C   GLN A  98     4476   4601   4047     78    -54   -295       C  
ATOM    574  O   GLN A  98     -11.213  14.561   4.298  1.00 42.79           O  
ANISOU  574  O   GLN A  98     5520   5628   5111     90    -72   -314       O  
ATOM    575  CB  GLN A  98      -9.551  13.020   2.721  1.00 34.90           C  
ANISOU  575  CB  GLN A  98     4571   4597   4092     82    -63   -250       C  
ATOM    576  CG  GLN A  98      -8.471  12.380   1.811  1.00 33.57           C  
ANISOU  576  CG  GLN A  98     4430   4409   3915     78    -59   -219       C  
ATOM    577  CD  GLN A  98      -8.790  10.924   1.555  1.00 32.06           C  
ANISOU  577  CD  GLN A  98     4240   4222   3717     71    -50   -201       C  
ATOM    578  OE1 GLN A  98      -7.989  10.140   1.031  1.00 25.39           O  
ANISOU  578  OE1 GLN A  98     3413   3370   2866     66    -43   -176       O  
ATOM    579  NE2 GLN A  98      -9.986  10.546   1.975  1.00 34.83           N  
ANISOU  579  NE2 GLN A  98     4573   4590   4073     70    -50   -215       N  
ATOM    580  N   GLN A  99     -10.508  13.568   6.211  1.00 33.02           N  
ANISOU  580  N   GLN A  99     4260   4445   3843     67    -38   -302       N  
ATOM    581  CA  GLN A  99     -11.367  14.289   7.145  1.00 32.40           C  
ANISOU  581  CA  GLN A  99     4151   4387   3771     67    -38   -338       C  
ATOM    582  C   GLN A  99     -10.495  14.643   8.354  1.00 28.37           C  
ANISOU  582  C   GLN A  99     3631   3904   3246     59    -25   -340       C  
ATOM    583  O   GLN A  99     -10.735  14.251   9.519  1.00 29.10           O  
ANISOU  583  O   GLN A  99     3702   4030   3324     45    -10   -347       O  
ATOM    584  CB  GLN A  99     -12.550  13.482   7.589  1.00 31.11           C  
ANISOU  584  CB  GLN A  99     3967   4247   3605     59    -30   -349       C  
ATOM    585  CG  GLN A  99     -13.347  14.194   8.656  1.00 32.34           C  
ANISOU  585  CG  GLN A  99     4091   4431   3767     56    -27   -388       C  
ATOM    586  CD  GLN A  99     -14.788  13.810   8.625  1.00 32.78           C  
ANISOU  586  CD  GLN A  99     4127   4495   3832     55    -29   -410       C  
ATOM    587  OE1 GLN A  99     -15.442  13.935   7.594  1.00 32.28           O  
ANISOU  587  OE1 GLN A  99     4071   4406   3788     68    -46   -416       O  
ATOM    588  NE2 GLN A  99     -15.300  13.340   9.751  1.00 34.03           N  
ANISOU  588  NE2 GLN A  99     4261   4692   3977     38    -11   -423       N  
ATOM    589  N   VAL A 100      -9.448  15.370   8.032  1.00 27.48           N  
ANISOU  589  N   VAL A 100     3534   3772   3134     66    -31   -331       N  
ATOM    590  CA  VAL A 100      -8.560  15.947   9.040  1.00 25.05           C  
ANISOU  590  CA  VAL A 100     3219   3483   2817     61    -22   -335       C  
ATOM    591  C   VAL A 100      -9.167  17.115   9.787  1.00 26.69           C  
ANISOU  591  C   VAL A 100     3401   3704   3036     66    -28   -374       C  
ATOM    592  O   VAL A 100      -9.586  18.122   9.178  1.00 26.77           O  
ANISOU  592  O   VAL A 100     3413   3692   3068     81    -47   -394       O  
ATOM    593  CB  VAL A 100      -7.308  16.472   8.326  1.00 24.19           C  
ANISOU  593  CB  VAL A 100     3134   3346   2709     68    -29   -318       C  
ATOM    594  CG1 VAL A 100      -6.475  17.388   9.187  1.00 22.83           C  
ANISOU  594  CG1 VAL A 100     2955   3187   2534     67    -25   -328       C  
ATOM    595  CG2 VAL A 100      -6.486  15.301   7.867  1.00 21.73           C  
ANISOU  595  CG2 VAL A 100     2843   3028   2384     60    -20   -282       C  
ATOM    596  N   ASP A 101      -9.128  17.016  11.120  1.00 25.04           N  
ANISOU  596  N   ASP A 101     3169   3532   2811     54    -12   -385       N  
ATOM    597  CA  ASP A 101      -9.778  18.000  11.993  1.00 25.61           C  
ANISOU  597  CA  ASP A 101     3213   3625   2893     56    -14   -425       C  
ATOM    598  C   ASP A 101      -8.787  19.028  12.495  1.00 26.66           C  
ANISOU  598  C   ASP A 101     3345   3759   3025     59    -15   -431       C  
ATOM    599  O   ASP A 101      -8.003  18.717  13.394  1.00 26.21           O  
ANISOU  599  O   ASP A 101     3286   3727   2948     47      0   -420       O  
ATOM    600  CB  ASP A 101     -10.442  17.285  13.165  1.00 25.68           C  
ANISOU  600  CB  ASP A 101     3196   3676   2884     37      4   -436       C  
ATOM    601  CG  ASP A 101     -11.438  18.179  13.906  1.00 26.94           C  
ANISOU  601  CG  ASP A 101     3323   3856   3056     39      3   -483       C  
ATOM    602  OD1 ASP A 101     -11.016  19.144  14.597  1.00 28.54           O  
ANISOU  602  OD1 ASP A 101     3514   4069   3260     41      2   -502       O  
ATOM    603  OD2 ASP A 101     -12.651  17.921  13.810  1.00 28.23           O  
ANISOU  603  OD2 ASP A 101     3471   4027   3229     38      1   -502       O  
ATOM    604  N   PHE A 102      -8.778  20.231  11.916  1.00 26.00           N  
ANISOU  604  N   PHE A 102     3266   3649   2964     76    -34   -448       N  
ATOM    605  CA  PHE A 102      -7.768  21.210  12.279  1.00 25.80           C  
ANISOU  605  CA  PHE A 102     3243   3620   2938     79    -36   -452       C  
ATOM    606  C   PHE A 102      -7.812  21.650  13.748  1.00 26.78           C  
ANISOU  606  C   PHE A 102     3337   3783   3054     71    -24   -479       C  
ATOM    607  O   PHE A 102      -6.773  21.755  14.356  1.00 24.71           O  
ANISOU  607  O   PHE A 102     3079   3533   2778     65    -14   -468       O  
ATOM    608  CB  PHE A 102      -7.809  22.415  11.295  1.00 27.80           C  
ANISOU  608  CB  PHE A 102     3510   3834   3219     98    -61   -464       C  
ATOM    609  CG  PHE A 102      -7.585  22.000   9.879  1.00 28.32           C  
ANISOU  609  CG  PHE A 102     3608   3863   3288    103    -71   -436       C  
ATOM    610  CD1 PHE A 102      -6.310  21.703   9.414  1.00 28.15           C  
ANISOU  610  CD1 PHE A 102     3613   3828   3254     99    -65   -403       C  
ATOM    611  CD2 PHE A 102      -8.653  21.842   9.024  1.00 29.03           C  
ANISOU  611  CD2 PHE A 102     3701   3934   3393    111    -86   -442       C  
ATOM    612  CE1 PHE A 102      -6.116  21.296   8.096  1.00 28.04           C  
ANISOU  612  CE1 PHE A 102     3629   3782   3243    102    -74   -378       C  
ATOM    613  CE2 PHE A 102      -8.468  21.451   7.702  1.00 27.78           C  
ANISOU  613  CE2 PHE A 102     3573   3743   3238    115    -96   -416       C  
ATOM    614  CZ  PHE A 102      -7.199  21.161   7.247  1.00 28.05           C  
ANISOU  614  CZ  PHE A 102     3634   3765   3259    109    -89   -384       C  
ATOM    615  N   GLU A 103      -9.013  21.846  14.291  1.00 26.53           N  
ANISOU  615  N   GLU A 103     3278   3772   3031     70    -24   -513       N  
ATOM    616  CA  GLU A 103      -9.190  22.191  15.696  1.00 26.37           C  
ANISOU  616  CA  GLU A 103     3227   3792   3001     59    -10   -541       C  
ATOM    617  C   GLU A 103      -8.576  21.177  16.662  1.00 25.06           C  
ANISOU  617  C   GLU A 103     3059   3660   2801     38     13   -518       C  
ATOM    618  O   GLU A 103      -8.101  21.539  17.762  1.00 23.04           O  
ANISOU  618  O   GLU A 103     2790   3432   2532     29     24   -529       O  
ATOM    619  CB  GLU A 103     -10.681  22.323  16.020  1.00 28.09           C  
ANISOU  619  CB  GLU A 103     3414   4026   3231     59    -12   -581       C  
ATOM    620  CG  GLU A 103     -11.356  23.519  15.349  1.00 29.91           C  
ANISOU  620  CG  GLU A 103     3638   4228   3498     80    -37   -613       C  
ATOM    621  CD  GLU A 103     -11.514  23.373  13.845  1.00 31.98           C  
ANISOU  621  CD  GLU A 103     3928   4446   3777     95    -57   -593       C  
ATOM    622  OE1 GLU A 103     -11.906  22.254  13.390  1.00 30.71           O  
ANISOU  622  OE1 GLU A 103     3777   4284   3607     88    -51   -572       O  
ATOM    623  OE2 GLU A 103     -11.229  24.368  13.127  1.00 30.05           O  
ANISOU  623  OE2 GLU A 103     3697   4167   3554    111    -79   -597       O  
ATOM    624  N   ALA A 104      -8.653  19.890  16.316  1.00 22.47           N  
ANISOU  624  N   ALA A 104     2746   3332   2459     28     21   -488       N  
ATOM    625  CA  ALA A 104      -7.972  18.860  17.108  1.00 22.11           C  
ANISOU  625  CA  ALA A 104     2705   3313   2383      9     39   -461       C  
ATOM    626  C   ALA A 104      -6.475  19.185  17.070  1.00 20.49           C  
ANISOU  626  C   ALA A 104     2518   3095   2172     13     38   -439       C  
ATOM    627  O   ALA A 104      -5.820  19.337  18.094  1.00 17.83           O  
ANISOU  627  O   ALA A 104     2173   2783   1818      3     48   -440       O  
ATOM    628  CB  ALA A 104      -8.261  17.443  16.552  1.00 22.51           C  
ANISOU  628  CB  ALA A 104     2771   3359   2424      1     44   -430       C  
ATOM    629  N   ILE A 105      -5.921  19.288  15.875  1.00 18.52           N  
ANISOU  629  N   ILE A 105     2294   2807   1935     27     26   -419       N  
ATOM    630  CA  ILE A 105      -4.516  19.585  15.684  1.00 18.40           C  
ANISOU  630  CA  ILE A 105     2298   2777   1917     31     24   -399       C  
ATOM    631  C   ILE A 105      -4.068  20.863  16.406  1.00 18.02           C  
ANISOU  631  C   ILE A 105     2236   2738   1873     35     22   -424       C  
ATOM    632  O   ILE A 105      -2.957  20.871  16.889  1.00 18.73           O  
ANISOU  632  O   ILE A 105     2331   2835   1951     31     29   -411       O  
ATOM    633  CB  ILE A 105      -4.060  19.739  14.184  1.00 19.30           C  
ANISOU  633  CB  ILE A 105     2441   2846   2047     45     11   -380       C  
ATOM    634  CG1 ILE A 105      -4.568  18.577  13.299  1.00 19.65           C  
ANISOU  634  CG1 ILE A 105     2500   2876   2090     43     10   -357       C  
ATOM    635  CG2 ILE A 105      -2.549  19.841  14.121  1.00 18.59           C  
ANISOU  635  CG2 ILE A 105     2368   2745   1949     45     13   -358       C  
ATOM    636  CD1 ILE A 105      -4.439  18.776  11.763  1.00 19.96           C  
ANISOU  636  CD1 ILE A 105     2565   2872   2146     56     -5   -345       C  
ATOM    637  N   ASN A 106      -4.855  21.940  16.327  1.00 18.73           N  
ANISOU  637  N   ASN A 106     2311   2822   1985     46     11   -459       N  
ATOM    638  CA  ASN A 106      -4.439  23.221  16.912  1.00 20.38           C  
ANISOU  638  CA  ASN A 106     2507   3035   2201     52      7   -485       C  
ATOM    639  C   ASN A 106      -4.389  23.026  18.413  1.00 20.12           C  
ANISOU  639  C   ASN A 106     2450   3048   2147     36     24   -497       C  
ATOM    640  O   ASN A 106      -3.502  23.516  19.036  1.00 20.68           O  
ANISOU  640  O   ASN A 106     2519   3129   2211     34     28   -498       O  
ATOM    641  CB  ASN A 106      -5.298  24.409  16.480  1.00 20.58           C  
ANISOU  641  CB  ASN A 106     2521   3042   2257     68    -12   -520       C  
ATOM    642  CG  ASN A 106      -5.112  24.709  15.000  1.00 21.43           C  
ANISOU  642  CG  ASN A 106     2657   3101   2383     83    -30   -504       C  
ATOM    643  OD1 ASN A 106      -4.908  25.842  14.537  1.00 24.21           O  
ANISOU  643  OD1 ASN A 106     3015   3427   2756     96    -47   -517       O  
ATOM    644  ND2 ASN A 106      -5.115  23.625  14.241  1.00 19.16           N  
ANISOU  644  ND2 ASN A 106     2390   2802   2088     79    -28   -474       N  
ATOM    645  N   ALA A 107      -5.339  22.252  18.979  1.00 22.02           N  
ANISOU  645  N   ALA A 107     2675   3318   2376     23     35   -504       N  
ATOM    646  CA  ALA A 107      -5.405  22.091  20.481  1.00 21.82           C  
ANISOU  646  CA  ALA A 107     2625   3340   2326      4     52   -519       C  
ATOM    647  C   ALA A 107      -4.284  21.248  21.098  1.00 21.42           C  
ANISOU  647  C   ALA A 107     2587   3306   2246    -11     64   -485       C  
ATOM    648  O   ALA A 107      -4.014  21.342  22.315  1.00 24.28           O  
ANISOU  648  O   ALA A 107     2934   3702   2589    -25     75   -494       O  
ATOM    649  CB  ALA A 107      -6.757  21.567  20.933  1.00 21.69           C  
ANISOU  649  CB  ALA A 107     2587   3350   2305     -9     61   -539       C  
ATOM    650  N   LEU A 108      -3.657  20.407  20.298  1.00 22.98           N  
ANISOU  650  N   LEU A 108     2812   3480   2440     -9     62   -446       N  
ATOM    651  CA  LEU A 108      -2.508  19.639  20.742  1.00 20.70           C  
ANISOU  651  CA  LEU A 108     2537   3200   2129    -20     70   -414       C  
ATOM    652  C   LEU A 108      -1.148  20.398  20.612  1.00 20.70           C  
ANISOU  652  C   LEU A 108     2549   3183   2134    -10     64   -407       C  
ATOM    653  O   LEU A 108      -0.162  19.944  21.185  1.00 22.33           O  
ANISOU  653  O   LEU A 108     2761   3400   2322    -19     70   -387       O  
ATOM    654  CB  LEU A 108      -2.428  18.310  19.990  1.00 19.82           C  
ANISOU  654  CB  LEU A 108     2447   3071   2010    -24     70   -376       C  
ATOM    655  CG  LEU A 108      -3.650  17.430  19.726  1.00 21.46           C  
ANISOU  655  CG  LEU A 108     2651   3285   2217    -32     73   -375       C  
ATOM    656  CD1 LEU A 108      -3.155  16.318  18.811  1.00 22.05           C  
ANISOU  656  CD1 LEU A 108     2753   3334   2290    -30     70   -336       C  
ATOM    657  CD2 LEU A 108      -4.348  16.861  20.984  1.00 20.77           C  
ANISOU  657  CD2 LEU A 108     2545   3242   2106    -55     87   -385       C  
ATOM    658  N   LYS A 109      -1.136  21.558  19.914  1.00 20.34           N  
ANISOU  658  N   LYS A 109     2505   3110   2114      8     53   -425       N  
ATOM    659  CA ALYS A 109       0.057  22.369  19.757  0.50 19.28           C  
ANISOU  659  CA ALYS A 109     2380   2959   1986     17     48   -422       C  
ATOM    660  C   LYS A 109       1.346  21.619  19.356  1.00 19.52           C  
ANISOU  660  C   LYS A 109     2435   2974   2007     15     50   -385       C  
ATOM    661  O   LYS A 109       2.392  21.692  20.110  1.00 19.06           O  
ANISOU  661  O   LYS A 109     2375   2930   1936     10     55   -378       O  
ATOM    662  CB ALYS A 109       0.343  23.144  21.058  0.50 19.55           C  
ANISOU  662  CB ALYS A 109     2392   3024   2012     12     54   -447       C  
ATOM    663  CG ALYS A 109      -0.735  24.150  21.404  0.50 19.44           C  
ANISOU  663  CG ALYS A 109     2353   3021   2013     17     50   -490       C  
ATOM    664  CD ALYS A 109      -0.896  25.301  20.415  0.50 19.11           C  
ANISOU  664  CD ALYS A 109     2316   2941   2002     37     32   -507       C  
ATOM    665  CE ALYS A 109      -2.234  26.013  20.599  0.50 18.61           C  
ANISOU  665  CE ALYS A 109     2227   2886   1957     42     26   -548       C  
ATOM    666  NZ ALYS A 109      -2.607  27.015  19.552  0.50 18.61           N  
ANISOU  666  NZ ALYS A 109     2234   2847   1989     62      5   -564       N  
ATOM    667  CA BLYS A 109       0.040  22.397  19.684  0.50 19.36           C  
ANISOU  667  CA BLYS A 109     2392   2967   1999     18     47   -423       C  
ATOM    668  CB BLYS A 109       0.250  23.447  20.807  0.50 19.95           C  
ANISOU  668  CB BLYS A 109     2443   3066   2071     17     50   -453       C  
ATOM    669  CG BLYS A 109      -0.862  24.509  20.878  0.50 19.34           C  
ANISOU  669  CG BLYS A 109     2344   2990   2013     25     42   -494       C  
ATOM    670  CD BLYS A 109      -0.658  25.861  20.154  0.50 19.16           C  
ANISOU  670  CD BLYS A 109     2326   2935   2020     44     26   -512       C  
ATOM    671  CE BLYS A 109       0.134  25.867  18.858  0.50 18.55           C  
ANISOU  671  CE BLYS A 109     2281   2815   1954     54     16   -484       C  
ATOM    672  NZ BLYS A 109      -0.385  25.005  17.742  0.50 18.06           N  
ANISOU  672  NZ BLYS A 109     2237   2730   1895     56     12   -462       N  
ATOM    673  N   PRO A 110       1.322  20.904  18.207  1.00 19.00           N  
ANISOU  673  N   PRO A 110     2391   2881   1948     19     46   -360       N  
ATOM    674  CA  PRO A 110       2.541  20.170  17.735  1.00 19.00           C  
ANISOU  674  CA  PRO A 110     2412   2865   1941     18     47   -327       C  
ATOM    675  C   PRO A 110       3.794  21.024  17.361  1.00 20.04           C  
ANISOU  675  C   PRO A 110     2557   2976   2083     27     43   -326       C  
ATOM    676  O   PRO A 110       3.695  22.146  16.818  1.00 21.35           O  
ANISOU  676  O   PRO A 110     2724   3122   2267     38     35   -343       O  
ATOM    677  CB  PRO A 110       2.001  19.436  16.496  1.00 19.17           C  
ANISOU  677  CB  PRO A 110     2451   2861   1971     22     43   -310       C  
ATOM    678  CG  PRO A 110       1.141  20.483  15.905  1.00 18.84           C  
ANISOU  678  CG  PRO A 110     2406   2803   1951     34     32   -335       C  
ATOM    679  CD  PRO A 110       0.373  21.086  17.083  1.00 20.00           C  
ANISOU  679  CD  PRO A 110     2523   2981   2093     30     35   -367       C  
ATOM    680  N   ASP A 111       4.995  20.527  17.653  1.00 20.19           N  
ANISOU  680  N   ASP A 111     2582   2998   2090     22     49   -306       N  
ATOM    681  CA  ASP A 111       6.221  21.082  17.001  1.00 21.94           C  
ANISOU  681  CA  ASP A 111     2820   3195   2322     29     46   -300       C  
ATOM    682  C   ASP A 111       6.431  20.562  15.505  1.00 22.04           C  
ANISOU  682  C   ASP A 111     2858   3172   2345     34     42   -278       C  
ATOM    683  O   ASP A 111       7.210  21.131  14.734  1.00 21.78           O  
ANISOU  683  O   ASP A 111     2839   3114   2323     39     39   -277       O  
ATOM    684  CB  ASP A 111       7.461  20.937  17.915  1.00 22.81           C  
ANISOU  684  CB  ASP A 111     2926   3322   2419     23     52   -293       C  
ATOM    685  CG  ASP A 111       7.486  19.617  18.655  1.00 23.51           C  
ANISOU  685  CG  ASP A 111     3011   3434   2487     11     57   -273       C  
ATOM    686  OD1 ASP A 111       6.678  18.779  18.270  1.00 25.44           O  
ANISOU  686  OD1 ASP A 111     3259   3676   2730      8     57   -262       O  
ATOM    687  OD2 ASP A 111       8.314  19.375  19.579  1.00 22.63           O  
ANISOU  687  OD2 ASP A 111     2894   3342   2363      4     60   -267       O  
ATOM    688  N   LEU A 112       5.667  19.556  15.050  1.00 18.97           N  
ANISOU  688  N   LEU A 112     2473   2780   1953     31     42   -265       N  
ATOM    689  CA  LEU A 112       5.824  19.040  13.689  1.00 19.17           C  
ANISOU  689  CA  LEU A 112     2521   2774   1987     34     39   -246       C  
ATOM    690  C   LEU A 112       4.530  18.338  13.243  1.00 19.23           C  
ANISOU  690  C   LEU A 112     2530   2781   1996     34     36   -242       C  
ATOM    691  O   LEU A 112       3.874  17.692  14.052  1.00 20.28           O  
ANISOU  691  O   LEU A 112     2649   2939   2118     26     40   -242       O  
ATOM    692  CB  LEU A 112       6.971  18.052  13.688  1.00 16.23           C  
ANISOU  692  CB  LEU A 112     2159   2402   1607     28     45   -222       C  
ATOM    693  CG  LEU A 112       7.235  17.087  12.499  1.00 14.92           C  
ANISOU  693  CG  LEU A 112     2013   2212   1445     28     45   -199       C  
ATOM    694  CD1 LEU A 112       7.731  18.095  11.453  1.00 14.80           C  
ANISOU  694  CD1 LEU A 112     2012   2168   1443     35     41   -206       C  
ATOM    695  CD2 LEU A 112       8.132  15.881  12.970  1.00 15.98           C  
ANISOU  695  CD2 LEU A 112     2147   2357   1569     21     50   -178       C  
ATOM    696  N   ILE A 113       4.236  18.417  11.948  1.00 19.73           N  
ANISOU  696  N   ILE A 113     2610   2814   2072     40     29   -238       N  
ATOM    697  CA  ILE A 113       3.057  17.817  11.298  1.00 19.48           C  
ANISOU  697  CA  ILE A 113     2583   2776   2045     41     25   -235       C  
ATOM    698  C   ILE A 113       3.629  17.001  10.131  1.00 18.01           C  
ANISOU  698  C   ILE A 113     2419   2564   1860     41     25   -210       C  
ATOM    699  O   ILE A 113       4.332  17.566   9.297  1.00 21.74           O  
ANISOU  699  O   ILE A 113     2908   3013   2341     44     22   -208       O  
ATOM    700  CB  ILE A 113       2.148  18.877  10.626  1.00 19.23           C  
ANISOU  700  CB  ILE A 113     2552   2725   2030     51     12   -255       C  
ATOM    701  CG1 ILE A 113       1.859  20.025  11.563  1.00 20.84           C  
ANISOU  701  CG1 ILE A 113     2737   2945   2238     54      9   -284       C  
ATOM    702  CG2 ILE A 113       0.835  18.225  10.153  1.00 20.07           C  
ANISOU  702  CG2 ILE A 113     2657   2828   2140     52      8   -255       C  
ATOM    703  CD1 ILE A 113       0.556  20.712  11.233  1.00 19.62           C  
ANISOU  703  CD1 ILE A 113     2574   2782   2098     63     -3   -307       C  
ATOM    704  N   ILE A 114       3.403  15.690  10.146  1.00 17.72           N  
ANISOU  704  N   ILE A 114     2383   2535   1816     34     30   -192       N  
ATOM    705  CA  ILE A 114       3.925  14.877   9.000  1.00 17.63           C  
ANISOU  705  CA  ILE A 114     2392   2500   1808     34     30   -171       C  
ATOM    706  C   ILE A 114       2.772  14.355   8.150  1.00 17.94           C  
ANISOU  706  C   ILE A 114     2437   2526   1852     36     25   -167       C  
ATOM    707  O   ILE A 114       1.900  13.711   8.676  1.00 19.30           O  
ANISOU  707  O   ILE A 114     2598   2716   2019     33     27   -167       O  
ATOM    708  CB  ILE A 114       4.778  13.713   9.523  1.00 17.81           C  
ANISOU  708  CB  ILE A 114     2413   2534   1819     26     38   -151       C  
ATOM    709  CG1 ILE A 114       5.997  14.215  10.323  1.00 17.96           C  
ANISOU  709  CG1 ILE A 114     2426   2564   1833     25     42   -154       C  
ATOM    710  CG2 ILE A 114       5.243  12.842   8.373  1.00 16.81           C  
ANISOU  710  CG2 ILE A 114     2305   2385   1698     26     39   -132       C  
ATOM    711  CD1 ILE A 114       6.699  13.170  11.128  1.00 18.16           C  
ANISOU  711  CD1 ILE A 114     2446   2606   1848     17     47   -138       C  
ATOM    712  N   ILE A 115       2.762  14.735   6.864  1.00 19.01           N  
ANISOU  712  N   ILE A 115     2591   2632   1998     41     18   -167       N  
ATOM    713  CA  ILE A 115       1.759  14.276   5.880  1.00 20.46           C  
ANISOU  713  CA  ILE A 115     2785   2800   2188     44     11   -163       C  
ATOM    714  C   ILE A 115       2.301  13.643   4.626  1.00 20.76           C  
ANISOU  714  C   ILE A 115     2845   2814   2228     43     12   -145       C  
ATOM    715  O   ILE A 115       3.479  13.738   4.304  1.00 17.84           O  
ANISOU  715  O   ILE A 115     2486   2436   1858     40     17   -138       O  
ATOM    716  CB  ILE A 115       0.951  15.457   5.343  1.00 21.50           C  
ANISOU  716  CB  ILE A 115     2921   2917   2332     53     -2   -182       C  
ATOM    717  CG1 ILE A 115       1.898  16.583   4.825  1.00 22.70           C  
ANISOU  717  CG1 ILE A 115     3088   3049   2489     55     -6   -186       C  
ATOM    718  CG2 ILE A 115       0.037  15.866   6.472  1.00 21.52           C  
ANISOU  718  CG2 ILE A 115     2899   2944   2335     55     -3   -202       C  
ATOM    719  CD1 ILE A 115       1.413  17.591   3.746  1.00 20.57           C  
ANISOU  719  CD1 ILE A 115     2835   2749   2232     61    -22   -195       C  
ATOM    720  N   SER A 116       1.360  13.075   3.873  1.00 20.01           N  
ANISOU  720  N   SER A 116     2756   2709   2137     44      7   -140       N  
ATOM    721  CA  SER A 116       1.661  12.455   2.585  1.00 17.33           C  
ANISOU  721  CA  SER A 116     2437   2346   1800     43      6   -125       C  
ATOM    722  C   SER A 116       0.554  12.810   1.605  1.00 17.88           C  
ANISOU  722  C   SER A 116     2517   2396   1878     48     -7   -132       C  
ATOM    723  O   SER A 116      -0.118  13.840   1.724  1.00 16.53           O  
ANISOU  723  O   SER A 116     2343   2223   1714     54    -17   -149       O  
ATOM    724  CB  SER A 116       1.859  10.914   2.743  1.00 16.72           C  
ANISOU  724  CB  SER A 116     2357   2279   1717     37     15   -107       C  
ATOM    725  OG  SER A 116       0.733  10.287   3.248  1.00 16.30           O  
ANISOU  725  OG  SER A 116     2290   2241   1663     36     14   -107       O  
ATOM    726  N   GLY A 117       0.383  11.987   0.588  1.00 17.64           N  
ANISOU  726  N   GLY A 117     2502   2352   1850     46     -7   -119       N  
ATOM    727  CA  GLY A 117      -0.330  12.402  -0.566  1.00 18.37           C  
ANISOU  727  CA  GLY A 117     2610   2420   1949     51    -20   -123       C  
ATOM    728  C   GLY A 117      -1.765  12.802  -0.406  1.00 18.77           C  
ANISOU  728  C   GLY A 117     2651   2472   2007     58    -33   -139       C  
ATOM    729  O   GLY A 117      -2.266  13.662  -1.150  1.00 19.21           O  
ANISOU  729  O   GLY A 117     2719   2508   2071     64    -48   -148       O  
ATOM    730  N   ARG A 118      -2.401  12.214   0.609  1.00 19.23           N  
ANISOU  730  N   ARG A 118     2687   2556   2064     58    -27   -142       N  
ATOM    731  CA  ARG A 118      -3.828  12.421   0.822  1.00 18.74           C  
ANISOU  731  CA  ARG A 118     2611   2499   2010     64    -37   -159       C  
ATOM    732  C   ARG A 118      -4.129  13.789   1.429  1.00 20.55           C  
ANISOU  732  C   ARG A 118     2829   2733   2246     71    -46   -183       C  
ATOM    733  O   ARG A 118      -5.302  14.163   1.534  1.00 21.48           O  
ANISOU  733  O   ARG A 118     2936   2852   2374     77    -57   -201       O  
ATOM    734  CB  ARG A 118      -4.403  11.345   1.716  1.00 19.36           C  
ANISOU  734  CB  ARG A 118     2669   2605   2083     59    -27   -156       C  
ATOM    735  CG  ARG A 118      -4.649   9.959   1.141  1.00 17.89           C  
ANISOU  735  CG  ARG A 118     2489   2414   1893     55    -22   -138       C  
ATOM    736  CD  ARG A 118      -5.253   9.161   2.285  1.00 17.28           C  
ANISOU  736  CD  ARG A 118     2389   2366   1810     48    -13   -139       C  
ATOM    737  NE  ARG A 118      -5.854   7.883   1.943  1.00 16.89           N  
ANISOU  737  NE  ARG A 118     2340   2317   1760     44    -10   -126       N  
ATOM    738  CZ  ARG A 118      -5.242   6.716   2.004  1.00 16.44           C  
ANISOU  738  CZ  ARG A 118     2287   2264   1696     36     -1   -105       C  
ATOM    739  NH1 ARG A 118      -3.972   6.658   2.406  1.00 16.37           N  
ANISOU  739  NH1 ARG A 118     2281   2259   1680     32      6    -94       N  
ATOM    740  NH2 ARG A 118      -5.846   5.580   1.662  1.00 17.64           N  
ANISOU  740  NH2 ARG A 118     2439   2415   1849     32      0    -94       N  
ATOM    741  N   GLN A 119      -3.083  14.504   1.873  1.00 22.22           N  
ANISOU  741  N   GLN A 119     3041   2947   2453     69    -42   -184       N  
ATOM    742  CA  GLN A 119      -3.278  15.838   2.482  1.00 22.92           C  
ANISOU  742  CA  GLN A 119     3119   3039   2550     75    -50   -207       C  
ATOM    743  C   GLN A 119      -2.602  16.955   1.750  1.00 25.64           C  
ANISOU  743  C   GLN A 119     3484   3357   2899     78    -61   -209       C  
ATOM    744  O   GLN A 119      -2.728  18.097   2.173  1.00 27.17           O  
ANISOU  744  O   GLN A 119     3671   3551   3102     84    -70   -228       O  
ATOM    745  CB  GLN A 119      -2.791  15.903   3.913  1.00 22.37           C  
ANISOU  745  CB  GLN A 119     3028   3000   2471     71    -37   -214       C  
ATOM    746  CG  GLN A 119      -3.495  15.000   4.878  1.00 21.86           C  
ANISOU  746  CG  GLN A 119     2941   2966   2400     66    -27   -216       C  
ATOM    747  CD  GLN A 119      -2.878  13.647   4.834  1.00 21.37           C  
ANISOU  747  CD  GLN A 119     2886   2910   2326     56    -14   -189       C  
ATOM    748  OE1 GLN A 119      -1.697  13.569   4.510  1.00 21.18           O  
ANISOU  748  OE1 GLN A 119     2876   2876   2297     54     -9   -175       O  
ATOM    749  NE2 GLN A 119      -3.615  12.589   5.193  1.00 19.60           N  
ANISOU  749  NE2 GLN A 119     2650   2702   2096     51     -8   -184       N  
ATOM    750  N   SER A 120      -1.881  16.639   0.697  1.00 25.55           N  
ANISOU  750  N   SER A 120     3498   3326   2884     74    -60   -190       N  
ATOM    751  CA  SER A 120      -1.140  17.594  -0.103  1.00 30.32           C  
ANISOU  751  CA  SER A 120     4125   3905   3491     72    -68   -189       C  
ATOM    752  C   SER A 120      -1.949  18.813  -0.483  1.00 31.77           C  
ANISOU  752  C   SER A 120     4314   4068   3688     81    -91   -207       C  
ATOM    753  O   SER A 120      -1.426  19.917  -0.599  1.00 34.62           O  
ANISOU  753  O   SER A 120     4685   4416   4054     82    -99   -213       O  
ATOM    754  CB  SER A 120      -0.685  16.884  -1.371  1.00 29.80           C  
ANISOU  754  CB  SER A 120     4085   3819   3419     65    -65   -168       C  
ATOM    755  OG  SER A 120       0.310  15.939  -1.063  1.00 29.57           O  
ANISOU  755  OG  SER A 120     4053   3804   3379     57    -45   -153       O  
ATOM    756  N   LYS A 121      -3.237  18.591  -0.707  1.00 33.54           N  
ANISOU  756  N   LYS A 121     4532   4289   3922     88   -103   -215       N  
ATOM    757  CA  LYS A 121      -4.155  19.673  -1.019  1.00 32.15           C  
ANISOU  757  CA  LYS A 121     4358   4095   3763     99   -128   -234       C  
ATOM    758  C   LYS A 121      -4.332  20.703   0.144  1.00 31.65           C  
ANISOU  758  C   LYS A 121     4270   4046   3709    106   -132   -260       C  
ATOM    759  O   LYS A 121      -4.608  21.868  -0.158  1.00 30.92           O  
ANISOU  759  O   LYS A 121     4184   3933   3630    113   -153   -274       O  
ATOM    760  CB  LYS A 121      -5.505  19.086  -1.525  1.00 32.27           C  
ANISOU  760  CB  LYS A 121     4370   4105   3787    105   -140   -239       C  
ATOM    761  CG  LYS A 121      -6.351  18.394  -0.453  1.00 32.70           C  
ANISOU  761  CG  LYS A 121     4391   4191   3842    108   -129   -251       C  
ATOM    762  CD  LYS A 121      -7.511  17.514  -0.930  1.00 32.58           C  
ANISOU  762  CD  LYS A 121     4373   4174   3832    111   -134   -251       C  
ATOM    763  CE  LYS A 121      -8.140  16.812   0.290  1.00 31.77           C  
ANISOU  763  CE  LYS A 121     4237   4108   3726    109   -119   -262       C  
ATOM    764  NZ  LYS A 121      -8.836  15.506   0.097  1.00 30.27           N  
ANISOU  764  NZ  LYS A 121     4042   3926   3532    105   -111   -253       N  
ATOM    765  N   PHE A 122      -4.129  20.295   1.414  1.00 30.20           N  
ANISOU  765  N   PHE A 122     4060   3896   3517    103   -113   -265       N  
ATOM    766  CA  PHE A 122      -4.202  21.201   2.628  1.00 29.81           C  
ANISOU  766  CA  PHE A 122     3986   3867   3475    107   -113   -290       C  
ATOM    767  C   PHE A 122      -2.828  21.676   3.171  1.00 29.54           C  
ANISOU  767  C   PHE A 122     3954   3839   3431    101   -101   -285       C  
ATOM    768  O   PHE A 122      -2.675  21.826   4.416  1.00 28.42           O  
ANISOU  768  O   PHE A 122     3788   3726   3286    100    -90   -298       O  
ATOM    769  CB  PHE A 122      -4.836  20.531   3.854  1.00 31.25           C  
ANISOU  769  CB  PHE A 122     4136   4086   3652    105    -99   -302       C  
ATOM    770  CG  PHE A 122      -6.093  19.766   3.599  1.00 32.51           C  
ANISOU  770  CG  PHE A 122     4288   4249   3817    108   -103   -306       C  
ATOM    771  CD1 PHE A 122      -6.907  20.038   2.518  1.00 32.76           C  
ANISOU  771  CD1 PHE A 122     4333   4252   3864    116   -124   -311       C  
ATOM    772  CD2 PHE A 122      -6.475  18.781   4.500  1.00 33.32           C  
ANISOU  772  CD2 PHE A 122     4368   4384   3909    101    -85   -306       C  
ATOM    773  CE1 PHE A 122      -8.068  19.312   2.322  1.00 33.06           C  
ANISOU  773  CE1 PHE A 122     4361   4294   3906    119   -127   -316       C  
ATOM    774  CE2 PHE A 122      -7.639  18.067   4.325  1.00 35.12           C  
ANISOU  774  CE2 PHE A 122     4586   4616   4140    102    -88   -311       C  
ATOM    775  CZ  PHE A 122      -8.436  18.328   3.223  1.00 33.30           C  
ANISOU  775  CZ  PHE A 122     4369   4358   3927    112   -108   -316       C  
ATOM    776  N   TYR A 123      -1.856  21.916   2.284  1.00 28.37           N  
ANISOU  776  N   TYR A 123     3833   3667   3278     96   -103   -268       N  
ATOM    777  CA  TYR A 123      -0.453  22.104   2.686  1.00 28.46           C  
ANISOU  777  CA  TYR A 123     3848   3685   3279     88    -88   -259       C  
ATOM    778  C   TYR A 123      -0.162  23.476   3.331  1.00 27.68           C  
ANISOU  778  C   TYR A 123     3741   3587   3190     93    -95   -280       C  
ATOM    779  O   TYR A 123       0.648  23.605   4.242  1.00 29.93           O  
ANISOU  779  O   TYR A 123     4013   3891   3467     89    -82   -283       O  
ATOM    780  CB  TYR A 123       0.508  21.892   1.505  1.00 25.38           C  
ANISOU  780  CB  TYR A 123     3490   3271   2881     80    -85   -236       C  
ATOM    781  CG  TYR A 123       1.956  22.220   1.853  1.00 25.32           C  
ANISOU  781  CG  TYR A 123     3486   3268   2865     72    -72   -231       C  
ATOM    782  CD1 TYR A 123       2.634  21.454   2.774  1.00 22.45           C  
ANISOU  782  CD1 TYR A 123     3106   2933   2491     67    -51   -225       C  
ATOM    783  CD2 TYR A 123       2.603  23.346   1.357  1.00 22.54           C  
ANISOU  783  CD2 TYR A 123     3152   2894   2517     69    -80   -234       C  
ATOM    784  CE1 TYR A 123       3.932  21.728   3.152  1.00 23.14           C  
ANISOU  784  CE1 TYR A 123     3195   3026   2573     61    -40   -222       C  
ATOM    785  CE2 TYR A 123       3.899  23.634   1.732  1.00 21.38           C  
ANISOU  785  CE2 TYR A 123     3006   2753   2364     62    -67   -231       C  
ATOM    786  CZ  TYR A 123       4.563  22.802   2.620  1.00 21.28           C  
ANISOU  786  CZ  TYR A 123     2977   2769   2341     59    -47   -225       C  
ATOM    787  OH  TYR A 123       5.834  22.998   3.126  1.00 22.24           O  
ANISOU  787  OH  TYR A 123     3095   2900   2456     53    -33   -224       O  
ATOM    788  N   ASP A 124      -0.825  24.497   2.840  1.00 29.04           N  
ANISOU  788  N   ASP A 124     3919   3735   3378    101   -119   -295       N  
ATOM    789  CA  ASP A 124      -0.618  25.842   3.358  1.00 29.09           C  
ANISOU  789  CA  ASP A 124     3919   3737   3395    106   -129   -315       C  
ATOM    790  C   ASP A 124      -1.194  25.946   4.749  1.00 28.00           C  
ANISOU  790  C   ASP A 124     3744   3633   3262    112   -123   -340       C  
ATOM    791  O   ASP A 124      -0.574  26.482   5.671  1.00 25.14           O  
ANISOU  791  O   ASP A 124     3368   3287   2898    111   -115   -351       O  
ATOM    792  CB  ASP A 124      -1.336  26.853   2.470  1.00 30.89           C  
ANISOU  792  CB  ASP A 124     4163   3930   3642    114   -159   -326       C  
ATOM    793  CG  ASP A 124      -0.785  26.914   1.041  1.00 30.32           C  
ANISOU  793  CG  ASP A 124     4130   3824   3566    106   -167   -303       C  
ATOM    794  OD1 ASP A 124       0.355  26.442   0.785  1.00 33.15           O  
ANISOU  794  OD1 ASP A 124     4502   4184   3907     94   -149   -282       O  
ATOM    795  OD2 ASP A 124      -1.500  27.453   0.180  1.00 31.76           O  
ANISOU  795  OD2 ASP A 124     4329   3977   3761    111   -193   -306       O  
ATOM    796  N   LYS A 125      -2.411  25.448   4.878  1.00 27.06           N  
ANISOU  796  N   LYS A 125     3610   3523   3148    117   -127   -350       N  
ATOM    797  CA  LYS A 125      -3.086  25.438   6.148  1.00 24.92           C  
ANISOU  797  CA  LYS A 125     3303   3285   2879    120   -121   -375       C  
ATOM    798  C   LYS A 125      -2.339  24.665   7.231  1.00 25.33           C  
ANISOU  798  C   LYS A 125     3340   3373   2911    110    -94   -366       C  
ATOM    799  O   LYS A 125      -2.335  25.078   8.375  1.00 25.80           O  
ANISOU  799  O   LYS A 125     3376   3458   2970    110    -87   -385       O  
ATOM    800  CB  LYS A 125      -4.444  24.793   5.990  1.00 24.89           C  
ANISOU  800  CB  LYS A 125     3288   3286   2882    125   -126   -383       C  
ATOM    801  CG  LYS A 125      -5.383  25.418   4.950  1.00 24.02           C  
ANISOU  801  CG  LYS A 125     3190   3141   2794    136   -155   -394       C  
ATOM    802  CD  LYS A 125      -6.794  24.839   5.001  0.10 24.05           C  
ANISOU  802  CD  LYS A 125     3177   3156   2807    141   -160   -409       C  
ATOM    803  CE  LYS A 125      -7.667  25.473   6.077  0.10 24.20           C  
ANISOU  803  CE  LYS A 125     3159   3197   2840    148   -164   -448       C  
ATOM    804  NZ  LYS A 125      -7.452  24.879   7.425  0.10 24.09           N  
ANISOU  804  NZ  LYS A 125     3118   3226   2808    138   -137   -452       N  
ATOM    805  N   LEU A 126      -1.739  23.516   6.929  1.00 22.20           N  
ANISOU  805  N   LEU A 126     2957   2981   2497    101    -79   -337       N  
ATOM    806  CA  LEU A 126      -1.193  22.742   8.088  1.00 22.59           C  
ANISOU  806  CA  LEU A 126     2990   3067   2529     91    -56   -330       C  
ATOM    807  C   LEU A 126       0.045  23.428   8.616  1.00 22.98           C  
ANISOU  807  C   LEU A 126     3039   3120   2572     89    -50   -331       C  
ATOM    808  O   LEU A 126       0.335  23.404   9.804  1.00 20.80           O  
ANISOU  808  O   LEU A 126     2743   2874   2287     84    -38   -339       O  
ATOM    809  CB  LEU A 126      -0.904  21.310   7.662  1.00 22.07           C  
ANISOU  809  CB  LEU A 126     2935   3003   2447     83    -44   -301       C  
ATOM    810  CG  LEU A 126      -2.200  20.521   7.491  1.00 21.25           C  
ANISOU  810  CG  LEU A 126     2824   2905   2346     84    -46   -303       C  
ATOM    811  CD1 LEU A 126      -2.024  19.309   6.573  1.00 21.89           C  
ANISOU  811  CD1 LEU A 126     2925   2974   2420     79    -41   -275       C  
ATOM    812  CD2 LEU A 126      -2.678  20.096   8.876  1.00 20.71           C  
ANISOU  812  CD2 LEU A 126     2726   2876   2268     78    -33   -316       C  
ATOM    813  N   LYS A 127       0.753  24.067   7.691  1.00 22.07           N  
ANISOU  813  N   LYS A 127     2948   2974   2464     90    -58   -323       N  
ATOM    814  CA  LYS A 127       1.980  24.746   8.001  1.00 22.73           C  
ANISOU  814  CA  LYS A 127     3035   3056   2544     87    -53   -323       C  
ATOM    815  C   LYS A 127       1.687  25.932   8.917  1.00 22.61           C  
ANISOU  815  C   LYS A 127     2998   3052   2539     94    -60   -353       C  
ATOM    816  O   LYS A 127       2.536  26.318   9.689  1.00 24.75           O  
ANISOU  816  O   LYS A 127     3261   3338   2805     91    -52   -358       O  
ATOM    817  CB  LYS A 127       2.664  25.230   6.716  1.00 22.54           C  
ANISOU  817  CB  LYS A 127     3044   2997   2526     86    -62   -309       C  
ATOM    818  CG  LYS A 127       4.193  25.200   6.764  1.00 21.76           C  
ANISOU  818  CG  LYS A 127     2954   2897   2415     77    -48   -295       C  
ATOM    819  CD  LYS A 127       4.716  25.589   5.379  1.00 22.08           C  
ANISOU  819  CD  LYS A 127     3028   2902   2460     73    -56   -282       C  
ATOM    820  CE  LYS A 127       6.228  25.705   5.366  1.00 21.99           C  
ANISOU  820  CE  LYS A 127     3026   2890   2440     64    -43   -272       C  
ATOM    821  NZ  LYS A 127       6.882  25.332   4.052  1.00 21.32           N  
ANISOU  821  NZ  LYS A 127     2971   2780   2350     54    -40   -252       N  
ATOM    822  N   GLU A 128       0.469  26.476   8.820  1.00 23.44           N  
ANISOU  822  N   GLU A 128     3094   3150   2661    103    -77   -375       N  
ATOM    823  CA  GLU A 128       0.002  27.569   9.687  1.00 23.40           C  
ANISOU  823  CA  GLU A 128     3064   3156   2669    110    -85   -408       C  
ATOM    824  C   GLU A 128       0.151  27.171  11.138  1.00 22.80           C  
ANISOU  824  C   GLU A 128     2961   3124   2579    104    -66   -417       C  
ATOM    825  O   GLU A 128       0.670  27.942  11.950  1.00 25.60           O  
ANISOU  825  O   GLU A 128     3302   3490   2934    104    -63   -433       O  
ATOM    826  CB  GLU A 128      -1.442  27.978   9.357  1.00 23.22           C  
ANISOU  826  CB  GLU A 128     3034   3122   2668    121   -106   -431       C  
ATOM    827  CG  GLU A 128      -1.627  29.078   8.310  1.00 23.37           C  
ANISOU  827  CG  GLU A 128     3073   3099   2708    130   -133   -437       C  
ATOM    828  CD  GLU A 128      -0.476  29.207   7.356  1.00 23.79           C  
ANISOU  828  CD  GLU A 128     3160   3124   2755    124   -133   -410       C  
ATOM    829  OE1 GLU A 128       0.623  28.873   7.781  1.00 25.05           O  
ANISOU  829  OE1 GLU A 128     3321   3299   2898    115   -114   -396       O  
ATOM    830  OE2 GLU A 128      -0.680  29.628   6.182  1.00 26.76           O  
ANISOU  830  OE2 GLU A 128     3562   3463   3141    127   -153   -403       O  
ATOM    831  N   ILE A 129      -0.203  25.932  11.424  1.00 23.99           N  
ANISOU  831  N   ILE A 129     3105   3296   2715     97    -53   -405       N  
ATOM    832  CA  ILE A 129      -0.205  25.447  12.820  1.00 23.97           C  
ANISOU  832  CA  ILE A 129     3076   3337   2696     88    -35   -413       C  
ATOM    833  C   ILE A 129       1.218  25.049  13.267  1.00 22.84           C  
ANISOU  833  C   ILE A 129     2940   3204   2534     79    -20   -392       C  
ATOM    834  O   ILE A 129       1.644  25.465  14.347  1.00 23.66           O  
ANISOU  834  O   ILE A 129     3026   3332   2631     76    -13   -405       O  
ATOM    835  CB  ILE A 129      -1.176  24.278  12.999  1.00 26.68           C  
ANISOU  835  CB  ILE A 129     3409   3698   3029     82    -28   -408       C  
ATOM    836  CG1 ILE A 129      -2.516  24.568  12.300  1.00 26.78           C  
ANISOU  836  CG1 ILE A 129     3420   3694   3063     92    -44   -425       C  
ATOM    837  CG2 ILE A 129      -1.431  24.046  14.481  1.00 28.12           C  
ANISOU  837  CG2 ILE A 129     3562   3925   3197     73    -13   -424       C  
ATOM    838  CD1 ILE A 129      -3.289  23.335  11.974  1.00 27.88           C  
ANISOU  838  CD1 ILE A 129     3560   3838   3194     87    -39   -412       C  
ATOM    839  N   ALA A 130       1.958  24.301  12.415  1.00 23.51           N  
ANISOU  839  N   ALA A 130     3050   3271   2612     76    -16   -361       N  
ATOM    840  CA  ALA A 130       3.321  23.842  12.734  1.00 23.51           C  
ANISOU  840  CA  ALA A 130     3056   3279   2597     68     -3   -341       C  
ATOM    841  C   ALA A 130       4.126  23.487  11.471  1.00 22.60           C  
ANISOU  841  C   ALA A 130     2971   3134   2484     67     -4   -315       C  
ATOM    842  O   ALA A 130       3.567  23.259  10.398  1.00 22.94           O  
ANISOU  842  O   ALA A 130     3029   3153   2534     70    -12   -308       O  
ATOM    843  CB  ALA A 130       3.277  22.636  13.646  1.00 23.50           C  
ANISOU  843  CB  ALA A 130     3043   3311   2577     58     11   -329       C  
ATOM    844  N   PRO A 131       5.463  23.474  11.577  1.00 26.05           N  
ANISOU  844  N   PRO A 131     3416   3570   2914     63      4   -304       N  
ATOM    845  CA  PRO A 131       6.136  23.079  10.357  1.00 25.33           C  
ANISOU  845  CA  PRO A 131     3350   3450   2823     60      5   -282       C  
ATOM    846  C   PRO A 131       5.671  21.692   9.848  1.00 24.07           C  
ANISOU  846  C   PRO A 131     3198   3291   2658     57      8   -262       C  
ATOM    847  O   PRO A 131       5.493  20.769  10.672  1.00 19.99           O  
ANISOU  847  O   PRO A 131     2667   2800   2129     52     17   -256       O  
ATOM    848  CB  PRO A 131       7.580  23.066  10.797  1.00 28.02           C  
ANISOU  848  CB  PRO A 131     3692   3799   3157     55     15   -275       C  
ATOM    849  CG  PRO A 131       7.650  24.281  11.663  1.00 28.33           C  
ANISOU  849  CG  PRO A 131     3715   3849   3201     59     12   -299       C  
ATOM    850  CD  PRO A 131       6.396  24.164  12.493  1.00 26.57           C  
ANISOU  850  CD  PRO A 131     3470   3649   2976     61     10   -314       C  
ATOM    851  N   THR A 132       5.520  21.582   8.513  1.00 26.68           N  
ANISOU  851  N   THR A 132     3551   3592   2994     58      2   -251       N  
ATOM    852  CA  THR A 132       4.816  20.461   7.829  1.00 24.28           C  
ANISOU  852  CA  THR A 132     3255   3282   2688     57      2   -236       C  
ATOM    853  C   THR A 132       5.686  19.662   6.792  1.00 21.91           C  
ANISOU  853  C   THR A 132     2977   2963   2385     51      8   -212       C  
ATOM    854  O   THR A 132       6.044  20.153   5.763  1.00 22.50           O  
ANISOU  854  O   THR A 132     3073   3013   2465     50      3   -210       O  
ATOM    855  CB  THR A 132       3.476  20.990   7.285  1.00 24.14           C  
ANISOU  855  CB  THR A 132     3238   3250   2682     64    -14   -249       C  
ATOM    856  OG1 THR A 132       2.507  20.965   8.358  1.00 26.14           O  
ANISOU  856  OG1 THR A 132     3466   3530   2935     67    -14   -266       O  
ATOM    857  CG2 THR A 132       2.945  20.191   6.069  1.00 23.69           C  
ANISOU  857  CG2 THR A 132     3200   3173   2628     64    -18   -233       C  
ATOM    858  N   LEU A 133       5.985  18.408   7.111  1.00 19.08           N  
ANISOU  858  N   LEU A 133     2613   2619   2016     46     18   -197       N  
ATOM    859  CA  LEU A 133       7.005  17.634   6.394  1.00 19.36           C  
ANISOU  859  CA  LEU A 133     2665   2643   2049     40     25   -178       C  
ATOM    860  C   LEU A 133       6.219  16.648   5.445  1.00 19.67           C  
ANISOU  860  C   LEU A 133     2715   2670   2090     40     23   -165       C  
ATOM    861  O   LEU A 133       5.310  15.966   5.889  1.00 20.12           O  
ANISOU  861  O   LEU A 133     2760   2740   2143     41     22   -163       O  
ATOM    862  CB  LEU A 133       7.903  16.914   7.423  1.00 19.06           C  
ANISOU  862  CB  LEU A 133     2612   2627   2001     35     36   -170       C  
ATOM    863  CG  LEU A 133       8.805  15.834   6.831  1.00 18.17           C  
ANISOU  863  CG  LEU A 133     2510   2505   1887     30     43   -152       C  
ATOM    864  CD1 LEU A 133       9.889  16.514   6.035  1.00 19.59           C  
ANISOU  864  CD1 LEU A 133     2706   2666   2073     28     46   -155       C  
ATOM    865  CD2 LEU A 133       9.357  14.779   7.807  1.00 17.46           C  
ANISOU  865  CD2 LEU A 133     2407   2438   1790     27     49   -141       C  
ATOM    866  N   PHE A 134       6.592  16.613   4.149  1.00 18.96           N  
ANISOU  866  N   PHE A 134     2647   2554   2004     37     21   -157       N  
ATOM    867  CA  PHE A 134       5.923  15.732   3.130  1.00 19.28           C  
ANISOU  867  CA  PHE A 134     2700   2580   2045     36     19   -145       C  
ATOM    868  C   PHE A 134       6.779  14.501   2.891  1.00 20.41           C  
ANISOU  868  C   PHE A 134     2847   2725   2184     30     29   -128       C  
ATOM    869  O   PHE A 134       7.943  14.631   2.425  1.00 18.57           O  
ANISOU  869  O   PHE A 134     2623   2481   1951     25     36   -125       O  
ATOM    870  CB  PHE A 134       5.726  16.477   1.784  1.00 18.20           C  
ANISOU  870  CB  PHE A 134     2587   2413   1914     36      9   -147       C  
ATOM    871  CG  PHE A 134       5.111  15.638   0.663  1.00 17.79           C  
ANISOU  871  CG  PHE A 134     2550   2346   1863     35      6   -135       C  
ATOM    872  CD1 PHE A 134       3.763  15.368   0.618  1.00 18.23           C  
ANISOU  872  CD1 PHE A 134     2601   2404   1923     41     -4   -138       C  
ATOM    873  CD2 PHE A 134       5.900  15.120  -0.336  1.00 17.71           C  
ANISOU  873  CD2 PHE A 134     2557   2321   1850     27     12   -124       C  
ATOM    874  CE1 PHE A 134       3.231  14.584  -0.417  1.00 16.31           C  
ANISOU  874  CE1 PHE A 134     2370   2146   1680     39     -7   -127       C  
ATOM    875  CE2 PHE A 134       5.373  14.338  -1.346  1.00 15.94           C  
ANISOU  875  CE2 PHE A 134     2345   2084   1626     25     10   -114       C  
ATOM    876  CZ  PHE A 134       4.034  14.093  -1.394  1.00 16.21           C  
ANISOU  876  CZ  PHE A 134     2376   2120   1665     32      0   -115       C  
ATOM    877  N   VAL A 135       6.150  13.333   3.081  1.00 17.96           N  
ANISOU  877  N   VAL A 135     2528   2424   1871     30     30   -118       N  
ATOM    878  CA  VAL A 135       6.770  12.041   3.024  1.00 19.11           C  
ANISOU  878  CA  VAL A 135     2674   2573   2015     26     38   -102       C  
ATOM    879  C   VAL A 135       5.905  11.144   2.157  1.00 17.97           C  
ANISOU  879  C   VAL A 135     2538   2418   1873     26     35    -93       C  
ATOM    880  O   VAL A 135       5.641  10.028   2.497  1.00 18.37           O  
ANISOU  880  O   VAL A 135     2580   2478   1922     24     37    -82       O  
ATOM    881  CB  VAL A 135       6.890  11.420   4.417  1.00 18.16           C  
ANISOU  881  CB  VAL A 135     2533   2479   1888     25     42    -98       C  
ATOM    882  CG1 VAL A 135       7.860  12.245   5.250  1.00 17.65           C  
ANISOU  882  CG1 VAL A 135     2461   2426   1822     24     45   -107       C  
ATOM    883  CG2 VAL A 135       5.523  11.306   5.087  1.00 17.29           C  
ANISOU  883  CG2 VAL A 135     2410   2385   1775     27     37   -102       C  
ATOM    884  N   GLY A 136       5.371  11.692   1.089  1.00 17.79           N  
ANISOU  884  N   GLY A 136     2531   2375   1855     27     28    -97       N  
ATOM    885  CA  GLY A 136       4.760  10.839   0.072  1.00 16.72           C  
ANISOU  885  CA  GLY A 136     2406   2226   1721     27     25    -88       C  
ATOM    886  C   GLY A 136       5.730   9.751  -0.365  1.00 15.66           C  
ANISOU  886  C   GLY A 136     2276   2087   1586     21     35    -75       C  
ATOM    887  O   GLY A 136       6.954   9.893  -0.295  1.00 15.47           O  
ANISOU  887  O   GLY A 136     2253   2063   1562     17     42    -76       O  
ATOM    888  N   LEU A 137       5.184   8.616  -0.777  1.00 15.72           N  
ANISOU  888  N   LEU A 137     2284   2092   1596     20     34    -65       N  
ATOM    889  CA  LEU A 137       5.931   7.608  -1.494  1.00 16.54           C  
ANISOU  889  CA  LEU A 137     2395   2187   1703     15     41    -55       C  
ATOM    890  C   LEU A 137       5.814   7.820  -2.963  1.00 16.24           C  
ANISOU  890  C   LEU A 137     2379   2126   1666     12     39    -56       C  
ATOM    891  O   LEU A 137       4.718   8.084  -3.434  1.00 17.18           O  
ANISOU  891  O   LEU A 137     2506   2238   1786     15     30    -58       O  
ATOM    892  CB  LEU A 137       5.383   6.219  -1.223  1.00 15.99           C  
ANISOU  892  CB  LEU A 137     2315   2124   1634     16     40    -43       C  
ATOM    893  CG  LEU A 137       5.586   5.630   0.163  1.00 16.57           C  
ANISOU  893  CG  LEU A 137     2370   2220   1706     16     42    -37       C  
ATOM    894  CD1 LEU A 137       5.021   4.238   0.261  1.00 18.09           C  
ANISOU  894  CD1 LEU A 137     2557   2416   1901     15     40    -24       C  
ATOM    895  CD2 LEU A 137       7.021   5.604   0.570  1.00 17.36           C  
ANISOU  895  CD2 LEU A 137     2465   2323   1806     13     48    -37       C  
ATOM    896  N   ASP A 138       6.934   7.636  -3.676  1.00 15.75           N  
ANISOU  896  N   ASP A 138     2327   2054   1605      5     47    -56       N  
ATOM    897  CA  ASP A 138       7.013   7.672  -5.152  1.00 16.30           C  
ANISOU  897  CA  ASP A 138     2418   2103   1674     -2     48    -56       C  
ATOM    898  C   ASP A 138       6.707   6.302  -5.728  1.00 15.37           C  
ANISOU  898  C   ASP A 138     2300   1981   1560     -3     50    -47       C  
ATOM    899  O   ASP A 138       7.487   5.337  -5.636  1.00 14.52           O  
ANISOU  899  O   ASP A 138     2183   1877   1457     -5     57    -44       O  
ATOM    900  CB  ASP A 138       8.420   8.155  -5.558  1.00 17.09           C  
ANISOU  900  CB  ASP A 138     2525   2196   1771    -11     58    -63       C  
ATOM    901  CG  ASP A 138       8.588   8.428  -7.028  1.00 17.35           C  
ANISOU  901  CG  ASP A 138     2583   2210   1801    -22     60    -65       C  
ATOM    902  OD1 ASP A 138       7.625   8.194  -7.775  1.00 19.02           O  
ANISOU  902  OD1 ASP A 138     2806   2412   2011    -21     53    -61       O  
ATOM    903  OD2 ASP A 138       9.688   8.923  -7.437  1.00 18.80           O  
ANISOU  903  OD2 ASP A 138     2775   2388   1981    -32     69    -72       O  
ATOM    904  N   ASN A 139       5.577   6.271  -6.396  1.00 16.01           N  
ANISOU  904  N   ASN A 139     2390   2052   1639      0     41    -45       N  
ATOM    905  CA  ASN A 139       5.167   5.058  -7.108  1.00 16.85           C  
ANISOU  905  CA  ASN A 139     2498   2152   1750     -1     41    -38       C  
ATOM    906  C   ASN A 139       6.239   4.492  -8.082  1.00 16.44           C  
ANISOU  906  C   ASN A 139     2456   2091   1700    -11     52    -38       C  
ATOM    907  O   ASN A 139       6.373   3.259  -8.304  1.00 15.13           O  
ANISOU  907  O   ASN A 139     2284   1925   1540    -12     56    -33       O  
ATOM    908  CB  ASN A 139       3.849   5.393  -7.830  1.00 17.02           C  
ANISOU  908  CB  ASN A 139     2534   2164   1770      2     29    -38       C  
ATOM    909  CG  ASN A 139       2.669   5.476  -6.857  1.00 17.06           C  
ANISOU  909  CG  ASN A 139     2524   2181   1777     11     20    -38       C  
ATOM    910  OD1 ASN A 139       2.704   4.864  -5.800  1.00 17.91           O  
ANISOU  910  OD1 ASN A 139     2612   2306   1888     14     24    -34       O  
ATOM    911  ND2 ASN A 139       1.599   6.073  -7.277  1.00 17.49           N  
ANISOU  911  ND2 ASN A 139     2587   2228   1832     16      8    -43       N  
ATOM    912  N   ALA A 140       7.034   5.388  -8.635  1.00 17.86           N  
ANISOU  912  N   ALA A 140     2650   2263   1874    -20     57    -46       N  
ATOM    913  CA  ALA A 140       8.023   4.990  -9.585  1.00 18.37           C  
ANISOU  913  CA  ALA A 140     2723   2319   1939    -31     68    -50       C  
ATOM    914  C   ALA A 140       9.377   4.601  -8.932  1.00 19.11           C  
ANISOU  914  C   ALA A 140     2800   2422   2038    -33     79    -55       C  
ATOM    915  O   ALA A 140      10.229   3.915  -9.486  1.00 16.57           O  
ANISOU  915  O   ALA A 140     2477   2096   1721    -40     89    -59       O  
ATOM    916  CB  ALA A 140       8.144   6.103 -10.606  1.00 19.31           C  
ANISOU  916  CB  ALA A 140     2868   2424   2047    -42     67    -56       C  
ATOM    917  N   ASN A 141       9.570   4.982  -7.684  1.00 18.15           N  
ANISOU  917  N   ASN A 141     2664   2314   1918    -26     77    -55       N  
ATOM    918  CA  ASN A 141      10.865   4.767  -7.033  1.00 16.78           C  
ANISOU  918  CA  ASN A 141     2475   2148   1751    -27     86    -60       C  
ATOM    919  C   ASN A 141      10.599   4.426  -5.531  1.00 15.87           C  
ANISOU  919  C   ASN A 141     2339   2050   1639    -16     79    -52       C  
ATOM    920  O   ASN A 141      11.020   5.184  -4.633  1.00 14.90           O  
ANISOU  920  O   ASN A 141     2209   1937   1514    -14     80    -56       O  
ATOM    921  CB  ASN A 141      11.674   6.084  -7.101  1.00 17.00           C  
ANISOU  921  CB  ASN A 141     2512   2174   1772    -35     92    -71       C  
ATOM    922  CG  ASN A 141      12.031   6.485  -8.543  1.00 17.30           C  
ANISOU  922  CG  ASN A 141     2573   2197   1804    -49     99    -78       C  
ATOM    923  OD1 ASN A 141      12.748   5.752  -9.270  1.00 18.28           O  
ANISOU  923  OD1 ASN A 141     2697   2317   1932    -57    109    -83       O  
ATOM    924  ND2 ASN A 141      11.585   7.669  -8.949  1.00 18.99           N  
ANISOU  924  ND2 ASN A 141     2805   2402   2007    -54     94    -79       N  
ATOM    925  N   PHE A 142       9.864   3.334  -5.295  1.00 15.38           N  
ANISOU  925  N   PHE A 142     2270   1992   1583    -11     73    -42       N  
ATOM    926  CA  PHE A 142       9.232   3.077  -3.959  1.00 14.46           C  
ANISOU  926  CA  PHE A 142     2137   1891   1466     -2     65    -33       C  
ATOM    927  C   PHE A 142      10.369   2.924  -2.931  1.00 15.06           C  
ANISOU  927  C   PHE A 142     2198   1979   1546     -2     68    -34       C  
ATOM    928  O   PHE A 142      10.380   3.608  -1.951  1.00 13.10           O  
ANISOU  928  O   PHE A 142     1942   1743   1292      1     66    -35       O  
ATOM    929  CB  PHE A 142       8.381   1.799  -3.938  1.00 15.38           C  
ANISOU  929  CB  PHE A 142     2248   2008   1587      1     60    -21       C  
ATOM    930  CG  PHE A 142       7.998   1.360  -2.559  1.00 14.85           C  
ANISOU  930  CG  PHE A 142     2165   1959   1520      5     53    -11       C  
ATOM    931  CD1 PHE A 142       8.893   0.643  -1.774  1.00 15.23           C  
ANISOU  931  CD1 PHE A 142     2200   2014   1574      5     53     -6       C  
ATOM    932  CD2 PHE A 142       6.799   1.738  -2.031  1.00 15.93           C  
ANISOU  932  CD2 PHE A 142     2299   2105   1648      8     48     -9       C  
ATOM    933  CE1 PHE A 142       8.575   0.321  -0.483  1.00 14.84           C  
ANISOU  933  CE1 PHE A 142     2138   1980   1520      7     46      3       C  
ATOM    934  CE2 PHE A 142       6.453   1.353  -0.727  1.00 13.02           C  
ANISOU  934  CE2 PHE A 142     1916   1755   1277      9     43     -1       C  
ATOM    935  CZ  PHE A 142       7.367   0.647   0.007  1.00 13.70           C  
ANISOU  935  CZ  PHE A 142     1992   1847   1367      8     43      6       C  
ATOM    936  N   LEU A 143      11.350   2.074  -3.214  1.00 14.29           N  
ANISOU  936  N   LEU A 143     2095   1876   1459     -4     72    -35       N  
ATOM    937  CA  LEU A 143      12.419   1.754  -2.192  1.00 17.10           C  
ANISOU  937  CA  LEU A 143     2435   2241   1821     -2     71    -36       C  
ATOM    938  C   LEU A 143      13.286   2.998  -1.884  1.00 17.98           C  
ANISOU  938  C   LEU A 143     2547   2358   1928     -4     77    -49       C  
ATOM    939  O   LEU A 143      13.455   3.408  -0.691  1.00 18.17           O  
ANISOU  939  O   LEU A 143     2560   2395   1948     -1     73    -47       O  
ATOM    940  CB  LEU A 143      13.258   0.549  -2.684  1.00 17.17           C  
ANISOU  940  CB  LEU A 143     2437   2240   1845     -3     72    -37       C  
ATOM    941  CG  LEU A 143      13.488  -0.802  -1.927  1.00 17.37           C  
ANISOU  941  CG  LEU A 143     2448   2269   1883      1     62    -27       C  
ATOM    942  CD1 LEU A 143      14.976  -1.193  -2.024  1.00 17.56           C  
ANISOU  942  CD1 LEU A 143     2462   2287   1922      0     65    -38       C  
ATOM    943  CD2 LEU A 143      12.993  -0.884  -0.434  1.00 17.56           C  
ANISOU  943  CD2 LEU A 143     2462   2309   1899      5     51    -13       C  
ATOM    944  N   SER A 144      13.742   3.676  -2.945  1.00 15.10           N  
ANISOU  944  N   SER A 144     2194   1981   1561    -11     87    -61       N  
ATOM    945  CA  SER A 144      14.458   4.994  -2.757  1.00 17.47           C  
ANISOU  945  CA  SER A 144     2499   2284   1857    -15     93    -73       C  
ATOM    946  C   SER A 144      13.687   5.908  -1.778  1.00 14.59           C  
ANISOU  946  C   SER A 144     2131   1931   1481     -9     86    -69       C  
ATOM    947  O   SER A 144      14.279   6.427  -0.776  1.00 13.89           O  
ANISOU  947  O   SER A 144     2032   1854   1392     -7     86    -74       O  
ATOM    948  CB  SER A 144      14.693   5.740  -4.099  1.00 18.12           C  
ANISOU  948  CB  SER A 144     2600   2351   1933    -26    102    -83       C  
ATOM    949  OG  SER A 144      15.353   4.946  -5.062  1.00 21.98           O  
ANISOU  949  OG  SER A 144     3090   2830   2430    -33    110    -89       O  
ATOM    950  N   SER A 145      12.345   6.036  -1.974  1.00 13.74           N  
ANISOU  950  N   SER A 145     2031   1822   1367     -6     80    -62       N  
ATOM    951  CA  SER A 145      11.565   7.091  -1.270  1.00 13.65           C  
ANISOU  951  CA  SER A 145     2020   1820   1348     -2     74    -64       C  
ATOM    952  C   SER A 145      11.300   6.592   0.123  1.00 13.54           C  
ANISOU  952  C   SER A 145     1987   1825   1333      4     68    -57       C  
ATOM    953  O   SER A 145      11.331   7.371   1.018  1.00 14.94           O  
ANISOU  953  O   SER A 145     2157   2014   1505      6     67    -61       O  
ATOM    954  CB  SER A 145      10.211   7.473  -1.889  1.00 14.86           C  
ANISOU  954  CB  SER A 145     2185   1965   1496      0     67    -62       C  
ATOM    955  OG  SER A 145       9.533   6.354  -2.370  1.00 15.18           O  
ANISOU  955  OG  SER A 145     2227   2001   1539      1     64    -52       O  
ATOM    956  N   PHE A 146      11.054   5.293   0.263  1.00 13.05           N  
ANISOU  956  N   PHE A 146     1918   1765   1275      5     65    -45       N  
ATOM    957  CA  PHE A 146      10.728   4.717   1.593  1.00 13.58           C  
ANISOU  957  CA  PHE A 146     1970   1851   1340      8     58    -35       C  
ATOM    958  C   PHE A 146      11.926   4.994   2.515  1.00 13.39           C  
ANISOU  958  C   PHE A 146     1934   1836   1316      8     60    -40       C  
ATOM    959  O   PHE A 146      11.776   5.492   3.648  1.00 14.48           O  
ANISOU  959  O   PHE A 146     2063   1992   1446     10     57    -41       O  
ATOM    960  CB  PHE A 146      10.465   3.211   1.440  1.00 13.30           C  
ANISOU  960  CB  PHE A 146     1931   1812   1310      8     54    -22       C  
ATOM    961  CG  PHE A 146      10.443   2.408   2.728  1.00 15.40           C  
ANISOU  961  CG  PHE A 146     2183   2093   1574      8     47    -10       C  
ATOM    962  CD1 PHE A 146      11.597   1.963   3.289  1.00 16.81           C  
ANISOU  962  CD1 PHE A 146     2354   2275   1759      8     44     -8       C  
ATOM    963  CD2 PHE A 146       9.225   2.098   3.345  1.00 17.85           C  
ANISOU  963  CD2 PHE A 146     2489   2415   1876      7     41      0       C  
ATOM    964  CE1 PHE A 146      11.592   1.192   4.469  1.00 17.47           C  
ANISOU  964  CE1 PHE A 146     2426   2371   1840      7     35      5       C  
ATOM    965  CE2 PHE A 146       9.177   1.320   4.514  1.00 17.35           C  
ANISOU  965  CE2 PHE A 146     2416   2368   1809      4     34     12       C  
ATOM    966  CZ  PHE A 146      10.375   0.900   5.098  1.00 17.01           C  
ANISOU  966  CZ  PHE A 146     2366   2326   1771      4     30     16       C  
ATOM    967  N   GLU A 147      13.110   4.647   2.036  1.00 13.56           N  
ANISOU  967  N   GLU A 147     1957   1849   1348      6     64    -44       N  
ATOM    968  CA  GLU A 147      14.349   4.820   2.804  1.00 14.13           C  
ANISOU  968  CA  GLU A 147     2017   1927   1422      7     65    -50       C  
ATOM    969  C   GLU A 147      14.565   6.311   3.192  1.00 13.43           C  
ANISOU  969  C   GLU A 147     1930   1847   1327      7     69    -63       C  
ATOM    970  O   GLU A 147      14.900   6.750   4.375  1.00 14.98           O  
ANISOU  970  O   GLU A 147     2115   2059   1518      8     66    -65       O  
ATOM    971  CB  GLU A 147      15.509   4.327   1.999  1.00 15.19           C  
ANISOU  971  CB  GLU A 147     2153   2048   1570      4     70    -57       C  
ATOM    972  CG  GLU A 147      15.628   2.830   1.986  1.00 17.08           C  
ANISOU  972  CG  GLU A 147     2385   2283   1820      6     63    -47       C  
ATOM    973  CD  GLU A 147      16.933   2.360   1.428  1.00 19.04           C  
ANISOU  973  CD  GLU A 147     2629   2520   2085      4     67    -57       C  
ATOM    974  OE1 GLU A 147      17.957   2.835   1.884  1.00 21.76           O  
ANISOU  974  OE1 GLU A 147     2966   2868   2432      4     69    -68       O  
ATOM    975  OE2 GLU A 147      16.896   1.511   0.495  1.00 23.30           O  
ANISOU  975  OE2 GLU A 147     3172   3047   2634      3     68    -57       O  
ATOM    976  N   ASN A 148      14.454   7.100   2.146  1.00 14.06           N  
ANISOU  976  N   ASN A 148     2023   1913   1405      3     76    -72       N  
ATOM    977  CA  ASN A 148      14.449   8.570   2.274  1.00 13.73           C  
ANISOU  977  CA  ASN A 148     1986   1873   1356      3     78    -83       C  
ATOM    978  C   ASN A 148      13.536   9.046   3.424  1.00 12.19           C  
ANISOU  978  C   ASN A 148     1782   1696   1152      8     71    -81       C  
ATOM    979  O   ASN A 148      13.899   9.894   4.263  1.00 14.06           O  
ANISOU  979  O   ASN A 148     2011   1944   1386      9     72    -89       O  
ATOM    980  CB  ASN A 148      14.032   9.273   1.000  1.00 15.59           C  
ANISOU  980  CB  ASN A 148     2242   2092   1591     -2     82    -89       C  
ATOM    981  CG  ASN A 148      14.317  10.759   0.993  1.00 15.03           C  
ANISOU  981  CG  ASN A 148     2177   2019   1516     -4     85   -101       C  
ATOM    982  OD1 ASN A 148      13.424  11.539   0.588  1.00 16.01           O  
ANISOU  982  OD1 ASN A 148     2312   2135   1634     -4     80   -103       O  
ATOM    983  ND2 ASN A 148      15.547  11.176   1.347  1.00 15.59           N  
ANISOU  983  ND2 ASN A 148     2242   2093   1589     -7     91   -111       N  
ATOM    984  N   ASN A 149      12.284   8.595   3.390  1.00 12.08           N  
ANISOU  984  N   ASN A 149     1771   1685   1136     10     66    -72       N  
ATOM    985  CA  ASN A 149      11.321   9.043   4.373  1.00 11.59           C  
ANISOU  985  CA  ASN A 149     1699   1639   1065     13     60    -73       C  
ATOM    986  C   ASN A 149      11.733   8.569   5.752  1.00 11.46           C  
ANISOU  986  C   ASN A 149     1666   1644   1044     13     58    -68       C  
ATOM    987  O   ASN A 149      11.672   9.336   6.724  1.00 11.55           O  
ANISOU  987  O   ASN A 149     1669   1672   1049     14     57    -75       O  
ATOM    988  CB  ASN A 149       9.897   8.603   4.111  1.00 12.21           C  
ANISOU  988  CB  ASN A 149     1780   1718   1141     14     55    -66       C  
ATOM    989  CG  ASN A 149       9.343   9.167   2.835  1.00 12.69           C  
ANISOU  989  CG  ASN A 149     1858   1759   1205     15     55    -72       C  
ATOM    990  OD1 ASN A 149       9.745  10.264   2.364  1.00 13.70           O  
ANISOU  990  OD1 ASN A 149     1995   1876   1333     14     57    -83       O  
ATOM    991  ND2 ASN A 149       8.406   8.458   2.278  1.00 12.42           N  
ANISOU  991  ND2 ASN A 149     1829   1719   1172     15     52    -64       N  
ATOM    992  N   VAL A 150      12.076   7.314   5.821  1.00 12.04           N  
ANISOU  992  N   VAL A 150     1737   1717   1122     11     56    -55       N  
ATOM    993  CA  VAL A 150      12.440   6.759   7.133  1.00 12.19           C  
ANISOU  993  CA  VAL A 150     1741   1754   1135     10     50    -48       C  
ATOM    994  C   VAL A 150      13.745   7.375   7.638  1.00 12.48           C  
ANISOU  994  C   VAL A 150     1772   1795   1175     11     53    -57       C  
ATOM    995  O   VAL A 150      13.804   7.836   8.835  1.00 11.32           O  
ANISOU  995  O   VAL A 150     1615   1668   1019     11     50    -60       O  
ATOM    996  CB  VAL A 150      12.551   5.243   7.018  1.00 12.69           C  
ANISOU  996  CB  VAL A 150     1804   1812   1205      9     45    -31       C  
ATOM    997  CG1 VAL A 150      13.331   4.640   8.183  1.00 13.35           C  
ANISOU  997  CG1 VAL A 150     1877   1908   1287      7     37    -24       C  
ATOM    998  CG2 VAL A 150      11.184   4.636   6.879  1.00 13.05           C  
ANISOU  998  CG2 VAL A 150     1853   1860   1247      7     42    -21       C  
ATOM    999  N   LEU A 151      14.783   7.436   6.831  1.00 11.89           N  
ANISOU  999  N   LEU A 151     1702   1704   1111     11     58    -64       N  
ATOM   1000  CA  LEU A 151      16.042   7.994   7.313  1.00 13.19           C  
ANISOU 1000  CA  LEU A 151     1860   1873   1279     12     60    -75       C  
ATOM   1001  C   LEU A 151      15.899   9.520   7.712  1.00 13.27           C  
ANISOU 1001  C   LEU A 151     1869   1892   1281     12     64    -89       C  
ATOM   1002  O   LEU A 151      16.561  10.027   8.683  1.00 13.11           O  
ANISOU 1002  O   LEU A 151     1839   1885   1258     13     63    -96       O  
ATOM   1003  CB  LEU A 151      17.176   7.701   6.337  1.00 14.74           C  
ANISOU 1003  CB  LEU A 151     2060   2051   1489     10     66    -81       C  
ATOM   1004  CG  LEU A 151      17.492   6.227   6.283  1.00 15.05           C  
ANISOU 1004  CG  LEU A 151     2096   2085   1538     11     59    -70       C  
ATOM   1005  CD1 LEU A 151      18.276   6.000   4.948  1.00 16.61           C  
ANISOU 1005  CD1 LEU A 151     2299   2262   1749      9     67    -79       C  
ATOM   1006  CD2 LEU A 151      18.271   5.715   7.513  1.00 16.89           C  
ANISOU 1006  CD2 LEU A 151     2314   2330   1773     13     49    -65       C  
ATOM   1007  N   SER A 152      15.072  10.277   6.988  1.00 12.76           N  
ANISOU 1007  N   SER A 152     1816   1819   1214     12     67    -95       N  
ATOM   1008  CA  SER A 152      14.903  11.705   7.158  1.00 13.57           C  
ANISOU 1008  CA  SER A 152     1919   1924   1312     13     69   -109       C  
ATOM   1009  C   SER A 152      14.232  11.936   8.528  1.00 14.91           C  
ANISOU 1009  C   SER A 152     2075   2118   1471     15     64   -109       C  
ATOM   1010  O   SER A 152      14.510  12.969   9.226  1.00 16.32           O  
ANISOU 1010  O   SER A 152     2246   2307   1646     16     65   -122       O  
ATOM   1011  CB  SER A 152      14.035  12.252   6.033  1.00 13.41           C  
ANISOU 1011  CB  SER A 152     1915   1887   1293     13     70   -112       C  
ATOM   1012  OG  SER A 152      14.758  12.430   4.836  1.00 13.28           O  
ANISOU 1012  OG  SER A 152     1912   1850   1283      8     77   -116       O  
ATOM   1013  N   VAL A 153      13.344  10.994   8.879  1.00 14.60           N  
ANISOU 1013  N   VAL A 153     2031   2088   1427     15     59    -96       N  
ATOM   1014  CA  VAL A 153      12.594  11.111  10.091  1.00 14.47           C  
ANISOU 1014  CA  VAL A 153     2003   2096   1399     14     55    -96       C  
ATOM   1015  C   VAL A 153      13.566  10.717  11.187  1.00 14.65           C  
ANISOU 1015  C   VAL A 153     2015   2134   1418     12     53    -92       C  
ATOM   1016  O   VAL A 153      13.614  11.401  12.207  1.00 16.21           O  
ANISOU 1016  O   VAL A 153     2203   2351   1608     11     52   -101       O  
ATOM   1017  CB  VAL A 153      11.346  10.224  10.160  1.00 15.13           C  
ANISOU 1017  CB  VAL A 153     2086   2185   1477     11     52    -85       C  
ATOM   1018  CG1 VAL A 153      10.786  10.360  11.535  1.00 15.05           C  
ANISOU 1018  CG1 VAL A 153     2062   2204   1453      8     49    -87       C  
ATOM   1019  CG2 VAL A 153      10.277  10.657   9.190  1.00 14.59           C  
ANISOU 1019  CG2 VAL A 153     2026   2103   1412     14     52    -90       C  
ATOM   1020  N   ALA A 154      14.318   9.647  10.986  1.00 14.06           N  
ANISOU 1020  N   ALA A 154     1942   2052   1350     11     50    -80       N  
ATOM   1021  CA  ALA A 154      15.253   9.174  12.046  1.00 14.04           C  
ANISOU 1021  CA  ALA A 154     1929   2062   1344      9     44    -75       C  
ATOM   1022  C   ALA A 154      16.321  10.252  12.371  1.00 15.45           C  
ANISOU 1022  C   ALA A 154     2102   2243   1525     12     48    -91       C  
ATOM   1023  O   ALA A 154      16.559  10.628  13.578  1.00 16.18           O  
ANISOU 1023  O   ALA A 154     2184   2356   1608     10     44    -95       O  
ATOM   1024  CB  ALA A 154      15.893   7.879  11.649  1.00 14.39           C  
ANISOU 1024  CB  ALA A 154     1976   2093   1399      9     39    -61       C  
ATOM   1025  N   LYS A 155      16.864  10.883  11.336  1.00 16.01           N  
ANISOU 1025  N   LYS A 155     2182   2295   1608     14     55   -103       N  
ATOM   1026  CA  LYS A 155      17.775  12.047  11.482  1.00 16.12           C  
ANISOU 1026  CA  LYS A 155     2192   2309   1624     15     61   -120       C  
ATOM   1027  C   LYS A 155      17.295  13.079  12.522  1.00 14.77           C  
ANISOU 1027  C   LYS A 155     2011   2158   1441     16     60   -130       C  
ATOM   1028  O   LYS A 155      18.076  13.513  13.325  1.00 15.08           O  
ANISOU 1028  O   LYS A 155     2041   2208   1479     16     59   -138       O  
ATOM   1029  CB  LYS A 155      18.034  12.740  10.138  1.00 18.33           C  
ANISOU 1029  CB  LYS A 155     2485   2566   1914     15     69   -130       C  
ATOM   1030  CG  LYS A 155      19.325  13.528  10.037  1.00 20.05           C  
ANISOU 1030  CG  LYS A 155     2700   2778   2138     14     76   -146       C  
ATOM   1031  CD  LYS A 155      19.972  13.337   8.656  1.00 21.12           C  
ANISOU 1031  CD  LYS A 155     2848   2891   2286     10     84   -149       C  
ATOM   1032  CE  LYS A 155      21.002  14.406   8.352  1.00 23.29           C  
ANISOU 1032  CE  LYS A 155     3125   3159   2566      7     92   -167       C  
ATOM   1033  NZ  LYS A 155      21.197  14.616   6.882  1.00 23.37           N  
ANISOU 1033  NZ  LYS A 155     3152   3147   2582      0    102   -171       N  
ATOM   1034  N   LEU A 156      16.023  13.377  12.546  1.00 13.82           N  
ANISOU 1034  N   LEU A 156     1893   2044   1314     16     59   -131       N  
ATOM   1035  CA  LEU A 156      15.512  14.488  13.334  1.00 16.01           C  
ANISOU 1035  CA  LEU A 156     2161   2338   1584     16     60   -145       C  
ATOM   1036  C   LEU A 156      15.788  14.074  14.786  1.00 15.03           C  
ANISOU 1036  C   LEU A 156     2023   2240   1448     13     55   -140       C  
ATOM   1037  O   LEU A 156      16.122  14.957  15.619  1.00 18.54           O  
ANISOU 1037  O   LEU A 156     2458   2699   1888     13     56   -154       O  
ATOM   1038  CB  LEU A 156      14.042  14.656  13.133  1.00 16.04           C  
ANISOU 1038  CB  LEU A 156     2167   2344   1583     17     59   -146       C  
ATOM   1039  CG  LEU A 156      13.437  14.956  11.790  1.00 18.09           C  
ANISOU 1039  CG  LEU A 156     2441   2580   1852     19     60   -148       C  
ATOM   1040  CD1 LEU A 156      11.915  14.973  11.984  1.00 18.21           C  
ANISOU 1040  CD1 LEU A 156     2453   2605   1862     20     57   -150       C  
ATOM   1041  CD2 LEU A 156      13.963  16.288  11.324  1.00 18.26           C  
ANISOU 1041  CD2 LEU A 156     2468   2588   1881     22     63   -165       C  
ATOM   1042  N   TYR A 157      15.751  12.775  15.050  1.00 15.84           N  
ANISOU 1042  N   TYR A 157     2125   2347   1546      9     49   -122       N  
ATOM   1043  CA  TYR A 157      16.015  12.171  16.415  1.00 17.47           C  
ANISOU 1043  CA  TYR A 157     2321   2577   1739      4     42   -113       C  
ATOM   1044  C   TYR A 157      17.366  11.566  16.711  1.00 18.87           C  
ANISOU 1044  C   TYR A 157     2496   2750   1922      5     35   -106       C  
ATOM   1045  O   TYR A 157      17.547  10.969  17.785  1.00 16.84           O  
ANISOU 1045  O   TYR A 157     2233   2510   1654      0     26    -96       O  
ATOM   1046  CB  TYR A 157      14.969  11.112  16.722  1.00 18.67           C  
ANISOU 1046  CB  TYR A 157     2475   2739   1880     -3     37    -96       C  
ATOM   1047  CG  TYR A 157      13.612  11.774  16.784  1.00 18.38           C  
ANISOU 1047  CG  TYR A 157     2435   2713   1835     -5     42   -106       C  
ATOM   1048  CD1 TYR A 157      13.180  12.507  17.938  1.00 19.23           C  
ANISOU 1048  CD1 TYR A 157     2530   2848   1929     -9     44   -119       C  
ATOM   1049  CD2 TYR A 157      12.790  11.770  15.708  1.00 18.82           C  
ANISOU 1049  CD2 TYR A 157     2499   2752   1899     -1     46   -106       C  
ATOM   1050  CE1 TYR A 157      11.961  13.148  17.976  1.00 20.09           C  
ANISOU 1050  CE1 TYR A 157     2633   2966   2033    -10     48   -132       C  
ATOM   1051  CE2 TYR A 157      11.548  12.363  15.753  1.00 19.28           C  
ANISOU 1051  CE2 TYR A 157     2553   2819   1953     -2     49   -118       C  
ATOM   1052  CZ  TYR A 157      11.129  13.048  16.893  1.00 19.52           C  
ANISOU 1052  CZ  TYR A 157     2570   2876   1970     -6     50   -131       C  
ATOM   1053  OH  TYR A 157       9.905  13.685  16.895  1.00 19.12           O  
ANISOU 1053  OH  TYR A 157     2514   2834   1919     -6     53   -146       O  
ATOM   1054  N   GLY A 158      18.309  11.719  15.793  1.00 18.09           N  
ANISOU 1054  N   GLY A 158     2403   2630   1840     10     39   -112       N  
ATOM   1055  CA  GLY A 158      19.618  11.080  15.894  1.00 19.94           C  
ANISOU 1055  CA  GLY A 158     2634   2857   2084     12     33   -108       C  
ATOM   1056  C   GLY A 158      19.579   9.560  15.774  1.00 18.95           C  
ANISOU 1056  C   GLY A 158     2513   2724   1962     10     22    -88       C  
ATOM   1057  O   GLY A 158      20.468   8.859  16.327  1.00 23.70           O  
ANISOU 1057  O   GLY A 158     3110   3327   2569     10     11    -81       O  
ATOM   1058  N   LEU A 159      18.524   8.996  15.183  1.00 19.33           N  
ANISOU 1058  N   LEU A 159     2569   2767   2009      8     24    -77       N  
ATOM   1059  CA  LEU A 159      18.355   7.517  15.155  1.00 20.21           C  
ANISOU 1059  CA  LEU A 159     2684   2873   2123      5     13    -56       C  
ATOM   1060  C   LEU A 159      18.733   6.786  13.793  1.00 21.08           C  
ANISOU 1060  C   LEU A 159     2802   2955   2252     10     15    -53       C  
ATOM   1061  O   LEU A 159      18.290   5.678  13.561  1.00 21.35           O  
ANISOU 1061  O   LEU A 159     2840   2983   2289      8      8    -38       O  
ATOM   1062  CB  LEU A 159      16.921   7.120  15.614  1.00 19.83           C  
ANISOU 1062  CB  LEU A 159     2638   2839   2057     -2     11    -43       C  
ATOM   1063  CG  LEU A 159      16.430   6.741  17.024  1.00 19.44           C  
ANISOU 1063  CG  LEU A 159     2583   2816   1987    -12      2    -31       C  
ATOM   1064  CD1 LEU A 159      17.378   6.856  18.229  1.00 18.33           C  
ANISOU 1064  CD1 LEU A 159     2435   2691   1840    -14     -7    -31       C  
ATOM   1065  CD2 LEU A 159      15.051   7.328  17.381  1.00 19.07           C  
ANISOU 1065  CD2 LEU A 159     2534   2788   1923    -18     10    -36       C  
ATOM   1066  N   GLU A 160      19.533   7.375  12.900  1.00 21.63           N  
ANISOU 1066  N   GLU A 160     2873   3008   2335     14     24    -69       N  
ATOM   1067  CA  GLU A 160      19.904   6.671  11.646  1.00 25.16           C  
ANISOU 1067  CA  GLU A 160     3326   3432   2800     16     27    -69       C  
ATOM   1068  C   GLU A 160      20.423   5.249  11.886  1.00 23.42           C  
ANISOU 1068  C   GLU A 160     3102   3206   2590     17     12    -55       C  
ATOM   1069  O   GLU A 160      20.164   4.324  11.064  1.00 21.63           O  
ANISOU 1069  O   GLU A 160     2881   2964   2374     17     11    -47       O  
ATOM   1070  CB  GLU A 160      20.958   7.468  10.874  1.00 28.00           C  
ANISOU 1070  CB  GLU A 160     3687   3780   3173     18     38    -89       C  
ATOM   1071  CG  GLU A 160      20.588   8.945  10.628  1.00 31.02           C  
ANISOU 1071  CG  GLU A 160     4074   4166   3547     17     50   -103       C  
ATOM   1072  CD  GLU A 160      21.201   9.955  11.643  1.00 36.58           C  
ANISOU 1072  CD  GLU A 160     4768   4885   4245     18     51   -115       C  
ATOM   1073  OE1 GLU A 160      21.151   9.765  12.896  1.00 34.59           O  
ANISOU 1073  OE1 GLU A 160     4507   4651   3984     18     41   -109       O  
ATOM   1074  OE2 GLU A 160      21.729  10.994  11.169  1.00 41.69           O  
ANISOU 1074  OE2 GLU A 160     5418   5526   4897     17     61   -132       O  
ATOM   1075  N   LYS A 161      21.241   5.058  12.944  1.00 19.45           N  
ANISOU 1075  N   LYS A 161     2589   2712   2088     18      0    -54       N  
ATOM   1076  CA  LYS A 161      21.846   3.739  13.151  1.00 22.54           C  
ANISOU 1076  CA  LYS A 161     2977   3095   2492     20    -17    -42       C  
ATOM   1077  C   LYS A 161      20.723   2.698  13.141  1.00 21.90           C  
ANISOU 1077  C   LYS A 161     2904   3013   2405     16    -24    -20       C  
ATOM   1078  O   LYS A 161      20.781   1.660  12.462  1.00 21.70           O  
ANISOU 1078  O   LYS A 161     2881   2971   2394     17    -30    -13       O  
ATOM   1079  CB  LYS A 161      22.638   3.700  14.484  1.00 22.05           C  
ANISOU 1079  CB  LYS A 161     2905   3046   2426     20    -32    -40       C  
ATOM   1080  CG  LYS A 161      23.486   2.437  14.650  1.00 21.90           C  
ANISOU 1080  CG  LYS A 161     2882   3014   2426     24    -53    -32       C  
ATOM   1081  CD  LYS A 161      23.790   2.091  16.121  1.00 22.58           C  
ANISOU 1081  CD  LYS A 161     2963   3114   2501     21    -74    -19       C  
ATOM   1082  CE  LYS A 161      24.386   0.712  16.281  1.00 22.87           C  
ANISOU 1082  CE  LYS A 161     2998   3136   2556     24    -98     -7       C  
ATOM   1083  NZ  LYS A 161      25.375   0.583  17.403  1.00 22.81           N  
ANISOU 1083  NZ  LYS A 161     2983   3134   2551     26   -119     -6       N  
ATOM   1084  N   GLU A 162      19.703   3.003  13.935  1.00 21.51           N  
ANISOU 1084  N   GLU A 162     2856   2983   2333      9    -24    -11       N  
ATOM   1085  CA  GLU A 162      18.636   2.066  14.216  1.00 22.51           C  
ANISOU 1085  CA  GLU A 162     2988   3114   2449      3    -32     11       C  
ATOM   1086  C   GLU A 162      17.808   1.838  12.966  1.00 20.21           C  
ANISOU 1086  C   GLU A 162     2706   2809   2165      4    -22     11       C  
ATOM   1087  O   GLU A 162      17.573   0.705  12.586  1.00 21.20           O  
ANISOU 1087  O   GLU A 162     2834   2921   2298      3    -30     25       O  
ATOM   1088  CB  GLU A 162      17.784   2.599  15.366  1.00 23.29           C  
ANISOU 1088  CB  GLU A 162     3086   3240   2522     -6    -32     16       C  
ATOM   1089  CG  GLU A 162      18.435   2.408  16.730  1.00 26.05           C  
ANISOU 1089  CG  GLU A 162     3429   3605   2862    -10    -47     23       C  
ATOM   1090  CD  GLU A 162      19.486   3.443  17.080  1.00 27.25           C  
ANISOU 1090  CD  GLU A 162     3574   3763   3018     -4    -44      5       C  
ATOM   1091  OE1 GLU A 162      19.940   4.239  16.235  1.00 28.27           O  
ANISOU 1091  OE1 GLU A 162     3701   3881   3159      3    -31    -15       O  
ATOM   1092  OE2 GLU A 162      19.893   3.457  18.242  1.00 28.38           O  
ANISOU 1092  OE2 GLU A 162     3712   3921   3150     -8    -55      9       O  
ATOM   1093  N   ALA A 163      17.492   2.928  12.300  1.00 18.70           N  
ANISOU 1093  N   ALA A 163     2517   2617   1971      6     -5     -5       N  
ATOM   1094  CA  ALA A 163      16.662   2.917  11.119  1.00 17.82           C  
ANISOU 1094  CA  ALA A 163     2415   2493   1863      6      5     -6       C  
ATOM   1095  C   ALA A 163      17.374   2.046  10.121  1.00 17.77           C  
ANISOU 1095  C   ALA A 163     2410   2464   1878     10      3     -6       C  
ATOM   1096  O   ALA A 163      16.774   1.107   9.638  1.00 17.36           O  
ANISOU 1096  O   ALA A 163     2363   2403   1831      9     -1      6       O  
ATOM   1097  CB  ALA A 163      16.484   4.353  10.633  1.00 18.08           C  
ANISOU 1097  CB  ALA A 163     2450   2528   1892      8     20    -25       C  
ATOM   1098  N   LEU A 164      18.666   2.275   9.900  1.00 17.86           N  
ANISOU 1098  N   LEU A 164     2416   2466   1903     15      4    -20       N  
ATOM   1099  CA  LEU A 164      19.456   1.552   8.923  1.00 18.87           C  
ANISOU 1099  CA  LEU A 164     2544   2574   2053     18      3    -26       C  
ATOM   1100  C   LEU A 164      19.401   0.052   9.148  1.00 18.46           C  
ANISOU 1100  C   LEU A 164     2489   2514   2010     18    -14     -8       C  
ATOM   1101  O   LEU A 164      19.287  -0.688   8.154  1.00 18.49           O  
ANISOU 1101  O   LEU A 164     2497   2501   2027     19    -12     -7       O  
ATOM   1102  CB  LEU A 164      20.935   2.047   8.919  1.00 19.33           C  
ANISOU 1102  CB  LEU A 164     2594   2628   2124     21      6    -45       C  
ATOM   1103  CG  LEU A 164      21.244   3.474   8.369  1.00 21.19           C  
ANISOU 1103  CG  LEU A 164     2832   2864   2356     20     24    -65       C  
ATOM   1104  CD1 LEU A 164      22.586   3.950   8.886  1.00 20.92           C  
ANISOU 1104  CD1 LEU A 164     2786   2833   2329     23     23    -81       C  
ATOM   1105  CD2 LEU A 164      21.201   3.651   6.857  1.00 21.19           C  
ANISOU 1105  CD2 LEU A 164     2841   2846   2363     18     39    -76       C  
ATOM   1106  N   GLU A 165      19.503  -0.392  10.427  1.00 18.63           N  
ANISOU 1106  N   GLU A 165     2506   2547   2025     17    -30      6       N  
ATOM   1107  CA  GLU A 165      19.425  -1.838  10.799  1.00 19.94           C  
ANISOU 1107  CA  GLU A 165     2672   2706   2199     16    -51     26       C  
ATOM   1108  C   GLU A 165      18.015  -2.382  10.427  1.00 21.00           C  
ANISOU 1108  C   GLU A 165     2815   2840   2324     10    -48     41       C  
ATOM   1109  O   GLU A 165      17.833  -3.525   9.980  1.00 21.16           O  
ANISOU 1109  O   GLU A 165     2838   2845   2356     10    -57     52       O  
ATOM   1110  CB  GLU A 165      19.767  -2.126  12.272  1.00 21.76           C  
ANISOU 1110  CB  GLU A 165     2898   2950   2421     13    -70     39       C  
ATOM   1111  CG  GLU A 165      21.094  -1.528  12.822  1.00 22.49           C  
ANISOU 1111  CG  GLU A 165     2980   3046   2520     18    -74     24       C  
ATOM   1112  CD  GLU A 165      21.022  -1.228  14.342  1.00 23.97           C  
ANISOU 1112  CD  GLU A 165     3165   3255   2685     12    -85     35       C  
ATOM   1113  OE1 GLU A 165      19.917  -1.223  14.916  1.00 28.19           O  
ANISOU 1113  OE1 GLU A 165     3706   3806   3198      3    -85     50       O  
ATOM   1114  OE2 GLU A 165      22.074  -1.062  14.967  1.00 23.48           O  
ANISOU 1114  OE2 GLU A 165     3096   3196   2630     15    -95     28       O  
ATOM   1115  N   LYS A 166      17.023  -1.534  10.589  1.00 22.12           N  
ANISOU 1115  N   LYS A 166     2962   2998   2446      6    -36     41       N  
ATOM   1116  CA  LYS A 166      15.659  -1.928  10.290  1.00 21.17           C  
ANISOU 1116  CA  LYS A 166     2850   2879   2316      1    -33     53       C  
ATOM   1117  C   LYS A 166      15.507  -2.018   8.776  1.00 20.71           C  
ANISOU 1117  C   LYS A 166     2796   2800   2271      5    -21     43       C  
ATOM   1118  O   LYS A 166      15.011  -3.003   8.259  1.00 18.86           O  
ANISOU 1118  O   LYS A 166     2566   2555   2045      4    -26     54       O  
ATOM   1119  CB  LYS A 166      14.655  -1.017  10.998  1.00 21.18           C  
ANISOU 1119  CB  LYS A 166     2851   2903   2292     -6    -25     53       C  
ATOM   1120  CG  LYS A 166      14.214  -1.664  12.323  1.00 23.34           C  
ANISOU 1120  CG  LYS A 166     3124   3195   2551    -16    -38     73       C  
ATOM   1121  CD  LYS A 166      15.228  -1.492  13.440  1.00 24.20           C  
ANISOU 1121  CD  LYS A 166     3226   3313   2655    -16    -49     73       C  
ATOM   1122  CE  LYS A 166      15.025  -2.601  14.502  1.00 25.15           C  
ANISOU 1122  CE  LYS A 166     3348   3441   2767    -27    -69     98       C  
ATOM   1123  NZ  LYS A 166      13.607  -2.971  14.750  1.00 25.86           N  
ANISOU 1123  NZ  LYS A 166     3443   3543   2839    -38    -66    112       N  
ATOM   1124  N   ILE A 167      16.053  -1.063   8.060  1.00 18.52           N  
ANISOU 1124  N   ILE A 167     2519   2518   1999      9     -8     24       N  
ATOM   1125  CA  ILE A 167      16.019  -1.192   6.612  1.00 18.33           C  
ANISOU 1125  CA  ILE A 167     2502   2476   1988     12      2     15       C  
ATOM   1126  C   ILE A 167      16.752  -2.409   6.061  1.00 19.47           C  
ANISOU 1126  C   ILE A 167     2642   2601   2154     15     -7     16       C  
ATOM   1127  O   ILE A 167      16.273  -3.049   5.169  1.00 17.88           O  
ANISOU 1127  O   ILE A 167     2446   2388   1960     14     -5     19       O  
ATOM   1128  CB  ILE A 167      16.544   0.067   5.940  1.00 17.47           C  
ANISOU 1128  CB  ILE A 167     2396   2364   1879     13     17     -7       C  
ATOM   1129  CG1 ILE A 167      15.646   1.253   6.235  1.00 17.74           C  
ANISOU 1129  CG1 ILE A 167     2435   2413   1894     11     25     -9       C  
ATOM   1130  CG2 ILE A 167      16.608  -0.129   4.423  1.00 17.28           C  
ANISOU 1130  CG2 ILE A 167     2379   2320   1866     13     27    -16       C  
ATOM   1131  CD1 ILE A 167      16.375   2.564   6.063  1.00 16.93           C  
ANISOU 1131  CD1 ILE A 167     2332   2311   1790     12     36    -28       C  
ATOM   1132  N   SER A 168      17.934  -2.703   6.611  1.00 19.37           N  
ANISOU 1132  N   SER A 168     2619   2586   2153     18    -17     12       N  
ATOM   1133  CA  SER A 168      18.721  -3.850   6.195  1.00 21.76           C  
ANISOU 1133  CA  SER A 168     2916   2871   2480     22    -27     11       C  
ATOM   1134  C   SER A 168      17.932  -5.119   6.345  1.00 22.41           C  
ANISOU 1134  C   SER A 168     3002   2948   2566     20    -42     32       C  
ATOM   1135  O   SER A 168      17.964  -5.980   5.432  1.00 23.05           O  
ANISOU 1135  O   SER A 168     3083   3012   2664     22    -43     31       O  
ATOM   1136  CB  SER A 168      20.014  -3.892   6.999  1.00 23.84           C  
ANISOU 1136  CB  SER A 168     3168   3135   2754     26    -40      5       C  
ATOM   1137  OG  SER A 168      21.021  -4.461   6.226  1.00 27.05           O  
ANISOU 1137  OG  SER A 168     3567   3524   3187     30    -41    -11       O  
ATOM   1138  N   ASP A 169      17.151  -5.233   7.435  1.00 23.05           N  
ANISOU 1138  N   ASP A 169     3086   3045   2629     15    -51     52       N  
ATOM   1139  CA  ASP A 169      16.356  -6.449   7.640  1.00 24.63           C  
ANISOU 1139  CA  ASP A 169     3290   3240   2829     11    -65     74       C  
ATOM   1140  C   ASP A 169      15.217  -6.494   6.639  1.00 21.96           C  
ANISOU 1140  C   ASP A 169     2959   2897   2486      9    -52     75       C  
ATOM   1141  O   ASP A 169      14.878  -7.558   6.204  1.00 21.25           O  
ANISOU 1141  O   ASP A 169     2872   2795   2408      8    -59     84       O  
ATOM   1142  CB  ASP A 169      15.893  -6.787   9.097  1.00 27.18           C  
ANISOU 1142  CB  ASP A 169     3613   3578   3134      3    -80     97       C  
ATOM   1143  CG  ASP A 169      14.753  -5.893   9.645  1.00 28.47           C  
ANISOU 1143  CG  ASP A 169     3783   3767   3270     -5    -68    101       C  
ATOM   1144  OD1 ASP A 169      14.785  -4.678   9.449  1.00 29.65           O  
ANISOU 1144  OD1 ASP A 169     3931   3924   3410     -3    -53     84       O  
ATOM   1145  OD2 ASP A 169      13.853  -6.396  10.356  1.00 31.61           O  
ANISOU 1145  OD2 ASP A 169     4183   4174   3652    -15    -76    120       O  
ATOM   1146  N   ILE A 170      14.672  -5.337   6.276  1.00 19.11           N  
ANISOU 1146  N   ILE A 170     2603   2545   2111      8    -34     64       N  
ATOM   1147  CA  ILE A 170      13.672  -5.236   5.175  1.00 19.02           C  
ANISOU 1147  CA  ILE A 170     2601   2529   2098      7    -21     61       C  
ATOM   1148  C   ILE A 170      14.293  -5.682   3.825  1.00 18.58           C  
ANISOU 1148  C   ILE A 170     2545   2450   2063     11    -16     48       C  
ATOM   1149  O   ILE A 170      13.724  -6.544   3.165  1.00 21.28           O  
ANISOU 1149  O   ILE A 170     2891   2782   2413     11    -18     55       O  
ATOM   1150  CB  ILE A 170      13.066  -3.840   5.151  1.00 17.68           C  
ANISOU 1150  CB  ILE A 170     2435   2372   1909      6     -6     51       C  
ATOM   1151  CG1 ILE A 170      11.873  -3.792   6.120  1.00 17.60           C  
ANISOU 1151  CG1 ILE A 170     2427   2381   1880     -1    -10     66       C  
ATOM   1152  CG2 ILE A 170      12.596  -3.368   3.755  1.00 17.23           C  
ANISOU 1152  CG2 ILE A 170     2389   2305   1855      7      8     39       C  
ATOM   1153  CD1 ILE A 170      11.583  -2.455   6.738  1.00 17.82           C  
ANISOU 1153  CD1 ILE A 170     2453   2427   1889     -2     -2     57       C  
ATOM   1154  N   LYS A 171      15.421  -5.106   3.407  1.00 19.26           N  
ANISOU 1154  N   LYS A 171     2628   2532   2158     15     -9     29       N  
ATOM   1155  CA  LYS A 171      16.099  -5.572   2.165  1.00 20.59           C  
ANISOU 1155  CA  LYS A 171     2795   2682   2347     17     -4     15       C  
ATOM   1156  C   LYS A 171      16.390  -7.104   2.193  1.00 20.36           C  
ANISOU 1156  C   LYS A 171     2759   2638   2339     20    -21     23       C  
ATOM   1157  O   LYS A 171      16.107  -7.809   1.222  1.00 22.54           O  
ANISOU 1157  O   LYS A 171     3037   2901   2626     20    -19     21       O  
ATOM   1158  CB  LYS A 171      17.356  -4.753   1.846  1.00 20.15           C  
ANISOU 1158  CB  LYS A 171     2734   2624   2298     18      7     -8       C  
ATOM   1159  CG  LYS A 171      17.095  -3.280   1.499  1.00 21.08           C  
ANISOU 1159  CG  LYS A 171     2861   2750   2398     15     24    -19       C  
ATOM   1160  CD  LYS A 171      18.370  -2.562   1.060  1.00 22.46           C  
ANISOU 1160  CD  LYS A 171     3032   2921   2580     14     35    -42       C  
ATOM   1161  CE  LYS A 171      18.130  -1.369   0.135  1.00 23.99           C  
ANISOU 1161  CE  LYS A 171     3240   3115   2762      8     53    -55       C  
ATOM   1162  NZ  LYS A 171      18.081  -1.819  -1.286  1.00 25.27           N  
ANISOU 1162  NZ  LYS A 171     3409   3262   2932      3     62    -63       N  
ATOM   1163  N   ASN A 172      16.945  -7.678   3.276  1.00 22.75           N  
ANISOU 1163  N   ASN A 172     3053   2943   2649     22    -39     33       N  
ATOM   1164  CA AASN A 172      17.166  -9.143   3.236  0.50 23.13           C  
ANISOU 1164  CA AASN A 172     3095   2975   2719     25    -57     42       C  
ATOM   1165  C   ASN A 172      15.856  -9.916   2.988  1.00 23.21           C  
ANISOU 1165  C   ASN A 172     3113   2981   2723     21    -61     60       C  
ATOM   1166  O   ASN A 172      15.843 -10.792   2.138  1.00 25.61           O  
ANISOU 1166  O   ASN A 172     3417   3269   3046     23    -63     57       O  
ATOM   1167  CB AASN A 172      17.942  -9.731   4.429  0.50 23.01           C  
ANISOU 1167  CB AASN A 172     3071   2959   2713     27    -81     51       C  
ATOM   1168  CG AASN A 172      18.244 -11.226   4.247  0.50 22.62           C  
ANISOU 1168  CG AASN A 172     3016   2889   2690     31   -102     57       C  
ATOM   1169  OD1AASN A 172      18.715 -11.668   3.189  0.50 23.43           O  
ANISOU 1169  OD1AASN A 172     3112   2975   2814     35    -97     40       O  
ATOM   1170  ND2AASN A 172      17.988 -12.002   5.291  0.50 23.17           N  
ANISOU 1170  ND2AASN A 172     3087   2959   2758     28   -125     81       N  
ATOM   1171  CA BASN A 172      17.127  -9.139   3.349  0.50 22.47           C  
ANISOU 1171  CA BASN A 172     3012   2893   2634     24    -59     43       C  
ATOM   1172  CB BASN A 172      17.581  -9.554   4.749  0.50 21.40           C  
ANISOU 1172  CB BASN A 172     2871   2762   2499     25    -81     58       C  
ATOM   1173  CG BASN A 172      19.032  -9.233   4.996  0.50 20.54           C  
ANISOU 1173  CG BASN A 172     2750   2650   2404     31    -85     40       C  
ATOM   1174  OD1BASN A 172      19.780  -8.937   4.071  0.50 18.55           O  
ANISOU 1174  OD1BASN A 172     2492   2389   2166     34    -72     17       O  
ATOM   1175  ND2BASN A 172      19.430  -9.254   6.267  0.50 19.78           N  
ANISOU 1175  ND2BASN A 172     2650   2562   2304     31   -102     51       N  
ATOM   1176  N   GLU A 173      14.763  -9.566   3.659  1.00 23.82           N  
ANISOU 1176  N   GLU A 173     3199   3075   2777     15    -59     77       N  
ATOM   1177  CA  GLU A 173      13.448 -10.185   3.434  1.00 25.64           C  
ANISOU 1177  CA  GLU A 173     3437   3304   3001     10    -60     92       C  
ATOM   1178  C   GLU A 173      13.000 -10.066   1.961  1.00 22.41           C  
ANISOU 1178  C   GLU A 173     3033   2885   2596     12    -44     79       C  
ATOM   1179  O   GLU A 173      12.507 -11.041   1.376  1.00 22.97           O  
ANISOU 1179  O   GLU A 173     3106   2944   2679     12    -49     85       O  
ATOM   1180  CB  GLU A 173      12.349  -9.554   4.317  1.00 27.72           C  
ANISOU 1180  CB  GLU A 173     3706   3590   3236      3    -57    105       C  
ATOM   1181  CG  GLU A 173      12.588  -9.477   5.824  1.00 30.58           C  
ANISOU 1181  CG  GLU A 173     4065   3967   3586     -2    -69    119       C  
ATOM   1182  CD  GLU A 173      12.375 -10.785   6.614  1.00 33.26           C  
ANISOU 1182  CD  GLU A 173     4405   4303   3930     -8    -91    143       C  
ATOM   1183  OE1 GLU A 173      12.697 -11.892   6.131  1.00 34.83           O  
ANISOU 1183  OE1 GLU A 173     4602   4481   4150     -5   -103    147       O  
ATOM   1184  OE2 GLU A 173      11.921 -10.693   7.777  1.00 35.29           O  
ANISOU 1184  OE2 GLU A 173     4664   4578   4167    -18    -98    158       O  
ATOM   1185  N   ILE A 174      13.159  -8.886   1.364  1.00 21.21           N  
ANISOU 1185  N   ILE A 174     2885   2738   2437     13    -27     62       N  
ATOM   1186  CA  ILE A 174      12.882  -8.681  -0.093  1.00 21.17           C  
ANISOU 1186  CA  ILE A 174     2886   2722   2434     13    -12     48       C  
ATOM   1187  C   ILE A 174      13.699  -9.620  -0.969  1.00 20.17           C  
ANISOU 1187  C   ILE A 174     2753   2576   2333     16    -15     37       C  
ATOM   1188  O   ILE A 174      13.143 -10.248  -1.838  1.00 19.23           O  
ANISOU 1188  O   ILE A 174     2639   2448   2222     16    -13     37       O  
ATOM   1189  CB  ILE A 174      13.155  -7.216  -0.561  1.00 20.27           C  
ANISOU 1189  CB  ILE A 174     2778   2614   2308     12      6     30       C  
ATOM   1190  CG1 ILE A 174      12.068  -6.266  -0.128  1.00 18.38           C  
ANISOU 1190  CG1 ILE A 174     2547   2391   2047     10     11     36       C  
ATOM   1191  CG2 ILE A 174      13.315  -7.089  -2.092  1.00 20.62           C  
ANISOU 1191  CG2 ILE A 174     2829   2645   2359     11     19     13       C  
ATOM   1192  CD1 ILE A 174      12.527  -4.841   0.030  1.00 17.16           C  
ANISOU 1192  CD1 ILE A 174     2395   2246   1881      9     21     23       C  
ATOM   1193  N   GLU A 175      15.001  -9.718  -0.734  1.00 20.68           N  
ANISOU 1193  N   GLU A 175     2807   2636   2413     19    -19     25       N  
ATOM   1194  CA AGLU A 175      15.815 -10.722  -1.413  0.50 21.29           C  
ANISOU 1194  CA AGLU A 175     2875   2696   2518     23    -25     13       C  
ATOM   1195  C   GLU A 175      15.335 -12.163  -1.110  1.00 20.99           C  
ANISOU 1195  C   GLU A 175     2835   2648   2494     25    -45     32       C  
ATOM   1196  O   GLU A 175      15.192 -12.962  -2.042  1.00 25.05           O  
ANISOU 1196  O   GLU A 175     3348   3148   3023     26    -44     27       O  
ATOM   1197  CB AGLU A 175      17.288 -10.554  -1.034  0.50 21.12           C  
ANISOU 1197  CB AGLU A 175     2841   2673   2511     27    -29     -2       C  
ATOM   1198  CG AGLU A 175      17.826  -9.182  -1.386  0.50 20.87           C  
ANISOU 1198  CG AGLU A 175     2812   2650   2468     24     -9    -22       C  
ATOM   1199  CD AGLU A 175      18.505  -9.181  -2.724  0.50 20.76           C  
ANISOU 1199  CD AGLU A 175     2795   2625   2467     21      6    -48       C  
ATOM   1200  OE1AGLU A 175      17.874  -9.577  -3.743  0.50 21.79           O  
ANISOU 1200  OE1AGLU A 175     2933   2749   2599     18     13    -49       O  
ATOM   1201  OE2AGLU A 175      19.687  -8.809  -2.760  0.50 22.70           O  
ANISOU 1201  OE2AGLU A 175     3032   2871   2723     21     11    -68       O  
ATOM   1202  CA BGLU A 175      15.856 -10.730  -1.380  0.50 21.87           C  
ANISOU 1202  CA BGLU A 175     2949   2770   2592     23    -25     13       C  
ATOM   1203  CB BGLU A 175      17.315 -10.605  -0.879  0.50 22.34           C  
ANISOU 1203  CB BGLU A 175     2995   2828   2666     27    -31     -1       C  
ATOM   1204  CG BGLU A 175      18.320 -11.578  -1.482  0.50 23.39           C  
ANISOU 1204  CG BGLU A 175     3114   2942   2830     32    -38    -18       C  
ATOM   1205  CD BGLU A 175      19.198 -12.254  -0.435  0.50 23.40           C  
ANISOU 1205  CD BGLU A 175     3102   2938   2850     38    -62    -13       C  
ATOM   1206  OE1BGLU A 175      18.682 -13.116   0.341  0.50 23.39           O  
ANISOU 1206  OE1BGLU A 175     3102   2934   2851     39    -83     11       O  
ATOM   1207  OE2BGLU A 175      20.401 -11.940  -0.403  0.50 22.07           O  
ANISOU 1207  OE2BGLU A 175     2922   2769   2695     41    -61    -33       O  
ATOM   1208  N   LYS A 176      15.092 -12.508   0.161  1.00 24.29           N  
ANISOU 1208  N   LYS A 176     3251   3071   2906     24    -62     54       N  
ATOM   1209  CA  LYS A 176      14.590 -13.855   0.564  1.00 25.30           C  
ANISOU 1209  CA  LYS A 176     3378   3190   3044     24    -83     74       C  
ATOM   1210  C   LYS A 176      13.326 -14.199  -0.238  1.00 28.63           C  
ANISOU 1210  C   LYS A 176     3809   3608   3460     20    -75     81       C  
ATOM   1211  O   LYS A 176      13.257 -15.248  -0.871  1.00 35.30           O  
ANISOU 1211  O   LYS A 176     4650   4437   4324     22    -82     81       O  
ATOM   1212  CB  LYS A 176      14.179 -13.933   2.052  1.00 26.16           C  
ANISOU 1212  CB  LYS A 176     3490   3312   3138     19    -98    100       C  
ATOM   1213  CG  LYS A 176      15.260 -14.343   3.059  1.00 26.00           C  
ANISOU 1213  CG  LYS A 176     3461   3287   3129     22   -120    104       C  
ATOM   1214  CD  LYS A 176      15.246 -13.428   4.307  1.00 25.83           C  
ANISOU 1214  CD  LYS A 176     3443   3288   3084     17   -120    114       C  
ATOM   1215  CE  LYS A 176      15.578 -14.133   5.617  1.00 26.84           C  
ANISOU 1215  CE  LYS A 176     3569   3415   3213     14   -148    134       C  
ATOM   1216  NZ  LYS A 176      14.331 -14.514   6.292  1.00 25.47           N  
ANISOU 1216  NZ  LYS A 176     3407   3253   3020      3   -153    161       N  
ATOM   1217  N   ALA A 177      12.356 -13.280  -0.183  1.00 28.67           N  
ANISOU 1217  N   ALA A 177     3825   3630   3440     15    -61     86       N  
ATOM   1218  CA  ALA A 177      11.065 -13.375  -0.902  1.00 28.07           C  
ANISOU 1218  CA  ALA A 177     3757   3553   3354     12    -52     90       C  
ATOM   1219  C   ALA A 177      11.231 -13.458  -2.429  1.00 30.57           C  
ANISOU 1219  C   ALA A 177     4075   3856   3683     15    -39     71       C  
ATOM   1220  O   ALA A 177      10.648 -14.339  -3.052  1.00 30.29           O  
ANISOU 1220  O   ALA A 177     4041   3810   3658     14    -42     75       O  
ATOM   1221  CB  ALA A 177      10.144 -12.196  -0.531  1.00 26.42           C  
ANISOU 1221  CB  ALA A 177     3557   3365   3117      8    -40     94       C  
ATOM   1222  N   LYS A 178      12.026 -12.568  -3.018  1.00 32.16           N  
ANISOU 1222  N   LYS A 178     4276   4059   3884     16    -25     50       N  
ATOM   1223  CA  LYS A 178      12.347 -12.614  -4.467  1.00 34.77           C  
ANISOU 1223  CA  LYS A 178     4608   4378   4225     16    -13     29       C  
ATOM   1224  C   LYS A 178      12.840 -14.000  -4.980  1.00 33.56           C  
ANISOU 1224  C   LYS A 178     4445   4206   4101     19    -23     24       C  
ATOM   1225  O   LYS A 178      12.468 -14.437  -6.084  1.00 40.20           O  
ANISOU 1225  O   LYS A 178     5289   5038   4948     18    -17     16       O  
ATOM   1226  CB  LYS A 178      13.408 -11.552  -4.849  1.00 31.65           C  
ANISOU 1226  CB  LYS A 178     4212   3986   3827     15      2      7       C  
ATOM   1227  CG  LYS A 178      12.881 -10.322  -5.577  1.00 32.49           C  
ANISOU 1227  CG  LYS A 178     4333   4099   3912     10     20     -1       C  
ATOM   1228  CD  LYS A 178      13.885  -9.158  -5.592  1.00 31.49           C  
ANISOU 1228  CD  LYS A 178     4207   3979   3779      7     32    -18       C  
ATOM   1229  CE  LYS A 178      14.949  -9.307  -6.664  0.50 31.93           C  
ANISOU 1229  CE  LYS A 178     4257   4024   3849      4     42    -43       C  
ATOM   1230  NZ  LYS A 178      15.366  -7.965  -7.157  0.50 31.34           N  
ANISOU 1230  NZ  LYS A 178     4192   3955   3759     -3     59    -59       N  
ATOM   1231  N   SER A 179      13.688 -14.658  -4.188  1.00 35.01           N  
ANISOU 1231  N   SER A 179     4615   4384   4302     24    -40     27       N  
ATOM   1232  CA  SER A 179      14.336 -15.926  -4.595  1.00 34.01           C  
ANISOU 1232  CA  SER A 179     4477   4238   4207     28    -52     18       C  
ATOM   1233  C   SER A 179      13.375 -17.082  -4.726  1.00 34.04           C  
ANISOU 1233  C   SER A 179     4483   4232   4219     28    -64     35       C  
ATOM   1234  O   SER A 179      13.698 -18.056  -5.390  1.00 35.14           O  
ANISOU 1234  O   SER A 179     4614   4355   4382     31    -71     25       O  
ATOM   1235  CB  SER A 179      15.430 -16.315  -3.614  1.00 34.57           C  
ANISOU 1235  CB  SER A 179     4535   4305   4296     33    -71     19       C  
ATOM   1236  OG  SER A 179      16.233 -15.189  -3.343  1.00 32.34           O  
ANISOU 1236  OG  SER A 179     4250   4034   4003     33    -61      6       O  
ATOM   1237  N   ILE A 180      12.219 -16.965  -4.070  1.00 32.35           N  
ANISOU 1237  N   ILE A 180     4279   4028   3984     24    -67     59       N  
ATOM   1238  CA  ILE A 180      11.163 -17.979  -4.042  1.00 30.17           C  
ANISOU 1238  CA  ILE A 180     4007   3745   3711     22    -78     78       C  
ATOM   1239  C   ILE A 180      10.022 -17.705  -5.040  1.00 26.11           C  
ANISOU 1239  C   ILE A 180     3503   3234   3184     18    -62     75       C  
ATOM   1240  O   ILE A 180       9.151 -18.544  -5.175  1.00 25.50           O  
ANISOU 1240  O   ILE A 180     3429   3151   3111     16    -69     88       O  
ATOM   1241  CB  ILE A 180      10.555 -18.025  -2.616  1.00 30.86           C  
ANISOU 1241  CB  ILE A 180     4098   3844   3782     17    -91    106       C  
ATOM   1242  CG1 ILE A 180      11.682 -18.220  -1.572  1.00 30.53           C  
ANISOU 1242  CG1 ILE A 180     4048   3800   3752     20   -109    110       C  
ATOM   1243  CG2 ILE A 180       9.468 -19.104  -2.519  1.00 31.36           C  
ANISOU 1243  CG2 ILE A 180     4166   3901   3849     12   -103    126       C  
ATOM   1244  CD1 ILE A 180      11.321 -17.786  -0.159  1.00 30.42           C  
ANISOU 1244  CD1 ILE A 180     4040   3804   3715     13   -116    131       C  
ATOM   1245  N   VAL A 181      10.011 -16.535  -5.699  1.00 26.68           N  
ANISOU 1245  N   VAL A 181     3583   3316   3240     17    -42     60       N  
ATOM   1246  CA  VAL A 181       8.992 -16.205  -6.717  1.00 25.04           C  
ANISOU 1246  CA  VAL A 181     3385   3108   3020     14    -28     56       C  
ATOM   1247  C   VAL A 181       9.113 -17.149  -7.926  1.00 25.16           C  
ANISOU 1247  C   VAL A 181     3397   3106   3056     15    -27     43       C  
ATOM   1248  O   VAL A 181      10.210 -17.412  -8.413  1.00 25.08           O  
ANISOU 1248  O   VAL A 181     3378   3088   3064     17    -26     25       O  
ATOM   1249  CB  VAL A 181       9.115 -14.721  -7.194  1.00 24.92           C  
ANISOU 1249  CB  VAL A 181     3380   3104   2985     12     -9     42       C  
ATOM   1250  CG1 VAL A 181       8.153 -14.391  -8.332  1.00 24.85           C  
ANISOU 1250  CG1 VAL A 181     3384   3095   2965      9      2     36       C  
ATOM   1251  CG2 VAL A 181       8.899 -13.754  -6.030  1.00 24.10           C  
ANISOU 1251  CG2 VAL A 181     3279   3018   2861     11    -10     53       C  
ATOM   1252  N   ASP A 182       7.997 -17.710  -8.359  1.00 23.57           N  
ANISOU 1252  N   ASP A 182     3201   2901   2853     14    -29     52       N  
ATOM   1253  CA  ASP A 182       7.960 -18.543  -9.578  1.00 23.87           C  
ANISOU 1253  CA  ASP A 182     3236   2924   2908     14    -27     40       C  
ATOM   1254  C   ASP A 182       7.899 -17.618 -10.816  1.00 24.97           C  
ANISOU 1254  C   ASP A 182     3386   3067   3034     11     -7     20       C  
ATOM   1255  O   ASP A 182       6.884 -16.980 -11.084  1.00 27.52           O  
ANISOU 1255  O   ASP A 182     3722   3397   3336      8      0     26       O  
ATOM   1256  CB  ASP A 182       6.763 -19.516  -9.516  1.00 24.30           C  
ANISOU 1256  CB  ASP A 182     3293   2974   2967     14    -37     57       C  
ATOM   1257  CG  ASP A 182       6.806 -20.645 -10.581  1.00 25.07           C  
ANISOU 1257  CG  ASP A 182     3384   3053   3088     16    -40     46       C  
ATOM   1258  OD1 ASP A 182       7.382 -20.430 -11.662  1.00 23.67           O  
ANISOU 1258  OD1 ASP A 182     3207   2872   2916     15    -28     23       O  
ATOM   1259  OD2 ASP A 182       6.250 -21.763 -10.335  1.00 22.89           O  
ANISOU 1259  OD2 ASP A 182     3104   2768   2825     16    -54     60       O  
ATOM   1260  N   GLU A 183       8.998 -17.569 -11.551  1.00 24.30           N  
ANISOU 1260  N   GLU A 183     3295   2976   2960     10      1     -3       N  
ATOM   1261  CA  GLU A 183       9.104 -16.742 -12.787  1.00 25.56           C  
ANISOU 1261  CA  GLU A 183     3466   3138   3107      3     20    -22       C  
ATOM   1262  C   GLU A 183       7.964 -17.046 -13.755  1.00 22.21           C  
ANISOU 1262  C   GLU A 183     3053   2710   2677      1     23    -20       C  
ATOM   1263  O   GLU A 183       7.557 -16.146 -14.512  1.00 24.15           O  
ANISOU 1263  O   GLU A 183     3313   2960   2902     -5     35    -27       O  
ATOM   1264  CB  GLU A 183      10.420 -16.986 -13.550  1.00 26.62           C  
ANISOU 1264  CB  GLU A 183     3590   3266   3258      1     28    -50       C  
ATOM   1265  CG  GLU A 183      11.562 -17.648 -12.777  1.00 29.38           C  
ANISOU 1265  CG  GLU A 183     3920   3609   3633      7     16    -55       C  
ATOM   1266  CD  GLU A 183      11.397 -19.147 -12.652  1.00 29.34           C  
ANISOU 1266  CD  GLU A 183     3903   3590   3656     13     -1    -49       C  
ATOM   1267  OE1 GLU A 183      11.209 -19.838 -13.678  1.00 26.18           O  
ANISOU 1267  OE1 GLU A 183     3500   3180   3266     11      2    -61       O  
ATOM   1268  OE2 GLU A 183      11.430 -19.662 -11.507  1.00 30.61           O  
ANISOU 1268  OE2 GLU A 183     4056   3748   3825     19    -20    -31       O  
ATOM   1269  N   ASP A 184       7.464 -18.286 -13.751  1.00 21.38           N  
ANISOU 1269  N   ASP A 184     2940   2594   2589      5     12    -12       N  
ATOM   1270  CA  ASP A 184       6.374 -18.683 -14.658  1.00 20.20           C  
ANISOU 1270  CA  ASP A 184     2799   2441   2437      3     13    -11       C  
ATOM   1271  C   ASP A 184       4.907 -18.304 -14.245  1.00 19.33           C  
ANISOU 1271  C   ASP A 184     2700   2337   2307      3     10     10       C  
ATOM   1272  O   ASP A 184       3.953 -18.667 -14.965  1.00 18.41           O  
ANISOU 1272  O   ASP A 184     2589   2216   2188      2     10     11       O  
ATOM   1273  CB  ASP A 184       6.438 -20.171 -14.903  1.00 22.51           C  
ANISOU 1273  CB  ASP A 184     3078   2718   2756      6      3    -13       C  
ATOM   1274  CG  ASP A 184       5.715 -20.603 -16.160  1.00 21.47           C  
ANISOU 1274  CG  ASP A 184     2952   2580   2625      3      8    -21       C  
ATOM   1275  OD1 ASP A 184       5.647 -19.826 -17.148  1.00 22.96           O  
ANISOU 1275  OD1 ASP A 184     3154   2773   2798     -3     22    -35       O  
ATOM   1276  OD2 ASP A 184       5.199 -21.749 -16.133  1.00 21.61           O  
ANISOU 1276  OD2 ASP A 184     2962   2587   2660      7     -3    -13       O  
ATOM   1277  N   LYS A 185       4.732 -17.571 -13.148  1.00 19.15           N  
ANISOU 1277  N   LYS A 185     2680   2327   2271      4      7     23       N  
ATOM   1278  CA  LYS A 185       3.403 -17.126 -12.735  1.00 18.42           C  
ANISOU 1278  CA  LYS A 185     2596   2243   2160      4      5     39       C  
ATOM   1279  C   LYS A 185       3.216 -15.602 -12.824  1.00 17.60           C  
ANISOU 1279  C   LYS A 185     2505   2150   2031      2     15     34       C  
ATOM   1280  O   LYS A 185       4.125 -14.841 -12.524  1.00 21.79           O  
ANISOU 1280  O   LYS A 185     3036   2686   2557      1     20     28       O  
ATOM   1281  CB  LYS A 185       3.153 -17.606 -11.304  1.00 19.11           C  
ANISOU 1281  CB  LYS A 185     2674   2336   2251      6     -8     59       C  
ATOM   1282  CG  LYS A 185       3.425 -19.120 -11.158  1.00 21.37           C  
ANISOU 1282  CG  LYS A 185     2948   2609   2562      8    -20     65       C  
ATOM   1283  CD  LYS A 185       2.736 -19.778  -9.957  1.00 22.87           C  
ANISOU 1283  CD  LYS A 185     3134   2802   2754      6    -34     89       C  
ATOM   1284  CE  LYS A 185       2.729 -21.294 -10.023  1.00 24.09           C  
ANISOU 1284  CE  LYS A 185     3280   2941   2933      7    -48     96       C  
ATOM   1285  NZ  LYS A 185       1.983 -21.841 -11.194  1.00 25.54           N  
ANISOU 1285  NZ  LYS A 185     3467   3115   3123      7    -44     89       N  
ATOM   1286  N   LYS A 186       2.013 -15.143 -13.159  1.00 16.14           N  
ANISOU 1286  N   LYS A 186     2331   1968   1833      2     16     38       N  
ATOM   1287  CA  LYS A 186       1.775 -13.724 -13.222  1.00 15.16           C  
ANISOU 1287  CA  LYS A 186     2219   1852   1688      1     22     34       C  
ATOM   1288  C   LYS A 186       0.589 -13.393 -12.298  1.00 14.08           C  
ANISOU 1288  C   LYS A 186     2082   1726   1541      3     15     47       C  
ATOM   1289  O   LYS A 186      -0.251 -14.257 -12.039  1.00 13.35           O  
ANISOU 1289  O   LYS A 186     1984   1633   1456      4      8     57       O  
ATOM   1290  CB  LYS A 186       1.417 -13.297 -14.651  1.00 16.41           C  
ANISOU 1290  CB  LYS A 186     2393   2003   1838     -3     28     21       C  
ATOM   1291  CG  LYS A 186       2.291 -13.858 -15.769  1.00 16.56           C  
ANISOU 1291  CG  LYS A 186     2412   2011   1867     -7     34      6       C  
ATOM   1292  CD  LYS A 186       1.575 -13.486 -17.054  1.00 16.70           C  
ANISOU 1292  CD  LYS A 186     2448   2024   1875    -12     37     -1       C  
ATOM   1293  CE  LYS A 186       2.377 -13.871 -18.293  1.00 17.68           C  
ANISOU 1293  CE  LYS A 186     2575   2139   2004    -19     46    -19       C  
ATOM   1294  NZ  LYS A 186       3.813 -13.632 -18.137  1.00 19.43           N  
ANISOU 1294  NZ  LYS A 186     2790   2363   2229    -23     55    -30       N  
ATOM   1295  N   ALA A 187       0.547 -12.129 -11.809  1.00 12.64           N  
ANISOU 1295  N   ALA A 187     1905   1555   1343      3     18     46       N  
ATOM   1296  CA  ALA A 187      -0.431 -11.694 -10.792  1.00 13.21           C  
ANISOU 1296  CA  ALA A 187     1974   1640   1406      5     13     55       C  
ATOM   1297  C   ALA A 187      -1.261 -10.498 -11.305  1.00 12.19           C  
ANISOU 1297  C   ALA A 187     1857   1512   1262      6     14     47       C  
ATOM   1298  O   ALA A 187      -0.812  -9.636 -12.107  1.00 11.51           O  
ANISOU 1298  O   ALA A 187     1784   1420   1169      5     19     37       O  
ATOM   1299  CB  ALA A 187       0.327 -11.284  -9.551  1.00 12.09           C  
ANISOU 1299  CB  ALA A 187     1824   1510   1260      5     14     60       C  
ATOM   1300  N   LEU A 188      -2.513 -10.452 -10.808  1.00 11.61           N  
ANISOU 1300  N   LEU A 188     1780   1446   1185      8      9     53       N  
ATOM   1301  CA  LEU A 188      -3.345  -9.299 -10.948  1.00 11.47           C  
ANISOU 1301  CA  LEU A 188     1771   1433   1156     11      7     45       C  
ATOM   1302  C   LEU A 188      -3.650  -8.644  -9.648  1.00 10.55           C  
ANISOU 1302  C   LEU A 188     1645   1333   1031     12      6     48       C  
ATOM   1303  O   LEU A 188      -3.953  -9.408  -8.677  1.00 11.94           O  
ANISOU 1303  O   LEU A 188     1807   1519   1210      9      4     58       O  
ATOM   1304  CB  LEU A 188      -4.651  -9.579 -11.677  1.00 10.72           C  
ANISOU 1304  CB  LEU A 188     1680   1331   1063     13      1     43       C  
ATOM   1305  CG  LEU A 188      -5.552  -8.377 -12.066  1.00 11.31           C  
ANISOU 1305  CG  LEU A 188     1765   1405   1128     17     -4     33       C  
ATOM   1306  CD1 LEU A 188      -5.061  -7.274 -13.033  1.00 10.97           C  
ANISOU 1306  CD1 LEU A 188     1740   1351   1076     17     -4     23       C  
ATOM   1307  CD2 LEU A 188      -6.892  -8.928 -12.505  1.00 11.18           C  
ANISOU 1307  CD2 LEU A 188     1746   1384   1117     19    -11     32       C  
ATOM   1308  N   ILE A 189      -3.430  -7.309  -9.561  1.00  9.66           N  
ANISOU 1308  N   ILE A 189     1538   1223    908     13      7     39       N  
ATOM   1309  CA  ILE A 189      -3.796  -6.505  -8.335  1.00  9.93           C  
ANISOU 1309  CA  ILE A 189     1564   1275    935     14      6     38       C  
ATOM   1310  C   ILE A 189      -5.149  -5.872  -8.587  1.00 10.16           C  
ANISOU 1310  C   ILE A 189     1595   1304    960     19      0     30       C  
ATOM   1311  O   ILE A 189      -5.308  -5.082  -9.552  1.00 10.94           O  
ANISOU 1311  O   ILE A 189     1708   1392   1057     22     -4     20       O  
ATOM   1312  CB  ILE A 189      -2.786  -5.413  -7.902  1.00  9.33           C  
ANISOU 1312  CB  ILE A 189     1490   1204    851     15     10     33       C  
ATOM   1313  CG1 ILE A 189      -1.342  -5.853  -7.879  1.00  9.87           C  
ANISOU 1313  CG1 ILE A 189     1558   1269    924     11     16     37       C  
ATOM   1314  CG2 ILE A 189      -3.218  -4.692  -6.586  1.00  9.09           C  
ANISOU 1314  CG2 ILE A 189     1448   1193    813     15      9     31       C  
ATOM   1315  CD1 ILE A 189      -0.280  -4.865  -7.577  1.00  9.81           C  
ANISOU 1315  CD1 ILE A 189     1553   1264    910     11     20     32       C  
ATOM   1316  N   ILE A 190      -6.134  -6.069  -7.731  1.00 10.17           N  
ANISOU 1316  N   ILE A 190     1583   1320    961     18     -2     31       N  
ATOM   1317  CA  ILE A 190      -7.410  -5.389  -7.786  1.00 10.45           C  
ANISOU 1317  CA  ILE A 190     1617   1359    996     22     -9     19       C  
ATOM   1318  C   ILE A 190      -7.922  -4.825  -6.451  1.00 11.26           C  
ANISOU 1318  C   ILE A 190     1704   1482   1092     21     -8     14       C  
ATOM   1319  O   ILE A 190      -7.571  -5.351  -5.358  1.00 12.69           O  
ANISOU 1319  O   ILE A 190     1873   1679   1269     14     -2     23       O  
ATOM   1320  CB  ILE A 190      -8.474  -6.314  -8.333  1.00  9.89           C  
ANISOU 1320  CB  ILE A 190     1544   1282    932     22    -13     20       C  
ATOM   1321  CG1 ILE A 190      -8.652  -7.488  -7.403  1.00  9.36           C  
ANISOU 1321  CG1 ILE A 190     1462   1228    868     15     -8     33       C  
ATOM   1322  CG2 ILE A 190      -8.052  -6.895  -9.687  1.00  9.40           C  
ANISOU 1322  CG2 ILE A 190     1496   1199    876     23    -14     24       C  
ATOM   1323  CD1 ILE A 190     -10.009  -8.078  -7.342  1.00  9.72           C  
ANISOU 1323  CD1 ILE A 190     1498   1277    917     13    -11     30       C  
ATOM   1324  N   LEU A 191      -8.680  -3.744  -6.519  1.00 11.30           N  
ANISOU 1324  N   LEU A 191     1709   1489   1096     27    -14     -2       N  
ATOM   1325  CA  LEU A 191      -9.327  -3.119  -5.370  1.00 11.92           C  
ANISOU 1325  CA  LEU A 191     1771   1587   1170     26    -14    -12       C  
ATOM   1326  C   LEU A 191     -10.770  -3.295  -5.503  1.00 13.00           C  
ANISOU 1326  C   LEU A 191     1900   1727   1313     28    -19    -22       C  
ATOM   1327  O   LEU A 191     -11.321  -3.233  -6.607  1.00 12.88           O  
ANISOU 1327  O   LEU A 191     1895   1694   1305     34    -28    -28       O  
ATOM   1328  CB  LEU A 191      -9.032  -1.651  -5.452  1.00 12.09           C  
ANISOU 1328  CB  LEU A 191     1799   1605   1189     33    -18    -25       C  
ATOM   1329  CG  LEU A 191      -9.463  -0.679  -4.356  1.00 12.83           C  
ANISOU 1329  CG  LEU A 191     1878   1717   1279     34    -19    -40       C  
ATOM   1330  CD1 LEU A 191      -8.259   0.037  -3.834  1.00 13.12           C  
ANISOU 1330  CD1 LEU A 191     1918   1759   1309     33    -14    -38       C  
ATOM   1331  CD2 LEU A 191     -10.539   0.290  -4.782  1.00 13.05           C  
ANISOU 1331  CD2 LEU A 191     1906   1739   1314     43    -31    -61       C  
ATOM   1332  N   THR A 192     -11.474  -3.471  -4.375  1.00 12.36           N  
ANISOU 1332  N   THR A 192     1799   1667   1228     22    -15    -27       N  
ATOM   1333  CA  THR A 192     -12.908  -3.524  -4.454  1.00 15.25           C  
ANISOU 1333  CA  THR A 192     2155   2038   1602     23    -19    -41       C  
ATOM   1334  C   THR A 192     -13.548  -2.436  -3.605  1.00 15.36           C  
ANISOU 1334  C   THR A 192     2154   2068   1613     25    -21    -62       C  
ATOM   1335  O   THR A 192     -13.061  -2.089  -2.492  1.00 16.76           O  
ANISOU 1335  O   THR A 192     2321   2264   1781     19    -13    -62       O  
ATOM   1336  CB  THR A 192     -13.520  -4.845  -4.013  1.00 15.19           C  
ANISOU 1336  CB  THR A 192     2136   2041   1594     12    -13    -31       C  
ATOM   1337  OG1 THR A 192     -13.196  -5.043  -2.624  1.00 16.03           O  
ANISOU 1337  OG1 THR A 192     2229   2171   1689      0     -3    -25       O  
ATOM   1338  CG2 THR A 192     -13.051  -5.919  -4.832  1.00 16.14           C  
ANISOU 1338  CG2 THR A 192     2268   2145   1718     11    -13    -14       C  
ATOM   1339  N   ASN A 193     -14.606  -1.844  -4.191  1.00 18.08           N  
ANISOU 1339  N   ASN A 193     2496   2404   1968     34    -32    -82       N  
ATOM   1340  CA  ASN A 193     -15.335  -0.769  -3.613  1.00 22.78           C  
ANISOU 1340  CA  ASN A 193     3077   3012   2567     39    -36   -107       C  
ATOM   1341  C   ASN A 193     -16.788  -0.736  -4.094  1.00 22.58           C  
ANISOU 1341  C   ASN A 193     3043   2982   2555     45    -47   -127       C  
ATOM   1342  O   ASN A 193     -16.997  -0.691  -5.265  1.00 23.54           O  
ANISOU 1342  O   ASN A 193     3179   3080   2684     54    -59   -127       O  
ATOM   1343  CB  ASN A 193     -14.647   0.509  -4.022  1.00 23.03           C  
ANISOU 1343  CB  ASN A 193     3122   3028   2599     49    -46   -113       C  
ATOM   1344  CG  ASN A 193     -15.129   1.684  -3.228  1.00 25.08           C  
ANISOU 1344  CG  ASN A 193     3365   3302   2861     53    -50   -138       C  
ATOM   1345  OD1 ASN A 193     -15.176   1.626  -2.017  1.00 25.19           O  
ANISOU 1345  OD1 ASN A 193     3361   3342   2868     44    -38   -142       O  
ATOM   1346  ND2 ASN A 193     -15.421   2.766  -3.900  1.00 26.26           N  
ANISOU 1346  ND2 ASN A 193     3523   3434   3021     65    -66   -153       N  
ATOM   1347  N   SER A 194     -17.793  -0.674  -3.215  1.00 25.30           N  
ANISOU 1347  N   SER A 194     3363   3348   2901     40    -43   -146       N  
ATOM   1348  CA  SER A 194     -19.183  -0.899  -3.658  1.00 30.30           C  
ANISOU 1348  CA  SER A 194     3987   3979   3548     44    -50   -163       C  
ATOM   1349  C   SER A 194     -19.167  -2.334  -4.163  1.00 31.82           C  
ANISOU 1349  C   SER A 194     4186   4164   3738     36    -44   -141       C  
ATOM   1350  O   SER A 194     -18.541  -3.219  -3.544  1.00 37.12           O  
ANISOU 1350  O   SER A 194     4857   4848   4398     23    -30   -121       O  
ATOM   1351  CB  SER A 194     -19.599   0.079  -4.779  1.00 32.59           C  
ANISOU 1351  CB  SER A 194     4287   4242   3852     62    -73   -180       C  
ATOM   1352  OG  SER A 194     -20.862  -0.247  -5.329  1.00 36.38           O  
ANISOU 1352  OG  SER A 194     4760   4716   4346     66    -82   -195       O  
ATOM   1353  N   ASN A 195     -19.759  -2.596  -5.313  1.00 29.96           N  
ANISOU 1353  N   ASN A 195     3960   3908   3514     45    -56   -144       N  
ATOM   1354  CA  ASN A 195     -19.427  -3.836  -5.930  1.00 29.29           C  
ANISOU 1354  CA  ASN A 195     3887   3813   3428     40    -52   -121       C  
ATOM   1355  C   ASN A 195     -18.652  -3.592  -7.219  1.00 26.67           C  
ANISOU 1355  C   ASN A 195     3582   3452   3098     50    -63   -109       C  
ATOM   1356  O   ASN A 195     -18.755  -4.387  -8.151  1.00 27.54           O  
ANISOU 1356  O   ASN A 195     3704   3548   3213     51    -66    -99       O  
ATOM   1357  CB  ASN A 195     -20.634  -4.756  -6.073  1.00 32.88           C  
ANISOU 1357  CB  ASN A 195     4329   4272   3891     35    -51   -127       C  
ATOM   1358  CG  ASN A 195     -21.677  -4.232  -7.017  1.00 34.38           C  
ANISOU 1358  CG  ASN A 195     4520   4446   4097     49    -69   -149       C  
ATOM   1359  OD1 ASN A 195     -22.361  -3.249  -6.737  1.00 41.80           O  
ANISOU 1359  OD1 ASN A 195     5447   5390   5044     56    -77   -175       O  
ATOM   1360  ND2 ASN A 195     -21.832  -4.915  -8.145  1.00 37.11           N  
ANISOU 1360  ND2 ASN A 195     4880   4771   4449     53    -76   -140       N  
ATOM   1361  N   LYS A 196     -17.858  -2.506  -7.223  1.00 21.16           N  
ANISOU 1361  N   LYS A 196     2896   2750   2396     56    -67   -111       N  
ATOM   1362  CA  LYS A 196     -16.995  -2.122  -8.340  1.00 19.56           C  
ANISOU 1362  CA  LYS A 196     2718   2521   2191     63    -76   -101       C  
ATOM   1363  C   LYS A 196     -15.524  -2.588  -8.155  1.00 17.11           C  
ANISOU 1363  C   LYS A 196     2418   2212   1869     55    -62    -78       C  
ATOM   1364  O   LYS A 196     -14.920  -2.476  -7.094  1.00 16.09           O  
ANISOU 1364  O   LYS A 196     2280   2101   1732     48    -52    -73       O  
ATOM   1365  CB  LYS A 196     -17.038  -0.591  -8.624  1.00 20.51           C  
ANISOU 1365  CB  LYS A 196     2847   2631   2316     74    -91   -118       C  
ATOM   1366  CG  LYS A 196     -18.311  -0.111  -9.348  1.00 20.87           C  
ANISOU 1366  CG  LYS A 196     2892   2662   2376     85   -112   -138       C  
ATOM   1367  CD  LYS A 196     -18.687   1.360  -9.139  1.00 22.32           C  
ANISOU 1367  CD  LYS A 196     3072   2843   2567     95   -127   -161       C  
ATOM   1368  CE  LYS A 196     -20.060   1.498  -8.432  1.00 21.07           C  
ANISOU 1368  CE  LYS A 196     2884   2700   2421     98   -131   -188       C  
ATOM   1369  NZ  LYS A 196     -20.369   2.739  -7.606  1.00 22.28           N  
ANISOU 1369  NZ  LYS A 196     3021   2863   2580    104   -137   -213       N  
ATOM   1370  N   ILE A 197     -14.961  -3.169  -9.210  1.00 14.40           N  
ANISOU 1370  N   ILE A 197     2094   1851   1526     55    -64    -64       N  
ATOM   1371  CA  ILE A 197     -13.571  -3.631  -9.236  1.00 13.15           C  
ANISOU 1371  CA  ILE A 197     1946   1690   1360     48    -53    -44       C  
ATOM   1372  C   ILE A 197     -12.672  -2.756 -10.034  1.00 12.80           C  
ANISOU 1372  C   ILE A 197     1923   1628   1311     52    -58    -44       C  
ATOM   1373  O   ILE A 197     -13.047  -2.224 -11.073  1.00 12.42           O  
ANISOU 1373  O   ILE A 197     1890   1562   1266     58    -71    -51       O  
ATOM   1374  CB  ILE A 197     -13.410  -5.086  -9.781  1.00 13.35           C  
ANISOU 1374  CB  ILE A 197     1975   1709   1389     43    -47    -29       C  
ATOM   1375  CG1 ILE A 197     -14.409  -6.074  -9.185  1.00 14.21           C  
ANISOU 1375  CG1 ILE A 197     2065   1831   1502     38    -43    -28       C  
ATOM   1376  CG2 ILE A 197     -11.972  -5.591  -9.585  1.00 13.38           C  
ANISOU 1376  CG2 ILE A 197     1985   1714   1387     36    -36    -12       C  
ATOM   1377  CD1 ILE A 197     -14.538  -7.386  -9.936  1.00 16.08           C  
ANISOU 1377  CD1 ILE A 197     2306   2057   1745     35    -42    -17       C  
ATOM   1378  N   SER A 198     -11.481  -2.546  -9.556  1.00 12.43           N  
ANISOU 1378  N   SER A 198     1879   1587   1257     48    -49    -35       N  
ATOM   1379  CA  SER A 198     -10.550  -1.734 -10.340  1.00 13.36           C  
ANISOU 1379  CA  SER A 198     2018   1689   1370     49    -53    -35       C  
ATOM   1380  C   SER A 198      -9.162  -2.206 -10.211  1.00 13.07           C  
ANISOU 1380  C   SER A 198     1985   1654   1327     42    -40    -21       C  
ATOM   1381  O   SER A 198      -8.796  -2.885  -9.237  1.00 12.75           O  
ANISOU 1381  O   SER A 198     1930   1629   1286     37    -30    -13       O  
ATOM   1382  CB  SER A 198     -10.665  -0.261 -10.045  1.00 14.53           C  
ANISOU 1382  CB  SER A 198     2167   1837   1516     55    -62    -48       C  
ATOM   1383  OG  SER A 198     -10.405   0.017  -8.689  1.00 15.79           O  
ANISOU 1383  OG  SER A 198     2309   2017   1671     53    -53    -51       O  
ATOM   1384  N   ALA A 199      -8.417  -2.083 -11.305  1.00 12.26           N  
ANISOU 1384  N   ALA A 199     1903   1535   1222     40    -41    -18       N  
ATOM   1385  CA  ALA A 199      -7.134  -2.659 -11.337  1.00 11.95           C  
ANISOU 1385  CA  ALA A 199     1866   1495   1179     34    -29     -7       C  
ATOM   1386  C   ALA A 199      -5.972  -1.706 -11.271  1.00 10.26           C  
ANISOU 1386  C   ALA A 199     1661   1279    958     31    -25     -9       C  
ATOM   1387  O   ALA A 199      -6.062  -0.470 -11.648  1.00 10.30           O  
ANISOU 1387  O   ALA A 199     1679   1276    958     33    -33    -18       O  
ATOM   1388  CB  ALA A 199      -6.972  -3.661 -12.494  1.00 13.29           C  
ANISOU 1388  CB  ALA A 199     2047   1651   1353     30    -27     -1       C  
ATOM   1389  N   PHE A 200      -4.895  -2.274 -10.693  1.00 10.12           N  
ANISOU 1389  N   PHE A 200     1636   1270    940     26    -13     -1       N  
ATOM   1390  CA  PHE A 200      -3.529  -1.717 -10.577  1.00 10.42           C  
ANISOU 1390  CA  PHE A 200     1679   1307    972     22     -5     -1       C  
ATOM   1391  C   PHE A 200      -2.446  -2.653 -11.046  1.00 10.17           C  
ANISOU 1391  C   PHE A 200     1650   1271    944     16      4      5       C  
ATOM   1392  O   PHE A 200      -2.604  -3.926 -10.928  1.00  9.61           O  
ANISOU 1392  O   PHE A 200     1569   1202    880     15      6     13       O  
ATOM   1393  CB  PHE A 200      -3.272  -1.485  -9.060  1.00  9.95           C  
ANISOU 1393  CB  PHE A 200     1601   1268    910     23     -1      0       C  
ATOM   1394  CG  PHE A 200      -4.273  -0.583  -8.415  1.00  9.35           C  
ANISOU 1394  CG  PHE A 200     1519   1201    834     29     -9     -9       C  
ATOM   1395  CD1 PHE A 200      -5.605  -0.981  -8.137  1.00  9.57           C  
ANISOU 1395  CD1 PHE A 200     1536   1235    865     32    -15    -11       C  
ATOM   1396  CD2 PHE A 200      -3.932   0.717  -8.091  1.00  8.99           C  
ANISOU 1396  CD2 PHE A 200     1477   1157    782     30    -11    -17       C  
ATOM   1397  CE1 PHE A 200      -6.499  -0.177  -7.552  1.00  9.55           C  
ANISOU 1397  CE1 PHE A 200     1525   1242    863     37    -21    -22       C  
ATOM   1398  CE2 PHE A 200      -4.861   1.557  -7.547  1.00  9.38           C  
ANISOU 1398  CE2 PHE A 200     1519   1213    832     36    -19    -28       C  
ATOM   1399  CZ  PHE A 200      -6.167   1.136  -7.238  1.00  8.90           C  
ANISOU 1399  CZ  PHE A 200     1446   1160    776     40    -24    -32       C  
ATOM   1400  N   GLY A 201      -1.406  -2.072 -11.633  1.00 10.31           N  
ANISOU 1400  N   GLY A 201     1681   1281    956     11      9      1       N  
ATOM   1401  CA  GLY A 201      -0.261  -2.796 -12.045  1.00  9.82           C  
ANISOU 1401  CA  GLY A 201     1619   1214    897      4     19      3       C  
ATOM   1402  C   GLY A 201       1.066  -2.263 -11.541  1.00  9.95           C  
ANISOU 1402  C   GLY A 201     1634   1237    911      0     28      0       C  
ATOM   1403  O   GLY A 201       1.205  -1.470 -10.587  1.00 10.07           O  
ANISOU 1403  O   GLY A 201     1642   1262    922      3     27     -1       O  
ATOM   1404  N   PRO A 202       2.115  -2.555 -12.276  1.00 10.78           N  
ANISOU 1404  N   PRO A 202     1745   1334   1017     -7     37     -4       N  
ATOM   1405  CA  PRO A 202       3.347  -1.785 -11.927  1.00 11.28           C  
ANISOU 1405  CA  PRO A 202     1808   1402   1076    -11     44    -10       C  
ATOM   1406  C   PRO A 202       3.331  -0.249 -11.838  1.00 11.01           C  
ANISOU 1406  C   PRO A 202     1786   1367   1031    -13     42    -16       C  
ATOM   1407  O   PRO A 202       2.688   0.452 -12.648  1.00 11.25           O  
ANISOU 1407  O   PRO A 202     1835   1387   1054    -15     35    -19       O  
ATOM   1408  CB  PRO A 202       4.352  -2.163 -13.046  1.00 11.11           C  
ANISOU 1408  CB  PRO A 202     1796   1370   1056    -22     55    -18       C  
ATOM   1409  CG  PRO A 202       3.522  -2.806 -14.048  1.00 11.60           C  
ANISOU 1409  CG  PRO A 202     1867   1422   1119    -23     50    -16       C  
ATOM   1410  CD  PRO A 202       2.167  -3.257 -13.551  1.00 11.34           C  
ANISOU 1410  CD  PRO A 202     1825   1392   1090    -13     39     -7       C  
ATOM   1411  N   GLN A 203       4.187   0.270 -10.957  1.00 12.46           N  
ANISOU 1411  N   GLN A 203     1960   1559   1213    -13     47    -18       N  
ATOM   1412  CA  GLN A 203       4.297   1.683 -10.640  1.00 13.71           C  
ANISOU 1412  CA  GLN A 203     2126   1719   1363    -13     44    -24       C  
ATOM   1413  C   GLN A 203       3.023   2.328 -10.099  1.00 13.72           C  
ANISOU 1413  C   GLN A 203     2126   1725   1362     -4     32    -22       C  
ATOM   1414  O   GLN A 203       2.862   3.552 -10.185  1.00 14.82           O  
ANISOU 1414  O   GLN A 203     2276   1859   1495     -4     26    -28       O  
ATOM   1415  CB  GLN A 203       4.896   2.550 -11.775  1.00 15.83           C  
ANISOU 1415  CB  GLN A 203     2418   1974   1622    -24     48    -32       C  
ATOM   1416  CG  GLN A 203       5.819   1.855 -12.731  1.00 18.58           C  
ANISOU 1416  CG  GLN A 203     2772   2316   1972    -35     60    -36       C  
ATOM   1417  CD  GLN A 203       7.284   2.188 -12.605  1.00 19.85           C  
ANISOU 1417  CD  GLN A 203     2931   2480   2133    -44     73    -44       C  
ATOM   1418  OE1 GLN A 203       7.708   2.979 -11.750  1.00 25.40           O  
ANISOU 1418  OE1 GLN A 203     3627   3190   2833    -41     73    -47       O  
ATOM   1419  NE2 GLN A 203       8.098   1.531 -13.414  1.00 22.85           N  
ANISOU 1419  NE2 GLN A 203     3312   2855   2514    -54     84    -51       N  
ATOM   1420  N   SER A 204       2.153   1.535  -9.491  1.00 13.93           N  
ANISOU 1420  N   SER A 204     2138   1760   1394      3     27    -16       N  
ATOM   1421  CA  SER A 204       0.969   2.082  -8.890  1.00 14.60           C  
ANISOU 1421  CA  SER A 204     2217   1851   1478     11     17    -18       C  
ATOM   1422  C   SER A 204       1.217   2.080  -7.406  1.00 13.24           C  
ANISOU 1422  C   SER A 204     2025   1698   1306     14     20    -16       C  
ATOM   1423  O   SER A 204       2.289   1.645  -6.986  1.00 13.42           O  
ANISOU 1423  O   SER A 204     2041   1728   1332     11     29    -13       O  
ATOM   1424  CB  SER A 204      -0.200   1.226  -9.259  1.00 16.45           C  
ANISOU 1424  CB  SER A 204     2451   2083   1718     14     11    -13       C  
ATOM   1425  OG  SER A 204      -0.107  -0.062  -8.621  1.00 17.25           O  
ANISOU 1425  OG  SER A 204     2535   2195   1825     14     16     -4       O  
ATOM   1426  N   ARG A 205       0.157   2.367  -6.642  1.00 12.77           N  
ANISOU 1426  N   ARG A 205     1955   1649   1246     20     13    -18       N  
ATOM   1427  CA  ARG A 205       0.265   2.457  -5.176  1.00 12.09           C  
ANISOU 1427  CA  ARG A 205     1850   1584   1159     21     16    -18       C  
ATOM   1428  C   ARG A 205       0.472   1.087  -4.459  1.00 11.69           C  
ANISOU 1428  C   ARG A 205     1785   1546   1111     19     21     -6       C  
ATOM   1429  O   ARG A 205       0.751   1.062  -3.158  1.00 11.74           O  
ANISOU 1429  O   ARG A 205     1775   1570   1114     18     24     -3       O  
ATOM   1430  CB  ARG A 205      -1.036   3.046  -4.591  1.00 12.45           C  
ANISOU 1430  CB  ARG A 205     1887   1640   1204     27      8    -26       C  
ATOM   1431  CG  ARG A 205      -2.284   2.212  -4.719  1.00 11.38           C  
ANISOU 1431  CG  ARG A 205     1746   1506   1072     29      3    -23       C  
ATOM   1432  CD  ARG A 205      -3.488   3.088  -4.375  1.00 12.62           C  
ANISOU 1432  CD  ARG A 205     1896   1669   1230     34     -6    -37       C  
ATOM   1433  NE  ARG A 205      -3.483   3.566  -2.934  1.00 11.93           N  
ANISOU 1433  NE  ARG A 205     1791   1605   1139     34     -2    -43       N  
ATOM   1434  CZ  ARG A 205      -4.404   4.428  -2.442  1.00 13.00           C  
ANISOU 1434  CZ  ARG A 205     1917   1749   1276     39     -9    -59       C  
ATOM   1435  NH1 ARG A 205      -5.441   4.935  -3.142  1.00 13.06           N  
ANISOU 1435  NH1 ARG A 205     1929   1743   1289     45    -21    -70       N  
ATOM   1436  NH2 ARG A 205      -4.326   4.758  -1.172  1.00 13.03           N  
ANISOU 1436  NH2 ARG A 205     1903   1774   1274     37     -4    -64       N  
ATOM   1437  N   PHE A 206       0.230  -0.031  -5.161  1.00 11.32           N  
ANISOU 1437  N   PHE A 206     1741   1490   1070     17     21      2       N  
ATOM   1438  CA  PHE A 206       0.505  -1.422  -4.686  1.00 12.26           C  
ANISOU 1438  CA  PHE A 206     1849   1614   1194     14     23     15       C  
ATOM   1439  C   PHE A 206       1.682  -2.010  -5.484  1.00 12.30           C  
ANISOU 1439  C   PHE A 206     1861   1606   1205     11     28     18       C  
ATOM   1440  O   PHE A 206       1.872  -3.235  -5.490  1.00 13.13           O  
ANISOU 1440  O   PHE A 206     1961   1709   1319      9     29     27       O  
ATOM   1441  CB  PHE A 206      -0.735  -2.244  -4.855  1.00 12.15           C  
ANISOU 1441  CB  PHE A 206     1832   1601   1184     15     19     20       C  
ATOM   1442  CG  PHE A 206      -1.984  -1.613  -4.236  1.00 11.30           C  
ANISOU 1442  CG  PHE A 206     1717   1505   1071     17     14     13       C  
ATOM   1443  CD1 PHE A 206      -2.025  -1.140  -2.993  1.00 12.05           C  
ANISOU 1443  CD1 PHE A 206     1799   1619   1159     16     15     11       C  
ATOM   1444  CD2 PHE A 206      -3.079  -1.358  -5.015  1.00 11.27           C  
ANISOU 1444  CD2 PHE A 206     1720   1493   1070     21      8      6       C  
ATOM   1445  CE1 PHE A 206      -3.208  -0.532  -2.496  1.00 11.17           C  
ANISOU 1445  CE1 PHE A 206     1679   1519   1044     18     12      1       C  
ATOM   1446  CE2 PHE A 206      -4.227  -0.810  -4.577  1.00 11.12           C  
ANISOU 1446  CE2 PHE A 206     1693   1483   1049     24      3     -3       C  
ATOM   1447  CZ  PHE A 206      -4.305  -0.330  -3.268  1.00 10.68           C  
ANISOU 1447  CZ  PHE A 206     1622   1448    987     22      5     -7       C  
ATOM   1448  N   GLY A 207       2.395  -1.109  -6.218  1.00 12.64           N  
ANISOU 1448  N   GLY A 207     1917   1639   1246     10     32      8       N  
ATOM   1449  CA  GLY A 207       3.450  -1.497  -7.208  1.00 15.13           C  
ANISOU 1449  CA  GLY A 207     2241   1941   1566      5     39      5       C  
ATOM   1450  C   GLY A 207       4.532  -2.395  -6.616  1.00 16.16           C  
ANISOU 1450  C   GLY A 207     2358   2076   1705      4     42     10       C  
ATOM   1451  O   GLY A 207       5.125  -3.233  -7.328  1.00 17.26           O  
ANISOU 1451  O   GLY A 207     2499   2206   1854      1     46     10       O  
ATOM   1452  N   ILE A 208       4.771  -2.283  -5.312  1.00 16.99           N  
ANISOU 1452  N   ILE A 208     2451   2197   1809      6     41     15       N  
ATOM   1453  CA  ILE A 208       5.833  -3.116  -4.662  1.00 16.46           C  
ANISOU 1453  CA  ILE A 208     2372   2133   1750      5     41     20       C  
ATOM   1454  C   ILE A 208       5.690  -4.667  -4.947  1.00 14.74           C  
ANISOU 1454  C   ILE A 208     2149   1908   1545      5     37     29       C  
ATOM   1455  O   ILE A 208       6.693  -5.296  -5.097  1.00 15.47           O  
ANISOU 1455  O   ILE A 208     2236   1993   1648      4     38     28       O  
ATOM   1456  CB  ILE A 208       5.935  -2.990  -3.117  1.00 16.63           C  
ANISOU 1456  CB  ILE A 208     2379   2172   1766      6     37     27       C  
ATOM   1457  CG1 ILE A 208       5.773  -1.586  -2.581  0.50 17.00           C  
ANISOU 1457  CG1 ILE A 208     2428   2230   1801      7     39     19       C  
ATOM   1458  CG2 ILE A 208       7.247  -3.434  -2.520  0.50 16.93           C  
ANISOU 1458  CG2 ILE A 208     2407   2212   1812      5     37     28       C  
ATOM   1459  CD1 ILE A 208       4.939  -1.617  -1.294  0.50 16.20           C  
ANISOU 1459  CD1 ILE A 208     2316   2148   1692      7     34     26       C  
ATOM   1460  N   ILE A 209       4.480  -5.209  -5.119  1.00 13.02           N  
ANISOU 1460  N   ILE A 209     1932   1689   1327      5     32     37       N  
ATOM   1461  CA  ILE A 209       4.291  -6.651  -5.453  1.00 12.95           C  
ANISOU 1461  CA  ILE A 209     1919   1671   1330      5     28     46       C  
ATOM   1462  C   ILE A 209       4.993  -6.992  -6.789  1.00 13.64           C  
ANISOU 1462  C   ILE A 209     2014   1742   1428      3     33     36       C  
ATOM   1463  O   ILE A 209       5.548  -8.064  -6.894  1.00 14.16           O  
ANISOU 1463  O   ILE A 209     2073   1801   1508      3     31     38       O  
ATOM   1464  CB  ILE A 209       2.747  -6.994  -5.502  1.00 13.03           C  
ANISOU 1464  CB  ILE A 209     1930   1683   1336      5     23     53       C  
ATOM   1465  CG1 ILE A 209       2.137  -7.178  -4.145  1.00 12.89           C  
ANISOU 1465  CG1 ILE A 209     1902   1683   1313      3     18     64       C  
ATOM   1466  CG2 ILE A 209       2.415  -8.121  -6.408  1.00 12.44           C  
ANISOU 1466  CG2 ILE A 209     1858   1595   1273      5     21     56       C  
ATOM   1467  CD1 ILE A 209       0.635  -6.839  -4.066  1.00 12.70           C  
ANISOU 1467  CD1 ILE A 209     1879   1666   1280      3     17     64       C  
ATOM   1468  N   HIS A 210       4.870  -6.122  -7.795  1.00 13.18           N  
ANISOU 1468  N   HIS A 210     1970   1677   1362      2     39     25       N  
ATOM   1469  CA  HIS A 210       5.565  -6.290  -9.060  1.00 13.18           C  
ANISOU 1469  CA  HIS A 210     1977   1663   1367     -2     46     13       C  
ATOM   1470  C   HIS A 210       7.012  -5.776  -9.125  1.00 14.00           C  
ANISOU 1470  C   HIS A 210     2080   1766   1472     -6     55      1       C  
ATOM   1471  O   HIS A 210       7.920  -6.356  -9.850  1.00 14.19           O  
ANISOU 1471  O   HIS A 210     2103   1782   1508    -10     61     -8       O  
ATOM   1472  CB  HIS A 210       4.783  -5.596 -10.170  1.00 12.35           C  
ANISOU 1472  CB  HIS A 210     1891   1551   1253     -5     48      7       C  
ATOM   1473  CG  HIS A 210       3.382  -6.108 -10.330  1.00 12.34           C  
ANISOU 1473  CG  HIS A 210     1890   1547   1250     -1     41     16       C  
ATOM   1474  ND1 HIS A 210       3.071  -7.457 -10.535  1.00 12.39           N  
ANISOU 1474  ND1 HIS A 210     1889   1548   1269      0     37     22       N  
ATOM   1475  CD2 HIS A 210       2.203  -5.476 -10.188  1.00 12.93           C  
ANISOU 1475  CD2 HIS A 210     1970   1626   1316      2     35     18       C  
ATOM   1476  CE1 HIS A 210       1.760  -7.569 -10.648  1.00 13.05           C  
ANISOU 1476  CE1 HIS A 210     1976   1632   1350      2     31     27       C  
ATOM   1477  NE2 HIS A 210       1.223  -6.368 -10.491  1.00 13.97           N  
ANISOU 1477  NE2 HIS A 210     2100   1754   1454      4     30     24       N  
ATOM   1478  N   ASP A 211       7.218  -4.632  -8.493  1.00 14.17           N  
ANISOU 1478  N   ASP A 211     2104   1797   1484     -6     57     -1       N  
ATOM   1479  CA  ASP A 211       8.335  -3.763  -8.799  1.00 14.74           C  
ANISOU 1479  CA  ASP A 211     2181   1868   1552    -11     66    -14       C  
ATOM   1480  C   ASP A 211       9.524  -3.977  -7.889  1.00 15.82           C  
ANISOU 1480  C   ASP A 211     2303   2012   1698    -10     67    -17       C  
ATOM   1481  O   ASP A 211      10.685  -3.721  -8.261  1.00 17.83           O  
ANISOU 1481  O   ASP A 211     2556   2262   1956    -15     75    -30       O  
ATOM   1482  CB  ASP A 211       7.948  -2.299  -8.652  1.00 15.10           C  
ANISOU 1482  CB  ASP A 211     2238   1918   1583    -12     67    -17       C  
ATOM   1483  CG  ASP A 211       6.831  -1.817  -9.608  1.00 16.70           C  
ANISOU 1483  CG  ASP A 211     2458   2112   1775    -14     64    -17       C  
ATOM   1484  OD1 ASP A 211       6.865  -2.145 -10.779  1.00 17.95           O  
ANISOU 1484  OD1 ASP A 211     2627   2259   1934    -19     67    -22       O  
ATOM   1485  OD2 ASP A 211       5.952  -1.071  -9.181  1.00 16.87           O  
ANISOU 1485  OD2 ASP A 211     2483   2138   1789    -10     57    -14       O  
ATOM   1486  N   VAL A 212       9.193  -4.462  -6.696  1.00 15.08           N  
ANISOU 1486  N   VAL A 212     2196   1926   1607     -3     57     -4       N  
ATOM   1487  CA  VAL A 212      10.169  -4.561  -5.626  1.00 17.73           C  
ANISOU 1487  CA  VAL A 212     2518   2271   1949     -1     55     -3       C  
ATOM   1488  C   VAL A 212      10.316  -6.062  -5.370  1.00 18.59           C  
ANISOU 1488  C   VAL A 212     2614   2374   2074      2     45      6       C  
ATOM   1489  O   VAL A 212      11.433  -6.572  -5.310  1.00 22.49           O  
ANISOU 1489  O   VAL A 212     3098   2863   2582      2     45     -1       O  
ATOM   1490  CB  VAL A 212       9.692  -3.721  -4.477  1.00 17.68           C  
ANISOU 1490  CB  VAL A 212     2510   2280   1930      1     51      4       C  
ATOM   1491  CG1 VAL A 212      10.470  -3.939  -3.195  1.00 19.74           C  
ANISOU 1491  CG1 VAL A 212     2756   2551   2194      4     45      8       C  
ATOM   1492  CG2 VAL A 212       9.733  -2.240  -4.864  1.00 18.36           C  
ANISOU 1492  CG2 VAL A 212     2607   2367   2003     -1     59     -8       C  
ATOM   1493  N   LEU A 213       9.192  -6.761  -5.232  1.00 17.45           N  
ANISOU 1493  N   LEU A 213     2471   2231   1930      3     38     20       N  
ATOM   1494  CA  LEU A 213       9.230  -8.232  -5.140  1.00 16.93           C  
ANISOU 1494  CA  LEU A 213     2396   2157   1881      5     28     28       C  
ATOM   1495  C   LEU A 213       9.313  -9.028  -6.434  1.00 16.28           C  
ANISOU 1495  C   LEU A 213     2316   2059   1811      4     31     20       C  
ATOM   1496  O   LEU A 213       9.504 -10.213  -6.372  1.00 18.87           O  
ANISOU 1496  O   LEU A 213     2635   2379   2156      6     23     25       O  
ATOM   1497  CB  LEU A 213       8.098  -8.776  -4.283  1.00 16.97           C  
ANISOU 1497  CB  LEU A 213     2398   2170   1880      6     18     48       C  
ATOM   1498  CG  LEU A 213       7.966  -8.007  -2.991  1.00 17.52           C  
ANISOU 1498  CG  LEU A 213     2464   2257   1935      5     15     55       C  
ATOM   1499  CD1 LEU A 213       6.609  -8.096  -2.296  1.00 19.42           C  
ANISOU 1499  CD1 LEU A 213     2706   2510   2164      3     10     69       C  
ATOM   1500  CD2 LEU A 213       9.055  -8.500  -2.074  1.00 16.75           C  
ANISOU 1500  CD2 LEU A 213     2356   2162   1848      6      7     59       C  
ATOM   1501  N   GLY A 214       9.131  -8.390  -7.581  1.00 14.06           N  
ANISOU 1501  N   GLY A 214     2047   1772   1523      0     42      8       N  
ATOM   1502  CA  GLY A 214       9.499  -9.006  -8.875  1.00 15.49           C  
ANISOU 1502  CA  GLY A 214     2231   1940   1716     -3     48     -4       C  
ATOM   1503  C   GLY A 214       8.402  -9.896  -9.378  1.00 14.80           C  
ANISOU 1503  C   GLY A 214     2147   1846   1632     -2     43      5       C  
ATOM   1504  O   GLY A 214       8.555 -10.537 -10.379  1.00 20.48           O  
ANISOU 1504  O   GLY A 214     2866   2554   2361     -4     46     -4       O  
ATOM   1505  N   ILE A 215       7.267 -10.005  -8.681  1.00 14.08           N  
ANISOU 1505  N   ILE A 215     2055   1760   1533      1     34     21       N  
ATOM   1506  CA  ILE A 215       6.166 -10.826  -9.240  1.00 13.92           C  
ANISOU 1506  CA  ILE A 215     2038   1733   1516      2     30     29       C  
ATOM   1507  C   ILE A 215       5.633 -10.256 -10.556  1.00 13.89           C  
ANISOU 1507  C   ILE A 215     2050   1723   1503     -2     38     18       C  
ATOM   1508  O   ILE A 215       5.290  -9.116 -10.701  1.00 13.68           O  
ANISOU 1508  O   ILE A 215     2035   1702   1461     -3     43     15       O  
ATOM   1509  CB  ILE A 215       5.028 -11.093  -8.233  1.00 14.24           C  
ANISOU 1509  CB  ILE A 215     2076   1784   1552      4     20     47       C  
ATOM   1510  CG1 ILE A 215       5.499 -11.975  -7.133  1.00 13.88           C  
ANISOU 1510  CG1 ILE A 215     2016   1740   1517      5     10     59       C  
ATOM   1511  CG2 ILE A 215       3.875 -11.937  -8.780  1.00 14.04           C  
ANISOU 1511  CG2 ILE A 215     2053   1752   1531      4     16     54       C  
ATOM   1512  CD1 ILE A 215       4.553 -11.974  -5.936  1.00 14.08           C  
ANISOU 1512  CD1 ILE A 215     2039   1779   1532      4      3     76       C  
ATOM   1513  N   ASN A 216       5.591 -11.122 -11.536  1.00 13.43           N  
ANISOU 1513  N   ASN A 216     1993   1654   1456     -3     39     13       N  
ATOM   1514  CA  ASN A 216       5.208 -10.682 -12.875  1.00 14.73           C  
ANISOU 1514  CA  ASN A 216     2173   1811   1611     -8     47      3       C  
ATOM   1515  C   ASN A 216       3.773 -10.231 -12.979  1.00 13.66           C  
ANISOU 1515  C   ASN A 216     2049   1679   1464     -6     42     11       C  
ATOM   1516  O   ASN A 216       2.879 -10.817 -12.428  1.00 14.06           O  
ANISOU 1516  O   ASN A 216     2093   1732   1518     -2     34     23       O  
ATOM   1517  CB  ASN A 216       5.430 -11.816 -13.852  1.00 17.01           C  
ANISOU 1517  CB  ASN A 216     2458   2088   1916    -10     48     -5       C  
ATOM   1518  CG  ASN A 216       6.901 -12.058 -14.168  1.00 19.15           C  
ANISOU 1518  CG  ASN A 216     2721   2355   2199    -14     56    -22       C  
ATOM   1519  OD1 ASN A 216       7.775 -11.208 -13.956  1.00 21.10           O  
ANISOU 1519  OD1 ASN A 216     2970   2608   2440    -18     63    -30       O  
ATOM   1520  ND2 ASN A 216       7.175 -13.281 -14.655  1.00 21.16           N  
ANISOU 1520  ND2 ASN A 216     2966   2601   2474    -14     54    -28       N  
ATOM   1521  N   ALA A 217       3.560  -9.098 -13.639  1.00 13.70           N  
ANISOU 1521  N   ALA A 217     2070   1683   1453    -10     46      4       N  
ATOM   1522  CA  ALA A 217       2.183  -8.718 -13.975  1.00 12.60           C  
ANISOU 1522  CA  ALA A 217     1942   1543   1304     -8     40      8       C  
ATOM   1523  C   ALA A 217       1.530  -9.405 -15.198  1.00 13.19           C  
ANISOU 1523  C   ALA A 217     2025   1606   1382    -10     39      5       C  
ATOM   1524  O   ALA A 217       2.071  -9.429 -16.320  1.00 12.60           O  
ANISOU 1524  O   ALA A 217     1960   1523   1306    -17     46     -6       O  
ATOM   1525  CB  ALA A 217       2.115  -7.221 -14.114  1.00 12.79           C  
ANISOU 1525  CB  ALA A 217     1981   1568   1311    -10     42      3       C  
ATOM   1526  N   VAL A 218       0.301  -9.841 -15.001  1.00 13.35           N  
ANISOU 1526  N   VAL A 218     2041   1626   1404     -5     30     14       N  
ATOM   1527  CA AVAL A 218      -0.541 -10.391 -16.056  0.50 13.47           C  
ANISOU 1527  CA AVAL A 218     2065   1632   1422     -5     27     12       C  
ATOM   1528  C   VAL A 218      -0.837  -9.323 -17.126  1.00 13.58           C  
ANISOU 1528  C   VAL A 218     2101   1640   1420    -10     27      3       C  
ATOM   1529  O   VAL A 218      -1.075  -9.618 -18.362  1.00 12.94           O  
ANISOU 1529  O   VAL A 218     2031   1548   1337    -15     27     -3       O  
ATOM   1530  CB AVAL A 218      -1.865 -10.920 -15.459  0.50 12.78           C  
ANISOU 1530  CB AVAL A 218     1969   1549   1339      1     18     23       C  
ATOM   1531  CG1AVAL A 218      -1.629 -12.115 -14.560  0.50 12.37           C  
ANISOU 1531  CG1AVAL A 218     1898   1500   1302      3     16     33       C  
ATOM   1532  CG2AVAL A 218      -2.603  -9.840 -14.706  0.50 12.66           C  
ANISOU 1532  CG2AVAL A 218     1955   1543   1312      5     13     26       C  
ATOM   1533  CA BVAL A 218      -0.519 -10.410 -16.074  0.50 13.53           C  
ANISOU 1533  CA BVAL A 218     2072   1640   1430     -6     27     12       C  
ATOM   1534  CB BVAL A 218      -1.789 -11.128 -15.504  0.50 12.95           C  
ANISOU 1534  CB BVAL A 218     1989   1569   1363      1     18     23       C  
ATOM   1535  CG1BVAL A 218      -2.996 -10.199 -15.371  0.50 12.77           C  
ANISOU 1535  CG1BVAL A 218     1974   1550   1329      5     11     24       C  
ATOM   1536  CG2BVAL A 218      -2.154 -12.334 -16.375  0.50 12.50           C  
ANISOU 1536  CG2BVAL A 218     1931   1502   1318      0     16     22       C  
ATOM   1537  N   ASP A 219      -0.890  -8.074 -16.690  1.00 14.24           N  
ANISOU 1537  N   ASP A 219     2192   1728   1491     -9     25      3       N  
ATOM   1538  CA  ASP A 219      -1.062  -6.978 -17.606  1.00 14.80           C  
ANISOU 1538  CA  ASP A 219     2285   1792   1548    -14     23     -4       C  
ATOM   1539  C   ASP A 219      -0.119  -5.810 -17.247  1.00 17.13           C  
ANISOU 1539  C   ASP A 219     2586   2091   1833    -19     28     -8       C  
ATOM   1540  O   ASP A 219      -0.338  -5.086 -16.304  1.00 15.09           O  
ANISOU 1540  O   ASP A 219     2323   1840   1571    -13     24     -4       O  
ATOM   1541  CB  ASP A 219      -2.520  -6.630 -17.714  1.00 15.16           C  
ANISOU 1541  CB  ASP A 219     2336   1834   1589     -8     10     -1       C  
ATOM   1542  CG  ASP A 219      -2.821  -5.484 -18.682  1.00 14.17           C  
ANISOU 1542  CG  ASP A 219     2236   1698   1450    -12      3     -7       C  
ATOM   1543  OD1 ASP A 219      -1.895  -4.820 -19.197  1.00 14.47           O  
ANISOU 1543  OD1 ASP A 219     2289   1733   1478    -22      9    -12       O  
ATOM   1544  OD2 ASP A 219      -4.034  -5.319 -18.961  1.00 14.80           O  
ANISOU 1544  OD2 ASP A 219     2322   1774   1529     -7    -10     -6       O  
ATOM   1545  N   GLU A 220       0.927  -5.627 -18.050  1.00 17.85           N  
ANISOU 1545  N   GLU A 220     2687   2177   1918    -30     38    -17       N  
ATOM   1546  CA  GLU A 220       1.938  -4.589 -17.841  1.00 19.72           C  
ANISOU 1546  CA  GLU A 220     2931   2417   2146    -36     45    -22       C  
ATOM   1547  C   GLU A 220       1.490  -3.236 -18.285  1.00 20.83           C  
ANISOU 1547  C   GLU A 220     3093   2551   2270    -40     38    -23       C  
ATOM   1548  O   GLU A 220       2.292  -2.294 -18.293  1.00 24.68           O  
ANISOU 1548  O   GLU A 220     3590   3038   2748    -48     43    -28       O  
ATOM   1549  CB  GLU A 220       3.170  -4.900 -18.741  1.00 21.65           C  
ANISOU 1549  CB  GLU A 220     3180   2657   2390    -50     60    -34       C  
ATOM   1550  CG  GLU A 220       3.917  -6.125 -18.291  1.00 23.27           C  
ANISOU 1550  CG  GLU A 220     3362   2867   2613    -47     67    -36       C  
ATOM   1551  CD  GLU A 220       4.933  -5.831 -17.187  1.00 23.33           C  
ANISOU 1551  CD  GLU A 220     3355   2884   2624    -45     73    -37       C  
ATOM   1552  OE1 GLU A 220       4.995  -4.656 -16.688  1.00 24.09           O  
ANISOU 1552  OE1 GLU A 220     3459   2985   2711    -45     71    -35       O  
ATOM   1553  OE2 GLU A 220       5.687  -6.784 -16.828  1.00 26.83           O  
ANISOU 1553  OE2 GLU A 220     3780   3329   3083    -43     77    -40       O  
ATOM   1554  N   ASN A 221       0.268  -3.138 -18.767  1.00 19.83           N  
ANISOU 1554  N   ASN A 221     2977   2417   2140    -36     25    -20       N  
ATOM   1555  CA  ASN A 221      -0.141  -1.960 -19.520  1.00 19.78           C  
ANISOU 1555  CA  ASN A 221     2996   2399   2119    -41     15    -22       C  
ATOM   1556  C   ASN A 221      -1.408  -1.346 -18.945  1.00 18.39           C  
ANISOU 1556  C   ASN A 221     2818   2223   1945    -29     -2    -18       C  
ATOM   1557  O   ASN A 221      -2.159  -0.711 -19.644  1.00 21.69           O  
ANISOU 1557  O   ASN A 221     3256   2630   2356    -29    -15    -19       O  
ATOM   1558  CB  ASN A 221      -0.284  -2.332 -20.986  1.00 19.29           C  
ANISOU 1558  CB  ASN A 221     2954   2326   2050    -52     15    -25       C  
ATOM   1559  CG  ASN A 221       1.022  -2.736 -21.596  1.00 20.82           C  
ANISOU 1559  CG  ASN A 221     3150   2521   2241    -67     33    -33       C  
ATOM   1560  OD1 ASN A 221       2.102  -2.404 -21.091  1.00 20.10           O  
ANISOU 1560  OD1 ASN A 221     3051   2436   2149    -72     44    -37       O  
ATOM   1561  ND2 ASN A 221       0.939  -3.502 -22.676  1.00 25.30           N  
ANISOU 1561  ND2 ASN A 221     3724   3082   2806    -75     36    -37       N  
ATOM   1562  N   ILE A 222      -1.579  -1.511 -17.621  1.00 16.03           N  
ANISOU 1562  N   ILE A 222     2497   1937   1656    -18     -1    -14       N  
ATOM   1563  CA  ILE A 222      -2.664  -0.870 -16.904  1.00 14.27           C  
ANISOU 1563  CA  ILE A 222     2269   1718   1435     -6    -15    -14       C  
ATOM   1564  C   ILE A 222      -2.252   0.515 -16.473  1.00 13.64           C  
ANISOU 1564  C   ILE A 222     2196   1638   1348     -7    -18    -17       C  
ATOM   1565  O   ILE A 222      -1.217   0.661 -15.873  1.00 14.64           O  
ANISOU 1565  O   ILE A 222     2316   1774   1474    -11     -6    -18       O  
ATOM   1566  CB  ILE A 222      -2.991  -1.616 -15.629  1.00 12.73           C  
ANISOU 1566  CB  ILE A 222     2046   1538   1252      3    -12     -9       C  
ATOM   1567  CG1 ILE A 222      -3.331  -3.103 -15.850  1.00 12.64           C  
ANISOU 1567  CG1 ILE A 222     2024   1528   1250      4     -8     -4       C  
ATOM   1568  CG2 ILE A 222      -4.118  -0.893 -14.880  1.00 12.52           C  
ANISOU 1568  CG2 ILE A 222     2013   1517   1227     13    -25    -12       C  
ATOM   1569  CD1 ILE A 222      -3.309  -3.868 -14.504  1.00 12.88           C  
ANISOU 1569  CD1 ILE A 222     2030   1575   1291      9     -3      2       C  
ATOM   1570  N   LYS A 223      -3.030   1.506 -16.873  1.00 15.58           N  
ANISOU 1570  N   LYS A 223     2457   1873   1589     -5    -34    -21       N  
ATOM   1571  CA  LYS A 223      -2.721   2.956 -16.624  1.00 14.60           C  
ANISOU 1571  CA  LYS A 223     2343   1745   1458     -6    -40    -25       C  
ATOM   1572  C   LYS A 223      -2.758   3.236 -15.111  1.00 16.23           C  
ANISOU 1572  C   LYS A 223     2527   1969   1672      4    -38    -27       C  
ATOM   1573  O   LYS A 223      -3.699   2.821 -14.501  1.00 14.82           O  
ANISOU 1573  O   LYS A 223     2331   1799   1502     14    -43    -27       O  
ATOM   1574  CB  LYS A 223      -3.749   3.838 -17.302  1.00 17.16           C  
ANISOU 1574  CB  LYS A 223     2687   2052   1780     -3    -63    -28       C  
ATOM   1575  CG  LYS A 223      -3.413   5.276 -17.092  1.00 17.33           C  
ANISOU 1575  CG  LYS A 223     2720   2068   1796     -5    -70    -32       C  
ATOM   1576  CD  LYS A 223      -3.968   6.293 -18.057  1.00 20.29           C  
ANISOU 1576  CD  LYS A 223     3124   2422   2165     -7    -92    -34       C  
ATOM   1577  CE  LYS A 223      -2.965   7.444 -18.205  1.00 23.99           C  
ANISOU 1577  CE  LYS A 223     3610   2882   2622    -19    -91    -35       C  
ATOM   1578  NZ  LYS A 223      -3.143   7.982 -19.571  1.00 23.35           N  
ANISOU 1578  NZ  LYS A 223     3565   2779   2529    -31   -106    -32       N  
ATOM   1579  N   VAL A 224      -1.808   4.004 -14.577  1.00 14.26           N  
ANISOU 1579  N   VAL A 224     2276   1724   1418      0    -31    -29       N  
ATOM   1580  CA  VAL A 224      -1.720   4.107 -13.129  1.00 14.25           C  
ANISOU 1580  CA  VAL A 224     2251   1741   1423      8    -26    -31       C  
ATOM   1581  C   VAL A 224      -2.687   5.240 -12.746  1.00 13.41           C  
ANISOU 1581  C   VAL A 224     2145   1632   1318     17    -44    -39       C  
ATOM   1582  O   VAL A 224      -2.768   6.257 -13.416  1.00 12.89           O  
ANISOU 1582  O   VAL A 224     2100   1551   1248     15    -56    -43       O  
ATOM   1583  CB  VAL A 224      -0.278   4.385 -12.670  1.00 14.23           C  
ANISOU 1583  CB  VAL A 224     2245   1745   1415      1    -12    -31       C  
ATOM   1584  CG1 VAL A 224      -0.286   4.801 -11.227  1.00 13.86           C  
ANISOU 1584  CG1 VAL A 224     2178   1716   1373      9    -11    -34       C  
ATOM   1585  CG2 VAL A 224       0.580   3.159 -12.847  1.00 13.94           C  
ANISOU 1585  CG2 VAL A 224     2203   1714   1381     -5      4    -26       C  
ATOM   1586  N   GLY A 225      -3.478   4.992 -11.723  1.00 11.57           N  
ANISOU 1586  N   GLY A 225     1889   1414   1093     27    -46    -42       N  
ATOM   1587  CA  GLY A 225      -4.509   5.844 -11.276  1.00 11.57           C  
ANISOU 1587  CA  GLY A 225     1884   1414   1099     37    -61    -52       C  
ATOM   1588  C   GLY A 225      -4.611   5.589  -9.795  1.00 10.92           C  
ANISOU 1588  C   GLY A 225     1773   1356   1020     41    -53    -54       C  
ATOM   1589  O   GLY A 225      -4.515   4.427  -9.340  1.00 11.45           O  
ANISOU 1589  O   GLY A 225     1826   1437   1089     40    -41    -47       O  
ATOM   1590  N   THR A 226      -4.867   6.656  -9.048  1.00 10.62           N  
ANISOU 1590  N   THR A 226     1727   1324    985     47    -60    -66       N  
ATOM   1591  CA  THR A 226      -4.901   6.649  -7.566  1.00 11.12           C  
ANISOU 1591  CA  THR A 226     1765   1412   1050     50    -52    -71       C  
ATOM   1592  C   THR A 226      -5.886   5.633  -7.049  1.00 10.65           C  
ANISOU 1592  C   THR A 226     1686   1367    995     53    -50    -70       C  
ATOM   1593  O   THR A 226      -5.606   4.949  -6.062  1.00 10.76           O  
ANISOU 1593  O   THR A 226     1682   1401   1006     49    -37    -64       O  
ATOM   1594  CB  THR A 226      -5.280   8.026  -7.043  1.00 10.81           C  
ANISOU 1594  CB  THR A 226     1721   1374   1014     57    -63    -87       C  
ATOM   1595  OG1 THR A 226      -4.255   8.993  -7.338  1.00 10.81           O  
ANISOU 1595  OG1 THR A 226     1737   1362   1009     53    -64    -87       O  
ATOM   1596  CG2 THR A 226      -5.418   7.916  -5.535  1.00 10.71           C  
ANISOU 1596  CG2 THR A 226     1680   1388   1001     58    -54    -93       C  
ATOM   1597  N   HIS A 227      -7.055   5.492  -7.698  1.00 11.15           N  
ANISOU 1597  N   HIS A 227     1752   1420   1065     58    -62    -75       N  
ATOM   1598  CA  HIS A 227      -7.998   4.439  -7.332  1.00 11.14           C  
ANISOU 1598  CA  HIS A 227     1734   1431   1068     59    -59    -74       C  
ATOM   1599  C   HIS A 227      -8.219   3.361  -8.389  1.00 11.81           C  
ANISOU 1599  C   HIS A 227     1830   1503   1155     56    -59    -64       C  
ATOM   1600  O   HIS A 227      -9.090   2.506  -8.316  1.00 12.99           O  
ANISOU 1600  O   HIS A 227     1968   1658   1308     57    -59    -63       O  
ATOM   1601  CB  HIS A 227      -9.283   5.044  -6.793  1.00 11.21           C  
ANISOU 1601  CB  HIS A 227     1727   1448   1085     66    -70    -93       C  
ATOM   1602  CG  HIS A 227      -9.099   5.816  -5.513  1.00 11.21           C  
ANISOU 1602  CG  HIS A 227     1710   1467   1084     67    -66   -104       C  
ATOM   1603  ND1 HIS A 227      -8.978   7.171  -5.448  1.00 11.34           N  
ANISOU 1603  ND1 HIS A 227     1730   1476   1102     73    -76   -118       N  
ATOM   1604  CD2 HIS A 227      -8.989   5.374  -4.254  1.00 11.31           C  
ANISOU 1604  CD2 HIS A 227     1701   1506   1091     62    -52   -103       C  
ATOM   1605  CE1 HIS A 227      -8.878   7.570  -4.190  1.00 12.06           C  
ANISOU 1605  CE1 HIS A 227     1802   1590   1192     72    -69   -127       C  
ATOM   1606  NE2 HIS A 227      -8.828   6.490  -3.440  1.00 11.11           N  
ANISOU 1606  NE2 HIS A 227     1666   1490   1065     65    -54   -118       N  
ATOM   1607  N   GLY A 228      -7.273   3.328  -9.306  1.00 11.29           N  
ANISOU 1607  N   GLY A 228     1785   1422   1084     51    -57    -54       N  
ATOM   1608  CA  GLY A 228      -7.288   2.278 -10.251  1.00 11.06           C  
ANISOU 1608  CA  GLY A 228     1765   1382   1055     48    -54    -44       C  
ATOM   1609  C   GLY A 228      -8.242   2.505 -11.387  1.00 11.25           C  
ANISOU 1609  C   GLY A 228     1803   1387   1083     52    -71    -50       C  
ATOM   1610  O   GLY A 228      -8.899   3.498 -11.462  1.00 10.77           O  
ANISOU 1610  O   GLY A 228     1747   1320   1026     58    -86    -62       O  
ATOM   1611  N   LYS A 229      -8.221   1.513 -12.252  1.00 11.61           N  
ANISOU 1611  N   LYS A 229     1857   1424   1128     48    -68    -41       N  
ATOM   1612  CA  LYS A 229      -8.963   1.641 -13.519  1.00 11.38           C  
ANISOU 1612  CA  LYS A 229     1847   1375   1102     50    -83    -45       C  
ATOM   1613  C   LYS A 229     -10.028   0.533 -13.578  1.00 11.01           C  
ANISOU 1613  C   LYS A 229     1787   1332   1063     54    -84    -44       C  
ATOM   1614  O   LYS A 229      -9.755  -0.627 -13.334  1.00 10.39           O  
ANISOU 1614  O   LYS A 229     1699   1263    986     50    -71    -35       O  
ATOM   1615  CB  LYS A 229      -8.048   1.585 -14.682  1.00 12.73           C  
ANISOU 1615  CB  LYS A 229     2042   1530   1263     41    -80    -37       C  
ATOM   1616  CG  LYS A 229      -7.047   2.693 -14.720  1.00 12.74           C  
ANISOU 1616  CG  LYS A 229     2058   1526   1256     36    -79    -38       C  
ATOM   1617  CD  LYS A 229      -7.493   4.118 -15.052  1.00 14.57           C  
ANISOU 1617  CD  LYS A 229     2305   1743   1487     40    -99    -47       C  
ATOM   1618  CE  LYS A 229      -6.353   5.061 -14.807  1.00 14.72           C  
ANISOU 1618  CE  LYS A 229     2333   1762   1497     34    -93    -47       C  
ATOM   1619  NZ  LYS A 229      -6.863   6.414 -14.589  1.00 15.66           N  
ANISOU 1619  NZ  LYS A 229     2457   1873   1620     41   -112    -57       N  
ATOM   1620  N   SER A 230     -11.230   0.990 -13.893  1.00 12.34           N  
ANISOU 1620  N   SER A 230     1957   1493   1239     62   -102    -56       N  
ATOM   1621  CA  SER A 230     -12.461   0.193 -13.915  1.00 14.02           C  
ANISOU 1621  CA  SER A 230     2157   1709   1462     67   -107    -60       C  
ATOM   1622  C   SER A 230     -12.239  -1.092 -14.706  1.00 13.33           C  
ANISOU 1622  C   SER A 230     2075   1616   1373     61    -99    -48       C  
ATOM   1623  O   SER A 230     -11.769  -1.031 -15.817  1.00 16.53           O  
ANISOU 1623  O   SER A 230     2503   2004   1772     57   -102    -44       O  
ATOM   1624  CB  SER A 230     -13.565   1.122 -14.546  1.00 14.89           C  
ANISOU 1624  CB  SER A 230     2275   1803   1579     76   -131    -75       C  
ATOM   1625  OG  SER A 230     -14.866   0.538 -14.788  1.00 18.02           O  
ANISOU 1625  OG  SER A 230     2662   2198   1986     82   -140    -83       O  
ATOM   1626  N   ILE A 231     -12.680  -2.209 -14.161  1.00 12.52           N  
ANISOU 1626  N   ILE A 231     1953   1526   1276     60    -90    -45       N  
ATOM   1627  CA  ILE A 231     -12.629  -3.534 -14.787  1.00 13.09           C  
ANISOU 1627  CA  ILE A 231     2028   1594   1351     55    -83    -35       C  
ATOM   1628  C   ILE A 231     -13.762  -4.470 -14.319  1.00 13.74           C  
ANISOU 1628  C   ILE A 231     2090   1687   1444     57    -82    -37       C  
ATOM   1629  O   ILE A 231     -14.486  -4.169 -13.377  1.00 13.71           O  
ANISOU 1629  O   ILE A 231     2068   1697   1444     60    -84    -46       O  
ATOM   1630  CB  ILE A 231     -11.277  -4.163 -14.631  1.00 12.47           C  
ANISOU 1630  CB  ILE A 231     1951   1520   1267     47    -67    -21       C  
ATOM   1631  CG1 ILE A 231     -10.913  -4.540 -13.189  1.00 11.99           C  
ANISOU 1631  CG1 ILE A 231     1868   1480   1207     44    -54    -16       C  
ATOM   1632  CG2 ILE A 231     -10.147  -3.357 -15.224  1.00 11.39           C  
ANISOU 1632  CG2 ILE A 231     1834   1373   1120     43    -66    -20       C  
ATOM   1633  CD1 ILE A 231     -10.122  -5.839 -13.033  1.00 12.27           C  
ANISOU 1633  CD1 ILE A 231     1898   1520   1244     37    -41     -2       C  
ATOM   1634  N   ASN A 232     -13.907  -5.612 -15.018  1.00 15.07           N  
ANISOU 1634  N   ASN A 232     2261   1849   1617     54    -80    -30       N  
ATOM   1635  CA  ASN A 232     -15.004  -6.534 -14.854  1.00 16.01           C  
ANISOU 1635  CA  ASN A 232     2365   1974   1746     56    -81    -33       C  
ATOM   1636  C   ASN A 232     -14.442  -7.916 -14.726  1.00 14.86           C  
ANISOU 1636  C   ASN A 232     2213   1832   1602     48    -67    -18       C  
ATOM   1637  O   ASN A 232     -13.274  -8.110 -15.028  1.00 13.88           O  
ANISOU 1637  O   ASN A 232     2099   1703   1473     43    -60     -9       O  
ATOM   1638  CB  ASN A 232     -16.081  -6.428 -15.980  1.00 16.61           C  
ANISOU 1638  CB  ASN A 232     2450   2033   1827     62    -97    -43       C  
ATOM   1639  CG  ASN A 232     -15.623  -6.749 -17.410  1.00 19.06           C  
ANISOU 1639  CG  ASN A 232     2783   2324   2134     60   -101    -37       C  
ATOM   1640  OD1 ASN A 232     -14.514  -7.150 -17.720  1.00 19.89           O  
ANISOU 1640  OD1 ASN A 232     2897   2426   2233     53    -91    -27       O  
ATOM   1641  ND2 ASN A 232     -16.581  -6.592 -18.325  1.00 22.36           N  
ANISOU 1641  ND2 ASN A 232     3210   2728   2557     66   -117    -47       N  
ATOM   1642  N   SER A 233     -15.235  -8.838 -14.207  1.00 16.35           N  
ANISOU 1642  N   SER A 233     2384   2030   1798     46    -64    -16       N  
ATOM   1643  CA  SER A 233     -14.837 -10.246 -14.098  1.00 15.22           C  
ANISOU 1643  CA  SER A 233     2235   1889   1660     38    -54     -2       C  
ATOM   1644  C   SER A 233     -14.472 -10.887 -15.468  1.00 15.13           C  
ANISOU 1644  C   SER A 233     2239   1858   1652     39    -56      1       C  
ATOM   1645  O   SER A 233     -13.607 -11.731 -15.490  1.00 16.07           O  
ANISOU 1645  O   SER A 233     2358   1975   1772     33    -48     12       O  
ATOM   1646  CB  SER A 233     -15.854 -11.116 -13.324  1.00 15.37           C  
ANISOU 1646  CB  SER A 233     2233   1920   1685     34    -51     -1       C  
ATOM   1647  OG  SER A 233     -15.995 -10.599 -12.002  1.00 15.30           O  
ANISOU 1647  OG  SER A 233     2211   1932   1672     31    -47     -4       O  
ATOM   1648  N   GLU A 234     -15.053 -10.422 -16.596  1.00 14.10           N  
ANISOU 1648  N   GLU A 234     2122   1713   1521     44    -68     -9       N  
ATOM   1649  CA  GLU A 234     -14.627 -10.930 -17.959  1.00 15.02           C  
ANISOU 1649  CA  GLU A 234     2256   1813   1638     43    -69     -7       C  
ATOM   1650  C   GLU A 234     -13.148 -10.619 -18.141  1.00 14.30           C  
ANISOU 1650  C   GLU A 234     2176   1718   1538     38    -61     -1       C  
ATOM   1651  O   GLU A 234     -12.425 -11.503 -18.619  1.00 14.36           O  
ANISOU 1651  O   GLU A 234     2186   1721   1548     33    -54      5       O  
ATOM   1652  CB  GLU A 234     -15.415 -10.343 -19.119  1.00 15.39           C  
ANISOU 1652  CB  GLU A 234     2319   1846   1684     48    -85    -18       C  
ATOM   1653  CG  GLU A 234     -16.842 -10.817 -19.299  1.00 16.45           C  
ANISOU 1653  CG  GLU A 234     2443   1978   1828     53    -94    -25       C  
ATOM   1654  CD  GLU A 234     -17.824 -10.106 -18.393  1.00 19.10           C  
ANISOU 1654  CD  GLU A 234     2765   2325   2168     59   -101    -36       C  
ATOM   1655  OE1 GLU A 234     -17.422  -9.113 -17.763  1.00 22.03           O  
ANISOU 1655  OE1 GLU A 234     3136   2702   2532     60   -100    -38       O  
ATOM   1656  OE2 GLU A 234     -19.000 -10.530 -18.294  1.00 22.41           O  
ANISOU 1656  OE2 GLU A 234     3171   2747   2598     63   -106    -44       O  
ATOM   1657  N   PHE A 235     -12.721  -9.390 -17.765  1.00 13.73           N  
ANISOU 1657  N   PHE A 235     2110   1649   1456     39    -63     -4       N  
ATOM   1658  CA  PHE A 235     -11.278  -8.937 -17.900  1.00 13.92           C  
ANISOU 1658  CA  PHE A 235     2147   1672   1472     33    -54      0       C  
ATOM   1659  C   PHE A 235     -10.401  -9.861 -17.063  1.00 13.30           C  
ANISOU 1659  C   PHE A 235     2053   1604   1398     29    -41     10       C  
ATOM   1660  O   PHE A 235      -9.293 -10.285 -17.412  1.00 15.45           O  
ANISOU 1660  O   PHE A 235     2329   1872   1670     23    -32     14       O  
ATOM   1661  CB  PHE A 235     -11.121  -7.467 -17.445  1.00 14.30           C  
ANISOU 1661  CB  PHE A 235     2200   1723   1510     36    -59     -6       C  
ATOM   1662  CG  PHE A 235      -9.725  -6.993 -17.352  1.00 14.25           C  
ANISOU 1662  CG  PHE A 235     2202   1718   1495     30    -50     -2       C  
ATOM   1663  CD1 PHE A 235      -8.977  -7.167 -16.183  1.00 14.74           C  
ANISOU 1663  CD1 PHE A 235     2249   1794   1558     28    -39      4       C  
ATOM   1664  CD2 PHE A 235      -9.145  -6.349 -18.420  1.00 14.96           C  
ANISOU 1664  CD2 PHE A 235     2315   1794   1575     25    -52     -6       C  
ATOM   1665  CE1 PHE A 235      -7.676  -6.761 -16.087  1.00 14.77           C  
ANISOU 1665  CE1 PHE A 235     2258   1798   1556     23    -30      6       C  
ATOM   1666  CE2 PHE A 235      -7.880  -5.865 -18.328  1.00 15.12           C  
ANISOU 1666  CE2 PHE A 235     2341   1816   1587     19    -43     -4       C  
ATOM   1667  CZ  PHE A 235      -7.120  -6.102 -17.198  1.00 14.38           C  
ANISOU 1667  CZ  PHE A 235     2231   1736   1497     18    -31      1       C  
ATOM   1668  N   ILE A 236     -10.924 -10.245 -15.927  1.00 14.23           N  
ANISOU 1668  N   ILE A 236     2151   1734   1521     30    -39     14       N  
ATOM   1669  CA  ILE A 236     -10.140 -11.030 -15.055  1.00 13.71           C  
ANISOU 1669  CA  ILE A 236     2073   1677   1459     25    -29     25       C  
ATOM   1670  C   ILE A 236      -9.954 -12.483 -15.669  1.00 14.04           C  
ANISOU 1670  C   ILE A 236     2112   1710   1512     22    -27     31       C  
ATOM   1671  O   ILE A 236      -8.830 -13.048 -15.647  1.00 14.15           O  
ANISOU 1671  O   ILE A 236     2125   1721   1530     18    -20     37       O  
ATOM   1672  CB  ILE A 236     -10.721 -11.079 -13.619  1.00 13.68           C  
ANISOU 1672  CB  ILE A 236     2050   1691   1455     24    -28     30       C  
ATOM   1673  CG1 ILE A 236     -10.751  -9.688 -12.881  1.00 12.65           C  
ANISOU 1673  CG1 ILE A 236     1920   1572   1316     27    -30     22       C  
ATOM   1674  CG2 ILE A 236     -10.010 -12.193 -12.909  1.00 12.96           C  
ANISOU 1674  CG2 ILE A 236     1948   1606   1370     18    -21     43       C  
ATOM   1675  CD1 ILE A 236     -11.444  -9.781 -11.511  1.00 12.96           C  
ANISOU 1675  CD1 ILE A 236     1940   1631   1354     25    -28     24       C  
ATOM   1676  N   LEU A 237     -11.030 -13.098 -16.177  1.00 13.90           N  
ANISOU 1676  N   LEU A 237     2093   1688   1502     24    -32     29       N  
ATOM   1677  CA  LEU A 237     -10.955 -14.408 -16.771  1.00 15.35           C  
ANISOU 1677  CA  LEU A 237     2274   1862   1697     21    -31     33       C  
ATOM   1678  C   LEU A 237     -10.091 -14.346 -18.005  1.00 17.15           C  
ANISOU 1678  C   LEU A 237     2517   2076   1923     20    -29     27       C  
ATOM   1679  O   LEU A 237      -9.285 -15.244 -18.203  1.00 16.76           O  
ANISOU 1679  O   LEU A 237     2464   2022   1881     16    -23     31       O  
ATOM   1680  CB  LEU A 237     -12.340 -15.004 -17.009  1.00 15.99           C  
ANISOU 1680  CB  LEU A 237     2348   1941   1785     23    -38     31       C  
ATOM   1681  CG  LEU A 237     -12.431 -16.171 -18.004  1.00 15.42           C  
ANISOU 1681  CG  LEU A 237     2278   1856   1725     22    -38     31       C  
ATOM   1682  CD1 LEU A 237     -12.173 -17.578 -17.411  1.00 15.66           C  
ANISOU 1682  CD1 LEU A 237     2294   1887   1769     18    -35     42       C  
ATOM   1683  CD2 LEU A 237     -13.840 -16.036 -18.564  1.00 15.52           C  
ANISOU 1683  CD2 LEU A 237     2292   1864   1738     27    -48     22       C  
ATOM   1684  N   GLU A 238     -10.207 -13.268 -18.808  1.00 17.35           N  
ANISOU 1684  N   GLU A 238     2559   2095   1936     21    -33     18       N  
ATOM   1685  CA  GLU A 238      -9.440 -13.155 -20.051  1.00 19.28           C  
ANISOU 1685  CA  GLU A 238     2822   2329   2176     17    -30     11       C  
ATOM   1686  C   GLU A 238      -7.920 -13.147 -19.814  1.00 17.54           C  
ANISOU 1686  C   GLU A 238     2599   2110   1953     11    -19     13       C  
ATOM   1687  O   GLU A 238      -7.145 -13.891 -20.486  1.00 16.45           O  
ANISOU 1687  O   GLU A 238     2463   1966   1821      6    -12     10       O  
ATOM   1688  CB  GLU A 238      -9.820 -11.887 -20.792  1.00 22.40           C  
ANISOU 1688  CB  GLU A 238     3237   2718   2557     17    -39      3       C  
ATOM   1689  CG  GLU A 238      -9.194 -11.724 -22.146  1.00 26.50           C  
ANISOU 1689  CG  GLU A 238     3776   3225   3067     10    -37     -3       C  
ATOM   1690  CD  GLU A 238      -9.067 -10.272 -22.452  1.00 28.94           C  
ANISOU 1690  CD  GLU A 238     4105   3530   3360      8    -43     -7       C  
ATOM   1691  OE1 GLU A 238     -10.144  -9.665 -22.627  1.00 31.95           O  
ANISOU 1691  OE1 GLU A 238     4493   3907   3738     14    -57    -10       O  
ATOM   1692  OE2 GLU A 238      -7.928  -9.754 -22.413  1.00 34.24           O  
ANISOU 1692  OE2 GLU A 238     4783   4204   4023      1    -34     -8       O  
ATOM   1693  N   LYS A 239      -7.525 -12.375 -18.800  1.00 15.97           N  
ANISOU 1693  N   LYS A 239     2397   1922   1750     12    -17     17       N  
ATOM   1694  CA  LYS A 239      -6.122 -12.333 -18.322  1.00 16.82           C  
ANISOU 1694  CA  LYS A 239     2500   2033   1856      8     -7     18       C  
ATOM   1695  C   LYS A 239      -5.646 -13.655 -17.658  1.00 16.23           C  
ANISOU 1695  C   LYS A 239     2407   1961   1798      8     -3     26       C  
ATOM   1696  O   LYS A 239      -4.479 -14.081 -17.861  1.00 18.03           O  
ANISOU 1696  O   LYS A 239     2632   2186   2032      4      4     23       O  
ATOM   1697  CB  LYS A 239      -5.909 -11.137 -17.401  1.00 18.67           C  
ANISOU 1697  CB  LYS A 239     2736   2279   2081     10     -7     20       C  
ATOM   1698  CG  LYS A 239      -6.042  -9.760 -18.104  1.00 18.32           C  
ANISOU 1698  CG  LYS A 239     2711   2228   2021      9    -11     11       C  
ATOM   1699  CD  LYS A 239      -5.248  -9.702 -19.414  1.00 21.33           C  
ANISOU 1699  CD  LYS A 239     3110   2599   2397      0     -6      4       C  
ATOM   1700  CE  LYS A 239      -5.284  -8.280 -19.942  1.00 23.56           C  
ANISOU 1700  CE  LYS A 239     3413   2875   2662     -3    -11     -2       C  
ATOM   1701  NZ  LYS A 239      -4.509  -8.148 -21.211  1.00 23.55           N  
ANISOU 1701  NZ  LYS A 239     3431   2864   2652    -14     -5     -9       N  
ATOM   1702  N   ASN A 240      -6.568 -14.352 -16.971  1.00 16.05           N  
ANISOU 1702  N   ASN A 240     2371   1943   1783     11     -8     35       N  
ATOM   1703  CA  ASN A 240      -6.303 -15.543 -16.194  1.00 16.27           C  
ANISOU 1703  CA  ASN A 240     2383   1973   1825     10     -8     45       C  
ATOM   1704  C   ASN A 240      -4.987 -15.648 -15.395  1.00 14.68           C  
ANISOU 1704  C   ASN A 240     2174   1777   1628      8     -4     50       C  
ATOM   1705  O   ASN A 240      -4.126 -16.551 -15.610  1.00 13.92           O  
ANISOU 1705  O   ASN A 240     2071   1672   1544      6     -2     50       O  
ATOM   1706  CB  ASN A 240      -6.415 -16.699 -17.128  1.00 15.47           C  
ANISOU 1706  CB  ASN A 240     2280   1859   1738      9     -9     43       C  
ATOM   1707  CG  ASN A 240      -6.476 -18.021 -16.410  1.00 17.15           C  
ANISOU 1707  CG  ASN A 240     2477   2072   1967      8    -13     54       C  
ATOM   1708  OD1 ASN A 240      -6.571 -18.112 -15.179  1.00 16.39           O  
ANISOU 1708  OD1 ASN A 240     2372   1985   1871      7    -15     66       O  
ATOM   1709  ND2 ASN A 240      -6.382 -19.046 -17.187  1.00 16.68           N  
ANISOU 1709  ND2 ASN A 240     2416   2001   1922      7    -14     51       N  
ATOM   1710  N   PRO A 241      -4.802 -14.669 -14.493  1.00 14.87           N  
ANISOU 1710  N   PRO A 241     2198   1813   1641      8     -2     52       N  
ATOM   1711  CA  PRO A 241      -3.708 -14.612 -13.625  1.00 14.66           C  
ANISOU 1711  CA  PRO A 241     2164   1791   1615      7      1     57       C  
ATOM   1712  C   PRO A 241      -3.587 -15.841 -12.748  1.00 13.91           C  
ANISOU 1712  C   PRO A 241     2054   1698   1534      5     -4     70       C  
ATOM   1713  O   PRO A 241      -4.572 -16.465 -12.493  1.00 14.88           O  
ANISOU 1713  O   PRO A 241     2172   1822   1660      4     -9     78       O  
ATOM   1714  CB  PRO A 241      -4.062 -13.407 -12.732  1.00 14.33           C  
ANISOU 1714  CB  PRO A 241     2122   1763   1558      8      1     58       C  
ATOM   1715  CG  PRO A 241      -5.503 -13.237 -12.720  1.00 15.00           C  
ANISOU 1715  CG  PRO A 241     2209   1853   1639     10     -4     59       C  
ATOM   1716  CD  PRO A 241      -5.984 -13.943 -13.990  1.00 14.29           C  
ANISOU 1716  CD  PRO A 241     2124   1748   1556     10     -6     54       C  
ATOM   1717  N   ASP A 242      -2.369 -16.098 -12.278  1.00 15.36           N  
ANISOU 1717  N   ASP A 242     2232   1881   1725      4     -4     73       N  
ATOM   1718  CA  ASP A 242      -2.041 -17.137 -11.327  1.00 15.37           C  
ANISOU 1718  CA  ASP A 242     2220   1882   1738      2    -11     86       C  
ATOM   1719  C   ASP A 242      -2.254 -16.675  -9.874  1.00 15.48           C  
ANISOU 1719  C   ASP A 242     2229   1912   1740      0    -13     98       C  
ATOM   1720  O   ASP A 242      -2.500 -17.451  -8.997  1.00 16.16           O  
ANISOU 1720  O   ASP A 242     2308   2002   1831     -4    -20    113       O  
ATOM   1721  CB  ASP A 242      -0.583 -17.613 -11.572  1.00 17.20           C  
ANISOU 1721  CB  ASP A 242     2447   2103   1984      3    -11     80       C  
ATOM   1722  CG  ASP A 242      -0.314 -18.000 -13.072  1.00 17.46           C  
ANISOU 1722  CG  ASP A 242     2485   2122   2028      4     -6     64       C  
ATOM   1723  OD1 ASP A 242      -0.630 -19.144 -13.518  1.00 20.97           O  
ANISOU 1723  OD1 ASP A 242     2924   2555   2487      5    -11     66       O  
ATOM   1724  OD2 ASP A 242       0.192 -17.127 -13.827  1.00 18.21           O  
ANISOU 1724  OD2 ASP A 242     2588   2216   2114      4      3     50       O  
ATOM   1725  N   TYR A 243      -2.131 -15.388  -9.609  1.00 14.75           N  
ANISOU 1725  N   TYR A 243     2142   1830   1632      1     -8     92       N  
ATOM   1726  CA  TYR A 243      -2.445 -14.877  -8.279  1.00 14.08           C  
ANISOU 1726  CA  TYR A 243     2052   1764   1535     -2     -9    101       C  
ATOM   1727  C   TYR A 243      -3.395 -13.713  -8.494  1.00 13.39           C  
ANISOU 1727  C   TYR A 243     1971   1684   1432      0     -5     92       C  
ATOM   1728  O   TYR A 243      -3.222 -12.951  -9.454  1.00 12.85           O  
ANISOU 1728  O   TYR A 243     1913   1609   1360      4      0     79       O  
ATOM   1729  CB  TYR A 243      -1.222 -14.431  -7.555  1.00 14.91           C  
ANISOU 1729  CB  TYR A 243     2154   1874   1638     -2     -8    102       C  
ATOM   1730  CG  TYR A 243      -0.034 -15.390  -7.588  1.00 15.86           C  
ANISOU 1730  CG  TYR A 243     2268   1982   1775     -2    -13    105       C  
ATOM   1731  CD1 TYR A 243      -0.024 -16.561  -6.831  1.00 17.61           C  
ANISOU 1731  CD1 TYR A 243     2482   2202   2007     -5    -24    121       C  
ATOM   1732  CD2 TYR A 243       1.150 -15.043  -8.244  1.00 15.81           C  
ANISOU 1732  CD2 TYR A 243     2264   1967   1774      2     -8     91       C  
ATOM   1733  CE1 TYR A 243       1.105 -17.386  -6.824  1.00 17.58           C  
ANISOU 1733  CE1 TYR A 243     2472   2185   2022     -4    -31    122       C  
ATOM   1734  CE2 TYR A 243       2.270 -15.822  -8.190  1.00 16.26           C  
ANISOU 1734  CE2 TYR A 243     2314   2015   1849      3    -13     91       C  
ATOM   1735  CZ  TYR A 243       2.229 -17.041  -7.544  1.00 17.28           C  
ANISOU 1735  CZ  TYR A 243     2435   2140   1991      1    -26    106       C  
ATOM   1736  OH  TYR A 243       3.421 -17.791  -7.521  1.00 18.00           O  
ANISOU 1736  OH  TYR A 243     2518   2219   2103      3    -33    103       O  
ATOM   1737  N   ILE A 244      -4.445 -13.602  -7.694  1.00 13.32           N  
ANISOU 1737  N   ILE A 244     1956   1689   1415     -3     -6     97       N  
ATOM   1738  CA  ILE A 244      -5.117 -12.322  -7.564  1.00 13.79           C  
ANISOU 1738  CA  ILE A 244     2019   1759   1461     -1     -3     87       C  
ATOM   1739  C   ILE A 244      -4.928 -11.746  -6.196  1.00 14.28           C  
ANISOU 1739  C   ILE A 244     2073   1840   1512     -5     -2     91       C  
ATOM   1740  O   ILE A 244      -5.332 -12.366  -5.209  1.00 15.58           O  
ANISOU 1740  O   ILE A 244     2229   2015   1674    -12     -4    102       O  
ATOM   1741  CB  ILE A 244      -6.622 -12.477  -7.852  1.00 13.91           C  
ANISOU 1741  CB  ILE A 244     2032   1776   1476     -1     -6     84       C  
ATOM   1742  CG1 ILE A 244      -6.687 -13.124  -9.251  1.00 13.20           C  
ANISOU 1742  CG1 ILE A 244     1951   1667   1398      2     -7     80       C  
ATOM   1743  CG2 ILE A 244      -7.374 -11.163  -7.911  1.00 14.03           C  
ANISOU 1743  CG2 ILE A 244     2051   1798   1481      3     -5     70       C  
ATOM   1744  CD1 ILE A 244      -8.059 -13.318  -9.851  1.00 13.87           C  
ANISOU 1744  CD1 ILE A 244     2037   1749   1486      4    -11     75       C  
ATOM   1745  N   PHE A 245      -4.380 -10.539  -6.157  1.00 13.18           N  
ANISOU 1745  N   PHE A 245     1938   1704   1365     -1      2     81       N  
ATOM   1746  CA  PHE A 245      -4.268  -9.831  -4.902  1.00 13.40           C  
ANISOU 1746  CA  PHE A 245     1959   1751   1381     -4      3     82       C  
ATOM   1747  C   PHE A 245      -5.412  -8.783  -4.868  1.00 14.34           C  
ANISOU 1747  C   PHE A 245     2078   1880   1491     -1      4     69       C  
ATOM   1748  O   PHE A 245      -5.488  -7.914  -5.715  1.00 15.58           O  
ANISOU 1748  O   PHE A 245     2244   2027   1647      5      4     57       O  
ATOM   1749  CB  PHE A 245      -2.910  -9.153  -4.734  1.00 12.97           C  
ANISOU 1749  CB  PHE A 245     1908   1696   1324     -2      6     79       C  
ATOM   1750  CG  PHE A 245      -1.761 -10.073  -4.787  1.00 13.70           C  
ANISOU 1750  CG  PHE A 245     2000   1779   1427     -3      5     88       C  
ATOM   1751  CD1 PHE A 245      -1.317 -10.708  -3.615  1.00 13.48           C  
ANISOU 1751  CD1 PHE A 245     1963   1760   1399     -9      0    102       C  
ATOM   1752  CD2 PHE A 245      -1.082 -10.360  -5.991  1.00 13.70           C  
ANISOU 1752  CD2 PHE A 245     2008   1761   1438      1      6     82       C  
ATOM   1753  CE1 PHE A 245      -0.200 -11.549  -3.614  1.00 13.15           C  
ANISOU 1753  CE1 PHE A 245     1919   1708   1369     -9     -4    109       C  
ATOM   1754  CE2 PHE A 245      -0.009 -11.214  -5.996  1.00 13.69           C  
ANISOU 1754  CE2 PHE A 245     2002   1751   1449      0      4     88       C  
ATOM   1755  CZ  PHE A 245       0.435 -11.829  -4.833  1.00 13.60           C  
ANISOU 1755  CZ  PHE A 245     1981   1746   1439     -4     -2    101       C  
ATOM   1756  N   VAL A 246      -6.170  -8.781  -3.755  1.00 13.42           N  
ANISOU 1756  N   VAL A 246     1950   1783   1368     -8      4     71       N  
ATOM   1757  CA  VAL A 246      -7.364  -8.054  -3.568  1.00 13.04           C  
ANISOU 1757  CA  VAL A 246     1897   1745   1314     -7      4     58       C  
ATOM   1758  C   VAL A 246      -7.177  -7.194  -2.358  1.00 13.11           C  
ANISOU 1758  C   VAL A 246     1897   1775   1311    -10      8     54       C  
ATOM   1759  O   VAL A 246      -6.837  -7.724  -1.309  1.00 14.59           O  
ANISOU 1759  O   VAL A 246     2076   1975   1492    -19     10     66       O  
ATOM   1760  CB  VAL A 246      -8.521  -9.052  -3.321  1.00 13.39           C  
ANISOU 1760  CB  VAL A 246     1931   1795   1360    -14      4     64       C  
ATOM   1761  CG1 VAL A 246      -9.849  -8.328  -3.276  1.00 13.54           C  
ANISOU 1761  CG1 VAL A 246     1944   1823   1377    -12      3     46       C  
ATOM   1762  CG2 VAL A 246      -8.474 -10.147  -4.387  1.00 12.85           C  
ANISOU 1762  CG2 VAL A 246     1871   1707   1305    -12      0     72       C  
ATOM   1763  N   VAL A 247      -7.373  -5.884  -2.552  1.00 12.30           N  
ANISOU 1763  N   VAL A 247     1795   1672   1205     -3      7     37       N  
ATOM   1764  CA  VAL A 247      -7.426  -4.825  -1.482  1.00 12.10           C  
ANISOU 1764  CA  VAL A 247     1761   1667   1170     -4     10     26       C  
ATOM   1765  C   VAL A 247      -8.856  -4.331  -1.286  1.00 12.60           C  
ANISOU 1765  C   VAL A 247     1813   1741   1232     -4      9      9       C  
ATOM   1766  O   VAL A 247      -9.370  -3.590  -2.112  1.00 12.88           O  
ANISOU 1766  O   VAL A 247     1855   1765   1274      6      3     -5       O  
ATOM   1767  CB  VAL A 247      -6.489  -3.620  -1.860  1.00 12.46           C  
ANISOU 1767  CB  VAL A 247     1816   1704   1214      4      9     18       C  
ATOM   1768  CG1 VAL A 247      -6.471  -2.561  -0.729  1.00 12.56           C  
ANISOU 1768  CG1 VAL A 247     1818   1737   1217      3     12      7       C  
ATOM   1769  CG2 VAL A 247      -5.080  -4.022  -2.121  1.00 12.51           C  
ANISOU 1769  CG2 VAL A 247     1831   1699   1222      4     11     30       C  
ATOM   1770  N   ASP A 248      -9.478  -4.606  -0.119  1.00 14.38           N  
ANISOU 1770  N   ASP A 248     2023   1990   1449    -15     13      9       N  
ATOM   1771  CA  ASP A 248     -10.868  -4.249   0.038  1.00 15.59           C  
ANISOU 1771  CA  ASP A 248     2164   2154   1604    -15     13     -9       C  
ATOM   1772  C   ASP A 248     -11.048  -2.871   0.601  1.00 17.17           C  
ANISOU 1772  C   ASP A 248     2356   2367   1800    -11     13    -30       C  
ATOM   1773  O   ASP A 248     -11.030  -2.667   1.823  1.00 18.78           O  
ANISOU 1773  O   ASP A 248     2547   2595   1992    -20     19    -33       O  
ATOM   1774  CB  ASP A 248     -11.618  -5.173   0.986  1.00 17.40           C  
ANISOU 1774  CB  ASP A 248     2381   2405   1827    -31     19     -4       C  
ATOM   1775  CG  ASP A 248     -13.146  -5.057   0.787  1.00 17.92           C  
ANISOU 1775  CG  ASP A 248     2435   2476   1898    -31     18    -23       C  
ATOM   1776  OD1 ASP A 248     -13.684  -4.111   0.145  1.00 20.36           O  
ANISOU 1776  OD1 ASP A 248     2744   2777   2217    -18     11    -44       O  
ATOM   1777  OD2 ASP A 248     -13.844  -5.963   1.229  1.00 19.91           O  
ANISOU 1777  OD2 ASP A 248     2678   2740   2147    -44     23    -18       O  
ATOM   1778  N   ARG A 249     -11.374  -1.934  -0.259  1.00 15.94           N  
ANISOU 1778  N   ARG A 249     2206   2197   1654      2      5    -47       N  
ATOM   1779  CA  ARG A 249     -11.486  -0.523   0.136  1.00 16.97           C  
ANISOU 1779  CA  ARG A 249     2330   2335   1784      9      2    -68       C  
ATOM   1780  C   ARG A 249     -12.720  -0.300   1.011  1.00 18.87           C  
ANISOU 1780  C   ARG A 249     2549   2599   2023      3      5    -89       C  
ATOM   1781  O   ARG A 249     -12.853   0.736   1.713  1.00 16.95           O  
ANISOU 1781  O   ARG A 249     2293   2369   1777      5      5   -108       O  
ATOM   1782  CB  ARG A 249     -11.394   0.434  -1.063  1.00 15.94           C  
ANISOU 1782  CB  ARG A 249     2214   2178   1663     24    -10    -78       C  
ATOM   1783  CG  ARG A 249     -11.646   1.896  -0.680  1.00 16.36           C  
ANISOU 1783  CG  ARG A 249     2261   2237   1719     31    -16   -102       C  
ATOM   1784  CD  ARG A 249     -11.349   2.787  -1.893  1.00 17.08           C  
ANISOU 1784  CD  ARG A 249     2371   2300   1819     44    -30   -107       C  
ATOM   1785  NE  ARG A 249     -11.528   4.199  -1.662  1.00 18.35           N  
ANISOU 1785  NE  ARG A 249     2527   2460   1984     52    -38   -128       N  
ATOM   1786  CZ  ARG A 249     -12.680   4.871  -1.712  1.00 20.05           C  
ANISOU 1786  CZ  ARG A 249     2733   2675   2210     60    -49   -152       C  
ATOM   1787  NH1 ARG A 249     -13.836   4.290  -2.033  1.00 22.63           N  
ANISOU 1787  NH1 ARG A 249     3052   3001   2545     61    -53   -159       N  
ATOM   1788  NH2 ARG A 249     -12.670   6.153  -1.472  1.00 18.78           N  
ANISOU 1788  NH2 ARG A 249     2568   2513   2054     67    -58   -170       N  
ATOM   1789  N   ASN A 250     -13.630  -1.284   0.961  1.00 18.26           N  
ANISOU 1789  N   ASN A 250     2465   2527   1948     -4      7    -86       N  
ATOM   1790  CA  ASN A 250     -14.905  -1.238   1.706  1.00 18.23           C  
ANISOU 1790  CA  ASN A 250     2438   2545   1943    -12     11   -106       C  
ATOM   1791  C   ASN A 250     -14.671  -1.222   3.241  1.00 20.04           C  
ANISOU 1791  C   ASN A 250     2653   2807   2156    -28     24   -106       C  
ATOM   1792  O   ASN A 250     -15.419  -0.616   3.975  1.00 21.69           O  
ANISOU 1792  O   ASN A 250     2842   3036   2363    -32     27   -130       O  
ATOM   1793  CB  ASN A 250     -15.862  -2.371   1.240  1.00 18.68           C  
ANISOU 1793  CB  ASN A 250     2492   2598   2006    -17     12   -102       C  
ATOM   1794  CG  ASN A 250     -16.377  -2.181  -0.225  1.00 18.38           C  
ANISOU 1794  CG  ASN A 250     2466   2532   1986     -1     -2   -110       C  
ATOM   1795  OD1 ASN A 250     -16.864  -1.076  -0.599  1.00 17.70           O  
ANISOU 1795  OD1 ASN A 250     2376   2438   1909     12    -12   -133       O  
ATOM   1796  ND2 ASN A 250     -16.166  -3.209  -1.091  1.00 20.43           N  
ANISOU 1796  ND2 ASN A 250     2739   2773   2249     -1     -4    -90       N  
ATOM   1797  N   VAL A 251     -13.595  -1.837   3.693  1.00 21.26           N  
ANISOU 1797  N   VAL A 251     2816   2964   2298    -37     29    -81       N  
ATOM   1798  CA  VAL A 251     -13.301  -1.889   5.141  1.00 23.47           C  
ANISOU 1798  CA  VAL A 251     3084   3274   2560    -54     40    -78       C  
ATOM   1799  C   VAL A 251     -12.921  -0.506   5.702  1.00 24.55           C  
ANISOU 1799  C   VAL A 251     3213   3421   2693    -48     40    -97       C  
ATOM   1800  O   VAL A 251     -13.483  -0.043   6.683  1.00 24.68           O  
ANISOU 1800  O   VAL A 251     3212   3464   2702    -57     46   -116       O  
ATOM   1801  CB  VAL A 251     -12.221  -2.971   5.423  1.00 25.73           C  
ANISOU 1801  CB  VAL A 251     3383   3557   2836    -64     42    -45       C  
ATOM   1802  CG1 VAL A 251     -11.800  -2.961   6.887  1.00 25.46           C  
ANISOU 1802  CG1 VAL A 251     3339   3551   2781    -81     50    -40       C  
ATOM   1803  CG2 VAL A 251     -12.715  -4.340   5.003  1.00 23.54           C  
ANISOU 1803  CG2 VAL A 251     3109   3272   2562    -72     42    -28       C  
ATOM   1804  N   ILE A 252     -12.006   0.159   5.041  1.00 25.40           N  
ANISOU 1804  N   ILE A 252     3335   3508   2808    -33     32    -94       N  
ATOM   1805  CA  ILE A 252     -11.517   1.460   5.387  1.00 25.96           C  
ANISOU 1805  CA  ILE A 252     3403   3582   2878    -25     31   -110       C  
ATOM   1806  C   ILE A 252     -12.640   2.495   5.392  1.00 26.19           C  
ANISOU 1806  C   ILE A 252     3417   3618   2917    -17     26   -144       C  
ATOM   1807  O   ILE A 252     -12.759   3.282   6.330  1.00 30.42           O  
ANISOU 1807  O   ILE A 252     3936   4174   3447    -21     30   -163       O  
ATOM   1808  CB  ILE A 252     -10.439   1.867   4.355  1.00 27.10           C  
ANISOU 1808  CB  ILE A 252     3569   3697   3030    -10     22    -99       C  
ATOM   1809  CG1 ILE A 252      -9.310   0.804   4.262  1.00 26.02           C  
ANISOU 1809  CG1 ILE A 252     3446   3553   2888    -16     26    -68       C  
ATOM   1810  CG2 ILE A 252      -9.926   3.268   4.626  1.00 26.77           C  
ANISOU 1810  CG2 ILE A 252     3524   3656   2989     -2     19   -116       C  
ATOM   1811  CD1 ILE A 252      -8.898   0.153   5.571  1.00 28.33           C  
ANISOU 1811  CD1 ILE A 252     3730   3870   3163    -33     35    -55       C  
ATOM   1812  N   LEU A 253     -13.485   2.446   4.362  1.00 27.89           N  
ANISOU 1812  N   LEU A 253     3635   3814   3148     -8     17   -152       N  
ATOM   1813  CA  LEU A 253     -14.455   3.479   4.036  1.00 26.94           C  
ANISOU 1813  CA  LEU A 253     3504   3690   3043      4      7   -184       C  
ATOM   1814  C   LEU A 253     -15.813   3.264   4.668  1.00 26.24           C  
ANISOU 1814  C   LEU A 253     3390   3624   2955     -5     13   -207       C  
ATOM   1815  O   LEU A 253     -16.613   4.168   4.637  1.00 33.34           O  
ANISOU 1815  O   LEU A 253     4276   4524   3867      4      5   -237       O  
ATOM   1816  CB  LEU A 253     -14.621   3.610   2.527  1.00 26.11           C  
ANISOU 1816  CB  LEU A 253     3417   3549   2954     21     -8   -182       C  
ATOM   1817  CG  LEU A 253     -13.830   4.663   1.717  1.00 26.29           C  
ANISOU 1817  CG  LEU A 253     3458   3546   2984     36    -21   -182       C  
ATOM   1818  CD1 LEU A 253     -14.462   6.044   1.801  1.00 27.31           C  
ANISOU 1818  CD1 LEU A 253     3577   3674   3127     47    -33   -215       C  
ATOM   1819  CD2 LEU A 253     -12.338   4.691   2.087  1.00 26.18           C  
ANISOU 1819  CD2 LEU A 253     3456   3534   2957     32    -13   -162       C  
ATOM   1820  N   GLY A 254     -16.070   2.099   5.250  1.00 25.64           N  
ANISOU 1820  N   GLY A 254     3309   3567   2867    -23     25   -193       N  
ATOM   1821  CA  GLY A 254     -17.294   1.894   6.031  1.00 28.42           C  
ANISOU 1821  CA  GLY A 254     3636   3947   3217    -37     34   -215       C  
ATOM   1822  C   GLY A 254     -18.549   1.555   5.232  1.00 29.52           C  
ANISOU 1822  C   GLY A 254     3768   4075   3372    -31     28   -230       C  
ATOM   1823  O   GLY A 254     -19.662   1.944   5.621  1.00 30.78           O  
ANISOU 1823  O   GLY A 254     3905   4251   3539    -34     29   -261       O  
ATOM   1824  N   ASN A 255     -18.377   0.787   4.153  1.00 29.97           N  
ANISOU 1824  N   ASN A 255     3846   4106   3436    -25     21   -207       N  
ATOM   1825  CA  ASN A 255     -19.506   0.197   3.412  1.00 30.83           C  
ANISOU 1825  CA  ASN A 255     3950   4205   3557    -22     16   -215       C  
ATOM   1826  C   ASN A 255     -19.865  -1.221   3.842  1.00 30.87           C  
ANISOU 1826  C   ASN A 255     3951   4226   3551    -43     30   -198       C  
ATOM   1827  O   ASN A 255     -19.001  -1.931   4.349  1.00 33.40           O  
ANISOU 1827  O   ASN A 255     4281   4553   3855    -56     38   -171       O  
ATOM   1828  CB  ASN A 255     -19.182   0.159   1.922  1.00 30.07           C  
ANISOU 1828  CB  ASN A 255     3878   4072   3475     -4      1   -202       C  
ATOM   1829  CG  ASN A 255     -18.581   1.441   1.442  1.00 29.64           C  
ANISOU 1829  CG  ASN A 255     3834   3999   3428     14    -13   -210       C  
ATOM   1830  OD1 ASN A 255     -18.864   2.497   1.986  1.00 32.11           O  
ANISOU 1830  OD1 ASN A 255     4133   4323   3745     18    -15   -236       O  
ATOM   1831  ND2 ASN A 255     -17.706   1.357   0.454  1.00 27.39           N  
ANISOU 1831  ND2 ASN A 255     3575   3687   3146     23    -20   -189       N  
ATOM   1832  N   LYS A 256     -21.113  -1.658   3.567  1.00 32.52           N  
ANISOU 1832  N   LYS A 256     4147   4437   3770    -46     30   -214       N  
ATOM   1833  CA  LYS A 256     -21.519  -3.079   3.782  1.00 32.92           C  
ANISOU 1833  CA  LYS A 256     4197   4499   3813    -65     40   -197       C  
ATOM   1834  C   LYS A 256     -20.711  -4.036   2.947  1.00 33.23           C  
ANISOU 1834  C   LYS A 256     4262   4513   3853    -62     36   -161       C  
ATOM   1835  O   LYS A 256     -20.265  -5.068   3.441  1.00 38.31           O  
ANISOU 1835  O   LYS A 256     4910   5163   4481    -79     45   -135       O  
ATOM   1836  CB  LYS A 256     -23.009  -3.327   3.463  1.00 29.58           C  
ANISOU 1836  CB  LYS A 256     3757   4079   3405    -67     39   -222       C  
ATOM   1837  CG  LYS A 256     -23.439  -4.779   3.276  0.20 29.88           C  
ANISOU 1837  CG  LYS A 256     3797   4116   3439    -81     46   -203       C  
ATOM   1838  CD  LYS A 256     -24.848  -4.861   2.706  0.20 30.01           C  
ANISOU 1838  CD  LYS A 256     3799   4130   3474    -77     42   -230       C  
ATOM   1839  CE  LYS A 256     -25.322  -6.298   2.555  0.20 29.77           C  
ANISOU 1839  CE  LYS A 256     3770   4100   3441    -92     49   -213       C  
ATOM   1840  NZ  LYS A 256     -25.200  -7.078   3.820  0.20 30.13           N  
ANISOU 1840  NZ  LYS A 256     3809   4175   3463   -123     67   -198       N  
ATOM   1841  N   GLU A 257     -20.545  -3.687   1.672  1.00 33.05           N  
ANISOU 1841  N   GLU A 257     4253   4458   3845    -40     21   -161       N  
ATOM   1842  CA  GLU A 257     -19.959  -4.592   0.667  1.00 32.17           C  
ANISOU 1842  CA  GLU A 257     4165   4321   3738    -36     16   -132       C  
ATOM   1843  C   GLU A 257     -18.600  -5.216   1.033  1.00 31.72           C  
ANISOU 1843  C   GLU A 257     4122   4263   3666    -44     22    -99       C  
ATOM   1844  O   GLU A 257     -17.730  -4.588   1.638  1.00 32.23           O  
ANISOU 1844  O   GLU A 257     4189   4335   3721    -44     24    -96       O  
ATOM   1845  CB  GLU A 257     -19.865  -3.922  -0.710  0.50 31.38           C  
ANISOU 1845  CB  GLU A 257     4080   4190   3654    -12     -1   -139       C  
ATOM   1846  CG  GLU A 257     -19.881  -2.402  -0.698  0.10 31.67           C  
ANISOU 1846  CG  GLU A 257     4113   4224   3697      2    -11   -163       C  
ATOM   1847  CD  GLU A 257     -21.284  -1.848  -0.886  0.10 31.46           C  
ANISOU 1847  CD  GLU A 257     4068   4199   3685      9    -19   -197       C  
ATOM   1848  OE1 GLU A 257     -22.107  -2.531  -1.532  0.10 31.28           O  
ANISOU 1848  OE1 GLU A 257     4044   4168   3672     10    -23   -199       O  
ATOM   1849  OE2 GLU A 257     -21.565  -0.740  -0.384  0.10 31.47           O  
ANISOU 1849  OE2 GLU A 257     4056   4211   3691     14    -23   -223       O  
ATOM   1850  N   ARG A 258     -18.427  -6.469   0.629  1.00 32.76           N  
ANISOU 1850  N   ARG A 258     4264   4385   3799    -50     23    -76       N  
ATOM   1851  CA  ARG A 258     -17.169  -7.196   0.837  1.00 31.42           C  
ANISOU 1851  CA  ARG A 258     4108   4209   3619    -57     25    -45       C  
ATOM   1852  C   ARG A 258     -16.702  -7.825  -0.448  1.00 28.96           C  
ANISOU 1852  C   ARG A 258     3816   3869   3320    -46     17    -29       C  
ATOM   1853  O   ARG A 258     -17.506  -8.106  -1.296  1.00 31.36           O  
ANISOU 1853  O   ARG A 258     4121   4160   3636    -40     12    -36       O  
ATOM   1854  CB  ARG A 258     -17.357  -8.283   1.863  1.00 33.16           C  
ANISOU 1854  CB  ARG A 258     4321   4450   3827    -80     35    -29       C  
ATOM   1855  CG  ARG A 258     -17.512  -7.694   3.238  1.00 31.99           C  
ANISOU 1855  CG  ARG A 258     4157   4333   3663    -94     45    -41       C  
ATOM   1856  CD  ARG A 258     -16.239  -6.981   3.671  1.00 32.56           C  
ANISOU 1856  CD  ARG A 258     4238   4408   3727    -89     44    -34       C  
ATOM   1857  NE  ARG A 258     -16.504  -5.591   4.046  1.00 33.94           N  
ANISOU 1857  NE  ARG A 258     4401   4595   3901    -82     45    -62       N  
ATOM   1858  CZ  ARG A 258     -16.574  -5.130   5.296  1.00 31.39           C  
ANISOU 1858  CZ  ARG A 258     4063   4300   3562    -95     54    -72       C  
ATOM   1859  NH1 ARG A 258     -16.396  -5.940   6.336  1.00 31.29           N  
ANISOU 1859  NH1 ARG A 258     4048   4308   3532   -118     62    -55       N  
ATOM   1860  NH2 ARG A 258     -16.832  -3.845   5.499  1.00 29.44           N  
ANISOU 1860  NH2 ARG A 258     3805   4062   3318    -86     53   -100       N  
ATOM   1861  N   ALA A 259     -15.400  -8.060  -0.522  1.00 28.50           N  
ANISOU 1861  N   ALA A 259     3772   3800   3258    -44     16     -8       N  
ATOM   1862  CA  ALA A 259     -14.703  -8.504  -1.734  1.00 29.03           C  
ANISOU 1862  CA  ALA A 259     3857   3839   3336    -33     10      5       C  
ATOM   1863  C   ALA A 259     -14.956  -9.994  -1.994  1.00 29.17           C  
ANISOU 1863  C   ALA A 259     3876   3849   3358    -42     10     23       C  
ATOM   1864  O   ALA A 259     -15.038 -10.476  -3.130  1.00 26.99           O  
ANISOU 1864  O   ALA A 259     3610   3552   3094    -34      4     26       O  
ATOM   1865  CB  ALA A 259     -13.211  -8.284  -1.532  1.00 28.63           C  
ANISOU 1865  CB  ALA A 259     3816   3783   3278    -31     10     19       C  
ATOM   1866  N   GLN A 260     -15.025 -10.745  -0.904  1.00 30.03           N  
ANISOU 1866  N   GLN A 260     3977   3976   3458    -60     16     35       N  
ATOM   1867  CA  GLN A 260     -15.405 -12.132  -0.935  1.00 31.60           C  
ANISOU 1867  CA  GLN A 260     4175   4171   3660    -71     17     51       C  
ATOM   1868  C   GLN A 260     -16.660 -12.305  -1.796  1.00 33.42           C  
ANISOU 1868  C   GLN A 260     4401   4394   3902    -66     15     36       C  
ATOM   1869  O   GLN A 260     -16.774 -13.282  -2.558  1.00 33.82           O  
ANISOU 1869  O   GLN A 260     4458   4429   3964    -65     11     46       O  
ATOM   1870  CB  GLN A 260     -15.699 -12.596   0.495  1.00 31.57           C  
ANISOU 1870  CB  GLN A 260     4160   4193   3640    -94     24     59       C  
ATOM   1871  CG  GLN A 260     -14.479 -13.019   1.329  1.00 32.13           C  
ANISOU 1871  CG  GLN A 260     4239   4269   3702   -103     24     83       C  
ATOM   1872  CD  GLN A 260     -13.622 -11.850   1.835  1.00 30.02           C  
ANISOU 1872  CD  GLN A 260     3971   4010   3425    -97     25     76       C  
ATOM   1873  OE1 GLN A 260     -13.914 -10.685   1.551  1.00 27.44           O  
ANISOU 1873  OE1 GLN A 260     3640   3685   3099    -85     26     54       O  
ATOM   1874  NE2 GLN A 260     -12.531 -12.172   2.569  1.00 27.77           N  
ANISOU 1874  NE2 GLN A 260     3692   3728   3131   -104     23     96       N  
ATOM   1875  N   GLY A 261     -17.596 -11.361  -1.658  1.00 31.52           N  
ANISOU 1875  N   GLY A 261     4149   4166   3662    -63     16     10       N  
ATOM   1876  CA  GLY A 261     -18.880 -11.432  -2.360  1.00 32.90           C  
ANISOU 1876  CA  GLY A 261     4316   4336   3847    -58     13     -8       C  
ATOM   1877  C   GLY A 261     -18.799 -11.192  -3.856  1.00 33.56           C  
ANISOU 1877  C   GLY A 261     4414   4391   3945    -38      2    -12       C  
ATOM   1878  O   GLY A 261     -19.210 -12.044  -4.664  1.00 30.84           O  
ANISOU 1878  O   GLY A 261     4073   4032   3611    -37     -2     -8       O  
ATOM   1879  N   ILE A 262     -18.283 -10.037  -4.255  1.00 30.44           N  
ANISOU 1879  N   ILE A 262     4027   3988   3551    -24     -4    -22       N  
ATOM   1880  CA  ILE A 262     -18.218  -9.780  -5.685  1.00 28.46           C  
ANISOU 1880  CA  ILE A 262     3791   3711   3311     -8    -15    -26       C  
ATOM   1881  C   ILE A 262     -17.282 -10.744  -6.471  1.00 27.28           C  
ANISOU 1881  C   ILE A 262     3658   3543   3166     -7    -16     -4       C  
ATOM   1882  O   ILE A 262     -17.526 -10.980  -7.653  1.00 25.47           O  
ANISOU 1882  O   ILE A 262     3438   3293   2946      1    -23     -6       O  
ATOM   1883  CB  ILE A 262     -17.989  -8.288  -6.061  1.00 30.58           C  
ANISOU 1883  CB  ILE A 262     4066   3973   3580      7    -23    -43       C  
ATOM   1884  CG1 ILE A 262     -18.029  -8.176  -7.594  1.00 28.94           C  
ANISOU 1884  CG1 ILE A 262     3875   3737   3382     20    -35    -45       C  
ATOM   1885  CG2 ILE A 262     -16.695  -7.748  -5.479  1.00 30.85           C  
ANISOU 1885  CG2 ILE A 262     4107   4013   3604      5    -18    -33       C  
ATOM   1886  CD1 ILE A 262     -18.002  -6.799  -8.228  1.00 27.60           C  
ANISOU 1886  CD1 ILE A 262     3716   3556   3215     34    -47    -61       C  
ATOM   1887  N   LEU A 263     -16.217 -11.258  -5.849  1.00 23.06           N  
ANISOU 1887  N   LEU A 263     3126   3011   2624    -15    -10     16       N  
ATOM   1888  CA  LEU A 263     -15.239 -12.128  -6.531  1.00 22.19           C  
ANISOU 1888  CA  LEU A 263     3030   2884   2519    -14    -11     34       C  
ATOM   1889  C   LEU A 263     -15.642 -13.583  -6.780  1.00 22.06           C  
ANISOU 1889  C   LEU A 263     3010   2860   2511    -22    -11     46       C  
ATOM   1890  O   LEU A 263     -15.109 -14.235  -7.672  1.00 24.78           O  
ANISOU 1890  O   LEU A 263     3365   3186   2864    -17    -15     55       O  
ATOM   1891  CB  LEU A 263     -13.899 -12.109  -5.765  1.00 22.78           C  
ANISOU 1891  CB  LEU A 263     3107   2964   2586    -19     -7     49       C  
ATOM   1892  CG  LEU A 263     -13.053 -10.829  -5.854  1.00 22.27           C  
ANISOU 1892  CG  LEU A 263     3050   2897   2515    -10     -8     41       C  
ATOM   1893  CD1 LEU A 263     -11.618 -11.308  -6.021  1.00 20.28           C  
ANISOU 1893  CD1 LEU A 263     2808   2635   2264    -10     -7     57       C  
ATOM   1894  CD2 LEU A 263     -13.391  -9.828  -6.965  1.00 20.96           C  
ANISOU 1894  CD2 LEU A 263     2893   2717   2352      4    -14     24       C  
ATOM   1895  N   ASP A 264     -16.646 -14.028  -6.075  1.00 21.86           N  
ANISOU 1895  N   ASP A 264     2971   2850   2484    -32     -8     44       N  
ATOM   1896  CA  ASP A 264     -17.095 -15.407  -6.162  1.00 23.28           C  
ANISOU 1896  CA  ASP A 264     3148   3026   2672    -42     -7     56       C  
ATOM   1897  C   ASP A 264     -18.182 -15.611  -7.210  1.00 21.51           C  
ANISOU 1897  C   ASP A 264     2923   2790   2459    -35    -12     43       C  
ATOM   1898  O   ASP A 264     -19.383 -15.649  -6.890  1.00 21.59           O  
ANISOU 1898  O   ASP A 264     2921   2813   2471    -41    -10     31       O  
ATOM   1899  CB  ASP A 264     -17.653 -15.720  -4.782  1.00 23.99           C  
ANISOU 1899  CB  ASP A 264     3224   3140   2751    -60      0     60       C  
ATOM   1900  CG  ASP A 264     -18.132 -17.126  -4.655  1.00 25.53           C  
ANISOU 1900  CG  ASP A 264     3415   3333   2951    -74      1     74       C  
ATOM   1901  OD1 ASP A 264     -18.005 -17.907  -5.626  1.00 31.12           O  
ANISOU 1901  OD1 ASP A 264     4130   4020   3673    -68     -5     81       O  
ATOM   1902  OD2 ASP A 264     -18.656 -17.443  -3.553  1.00 28.63           O  
ANISOU 1902  OD2 ASP A 264     3798   3746   3335    -92      7     78       O  
ATOM   1903  N   ASN A 265     -17.788 -15.723  -8.476  1.00 22.09           N  
ANISOU 1903  N   ASN A 265     3009   2841   2542    -23    -18     43       N  
ATOM   1904  CA  ASN A 265     -18.719 -15.932  -9.546  1.00 21.11           C  
ANISOU 1904  CA  ASN A 265     2887   2705   2430    -15    -24     31       C  
ATOM   1905  C   ASN A 265     -18.045 -16.894 -10.458  1.00 20.85           C  
ANISOU 1905  C   ASN A 265     2865   2652   2406    -13    -27     44       C  
ATOM   1906  O   ASN A 265     -16.847 -17.128 -10.275  1.00 20.26           O  
ANISOU 1906  O   ASN A 265     2797   2573   2329    -15    -25     58       O  
ATOM   1907  CB  ASN A 265     -19.033 -14.598 -10.258  1.00 21.93           C  
ANISOU 1907  CB  ASN A 265     2996   2803   2532     -1    -32     10       C  
ATOM   1908  CG  ASN A 265     -17.798 -13.901 -10.799  1.00 21.10           C  
ANISOU 1908  CG  ASN A 265     2909   2686   2423      8    -34     14       C  
ATOM   1909  OD1 ASN A 265     -17.269 -14.272 -11.841  1.00 21.46           O  
ANISOU 1909  OD1 ASN A 265     2967   2713   2473     12    -38     19       O  
ATOM   1910  ND2 ASN A 265     -17.347 -12.865 -10.100  1.00 19.31           N  
ANISOU 1910  ND2 ASN A 265     2680   2470   2186      9    -32     10       N  
ATOM   1911  N   ALA A 266     -18.820 -17.394 -11.429  1.00 20.32           N  
ANISOU 1911  N   ALA A 266     2798   2572   2349     -9    -33     37       N  
ATOM   1912  CA  ALA A 266     -18.452 -18.464 -12.365  1.00 21.37           C  
ANISOU 1912  CA  ALA A 266     2939   2686   2494     -7    -35     46       C  
ATOM   1913  C   ALA A 266     -17.376 -18.066 -13.370  1.00 22.92           C  
ANISOU 1913  C   ALA A 266     3152   2866   2690      3    -38     45       C  
ATOM   1914  O   ALA A 266     -16.586 -18.921 -13.799  1.00 23.80           O  
ANISOU 1914  O   ALA A 266     3268   2965   2808      1    -38     56       O  
ATOM   1915  CB  ALA A 266     -19.679 -18.957 -13.102  1.00 20.45           C  
ANISOU 1915  CB  ALA A 266     2819   2563   2388     -5    -40     35       C  
ATOM   1916  N   LEU A 267     -17.312 -16.789 -13.742  1.00 20.96           N  
ANISOU 1916  N   LEU A 267     2912   2617   2434     11    -42     33       N  
ATOM   1917  CA  LEU A 267     -16.148 -16.360 -14.474  1.00 21.75           C  
ANISOU 1917  CA  LEU A 267     3029   2706   2531     17    -42     34       C  
ATOM   1918  C   LEU A 267     -14.902 -16.462 -13.633  1.00 21.45           C  
ANISOU 1918  C   LEU A 267     2989   2674   2488     11    -35     48       C  
ATOM   1919  O   LEU A 267     -13.970 -17.139 -14.044  1.00 24.46           O  
ANISOU 1919  O   LEU A 267     3375   3044   2874     10    -34     55       O  
ATOM   1920  CB  LEU A 267     -16.266 -14.971 -15.117  1.00 21.58           C  
ANISOU 1920  CB  LEU A 267     3019   2679   2501     26    -49     20       C  
ATOM   1921  CG  LEU A 267     -17.289 -14.717 -16.216  1.00 20.23           C  
ANISOU 1921  CG  LEU A 267     2855   2497   2334     33    -59      6       C  
ATOM   1922  CD1 LEU A 267     -17.188 -13.266 -16.674  1.00 19.10           C  
ANISOU 1922  CD1 LEU A 267     2726   2349   2181     41    -67     -6       C  
ATOM   1923  CD2 LEU A 267     -17.109 -15.634 -17.419  1.00 20.69           C  
ANISOU 1923  CD2 LEU A 267     2922   2538   2399     33    -61      8       C  
ATOM   1924  N   VAL A 268     -14.839 -15.784 -12.494  1.00 22.54           N  
ANISOU 1924  N   VAL A 268     3120   2828   2616      8    -32     49       N  
ATOM   1925  CA  VAL A 268     -13.610 -15.738 -11.718  1.00 25.58           C  
ANISOU 1925  CA  VAL A 268     3505   3219   2996      4    -27     60       C  
ATOM   1926  C   VAL A 268     -13.117 -17.122 -11.301  1.00 27.26           C  
ANISOU 1926  C   VAL A 268     3711   3428   3217     -4    -25     77       C  
ATOM   1927  O   VAL A 268     -11.907 -17.378 -11.336  1.00 25.38           O  
ANISOU 1927  O   VAL A 268     3477   3184   2981     -4    -24     85       O  
ATOM   1928  CB  VAL A 268     -13.741 -14.876 -10.437  1.00 28.29           C  
ANISOU 1928  CB  VAL A 268     3839   3582   3327      0    -23     59       C  
ATOM   1929  CG1 VAL A 268     -12.475 -14.958  -9.606  1.00 28.68           C  
ANISOU 1929  CG1 VAL A 268     3888   3637   3371     -5    -19     72       C  
ATOM   1930  CG2 VAL A 268     -14.030 -13.400 -10.773  1.00 29.24           C  
ANISOU 1930  CG2 VAL A 268     3966   3704   3440      9    -26     41       C  
ATOM   1931  N   ALA A 269     -14.042 -17.992 -10.888  1.00 27.15           N  
ANISOU 1931  N   ALA A 269     3687   3420   3209    -12    -26     83       N  
ATOM   1932  CA  ALA A 269     -13.709 -19.305 -10.358  1.00 25.74           C  
ANISOU 1932  CA  ALA A 269     3503   3239   3038    -21    -26    100       C  
ATOM   1933  C   ALA A 269     -12.980 -20.233 -11.356  1.00 26.70           C  
ANISOU 1933  C   ALA A 269     3630   3339   3175    -17    -30    104       C  
ATOM   1934  O   ALA A 269     -12.297 -21.178 -10.912  1.00 26.35           O  
ANISOU 1934  O   ALA A 269     3583   3290   3139    -23    -33    119       O  
ATOM   1935  CB  ALA A 269     -14.971 -19.996  -9.891  1.00 26.15           C  
ANISOU 1935  CB  ALA A 269     3544   3299   3092    -31    -26    103       C  
ATOM   1936  N   LYS A 270     -13.142 -19.917 -12.656  1.00 25.43           N  
ANISOU 1936  N   LYS A 270     3479   3167   3018     -8    -31     90       N  
ATOM   1937  CA  LYS A 270     -12.545 -20.613 -13.815  1.00 27.64           C  
ANISOU 1937  CA  LYS A 270     3765   3427   3310     -3    -33     88       C  
ATOM   1938  C   LYS A 270     -11.062 -20.349 -14.027  1.00 24.48           C  
ANISOU 1938  C   LYS A 270     3371   3021   2910     -1    -31     88       C  
ATOM   1939  O   LYS A 270     -10.460 -20.963 -14.929  1.00 25.65           O  
ANISOU 1939  O   LYS A 270     3523   3155   3069      2    -32     85       O  
ATOM   1940  CB  LYS A 270     -13.310 -20.263 -15.122  1.00 28.07           C  
ANISOU 1940  CB  LYS A 270     3827   3473   3365      4    -36     73       C  
ATOM   1941  CG  LYS A 270     -14.487 -21.157 -15.550  1.00 28.61           C  
ANISOU 1941  CG  LYS A 270     3890   3536   3444      2    -40     71       C  
ATOM   1942  CD  LYS A 270     -14.812 -21.098 -17.069  1.00 29.67           C  
ANISOU 1942  CD  LYS A 270     4035   3656   3582     10    -43     57       C  
ATOM   1943  CE  LYS A 270     -15.760 -19.953 -17.493  1.00 28.88           C  
ANISOU 1943  CE  LYS A 270     3941   3560   3472     16    -47     43       C  
ATOM   1944  NZ  LYS A 270     -16.169 -20.038 -18.928  1.00 27.89           N  
ANISOU 1944  NZ  LYS A 270     3826   3420   3350     21    -52     31       N  
ATOM   1945  N   THR A 271     -10.491 -19.417 -13.261  1.00 22.96           N  
ANISOU 1945  N   THR A 271     3179   2840   2705     -1    -28     90       N  
ATOM   1946  CA  THR A 271      -9.086 -18.963 -13.461  1.00 21.67           C  
ANISOU 1946  CA  THR A 271     3022   2672   2540      2    -24     87       C  
ATOM   1947  C   THR A 271      -8.095 -19.747 -12.617  1.00 19.82           C  
ANISOU 1947  C   THR A 271     2779   2437   2314     -3    -26    100       C  
ATOM   1948  O   THR A 271      -8.360 -20.118 -11.483  1.00 19.05           O  
ANISOU 1948  O   THR A 271     2674   2349   2215     -9    -29    113       O  
ATOM   1949  CB  THR A 271      -8.898 -17.496 -13.036  1.00 20.23           C  
ANISOU 1949  CB  THR A 271     2844   2501   2340      4    -21     81       C  
ATOM   1950  OG1 THR A 271      -9.374 -17.323 -11.730  1.00 20.29           O  
ANISOU 1950  OG1 THR A 271     2843   2526   2341     -1    -21     89       O  
ATOM   1951  CG2 THR A 271      -9.644 -16.512 -13.975  1.00 21.38           C  
ANISOU 1951  CG2 THR A 271     3001   2644   2477      9    -21     66       C  
ATOM   1952  N   LYS A 272      -6.880 -19.874 -13.126  1.00 20.07           N  
ANISOU 1952  N   LYS A 272     2814   2458   2353      0    -25     95       N  
ATOM   1953  CA  LYS A 272      -5.814 -20.467 -12.373  1.00 20.39           C  
ANISOU 1953  CA  LYS A 272     2848   2498   2403     -3    -28    105       C  
ATOM   1954  C   LYS A 272      -5.729 -20.000 -10.906  1.00 19.23           C  
ANISOU 1954  C   LYS A 272     2696   2367   2245     -7    -29    117       C  
ATOM   1955  O   LYS A 272      -5.575 -20.831 -10.008  1.00 18.01           O  
ANISOU 1955  O   LYS A 272     2534   2213   2097    -12    -36    132       O  
ATOM   1956  CB  LYS A 272      -4.480 -20.250 -13.110  1.00 20.78           C  
ANISOU 1956  CB  LYS A 272     2900   2538   2458      1    -24     93       C  
ATOM   1957  CG  LYS A 272      -4.363 -20.973 -14.443  1.00 22.24           C  
ANISOU 1957  CG  LYS A 272     3087   2707   2657      3    -24     81       C  
ATOM   1958  CD  LYS A 272      -3.017 -20.626 -15.024  1.00 21.13           C  
ANISOU 1958  CD  LYS A 272     2949   2561   2520      5    -17     67       C  
ATOM   1959  CE  LYS A 272      -3.081 -19.566 -16.122  1.00 22.56           C  
ANISOU 1959  CE  LYS A 272     3144   2743   2686      5     -8     52       C  
ATOM   1960  NZ  LYS A 272      -2.020 -18.488 -16.147  1.00 21.84           N  
ANISOU 1960  NZ  LYS A 272     3058   2656   2583      4      0     42       N  
ATOM   1961  N   ALA A 273      -5.847 -18.702 -10.658  1.00 17.74           N  
ANISOU 1961  N   ALA A 273     2512   2191   2039     -5    -23    111       N  
ATOM   1962  CA  ALA A 273      -5.870 -18.188  -9.312  1.00 17.73           C  
ANISOU 1962  CA  ALA A 273     2505   2206   2024    -10    -23    120       C  
ATOM   1963  C   ALA A 273      -6.985 -18.774  -8.411  1.00 18.71           C  
ANISOU 1963  C   ALA A 273     2623   2341   2145    -19    -27    132       C  
ATOM   1964  O   ALA A 273      -6.732 -19.211  -7.251  1.00 17.53           O  
ANISOU 1964  O   ALA A 273     2468   2200   1995    -27    -31    147       O  
ATOM   1965  CB  ALA A 273      -6.026 -16.725  -9.414  1.00 17.75           C  
ANISOU 1965  CB  ALA A 273     2515   2219   2011     -6    -17    108       C  
ATOM   1966  N   ALA A 274      -8.219 -18.749  -8.883  1.00 17.53           N  
ANISOU 1966  N   ALA A 274     2474   2193   1994    -18    -26    126       N  
ATOM   1967  CA  ALA A 274      -9.330 -19.247  -8.039  1.00 18.84           C  
ANISOU 1967  CA  ALA A 274     2632   2370   2156    -28    -27    136       C  
ATOM   1968  C   ALA A 274      -9.111 -20.766  -7.908  1.00 19.21           C  
ANISOU 1968  C   ALA A 274     2675   2405   2219    -35    -35    152       C  
ATOM   1969  O   ALA A 274      -9.113 -21.318  -6.776  1.00 19.13           O  
ANISOU 1969  O   ALA A 274     2660   2403   2205    -46    -39    168       O  
ATOM   1970  CB  ALA A 274     -10.699 -18.890  -8.633  1.00 18.85           C  
ANISOU 1970  CB  ALA A 274     2633   2374   2154    -26    -24    123       C  
ATOM   1971  N   GLN A 275      -8.849 -21.429  -9.044  1.00 19.71           N  
ANISOU 1971  N   GLN A 275     2741   2449   2298    -28    -38    147       N  
ATOM   1972  CA  GLN A 275      -8.601 -22.882  -9.033  1.00 22.23           C  
ANISOU 1972  CA  GLN A 275     3057   2754   2636    -33    -47    160       C  
ATOM   1973  C   GLN A 275      -7.630 -23.221  -7.900  1.00 22.74           C  
ANISOU 1973  C   GLN A 275     3118   2820   2701    -39    -54    176       C  
ATOM   1974  O   GLN A 275      -8.020 -23.885  -6.943  1.00 27.75           O  
ANISOU 1974  O   GLN A 275     3749   3460   3333    -50    -60    193       O  
ATOM   1975  CB  GLN A 275      -8.063 -23.350 -10.372  1.00 24.30           C  
ANISOU 1975  CB  GLN A 275     3322   2996   2915    -23    -48    149       C  
ATOM   1976  CG  GLN A 275      -9.172 -23.630 -11.376  1.00 26.05           C  
ANISOU 1976  CG  GLN A 275     3545   3211   3142    -21    -46    140       C  
ATOM   1977  CD  GLN A 275      -8.650 -24.011 -12.741  1.00 28.41           C  
ANISOU 1977  CD  GLN A 275     3847   3492   3455    -13    -47    127       C  
ATOM   1978  OE1 GLN A 275      -7.489 -24.387 -12.891  1.00 29.14           O  
ANISOU 1978  OE1 GLN A 275     3938   3574   3559    -11    -49    126       O  
ATOM   1979  NE2 GLN A 275      -9.508 -23.902 -13.745  1.00 29.13           N  
ANISOU 1979  NE2 GLN A 275     3943   3580   3547    -10    -44    115       N  
ATOM   1980  N   ASN A 276      -6.444 -22.646  -7.948  1.00 24.04           N  
ANISOU 1980  N   ASN A 276     3286   2984   2866    -32    -53    170       N  
ATOM   1981  CA  ASN A 276      -5.341 -23.023  -7.078  1.00 21.97           C  
ANISOU 1981  CA  ASN A 276     3020   2718   2608    -35    -62    183       C  
ATOM   1982  C   ASN A 276      -5.326 -22.308  -5.703  1.00 21.13           C  
ANISOU 1982  C   ASN A 276     2913   2633   2481    -43    -61    192       C  
ATOM   1983  O   ASN A 276      -4.276 -22.163  -5.109  1.00 22.21           O  
ANISOU 1983  O   ASN A 276     3049   2770   2618    -42    -65    197       O  
ATOM   1984  CB  ASN A 276      -3.999 -22.823  -7.829  1.00 22.69           C  
ANISOU 1984  CB  ASN A 276     3113   2798   2712    -24    -61    169       C  
ATOM   1985  CG  ASN A 276      -3.967 -23.556  -9.158  1.00 22.74           C  
ANISOU 1985  CG  ASN A 276     3118   2784   2737    -18    -62    158       C  
ATOM   1986  OD1 ASN A 276      -3.510 -23.015 -10.163  1.00 24.53           O  
ANISOU 1986  OD1 ASN A 276     3348   3006   2966    -10    -54    140       O  
ATOM   1987  ND2 ASN A 276      -4.480 -24.764  -9.171  1.00 23.98           N  
ANISOU 1987  ND2 ASN A 276     3272   2931   2909    -22    -71    169       N  
ATOM   1988  N   LYS A 277      -6.498 -21.914  -5.222  1.00 20.55           N  
ANISOU 1988  N   LYS A 277     2840   2577   2392    -51    -54    194       N  
ATOM   1989  CA  LYS A 277      -6.724 -21.100  -3.990  1.00 19.61           C  
ANISOU 1989  CA  LYS A 277     2719   2481   2250    -59    -50    199       C  
ATOM   1990  C   LYS A 277      -5.710 -19.957  -3.756  1.00 20.01           C  
ANISOU 1990  C   LYS A 277     2771   2539   2292    -52    -46    190       C  
ATOM   1991  O   LYS A 277      -5.209 -19.753  -2.660  1.00 19.92           O  
ANISOU 1991  O   LYS A 277     2759   2539   2271    -58    -49    200       O  
ATOM   1992  CB  LYS A 277      -6.903 -22.014  -2.755  1.00 19.16           C  
ANISOU 1992  CB  LYS A 277     2660   2430   2189    -76    -60    222       C  
ATOM   1993  CG  LYS A 277      -8.045 -23.006  -2.860  1.00 20.97           C  
ANISOU 1993  CG  LYS A 277     2888   2657   2424    -86    -62    230       C  
ATOM   1994  CD  LYS A 277      -7.658 -24.297  -2.145  1.00 20.36           C  
ANISOU 1994  CD  LYS A 277     2812   2570   2356    -98    -78    254       C  
ATOM   1995  CE  LYS A 277      -8.592 -25.483  -2.349  1.00 20.75           C  
ANISOU 1995  CE  LYS A 277     2860   2610   2415   -108    -83    264       C  
ATOM   1996  NZ  LYS A 277      -9.956 -25.520  -1.738  1.00 19.81           N  
ANISOU 1996  NZ  LYS A 277     2739   2510   2279   -125    -75    268       N  
ATOM   1997  N   LYS A 278      -5.414 -19.212  -4.842  1.00 18.32           N  
ANISOU 1997  N   LYS A 278     2561   2318   2082    -39    -39    172       N  
ATOM   1998  CA  LYS A 278      -4.560 -18.025  -4.789  1.00 19.37           C  
ANISOU 1998  CA  LYS A 278     2696   2457   2206    -32    -33    161       C  
ATOM   1999  C   LYS A 278      -5.285 -16.705  -5.106  1.00 18.34           C  
ANISOU 1999  C   LYS A 278     2568   2338   2061    -28    -23    145       C  
ATOM   2000  O   LYS A 278      -4.636 -15.779  -5.618  1.00 16.93           O  
ANISOU 2000  O   LYS A 278     2395   2156   1880    -20    -18    132       O  
ATOM   2001  CB  LYS A 278      -3.345 -18.209  -5.714  1.00 20.60           C  
ANISOU 2001  CB  LYS A 278     2855   2594   2378    -23    -35    153       C  
ATOM   2002  CG  LYS A 278      -2.389 -19.264  -5.149  1.00 21.38           C  
ANISOU 2002  CG  LYS A 278     2949   2683   2490    -26    -47    167       C  
ATOM   2003  CD  LYS A 278      -1.616 -18.765  -3.912  1.00 23.26           C  
ANISOU 2003  CD  LYS A 278     3185   2934   2719    -29    -50    175       C  
ATOM   2004  CE  LYS A 278      -0.748 -19.929  -3.496  1.00 23.53           C  
ANISOU 2004  CE  LYS A 278     3216   2955   2771    -31    -65    188       C  
ATOM   2005  NZ  LYS A 278      -0.097 -19.952  -2.174  1.00 25.95           N  
ANISOU 2005  NZ  LYS A 278     3520   3270   3070    -37    -75    202       N  
ATOM   2006  N   ILE A 279      -6.575 -16.617  -4.754  1.00 17.58           N  
ANISOU 2006  N   ILE A 279     2469   2254   1956    -34    -21    145       N  
ATOM   2007  CA  ILE A 279      -7.194 -15.301  -4.449  1.00 17.35           C  
ANISOU 2007  CA  ILE A 279     2439   2241   1911    -32    -14    132       C  
ATOM   2008  C   ILE A 279      -6.804 -14.817  -3.065  1.00 16.78           C  
ANISOU 2008  C   ILE A 279     2362   2190   1825    -40    -13    138       C  
ATOM   2009  O   ILE A 279      -7.230 -15.388  -2.038  1.00 16.45           O  
ANISOU 2009  O   ILE A 279     2314   2160   1777    -53    -14    151       O  
ATOM   2010  CB  ILE A 279      -8.727 -15.317  -4.511  1.00 19.19           C  
ANISOU 2010  CB  ILE A 279     2668   2483   2141    -36    -11    126       C  
ATOM   2011  CG1 ILE A 279      -9.193 -15.638  -5.935  1.00 20.03           C  
ANISOU 2011  CG1 ILE A 279     2780   2571   2260    -28    -13    118       C  
ATOM   2012  CG2 ILE A 279      -9.270 -13.945  -4.154  1.00 18.55           C  
ANISOU 2012  CG2 ILE A 279     2583   2418   2046    -34     -6    111       C  
ATOM   2013  CD1 ILE A 279     -10.564 -16.326  -5.942  1.00 22.03           C  
ANISOU 2013  CD1 ILE A 279     3026   2827   2516    -34    -14    119       C  
ATOM   2014  N   ILE A 280      -6.070 -13.724  -3.013  1.00 14.75           N  
ANISOU 2014  N   ILE A 280     2107   1936   1562    -33     -9    129       N  
ATOM   2015  CA  ILE A 280      -5.457 -13.281  -1.733  1.00 13.97           C  
ANISOU 2015  CA  ILE A 280     2004   1854   1451    -39     -9    135       C  
ATOM   2016  C   ILE A 280      -6.028 -11.941  -1.280  1.00 13.83           C  
ANISOU 2016  C   ILE A 280     1983   1855   1418    -38     -2    120       C  
ATOM   2017  O   ILE A 280      -5.859 -10.937  -1.977  1.00 15.23           O  
ANISOU 2017  O   ILE A 280     2164   2026   1595    -28      1    105       O  
ATOM   2018  CB  ILE A 280      -3.921 -13.188  -1.887  1.00 14.32           C  
ANISOU 2018  CB  ILE A 280     2053   1887   1501    -33    -11    137       C  
ATOM   2019  CG1 ILE A 280      -3.269 -14.552  -2.314  1.00 16.02           C  
ANISOU 2019  CG1 ILE A 280     2270   2083   1735    -33    -20    149       C  
ATOM   2020  CG2 ILE A 280      -3.309 -12.654  -0.599  1.00 13.53           C  
ANISOU 2020  CG2 ILE A 280     1948   1805   1389    -38    -11    141       C  
ATOM   2021  CD1 ILE A 280      -4.034 -15.820  -2.010  1.00 17.15           C  
ANISOU 2021  CD1 ILE A 280     2410   2225   1883    -43    -26    164       C  
ATOM   2022  N   TYR A 281      -6.663 -11.912  -0.074  1.00 14.84           N  
ANISOU 2022  N   TYR A 281     2102   2005   1533    -50      0    124       N  
ATOM   2023  CA  TYR A 281      -7.248 -10.754   0.433  1.00 15.71           C  
ANISOU 2023  CA  TYR A 281     2205   2133   1630    -51      6    109       C  
ATOM   2024  C   TYR A 281      -6.185 -10.116   1.311  1.00 17.00           C  
ANISOU 2024  C   TYR A 281     2368   2308   1784    -52      7    111       C  
ATOM   2025  O   TYR A 281      -6.030 -10.458   2.519  1.00 19.23           O  
ANISOU 2025  O   TYR A 281     2645   2606   2055    -65      6    123       O  
ATOM   2026  CB  TYR A 281      -8.569 -11.028   1.194  1.00 15.29           C  
ANISOU 2026  CB  TYR A 281     2141   2099   1567    -64     10    108       C  
ATOM   2027  CG  TYR A 281      -9.594 -11.631   0.302  1.00 17.17           C  
ANISOU 2027  CG  TYR A 281     2380   2327   1816    -62      9    104       C  
ATOM   2028  CD1 TYR A 281     -10.402 -10.845  -0.537  1.00 16.83           C  
ANISOU 2028  CD1 TYR A 281     2336   2279   1778    -52     10     83       C  
ATOM   2029  CD2 TYR A 281      -9.645 -13.008   0.154  1.00 17.26           C  
ANISOU 2029  CD2 TYR A 281     2395   2329   1836    -70      4    122       C  
ATOM   2030  CE1 TYR A 281     -11.338 -11.456  -1.401  1.00 17.47           C  
ANISOU 2030  CE1 TYR A 281     2418   2349   1870    -50      8     80       C  
ATOM   2031  CE2 TYR A 281     -10.570 -13.618  -0.650  1.00 19.24           C  
ANISOU 2031  CE2 TYR A 281     2645   2570   2097    -69      3    119       C  
ATOM   2032  CZ  TYR A 281     -11.367 -12.869  -1.448  1.00 19.57           C  
ANISOU 2032  CZ  TYR A 281     2686   2608   2142    -58      5     98       C  
ATOM   2033  OH  TYR A 281     -12.228 -13.525  -2.275  1.00 24.11           O  
ANISOU 2033  OH  TYR A 281     3261   3172   2729    -57      3     96       O  
ATOM   2034  N   LEU A 282      -5.472  -9.167   0.696  1.00 15.19           N  
ANISOU 2034  N   LEU A 282     2145   2069   1559    -39      8     99       N  
ATOM   2035  CA  LEU A 282      -4.438  -8.433   1.388  1.00 14.41           C  
ANISOU 2035  CA  LEU A 282     2045   1979   1452    -38      9     98       C  
ATOM   2036  C   LEU A 282      -5.081  -7.508   2.446  1.00 14.22           C  
ANISOU 2036  C   LEU A 282     2011   1980   1413    -44     14     88       C  
ATOM   2037  O   LEU A 282      -6.176  -7.051   2.302  1.00 15.17           O  
ANISOU 2037  O   LEU A 282     2126   2106   1530    -43     17     74       O  
ATOM   2038  CB  LEU A 282      -3.567  -7.620   0.413  1.00 14.26           C  
ANISOU 2038  CB  LEU A 282     2035   1942   1440    -25     10     87       C  
ATOM   2039  CG  LEU A 282      -2.701  -8.491  -0.481  1.00 14.19           C  
ANISOU 2039  CG  LEU A 282     2035   1912   1446    -21      7     96       C  
ATOM   2040  CD1 LEU A 282      -2.092  -7.516  -1.438  1.00 13.44           C  
ANISOU 2040  CD1 LEU A 282     1948   1804   1354    -11     10     82       C  
ATOM   2041  CD2 LEU A 282      -1.633  -9.346   0.270  1.00 14.77           C  
ANISOU 2041  CD2 LEU A 282     2105   1985   1522    -26      1    112       C  
ATOM   2042  N   ASP A 283      -4.385  -7.298   3.557  1.00 15.24           N  
ANISOU 2042  N   ASP A 283     2136   2124   1531    -51     15     93       N  
ATOM   2043  CA  ASP A 283      -4.925  -6.409   4.575  1.00 14.83           C  
ANISOU 2043  CA  ASP A 283     2073   2098   1463    -57     20     81       C  
ATOM   2044  C   ASP A 283      -4.962  -4.908   4.227  1.00 14.46           C  
ANISOU 2044  C   ASP A 283     2025   2051   1417    -45     24     58       C  
ATOM   2045  O   ASP A 283      -3.903  -4.262   4.115  1.00 14.30           O  
ANISOU 2045  O   ASP A 283     2010   2025   1398    -37     23     56       O  
ATOM   2046  CB  ASP A 283      -4.167  -6.676   5.891  1.00 14.78           C  
ANISOU 2046  CB  ASP A 283     2064   2108   1444    -69     19     95       C  
ATOM   2047  CG  ASP A 283      -4.829  -6.004   7.133  1.00 15.71           C  
ANISOU 2047  CG  ASP A 283     2169   2256   1542    -80     25     85       C  
ATOM   2048  OD1 ASP A 283      -5.648  -5.083   7.043  1.00 16.41           O  
ANISOU 2048  OD1 ASP A 283     2250   2355   1630    -77     31     63       O  
ATOM   2049  OD2 ASP A 283      -4.397  -6.351   8.254  1.00 16.91           O  
ANISOU 2049  OD2 ASP A 283     2319   2425   1682    -94     23     97       O  
ATOM   2050  N   PRO A 284      -6.176  -4.350   3.987  1.00 14.71           N  
ANISOU 2050  N   PRO A 284     2051   2088   1449    -43     26     40       N  
ATOM   2051  CA  PRO A 284      -6.282  -2.936   3.555  1.00 14.91           C  
ANISOU 2051  CA  PRO A 284     2076   2110   1478    -30     26     18       C  
ATOM   2052  C   PRO A 284      -5.755  -1.935   4.505  1.00 15.64           C  
ANISOU 2052  C   PRO A 284     2162   2220   1561    -31     29      9       C  
ATOM   2053  O   PRO A 284      -5.356  -0.880   4.059  1.00 14.82           O  
ANISOU 2053  O   PRO A 284     2063   2107   1461    -20     28     -3       O  
ATOM   2054  CB  PRO A 284      -7.783  -2.687   3.377  1.00 16.00           C  
ANISOU 2054  CB  PRO A 284     2205   2254   1619    -30     26      1       C  
ATOM   2055  CG  PRO A 284      -8.440  -3.801   4.092  1.00 14.74           C  
ANISOU 2055  CG  PRO A 284     2038   2111   1453    -46     30     12       C  
ATOM   2056  CD  PRO A 284      -7.517  -4.948   4.123  1.00 14.72           C  
ANISOU 2056  CD  PRO A 284     2044   2099   1449    -51     28     38       C  
ATOM   2057  N   GLU A 285      -5.795  -2.198   5.811  1.00 16.25           N  
ANISOU 2057  N   GLU A 285     2229   2322   1624    -45     33     14       N  
ATOM   2058  CA  GLU A 285      -5.254  -1.198   6.719  1.00 18.06           C  
ANISOU 2058  CA  GLU A 285     2452   2568   1844    -46     36      4       C  
ATOM   2059  C   GLU A 285      -3.758  -1.047   6.550  1.00 16.11           C  
ANISOU 2059  C   GLU A 285     2215   2308   1599    -39     33     14       C  
ATOM   2060  O   GLU A 285      -3.203  -0.064   6.984  1.00 18.62           O  
ANISOU 2060  O   GLU A 285     2529   2633   1912    -36     35      4       O  
ATOM   2061  CB  GLU A 285      -5.546  -1.584   8.186  1.00 18.06           C  
ANISOU 2061  CB  GLU A 285     2439   2598   1825    -64     41      9       C  
ATOM   2062  CG  GLU A 285      -6.832  -1.034   8.717  1.00 20.29           C  
ANISOU 2062  CG  GLU A 285     2705   2902   2101    -71     47    -13       C  
ATOM   2063  CD  GLU A 285      -7.342  -1.645  10.035  1.00 20.07           C  
ANISOU 2063  CD  GLU A 285     2666   2905   2053    -93     53     -7       C  
ATOM   2064  OE1 GLU A 285      -6.699  -2.494  10.734  1.00 21.26           O  
ANISOU 2064  OE1 GLU A 285     2822   3063   2193   -107     52     16       O  
ATOM   2065  OE2 GLU A 285      -8.494  -1.300  10.314  1.00 21.86           O  
ANISOU 2065  OE2 GLU A 285     2879   3149   2278    -99     59    -27       O  
ATOM   2066  N   TYR A 286      -3.120  -2.047   5.965  1.00 16.46           N  
ANISOU 2066  N   TYR A 286     2269   2334   1650    -38     30     33       N  
ATOM   2067  CA  TYR A 286      -1.717  -1.962   5.593  1.00 15.75           C  
ANISOU 2067  CA  TYR A 286     2189   2229   1567    -31     27     40       C  
ATOM   2068  C   TYR A 286      -1.645  -1.448   4.140  1.00 14.43           C  
ANISOU 2068  C   TYR A 286     2033   2037   1414    -18     26     30       C  
ATOM   2069  O   TYR A 286      -0.973  -0.541   3.882  1.00 18.19           O  
ANISOU 2069  O   TYR A 286     2513   2507   1891    -11     27     21       O  
ATOM   2070  CB  TYR A 286      -1.015  -3.307   5.742  1.00 15.67           C  
ANISOU 2070  CB  TYR A 286     2183   2212   1559    -37     22     63       C  
ATOM   2071  CG  TYR A 286      -0.728  -3.801   7.197  1.00 17.47           C  
ANISOU 2071  CG  TYR A 286     2403   2461   1773    -51     20     76       C  
ATOM   2072  CD1 TYR A 286      -1.658  -4.601   7.833  1.00 16.45           C  
ANISOU 2072  CD1 TYR A 286     2269   2346   1634    -65     20     86       C  
ATOM   2073  CD2 TYR A 286       0.463  -3.547   7.802  1.00 17.68           C  
ANISOU 2073  CD2 TYR A 286     2430   2492   1796    -51     18     80       C  
ATOM   2074  CE1 TYR A 286      -1.446  -5.120   9.091  1.00 17.93           C  
ANISOU 2074  CE1 TYR A 286     2452   2552   1807    -81     17    100       C  
ATOM   2075  CE2 TYR A 286       0.683  -4.019   9.099  1.00 19.83           C  
ANISOU 2075  CE2 TYR A 286     2698   2783   2055    -64     14     93       C  
ATOM   2076  CZ  TYR A 286      -0.266  -4.807   9.717  1.00 18.83           C  
ANISOU 2076  CZ  TYR A 286     2568   2670   1917    -80     13    103       C  
ATOM   2077  OH  TYR A 286      -0.058  -5.343  11.049  1.00 16.41           O  
ANISOU 2077  OH  TYR A 286     2259   2383   1594    -96      8    119       O  
ATOM   2078  N   TRP A 287      -2.301  -2.099   3.209  1.00 13.62           N  
ANISOU 2078  N   TRP A 287     1936   1920   1320    -16     24     33       N  
ATOM   2079  CA  TRP A 287      -2.009  -1.819   1.768  1.00 14.01           C  
ANISOU 2079  CA  TRP A 287     1999   1944   1381     -5     23     28       C  
ATOM   2080  C   TRP A 287      -2.643  -0.524   1.273  1.00 13.87           C  
ANISOU 2080  C   TRP A 287     1983   1922   1364      2     21      8       C  
ATOM   2081  O   TRP A 287      -2.020   0.171   0.467  1.00 14.17           O  
ANISOU 2081  O   TRP A 287     2033   1945   1406      9     21      2       O  
ATOM   2082  CB  TRP A 287      -2.424  -3.015   0.976  1.00 13.87           C  
ANISOU 2082  CB  TRP A 287     1986   1912   1371     -7     20     39       C  
ATOM   2083  CG  TRP A 287      -1.529  -4.195   1.217  1.00 14.63           C  
ANISOU 2083  CG  TRP A 287     2082   2004   1471    -12     18     57       C  
ATOM   2084  CD1 TRP A 287      -1.558  -5.073   2.266  1.00 13.42           C  
ANISOU 2084  CD1 TRP A 287     1922   1865   1312    -22     16     72       C  
ATOM   2085  CD2 TRP A 287      -0.366  -4.536   0.447  1.00 13.54           C  
ANISOU 2085  CD2 TRP A 287     1953   1847   1343     -7     18     61       C  
ATOM   2086  NE1 TRP A 287      -0.547  -5.953   2.179  1.00 13.95           N  
ANISOU 2086  NE1 TRP A 287     1992   1920   1386    -22     12     85       N  
ATOM   2087  CE2 TRP A 287       0.204  -5.684   1.059  1.00 13.42           C  
ANISOU 2087  CE2 TRP A 287     1934   1834   1331    -13     14     78       C  
ATOM   2088  CE3 TRP A 287       0.226  -4.013  -0.739  1.00 13.72           C  
ANISOU 2088  CE3 TRP A 287     1988   1852   1373      0     20     52       C  
ATOM   2089  CZ2 TRP A 287       1.385  -6.286   0.595  1.00 13.86           C  
ANISOU 2089  CZ2 TRP A 287     1994   1875   1398    -11     11     84       C  
ATOM   2090  CZ3 TRP A 287       1.367  -4.629  -1.196  1.00 14.19           C  
ANISOU 2090  CZ3 TRP A 287     2052   1899   1442      1     20     57       C  
ATOM   2091  CH2 TRP A 287       1.923  -5.792  -0.547  1.00 14.68           C  
ANISOU 2091  CH2 TRP A 287     2106   1962   1509     -4     15     72       C  
ATOM   2092  N   TYR A 288      -3.837  -0.165   1.790  1.00 15.02           N  
ANISOU 2092  N   TYR A 288     2118   2083   1505      1     21     -3       N  
ATOM   2093  CA  TYR A 288      -4.589   1.021   1.401  1.00 14.64           C  
ANISOU 2093  CA  TYR A 288     2070   2031   1460      9     17    -24       C  
ATOM   2094  C   TYR A 288      -4.394   2.260   2.267  1.00 14.46           C  
ANISOU 2094  C   TYR A 288     2039   2024   1432     10     18    -39       C  
ATOM   2095  O   TYR A 288      -4.298   3.412   1.801  1.00 15.79           O  
ANISOU 2095  O   TYR A 288     2213   2182   1605     19     14    -53       O  
ATOM   2096  CB  TYR A 288      -6.124   0.729   1.378  1.00 14.58           C  
ANISOU 2096  CB  TYR A 288     2053   2030   1456      7     15    -32       C  
ATOM   2097  CG  TYR A 288      -6.853   1.822   0.649  1.00 14.79           C  
ANISOU 2097  CG  TYR A 288     2084   2046   1491     18      7    -52       C  
ATOM   2098  CD1 TYR A 288      -6.687   1.998  -0.697  1.00 15.04           C  
ANISOU 2098  CD1 TYR A 288     2133   2050   1530     26      0    -51       C  
ATOM   2099  CD2 TYR A 288      -7.684   2.730   1.314  1.00 14.50           C  
ANISOU 2099  CD2 TYR A 288     2032   2023   1453     20      5    -73       C  
ATOM   2100  CE1 TYR A 288      -7.323   3.046  -1.361  1.00 13.88           C  
ANISOU 2100  CE1 TYR A 288     1992   1891   1391     35    -11    -68       C  
ATOM   2101  CE2 TYR A 288      -8.354   3.761   0.687  1.00 14.47           C  
ANISOU 2101  CE2 TYR A 288     2032   2008   1460     30     -6    -93       C  
ATOM   2102  CZ  TYR A 288      -8.150   3.964  -0.692  1.00 14.46           C  
ANISOU 2102  CZ  TYR A 288     2050   1977   1466     39    -15    -90       C  
ATOM   2103  OH  TYR A 288      -8.729   5.016  -1.351  1.00 15.78           O  
ANISOU 2103  OH  TYR A 288     2223   2129   1642     49    -28   -107       O  
ATOM   2104  N   LEU A 289      -4.472   2.007   3.584  1.00 15.44           N  
ANISOU 2104  N   LEU A 289     2148   2173   1545      1     24    -37       N  
ATOM   2105  CA  LEU A 289      -4.213   3.045   4.526  1.00 18.12           C  
ANISOU 2105  CA  LEU A 289     2477   2530   1878      0     26    -50       C  
ATOM   2106  C   LEU A 289      -2.695   3.326   4.601  1.00 19.36           C  
ANISOU 2106  C   LEU A 289     2643   2681   2033      2     28    -42       C  
ATOM   2107  O   LEU A 289      -2.264   4.352   4.071  1.00 24.15           O  
ANISOU 2107  O   LEU A 289     3257   3275   2645     11     25    -52       O  
ATOM   2108  CB  LEU A 289      -4.877   2.704   5.877  1.00 18.28           C  
ANISOU 2108  CB  LEU A 289     2479   2580   1885    -12     32    -52       C  
ATOM   2109  CG  LEU A 289      -6.373   2.872   6.198  1.00 18.85           C  
ANISOU 2109  CG  LEU A 289     2536   2668   1958    -15     32    -70       C  
ATOM   2110  CD1 LEU A 289      -6.571   2.641   7.686  1.00 18.53           C  
ANISOU 2110  CD1 LEU A 289     2479   2661   1901    -31     40    -71       C  
ATOM   2111  CD2 LEU A 289      -6.814   4.264   5.894  1.00 18.34           C  
ANISOU 2111  CD2 LEU A 289     2468   2599   1902     -4     27    -97       C  
ATOM   2112  N   ALA A 290      -1.913   2.441   5.235  1.00 20.58           N  
ANISOU 2112  N   ALA A 290     2796   2844   2181     -6     31    -24       N  
ATOM   2113  CA  ALA A 290      -0.504   2.716   5.530  1.00 20.74           C  
ANISOU 2113  CA  ALA A 290     2820   2862   2198     -5     32    -19       C  
ATOM   2114  C   ALA A 290       0.361   2.846   4.315  1.00 20.24           C  
ANISOU 2114  C   ALA A 290     2772   2772   2146      3     31    -17       C  
ATOM   2115  O   ALA A 290       1.364   3.571   4.333  1.00 21.95           O  
ANISOU 2115  O   ALA A 290     2992   2985   2363      6     32    -21       O  
ATOM   2116  CB  ALA A 290       0.097   1.682   6.455  1.00 20.92           C  
ANISOU 2116  CB  ALA A 290     2837   2897   2213    -15     33     -1       C  
ATOM   2117  N   SER A 291      -0.039   2.160   3.243  1.00 23.10           N  
ANISOU 2117  N   SER A 291     3144   3117   2516      5     29    -10       N  
ATOM   2118  CA  SER A 291       0.539   2.319   1.917  1.00 24.67           C  
ANISOU 2118  CA  SER A 291     3359   3290   2725     11     28    -11       C  
ATOM   2119  C   SER A 291       2.008   1.874   1.960  1.00 23.87           C  
ANISOU 2119  C   SER A 291     3261   3184   2625      9     31     -1       C  
ATOM   2120  O   SER A 291       2.822   2.288   1.136  1.00 22.18           O  
ANISOU 2120  O   SER A 291     3057   2954   2416     12     32     -5       O  
ATOM   2121  CB  SER A 291       0.352   3.773   1.407  1.00 25.36           C  
ANISOU 2121  CB  SER A 291     3453   3370   2814     18     25    -29       C  
ATOM   2122  OG  SER A 291      -0.994   4.259   1.608  1.00 26.87           O  
ANISOU 2122  OG  SER A 291     3637   3568   3004     20     21    -41       O  
ATOM   2123  N   GLY A 292       2.320   1.027   2.965  1.00 23.13           N  
ANISOU 2123  N   GLY A 292     3157   3104   2527      3     31     11       N  
ATOM   2124  CA  GLY A 292       3.673   0.515   3.203  1.00 23.62           C  
ANISOU 2124  CA  GLY A 292     3219   3163   2592      1     31     20       C  
ATOM   2125  C   GLY A 292       4.751   1.546   3.461  1.00 22.25           C  
ANISOU 2125  C   GLY A 292     3045   2991   2417      4     34     10       C  
ATOM   2126  O   GLY A 292       5.937   1.274   3.233  1.00 22.45           O  
ANISOU 2126  O   GLY A 292     3074   3008   2449      5     35     13       O  
ATOM   2127  N   ASN A 293       4.361   2.728   3.953  1.00 20.09           N  
ANISOU 2127  N   ASN A 293     2768   2730   2136      6     35     -3       N  
ATOM   2128  CA  ASN A 293       5.325   3.790   4.239  1.00 19.27           C  
ANISOU 2128  CA  ASN A 293     2663   2627   2030      8     38    -14       C  
ATOM   2129  C   ASN A 293       5.772   3.751   5.660  1.00 17.91           C  
ANISOU 2129  C   ASN A 293     2478   2477   1850      4     38    -10       C  
ATOM   2130  O   ASN A 293       5.914   4.849   6.256  1.00 17.91           O  
ANISOU 2130  O   ASN A 293     2473   2489   1844      5     40    -23       O  
ATOM   2131  CB  ASN A 293       4.692   5.160   3.995  1.00 17.71           C  
ANISOU 2131  CB  ASN A 293     2469   2430   1832     12     39    -31       C  
ATOM   2132  CG  ASN A 293       5.701   6.365   3.829  1.00 18.16           C  
ANISOU 2132  CG  ASN A 293     2531   2480   1890     15     41    -43       C  
ATOM   2133  OD1 ASN A 293       6.928   6.245   3.596  1.00 19.37           O  
ANISOU 2133  OD1 ASN A 293     2688   2626   2047     14     45    -41       O  
ATOM   2134  ND2 ASN A 293       5.120   7.531   3.860  1.00 16.95           N  
ANISOU 2134  ND2 ASN A 293     2377   2328   1735     19     39    -57       N  
ATOM   2135  N   GLY A 294       5.966   2.543   6.205  1.00 20.70           N  
ANISOU 2135  N   GLY A 294     2827   2837   2202     -2     34      6       N  
ATOM   2136  CA  GLY A 294       6.523   2.359   7.517  1.00 21.64           C  
ANISOU 2136  CA  GLY A 294     2936   2974   2312     -7     31     12       C  
ATOM   2137  C   GLY A 294       7.351   1.119   7.756  1.00 23.67           C  
ANISOU 2137  C   GLY A 294     3193   3226   2574    -10     25     29       C  
ATOM   2138  O   GLY A 294       7.230   0.105   7.072  1.00 21.59           O  
ANISOU 2138  O   GLY A 294     2935   2949   2320    -10     22     39       O  
ATOM   2139  N   LEU A 295       8.219   1.219   8.749  1.00 23.27           N  
ANISOU 2139  N   LEU A 295     3136   3187   2519    -12     21     31       N  
ATOM   2140  CA  LEU A 295       9.152   0.179   9.066  1.00 24.29           C  
ANISOU 2140  CA  LEU A 295     3263   3311   2654    -14     12     45       C  
ATOM   2141  C   LEU A 295       8.433  -1.174   9.366  1.00 25.06           C  
ANISOU 2141  C   LEU A 295     3362   3410   2749    -22      4     65       C  
ATOM   2142  O   LEU A 295       8.780  -2.219   8.822  1.00 25.51           O  
ANISOU 2142  O   LEU A 295     3423   3451   2819    -21     -3     76       O  
ATOM   2143  CB  LEU A 295      10.045   0.667  10.219  1.00 23.14           C  
ANISOU 2143  CB  LEU A 295     3110   3180   2500    -16      9     43       C  
ATOM   2144  CG  LEU A 295      11.209   1.654   9.865  1.00 21.27           C  
ANISOU 2144  CG  LEU A 295     2873   2936   2272     -8     14     26       C  
ATOM   2145  CD1 LEU A 295      12.055   2.140  11.024  1.00 19.68           C  
ANISOU 2145  CD1 LEU A 295     2664   2751   2063     -9     10     23       C  
ATOM   2146  CD2 LEU A 295      12.163   1.102   8.818  1.00 18.57           C  
ANISOU 2146  CD2 LEU A 295     2536   2570   1950     -2     13     25       C  
ATOM   2147  N   GLU A 296       7.402  -1.130  10.205  1.00 27.37           N  
ANISOU 2147  N   GLU A 296     3650   3724   3025    -32      4     69       N  
ATOM   2148  CA  GLU A 296       6.656  -2.332  10.575  1.00 27.90           C  
ANISOU 2148  CA  GLU A 296     3719   3796   3087    -42     -2     88       C  
ATOM   2149  C   GLU A 296       5.676  -2.774   9.487  1.00 25.93           C  
ANISOU 2149  C   GLU A 296     3474   3532   2845    -40      1     89       C  
ATOM   2150  O   GLU A 296       5.716  -3.955   9.083  1.00 26.63           O  
ANISOU 2150  O   GLU A 296     3567   3606   2944    -41     -6    103       O  
ATOM   2151  CB  GLU A 296       5.942  -2.115  11.903  1.00 31.06           C  
ANISOU 2151  CB  GLU A 296     4112   4225   3465    -56     -2     91       C  
ATOM   2152  CG  GLU A 296       6.966  -1.765  12.974  1.00 32.99           C  
ANISOU 2152  CG  GLU A 296     4352   4482   3700    -58     -7     92       C  
ATOM   2153  CD  GLU A 296       6.388  -1.642  14.350  1.00 36.47           C  
ANISOU 2153  CD  GLU A 296     4788   4954   4118    -74     -7     95       C  
ATOM   2154  OE1 GLU A 296       5.163  -1.398  14.463  1.00 42.73           O  
ANISOU 2154  OE1 GLU A 296     5576   5761   4900    -81      1     89       O  
ATOM   2155  OE2 GLU A 296       7.176  -1.787  15.300  1.00 34.65           O  
ANISOU 2155  OE2 GLU A 296     4555   4732   3878    -79    -16    104       O  
ATOM   2156  N   SER A 297       4.847  -1.839   9.007  1.00 25.27           N  
ANISOU 2156  N   SER A 297     3390   3451   2759    -36     11     72       N  
ATOM   2157  CA  SER A 297       3.887  -2.101   7.915  1.00 24.65           C  
ANISOU 2157  CA  SER A 297     3317   3360   2689    -33     15     70       C  
ATOM   2158  C   SER A 297       4.587  -2.847   6.772  1.00 21.59           C  
ANISOU 2158  C   SER A 297     2938   2945   2320    -25     11     76       C  
ATOM   2159  O   SER A 297       4.259  -4.007   6.463  1.00 21.35           O  
ANISOU 2159  O   SER A 297     2910   2905   2295    -29      6     89       O  
ATOM   2160  CB  SER A 297       3.179  -0.813   7.392  1.00 22.30           C  
ANISOU 2160  CB  SER A 297     3019   3064   2390    -26     23     48       C  
ATOM   2161  OG  SER A 297       4.018   0.170   6.774  1.00 24.25           O  
ANISOU 2161  OG  SER A 297     3271   3299   2644    -16     26     35       O  
ATOM   2162  N   LEU A 298       5.636  -2.220   6.224  1.00 21.24           N  
ANISOU 2162  N   LEU A 298     2896   2889   2284    -17     14     65       N  
ATOM   2163  CA  LEU A 298       6.319  -2.752   5.083  1.00 18.80           C  
ANISOU 2163  CA  LEU A 298     2595   2557   1993    -11     13     66       C  
ATOM   2164  C   LEU A 298       6.809  -4.158   5.373  1.00 17.48           C  
ANISOU 2164  C   LEU A 298     2426   2383   1833    -14      3     83       C  
ATOM   2165  O   LEU A 298       6.647  -5.015   4.529  1.00 18.66           O  
ANISOU 2165  O   LEU A 298     2579   2516   1995    -13      0     88       O  
ATOM   2166  CB  LEU A 298       7.490  -1.862   4.599  1.00 18.36           C  
ANISOU 2166  CB  LEU A 298     2542   2492   1943     -4     18     51       C  
ATOM   2167  CG  LEU A 298       8.122  -2.275   3.242  1.00 18.17           C  
ANISOU 2167  CG  LEU A 298     2525   2444   1936      0     21     47       C  
ATOM   2168  CD1 LEU A 298       7.129  -2.508   2.113  1.00 17.40           C  
ANISOU 2168  CD1 LEU A 298     2436   2334   1841      1     24     46       C  
ATOM   2169  CD2 LEU A 298       9.116  -1.216   2.776  1.00 18.24           C  
ANISOU 2169  CD2 LEU A 298     2536   2446   1946      4     28     30       C  
ATOM   2170  N   LYS A 299       7.500  -4.380   6.527  1.00 16.53           N  
ANISOU 2170  N   LYS A 299     2300   2274   1709    -19     -5     92       N  
ATOM   2171  CA  LYS A 299       8.034  -5.704   6.821  1.00 18.10           C  
ANISOU 2171  CA  LYS A 299     2497   2463   1916    -22    -19    109       C  
ATOM   2172  C   LYS A 299       6.871  -6.700   6.933  1.00 18.59           C  
ANISOU 2172  C   LYS A 299     2561   2527   1974    -30    -24    124       C  
ATOM   2173  O   LYS A 299       6.925  -7.769   6.356  1.00 18.70           O  
ANISOU 2173  O   LYS A 299     2577   2523   2003    -29    -31    133       O  
ATOM   2174  CB  LYS A 299       8.855  -5.680   8.115  1.00 17.20           C  
ANISOU 2174  CB  LYS A 299     2377   2362   1795    -26    -29    115       C  
ATOM   2175  CG  LYS A 299       9.378  -7.034   8.451  1.00 18.31           C  
ANISOU 2175  CG  LYS A 299     2518   2492   1947    -29    -46    133       C  
ATOM   2176  CD  LYS A 299      10.557  -6.971   9.410  1.00 19.71           C  
ANISOU 2176  CD  LYS A 299     2690   2674   2124    -29    -58    136       C  
ATOM   2177  CE  LYS A 299      10.912  -8.372   9.815  1.00 19.84           C  
ANISOU 2177  CE  LYS A 299     2707   2679   2151    -33    -79    156       C  
ATOM   2178  NZ  LYS A 299      12.227  -8.469  10.459  1.00 19.89           N  
ANISOU 2178  NZ  LYS A 299     2709   2682   2165    -29    -93    157       N  
ATOM   2179  N   THR A 300       5.833  -6.316   7.692  1.00 19.66           N  
ANISOU 2179  N   THR A 300     2695   2685   2092    -39    -20    126       N  
ATOM   2180  CA  THR A 300       4.545  -7.043   7.747  1.00 21.81           C  
ANISOU 2180  CA  THR A 300     2969   2961   2358    -48    -20    137       C  
ATOM   2181  C   THR A 300       4.071  -7.454   6.334  1.00 19.95           C  
ANISOU 2181  C   THR A 300     2738   2704   2137    -41    -17    133       C  
ATOM   2182  O   THR A 300       3.880  -8.673   6.036  1.00 20.10           O  
ANISOU 2182  O   THR A 300     2759   2711   2166    -44    -25    147       O  
ATOM   2183  CB  THR A 300       3.420  -6.230   8.454  1.00 25.43           C  
ANISOU 2183  CB  THR A 300     3422   3445   2795    -56    -11    130       C  
ATOM   2184  OG1 THR A 300       3.810  -5.761   9.778  1.00 26.67           O  
ANISOU 2184  OG1 THR A 300     3574   3624   2936    -64    -13    131       O  
ATOM   2185  CG2 THR A 300       2.133  -7.095   8.577  1.00 27.79           C  
ANISOU 2185  CG2 THR A 300     3722   3751   3089    -68    -12    141       C  
ATOM   2186  N   MET A 301       3.992  -6.422   5.474  1.00 16.16           N  
ANISOU 2186  N   MET A 301     2261   2221   1661    -32     -6    114       N  
ATOM   2187  CA  MET A 301       3.537  -6.539   4.046  1.00 14.56           C  
ANISOU 2187  CA  MET A 301     2064   1999   1469    -24     -1    107       C  
ATOM   2188  C   MET A 301       4.325  -7.468   3.160  1.00 14.72           C  
ANISOU 2188  C   MET A 301     2089   1996   1510    -19     -6    111       C  
ATOM   2189  O   MET A 301       3.737  -8.311   2.488  1.00 15.82           O  
ANISOU 2189  O   MET A 301     2230   2123   1657    -20     -8    117       O  
ATOM   2190  CB  MET A 301       3.434  -5.147   3.390  1.00 15.51           C  
ANISOU 2190  CB  MET A 301     2187   2118   1587    -17      9     87       C  
ATOM   2191  CG  MET A 301       2.243  -4.325   3.834  1.00 15.64           C  
ANISOU 2191  CG  MET A 301     2201   2153   1590    -20     14     78       C  
ATOM   2192  SD  MET A 301       2.442  -2.556   3.602  1.00 18.63           S  
ANISOU 2192  SD  MET A 301     2581   2535   1964    -12     21     56       S  
ATOM   2193  CE  MET A 301       1.904  -2.411   1.891  1.00 18.08           C  
ANISOU 2193  CE  MET A 301     2523   2441   1905     -4     23     47       C  
ATOM   2194  N   ILE A 302       5.638  -7.351   3.177  1.00 14.60           N  
ANISOU 2194  N   ILE A 302     2071   1973   1502    -15     -9    107       N  
ATOM   2195  CA  ILE A 302       6.486  -8.252   2.467  1.00 15.50           C  
ANISOU 2195  CA  ILE A 302     2187   2068   1636    -11    -14    109       C  
ATOM   2196  C   ILE A 302       6.223  -9.748   2.888  1.00 16.21           C  
ANISOU 2196  C   ILE A 302     2274   2152   1733    -17    -28    129       C  
ATOM   2197  O   ILE A 302       6.124 -10.655   2.051  1.00 17.50           O  
ANISOU 2197  O   ILE A 302     2440   2298   1912    -14    -31    132       O  
ATOM   2198  CB  ILE A 302       7.967  -7.849   2.681  1.00 15.69           C  
ANISOU 2198  CB  ILE A 302     2207   2089   1667     -6    -15    101       C  
ATOM   2199  CG1 ILE A 302       8.340  -6.485   2.066  1.00 16.40           C  
ANISOU 2199  CG1 ILE A 302     2301   2179   1753     -1     -2     80       C  
ATOM   2200  CG2 ILE A 302       8.939  -8.914   2.285  1.00 15.61           C  
ANISOU 2200  CG2 ILE A 302     2193   2060   1678     -3    -25    103       C  
ATOM   2201  CD1 ILE A 302       9.258  -5.725   3.028  1.00 17.25           C  
ANISOU 2201  CD1 ILE A 302     2402   2299   1854     -1     -2     76       C  
ATOM   2202  N   LEU A 303       6.159 -10.031   4.196  1.00 18.20           N  
ANISOU 2202  N   LEU A 303     2523   2418   1974    -25    -37    144       N  
ATOM   2203  CA  LEU A 303       5.905 -11.385   4.664  1.00 19.97           C  
ANISOU 2203  CA  LEU A 303     2747   2638   2204    -32    -52    165       C  
ATOM   2204  C   LEU A 303       4.549 -11.919   4.163  1.00 17.91           C  
ANISOU 2204  C   LEU A 303     2490   2375   1941    -37    -48    170       C  
ATOM   2205  O   LEU A 303       4.399 -13.109   3.834  1.00 18.50           O  
ANISOU 2205  O   LEU A 303     2565   2434   2028    -39    -58    181       O  
ATOM   2206  CB  LEU A 303       5.917 -11.406   6.201  1.00 20.51           C  
ANISOU 2206  CB  LEU A 303     2814   2725   2255    -44    -61    180       C  
ATOM   2207  CG  LEU A 303       7.187 -10.835   6.845  1.00 22.11           C  
ANISOU 2207  CG  LEU A 303     3012   2932   2457    -40    -65    175       C  
ATOM   2208  CD1 LEU A 303       7.533 -11.525   8.151  1.00 22.56           C  
ANISOU 2208  CD1 LEU A 303     3069   2996   2508    -50    -84    195       C  
ATOM   2209  CD2 LEU A 303       8.401 -10.856   5.898  1.00 21.56           C  
ANISOU 2209  CD2 LEU A 303     2940   2841   2411    -26    -66    161       C  
ATOM   2210  N   GLU A 304       3.557 -11.024   4.147  1.00 17.57           N  
ANISOU 2210  N   GLU A 304     2447   2347   1882    -39    -36    161       N  
ATOM   2211  CA  GLU A 304       2.217 -11.362   3.661  1.00 16.73           C  
ANISOU 2211  CA  GLU A 304     2343   2241   1774    -43    -31    163       C  
ATOM   2212  C   GLU A 304       2.251 -11.871   2.217  1.00 16.26           C  
ANISOU 2212  C   GLU A 304     2287   2158   1733    -34    -30    157       C  
ATOM   2213  O   GLU A 304       1.742 -12.951   1.926  1.00 16.04           O  
ANISOU 2213  O   GLU A 304     2260   2120   1714    -38    -36    167       O  
ATOM   2214  CB  GLU A 304       1.284 -10.172   3.776  1.00 16.40           C  
ANISOU 2214  CB  GLU A 304     2299   2217   1715    -44    -18    149       C  
ATOM   2215  CG  GLU A 304      -0.167 -10.439   3.549  1.00 17.94           C  
ANISOU 2215  CG  GLU A 304     2494   2416   1905    -49    -14    150       C  
ATOM   2216  CD  GLU A 304      -1.088  -9.265   3.821  1.00 18.14           C  
ANISOU 2216  CD  GLU A 304     2516   2462   1917    -51     -4    134       C  
ATOM   2217  OE1 GLU A 304      -0.657  -8.090   3.924  1.00 19.32           O  
ANISOU 2217  OE1 GLU A 304     2663   2616   2059    -44      1    121       O  
ATOM   2218  OE2 GLU A 304      -2.289  -9.534   3.965  1.00 22.85           O  
ANISOU 2218  OE2 GLU A 304     3108   3066   2506    -58     -2    135       O  
ATOM   2219  N   ILE A 305       2.906 -11.151   1.333  1.00 16.24           N  
ANISOU 2219  N   ILE A 305     2287   2146   1738    -24    -23    140       N  
ATOM   2220  CA  ILE A 305       3.128 -11.717   0.011  1.00 15.88           C  
ANISOU 2220  CA  ILE A 305     2245   2078   1710    -17    -22    134       C  
ATOM   2221  C   ILE A 305       3.916 -13.005  -0.010  1.00 17.38           C  
ANISOU 2221  C   ILE A 305     2433   2253   1920    -17    -35    144       C  
ATOM   2222  O   ILE A 305       3.559 -13.944  -0.770  1.00 18.24           O  
ANISOU 2222  O   ILE A 305     2542   2346   2041    -16    -38    147       O  
ATOM   2223  CB  ILE A 305       3.822 -10.733  -0.934  1.00 15.19           C  
ANISOU 2223  CB  ILE A 305     2162   1983   1626     -9    -12    114       C  
ATOM   2224  CG1 ILE A 305       3.070  -9.455  -0.869  1.00 14.36           C  
ANISOU 2224  CG1 ILE A 305     2061   1892   1504     -9     -3    105       C  
ATOM   2225  CG2 ILE A 305       3.962 -11.379  -2.318  1.00 15.16           C  
ANISOU 2225  CG2 ILE A 305     2163   1959   1639     -4    -11    108       C  
ATOM   2226  CD1 ILE A 305       1.696  -9.571  -1.446  1.00 13.74           C  
ANISOU 2226  CD1 ILE A 305     1986   1812   1422    -10      0    104       C  
ATOM   2227  N   LYS A 306       5.011 -13.091   0.708  1.00 18.70           N  
ANISOU 2227  N   LYS A 306     2595   2420   2090    -17    -43    148       N  
ATOM   2228  CA  LYS A 306       5.823 -14.352   0.611  1.00 22.83           C  
ANISOU 2228  CA  LYS A 306     3114   2924   2636    -15    -58    155       C  
ATOM   2229  C   LYS A 306       4.987 -15.569   1.017  1.00 24.30           C  
ANISOU 2229  C   LYS A 306     3301   3107   2825    -23    -70    176       C  
ATOM   2230  O   LYS A 306       4.964 -16.589   0.340  1.00 25.77           O  
ANISOU 2230  O   LYS A 306     3486   3275   3029    -21    -76    178       O  
ATOM   2231  CB  LYS A 306       7.097 -14.255   1.468  1.00 25.77           C  
ANISOU 2231  CB  LYS A 306     3481   3298   3012    -13    -67    157       C  
ATOM   2232  CG  LYS A 306       7.588 -15.601   2.021  1.00 28.91           C  
ANISOU 2232  CG  LYS A 306     3874   3683   3426    -15    -89    173       C  
ATOM   2233  CD  LYS A 306       8.922 -15.445   2.723  1.00 30.75           C  
ANISOU 2233  CD  LYS A 306     4103   3916   3667    -12   -100    171       C  
ATOM   2234  CE  LYS A 306       8.790 -14.746   4.078  1.00 31.80           C  
ANISOU 2234  CE  LYS A 306     4236   4071   3774    -20   -101    181       C  
ATOM   2235  NZ  LYS A 306      10.069 -14.072   4.444  1.00 34.39           N  
ANISOU 2235  NZ  LYS A 306     4559   4402   4106    -13   -103    170       N  
ATOM   2236  N   ASN A 307       4.291 -15.413   2.126  1.00 26.34           N  
ANISOU 2236  N   ASN A 307     3561   3384   3063    -33    -72    190       N  
ATOM   2237  CA  ASN A 307       3.451 -16.444   2.710  1.00 29.80           C  
ANISOU 2237  CA  ASN A 307     4000   3823   3498    -45    -82    211       C  
ATOM   2238  C   ASN A 307       2.339 -16.830   1.742  1.00 27.62           C  
ANISOU 2238  C   ASN A 307     3727   3541   3227    -45    -75    208       C  
ATOM   2239  O   ASN A 307       1.863 -17.983   1.726  1.00 27.72           O  
ANISOU 2239  O   ASN A 307     3740   3543   3248    -51    -85    222       O  
ATOM   2240  CB  ASN A 307       2.831 -15.913   3.990  1.00 28.63           C  
ANISOU 2240  CB  ASN A 307     3853   3701   3323    -58    -80    220       C  
ATOM   2241  CG  ASN A 307       3.708 -16.128   5.228  1.00 31.38           C  
ANISOU 2241  CG  ASN A 307     4201   4055   3667    -64    -95    235       C  
ATOM   2242  OD1 ASN A 307       4.943 -16.251   5.165  1.00 32.25           O  
ANISOU 2242  OD1 ASN A 307     4308   4152   3792    -56   -105    231       O  
ATOM   2243  ND2 ASN A 307       3.052 -16.219   6.365  1.00 35.13           N  
ANISOU 2243  ND2 ASN A 307     4678   4549   4121    -80    -98    250       N  
ATOM   2244  N   ALA A 308       1.921 -15.833   0.967  1.00 28.82           N  
ANISOU 2244  N   ALA A 308     3881   3698   3373    -39    -59    189       N  
ATOM   2245  CA  ALA A 308       0.900 -15.987  -0.057  1.00 28.98           C  
ANISOU 2245  CA  ALA A 308     3903   3711   3396    -37    -51    183       C  
ATOM   2246  C   ALA A 308       1.358 -16.846  -1.223  1.00 29.12           C  
ANISOU 2246  C   ALA A 308     3922   3705   3438    -29    -55    178       C  
ATOM   2247  O   ALA A 308       0.587 -17.715  -1.630  1.00 33.13           O  
ANISOU 2247  O   ALA A 308     4430   4204   3953    -32    -58    184       O  
ATOM   2248  CB  ALA A 308       0.402 -14.623  -0.553  1.00 28.90           C  
ANISOU 2248  CB  ALA A 308     3896   3713   3373    -31    -35    164       C  
ATOM   2249  N   VAL A 309       2.576 -16.630  -1.756  1.00 27.36           N  
ANISOU 2249  N   VAL A 309     3697   3471   3227    -20    -55    166       N  
ATOM   2250  CA  VAL A 309       2.969 -17.215  -3.054  1.00 27.54           C  
ANISOU 2250  CA  VAL A 309     3720   3473   3272    -13    -54    154       C  
ATOM   2251  C   VAL A 309       3.993 -18.356  -2.939  1.00 29.04           C  
ANISOU 2251  C   VAL A 309     3904   3646   3486    -10    -70    160       C  
ATOM   2252  O   VAL A 309       4.316 -19.004  -3.958  1.00 31.12           O  
ANISOU 2252  O   VAL A 309     4165   3891   3769     -5    -71    150       O  
ATOM   2253  CB  VAL A 309       3.529 -16.150  -4.063  1.00 24.40           C  
ANISOU 2253  CB  VAL A 309     3325   3073   2872     -5    -39    131       C  
ATOM   2254  CG1 VAL A 309       2.609 -14.945  -4.272  1.00 23.07           C  
ANISOU 2254  CG1 VAL A 309     3164   2918   2682     -6    -26    124       C  
ATOM   2255  CG2 VAL A 309       4.923 -15.683  -3.687  1.00 24.68           C  
ANISOU 2255  CG2 VAL A 309     3357   3109   2911     -2    -40    124       C  
ATOM   2256  N   LYS A 310       4.536 -18.610  -1.741  1.00 24.36           N  
ANISOU 2256  N   LYS A 310     3307   3057   2892    -14    -83    174       N  
ATOM   2257  CA  LYS A 310       5.518 -19.714  -1.587  1.00 26.77           C  
ANISOU 2257  CA  LYS A 310     3606   3344   3222    -11   -102    179       C  
ATOM   2258  C   LYS A 310       4.844 -21.064  -1.763  1.00 24.81           C  
ANISOU 2258  C   LYS A 310     3358   3081   2988    -16   -114    193       C  
ATOM   2259  O   LYS A 310       3.644 -21.185  -1.549  1.00 24.82           O  
ANISOU 2259  O   LYS A 310     3364   3091   2975    -24   -111    205       O  
ATOM   2260  CB  LYS A 310       6.177 -19.691  -0.218  1.00 26.10           C  
ANISOU 2260  CB  LYS A 310     3520   3266   3132    -15   -116    193       C  
ATOM   2261  CG  LYS A 310       5.191 -19.724   0.923  1.00 27.22           C  
ANISOU 2261  CG  LYS A 310     3667   3425   3251    -29   -120    215       C  
ATOM   2262  CD  LYS A 310       5.692 -20.577   2.071  1.00 27.58           C  
ANISOU 2262  CD  LYS A 310     3712   3466   3302    -36   -144    237       C  
ATOM   2263  CE  LYS A 310       4.744 -20.457   3.239  1.00 29.95           C  
ANISOU 2263  CE  LYS A 310     4019   3786   3575    -52   -145    257       C  
ATOM   2264  NZ  LYS A 310       5.104 -19.281   4.078  1.00 30.33           N  
ANISOU 2264  NZ  LYS A 310     4067   3857   3601    -54   -138    253       N  
TER    2265      LYS A 310                                                      
HETATM 2266 FE    FE A1311      -8.437   6.828  -1.293  1.00 17.35          FE3+
HETATM 2267  C1  LCM A1312      -9.440   7.248   2.829  1.00 18.67           C  
HETATM 2268  C2  LCM A1312      -9.367   7.137   1.440  1.00 18.78           C  
HETATM 2269  C3  LCM A1312     -10.426   7.678   0.650  1.00 22.01           C  
HETATM 2270  C4  LCM A1312     -11.637   8.218   1.295  1.00 21.35           C  
HETATM 2271  C5  LCM A1312     -11.701   8.240   2.714  1.00 19.25           C  
HETATM 2272  C6  LCM A1312     -10.599   7.780   3.428  1.00 20.87           C  
HETATM 2273  C7  LCM A1312     -12.656   8.821   0.396  1.00 24.75           C  
HETATM 2274  N8  LCM A1312     -12.195   9.024  -0.862  1.00 22.53           N  
HETATM 2275  O9  LCM A1312     -13.642   9.385   0.878  1.00 27.23           O  
HETATM 2276  C10 LCM A1312     -12.448  10.187  -1.688  1.00 24.50           C  
HETATM 2277  C11 LCM A1312     -11.504  11.276  -1.059  1.00 22.78           C  
HETATM 2278  C12 LCM A1312     -11.098  12.379  -2.025  1.00 20.73           C  
HETATM 2279  C13 LCM A1312      -9.598  12.647  -2.144  1.00 18.92           C  
HETATM 2280  N14 LCM A1312      -8.715  11.473  -2.073  1.00 16.08           N  
HETATM 2281  C15 LCM A1312      -7.369  11.569  -2.310  1.00 14.57           C  
HETATM 2282  C16 LCM A1312      -6.396  10.406  -2.196  1.00 14.45           C  
HETATM 2283  O17 LCM A1312      -6.912  12.643  -2.651  1.00 16.92           O  
HETATM 2284  C18 LCM A1312      -6.911   9.030  -1.882  1.00 13.44           C  
HETATM 2285  C19 LCM A1312      -5.952   7.944  -1.746  1.00 13.03           C  
HETATM 2286  C20 LCM A1312      -4.581   8.222  -1.933  1.00 12.85           C  
HETATM 2287  C21 LCM A1312      -4.121   9.477  -2.248  1.00 16.00           C  
HETATM 2288  C22 LCM A1312      -5.007  10.557  -2.395  1.00 13.89           C  
HETATM 2289  O23 LCM A1312      -8.236   8.744  -1.528  1.00 16.35           O  
HETATM 2290  O24 LCM A1312      -6.589   6.777  -1.475  1.00 17.77           O  
HETATM 2291  O25 LCM A1312     -10.333   7.567  -0.675  1.00 18.03           O  
HETATM 2292  O26 LCM A1312      -8.256   6.743   0.868  1.00 15.05           O  
HETATM 2293  O   HOH A2001      11.866   9.416  -5.870  1.00 33.08           O  
HETATM 2294  O   HOH A2002      17.131  13.719   4.164  1.00 19.70           O  
HETATM 2295  O   HOH A2003      23.746  18.713   7.127  1.00 21.82           O  
HETATM 2296  O   HOH A2004      19.469  27.431  13.980  1.00 17.11           O  
HETATM 2297  O   HOH A2005      11.954  29.865   2.280  1.00 27.27           O  
HETATM 2298  O   HOH A2006       7.466  26.060   8.477  1.00 35.03           O  
HETATM 2299  O   HOH A2007      -2.434   9.735   4.894  1.00 18.32           O  
HETATM 2300  O   HOH A2008      -1.652   6.974   5.820  1.00 18.80           O  
HETATM 2301  O   HOH A2009       8.262   5.879   7.236  1.00 19.74           O  
HETATM 2302  O   HOH A2010      13.797  11.732  24.320  1.00 20.38           O  
HETATM 2303  O   HOH A2011      -1.756   6.857  -4.551  1.00 18.96           O  
HETATM 2304  O   HOH A2012     -10.458   9.942   6.891  1.00 26.25           O  
HETATM 2305  O   HOH A2013      -0.394  -3.338  17.885  1.00 22.10           O  
HETATM 2306  O   HOH A2014      -6.054   6.974  19.363  1.00 22.09           O  
HETATM 2307  O   HOH A2015      -7.283   7.519  21.498  1.00 30.01           O  
HETATM 2308  O   HOH A2016      -9.376  15.008  20.034  1.00 18.28           O  
HETATM 2309  O   HOH A2017       3.175   5.623 -13.444  1.00 33.37           O  
HETATM 2310  O   HOH A2018     -10.914  18.084   6.673  1.00 30.08           O  
HETATM 2311  O   HOH A2019     -14.853  -2.204 -17.539  1.00 26.53           O  
HETATM 2312  O   HOH A2020      -3.056  23.660  22.975  1.00 39.47           O  
HETATM 2313  O   HOH A2021       1.737  24.001  17.961  1.00 23.74           O  
HETATM 2314  O   HOH A2022     -10.320  -8.010   3.197  1.00 19.61           O  
HETATM 2315  O   HOH A2023       1.701   9.536  -0.546  1.00 18.11           O  
HETATM 2316  O   HOH A2024      -1.308   7.405   1.778  1.00 23.23           O  
HETATM 2317  O   HOH A2025      -3.880  24.360   0.429  1.00 25.78           O  
HETATM 2318  O   HOH A2026       6.703   0.392  -6.872  1.00 25.46           O  
HETATM 2319  O   HOH A2027      -0.995   6.303  -7.157  1.00 21.02           O  
HETATM 2320  O   HOH A2028      13.382   2.862  -5.700  1.00 20.08           O  
HETATM 2321  O   HOH A2029      11.508   0.547  -5.648  1.00 20.52           O  
HETATM 2322  O   HOH A2030       9.222   1.050  -7.316  1.00 19.31           O  
HETATM 2323  O   HOH A2031      16.961   6.797  -0.779  1.00 25.29           O  
HETATM 2324  O   HOH A2032      17.857   9.997   2.695  1.00 21.25           O  
HETATM 2325  O   HOH A2033      22.241   6.752  14.855  1.00 30.48           O  
HETATM 2326  O   HOH A2034      23.118   0.510  10.617  1.00 20.88           O  
HETATM 2327  O   HOH A2035      16.772  -5.980  -1.059  1.00 33.71           O  
HETATM 2328  O   HOH A2036      13.593  -5.457  -5.463  1.00 24.61           O  
HETATM 2329  O   HOH A2037       5.386 -17.295  -7.064  1.00 24.94           O  
HETATM 2330  O   HOH A2038       6.389 -13.677 -11.411  1.00 21.92           O  
HETATM 2331  O   HOH A2039       7.426 -16.206 -17.502  1.00 27.39           O  
HETATM 2332  O   HOH A2040       1.849 -21.129 -15.012  1.00 28.95           O  
HETATM 2333  O   HOH A2041       6.943 -23.676 -14.800  1.00 30.70           O  
HETATM 2334  O   HOH A2042      -1.404 -21.323 -11.624  1.00 30.40           O  
HETATM 2335  O   HOH A2043      -1.207  -6.773 -14.180  1.00 16.56           O  
HETATM 2336  O   HOH A2044      -1.519  -6.317 -11.475  1.00  9.88           O  
HETATM 2337  O   HOH A2045     -12.844  -0.580  -7.610  1.00 17.45           O  
HETATM 2338  O   HOH A2046     -17.158  -5.523  -2.510  1.00 26.46           O  
HETATM 2339  O   HOH A2047     -16.383  -4.039 -11.556  1.00 21.50           O  
HETATM 2340  O   HOH A2048     -15.525  -0.939 -12.159  1.00 19.27           O  
HETATM 2341  O   HOH A2049      -4.277   1.795 -12.079  1.00 12.27           O  
HETATM 2342  O   HOH A2050      -1.827   0.547 -12.091  1.00 19.05           O  
HETATM 2343  O   HOH A2051       3.489   5.886 -11.321  1.00 28.20           O  
HETATM 2344  O   HOH A2052       4.638   1.350  -5.273  1.00 19.55           O  
HETATM 2345  O   HOH A2053      -2.040   3.698  -7.999  1.00 14.70           O  
HETATM 2346  O   HOH A2054       3.310  -0.321  -3.273  1.00 23.20           O  
HETATM 2347  O   HOH A2055       2.504   2.948  -1.927  1.00 19.83           O  
HETATM 2348  O   HOH A2056      -2.118   2.546  -0.841  1.00 15.91           O  
HETATM 2349  O   HOH A2057       9.145  -8.146 -13.748  1.00 26.54           O  
HETATM 2350  O   HOH A2058       6.300  -7.154 -13.749  1.00 24.72           O  
HETATM 2351  O   HOH A2059       0.945  -6.990 -20.726  1.00 31.53           O  
HETATM 2352  O   HOH A2060       1.445  -0.030 -16.745  1.00 26.38           O  
HETATM 2353  O   HOH A2061      -3.096  -1.370 -22.037  1.00 21.37           O  
HETATM 2354  O   HOH A2062      -5.501   0.891 -18.113  1.00 20.32           O  
HETATM 2355  O   HOH A2063      -5.069   9.158 -10.977  1.00 16.77           O  
HETATM 2356  O   HOH A2064      -5.661  11.549  -8.045  1.00 18.56           O  
HETATM 2357  O   HOH A2065      -7.832   5.836 -11.741  1.00 16.88           O  
HETATM 2358  O   HOH A2066      -7.662   7.352 -17.178  1.00 20.01           O  
HETATM 2359  O   HOH A2067     -16.165  -2.536 -15.459  1.00 30.00           O  
HETATM 2360  O   HOH A2068     -12.994  -4.723 -18.059  1.00 20.37           O  
HETATM 2361  O   HOH A2069     -17.998  -8.972 -15.205  1.00 27.37           O  
HETATM 2362  O   HOH A2070     -13.001  -8.428 -21.286  1.00 24.38           O  
HETATM 2363  O   HOH A2071      -1.926 -20.345  -9.221  1.00 18.91           O  
HETATM 2364  O   HOH A2072      -8.560  -7.097   1.148  1.00 19.36           O  
HETATM 2365  O   HOH A2073     -12.832  -8.371   2.331  1.00 21.49           O  
HETATM 2366  O   HOH A2074     -26.749  -8.406   6.615  1.00 33.10           O  
HETATM 2367  O   HOH A2075     -11.678 -14.968   2.714  1.00 25.06           O  
HETATM 2368  O   HOH A2076      -8.207 -18.274  -3.006  1.00 22.34           O  
HETATM 2369  O   HOH A2077      -0.757 -13.261   3.000  1.00 30.63           O  
HETATM 2370  O   HOH A2078       5.854 -23.097  -2.216  1.00 33.18           O  
CONECT 1606 2266                                                                
CONECT 2103 2266                                                                
CONECT 2266 1606 2103 2289 2290                                                 
CONECT 2266 2291 2292                                                           
CONECT 2267 2268 2272                                                           
CONECT 2268 2267 2269 2292                                                      
CONECT 2269 2268 2270 2291                                                      
CONECT 2270 2269 2271 2273                                                      
CONECT 2271 2270 2272                                                           
CONECT 2272 2267 2271                                                           
CONECT 2273 2270 2274 2275                                                      
CONECT 2274 2273 2276                                                           
CONECT 2275 2273                                                                
CONECT 2276 2274 2277                                                           
CONECT 2277 2276 2278                                                           
CONECT 2278 2277 2279                                                           
CONECT 2279 2278 2280                                                           
CONECT 2280 2279 2281                                                           
CONECT 2281 2280 2282 2283                                                      
CONECT 2282 2281 2284 2288                                                      
CONECT 2283 2281                                                                
CONECT 2284 2282 2285 2289                                                      
CONECT 2285 2284 2286 2290                                                      
CONECT 2286 2285 2287                                                           
CONECT 2287 2286 2288                                                           
CONECT 2288 2282 2287                                                           
CONECT 2289 2266 2284                                                           
CONECT 2290 2266 2285                                                           
CONECT 2291 2266 2269                                                           
CONECT 2292 2266 2268                                                           
MASTER      345    0    2   17   18    0    4    6 2369    1   30   23          
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.