CNRS Nantes University US2B US2B
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***  HYDROLASE 14-JUN-24 8ZXG  ***

elNémo ID: 24071808113545719

Job options:

ID        	=	 24071808113545719
JOBID     	=	 HYDROLASE 14-JUN-24 8ZXG
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    HYDROLASE                               14-JUN-24   8ZXG              
TITLE     CRYSTAL STRUCTURE OF PARAOXONASE FROM BACILLUS SP. STRAIN S3WAHI      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PARAOXONASE FROM BACILLUS SP. STRAIN S3WAHI;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SP. (IN: FIRMICUTES);                  
SOURCE   3 ORGANISM_TAXID: 1409;                                                
SOURCE   4 STRAIN: S3WAHI;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    STRUCTURAL PROTEIN, HYDROLASE, METALLO-B-LACTAMASES, ENZYME           
KEYWDS   2 PROMISCUITY, FUNCTION, METALLOHYDROLASE, PARAOXONASE,                
KEYWDS   3 OGRANOPHOSPHATE-DEGRADING ENZYME                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.AZMAN,N.D.MUHD NOOR,A.T.C.LEOW,S.A.MOHD NOOR,M.S.MOHAMAD ALI      
JRNL        AUTH   A.A.AZMAN,N.D.MUHD NOOR,A.T.C.LEOW,S.A.MOHD NOOR,            
JRNL        AUTH 2 M.S.MOHAMAD ALI                                              
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF PARAOXONASE FROM BACILLUS SP.  
JRNL        TITL 2 STRAIN S3WAHI                                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0425                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 67871                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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) : 1.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4903                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2365                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 107                                     
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.66400                                              
REMARK   3    B22 (A**2) : 0.66400                                              
REMARK   3    B33 (A**2) : -1.32700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.036         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.235         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2552 ; 0.024 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  2429 ; 0.004 ; 0.016       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3473 ; 1.997 ; 1.834       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5591 ; 0.759 ; 1.733       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   330 ; 7.072 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    14 ;14.577 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;16.335 ;10.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   415 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2932 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   551 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   552 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   563 ; 0.728 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1230 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    84 ; 0.132 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 1.038 ; 0.200       
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):  1259 ;13.247 ; 3.510       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1259 ;13.235 ; 3.510       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1577 ;17.810 ; 6.329       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1578 ;17.809 ; 6.331       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1293 ;13.881 ; 3.841       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1288 ;13.835 ; 3.846       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1884 ;18.435 ; 6.920       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1879 ;18.426 ; 6.920       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4981 ; 5.735 ; 3.000       
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  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 8ZXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-24.                  
REMARK 100 THE DEPOSITION ID IS D_1300048673.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-24                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.15                             
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.3                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67871                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.494                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.30                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 29.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.87100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: ALPHAFOLD                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES MONOHYDRATE PH 6.5 1.6 M       
REMARK 280  MAGENSIUM SULFATE HEPTAHYDRATE, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.63300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       38.91150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       38.91150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.81650            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       38.91150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       38.91150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      101.44950            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       38.91150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       38.91150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       33.81650            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       38.91150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       38.91150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      101.44950            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       67.63300            
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 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -517.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 A 468  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 559  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   310                                                      
REMARK 465     TRP A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     TYR A   313                                                      
REMARK 465     TYR A   314                                                      
REMARK 465     ALA A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  26    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  54    CE   NZ                                             
REMARK 470     ARG A  80    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A  98    CD   OE1  NE2                                       
REMARK 470     ILE A 100    CD1                                                 
REMARK 470     LYS A 101    CE   NZ                                             
REMARK 470     GLN A 105    CD   OE1  NE2                                       
REMARK 470     LEU A 108    CD2                                                 
REMARK 470     GLN A 113    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 148    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 173    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 188    CG1  CG2  CD1                                       
REMARK 470     ILE A 202    CD1                                                 
REMARK 470     LEU A 209    CG   CD1  CD2                                       
REMARK 470     GLN A 246    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 247    CG   CD   CE   NZ                                   
REMARK 470     GLN A 262    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 272    NZ                                                  
REMARK 470     GLU A 279    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 280    CG   CD   CE   NZ                                   
REMARK 470     ILE A 286    CD1                                                 
REMARK 470     SER A 287    CB   OG                                             
REMARK 470     LEU A 293    CG   CD1  CD2                                       
REMARK 470     TYR A 298    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 298    OH                                                  
REMARK 470     GLN A 301    CG   CD   OE1  NE2                                  
REMARK 470     MET A 303    CG   SD   CE                                        
REMARK 470     ILE A 304    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O2   SO4 A   468     O3   SO4 A   468     7555     0.40            
REMARK 500   O1   SO4 A   468     O4   SO4 A   468     7555     0.60            
REMARK 500   C    LEU A    42     CA   LEU A   127     7555     0.74            
REMARK 500   CA   ALA A    43     CG   LEU A   127     7555     0.79            
REMARK 500   O    LEU A    42     N    LEU A   127     7555     0.82            
REMARK 500   CB   LEU A    42     N    THR A   128     7555     0.93            
REMARK 500   CB   LEU A    42     C    LEU A   127     7555     1.04            
REMARK 500   N    ALA A    43     CA   LEU A   127     7555     1.10            
REMARK 500   CG   LEU A    42     CA   THR A   128     7555     1.12            
REMARK 500   CB   ALA A    43     CG   LEU A   127     7555     1.18            
REMARK 500   CA   ALA A    43     CB   LEU A   127     7555     1.35            
REMARK 500   N    ALA A    43     CB   LEU A   127     7555     1.36            
REMARK 500   CA   LEU A    42     C    LEU A   127     7555     1.39            
REMARK 500   O    ALA A    43     CD1  LEU A   127     7555     1.39            
REMARK 500   CD1  LEU A    42     CB   THR A   128     7555     1.43            
REMARK 500   CD1  LEU A    42     CA   THR A   128     7555     1.44            
REMARK 500   S    SO4 A   468     O1   SO4 A   468     7555     1.44            
REMARK 500   C    LEU A    42     N    LEU A   127     7555     1.45            
REMARK 500   S    SO4 A   468     O4   SO4 A   468     7555     1.45            
REMARK 500   S    SO4 A   468     O3   SO4 A   468     7555     1.47            
REMARK 500   S    SO4 A   468     O2   SO4 A   468     7555     1.51            
REMARK 500   CB   ALA A    43     CD2  LEU A   127     7555     1.55            
REMARK 500   CB   LEU A    42     O    LEU A   127     7555     1.58            
REMARK 500   O    LEU A    42     CA   LEU A   127     7555     1.60            
REMARK 500   O    LEU A   126     O    HOH A   567     7555     1.62            
REMARK 500   CB   LEU A    42     CA   THR A   128     7555     1.67            
REMARK 500   O    HOH A   513     O    HOH A   579     4444     1.71            
REMARK 500   C    ALA A    43     CD1  LEU A   127     7555     1.73            
REMARK 500   C    LEU A    42     C    LEU A   127     7555     1.78            
REMARK 500   CD1  LEU A    42     OG1  THR A   128     7555     1.79            
REMARK 500   CA   ALA A    43     CD1  LEU A   127     7555     1.83            
REMARK 500   CG   LEU A    42     N    THR A   128     7555     1.86            
REMARK 500   CA   LEU A    42     N    THR A   128     7555     1.87            
REMARK 500   C    ALA A    43     CG   LEU A   127     7555     1.90            
REMARK 500   CA   LEU A    42     CA   LEU A   127     7555     1.93            
REMARK 500   CD2  LEU A    42     CA   THR A   128     7555     1.98            
REMARK 500   O4   SO4 A   468     O4   SO4 A   468     7555     1.98            
REMARK 500   CA   LEU A    42     O    LEU A   127     7555     2.01            
REMARK 500   CB   ALA A    43     CB   LEU A   127     7555     2.02            
REMARK 500   CD2  LEU A    42     C    THR A   128     7555     2.04            
REMARK 500   O    LEU A    42     C    LEU A   126     7555     2.10            
REMARK 500   OE2  GLU A    45     CB   ALA A   125     7555     2.11            
REMARK 500   N    LEU A    42     O    LEU A   127     7555     2.11            
REMARK 500   CD2  LEU A    42     N    LYS A   129     7555     2.12            
REMARK 500   O1   SO4 A   468     O3   SO4 A   468     7555     2.12            
REMARK 500   CA   ALA A    43     CA   LEU A   127     7555     2.13            
REMARK 500   CD2  LEU A   127     O    HOH A   563     7555     2.14            
REMARK 500   N    ALA A    43     CG   LEU A   127     7555     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 283   C     PRO A 283   O       0.122                       
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    ARG A   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LEU A  28   CB  -  CG  -  CD2 ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    LEU A 126   CB  -  CG  -  CD2 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO A 283   N   -  CA  -  CB  ANGL. DEV. = -13.2 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  12       37.10    -89.46                                   
REMARK 500    GLU A  16      -42.20     74.26                                   
REMARK 500    ASP A  32      159.83     72.77                                   
REMARK 500    GLN A 123     -109.36     51.24                                   
REMARK 500    ALA A 125     -174.99   -170.40                                   
REMARK 500    LEU A 126       28.59   -155.04                                   
REMARK 500    THR A 128      127.70   -177.91                                   
REMARK 500    LYS A 129      -93.33    -84.48                                   
REMARK 500    THR A 130      144.48   -176.73                                   
REMARK 500    MET A 131      -10.85     68.03                                   
REMARK 500    MET A 131      -10.85     68.03                                   
REMARK 500    LEU A 284     -142.17     54.08                                   
REMARK 500    THR A 285      -59.98     65.19                                   
REMARK 500    ASP A 294      174.84    -54.18                                   
REMARK 500    PHE A 295       -0.47     60.41                                   
REMARK 500    MET A 303      -57.91    155.81                                   
REMARK 500    ASP A 305      -48.13    142.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  125     LEU A  126                 -144.33                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 144         0.20    SIDE CHAIN                              
REMARK 500    ARG A 204         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 579        DISTANCE =  6.52 ANGSTROMS                       
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                              MG A 412  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  45   O                                                      
REMARK 620 2 TYR A  53   O   114.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 415  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A  63   O                                                      
REMARK 620 2 THR A 166   O   142.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 466  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  65   NE2                                                    
REMARK 620 2 HIS A  67   ND1  88.6                                              
REMARK 620 3 HIS A 163   NE2  99.8  92.4                                        
REMARK 620 4 ASP A 182   OD2  89.1 175.2  92.2                                  
REMARK 620 5 GOL A 402   O3  168.4 103.0  79.3  79.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 467  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  69   OD2                                                    
REMARK 620 2 HIS A  70   NE2  87.3                                              
REMARK 620 3 ASP A 182   OD2 168.5  92.8                                        
REMARK 620 4 HIS A 230   NE2  85.9 103.9 105.2                                  
REMARK 620 5 GOL A 402   O3   91.2 173.6  87.5  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 451  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE1                                                    
REMARK 620 2 GLY A 115   O    82.6                                              
REMARK 620 3 THR A 265   OG1  82.3   5.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 421  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP A  92   O                                                      
REMARK 620 2 SER A 134   OG  124.4                                              
REMARK 620 3 CYS A 135   O   125.2 100.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 428  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 113   O                                                      
REMARK 620 2 SER A 307   O   100.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 416  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 152   O                                                      
REMARK 620 2 PHE A 155   O    82.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 409  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 154   O                                                      
REMARK 620 2 TYR A 171   O    81.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 459  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 188   O                                                      
REMARK 620 2 SER A 190   OG  120.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 432  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 193   O                                                      
REMARK 620 2 GLU A 195   OE2  95.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 443  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 213   O                                                      
REMARK 620 2 GLU A 213   OE1 103.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 218   O                                                      
REMARK 620 2 MET A 221   O    90.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 410  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 230   O                                                      
REMARK 620 2 GLU A 232   O   110.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 439  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 250   O                                                      
REMARK 620 2 ASN A 257   OD1 101.6                                              
REMARK 620 N                    1                                               
DBREF  8ZXG A    1   316  PDB    8ZXG     8ZXG             1    316             
SEQRES   1 A  316  MET THR VAL ILE HIS ARG MET GLU ILE PRO VAL PRO PHE          
SEQRES   2 A  316  ALA VAL GLU THR VAL ASN VAL PHE LEU VAL GLU GLY GLU          
SEQRES   3 A  316  THR LEU THR LEU ILE ASP THR GLY THR ASN THR LYS GLU          
SEQRES   4 A  316  SER ARG LEU ALA LEU GLU LYS GLN LEU ALA ALA LEU GLY          
SEQRES   5 A  316  TYR LYS VAL GLU ASP ILE GLU THR VAL VAL LEU THR HIS          
SEQRES   6 A  316  HIS HIS ALA ASP HIS CYS GLY LEU LEU ASP ILE PHE SER          
SEQRES   7 A  316  GLU ARG THR ASN ILE VAL GLY HIS PRO TRP ASN GLU PRO          
SEQRES   8 A  316  TRP ILE THR GLN ASN PRO GLN PHE ILE LYS ARG TYR GLN          
SEQRES   9 A  316  GLN PHE PHE LEU GLU ALA SER VAL GLN PHE GLY VAL PRO          
SEQRES  10 A  316  GLU VAL LEU LEU PRO GLN GLY ALA LEU LEU THR LYS THR          
SEQRES  11 A  316  MET ILE TYR SER CYS LYS ARG SER LEU THR HIS THR VAL          
SEQRES  12 A  316  ARG GLU GLY ASP ARG ILE ALA SER LEU PRO GLU PHE THR          
SEQRES  13 A  316  VAL ILE GLU THR PRO GLY HIS ALA SER THR HIS ILE SER          
SEQRES  14 A  316  LEU TYR ARG GLU ARG ASP GLY VAL LEU ILE GLY GLY ASP          
SEQRES  15 A  316  ALA LEU ILE GLY HIS ILE SER SER ASN PRO ILE LEU GLU          
SEQRES  16 A  316  PRO PRO TYR GLU GLY GLU ILE GLU ARG ALA GLN PRO MET          
SEQRES  17 A  316  LEU GLN TYR ASN GLU THR LEU LYS ARG LEU ALA ARG MET          
SEQRES  18 A  316  ASN ILE SER ARG VAL LEU SER GLY HIS GLY GLU ASP VAL          
SEQRES  19 A  316  LEU ASP VAL VAL GLY LEU VAL ASN GLU ARG LEU GLN LYS          
SEQRES  20 A  316  GLN GLU ALA ARG ALA PHE LYS VAL LEU ASN LEU LEU LYS          
SEQRES  21 A  316  ALA GLN PRO MET THR ALA PHE GLU VAL CYS VAL LYS LEU          
SEQRES  22 A  316  PHE PRO THR LEU TYR GLU LYS GLN LEU PRO LEU THR ILE          
SEQRES  23 A  316  SER GLU ASN VAL GLY GLN LEU ASP PHE LEU ALA TYR ASN          
SEQRES  24 A  316  GLN GLN VAL MET ILE ASP LYS SER SER LYS GLN TRP ILE          
SEQRES  25 A  316  TYR TYR ALA LYS                                              
HET    GOL  A 401       6                                                       
HET    GOL  A 402      12                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405      12                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HET     MG  A 408       1                                                       
HET     MG  A 409       1                                                       
HET     MG  A 410       1                                                       
HET     MG  A 411       1                                                       
HET     MG  A 412       1                                                       
HET     MG  A 413       1                                                       
HET     MG  A 414       1                                                       
HET     MG  A 415       1                                                       
HET     MG  A 416       1                                                       
HET     MG  A 417       1                                                       
HET     MG  A 418       1                                                       
HET     MG  A 419       1                                                       
HET     MG  A 420       1                                                       
HET     MG  A 421       1                                                       
HET     MG  A 422       1                                                       
HET     MG  A 423       1                                                       
HET     MG  A 424       1                                                       
HET     MG  A 425       1                                                       
HET     MG  A 426       1                                                       
HET     MG  A 427       1                                                       
HET     MG  A 428       1                                                       
HET     MG  A 429       1                                                       
HET     MG  A 430       1                                                       
HET     MG  A 431       1                                                       
HET     MG  A 432       1                                                       
HET     MG  A 433       1                                                       
HET     MG  A 434       1                                                       
HET     MG  A 435       1                                                       
HET     MG  A 436       1                                                       
HET     MG  A 437       1                                                       
HET     MG  A 438       1                                                       
HET     MG  A 439       1                                                       
HET     MG  A 440       1                                                       
HET     MG  A 441       1                                                       
HET     MG  A 442       1                                                       
HET     MG  A 443       1                                                       
HET     MG  A 444       1                                                       
HET     MG  A 445       1                                                       
HET     MG  A 446       1                                                       
HET     MG  A 447       1                                                       
HET     MG  A 448       1                                                       
HET     MG  A 449       1                                                       
HET     MG  A 450       1                                                       
HET     MG  A 451       1                                                       
HET     MG  A 452       1                                                       
HET     MG  A 453       1                                                       
HET     MG  A 454       1                                                       
HET     MG  A 455       1                                                       
HET     MG  A 456       1                                                       
HET     MG  A 457       1                                                       
HET     MG  A 458       1                                                       
HET     MG  A 459       1                                                       
HET     MG  A 460       1                                                       
HET     MG  A 461       1                                                       
HET     MG  A 462       1                                                       
HET     MG  A 463       1                                                       
HET     MG  A 464       1                                                       
HET     MG  A 465       1                                                       
HET     ZN  A 466       1                                                       
HET     ZN  A 467       1                                                       
HET    SO4  A 468       5                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    7(C3 H8 O3)                                                  
FORMUL   9   MG    58(MG 2+)                                                    
FORMUL  67   ZN    2(ZN 2+)                                                     
FORMUL  69  SO4    O4 S 2-                                                      
FORMUL  70  HOH   *79(H2 O)                                                     
HELIX    1   1 THR A   37  LEU A   51  1                                  15
HELIX    2   2 LYS A   54  ILE A   58  1                                   5
HELIX    3   3 HIS A   67  PHE A   77  1                                  11
HELIX    4   4 TRP A   88  PHE A  114  1                                  27
HELIX    5   5 PRO A  117  LEU A  121  1                                   5
HELIX    6   6 GLN A  206  MET A  221  1                                  16
HELIX    7   7 ASP A  236  GLN A  262  1                                  27
HELIX    8   8 THR A  265  PHE A  274  1                                  10
HELIX    9   9 THR A  276  GLN A  281  1                                   6
HELIX   10  10 THR A  285  ALA A  297  1                                  13
SHEET    1   1 1 VAL A   3  PRO A  10  0
SHEET    2   2 1 THR A  17  GLU A  24  0
SHEET    3   3 1 LEU A  28  ILE A  31  0
SHEET    4   4 1 THR A  60  VAL A  62  0
SHEET    5   5 1 ASN A  82  GLY A  85  0
SHEET    6   6 1 HIS A 141  THR A 142  0
SHEET    7   7 1 PHE A 155  GLU A 159  0
SHEET    8   8 1 ILE A 168  ARG A 172  0
SHEET    9   9 1 VAL A 177  GLY A 181  0
SHEET   10  10 1 ARG A 225  SER A 228  0
LINK         O   ARG A   6                MG    MG A 423     1555   1555  2.86  
LINK         O   ARG A   6                MG    MG A 424     1555   1555  2.78  
LINK         OD1 ASN A  36                MG    MG A 414     1555   1555  2.97  
LINK         O   GLU A  45                MG    MG A 412     1555   1555  2.78  
LINK         OE1 GLN A  47                MG    MG A 425     1555   1555  2.75  
LINK         O   TYR A  53                MG    MG A 412     1555   1555  2.85  
LINK         OE1 GLU A  56                MG    MG A 440     1555   1555  2.82  
LINK         OE1 GLU A  59                MG    MG A 417     1555   1555  2.72  
LINK         O   LEU A  63                MG    MG A 415     1555   1555  2.75  
LINK         NE2 HIS A  65                ZN    ZN A 466     1555   1555  2.23  
LINK         ND1 HIS A  67                ZN    ZN A 466     1555   1555  2.17  
LINK         OD2 ASP A  69                ZN    ZN A 467     1555   1555  2.17  
LINK         NE2 HIS A  70                ZN    ZN A 467     1555   1555  2.15  
LINK         OD2 ASP A  75                MG    MG A 449     1555   1555  2.75  
LINK         OE1 GLU A  79                MG    MG A 451     1555   6444  2.74  
LINK         O   TRP A  92                MG    MG A 421     1555   1555  2.61  
LINK         O   GLN A  98                MG    MG A 462     1555   1555  2.77  
LINK         O   GLN A 113                MG    MG A 428     1555   1555  2.73  
LINK         O   GLY A 115                MG    MG A 451     1555   1555  2.75  
LINK         OG1 THR A 130                MG    MG A 441     1555   1555  2.54  
LINK         OG  SER A 134                MG    MG A 421     1555   1555  2.48  
LINK         O   CYS A 135                MG    MG A 421     1555   1555  2.60  
LINK         OE2 GLU A 145                MG    MG A 420     1555   4444  2.68  
LINK         O   LEU A 152                MG    MG A 416     1555   1555  2.81  
LINK         O   GLU A 154                MG    MG A 409     1555   1555  2.97  
LINK         O   PHE A 155                MG    MG A 416     1555   1555  2.79  
LINK         OE1 GLU A 159                MG    MG A 419     1555   4444  2.67  
LINK         NE2 HIS A 163                ZN    ZN A 466     1555   1555  2.11  
LINK         O   THR A 166                MG    MG A 415     1555   1555  2.84  
LINK         O   TYR A 171                MG    MG A 409     1555   1555  3.00  
LINK         OD2 ASP A 182                ZN    ZN A 466     1555   1555  2.33  
LINK         OD2 ASP A 182                ZN    ZN A 467     1555   1555  2.09  
LINK         O   ALA A 183                MG    MG A 408     1555   1555  2.99  
LINK         O   ILE A 188                MG    MG A 459     1555   1555  2.80  
LINK         OG  SER A 190                MG    MG A 459     1555   1555  2.45  
LINK         O   PRO A 192                MG    MG A 446     1555   1555  2.93  
LINK         O   ILE A 193                MG    MG A 432     1555   1555  2.93  
LINK         O   LEU A 194                MG    MG A 431     1555   1555  2.77  
LINK         OE2 GLU A 195                MG    MG A 432     1555   1555  2.66  
LINK         OH  TYR A 211                MG    MG A 460     1555   1555  2.47  
LINK         O   GLU A 213                MG    MG A 443     1555   1555  2.87  
LINK         OE1 GLU A 213                MG    MG A 443     1555   1555  2.69  
LINK         O   LEU A 218                MG    MG A 445     1555   1555  2.77  
LINK         O   MET A 221                MG    MG A 445     1555   1555  2.55  
LINK         O   HIS A 230                MG    MG A 410     1555   1555  2.65  
LINK         NE2 HIS A 230                ZN    ZN A 467     1555   1555  2.11  
LINK         O   GLU A 232                MG    MG A 410     1555   1555  2.70  
LINK         OE1 GLU A 232                MG    MG A 448     1555   1555  2.72  
LINK         O   ALA A 250                MG    MG A 439     1555   8554  2.86  
LINK         OD1 ASN A 257                MG    MG A 439     1555   1555  2.87  
LINK         OG1 THR A 265                MG    MG A 451     1555   1555  2.76  
LINK         O   GLU A 268                MG    MG A 450     1555   1555  2.75  
LINK         OG1 THR A 276                MG    MG A 454     1555   1555  2.17  
LINK         O   SER A 307                MG    MG A 428     1555   1555  2.73  
LINK         O3 BGOL A 402                ZN    ZN A 466     1555   1555  2.29  
LINK         O3 AGOL A 402                ZN    ZN A 467     1555   1555  2.17  
CRYST1   77.823   77.823  135.266  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012850  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012850  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007393        0.00000                         
ATOM      1  N   MET A   1     -36.797  13.767   0.656  1.00 52.71           N
ANISOU    1  N   MET A   1     6882   4660   8484    577   -472    373       N
ATOM      2  CA  MET A   1     -37.357  12.519   0.093  1.00 48.08           C
ANISOU    2  CA  MET A   1     7325   3462   7480   1015   -213   1097       C
ATOM      3  C   MET A   1     -36.307  11.412   0.197  1.00 41.84           C
ANISOU    3  C   MET A   1     6859   3976   5062   1487    509     52       C
ATOM      4  O   MET A   1     -36.069  10.945   1.309  1.00 46.65           O
ANISOU    4  O   MET A   1     8116   4641   4966    262    168    223       O
ATOM      5  CB  MET A   1     -37.873  12.715  -1.331  1.00 53.62           C
ANISOU    5  CB  MET A   1     7852   4930   7592   2027    -81    308       C
ATOM      6  CG  MET A   1     -39.028  11.798  -1.691  1.00 58.73           C
ANISOU    6  CG  MET A   1     7527   6061   8727   2047    585   -473       C
ATOM      7  SD  MET A   1     -39.960  12.532  -3.052  1.00 78.93           S
ANISOU    7  SD  MET A   1     9574   9541  10872   1084   -847    263       S
ATOM      8  CE  MET A   1     -40.872  13.775  -2.136  1.00 59.47           C
ANISOU    8  CE  MET A   1     3441   8116  11040    922  -2378   -760       C
ATOM      9  N   THR A   2     -35.584  11.062  -0.889  1.00 36.29           N
ANISOU    9  N   THR A   2     5290   3948   4549    594    214    257       N
ATOM     10  CA  THR A   2     -34.793   9.843  -0.833  1.00 33.08           C
ANISOU   10  CA  THR A   2     4496   3559   4515    134    -39    296       C
ATOM     11  C   THR A   2     -33.445  10.125  -0.173  1.00 31.67           C
ANISOU   11  C   THR A   2     5152   2483   4397   -163   -248     70       C
ATOM     12  O   THR A   2     -32.868  11.223  -0.280  1.00 31.12           O
ANISOU   12  O   THR A   2     4636   2878   4309    -99   -277   -189       O
ATOM     13  CB  THR A   2     -34.585   9.178  -2.202  1.00 34.97           C
ANISOU   13  CB  THR A   2     5062   3879   4346    579   -131    492       C
ATOM     14  OG1 THR A   2     -33.882  10.104  -3.028  1.00 35.01           O
ANISOU   14  OG1 THR A   2     5214   4309   3780   -457    -54     70       O
ATOM     15  CG2 THR A   2     -35.895   8.737  -2.829  1.00 40.41           C
ANISOU   15  CG2 THR A   2     5550   5176   4628   -142   -521    570       C
ATOM     16  N   VAL A   3     -32.982   9.118   0.551  1.00 29.84           N
ANISOU   16  N   VAL A   3     4464   2537   4336    222   -345   -170       N
ATOM     17  CA  VAL A   3     -31.623   9.019   1.021  1.00 29.67           C
ANISOU   17  CA  VAL A   3     4335   2548   4391     59   -438   -373       C
ATOM     18  C   VAL A   3     -30.987   7.802   0.352  1.00 27.85           C
ANISOU   18  C   VAL A   3     3796   2762   4023    360   -212   -237       C
ATOM     19  O   VAL A   3     -31.600   6.748   0.316  1.00 28.60           O
ANISOU   19  O   VAL A   3     3390   2701   4774   -168     10   -281       O
ATOM     20  CB  VAL A   3     -31.539   8.889   2.553  1.00 36.65           C
ANISOU   20  CB  VAL A   3     5308   4000   4616    763   -538  -1049       C
ATOM     21  CG1 VAL A   3     -30.090   8.931   2.993  1.00 38.06           C
ANISOU   21  CG1 VAL A   3     5320   4238   4902    291   -968  -1190       C
ATOM     22  CG2 VAL A   3     -32.344   9.967   3.265  1.00 39.74           C
ANISOU   22  CG2 VAL A   3     5527   4674   4898    291   -679  -1299       C
ATOM     23  N   ILE A   4     -29.823   7.989  -0.268  1.00 28.52           N
ANISOU   23  N   ILE A   4     3864   2456   4515    107   -120   -264       N
ATOM     24  CA  ILE A   4     -29.115   6.897  -0.931  1.00 26.92           C
ANISOU   24  CA  ILE A   4     3630   2602   3995     91   -238   -493       C
ATOM     25  C   ILE A   4     -27.826   6.623  -0.182  1.00 25.45           C
ANISOU   25  C   ILE A   4     3381   2723   3565   -153   -209   -510       C
ATOM     26  O   ILE A   4     -27.090   7.543   0.176  1.00 27.66           O
ANISOU   26  O   ILE A   4     3715   2503   4292   -379   -842    -41       O
ATOM     27  CB  ILE A   4     -28.825   7.226  -2.399  1.00 29.27           C
ANISOU   27  CB  ILE A   4     4091   3031   3999     41   -407   -356       C
ATOM     28  CG1 ILE A   4     -30.089   7.635  -3.112  1.00 30.30           C
ANISOU   28  CG1 ILE A   4     4360   2720   4435     -8   -765   -197       C
ATOM     29  CG2 ILE A   4     -28.122   6.070  -3.097  1.00 27.82           C
ANISOU   29  CG2 ILE A   4     3647   3227   3694   -180   -199    -46       C
ATOM     30  CD1 ILE A   4     -29.895   7.908  -4.579  1.00 33.36           C
ANISOU   30  CD1 ILE A   4     5107   3435   4134    824   -607    -50       C
ATOM     31  N   HIS A   5     -27.581   5.333   0.053  1.00 25.69           N
ANISOU   31  N   HIS A   5     3651   2458   3652   -259   -536   -241       N
ATOM     32  CA  HIS A   5     -26.395   4.889   0.772  1.00 26.84           C
ANISOU   32  CA  HIS A   5     3867   2657   3676     36   -487   -582       C
ATOM     33  C   HIS A   5     -25.633   3.905  -0.109  1.00 25.04           C
ANISOU   33  C   HIS A   5     3457   3058   3000    -34   -468   -457       C
ATOM     34  O   HIS A   5     -26.227   3.035  -0.726  1.00 26.37           O
ANISOU   34  O   HIS A   5     3201   3094   3724   -152   -256   -673       O
ATOM     35  CB  HIS A   5     -26.784   4.101   2.030  1.00 26.84           C
ANISOU   35  CB  HIS A   5     3993   3111   3094    177   -483   -562       C
ATOM     36  CG  HIS A   5     -27.676   4.834   2.922  1.00 31.82           C
ANISOU   36  CG  HIS A   5     4743   4025   3321    395   -298   -519       C
ATOM     37  ND1 HIS A   5     -27.203   5.592   3.961  1.00 35.35           N
ANISOU   37  ND1 HIS A   5     5178   4356   3896    583   -521  -1021       N
ATOM     38  CD2 HIS A   5     -28.995   4.963   2.902  1.00 34.76           C
ANISOU   38  CD2 HIS A   5     4852   4803   3551    907   -498   -855       C
ATOM     39  CE1 HIS A   5     -28.251   6.171   4.539  1.00 42.65           C
ANISOU   39  CE1 HIS A   5     6271   6121   3813    874   -125  -1375       C
ATOM     40  NE2 HIS A   5     -29.352   5.781   3.926  1.00 41.93           N
ANISOU   40  NE2 HIS A   5     5915   5552   4466   1608    -24  -1217       N
ATOM     41  N   ARG A   6     -24.317   4.065  -0.142  1.00 24.53           N
ANISOU   41  N   ARG A   6     3295   2475   3548   -403   -315   -360       N
ATOM     42  CA  ARG A   6     -23.425   3.124  -0.772  1.00 24.01           C
ANISOU   42  CA  ARG A   6     3206   2664   3253    -91   -294   -461       C
ATOM     43  C   ARG A   6     -22.975   2.088   0.243  1.00 26.13           C
ANISOU   43  C   ARG A   6     3671   3305   2952   -264   -442   -418       C
ATOM     44  O   ARG A   6     -22.469   2.477   1.298  1.00 25.97           O
ANISOU   44  O   ARG A   6     3909   2750   3207   -161   -524   -294       O
ATOM     45  CB  ARG A   6     -22.178   3.807  -1.334  1.00 27.41           C
ANISOU   45  CB  ARG A   6     3900   2984   3529   -473   -219   -131       C
ATOM     46  CG  ARG A   6     -21.169   2.908  -2.023  1.00 30.35           C
ANISOU   46  CG  ARG A   6     4213   3307   4012   -169     78   -171       C
ATOM     47  CD  ARG A   6     -20.066   3.893  -2.486  1.00 43.80           C
ANISOU   47  CD  ARG A   6     4604   5655   6385     29    578   -714       C
ATOM     48  NE  ARG A   6     -18.812   3.177  -2.596  1.00 54.28           N
ANISOU   48  NE  ARG A   6     5521   7065   8038   -429    258   -201       N
ATOM     49  CZ  ARG A   6     -17.699   3.662  -3.107  1.00 55.25           C
ANISOU   49  CZ  ARG A   6     5560   7751   7683   -783   1226    -49       C
ATOM     50  NH1 ARG A   6     -17.548   4.958  -3.367  1.00 60.91           N
ANISOU   50  NH1 ARG A   6     5585   7936   9622   -346   1444   -770       N
ATOM     51  NH2 ARG A   6     -16.727   2.804  -3.325  1.00 47.31           N
ANISOU   51  NH2 ARG A   6     4358   8248   5369  -1149   -286   -135       N
ATOM     52  N   MET A   7     -23.128   0.792  -0.094  1.00 23.30           N
ANISOU   52  N   MET A   7     3107   2607   3139   -224   -572     57       N
ATOM     53  CA  MET A   7     -22.577  -0.241   0.745  1.00 20.81           C
ANISOU   53  CA  MET A   7     2677   2651   2580   -209   -275   -415       C
ATOM     54  C   MET A   7     -21.543  -0.978  -0.105  1.00 21.11           C
ANISOU   54  C   MET A   7     2498   2650   2874   -101   -195   -373       C
ATOM     55  O   MET A   7     -21.804  -1.311  -1.238  1.00 24.54           O
ANISOU   55  O   MET A   7     2875   3519   2928     -8   -428   -286       O
ATOM     56  CB  MET A   7     -23.646  -1.201   1.291  1.00 23.22           C
ANISOU   56  CB  MET A   7     2838   2905   3079   -272     34    -89       C
ATOM     57  CG  MET A   7     -24.609  -0.508   2.243  1.00 25.67           C
ANISOU   57  CG  MET A   7     3126   3704   2923   -487   -128   -232       C
ATOM     58  SD  MET A   7     -25.900  -1.592   2.866  1.00 27.73           S
ANISOU   58  SD  MET A   7     3584   3543   3410   -473   -102   -215       S
ATOM     59  CE  MET A   7     -26.791  -1.916   1.370  1.00 26.11           C
ANISOU   59  CE  MET A   7     3481   2968   3473   -177   -380    151       C
ATOM     60  N   GLU A   8     -20.347  -1.159   0.440  1.00 23.91           N
ANISOU   60  N   GLU A   8     3117   3187   2782     19   -423   -254       N
ATOM     61  CA  GLU A   8     -19.272  -1.849  -0.261  1.00 22.78           C
ANISOU   61  CA  GLU A   8     3029   2900   2728   -315   -161   -226       C
ATOM     62  C   GLU A   8     -19.282  -3.307   0.195  1.00 24.05           C
ANISOU   62  C   GLU A   8     3168   3202   2769   -317   -311    223       C
ATOM     63  O   GLU A   8     -19.055  -3.590   1.366  1.00 25.05           O
ANISOU   63  O   GLU A   8     3630   3135   2751   -345   -327     17       O
ATOM     64  CB  GLU A   8     -17.929  -1.184   0.037  1.00 23.85           C
ANISOU   64  CB  GLU A   8     2850   3026   3185   -119   -407    -80       C
ATOM     65  CG  GLU A   8     -17.855   0.220  -0.517  1.00 28.16           C
ANISOU   65  CG  GLU A   8     3374   3355   3969   -246   -721    106       C
ATOM     66  CD  GLU A   8     -16.590   0.972  -0.244  1.00 37.77           C
ANISOU   66  CD  GLU A   8     4142   4155   6052   -608  -1217    651       C
ATOM     67  OE1 GLU A   8     -16.635   2.161  -0.546  1.00 42.94           O
ANISOU   67  OE1 GLU A   8     5886   4269   6162  -1223  -1420    673       O
ATOM     68  OE2 GLU A   8     -15.626   0.405   0.275  1.00 45.40           O
ANISOU   68  OE2 GLU A   8     4839   4430   7982   -815  -2075   1240       O
ATOM     69  N   ILE A   9     -19.567  -4.213  -0.742  1.00 22.19           N
ANISOU   69  N   ILE A   9     2871   2860   2700   -139   -376    241       N
ATOM     70  CA  ILE A   9     -19.724  -5.624  -0.436  1.00 22.81           C
ANISOU   70  CA  ILE A   9     2745   2839   3082   -137   -291    152       C
ATOM     71  C   ILE A   9     -18.535  -6.399  -0.987  1.00 21.31           C
ANISOU   71  C   ILE A   9     2286   2719   3091   -391   -398    195       C
ATOM     72  O   ILE A   9     -18.207  -6.307  -2.187  1.00 22.42           O
ANISOU   72  O   ILE A   9     2715   2877   2928    -14   -261    236       O
ATOM     73  CB  ILE A   9     -21.047  -6.160  -1.029  1.00 22.57           C
ANISOU   73  CB  ILE A   9     2736   2915   2926   -118   -203    206       C
ATOM     74  CG1 ILE A   9     -22.255  -5.343  -0.572  1.00 24.34           C
ANISOU   74  CG1 ILE A   9     2706   3266   3278     89   -404    378       C
ATOM     75  CG2 ILE A   9     -21.221  -7.628  -0.700  1.00 24.16           C
ANISOU   75  CG2 ILE A   9     2942   2760   3478    -85   -330    288       C
ATOM     76  CD1 ILE A   9     -22.464  -5.205   0.921  1.00 24.33           C
ANISOU   76  CD1 ILE A   9     3125   3096   3024     16    -47     28       C
ATOM     77  N   PRO A  10     -17.799  -7.137  -0.127  1.00 22.48           N
ANISOU   77  N   PRO A  10     2605   2996   2939   -250   -414    203       N
ATOM     78  CA  PRO A  10     -16.668  -7.930  -0.613  1.00 22.60           C
ANISOU   78  CA  PRO A  10     2421   3048   3119    108   -453    249       C
ATOM     79  C   PRO A  10     -17.096  -9.001  -1.624  1.00 22.17           C
ANISOU   79  C   PRO A  10     2521   2883   3019    137   -612    512       C
ATOM     80  O   PRO A  10     -18.141  -9.673  -1.446  1.00 24.00           O
ANISOU   80  O   PRO A  10     2578   2928   3611   -170   -127    258       O
ATOM     81  CB  PRO A  10     -16.093  -8.504   0.681  1.00 25.58           C
ANISOU   81  CB  PRO A  10     2857   3297   3563    -60   -742    866       C
ATOM     82  CG  PRO A  10     -17.208  -8.507   1.633  1.00 30.05           C
ANISOU   82  CG  PRO A  10     3701   4092   3626    429   -271    745       C
ATOM     83  CD  PRO A  10     -18.075  -7.352   1.298  1.00 24.84           C
ANISOU   83  CD  PRO A  10     2776   3354   3309     93   -211    264       C
ATOM     84  N   VAL A  11     -16.292  -9.132  -2.694  1.00 23.28           N
ANISOU   84  N   VAL A  11     2615   3093   3137   -169   -335    255       N
ATOM     85  CA  VAL A  11     -16.486 -10.168  -3.694  1.00 22.02           C
ANISOU   85  CA  VAL A  11     2473   2562   3332      0   -227    359       C
ATOM     86  C   VAL A  11     -15.169 -10.876  -3.913  1.00 23.35           C
ANISOU   86  C   VAL A  11     2644   2780   3448    289   -409    135       C
ATOM     87  O   VAL A  11     -14.108 -10.266  -3.706  1.00 28.00           O
ANISOU   87  O   VAL A  11     2796   3125   4718    321   -426    116       O
ATOM     88  CB  VAL A  11     -17.061  -9.603  -5.021  1.00 24.19           C
ANISOU   88  CB  VAL A  11     2913   2843   3435     53   -375    451       C
ATOM     89  CG1 VAL A  11     -18.448  -9.016  -4.758  1.00 25.37           C
ANISOU   89  CG1 VAL A  11     3102   3062   3474     22   -704    226       C
ATOM     90  CG2 VAL A  11     -16.137  -8.560  -5.620  1.00 23.22           C
ANISOU   90  CG2 VAL A  11     2964   2567   3291   -305   -205    356       C
ATOM     91  N   PRO A  12     -15.196 -12.153  -4.342  1.00 24.37           N
ANISOU   91  N   PRO A  12     2760   2832   3666    184     64    413       N
ATOM     92  CA  PRO A  12     -13.976 -12.955  -4.447  1.00 26.17           C
ANISOU   92  CA  PRO A  12     2510   3089   4343    427     -2    429       C
ATOM     93  C   PRO A  12     -13.312 -12.821  -5.805  1.00 30.55           C
ANISOU   93  C   PRO A  12     3237   3840   4531    863    232    487       C
ATOM     94  O   PRO A  12     -12.813 -13.789  -6.350  1.00 36.70           O
ANISOU   94  O   PRO A  12     4452   4539   4955   1207    540    894       O
ATOM     95  CB  PRO A  12     -14.531 -14.357  -4.257  1.00 28.20           C
ANISOU   95  CB  PRO A  12     3444   2624   4648    745   -235    426       C
ATOM     96  CG  PRO A  12     -15.864 -14.320  -4.924  1.00 30.40           C
ANISOU   96  CG  PRO A  12     3845   3242   4465    687    197    250       C
ATOM     97  CD  PRO A  12     -16.409 -12.981  -4.487  1.00 24.11           C
ANISOU   97  CD  PRO A  12     2821   2526   3814     43    -25    438       C
ATOM     98  N   PHE A  13     -13.366 -11.620  -6.339  1.00 30.52           N
ANISOU   98  N   PHE A  13     3214   3750   4633    695    805    736       N
ATOM     99  CA  PHE A  13     -12.827 -11.253  -7.629  1.00 29.26           C
ANISOU   99  CA  PHE A  13     3257   3806   4054    608    -53    271       C
ATOM    100  C   PHE A  13     -11.747 -10.196  -7.434  1.00 28.23           C
ANISOU  100  C   PHE A  13     3014   3755   3956     99    -36    561       C
ATOM    101  O   PHE A  13     -11.666  -9.587  -6.372  1.00 28.95           O
ANISOU  101  O   PHE A  13     3153   3966   3881   -101    -35    650       O
ATOM    102  CB  PHE A  13     -13.940 -10.688  -8.511  1.00 31.52           C
ANISOU  102  CB  PHE A  13     3656   4250   4069    408    -69    634       C
ATOM    103  CG  PHE A  13     -15.136 -11.607  -8.750  1.00 28.81           C
ANISOU  103  CG  PHE A  13     3582   3269   4095     32   -228    412       C
ATOM    104  CD1 PHE A  13     -14.991 -12.963  -8.974  1.00 33.53           C
ANISOU  104  CD1 PHE A  13     4161   3539   5041   -217    194    130       C
ATOM    105  CD2 PHE A  13     -16.409 -11.089  -8.834  1.00 27.56           C
ANISOU  105  CD2 PHE A  13     3664   2680   4129    -20     17    178       C
ATOM    106  CE1 PHE A  13     -16.096 -13.775  -9.191  1.00 31.50           C
ANISOU  106  CE1 PHE A  13     3850   3415   4704    -71   -129    536       C
ATOM    107  CE2 PHE A  13     -17.514 -11.900  -9.078  1.00 29.00           C
ANISOU  107  CE2 PHE A  13     3652   3354   4010     86    159    166       C
ATOM    108  CZ  PHE A  13     -17.361 -13.244  -9.253  1.00 30.14           C
ANISOU  108  CZ  PHE A  13     4118   3197   4137    -18     15    263       C
ATOM    109  N   ALA A  14     -10.980  -9.950  -8.500  1.00 30.93           N
ANISOU  109  N   ALA A  14     3293   3861   4598    267    106    437       N
ATOM    110  CA  ALA A  14      -9.858  -9.028  -8.413  1.00 32.68           C
ANISOU  110  CA  ALA A  14     3268   4312   4835   -100    307    492       C
ATOM    111  C   ALA A  14     -10.278  -7.625  -7.994  1.00 29.50           C
ANISOU  111  C   ALA A  14     2714   3972   4524   -365    479    542       C
ATOM    112  O   ALA A  14      -9.487  -6.926  -7.344  1.00 30.72           O
ANISOU  112  O   ALA A  14     3048   4133   4492   -449    234    550       O
ATOM    113  CB  ALA A  14      -9.103  -9.037  -9.715  1.00 35.01           C
ANISOU  113  CB  ALA A  14     3824   4573   4905   -472    702    952       C
ATOM    114  N   VAL A  15     -11.493  -7.214  -8.367  1.00 30.13           N
ANISOU  114  N   VAL A  15     3004   4109   4336   -416    -23    546       N
ATOM    115  CA AVAL A  15     -12.009  -5.888  -8.058  0.50 26.84           C
ANISOU  115  CA AVAL A  15     2821   3212   4164   -146    -97    786       C
ATOM    116  CA BVAL A  15     -12.034  -5.887  -8.058  0.50 29.04           C
ANISOU  116  CA BVAL A  15     3154   3603   4275   -227     47    500       C
ATOM    117  C   VAL A  15     -12.297  -5.717  -6.552  1.00 27.86           C
ANISOU  117  C   VAL A  15     3018   3541   4028    -83    153    189       C
ATOM    118  O   VAL A  15     -12.485  -4.586  -6.064  1.00 29.61           O
ANISOU  118  O   VAL A  15     3545   3440   4267   -192    -38    307       O
ATOM    119  CB AVAL A  15     -13.260  -5.653  -8.927  0.50 26.91           C
ANISOU  119  CB AVAL A  15     2988   3132   4104   -140   -231   1055       C
ATOM    120  CB BVAL A  15     -13.332  -5.555  -8.829  0.50 33.04           C
ANISOU  120  CB BVAL A  15     3656   4472   4426   -307   -151    474       C
ATOM    121  CG1AVAL A  15     -14.481  -6.418  -8.411  0.50 25.28           C
ANISOU  121  CG1AVAL A  15     2308   2988   4308    160   -578   1206       C
ATOM    122  CG1BVAL A  15     -13.089  -5.315 -10.305  0.50 38.32           C
ANISOU  122  CG1BVAL A  15     4708   5046   4806   -416   -152    353       C
ATOM    123  CG2AVAL A  15     -13.564  -4.172  -9.028  0.50 24.43           C
ANISOU  123  CG2AVAL A  15     2692   2549   4043   -120   -159   1310       C
ATOM    124  CG2BVAL A  15     -14.428  -6.601  -8.611  0.50 30.84           C
ANISOU  124  CG2BVAL A  15     3299   4016   4402     -5    -44    616       C
ATOM    125  N   GLU A  16     -12.351  -6.853  -5.818  1.00 26.62           N
ANISOU  125  N   GLU A  16     2833   3360   3922   -137     10    406       N
ATOM    126  CA  GLU A  16     -12.388  -6.909  -4.364  1.00 28.36           C
ANISOU  126  CA  GLU A  16     2620   3627   4529    -19   -233    310       C
ATOM    127  C   GLU A  16     -13.727  -6.515  -3.745  1.00 25.96           C
ANISOU  127  C   GLU A  16     2960   3194   3710   -223   -450    133       C
ATOM    128  O   GLU A  16     -14.147  -7.155  -2.771  1.00 25.44           O
ANISOU  128  O   GLU A  16     2733   3250   3681    -73   -347    313       O
ATOM    129  CB  GLU A  16     -11.274  -6.128  -3.659  1.00 32.53           C
ANISOU  129  CB  GLU A  16     2987   4394   4980    -84   -471    597       C
ATOM    130  CG  GLU A  16      -9.894  -6.659  -4.006  1.00 39.48           C
ANISOU  130  CG  GLU A  16     3669   5950   5379    486   -741    147       C
ATOM    131  CD  GLU A  16      -8.828  -5.987  -3.164  1.00 49.11           C
ANISOU  131  CD  GLU A  16     4364   7146   7150     17  -1150   -643       C
ATOM    132  OE1 GLU A  16      -7.690  -6.393  -3.359  1.00 60.44           O
ANISOU  132  OE1 GLU A  16     5575   8226   9166   1224   -791   -463       O
ATOM    133  OE2 GLU A  16      -9.143  -5.117  -2.315  1.00 57.41           O
ANISOU  133  OE2 GLU A  16     6031   6496   9287   -200  -2590  -1310       O
ATOM    134  N   THR A  17     -14.359  -5.453  -4.263  1.00 24.55           N
ANISOU  134  N   THR A  17     2630   3155   3543   -193   -383    171       N
ATOM    135  CA  THR A  17     -15.616  -4.954  -3.688  1.00 25.43           C
ANISOU  135  CA  THR A  17     3319   3271   3071   -257   -731     84       C
ATOM    136  C   THR A  17     -16.532  -4.598  -4.845  1.00 21.86           C
ANISOU  136  C   THR A  17     2729   2509   3070   -232   -610   -165       C
ATOM    137  O   THR A  17     -16.079  -4.191  -5.899  1.00 23.53           O
ANISOU  137  O   THR A  17     2868   2971   3103      6   -582    289       O
ATOM    138  CB  THR A  17     -15.477  -3.751  -2.761  1.00 30.87           C
ANISOU  138  CB  THR A  17     4077   4305   3349   -219  -1319     57       C
ATOM    139  OG1 THR A  17     -15.019  -2.647  -3.483  1.00 34.60           O
ANISOU  139  OG1 THR A  17     4852   3319   4974   -595  -1194    148       O
ATOM    140  CG2 THR A  17     -14.508  -4.120  -1.672  1.00 35.11           C
ANISOU  140  CG2 THR A  17     5182   3810   4348    284  -2013    418       C
ATOM    141  N   VAL A  18     -17.823  -4.726  -4.589  1.00 22.46           N
ANISOU  141  N   VAL A  18     2727   2938   2871   -286   -496    321       N
ATOM    142  CA  VAL A  18     -18.865  -4.197  -5.447  1.00 20.65           C
ANISOU  142  CA  VAL A  18     2630   2494   2721   -205   -427    216       C
ATOM    143  C   VAL A  18     -19.631  -3.152  -4.634  1.00 21.58           C
ANISOU  143  C   VAL A  18     2645   2971   2585   -522   -452     55       C
ATOM    144  O   VAL A  18     -19.823  -3.306  -3.411  1.00 22.50           O
ANISOU  144  O   VAL A  18     2858   2783   2908   -166   -167    162       O
ATOM    145  CB  VAL A  18     -19.817  -5.294  -5.986  1.00 20.65           C
ANISOU  145  CB  VAL A  18     2927   2203   2716   -271   -472    162       C
ATOM    146  CG1 VAL A  18     -20.638  -5.977  -4.908  1.00 22.66           C
ANISOU  146  CG1 VAL A  18     3111   2525   2973    -61   -226    235       C
ATOM    147  CG2 VAL A  18     -20.744  -4.745  -7.064  1.00 20.54           C
ANISOU  147  CG2 VAL A  18     2854   2345   2606   -383   -345    214       C
ATOM    148  N   ASN A  19     -20.044  -2.083  -5.317  1.00 21.11           N
ANISOU  148  N   ASN A  19     2756   2482   2782    -57    -17   -132       N
ATOM    149  CA  ASN A  19     -20.871  -1.073  -4.683  1.00 21.89           C
ANISOU  149  CA  ASN A  19     2710   2607   2999   -259   -166   -114       C
ATOM    150  C   ASN A  19     -22.327  -1.430  -4.911  1.00 22.14           C
ANISOU  150  C   ASN A  19     3069   2493   2850   -122   -265   -111       C
ATOM    151  O   ASN A  19     -22.725  -1.621  -6.064  1.00 23.79           O
ANISOU  151  O   ASN A  19     2903   3204   2932     10   -406   -109       O
ATOM    152  CB  ASN A  19     -20.631   0.301  -5.264  1.00 21.74           C
ANISOU  152  CB  ASN A  19     3133   2239   2887   -179    182    -33       C
ATOM    153  CG  ASN A  19     -19.224   0.791  -5.056  1.00 24.71           C
ANISOU  153  CG  ASN A  19     3375   2863   3151   -597   -374   -129       C
ATOM    154  OD1 ASN A  19     -18.591   0.506  -4.013  1.00 27.15           O
ANISOU  154  OD1 ASN A  19     3613   3445   3259   -893   -589    308       O
ATOM    155  ND2 ASN A  19     -18.767   1.592  -6.033  1.00 28.30           N
ANISOU  155  ND2 ASN A  19     3870   3660   3222   -922   -367    298       N
ATOM    156  N   VAL A  20     -23.101  -1.491  -3.809  1.00 21.92           N
ANISOU  156  N   VAL A  20     2843   2687   2798   -218   -367     56       N
ATOM    157  CA  VAL A  20     -24.528  -1.661  -3.911  1.00 21.50           C
ANISOU  157  CA  VAL A  20     2812   2680   2679   -143   -112   -289       C
ATOM    158  C   VAL A  20     -25.157  -0.419  -3.283  1.00 22.34           C
ANISOU  158  C   VAL A  20     2886   2667   2934   -254   -383   -174       C
ATOM    159  O   VAL A  20     -24.540   0.218  -2.420  1.00 23.57           O
ANISOU  159  O   VAL A  20     2872   2858   3226    -89   -483   -497       O
ATOM    160  CB  VAL A  20     -25.028  -2.965  -3.277  1.00 22.53           C
ANISOU  160  CB  VAL A  20     2729   2579   3251   -169   -271    -84       C
ATOM    161  CG1 VAL A  20     -24.321  -4.172  -3.859  1.00 23.18           C
ANISOU  161  CG1 VAL A  20     2804   2675   3329     88   -603   -377       C
ATOM    162  CG2 VAL A  20     -24.948  -2.939  -1.769  1.00 23.34           C
ANISOU  162  CG2 VAL A  20     2743   2789   3334   -141   -323   -207       C
ATOM    163  N   PHE A  21     -26.334  -0.038  -3.729  1.00 21.31           N
ANISOU  163  N   PHE A  21     2895   2430   2771   -138   -341     -1       N
ATOM    164  CA  PHE A  21     -26.920   1.234  -3.339  1.00 21.43           C
ANISOU  164  CA  PHE A  21     3072   2571   2500     -9   -331   -442       C
ATOM    165  C   PHE A  21     -28.291   1.012  -2.720  1.00 21.74           C
ANISOU  165  C   PHE A  21     3055   2384   2820     54   -289    -35       C
ATOM    166  O   PHE A  21     -29.152   0.411  -3.346  1.00 22.97           O
ANISOU  166  O   PHE A  21     2852   2931   2944   -198     17   -491       O
ATOM    167  CB  PHE A  21     -26.987   2.193  -4.538  1.00 22.66           C
ANISOU  167  CB  PHE A  21     3190   2590   2829    -68   -479   -422       C
ATOM    168  CG  PHE A  21     -25.618   2.543  -5.083  1.00 22.41           C
ANISOU  168  CG  PHE A  21     3002   2577   2936     -9   -106   -160       C
ATOM    169  CD1 PHE A  21     -24.859   3.544  -4.477  1.00 22.32           C
ANISOU  169  CD1 PHE A  21     3149   2611   2722    210   -213   -387       C
ATOM    170  CD2 PHE A  21     -24.992   1.737  -6.020  1.00 21.66           C
ANISOU  170  CD2 PHE A  21     2938   2446   2845      9   -169   -192       C
ATOM    171  CE1 PHE A  21     -23.574   3.809  -4.891  1.00 24.52           C
ANISOU  171  CE1 PHE A  21     3523   2571   3221   -192     13    124       C
ATOM    172  CE2 PHE A  21     -23.697   2.046  -6.444  1.00 23.42           C
ANISOU  172  CE2 PHE A  21     3329   2657   2910   -188    168     -5       C
ATOM    173  CZ  PHE A  21     -23.016   3.082  -5.897  1.00 24.90           C
ANISOU  173  CZ  PHE A  21     3550   2914   2996   -291    208     49       C
ATOM    174  N   LEU A  22     -28.454   1.451  -1.471  1.00 22.58           N
ANISOU  174  N   LEU A  22     3000   2607   2972    -46   -332   -331       N
ATOM    175  CA  LEU A  22     -29.715   1.336  -0.768  1.00 23.11           C
ANISOU  175  CA  LEU A  22     3168   2524   3088     33    -85   -212       C
ATOM    176  C   LEU A  22     -30.427   2.687  -0.828  1.00 23.96           C
ANISOU  176  C   LEU A  22     3441   2515   3148   -106   -207   -343       C
ATOM    177  O   LEU A  22     -29.882   3.697  -0.396  1.00 25.41           O
ANISOU  177  O   LEU A  22     3615   2426   3614   -114   -515   -225       O
ATOM    178  CB  LEU A  22     -29.483   0.968   0.695  1.00 23.06           C
ANISOU  178  CB  LEU A  22     3130   2461   3172     81   -395   -300       C
ATOM    179  CG  LEU A  22     -30.709   0.643   1.536  1.00 25.15           C
ANISOU  179  CG  LEU A  22     3272   3091   3193     32    121   -427       C
ATOM    180  CD1 LEU A  22     -31.213  -0.714   1.119  1.00 24.68           C
ANISOU  180  CD1 LEU A  22     3104   3359   2915   -424    -17     22       C
ATOM    181  CD2 LEU A  22     -30.371   0.679   3.000  1.00 27.43           C
ANISOU  181  CD2 LEU A  22     4015   2946   3461   -453    -65     75       C
ATOM    182  N   VAL A  23     -31.637   2.685  -1.372  1.00 23.69           N
ANISOU  182  N   VAL A  23     3244   2480   3278     25   -356   -409       N
ATOM    183  CA  VAL A  23     -32.422   3.880  -1.530  1.00 25.29           C
ANISOU  183  CA  VAL A  23     3487   2697   3424    -33   -227    -82       C
ATOM    184  C   VAL A  23     -33.545   3.846  -0.517  1.00 23.49           C
ANISOU  184  C   VAL A  23     3255   2631   3040   -168   -304     -9       C
ATOM    185  O   VAL A  23     -34.415   2.986  -0.579  1.00 24.39           O
ANISOU  185  O   VAL A  23     3010   2841   3415   -150    -41   -300       O
ATOM    186  CB  VAL A  23     -32.975   4.020  -2.959  1.00 24.73           C
ANISOU  186  CB  VAL A  23     3466   2757   3172    183   -136    113       C
ATOM    187  CG1 VAL A  23     -33.749   5.330  -3.099  1.00 26.23           C
ANISOU  187  CG1 VAL A  23     3816   2823   3327    437   -196   -226       C
ATOM    188  CG2 VAL A  23     -31.840   3.917  -3.985  1.00 25.66           C
ANISOU  188  CG2 VAL A  23     3258   2904   3587   -347   -336     97       C
ATOM    189  N   GLU A  24     -33.489   4.762   0.438  1.00 25.44           N
ANISOU  189  N   GLU A  24     3380   2886   3400     57   -164   -424       N
ATOM    190  CA  GLU A  24     -34.558   4.899   1.410  1.00 26.03           C
ANISOU  190  CA  GLU A  24     3496   2819   3575   -102    -69   -191       C
ATOM    191  C   GLU A  24     -35.573   5.896   0.859  1.00 27.32           C
ANISOU  191  C   GLU A  24     3540   3110   3731     25    299    -57       C
ATOM    192  O   GLU A  24     -35.356   7.106   0.900  1.00 31.79           O
ANISOU  192  O   GLU A  24     4949   3065   4066    -84    -15    -24       O
ATOM    193  CB  GLU A  24     -33.986   5.461   2.699  1.00 30.41           C
ANISOU  193  CB  GLU A  24     4519   3410   3623    228     86   -915       C
ATOM    194  CG  GLU A  24     -32.946   4.613   3.383  1.00 31.88           C
ANISOU  194  CG  GLU A  24     5110   3508   3495    233   -225   -411       C
ATOM    195  CD  GLU A  24     -32.493   5.322   4.652  1.00 34.67           C
ANISOU  195  CD  GLU A  24     5539   3711   3924      3   -359   -701       C
ATOM    196  OE1 GLU A  24     -31.846   6.366   4.586  1.00 37.51           O
ANISOU  196  OE1 GLU A  24     5927   4009   4316    186   -696  -1036       O
ATOM    197  OE2 GLU A  24     -32.790   4.854   5.707  1.00 43.49           O
ANISOU  197  OE2 GLU A  24     7851   4447   4227   -836   -385   -329       O
ATOM    198  N   GLY A  25     -36.660   5.372   0.342  1.00 29.98           N
ANISOU  198  N   GLY A  25     3859   3466   4067    609    138   -388       N
ATOM    199  CA  GLY A  25     -37.748   6.154  -0.204  1.00 32.37           C
ANISOU  199  CA  GLY A  25     4199   3955   4144    790    -78   -183       C
ATOM    200  C   GLY A  25     -39.038   5.804   0.554  1.00 31.89           C
ANISOU  200  C   GLY A  25     3773   4089   4255    799    538   -458       C
ATOM    201  O   GLY A  25     -39.006   5.432   1.741  1.00 32.94           O
ANISOU  201  O   GLY A  25     3832   4335   4349    473    227   -611       O
ATOM    202  N   GLU A  26     -40.165   5.874  -0.161  1.00 32.60           N
ANISOU  202  N   GLU A  26     3994   3897   4497    869    317   -347       N
ATOM    203  CA  GLU A  26     -41.433   5.464   0.417  1.00 30.71           C
ANISOU  203  CA  GLU A  26     3617   4235   3815    637    516   -428       C
ATOM    204  C   GLU A  26     -41.335   3.986   0.805  1.00 31.35           C
ANISOU  204  C   GLU A  26     3804   4083   4023    353    611   -133       C
ATOM    205  O   GLU A  26     -41.913   3.580   1.817  1.00 33.76           O
ANISOU  205  O   GLU A  26     4092   4583   4151    828   1257    -93       O
ATOM    206  CB  GLU A  26     -42.626   5.777  -0.486  1.00 34.96           C
ANISOU  206  CB  GLU A  26     4960   4601   3720   1216    336   -851       C
ATOM    207  N   THR A  27     -40.595   3.223  -0.008  1.00 29.80           N
ANISOU  207  N   THR A  27     3329   3845   4150    653    412     89       N
ATOM    208  CA  THR A  27     -40.196   1.849   0.297  1.00 29.03           C
ANISOU  208  CA  THR A  27     3323   3771   3937    419    276     49       C
ATOM    209  C   THR A  27     -38.680   1.779   0.132  1.00 25.57           C
ANISOU  209  C   THR A  27     3386   3390   2940    277    246    -40       C
ATOM    210  O   THR A  27     -38.071   2.745  -0.336  1.00 26.94           O
ANISOU  210  O   THR A  27     3264   3553   3418    316    498   -204       O
ATOM    211  CB  THR A  27     -40.871   0.850  -0.645  1.00 30.83           C
ANISOU  211  CB  THR A  27     3221   3743   4750    -40    134   -169       C
ATOM    212  OG1 THR A  27     -40.448   1.073  -1.990  1.00 30.54           O
ANISOU  212  OG1 THR A  27     3592   4191   3822    352   -172    -98       O
ATOM    213  CG2 THR A  27     -42.384   0.944  -0.611  1.00 37.87           C
ANISOU  213  CG2 THR A  27     4185   4820   5384    336    755   -544       C
ATOM    214  N   LEU A  28     -38.111   0.658   0.557  1.00 24.28           N
ANISOU  214  N   LEU A  28     3324   2771   3129    121   -118   -118       N
ATOM    215  CA  LEU A  28     -36.672   0.457   0.547  1.00 24.57           C
ANISOU  215  CA  LEU A  28     3073   2969   3292    142    -82   -158       C
ATOM    216  C   LEU A  28     -36.265  -0.337  -0.691  1.00 24.93           C
ANISOU  216  C   LEU A  28     3052   2893   3526    157    -34   -377       C
ATOM    217  O   LEU A  28     -36.820  -1.424  -0.924  1.00 23.57           O
ANISOU  217  O   LEU A  28     2815   2928   3210     -3    195   -212       O
ATOM    218  CB  LEU A  28     -36.318  -0.345   1.785  1.00 29.40           C
ANISOU  218  CB  LEU A  28     4987   3087   3096   -193    -45     84       C
ATOM    219  CG  LEU A  28     -35.249   0.099   2.724  1.00 36.22           C
ANISOU  219  CG  LEU A  28     5384   3719   4660   -557   -878    422       C
ATOM    220  CD1 LEU A  28     -34.712  -1.157   3.436  1.00 28.82           C
ANISOU  220  CD1 LEU A  28     4666   2872   3414   -534   -397    104       C
ATOM    221  CD2 LEU A  28     -34.259   1.155   2.441  1.00 28.43           C
ANISOU  221  CD2 LEU A  28     3918   2536   4348   -760   -413    -74       C
ATOM    222  N   THR A  29     -35.372   0.242  -1.516  1.00 22.77           N
ANISOU  222  N   THR A  29     2617   2780   3253     85   -254   -350       N
ATOM    223  CA  THR A  29     -34.877  -0.416  -2.718  1.00 22.09           C
ANISOU  223  CA  THR A  29     2709   2768   2916    109     81   -285       C
ATOM    224  C   THR A  29     -33.377  -0.661  -2.578  1.00 21.92           C
ANISOU  224  C   THR A  29     2907   2455   2965      0   -218   -437       C
ATOM    225  O   THR A  29     -32.641   0.178  -2.052  1.00 24.40           O
ANISOU  225  O   THR A  29     2993   2454   3824    -79    -69   -728       O
ATOM    226  CB  THR A  29     -35.154   0.457  -3.924  1.00 24.06           C
ANISOU  226  CB  THR A  29     3046   3103   2994    218    -39   -323       C
ATOM    227  OG1 THR A  29     -36.556   0.701  -3.996  1.00 24.67           O
ANISOU  227  OG1 THR A  29     2885   3130   3358    292     48   -298       O
ATOM    228  CG2 THR A  29     -34.627  -0.141  -5.218  1.00 23.98           C
ANISOU  228  CG2 THR A  29     2814   2834   3463    288   -140     44       C
ATOM    229  N   LEU A  30     -32.914  -1.829  -3.015  1.00 21.15           N
ANISOU  229  N   LEU A  30     2595   2556   2884     64     35   -385       N
ATOM    230  CA  LEU A  30     -31.501  -2.102  -3.132  1.00 20.86           C
ANISOU  230  CA  LEU A  30     2502   2657   2767   -177   -119    -69       C
ATOM    231  C   LEU A  30     -31.152  -2.221  -4.615  1.00 19.81           C
ANISOU  231  C   LEU A  30     2663   2176   2688     37   -193   -165       C
ATOM    232  O   LEU A  30     -31.795  -2.986  -5.323  1.00 21.80           O
ANISOU  232  O   LEU A  30     3017   2625   2641   -182     34   -376       O
ATOM    233  CB  LEU A  30     -31.154  -3.406  -2.424  1.00 20.29           C
ANISOU  233  CB  LEU A  30     2621   2346   2743   -295    -90   -120       C
ATOM    234  CG  LEU A  30     -29.685  -3.796  -2.380  1.00 22.53           C
ANISOU  234  CG  LEU A  30     2940   2489   3133   -131    -31    103       C
ATOM    235  CD1 LEU A  30     -28.877  -2.772  -1.576  1.00 24.72           C
ANISOU  235  CD1 LEU A  30     2671   2854   3868   -267   -186    163       C
ATOM    236  CD2 LEU A  30     -29.487  -5.207  -1.809  1.00 23.82           C
ANISOU  236  CD2 LEU A  30     3093   2672   3286   -313   -295    204       C
ATOM    237  N   ILE A  31     -30.061  -1.564  -5.044  1.00 19.76           N
ANISOU  237  N   ILE A  31     2460   2377   2671   -197    -71   -381       N
ATOM    238  CA  ILE A  31     -29.550  -1.723  -6.391  1.00 20.04           C
ANISOU  238  CA  ILE A  31     2361   2448   2806   -153   -248    -44       C
ATOM    239  C   ILE A  31     -28.270  -2.552  -6.311  1.00 20.27           C
ANISOU  239  C   ILE A  31     2473   2231   3000    -44   -226     52       C
ATOM    240  O   ILE A  31     -27.271  -2.104  -5.739  1.00 20.95           O
ANISOU  240  O   ILE A  31     2530   2488   2940   -178   -308    -78       O
ATOM    241  CB  ILE A  31     -29.338  -0.363  -7.062  1.00 22.38           C
ANISOU  241  CB  ILE A  31     2733   2712   3058     27   -330    -12       C
ATOM    242  CG1 ILE A  31     -30.672   0.386  -7.151  1.00 27.12           C
ANISOU  242  CG1 ILE A  31     3373   3101   3829    246    -87    157       C
ATOM    243  CG2 ILE A  31     -28.727  -0.572  -8.433  1.00 23.13           C
ANISOU  243  CG2 ILE A  31     2693   2805   3291     90   -179    174       C
ATOM    244  CD1 ILE A  31     -30.605   1.782  -6.695  1.00 34.95           C
ANISOU  244  CD1 ILE A  31     3988   4339   4953     60   -895   -983       C
ATOM    245  N   ASP A  32     -28.318  -3.758  -6.880  1.00 20.79           N
ANISOU  245  N   ASP A  32     2716   2370   2811   -151   -280    152       N
ATOM    246  CA  ASP A  32     -27.235  -4.739  -6.904  1.00 19.33           C
ANISOU  246  CA  ASP A  32     2429   2467   2448    261   -515    -20       C
ATOM    247  C   ASP A  32     -27.032  -5.381  -5.527  1.00 19.12           C
ANISOU  247  C   ASP A  32     2622   2344   2300     -8   -105    -45       C
ATOM    248  O   ASP A  32     -27.496  -4.850  -4.517  1.00 20.42           O
ANISOU  248  O   ASP A  32     2470   2488   2799     37   -159      2       O
ATOM    249  CB  ASP A  32     -26.003  -4.166  -7.581  1.00 20.76           C
ANISOU  249  CB  ASP A  32     2763   2280   2843     12   -320     63       C
ATOM    250  CG  ASP A  32     -26.179  -3.867  -9.053  1.00 20.33           C
ANISOU  250  CG  ASP A  32     2583   2163   2980    409   -311   -140       C
ATOM    251  OD1 ASP A  32     -27.184  -4.416  -9.646  1.00 20.72           O
ANISOU  251  OD1 ASP A  32     2753   2683   2436     86   -148     67       O
ATOM    252  OD2 ASP A  32     -25.329  -3.166  -9.631  1.00 21.61           O
ANISOU  252  OD2 ASP A  32     2706   2678   2827    -97   -216     70       O
ATOM    253  N   THR A  33     -26.373  -6.580  -5.497  1.00 20.09           N
ANISOU  253  N   THR A  33     2599   2194   2840    231   -226    -12       N
ATOM    254  CA  THR A  33     -26.434  -7.370  -4.288  1.00 20.29           C
ANISOU  254  CA  THR A  33     2684   2461   2564    221   -125    268       C
ATOM    255  C   THR A  33     -25.102  -7.842  -3.701  1.00 21.07           C
ANISOU  255  C   THR A  33     2871   2370   2763    -34   -198    -34       C
ATOM    256  O   THR A  33     -25.072  -8.131  -2.503  1.00 22.97           O
ANISOU  256  O   THR A  33     2953   2993   2781    196    -95     90       O
ATOM    257  CB  THR A  33     -27.314  -8.597  -4.486  1.00 22.02           C
ANISOU  257  CB  THR A  33     2523   2662   3183     39     84     96       C
ATOM    258  OG1 THR A  33     -26.646  -9.533  -5.332  1.00 21.70           O
ANISOU  258  OG1 THR A  33     2797   2467   2981    206    -57    135       O
ATOM    259  CG2 THR A  33     -28.656  -8.276  -5.063  1.00 22.02           C
ANISOU  259  CG2 THR A  33     2459   2505   3402   -236   -102     62       C
ATOM    260  N   GLY A  34     -24.100  -8.073  -4.541  1.00 20.26           N
ANISOU  260  N   GLY A  34     2557   2320   2821     69   -281    159       N
ATOM    261  CA  GLY A  34     -22.973  -8.889  -4.137  1.00 20.04           C
ANISOU  261  CA  GLY A  34     2495   2477   2643    -49   -260     77       C
ATOM    262  C   GLY A  34     -23.058 -10.319  -4.658  1.00 20.20           C
ANISOU  262  C   GLY A  34     2408   2614   2654    -62   -222     62       C
ATOM    263  O   GLY A  34     -24.109 -10.770  -5.078  1.00 21.12           O
ANISOU  263  O   GLY A  34     2552   2634   2838    123   -401    154       O
ATOM    264  N   THR A  35     -21.932 -11.026  -4.644  1.00 20.52           N
ANISOU  264  N   THR A  35     2177   2621   2998    -47   -238     74       N
ATOM    265  CA  THR A  35     -21.877 -12.420  -5.045  1.00 20.45           C
ANISOU  265  CA  THR A  35     2582   2740   2447     61   -311    173       C
ATOM    266  C   THR A  35     -22.634 -13.339  -4.072  1.00 19.54           C
ANISOU  266  C   THR A  35     2279   2643   2502    263   -324    130       C
ATOM    267  O   THR A  35     -22.839 -13.001  -2.908  1.00 21.60           O
ANISOU  267  O   THR A  35     2707   2542   2959    337   -150    126       O
ATOM    268  CB  THR A  35     -20.410 -12.843  -5.117  1.00 21.50           C
ANISOU  268  CB  THR A  35     2623   2687   2860    418   -161    196       C
ATOM    269  OG1 THR A  35     -19.702 -12.355  -3.970  1.00 22.60           O
ANISOU  269  OG1 THR A  35     2674   3036   2878    205   -373     86       O
ATOM    270  CG2 THR A  35     -19.705 -12.396  -6.380  1.00 21.16           C
ANISOU  270  CG2 THR A  35     2484   2851   2705    106   -371    151       C
ATOM    271  N   ASN A  36     -22.943 -14.543  -4.551  1.00 21.25           N
ANISOU  271  N   ASN A  36     3096   2518   2459    217   -374    308       N
ATOM    272  CA  ASN A  36     -23.526 -15.580  -3.723  1.00 20.18           C
ANISOU  272  CA  ASN A  36     2682   2456   2529     -6   -398    207       C
ATOM    273  C   ASN A  36     -22.417 -16.213  -2.878  1.00 21.80           C
ANISOU  273  C   ASN A  36     2779   2436   3067    172   -423    254       C
ATOM    274  O   ASN A  36     -21.936 -17.303  -3.219  1.00 23.01           O
ANISOU  274  O   ASN A  36     2980   2594   3170    184   -507    233       O
ATOM    275  CB  ASN A  36     -24.213 -16.625  -4.570  1.00 21.37           C
ANISOU  275  CB  ASN A  36     2260   2668   3190    161   -592     84       C
ATOM    276  CG  ASN A  36     -25.075 -17.545  -3.764  1.00 24.11           C
ANISOU  276  CG  ASN A  36     2873   2790   3497   -145   -153    145       C
ATOM    277  OD1 ASN A  36     -25.145 -17.482  -2.535  1.00 25.24           O
ANISOU  277  OD1 ASN A  36     3212   2975   3404   -415   -318    -11       O
ATOM    278  ND2 ASN A  36     -25.763 -18.412  -4.486  1.00 29.96           N
ANISOU  278  ND2 ASN A  36     4302   3663   3418   -672   -504   -141       N
ATOM    279  N   THR A  37     -22.037 -15.522  -1.825  1.00 20.95           N
ANISOU  279  N   THR A  37     2999   2345   2616    293   -439    204       N
ATOM    280  CA  THR A  37     -21.051 -16.005  -0.873  1.00 19.79           C
ANISOU  280  CA  THR A  37     2439   2351   2730    227   -409    228       C
ATOM    281  C   THR A  37     -21.513 -15.684   0.536  1.00 20.75           C
ANISOU  281  C   THR A  37     2676   2592   2616    158   -447    -67       C
ATOM    282  O   THR A  37     -22.255 -14.729   0.739  1.00 21.78           O
ANISOU  282  O   THR A  37     2711   2595   2969    383   -329    128       O
ATOM    283  CB  THR A  37     -19.666 -15.413  -1.116  1.00 22.88           C
ANISOU  283  CB  THR A  37     2720   2730   3244    321   -285    545       C
ATOM    284  OG1 THR A  37     -19.692 -14.023  -0.800  1.00 23.72           O
ANISOU  284  OG1 THR A  37     3103   2564   3347    471     94    -41       O
ATOM    285  CG2 THR A  37     -19.142 -15.721  -2.507  1.00 22.12           C
ANISOU  285  CG2 THR A  37     2638   2608   3159    379   -153    336       C
ATOM    286  N   LYS A  38     -21.090 -16.506   1.503  1.00 22.22           N
ANISOU  286  N   LYS A  38     3045   2367   3030     28   -621    359       N
ATOM    287  CA  LYS A  38     -21.354 -16.213   2.914  1.00 21.67           C
ANISOU  287  CA  LYS A  38     2912   2358   2965     93   -374    318       C
ATOM    288  C   LYS A  38     -20.765 -14.850   3.271  1.00 21.15           C
ANISOU  288  C   LYS A  38     2803   2642   2591     37   -415    402       C
ATOM    289  O   LYS A  38     -21.373 -14.082   4.001  1.00 23.07           O
ANISOU  289  O   LYS A  38     3090   2647   3030     18   -160    -92       O
ATOM    290  CB  LYS A  38     -20.759 -17.334   3.766  1.00 23.92           C
ANISOU  290  CB  LYS A  38     2907   2938   3245   -200   -410    583       C
ATOM    291  CG  LYS A  38     -21.309 -18.727   3.440  1.00 24.67           C
ANISOU  291  CG  LYS A  38     3549   2607   3216   -105   -719    602       C
ATOM    292  CD  LYS A  38     -20.333 -19.848   3.957  1.00 30.42           C
ANISOU  292  CD  LYS A  38     4351   3046   4161   -464   -983    725       C
ATOM    293  CE  LYS A  38     -20.744 -21.139   3.439  1.00 31.72           C
ANISOU  293  CE  LYS A  38     4818   3301   3932    411   -958    612       C
ATOM    294  NZ  LYS A  38     -19.962 -22.329   3.743  1.00 32.36           N
ANISOU  294  NZ  LYS A  38     3139   4526   4629   -277   -496    146       N
ATOM    295  N   GLU A  39     -19.553 -14.568   2.766  1.00 22.26           N
ANISOU  295  N   GLU A  39     2993   2524   2941     72   -295    -66       N
ATOM    296  CA  GLU A  39     -18.870 -13.311   3.087  1.00 21.55           C
ANISOU  296  CA  GLU A  39     2764   2508   2914      3   -347    305       C
ATOM    297  C   GLU A  39     -19.683 -12.109   2.589  1.00 20.43           C
ANISOU  297  C   GLU A  39     2401   2494   2868      8    -10    278       C
ATOM    298  O   GLU A  39     -19.853 -11.168   3.342  1.00 22.83           O
ANISOU  298  O   GLU A  39     3153   2681   2838    186   -387    -16       O
ATOM    299  CB  GLU A  39     -17.495 -13.334   2.437  1.00 23.00           C
ANISOU  299  CB  GLU A  39     2600   2569   3569    159   -549      1       C
ATOM    300  CG  GLU A  39     -16.669 -12.084   2.671  1.00 23.89           C
ANISOU  300  CG  GLU A  39     3053   2343   3682    114   -482    202       C
ATOM    301  CD  GLU A  39     -15.358 -12.008   1.905  1.00 27.77           C
ANISOU  301  CD  GLU A  39     3247   3213   4091   -200   -613   -252       C
ATOM    302  OE1 GLU A  39     -14.482 -11.251   2.362  1.00 27.37           O
ANISOU  302  OE1 GLU A  39     2926   3683   3791   -373   -619    199       O
ATOM    303  OE2 GLU A  39     -15.258 -12.607   0.803  1.00 28.86           O
ANISOU  303  OE2 GLU A  39     2975   2852   5137   -387    252   -243       O
ATOM    304  N   SER A  40     -20.191 -12.175   1.350  1.00 20.29           N
ANISOU  304  N   SER A  40     2571   2564   2576    279   -169     27       N
ATOM    305  CA  SER A  40     -20.997 -11.083   0.838  1.00 19.48           C
ANISOU  305  CA  SER A  40     2445   2227   2730    249   -266    284       C
ATOM    306  C   SER A  40     -22.252 -10.914   1.693  1.00 20.89           C
ANISOU  306  C   SER A  40     3169   2262   2504     15   -163    104       C
ATOM    307  O   SER A  40     -22.652  -9.797   2.000  1.00 21.11           O
ANISOU  307  O   SER A  40     3016   2097   2909    101   -357    -17       O
ATOM    308  CB  SER A  40     -21.342 -11.268  -0.648  1.00 21.20           C
ANISOU  308  CB  SER A  40     3112   2436   2508    218   -426     98       C
ATOM    309  OG  SER A  40     -20.213 -11.303  -1.496  1.00 22.65           O
ANISOU  309  OG  SER A  40     2813   2952   2840    -23     12    -11       O
ATOM    310  N   ARG A  41     -22.940 -12.040   1.968  1.00 20.18           N
ANISOU  310  N   ARG A  41     2535   2470   2663    112   -130    -37       N
ATOM    311  CA  ARG A  41     -24.182 -11.981   2.704  1.00 20.42           C
ANISOU  311  CA  ARG A  41     2712   2314   2731    -55   -185    131       C
ATOM    312  C   ARG A  41     -23.979 -11.363   4.084  1.00 22.37           C
ANISOU  312  C   ARG A  41     2885   2729   2885    -47   -288    271       C
ATOM    313  O   ARG A  41     -24.740 -10.508   4.517  1.00 23.06           O
ANISOU  313  O   ARG A  41     3080   2830   2852    140   -403   -163       O
ATOM    314  CB  ARG A  41     -24.799 -13.380   2.792  1.00 21.04           C
ANISOU  314  CB  ARG A  41     2758   2483   2752   -152   -177     36       C
ATOM    315  CG  ARG A  41     -26.095 -13.348   3.560  1.00 23.10           C
ANISOU  315  CG  ARG A  41     2901   2947   2930     37    -11    -20       C
ATOM    316  CD  ARG A  41     -26.803 -14.673   3.508  1.00 26.88           C
ANISOU  316  CD  ARG A  41     3472   3277   3465   -260    223      3       C
ATOM    317  NE  ARG A  41     -28.077 -14.635   4.207  1.00 30.27           N
ANISOU  317  NE  ARG A  41     4005   3462   4034    -71    522    265       N
ATOM    318  CZ  ARG A  41     -28.980 -15.606   4.179  1.00 37.56           C
ANISOU  318  CZ  ARG A  41     4443   4030   5800   -789    965    -78       C
ATOM    319  NH1 ARG A  41     -28.672 -16.769   3.615  1.00 39.18           N
ANISOU  319  NH1 ARG A  41     4700   4388   5797   -433    892    -59       N
ATOM    320  NH2 ARG A  41     -30.138 -15.437   4.811  1.00 40.90           N
ANISOU  320  NH2 ARG A  41     4672   4347   6522   -598   1831     11       N
ATOM    321  N   LEU A  42     -22.944 -11.849   4.793  1.00 21.19           N
ANISOU  321  N   LEU A  42     2599   2934   2520     24   -420     44       N
ATOM    322  CA  LEU A  42     -22.674 -11.351   6.137  1.00 22.01           C
ANISOU  322  CA  LEU A  42     2725   2957   2680    158   -307    271       C
ATOM    323  C   LEU A  42     -22.398  -9.824   6.113  1.00 22.07           C
ANISOU  323  C   LEU A  42     2698   2810   2875     72   -417    156       C
ATOM    324  O   LEU A  42     -22.862  -9.052   6.983  1.00 24.30           O
ANISOU  324  O   LEU A  42     3337   3113   2785    116    -97    117       O
ATOM    325  CB  LEU A  42     -21.511 -12.146   6.754  1.00 22.53           C
ANISOU  325  CB  LEU A  42     3212   2793   2554    216   -542    152       C
ATOM    326  CG  LEU A  42     -21.922 -13.571   7.179  1.00 30.15           C
ANISOU  326  CG  LEU A  42     4648   3095   3710    471    480    543       C
ATOM    327  CD1 LEU A  42     -20.715 -14.465   7.683  1.00 31.26           C
ANISOU  327  CD1 LEU A  42     5076   3531   3271    650   -247    602       C
ATOM    328  CD2 LEU A  42     -23.256 -13.492   8.074  1.00 38.69           C
ANISOU  328  CD2 LEU A  42     5793   3953   4956    528    611    415       C
ATOM    329  N   ALA A  43     -21.651  -9.385   5.086  1.00 22.58           N
ANISOU  329  N   ALA A  43     3099   2649   2831      4   -172    208       N
ATOM    330  CA  ALA A  43     -21.320  -7.959   4.978  1.00 21.77           C
ANISOU  330  CA  ALA A  43     2999   2450   2821   -164   -401    -57       C
ATOM    331  C   ALA A  43     -22.602  -7.143   4.706  1.00 22.65           C
ANISOU  331  C   ALA A  43     2762   2936   2909   -115   -137      3       C
ATOM    332  O   ALA A  43     -22.795  -6.053   5.297  1.00 24.18           O
ANISOU  332  O   ALA A  43     3378   2769   3038   -151   -476   -208       O
ATOM    333  CB  ALA A  43     -20.260  -7.801   3.848  1.00 25.25           C
ANISOU  333  CB  ALA A  43     3387   2930   3278   -181   -242     -1       C
ATOM    334  N   LEU A  44     -23.450  -7.652   3.784  1.00 21.48           N
ANISOU  334  N   LEU A  44     2935   2367   2860     -4   -378    -67       N
ATOM    335  CA  LEU A  44     -24.682  -6.922   3.495  1.00 21.52           C
ANISOU  335  CA  LEU A  44     2788   2644   2744    -18   -411   -131       C
ATOM    336  C   LEU A  44     -25.539  -6.816   4.754  1.00 21.37           C
ANISOU  336  C   LEU A  44     2867   2601   2651   -171   -406    -73       C
ATOM    337  O   LEU A  44     -26.124  -5.781   5.056  1.00 23.06           O
ANISOU  337  O   LEU A  44     3416   2564   2780     42   -277    -89       O
ATOM    338  CB  LEU A  44     -25.389  -7.614   2.354  1.00 20.42           C
ANISOU  338  CB  LEU A  44     2566   2482   2708   -278   -206   -127       C
ATOM    339  CG  LEU A  44     -26.705  -7.004   1.925  1.00 22.15           C
ANISOU  339  CG  LEU A  44     2553   2696   3168    -47   -363     42       C
ATOM    340  CD1 LEU A  44     -26.525  -5.615   1.392  1.00 24.24           C
ANISOU  340  CD1 LEU A  44     2862   2610   3739    104   -524     73       C
ATOM    341  CD2 LEU A  44     -27.389  -7.893   0.861  1.00 23.23           C
ANISOU  341  CD2 LEU A  44     2604   2977   3245    120   -491   -159       C
ATOM    342  N   GLU A  45     -25.661  -7.938   5.452  1.00 22.08           N
ANISOU  342  N   GLU A  45     2850   2742   2795     52   -243    132       N
ATOM    343  CA  GLU A  45     -26.522  -7.958   6.631  1.00 22.45           C
ANISOU  343  CA  GLU A  45     2878   2754   2898    208     96    -79       C
ATOM    344  C   GLU A  45     -25.973  -6.991   7.680  1.00 22.13           C
ANISOU  344  C   GLU A  45     2997   2828   2583   -317   -364     63       C
ATOM    345  O   GLU A  45     -26.731  -6.295   8.340  1.00 25.20           O
ANISOU  345  O   GLU A  45     3252   3077   3247    120    -33   -569       O
ATOM    346  CB  GLU A  45     -26.693  -9.353   7.194  1.00 22.44           C
ANISOU  346  CB  GLU A  45     2805   2722   3000    282    117    -96       C
ATOM    347  CG  GLU A  45     -27.508 -10.256   6.273  1.00 25.79           C
ANISOU  347  CG  GLU A  45     3547   2981   3274   -158    -76     26       C
ATOM    348  CD  GLU A  45     -27.617 -11.716   6.695  1.00 29.62           C
ANISOU  348  CD  GLU A  45     3959   3672   3623   -181   -650    299       C
ATOM    349  OE1 GLU A  45     -28.454 -12.450   6.151  1.00 34.36           O
ANISOU  349  OE1 GLU A  45     3877   3919   5257   -766    322   -906       O
ATOM    350  OE2 GLU A  45     -26.750 -12.172   7.461  1.00 37.27           O
ANISOU  350  OE2 GLU A  45     5988   3711   4461    102   -589    638       O
ATOM    351  N   LYS A  46     -24.658  -6.999   7.862  1.00 23.64           N
ANISOU  351  N   LYS A  46     3514   2751   2719   -117   -248   -134       N
ATOM    352  CA  LYS A  46     -24.059  -6.140   8.892  1.00 25.00           C
ANISOU  352  CA  LYS A  46     3349   3267   2884   -139   -359   -272       C
ATOM    353  C   LYS A  46     -24.252  -4.664   8.558  1.00 24.24           C
ANISOU  353  C   LYS A  46     2982   2918   3309     73   -295    -97       C
ATOM    354  O   LYS A  46     -24.623  -3.878   9.435  1.00 26.65           O
ANISOU  354  O   LYS A  46     3690   3185   3250    284   -228   -336       O
ATOM    355  CB  LYS A  46     -22.565  -6.415   8.989  1.00 26.53           C
ANISOU  355  CB  LYS A  46     3302   3200   3578   -235   -166   -594       C
ATOM    356  CG  LYS A  46     -21.779  -5.568   9.999  1.00 34.43           C
ANISOU  356  CG  LYS A  46     4210   4544   4328   -615   -793  -1071       C
ATOM    357  CD  LYS A  46     -20.275  -5.859  10.033  1.00 38.89           C
ANISOU  357  CD  LYS A  46     4447   5606   4725    168   -917  -1381       C
ATOM    358  CE  LYS A  46     -19.577  -5.242  11.234  1.00 52.35           C
ANISOU  358  CE  LYS A  46     5770   7217   6901   -884  -1521  -1978       C
ATOM    359  NZ  LYS A  46     -18.175  -5.022  10.925  1.00 61.84           N
ANISOU  359  NZ  LYS A  46     5807   9068   8622   -333  -1954  -1425       N
ATOM    360  N   GLN A  47     -24.049  -4.319   7.287  1.00 23.16           N
ANISOU  360  N   GLN A  47     3176   2578   3044   -115   -263   -327       N
ATOM    361  CA  GLN A  47     -24.175  -2.911   6.881  1.00 22.84           C
ANISOU  361  CA  GLN A  47     3018   2334   3328   -151   -402   -193       C
ATOM    362  C   GLN A  47     -25.637  -2.456   6.901  1.00 26.21           C
ANISOU  362  C   GLN A  47     3421   3127   3412   -110   -398   -298       C
ATOM    363  O   GLN A  47     -25.955  -1.345   7.335  1.00 26.95           O
ANISOU  363  O   GLN A  47     3630   2695   3913   -329   -601   -478       O
ATOM    364  CB  GLN A  47     -23.482  -2.693   5.536  1.00 25.18           C
ANISOU  364  CB  GLN A  47     3369   2852   3344   -471   -218   -371       C
ATOM    365  CG  GLN A  47     -21.975  -2.842   5.623  1.00 27.19           C
ANISOU  365  CG  GLN A  47     3360   3177   3793   -745   -486    138       C
ATOM    366  CD  GLN A  47     -21.226  -2.558   4.338  1.00 27.85           C
ANISOU  366  CD  GLN A  47     3331   3521   3728  -1190   -703    326       C
ATOM    367  OE1 GLN A  47     -21.429  -1.527   3.680  1.00 32.44           O
ANISOU  367  OE1 GLN A  47     4029   4426   3872   -854  -1211    928       O
ATOM    368  NE2 GLN A  47     -20.394  -3.491   3.916  1.00 29.57           N
ANISOU  368  NE2 GLN A  47     4157   3771   3306   -730   -123    -80       N
ATOM    369  N   LEU A  48     -26.547  -3.350   6.512  1.00 23.56           N
ANISOU  369  N   LEU A  48     3416   2642   2892     22   -177   -463       N
ATOM    370  CA  LEU A  48     -27.961  -3.022   6.630  1.00 23.56           C
ANISOU  370  CA  LEU A  48     3249   2766   2935    168   -383   -515       C
ATOM    371  C   LEU A  48     -28.330  -2.802   8.102  1.00 24.15           C
ANISOU  371  C   LEU A  48     3555   3032   2589    178   -402   -406       C
ATOM    372  O   LEU A  48     -29.108  -1.900   8.432  1.00 26.37           O
ANISOU  372  O   LEU A  48     3692   2846   3479    -41   -129   -702       O
ATOM    373  CB  LEU A  48     -28.813  -4.142   6.054  1.00 23.74           C
ANISOU  373  CB  LEU A  48     3055   2719   3244     61   -410   -717       C
ATOM    374  CG  LEU A  48     -28.899  -4.162   4.513  1.00 23.07           C
ANISOU  374  CG  LEU A  48     2959   2909   2897     25   -598   -639       C
ATOM    375  CD1 LEU A  48     -29.596  -5.434   4.114  1.00 23.63           C
ANISOU  375  CD1 LEU A  48     2946   2743   3288    184   -388   -295       C
ATOM    376  CD2 LEU A  48     -29.582  -2.954   3.972  1.00 24.44           C
ANISOU  376  CD2 LEU A  48     2628   3579   3079     93   -431   -144       C
ATOM    377  N   ALA A  49     -27.831  -3.684   8.974  1.00 24.25           N
ANISOU  377  N   ALA A  49     3375   2799   3040    233   -259   -545       N
ATOM    378  CA  ALA A  49     -28.172  -3.577  10.397  1.00 26.36           C
ANISOU  378  CA  ALA A  49     3453   3258   3306    137   -309   -539       C
ATOM    379  C   ALA A  49     -27.729  -2.241  10.982  1.00 27.15           C
ANISOU  379  C   ALA A  49     4019   3104   3192    269   -159   -648       C
ATOM    380  O   ALA A  49     -28.415  -1.645  11.848  1.00 30.52           O
ANISOU  380  O   ALA A  49     4344   3396   3858    -12    187  -1081       O
ATOM    381  CB  ALA A  49     -27.596  -4.731  11.168  1.00 28.94           C
ANISOU  381  CB  ALA A  49     4485   3751   2761     82   -232   -617       C
ATOM    382  N   ALA A  50     -26.568  -1.770  10.553  1.00 26.11           N
ANISOU  382  N   ALA A  50     3705   2961   3255    311   -400   -766       N
ATOM    383  CA  ALA A  50     -26.097  -0.504  11.063  1.00 28.33           C
ANISOU  383  CA  ALA A  50     4267   2959   3539    375   -531  -1126       C
ATOM    384  C   ALA A  50     -27.015   0.649  10.643  1.00 28.24           C
ANISOU  384  C   ALA A  50     3946   2883   3901     -8   -263   -631       C
ATOM    385  O   ALA A  50     -27.003   1.700  11.315  1.00 30.46           O
ANISOU  385  O   ALA A  50     4045   3318   4212     45   -450  -1164       O
ATOM    386  CB  ALA A  50     -24.670  -0.280  10.642  1.00 31.04           C
ANISOU  386  CB  ALA A  50     3697   3642   4456    741   -536  -1380       C
ATOM    387  N   LEU A  51     -27.719   0.460   9.524  1.00 29.04           N
ANISOU  387  N   LEU A  51     4290   3147   3595    212   -538  -1181       N
ATOM    388  CA  LEU A  51     -28.692   1.421   9.014  1.00 29.23           C
ANISOU  388  CA  LEU A  51     4121   3161   3824    171   -436   -752       C
ATOM    389  C   LEU A  51     -30.085   1.177   9.608  1.00 28.93           C
ANISOU  389  C   LEU A  51     4149   3670   3174    102   -613  -1023       C
ATOM    390  O   LEU A  51     -31.029   1.928   9.304  1.00 31.79           O
ANISOU  390  O   LEU A  51     3814   4789   3478    570   -585  -1200       O
ATOM    391  CB  LEU A  51     -28.719   1.398   7.486  1.00 28.22           C
ANISOU  391  CB  LEU A  51     3843   2908   3969    238   -373   -648       C
ATOM    392  CG  LEU A  51     -27.433   1.850   6.764  1.00 30.50           C
ANISOU  392  CG  LEU A  51     3646   3320   4622    597   -457   -537       C
ATOM    393  CD1 LEU A  51     -27.330   1.513   5.273  1.00 33.39           C
ANISOU  393  CD1 LEU A  51     4289   3718   4678    616   -438    174       C
ATOM    394  CD2 LEU A  51     -27.278   3.360   6.922  1.00 39.30           C
ANISOU  394  CD2 LEU A  51     4974   3861   6098     96     18   -674       C
ATOM    395  N   GLY A  52     -30.206   0.154  10.452  1.00 27.30           N
ANISOU  395  N   GLY A  52     3750   2979   3645     97     22  -1004       N
ATOM    396  CA  GLY A  52     -31.439  -0.178  11.131  1.00 29.09           C
ANISOU  396  CA  GLY A  52     3973   3294   3787   -107    203   -828       C
ATOM    397  C   GLY A  52     -32.377  -1.077  10.354  1.00 27.05           C
ANISOU  397  C   GLY A  52     3457   3831   2990    170    -16   -747       C
ATOM    398  O   GLY A  52     -33.565  -1.144  10.695  1.00 27.63           O
ANISOU  398  O   GLY A  52     3675   3358   3465   -304    119   -892       O
ATOM    399  N   TYR A  53     -31.821  -1.812   9.366  1.00 23.87           N
ANISOU  399  N   TYR A  53     3107   3088   2875    268     19   -472       N
ATOM    400  CA  TYR A  53     -32.645  -2.630   8.499  1.00 23.83           C
ANISOU  400  CA  TYR A  53     3163   3250   2642    -40   -118   -118       C
ATOM    401  C   TYR A  53     -32.204  -4.081   8.501  1.00 24.65           C
ANISOU  401  C   TYR A  53     3254   3382   2729     15   -206    119       C
ATOM    402  O   TYR A  53     -31.045  -4.411   8.826  1.00 26.14           O
ANISOU  402  O   TYR A  53     3743   2957   3231     39   -509   -259       O
ATOM    403  CB  TYR A  53     -32.572  -2.154   7.041  1.00 26.33           C
ANISOU  403  CB  TYR A  53     3749   3284   2973     24   -145   -302       C
ATOM    404  CG  TYR A  53     -33.071  -0.742   6.832  1.00 24.73           C
ANISOU  404  CG  TYR A  53     3499   3082   2814   -125   -338   -388       C
ATOM    405  CD1 TYR A  53     -34.391  -0.423   7.052  1.00 25.98           C
ANISOU  405  CD1 TYR A  53     3331   3311   3230   -340   -145   -505       C
ATOM    406  CD2 TYR A  53     -32.219   0.259   6.401  1.00 26.49           C
ANISOU  406  CD2 TYR A  53     3709   3282   3074    -82    -30   -276       C
ATOM    407  CE1 TYR A  53     -34.868   0.847   6.795  1.00 29.28           C
ANISOU  407  CE1 TYR A  53     4076   3623   3428   -156   -180   -107       C
ATOM    408  CE2 TYR A  53     -32.680   1.522   6.179  1.00 28.82           C
ANISOU  408  CE2 TYR A  53     4379   3159   3411   -322   -284   -368       C
ATOM    409  CZ  TYR A  53     -34.003   1.822   6.366  1.00 27.31           C
ANISOU  409  CZ  TYR A  53     3955   3620   2800      6    -51   -316       C
ATOM    410  OH  TYR A  53     -34.431   3.098   6.150  1.00 32.32           O
ANISOU  410  OH  TYR A  53     5234   3238   3807    542   -840   -244       O
ATOM    411  N   LYS A  54     -33.150  -4.947   8.170  1.00 25.05           N
ANISOU  411  N   LYS A  54     3379   3157   2982     73   -106   -386       N
ATOM    412  CA  LYS A  54     -32.872  -6.349   7.910  1.00 26.16           C
ANISOU  412  CA  LYS A  54     4050   2882   3006   -201   -188   -182       C
ATOM    413  C   LYS A  54     -33.108  -6.576   6.415  1.00 24.79           C
ANISOU  413  C   LYS A  54     3690   2738   2989   -251    126   -129       C
ATOM    414  O   LYS A  54     -33.815  -5.791   5.768  1.00 24.26           O
ANISOU  414  O   LYS A  54     3433   2854   2931   -147    -70   -336       O
ATOM    415  CB  LYS A  54     -33.808  -7.242   8.725  1.00 28.36           C
ANISOU  415  CB  LYS A  54     4694   3345   2735   -292    106   -247       C
ATOM    416  CG  LYS A  54     -33.650  -7.221  10.255  1.00 33.85           C
ANISOU  416  CG  LYS A  54     5561   4159   3143   -898    735   -267       C
ATOM    417  CD  LYS A  54     -34.724  -8.097  10.912  1.00 42.07           C
ANISOU  417  CD  LYS A  54     6387   5104   4493  -1389    881     67       C
ATOM    418  N   VAL A  55     -32.532  -7.658   5.881  1.00 25.54           N
ANISOU  418  N   VAL A  55     3955   2768   2979   -137     10   -116       N
ATOM    419  CA  VAL A  55     -32.777  -8.038   4.499  1.00 24.89           C
ANISOU  419  CA  VAL A  55     3824   2773   2859   -284    239   -202       C
ATOM    420  C   VAL A  55     -34.276  -8.031   4.168  1.00 24.44           C
ANISOU  420  C   VAL A  55     3697   2561   3028   -255    189   -365       C
ATOM    421  O   VAL A  55     -34.663  -7.592   3.086  1.00 24.79           O
ANISOU  421  O   VAL A  55     3457   3056   2906   -367    104   -169       O
ATOM    422  CB  VAL A  55     -32.098  -9.373   4.185  1.00 26.70           C
ANISOU  422  CB  VAL A  55     4290   2752   3101   -330    -60   -421       C
ATOM    423  CG1 VAL A  55     -32.606  -9.982   2.876  1.00 27.76           C
ANISOU  423  CG1 VAL A  55     4473   2918   3155    111   -190   -292       C
ATOM    424  CG2 VAL A  55     -30.583  -9.221   4.117  1.00 28.46           C
ANISOU  424  CG2 VAL A  55     3999   3174   3639   -143    -91   -479       C
ATOM    425  N   GLU A  56     -35.116  -8.557   5.069  1.00 25.68           N
ANISOU  425  N   GLU A  56     3673   3040   3046   -528     54   -207       N
ATOM    426  CA  GLU A  56     -36.550  -8.686   4.818  1.00 25.62           C
ANISOU  426  CA  GLU A  56     3340   3489   2906   -166      0    -51       C
ATOM    427  C   GLU A  56     -37.240  -7.322   4.650  1.00 26.11           C
ANISOU  427  C   GLU A  56     3784   3494   2643   -356    175   -181       C
ATOM    428  O   GLU A  56     -38.372  -7.260   4.150  1.00 29.76           O
ANISOU  428  O   GLU A  56     3873   3947   3488   -955   -208     54       O
ATOM    429  CB  GLU A  56     -37.217  -9.502   5.915  1.00 31.99           C
ANISOU  429  CB  GLU A  56     3702   4770   3683   -717    242    165       C
ATOM    430  CG  GLU A  56     -37.138  -8.884   7.299  1.00 39.24           C
ANISOU  430  CG  GLU A  56     5198   5535   4175   -718   1131    331       C
ATOM    431  CD  GLU A  56     -37.432  -9.806   8.486  1.00 53.62           C
ANISOU  431  CD  GLU A  56     7306   7080   5988      3   1255   1762       C
ATOM    432  OE1 GLU A  56     -36.609 -10.641   8.952  1.00 62.94           O
ANISOU  432  OE1 GLU A  56     9172   8331   6410    -74   1519   2797       O
ATOM    433  OE2 GLU A  56     -38.553  -9.640   8.945  1.00 58.12           O
ANISOU  433  OE2 GLU A  56     6306   8698   7077   -892   2385   3979       O
ATOM    434  N   ASP A  57     -36.581  -6.223   5.039  1.00 25.15           N
ANISOU  434  N   ASP A  57     3292   3464   2800   -559     88   -257       N
ATOM    435  CA  ASP A  57     -37.174  -4.890   4.883  1.00 24.39           C
ANISOU  435  CA  ASP A  57     3183   3365   2720   -232    303   -130       C
ATOM    436  C   ASP A  57     -37.084  -4.373   3.441  1.00 23.97           C
ANISOU  436  C   ASP A  57     3249   2993   2867   -343   -207   -245       C
ATOM    437  O   ASP A  57     -37.778  -3.432   3.079  1.00 25.26           O
ANISOU  437  O   ASP A  57     3202   3458   2937      2     56   -127       O
ATOM    438  CB  ASP A  57     -36.501  -3.886   5.800  1.00 25.87           C
ANISOU  438  CB  ASP A  57     3270   3728   2831   -260     26   -256       C
ATOM    439  CG  ASP A  57     -36.665  -4.159   7.295  1.00 25.60           C
ANISOU  439  CG  ASP A  57     3295   3307   3125   -104     49   -191       C
ATOM    440  OD1 ASP A  57     -37.754  -4.623   7.693  1.00 31.11           O
ANISOU  440  OD1 ASP A  57     3685   4720   3417   -786    433   -507       O
ATOM    441  OD2 ASP A  57     -35.743  -3.845   8.068  1.00 28.42           O
ANISOU  441  OD2 ASP A  57     3659   3980   3157    455   -317   -607       O
ATOM    442  N   ILE A  58     -36.204  -4.969   2.627  1.00 23.36           N
ANISOU  442  N   ILE A  58     3036   3004   2836   -264   -247   -133       N
ATOM    443  CA  ILE A  58     -36.017  -4.519   1.258  1.00 23.06           C
ANISOU  443  CA  ILE A  58     2690   3299   2775   -330      4   -297       C
ATOM    444  C   ILE A  58     -37.224  -4.998   0.441  1.00 23.37           C
ANISOU  444  C   ILE A  58     3031   3270   2580   -155     -8   -293       C
ATOM    445  O   ILE A  58     -37.479  -6.188   0.348  1.00 24.54           O
ANISOU  445  O   ILE A  58     3135   3066   3122   -189     30   -247       O
ATOM    446  CB  ILE A  58     -34.674  -5.024   0.706  1.00 24.11           C
ANISOU  446  CB  ILE A  58     2878   3481   2802   -247    -16   -209       C
ATOM    447  CG1 ILE A  58     -33.510  -4.343   1.509  1.00 25.03           C
ANISOU  447  CG1 ILE A  58     3203   3616   2689     67   -299    209       C
ATOM    448  CG2 ILE A  58     -34.581  -4.735  -0.789  1.00 23.69           C
ANISOU  448  CG2 ILE A  58     2782   3513   2705   -573    -40      8       C
ATOM    449  CD1 ILE A  58     -32.158  -4.946   1.288  1.00 25.06           C
ANISOU  449  CD1 ILE A  58     3361   3197   2964    182   -273   -226       C
ATOM    450  N   GLU A  59     -37.914  -4.055  -0.214  1.00 23.85           N
ANISOU  450  N   GLU A  59     3073   3153   2837    121     56    -31       N
ATOM    451  CA  GLU A  59     -39.116  -4.362  -0.962  1.00 24.77           C
ANISOU  451  CA  GLU A  59     3162   3657   2594     80    158   -343       C
ATOM    452  C   GLU A  59     -38.871  -4.470  -2.458  1.00 23.53           C
ANISOU  452  C   GLU A  59     2790   3210   2940    208    262   -232       C
ATOM    453  O   GLU A  59     -39.718  -5.054  -3.154  1.00 24.26           O
ANISOU  453  O   GLU A  59     2821   3228   3167     73     94   -294       O
ATOM    454  CB  GLU A  59     -40.095  -3.246  -0.619  1.00 28.23           C
ANISOU  454  CB  GLU A  59     3812   4179   2735    622    100   -151       C
ATOM    455  CG  GLU A  59     -41.381  -3.173  -1.423  1.00 36.55           C
ANISOU  455  CG  GLU A  59     4291   6096   3498    764    201   -394       C
ATOM    456  CD  GLU A  59     -41.337  -2.303  -2.684  1.00 41.38           C
ANISOU  456  CD  GLU A  59     5348   6179   4194    507   -114    182       C
ATOM    457  OE1 GLU A  59     -42.398  -2.434  -3.383  1.00 44.10           O
ANISOU  457  OE1 GLU A  59     4456   7273   5027    133   -241    384       O
ATOM    458  OE2 GLU A  59     -40.322  -1.531  -3.005  1.00 43.70           O
ANISOU  458  OE2 GLU A  59     7480   4611   4513   1795   1686    651       O
ATOM    459  N   THR A  60     -37.792  -3.842  -2.971  1.00 22.49           N
ANISOU  459  N   THR A  60     2732   3162   2650    -20     54   -261       N
ATOM    460  CA  THR A  60     -37.448  -3.951  -4.381  1.00 22.58           C
ANISOU  460  CA  THR A  60     2276   3113   3189     -3     68    -48       C
ATOM    461  C   THR A  60     -35.937  -4.132  -4.473  1.00 22.79           C
ANISOU  461  C   THR A  60     2625   3291   2743    -70    105     52       C
ATOM    462  O   THR A  60     -35.180  -3.421  -3.804  1.00 22.41           O
ANISOU  462  O   THR A  60     2790   3003   2720   -116    -20   -241       O
ATOM    463  CB  THR A  60     -37.911  -2.719  -5.174  1.00 25.02           C
ANISOU  463  CB  THR A  60     3104   3557   2846   -225     38    108       C
ATOM    464  OG1 THR A  60     -39.324  -2.621  -5.178  1.00 25.85           O
ANISOU  464  OG1 THR A  60     2807   3465   3549    240    183    159       O
ATOM    465  CG2 THR A  60     -37.388  -2.691  -6.607  1.00 24.57           C
ANISOU  465  CG2 THR A  60     2976   3213   3146   -219    -93     54       C
ATOM    466  N   VAL A  61     -35.516  -5.040  -5.345  1.00 22.06           N
ANISOU  466  N   VAL A  61     2470   3094   2817   -237    -93   -199       N
ATOM    467  CA  VAL A  61     -34.115  -5.171  -5.740  1.00 20.20           C
ANISOU  467  CA  VAL A  61     2612   2635   2426     23   -107      4       C
ATOM    468  C   VAL A  61     -34.069  -4.888  -7.241  1.00 21.72           C
ANISOU  468  C   VAL A  61     2453   2821   2977    138     58   -140       C
ATOM    469  O   VAL A  61     -34.807  -5.498  -8.003  1.00 22.41           O
ANISOU  469  O   VAL A  61     2791   2988   2735    -67   -248   -118       O
ATOM    470  CB  VAL A  61     -33.494  -6.532  -5.404  1.00 21.50           C
ANISOU  470  CB  VAL A  61     2665   2528   2978   -169   -131   -111       C
ATOM    471  CG1 VAL A  61     -32.069  -6.669  -5.945  1.00 23.31           C
ANISOU  471  CG1 VAL A  61     2706   2997   3155    138   -321   -127       C
ATOM    472  CG2 VAL A  61     -33.520  -6.756  -3.913  1.00 21.63           C
ANISOU  472  CG2 VAL A  61     2758   2653   2809   -134   -283     72       C
ATOM    473  N   VAL A  62     -33.174  -3.991  -7.651  1.00 20.54           N
ANISOU  473  N   VAL A  62     2327   2667   2810   -135    -34   -221       N
ATOM    474  CA  VAL A  62     -32.909  -3.688  -9.053  1.00 20.27           C
ANISOU  474  CA  VAL A  62     2277   2649   2776    174    -12   -237       C
ATOM    475  C   VAL A  62     -31.524  -4.241  -9.420  1.00 20.28           C
ANISOU  475  C   VAL A  62     2363   2757   2584    139    105     58       C
ATOM    476  O   VAL A  62     -30.574  -4.015  -8.663  1.00 21.27           O
ANISOU  476  O   VAL A  62     2546   2785   2751    -51     39   -170       O
ATOM    477  CB  VAL A  62     -32.964  -2.186  -9.339  1.00 21.58           C
ANISOU  477  CB  VAL A  62     2584   2881   2736     -6    -97   -151       C
ATOM    478  CG1 VAL A  62     -32.719  -1.898 -10.824  1.00 23.74           C
ANISOU  478  CG1 VAL A  62     2866   2952   3200     15     -9     67       C
ATOM    479  CG2 VAL A  62     -34.289  -1.582  -8.861  1.00 23.51           C
ANISOU  479  CG2 VAL A  62     2874   3308   2749    134    211      6       C
ATOM    480  N   LEU A  63     -31.420  -4.921 -10.564  1.00 19.64           N
ANISOU  480  N   LEU A  63     2283   2672   2508    -23    -82     87       N
ATOM    481  CA  LEU A  63     -30.147  -5.408 -11.053  1.00 20.17           C
ANISOU  481  CA  LEU A  63     2352   2503   2807     98   -159    -51       C
ATOM    482  C   LEU A  63     -29.688  -4.510 -12.199  1.00 20.82           C
ANISOU  482  C   LEU A  63     2471   2676   2765    126   -154   -119       C
ATOM    483  O   LEU A  63     -30.419  -4.345 -13.186  1.00 21.21           O
ANISOU  483  O   LEU A  63     2374   2958   2727   -123   -281     59       O
ATOM    484  CB  LEU A  63     -30.320  -6.806 -11.635  1.00 24.20           C
ANISOU  484  CB  LEU A  63     2750   2964   3481     91   -485   -142       C
ATOM    485  CG  LEU A  63     -30.826  -7.903 -10.738  1.00 26.15           C
ANISOU  485  CG  LEU A  63     3692   2550   3693     87   -235     61       C
ATOM    486  CD1 LEU A  63     -30.816  -9.140 -11.644  1.00 27.73           C
ANISOU  486  CD1 LEU A  63     3518   3008   4009     24   -761    -34       C
ATOM    487  CD2 LEU A  63     -29.911  -8.019  -9.524  1.00 28.50           C
ANISOU  487  CD2 LEU A  63     3588   3115   4126   -175   -680    602       C
ATOM    488  N   THR A  64     -28.465  -3.975 -12.108  1.00 21.21           N
ANISOU  488  N   THR A  64     2661   2675   2722     27   -566     48       N
ATOM    489  CA  THR A  64     -27.892  -3.306 -13.248  1.00 20.29           C
ANISOU  489  CA  THR A  64     2401   2389   2918    -14    -76    218       C
ATOM    490  C   THR A  64     -27.546  -4.285 -14.358  1.00 19.05           C
ANISOU  490  C   THR A  64     2111   2311   2815    161   -349    249       C
ATOM    491  O   THR A  64     -27.606  -3.920 -15.539  1.00 20.60           O
ANISOU  491  O   THR A  64     2455   2540   2831    162   -264    187       O
ATOM    492  CB  THR A  64     -26.672  -2.447 -12.892  1.00 20.31           C
ANISOU  492  CB  THR A  64     2394   2334   2990     88   -196     35       C
ATOM    493  OG1 THR A  64     -25.636  -3.287 -12.339  1.00 20.56           O
ANISOU  493  OG1 THR A  64     2402   2593   2818   -181   -116    150       O
ATOM    494  CG2 THR A  64     -27.023  -1.327 -11.937  1.00 21.96           C
ANISOU  494  CG2 THR A  64     2889   2509   2944     75   -124     31       C
ATOM    495  N   HIS A  65     -27.149  -5.506 -13.988  1.00 19.03           N
ANISOU  495  N   HIS A  65     2357   2404   2470    276   -327     95       N
ATOM    496  CA  HIS A  65     -26.816  -6.541 -14.956  1.00 19.75           C
ANISOU  496  CA  HIS A  65     2588   2314   2601    163   -156    240       C
ATOM    497  C   HIS A  65     -26.654  -7.901 -14.260  1.00 19.02           C
ANISOU  497  C   HIS A  65     2449   2296   2481    154    -72    257       C
ATOM    498  O   HIS A  65     -26.728  -7.985 -13.052  1.00 20.41           O
ANISOU  498  O   HIS A  65     2657   2495   2601     41    -91    -47       O
ATOM    499  CB  HIS A  65     -25.574  -6.141 -15.775  1.00 19.77           C
ANISOU  499  CB  HIS A  65     2513   2301   2699     34   -218    196       C
ATOM    500  CG  HIS A  65     -24.289  -5.990 -15.037  1.00 20.11           C
ANISOU  500  CG  HIS A  65     2389   2565   2687     78   -127    222       C
ATOM    501  ND1 HIS A  65     -24.098  -5.100 -14.002  1.00 21.24           N
ANISOU  501  ND1 HIS A  65     2706   2787   2576    -52   -373     78       N
ATOM    502  CD2 HIS A  65     -23.084  -6.582 -15.271  1.00 20.76           C
ANISOU  502  CD2 HIS A  65     2764   2594   2529    402   -283    127       C
ATOM    503  CE1 HIS A  65     -22.823  -5.117 -13.662  1.00 21.96           C
ANISOU  503  CE1 HIS A  65     2657   2678   3007    -31   -183   -169       C
ATOM    504  NE2 HIS A  65     -22.187  -6.005 -14.416  1.00 21.39           N
ANISOU  504  NE2 HIS A  65     2294   2965   2869    201   -541    -45       N
ATOM    505  N   HIS A  66     -26.429  -8.953 -15.069  1.00 19.30           N
ANISOU  505  N   HIS A  66     2149   2568   2615    221    -58    -72       N
ATOM    506  CA  HIS A  66     -26.497 -10.330 -14.583  1.00 19.38           C
ANISOU  506  CA  HIS A  66     2296   2443   2623      9     -5   -103       C
ATOM    507  C   HIS A  66     -25.191 -10.849 -13.968  1.00 19.26           C
ANISOU  507  C   HIS A  66     2326   2380   2612    -49   -404   -182       C
ATOM    508  O   HIS A  66     -25.161 -11.957 -13.466  1.00 21.18           O
ANISOU  508  O   HIS A  66     2691   2479   2875     13   -220    -79       O
ATOM    509  CB  HIS A  66     -26.847 -11.258 -15.733  1.00 20.71           C
ANISOU  509  CB  HIS A  66     2556   2639   2674    116   -453      8       C
ATOM    510  CG  HIS A  66     -25.759 -11.435 -16.750  1.00 20.35           C
ANISOU  510  CG  HIS A  66     2297   2764   2671     33   -140   -251       C
ATOM    511  ND1 HIS A  66     -25.653 -10.666 -17.876  1.00 21.70           N
ANISOU  511  ND1 HIS A  66     2871   2696   2677     92   -408    -88       N
ATOM    512  CD2 HIS A  66     -24.766 -12.355 -16.826  1.00 22.12           C
ANISOU  512  CD2 HIS A  66     2726   2578   3100    118   -435   -144       C
ATOM    513  CE1 HIS A  66     -24.627 -11.060 -18.594  1.00 22.05           C
ANISOU  513  CE1 HIS A  66     3089   2196   3091     58   -312     21       C
ATOM    514  NE2 HIS A  66     -24.063 -12.084 -17.964  1.00 21.89           N
ANISOU  514  NE2 HIS A  66     2938   2831   2547    -17    -82    -89       N
ATOM    515  N   HIS A  67     -24.115 -10.038 -14.021  1.00 19.49           N
ANISOU  515  N   HIS A  67     2549   2520   2335     55   -253    191       N
ATOM    516  CA  HIS A  67     -22.855 -10.530 -13.484  1.00 19.21           C
ANISOU  516  CA  HIS A  67     2370   2334   2595    104   -183    185       C
ATOM    517  C   HIS A  67     -23.038 -10.871 -11.992  1.00 19.58           C
ANISOU  517  C   HIS A  67     2367   2641   2430   -140   -110    190       C
ATOM    518  O   HIS A  67     -23.784 -10.229 -11.289  1.00 20.55           O
ANISOU  518  O   HIS A  67     2555   2964   2289   -113   -309     66       O
ATOM    519  CB  HIS A  67     -21.746  -9.518 -13.693  1.00 19.36           C
ANISOU  519  CB  HIS A  67     2015   2720   2621     25   -150    147       C
ATOM    520  CG  HIS A  67     -21.354  -9.312 -15.118  1.00 20.45           C
ANISOU  520  CG  HIS A  67     2490   2567   2713    155    -32    180       C
ATOM    521  ND1 HIS A  67     -20.530  -8.322 -15.569  1.00 21.22           N
ANISOU  521  ND1 HIS A  67     2255   2822   2985   -177   -269    117       N
ATOM    522  CD2 HIS A  67     -21.667 -10.068 -16.211  1.00 21.57           C
ANISOU  522  CD2 HIS A  67     2226   3131   2838     38    -85    227       C
ATOM    523  CE1 HIS A  67     -20.344  -8.479 -16.871  1.00 22.34           C
ANISOU  523  CE1 HIS A  67     2650   2834   3005   -100    135     53       C
ATOM    524  NE2 HIS A  67     -21.042  -9.543 -17.305  1.00 21.40           N
ANISOU  524  NE2 HIS A  67     2394   2698   3039    257     33    318       N
ATOM    525  N   ALA A  68     -22.360 -11.933 -11.559  1.00 20.05           N
ANISOU  525  N   ALA A  68     2384   2364   2868    273   -189     59       N
ATOM    526  CA  ALA A  68     -22.594 -12.520 -10.248  1.00 20.88           C
ANISOU  526  CA  ALA A  68     2618   2420   2895    105    -53    204       C
ATOM    527  C   ALA A  68     -22.389 -11.567  -9.072  1.00 18.66           C
ANISOU  527  C   ALA A  68     2246   2008   2835    122   -253     52       C
ATOM    528  O   ALA A  68     -23.056 -11.705  -8.029  1.00 21.33           O
ANISOU  528  O   ALA A  68     2505   2741   2859    -20   -229     71       O
ATOM    529  CB  ALA A  68     -21.713 -13.739 -10.060  1.00 21.92           C
ANISOU  529  CB  ALA A  68     2974   2178   3175     65   -242    -46       C
ATOM    530  N   ASP A  69     -21.459 -10.598  -9.249  1.00 19.76           N
ANISOU  530  N   ASP A  69     2354   2657   2498    -58    -71    113       N
ATOM    531  CA  ASP A  69     -21.247  -9.614  -8.206  1.00 19.21           C
ANISOU  531  CA  ASP A  69     2323   2460   2516     60   -172    -22       C
ATOM    532  C   ASP A  69     -22.447  -8.668  -7.989  1.00 19.52           C
ANISOU  532  C   ASP A  69     2367   2185   2866     85    -92    120       C
ATOM    533  O   ASP A  69     -22.531  -8.023  -6.943  1.00 20.87           O
ANISOU  533  O   ASP A  69     2482   2580   2868   -155   -392     62       O
ATOM    534  CB  ASP A  69     -19.934  -8.873  -8.401  1.00 19.58           C
ANISOU  534  CB  ASP A  69     2483   2543   2412   -297   -188   -103       C
ATOM    535  CG  ASP A  69     -19.607  -8.377  -9.818  1.00 20.72           C
ANISOU  535  CG  ASP A  69     2273   2869   2732    268   -163    740       C
ATOM    536  OD1 ASP A  69     -19.887  -8.958 -10.944  1.00 23.44           O
ANISOU  536  OD1 ASP A  69     2840   3135   2929    -27   -136   -169       O
ATOM    537  OD2 ASP A  69     -19.054  -7.226  -9.904  1.00 22.82           O
ANISOU  537  OD2 ASP A  69     2704   2504   3461   -164   -373    257       O
ATOM    538  N   HIS A  70     -23.350  -8.620  -8.966  1.00 19.37           N
ANISOU  538  N   HIS A  70     2650   2282   2430   -272    -37    -27       N
ATOM    539  CA  HIS A  70     -24.501  -7.737  -8.912  1.00 19.82           C
ANISOU  539  CA  HIS A  70     2598   2361   2571     33   -182    118       C
ATOM    540  C   HIS A  70     -25.817  -8.445  -8.571  1.00 19.41           C
ANISOU  540  C   HIS A  70     2447   2633   2296    -89   -172    265       C
ATOM    541  O   HIS A  70     -26.726  -7.793  -8.089  1.00 21.71           O
ANISOU  541  O   HIS A  70     2579   2771   2899    144    213   -107       O
ATOM    542  CB  HIS A  70     -24.570  -6.901 -10.181  1.00 19.46           C
ANISOU  542  CB  HIS A  70     2233   2435   2725   -118   -142    274       C
ATOM    543  CG  HIS A  70     -23.327  -6.113 -10.422  1.00 20.85           C
ANISOU  543  CG  HIS A  70     2498   2446   2977     28    -56    306       C
ATOM    544  ND1 HIS A  70     -23.192  -4.792 -10.092  1.00 20.73           N
ANISOU  544  ND1 HIS A  70     2548   2568   2760   -249      2    239       N
ATOM    545  CD2 HIS A  70     -22.131  -6.521 -10.854  1.00 19.81           C
ANISOU  545  CD2 HIS A  70     2605   2298   2625    -66     48    308       C
ATOM    546  CE1 HIS A  70     -21.940  -4.410 -10.329  1.00 20.02           C
ANISOU  546  CE1 HIS A  70     2341   2248   3016   -278   -164     16       C
ATOM    547  NE2 HIS A  70     -21.279  -5.448 -10.798  1.00 20.78           N
ANISOU  547  NE2 HIS A  70     2551   2440   2906     34   -101    155       N
ATOM    548  N   CYS A  71     -25.932  -9.743  -8.884  1.00 20.79           N
ANISOU  548  N   CYS A  71     2435   2524   2942    313   -244    279       N
ATOM    549  CA  CYS A  71     -27.177 -10.473  -8.667  1.00 20.61           C
ANISOU  549  CA  CYS A  71     2400   2337   3092   -249   -403    167       C
ATOM    550  C   CYS A  71     -27.049 -11.656  -7.702  1.00 19.63           C
ANISOU  550  C   CYS A  71     2419   2435   2604     82   -352    -43       C
ATOM    551  O   CYS A  71     -28.027 -12.353  -7.497  1.00 21.95           O
ANISOU  551  O   CYS A  71     2504   2734   3101   -110   -232    288       O
ATOM    552  CB  CYS A  71     -27.723 -10.975 -10.010  1.00 23.66           C
ANISOU  552  CB  CYS A  71     2474   2629   3887   -409   -706     93       C
ATOM    553  SG  CYS A  71     -26.744 -12.346 -10.681  1.00 27.26           S
ANISOU  553  SG  CYS A  71     2918   4121   3318   -576   -124   -625       S
ATOM    554  N   GLY A  72     -25.824 -11.963  -7.234  1.00 19.85           N
ANISOU  554  N   GLY A  72     2472   2297   2772   -150   -207    343       N
ATOM    555  CA  GLY A  72     -25.604 -13.264  -6.620  1.00 20.62           C
ANISOU  555  CA  GLY A  72     2670   2320   2846    -82    -95     79       C
ATOM    556  C   GLY A  72     -26.420 -13.577  -5.373  1.00 21.25           C
ANISOU  556  C   GLY A  72     2563   2806   2705    -35    -42     80       C
ATOM    557  O   GLY A  72     -26.652 -14.764  -5.124  1.00 22.54           O
ANISOU  557  O   GLY A  72     2696   2474   3395   -156     36    145       O
ATOM    558  N   LEU A  73     -26.823 -12.561  -4.605  1.00 20.89           N
ANISOU  558  N   LEU A  73     2761   2517   2658      8   -239     11       N
ATOM    559  CA  LEU A  73     -27.559 -12.815  -3.355  1.00 20.71           C
ANISOU  559  CA  LEU A  73     2761   2777   2330    199   -206    311       C
ATOM    560  C   LEU A  73     -29.079 -12.722  -3.554  1.00 22.49           C
ANISOU  560  C   LEU A  73     2919   2781   2844     69   -314     74       C
ATOM    561  O   LEU A  73     -29.811 -12.661  -2.582  1.00 22.20           O
ANISOU  561  O   LEU A  73     2870   2773   2793   -144   -173     53       O
ATOM    562  CB  LEU A  73     -27.091 -11.847  -2.275  1.00 21.46           C
ANISOU  562  CB  LEU A  73     2893   2441   2820    181   -216    105       C
ATOM    563  CG  LEU A  73     -25.714 -12.114  -1.688  1.00 22.12           C
ANISOU  563  CG  LEU A  73     2803   2691   2909      7   -123    -60       C
ATOM    564  CD1 LEU A  73     -25.369 -11.021  -0.749  1.00 22.79           C
ANISOU  564  CD1 LEU A  73     3025   2546   3089    -86   -565      7       C
ATOM    565  CD2 LEU A  73     -25.635 -13.466  -1.037  1.00 22.30           C
ANISOU  565  CD2 LEU A  73     2992   2758   2721     88    -72    -39       C
ATOM    566  N   LEU A  74     -29.562 -12.744  -4.814  1.00 22.14           N
ANISOU  566  N   LEU A  74     2919   2743   2750    -12     52     90       N
ATOM    567  CA  LEU A  74     -30.998 -12.583  -5.052  1.00 23.11           C
ANISOU  567  CA  LEU A  74     2810   3056   2914   -177   -253    -21       C
ATOM    568  C   LEU A  74     -31.865 -13.549  -4.255  1.00 22.32           C
ANISOU  568  C   LEU A  74     2942   2825   2712   -102   -251     53       C
ATOM    569  O   LEU A  74     -32.975 -13.201  -3.881  1.00 25.10           O
ANISOU  569  O   LEU A  74     2742   3297   3496   -222    -19   -240       O
ATOM    570  CB  LEU A  74     -31.303 -12.676  -6.536  1.00 25.24           C
ANISOU  570  CB  LEU A  74     3149   3528   2912   -399   -162     96       C
ATOM    571  CG  LEU A  74     -31.179 -11.393  -7.337  1.00 27.53           C
ANISOU  571  CG  LEU A  74     3778   3484   3197    -22   -395     90       C
ATOM    572  CD1 LEU A  74     -31.698 -11.653  -8.745  1.00 26.21           C
ANISOU  572  CD1 LEU A  74     3342   3291   3325    667   -451     79       C
ATOM    573  CD2 LEU A  74     -31.860 -10.207  -6.693  1.00 25.77           C
ANISOU  573  CD2 LEU A  74     2988   3079   3726   -324   -475     36       C
ATOM    574  N   ASP A  75     -31.368 -14.759  -3.988  1.00 21.91           N
ANISOU  574  N   ASP A  75     2756   2872   2697   -280    -72    -94       N
ATOM    575  CA  ASP A  75     -32.176 -15.776  -3.302  1.00 23.56           C
ANISOU  575  CA  ASP A  75     2948   2948   3057   -724   -166   -209       C
ATOM    576  C   ASP A  75     -32.549 -15.382  -1.867  1.00 22.66           C
ANISOU  576  C   ASP A  75     2692   2896   3021   -441     62   -185       C
ATOM    577  O   ASP A  75     -33.552 -15.905  -1.349  1.00 25.73           O
ANISOU  577  O   ASP A  75     3111   3270   3396   -381    278     83       O
ATOM    578  CB  ASP A  75     -31.478 -17.133  -3.317  1.00 25.16           C
ANISOU  578  CB  ASP A  75     3716   2619   3224   -614    -33   -152       C
ATOM    579  CG  ASP A  75     -31.028 -17.639  -4.697  1.00 33.25           C
ANISOU  579  CG  ASP A  75     4652   3429   4552    -16    -66   -404       C
ATOM    580  OD1 ASP A  75     -31.829 -17.542  -5.620  1.00 39.11           O
ANISOU  580  OD1 ASP A  75     6065   4041   4753    565    210   -342       O
ATOM    581  OD2 ASP A  75     -29.855 -18.182  -4.869  1.00 39.13           O
ANISOU  581  OD2 ASP A  75     5308   4694   4867      2   -738   -921       O
ATOM    582  N   ILE A  76     -31.782 -14.465  -1.247  1.00 22.44           N
ANISOU  582  N   ILE A  76     2955   2785   2787   -449   -108    -35       N
ATOM    583  CA  ILE A  76     -31.971 -14.183   0.176  1.00 22.55           C
ANISOU  583  CA  ILE A  76     3152   2583   2832   -576     21   -169       C
ATOM    584  C   ILE A  76     -33.180 -13.291   0.458  1.00 23.21           C
ANISOU  584  C   ILE A  76     3215   2860   2742   -337   -348     26       C
ATOM    585  O   ILE A  76     -33.672 -13.243   1.617  1.00 23.37           O
ANISOU  585  O   ILE A  76     2973   2833   3073   -107    242     14       O
ATOM    586  CB  ILE A  76     -30.715 -13.645   0.843  1.00 23.73           C
ANISOU  586  CB  ILE A  76     3069   3167   2780   -401   -177   -108       C
ATOM    587  CG1 ILE A  76     -30.455 -12.182   0.517  1.00 23.87           C
ANISOU  587  CG1 ILE A  76     2762   3520   2787   -199   -154    -58       C
ATOM    588  CG2 ILE A  76     -29.494 -14.557   0.595  1.00 25.10           C
ANISOU  588  CG2 ILE A  76     3227   3315   2993   -210   -288   -284       C
ATOM    589  CD1 ILE A  76     -29.279 -11.599   1.286  1.00 26.66           C
ANISOU  589  CD1 ILE A  76     3180   3976   2973   -750    -11   -180       C
ATOM    590  N   PHE A  77     -33.645 -12.571  -0.571  1.00 22.01           N
ANISOU  590  N   PHE A  77     2960   2768   2634   -420   -202   -155       N
ATOM    591  CA  PHE A  77     -34.666 -11.574  -0.344  1.00 22.81           C
ANISOU  591  CA  PHE A  77     3121   2696   2852   -256   -190    -27       C
ATOM    592  C   PHE A  77     -36.020 -12.242  -0.114  1.00 22.78           C
ANISOU  592  C   PHE A  77     2729   2956   2969     82     44     51       C
ATOM    593  O   PHE A  77     -36.271 -13.351  -0.583  1.00 24.11           O
ANISOU  593  O   PHE A  77     3013   2876   3270   -259    113    -32       O
ATOM    594  CB  PHE A  77     -34.688 -10.565  -1.487  1.00 23.11           C
ANISOU  594  CB  PHE A  77     2809   3058   2913   -194   -226     49       C
ATOM    595  CG  PHE A  77     -33.366  -9.829  -1.585  1.00 21.90           C
ANISOU  595  CG  PHE A  77     2567   2861   2893   -235   -243    210       C
ATOM    596  CD1 PHE A  77     -33.093  -8.787  -0.739  1.00 24.60           C
ANISOU  596  CD1 PHE A  77     3206   3026   3117   -542     65    150       C
ATOM    597  CD2 PHE A  77     -32.383 -10.242  -2.461  1.00 24.36           C
ANISOU  597  CD2 PHE A  77     3083   2767   3404   -298    250    112       C
ATOM    598  CE1 PHE A  77     -31.857  -8.156  -0.773  1.00 24.81           C
ANISOU  598  CE1 PHE A  77     3370   2827   3231   -931     16   -181       C
ATOM    599  CE2 PHE A  77     -31.126  -9.628  -2.452  1.00 23.21           C
ANISOU  599  CE2 PHE A  77     2747   2899   3173   -340    238    150       C
ATOM    600  CZ  PHE A  77     -30.868  -8.590  -1.603  1.00 24.11           C
ANISOU  600  CZ  PHE A  77     3136   3213   2812   -599     67    191       C
ATOM    601  N   SER A  78     -36.927 -11.507   0.548  1.00 23.80           N
ANISOU  601  N   SER A  78     2928   3035   3082   -272    119   -191       N
ATOM    602  CA  SER A  78     -38.218 -12.047   0.926  1.00 25.09           C
ANISOU  602  CA  SER A  78     2650   3485   3397   -308    127   -159       C
ATOM    603  C   SER A  78     -39.011 -12.393  -0.332  1.00 23.63           C
ANISOU  603  C   SER A  78     2511   2863   3604   -401    147   -318       C
ATOM    604  O   SER A  78     -38.801 -11.819  -1.411  1.00 24.67           O
ANISOU  604  O   SER A  78     2968   3055   3351   -630     76   -347       O
ATOM    605  CB  SER A  78     -39.000 -11.039   1.723  1.00 29.11           C
ANISOU  605  CB  SER A  78     3712   3883   3467   -416    521   -306       C
ATOM    606  OG  SER A  78     -39.611 -10.096   0.850  1.00 33.59           O
ANISOU  606  OG  SER A  78     4032   4308   4424    331    -36   -400       O
ATOM    607  N   GLU A  79     -39.986 -13.284  -0.156  1.00 29.88           N
ANISOU  607  N   GLU A  79     3169   3530   4656  -1110      6    315       N
ATOM    608  CA  GLU A  79     -40.818 -13.685  -1.264  1.00 31.68           C
ANISOU  608  CA  GLU A  79     3483   3698   4854   -604   -797     80       C
ATOM    609  C   GLU A  79     -41.701 -12.549  -1.785  1.00 29.67           C
ANISOU  609  C   GLU A  79     3440   3304   4528   -472    -15    288       C
ATOM    610  O   GLU A  79     -42.151 -12.664  -2.921  1.00 31.69           O
ANISOU  610  O   GLU A  79     3865   3942   4232   -382   -526   -213       O
ATOM    611  CB  GLU A  79     -41.597 -14.934  -0.856  1.00 42.82           C
ANISOU  611  CB  GLU A  79     4627   4649   6993   -902   -683    374       C
ATOM    612  CG  GLU A  79     -40.728 -16.197  -0.849  1.00 52.87           C
ANISOU  612  CG  GLU A  79     5877   5516   8697   -399   -644    785       C
ATOM    613  CD  GLU A  79     -39.880 -16.464  -2.112  1.00 62.19           C
ANISOU  613  CD  GLU A  79     6141   7528   9962    436  -1168     14       C
ATOM    614  OE1 GLU A  79     -40.470 -16.439  -3.234  1.00 70.17           O
ANISOU  614  OE1 GLU A  79     6706   8323  11630   -622  -3174    -29       O
ATOM    615  OE2 GLU A  79     -38.624 -16.676  -2.013  1.00 62.57           O
ANISOU  615  OE2 GLU A  79     5953   5871  11951    438  -2796   -371       O
ATOM    616  N   ARG A  80     -41.866 -11.444  -1.020  1.00 28.30           N
ANISOU  616  N   ARG A  80     2825   3969   3959   -785     44    307       N
ATOM    617  CA AARG A  80     -42.658 -10.296  -1.449  0.50 31.78           C
ANISOU  617  CA AARG A  80     3242   4239   4596   -550    474    375       C
ATOM    618  CA BARG A  80     -42.658 -10.296  -1.449  0.50 31.78           C
ANISOU  618  CA BARG A  80     3242   4239   4596   -549    475    375       C
ATOM    619  C   ARG A  80     -41.857  -9.295  -2.280  1.00 30.73           C
ANISOU  619  C   ARG A  80     3028   4042   4606   -480    364    365       C
ATOM    620  O   ARG A  80     -42.423  -8.349  -2.858  1.00 32.59           O
ANISOU  620  O   ARG A  80     2955   4366   5063     68    387    522       O
ATOM    621  CB AARG A  80     -43.221  -9.515  -0.254  0.50 35.14           C
ANISOU  621  CB AARG A  80     3788   4330   5232   -205   1678    481       C
ATOM    622  CB BARG A  80     -43.221  -9.514  -0.254  0.50 35.14           C
ANISOU  622  CB BARG A  80     3788   4330   5232   -204   1682    481       C
ATOM    623  CG AARG A  80     -43.411 -10.379   0.987  0.50 46.47           C
ANISOU  623  CG AARG A  80     5579   5949   6127     95    922    293       C
ATOM    624  CG BARG A  80     -43.400 -10.374   0.990  0.50 46.53           C
ANISOU  624  CG BARG A  80     5588   5963   6127    106    921    285       C
ATOM    625  N   THR A  81     -40.545  -9.508  -2.352  1.00 24.76           N
ANISOU  625  N   THR A  81     2754   3269   3382   -249    229   -224       N
ATOM    626  CA  THR A  81     -39.646  -8.510  -2.896  1.00 23.71           C
ANISOU  626  CA  THR A  81     2707   3201   3101   -219    115     11       C
ATOM    627  C   THR A  81     -39.785  -8.503  -4.417  1.00 23.83           C
ANISOU  627  C   THR A  81     2792   2872   3390    -84   -222     33       C
ATOM    628  O   THR A  81     -39.762  -9.538  -5.072  1.00 25.56           O
ANISOU  628  O   THR A  81     3210   3273   3228     16   -102   -254       O
ATOM    629  CB  THR A  81     -38.205  -8.850  -2.482  1.00 24.06           C
ANISOU  629  CB  THR A  81     2395   3079   3667   -654   -135    -27       C
ATOM    630  OG1 THR A  81     -38.149  -8.844  -1.044  1.00 26.86           O
ANISOU  630  OG1 THR A  81     2937   3882   3387   -755   -196    152       O
ATOM    631  CG2 THR A  81     -37.249  -7.818  -3.059  1.00 23.68           C
ANISOU  631  CG2 THR A  81     3075   2746   3174   -572   -133     14       C
ATOM    632  N   ASN A  82     -39.937  -7.315  -4.998  1.00 22.51           N
ANISOU  632  N   ASN A  82     2530   2956   3066    227     25   -249       N
ATOM    633  CA  ASN A  82     -39.907  -7.150  -6.443  1.00 23.11           C
ANISOU  633  CA  ASN A  82     2537   3127   3116   -271   -197     85       C
ATOM    634  C   ASN A  82     -38.458  -7.250  -6.916  1.00 22.47           C
ANISOU  634  C   ASN A  82     2782   2883   2871    -65   -162     52       C
ATOM    635  O   ASN A  82     -37.563  -6.687  -6.267  1.00 23.98           O
ANISOU  635  O   ASN A  82     2562   3515   3033   -156     74   -413       O
ATOM    636  CB  ASN A  82     -40.401  -5.784  -6.892  1.00 24.84           C
ANISOU  636  CB  ASN A  82     2770   3567   3103   -261    -79    -37       C
ATOM    637  CG  ASN A  82     -41.781  -5.472  -6.383  1.00 27.95           C
ANISOU  637  CG  ASN A  82     3183   3983   3452    243    -31    258       C
ATOM    638  OD1 ASN A  82     -42.715  -6.209  -6.685  1.00 28.93           O
ANISOU  638  OD1 ASN A  82     2709   4328   3955      1   -229   -392       O
ATOM    639  ND2 ASN A  82     -41.922  -4.430  -5.562  1.00 32.14           N
ANISOU  639  ND2 ASN A  82     3418   4474   4321    533     96   -209       N
ATOM    640  N   ILE A  83     -38.220  -7.998  -7.970  1.00 22.01           N
ANISOU  640  N   ILE A  83     2421   3032   2908   -191   -159   -117       N
ATOM    641  CA AILE A  83     -36.902  -8.177  -8.546  0.50 21.27           C
ANISOU  641  CA AILE A  83     2443   3123   2513   -236   -391   -147       C
ATOM    642  CA BILE A  83     -36.902  -8.177  -8.546  0.50 21.27           C
ANISOU  642  CA BILE A  83     2443   3123   2513   -236   -391   -147       C
ATOM    643  C   ILE A  83     -36.947  -7.684  -9.997  1.00 21.25           C
ANISOU  643  C   ILE A  83     2536   2917   2620    298    -37    204       C
ATOM    644  O   ILE A  83     -37.642  -8.240 -10.861  1.00 21.86           O
ANISOU  644  O   ILE A  83     2493   3168   2647   -200   -232   -104       O
ATOM    645  CB AILE A  83     -36.495  -9.654  -8.509  0.50 23.02           C
ANISOU  645  CB AILE A  83     2714   3332   2701      6    -85    137       C
ATOM    646  CB BILE A  83     -36.495  -9.654  -8.509  0.50 23.02           C
ANISOU  646  CB BILE A  83     2714   3332   2701      6    -84    138       C
ATOM    647  CG1AILE A  83     -36.679 -10.277  -7.151  0.50 28.65           C
ANISOU  647  CG1AILE A  83     3378   4219   3288     13    390    191       C
ATOM    648  CG1BILE A  83     -36.680 -10.277  -7.151  0.50 28.65           C
ANISOU  648  CG1BILE A  83     3380   4218   3288     13    391    192       C
ATOM    649  CG2AILE A  83     -35.068  -9.800  -9.029  0.50 23.57           C
ANISOU  649  CG2AILE A  83     2620   3485   2852   -145    -87     32       C
ATOM    650  CG2BILE A  83     -35.068  -9.800  -9.029  0.50 23.57           C
ANISOU  650  CG2BILE A  83     2620   3485   2852   -145    -87     33       C
ATOM    651  CD1AILE A  83     -35.773  -9.751  -6.103  0.50 29.11           C
ANISOU  651  CD1AILE A  83     3595   4197   3267    -65    233    320       C
ATOM    652  CD1BILE A  83     -35.773  -9.752  -6.102  0.50 29.10           C
ANISOU  652  CD1BILE A  83     3595   4196   3266    -68    235    321       C
ATOM    653  N   VAL A  84     -36.221  -6.589 -10.235  1.00 20.88           N
ANISOU  653  N   VAL A  84     2245   2918   2772    -74   -207    119       N
ATOM    654  CA  VAL A  84     -36.433  -5.814 -11.418  1.00 20.73           C
ANISOU  654  CA  VAL A  84     2366   2722   2785    112   -275    101       C
ATOM    655  C   VAL A  84     -35.120  -5.668 -12.186  1.00 20.74           C
ANISOU  655  C   VAL A  84     2674   2785   2422    107   -247     33       C
ATOM    656  O   VAL A  84     -34.085  -5.310 -11.642  1.00 22.23           O
ANISOU  656  O   VAL A  84     2617   3177   2651    -21   -387    -95       O
ATOM    657  CB  VAL A  84     -36.990  -4.414 -11.069  1.00 24.63           C
ANISOU  657  CB  VAL A  84     3224   3004   3130    630   -276    123       C
ATOM    658  CG1 VAL A  84     -37.322  -3.648 -12.321  1.00 25.18           C
ANISOU  658  CG1 VAL A  84     2918   3161   3487    963     -4    105       C
ATOM    659  CG2 VAL A  84     -38.139  -4.474 -10.097  1.00 25.80           C
ANISOU  659  CG2 VAL A  84     2875   3414   3515    459    -72   -162       C
ATOM    660  N   GLY A  85     -35.171  -5.893 -13.493  1.00 21.07           N
ANISOU  660  N   GLY A  85     2249   2970   2789    -26   -250    -44       N
ATOM    661  CA  GLY A  85     -33.990  -5.705 -14.317  1.00 21.73           C
ANISOU  661  CA  GLY A  85     2539   2938   2780    313   -293    -77       C
ATOM    662  C   GLY A  85     -34.304  -5.856 -15.800  1.00 20.69           C
ANISOU  662  C   GLY A  85     2368   2739   2756    401   -280   -108       C
ATOM    663  O   GLY A  85     -35.437  -6.099 -16.188  1.00 21.88           O
ANISOU  663  O   GLY A  85     2366   3216   2731   -109   -365   -125       O
ATOM    664  N   HIS A  86     -33.278  -5.742 -16.627  1.00 20.07           N
ANISOU  664  N   HIS A  86     2268   2704   2654    125   -363    -72       N
ATOM    665  CA  HIS A  86     -33.390  -6.039 -18.050  1.00 20.03           C
ANISOU  665  CA  HIS A  86     2499   2560   2549    -52    -98     61       C
ATOM    666  C   HIS A  86     -33.977  -7.447 -18.215  1.00 20.25           C
ANISOU  666  C   HIS A  86     2627   2455   2613   -233   -190   -326       C
ATOM    667  O   HIS A  86     -33.628  -8.380 -17.489  1.00 21.30           O
ANISOU  667  O   HIS A  86     2554   2883   2655    111   -319    -59       O
ATOM    668  CB  HIS A  86     -32.009  -5.966 -18.683  1.00 20.59           C
ANISOU  668  CB  HIS A  86     2627   2488   2707    178    -97   -139       C
ATOM    669  CG  HIS A  86     -31.964  -5.983 -20.151  1.00 22.10           C
ANISOU  669  CG  HIS A  86     2823   2889   2687    329   -139      3       C
ATOM    670  ND1 HIS A  86     -32.261  -7.080 -20.923  1.00 23.22           N
ANISOU  670  ND1 HIS A  86     2978   3182   2665   -128   -231   -255       N
ATOM    671  CD2 HIS A  86     -31.622  -4.979 -20.995  1.00 23.58           C
ANISOU  671  CD2 HIS A  86     2798   2964   3198    -27   -617     62       C
ATOM    672  CE1 HIS A  86     -32.087  -6.711 -22.222  1.00 25.71           C
ANISOU  672  CE1 HIS A  86     3787   3449   2531   -208   -118   -213       C
ATOM    673  NE2 HIS A  86     -31.651  -5.456 -22.293  1.00 25.95           N
ANISOU  673  NE2 HIS A  86     3123   3541   3197    -72   -364     37       N
ATOM    674  N   PRO A  87     -34.888  -7.650 -19.183  1.00 21.56           N
ANISOU  674  N   PRO A  87     2634   2885   2672     22   -502    306       N
ATOM    675  CA  PRO A  87     -35.497  -8.956 -19.354  1.00 22.39           C
ANISOU  675  CA  PRO A  87     2548   2784   3174    -40   -372     25       C
ATOM    676  C   PRO A  87     -34.526 -10.092 -19.598  1.00 21.50           C
ANISOU  676  C   PRO A  87     2493   3056   2621     84   -519   -193       C
ATOM    677  O   PRO A  87     -34.818 -11.226 -19.239  1.00 22.86           O
ANISOU  677  O   PRO A  87     2805   2915   2966    -95   -504     97       O
ATOM    678  CB  PRO A  87     -36.431  -8.756 -20.558  1.00 25.34           C
ANISOU  678  CB  PRO A  87     2885   3342   3400     -4   -485     33       C
ATOM    679  CG  PRO A  87     -35.825  -7.564 -21.306  1.00 24.37           C
ANISOU  679  CG  PRO A  87     2972   3363   2924    -12   -432    -41       C
ATOM    680  CD  PRO A  87     -35.393  -6.676 -20.166  1.00 23.30           C
ANISOU  680  CD  PRO A  87     2613   2996   3242   -217   -582    164       C
ATOM    681  N   TRP A  88     -33.389  -9.778 -20.257  1.00 20.63           N
ANISOU  681  N   TRP A  88     2602   2522   2712    101   -528     79       N
ATOM    682  CA ATRP A  88     -32.452 -10.847 -20.613  0.50 22.82           C
ANISOU  682  CA ATRP A  88     2832   2822   3016    102   -343     23       C
ATOM    683  CA BTRP A  88     -32.465 -10.861 -20.617  0.50 22.57           C
ANISOU  683  CA BTRP A  88     2784   2836   2958     69   -280     68       C
ATOM    684  C   TRP A  88     -31.687 -11.404 -19.413  1.00 22.05           C
ANISOU  684  C   TRP A  88     2932   3060   2385   -157   -289     73       C
ATOM    685  O   TRP A  88     -30.957 -12.400 -19.504  1.00 23.99           O
ANISOU  685  O   TRP A  88     3206   2831   3078     85    -45   -228       O
ATOM    686  CB ATRP A  88     -31.515 -10.415 -21.727  0.50 25.16           C
ANISOU  686  CB ATRP A  88     3222   3443   2896   -140   -439     87       C
ATOM    687  CB BTRP A  88     -31.556 -10.465 -21.771  0.50 24.19           C
ANISOU  687  CB BTRP A  88     3044   3417   2727   -260   -359    130       C
ATOM    688  CG ATRP A  88     -31.802 -11.034 -23.069  0.50 30.15           C
ANISOU  688  CG ATRP A  88     3733   4413   3311   -281   -742   -274       C
ATOM    689  CG BTRP A  88     -32.275 -10.009 -23.021  0.50 25.49           C
ANISOU  689  CG BTRP A  88     2925   3991   2769   -315   -530     69       C
ATOM    690  CD1ATRP A  88     -32.610 -12.092 -23.408  0.50 28.48           C
ANISOU  690  CD1ATRP A  88     3741   4058   3020    306   -746   -125       C
ATOM    691  CD1BTRP A  88     -33.612  -9.860 -23.252  0.50 24.90           C
ANISOU  691  CD1BTRP A  88     3124   3875   2461   -268   -299   -397       C
ATOM    692  CD2ATRP A  88     -31.162 -10.612 -24.291  0.50 30.38           C
ANISOU  692  CD2ATRP A  88     3480   4758   3304     72   -331     52       C
ATOM    693  CD2BTRP A  88     -31.616  -9.608 -24.246  0.50 26.68           C
ANISOU  693  CD2BTRP A  88     2915   4727   2495   -235   -308   -325       C
ATOM    694  NE1ATRP A  88     -32.517 -12.339 -24.758  0.50 30.96           N
ANISOU  694  NE1ATRP A  88     3592   4702   3470    666   -425    134       N
ATOM    695  NE1BTRP A  88     -33.838  -9.396 -24.526  0.50 25.90           N
ANISOU  695  NE1BTRP A  88     2746   4322   2772   -426   -626    -22       N
ATOM    696  CE2ATRP A  88     -31.631 -11.461 -25.316  0.50 29.92           C
ANISOU  696  CE2ATRP A  88     3639   4831   2897    453   -590     86       C
ATOM    697  CE2BTRP A  88     -32.624  -9.225 -25.160  0.50 27.16           C
ANISOU  697  CE2BTRP A  88     3162   4745   2411   -313   -260   -259       C
ATOM    698  CE3ATRP A  88     -30.235  -9.607 -24.615  0.50 29.54           C
ANISOU  698  CE3ATRP A  88     3493   4400   3330    438   -514    489       C
ATOM    699  CE3BTRP A  88     -30.270  -9.515 -24.629  0.50 28.18           C
ANISOU  699  CE3BTRP A  88     3072   4794   2842    -68   -267    107       C
ATOM    700  CZ2ATRP A  88     -31.206 -11.341 -26.637  0.50 34.09           C
ANISOU  700  CZ2ATRP A  88     4175   5409   3368     72   -388    670       C
ATOM    701  CZ2BTRP A  88     -32.330  -8.745 -26.432  0.50 29.37           C
ANISOU  701  CZ2BTRP A  88     2888   5791   2482   -461   -726    586       C
ATOM    702  CZ3ATRP A  88     -29.803  -9.507 -25.918  0.50 31.57           C
ANISOU  702  CZ3ATRP A  88     3926   4673   3396    536   -489    965       C
ATOM    703  CZ3BTRP A  88     -29.980  -9.118 -25.914  0.50 31.23           C
ANISOU  703  CZ3BTRP A  88     3510   5392   2963    -14   -109    199       C
ATOM    704  CH2ATRP A  88     -30.292 -10.353 -26.916  0.50 34.19           C
ANISOU  704  CH2ATRP A  88     3790   5371   3831    282   -414    753       C
ATOM    705  CH2BTRP A  88     -30.996  -8.730 -26.797  0.50 30.54           C
ANISOU  705  CH2BTRP A  88     3294   5581   2727   -629   -282    404       C
ATOM    706  N   ASN A  89     -31.858 -10.750 -18.234  1.00 20.65           N
ANISOU  706  N   ASN A  89     2544   2892   2408    126   -474     75       N
ATOM    707  CA  ASN A  89     -31.308 -11.348 -17.008  1.00 20.07           C
ANISOU  707  CA  ASN A  89     2810   2700   2114   -141   -303    -72       C
ATOM    708  C   ASN A  89     -31.897 -12.731 -16.764  1.00 21.48           C
ANISOU  708  C   ASN A  89     2760   2819   2583   -116   -223   -161       C
ATOM    709  O   ASN A  89     -31.230 -13.584 -16.173  1.00 21.49           O
ANISOU  709  O   ASN A  89     2659   2822   2685     26   -261   -262       O
ATOM    710  CB  ASN A  89     -31.615 -10.509 -15.773  1.00 20.56           C
ANISOU  710  CB  ASN A  89     2844   2642   2324   -178   -306    -43       C
ATOM    711  CG  ASN A  89     -30.701  -9.298 -15.693  1.00 22.79           C
ANISOU  711  CG  ASN A  89     2857   3079   2722   -124   -122   -115       C
ATOM    712  OD1 ASN A  89     -29.483  -9.412 -15.520  1.00 22.27           O
ANISOU  712  OD1 ASN A  89     2511   2868   3083     -4   -251   -218       O
ATOM    713  ND2 ASN A  89     -31.265  -8.111 -15.734  1.00 21.48           N
ANISOU  713  ND2 ASN A  89     2560   2851   2751     29   -368   -254       N
ATOM    714  N   GLU A  90     -33.161 -12.945 -17.171  1.00 22.62           N
ANISOU  714  N   GLU A  90     2841   3061   2694     21   -547    -99       N
ATOM    715  CA  GLU A  90     -33.928 -14.119 -16.710  1.00 21.32           C
ANISOU  715  CA  GLU A  90     2541   2777   2782    -73   -213   -398       C
ATOM    716  C   GLU A  90     -33.190 -15.453 -16.885  1.00 22.69           C
ANISOU  716  C   GLU A  90     2800   2924   2897   -309   -466   -407       C
ATOM    717  O   GLU A  90     -33.109 -16.222 -15.902  1.00 23.65           O
ANISOU  717  O   GLU A  90     2982   2960   3043   -114   -384   -234       O
ATOM    718  CB  GLU A  90     -35.298 -14.137 -17.352  1.00 22.86           C
ANISOU  718  CB  GLU A  90     2837   3001   2847    254   -113   -368       C
ATOM    719  CG  GLU A  90     -36.209 -15.207 -16.759  1.00 24.12           C
ANISOU  719  CG  GLU A  90     2883   3126   3156   -259   -296   -206       C
ATOM    720  CD  GLU A  90     -36.786 -14.940 -15.387  1.00 23.88           C
ANISOU  720  CD  GLU A  90     2834   3265   2976   -339   -468   -177       C
ATOM    721  OE1 GLU A  90     -37.674 -15.713 -14.979  1.00 25.46           O
ANISOU  721  OE1 GLU A  90     2790   3061   3824   -661   -188     -8       O
ATOM    722  OE2 GLU A  90     -36.325 -13.960 -14.738  1.00 23.96           O
ANISOU  722  OE2 GLU A  90     2694   3357   3054   -215   -148   -292       O
ATOM    723  N   PRO A  91     -32.669 -15.824 -18.080  1.00 22.29           N
ANISOU  723  N   PRO A  91     2614   3027   2828   -225    -97   -126       N
ATOM    724  CA  PRO A  91     -32.006 -17.121 -18.210  1.00 23.69           C
ANISOU  724  CA  PRO A  91     2921   2763   3316   -138    102   -213       C
ATOM    725  C   PRO A  91     -30.807 -17.262 -17.290  1.00 22.83           C
ANISOU  725  C   PRO A  91     2794   2863   3019   -236     59   -249       C
ATOM    726  O   PRO A  91     -30.617 -18.320 -16.715  1.00 24.89           O
ANISOU  726  O   PRO A  91     2958   2658   3842   -216   -171   -151       O
ATOM    727  CB  PRO A  91     -31.611 -17.215 -19.676  1.00 26.73           C
ANISOU  727  CB  PRO A  91     3638   3300   3217   -186   -321   -558       C
ATOM    728  CG  PRO A  91     -31.670 -15.814 -20.178  1.00 26.91           C
ANISOU  728  CG  PRO A  91     4105   3083   3035   -218    110   -817       C
ATOM    729  CD  PRO A  91     -32.726 -15.100 -19.363  1.00 24.32           C
ANISOU  729  CD  PRO A  91     3172   3035   3035    -29   -204   -368       C
ATOM    730  N   TRP A  92     -30.042 -16.157 -17.121  1.00 23.12           N
ANISOU  730  N   TRP A  92     2685   3054   3044    -80    -47   -155       N
ATOM    731  CA  TRP A  92     -28.845 -16.179 -16.287  1.00 21.06           C
ANISOU  731  CA  TRP A  92     2500   2508   2992    -96   -315   -176       C
ATOM    732  C   TRP A  92     -29.210 -16.423 -14.835  1.00 21.81           C
ANISOU  732  C   TRP A  92     2345   2876   3065   -129   -111   -251       C
ATOM    733  O   TRP A  92     -28.679 -17.316 -14.200  1.00 23.95           O
ANISOU  733  O   TRP A  92     2769   3008   3323    308   -149    -32       O
ATOM    734  CB  TRP A  92     -28.103 -14.848 -16.411  1.00 22.52           C
ANISOU  734  CB  TRP A  92     2624   3084   2850   -380   -235   -138       C
ATOM    735  CG  TRP A  92     -27.591 -14.501 -17.775  1.00 21.11           C
ANISOU  735  CG  TRP A  92     2617   2501   2904     -3    -87   -119       C
ATOM    736  CD1 TRP A  92     -28.231 -13.733 -18.683  1.00 24.38           C
ANISOU  736  CD1 TRP A  92     2776   3396   3090     34     42    208       C
ATOM    737  CD2 TRP A  92     -26.303 -14.798 -18.339  1.00 23.30           C
ANISOU  737  CD2 TRP A  92     2693   2967   3192    -51    282   -322       C
ATOM    738  NE1 TRP A  92     -27.458 -13.549 -19.804  1.00 24.77           N
ANISOU  738  NE1 TRP A  92     3073   3136   3201     60     55     54       N
ATOM    739  CE2 TRP A  92     -26.260 -14.184 -19.602  1.00 24.74           C
ANISOU  739  CE2 TRP A  92     2944   3046   3409    -72    234   -340       C
ATOM    740  CE3 TRP A  92     -25.177 -15.480 -17.880  1.00 25.78           C
ANISOU  740  CE3 TRP A  92     3121   3354   3321    231     41   -222       C
ATOM    741  CZ2 TRP A  92     -25.124 -14.244 -20.408  1.00 27.41           C
ANISOU  741  CZ2 TRP A  92     2892   3664   3860   -224    224   -429       C
ATOM    742  CZ3 TRP A  92     -24.048 -15.563 -18.696  1.00 25.57           C
ANISOU  742  CZ3 TRP A  92     2539   3187   3989    -76    259   -542       C
ATOM    743  CH2 TRP A  92     -24.038 -14.944 -19.937  1.00 27.84           C
ANISOU  743  CH2 TRP A  92     2995   3563   4021   -412    539   -229       C
ATOM    744  N   ILE A  93     -30.110 -15.582 -14.307  1.00 20.94           N
ANISOU  744  N   ILE A  93     2272   2604   3080    130   -247     35       N
ATOM    745  CA  ILE A  93     -30.409 -15.561 -12.877  1.00 20.82           C
ANISOU  745  CA  ILE A  93     2419   2611   2883     -8   -189     63       C
ATOM    746  C   ILE A  93     -31.247 -16.740 -12.425  1.00 20.95           C
ANISOU  746  C   ILE A  93     2376   2592   2991     89     -4    -88       C
ATOM    747  O   ILE A  93     -31.203 -17.050 -11.249  1.00 23.94           O
ANISOU  747  O   ILE A  93     2829   3432   2836   -317   -440     48       O
ATOM    748  CB  ILE A  93     -30.986 -14.221 -12.415  1.00 20.71           C
ANISOU  748  CB  ILE A  93     2436   2320   3111     59   -192     69       C
ATOM    749  CG1 ILE A  93     -32.326 -13.911 -12.980  1.00 21.83           C
ANISOU  749  CG1 ILE A  93     2343   2860   3092    352   -175   -105       C
ATOM    750  CG2 ILE A  93     -29.973 -13.083 -12.705  1.00 21.26           C
ANISOU  750  CG2 ILE A  93     2507   2407   3162    266   -314     12       C
ATOM    751  CD1 ILE A  93     -32.946 -12.708 -12.310  1.00 22.85           C
ANISOU  751  CD1 ILE A  93     2564   3147   2971    310   -488     15       C
ATOM    752  N   THR A  94     -31.992 -17.382 -13.351  1.00 22.23           N
ANISOU  752  N   THR A  94     2557   2724   3165      1   -292   -154       N
ATOM    753  CA  THR A  94     -32.745 -18.582 -12.999  1.00 23.70           C
ANISOU  753  CA  THR A  94     3012   2507   3487   -141    241    -27       C
ATOM    754  C   THR A  94     -31.908 -19.853 -13.200  1.00 25.19           C
ANISOU  754  C   THR A  94     2785   2903   3881    -21     -8     40       C
ATOM    755  O   THR A  94     -32.344 -20.947 -12.825  1.00 27.69           O
ANISOU  755  O   THR A  94     3443   2642   4435    146    219    166       O
ATOM    756  CB  THR A  94     -34.029 -18.649 -13.821  1.00 24.97           C
ANISOU  756  CB  THR A  94     2899   2703   3888   -196    197    146       C
ATOM    757  OG1 THR A  94     -33.715 -18.773 -15.202  1.00 26.09           O
ANISOU  757  OG1 THR A  94     3106   3262   3543   -215     12   -118       O
ATOM    758  CG2 THR A  94     -34.977 -17.514 -13.485  1.00 26.56           C
ANISOU  758  CG2 THR A  94     3099   3180   3813   -138     50   -103       C
ATOM    759  N   GLN A  95     -30.753 -19.712 -13.848  1.00 25.04           N
ANISOU  759  N   GLN A  95     2994   2763   3759   -211    -70   -207       N
ATOM    760  CA  GLN A  95     -29.918 -20.851 -14.220  1.00 29.19           C
ANISOU  760  CA  GLN A  95     3838   3148   4106    -10     54   -143       C
ATOM    761  C   GLN A  95     -30.767 -21.865 -14.990  1.00 30.72           C
ANISOU  761  C   GLN A  95     3932   3660   4082   -144    404   -319       C
ATOM    762  O   GLN A  95     -30.752 -23.038 -14.733  1.00 35.37           O
ANISOU  762  O   GLN A  95     4649   3284   5507   -279    658   -534       O
ATOM    763  CB  GLN A  95     -29.210 -21.462 -13.019  1.00 32.62           C
ANISOU  763  CB  GLN A  95     4209   3344   4840    985   -122   -325       C
ATOM    764  CG  GLN A  95     -28.347 -20.475 -12.272  1.00 34.46           C
ANISOU  764  CG  GLN A  95     4705   3804   4582    659   -523   -783       C
ATOM    765  CD  GLN A  95     -27.309 -21.137 -11.417  1.00 39.55           C
ANISOU  765  CD  GLN A  95     5709   3458   5862   1631   -473   -692       C
ATOM    766  OE1 GLN A  95     -26.848 -22.262 -11.697  1.00 41.31           O
ANISOU  766  OE1 GLN A  95     6258   3732   5706   2237  -1368  -1604       O
ATOM    767  NE2 GLN A  95     -26.911 -20.429 -10.376  1.00 42.33           N
ANISOU  767  NE2 GLN A  95     4956   4741   6387   1959   -980  -1428       N
ATOM    768  N   ASN A  96     -31.456 -21.350 -16.000  1.00 32.12           N
ANISOU  768  N   ASN A  96     3901   4159   4143   -236    206  -1120       N
ATOM    769  CA  ASN A  96     -32.338 -22.106 -16.873  1.00 31.53           C
ANISOU  769  CA  ASN A  96     4117   3825   4039   -450    217   -839       C
ATOM    770  C   ASN A  96     -31.544 -23.282 -17.437  1.00 35.22           C
ANISOU  770  C   ASN A  96     4949   4045   4389   -267    701  -1126       C
ATOM    771  O   ASN A  96     -30.486 -23.067 -18.007  1.00 33.61           O
ANISOU  771  O   ASN A  96     3962   4043   4764   -475    520   -995       O
ATOM    772  CB  ASN A  96     -32.860 -21.179 -17.961  1.00 36.99           C
ANISOU  772  CB  ASN A  96     3991   4876   5189    305    247   -544       C
ATOM    773  CG  ASN A  96     -33.679 -21.911 -18.994  1.00 39.28           C
ANISOU  773  CG  ASN A  96     3855   5754   5317   -475   -161   -695       C
ATOM    774  OD1 ASN A  96     -33.148 -22.354 -20.015  1.00 39.63           O
ANISOU  774  OD1 ASN A  96     4642   4671   5744    447   -580  -1497       O
ATOM    775  ND2 ASN A  96     -34.967 -22.068 -18.730  1.00 44.05           N
ANISOU  775  ND2 ASN A  96     4169   7364   5204  -1192   -276   -787       N
ATOM    776  N   PRO A  97     -31.987 -24.549 -17.242  1.00 38.69           N
ANISOU  776  N   PRO A  97     5388   3612   5701  -1013   1197  -1357       N
ATOM    777  CA  PRO A  97     -31.208 -25.725 -17.677  1.00 40.61           C
ANISOU  777  CA  PRO A  97     4842   4599   5989   -992    492  -1578       C
ATOM    778  C   PRO A  97     -30.739 -25.682 -19.125  1.00 38.27           C
ANISOU  778  C   PRO A  97     4710   3972   5859   -782    305  -1420       C
ATOM    779  O   PRO A  97     -29.596 -26.036 -19.427  1.00 39.51           O
ANISOU  779  O   PRO A  97     4458   4403   6150   -526    642  -1601       O
ATOM    780  CB  PRO A  97     -32.200 -26.838 -17.432  1.00 43.01           C
ANISOU  780  CB  PRO A  97     6038   4501   5802   -902    881  -1174       C
ATOM    781  CG  PRO A  97     -32.854 -26.395 -16.182  1.00 41.08           C
ANISOU  781  CG  PRO A  97     4791   4138   6679   -635   1308  -1181       C
ATOM    782  CD  PRO A  97     -33.208 -24.936 -16.518  1.00 44.21           C
ANISOU  782  CD  PRO A  97     6078   4926   5794   -480    837  -1243       C
ATOM    783  N   GLN A  98     -31.646 -25.256 -20.017  1.00 38.18           N
ANISOU  783  N   GLN A  98     4727   3709   6072  -1474    514  -1163       N
ATOM    784  CA  GLN A  98     -31.319 -25.200 -21.427  1.00 41.73           C
ANISOU  784  CA  GLN A  98     4858   4881   6117   -903    790  -1154       C
ATOM    785  C   GLN A  98     -30.233 -24.139 -21.629  1.00 37.34           C
ANISOU  785  C   GLN A  98     4152   4267   5767   -810    420  -1649       C
ATOM    786  O   GLN A  98     -29.301 -24.390 -22.375  1.00 38.16           O
ANISOU  786  O   GLN A  98     3882   4632   5984  -1092    828  -1992       O
ATOM    787  CB  GLN A  98     -32.538 -24.933 -22.308  1.00 45.06           C
ANISOU  787  CB  GLN A  98     4309   5134   7679  -1311    184   -710       C
ATOM    788  CG  GLN A  98     -33.452 -26.139 -22.544  1.00 50.64           C
ANISOU  788  CG  GLN A  98     4576   6057   8608  -1600    420   -959       C
ATOM    789  N   PHE A  99     -30.365 -22.963 -20.978  1.00 35.49           N
ANISOU  789  N   PHE A  99     3439   4297   5748   -637    404  -1646       N
ATOM    790  CA  PHE A  99     -29.356 -21.895 -21.058  1.00 34.78           C
ANISOU  790  CA  PHE A  99     4203   3852   5161   -459    552  -1164       C
ATOM    791  C   PHE A  99     -27.988 -22.397 -20.575  1.00 34.98           C
ANISOU  791  C   PHE A  99     4074   4115   5103   -504    462  -1176       C
ATOM    792  O   PHE A  99     -26.977 -22.149 -21.208  1.00 33.72           O
ANISOU  792  O   PHE A  99     3512   3434   5866   -396    695  -1335       O
ATOM    793  CB  PHE A  99     -29.788 -20.663 -20.267  1.00 35.97           C
ANISOU  793  CB  PHE A  99     4137   3768   5760     99    399   -569       C
ATOM    794  CG  PHE A  99     -28.803 -19.514 -20.316  1.00 34.71           C
ANISOU  794  CG  PHE A  99     4201   3597   5392    143    430    -62       C
ATOM    795  CD1 PHE A  99     -28.806 -18.620 -21.391  1.00 37.49           C
ANISOU  795  CD1 PHE A  99     5188   3806   5249    -15    476   -444       C
ATOM    796  CD2 PHE A  99     -27.855 -19.355 -19.319  1.00 38.41           C
ANISOU  796  CD2 PHE A  99     5354   3645   5597    175    484  -1046       C
ATOM    797  CE1 PHE A  99     -27.862 -17.610 -21.463  1.00 38.61           C
ANISOU  797  CE1 PHE A  99     5297   3704   5670   -163    190   -382       C
ATOM    798  CE2 PHE A  99     -26.929 -18.334 -19.385  1.00 36.61           C
ANISOU  798  CE2 PHE A  99     5120   2676   6112   -148    199   -936       C
ATOM    799  CZ  PHE A  99     -26.921 -17.481 -20.470  1.00 42.64           C
ANISOU  799  CZ  PHE A  99     6258   3942   6003   -550   -209   -950       C
ATOM    800  N   ILE A 100     -27.961 -23.074 -19.421  1.00 33.34           N
ANISOU  800  N   ILE A 100     4278   3834   4556   -613    569  -1288       N
ATOM    801  CA  ILE A 100     -26.739 -23.598 -18.832  1.00 38.14           C
ANISOU  801  CA  ILE A 100     4526   4148   5816   -442    176  -1286       C
ATOM    802  C   ILE A 100     -26.066 -24.594 -19.769  1.00 33.60           C
ANISOU  802  C   ILE A 100     4155   3804   4806   -580    535  -1005       C
ATOM    803  O   ILE A 100     -24.845 -24.565 -19.910  1.00 35.45           O
ANISOU  803  O   ILE A 100     4407   3355   5709    279    520   -416       O
ATOM    804  CB  ILE A 100     -27.043 -24.229 -17.459  1.00 39.82           C
ANISOU  804  CB  ILE A 100     4616   5012   5504   -702    368  -1215       C
ATOM    805  CG1 ILE A 100     -27.513 -23.164 -16.455  1.00 42.34           C
ANISOU  805  CG1 ILE A 100     5000   5068   6020   -684     60  -1380       C
ATOM    806  CG2 ILE A 100     -25.864 -25.066 -16.944  1.00 42.36           C
ANISOU  806  CG2 ILE A 100     5258   5879   4959   -655    106  -1023       C
ATOM    807  N   LYS A 101     -26.864 -25.455 -20.418  1.00 34.04           N
ANISOU  807  N   LYS A 101     4227   3681   5027   -278    906  -1071       N
ATOM    808  CA  LYS A 101     -26.313 -26.436 -21.337  1.00 37.13           C
ANISOU  808  CA  LYS A 101     4520   3864   5723   -504    871  -1658       C
ATOM    809  C   LYS A 101     -25.660 -25.676 -22.485  1.00 35.08           C
ANISOU  809  C   LYS A 101     4166   3738   5425   -488    387  -1182       C
ATOM    810  O   LYS A 101     -24.537 -26.027 -22.869  1.00 36.36           O
ANISOU  810  O   LYS A 101     4155   3961   5699   -258    703   -943       O
ATOM    811  CB  LYS A 101     -27.368 -27.480 -21.782  1.00 42.17           C
ANISOU  811  CB  LYS A 101     4919   4374   6729   -717    812  -1958       C
ATOM    812  CG  LYS A 101     -27.045 -28.373 -22.964  1.00 46.91           C
ANISOU  812  CG  LYS A 101     5257   5154   7414  -1143    982  -1621       C
ATOM    813  CD  LYS A 101     -28.248 -29.076 -23.608  1.00 48.99           C
ANISOU  813  CD  LYS A 101     5590   4857   8167   -853    564  -1488       C
ATOM    814  N   ARG A 102     -26.349 -24.633 -22.998  1.00 34.06           N
ANISOU  814  N   ARG A 102     3687   3835   5419    119    376  -1378       N
ATOM    815  CA  ARG A 102     -25.818 -23.805 -24.079  1.00 32.90           C
ANISOU  815  CA  ARG A 102     3817   4022   4660    118   -226  -1000       C
ATOM    816  C   ARG A 102     -24.540 -23.083 -23.645  1.00 33.29           C
ANISOU  816  C   ARG A 102     3688   4143   4818   -131     54  -1164       C
ATOM    817  O   ARG A 102     -23.601 -22.971 -24.434  1.00 33.62           O
ANISOU  817  O   ARG A 102     3566   4494   4716      2    350  -1038       O
ATOM    818  CB  ARG A 102     -26.829 -22.771 -24.596  1.00 40.61           C
ANISOU  818  CB  ARG A 102     3704   5756   5968    175   -324  -1101       C
ATOM    819  CG  ARG A 102     -27.947 -23.414 -25.406  1.00 46.48           C
ANISOU  819  CG  ARG A 102     4919   6119   6622   -176   -448   -840       C
ATOM    820  CD  ARG A 102     -29.060 -22.397 -25.699  1.00 52.17           C
ANISOU  820  CD  ARG A 102     5934   6625   7264    653   -176     42       C
ATOM    821  NE  ARG A 102     -28.557 -21.323 -26.561  1.00 50.48           N
ANISOU  821  NE  ARG A 102     6913   5883   6382    797     67   -394       N
ATOM    822  CZ  ARG A 102     -28.467 -21.388 -27.887  1.00 54.79           C
ANISOU  822  CZ  ARG A 102     8120   6362   6335   -163   -664    229       C
ATOM    823  NH1 ARG A 102     -29.125 -22.311 -28.580  1.00 54.37           N
ANISOU  823  NH1 ARG A 102     9493   5121   6045    437   -462   -769       N
ATOM    824  NH2 ARG A 102     -27.760 -20.485 -28.537  1.00 54.70           N
ANISOU  824  NH2 ARG A 102     7697   7042   6042   -468    115    277       N
ATOM    825  N   TYR A 103     -24.567 -22.532 -22.421  1.00 31.98           N
ANISOU  825  N   TYR A 103     3580   3880   4690   -330    102  -1102       N
ATOM    826  CA  TYR A 103     -23.409 -21.828 -21.862  1.00 31.06           C
ANISOU  826  CA  TYR A 103     3445   3813   4545    -53   -301  -1631       C
ATOM    827  C   TYR A 103     -22.182 -22.742 -21.824  1.00 31.48           C
ANISOU  827  C   TYR A 103     3946   3530   4486    230   -139   -636       C
ATOM    828  O   TYR A 103     -21.083 -22.334 -22.217  1.00 32.04           O
ANISOU  828  O   TYR A 103     3248   3545   5379    365    -12   -359       O
ATOM    829  CB  TYR A 103     -23.793 -21.293 -20.482  1.00 33.72           C
ANISOU  829  CB  TYR A 103     4186   3475   5153   -200   -396  -1000       C
ATOM    830  CG  TYR A 103     -22.718 -20.540 -19.733  1.00 35.04           C
ANISOU  830  CG  TYR A 103     3813   4154   5347    742  -1245  -1236       C
ATOM    831  CD1 TYR A 103     -21.874 -21.248 -18.913  1.00 44.93           C
ANISOU  831  CD1 TYR A 103     5193   4986   6890   1122  -1715   -845       C
ATOM    832  CD2 TYR A 103     -22.577 -19.166 -19.769  1.00 41.50           C
ANISOU  832  CD2 TYR A 103     4840   4689   6240    360  -1364  -1095       C
ATOM    833  CE1 TYR A 103     -20.906 -20.629 -18.149  1.00 51.84           C
ANISOU  833  CE1 TYR A 103     6290   5771   7637    347  -2026  -1058       C
ATOM    834  CE2 TYR A 103     -21.614 -18.514 -18.994  1.00 40.99           C
ANISOU  834  CE2 TYR A 103     5001   3632   6943   -300  -1588   -763       C
ATOM    835  CZ  TYR A 103     -20.763 -19.256 -18.189  1.00 50.83           C
ANISOU  835  CZ  TYR A 103     5997   5504   7812    -58  -1681   -579       C
ATOM    836  OH  TYR A 103     -19.766 -18.783 -17.374  1.00 51.20           O
ANISOU  836  OH  TYR A 103     7382   5000   7070    523  -2379     63       O
ATOM    837  N   GLN A 104     -22.363 -23.952 -21.290  1.00 32.14           N
ANISOU  837  N   GLN A 104     4110   3477   4624    648    123   -350       N
ATOM    838  CA  GLN A 104     -21.262 -24.896 -21.157  1.00 34.94           C
ANISOU  838  CA  GLN A 104     4456   3706   5112    612    393    126       C
ATOM    839  C   GLN A 104     -20.727 -25.270 -22.536  1.00 34.37           C
ANISOU  839  C   GLN A 104     4181   4029   4848    845    374   -488       C
ATOM    840  O   GLN A 104     -19.515 -25.308 -22.708  1.00 35.97           O
ANISOU  840  O   GLN A 104     3976   4064   5625    824    355    135       O
ATOM    841  CB  GLN A 104     -21.699 -26.156 -20.415  1.00 40.00           C
ANISOU  841  CB  GLN A 104     4989   4869   5340    325    744    602       C
ATOM    842  CG  GLN A 104     -21.953 -25.896 -18.934  1.00 44.37           C
ANISOU  842  CG  GLN A 104     6101   5766   4990    688    310   1043       C
ATOM    843  CD  GLN A 104     -22.783 -26.987 -18.293  1.00 51.47           C
ANISOU  843  CD  GLN A 104     7385   6770   5402   -160   1051    220       C
ATOM    844  OE1 GLN A 104     -23.284 -27.881 -18.984  1.00 59.60           O
ANISOU  844  OE1 GLN A 104     8286   5382   8975    368   1791   -798       O
ATOM    845  NE2 GLN A 104     -22.975 -26.908 -16.982  1.00 62.97           N
ANISOU  845  NE2 GLN A 104     8838   9063   6025     83    -61    745       N
ATOM    846  N   GLN A 105     -21.627 -25.552 -23.498  1.00 33.79           N
ANISOU  846  N   GLN A 105     3862   3851   5128    152    339   -730       N
ATOM    847  CA  GLN A 105     -21.215 -25.878 -24.860  1.00 36.27           C
ANISOU  847  CA  GLN A 105     4228   4029   5522    370    325   -866       C
ATOM    848  C   GLN A 105     -20.460 -24.713 -25.517  1.00 31.68           C
ANISOU  848  C   GLN A 105     3839   3455   4741    594    -49   -794       C
ATOM    849  O   GLN A 105     -19.423 -24.903 -26.130  1.00 35.90           O
ANISOU  849  O   GLN A 105     4098   3788   5752    753    443   -657       O
ATOM    850  CB  GLN A 105     -22.410 -26.307 -25.701  1.00 39.10           C
ANISOU  850  CB  GLN A 105     4532   4682   5641    143    424  -1600       C
ATOM    851  CG  GLN A 105     -22.081 -26.606 -27.152  1.00 42.66           C
ANISOU  851  CG  GLN A 105     4726   5861   5621   -567    763  -1117       C
ATOM    852  N   PHE A 106     -20.926 -23.478 -25.293  1.00 30.98           N
ANISOU  852  N   PHE A 106     3488   3601   4681    630    156   -620       N
ATOM    853  CA  PHE A 106     -20.276 -22.318 -25.869  1.00 31.26           C
ANISOU  853  CA  PHE A 106     3681   3757   4441    569    282   -279       C
ATOM    854  C   PHE A 106     -18.850 -22.201 -25.342  1.00 30.88           C
ANISOU  854  C   PHE A 106     3647   3622   4464    591    165   -156       C
ATOM    855  O   PHE A 106     -17.912 -21.976 -26.108  1.00 31.48           O
ANISOU  855  O   PHE A 106     3283   3952   4725    612    560   -335       O
ATOM    856  CB  PHE A 106     -21.089 -21.057 -25.574  1.00 33.62           C
ANISOU  856  CB  PHE A 106     4076   3939   4759    657    372    -68       C
ATOM    857  CG  PHE A 106     -20.365 -19.799 -26.003  1.00 36.74           C
ANISOU  857  CG  PHE A 106     3760   4118   6080    802    754   -440       C
ATOM    858  CD1 PHE A 106     -20.382 -19.376 -27.331  1.00 42.88           C
ANISOU  858  CD1 PHE A 106     4543   5160   6587    478    892   -248       C
ATOM    859  CD2 PHE A 106     -19.679 -19.032 -25.073  1.00 36.10           C
ANISOU  859  CD2 PHE A 106     3171   4010   6535    368    496   -431       C
ATOM    860  CE1 PHE A 106     -19.705 -18.225 -27.716  1.00 42.40           C
ANISOU  860  CE1 PHE A 106     4604   4889   6619    114    993   -129       C
ATOM    861  CE2 PHE A 106     -18.964 -17.912 -25.478  1.00 36.62           C
ANISOU  861  CE2 PHE A 106     3416   4026   6470    127   1202    497       C
ATOM    862  CZ  PHE A 106     -19.001 -17.502 -26.786  1.00 39.97           C
ANISOU  862  CZ  PHE A 106     4140   4391   6656    347    554    -72       C
ATOM    863  N   PHE A 107     -18.686 -22.303 -24.025  1.00 32.09           N
ANISOU  863  N   PHE A 107     3058   4222   4911    391    430   -251       N
ATOM    864  CA  PHE A 107     -17.362 -22.077 -23.469  1.00 33.45           C
ANISOU  864  CA  PHE A 107     2698   4654   5357    327    250   -542       C
ATOM    865  C   PHE A 107     -16.407 -23.205 -23.850  1.00 33.99           C
ANISOU  865  C   PHE A 107     3578   4157   5180    800   -186    -29       C
ATOM    866  O   PHE A 107     -15.236 -22.934 -24.128  1.00 35.79           O
ANISOU  866  O   PHE A 107     3208   5390   5000    126   -237    120       O
ATOM    867  CB  PHE A 107     -17.458 -21.734 -21.986  1.00 38.89           C
ANISOU  867  CB  PHE A 107     3714   5005   6058    266    171  -1114       C
ATOM    868  CG  PHE A 107     -17.806 -20.256 -21.862  1.00 44.22           C
ANISOU  868  CG  PHE A 107     4232   5359   7211    369   -482   -589       C
ATOM    869  CD1 PHE A 107     -16.821 -19.281 -21.973  1.00 44.91           C
ANISOU  869  CD1 PHE A 107     4887   4911   7266    249   -322   -479       C
ATOM    870  CD2 PHE A 107     -19.117 -19.838 -21.687  1.00 44.09           C
ANISOU  870  CD2 PHE A 107     4427   4878   7447    411   -267  -1416       C
ATOM    871  CE1 PHE A 107     -17.143 -17.936 -21.872  1.00 48.11           C
ANISOU  871  CE1 PHE A 107     4843   5307   8129     87    -96   -930       C
ATOM    872  CE2 PHE A 107     -19.426 -18.495 -21.595  1.00 45.05           C
ANISOU  872  CE2 PHE A 107     3904   5369   7845    255   -767   -923       C
ATOM    873  CZ  PHE A 107     -18.446 -17.547 -21.690  1.00 47.47           C
ANISOU  873  CZ  PHE A 107     4897   5128   8011    -61   -359   -661       C
ATOM    874  N   LEU A 108     -16.902 -24.441 -23.947  1.00 32.99           N
ANISOU  874  N   LEU A 108     3662   4213   4658    948   -269   -179       N
ATOM    875  CA  LEU A 108     -16.055 -25.531 -24.405  1.00 37.32           C
ANISOU  875  CA  LEU A 108     4259   4654   5264   1461    -62   -541       C
ATOM    876  C   LEU A 108     -15.598 -25.240 -25.833  1.00 37.01           C
ANISOU  876  C   LEU A 108     4087   4085   5892   1399   -114   -446       C
ATOM    877  O   LEU A 108     -14.412 -25.278 -26.141  1.00 42.72           O
ANISOU  877  O   LEU A 108     4015   5394   6824   1037     61   -588       O
ATOM    878  CB  LEU A 108     -16.829 -26.837 -24.269  1.00 39.09           C
ANISOU  878  CB  LEU A 108     5165   4293   5396   1242     95   -575       C
ATOM    879  CG  LEU A 108     -15.984 -28.096 -24.031  1.00 49.89           C
ANISOU  879  CG  LEU A 108     6713   5315   6928   1384    158   -397       C
ATOM    880  CD1 LEU A 108     -16.612 -29.264 -24.748  1.00 52.33           C
ANISOU  880  CD1 LEU A 108     6397   6031   7453   1291   -380   -394       C
ATOM    881  N   GLU A 109     -16.531 -24.899 -26.707  1.00 36.23           N
ANISOU  881  N   GLU A 109     4390   4034   5343    981     -3   -776       N
ATOM    882  CA  GLU A 109     -16.201 -24.597 -28.089  1.00 35.43           C
ANISOU  882  CA  GLU A 109     4277   4482   4704    828    192   -476       C
ATOM    883  C   GLU A 109     -15.289 -23.389 -28.192  1.00 34.99           C
ANISOU  883  C   GLU A 109     4194   4775   4325    900    512   -486       C
ATOM    884  O   GLU A 109     -14.375 -23.415 -29.012  1.00 36.47           O
ANISOU  884  O   GLU A 109     4119   4838   4899    590   1181   -557       O
ATOM    885  CB  GLU A 109     -17.487 -24.368 -28.884  1.00 37.71           C
ANISOU  885  CB  GLU A 109     4358   5359   4610    925    213   -381       C
ATOM    886  CG  GLU A 109     -18.202 -25.686 -29.121  1.00 47.71           C
ANISOU  886  CG  GLU A 109     5831   6171   6126    445   -417   -488       C
ATOM    887  CD  GLU A 109     -19.520 -25.572 -29.837  1.00 52.04           C
ANISOU  887  CD  GLU A 109     6164   6705   6903    703  -1144   -448       C
ATOM    888  OE1 GLU A 109     -20.239 -26.583 -29.831  1.00 59.82           O
ANISOU  888  OE1 GLU A 109     6805   7821   8102    339  -1613  -1320       O
ATOM    889  OE2 GLU A 109     -19.810 -24.492 -30.375  1.00 62.08           O
ANISOU  889  OE2 GLU A 109     6703   7854   9032   -176  -2177     86       O
ATOM    890  N   ALA A 110     -15.595 -22.334 -27.423  1.00 31.35           N
ANISOU  890  N   ALA A 110     3187   4286   4438    407     37   -410       N
ATOM    891  CA  ALA A 110     -14.762 -21.130 -27.426  1.00 34.01           C
ANISOU  891  CA  ALA A 110     3787   4711   4422    298    -91   -353       C
ATOM    892  C   ALA A 110     -13.308 -21.443 -27.032  1.00 34.86           C
ANISOU  892  C   ALA A 110     3759   4628   4857    455     38    -87       C
ATOM    893  O   ALA A 110     -12.389 -20.959 -27.685  1.00 35.52           O
ANISOU  893  O   ALA A 110     3865   4897   4735    695    263    257       O
ATOM    894  CB  ALA A 110     -15.355 -20.070 -26.548  1.00 35.79           C
ANISOU  894  CB  ALA A 110     3622   4710   5267    155    430   -233       C
ATOM    895  N   SER A 111     -13.104 -22.277 -25.997  1.00 35.38           N
ANISOU  895  N   SER A 111     3503   4964   4975    694     55   -286       N
ATOM    896  CA  SER A 111     -11.773 -22.618 -25.534  1.00 35.98           C
ANISOU  896  CA  SER A 111     3431   5080   5160    154      6    144       C
ATOM    897  C   SER A 111     -10.942 -23.176 -26.674  1.00 36.94           C
ANISOU  897  C   SER A 111     3556   5123   5358    702    104    491       C
ATOM    898  O   SER A 111      -9.785 -22.796 -26.797  1.00 36.95           O
ANISOU  898  O   SER A 111     2886   5745   5407    457    152    394       O
ATOM    899  CB  SER A 111     -11.758 -23.565 -24.323  1.00 38.65           C
ANISOU  899  CB  SER A 111     3718   5753   5215   -326   -100    355       C
ATOM    900  OG  SER A 111     -12.384 -24.826 -24.565  1.00 45.88           O
ANISOU  900  OG  SER A 111     5329   5992   6109    -91   -425    397       O
ATOM    901  N   VAL A 112     -11.550 -24.054 -27.474  1.00 36.79           N
ANISOU  901  N   VAL A 112     3982   4507   5488   1099    517    454       N
ATOM    902  CA  VAL A 112     -10.889 -24.686 -28.595  1.00 37.70           C
ANISOU  902  CA  VAL A 112     4257   4459   5609   1520    627    643       C
ATOM    903  C   VAL A 112     -10.629 -23.650 -29.693  1.00 36.30           C
ANISOU  903  C   VAL A 112     4018   4216   5556    981    675    430       C
ATOM    904  O   VAL A 112      -9.486 -23.482 -30.104  1.00 41.36           O
ANISOU  904  O   VAL A 112     3835   6172   5706   1628    523    154       O
ATOM    905  CB  VAL A 112     -11.733 -25.853 -29.128  1.00 44.42           C
ANISOU  905  CB  VAL A 112     5389   4847   6640   1323   1535    373       C
ATOM    906  CG1 VAL A 112     -11.050 -26.468 -30.342  1.00 47.85           C
ANISOU  906  CG1 VAL A 112     6321   4753   7106   1264   2126    195       C
ATOM    907  CG2 VAL A 112     -12.000 -26.923 -28.067  1.00 44.61           C
ANISOU  907  CG2 VAL A 112     4514   5242   7195   1733   1744    633       C
ATOM    908  N   GLN A 113     -11.677 -22.907 -30.093  1.00 37.57           N
ANISOU  908  N   GLN A 113     4305   4789   5180   1458    949    514       N
ATOM    909  CA  GLN A 113     -11.600 -21.865 -31.121  1.00 34.17           C
ANISOU  909  CA  GLN A 113     4222   3716   5044   1539    691    511       C
ATOM    910  C   GLN A 113     -10.463 -20.872 -30.834  1.00 35.85           C
ANISOU  910  C   GLN A 113     3624   5289   4708   1162    580    429       C
ATOM    911  O   GLN A 113      -9.690 -20.494 -31.735  1.00 38.53           O
ANISOU  911  O   GLN A 113     4459   5079   5103   1423    984    200       O
ATOM    912  CB  GLN A 113     -12.972 -21.200 -31.312  1.00 40.40           C
ANISOU  912  CB  GLN A 113     4433   5503   5413   1335    -64   1401       C
ATOM    913  N   PHE A 114     -10.340 -20.465 -29.574  1.00 34.40           N
ANISOU  913  N   PHE A 114     3428   4707   4936    871    847    644       N
ATOM    914  CA  PHE A 114      -9.369 -19.454 -29.201  1.00 32.08           C
ANISOU  914  CA  PHE A 114     3394   4286   4510    651    390    959       C
ATOM    915  C   PHE A 114      -7.977 -20.053 -28.994  1.00 33.52           C
ANISOU  915  C   PHE A 114     3257   4511   4969    762    738    446       C
ATOM    916  O   PHE A 114      -7.035 -19.297 -28.782  1.00 35.33           O
ANISOU  916  O   PHE A 114     3697   4427   5298    695    650    482       O
ATOM    917  CB  PHE A 114      -9.802 -18.755 -27.923  1.00 35.77           C
ANISOU  917  CB  PHE A 114     3561   4439   5589    666    887    920       C
ATOM    918  CG  PHE A 114     -11.165 -18.094 -27.967  1.00 36.67           C
ANISOU  918  CG  PHE A 114     3387   4286   6260    568    746    847       C
ATOM    919  CD1 PHE A 114     -11.726 -17.644 -29.164  1.00 41.04           C
ANISOU  919  CD1 PHE A 114     4262   4449   6883   1590   -129    279       C
ATOM    920  CD2 PHE A 114     -11.875 -17.925 -26.786  1.00 41.06           C
ANISOU  920  CD2 PHE A 114     4068   4715   6818   1195    992    182       C
ATOM    921  CE1 PHE A 114     -12.962 -17.016 -29.165  1.00 42.80           C
ANISOU  921  CE1 PHE A 114     4485   4422   7356   1328    -64   -262       C
ATOM    922  CE2 PHE A 114     -13.100 -17.272 -26.801  1.00 40.84           C
ANISOU  922  CE2 PHE A 114     3486   4490   7541    613   1171    710       C
ATOM    923  CZ  PHE A 114     -13.665 -16.885 -28.000  1.00 42.81           C
ANISOU  923  CZ  PHE A 114     4413   4659   7196   1223    250    915       C
ATOM    924  N   GLY A 115      -7.867 -21.388 -28.973  1.00 36.31           N
ANISOU  924  N   GLY A 115     3768   4642   5386    715    633   1068       N
ATOM    925  CA  GLY A 115      -6.613 -22.080 -28.688  1.00 34.21           C
ANISOU  925  CA  GLY A 115     3825   4260   4915    466     98    345       C
ATOM    926  C   GLY A 115      -6.095 -21.943 -27.253  1.00 35.04           C
ANISOU  926  C   GLY A 115     3285   4731   5298   1025     58    946       C
ATOM    927  O   GLY A 115      -4.864 -21.891 -27.033  1.00 34.13           O
ANISOU  927  O   GLY A 115     2858   4425   5685    472    163    650       O
ATOM    928  N   VAL A 116      -7.009 -21.971 -26.279  1.00 31.86           N
ANISOU  928  N   VAL A 116     3284   4124   4695    613      6    533       N
ATOM    929  CA  VAL A 116      -6.617 -21.938 -24.887  1.00 32.43           C
ANISOU  929  CA  VAL A 116     3416   4194   4711    443    515    868       C
ATOM    930  C   VAL A 116      -6.100 -23.317 -24.499  1.00 33.85           C
ANISOU  930  C   VAL A 116     3599   4115   5145    431    309    899       C
ATOM    931  O   VAL A 116      -6.791 -24.336 -24.704  1.00 34.56           O
ANISOU  931  O   VAL A 116     3423   4463   5246    440     68    740       O
ATOM    932  CB  VAL A 116      -7.716 -21.479 -23.939  1.00 32.62           C
ANISOU  932  CB  VAL A 116     3258   4490   4644    760    663    488       C
ATOM    933  CG1 VAL A 116      -7.199 -21.368 -22.512  1.00 38.89           C
ANISOU  933  CG1 VAL A 116     4380   5617   4778   1011   1001    610       C
ATOM    934  CG2 VAL A 116      -8.341 -20.187 -24.402  1.00 35.43           C
ANISOU  934  CG2 VAL A 116     3338   4731   5392   1009    458    578       C
ATOM    935  N   PRO A 117      -4.865 -23.394 -23.959  1.00 32.62           N
ANISOU  935  N   PRO A 117     3392   4013   4988    333    195    630       N
ATOM    936  CA  PRO A 117      -4.318 -24.666 -23.520  1.00 32.07           C
ANISOU  936  CA  PRO A 117     3375   4068   4742    833     10    773       C
ATOM    937  C   PRO A 117      -5.193 -25.196 -22.405  1.00 34.97           C
ANISOU  937  C   PRO A 117     3813   4653   4818    880    228    563       C
ATOM    938  O   PRO A 117      -5.564 -24.447 -21.509  1.00 37.63           O
ANISOU  938  O   PRO A 117     4030   5096   5174   1357    675    922       O
ATOM    939  CB  PRO A 117      -2.942 -24.332 -23.011  1.00 33.91           C
ANISOU  939  CB  PRO A 117     3109   4353   5423    848     49    811       C
ATOM    940  CG  PRO A 117      -2.581 -23.078 -23.674  1.00 38.27           C
ANISOU  940  CG  PRO A 117     3231   4792   6519    390   -263   1077       C
ATOM    941  CD  PRO A 117      -3.857 -22.315 -23.833  1.00 34.12           C
ANISOU  941  CD  PRO A 117     3272   4077   5614    871     95    537       C
ATOM    942  N   GLU A 118      -5.465 -26.483 -22.464  1.00 31.79           N
ANISOU  942  N   GLU A 118     3148   3754   5176   1054    839    348       N
ATOM    943  CA  GLU A 118      -6.401 -27.104 -21.551  1.00 35.23           C
ANISOU  943  CA  GLU A 118     3082   5015   5290    928    586    647       C
ATOM    944  C   GLU A 118      -5.959 -26.878 -20.100  1.00 37.65           C
ANISOU  944  C   GLU A 118     3676   4958   5671    532    780    825       C
ATOM    945  O   GLU A 118      -6.812 -26.773 -19.235  1.00 41.81           O
ANISOU  945  O   GLU A 118     4407   5538   5941   1236   1389    763       O
ATOM    946  CB  GLU A 118      -6.596 -28.561 -21.967  1.00 36.65           C
ANISOU  946  CB  GLU A 118     3306   5189   5431    482    813    864       C
ATOM    947  CG  GLU A 118      -7.296 -28.767 -23.304  1.00 44.94           C
ANISOU  947  CG  GLU A 118     4456   6076   6543    569    325    437       C
ATOM    948  CD  GLU A 118      -6.476 -28.849 -24.588  1.00 49.13           C
ANISOU  948  CD  GLU A 118     5312   6913   6441     41    350   -442       C
ATOM    949  OE1 GLU A 118      -6.843 -29.775 -25.368  1.00 55.43           O
ANISOU  949  OE1 GLU A 118     8164   6714   6184   -200    207   -986       O
ATOM    950  OE2 GLU A 118      -5.513 -28.026 -24.823  1.00 45.17           O
ANISOU  950  OE2 GLU A 118     3577   7212   6374    531   -552    403       O
ATOM    951  N   VAL A 119      -4.635 -26.802 -19.823  1.00 33.98           N
ANISOU  951  N   VAL A 119     3578   5130   4203   1186    161    701       N
ATOM    952  CA  VAL A 119      -4.163 -26.670 -18.453  1.00 37.03           C
ANISOU  952  CA  VAL A 119     3804   5793   4471    873    497    767       C
ATOM    953  C   VAL A 119      -4.623 -25.352 -17.829  1.00 39.05           C
ANISOU  953  C   VAL A 119     4502   6194   4143    715    844    898       C
ATOM    954  O   VAL A 119      -4.649 -25.261 -16.611  1.00 48.28           O
ANISOU  954  O   VAL A 119     5753   8403   4189   1413   1593    207       O
ATOM    955  CB  VAL A 119      -2.639 -26.775 -18.307  1.00 37.51           C
ANISOU  955  CB  VAL A 119     4346   5726   4178    114    188    834       C
ATOM    956  CG1 VAL A 119      -2.146 -28.154 -18.630  1.00 41.07           C
ANISOU  956  CG1 VAL A 119     4888   6157   4561    307    363    491       C
ATOM    957  CG2 VAL A 119      -1.925 -25.705 -19.101  1.00 40.19           C
ANISOU  957  CG2 VAL A 119     4489   5930   4852     43    722   1077       C
ATOM    958  N   LEU A 120      -4.924 -24.330 -18.645  1.00 40.74           N
ANISOU  958  N   LEU A 120     3904   6528   5048   1511    810    601       N
ATOM    959  CA  LEU A 120      -5.266 -23.027 -18.101  1.00 46.33           C
ANISOU  959  CA  LEU A 120     4333   7225   6044   1155    749   -298       C
ATOM    960  C   LEU A 120      -6.771 -22.955 -17.852  1.00 49.54           C
ANISOU  960  C   LEU A 120     4108   7979   6736   2361    354  -1354       C
ATOM    961  O   LEU A 120      -7.215 -22.086 -17.101  1.00 58.93           O
ANISOU  961  O   LEU A 120     7902   7310   7179   2483    566  -1542       O
ATOM    962  CB  LEU A 120      -4.771 -21.917 -19.035  1.00 48.37           C
ANISOU  962  CB  LEU A 120     4742   7387   6248   1348   -139   -161       C
ATOM    963  CG  LEU A 120      -3.306 -21.483 -18.871  1.00 55.89           C
ANISOU  963  CG  LEU A 120     5450   8190   7597   1289    272   -272       C
ATOM    964  CD1 LEU A 120      -2.527 -22.348 -17.899  1.00 57.54           C
ANISOU  964  CD1 LEU A 120     5573   8296   7993   2273    499    -91       C
ATOM    965  CD2 LEU A 120      -2.556 -21.449 -20.198  1.00 56.46           C
ANISOU  965  CD2 LEU A 120     4788   7993   8670   1395    420   -673       C
ATOM    966  N   LEU A 121      -7.539 -23.869 -18.462  1.00 54.24           N
ANISOU  966  N   LEU A 121     4279   8791   7540   1749   1292  -2280       N
ATOM    967  CA  LEU A 121      -8.999 -23.805 -18.453  1.00 54.59           C
ANISOU  967  CA  LEU A 121     3898   9338   7507   2489    781  -1590       C
ATOM    968  C   LEU A 121      -9.515 -24.074 -17.049  1.00 61.21           C
ANISOU  968  C   LEU A 121     4629  10147   8483   1631    718   -727       C
ATOM    969  O   LEU A 121      -8.894 -24.828 -16.295  1.00 51.82           O
ANISOU  969  O   LEU A 121     3759   9317   6614    632    135   -215       O
ATOM    970  CB  LEU A 121      -9.619 -24.809 -19.420  1.00 56.86           C
ANISOU  970  CB  LEU A 121     3819   9730   8056   2225   -152   -567       C
ATOM    971  CG  LEU A 121      -9.440 -24.497 -20.908  1.00 59.35           C
ANISOU  971  CG  LEU A 121     4288  10338   7924   1454   -244   -507       C
ATOM    972  CD1 LEU A 121     -10.134 -25.539 -21.780  1.00 63.20           C
ANISOU  972  CD1 LEU A 121     4391  10966   8656    837   -131   -363       C
ATOM    973  CD2 LEU A 121      -9.945 -23.085 -21.184  1.00 56.90           C
ANISOU  973  CD2 LEU A 121     3990  10476   7153   1047   -526     18       C
ATOM    974  N   PRO A 122     -10.717 -23.533 -16.693  1.00 70.10           N
ANISOU  974  N   PRO A 122     5662  11312   9661   1900    947     55       N
ATOM    975  CA  PRO A 122     -11.298 -23.756 -15.375  1.00 73.43           C
ANISOU  975  CA  PRO A 122     7216  11787   8897   1973   1310    161       C
ATOM    976  C   PRO A 122     -11.155 -25.236 -15.040  1.00 76.93           C
ANISOU  976  C   PRO A 122     9025  12313   7891   2186    682    856       C
ATOM    977  O   PRO A 122     -10.803 -25.589 -13.916  1.00 72.17           O
ANISOU  977  O   PRO A 122     8440  12775   6206   1694    257   1558       O
ATOM    978  CB  PRO A 122     -12.763 -23.287 -15.497  1.00 77.63           C
ANISOU  978  CB  PRO A 122     7321  12003  10173   1492   1046    409       C
ATOM    979  CG  PRO A 122     -12.977 -23.099 -16.992  1.00 76.37           C
ANISOU  979  CG  PRO A 122     6628  12134  10255   1470   1359    232       C
ATOM    980  CD  PRO A 122     -11.605 -22.727 -17.544  1.00 72.01           C
ANISOU  980  CD  PRO A 122     5810  11433  10118   2053   1363     97       C
ATOM    981  N   GLN A 123     -11.419 -26.078 -16.050  1.00 86.95           N
ANISOU  981  N   GLN A 123    10172  13210   9656   1609   1589    -34       N
ATOM    982  CA  GLN A 123     -11.159 -27.509 -15.993  1.00102.49           C
ANISOU  982  CA  GLN A 123    11703  14684  12556   1827   1077   -768       C
ATOM    983  C   GLN A 123     -11.786 -28.073 -14.717  1.00108.04           C
ANISOU  983  C   GLN A 123    13351  16034  11665   1368    444    -43       C
ATOM    984  O   GLN A 123     -13.013 -28.157 -14.626  1.00116.62           O
ANISOU  984  O   GLN A 123    14241  17529  12541    696   1220    503       O
ATOM    985  CB  GLN A 123      -9.665 -27.772 -16.215  1.00109.17           C
ANISOU  985  CB  GLN A 123    11492  15637  14350   2202    262  -1839       C
ATOM    986  CG  GLN A 123      -9.353 -29.222 -16.578  1.00114.23           C
ANISOU  986  CG  GLN A 123    11206  16361  15835   2103   -517  -2627       C
ATOM    987  CD  GLN A 123      -8.290 -29.360 -17.646  1.00113.11           C
ANISOU  987  CD  GLN A 123    10555  15775  16645   2565  -1406  -2985       C
ATOM    988  OE1 GLN A 123      -7.087 -29.423 -17.359  1.00112.67           O
ANISOU  988  OE1 GLN A 123    11454  13894  17459   2696  -3392  -2793       O
ATOM    989  NE2 GLN A 123      -8.737 -29.441 -18.893  1.00106.82           N
ANISOU  989  NE2 GLN A 123     8467  14879  17240   2474  -3001  -3255       N
ATOM    990  N   GLY A 124     -10.956 -28.465 -13.742  1.00101.40           N
ANISOU  990  N   GLY A 124    12388  15349  10790   1058   -289   -442       N
ATOM    991  CA  GLY A 124     -11.449 -28.748 -12.406  1.00 98.93           C
ANISOU  991  CA  GLY A 124    12504  14481  10604    500   -612  -1458       C
ATOM    992  C   GLY A 124     -11.881 -27.453 -11.727  1.00 89.96           C
ANISOU  992  C   GLY A 124    10818  14237   9125   -696   -780  -2115       C
ATOM    993  O   GLY A 124     -13.071 -27.146 -11.672  1.00 96.56           O
ANISOU  993  O   GLY A 124    11622  16853   8213   -226  -2055   -442       O
ATOM    994  N   ALA A 125     -10.888 -26.677 -11.269  1.00 82.82           N
ANISOU  994  N   ALA A 125     9970  12339   9160   -454   -412  -2135       N
ATOM    995  CA  ALA A 125     -11.153 -25.435 -10.554  1.00 58.30           C
ANISOU  995  CA  ALA A 125     6056   9818   6278  -1418  -2045  -1711       C
ATOM    996  C   ALA A 125      -9.877 -24.616 -10.342  1.00 63.00           C
ANISOU  996  C   ALA A 125     6466  10230   7242  -1034  -1061  -1122       C
ATOM    997  O   ALA A 125      -8.804 -25.000 -10.853  1.00 64.70           O
ANISOU  997  O   ALA A 125     7139  10756   6686  -1437   -755   -573       O
ATOM    998  CB  ALA A 125     -11.851 -25.783  -9.305  1.00 49.04           C
ANISOU  998  CB  ALA A 125     1833  10013   6786  -1209  -1559  -2398       C
ATOM    999  N   LEU A 126     -10.041 -23.500  -9.589  1.00 38.38           N
ANISOU  999  N   LEU A 126     3940   7433   3208  -1078   -446   -439       N
ATOM   1000  CA  LEU A 126      -9.323 -22.270  -9.833  1.00 55.94           C
ANISOU 1000  CA  LEU A 126     6993   8865   5399   -548   -787    785       C
ATOM   1001  C   LEU A 126      -9.243 -21.477  -8.545  1.00 78.19           C
ANISOU 1001  C   LEU A 126    10068  11425   8217   -646   -350   -464       C
ATOM   1002  O   LEU A 126      -9.216 -20.250  -8.574  1.00 96.03           O
ANISOU 1002  O   LEU A 126    12773  11737  11975  -1901    877    504       O
ATOM   1003  CB  LEU A 126      -9.993 -21.398 -10.891  1.00 60.69           C
ANISOU 1003  CB  LEU A 126     8284   8743   6032  -1036   -940   3331       C
ATOM   1004  CG  LEU A 126      -9.226 -21.188 -12.208  1.00 75.96           C
ANISOU 1004  CG  LEU A 126     9426  11549   7885  -1296   -313    474       C
ATOM   1005  CD1 LEU A 126      -7.867 -20.917 -11.790  1.00 86.11           C
ANISOU 1005  CD1 LEU A 126    10254  12390  10075  -1102   -367    390       C
ATOM   1006  CD2 LEU A 126      -9.107 -22.281 -13.233  1.00 80.32           C
ANISOU 1006  CD2 LEU A 126    10341  12211   7964  -1467   -735   -521       C
ATOM   1007  N   LEU A 127      -9.255 -22.213  -7.434  1.00 97.76           N
ANISOU 1007  N   LEU A 127    12567  13857  10720   -718   -295    421       N
ATOM   1008  CA  LEU A 127      -9.707 -21.670  -6.141  1.00111.55           C
ANISOU 1008  CA  LEU A 127    12654  17795  11935   -288  -1522  -1290       C
ATOM   1009  C   LEU A 127     -11.210 -21.311  -6.344  1.00126.65           C
ANISOU 1009  C   LEU A 127    12463  20026  15630    341  -2367  -1931       C
ATOM   1010  O   LEU A 127     -11.844 -20.905  -5.329  1.00125.92           O
ANISOU 1010  O   LEU A 127    11400  21570  14875   -545  -2520  -2291       O
ATOM   1011  CB  LEU A 127      -8.864 -20.488  -5.547  1.00120.14           C
ANISOU 1011  CB  LEU A 127    14334  19618  11697   -515  -2608  -1607       C
ATOM   1012  CG  LEU A 127      -7.438 -20.732  -4.872  1.00130.15           C
ANISOU 1012  CG  LEU A 127    15999  21608  11845   -149  -2970  -1523       C
ATOM   1013  CD1 LEU A 127      -6.300 -21.491  -5.725  1.00139.35           C
ANISOU 1013  CD1 LEU A 127    16882  22472  13594    201  -2298  -1478       C
ATOM   1014  CD2 LEU A 127      -6.538 -19.478  -4.307  1.00127.98           C
ANISOU 1014  CD2 LEU A 127    16853  22285   9487   -135  -3689  -1756       C
ATOM   1015  N   THR A 128     -11.788 -21.606  -7.609  1.00133.07           N
ANISOU 1015  N   THR A 128    11665  20779  18118    832  -4445  -2168       N
ATOM   1016  CA  THR A 128     -13.198 -21.300  -8.032  1.00142.18           C
ANISOU 1016  CA  THR A 128    13314  20469  20237   1439  -5976  -1645       C
ATOM   1017  C   THR A 128     -13.607 -21.778  -9.476  1.00136.58           C
ANISOU 1017  C   THR A 128    13680  18187  20029   1374  -4367  -2003       C
ATOM   1018  O   THR A 128     -12.920 -21.429 -10.443  1.00144.95           O
ANISOU 1018  O   THR A 128    13636  19636  21804   2457  -2574   -981       O
ATOM   1019  CB  THR A 128     -13.399 -19.771  -7.748  1.00159.19           C
ANISOU 1019  CB  THR A 128    16423  20752  23311    889  -6624  -1053       C
ATOM   1020  OG1 THR A 128     -14.473 -19.074  -8.408  1.00178.83           O
ANISOU 1020  OG1 THR A 128    19838  21388  26721   1711  -6893    302       O
ATOM   1021  CG2 THR A 128     -12.239 -18.929  -8.238  1.00156.41           C
ANISOU 1021  CG2 THR A 128    16427  19783  23219    692  -7375   -479       C
ATOM   1022  N   LYS A 129     -14.758 -22.547  -9.624  1.00118.08           N
ANISOU 1022  N   LYS A 129    14259  14567  16040    785  -3860  -2686       N
ATOM   1023  CA  LYS A 129     -15.113 -23.288 -10.838  1.00 98.01           C
ANISOU 1023  CA  LYS A 129    12706  10946  13588   -673  -3038  -1973       C
ATOM   1024  C   LYS A 129     -15.809 -22.241 -11.717  1.00105.64           C
ANISOU 1024  C   LYS A 129    13934  14496  11707   -884  -2944  -1316       C
ATOM   1025  O   LYS A 129     -15.086 -21.474 -12.354  1.00109.13           O
ANISOU 1025  O   LYS A 129    13800  17516  10147  -2620  -2271  -1969       O
ATOM   1026  CB  LYS A 129     -15.926 -24.608 -10.770  1.00 82.98           C
ANISOU 1026  CB  LYS A 129    13289   7205  11034    666  -1625  -2593       C
ATOM   1027  CG  LYS A 129     -16.213 -25.369  -9.457  1.00 67.89           C
ANISOU 1027  CG  LYS A 129    11648   3010  11138    285  -1090  -2435       C
ATOM   1028  CD  LYS A 129     -15.408 -26.618  -9.092  1.00 63.88           C
ANISOU 1028  CD  LYS A 129    10175   4450   9646   -827   -943   -942       C
ATOM   1029  CE  LYS A 129     -15.349 -26.857  -7.606  1.00 61.01           C
ANISOU 1029  CE  LYS A 129     8999   4594   9587   -639   -326  -1371       C
ATOM   1030  NZ  LYS A 129     -14.835 -25.710  -6.861  1.00 53.47           N
ANISOU 1030  NZ  LYS A 129     7873   4536   7908    740   -219  -1577       N
ATOM   1031  N   THR A 130     -17.166 -22.124 -11.665  1.00110.44           N
ANISOU 1031  N   THR A 130    13306  15651  13005   -539  -1479  -1023       N
ATOM   1032  CA  THR A 130     -17.940 -21.234 -12.544  1.00103.15           C
ANISOU 1032  CA  THR A 130    11409  15050  12732    595   -567  -1509       C
ATOM   1033  C   THR A 130     -19.453 -21.231 -12.224  1.00 96.70           C
ANISOU 1033  C   THR A 130    12211  12357  12174   2170    524  -1556       C
ATOM   1034  O   THR A 130     -19.976 -22.298 -11.889  1.00108.41           O
ANISOU 1034  O   THR A 130    14836  12692  13663   2522   2452  -1865       O
ATOM   1035  CB  THR A 130     -17.700 -21.665 -13.996  1.00110.21           C
ANISOU 1035  CB  THR A 130    13031  15672  13170    151    -62  -2275       C
ATOM   1036  OG1 THR A 130     -17.392 -23.059 -13.994  1.00114.66           O
ANISOU 1036  OG1 THR A 130    14351  15326  13889   -430    334  -3795       O
ATOM   1037  CG2 THR A 130     -16.586 -20.878 -14.671  1.00109.05           C
ANISOU 1037  CG2 THR A 130    13174  15698  12561    -66    -30  -1924       C
ATOM   1038  N   MET A 131     -20.145 -20.047 -12.366  1.00 73.06           N
ANISOU 1038  N   MET A 131     9774   9359   8625    720   -241  -1275       N
ATOM   1039  CA AMET A 131     -21.597 -19.870 -12.194  0.50 53.18           C
ANISOU 1039  CA AMET A 131     8423   6061   5720   1365   -819  -1508       C
ATOM   1040  CA BMET A 131     -21.597 -19.870 -12.194  0.50 53.24           C
ANISOU 1040  CA BMET A 131     8426   6060   5740   1366   -809  -1503       C
ATOM   1041  C   MET A 131     -21.998 -20.064 -10.726  1.00 42.27           C
ANISOU 1041  C   MET A 131     5536   4364   6161   1699   -410  -1368       C
ATOM   1042  O   MET A 131     -23.127 -19.737 -10.240  1.00 33.72           O
ANISOU 1042  O   MET A 131     4038   3511   5264    514  -1879   -314       O
ATOM   1043  CB AMET A 131     -22.375 -20.840 -13.086  0.50 62.04           C
ANISOU 1043  CB AMET A 131     8571   8002   6999    112  -1855  -1229       C
ATOM   1044  CB BMET A 131     -22.375 -20.840 -13.086  0.50 62.15           C
ANISOU 1044  CB BMET A 131     8573   7989   7049    109  -1834  -1228       C
ATOM   1045  CG AMET A 131     -22.832 -20.206 -14.396  0.50 66.72           C
ANISOU 1045  CG AMET A 131    10194   8033   7125   -245  -1703  -1100       C
ATOM   1046  CG BMET A 131     -22.835 -20.206 -14.394  0.50 66.90           C
ANISOU 1046  CG BMET A 131    10194   8005   7219   -243  -1676  -1083       C
ATOM   1047  SD AMET A 131     -24.405 -19.336 -14.231  0.50 75.46           S
ANISOU 1047  SD AMET A 131    10485   8920   9266  -1381  -1696  -1760       S
ATOM   1048  SD BMET A 131     -24.405 -19.331 -14.223  0.50 75.73           S
ANISOU 1048  SD BMET A 131    10493   8864   9418  -1383  -1636  -1753       S
ATOM   1049  CE AMET A 131     -24.243 -18.056 -15.478  0.50 68.73           C
ANISOU 1049  CE AMET A 131     9198   9149   7766   -366  -3236  -1218       C
ATOM   1050  CE BMET A 131     -24.249 -18.061 -15.481  0.50 69.36           C
ANISOU 1050  CE BMET A 131     9259   9106   7987   -376  -3100  -1200       C
ATOM   1051  N   ILE A 132     -21.045 -20.557  -9.983  1.00 36.84           N
ANISOU 1051  N   ILE A 132     5197   3768   5034   1814   -458   -780       N
ATOM   1052  CA  ILE A 132     -21.267 -20.893  -8.593  1.00 33.58           C
ANISOU 1052  CA  ILE A 132     3502   4121   5138    943   -814   -488       C
ATOM   1053  C   ILE A 132     -21.468 -19.644  -7.772  1.00 27.14           C
ANISOU 1053  C   ILE A 132     3287   2892   4133    391   -670    -52       C
ATOM   1054  O   ILE A 132     -21.958 -19.806  -6.641  1.00 31.51           O
ANISOU 1054  O   ILE A 132     3779   3355   4839   -361   -706    295       O
ATOM   1055  CB  ILE A 132     -20.086 -21.731  -8.066  1.00 41.51           C
ANISOU 1055  CB  ILE A 132     4994   4528   6248   2281   -617   -829       C
ATOM   1056  CG1 ILE A 132     -18.775 -21.038  -8.350  1.00 39.78           C
ANISOU 1056  CG1 ILE A 132     3878   5330   5908   2491   -590  -1146       C
ATOM   1057  CG2 ILE A 132     -20.173 -23.156  -8.589  1.00 51.87           C
ANISOU 1057  CG2 ILE A 132     6442   5526   7740   1945   -550   -440       C
ATOM   1058  CD1 ILE A 132     -17.606 -21.883  -7.869  1.00 48.45           C
ANISOU 1058  CD1 ILE A 132     3870   6334   8206   1627  -1803  -1698       C
ATOM   1059  N   TYR A 133     -21.100 -18.430  -8.301  1.00 27.99           N
ANISOU 1059  N   TYR A 133     3563   3425   3648    -69   -697     73       N
ATOM   1060  CA  TYR A 133     -21.273 -17.232  -7.481  1.00 22.61           C
ANISOU 1060  CA  TYR A 133     2747   2754   3088     86   -388    -18       C
ATOM   1061  C   TYR A 133     -22.572 -16.498  -7.808  1.00 22.38           C
ANISOU 1061  C   TYR A 133     2694   2875   2935    279   -282     46       C
ATOM   1062  O   TYR A 133     -22.833 -15.424  -7.256  1.00 22.33           O
ANISOU 1062  O   TYR A 133     2687   2793   3005     26   -226   -283       O
ATOM   1063  CB  TYR A 133     -20.118 -16.252  -7.735  1.00 23.17           C
ANISOU 1063  CB  TYR A 133     2802   2845   3159     21   -137    283       C
ATOM   1064  CG  TYR A 133     -18.798 -16.723  -7.175  1.00 21.63           C
ANISOU 1064  CG  TYR A 133     2818   2456   2944   -154   -189     73       C
ATOM   1065  CD1 TYR A 133     -18.647 -16.980  -5.816  1.00 21.92           C
ANISOU 1065  CD1 TYR A 133     2426   2830   3073     87   -116    451       C
ATOM   1066  CD2 TYR A 133     -17.694 -16.875  -7.992  1.00 23.79           C
ANISOU 1066  CD2 TYR A 133     3033   3156   2852    333    -19     39       C
ATOM   1067  CE1 TYR A 133     -17.438 -17.408  -5.320  1.00 22.89           C
ANISOU 1067  CE1 TYR A 133     2757   2812   3127     48   -260    250       C
ATOM   1068  CE2 TYR A 133     -16.461 -17.230  -7.482  1.00 24.06           C
ANISOU 1068  CE2 TYR A 133     2590   3449   3104    412    -63    131       C
ATOM   1069  CZ  TYR A 133     -16.322 -17.465  -6.126  1.00 23.91           C
ANISOU 1069  CZ  TYR A 133     2930   3060   3094    634   -134    442       C
ATOM   1070  OH  TYR A 133     -15.109 -17.809  -5.567  1.00 25.72           O
ANISOU 1070  OH  TYR A 133     2765   3672   3337    511   -533    433       O
ATOM   1071  N   SER A 134     -23.421 -17.142  -8.628  1.00 24.16           N
ANISOU 1071  N   SER A 134     2777   2900   3503    466   -328    -92       N
ATOM   1072  CA  SER A 134     -24.685 -16.544  -9.027  1.00 23.87           C
ANISOU 1072  CA  SER A 134     2803   3071   3195    192   -377    191       C
ATOM   1073  C   SER A 134     -25.876 -17.113  -8.227  1.00 22.04           C
ANISOU 1073  C   SER A 134     2957   2654   2762    128   -286   -320       C
ATOM   1074  O   SER A 134     -25.721 -18.027  -7.412  1.00 24.16           O
ANISOU 1074  O   SER A 134     2911   3163   3105    -92   -464     52       O
ATOM   1075  CB  SER A 134     -24.886 -16.695 -10.506  1.00 27.37           C
ANISOU 1075  CB  SER A 134     3200   3943   3255    658   -360    207       C
ATOM   1076  OG  SER A 134     -25.915 -15.804 -10.975  1.00 29.78           O
ANISOU 1076  OG  SER A 134     3721   3742   3853    340   -185   -122       O
ATOM   1077  N   CYS A 135     -27.041 -16.514  -8.452  1.00 24.14           N
ANISOU 1077  N   CYS A 135     2938   2809   3424    128   -276     82       N
ATOM   1078  CA  CYS A 135     -28.280 -16.851  -7.765  1.00 23.02           C
ANISOU 1078  CA  CYS A 135     2873   2732   3141    218   -258     45       C
ATOM   1079  C   CYS A 135     -29.097 -17.859  -8.567  1.00 22.64           C
ANISOU 1079  C   CYS A 135     2926   2631   3045    100   -179    -19       C
ATOM   1080  O   CYS A 135     -28.666 -18.259  -9.664  1.00 25.37           O
ANISOU 1080  O   CYS A 135     3221   3012   3405     10    -93   -335       O
ATOM   1081  CB  CYS A 135     -29.073 -15.572  -7.555  1.00 21.27           C
ANISOU 1081  CB  CYS A 135     2478   2532   3071      2   -311    -49       C
ATOM   1082  SG  CYS A 135     -29.505 -14.752  -9.113  1.00 23.69           S
ANISOU 1082  SG  CYS A 135     2936   2863   3202    109   -371     23       S
ATOM   1083  N   LYS A 136     -30.267 -18.218  -8.035  1.00 23.70           N
ANISOU 1083  N   LYS A 136     3018   2961   3025   -109    102    -91       N
ATOM   1084  CA  LYS A 136     -31.233 -19.040  -8.760  1.00 23.88           C
ANISOU 1084  CA  LYS A 136     3289   2676   3108   -279   -238   -256       C
ATOM   1085  C   LYS A 136     -32.623 -18.506  -8.428  1.00 23.45           C
ANISOU 1085  C   LYS A 136     3031   2531   3350   -472    184    308       C
ATOM   1086  O   LYS A 136     -33.329 -19.078  -7.582  1.00 29.38           O
ANISOU 1086  O   LYS A 136     3367   3223   4574    573    832   1041       O
ATOM   1087  CB  LYS A 136     -31.054 -20.531  -8.481  1.00 28.19           C
ANISOU 1087  CB  LYS A 136     3923   2939   3847   -398   -580    193       C
ATOM   1088  CG  LYS A 136     -31.751 -21.466  -9.410  1.00 34.10           C
ANISOU 1088  CG  LYS A 136     3849   3621   5487   -364   -683   -272       C
ATOM   1089  CD  LYS A 136     -31.282 -22.921  -9.272  1.00 39.75           C
ANISOU 1089  CD  LYS A 136     5307   2734   7061   -746   -266   -107       C
ATOM   1090  CE  LYS A 136     -32.019 -23.699 -10.284  1.00 46.25           C
ANISOU 1090  CE  LYS A 136     5289   4472   7813  -1088   -395   -985       C
ATOM   1091  NZ  LYS A 136     -33.414 -23.928  -9.892  1.00 50.47           N
ANISOU 1091  NZ  LYS A 136     5605   5894   7676  -1266   -201   -457       N
ATOM   1092  N   ARG A 137     -32.985 -17.400  -9.081  1.00 22.54           N
ANISOU 1092  N   ARG A 137     2779   2700   3084   -462    -64    235       N
ATOM   1093  CA  ARG A 137     -34.190 -16.673  -8.751  1.00 24.40           C
ANISOU 1093  CA  ARG A 137     2763   3030   3478   -372    123    478       C
ATOM   1094  C   ARG A 137     -34.674 -15.886  -9.959  1.00 24.33           C
ANISOU 1094  C   ARG A 137     2708   2969   3569    -77   -194    448       C
ATOM   1095  O   ARG A 137     -33.849 -15.316 -10.673  1.00 25.58           O
ANISOU 1095  O   ARG A 137     2803   3318   3596   -259   -118    544       O
ATOM   1096  CB  ARG A 137     -33.930 -15.715  -7.599  1.00 25.95           C
ANISOU 1096  CB  ARG A 137     3285   3177   3397    204    -92    536       C
ATOM   1097  CG  ARG A 137     -35.145 -14.887  -7.243  1.00 33.92           C
ANISOU 1097  CG  ARG A 137     4111   4226   4549    934    -32    455       C
ATOM   1098  CD  ARG A 137     -35.467 -14.889  -5.876  1.00 34.81           C
ANISOU 1098  CD  ARG A 137     3924   5092   4210   1381   -618    641       C
ATOM   1099  NE  ARG A 137     -36.572 -14.063  -5.399  1.00 27.14           N
ANISOU 1099  NE  ARG A 137     2795   4262   3253    396   -369   -406       N
ATOM   1100  CZ  ARG A 137     -36.714 -13.745  -4.143  1.00 25.95           C
ANISOU 1100  CZ  ARG A 137     2852   3991   3017   -315   -186   -152       C
ATOM   1101  NH1 ARG A 137     -35.717 -13.924  -3.306  1.00 29.51           N
ANISOU 1101  NH1 ARG A 137     3134   5231   2847     27   -129    212       N
ATOM   1102  NH2 ARG A 137     -37.780 -13.145  -3.764  1.00 25.28           N
ANISOU 1102  NH2 ARG A 137     2766   3578   3261   -382   -100   -121       N
ATOM   1103  N   SER A 138     -36.006 -15.798 -10.137  1.00 23.83           N
ANISOU 1103  N   SER A 138     2456   2841   3758    -23     -2     54       N
ATOM   1104  CA  SER A 138     -36.573 -15.082 -11.278  1.00 24.52           C
ANISOU 1104  CA  SER A 138     2418   3117   3780    136   -211   -215       C
ATOM   1105  C   SER A 138     -36.733 -13.583 -11.002  1.00 22.28           C
ANISOU 1105  C   SER A 138     2315   3071   3081     27   -286    -73       C
ATOM   1106  O   SER A 138     -36.914 -13.156  -9.856  1.00 23.68           O
ANISOU 1106  O   SER A 138     2840   3237   2920   -148    -48     88       O
ATOM   1107  CB  SER A 138     -37.952 -15.659 -11.585  1.00 24.80           C
ANISOU 1107  CB  SER A 138     2957   2756   3710   -166    138   -260       C
ATOM   1108  OG  SER A 138     -38.596 -14.991 -12.634  1.00 26.21           O
ANISOU 1108  OG  SER A 138     2878   3378   3702    -40   -139    123       O
ATOM   1109  N   LEU A 139     -36.742 -12.811 -12.078  1.00 21.67           N
ANISOU 1109  N   LEU A 139     2351   3044   2837    232    -16    105       N
ATOM   1110  CA  LEU A 139     -37.282 -11.465 -12.048  1.00 21.37           C
ANISOU 1110  CA  LEU A 139     2409   2579   3131    202    -20    -17       C
ATOM   1111  C   LEU A 139     -38.751 -11.514 -11.704  1.00 22.38           C
ANISOU 1111  C   LEU A 139     2578   2992   2932   -238   -411     62       C
ATOM   1112  O   LEU A 139     -39.410 -12.542 -12.017  1.00 24.03           O
ANISOU 1112  O   LEU A 139     2491   3217   3423   -390   -157   -186       O
ATOM   1113  CB  LEU A 139     -37.125 -10.818 -13.420  1.00 23.20           C
ANISOU 1113  CB  LEU A 139     2479   3192   3141    -35   -287     14       C
ATOM   1114  CG  LEU A 139     -35.707 -10.575 -13.935  1.00 21.62           C
ANISOU 1114  CG  LEU A 139     2304   2989   2920    101    -38    128       C
ATOM   1115  CD1 LEU A 139     -35.864 -10.047 -15.347  1.00 24.70           C
ANISOU 1115  CD1 LEU A 139     2597   3237   3550   -141   -164   -187       C
ATOM   1116  CD2 LEU A 139     -34.904  -9.599 -13.112  1.00 21.52           C
ANISOU 1116  CD2 LEU A 139     2306   2848   3024   -211   -196   -111       C
ATOM   1117  N   THR A 140     -39.276 -10.434 -11.119  1.00 23.48           N
ANISOU 1117  N   THR A 140     2571   3020   3332   -216   -170   -290       N
ATOM   1118  CA  THR A 140     -40.733 -10.260 -11.053  1.00 22.81           C
ANISOU 1118  CA  THR A 140     2345   2941   3382   -297   -125     29       C
ATOM   1119  C   THR A 140     -41.175  -9.279 -12.130  1.00 22.69           C
ANISOU 1119  C   THR A 140     2418   3119   3084   -450    -29   -157       C
ATOM   1120  O   THR A 140     -42.324  -9.304 -12.530  1.00 25.52           O
ANISOU 1120  O   THR A 140     2554   3833   3308   -668   -109    227       O
ATOM   1121  CB  THR A 140     -41.149  -9.799  -9.652  1.00 22.73           C
ANISOU 1121  CB  THR A 140     2240   3361   3034    -25      3     87       C
ATOM   1122  OG1 THR A 140     -40.513  -8.547  -9.396  1.00 24.37           O
ANISOU 1122  OG1 THR A 140     2595   3252   3414   -281   -289   -110       O
ATOM   1123  CG2 THR A 140     -40.796 -10.886  -8.646  1.00 25.44           C
ANISOU 1123  CG2 THR A 140     2555   3390   3720   -311     76   -241       C
ATOM   1124  N   HIS A 141     -40.276  -8.370 -12.532  1.00 23.64           N
ANISOU 1124  N   HIS A 141     2739   3252   2992   -189   -131    111       N
ATOM   1125  CA  HIS A 141     -40.572  -7.314 -13.479  1.00 23.82           C
ANISOU 1125  CA  HIS A 141     2404   3549   3099    129   -372      5       C
ATOM   1126  C   HIS A 141     -39.374  -7.037 -14.394  1.00 23.40           C
ANISOU 1126  C   HIS A 141     2443   3316   3130    272   -216    152       C
ATOM   1127  O   HIS A 141     -38.230  -7.116 -13.935  1.00 24.17           O
ANISOU 1127  O   HIS A 141     2749   3362   3072     99   -350     36       O
ATOM   1128  CB  HIS A 141     -40.914  -6.020 -12.758  1.00 25.61           C
ANISOU 1128  CB  HIS A 141     2961   3597   3173    500   -242    341       C
ATOM   1129  CG  HIS A 141     -42.043  -6.123 -11.817  1.00 27.19           C
ANISOU 1129  CG  HIS A 141     2731   4028   3570    322    -55     89       C
ATOM   1130  ND1 HIS A 141     -43.354  -5.799 -12.104  1.00 36.01           N
ANISOU 1130  ND1 HIS A 141     3683   5340   4660    844     53    470       N
ATOM   1131  CD2 HIS A 141     -42.010  -6.540 -10.525  1.00 26.66           C
ANISOU 1131  CD2 HIS A 141     2790   3843   3496    270   -889     60       C
ATOM   1132  CE1 HIS A 141     -44.094  -6.035 -11.006  1.00 35.44           C
ANISOU 1132  CE1 HIS A 141     3656   5766   4042    754    165    672       C
ATOM   1133  NE2 HIS A 141     -43.269  -6.485 -10.037  1.00 37.24           N
ANISOU 1133  NE2 HIS A 141     3730   5437   4982   -382   -148   -245       N
ATOM   1134  N   THR A 142     -39.663  -6.777 -15.673  1.00 23.88           N
ANISOU 1134  N   THR A 142     2506   3444   3124    204   -424     77       N
ATOM   1135  CA  THR A 142     -38.663  -6.414 -16.663  1.00 23.28           C
ANISOU 1135  CA  THR A 142     2639   3094   3113    320   -701    192       C
ATOM   1136  C   THR A 142     -38.738  -4.925 -16.920  1.00 22.74           C
ANISOU 1136  C   THR A 142     2514   3199   2926    501   -265    -34       C
ATOM   1137  O   THR A 142     -39.818  -4.348 -16.936  1.00 24.40           O
ANISOU 1137  O   THR A 142     2324   3068   3878    191   -231     50       O
ATOM   1138  CB  THR A 142     -38.780  -7.238 -17.957  1.00 25.56           C
ANISOU 1138  CB  THR A 142     3070   3179   3464    449   -152   -169       C
ATOM   1139  OG1 THR A 142     -39.890  -6.805 -18.716  1.00 26.65           O
ANISOU 1139  OG1 THR A 142     3270   3615   3242    132   -698    219       O
ATOM   1140  CG2 THR A 142     -38.820  -8.712 -17.662  1.00 25.04           C
ANISOU 1140  CG2 THR A 142     2922   3118   3472    -40   -201      8       C
ATOM   1141  N   VAL A 143     -37.584  -4.335 -17.247  1.00 23.67           N
ANISOU 1141  N   VAL A 143     2803   3122   3068    255    -32    152       N
ATOM   1142  CA  VAL A 143     -37.484  -2.938 -17.637  1.00 22.16           C
ANISOU 1142  CA  VAL A 143     2523   3037   2859     51   -338      8       C
ATOM   1143  C   VAL A 143     -36.589  -2.775 -18.860  1.00 22.59           C
ANISOU 1143  C   VAL A 143     2636   3013   2934    352   -297    -96       C
ATOM   1144  O   VAL A 143     -35.614  -3.509 -19.055  1.00 23.78           O
ANISOU 1144  O   VAL A 143     2913   3096   3024    468     19     34       O
ATOM   1145  CB  VAL A 143     -36.944  -2.003 -16.534  1.00 23.85           C
ANISOU 1145  CB  VAL A 143     3149   3092   2822     78   -437     49       C
ATOM   1146  CG1 VAL A 143     -38.019  -1.742 -15.485  1.00 25.21           C
ANISOU 1146  CG1 VAL A 143     3305   3132   3140    484   -287    223       C
ATOM   1147  CG2 VAL A 143     -35.644  -2.537 -15.961  1.00 23.22           C
ANISOU 1147  CG2 VAL A 143     2701   2808   3315   -110   -807     91       C
ATOM   1148  N   ARG A 144     -36.951  -1.793 -19.694  1.00 23.74           N
ANISOU 1148  N   ARG A 144     2944   3098   2979    190   -103    249       N
ATOM   1149  CA AARG A 144     -36.180  -1.391 -20.855  0.50 23.66           C
ANISOU 1149  CA AARG A 144     3102   3132   2756    133   -351    173       C
ATOM   1150  CA BARG A 144     -36.191  -1.388 -20.861  0.50 24.55           C
ANISOU 1150  CA BARG A 144     3318   3161   2849    128   -355    230       C
ATOM   1151  C   ARG A 144     -36.098   0.142 -20.904  1.00 24.08           C
ANISOU 1151  C   ARG A 144     3390   3062   2697    181   -589    252       C
ATOM   1152  O   ARG A 144     -36.584   0.853 -20.021  1.00 24.97           O
ANISOU 1152  O   ARG A 144     3503   3166   2819    226   -285    106       O
ATOM   1153  CB AARG A 144     -36.822  -2.031 -22.084  0.50 24.21           C
ANISOU 1153  CB AARG A 144     2959   3362   2878   -302    -64    359       C
ATOM   1154  CB BARG A 144     -36.920  -1.911 -22.095  0.50 27.50           C
ANISOU 1154  CB BARG A 144     3668   3618   3163   -352   -164    424       C
ATOM   1155  CG AARG A 144     -36.474  -3.493 -22.297  0.50 23.31           C
ANISOU 1155  CG AARG A 144     2207   3717   2931   -166    318    -64       C
ATOM   1156  CG BARG A 144     -37.032  -3.413 -22.238  0.50 31.82           C
ANISOU 1156  CG BARG A 144     4258   4108   3723   -443   -138    258       C
ATOM   1157  CD AARG A 144     -37.009  -3.941 -23.652  0.50 23.56           C
ANISOU 1157  CD AARG A 144     2268   4025   2658   -761    -45    376       C
ATOM   1158  CD BARG A 144     -35.779  -3.896 -22.805  0.50 35.91           C
ANISOU 1158  CD BARG A 144     4261   5003   4380   -679     -2    341       C
ATOM   1159  NE AARG A 144     -35.984  -4.685 -24.385  0.50 32.71           N
ANISOU 1159  NE AARG A 144     3833   5285   3311   -304   -533    544       N
ATOM   1160  NE BARG A 144     -35.995  -4.911 -23.837  0.50 34.24           N
ANISOU 1160  NE BARG A 144     4412   5558   3039   -419    302    748       N
ATOM   1161  CZ AARG A 144     -34.717  -4.225 -24.378  0.50 30.11           C
ANISOU 1161  CZ AARG A 144     3246   4792   3402   -861   -205   1286       C
ATOM   1162  CZ BARG A 144     -34.965  -5.157 -24.636  0.50 27.59           C
ANISOU 1162  CZ BARG A 144     2629   4781   3072   -358   -291    398       C
ATOM   1163  NH1AARG A 144     -34.211  -3.809 -23.243  0.50 42.06           N
ANISOU 1163  NH1AARG A 144     4671   5613   5696  -1363      9    139       N
ATOM   1164  NH1BARG A 144     -34.830  -6.373 -25.025  0.50 24.01           N
ANISOU 1164  NH1BARG A 144     2554   3629   2939   -331   -458    260       N
ATOM   1165  NH2AARG A 144     -33.935  -4.314 -25.457  0.50 35.32           N
ANISOU 1165  NH2AARG A 144     4840   4822   3757     69  -1231   -481       N
ATOM   1166  NH2BARG A 144     -34.011  -4.248 -24.764  0.50 30.72           N
ANISOU 1166  NH2BARG A 144     3870   3221   4582   -703  -1672      6       N
ATOM   1167  N   GLU A 145     -35.445   0.653 -21.955  1.00 24.23           N
ANISOU 1167  N   GLU A 145     3445   2934   2829    207   -208    306       N
ATOM   1168  CA  GLU A 145     -35.188   2.060 -22.104  1.00 24.85           C
ANISOU 1168  CA  GLU A 145     3530   3068   2841    396   -469      2       C
ATOM   1169  C   GLU A 145     -36.458   2.879 -21.870  1.00 24.61           C
ANISOU 1169  C   GLU A 145     3176   3099   3076    274   -555    340       C
ATOM   1170  O   GLU A 145     -37.506   2.620 -22.502  1.00 27.18           O
ANISOU 1170  O   GLU A 145     3216   3825   3286    307   -692    153       O
ATOM   1171  CB  GLU A 145     -34.701   2.313 -23.530  1.00 28.48           C
ANISOU 1171  CB  GLU A 145     3881   3597   3344    402   -330     53       C
ATOM   1172  CG  GLU A 145     -34.379   3.767 -23.792  1.00 28.16           C
ANISOU 1172  CG  GLU A 145     3779   3629   3293    111   -364    577       C
ATOM   1173  CD  GLU A 145     -33.070   4.211 -23.175  1.00 30.56           C
ANISOU 1173  CD  GLU A 145     4056   3800   3756    310   -518    686       C
ATOM   1174  OE1 GLU A 145     -33.080   5.289 -22.568  1.00 32.71           O
ANISOU 1174  OE1 GLU A 145     4305   3751   4372   -230   -517    217       O
ATOM   1175  OE2 GLU A 145     -32.052   3.447 -23.272  1.00 30.03           O
ANISOU 1175  OE2 GLU A 145     4088   3919   3402    842   -276    416       O
ATOM   1176  N   GLY A 146     -36.302   3.875 -20.994  1.00 26.05           N
ANISOU 1176  N   GLY A 146     3522   3280   3095    324   -719    488       N
ATOM   1177  CA  GLY A 146     -37.333   4.845 -20.689  1.00 27.88           C
ANISOU 1177  CA  GLY A 146     3623   3132   3839    655   -678    304       C
ATOM   1178  C   GLY A 146     -38.330   4.443 -19.604  1.00 27.23           C
ANISOU 1178  C   GLY A 146     3475   3197   3676    779   -376    164       C
ATOM   1179  O   GLY A 146     -39.144   5.269 -19.144  1.00 29.36           O
ANISOU 1179  O   GLY A 146     3571   3700   3883   1377   -251     35       O
ATOM   1180  N   ASP A 147     -38.206   3.210 -19.123  1.00 25.51           N
ANISOU 1180  N   ASP A 147     2898   3447   3348    503   -303    207       N
ATOM   1181  CA  ASP A 147     -39.108   2.711 -18.095  1.00 25.68           C
ANISOU 1181  CA  ASP A 147     3125   3210   3422    597   -425     46       C
ATOM   1182  C   ASP A 147     -38.834   3.333 -16.733  1.00 25.40           C
ANISOU 1182  C   ASP A 147     3322   3196   3133    623   -123     29       C
ATOM   1183  O   ASP A 147     -37.759   3.866 -16.490  1.00 27.27           O
ANISOU 1183  O   ASP A 147     3467   3411   3484    469   -105    121       O
ATOM   1184  CB  ASP A 147     -39.081   1.205 -18.010  1.00 26.56           C
ANISOU 1184  CB  ASP A 147     3085   3221   3786    760   -191    224       C
ATOM   1185  CG  ASP A 147     -39.741   0.482 -19.175  1.00 27.65           C
ANISOU 1185  CG  ASP A 147     3313   3731   3461    570   -375    201       C
ATOM   1186  OD1 ASP A 147     -40.455   1.171 -19.994  1.00 30.42           O
ANISOU 1186  OD1 ASP A 147     4119   3956   3484   1089   -680   -246       O
ATOM   1187  OD2 ASP A 147     -39.548  -0.766 -19.231  1.00 27.58           O
ANISOU 1187  OD2 ASP A 147     3233   3422   3824    496   -625    102       O
ATOM   1188  N   ARG A 148     -39.871   3.280 -15.877  1.00 28.47           N
ANISOU 1188  N   ARG A 148     3489   4042   3286    720   -153     55       N
ATOM   1189  CA  ARG A 148     -39.769   3.787 -14.511  1.00 29.72           C
ANISOU 1189  CA  ARG A 148     3595   4225   3471    749    235    108       C
ATOM   1190  C   ARG A 148     -39.944   2.575 -13.603  1.00 27.86           C
ANISOU 1190  C   ARG A 148     3855   3373   3357     61   -341    -49       C
ATOM   1191  O   ARG A 148     -40.712   1.691 -13.900  1.00 35.29           O
ANISOU 1191  O   ARG A 148     3941   5268   4200   -673  -1031    454       O
ATOM   1192  CB  ARG A 148     -40.771   4.911 -14.212  1.00 36.05           C
ANISOU 1192  CB  ARG A 148     4151   5468   4076   1371    321   -735       C
ATOM   1193  N   ILE A 149     -39.220   2.526 -12.499  1.00 27.73           N
ANISOU 1193  N   ILE A 149     3603   3758   3173   -308   -146    -54       N
ATOM   1194  CA  ILE A 149     -39.398   1.529 -11.458  1.00 27.43           C
ANISOU 1194  CA  ILE A 149     3406   3766   3251    -40   -252    141       C
ATOM   1195  C   ILE A 149     -40.198   2.192 -10.347  1.00 26.31           C
ANISOU 1195  C   ILE A 149     2676   4073   3246    113   -483    126       C
ATOM   1196  O   ILE A 149     -39.852   3.298  -9.895  1.00 27.56           O
ANISOU 1196  O   ILE A 149     3408   3818   3245    416    -79    276       O
ATOM   1197  CB  ILE A 149     -37.998   1.069 -11.013  1.00 25.75           C
ANISOU 1197  CB  ILE A 149     2876   3716   3191     81   -126   -223       C
ATOM   1198  CG1 ILE A 149     -37.285   0.434 -12.193  1.00 28.18           C
ANISOU 1198  CG1 ILE A 149     3705   3941   3062   -228    -50    -30       C
ATOM   1199  CG2 ILE A 149     -38.010   0.133  -9.799  1.00 26.83           C
ANISOU 1199  CG2 ILE A 149     3459   3504   3230    424    -69   -132       C
ATOM   1200  CD1 ILE A 149     -35.803   0.224 -11.966  1.00 28.38           C
ANISOU 1200  CD1 ILE A 149     3212   4135   3434    347    238    246       C
ATOM   1201  N   ALA A 150     -41.269   1.508  -9.926  1.00 27.74           N
ANISOU 1201  N   ALA A 150     2893   4239   3409    -72   -239    119       N
ATOM   1202  CA  ALA A 150     -42.243   2.101  -9.019  1.00 33.36           C
ANISOU 1202  CA  ALA A 150     3627   5118   3929   -136   -214    165       C
ATOM   1203  C   ALA A 150     -41.607   2.657  -7.751  1.00 29.44           C
ANISOU 1203  C   ALA A 150     2921   4656   3609    258    -64    121       C
ATOM   1204  O   ALA A 150     -42.016   3.725  -7.289  1.00 32.81           O
ANISOU 1204  O   ALA A 150     3670   4399   4398    736   -239    445       O
ATOM   1205  CB  ALA A 150     -43.330   1.083  -8.711  1.00 34.19           C
ANISOU 1205  CB  ALA A 150     3654   5128   4207    164   -796    610       C
ATOM   1206  N   SER A 151     -40.613   1.943  -7.209  1.00 26.59           N
ANISOU 1206  N   SER A 151     2919   3901   3284    863    108     75       N
ATOM   1207  CA  SER A 151     -39.993   2.325  -5.943  1.00 26.84           C
ANISOU 1207  CA  SER A 151     2700   4161   3336    519    134     16       C
ATOM   1208  C   SER A 151     -38.968   3.448  -6.109  1.00 25.92           C
ANISOU 1208  C   SER A 151     2971   3569   3310    711     58   -120       C
ATOM   1209  O   SER A 151     -38.513   3.978  -5.077  1.00 28.58           O
ANISOU 1209  O   SER A 151     3760   3639   3458    531   -174     59       O
ATOM   1210  CB  SER A 151     -39.348   1.121  -5.268  1.00 27.48           C
ANISOU 1210  CB  SER A 151     3204   3625   3612    154   -269    231       C
ATOM   1211  OG  SER A 151     -38.296   0.625  -6.055  1.00 26.21           O
ANISOU 1211  OG  SER A 151     3527   3334   3096    440    117     86       O
ATOM   1212  N   LEU A 152     -38.637   3.810  -7.365  1.00 25.43           N
ANISOU 1212  N   LEU A 152     3022   3286   3354    494   -136   -105       N
ATOM   1213  CA  LEU A 152     -37.602   4.806  -7.673  1.00 26.92           C
ANISOU 1213  CA  LEU A 152     3314   3408   3507    583    -33      8       C
ATOM   1214  C   LEU A 152     -38.183   5.852  -8.619  1.00 26.13           C
ANISOU 1214  C   LEU A 152     3408   2978   3541    347    -24    141       C
ATOM   1215  O   LEU A 152     -37.726   6.007  -9.756  1.00 27.47           O
ANISOU 1215  O   LEU A 152     3824   3121   3493    291   -526    299       O
ATOM   1216  CB  LEU A 152     -36.378   4.151  -8.310  1.00 25.62           C
ANISOU 1216  CB  LEU A 152     3054   3141   3538    389   -141    -32       C
ATOM   1217  CG  LEU A 152     -35.641   3.132  -7.453  1.00 26.31           C
ANISOU 1217  CG  LEU A 152     3348   2991   3658    297   -258   -124       C
ATOM   1218  CD1 LEU A 152     -34.529   2.555  -8.320  1.00 26.58           C
ANISOU 1218  CD1 LEU A 152     3572   2804   3723    735   -365     10       C
ATOM   1219  CD2 LEU A 152     -35.080   3.830  -6.217  1.00 26.60           C
ANISOU 1219  CD2 LEU A 152     3312   2918   3875    642   -223   -364       C
ATOM   1220  N   PRO A 153     -39.219   6.604  -8.205  1.00 28.58           N
ANISOU 1220  N   PRO A 153     3656   3494   3708    586    -38    340       N
ATOM   1221  CA  PRO A 153     -39.911   7.493  -9.141  1.00 32.07           C
ANISOU 1221  CA  PRO A 153     3966   3522   4696    748   -119    642       C
ATOM   1222  C   PRO A 153     -39.104   8.581  -9.872  1.00 29.26           C
ANISOU 1222  C   PRO A 153     3472   3173   4470    700   -123    143       C
ATOM   1223  O   PRO A 153     -39.499   9.032 -10.961  1.00 34.49           O
ANISOU 1223  O   PRO A 153     4613   4262   4227    882   -343    409       O
ATOM   1224  CB  PRO A 153     -40.966   8.093  -8.234  1.00 33.58           C
ANISOU 1224  CB  PRO A 153     3699   3923   5136    846     -3    614       C
ATOM   1225  CG  PRO A 153     -40.438   8.007  -6.865  1.00 35.43           C
ANISOU 1225  CG  PRO A 153     4307   4330   4826   1078   -157     62       C
ATOM   1226  CD  PRO A 153     -39.818   6.622  -6.861  1.00 30.71           C
ANISOU 1226  CD  PRO A 153     3568   3748   4353    749    187    150       C
ATOM   1227  N   GLU A 154     -37.973   9.002  -9.301  1.00 28.51           N
ANISOU 1227  N   GLU A 154     3735   3188   3910    595     33   -170       N
ATOM   1228  CA  GLU A 154     -37.231  10.114  -9.892  1.00 29.94           C
ANISOU 1228  CA  GLU A 154     3438   3363   4576    766   -148   -251       C
ATOM   1229  C   GLU A 154     -36.271   9.625 -10.968  1.00 28.50           C
ANISOU 1229  C   GLU A 154     3444   3290   4095    415     91   -107       C
ATOM   1230  O   GLU A 154     -35.614  10.427 -11.633  1.00 30.63           O
ANISOU 1230  O   GLU A 154     3907   3260   4471    757    144   -292       O
ATOM   1231  CB  GLU A 154     -36.425  10.901  -8.860  1.00 32.35           C
ANISOU 1231  CB  GLU A 154     4000   3765   4526    520    177   -772       C
ATOM   1232  CG  GLU A 154     -37.289  11.549  -7.785  1.00 34.19           C
ANISOU 1232  CG  GLU A 154     4018   4588   4384    479    242   -674       C
ATOM   1233  CD  GLU A 154     -36.557  12.688  -7.123  1.00 36.04           C
ANISOU 1233  CD  GLU A 154     5257   3974   4461    442    430   -254       C
ATOM   1234  OE1 GLU A 154     -36.872  13.831  -7.479  1.00 42.09           O
ANISOU 1234  OE1 GLU A 154     6620   3962   5409    727     -3   -483       O
ATOM   1235  OE2 GLU A 154     -35.635  12.433  -6.319  1.00 38.11           O
ANISOU 1235  OE2 GLU A 154     5705   3844   4930    270    454   -798       O
ATOM   1236  N   PHE A 155     -36.173   8.291 -11.112  1.00 26.85           N
ANISOU 1236  N   PHE A 155     3496   3054   3652    101    -72     21       N
ATOM   1237  CA  PHE A 155     -35.198   7.711 -12.016  1.00 24.89           C
ANISOU 1237  CA  PHE A 155     3267   2756   3433    289   -334    -29       C
ATOM   1238  C   PHE A 155     -35.837   7.168 -13.292  1.00 25.15           C
ANISOU 1238  C   PHE A 155     3297   3031   3228    340   -401    315       C
ATOM   1239  O   PHE A 155     -36.997   6.742 -13.298  1.00 29.10           O
ANISOU 1239  O   PHE A 155     3907   3709   3440    657   -357    215       O
ATOM   1240  CB  PHE A 155     -34.457   6.556 -11.335  1.00 25.72           C
ANISOU 1240  CB  PHE A 155     3464   3093   3217    474   -316    -30       C
ATOM   1241  CG  PHE A 155     -33.450   7.008 -10.303  1.00 25.62           C
ANISOU 1241  CG  PHE A 155     3617   2961   3155    -53   -173    341       C
ATOM   1242  CD1 PHE A 155     -33.826   7.231  -8.987  1.00 26.57           C
ANISOU 1242  CD1 PHE A 155     3414   3367   3313     19   -133    -89       C
ATOM   1243  CD2 PHE A 155     -32.127   7.250 -10.671  1.00 26.40           C
ANISOU 1243  CD2 PHE A 155     3438   3219   3376     53    -46   -180       C
ATOM   1244  CE1 PHE A 155     -32.876   7.644  -8.063  1.00 28.69           C
ANISOU 1244  CE1 PHE A 155     4253   3450   3199   -226   -375   -308       C
ATOM   1245  CE2 PHE A 155     -31.199   7.656  -9.742  1.00 26.58           C
ANISOU 1245  CE2 PHE A 155     3272   3166   3660     65    -25   -227       C
ATOM   1246  CZ  PHE A 155     -31.572   7.825  -8.432  1.00 29.60           C
ANISOU 1246  CZ  PHE A 155     3685   3567   3995     59   -162   -197       C
ATOM   1247  N   THR A 156     -35.055   7.170 -14.360  1.00 25.22           N
ANISOU 1247  N   THR A 156     3512   3005   3064    518   -247     -9       N
ATOM   1248  CA ATHR A 156     -35.423   6.548 -15.629  0.50 26.67           C
ANISOU 1248  CA ATHR A 156     3665   3003   3463    705   -444     16       C
ATOM   1249  CA BTHR A 156     -35.447   6.512 -15.602  0.50 27.14           C
ANISOU 1249  CA BTHR A 156     3684   3175   3452    596   -377     32       C
ATOM   1250  C   THR A 156     -34.413   5.450 -15.954  1.00 25.03           C
ANISOU 1250  C   THR A 156     3546   2650   3314    489   -182    100       C
ATOM   1251  O   THR A 156     -33.218   5.629 -15.794  1.00 26.54           O
ANISOU 1251  O   THR A 156     3416   3328   3338    617   -412    144       O
ATOM   1252  CB ATHR A 156     -35.416   7.635 -16.709  0.50 28.66           C
ANISOU 1252  CB ATHR A 156     4307   2945   3638   1351   -824    236       C
ATOM   1253  CB BTHR A 156     -35.560   7.530 -16.733  0.50 31.66           C
ANISOU 1253  CB BTHR A 156     4665   3692   3672    961   -656    423       C
ATOM   1254  OG1ATHR A 156     -36.486   8.519 -16.372  0.50 30.67           O
ANISOU 1254  OG1ATHR A 156     4921   2979   3754   2080   -526     15       O
ATOM   1255  OG1BTHR A 156     -35.963   6.791 -17.875  0.50 41.03           O
ANISOU 1255  OG1BTHR A 156     6103   5047   4442    814    -49    557       O
ATOM   1256  CG2ATHR A 156     -35.611   7.089 -18.107  0.50 33.46           C
ANISOU 1256  CG2ATHR A 156     5388   3326   4001   1173   -329    627       C
ATOM   1257  CG2BTHR A 156     -34.237   8.157 -17.097  0.50 32.08           C
ANISOU 1257  CG2BTHR A 156     4904   3471   3814   1151    -94    706       C
ATOM   1258  N   VAL A 157     -34.920   4.318 -16.450  1.00 23.27           N
ANISOU 1258  N   VAL A 157     2777   2759   3304    246   -189    104       N
ATOM   1259  CA  VAL A 157     -34.066   3.242 -16.902  1.00 22.40           C
ANISOU 1259  CA  VAL A 157     2655   2817   3040    159   -391    204       C
ATOM   1260  C   VAL A 157     -33.458   3.612 -18.262  1.00 22.97           C
ANISOU 1260  C   VAL A 157     3133   2536   3058    204   -559    -45       C
ATOM   1261  O   VAL A 157     -34.184   3.957 -19.186  1.00 24.96           O
ANISOU 1261  O   VAL A 157     3138   3397   2949    480   -439     71       O
ATOM   1262  CB  VAL A 157     -34.843   1.922 -17.006  1.00 24.35           C
ANISOU 1262  CB  VAL A 157     2705   3061   3484    253   -420     19       C
ATOM   1263  CG1 VAL A 157     -34.004   0.820 -17.659  1.00 24.96           C
ANISOU 1263  CG1 VAL A 157     3002   3376   3108     65   -260    135       C
ATOM   1264  CG2 VAL A 157     -35.360   1.464 -15.649  1.00 25.41           C
ANISOU 1264  CG2 VAL A 157     3016   3459   3178     46    -68    -85       C
ATOM   1265  N   ILE A 158     -32.121   3.480 -18.353  1.00 23.93           N
ANISOU 1265  N   ILE A 158     3358   2813   2923    331   -140    165       N
ATOM   1266  CA AILE A 158     -31.314   3.667 -19.552  0.25 23.34           C
ANISOU 1266  CA AILE A 158     3405   2468   2997    472    -13     45       C
ATOM   1267  CA BILE A 158     -31.314   3.667 -19.552  0.25 23.35           C
ANISOU 1267  CA BILE A 158     3401   2470   3001    472    -12     42       C
ATOM   1268  CA CILE A 158     -31.408   3.633 -19.605  0.50 23.78           C
ANISOU 1268  CA CILE A 158     3213   2680   3143    508   -349    101       C
ATOM   1269  C   ILE A 158     -30.689   2.319 -19.924  1.00 23.40           C
ANISOU 1269  C   ILE A 158     3027   2703   3160    394    -77    -76       C
ATOM   1270  O   ILE A 158     -29.991   1.702 -19.107  1.00 25.55           O
ANISOU 1270  O   ILE A 158     3837   3026   2844    243   -569    123       O
ATOM   1271  CB AILE A 158     -30.197   4.721 -19.335  0.25 23.08           C
ANISOU 1271  CB AILE A 158     3705   2020   3045    569    640     64       C
ATOM   1272  CB BILE A 158     -30.198   4.722 -19.334  0.25 23.10           C
ANISOU 1272  CB BILE A 158     3698   2023   3055    571    641     56       C
ATOM   1273  CB CILE A 158     -30.466   4.859 -19.585  0.50 32.11           C
ANISOU 1273  CB CILE A 158     4510   3353   4336    -52    198    244       C
ATOM   1274  CG1AILE A 158     -30.750   6.018 -18.749  0.25 23.76           C
ANISOU 1274  CG1AILE A 158     3916   1806   3306    448    752    169       C
ATOM   1275  CG1BILE A 158     -30.752   6.019 -18.750  0.25 23.79           C
ANISOU 1275  CG1BILE A 158     3903   1812   3323    450    756    155       C
ATOM   1276  CG1CILE A 158     -29.278   4.747 -20.465  0.50 38.40           C
ANISOU 1276  CG1CILE A 158     4456   4135   6001    230   -274    262       C
ATOM   1277  CG2AILE A 158     -29.484   5.035 -20.649  0.25 24.84           C
ANISOU 1277  CG2AILE A 158     3847   2486   3104    597    411     12       C
ATOM   1278  CG2BILE A 158     -29.483   5.034 -20.648  0.25 24.86           C
ANISOU 1278  CG2BILE A 158     3840   2488   3118    598    413      5       C
ATOM   1279  CG2CILE A 158     -29.960   5.215 -18.197  0.50 34.37           C
ANISOU 1279  CG2CILE A 158     4109   3964   4988    -23   -980    520       C
ATOM   1280  CD1AILE A 158     -31.824   6.577 -19.620  0.25 23.59           C
ANISOU 1280  CD1AILE A 158     3806   1890   3265    611    643    342       C
ATOM   1281  CD1BILE A 158     -31.820   6.581 -19.626  0.25 23.64           C
ANISOU 1281  CD1BILE A 158     3784   1906   3294    612    648    319       C
ATOM   1282  CD1CILE A 158     -28.223   5.765 -20.074  0.50 40.35           C
ANISOU 1282  CD1CILE A 158     4629   3945   6757    126   -377    534       C
ATOM   1283  N   GLU A 159     -30.923   1.855 -21.158  1.00 22.82           N
ANISOU 1283  N   GLU A 159     3188   2603   2879    464   -139     16       N
ATOM   1284  CA  GLU A 159     -30.186   0.694 -21.593  1.00 22.36           C
ANISOU 1284  CA  GLU A 159     2877   2821   2798    184   -179    221       C
ATOM   1285  C   GLU A 159     -28.744   1.109 -21.901  1.00 23.10           C
ANISOU 1285  C   GLU A 159     3210   2747   2818     86   -182    111       C
ATOM   1286  O   GLU A 159     -28.505   2.016 -22.697  1.00 24.81           O
ANISOU 1286  O   GLU A 159     3226   3012   3188    245   -204    683       O
ATOM   1287  CB  GLU A 159     -30.823   0.011 -22.798  1.00 24.47           C
ANISOU 1287  CB  GLU A 159     3356   3188   2753    242   -169    -77       C
ATOM   1288  CG  GLU A 159     -32.137  -0.650 -22.471  1.00 25.12           C
ANISOU 1288  CG  GLU A 159     3134   3419   2989     35   -162   -124       C
ATOM   1289  CD  GLU A 159     -32.852  -1.235 -23.672  1.00 26.01           C
ANISOU 1289  CD  GLU A 159     3293   3777   2812   -104   -227   -340       C
ATOM   1290  OE1 GLU A 159     -34.101  -1.169 -23.699  1.00 26.96           O
ANISOU 1290  OE1 GLU A 159     3177   3762   3306    216   -275   -250       O
ATOM   1291  OE2 GLU A 159     -32.169  -1.738 -24.617  1.00 29.16           O
ANISOU 1291  OE2 GLU A 159     3845   3855   3380     94   -239   -361       O
ATOM   1292  N   THR A 160     -27.783   0.386 -21.283  1.00 23.90           N
ANISOU 1292  N   THR A 160     3348   2938   2794    -11    -95    267       N
ATOM   1293  CA  THR A 160     -26.373   0.704 -21.392  1.00 22.39           C
ANISOU 1293  CA  THR A 160     3246   2556   2705   -147    -51    428       C
ATOM   1294  C   THR A 160     -25.580  -0.534 -21.758  1.00 22.45           C
ANISOU 1294  C   THR A 160     3040   3049   2439    -40    -75    155       C
ATOM   1295  O   THR A 160     -24.708  -0.975 -20.986  1.00 22.73           O
ANISOU 1295  O   THR A 160     3068   2760   2807    -44   -140     77       O
ATOM   1296  CB  THR A 160     -25.847   1.379 -20.109  1.00 22.51           C
ANISOU 1296  CB  THR A 160     2989   2528   3034    322   -127     31       C
ATOM   1297  OG1 THR A 160     -26.267   0.671 -18.937  1.00 22.11           O
ANISOU 1297  OG1 THR A 160     3186   2706   2511     28   -120    256       O
ATOM   1298  CG2 THR A 160     -26.353   2.809 -20.046  1.00 24.88           C
ANISOU 1298  CG2 THR A 160     3509   2842   3104    -42    -19    508       C
ATOM   1299  N   PRO A 161     -25.929  -1.211 -22.876  1.00 22.79           N
ANISOU 1299  N   PRO A 161     2925   2987   2748     30    127    139       N
ATOM   1300  CA  PRO A 161     -25.250  -2.434 -23.283  1.00 23.96           C
ANISOU 1300  CA  PRO A 161     3330   2947   2829    217     50    -71       C
ATOM   1301  C   PRO A 161     -23.792  -2.229 -23.637  1.00 23.98           C
ANISOU 1301  C   PRO A 161     3530   2928   2654   -130    221   -180       C
ATOM   1302  O   PRO A 161     -23.340  -1.129 -23.902  1.00 24.92           O
ANISOU 1302  O   PRO A 161     3379   2861   3228   -102    110    264       O
ATOM   1303  CB  PRO A 161     -26.045  -2.880 -24.485  1.00 25.70           C
ANISOU 1303  CB  PRO A 161     3352   3467   2945    -85     34    -87       C
ATOM   1304  CG  PRO A 161     -26.484  -1.575 -25.064  1.00 26.62           C
ANISOU 1304  CG  PRO A 161     3742   3208   3164   -125   -324   -226       C
ATOM   1305  CD  PRO A 161     -26.882  -0.773 -23.894  1.00 24.64           C
ANISOU 1305  CD  PRO A 161     3381   3163   2817     44   -192    401       C
ATOM   1306  N   GLY A 162     -23.051  -3.332 -23.624  1.00 24.85           N
ANISOU 1306  N   GLY A 162     3571   2786   3085    -99    110    288       N
ATOM   1307  CA  GLY A 162     -21.652  -3.321 -23.953  1.00 27.32           C
ANISOU 1307  CA  GLY A 162     3502   3485   3392   -169    229    167       C
ATOM   1308  C   GLY A 162     -20.869  -4.149 -22.931  1.00 24.93           C
ANISOU 1308  C   GLY A 162     3417   3297   2758    -93    193    216       C
ATOM   1309  O   GLY A 162     -20.328  -5.221 -23.254  1.00 29.26           O
ANISOU 1309  O   GLY A 162     4039   3519   3559    138    133     28       O
ATOM   1310  N   HIS A 163     -20.833  -3.655 -21.698  1.00 24.21           N
ANISOU 1310  N   HIS A 163     2864   3400   2937    -53    228     82       N
ATOM   1311  CA  HIS A 163     -20.225  -4.402 -20.624  1.00 24.09           C
ANISOU 1311  CA  HIS A 163     3132   3098   2924    -99     90    600       C
ATOM   1312  C   HIS A 163     -20.906  -5.764 -20.486  1.00 23.40           C
ANISOU 1312  C   HIS A 163     2988   2943   2958     58    163     56       C
ATOM   1313  O   HIS A 163     -20.256  -6.773 -20.240  1.00 25.28           O
ANISOU 1313  O   HIS A 163     2988   2705   3911     96    -37    250       O
ATOM   1314  CB  HIS A 163     -20.340  -3.613 -19.316  1.00 25.89           C
ANISOU 1314  CB  HIS A 163     3154   3391   3293   -510    275    281       C
ATOM   1315  CG  HIS A 163     -19.821  -4.366 -18.142  1.00 25.00           C
ANISOU 1315  CG  HIS A 163     3353   3205   2942    -17    -60    301       C
ATOM   1316  ND1 HIS A 163     -18.475  -4.538 -17.893  1.00 26.37           N
ANISOU 1316  ND1 HIS A 163     2978   3530   3513   -343   -110    234       N
ATOM   1317  CD2 HIS A 163     -20.461  -4.996 -17.135  1.00 24.13           C
ANISOU 1317  CD2 HIS A 163     2927   3046   3197   -481     56    147       C
ATOM   1318  CE1 HIS A 163     -18.313  -5.241 -16.765  1.00 26.39           C
ANISOU 1318  CE1 HIS A 163     2971   3522   3534   -205     79    356       C
ATOM   1319  NE2 HIS A 163     -19.491  -5.506 -16.283  1.00 22.36           N
ANISOU 1319  NE2 HIS A 163     2993   2616   2887     76    -71    458       N
ATOM   1320  N   ALA A 164     -22.217  -5.770 -20.605  1.00 22.97           N
ANISOU 1320  N   ALA A 164     2733   2648   3348     73    223     34       N
ATOM   1321  CA  ALA A 164     -23.035  -6.985 -20.623  1.00 21.45           C
ANISOU 1321  CA  ALA A 164     2837   2401   2911    156     80    247       C
ATOM   1322  C   ALA A 164     -24.283  -6.685 -21.450  1.00 22.03           C
ANISOU 1322  C   ALA A 164     2755   2680   2933     13   -132    133       C
ATOM   1323  O   ALA A 164     -24.713  -5.542 -21.504  1.00 22.48           O
ANISOU 1323  O   ALA A 164     2795   2602   3145    241     -6    114       O
ATOM   1324  CB  ALA A 164     -23.452  -7.379 -19.216  1.00 23.42           C
ANISOU 1324  CB  ALA A 164     3122   2765   3011     71   -234    199       C
ATOM   1325  N   SER A 165     -24.912  -7.728 -21.979  1.00 22.49           N
ANISOU 1325  N   SER A 165     2836   2829   2880    225   -191    -45       N
ATOM   1326  CA  SER A 165     -26.118  -7.599 -22.769  1.00 22.22           C
ANISOU 1326  CA  SER A 165     2864   2829   2750    264   -190    -81       C
ATOM   1327  C   SER A 165     -27.290  -7.121 -21.923  1.00 21.49           C
ANISOU 1327  C   SER A 165     2967   2528   2670    193    -52   -289       C
ATOM   1328  O   SER A 165     -28.254  -6.536 -22.469  1.00 25.43           O
ANISOU 1328  O   SER A 165     3237   3371   3053    686   -248    -44       O
ATOM   1329  CB  SER A 165     -26.465  -8.896 -23.482  1.00 24.23           C
ANISOU 1329  CB  SER A 165     2559   3424   3222     35    -11   -612       C
ATOM   1330  OG  SER A 165     -26.559  -9.997 -22.624  1.00 24.36           O
ANISOU 1330  OG  SER A 165     3225   2963   3067     76    232   -325       O
ATOM   1331  N   THR A 166     -27.226  -7.434 -20.641  1.00 20.74           N
ANISOU 1331  N   THR A 166     2715   2644   2521    107   -348    -24       N
ATOM   1332  CA  THR A 166     -28.308  -7.148 -19.699  1.00 20.74           C
ANISOU 1332  CA  THR A 166     2680   2674   2526    351   -159    -33       C
ATOM   1333  C   THR A 166     -28.118  -5.812 -19.016  1.00 21.01           C
ANISOU 1333  C   THR A 166     2641   2513   2829    132   -436     33       C
ATOM   1334  O   THR A 166     -28.891  -5.513 -18.100  1.00 22.35           O
ANISOU 1334  O   THR A 166     2636   2890   2966     30   -409    -84       O
ATOM   1335  CB  THR A 166     -28.314  -8.261 -18.658  1.00 19.76           C
ANISOU 1335  CB  THR A 166     2281   2641   2588    146   -403    -15       C
ATOM   1336  OG1 THR A 166     -26.998  -8.306 -18.101  1.00 20.04           O
ANISOU 1336  OG1 THR A 166     2495   2483   2637     62   -155     -1       O
ATOM   1337  CG2 THR A 166     -28.686  -9.613 -19.207  1.00 21.97           C
ANISOU 1337  CG2 THR A 166     2428   3198   2722    113   -150    -25       C
ATOM   1338  N   HIS A 167     -27.169  -4.999 -19.486  1.00 20.90           N
ANISOU 1338  N   HIS A 167     2857   2490   2595   -119     55    184       N
ATOM   1339  CA  HIS A 167     -26.765  -3.836 -18.680  1.00 20.32           C
ANISOU 1339  CA  HIS A 167     2756   2429   2534    265   -122    151       C
ATOM   1340  C   HIS A 167     -27.723  -2.664 -18.817  1.00 21.25           C
ANISOU 1340  C   HIS A 167     2596   2675   2805    104     28     68       C
ATOM   1341  O   HIS A 167     -27.980  -2.192 -19.917  1.00 21.81           O
ANISOU 1341  O   HIS A 167     2956   2670   2660    114   -180     16       O
ATOM   1342  CB  HIS A 167     -25.318  -3.451 -19.015  1.00 21.81           C
ANISOU 1342  CB  HIS A 167     2697   2803   2785    -72   -174    219       C
ATOM   1343  CG  HIS A 167     -24.686  -2.698 -17.920  1.00 22.07           C
ANISOU 1343  CG  HIS A 167     2788   2844   2754     51    -76    -54       C
ATOM   1344  ND1 HIS A 167     -24.930  -1.364 -17.688  1.00 21.55           N
ANISOU 1344  ND1 HIS A 167     2840   2488   2859   -205    183    -41       N
ATOM   1345  CD2 HIS A 167     -23.938  -3.152 -16.865  1.00 21.98           C
ANISOU 1345  CD2 HIS A 167     2860   2608   2884     68   -270    188       C
ATOM   1346  CE1 HIS A 167     -24.302  -1.016 -16.565  1.00 23.62           C
ANISOU 1346  CE1 HIS A 167     2805   3091   3078   -225   -280   -103       C
ATOM   1347  NE2 HIS A 167     -23.690  -2.078 -16.053  1.00 22.03           N
ANISOU 1347  NE2 HIS A 167     2572   2770   3027    140   -272    145       N
ATOM   1348  N   ILE A 168     -28.095  -2.112 -17.668  1.00 20.99           N
ANISOU 1348  N   ILE A 168     2629   2753   2592     56    -73    146       N
ATOM   1349  CA  ILE A 168     -28.926  -0.911 -17.580  1.00 21.68           C
ANISOU 1349  CA  ILE A 168     2944   2512   2781     80   -229    199       C
ATOM   1350  C   ILE A 168     -28.280   0.024 -16.549  1.00 21.32           C
ANISOU 1350  C   ILE A 168     2765   2780   2555    138   -282    241       C
ATOM   1351  O   ILE A 168     -27.516  -0.432 -15.676  1.00 21.37           O
ANISOU 1351  O   ILE A 168     2719   2613   2787    192   -290    -77       O
ATOM   1352  CB  ILE A 168     -30.379  -1.187 -17.212  1.00 21.12           C
ANISOU 1352  CB  ILE A 168     2739   2495   2790    142    -90    171       C
ATOM   1353  CG1 ILE A 168     -30.515  -1.721 -15.794  1.00 21.65           C
ANISOU 1353  CG1 ILE A 168     2808   2793   2624    482    -18    102       C
ATOM   1354  CG2 ILE A 168     -30.990  -2.116 -18.258  1.00 22.40           C
ANISOU 1354  CG2 ILE A 168     2802   2996   2712   -178   -197    131       C
ATOM   1355  CD1 ILE A 168     -31.934  -1.992 -15.311  1.00 24.53           C
ANISOU 1355  CD1 ILE A 168     3233   3355   2732    527     17    379       C
ATOM   1356  N   SER A 169     -28.603   1.298 -16.645  1.00 22.09           N
ANISOU 1356  N   SER A 169     2949   2720   2725    303   -136    199       N
ATOM   1357  CA  SER A 169     -28.197   2.319 -15.687  1.00 21.64           C
ANISOU 1357  CA  SER A 169     2536   2545   3140    257    -26    235       C
ATOM   1358  C   SER A 169     -29.469   3.100 -15.320  1.00 21.98           C
ANISOU 1358  C   SER A 169     2832   2584   2935    326   -215    154       C
ATOM   1359  O   SER A 169     -30.443   3.039 -16.064  1.00 24.16           O
ANISOU 1359  O   SER A 169     3195   2856   3128    387   -392   -185       O
ATOM   1360  CB  SER A 169     -27.091   3.204 -16.260  1.00 22.34           C
ANISOU 1360  CB  SER A 169     2877   2676   2933    162   -328    178       C
ATOM   1361  OG  SER A 169     -25.973   2.463 -16.735  1.00 22.60           O
ANISOU 1361  OG  SER A 169     2767   2449   3369     73    -70     36       O
ATOM   1362  N   LEU A 170     -29.445   3.829 -14.200  1.00 22.27           N
ANISOU 1362  N   LEU A 170     2900   2738   2825    308   -119   -201       N
ATOM   1363  CA  LEU A 170     -30.604   4.558 -13.731  1.00 22.97           C
ANISOU 1363  CA  LEU A 170     3202   2322   3202    235    -95   -131       C
ATOM   1364  C   LEU A 170     -30.244   6.037 -13.683  1.00 24.41           C
ANISOU 1364  C   LEU A 170     3275   2685   3313    -24     40     -1       C
ATOM   1365  O   LEU A 170     -29.316   6.405 -12.964  1.00 26.19           O
ANISOU 1365  O   LEU A 170     3357   2985   3610    222   -352    306       O
ATOM   1366  CB  LEU A 170     -31.020   4.041 -12.353  1.00 24.32           C
ANISOU 1366  CB  LEU A 170     3373   2767   3100    111    146   -238       C
ATOM   1367  CG  LEU A 170     -31.313   2.549 -12.243  1.00 24.54           C
ANISOU 1367  CG  LEU A 170     3332   2857   3134     36    -82    105       C
ATOM   1368  CD1 LEU A 170     -31.658   2.137 -10.841  1.00 27.55           C
ANISOU 1368  CD1 LEU A 170     3801   3466   3200   -309   -283   -194       C
ATOM   1369  CD2 LEU A 170     -32.332   2.031 -13.223  1.00 25.63           C
ANISOU 1369  CD2 LEU A 170     3329   3148   3263   -168     78    -31       C
ATOM   1370  N   TYR A 171     -31.000   6.861 -14.442  1.00 26.10           N
ANISOU 1370  N   TYR A 171     3657   2992   3268    178   -345    126       N
ATOM   1371  CA  TYR A 171     -30.700   8.285 -14.550  1.00 25.78           C
ANISOU 1371  CA  TYR A 171     3531   2882   3384    294   -200    205       C
ATOM   1372  C   TYR A 171     -31.739   9.118 -13.818  1.00 24.79           C
ANISOU 1372  C   TYR A 171     2847   3094   3480     71   -111    130       C
ATOM   1373  O   TYR A 171     -32.926   8.925 -14.040  1.00 26.49           O
ANISOU 1373  O   TYR A 171     3194   2956   3916    320     76   -160       O
ATOM   1374  CB  TYR A 171     -30.677   8.715 -16.025  1.00 25.53           C
ANISOU 1374  CB  TYR A 171     3391   3127   3183    600   -456     60       C
ATOM   1375  CG  TYR A 171     -30.359  10.178 -16.269  1.00 26.90           C
ANISOU 1375  CG  TYR A 171     4052   2996   3173    624    -35     82       C
ATOM   1376  CD1 TYR A 171     -29.116  10.693 -15.933  1.00 31.64           C
ANISOU 1376  CD1 TYR A 171     4549   3332   4140    215   -134    179       C
ATOM   1377  CD2 TYR A 171     -31.273  11.047 -16.832  1.00 32.37           C
ANISOU 1377  CD2 TYR A 171     4692   3608   4000    452   -595   -207       C
ATOM   1378  CE1 TYR A 171     -28.779  12.024 -16.133  1.00 32.28           C
ANISOU 1378  CE1 TYR A 171     5275   3212   3777    637    178    214       C
ATOM   1379  CE2 TYR A 171     -30.940  12.385 -17.067  1.00 35.21           C
ANISOU 1379  CE2 TYR A 171     5256   3771   4349    607     41    239       C
ATOM   1380  CZ  TYR A 171     -29.685  12.871 -16.747  1.00 33.41           C
ANISOU 1380  CZ  TYR A 171     5538   3072   4086    495     16    759       C
ATOM   1381  OH  TYR A 171     -29.356  14.210 -16.921  1.00 36.19           O
ANISOU 1381  OH  TYR A 171     6111   3056   4582    752    -70    864       O
ATOM   1382  N   ARG A 172     -31.299  10.085 -13.025  1.00 26.23           N
ANISOU 1382  N   ARG A 172     3222   3110   3635    149     12     -2       N
ATOM   1383  CA  ARG A 172     -32.176  11.000 -12.318  1.00 28.06           C
ANISOU 1383  CA  ARG A 172     4191   2871   3601    486   -352   -131       C
ATOM   1384  C   ARG A 172     -32.029  12.383 -12.956  1.00 30.34           C
ANISOU 1384  C   ARG A 172     4325   3187   4015    430     96     95       C
ATOM   1385  O   ARG A 172     -31.031  13.085 -12.736  1.00 30.85           O
ANISOU 1385  O   ARG A 172     4513   3155   4051    684      1     94       O
ATOM   1386  CB  ARG A 172     -31.779  11.056 -10.834  1.00 28.06           C
ANISOU 1386  CB  ARG A 172     4423   2664   3576     39   -144   -134       C
ATOM   1387  CG  ARG A 172     -32.791  11.892 -10.067  1.00 29.41           C
ANISOU 1387  CG  ARG A 172     4531   2629   4014    556   -184   -604       C
ATOM   1388  CD  ARG A 172     -32.762  11.628  -8.608  1.00 31.70           C
ANISOU 1388  CD  ARG A 172     4280   3746   4017    533    515   -525       C
ATOM   1389  NE  ARG A 172     -31.470  11.973  -8.018  1.00 30.38           N
ANISOU 1389  NE  ARG A 172     4259   3162   4122    202   -286   -489       N
ATOM   1390  CZ  ARG A 172     -31.067  11.693  -6.785  1.00 30.63           C
ANISOU 1390  CZ  ARG A 172     4487   3164   3988    387    118   -326       C
ATOM   1391  NH1 ARG A 172     -31.799  10.930  -6.020  1.00 30.38           N
ANISOU 1391  NH1 ARG A 172     4299   3422   3821    399   -237    233       N
ATOM   1392  NH2 ARG A 172     -29.891  12.155  -6.346  1.00 33.77           N
ANISOU 1392  NH2 ARG A 172     4955   3725   4152     70   -315    104       N
ATOM   1393  N   GLU A 173     -33.024  12.756 -13.770  1.00 30.81           N
ANISOU 1393  N   GLU A 173     4651   3282   3775    149    -33     76       N
ATOM   1394  CA  GLU A 173     -32.982  13.999 -14.532  1.00 33.39           C
ANISOU 1394  CA  GLU A 173     5064   3084   4539    583    -72    173       C
ATOM   1395  C   GLU A 173     -32.882  15.222 -13.625  1.00 32.78           C
ANISOU 1395  C   GLU A 173     5234   3214   4005    595   -169    340       C
ATOM   1396  O   GLU A 173     -32.257  16.186 -14.007  1.00 36.77           O
ANISOU 1396  O   GLU A 173     5695   2963   5311    385    377    576       O
ATOM   1397  CB  GLU A 173     -34.180  14.070 -15.475  1.00 38.42           C
ANISOU 1397  CB  GLU A 173     5704   4251   4642    -94   -622    949       C
ATOM   1398  N   ARG A 174     -33.464  15.161 -12.419  1.00 35.39           N
ANISOU 1398  N   ARG A 174     5956   2946   4546    715   -379      7       N
ATOM   1399  CA  ARG A 174     -33.502  16.321 -11.541  1.00 33.29           C
ANISOU 1399  CA  ARG A 174     5298   2949   4400    785     79   -163       C
ATOM   1400  C   ARG A 174     -32.105  16.909 -11.324  1.00 32.69           C
ANISOU 1400  C   ARG A 174     4802   2833   4786    464   -341     51       C
ATOM   1401  O   ARG A 174     -31.937  18.128 -11.430  1.00 36.20           O
ANISOU 1401  O   ARG A 174     6085   2420   5250    530    413    371       O
ATOM   1402  CB  ARG A 174     -34.173  16.027 -10.200  1.00 35.62           C
ANISOU 1402  CB  ARG A 174     5677   3139   4717    451     10   -560       C
ATOM   1403  CG  ARG A 174     -34.125  17.209  -9.241  1.00 37.12           C
ANISOU 1403  CG  ARG A 174     5685   3308   5112    130    290   -897       C
ATOM   1404  CD  ARG A 174     -34.934  16.929  -7.998  1.00 36.91           C
ANISOU 1404  CD  ARG A 174     6095   3223   4705   -178    285   -841       C
ATOM   1405  NE  ARG A 174     -34.623  15.671  -7.308  1.00 38.32           N
ANISOU 1405  NE  ARG A 174     6186   3403   4969   -180    445   -230       N
ATOM   1406  CZ  ARG A 174     -33.540  15.434  -6.587  1.00 37.23           C
ANISOU 1406  CZ  ARG A 174     5638   3952   4555   -173    772    -37       C
ATOM   1407  NH1 ARG A 174     -33.410  14.291  -5.958  1.00 37.83           N
ANISOU 1407  NH1 ARG A 174     6162   3429   4781     -3    752   -520       N
ATOM   1408  NH2 ARG A 174     -32.610  16.353  -6.448  1.00 37.37           N
ANISOU 1408  NH2 ARG A 174     5770   3745   4682    169    638   -412       N
ATOM   1409  N   ASP A 175     -31.136  16.058 -10.948  1.00 31.95           N
ANISOU 1409  N   ASP A 175     5442   2156   4540    853     15    -54       N
ATOM   1410  CA  ASP A 175     -29.791  16.495 -10.613  1.00 31.26           C
ANISOU 1410  CA  ASP A 175     4710   2416   4751    350    -58    -72       C
ATOM   1411  C   ASP A 175     -28.677  15.814 -11.423  1.00 31.44           C
ANISOU 1411  C   ASP A 175     4803   2360   4782    415    -25    -91       C
ATOM   1412  O   ASP A 175     -27.485  16.074 -11.172  1.00 33.07           O
ANISOU 1412  O   ASP A 175     4665   3161   4738    106    -96   -164       O
ATOM   1413  CB  ASP A 175     -29.537  16.276  -9.134  1.00 35.80           C
ANISOU 1413  CB  ASP A 175     5688   3042   4871    258    240    -79       C
ATOM   1414  CG  ASP A 175     -29.619  14.836  -8.642  1.00 33.16           C
ANISOU 1414  CG  ASP A 175     4873   3156   4571   -238    276     -1       C
ATOM   1415  OD1 ASP A 175     -30.020  13.963  -9.459  1.00 31.33           O
ANISOU 1415  OD1 ASP A 175     4506   2960   4437    -79    -65   -173       O
ATOM   1416  OD2 ASP A 175     -29.287  14.611  -7.448  1.00 33.54           O
ANISOU 1416  OD2 ASP A 175     5056   3398   4289     23     20   -284       O
ATOM   1417  N   GLY A 176     -29.040  14.975 -12.397  1.00 32.45           N
ANISOU 1417  N   GLY A 176     5372   2965   3993    160    185    325       N
ATOM   1418  CA  GLY A 176     -28.073  14.393 -13.337  1.00 29.40           C
ANISOU 1418  CA  GLY A 176     4198   2834   4139    237   -166    367       C
ATOM   1419  C   GLY A 176     -27.295  13.222 -12.760  1.00 27.03           C
ANISOU 1419  C   GLY A 176     3799   2832   3639     37   -175    334       C
ATOM   1420  O   GLY A 176     -26.299  12.820 -13.349  1.00 29.76           O
ANISOU 1420  O   GLY A 176     4110   3165   4034    -15   -174     43       O
ATOM   1421  N   VAL A 177     -27.787  12.646 -11.652  1.00 26.95           N
ANISOU 1421  N   VAL A 177     3708   2854   3680    342     10    237       N
ATOM   1422  CA  VAL A 177     -27.102  11.507 -11.032  1.00 26.64           C
ANISOU 1422  CA  VAL A 177     4128   2332   3663     -3   -530    -12       C
ATOM   1423  C   VAL A 177     -27.427  10.245 -11.831  1.00 25.58           C
ANISOU 1423  C   VAL A 177     3580   2343   3795     17   -262     85       C
ATOM   1424  O   VAL A 177     -28.572  10.018 -12.198  1.00 27.26           O
ANISOU 1424  O   VAL A 177     4027   2379   3950    138   -332     82       O
ATOM   1425  CB  VAL A 177     -27.469  11.356  -9.546  1.00 30.80           C
ANISOU 1425  CB  VAL A 177     4601   2986   4114   -116   -579    -55       C
ATOM   1426  CG1 VAL A 177     -27.078   9.989  -8.988  1.00 31.73           C
ANISOU 1426  CG1 VAL A 177     4679   3300   4074    365   -352    -76       C
ATOM   1427  CG2 VAL A 177     -26.838  12.475  -8.715  1.00 32.01           C
ANISOU 1427  CG2 VAL A 177     5007   3326   3830     98   -703   -406       C
ATOM   1428  N   LEU A 178     -26.414   9.443 -12.110  1.00 25.56           N
ANISOU 1428  N   LEU A 178     3915   2438   3359    213   -406    -77       N
ATOM   1429  CA  LEU A 178     -26.576   8.150 -12.764  1.00 24.85           C
ANISOU 1429  CA  LEU A 178     3483   2550   3407   -262   -232     34       C
ATOM   1430  C   LEU A 178     -26.121   7.055 -11.812  1.00 24.60           C
ANISOU 1430  C   LEU A 178     3375   2743   3227     66   -103     54       C
ATOM   1431  O   LEU A 178     -25.006   7.134 -11.310  1.00 25.41           O
ANISOU 1431  O   LEU A 178     3445   2682   3527   -285   -150    169       O
ATOM   1432  CB  LEU A 178     -25.720   8.082 -14.030  1.00 25.94           C
ANISOU 1432  CB  LEU A 178     3757   2518   3579   -204    -53    270       C
ATOM   1433  CG  LEU A 178     -25.945   6.837 -14.889  1.00 25.46           C
ANISOU 1433  CG  LEU A 178     3727   2700   3245    -60    -12    239       C
ATOM   1434  CD1 LEU A 178     -27.231   6.974 -15.692  1.00 24.70           C
ANISOU 1434  CD1 LEU A 178     3496   2479   3411    160     48    332       C
ATOM   1435  CD2 LEU A 178     -24.815   6.569 -15.792  1.00 26.36           C
ANISOU 1435  CD2 LEU A 178     3645   3111   3259   -117   -241    151       C
ATOM   1436  N   ILE A 179     -26.987   6.074 -11.548  1.00 22.98           N
ANISOU 1436  N   ILE A 179     3176   2560   2996    280   -123    -29       N
ATOM   1437  CA  ILE A 179     -26.548   4.851 -10.908  1.00 22.67           C
ANISOU 1437  CA  ILE A 179     3253   2213   3147    224   -172    157       C
ATOM   1438  C   ILE A 179     -26.096   3.993 -12.076  1.00 22.31           C
ANISOU 1438  C   ILE A 179     2987   2354   3134    -27    -61    121       C
ATOM   1439  O   ILE A 179     -26.928   3.488 -12.838  1.00 23.47           O
ANISOU 1439  O   ILE A 179     3061   2597   3259     49   -173    143       O
ATOM   1440  CB  ILE A 179     -27.660   4.218 -10.056  1.00 24.70           C
ANISOU 1440  CB  ILE A 179     3213   3004   3169    137   -158     15       C
ATOM   1441  CG1 ILE A 179     -28.172   5.219  -9.011  1.00 28.99           C
ANISOU 1441  CG1 ILE A 179     4039   3519   3458    614    297     53       C
ATOM   1442  CG2 ILE A 179     -27.132   2.925  -9.429  1.00 26.15           C
ANISOU 1442  CG2 ILE A 179     3328   3115   3492     -9    154    353       C
ATOM   1443  CD1 ILE A 179     -29.369   4.780  -8.167  1.00 33.00           C
ANISOU 1443  CD1 ILE A 179     4783   3784   3969    837    471     53       C
ATOM   1444  N   GLY A 180     -24.765   3.914 -12.290  1.00 22.94           N
ANISOU 1444  N   GLY A 180     2765   2710   3242    -96   -175    214       N
ATOM   1445  CA  GLY A 180     -24.241   3.497 -13.587  1.00 23.79           C
ANISOU 1445  CA  GLY A 180     3310   2624   3104    144    158    -55       C
ATOM   1446  C   GLY A 180     -24.078   2.001 -13.791  1.00 22.85           C
ANISOU 1446  C   GLY A 180     2979   2679   3024    324    -66    217       C
ATOM   1447  O   GLY A 180     -23.973   1.570 -14.949  1.00 23.64           O
ANISOU 1447  O   GLY A 180     3346   2796   2840    -39     -3    127       O
ATOM   1448  N   GLY A 181     -24.030   1.218 -12.695  1.00 21.07           N
ANISOU 1448  N   GLY A 181     2650   2413   2943    -68    -75   -189       N
ATOM   1449  CA  GLY A 181     -23.548  -0.137 -12.866  1.00 21.81           C
ANISOU 1449  CA  GLY A 181     2741   2720   2824    -39    -66    -38       C
ATOM   1450  C   GLY A 181     -22.080  -0.144 -13.280  1.00 21.87           C
ANISOU 1450  C   GLY A 181     2629   2655   3026     18   -141    178       C
ATOM   1451  O   GLY A 181     -21.301   0.709 -12.831  1.00 23.49           O
ANISOU 1451  O   GLY A 181     2980   2770   3177   -548   -321    280       O
ATOM   1452  N   ASP A 182     -21.743  -1.082 -14.179  1.00 21.81           N
ANISOU 1452  N   ASP A 182     2926   2580   2779   -290   -319     17       N
ATOM   1453  CA  ASP A 182     -20.393  -1.250 -14.652  1.00 21.87           C
ANISOU 1453  CA  ASP A 182     2615   2936   2757   -261   -142    153       C
ATOM   1454  C   ASP A 182     -20.148  -0.618 -16.027  1.00 23.00           C
ANISOU 1454  C   ASP A 182     2846   2663   3230   -216    -71    222       C
ATOM   1455  O   ASP A 182     -19.139  -0.895 -16.662  1.00 24.78           O
ANISOU 1455  O   ASP A 182     2780   3043   3594    207    386    329       O
ATOM   1456  CB  ASP A 182     -20.008  -2.718 -14.637  1.00 22.63           C
ANISOU 1456  CB  ASP A 182     2994   2694   2910   -251   -212    455       C
ATOM   1457  CG  ASP A 182     -19.844  -3.361 -13.257  1.00 21.06           C
ANISOU 1457  CG  ASP A 182     2616   2651   2735   -359     51    207       C
ATOM   1458  OD1 ASP A 182     -20.053  -2.597 -12.238  1.00 22.94           O
ANISOU 1458  OD1 ASP A 182     3002   2741   2974    -55    -63    205       O
ATOM   1459  OD2 ASP A 182     -19.566  -4.618 -13.209  1.00 21.64           O
ANISOU 1459  OD2 ASP A 182     3137   1976   3108    -30     -4    389       O
ATOM   1460  N   ALA A 183     -21.045   0.249 -16.484  1.00 23.46           N
ANISOU 1460  N   ALA A 183     3035   2672   3206    -14    202    440       N
ATOM   1461  CA  ALA A 183     -20.883   0.851 -17.792  1.00 24.27           C
ANISOU 1461  CA  ALA A 183     3146   2831   3247   -130    -17    521       C
ATOM   1462  C   ALA A 183     -19.659   1.748 -17.867  1.00 25.75           C
ANISOU 1462  C   ALA A 183     3278   3069   3435   -139    231    333       C
ATOM   1463  O   ALA A 183     -18.986   1.738 -18.894  1.00 30.71           O
ANISOU 1463  O   ALA A 183     4268   3880   3521   -796    565    460       O
ATOM   1464  CB  ALA A 183     -22.103   1.618 -18.214  1.00 25.87           C
ANISOU 1464  CB  ALA A 183     3359   2970   3498    -87   -356    586       C
ATOM   1465  N   LEU A 184     -19.370   2.442 -16.761  1.00 25.74           N
ANISOU 1465  N   LEU A 184     3265   3012   3502   -329    239    471       N
ATOM   1466  CA  LEU A 184     -18.258   3.373 -16.695  1.00 27.91           C
ANISOU 1466  CA  LEU A 184     3731   3039   3834   -376    341    158       C
ATOM   1467  C   LEU A 184     -17.682   3.308 -15.286  1.00 30.72           C
ANISOU 1467  C   LEU A 184     3601   3807   4265   -316    -20    -39       C
ATOM   1468  O   LEU A 184     -18.361   3.674 -14.306  1.00 36.78           O
ANISOU 1468  O   LEU A 184     4915   4213   4846    600   -764     89       O
ATOM   1469  CB  LEU A 184     -18.730   4.776 -17.021  1.00 31.82           C
ANISOU 1469  CB  LEU A 184     4082   3169   4837   -677    370    567       C
ATOM   1470  CG  LEU A 184     -17.598   5.788 -17.204  1.00 35.29           C
ANISOU 1470  CG  LEU A 184     4466   3687   5255   -655    703    792       C
ATOM   1471  CD1 LEU A 184     -16.558   5.374 -18.253  1.00 39.46           C
ANISOU 1471  CD1 LEU A 184     5455   4149   5390   -994    909    247       C
ATOM   1472  CD2 LEU A 184     -18.187   7.144 -17.587  1.00 41.77           C
ANISOU 1472  CD2 LEU A 184     6423   3789   5658    -11     91    962       C
ATOM   1473  N   ILE A 185     -16.496   2.736 -15.185  1.00 31.68           N
ANISOU 1473  N   ILE A 185     3566   4104   4368    202    -54    229       N
ATOM   1474  CA  ILE A 185     -15.791   2.596 -13.916  1.00 31.69           C
ANISOU 1474  CA  ILE A 185     3650   3756   4634   -461   -101     55       C
ATOM   1475  C   ILE A 185     -14.550   3.485 -13.979  1.00 33.51           C
ANISOU 1475  C   ILE A 185     3765   3631   5338   -424     55    360       C
ATOM   1476  O   ILE A 185     -13.824   3.478 -14.975  1.00 36.77           O
ANISOU 1476  O   ILE A 185     4628   4027   5314   -321    546    854       O
ATOM   1477  CB  ILE A 185     -15.443   1.116 -13.693  1.00 33.31           C
ANISOU 1477  CB  ILE A 185     3574   4230   4852   -246   -375    486       C
ATOM   1478  CG1 ILE A 185     -16.703   0.286 -13.658  1.00 33.77           C
ANISOU 1478  CG1 ILE A 185     4064   4676   4092   -869   -598    266       C
ATOM   1479  CG2 ILE A 185     -14.605   0.911 -12.427  1.00 34.54           C
ANISOU 1479  CG2 ILE A 185     4053   4095   4976   -579   -571    285       C
ATOM   1480  CD1 ILE A 185     -16.439  -1.184 -13.685  1.00 35.91           C
ANISOU 1480  CD1 ILE A 185     4499   4818   4326   -491   -323    605       C
ATOM   1481  N   GLY A 186     -14.334   4.246 -12.911  1.00 34.58           N
ANISOU 1481  N   GLY A 186     4283   4329   4525   -275    115   1012       N
ATOM   1482  CA  GLY A 186     -13.309   5.270 -12.869  1.00 34.60           C
ANISOU 1482  CA  GLY A 186     3683   3878   5585   -446   -370    828       C
ATOM   1483  C   GLY A 186     -11.864   4.787 -13.014  1.00 41.26           C
ANISOU 1483  C   GLY A 186     4423   5155   6097   -337    242    930       C
ATOM   1484  O   GLY A 186     -11.038   5.490 -13.616  1.00 46.50           O
ANISOU 1484  O   GLY A 186     5333   5423   6910   -915    687   1008       O
ATOM   1485  N   HIS A 187     -11.561   3.620 -12.438  1.00 39.44           N
ANISOU 1485  N   HIS A 187     3884   4760   6339   -412   -484    368       N
ATOM   1486  CA  HIS A 187     -10.178   3.202 -12.249  1.00 44.01           C
ANISOU 1486  CA  HIS A 187     4516   5751   6455   -308   -375    586       C
ATOM   1487  C   HIS A 187      -9.767   2.151 -13.272  1.00 43.46           C
ANISOU 1487  C   HIS A 187     3847   5467   7198   -766   -445   -454       C
ATOM   1488  O   HIS A 187      -8.555   1.947 -13.482  1.00 51.61           O
ANISOU 1488  O   HIS A 187     4179   7166   8266   -381    -41    151       O
ATOM   1489  CB  HIS A 187      -9.916   2.762 -10.797  1.00 44.52           C
ANISOU 1489  CB  HIS A 187     4773   6274   5867   -962  -1384    759       C
ATOM   1490  CG  HIS A 187     -10.725   1.601 -10.302  1.00 47.44           C
ANISOU 1490  CG  HIS A 187     5466   5910   6650   -775   -437   1559       C
ATOM   1491  ND1 HIS A 187     -12.067   1.727 -10.019  1.00 46.69           N
ANISOU 1491  ND1 HIS A 187     5623   5860   6257  -1057   -787    855       N
ATOM   1492  CD2 HIS A 187     -10.415   0.309 -10.057  1.00 53.68           C
ANISOU 1492  CD2 HIS A 187     5948   6862   7588    203   -148   1588       C
ATOM   1493  CE1 HIS A 187     -12.543   0.549  -9.611  1.00 47.74           C
ANISOU 1493  CE1 HIS A 187     5580   6481   6077   -223   -470   2001       C
ATOM   1494  NE2 HIS A 187     -11.553  -0.328  -9.616  1.00 54.56           N
ANISOU 1494  NE2 HIS A 187     6954   5532   8244   -180   -334   1284       N
ATOM   1495  N   ILE A 188     -10.751   1.473 -13.875  1.00 42.22           N
ANISOU 1495  N   ILE A 188     4023   4920   7099   -706    -41    -78       N
ATOM   1496  CA  ILE A 188     -10.456   0.378 -14.791  1.00 40.93           C
ANISOU 1496  CA  ILE A 188     4589   4917   6046   -130   -523   -508       C
ATOM   1497  C   ILE A 188     -11.491   0.336 -15.918  1.00 42.82           C
ANISOU 1497  C   ILE A 188     4423   5836   6012    -49   -247   -338       C
ATOM   1498  O   ILE A 188     -12.650   0.722 -15.767  1.00 41.98           O
ANISOU 1498  O   ILE A 188     4477   4703   6771   -154    112    281       O
ATOM   1499  CB  ILE A 188     -10.372  -0.959 -14.031  1.00 47.26           C
ANISOU 1499  CB  ILE A 188     6516   4921   6521  -1097   -378     68       C
ATOM   1500  N   SER A 189     -11.054  -0.113 -17.093  1.00 42.52           N
ANISOU 1500  N   SER A 189     4231   5442   6482   -399   -217   -521       N
ATOM   1501  CA  SER A 189     -11.974  -0.249 -18.208  1.00 39.95           C
ANISOU 1501  CA  SER A 189     5218   3912   6048   -206   -201   -316       C
ATOM   1502  C   SER A 189     -12.948  -1.381 -17.870  1.00 41.27           C
ANISOU 1502  C   SER A 189     4643   4409   6631   -576   -254    183       C
ATOM   1503  O   SER A 189     -12.609  -2.270 -17.071  1.00 43.44           O
ANISOU 1503  O   SER A 189     5321   5158   6025   -647  -1558    467       O
ATOM   1504  CB  SER A 189     -11.219  -0.496 -19.489  1.00 48.31           C
ANISOU 1504  CB  SER A 189     6115   5896   6343    588    387     19       C
ATOM   1505  OG  SER A 189     -10.296  -1.547 -19.268  1.00 53.09           O
ANISOU 1505  OG  SER A 189     5988   7187   6997    975    -37   -686       O
ATOM   1506  N   SER A 190     -14.151  -1.297 -18.438  1.00 39.14           N
ANISOU 1506  N   SER A 190     4670   4727   5475   -435   -212    118       N
ATOM   1507  CA  SER A 190     -15.249  -2.214 -18.163  1.00 39.85           C
ANISOU 1507  CA  SER A 190     4456   5073   5613   -301    427   -191       C
ATOM   1508  C   SER A 190     -15.683  -2.854 -19.479  1.00 40.76           C
ANISOU 1508  C   SER A 190     4352   5526   5609    167    233   -433       C
ATOM   1509  O   SER A 190     -16.874  -3.021 -19.719  1.00 37.18           O
ANISOU 1509  O   SER A 190     4094   4610   5422   -409    685   -143       O
ATOM   1510  CB  SER A 190     -16.436  -1.510 -17.490  1.00 36.54           C
ANISOU 1510  CB  SER A 190     3573   5862   4449   -774    928   -277       C
ATOM   1511  OG  SER A 190     -16.579  -0.174 -17.903  1.00 42.49           O
ANISOU 1511  OG  SER A 190     4854   5831   5460    123   -113   -561       O
ATOM   1512  N   ASN A 191     -14.684  -3.246 -20.297  1.00 39.00           N
ANISOU 1512  N   ASN A 191     4718   5018   5081   -439     58   -895       N
ATOM   1513  CA  ASN A 191     -14.913  -3.616 -21.680  1.00 37.91           C
ANISOU 1513  CA  ASN A 191     4713   4172   5519   -315    764   -538       C
ATOM   1514  C   ASN A 191     -15.816  -4.846 -21.744  1.00 34.11           C
ANISOU 1514  C   ASN A 191     3289   4944   4726   -754    131   -418       C
ATOM   1515  O   ASN A 191     -15.916  -5.555 -20.781  1.00 37.31           O
ANISOU 1515  O   ASN A 191     4442   4550   5185   -368    -22    491       O
ATOM   1516  CB  ASN A 191     -13.598  -3.921 -22.362  1.00 38.84           C
ANISOU 1516  CB  ASN A 191     4179   4784   5794   -422    812   -500       C
ATOM   1517  CG  ASN A 191     -12.930  -2.645 -22.822  1.00 43.13           C
ANISOU 1517  CG  ASN A 191     5425   4783   6180   -971   1400     67       C
ATOM   1518  OD1 ASN A 191     -13.505  -1.545 -22.672  1.00 50.78           O
ANISOU 1518  OD1 ASN A 191     5902   5881   7509   -388    513   -305       O
ATOM   1519  ND2 ASN A 191     -11.740  -2.763 -23.381  1.00 46.72           N
ANISOU 1519  ND2 ASN A 191     5776   5507   6469    273   1277    551       N
ATOM   1520  N   PRO A 192     -16.450  -5.153 -22.900  1.00 40.30           N
ANISOU 1520  N   PRO A 192     4812   5344   5158   -654    181     44       N
ATOM   1521  CA  PRO A 192     -17.354  -6.285 -23.003  1.00 31.20           C
ANISOU 1521  CA  PRO A 192     3144   4742   3969     64     92    119       C
ATOM   1522  C   PRO A 192     -16.788  -7.579 -22.459  1.00 32.29           C
ANISOU 1522  C   PRO A 192     2471   4836   4961    231    540    505       C
ATOM   1523  O   PRO A 192     -15.704  -7.945 -22.840  1.00 35.69           O
ANISOU 1523  O   PRO A 192     3652   4863   5044    618    974    774       O
ATOM   1524  CB  PRO A 192     -17.588  -6.391 -24.536  1.00 33.25           C
ANISOU 1524  CB  PRO A 192     3092   4844   4696    807    -70    302       C
ATOM   1525  CG  PRO A 192     -17.462  -4.979 -25.017  1.00 39.63           C
ANISOU 1525  CG  PRO A 192     4861   5090   5107    423   -236    663       C
ATOM   1526  CD  PRO A 192     -16.354  -4.407 -24.164  1.00 44.44           C
ANISOU 1526  CD  PRO A 192     5786   5739   5361   -143   -395     85       C
ATOM   1527  N   ILE A 193     -17.587  -8.221 -21.583  1.00 34.68           N
ANISOU 1527  N   ILE A 193     3095   5493   4589   -309    610   -147       N
ATOM   1528  CA  ILE A 193     -17.374  -9.557 -21.077  1.00 32.66           C
ANISOU 1528  CA  ILE A 193     3617   4342   4449  -1072    -38   -273       C
ATOM   1529  C   ILE A 193     -18.087 -10.546 -21.996  1.00 33.50           C
ANISOU 1529  C   ILE A 193     3711   4487   4531   -694   -325   -149       C
ATOM   1530  O   ILE A 193     -19.293 -10.417 -22.175  1.00 33.30           O
ANISOU 1530  O   ILE A 193     3858   4080   4712   -116     81   -237       O
ATOM   1531  CB  ILE A 193     -17.902  -9.653 -19.629  1.00 35.87           C
ANISOU 1531  CB  ILE A 193     3737   5496   4396   -767    250   -754       C
ATOM   1532  CG1 ILE A 193     -17.272  -8.557 -18.701  1.00 40.68           C
ANISOU 1532  CG1 ILE A 193     3985   6971   4500  -1358   1000   -821       C
ATOM   1533  CG2 ILE A 193     -17.738 -11.069 -19.069  1.00 35.34           C
ANISOU 1533  CG2 ILE A 193     3300   4944   5185   -608    716   -400       C
ATOM   1534  CD1 ILE A 193     -15.772  -8.520 -18.749  1.00 46.57           C
ANISOU 1534  CD1 ILE A 193     4142   7940   5611   -887    934   -893       C
ATOM   1535  N   LEU A 194     -17.310 -11.454 -22.617  1.00 30.44           N
ANISOU 1535  N   LEU A 194     3093   4545   3930    -77    219    101       N
ATOM   1536  CA  LEU A 194     -17.851 -12.433 -23.567  1.00 32.61           C
ANISOU 1536  CA  LEU A 194     3462   4961   3968   -455    212     97       C
ATOM   1537  C   LEU A 194     -19.053 -13.212 -23.047  1.00 29.47           C
ANISOU 1537  C   LEU A 194     3117   4578   3502   -204    -74    188       C
ATOM   1538  O   LEU A 194     -19.016 -13.742 -21.952  1.00 32.01           O
ANISOU 1538  O   LEU A 194     3403   4859   3900     81   -146     63       O
ATOM   1539  CB  LEU A 194     -16.801 -13.446 -24.004  1.00 39.05           C
ANISOU 1539  CB  LEU A 194     2654   6637   5546    344    540    134       C
ATOM   1540  CG  LEU A 194     -16.156 -13.236 -25.369  1.00 50.68           C
ANISOU 1540  CG  LEU A 194     5126   8083   6047    843    265   -635       C
ATOM   1541  CD1 LEU A 194     -15.143 -14.333 -25.524  1.00 52.57           C
ANISOU 1541  CD1 LEU A 194     4790   8573   6611    939    927   -366       C
ATOM   1542  CD2 LEU A 194     -17.185 -13.306 -26.475  1.00 50.21           C
ANISOU 1542  CD2 LEU A 194     5831   7431   5813   1078    177  -2687       C
ATOM   1543  N   GLU A 195     -20.063 -13.386 -23.909  1.00 27.43           N
ANISOU 1543  N   GLU A 195     2723   4051   3648    287   -117   -404       N
ATOM   1544  CA  GLU A 195     -21.260 -14.145 -23.571  1.00 24.54           C
ANISOU 1544  CA  GLU A 195     2665   3339   3318    340    -55   -385       C
ATOM   1545  C   GLU A 195     -21.602 -15.120 -24.676  1.00 26.29           C
ANISOU 1545  C   GLU A 195     2762   3601   3625    602      2   -216       C
ATOM   1546  O   GLU A 195     -21.337 -14.841 -25.854  1.00 28.35           O
ANISOU 1546  O   GLU A 195     3151   3727   3894    181    297   -556       O
ATOM   1547  CB  GLU A 195     -22.450 -13.176 -23.486  1.00 25.16           C
ANISOU 1547  CB  GLU A 195     2624   3519   3418    423    -17     11       C
ATOM   1548  CG  GLU A 195     -22.317 -12.169 -22.364  1.00 24.66           C
ANISOU 1548  CG  GLU A 195     2876   3320   3172   -179     19   -317       C
ATOM   1549  CD  GLU A 195     -23.466 -11.171 -22.281  1.00 24.72           C
ANISOU 1549  CD  GLU A 195     2732   3617   3043     72    -74   -124       C
ATOM   1550  OE1 GLU A 195     -24.452 -11.354 -23.064  1.00 25.30           O
ANISOU 1550  OE1 GLU A 195     3159   3293   3162    272   -239   -323       O
ATOM   1551  OE2 GLU A 195     -23.381 -10.200 -21.502  1.00 23.55           O
ANISOU 1551  OE2 GLU A 195     2926   2916   3104    -21     34   -104       O
ATOM   1552  N   PRO A 196     -22.329 -16.209 -24.341  1.00 27.78           N
ANISOU 1552  N   PRO A 196     2941   3379   4233    405   -474   -519       N
ATOM   1553  CA  PRO A 196     -22.898 -17.072 -25.371  1.00 29.26           C
ANISOU 1553  CA  PRO A 196     2952   3722   4443    801   -199   -954       C
ATOM   1554  C   PRO A 196     -23.995 -16.327 -26.122  1.00 29.61           C
ANISOU 1554  C   PRO A 196     2993   4017   4240    234   -378   -601       C
ATOM   1555  O   PRO A 196     -24.663 -15.472 -25.546  1.00 29.91           O
ANISOU 1555  O   PRO A 196     3338   4111   3915    763   -402   -287       O
ATOM   1556  CB  PRO A 196     -23.403 -18.281 -24.608  1.00 31.10           C
ANISOU 1556  CB  PRO A 196     3323   3466   5028    105    234   -991       C
ATOM   1557  CG  PRO A 196     -23.513 -17.868 -23.176  1.00 38.97           C
ANISOU 1557  CG  PRO A 196     4684   4698   5424     -6     62   -603       C
ATOM   1558  CD  PRO A 196     -22.666 -16.629 -22.979  1.00 32.63           C
ANISOU 1558  CD  PRO A 196     3661   4170   4567    549   -321   -452       C
ATOM   1559  N   PRO A 197     -24.265 -16.712 -27.384  1.00 33.96           N
ANISOU 1559  N   PRO A 197     3299   5224   4382    547   -381   -713       N
ATOM   1560  CA  PRO A 197     -25.450 -16.248 -28.089  1.00 37.75           C
ANISOU 1560  CA  PRO A 197     4166   5301   4875    688   -646   -664       C
ATOM   1561  C   PRO A 197     -26.659 -16.770 -27.325  1.00 30.94           C
ANISOU 1561  C   PRO A 197     3759   3607   4388    421  -1344   -266       C
ATOM   1562  O   PRO A 197     -26.663 -17.920 -26.865  1.00 32.79           O
ANISOU 1562  O   PRO A 197     3773   3557   5130    859   -569    193       O
ATOM   1563  CB  PRO A 197     -25.367 -16.858 -29.487  1.00 40.96           C
ANISOU 1563  CB  PRO A 197     4832   6287   4444    458   -819   -884       C
ATOM   1564  CG  PRO A 197     -23.944 -17.331 -29.611  1.00 45.12           C
ANISOU 1564  CG  PRO A 197     5201   6766   5175    890   -553   -920       C
ATOM   1565  CD  PRO A 197     -23.441 -17.628 -28.198  1.00 41.24           C
ANISOU 1565  CD  PRO A 197     4601   6157   4910    736   -541  -1187       C
ATOM   1566  N   TYR A 198     -27.704 -15.943 -27.248  1.00 29.45           N
ANISOU 1566  N   TYR A 198     3544   3570   4077    574   -773    101       N
ATOM   1567  CA  TYR A 198     -28.948 -16.393 -26.678  1.00 29.51           C
ANISOU 1567  CA  TYR A 198     3846   3549   3816    446   -677   -123       C
ATOM   1568  C   TYR A 198     -29.629 -17.312 -27.687  1.00 28.83           C
ANISOU 1568  C   TYR A 198     3331   3512   4112    492   -476   -501       C
ATOM   1569  O   TYR A 198     -29.414 -17.204 -28.895  1.00 29.48           O
ANISOU 1569  O   TYR A 198     3490   3562   4149    788   -916   -521       O
ATOM   1570  CB  TYR A 198     -29.839 -15.198 -26.366  1.00 27.44           C
ANISOU 1570  CB  TYR A 198     3821   3177   3428    348   -436    -60       C
ATOM   1571  CG  TYR A 198     -29.386 -14.317 -25.211  1.00 25.08           C
ANISOU 1571  CG  TYR A 198     3129   2911   3489    431   -417    -88       C
ATOM   1572  CD1 TYR A 198     -29.751 -14.612 -23.898  1.00 28.70           C
ANISOU 1572  CD1 TYR A 198     3389   3886   3631     -8   -218     19       C
ATOM   1573  CD2 TYR A 198     -28.600 -13.192 -25.420  1.00 28.27           C
ANISOU 1573  CD2 TYR A 198     3917   3303   3522    246   -643    368       C
ATOM   1574  CE1 TYR A 198     -29.384 -13.795 -22.837  1.00 26.80           C
ANISOU 1574  CE1 TYR A 198     3023   3542   3618    156    -42    -80       C
ATOM   1575  CE2 TYR A 198     -28.189 -12.399 -24.364  1.00 27.24           C
ANISOU 1575  CE2 TYR A 198     3670   3412   3266    -73   -368    -42       C
ATOM   1576  CZ  TYR A 198     -28.563 -12.707 -23.072  1.00 25.96           C
ANISOU 1576  CZ  TYR A 198     2770   3586   3508    -16   -309    -37       C
ATOM   1577  OH  TYR A 198     -28.219 -11.889 -22.064  1.00 26.07           O
ANISOU 1577  OH  TYR A 198     2964   3483   3459     60   -107   -258       O
ATOM   1578  N   GLU A 199     -30.528 -18.161 -27.190  1.00 34.25           N
ANISOU 1578  N   GLU A 199     3694   4002   5318    -42  -1795    282       N
ATOM   1579  CA  GLU A 199     -31.354 -18.953 -28.094  1.00 34.89           C
ANISOU 1579  CA  GLU A 199     4367   3479   5412    -45  -1880     40       C
ATOM   1580  C   GLU A 199     -32.163 -17.996 -28.947  1.00 33.23           C
ANISOU 1580  C   GLU A 199     3843   3315   5466   -164  -1399     10       C
ATOM   1581  O   GLU A 199     -32.726 -17.044 -28.432  1.00 35.15           O
ANISOU 1581  O   GLU A 199     3813   3948   5593   -224  -1125    241       O
ATOM   1582  CB  GLU A 199     -32.258 -19.890 -27.291  1.00 42.05           C
ANISOU 1582  CB  GLU A 199     4549   4234   7193   -143  -1927    482       C
ATOM   1583  CG  GLU A 199     -33.449 -20.459 -28.051  1.00 51.91           C
ANISOU 1583  CG  GLU A 199     5598   5344   8782   -786  -2455    -92       C
ATOM   1584  CD  GLU A 199     -33.357 -21.838 -28.666  1.00 62.40           C
ANISOU 1584  CD  GLU A 199     6665   6338  10705    938  -2445   -227       C
ATOM   1585  OE1 GLU A 199     -32.239 -22.406 -28.814  1.00 77.10           O
ANISOU 1585  OE1 GLU A 199     8422   8669  12203    869  -1654  -1153       O
ATOM   1586  OE2 GLU A 199     -34.463 -22.359 -28.959  1.00 68.35           O
ANISOU 1586  OE2 GLU A 199     6718   6913  12339    904  -2198    150       O
ATOM   1587  N   GLY A 200     -32.159 -18.218 -30.259  1.00 37.33           N
ANISOU 1587  N   GLY A 200     4005   4218   5959    202  -1783    263       N
ATOM   1588  CA  GLY A 200     -32.924 -17.356 -31.119  1.00 33.40           C
ANISOU 1588  CA  GLY A 200     3374   4160   5154   -512  -1453    254       C
ATOM   1589  C   GLY A 200     -32.167 -16.158 -31.636  1.00 33.38           C
ANISOU 1589  C   GLY A 200     3673   3925   5086    -64  -1265   -221       C
ATOM   1590  O   GLY A 200     -32.632 -15.514 -32.580  1.00 32.81           O
ANISOU 1590  O   GLY A 200     3632   3995   4838    525  -1055   -469       O
ATOM   1591  N   GLU A 201     -31.030 -15.858 -31.006  1.00 28.63           N
ANISOU 1591  N   GLU A 201     2916   3449   4513    325  -1007   -151       N
ATOM   1592  CA  GLU A 201     -30.256 -14.708 -31.421  1.00 30.73           C
ANISOU 1592  CA  GLU A 201     2983   3685   5008    569   -868     73       C
ATOM   1593  C   GLU A 201     -29.540 -15.049 -32.724  1.00 32.61           C
ANISOU 1593  C   GLU A 201     3244   4383   4762    469  -1106   -446       C
ATOM   1594  O   GLU A 201     -28.715 -15.970 -32.822  1.00 37.31           O
ANISOU 1594  O   GLU A 201     3947   4977   5250   1871   -909   -346       O
ATOM   1595  CB  GLU A 201     -29.350 -14.242 -30.293  1.00 33.42           C
ANISOU 1595  CB  GLU A 201     3544   4139   5013    -29   -681   -201       C
ATOM   1596  CG  GLU A 201     -28.492 -13.045 -30.659  1.00 34.44           C
ANISOU 1596  CG  GLU A 201     3657   4888   4543   -283   -708    350       C
ATOM   1597  CD  GLU A 201     -27.702 -12.546 -29.463  1.00 41.21           C
ANISOU 1597  CD  GLU A 201     5968   4890   4800   -207  -1986    120       C
ATOM   1598  OE1 GLU A 201     -27.259 -13.418 -28.671  1.00 36.39           O
ANISOU 1598  OE1 GLU A 201     4073   3932   5821    719  -1459   -366       O
ATOM   1599  OE2 GLU A 201     -27.568 -11.307 -29.265  1.00 50.62           O
ANISOU 1599  OE2 GLU A 201     7566   5427   6239     18  -1930   -538       O
ATOM   1600  N   ILE A 202     -29.844 -14.275 -33.740  1.00 30.32           N
ANISOU 1600  N   ILE A 202     3342   3490   4686    345   -977   -163       N
ATOM   1601  CA  ILE A 202     -29.256 -14.465 -35.040  1.00 37.14           C
ANISOU 1601  CA  ILE A 202     4123   4796   5191    466   -842   -181       C
ATOM   1602  C   ILE A 202     -27.985 -13.662 -34.970  1.00 41.94           C
ANISOU 1602  C   ILE A 202     4979   5606   5350     84   -206    285       C
ATOM   1603  O   ILE A 202     -26.917 -14.137 -35.372  1.00 41.09           O
ANISOU 1603  O   ILE A 202     3295   6505   5813    -42    258    662       O
ATOM   1604  CB  ILE A 202     -30.203 -13.943 -36.137  1.00 39.17           C
ANISOU 1604  CB  ILE A 202     6102   4368   4413    655  -1205   -769       C
ATOM   1605  CG1 ILE A 202     -31.402 -14.878 -36.324  1.00 41.33           C
ANISOU 1605  CG1 ILE A 202     4712   6715   4277   -178   -895   -360       C
ATOM   1606  CG2 ILE A 202     -29.413 -13.676 -37.408  1.00 49.49           C
ANISOU 1606  CG2 ILE A 202     6994   6357   5452    260   -974   -192       C
ATOM   1607  N   GLU A 203     -28.155 -12.484 -34.323  1.00 43.90           N
ANISOU 1607  N   GLU A 203     5353   5719   5607   -640   -355    483       N
ATOM   1608  CA  GLU A 203     -27.044 -11.584 -34.127  1.00 48.69           C
ANISOU 1608  CA  GLU A 203     6785   6488   5228   -911   -257   -142       C
ATOM   1609  C   GLU A 203     -27.313 -10.605 -32.994  1.00 47.77           C
ANISOU 1609  C   GLU A 203     5797   6235   6119   -971   -352   -101       C
ATOM   1610  O   GLU A 203     -28.451 -10.298 -32.620  1.00 47.57           O
ANISOU 1610  O   GLU A 203     5712   6077   6285  -1078   -765    864       O
ATOM   1611  CB  GLU A 203     -26.779 -10.764 -35.384  1.00 47.54           C
ANISOU 1611  CB  GLU A 203     6253   6867   4942   -330   -858    474       C
ATOM   1612  CG  GLU A 203     -27.791  -9.643 -35.620  1.00 41.31           C
ANISOU 1612  CG  GLU A 203     4597   5920   5179   -506   -995    225       C
ATOM   1613  CD  GLU A 203     -27.351  -8.829 -36.827  1.00 45.08           C
ANISOU 1613  CD  GLU A 203     5220   6478   5432   -160    548    706       C
ATOM   1614  OE1 GLU A 203     -26.419  -9.352 -37.545  1.00 51.96           O
ANISOU 1614  OE1 GLU A 203     6392   8177   5175    937     85    551       O
ATOM   1615  OE2 GLU A 203     -27.942  -7.730 -37.062  1.00 36.01           O
ANISOU 1615  OE2 GLU A 203     4069   5328   4287   -196    323    572       O
ATOM   1616  N   ARG A 204     -26.206 -10.047 -32.559  1.00 40.39           N
ANISOU 1616  N   ARG A 204     2689   6440   6219    156   -651   -100       N
ATOM   1617  CA  ARG A 204     -26.154  -9.006 -31.548  1.00 50.19           C
ANISOU 1617  CA  ARG A 204     5305   7299   6465   -262   -151     23       C
ATOM   1618  C   ARG A 204     -25.350  -7.855 -32.134  1.00 45.13           C
ANISOU 1618  C   ARG A 204     5191   6499   5456    -84    -68   -276       C
ATOM   1619  O   ARG A 204     -24.731  -8.007 -33.169  1.00 43.65           O
ANISOU 1619  O   ARG A 204     5217   6118   5248   -753   -893    520       O
ATOM   1620  CB  ARG A 204     -25.444  -9.448 -30.258  1.00 54.81           C
ANISOU 1620  CB  ARG A 204     6945   8508   5371   -850   -947    440       C
ATOM   1621  CG  ARG A 204     -24.061 -10.075 -30.426  1.00 59.84           C
ANISOU 1621  CG  ARG A 204     7285   8922   6531  -1292   -503    924       C
ATOM   1622  CD  ARG A 204     -23.372 -10.206 -29.084  1.00 62.30           C
ANISOU 1622  CD  ARG A 204     7152   8622   7897  -1702   -834   1981       C
ATOM   1623  NE  ARG A 204     -22.318 -11.222 -28.939  1.00 70.02           N
ANISOU 1623  NE  ARG A 204     8151   8838   9615  -1363    274   1590       N
ATOM   1624  CZ  ARG A 204     -21.129 -11.252 -29.539  1.00 67.03           C
ANISOU 1624  CZ  ARG A 204     9457   8687   7323   -711    495   1809       C
ATOM   1625  NH1 ARG A 204     -20.099 -11.839 -28.923  1.00 66.44           N
ANISOU 1625  NH1 ARG A 204     9278   8101   7867   -473    296   1504       N
ATOM   1626  NH2 ARG A 204     -20.940 -10.589 -30.671  1.00 55.37           N
ANISOU 1626  NH2 ARG A 204     9101   8221   3716  -1178   -525    519       N
ATOM   1627  N   ALA A 205     -25.322  -6.720 -31.444  1.00 45.55           N
ANISOU 1627  N   ALA A 205     4945   6672   5690   -703     17   -399       N
ATOM   1628  CA  ALA A 205     -24.465  -5.654 -31.880  1.00 39.92           C
ANISOU 1628  CA  ALA A 205     4798   6110   4258   -160  -1001   -967       C
ATOM   1629  C   ALA A 205     -23.033  -6.120 -31.660  1.00 41.55           C
ANISOU 1629  C   ALA A 205     4379   5907   5501    330   -248   -446       C
ATOM   1630  O   ALA A 205     -22.753  -6.857 -30.712  1.00 43.53           O
ANISOU 1630  O   ALA A 205     4769   6043   5728   -659    307   -130       O
ATOM   1631  CB  ALA A 205     -24.776  -4.383 -31.121  1.00 44.03           C
ANISOU 1631  CB  ALA A 205     4858   6734   5137    414  -1453  -1050       C
ATOM   1632  N   GLN A 206     -22.148  -5.682 -32.544  1.00 40.82           N
ANISOU 1632  N   GLN A 206     4724   6291   4495   -152   -515   -150       N
ATOM   1633  CA  GLN A 206     -20.720  -5.801 -32.309  1.00 34.82           C
ANISOU 1633  CA  GLN A 206     3915   4927   4389    470   -488   -271       C
ATOM   1634  C   GLN A 206     -20.462  -5.281 -30.894  1.00 35.64           C
ANISOU 1634  C   GLN A 206     4264   4328   4949   -119   -582    229       C
ATOM   1635  O   GLN A 206     -20.709  -4.116 -30.600  1.00 33.45           O
ANISOU 1635  O   GLN A 206     3620   4057   5034    225   -328     -5       O
ATOM   1636  CB  GLN A 206     -20.088  -4.932 -33.399  1.00 35.60           C
ANISOU 1636  CB  GLN A 206     4352   4847   4327    571   -898   -185       C
ATOM   1637  CG  GLN A 206     -18.659  -5.300 -33.773  1.00 37.36           C
ANISOU 1637  CG  GLN A 206     4454   4760   4979    408   -782    370       C
ATOM   1638  CD  GLN A 206     -17.754  -5.366 -32.568  1.00 38.62           C
ANISOU 1638  CD  GLN A 206     3653   5249   5774    397  -1007    149       C
ATOM   1639  OE1 GLN A 206     -17.520  -4.350 -31.918  1.00 39.67           O
ANISOU 1639  OE1 GLN A 206     4421   4580   6071    804   -145   -433       O
ATOM   1640  NE2 GLN A 206     -17.239  -6.561 -32.286  1.00 39.16           N
ANISOU 1640  NE2 GLN A 206     3347   4443   7088    649   -303    232       N
ATOM   1641  N   PRO A 207     -20.050  -6.112 -29.931  1.00 34.56           N
ANISOU 1641  N   PRO A 207     4323   4593   4216   -280   -373    623       N
ATOM   1642  CA  PRO A 207     -19.991  -5.672 -28.541  1.00 36.17           C
ANISOU 1642  CA  PRO A 207     3656   5080   5008   -486   -679   -224       C
ATOM   1643  C   PRO A 207     -19.139  -4.471 -28.186  1.00 32.19           C
ANISOU 1643  C   PRO A 207     3542   4186   4501    117    -82    -47       C
ATOM   1644  O   PRO A 207     -19.569  -3.676 -27.364  1.00 32.22           O
ANISOU 1644  O   PRO A 207     3281   3626   5335   -157    122   -550       O
ATOM   1645  CB  PRO A 207     -19.472  -6.891 -27.862  1.00 36.42           C
ANISOU 1645  CB  PRO A 207     3661   5273   4903   -544   -521    481       C
ATOM   1646  CG  PRO A 207     -19.977  -8.037 -28.680  1.00 33.78           C
ANISOU 1646  CG  PRO A 207     3070   5253   4511   -618     17     35       C
ATOM   1647  CD  PRO A 207     -19.753  -7.542 -30.102  1.00 36.52           C
ANISOU 1647  CD  PRO A 207     3757   4896   5222   -602   -564    -29       C
ATOM   1648  N   MET A 208     -17.902  -4.416 -28.699  1.00 36.07           N
ANISOU 1648  N   MET A 208     3461   4756   5487    248    392  -1060       N
ATOM   1649  CA  MET A 208     -17.058  -3.258 -28.456  1.00 33.04           C
ANISOU 1649  CA  MET A 208     3289   4690   4574    -49    379   -400       C
ATOM   1650  C   MET A 208     -17.701  -2.002 -29.055  1.00 32.89           C
ANISOU 1650  C   MET A 208     3185   4703   4610    133    364   -482       C
ATOM   1651  O   MET A 208     -17.664  -0.966 -28.424  1.00 34.95           O
ANISOU 1651  O   MET A 208     3848   4763   4667   -140    523   -364       O
ATOM   1652  CB  MET A 208     -15.653  -3.456 -29.017  1.00 34.36           C
ANISOU 1652  CB  MET A 208     3720   4449   4888     63    341   -873       C
ATOM   1653  CG  MET A 208     -14.604  -2.458 -28.617  1.00 37.52           C
ANISOU 1653  CG  MET A 208     4997   4799   4461   -301    244   -620       C
ATOM   1654  SD  MET A 208     -14.143  -2.649 -26.899  1.00 43.46           S
ANISOU 1654  SD  MET A 208     4859   6255   5397   -281     44     45       S
ATOM   1655  CE  MET A 208     -13.674  -4.365 -26.735  1.00 43.62           C
ANISOU 1655  CE  MET A 208     6521   5810   4242   -716   -801   1050       C
ATOM   1656  N   LEU A 209     -18.263  -2.076 -30.281  1.00 34.97           N
ANISOU 1656  N   LEU A 209     4263   4304   4720    848    229   -758       N
ATOM   1657  CA  LEU A 209     -18.867  -0.885 -30.878  1.00 36.16           C
ANISOU 1657  CA  LEU A 209     4191   4895   4654    483   -285   -655       C
ATOM   1658  C   LEU A 209     -20.060  -0.465 -30.013  1.00 34.99           C
ANISOU 1658  C   LEU A 209     4154   5212   3928    501    154   -427       C
ATOM   1659  O   LEU A 209     -20.268   0.716 -29.789  1.00 38.08           O
ANISOU 1659  O   LEU A 209     5202   5061   4204    514    176    205       O
ATOM   1660  CB  LEU A 209     -19.263  -0.943 -32.354  1.00 37.90           C
ANISOU 1660  CB  LEU A 209     5089   4640   4672    -99     74    -24       C
ATOM   1661  N   GLN A 210     -20.828  -1.428 -29.506  1.00 36.15           N
ANISOU 1661  N   GLN A 210     4370   4958   4408    514   -279   -560       N
ATOM   1662  CA  GLN A 210     -21.952  -1.148 -28.614  1.00 33.72           C
ANISOU 1662  CA  GLN A 210     3976   4900   3936    675   -251    366       C
ATOM   1663  C   GLN A 210     -21.480  -0.468 -27.329  1.00 30.00           C
ANISOU 1663  C   GLN A 210     3697   3785   3917    133    304    286       C
ATOM   1664  O   GLN A 210     -22.100   0.497 -26.877  1.00 30.25           O
ANISOU 1664  O   GLN A 210     3815   3737   3940    569    492    231       O
ATOM   1665  CB  GLN A 210     -22.658  -2.477 -28.363  1.00 39.56           C
ANISOU 1665  CB  GLN A 210     4082   5815   5132    601    145    345       C
ATOM   1666  CG  GLN A 210     -23.986  -2.361 -27.641  1.00 44.01           C
ANISOU 1666  CG  GLN A 210     5054   6354   5315    450    374    450       C
ATOM   1667  CD  GLN A 210     -24.748  -3.672 -27.732  1.00 51.78           C
ANISOU 1667  CD  GLN A 210     5151   7538   6986   -677   -529   -368       C
ATOM   1668  OE1 GLN A 210     -24.207  -4.763 -27.467  1.00 54.15           O
ANISOU 1668  OE1 GLN A 210     5331   7505   7736   -891  -1333    759       O
ATOM   1669  NE2 GLN A 210     -26.006  -3.570 -28.128  1.00 57.19           N
ANISOU 1669  NE2 GLN A 210     5079   9786   6866    543   -601   -606       N
ATOM   1670  N   TYR A 211     -20.419  -1.014 -26.722  1.00 28.77           N
ANISOU 1670  N   TYR A 211     3644   3335   3951     21     61    193       N
ATOM   1671  CA  TYR A 211     -19.849  -0.421 -25.516  1.00 26.40           C
ANISOU 1671  CA  TYR A 211     3158   3277   3595    -59    -29    240       C
ATOM   1672  C   TYR A 211     -19.461   1.030 -25.823  1.00 27.63           C
ANISOU 1672  C   TYR A 211     4085   3110   3303   -100    450    601       C
ATOM   1673  O   TYR A 211     -19.773   1.910 -25.071  1.00 27.30           O
ANISOU 1673  O   TYR A 211     3596   3380   3396    -75    339    257       O
ATOM   1674  CB  TYR A 211     -18.662  -1.247 -25.032  1.00 27.27           C
ANISOU 1674  CB  TYR A 211     3338   3251   3773     66     -6    589       C
ATOM   1675  CG  TYR A 211     -17.968  -0.737 -23.775  1.00 28.95           C
ANISOU 1675  CG  TYR A 211     3530   3677   3795    128   -175    130       C
ATOM   1676  CD1 TYR A 211     -18.473  -0.999 -22.509  1.00 33.69           C
ANISOU 1676  CD1 TYR A 211     3773   4602   4427   -834    275      4       C
ATOM   1677  CD2 TYR A 211     -16.788  -0.004 -23.845  1.00 34.90           C
ANISOU 1677  CD2 TYR A 211     4265   4399   4597   -198   -315    132       C
ATOM   1678  CE1 TYR A 211     -17.854  -0.544 -21.361  1.00 32.70           C
ANISOU 1678  CE1 TYR A 211     3671   4611   4143   -477   -273    -39       C
ATOM   1679  CE2 TYR A 211     -16.165   0.467 -22.691  1.00 36.15           C
ANISOU 1679  CE2 TYR A 211     4801   4572   4362    -33   -250    156       C
ATOM   1680  CZ  TYR A 211     -16.698   0.193 -21.450  1.00 33.19           C
ANISOU 1680  CZ  TYR A 211     3920   3976   4713      0    -82   -157       C
ATOM   1681  OH  TYR A 211     -16.103   0.667 -20.299  1.00 40.43           O
ANISOU 1681  OH  TYR A 211     4573   5771   5016   -219   -416    106       O
ATOM   1682  N   ASN A 212     -18.763   1.258 -26.943  1.00 31.30           N
ANISOU 1682  N   ASN A 212     4260   3602   4029    127    794    818       N
ATOM   1683  CA  ASN A 212     -18.343   2.601 -27.332  1.00 31.69           C
ANISOU 1683  CA  ASN A 212     4205   3754   4082    176    706   1252       C
ATOM   1684  C   ASN A 212     -19.555   3.525 -27.548  1.00 32.68           C
ANISOU 1684  C   ASN A 212     4532   3771   4113     17   1069    841       C
ATOM   1685  O   ASN A 212     -19.540   4.707 -27.165  1.00 34.81           O
ANISOU 1685  O   ASN A 212     4988   3862   4375   -129    593    645       O
ATOM   1686  CB  ASN A 212     -17.416   2.518 -28.539  1.00 35.83           C
ANISOU 1686  CB  ASN A 212     3910   4468   5235    316    922    955       C
ATOM   1687  CG  ASN A 212     -16.087   1.840 -28.245  1.00 33.76           C
ANISOU 1687  CG  ASN A 212     4734   4286   3807    764    494   1167       C
ATOM   1688  OD1 ASN A 212     -15.687   1.638 -27.085  1.00 35.91           O
ANISOU 1688  OD1 ASN A 212     4081   4965   4599   -351    373   1044       O
ATOM   1689  ND2 ASN A 212     -15.324   1.617 -29.302  1.00 41.14           N
ANISOU 1689  ND2 ASN A 212     5171   5341   5119    432   1022    878       N
ATOM   1690  N   GLU A 213     -20.623   2.999 -28.159  1.00 32.41           N
ANISOU 1690  N   GLU A 213     4939   4117   3257    820    680    723       N
ATOM   1691  CA  GLU A 213     -21.815   3.791 -28.378  1.00 34.50           C
ANISOU 1691  CA  GLU A 213     5042   4245   3822   1005    862    653       C
ATOM   1692  C   GLU A 213     -22.483   4.139 -27.054  1.00 29.04           C
ANISOU 1692  C   GLU A 213     4527   3110   3396    304    116    370       C
ATOM   1693  O   GLU A 213     -22.943   5.263 -26.877  1.00 30.47           O
ANISOU 1693  O   GLU A 213     4861   2972   3743    727    301    678       O
ATOM   1694  CB  GLU A 213     -22.749   3.095 -29.358  1.00 37.78           C
ANISOU 1694  CB  GLU A 213     5445   4875   4034   1108    537   -156       C
ATOM   1695  CG  GLU A 213     -22.265   3.229 -30.801  1.00 47.71           C
ANISOU 1695  CG  GLU A 213     7134   6349   4643   1465    -54    333       C
ATOM   1696  CD  GLU A 213     -21.924   4.616 -31.388  1.00 54.10           C
ANISOU 1696  CD  GLU A 213     7429   7007   6118    738    424    463       C
ATOM   1697  OE1 GLU A 213     -22.710   5.602 -31.216  1.00 52.58           O
ANISOU 1697  OE1 GLU A 213     8615   6343   5021   1268    170     61       O
ATOM   1698  OE2 GLU A 213     -20.864   4.698 -32.091  1.00 56.58           O
ANISOU 1698  OE2 GLU A 213     8338   6864   6298    715   1600    995       O
ATOM   1699  N   THR A 214     -22.489   3.195 -26.121  1.00 28.68           N
ANISOU 1699  N   THR A 214     4502   3103   3292     90    298    256       N
ATOM   1700  CA  THR A 214     -23.023   3.469 -24.807  1.00 27.64           C
ANISOU 1700  CA  THR A 214     4270   3107   3123   -201    159    706       C
ATOM   1701  C   THR A 214     -22.204   4.571 -24.132  1.00 27.67           C
ANISOU 1701  C   THR A 214     3560   3439   3514    -34    147    685       C
ATOM   1702  O   THR A 214     -22.795   5.516 -23.580  1.00 27.77           O
ANISOU 1702  O   THR A 214     3919   2943   3688    211    395    587       O
ATOM   1703  CB  THR A 214     -23.055   2.178 -24.009  1.00 24.59           C
ANISOU 1703  CB  THR A 214     3463   2741   3138    258    -65    487       C
ATOM   1704  OG1 THR A 214     -24.115   1.350 -24.503  1.00 26.16           O
ANISOU 1704  OG1 THR A 214     3045   3229   3668    -13    153    201       O
ATOM   1705  CG2 THR A 214     -23.259   2.437 -22.527  1.00 26.77           C
ANISOU 1705  CG2 THR A 214     3713   3104   3353    117      9    520       C
ATOM   1706  N   LEU A 215     -20.859   4.487 -24.244  1.00 27.60           N
ANISOU 1706  N   LEU A 215     3806   2920   3761   -373     96    555       N
ATOM   1707  CA  LEU A 215     -20.002   5.534 -23.679  1.00 29.15           C
ANISOU 1707  CA  LEU A 215     3763   3307   4005    208     11    590       C
ATOM   1708  C   LEU A 215     -20.323   6.911 -24.276  1.00 27.44           C
ANISOU 1708  C   LEU A 215     3390   3156   3877   -183    206    562       C
ATOM   1709  O   LEU A 215     -20.469   7.906 -23.559  1.00 30.03           O
ANISOU 1709  O   LEU A 215     4294   3029   4088   -117    368    625       O
ATOM   1710  CB  LEU A 215     -18.532   5.187 -23.838  1.00 31.25           C
ANISOU 1710  CB  LEU A 215     3901   3290   4683   -360    198    774       C
ATOM   1711  CG  LEU A 215     -18.022   4.038 -22.958  1.00 31.72           C
ANISOU 1711  CG  LEU A 215     3684   3237   5132    -48    180    714       C
ATOM   1712  CD1 LEU A 215     -16.530   4.069 -23.089  1.00 36.14           C
ANISOU 1712  CD1 LEU A 215     4266   3857   5610    183   -355    343       C
ATOM   1713  CD2 LEU A 215     -18.392   4.143 -21.525  1.00 34.74           C
ANISOU 1713  CD2 LEU A 215     3987   3768   5446   -203   -545    683       C
ATOM   1714  N   LYS A 216     -20.437   6.984 -25.584  1.00 30.50           N
ANISOU 1714  N   LYS A 216     4480   3164   3943    349    454    867       N
ATOM   1715  CA  LYS A 216     -20.732   8.244 -26.250  1.00 31.31           C
ANISOU 1715  CA  LYS A 216     4410   3046   4439    -96    315   1012       C
ATOM   1716  C   LYS A 216     -22.095   8.806 -25.833  1.00 32.44           C
ANISOU 1716  C   LYS A 216     4640   3418   4267   -259    400    530       C
ATOM   1717  O   LYS A 216     -22.251  10.020 -25.624  1.00 31.66           O
ANISOU 1717  O   LYS A 216     4519   3536   3976    -44    121    599       O
ATOM   1718  CB  LYS A 216     -20.638   8.028 -27.771  1.00 33.39           C
ANISOU 1718  CB  LYS A 216     4600   3732   4354    281    655   1376       C
ATOM   1719  CG  LYS A 216     -19.228   7.777 -28.291  1.00 37.18           C
ANISOU 1719  CG  LYS A 216     5224   4368   4535    177    499   1400       C
ATOM   1720  CD  LYS A 216     -19.174   7.363 -29.760  1.00 43.03           C
ANISOU 1720  CD  LYS A 216     5894   5570   4885    478    866   1499       C
ATOM   1721  CE  LYS A 216     -17.790   7.030 -30.214  1.00 51.63           C
ANISOU 1721  CE  LYS A 216     6968   7271   5379    676    612    925       C
ATOM   1722  NZ  LYS A 216     -17.738   6.698 -31.639  1.00 59.82           N
ANISOU 1722  NZ  LYS A 216     8633   8573   5523     97    958    914       N
ATOM   1723  N   ARG A 217     -23.074   7.909 -25.656  1.00 29.99           N
ANISOU 1723  N   ARG A 217     4846   2987   3562    213    258    708       N
ATOM   1724  CA  ARG A 217     -24.378   8.331 -25.210  1.00 30.43           C
ANISOU 1724  CA  ARG A 217     4603   3341   3616    288    112    939       C
ATOM   1725  C   ARG A 217     -24.281   8.962 -23.816  1.00 30.05           C
ANISOU 1725  C   ARG A 217     4110   3328   3979    141    -98    877       C
ATOM   1726  O   ARG A 217     -24.887  10.022 -23.592  1.00 31.65           O
ANISOU 1726  O   ARG A 217     4801   3109   4116    632     63    527       O
ATOM   1727  CB  ARG A 217     -25.369   7.170 -25.296  1.00 32.84           C
ANISOU 1727  CB  ARG A 217     5163   3239   4076    327   -213    748       C
ATOM   1728  CG  ARG A 217     -26.705   7.681 -24.815  1.00 35.83           C
ANISOU 1728  CG  ARG A 217     4633   4313   4667   -118    -59    625       C
ATOM   1729  CD  ARG A 217     -27.722   6.611 -24.824  1.00 41.05           C
ANISOU 1729  CD  ARG A 217     4761   4555   6281   -205    797   1101       C
ATOM   1730  NE  ARG A 217     -28.867   7.116 -24.066  1.00 39.16           N
ANISOU 1730  NE  ARG A 217     4366   4210   6303    322    754   1003       N
ATOM   1731  CZ  ARG A 217     -29.845   6.330 -23.699  1.00 34.65           C
ANISOU 1731  CZ  ARG A 217     4098   3880   5189    -14    904   1085       C
ATOM   1732  NH1 ARG A 217     -29.654   5.021 -23.773  1.00 34.03           N
ANISOU 1732  NH1 ARG A 217     5187   3587   4156    -96    124    943       N
ATOM   1733  NH2 ARG A 217     -30.958   6.893 -23.235  1.00 36.56           N
ANISOU 1733  NH2 ARG A 217     4957   3841   5093    714    742    988       N
ATOM   1734  N   LEU A 218     -23.541   8.299 -22.910  1.00 30.58           N
ANISOU 1734  N   LEU A 218     4200   3424   3993    508    294    826       N
ATOM   1735  CA  LEU A 218     -23.389   8.788 -21.547  1.00 28.41           C
ANISOU 1735  CA  LEU A 218     4097   3046   3652    145   -223    924       C
ATOM   1736  C   LEU A 218     -22.703  10.144 -21.555  1.00 28.57           C
ANISOU 1736  C   LEU A 218     4068   3183   3605    -42     41    775       C
ATOM   1737  O   LEU A 218     -23.080  11.019 -20.784  1.00 30.65           O
ANISOU 1737  O   LEU A 218     4152   3055   4437    282    446    553       O
ATOM   1738  CB  LEU A 218     -22.624   7.792 -20.686  1.00 30.35           C
ANISOU 1738  CB  LEU A 218     4730   3037   3764    298    122    787       C
ATOM   1739  CG  LEU A 218     -23.362   6.474 -20.430  1.00 30.64           C
ANISOU 1739  CG  LEU A 218     4842   2827   3973    261    772    648       C
ATOM   1740  CD1 LEU A 218     -22.461   5.537 -19.664  1.00 36.32           C
ANISOU 1740  CD1 LEU A 218     5870   3343   4587    566    801   1076       C
ATOM   1741  CD2 LEU A 218     -24.678   6.665 -19.733  1.00 33.00           C
ANISOU 1741  CD2 LEU A 218     5357   3311   3869    160    911    333       C
ATOM   1742  N   ALA A 219     -21.736  10.306 -22.456  1.00 30.18           N
ANISOU 1742  N   ALA A 219     4362   2825   4280   -260    353    900       N
ATOM   1743  CA  ALA A 219     -20.979  11.562 -22.549  1.00 34.34           C
ANISOU 1743  CA  ALA A 219     4869   2980   5199   -352    147    904       C
ATOM   1744  C   ALA A 219     -21.838  12.736 -22.991  1.00 34.80           C
ANISOU 1744  C   ALA A 219     5404   3241   4577     74    411    948       C
ATOM   1745  O   ALA A 219     -21.518  13.904 -22.700  1.00 37.21           O
ANISOU 1745  O   ALA A 219     5102   2948   6088    193    -11   1158       O
ATOM   1746  CB  ALA A 219     -19.775  11.418 -23.456  1.00 34.40           C
ANISOU 1746  CB  ALA A 219     5002   2954   5112   -283    296    846       C
ATOM   1747  N   ARG A 220     -22.877  12.418 -23.752  1.00 33.85           N
ANISOU 1747  N   ARG A 220     5276   3321   4264     86    178    391       N
ATOM   1748  CA  ARG A 220     -23.820  13.403 -24.280  1.00 36.60           C
ANISOU 1748  CA  ARG A 220     5863   3486   4557    591    127   1094       C
ATOM   1749  C   ARG A 220     -24.948  13.745 -23.296  1.00 36.44           C
ANISOU 1749  C   ARG A 220     5670   3556   4618    656   -284    850       C
ATOM   1750  O   ARG A 220     -25.700  14.731 -23.492  1.00 43.04           O
ANISOU 1750  O   ARG A 220     6082   4891   5381   1246    773    550       O
ATOM   1751  CB  ARG A 220     -24.398  12.903 -25.617  1.00 37.77           C
ANISOU 1751  CB  ARG A 220     6650   3279   4423   1335     12   1095       C
ATOM   1752  CG  ARG A 220     -23.409  12.875 -26.772  1.00 45.49           C
ANISOU 1752  CG  ARG A 220     7201   5180   4901   1539    -95    952       C
ATOM   1753  CD  ARG A 220     -24.087  12.491 -28.107  1.00 48.47           C
ANISOU 1753  CD  ARG A 220     7979   5264   5172   1344   -410    558       C
ATOM   1754  NE  ARG A 220     -24.924  11.280 -28.022  1.00 58.04           N
ANISOU 1754  NE  ARG A 220     9647   6092   6312   1187   -154    527       N
ATOM   1755  CZ  ARG A 220     -24.659  10.082 -28.551  1.00 52.77           C
ANISOU 1755  CZ  ARG A 220     9175   6254   4622    911   -885    829       C
ATOM   1756  NH1 ARG A 220     -23.484   9.850 -29.090  1.00 57.43           N
ANISOU 1756  NH1 ARG A 220     8065   7250   6506   1953  -1856    709       N
ATOM   1757  NH2 ARG A 220     -25.569   9.122 -28.544  1.00 55.12           N
ANISOU 1757  NH2 ARG A 220    10585   5722   4635    -97   -626   1647       N
ATOM   1758  N   MET A 221     -25.117  12.886 -22.278  1.00 34.76           N
ANISOU 1758  N   MET A 221     4892   3706   4608    342    140    457       N
ATOM   1759  CA AMET A 221     -26.140  13.089 -21.282  0.50 35.65           C
ANISOU 1759  CA AMET A 221     5402   3827   4316    587    -89    635       C
ATOM   1760  CA BMET A 221     -26.129  13.060 -21.260  0.50 36.76           C
ANISOU 1760  CA BMET A 221     5651   3878   4438    425   -338    569       C
ATOM   1761  C   MET A 221     -25.653  14.164 -20.310  1.00 38.13           C
ANISOU 1761  C   MET A 221     6154   3876   4456    894   -110    668       C
ATOM   1762  O   MET A 221     -24.468  14.470 -20.178  1.00 42.01           O
ANISOU 1762  O   MET A 221     7092   4154   4715   -773   -321    630       O
ATOM   1763  CB AMET A 221     -26.443  11.767 -20.573  0.50 34.99           C
ANISOU 1763  CB AMET A 221     4744   3968   4584    640    700    346       C
ATOM   1764  CB BMET A 221     -26.359  11.731 -20.519  0.50 38.31           C
ANISOU 1764  CB BMET A 221     5614   3960   4984    142   -148    226       C
ATOM   1765  CG AMET A 221     -27.094  10.761 -21.475  0.50 34.08           C
ANISOU 1765  CG AMET A 221     4444   3817   4688   1115    916    297       C
ATOM   1766  CG BMET A 221     -27.791  11.225 -20.547  0.50 41.55           C
ANISOU 1766  CG BMET A 221     5920   4269   5600     61   -820    206       C
ATOM   1767  SD AMET A 221     -27.568   9.230 -20.658  0.50 38.08           S
ANISOU 1767  SD AMET A 221     5344   3754   5373   1040    967    579       S
ATOM   1768  SD BMET A 221     -28.024   9.528 -19.985  0.50 41.26           S
ANISOU 1768  SD BMET A 221     5397   3930   6348    186   -704    206       S
ATOM   1769  CE AMET A 221     -28.589   9.778 -19.293  0.50 34.56           C
ANISOU 1769  CE AMET A 221     4383   4502   4246    698   1252   1423       C
ATOM   1770  CE BMET A 221     -27.395   8.647 -21.417  0.50 46.16           C
ANISOU 1770  CE BMET A 221     6877   4175   6487   -108    -47    214       C
ATOM   1771  N   ASN A 222     -26.565  14.733 -19.593  1.00 42.03           N
ANISOU 1771  N   ASN A 222     6766   4918   4284   1494   -466    238       N
ATOM   1772  CA  ASN A 222     -26.137  15.736 -18.642  1.00 43.29           C
ANISOU 1772  CA  ASN A 222     7435   4237   4775    462    -22    391       C
ATOM   1773  C   ASN A 222     -25.906  15.029 -17.314  1.00 39.27           C
ANISOU 1773  C   ASN A 222     5875   4595   4451    688   -267    654       C
ATOM   1774  O   ASN A 222     -26.830  14.950 -16.526  1.00 43.43           O
ANISOU 1774  O   ASN A 222     6891   4490   5120   2066    -75   -557       O
ATOM   1775  CB  ASN A 222     -27.186  16.829 -18.577  1.00 49.45           C
ANISOU 1775  CB  ASN A 222     8256   4560   5972   1225    120    512       C
ATOM   1776  CG  ASN A 222     -26.700  17.946 -17.695  1.00 64.37           C
ANISOU 1776  CG  ASN A 222     9871   5851   8733    241    937   -901       C
ATOM   1777  OD1 ASN A 222     -27.494  18.594 -16.996  1.00 76.45           O
ANISOU 1777  OD1 ASN A 222    11535   8617   8896    385   2451   -751       O
ATOM   1778  ND2 ASN A 222     -25.394  18.187 -17.736  1.00 73.12           N
ANISOU 1778  ND2 ASN A 222     9948   7199  10634    238    943   -923       N
ATOM   1779  N   ILE A 223     -24.757  14.359 -17.143  1.00 35.06           N
ANISOU 1779  N   ILE A 223     5098   3560   4663   -128   -352    784       N
ATOM   1780  CA  ILE A 223     -24.548  13.595 -15.915  1.00 29.51           C
ANISOU 1780  CA  ILE A 223     4084   3144   3983     34    402    631       C
ATOM   1781  C   ILE A 223     -23.611  14.352 -14.976  1.00 31.01           C
ANISOU 1781  C   ILE A 223     4073   2943   4767    124    408    446       C
ATOM   1782  O   ILE A 223     -22.493  14.727 -15.357  1.00 35.93           O
ANISOU 1782  O   ILE A 223     4331   3815   5507   -567    566    450       O
ATOM   1783  CB  ILE A 223     -24.023  12.176 -16.235  1.00 30.77           C
ANISOU 1783  CB  ILE A 223     4175   3248   4267    -14    387    415       C
ATOM   1784  CG1 ILE A 223     -25.061  11.328 -16.997  1.00 28.95           C
ANISOU 1784  CG1 ILE A 223     4118   3051   3832    416    -54    454       C
ATOM   1785  CG2 ILE A 223     -23.562  11.458 -14.974  1.00 30.09           C
ANISOU 1785  CG2 ILE A 223     4469   2694   4269    -26    230    498       C
ATOM   1786  CD1 ILE A 223     -24.460  10.104 -17.654  1.00 31.67           C
ANISOU 1786  CD1 ILE A 223     4230   3265   4540    -59    124    368       C
ATOM   1787  N   SER A 224     -24.096  14.598 -13.768  1.00 30.47           N
ANISOU 1787  N   SER A 224     4450   2570   4558    201   -381    235       N
ATOM   1788  CA  SER A 224     -23.335  15.238 -12.709  1.00 33.96           C
ANISOU 1788  CA  SER A 224     4544   3013   5347   -263   -408    -60       C
ATOM   1789  C   SER A 224     -22.367  14.292 -12.012  1.00 32.53           C
ANISOU 1789  C   SER A 224     4172   2912   5275   -524   -355    215       C
ATOM   1790  O   SER A 224     -21.309  14.738 -11.616  1.00 40.37           O
ANISOU 1790  O   SER A 224     4498   3127   7713   -508  -1206    449       O
ATOM   1791  CB  SER A 224     -24.236  15.867 -11.695  1.00 33.95           C
ANISOU 1791  CB  SER A 224     4667   3328   4904     98   -453   -100       C
ATOM   1792  OG  SER A 224     -25.176  14.968 -11.130  1.00 33.77           O
ANISOU 1792  OG  SER A 224     5032   3197   4601     16   -299     30       O
ATOM   1793  N   ARG A 225     -22.795  13.053 -11.778  1.00 31.56           N
ANISOU 1793  N   ARG A 225     4165   2456   5370   -445   -555    237       N
ATOM   1794  CA  ARG A 225     -22.059  12.117 -10.954  1.00 30.46           C
ANISOU 1794  CA  ARG A 225     4540   2288   4746   -102   -211    -51       C
ATOM   1795  C   ARG A 225     -22.537  10.726 -11.328  1.00 30.51           C
ANISOU 1795  C   ARG A 225     4105   2672   4815   -530   -474    213       C
ATOM   1796  O   ARG A 225     -23.768  10.519 -11.392  1.00 29.47           O
ANISOU 1796  O   ARG A 225     3972   2657   4568     37   -362    -45       O
ATOM   1797  CB  ARG A 225     -22.322  12.428  -9.486  1.00 34.82           C
ANISOU 1797  CB  ARG A 225     5089   2687   5453   -930   -476   -494       C
ATOM   1798  CG  ARG A 225     -21.820  11.509  -8.406  1.00 38.14           C
ANISOU 1798  CG  ARG A 225     5325   3414   5750   -200     -4   -127       C
ATOM   1799  CD  ARG A 225     -22.362  12.048  -7.076  1.00 40.82           C
ANISOU 1799  CD  ARG A 225     6185   4173   5153   -591   -426   -204       C
ATOM   1800  NE  ARG A 225     -21.769  11.331  -5.961  1.00 45.18           N
ANISOU 1800  NE  ARG A 225     6535   4089   6541   -326   -481      2       N
ATOM   1801  CZ  ARG A 225     -22.206  11.368  -4.716  1.00 48.46           C
ANISOU 1801  CZ  ARG A 225     7179   4478   6757    192    706   -484       C
ATOM   1802  NH1 ARG A 225     -21.601  10.586  -3.806  1.00 47.99           N
ANISOU 1802  NH1 ARG A 225     6883   5078   6271   -334    425  -1198       N
ATOM   1803  NH2 ARG A 225     -23.237  12.165  -4.397  1.00 53.07           N
ANISOU 1803  NH2 ARG A 225     6939   4791   8433    -35   -331    148       N
ATOM   1804  N   VAL A 226     -21.588   9.819 -11.602  1.00 28.09           N
ANISOU 1804  N   VAL A 226     3740   2715   4220   -616   -440    -14       N
ATOM   1805  CA  VAL A 226     -21.934   8.412 -11.764  1.00 25.94           C
ANISOU 1805  CA  VAL A 226     3865   2682   3308   -536   -336    113       C
ATOM   1806  C   VAL A 226     -21.617   7.688 -10.464  1.00 25.44           C
ANISOU 1806  C   VAL A 226     3274   2656   3737     34   -362    179       C
ATOM   1807  O   VAL A 226     -20.477   7.743 -10.015  1.00 28.03           O
ANISOU 1807  O   VAL A 226     3731   2992   3926   -242   -214     72       O
ATOM   1808  CB  VAL A 226     -21.159   7.753 -12.920  1.00 27.83           C
ANISOU 1808  CB  VAL A 226     3926   3035   3614   -288     35     14       C
ATOM   1809  CG1 VAL A 226     -21.499   6.268 -13.036  1.00 29.57           C
ANISOU 1809  CG1 VAL A 226     4600   3165   3472   -633    -22     45       C
ATOM   1810  CG2 VAL A 226     -21.320   8.491 -14.260  1.00 27.76           C
ANISOU 1810  CG2 VAL A 226     4338   2995   3216    -19    -31     16       C
ATOM   1811  N   LEU A 227     -22.610   7.029  -9.883  1.00 24.51           N
ANISOU 1811  N   LEU A 227     3343   2667   3302   -122   -377    122       N
ATOM   1812  CA  LEU A 227     -22.422   6.098  -8.784  1.00 24.65           C
ANISOU 1812  CA  LEU A 227     3378   2661   3328    -21   -557    129       C
ATOM   1813  C   LEU A 227     -22.133   4.732  -9.397  1.00 24.83           C
ANISOU 1813  C   LEU A 227     3520   2795   3119   -269   -282    152       C
ATOM   1814  O   LEU A 227     -23.041   4.132  -9.967  1.00 24.80           O
ANISOU 1814  O   LEU A 227     3231   2815   3378     75   -237    237       O
ATOM   1815  CB  LEU A 227     -23.669   6.047  -7.902  1.00 26.12           C
ANISOU 1815  CB  LEU A 227     3860   2777   3289   -256   -319    -95       C
ATOM   1816  CG  LEU A 227     -24.209   7.395  -7.412  1.00 29.41           C
ANISOU 1816  CG  LEU A 227     4011   3548   3616   -156     41   -208       C
ATOM   1817  CD1 LEU A 227     -25.449   7.178  -6.600  1.00 28.93           C
ANISOU 1817  CD1 LEU A 227     3890   3181   3922    445    327   -682       C
ATOM   1818  CD2 LEU A 227     -23.177   8.093  -6.658  1.00 32.22           C
ANISOU 1818  CD2 LEU A 227     4135   3648   4458   -257    143   -724       C
ATOM   1819  N   SER A 228     -20.875   4.308  -9.368  1.00 24.70           N
ANISOU 1819  N   SER A 228     3313   2623   3448    -13   -127    169       N
ATOM   1820  CA  SER A 228     -20.432   3.179 -10.162  1.00 24.98           C
ANISOU 1820  CA  SER A 228     3034   2699   3760    -93    232    258       C
ATOM   1821  C   SER A 228     -20.561   1.871  -9.392  1.00 23.30           C
ANISOU 1821  C   SER A 228     2859   2508   3485   -225    -15    159       C
ATOM   1822  O   SER A 228     -20.629   1.844  -8.152  1.00 24.57           O
ANISOU 1822  O   SER A 228     3387   2718   3231   -201     31     25       O
ATOM   1823  CB  SER A 228     -19.005   3.348 -10.558  1.00 30.51           C
ANISOU 1823  CB  SER A 228     3796   2658   5138   -273    964    480       C
ATOM   1824  OG  SER A 228     -18.612   2.381 -11.509  1.00 37.26           O
ANISOU 1824  OG  SER A 228     4844   3670   5643     78    934    182       O
ATOM   1825  N   GLY A 229     -20.615   0.775 -10.152  1.00 23.35           N
ANISOU 1825  N   GLY A 229     3159   2684   3030     55    -65   -125       N
ATOM   1826  CA  GLY A 229     -20.664  -0.547  -9.554  1.00 22.77           C
ANISOU 1826  CA  GLY A 229     2984   2159   3506   -272    -21    134       C
ATOM   1827  C   GLY A 229     -19.394  -0.910  -8.799  1.00 22.78           C
ANISOU 1827  C   GLY A 229     3053   2536   3067   -543      8     13       C
ATOM   1828  O   GLY A 229     -19.431  -1.765  -7.938  1.00 23.67           O
ANISOU 1828  O   GLY A 229     3188   2864   2942   -436   -115    216       O
ATOM   1829  N   HIS A 230     -18.268  -0.262  -9.168  1.00 23.08           N
ANISOU 1829  N   HIS A 230     2888   2810   3073     22   -386    336       N
ATOM   1830  CA  HIS A 230     -17.008  -0.510  -8.512  1.00 22.53           C
ANISOU 1830  CA  HIS A 230     2668   2494   3400   -653   -313    271       C
ATOM   1831  C   HIS A 230     -16.221   0.784  -8.399  1.00 25.80           C
ANISOU 1831  C   HIS A 230     3127   2927   3749   -550   -437     -6       C
ATOM   1832  O   HIS A 230     -16.204   1.577  -9.311  1.00 27.68           O
ANISOU 1832  O   HIS A 230     3622   2997   3900   -479   -555     20       O
ATOM   1833  CB  HIS A 230     -16.187  -1.546  -9.266  1.00 22.77           C
ANISOU 1833  CB  HIS A 230     2584   2889   3179   -103   -277    502       C
ATOM   1834  CG  HIS A 230     -16.883  -2.836  -9.482  1.00 22.73           C
ANISOU 1834  CG  HIS A 230     2531   2658   3448   -315   -187    386       C
ATOM   1835  ND1 HIS A 230     -16.974  -3.809  -8.506  1.00 22.27           N
ANISOU 1835  ND1 HIS A 230     2782   2585   3095   -467   -436    273       N
ATOM   1836  CD2 HIS A 230     -17.578  -3.282 -10.535  1.00 23.21           C
ANISOU 1836  CD2 HIS A 230     2741   2860   3216   -112   -203    536       C
ATOM   1837  CE1 HIS A 230     -17.727  -4.819  -8.995  1.00 20.48           C
ANISOU 1837  CE1 HIS A 230     2823   2454   2502   -591   -434     52       C
ATOM   1838  NE2 HIS A 230     -18.123  -4.481 -10.209  1.00 21.78           N
ANISOU 1838  NE2 HIS A 230     2690   2425   3159   -688   -178     37       N
ATOM   1839  N   GLY A 231     -15.577   0.967  -7.252  1.00 29.68           N
ANISOU 1839  N   GLY A 231     4153   2718   4405   -751  -1239    108       N
ATOM   1840  CA  GLY A 231     -14.693   2.109  -7.112  1.00 29.68           C
ANISOU 1840  CA  GLY A 231     4018   3148   4112   -713  -1377    277       C
ATOM   1841  C   GLY A 231     -15.399   3.438  -6.843  1.00 29.50           C
ANISOU 1841  C   GLY A 231     3825   3191   4192   -702   -787   -228       C
ATOM   1842  O   GLY A 231     -16.562   3.482  -6.455  1.00 29.00           O
ANISOU 1842  O   GLY A 231     3577   3331   4111   -773   -607    -19       O
ATOM   1843  N   GLU A 232     -14.658   4.534  -7.083  1.00 29.65           N
ANISOU 1843  N   GLU A 232     3834   3273   4158   -752   -928    314       N
ATOM   1844  CA  GLU A 232     -15.161   5.836  -6.678  1.00 29.19           C
ANISOU 1844  CA  GLU A 232     3691   3135   4264   -665   -736    253       C
ATOM   1845  C   GLU A 232     -16.100   6.406  -7.736  1.00 27.23           C
ANISOU 1845  C   GLU A 232     3415   2987   3943   -777   -186    311       C
ATOM   1846  O   GLU A 232     -16.129   5.963  -8.887  1.00 30.17           O
ANISOU 1846  O   GLU A 232     4264   3426   3774   -176   -340    140       O
ATOM   1847  CB  GLU A 232     -13.994   6.782  -6.416  1.00 34.61           C
ANISOU 1847  CB  GLU A 232     4791   3068   5290  -1091   -910     16       C
ATOM   1848  CG  GLU A 232     -13.120   6.356  -5.231  1.00 40.81           C
ANISOU 1848  CG  GLU A 232     5110   3975   6421   -981  -1781    183       C
ATOM   1849  CD  GLU A 232     -13.921   6.048  -3.964  1.00 49.83           C
ANISOU 1849  CD  GLU A 232     7431   4892   6612     61  -1351    -51       C
ATOM   1850  OE1 GLU A 232     -14.563   6.977  -3.439  1.00 54.89           O
ANISOU 1850  OE1 GLU A 232     7445   6994   6418    642  -2021  -1075       O
ATOM   1851  OE2 GLU A 232     -13.990   4.878  -3.534  1.00 61.54           O
ANISOU 1851  OE2 GLU A 232     8424   6447   8513    328  -2250   1338       O
ATOM   1852  N   ASP A 233     -16.873   7.411  -7.319  1.00 30.02           N
ANISOU 1852  N   ASP A 233     4053   3245   4107   -275   -300    -37       N
ATOM   1853  CA  ASP A 233     -17.792   8.047  -8.249  1.00 28.11           C
ANISOU 1853  CA  ASP A 233     3844   2739   4098   -626   -492     33       C
ATOM   1854  C   ASP A 233     -16.996   8.624  -9.423  1.00 29.50           C
ANISOU 1854  C   ASP A 233     3786   3262   4161   -842   -476    124       C
ATOM   1855  O   ASP A 233     -15.869   9.089  -9.205  1.00 31.63           O
ANISOU 1855  O   ASP A 233     3919   3656   4442   -961   -497    461       O
ATOM   1856  CB  ASP A 233     -18.572   9.146  -7.544  1.00 30.61           C
ANISOU 1856  CB  ASP A 233     4183   3245   4201   -188   -281   -369       C
ATOM   1857  CG  ASP A 233     -19.467   8.727  -6.399  1.00 32.26           C
ANISOU 1857  CG  ASP A 233     3990   4236   4032    -25   -628   -466       C
ATOM   1858  OD1 ASP A 233     -19.665   7.509  -6.223  1.00 34.11           O
ANISOU 1858  OD1 ASP A 233     4474   3973   4511   -436   -283     11       O
ATOM   1859  OD2 ASP A 233     -19.904   9.658  -5.663  1.00 35.39           O
ANISOU 1859  OD2 ASP A 233     4544   4110   4792   -322     18   -868       O
ATOM   1860  N   VAL A 234     -17.667   8.746 -10.588  1.00 29.56           N
ANISOU 1860  N   VAL A 234     3988   2960   4284   -815   -631    414       N
ATOM   1861  CA  VAL A 234     -17.150   9.425 -11.761  1.00 30.09           C
ANISOU 1861  CA  VAL A 234     3981   3002   4451   -381   -240    344       C
ATOM   1862  C   VAL A 234     -17.818  10.806 -11.876  1.00 30.44           C
ANISOU 1862  C   VAL A 234     4085   3068   4412   -185   -900   -231       C
ATOM   1863  O   VAL A 234     -19.020  10.901 -11.981  1.00 30.72           O
ANISOU 1863  O   VAL A 234     4066   3047   4558   -621   -303    105       O
ATOM   1864  CB  VAL A 234     -17.342   8.588 -13.034  1.00 31.87           C
ANISOU 1864  CB  VAL A 234     4424   3340   4345   -191   -459    451       C
ATOM   1865  CG1 VAL A 234     -16.825   9.311 -14.256  1.00 34.65           C
ANISOU 1865  CG1 VAL A 234     4939   3534   4693   -389    -13    833       C
ATOM   1866  CG2 VAL A 234     -16.640   7.255 -12.964  1.00 31.83           C
ANISOU 1866  CG2 VAL A 234     4149   3433   4511   -413    -59    519       C
ATOM   1867  N   LEU A 235     -17.016  11.874 -11.742  1.00 32.96           N
ANISOU 1867  N   LEU A 235     4644   3372   4507   -831   -265   -235       N
ATOM   1868  CA  LEU A 235     -17.539  13.239 -11.839  1.00 34.97           C
ANISOU 1868  CA  LEU A 235     5165   3515   4607   -488    -38     24       C
ATOM   1869  C   LEU A 235     -17.328  13.819 -13.240  1.00 33.65           C
ANISOU 1869  C   LEU A 235     4470   3760   4554   -338     52    341       C
ATOM   1870  O   LEU A 235     -18.064  14.707 -13.647  1.00 41.53           O
ANISOU 1870  O   LEU A 235     5848   3862   6071     28    690    680       O
ATOM   1871  CB  LEU A 235     -16.970  14.179 -10.770  1.00 39.10           C
ANISOU 1871  CB  LEU A 235     5720   4153   4983   -531    241   -426       C
ATOM   1872  CG  LEU A 235     -17.162  13.745  -9.313  1.00 43.29           C
ANISOU 1872  CG  LEU A 235     6389   4959   5100  -1123    290   -900       C
ATOM   1873  CD1 LEU A 235     -16.756  14.800  -8.310  1.00 50.65           C
ANISOU 1873  CD1 LEU A 235     7669   5490   6087  -1373   -161   -815       C
ATOM   1874  CD2 LEU A 235     -18.586  13.362  -9.101  1.00 47.59           C
ANISOU 1874  CD2 LEU A 235     7091   5207   5783  -1040    647   -403       C
ATOM   1875  N   ASP A 236     -16.345  13.327 -13.994  1.00 33.33           N
ANISOU 1875  N   ASP A 236     4908   3371   4385   -689    429    239       N
ATOM   1876  CA  ASP A 236     -16.087  13.860 -15.326  1.00 35.12           C
ANISOU 1876  CA  ASP A 236     5193   3692   4460   -624    481    154       C
ATOM   1877  C   ASP A 236     -16.269  12.767 -16.369  1.00 31.21           C
ANISOU 1877  C   ASP A 236     4418   3191   4248   -849    366    263       C
ATOM   1878  O   ASP A 236     -15.304  12.164 -16.816  1.00 33.75           O
ANISOU 1878  O   ASP A 236     4344   3328   5152   -433    501     35       O
ATOM   1879  CB  ASP A 236     -14.712  14.506 -15.409  1.00 39.22           C
ANISOU 1879  CB  ASP A 236     5558   4075   5269  -1132    638   -101       C
ATOM   1880  CG  ASP A 236     -14.279  15.012 -16.774  1.00 40.30           C
ANISOU 1880  CG  ASP A 236     4923   4858   5531  -1279    384    267       C
ATOM   1881  OD1 ASP A 236     -15.165  15.251 -17.644  1.00 40.83           O
ANISOU 1881  OD1 ASP A 236     6129   3651   5733   -890     99    104       O
ATOM   1882  OD2 ASP A 236     -13.051  15.220 -16.946  1.00 47.49           O
ANISOU 1882  OD2 ASP A 236     5175   6038   6829  -2333   1131    833       O
ATOM   1883  N   VAL A 237     -17.529  12.562 -16.776  1.00 33.26           N
ANISOU 1883  N   VAL A 237     4619   3729   4289   -265    399    511       N
ATOM   1884  CA  VAL A 237     -17.878  11.486 -17.688  1.00 31.14           C
ANISOU 1884  CA  VAL A 237     4593   3012   4228   -329    318    413       C
ATOM   1885  C   VAL A 237     -17.275  11.748 -19.062  1.00 31.84           C
ANISOU 1885  C   VAL A 237     4507   3236   4356   -184    564    849       C
ATOM   1886  O   VAL A 237     -16.752  10.838 -19.693  1.00 34.46           O
ANISOU 1886  O   VAL A 237     4209   3888   4998   -121    690    498       O
ATOM   1887  CB  VAL A 237     -19.403  11.365 -17.789  1.00 30.98           C
ANISOU 1887  CB  VAL A 237     4059   3512   4200    363    663    916       C
ATOM   1888  CG1 VAL A 237     -19.850  10.454 -18.938  1.00 34.58           C
ANISOU 1888  CG1 VAL A 237     5054   3648   4438    -19    353    937       C
ATOM   1889  CG2 VAL A 237     -19.997  10.947 -16.446  1.00 33.22           C
ANISOU 1889  CG2 VAL A 237     4167   3875   4580    354    490   1048       C
ATOM   1890  N   VAL A 238     -17.390  12.988 -19.557  1.00 33.41           N
ANISOU 1890  N   VAL A 238     4493   3688   4513   -324    254    990       N
ATOM   1891  CA  VAL A 238     -16.849  13.296 -20.874  1.00 35.15           C
ANISOU 1891  CA  VAL A 238     4818   3853   4682   -529    344   1019       C
ATOM   1892  C   VAL A 238     -15.354  12.979 -20.935  1.00 34.53           C
ANISOU 1892  C   VAL A 238     4769   3630   4719   -992     77    668       C
ATOM   1893  O   VAL A 238     -14.876  12.328 -21.877  1.00 36.79           O
ANISOU 1893  O   VAL A 238     5046   3713   5219   -462   1056    570       O
ATOM   1894  CB  VAL A 238     -17.135  14.754 -21.252  1.00 38.19           C
ANISOU 1894  CB  VAL A 238     4982   3809   5718   -786    305   1070       C
ATOM   1895  CG1 VAL A 238     -16.303  15.156 -22.449  1.00 41.74           C
ANISOU 1895  CG1 VAL A 238     6051   4526   5283   -426    168   1579       C
ATOM   1896  CG2 VAL A 238     -18.598  15.051 -21.461  1.00 39.10           C
ANISOU 1896  CG2 VAL A 238     5863   3332   5660   -790    134    663       C
ATOM   1897  N   GLY A 239     -14.617  13.431 -19.909  1.00 35.20           N
ANISOU 1897  N   GLY A 239     4665   3844   4867   -902    265    327       N
ATOM   1898  CA  GLY A 239     -13.179  13.198 -19.834  1.00 39.03           C
ANISOU 1898  CA  GLY A 239     5034   4707   5089   -988    395     33       C
ATOM   1899  C   GLY A 239     -12.823  11.713 -19.812  1.00 35.87           C
ANISOU 1899  C   GLY A 239     4703   4521   4403  -1089    298    388       C
ATOM   1900  O   GLY A 239     -11.902  11.276 -20.509  1.00 39.34           O
ANISOU 1900  O   GLY A 239     4332   5577   5038  -1015    642    -77       O
ATOM   1901  N   LEU A 240     -13.582  10.953 -19.001  1.00 37.83           N
ANISOU 1901  N   LEU A 240     5615   4061   4697  -1254    481    905       N
ATOM   1902  CA  LEU A 240     -13.305   9.541 -18.818  1.00 38.18           C
ANISOU 1902  CA  LEU A 240     5324   4349   4834    -30    603    572       C
ATOM   1903  C   LEU A 240     -13.601   8.801 -20.117  1.00 32.35           C
ANISOU 1903  C   LEU A 240     3953   3714   4623    -70     44    394       C
ATOM   1904  O   LEU A 240     -12.807   7.980 -20.576  1.00 35.77           O
ANISOU 1904  O   LEU A 240     4508   4254   4828    522    588    179       O
ATOM   1905  CB  LEU A 240     -14.096   8.971 -17.646  1.00 37.69           C
ANISOU 1905  CB  LEU A 240     5237   3609   5474    -30    802    875       C
ATOM   1906  CG  LEU A 240     -13.716   7.530 -17.329  1.00 40.24           C
ANISOU 1906  CG  LEU A 240     5771   4281   5237    720    841    774       C
ATOM   1907  CD1 LEU A 240     -12.193   7.409 -17.188  1.00 47.42           C
ANISOU 1907  CD1 LEU A 240     6384   5805   5827    689    398    165       C
ATOM   1908  CD2 LEU A 240     -14.430   7.045 -16.103  1.00 40.26           C
ANISOU 1908  CD2 LEU A 240     6571   4009   4717    813   1244    422       C
ATOM   1909  N   VAL A 241     -14.728   9.144 -20.743  1.00 32.85           N
ANISOU 1909  N   VAL A 241     3914   3777   4790   -101    371    539       N
ATOM   1910  CA  VAL A 241     -15.090   8.504 -21.991  1.00 31.81           C
ANISOU 1910  CA  VAL A 241     4112   3496   4476   -636    330    695       C
ATOM   1911  C   VAL A 241     -14.015   8.761 -23.048  1.00 33.04           C
ANISOU 1911  C   VAL A 241     3739   4058   4755   -405    427    676       C
ATOM   1912  O   VAL A 241     -13.632   7.861 -23.777  1.00 36.22           O
ANISOU 1912  O   VAL A 241     4131   4185   5447    273    936    531       O
ATOM   1913  CB  VAL A 241     -16.477   8.975 -22.449  1.00 30.72           C
ANISOU 1913  CB  VAL A 241     3717   3308   4649   -620    337    490       C
ATOM   1914  CG1 VAL A 241     -16.720   8.645 -23.907  1.00 30.68           C
ANISOU 1914  CG1 VAL A 241     3751   3348   4559   -468    468    326       C
ATOM   1915  CG2 VAL A 241     -17.556   8.372 -21.573  1.00 30.35           C
ANISOU 1915  CG2 VAL A 241     3674   3497   4362   -410    287    478       C
ATOM   1916  N   ASN A 242     -13.598  10.011 -23.198  1.00 35.34           N
ANISOU 1916  N   ASN A 242     4229   3831   5369   -587   1077    775       N
ATOM   1917  CA  ASN A 242     -12.592  10.341 -24.203  1.00 35.75           C
ANISOU 1917  CA  ASN A 242     4378   4011   5196   -706   1238    416       C
ATOM   1918  C   ASN A 242     -11.327   9.509 -24.009  1.00 36.67           C
ANISOU 1918  C   ASN A 242     4186   4732   5015  -1124    604    453       C
ATOM   1919  O   ASN A 242     -10.770   8.976 -24.984  1.00 40.80           O
ANISOU 1919  O   ASN A 242     4999   5315   5189   -681   1121    482       O
ATOM   1920  CB  ASN A 242     -12.310  11.838 -24.216  1.00 37.18           C
ANISOU 1920  CB  ASN A 242     4877   4284   4968   -578   1503    497       C
ATOM   1921  CG  ASN A 242     -13.424  12.609 -24.873  1.00 42.96           C
ANISOU 1921  CG  ASN A 242     6197   4672   5454   -282   1323    712       C
ATOM   1922  OD1 ASN A 242     -14.175  12.059 -25.687  1.00 52.73           O
ANISOU 1922  OD1 ASN A 242     7212   5509   7315     48    125   1127       O
ATOM   1923  ND2 ASN A 242     -13.511  13.895 -24.579  1.00 51.39           N
ANISOU 1923  ND2 ASN A 242     7181   4796   7550   -512   1129    867       N
ATOM   1924  N   GLU A 243     -10.890   9.415 -22.743  1.00 37.15           N
ANISOU 1924  N   GLU A 243     4380   5041   4694   -494    328   -162       N
ATOM   1925  CA  GLU A 243      -9.704   8.650 -22.382  1.00 40.53           C
ANISOU 1925  CA  GLU A 243     4463   5611   5327      4    386    260       C
ATOM   1926  C   GLU A 243      -9.870   7.170 -22.752  1.00 39.21           C
ANISOU 1926  C   GLU A 243     4585   5757   4555   -163    599    -94       C
ATOM   1927  O   GLU A 243      -8.954   6.538 -23.276  1.00 41.51           O
ANISOU 1927  O   GLU A 243     4762   6385   4625     -1    642    -90       O
ATOM   1928  CB  GLU A 243      -9.435   8.820 -20.887  1.00 43.80           C
ANISOU 1928  CB  GLU A 243     4641   6147   5856    867    395    513       C
ATOM   1929  CG  GLU A 243      -8.243   8.011 -20.369  1.00 50.80           C
ANISOU 1929  CG  GLU A 243     5448   7458   6396   1348   -471    471       C
ATOM   1930  CD  GLU A 243      -8.350   7.591 -18.904  1.00 64.26           C
ANISOU 1930  CD  GLU A 243     8379   8701   7336   1303   -759    398       C
ATOM   1931  OE1 GLU A 243      -8.154   6.386 -18.595  1.00 76.08           O
ANISOU 1931  OE1 GLU A 243     9481   9566   9860   3052   -589    187       O
ATOM   1932  OE2 GLU A 243      -8.653   8.466 -18.062  1.00 68.89           O
ANISOU 1932  OE2 GLU A 243     9678   9369   7129   -199  -2311   -699       O
ATOM   1933  N   ARG A 244     -11.041   6.612 -22.432  1.00 36.14           N
ANISOU 1933  N   ARG A 244     3933   5460   4340    293    474   -248       N
ATOM   1934  CA  ARG A 244     -11.297   5.204 -22.657  1.00 38.91           C
ANISOU 1934  CA  ARG A 244     4584   5487   4713    887     77    291       C
ATOM   1935  C   ARG A 244     -11.355   4.889 -24.155  1.00 34.06           C
ANISOU 1935  C   ARG A 244     4339   4894   3710    113    792    468       C
ATOM   1936  O   ARG A 244     -10.823   3.855 -24.582  1.00 35.95           O
ANISOU 1936  O   ARG A 244     4359   4516   4784    160    706     44       O
ATOM   1937  CB  ARG A 244     -12.559   4.752 -21.926  1.00 38.72           C
ANISOU 1937  CB  ARG A 244     4771   5697   4244    878    212   1077       C
ATOM   1938  CG  ARG A 244     -12.454   4.770 -20.403  1.00 43.11           C
ANISOU 1938  CG  ARG A 244     5803   5770   4806    997    414   1204       C
ATOM   1939  CD  ARG A 244     -11.390   3.772 -19.895  1.00 42.57           C
ANISOU 1939  CD  ARG A 244     5707   6202   4265    613    -80   1194       C
ATOM   1940  NE  ARG A 244     -10.987   3.963 -18.499  1.00 42.62           N
ANISOU 1940  NE  ARG A 244     5694   5610   4889   -220    329   1403       N
ATOM   1941  CZ  ARG A 244     -11.864   3.790 -17.510  1.00 39.83           C
ANISOU 1941  CZ  ARG A 244     5072   5077   4984   -380    618   1233       C
ATOM   1942  NH1 ARG A 244     -11.548   4.026 -16.253  1.00 43.08           N
ANISOU 1942  NH1 ARG A 244     4631   5736   6003   -669   -129   1027       N
ATOM   1943  NH2 ARG A 244     -13.068   3.365 -17.822  1.00 41.43           N
ANISOU 1943  NH2 ARG A 244     4782   4864   6097   -197    513    768       N
ATOM   1944  N   LEU A 245     -12.027   5.761 -24.925  1.00 33.96           N
ANISOU 1944  N   LEU A 245     3618   4756   4529   -220    791    652       N
ATOM   1945  CA  LEU A 245     -12.105   5.604 -26.374  1.00 33.80           C
ANISOU 1945  CA  LEU A 245     4268   3920   4654    -51    689    352       C
ATOM   1946  C   LEU A 245     -10.700   5.678 -26.979  1.00 34.76           C
ANISOU 1946  C   LEU A 245     3823   4418   4966   -256    543    348       C
ATOM   1947  O   LEU A 245     -10.371   4.910 -27.886  1.00 38.88           O
ANISOU 1947  O   LEU A 245     4861   4895   5016   -912    926    367       O
ATOM   1948  CB  LEU A 245     -13.020   6.671 -26.976  1.00 35.32           C
ANISOU 1948  CB  LEU A 245     3959   4891   4571    234    352     81       C
ATOM   1949  CG  LEU A 245     -14.511   6.544 -26.642  1.00 36.59           C
ANISOU 1949  CG  LEU A 245     4069   4737   5095    432    630    156       C
ATOM   1950  CD1 LEU A 245     -15.263   7.729 -27.178  1.00 40.96           C
ANISOU 1950  CD1 LEU A 245     4944   5840   4779   -251    654    718       C
ATOM   1951  CD2 LEU A 245     -15.086   5.247 -27.164  1.00 40.42           C
ANISOU 1951  CD2 LEU A 245     4638   5101   5620    661    561    -32       C
ATOM   1952  N   GLN A 246      -9.863   6.601 -26.476  1.00 35.70           N
ANISOU 1952  N   GLN A 246     4131   4307   5125   -673    937    352       N
ATOM   1953  CA  GLN A 246      -8.492   6.742 -26.974  1.00 38.77           C
ANISOU 1953  CA  GLN A 246     4367   5197   5168   -571   1286   -440       C
ATOM   1954  C   GLN A 246      -7.704   5.453 -26.709  1.00 40.47           C
ANISOU 1954  C   GLN A 246     4332   5601   5443   -357    931    148       C
ATOM   1955  O   GLN A 246      -6.987   4.942 -27.596  1.00 41.97           O
ANISOU 1955  O   GLN A 246     5109   4858   5978   -588   1414    303       O
ATOM   1956  CB  GLN A 246      -7.836   7.992 -26.372  1.00 43.58           C
ANISOU 1956  CB  GLN A 246     5017   6169   5374  -1143   1156  -1060       C
ATOM   1957  N   LYS A 247      -7.861   4.920 -25.488  1.00 37.21           N
ANISOU 1957  N   LYS A 247     3960   4912   5267   -335   1127   -126       N
ATOM   1958  CA  LYS A 247      -7.127   3.732 -25.071  1.00 37.70           C
ANISOU 1958  CA  LYS A 247     3666   5003   5656   -138    938    429       C
ATOM   1959  C   LYS A 247      -7.557   2.532 -25.910  1.00 37.90           C
ANISOU 1959  C   LYS A 247     3958   5030   5412   -199    880    325       C
ATOM   1960  O   LYS A 247      -6.736   1.698 -26.282  1.00 39.86           O
ANISOU 1960  O   LYS A 247     4468   4630   6046    -70   1048    583       O
ATOM   1961  CB  LYS A 247      -7.216   3.467 -23.564  1.00 41.21           C
ANISOU 1961  CB  LYS A 247     4138   5266   6255    499   1488    441       C
ATOM   1962  N   GLN A 248      -8.858   2.442 -26.192  1.00 36.57           N
ANISOU 1962  N   GLN A 248     3900   4800   5195    170   1049    406       N
ATOM   1963  CA  GLN A 248      -9.399   1.336 -26.964  1.00 36.91           C
ANISOU 1963  CA  GLN A 248     4530   3841   5654    540   1138    101       C
ATOM   1964  C   GLN A 248      -8.819   1.359 -28.376  1.00 36.14           C
ANISOU 1964  C   GLN A 248     4577   3921   5234    180   1107    701       C
ATOM   1965  O   GLN A 248      -8.433   0.330 -28.917  1.00 39.59           O
ANISOU 1965  O   GLN A 248     5790   3847   5404    138   1182    272       O
ATOM   1966  CB  GLN A 248     -10.925   1.373 -26.977  1.00 39.08           C
ANISOU 1966  CB  GLN A 248     4659   4495   5693    318    228    230       C
ATOM   1967  CG  GLN A 248     -11.531   0.077 -27.503  1.00 44.78           C
ANISOU 1967  CG  GLN A 248     6108   4705   6202   -383   1045    406       C
ATOM   1968  CD  GLN A 248     -11.804   0.083 -28.988  1.00 51.15           C
ANISOU 1968  CD  GLN A 248     6496   5772   7164    177    785    293       C
ATOM   1969  OE1 GLN A 248     -12.393   1.040 -29.518  1.00 50.36           O
ANISOU 1969  OE1 GLN A 248     6744   5751   6638   1044   1601    554       O
ATOM   1970  NE2 GLN A 248     -11.357  -0.983 -29.662  1.00 51.44           N
ANISOU 1970  NE2 GLN A 248     6239   5184   8123    -92    788   -147       N
ATOM   1971  N   GLU A 249      -8.747   2.547 -28.958  1.00 38.17           N
ANISOU 1971  N   GLU A 249     4997   4208   5296   -202    860    853       N
ATOM   1972  CA  GLU A 249      -8.200   2.692 -30.294  1.00 38.40           C
ANISOU 1972  CA  GLU A 249     5315   4066   5208    -18   1049    658       C
ATOM   1973  C   GLU A 249      -6.734   2.259 -30.326  1.00 35.98           C
ANISOU 1973  C   GLU A 249     4628   4134   4909   -169    500    669       C
ATOM   1974  O   GLU A 249      -6.308   1.520 -31.222  1.00 39.11           O
ANISOU 1974  O   GLU A 249     5118   4575   5166    447    704    394       O
ATOM   1975  CB  GLU A 249      -8.384   4.133 -30.756  1.00 43.36           C
ANISOU 1975  CB  GLU A 249     6075   4428   5971    674   1165   1422       C
ATOM   1976  CG  GLU A 249      -7.845   4.324 -32.171  1.00 51.26           C
ANISOU 1976  CG  GLU A 249     7437   5543   6497     78   1561   1262       C
ATOM   1977  CD  GLU A 249      -8.429   5.486 -32.940  1.00 59.69           C
ANISOU 1977  CD  GLU A 249     9560   5716   7402    455   1370   1360       C
ATOM   1978  OE1 GLU A 249      -8.886   5.269 -34.091  1.00 70.83           O
ANISOU 1978  OE1 GLU A 249    10624   7936   8352    355    901   1228       O
ATOM   1979  OE2 GLU A 249      -8.397   6.602 -32.382  1.00 70.31           O
ANISOU 1979  OE2 GLU A 249    12543   6332   7841   -123   1682    871       O
ATOM   1980  N   ALA A 250      -5.951   2.719 -29.341  1.00 36.95           N
ANISOU 1980  N   ALA A 250     4102   4912   5023     82    733    352       N
ATOM   1981  CA  ALA A 250      -4.547   2.326 -29.261  1.00 37.90           C
ANISOU 1981  CA  ALA A 250     4166   4802   5432     97    831    797       C
ATOM   1982  C   ALA A 250      -4.407   0.815 -29.170  1.00 38.60           C
ANISOU 1982  C   ALA A 250     4740   4659   5266   -169   1230    546       C
ATOM   1983  O   ALA A 250      -3.579   0.242 -29.861  1.00 38.52           O
ANISOU 1983  O   ALA A 250     4432   4374   5830    209   1825    827       O
ATOM   1984  CB  ALA A 250      -3.870   2.974 -28.087  1.00 38.51           C
ANISOU 1984  CB  ALA A 250     4028   5173   5432     86    561   1438       C
ATOM   1985  N   ARG A 251      -5.229   0.168 -28.333  1.00 37.98           N
ANISOU 1985  N   ARG A 251     4372   4648   5413   -252   1605    902       N
ATOM   1986  CA  ARG A 251      -5.113  -1.266 -28.163  1.00 41.56           C
ANISOU 1986  CA  ARG A 251     5200   4853   5735      1   1165   1009       C
ATOM   1987  C   ARG A 251      -5.455  -1.992 -29.457  1.00 37.56           C
ANISOU 1987  C   ARG A 251     4121   4493   5656    609   1024   1056       C
ATOM   1988  O   ARG A 251      -4.842  -3.005 -29.805  1.00 41.92           O
ANISOU 1988  O   ARG A 251     5507   4303   6117    607   1274   1062       O
ATOM   1989  CB  ARG A 251      -5.990  -1.723 -26.994  1.00 43.11           C
ANISOU 1989  CB  ARG A 251     5298   4923   6158   -453   1722   1007       C
ATOM   1990  CG  ARG A 251      -5.829  -3.222 -26.797  1.00 48.23           C
ANISOU 1990  CG  ARG A 251     7140   4444   6741    218   1634   1051       C
ATOM   1991  CD  ARG A 251      -6.522  -3.790 -25.555  1.00 51.98           C
ANISOU 1991  CD  ARG A 251     7384   5828   6539   -260   1328   1264       C
ATOM   1992  NE  ARG A 251      -5.805  -3.356 -24.353  1.00 54.69           N
ANISOU 1992  NE  ARG A 251     6300   7491   6988   -374    748   1223       N
ATOM   1993  CZ  ARG A 251      -6.271  -3.405 -23.114  1.00 58.97           C
ANISOU 1993  CZ  ARG A 251     7113   7725   7567    155    855   1382       C
ATOM   1994  NH1 ARG A 251      -7.509  -3.836 -22.866  1.00 57.87           N
ANISOU 1994  NH1 ARG A 251     6454   7742   7790    928    420   1753       N
ATOM   1995  NH2 ARG A 251      -5.488  -3.008 -22.120  1.00 61.20           N
ANISOU 1995  NH2 ARG A 251     7326   7989   7937    450    724   1386       N
ATOM   1996  N   ALA A 252      -6.455  -1.484 -30.164  1.00 40.01           N
ANISOU 1996  N   ALA A 252     5010   4634   5557    769   1319    927       N
ATOM   1997  CA  ALA A 252      -6.872  -2.112 -31.393  1.00 43.23           C
ANISOU 1997  CA  ALA A 252     5324   5080   6022   1093   1206    947       C
ATOM   1998  C   ALA A 252      -5.699  -2.063 -32.353  1.00 39.72           C
ANISOU 1998  C   ALA A 252     5294   4477   5320    434   1177    983       C
ATOM   1999  O   ALA A 252      -5.396  -3.066 -32.986  1.00 44.58           O
ANISOU 1999  O   ALA A 252     6097   5359   5483    933   1474    650       O
ATOM   2000  CB  ALA A 252      -8.093  -1.429 -31.961  1.00 44.97           C
ANISOU 2000  CB  ALA A 252     5221   5609   6258   1317   1328   1603       C
ATOM   2001  N   PHE A 253      -5.037  -0.896 -32.435  1.00 40.37           N
ANISOU 2001  N   PHE A 253     5466   4361   5512    360   1025    415       N
ATOM   2002  CA  PHE A 253      -3.878  -0.764 -33.302  1.00 41.81           C
ANISOU 2002  CA  PHE A 253     5397   4626   5862    754   1399    942       C
ATOM   2003  C   PHE A 253      -2.767  -1.712 -32.854  1.00 44.22           C
ANISOU 2003  C   PHE A 253     6106   4666   6029    840   1176    746       C
ATOM   2004  O   PHE A 253      -2.090  -2.288 -33.698  1.00 44.71           O
ANISOU 2004  O   PHE A 253     6229   5187   5570    785   2565    876       O
ATOM   2005  CB  PHE A 253      -3.367   0.673 -33.370  1.00 42.01           C
ANISOU 2005  CB  PHE A 253     6055   4632   5276    768   1507    683       C
ATOM   2006  CG  PHE A 253      -4.115   1.544 -34.372  1.00 42.87           C
ANISOU 2006  CG  PHE A 253     6078   4845   5366   1374   1605   1366       C
ATOM   2007  CD1 PHE A 253      -4.018   1.294 -35.743  1.00 46.59           C
ANISOU 2007  CD1 PHE A 253     5765   5770   6168   1391   1755   1629       C
ATOM   2008  CD2 PHE A 253      -4.905   2.607 -33.947  1.00 49.48           C
ANISOU 2008  CD2 PHE A 253     7361   6397   5043   1616   2078   1758       C
ATOM   2009  CE1 PHE A 253      -4.700   2.078 -36.661  1.00 50.08           C
ANISOU 2009  CE1 PHE A 253     7182   5684   6162   1277   2123   2075       C
ATOM   2010  CE2 PHE A 253      -5.567   3.402 -34.870  1.00 50.73           C
ANISOU 2010  CE2 PHE A 253     6593   5861   6820   2550   1837   1173       C
ATOM   2011  CZ  PHE A 253      -5.466   3.133 -36.227  1.00 49.87           C
ANISOU 2011  CZ  PHE A 253     6605   6650   5694   1993   2305   2161       C
ATOM   2012  N   LYS A 254      -2.561  -1.844 -31.538  1.00 44.02           N
ANISOU 2012  N   LYS A 254     5139   5216   6370   1173   1620   1457       N
ATOM   2013  CA  LYS A 254      -1.509  -2.714 -31.033  1.00 41.78           C
ANISOU 2013  CA  LYS A 254     5406   4664   5804    812   1372   1838       C
ATOM   2014  C   LYS A 254      -1.772  -4.142 -31.499  1.00 43.40           C
ANISOU 2014  C   LYS A 254     5428   4902   6159    808   1769   1073       C
ATOM   2015  O   LYS A 254      -0.851  -4.786 -31.970  1.00 45.00           O
ANISOU 2015  O   LYS A 254     4686   4846   7567    707   1920    896       O
ATOM   2016  CB  LYS A 254      -1.387  -2.633 -29.505  1.00 40.71           C
ANISOU 2016  CB  LYS A 254     4312   5025   6129    635   1383   1848       C
ATOM   2017  CG  LYS A 254      -0.353  -3.543 -28.900  1.00 42.18           C
ANISOU 2017  CG  LYS A 254     4886   4587   6554   1575   1517   1255       C
ATOM   2018  CD  LYS A 254      -0.224  -3.404 -27.391  1.00 45.20           C
ANISOU 2018  CD  LYS A 254     5165   5044   6964   1025   1039    814       C
ATOM   2019  CE  LYS A 254       0.845  -4.316 -26.856  1.00 49.58           C
ANISOU 2019  CE  LYS A 254     6813   4766   7258    902    846    718       C
ATOM   2020  NZ  LYS A 254       0.898  -4.169 -25.400  1.00 58.68           N
ANISOU 2020  NZ  LYS A 254     7237   6726   8333   -231    934    894       N
ATOM   2021  N   VAL A 255      -3.020  -4.617 -31.354  1.00 41.24           N
ANISOU 2021  N   VAL A 255     5205   4547   5917   1118   1838   1458       N
ATOM   2022  CA  VAL A 255      -3.400  -5.939 -31.824  1.00 40.61           C
ANISOU 2022  CA  VAL A 255     5643   3697   6089   1437   1672   1492       C
ATOM   2023  C   VAL A 255      -3.156  -6.061 -33.326  1.00 45.04           C
ANISOU 2023  C   VAL A 255     7242   4235   5636   1800   1708   1102       C
ATOM   2024  O   VAL A 255      -2.599  -7.061 -33.795  1.00 43.56           O
ANISOU 2024  O   VAL A 255     6897   4410   5245   1114   1499    708       O
ATOM   2025  CB  VAL A 255      -4.859  -6.296 -31.481  1.00 42.46           C
ANISOU 2025  CB  VAL A 255     5596   4307   6229    864   1371   1153       C
ATOM   2026  CG1 VAL A 255      -5.288  -7.594 -32.148  1.00 44.56           C
ANISOU 2026  CG1 VAL A 255     5876   4399   6656    401   1783    781       C
ATOM   2027  CG2 VAL A 255      -5.084  -6.325 -29.970  1.00 39.34           C
ANISOU 2027  CG2 VAL A 255     4880   4160   5906    534    799   1255       C
ATOM   2028  N   LEU A 256      -3.585  -5.043 -34.092  1.00 46.09           N
ANISOU 2028  N   LEU A 256     7851   4408   5254   1763   2352   1239       N
ATOM   2029  CA  LEU A 256      -3.406  -5.111 -35.537  1.00 47.91           C
ANISOU 2029  CA  LEU A 256     8331   4562   5310   1628   1873    921       C
ATOM   2030  C   LEU A 256      -1.918  -5.259 -35.887  1.00 50.98           C
ANISOU 2030  C   LEU A 256     8087   5157   6126    750   2378    870       C
ATOM   2031  O   LEU A 256      -1.557  -6.131 -36.697  1.00 51.71           O
ANISOU 2031  O   LEU A 256     8532   4512   6604    664   2283    499       O
ATOM   2032  CB  LEU A 256      -4.074  -3.921 -36.205  1.00 49.83           C
ANISOU 2032  CB  LEU A 256     9040   4826   5065   1665   2863   1350       C
ATOM   2033  CG  LEU A 256      -4.134  -3.963 -37.733  1.00 55.27           C
ANISOU 2033  CG  LEU A 256     9669   5367   5963   1718   1851    868       C
ATOM   2034  CD1 LEU A 256      -5.074  -5.062 -38.237  1.00 59.29           C
ANISOU 2034  CD1 LEU A 256     9676   5642   7209   1912   1693    735       C
ATOM   2035  CD2 LEU A 256      -4.585  -2.600 -38.156  1.00 57.86           C
ANISOU 2035  CD2 LEU A 256    10253   6128   5604   1440   1897   2410       C
ATOM   2036  N   ASN A 257      -1.051  -4.485 -35.207  1.00 48.59           N
ANISOU 2036  N   ASN A 257     6774   4986   6701   1337   2112   1303       N
ATOM   2037  CA  ASN A 257       0.386  -4.514 -35.469  1.00 48.07           C
ANISOU 2037  CA  ASN A 257     7006   4735   6523    986   2217   1212       C
ATOM   2038  C   ASN A 257       1.012  -5.832 -35.001  1.00 51.38           C
ANISOU 2038  C   ASN A 257     7285   5218   7019   1219   2498   1822       C
ATOM   2039  O   ASN A 257       1.970  -6.307 -35.616  1.00 52.41           O
ANISOU 2039  O   ASN A 257     7113   5279   7521    269   2684   1127       O
ATOM   2040  CB  ASN A 257       1.063  -3.270 -34.911  1.00 47.11           C
ANISOU 2040  CB  ASN A 257     6805   5022   6072   1099   1869   1621       C
ATOM   2041  CG  ASN A 257       0.811  -2.102 -35.835  1.00 46.57           C
ANISOU 2041  CG  ASN A 257     7077   4425   6190   1312   1971   1170       C
ATOM   2042  OD1 ASN A 257       0.029  -1.193 -35.535  1.00 52.63           O
ANISOU 2042  OD1 ASN A 257     7737   4839   7419   1007   2251    628       O
ATOM   2043  ND2 ASN A 257       1.361  -2.167 -37.023  1.00 47.21           N
ANISOU 2043  ND2 ASN A 257     7096   4648   6193   1270   2730   1938       N
ATOM   2044  N   LEU A 258       0.470  -6.438 -33.933  1.00 50.41           N
ANISOU 2044  N   LEU A 258     6707   5714   6732    728   2700   1866       N
ATOM   2045  CA  LEU A 258       0.988  -7.715 -33.459  1.00 52.85           C
ANISOU 2045  CA  LEU A 258     6912   5664   7504   1449   2975   1119       C
ATOM   2046  C   LEU A 258       0.795  -8.783 -34.528  1.00 56.05           C
ANISOU 2046  C   LEU A 258     7020   5927   8351   1221   2383    437       C
ATOM   2047  O   LEU A 258       1.683  -9.608 -34.752  1.00 55.76           O
ANISOU 2047  O   LEU A 258     7114   5568   8506    978   2923    436       O
ATOM   2048  CB  LEU A 258       0.313  -8.158 -32.161  1.00 48.30           C
ANISOU 2048  CB  LEU A 258     5884   4602   7867   1439   3186   1762       C
ATOM   2049  CG  LEU A 258       0.827  -7.470 -30.892  1.00 55.26           C
ANISOU 2049  CG  LEU A 258     6727   6460   7809   1431   3063   1796       C
ATOM   2050  CD1 LEU A 258      -0.111  -7.734 -29.718  1.00 58.28           C
ANISOU 2050  CD1 LEU A 258     7201   6774   8168   1466   3241   2120       C
ATOM   2051  CD2 LEU A 258       2.243  -7.931 -30.579  1.00 56.61           C
ANISOU 2051  CD2 LEU A 258     7293   6054   8162   1140   2118   2199       C
ATOM   2052  N   LEU A 259      -0.393  -8.763 -35.138  1.00 46.41           N
ANISOU 2052  N   LEU A 259     5721   4334   7578   1411   2044    406       N
ATOM   2053  CA  LEU A 259      -0.815  -9.740 -36.129  1.00 51.00           C
ANISOU 2053  CA  LEU A 259     6619   5706   7053    677   2157    599       C
ATOM   2054  C   LEU A 259      -0.040  -9.605 -37.432  1.00 52.11           C
ANISOU 2054  C   LEU A 259     7238   5365   7197    642   1954    740       C
ATOM   2055  O   LEU A 259       0.298 -10.606 -38.049  1.00 49.46           O
ANISOU 2055  O   LEU A 259     6178   6111   6502   1616   2224    951       O
ATOM   2056  CB  LEU A 259      -2.321  -9.562 -36.353  1.00 48.06           C
ANISOU 2056  CB  LEU A 259     6079   5411   6769   1242   1472   1461       C
ATOM   2057  CG  LEU A 259      -3.260 -10.062 -35.242  1.00 49.25           C
ANISOU 2057  CG  LEU A 259     6209   5874   6628   1588   1745   1092       C
ATOM   2058  CD1 LEU A 259      -4.704  -9.779 -35.627  1.00 51.88           C
ANISOU 2058  CD1 LEU A 259     6222   6485   7003    782   2083    815       C
ATOM   2059  CD2 LEU A 259      -3.114 -11.547 -34.940  1.00 47.27           C
ANISOU 2059  CD2 LEU A 259     6097   5764   6099    882   1686   1059       C
ATOM   2060  N   LYS A 260       0.176  -8.370 -37.868  1.00 55.58           N
ANISOU 2060  N   LYS A 260     7677   6132   7307      4   3030    776       N
ATOM   2061  CA  LYS A 260       1.043  -8.115 -39.011  1.00 62.44           C
ANISOU 2061  CA  LYS A 260     8986   7097   7640    310   2887   1691       C
ATOM   2062  C   LYS A 260       2.375  -8.848 -38.836  1.00 69.09           C
ANISOU 2062  C   LYS A 260     8267   7743  10242    -79   3183   1443       C
ATOM   2063  O   LYS A 260       2.825  -9.502 -39.771  1.00 76.19           O
ANISOU 2063  O   LYS A 260    11773   7001  10176   1828    662  -2081       O
ATOM   2064  CB  LYS A 260       1.118  -6.598 -39.208  1.00 72.18           C
ANISOU 2064  CB  LYS A 260    10675   7657   9092    931   1672    824       C
ATOM   2065  CG  LYS A 260      -0.049  -6.103 -40.046  1.00 71.19           C
ANISOU 2065  CG  LYS A 260    11075   5847  10128    419   1868   1770       C
ATOM   2066  CD  LYS A 260      -0.327  -4.611 -39.961  1.00 73.58           C
ANISOU 2066  CD  LYS A 260    11199   6398  10358    130   2285   1444       C
ATOM   2067  CE  LYS A 260      -1.227  -4.149 -41.057  1.00 71.16           C
ANISOU 2067  CE  LYS A 260    10844   5683  10512   -123   2590   2624       C
ATOM   2068  NZ  LYS A 260      -1.411  -2.701 -40.997  1.00 74.13           N
ANISOU 2068  NZ  LYS A 260    11653   6251  10261    659   2916   2899       N
ATOM   2069  N   ALA A 261       2.979  -8.770 -37.639  1.00 61.69           N
ANISOU 2069  N   ALA A 261     6441   7524   9476   -308   5149   3025       N
ATOM   2070  CA  ALA A 261       4.246  -9.439 -37.363  1.00 61.26           C
ANISOU 2070  CA  ALA A 261     6451   6797  10027   -293   5201   1613       C
ATOM   2071  C   ALA A 261       4.089 -10.963 -37.360  1.00 67.09           C
ANISOU 2071  C   ALA A 261     7893   6382  11215    295   4506   1356       C
ATOM   2072  O   ALA A 261       4.827 -11.673 -38.043  1.00 62.24           O
ANISOU 2072  O   ALA A 261     7747   6044   9858  -1590   5544   1250       O
ATOM   2073  CB  ALA A 261       4.811  -8.951 -36.049  1.00 66.56           C
ANISOU 2073  CB  ALA A 261     7544   7670  10076   -752   4874   1936       C
ATOM   2074  N   GLN A 262       3.148 -11.497 -36.577  1.00 67.20           N
ANISOU 2074  N   GLN A 262     8207   6240  11087    222   4623    954       N
ATOM   2075  CA  GLN A 262       2.972 -12.944 -36.525  1.00 63.61           C
ANISOU 2075  CA  GLN A 262     8126   6100   9941    185   3425    565       C
ATOM   2076  C   GLN A 262       1.482 -13.269 -36.497  1.00 60.09           C
ANISOU 2076  C   GLN A 262     7545   5942   9343    430   3001   -157       C
ATOM   2077  O   GLN A 262       0.813 -12.826 -35.572  1.00 53.28           O
ANISOU 2077  O   GLN A 262     6971   3977   9296    350   2851   -157       O
ATOM   2078  CB  GLN A 262       3.650 -13.533 -35.283  1.00 68.94           C
ANISOU 2078  CB  GLN A 262     6756   8521  10918   1143   2875    351       C
ATOM   2079  N   PRO A 263       0.894 -14.023 -37.465  1.00 60.34           N
ANISOU 2079  N   PRO A 263     7847   7086   7994    578   3413   -324       N
ATOM   2080  CA  PRO A 263      -0.509 -14.441 -37.336  1.00 60.28           C
ANISOU 2080  CA  PRO A 263     7591   6381   8934   1005   2066    216       C
ATOM   2081  C   PRO A 263      -0.689 -15.341 -36.104  1.00 58.90           C
ANISOU 2081  C   PRO A 263     7072   6489   8816    343   2886    344       C
ATOM   2082  O   PRO A 263       0.186 -16.148 -35.779  1.00 70.21           O
ANISOU 2082  O   PRO A 263    10518   5254  10904   -953   1066   2029       O
ATOM   2083  CB  PRO A 263      -0.820 -15.135 -38.677  1.00 62.63           C
ANISOU 2083  CB  PRO A 263     8045   7404   8349   1071   2751   -276       C
ATOM   2084  CG  PRO A 263       0.256 -14.621 -39.622  1.00 62.64           C
ANISOU 2084  CG  PRO A 263     7912   7617   8270    959   2890   -396       C
ATOM   2085  CD  PRO A 263       1.502 -14.479 -38.732  1.00 65.69           C
ANISOU 2085  CD  PRO A 263     8720   7895   8344    233   3082   -548       C
ATOM   2086  N   MET A 264      -1.794 -15.168 -35.360  1.00 53.84           N
ANISOU 2086  N   MET A 264     6981   5631   7845    679   2170   1125       N
ATOM   2087  CA  MET A 264      -1.852 -15.804 -34.059  1.00 50.64           C
ANISOU 2087  CA  MET A 264     5358   6031   7854    515   2241    342       C
ATOM   2088  C   MET A 264      -3.264 -16.265 -33.742  1.00 46.91           C
ANISOU 2088  C   MET A 264     5198   6253   6374    328   2369    588       C
ATOM   2089  O   MET A 264      -4.230 -15.732 -34.290  1.00 45.29           O
ANISOU 2089  O   MET A 264     5381   6575   5253    641   2539   1038       O
ATOM   2090  CB  MET A 264      -1.433 -14.829 -32.959  1.00 49.34           C
ANISOU 2090  CB  MET A 264     5429   5773   7545    975   1562    541       C
ATOM   2091  CG  MET A 264       0.049 -14.589 -32.894  1.00 51.83           C
ANISOU 2091  CG  MET A 264     5765   6216   7712    390   2068     87       C
ATOM   2092  SD  MET A 264       0.417 -13.442 -31.557  1.00 51.71           S
ANISOU 2092  SD  MET A 264     5535   5717   8393    586   2302    873       S
ATOM   2093  CE  MET A 264       0.076 -11.966 -32.526  1.00 55.61           C
ANISOU 2093  CE  MET A 264     7086   5022   9020     45   1925    509       C
ATOM   2094  N   THR A 265      -3.350 -17.220 -32.814  1.00 40.34           N
ANISOU 2094  N   THR A 265     4514   4519   6296    788   2104      1       N
ATOM   2095  CA  THR A 265      -4.653 -17.504 -32.196  1.00 39.89           C
ANISOU 2095  CA  THR A 265     4713   4495   5950    601   1825    887       C
ATOM   2096  C   THR A 265      -5.027 -16.362 -31.246  1.00 41.78           C
ANISOU 2096  C   THR A 265     4319   5002   6553    796   1101    580       C
ATOM   2097  O   THR A 265      -4.177 -15.540 -30.868  1.00 38.21           O
ANISOU 2097  O   THR A 265     4177   5093   5247   1100    761    998       O
ATOM   2098  CB  THR A 265      -4.611 -18.823 -31.405  1.00 35.61           C
ANISOU 2098  CB  THR A 265     3504   4793   5232   1448    690   1425       C
ATOM   2099  OG1 THR A 265      -3.742 -18.609 -30.293  1.00 40.49           O
ANISOU 2099  OG1 THR A 265     4281   5314   5790   1265   1232   1306       O
ATOM   2100  CG2 THR A 265      -4.267 -20.019 -32.265  1.00 39.68           C
ANISOU 2100  CG2 THR A 265     4174   5629   5273    897   1071   1034       C
ATOM   2101  N   ALA A 266      -6.288 -16.373 -30.772  1.00 34.93           N
ANISOU 2101  N   ALA A 266     3272   4451   5547    534    965    828       N
ATOM   2102  CA  ALA A 266      -6.734 -15.405 -29.782  1.00 33.55           C
ANISOU 2102  CA  ALA A 266     3298   4196   5255    757    700    883       C
ATOM   2103  C   ALA A 266      -5.900 -15.531 -28.513  1.00 33.57           C
ANISOU 2103  C   ALA A 266     3290   3814   5651    704    578    591       C
ATOM   2104  O   ALA A 266      -5.529 -14.514 -27.923  1.00 35.46           O
ANISOU 2104  O   ALA A 266     3489   4227   5756    498    361    668       O
ATOM   2105  CB  ALA A 266      -8.220 -15.577 -29.500  1.00 31.45           C
ANISOU 2105  CB  ALA A 266     3440   3707   4801    574    569    846       C
ATOM   2106  N   PHE A 267      -5.614 -16.790 -28.114  1.00 33.43           N
ANISOU 2106  N   PHE A 267     3317   4119   5265    731    807   1046       N
ATOM   2107  CA  PHE A 267      -4.875 -17.025 -26.889  1.00 32.89           C
ANISOU 2107  CA  PHE A 267     2920   4350   5228    605    588    531       C
ATOM   2108  C   PHE A 267      -3.482 -16.426 -27.033  1.00 33.16           C
ANISOU 2108  C   PHE A 267     2659   4149   5792    410    382    566       C
ATOM   2109  O   PHE A 267      -2.983 -15.818 -26.100  1.00 38.68           O
ANISOU 2109  O   PHE A 267     3411   5470   5814    210    418    -61       O
ATOM   2110  CB  PHE A 267      -4.785 -18.501 -26.496  1.00 36.72           C
ANISOU 2110  CB  PHE A 267     3990   4441   5523    756    652    676       C
ATOM   2111  CG  PHE A 267      -3.895 -18.736 -25.290  1.00 35.89           C
ANISOU 2111  CG  PHE A 267     3542   4775   5318    920    634    101       C
ATOM   2112  CD1 PHE A 267      -4.305 -18.369 -24.014  1.00 35.05           C
ANISOU 2112  CD1 PHE A 267     4390   4067   4861    153    267    428       C
ATOM   2113  CD2 PHE A 267      -2.634 -19.321 -25.446  1.00 38.89           C
ANISOU 2113  CD2 PHE A 267     3569   4657   6551    470    618    485       C
ATOM   2114  CE1 PHE A 267      -3.481 -18.589 -22.922  1.00 38.07           C
ANISOU 2114  CE1 PHE A 267     4100   4591   5774    -14   -214     75       C
ATOM   2115  CE2 PHE A 267      -1.823 -19.505 -24.354  1.00 38.24           C
ANISOU 2115  CE2 PHE A 267     4160   4347   6023    171    672    512       C
ATOM   2116  CZ  PHE A 267      -2.262 -19.172 -23.094  1.00 38.38           C
ANISOU 2116  CZ  PHE A 267     3787   4877   5918   -229    603    -84       C
ATOM   2117  N   GLU A 268      -2.884 -16.633 -28.199  1.00 34.13           N
ANISOU 2117  N   GLU A 268     2986   4120   5861    513    755    627       N
ATOM   2118  CA  GLU A 268      -1.541 -16.119 -28.440  1.00 37.36           C
ANISOU 2118  CA  GLU A 268     2982   4547   6663    802    727    918       C
ATOM   2119  C   GLU A 268      -1.481 -14.598 -28.365  1.00 38.92           C
ANISOU 2119  C   GLU A 268     3350   5021   6418    733    487    501       C
ATOM   2120  O   GLU A 268      -0.550 -14.033 -27.811  1.00 43.56           O
ANISOU 2120  O   GLU A 268     3664   6095   6793     29    795    682       O
ATOM   2121  CB  GLU A 268      -1.074 -16.630 -29.792  1.00 36.91           C
ANISOU 2121  CB  GLU A 268     3583   3817   6625    661   1119    777       C
ATOM   2122  CG  GLU A 268      -0.648 -18.091 -29.739  1.00 42.32           C
ANISOU 2122  CG  GLU A 268     3845   4386   7847   1294    778    731       C
ATOM   2123  CD  GLU A 268      -0.178 -18.584 -31.095  1.00 51.09           C
ANISOU 2123  CD  GLU A 268     4918   6330   8163   1492   1713    139       C
ATOM   2124  OE1 GLU A 268      -0.856 -18.406 -32.136  1.00 48.24           O
ANISOU 2124  OE1 GLU A 268     4092   5547   8689    596   1752    527       O
ATOM   2125  OE2 GLU A 268       0.899 -19.206 -31.069  1.00 63.02           O
ANISOU 2125  OE2 GLU A 268     5934   7959  10052   2395   -197    121       O
ATOM   2126  N   VAL A 269      -2.506 -13.930 -28.900  1.00 40.43           N
ANISOU 2126  N   VAL A 269     3538   5623   6200    844   1447    944       N
ATOM   2127  CA  VAL A 269      -2.578 -12.477 -28.835  1.00 36.65           C
ANISOU 2127  CA  VAL A 269     3585   4818   5523    799   1163    871       C
ATOM   2128  C   VAL A 269      -2.714 -12.090 -27.372  1.00 37.00           C
ANISOU 2128  C   VAL A 269     3352   4435   6269    545    716    778       C
ATOM   2129  O   VAL A 269      -2.090 -11.137 -26.930  1.00 36.87           O
ANISOU 2129  O   VAL A 269     3747   4366   5896      1    784    732       O
ATOM   2130  CB  VAL A 269      -3.746 -11.933 -29.675  1.00 38.30           C
ANISOU 2130  CB  VAL A 269     4177   4754   5620    771   1439    342       C
ATOM   2131  CG1 VAL A 269      -3.861 -10.411 -29.575  1.00 38.30           C
ANISOU 2131  CG1 VAL A 269     4235   4727   5589    553   1196    445       C
ATOM   2132  CG2 VAL A 269      -3.678 -12.361 -31.133  1.00 36.91           C
ANISOU 2132  CG2 VAL A 269     4407   4457   5161    512   1230    691       C
ATOM   2133  N   CYS A 270      -3.580 -12.821 -26.651  1.00 34.80           N
ANISOU 2133  N   CYS A 270     3141   4769   5310     43    673    996       N
ATOM   2134  CA  CYS A 270      -3.859 -12.570 -25.241  1.00 36.97           C
ANISOU 2134  CA  CYS A 270     3758   4647   5641    -38    346    707       C
ATOM   2135  C   CYS A 270      -2.551 -12.571 -24.438  1.00 33.79           C
ANISOU 2135  C   CYS A 270     3564   3511   5765     92    147    328       C
ATOM   2136  O   CYS A 270      -2.295 -11.681 -23.630  1.00 39.73           O
ANISOU 2136  O   CYS A 270     4224   4920   5950   -598    444    740       O
ATOM   2137  CB  CYS A 270      -4.905 -13.567 -24.734  1.00 31.85           C
ANISOU 2137  CB  CYS A 270     2937   4224   4939    163   -417    182       C
ATOM   2138  SG  CYS A 270      -5.340 -13.264 -23.010  1.00 39.84           S
ANISOU 2138  SG  CYS A 270     3915   5488   5733    -11     24    710       S
ATOM   2139  N   VAL A 271      -1.688 -13.566 -24.687  1.00 37.94           N
ANISOU 2139  N   VAL A 271     3105   4657   6653   -162    531     17       N
ATOM   2140  CA  VAL A 271      -0.419 -13.677 -23.977  1.00 39.18           C
ANISOU 2140  CA  VAL A 271     3163   4958   6765    537    219    442       C
ATOM   2141  C   VAL A 271       0.500 -12.502 -24.308  1.00 39.69           C
ANISOU 2141  C   VAL A 271     4034   4319   6727   -190   -386    234       C
ATOM   2142  O   VAL A 271       1.272 -12.045 -23.451  1.00 42.83           O
ANISOU 2142  O   VAL A 271     4272   5302   6700    561   -965    722       O
ATOM   2143  CB  VAL A 271       0.305 -15.005 -24.285  1.00 41.83           C
ANISOU 2143  CB  VAL A 271     3508   5421   6963     91     90    265       C
ATOM   2144  CG1 VAL A 271       1.669 -15.016 -23.625  1.00 47.08           C
ANISOU 2144  CG1 VAL A 271     3756   6554   7577     16     99    434       C
ATOM   2145  CG2 VAL A 271      -0.509 -16.207 -23.834  1.00 44.56           C
ANISOU 2145  CG2 VAL A 271     3726   6167   7039    -95   -474    588       C
ATOM   2146  N   LYS A 272       0.454 -12.030 -25.566  1.00 39.55           N
ANISOU 2146  N   LYS A 272     3757   4404   6867   -308    247    600       N
ATOM   2147  CA  LYS A 272       1.232 -10.852 -25.946  1.00 42.59           C
ANISOU 2147  CA  LYS A 272     4245   4642   7294   -797    718    531       C
ATOM   2148  C   LYS A 272       0.686  -9.590 -25.286  1.00 40.93           C
ANISOU 2148  C   LYS A 272     3386   4751   7415   -684    -23    529       C
ATOM   2149  O   LYS A 272       1.507  -8.770 -24.835  1.00 42.41           O
ANISOU 2149  O   LYS A 272     3791   4319   8003   -759    178   -143       O
ATOM   2150  CB  LYS A 272       1.239 -10.550 -27.446  1.00 47.83           C
ANISOU 2150  CB  LYS A 272     5564   5025   7584   -349    760   1296       C
ATOM   2151  CG  LYS A 272       1.741 -11.687 -28.314  1.00 55.49           C
ANISOU 2151  CG  LYS A 272     6610   5619   8853   -176    910    874       C
ATOM   2152  CD  LYS A 272       3.256 -11.830 -28.374  1.00 59.11           C
ANISOU 2152  CD  LYS A 272     6989   5556   9914    157    782   1060       C
ATOM   2153  CE  LYS A 272       3.730 -12.367 -29.701  1.00 64.80           C
ANISOU 2153  CE  LYS A 272     8698   6735   9188   -391    778   1271       C
ATOM   2154  N   LEU A 273      -0.662  -9.437 -25.262  1.00 44.35           N
ANISOU 2154  N   LEU A 273     3774   5532   7545   -433   -230   1040       N
ATOM   2155  CA  LEU A 273      -1.279  -8.227 -24.728  1.00 43.35           C
ANISOU 2155  CA  LEU A 273     3439   5889   7142   -451   -170    939       C
ATOM   2156  C   LEU A 273      -1.162  -8.187 -23.210  1.00 47.36           C
ANISOU 2156  C   LEU A 273     4293   5449   8253   -518   -451    979       C
ATOM   2157  O   LEU A 273      -0.981  -7.108 -22.637  1.00 52.38           O
ANISOU 2157  O   LEU A 273     5344   4909   9647   -593   -163    500       O
ATOM   2158  CB  LEU A 273      -2.757  -8.114 -25.078  1.00 41.83           C
ANISOU 2158  CB  LEU A 273     3489   5185   7221  -1089   -163   1181       C
ATOM   2159  CG  LEU A 273      -3.107  -7.684 -26.488  1.00 44.65           C
ANISOU 2159  CG  LEU A 273     4627   5842   6495   -839     94   1282       C
ATOM   2160  CD1 LEU A 273      -4.607  -7.788 -26.589  1.00 39.80           C
ANISOU 2160  CD1 LEU A 273     4289   4768   6066   -202     79   1406       C
ATOM   2161  CD2 LEU A 273      -2.641  -6.270 -26.757  1.00 45.10           C
ANISOU 2161  CD2 LEU A 273     4899   5448   6790   -478    183   1558       C
ATOM   2162  N   PHE A 274      -1.339  -9.361 -22.578  1.00 39.31           N
ANISOU 2162  N   PHE A 274     2929   4863   7143   -480   -271   1189       N
ATOM   2163  CA  PHE A 274      -1.383  -9.445 -21.129  1.00 44.46           C
ANISOU 2163  CA  PHE A 274     4174   5209   7509   -174   -194   1115       C
ATOM   2164  C   PHE A 274      -0.332 -10.439 -20.639  1.00 48.81           C
ANISOU 2164  C   PHE A 274     4206   6149   8192    494    -61    629       C
ATOM   2165  O   PHE A 274      -0.662 -11.535 -20.169  1.00 47.47           O
ANISOU 2165  O   PHE A 274     3829   6022   8186     49     45    194       O
ATOM   2166  CB  PHE A 274      -2.822  -9.823 -20.762  1.00 44.08           C
ANISOU 2166  CB  PHE A 274     4078   6121   6549    -68     26   1185       C
ATOM   2167  CG  PHE A 274      -3.867  -8.876 -21.335  1.00 43.83           C
ANISOU 2167  CG  PHE A 274     3730   5652   7271    163   -730    248       C
ATOM   2168  CD1 PHE A 274      -3.973  -7.571 -20.877  1.00 44.96           C
ANISOU 2168  CD1 PHE A 274     4009   6296   6775    138  -1341     42       C
ATOM   2169  CD2 PHE A 274      -4.723  -9.274 -22.355  1.00 39.69           C
ANISOU 2169  CD2 PHE A 274     3366   5183   6530   -181    316   1105       C
ATOM   2170  CE1 PHE A 274      -4.892  -6.704 -21.425  1.00 47.03           C
ANISOU 2170  CE1 PHE A 274     3230   6566   8074   1330   -546   -174       C
ATOM   2171  CE2 PHE A 274      -5.677  -8.421 -22.859  1.00 42.20           C
ANISOU 2171  CE2 PHE A 274     3343   5463   7229     48    348    557       C
ATOM   2172  CZ  PHE A 274      -5.750  -7.138 -22.414  1.00 44.31           C
ANISOU 2172  CZ  PHE A 274     3220   5902   7714   -150   -188   -156       C
ATOM   2173  N   PRO A 275       0.971 -10.093 -20.701  1.00 45.85           N
ANISOU 2173  N   PRO A 275     4340   4779   8300    561   -646      0       N
ATOM   2174  CA  PRO A 275       2.017 -11.078 -20.404  1.00 49.44           C
ANISOU 2174  CA  PRO A 275     4295   6021   8468   1299   -451    719       C
ATOM   2175  C   PRO A 275       2.046 -11.552 -18.953  1.00 50.82           C
ANISOU 2175  C   PRO A 275     4375   7427   7507   1058   -825    330       C
ATOM   2176  O   PRO A 275       2.621 -12.607 -18.662  1.00 48.92           O
ANISOU 2176  O   PRO A 275     4380   7492   6716     -8   -498   -530       O
ATOM   2177  CB  PRO A 275       3.297 -10.344 -20.811  1.00 52.37           C
ANISOU 2177  CB  PRO A 275     5575   5467   8855    705   -756    810       C
ATOM   2178  CG  PRO A 275       2.954  -8.885 -20.623  1.00 51.99           C
ANISOU 2178  CG  PRO A 275     5622   5363   8769    553   -558    720       C
ATOM   2179  CD  PRO A 275       1.509  -8.776 -21.046  1.00 46.46           C
ANISOU 2179  CD  PRO A 275     4627   5322   7704    603    423   1119       C
ATOM   2180  N   THR A 276       1.423 -10.772 -18.059  1.00 52.02           N
ANISOU 2180  N   THR A 276     4479   7601   7684   1371    296   1070       N
ATOM   2181  CA  THR A 276       1.422 -11.039 -16.630  1.00 60.84           C
ANISOU 2181  CA  THR A 276     5802   9072   8241   1137    -78    775       C
ATOM   2182  C   THR A 276       0.050 -11.552 -16.185  1.00 65.60           C
ANISOU 2182  C   THR A 276     7433   9106   8385    227   -304   1956       C
ATOM   2183  O   THR A 276      -0.033 -12.479 -15.394  1.00 72.87           O
ANISOU 2183  O   THR A 276     8921   9868   8896   1840   -324   2997       O
ATOM   2184  CB  THR A 276       1.830  -9.752 -15.908  1.00 68.55           C
ANISOU 2184  CB  THR A 276     6582   9963   9501    740    185    606       C
ATOM   2185  OG1 THR A 276       0.939  -8.720 -16.320  1.00 72.36           O
ANISOU 2185  OG1 THR A 276     7494   9824  10176   1173   1022   1682       O
ATOM   2186  CG2 THR A 276       3.246  -9.320 -16.252  1.00 71.37           C
ANISOU 2186  CG2 THR A 276     7672   9867   9580    217    485   -229       C
ATOM   2187  N   LEU A 277      -1.030 -10.967 -16.711  1.00 63.96           N
ANISOU 2187  N   LEU A 277     6217   9884   8202   -719   -879   1617       N
ATOM   2188  CA  LEU A 277      -2.367 -11.212 -16.193  1.00 67.11           C
ANISOU 2188  CA  LEU A 277     7239   9983   8277  -1133   -892    834       C
ATOM   2189  C   LEU A 277      -3.004 -12.479 -16.770  1.00 62.13           C
ANISOU 2189  C   LEU A 277     5691   9978   7938   -396  -2240    836       C
ATOM   2190  O   LEU A 277      -3.966 -12.972 -16.193  1.00 71.96           O
ANISOU 2190  O   LEU A 277     6679  12214   8446  -1488  -1925   1194       O
ATOM   2191  CB  LEU A 277      -3.212  -9.979 -16.493  1.00 67.58           C
ANISOU 2191  CB  LEU A 277     8251   9245   8182  -1345   -811    937       C
ATOM   2192  CG  LEU A 277      -2.737  -8.666 -15.861  1.00 72.51           C
ANISOU 2192  CG  LEU A 277     9769   9529   8252  -1364   -791   1051       C
ATOM   2193  CD1 LEU A 277      -3.473  -7.504 -16.501  1.00 70.87           C
ANISOU 2193  CD1 LEU A 277     9198   8808   8922  -1470   -776   1010       C
ATOM   2194  CD2 LEU A 277      -2.937  -8.672 -14.348  1.00 71.92           C
ANISOU 2194  CD2 LEU A 277    10259   8998   8067   -976   -239   1310       C
ATOM   2195  N   TYR A 278      -2.477 -13.025 -17.877  1.00 57.13           N
ANISOU 2195  N   TYR A 278     5939   7794   7974    488  -2527   1059       N
ATOM   2196  CA  TYR A 278      -3.170 -14.103 -18.578  1.00 55.05           C
ANISOU 2196  CA  TYR A 278     6014   6785   8118    293  -1675   1376       C
ATOM   2197  C   TYR A 278      -3.307 -15.364 -17.718  1.00 56.38           C
ANISOU 2197  C   TYR A 278     5870   6524   9030   -736  -1411   1675       C
ATOM   2198  O   TYR A 278      -4.244 -16.127 -17.923  1.00 57.11           O
ANISOU 2198  O   TYR A 278     5531   6356   9814  -1545   -633   2262       O
ATOM   2199  CB  TYR A 278      -2.514 -14.498 -19.906  1.00 52.94           C
ANISOU 2199  CB  TYR A 278     5096   7260   7758    864  -1180    803       C
ATOM   2200  CG  TYR A 278      -1.258 -15.352 -19.847  1.00 54.97           C
ANISOU 2200  CG  TYR A 278     5753   6457   8674   1708   -595   -584       C
ATOM   2201  CD1 TYR A 278      -1.326 -16.744 -19.818  1.00 58.33           C
ANISOU 2201  CD1 TYR A 278     5026   6967  10169   1410     95    -42       C
ATOM   2202  CD2 TYR A 278      -0.004 -14.761 -19.880  1.00 62.75           C
ANISOU 2202  CD2 TYR A 278     5936   8065   9840   1383   -326    -79       C
ATOM   2203  CE1 TYR A 278      -0.177 -17.519 -19.801  1.00 59.71           C
ANISOU 2203  CE1 TYR A 278     6415   5490  10782   2348    238  -1152       C
ATOM   2204  CE2 TYR A 278       1.154 -15.526 -19.860  1.00 63.32           C
ANISOU 2204  CE2 TYR A 278     6275   7212  10572   2244   -250    239       C
ATOM   2205  CZ  TYR A 278       1.065 -16.905 -19.820  1.00 64.73           C
ANISOU 2205  CZ  TYR A 278     6622   7033  10939   1503   -236   -975       C
ATOM   2206  OH  TYR A 278       2.215 -17.628 -19.805  1.00 66.73           O
ANISOU 2206  OH  TYR A 278     7433   6780  11141   2617     45    -10       O
ATOM   2207  N   GLU A 279      -2.373 -15.616 -16.796  1.00 57.59           N
ANISOU 2207  N   GLU A 279     7209   5966   8707   -921  -1278   2010       N
ATOM   2208  CA  GLU A 279      -2.461 -16.785 -15.931  1.00 59.35           C
ANISOU 2208  CA  GLU A 279     6951   6647   8950    236  -2518   3086       C
ATOM   2209  C   GLU A 279      -3.450 -16.554 -14.785  1.00 64.51           C
ANISOU 2209  C   GLU A 279     9200   7371   7939   -818  -1729   3165       C
ATOM   2210  O   GLU A 279      -4.236 -17.447 -14.463  1.00 69.03           O
ANISOU 2210  O   GLU A 279    10456   8346   7427  -1683  -1953   2373       O
ATOM   2211  N   LYS A 280      -3.417 -15.348 -14.191  1.00 72.47           N
ANISOU 2211  N   LYS A 280    10929   9609   6996  -1272  -1464   2285       N
ATOM   2212  CA  LYS A 280      -4.233 -14.993 -13.034  1.00 73.48           C
ANISOU 2212  CA  LYS A 280    10885  10162   6871  -1824  -1290   1664       C
ATOM   2213  C   LYS A 280      -5.692 -14.701 -13.410  1.00 71.64           C
ANISOU 2213  C   LYS A 280     9784  10594   6840  -2724    182    901       C
ATOM   2214  O   LYS A 280      -6.598 -15.102 -12.667  1.00 65.07           O
ANISOU 2214  O   LYS A 280     9292   9832   5600  -2935    632   -381       O
ATOM   2215  CB  LYS A 280      -3.610 -13.794 -12.304  1.00 74.51           C
ANISOU 2215  CB  LYS A 280    11221  10230   6858  -1906  -2139   1985       C
ATOM   2216  N   GLN A 281      -5.904 -13.980 -14.531  1.00 73.44           N
ANISOU 2216  N   GLN A 281    10011  10844   7048  -2483    462    946       N
ATOM   2217  CA  GLN A 281      -7.224 -13.584 -15.022  1.00 68.37           C
ANISOU 2217  CA  GLN A 281     9518  10580   5878  -2727    570    416       C
ATOM   2218  C   GLN A 281      -7.357 -13.923 -16.516  1.00 69.84           C
ANISOU 2218  C   GLN A 281     8737  11725   6076  -2383   1134   -766       C
ATOM   2219  O   GLN A 281      -6.418 -14.400 -17.143  1.00 81.92           O
ANISOU 2219  O   GLN A 281    10831  13484   6809  -1226   2104    241       O
ATOM   2220  CB  GLN A 281      -7.470 -12.093 -14.758  1.00 66.65           C
ANISOU 2220  CB  GLN A 281     9615  10433   5274  -2650    322   -148       C
ATOM   2221  CG  GLN A 281      -7.646 -11.726 -13.286  1.00 70.10           C
ANISOU 2221  CG  GLN A 281    11139   9314   6183  -1999   -206   -161       C
ATOM   2222  CD  GLN A 281      -7.284 -10.290 -12.974  1.00 66.17           C
ANISOU 2222  CD  GLN A 281    10567   8837   5736  -1416  -1033   -297       C
ATOM   2223  OE1 GLN A 281      -6.215 -10.015 -12.421  1.00 65.77           O
ANISOU 2223  OE1 GLN A 281     9647   6088   9253     28  -1445   -476       O
ATOM   2224  NE2 GLN A 281      -8.157  -9.355 -13.324  1.00 65.75           N
ANISOU 2224  NE2 GLN A 281    11022   9010   4950  -1014   -499   1160       N
ATOM   2225  N   LEU A 282      -8.542 -13.686 -17.086  1.00 73.29           N
ANISOU 2225  N   LEU A 282    10422  11794   5629  -1809    420   -466       N
ATOM   2226  CA  LEU A 282      -8.837 -14.084 -18.459  1.00 69.93           C
ANISOU 2226  CA  LEU A 282    10291   9819   6461  -1326   -115   1115       C
ATOM   2227  C   LEU A 282      -9.907 -13.153 -19.021  1.00 64.97           C
ANISOU 2227  C   LEU A 282     8129   9787   6768   -716   -168   1825       C
ATOM   2228  O   LEU A 282     -11.110 -13.391 -18.861  1.00 68.25           O
ANISOU 2228  O   LEU A 282     6135  11591   8207    430   4244   1866       O
ATOM   2229  CB  LEU A 282      -9.229 -15.552 -18.600  1.00 68.47           C
ANISOU 2229  CB  LEU A 282    10806   8656   6552  -1186  -1752  -1095       C
ATOM   2230  CG  LEU A 282     -10.075 -16.145 -17.466  1.00 71.33           C
ANISOU 2230  CG  LEU A 282    10018   9225   7859  -1291  -1629  -1926       C
ATOM   2231  CD1 LEU A 282     -11.575 -15.985 -17.687  1.00 69.36           C
ANISOU 2231  CD1 LEU A 282     9635   9115   7603   -561  -2309  -2971       C
ATOM   2232  CD2 LEU A 282      -9.708 -17.613 -17.255  1.00 68.97           C
ANISOU 2232  CD2 LEU A 282    10226   8820   7158  -1530  -1736   -933       C
ATOM   2233  N   PRO A 283      -9.457 -12.051 -19.677  1.00 47.53           N
ANISOU 2233  N   PRO A 283     6841   7211   4007    965   1287   1459       N
ATOM   2234  CA  PRO A 283     -10.282 -11.223 -20.572  1.00 47.00           C
ANISOU 2234  CA  PRO A 283     4549   7444   5865    868   1312   1346       C
ATOM   2235  C   PRO A 283      -9.818 -10.878 -22.012  1.00 54.27           C
ANISOU 2235  C   PRO A 283     5297   8964   6358   2825   2701   -511       C
ATOM   2236  O   PRO A 283      -8.597 -11.171 -22.507  1.00 51.38           O
ANISOU 2236  O   PRO A 283     4116   8679   6726    264    -40  -2714       O
ATOM   2237  CB  PRO A 283     -10.051 -10.036 -19.690  1.00 47.95           C
ANISOU 2237  CB  PRO A 283     4464   7635   6119   2234   3491    553       C
ATOM   2238  CG  PRO A 283      -8.514 -10.056 -19.489  1.00 57.86           C
ANISOU 2238  CG  PRO A 283     5889   8169   7926   1827    748    491       C
ATOM   2239  CD  PRO A 283      -8.100 -11.509 -19.640  1.00 55.70           C
ANISOU 2239  CD  PRO A 283     7493   6833   6836   1105   -374   -256       C
ATOM   2240  N   LEU A 284     -10.875 -10.185 -22.570  1.00 54.67           N
ANISOU 2240  N   LEU A 284     5819   7871   7084    755   1816    -60       N
ATOM   2241  CA  LEU A 284     -10.836  -9.219 -23.629  1.00 47.62           C
ANISOU 2241  CA  LEU A 284     4777   8114   5202   2701     23   -968       C
ATOM   2242  C   LEU A 284     -10.106 -10.016 -24.710  1.00 57.08           C
ANISOU 2242  C   LEU A 284     5591  10176   5920    588   1015  -1028       C
ATOM   2243  O   LEU A 284     -10.265 -11.259 -24.828  1.00 71.45           O
ANISOU 2243  O   LEU A 284     4620  14328   8198   3043   1849  -1698       O
ATOM   2244  CB  LEU A 284     -10.114  -7.934 -23.144  1.00 47.46           C
ANISOU 2244  CB  LEU A 284     5083   7694   5255   3796   1159   -238       C
ATOM   2245  CG  LEU A 284     -10.772  -6.558 -23.402  1.00 60.71           C
ANISOU 2245  CG  LEU A 284     7549   9044   6475   2138    625    630       C
ATOM   2246  CD1 LEU A 284      -9.861  -5.556 -24.137  1.00 60.72           C
ANISOU 2246  CD1 LEU A 284     7398   9011   6660   1163    618    -52       C
ATOM   2247  CD2 LEU A 284     -12.093  -6.639 -24.138  1.00 70.22           C
ANISOU 2247  CD2 LEU A 284     7449  10559   8673   2550    515   1009       C
ATOM   2248  N   THR A 285      -9.265  -9.311 -25.425  1.00 43.67           N
ANISOU 2248  N   THR A 285     4802   5982   5808  -1787   -169   -346       N
ATOM   2249  CA  THR A 285      -8.545  -9.829 -26.575  1.00 34.60           C
ANISOU 2249  CA  THR A 285     3351   4269   5524    537    327    723       C
ATOM   2250  C   THR A 285      -9.516 -10.184 -27.707  1.00 33.09           C
ANISOU 2250  C   THR A 285     3237   4013   5321    331    795    431       C
ATOM   2251  O   THR A 285      -9.433  -9.616 -28.783  1.00 34.94           O
ANISOU 2251  O   THR A 285     3695   4082   5500    701    963    568       O
ATOM   2252  CB  THR A 285      -7.622 -11.004 -26.261  1.00 34.36           C
ANISOU 2252  CB  THR A 285     3228   4411   5417    468    650    401       C
ATOM   2253  OG1 THR A 285      -6.709 -10.649 -25.212  1.00 33.92           O
ANISOU 2253  OG1 THR A 285     2821   4229   5836     96    548    936       O
ATOM   2254  CG2 THR A 285      -6.892 -11.438 -27.517  1.00 37.60           C
ANISOU 2254  CG2 THR A 285     3539   5172   5574    311    761    501       C
ATOM   2255  N   ILE A 286     -10.454 -11.110 -27.446  1.00 34.42           N
ANISOU 2255  N   ILE A 286     3421   4230   5428    414    798    440       N
ATOM   2256  CA  ILE A 286     -11.445 -11.515 -28.421  1.00 33.74           C
ANISOU 2256  CA  ILE A 286     3953   4050   4816    734    878    304       C
ATOM   2257  C   ILE A 286     -12.320 -10.314 -28.768  1.00 34.51           C
ANISOU 2257  C   ILE A 286     3608   4573   4932    747    630   -211       C
ATOM   2258  O   ILE A 286     -12.632 -10.116 -29.945  1.00 36.94           O
ANISOU 2258  O   ILE A 286     3789   5091   5154    924    403    745       O
ATOM   2259  CB  ILE A 286     -12.248 -12.719 -27.909  1.00 38.20           C
ANISOU 2259  CB  ILE A 286     4285   4478   5753    552    725    -31       C
ATOM   2260  CG1 ILE A 286     -11.351 -13.931 -27.794  1.00 39.63           C
ANISOU 2260  CG1 ILE A 286     4549   4785   5725    603   1540   -270       C
ATOM   2261  CG2 ILE A 286     -13.449 -12.984 -28.812  1.00 38.01           C
ANISOU 2261  CG2 ILE A 286     4147   4892   5402   1098    650    374       C
ATOM   2262  N   SER A 287     -12.682  -9.488 -27.761  1.00 32.19           N
ANISOU 2262  N   SER A 287     3545   4118   4568    915    632    592       N
ATOM   2263  CA  SER A 287     -13.437  -8.284 -28.070  1.00 34.49           C
ANISOU 2263  CA  SER A 287     4218   4300   4584   1186    802    655       C
ATOM   2264  C   SER A 287     -12.727  -7.414 -29.104  1.00 34.75           C
ANISOU 2264  C   SER A 287     3580   5080   4542    435    633    331       C
ATOM   2265  O   SER A 287     -13.391  -6.868 -29.988  1.00 35.52           O
ANISOU 2265  O   SER A 287     4278   4944   4274   1078     74    223       O
ATOM   2266  N   GLU A 288     -11.397  -7.240 -28.936  1.00 35.49           N
ANISOU 2266  N   GLU A 288     3637   4943   4903    448    354    311       N
ATOM   2267  CA  GLU A 288     -10.618  -6.410 -29.851  1.00 34.27           C
ANISOU 2267  CA  GLU A 288     3707   4393   4922    725    330    641       C
ATOM   2268  C   GLU A 288     -10.523  -7.065 -31.231  1.00 36.20           C
ANISOU 2268  C   GLU A 288     4058   4853   4843    859    550    477       C
ATOM   2269  O   GLU A 288     -10.790  -6.416 -32.238  1.00 37.41           O
ANISOU 2269  O   GLU A 288     4669   5414   4131    796    488    704       O
ATOM   2270  CB  GLU A 288      -9.195  -6.172 -29.356  1.00 35.47           C
ANISOU 2270  CB  GLU A 288     3921   4632   4924    273    188    337       C
ATOM   2271  CG  GLU A 288      -9.169  -5.347 -28.078  1.00 39.99           C
ANISOU 2271  CG  GLU A 288     4529   5240   5426    456    830    400       C
ATOM   2272  CD  GLU A 288      -9.595  -3.913 -28.207  1.00 46.09           C
ANISOU 2272  CD  GLU A 288     6003   5487   6021    983    816    195       C
ATOM   2273  OE1 GLU A 288      -9.470  -3.298 -29.279  1.00 49.92           O
ANISOU 2273  OE1 GLU A 288     6587   4873   7509    703   1185   1484       O
ATOM   2274  OE2 GLU A 288     -10.101  -3.442 -27.170  1.00 55.83           O
ANISOU 2274  OE2 GLU A 288     7190   7334   6688   1615    110    -67       O
ATOM   2275  N   ASN A 289     -10.255  -8.381 -31.248  1.00 33.41           N
ANISOU 2275  N   ASN A 289     3486   4398   4811    722    585    489       N
ATOM   2276  CA  ASN A 289     -10.164  -9.104 -32.503  1.00 32.68           C
ANISOU 2276  CA  ASN A 289     4238   3739   4440    635    623    717       C
ATOM   2277  C   ASN A 289     -11.487  -9.051 -33.259  1.00 34.53           C
ANISOU 2277  C   ASN A 289     4160   4622   4339    611    948    207       C
ATOM   2278  O   ASN A 289     -11.485  -8.802 -34.456  1.00 38.99           O
ANISOU 2278  O   ASN A 289     5693   4788   4332    364    500    104       O
ATOM   2279  CB  ASN A 289      -9.739 -10.554 -32.332  1.00 34.83           C
ANISOU 2279  CB  ASN A 289     4335   3824   5076    394    826    347       C
ATOM   2280  CG  ASN A 289      -8.286 -10.713 -31.993  1.00 36.11           C
ANISOU 2280  CG  ASN A 289     4041   4940   4737      7    821   1250       C
ATOM   2281  OD1 ASN A 289      -7.396 -10.246 -32.758  1.00 43.89           O
ANISOU 2281  OD1 ASN A 289     4998   5745   5932   -557   1032    919       O
ATOM   2282  ND2 ASN A 289      -8.048 -11.662 -31.098  1.00 42.93           N
ANISOU 2282  ND2 ASN A 289     4553   6739   5019    -89   1126   1006       N
ATOM   2283  N   VAL A 290     -12.604  -9.223 -32.533  1.00 39.73           N
ANISOU 2283  N   VAL A 290     4765   5904   4425    551    928    157       N
ATOM   2284  CA  VAL A 290     -13.923  -9.243 -33.137  1.00 37.02           C
ANISOU 2284  CA  VAL A 290     5007   4936   4124    367    744   -612       C
ATOM   2285  C   VAL A 290     -14.296  -7.863 -33.699  1.00 41.69           C
ANISOU 2285  C   VAL A 290     5964   5470   4405    599    393   -641       C
ATOM   2286  O   VAL A 290     -14.952  -7.755 -34.745  1.00 42.55           O
ANISOU 2286  O   VAL A 290     6294   5756   4117    439    510   -423       O
ATOM   2287  CB  VAL A 290     -14.968  -9.837 -32.175  1.00 35.24           C
ANISOU 2287  CB  VAL A 290     4393   4233   4761    460    223   -323       C
ATOM   2288  CG1 VAL A 290     -16.360  -9.572 -32.693  1.00 47.63           C
ANISOU 2288  CG1 VAL A 290     5761   5909   6427   -410   -216    498       C
ATOM   2289  CG2 VAL A 290     -14.834 -11.365 -31.982  1.00 45.19           C
ANISOU 2289  CG2 VAL A 290     5694   4545   6931   -763  -1904    101       C
ATOM   2290  N   GLY A 291     -13.882  -6.810 -32.990  1.00 35.18           N
ANISOU 2290  N   GLY A 291     4894   4259   4212    468   -209    295       N
ATOM   2291  CA  GLY A 291     -14.034  -5.415 -33.382  1.00 38.58           C
ANISOU 2291  CA  GLY A 291     4650   4932   5077    943   -132   1103       C
ATOM   2292  C   GLY A 291     -13.307  -5.141 -34.700  1.00 41.77           C
ANISOU 2292  C   GLY A 291     6086   5124   4660   1075    278    569       C
ATOM   2293  O   GLY A 291     -13.870  -4.546 -35.618  1.00 47.08           O
ANISOU 2293  O   GLY A 291     7758   5395   4734   1719    376    311       O
ATOM   2294  N   GLN A 292     -12.074  -5.652 -34.810  1.00 44.96           N
ANISOU 2294  N   GLN A 292     6371   5183   5530   1307    796    216       N
ATOM   2295  CA  GLN A 292     -11.239  -5.507 -35.996  1.00 48.72           C
ANISOU 2295  CA  GLN A 292     7250   4705   6559    506   1044   -241       C
ATOM   2296  C   GLN A 292     -11.751  -6.365 -37.160  1.00 54.31           C
ANISOU 2296  C   GLN A 292     6975   5593   8068    764   1215  -2355       C
ATOM   2297  O   GLN A 292     -11.719  -5.905 -38.289  1.00 53.94           O
ANISOU 2297  O   GLN A 292     8941   5238   6317    731  -1932   1249       O
ATOM   2298  CB  GLN A 292      -9.788  -5.777 -35.591  1.00 46.62           C
ANISOU 2298  CB  GLN A 292     7157   4260   6298    870   2908    241       C
ATOM   2299  CG  GLN A 292      -9.340  -4.728 -34.587  1.00 53.47           C
ANISOU 2299  CG  GLN A 292     7898   5874   6546   1110   2421    698       C
ATOM   2300  CD  GLN A 292      -7.862  -4.665 -34.373  1.00 57.00           C
ANISOU 2300  CD  GLN A 292     7856   6792   7008    964   4041   1361       C
ATOM   2301  OE1 GLN A 292      -7.207  -5.678 -34.110  1.00 65.73           O
ANISOU 2301  OE1 GLN A 292     9416   6364   9194   1865   3006   1150       O
ATOM   2302  NE2 GLN A 292      -7.332  -3.468 -34.575  1.00 69.43           N
ANISOU 2302  NE2 GLN A 292    10299   6778   9304    935   3431   1318       N
ATOM   2303  N   LEU A 293     -12.269  -7.573 -36.880  1.00 56.00           N
ANISOU 2303  N   LEU A 293     8315   5702   7261    944    -39  -1594       N
ATOM   2304  CA  LEU A 293     -12.847  -8.438 -37.900  1.00 54.18           C
ANISOU 2304  CA  LEU A 293     9782   5958   4846    799    896   -461       C
ATOM   2305  C   LEU A 293     -14.112  -7.800 -38.483  1.00 61.63           C
ANISOU 2305  C   LEU A 293    10420   7181   5815    461    836   -267       C
ATOM   2306  O   LEU A 293     -14.248  -7.786 -39.700  1.00 67.74           O
ANISOU 2306  O   LEU A 293    12664   8210   4865    299    669     31       O
ATOM   2307  CB  LEU A 293     -13.128  -9.845 -37.386  1.00 56.40           C
ANISOU 2307  CB  LEU A 293    10280   6451   4697     94   1405   -305       C
ATOM   2308  N   ASP A 294     -15.038  -7.300 -37.642  1.00 54.56           N
ANISOU 2308  N   ASP A 294    11067   5601   4063    931    998    -55       N
ATOM   2309  CA  ASP A 294     -16.014  -6.300 -38.061  1.00 59.81           C
ANISOU 2309  CA  ASP A 294    10433   7153   5139    864    826      0       C
ATOM   2310  C   ASP A 294     -15.121  -5.202 -38.639  1.00 64.30           C
ANISOU 2310  C   ASP A 294     9930   7802   6698   1225    913    771       C
ATOM   2311  O   ASP A 294     -13.907  -5.353 -38.603  1.00 88.30           O
ANISOU 2311  O   ASP A 294    11364  10775  11412    233    123    548       O
ATOM   2312  CB  ASP A 294     -16.932  -5.923 -36.892  1.00 57.98           C
ANISOU 2312  CB  ASP A 294     9256   5707   7065   -517   1367    684       C
ATOM   2313  CG  ASP A 294     -18.249  -5.163 -37.125  1.00 64.41           C
ANISOU 2313  CG  ASP A 294    10161   5811   8501  -1234     43    678       C
ATOM   2314  OD1 ASP A 294     -18.187  -3.930 -37.386  1.00 68.32           O
ANISOU 2314  OD1 ASP A 294    12181   5796   7980  -1216   -562    -51       O
ATOM   2315  OD2 ASP A 294     -19.373  -5.765 -36.881  1.00 65.31           O
ANISOU 2315  OD2 ASP A 294    10778   6904   7132   -919   -514   1224       O
ATOM   2316  N   PHE A 295     -15.637  -4.134 -39.231  1.00 69.59           N
ANISOU 2316  N   PHE A 295    11294   8657   6492   2083   1542   1004       N
ATOM   2317  CA  PHE A 295     -14.730  -3.058 -39.614  1.00 75.72           C
ANISOU 2317  CA  PHE A 295    11709   8688   8372   1459    377   1047       C
ATOM   2318  C   PHE A 295     -13.658  -3.526 -40.616  1.00 79.84           C
ANISOU 2318  C   PHE A 295    11611   9347   9377   1245   -531    207       C
ATOM   2319  O   PHE A 295     -12.806  -2.729 -41.001  1.00 76.92           O
ANISOU 2319  O   PHE A 295    12778  10150   6297   1349    843    239       O
ATOM   2320  CB  PHE A 295     -14.123  -2.459 -38.333  1.00 69.76           C
ANISOU 2320  CB  PHE A 295    11724   7764   7020   1984    158   1585       C
ATOM   2321  CG  PHE A 295     -14.774  -1.183 -37.803  1.00 79.71           C
ANISOU 2321  CG  PHE A 295    12362   9111   8815   2002   1525   -717       C
ATOM   2322  CD1 PHE A 295     -16.021  -0.749 -38.259  1.00 82.66           C
ANISOU 2322  CD1 PHE A 295    12213   9998   9197   1781   1659  -1099       C
ATOM   2323  CD2 PHE A 295     -14.115  -0.396 -36.858  1.00 86.54           C
ANISOU 2323  CD2 PHE A 295    12243  11644   8993   2358   1999  -1212       C
ATOM   2324  CE1 PHE A 295     -16.585   0.435 -37.789  1.00 90.62           C
ANISOU 2324  CE1 PHE A 295    13206  10660  10567   2342   1500   -841       C
ATOM   2325  CE2 PHE A 295     -14.682   0.789 -36.390  1.00 90.17           C
ANISOU 2325  CE2 PHE A 295    12983  11792   9486   1929   1956  -1170       C
ATOM   2326  CZ  PHE A 295     -15.920   1.197 -36.846  1.00 91.61           C
ANISOU 2326  CZ  PHE A 295    13672  10227  10910   3042   1542  -1097       C
ATOM   2327  N   LEU A 296     -13.663  -4.811 -41.005  1.00 78.06           N
ANISOU 2327  N   LEU A 296    11125   8206  10327   1085  -3616   -261       N
ATOM   2328  CA  LEU A 296     -12.907  -5.346 -42.139  1.00 74.94           C
ANISOU 2328  CA  LEU A 296    10694   8498   9283   -801  -4808   1244       C
ATOM   2329  C   LEU A 296     -11.402  -4.983 -42.092  1.00 93.33           C
ANISOU 2329  C   LEU A 296    14305   9557  11598   1489  -5971   2269       C
ATOM   2330  O   LEU A 296     -10.837  -4.528 -43.147  1.00 96.00           O
ANISOU 2330  O   LEU A 296    16081  10140  10254  -6141   2574   2699       O
ATOM   2331  CB  LEU A 296     -13.617  -4.882 -43.419  1.00 78.89           C
ANISOU 2331  CB  LEU A 296    10348  10426   9203   -511  -4580    244       C
ATOM   2332  CG  LEU A 296     -14.809  -5.725 -43.901  1.00 82.91           C
ANISOU 2332  CG  LEU A 296    10055  11775   9674    892  -4084     55       C
ATOM   2333  CD1 LEU A 296     -14.524  -7.228 -43.896  1.00 87.37           C
ANISOU 2333  CD1 LEU A 296    10582  12211  10402    951  -3971    660       C
ATOM   2334  CD2 LEU A 296     -16.080  -5.423 -43.121  1.00 83.23           C
ANISOU 2334  CD2 LEU A 296    10683  11780   9160   2011  -3734   -273       C
ATOM   2335  N   ALA A 297     -10.810  -5.242 -40.882  1.00 87.34           N
ANISOU 2335  N   ALA A 297    12996  13682   6507   1462  -2888   3063       N
ATOM   2336  CA  ALA A 297      -9.455  -4.860 -40.429  1.00 81.51           C
ANISOU 2336  CA  ALA A 297    13591  12008   5371    553  -2521   2511       C
ATOM   2337  C   ALA A 297      -8.526  -6.096 -40.424  1.00 69.59           C
ANISOU 2337  C   ALA A 297    11678   9554   5210   -384  -1731   1335       C
ATOM   2338  O   ALA A 297      -7.290  -6.168 -40.726  1.00 85.48           O
ANISOU 2338  O   ALA A 297    11821  11538   9120   1802  -3687    593       O
ATOM   2339  CB  ALA A 297      -9.634  -4.293 -39.012  1.00 83.80           C
ANISOU 2339  CB  ALA A 297    14105  10449   7287    851  -2375   1109       C
ATOM   2340  N   TYR A 298      -9.133  -7.218 -40.067  1.00 85.80           N
ANISOU 2340  N   TYR A 298    13285  11704   7613    123  -1795   -297       N
ATOM   2341  CA  TYR A 298      -8.361  -8.426 -39.894  1.00 75.08           C
ANISOU 2341  CA  TYR A 298    12620  11037   4871  -1926   -872  -1327       C
ATOM   2342  C   TYR A 298      -9.232  -9.555 -40.420  1.00 65.41           C
ANISOU 2342  C   TYR A 298    12519   8450   3884   -384   -180    423       C
ATOM   2343  O   TYR A 298     -10.456  -9.434 -40.435  1.00 61.43           O
ANISOU 2343  O   TYR A 298    11899   8691   2750     23    593   1098       O
ATOM   2344  N   ASN A 299      -8.569 -10.620 -40.869  1.00 67.45           N
ANISOU 2344  N   ASN A 299    14617   7310   3701   -148    867    -78       N
ATOM   2345  CA  ASN A 299      -9.235 -11.789 -41.402  1.00 75.48           C
ANISOU 2345  CA  ASN A 299    14986   7535   6159    181    589    975       C
ATOM   2346  C   ASN A 299      -8.969 -12.940 -40.438  1.00 76.44           C
ANISOU 2346  C   ASN A 299    15115   6692   7237   -480    580   1586       C
ATOM   2347  O   ASN A 299      -7.944 -12.954 -39.755  1.00 86.68           O
ANISOU 2347  O   ASN A 299    15995   8170   8768  -1109    786   1732       O
ATOM   2348  CB  ASN A 299      -8.754 -12.159 -42.806  1.00 74.65           C
ANISOU 2348  CB  ASN A 299    14825   7199   6338   1118    880     33       C
ATOM   2349  CG  ASN A 299      -8.032 -11.061 -43.565  1.00 77.86           C
ANISOU 2349  CG  ASN A 299    14250   8925   6409    772   1489   -965       C
ATOM   2350  OD1 ASN A 299      -7.973  -9.905 -43.134  1.00 84.16           O
ANISOU 2350  OD1 ASN A 299    13428  10638   7910   1099   1775  -2197       O
ATOM   2351  ND2 ASN A 299      -7.457 -11.409 -44.709  1.00 81.62           N
ANISOU 2351  ND2 ASN A 299    13583  10606   6824    309   2290     33       N
ATOM   2352  N   GLN A 300      -9.897 -13.897 -40.391  1.00 78.17           N
ANISOU 2352  N   GLN A 300    14334   7602   7766   -486   -220   1873       N
ATOM   2353  CA  GLN A 300      -9.689 -15.114 -39.618  1.00 75.50           C
ANISOU 2353  CA  GLN A 300    13677   6355   8655    774   -530    844       C
ATOM   2354  C   GLN A 300      -9.423 -16.278 -40.569  1.00 77.91           C
ANISOU 2354  C   GLN A 300    12613   8830   8158    595    -55    253       C
ATOM   2355  O   GLN A 300     -10.234 -16.588 -41.439  1.00 79.66           O
ANISOU 2355  O   GLN A 300    12010  10166   8092  -1213    466   -386       O
ATOM   2356  CB  GLN A 300     -10.787 -15.553 -38.642  1.00 81.13           C
ANISOU 2356  CB  GLN A 300    13096   8230   9499    382   -770   -182       C
ATOM   2357  CG  GLN A 300     -12.122 -14.821 -38.745  1.00 82.10           C
ANISOU 2357  CG  GLN A 300    13523   7383  10289    491  -1073    602       C
ATOM   2358  CD  GLN A 300     -12.343 -13.872 -37.594  1.00 79.68           C
ANISOU 2358  CD  GLN A 300    12941   8083   9252    274  -1476    194       C
ATOM   2359  OE1 GLN A 300     -13.283 -14.022 -36.804  1.00 84.65           O
ANISOU 2359  OE1 GLN A 300    12020   9775  10369   -354  -1622   1543       O
ATOM   2360  NE2 GLN A 300     -11.456 -12.899 -37.478  1.00 88.18           N
ANISOU 2360  NE2 GLN A 300    13009   9507  10987   -217  -1344    863       N
ATOM   2361  N   GLN A 301      -8.271 -16.924 -40.371  1.00 73.22           N
ANISOU 2361  N   GLN A 301    13018   5980   8822   1426    684    -60       N
ATOM   2362  CA  GLN A 301      -7.955 -18.189 -41.010  1.00 74.60           C
ANISOU 2362  CA  GLN A 301    13483   6796   8063    765    598   -162       C
ATOM   2363  C   GLN A 301      -8.674 -19.279 -40.226  1.00 76.74           C
ANISOU 2363  C   GLN A 301    13857   6363   8937   1058     92    634       C
ATOM   2364  O   GLN A 301      -8.091 -19.947 -39.363  1.00 79.38           O
ANISOU 2364  O   GLN A 301    13474   7292   9396    968   1550   2433       O
ATOM   2365  CB  GLN A 301      -6.447 -18.432 -41.076  1.00 73.29           C
ANISOU 2365  CB  GLN A 301    13431   7617   6800   1164    313     80       C
ATOM   2366  N   VAL A 302      -9.979 -19.391 -40.496  1.00 80.82           N
ANISOU 2366  N   VAL A 302    14958   7183   8567    276   -222    186       N
ATOM   2367  CA  VAL A 302     -10.781 -20.474 -39.957  1.00 70.48           C
ANISOU 2367  CA  VAL A 302    14671   5843   6265    -20   -684   -182       C
ATOM   2368  C   VAL A 302     -10.443 -21.711 -40.790  1.00 75.37           C
ANISOU 2368  C   VAL A 302    15346   6712   6577    889   -477   -193       C
ATOM   2369  O   VAL A 302     -10.089 -21.586 -41.965  1.00 83.06           O
ANISOU 2369  O   VAL A 302    15687   7746   8126    506   1968   -985       O
ATOM   2370  CB  VAL A 302     -12.285 -20.129 -39.986  1.00 66.12           C
ANISOU 2370  CB  VAL A 302    14327   5043   5753    428   -462   -697       C
ATOM   2371  CG1 VAL A 302     -13.111 -21.122 -39.185  1.00 69.88           C
ANISOU 2371  CG1 VAL A 302    14264   6937   5351    629   -576   -158       C
ATOM   2372  CG2 VAL A 302     -12.576 -18.715 -39.491  1.00 64.66           C
ANISOU 2372  CG2 VAL A 302    14246   4215   6108   -411   -857   -109       C
ATOM   2373  N   MET A 303     -10.520 -22.900 -40.183  1.00 73.44           N
ANISOU 2373  N   MET A 303    15031   5400   7472    957   -519   -660       N
ATOM   2374  CA  MET A 303     -10.116 -24.119 -40.870  1.00 79.45           C
ANISOU 2374  CA  MET A 303    14447   6157   9583    157    -32  -1179       C
ATOM   2375  C   MET A 303      -9.724 -25.203 -39.870  1.00 81.69           C
ANISOU 2375  C   MET A 303    13247   6778  11016   -946    -34  -1158       C
ATOM   2376  O   MET A 303     -10.281 -26.299 -39.918  1.00 88.64           O
ANISOU 2376  O   MET A 303    14388   7124  12169  -1920   -347  -2292       O
ATOM   2377  CB  MET A 303      -8.911 -23.889 -41.793  1.00 78.75           C
ANISOU 2377  CB  MET A 303    14417   5592   9910    436   -157  -1091       C
ATOM   2378  N   ILE A 304      -8.734 -24.903 -39.013  1.00 71.97           N
ANISOU 2378  N   ILE A 304    11275   6204   9867   -968   1112  -2994       N
ATOM   2379  CA  ILE A 304      -8.138 -25.903 -38.141  1.00 71.80           C
ANISOU 2379  CA  ILE A 304     9192   7687  10400  -1399    440  -2069       C
ATOM   2380  C   ILE A 304      -9.165 -26.316 -37.092  1.00 74.93           C
ANISOU 2380  C   ILE A 304     9369   8844  10256   -690    398  -2658       C
ATOM   2381  O   ILE A 304      -9.527 -27.488 -36.990  1.00 91.62           O
ANISOU 2381  O   ILE A 304    12079  10626  12105  -1894     86   -913       O
ATOM   2382  CB  ILE A 304      -6.848 -25.382 -37.480  1.00 71.80           C
ANISOU 2382  CB  ILE A 304     8765   6908  11606  -2217    779  -2124       C
ATOM   2383  N   ASP A 305      -9.640 -25.305 -36.365  1.00 56.10           N
ANISOU 2383  N   ASP A 305     4737   8747   7832   -687    -76  -3079       N
ATOM   2384  CA  ASP A 305     -10.479 -25.412 -35.171  1.00 57.80           C
ANISOU 2384  CA  ASP A 305     6171   7914   7875    126   -711  -1735       C
ATOM   2385  C   ASP A 305     -10.014 -24.305 -34.246  1.00 43.01           C
ANISOU 2385  C   ASP A 305     4179   5982   6179   1926   -923  -1040       C
ATOM   2386  O   ASP A 305     -10.830 -23.534 -33.714  1.00 48.22           O
ANISOU 2386  O   ASP A 305     4519   7189   6615   1187    408  -1130       O
ATOM   2387  CB  ASP A 305     -10.397 -26.725 -34.401  1.00 60.12           C
ANISOU 2387  CB  ASP A 305     5666   8491   8687    -45  -1094  -1975       C
ATOM   2388  CG  ASP A 305     -11.546 -27.700 -34.615  1.00 64.31           C
ANISOU 2388  CG  ASP A 305     6277   8186   9971   -131  -1364  -2665       C
ATOM   2389  OD1 ASP A 305     -12.701 -27.237 -34.680  1.00 72.36           O
ANISOU 2389  OD1 ASP A 305     6486   9490  11517   1197   -731  -2767       O
ATOM   2390  OD2 ASP A 305     -11.280 -28.920 -34.645  1.00 75.24           O
ANISOU 2390  OD2 ASP A 305     8577   8550  11460    226  -1103  -3429       O
ATOM   2391  N   LYS A 306      -8.688 -24.247 -34.092  1.00 46.89           N
ANISOU 2391  N   LYS A 306     5343   5684   6790   1300    435   -718       N
ATOM   2392  CA  LYS A 306      -8.041 -23.069 -33.550  1.00 42.76           C
ANISOU 2392  CA  LYS A 306     4986   6162   5099   1325    670   -176       C
ATOM   2393  C   LYS A 306      -7.973 -22.028 -34.662  1.00 46.20           C
ANISOU 2393  C   LYS A 306     5389   6327   5837   1517   1142    106       C
ATOM   2394  O   LYS A 306      -7.175 -22.170 -35.587  1.00 44.23           O
ANISOU 2394  O   LYS A 306     5428   6051   5325   2374   1617   -704       O
ATOM   2395  CB  LYS A 306      -6.676 -23.376 -32.946  1.00 42.16           C
ANISOU 2395  CB  LYS A 306     4502   6239   5276   1285    970   -193       C
ATOM   2396  CG  LYS A 306      -6.757 -24.391 -31.818  1.00 45.60           C
ANISOU 2396  CG  LYS A 306     4917   6573   5837    810   1299   -600       C
ATOM   2397  CD  LYS A 306      -6.600 -25.871 -32.157  1.00 47.91           C
ANISOU 2397  CD  LYS A 306     4055   6328   7821    879    426   -257       C
ATOM   2398  CE  LYS A 306      -7.315 -26.701 -31.136  1.00 51.99           C
ANISOU 2398  CE  LYS A 306     5219   7362   7171   1257   1948   -983       C
ATOM   2399  NZ  LYS A 306      -7.843 -25.993 -29.950  1.00 61.61           N
ANISOU 2399  NZ  LYS A 306     6074   8403   8932    426   1284  -1018       N
ATOM   2400  N   SER A 307      -8.835 -21.002 -34.557  1.00 42.90           N
ANISOU 2400  N   SER A 307     5185   5713   5402   2034   1182    -44       N
ATOM   2401  CA  SER A 307      -8.880 -19.929 -35.535  1.00 42.15           C
ANISOU 2401  CA  SER A 307     5549   4923   5544   1567   1319    -37       C
ATOM   2402  C   SER A 307      -7.541 -19.192 -35.531  1.00 46.85           C
ANISOU 2402  C   SER A 307     6553   5615   5633   1772   1118    548       C
ATOM   2403  O   SER A 307      -6.907 -19.002 -34.483  1.00 45.19           O
ANISOU 2403  O   SER A 307     5663   5910   5596   1616   1934    942       O
ATOM   2404  CB  SER A 307     -10.080 -18.987 -35.295  1.00 44.05           C
ANISOU 2404  CB  SER A 307     6038   5454   5246   2206   1043   1024       C
ATOM   2405  OG  SER A 307     -11.326 -19.680 -35.391  1.00 57.30           O
ANISOU 2405  OG  SER A 307     7772   8936   5065   1021   2171    524       O
ATOM   2406  N   SER A 308      -7.096 -18.781 -36.723  1.00 48.72           N
ANISOU 2406  N   SER A 308     7155   5949   5407   1514   2082   -529       N
ATOM   2407  CA ASER A 308      -5.883 -17.992 -36.848  0.50 47.71           C
ANISOU 2407  CA ASER A 308     7023   5460   5647   1271   2316   -781       C
ATOM   2408  CA BSER A 308      -5.886 -17.989 -36.841  0.50 50.31           C
ANISOU 2408  CA BSER A 308     7657   5436   6022   1202   2007   -530       C
ATOM   2409  C   SER A 308      -6.237 -16.607 -37.384  1.00 52.04           C
ANISOU 2409  C   SER A 308     8433   5521   5821    334   1716   -464       C
ATOM   2410  O   SER A 308      -6.929 -16.479 -38.394  1.00 53.99           O
ANISOU 2410  O   SER A 308     9833   5688   4991    755   1344  -1260       O
ATOM   2411  CB ASER A 308      -4.853 -18.689 -37.722  0.50 50.91           C
ANISOU 2411  CB ASER A 308     6699   5907   6737   1114   2743   -983       C
ATOM   2412  CB BSER A 308      -4.851 -18.705 -37.684  0.50 54.08           C
ANISOU 2412  CB BSER A 308     7826   5633   7089   1504   2306   -721       C
ATOM   2413  OG ASER A 308      -3.681 -17.894 -37.844  0.50 49.32           O
ANISOU 2413  OG ASER A 308     5975   5674   7091   1091   2886   -520       O
ATOM   2414  OG BSER A 308      -4.241 -19.738 -36.915  0.50 50.40           O
ANISOU 2414  OG BSER A 308     7199   4753   7199   2011   2959   -714       O
ATOM   2415  N   LYS A 309      -5.783 -15.564 -36.684  1.00 50.80           N
ANISOU 2415  N   LYS A 309     8932   4991   5377    270   1403   -481       N
ATOM   2416  CA ALYS A 309      -6.091 -14.208 -37.106  0.50 52.52           C
ANISOU 2416  CA ALYS A 309     8511   5050   6395    962   1332   -726       C
ATOM   2417  CA BLYS A 309      -6.083 -14.201 -37.093  0.50 52.25           C
ANISOU 2417  CA BLYS A 309     8728   5099   6026    848   1070   -840       C
ATOM   2418  C   LYS A 309      -4.941 -13.662 -37.976  1.00 51.09           C
ANISOU 2418  C   LYS A 309     8069   5120   6224   1141   1990  -1962       C
ATOM   2419  O   LYS A 309      -3.759 -13.777 -37.537  1.00 54.69           O
ANISOU 2419  O   LYS A 309     8359   6603   5818    479   2350   -747       O
ATOM   2420  CB ALYS A 309      -6.461 -13.356 -35.884  0.50 49.41           C
ANISOU 2420  CB ALYS A 309     8010   4835   5930   1103   1138   -370       C
ATOM   2421  CB BLYS A 309      -6.325 -13.312 -35.865  0.50 50.02           C
ANISOU 2421  CB BLYS A 309     8681   5132   5193    890    324   -661       C
ATOM   2422  CG ALYS A 309      -7.834 -13.661 -35.274  0.50 48.07           C
ANISOU 2422  CG ALYS A 309     7378   5032   5855   1479   1049   -212       C
ATOM   2423  CG BLYS A 309      -7.496 -13.681 -34.949  0.50 47.88           C
ANISOU 2423  CG BLYS A 309     8063   5392   4735   1193    -13   -653       C
ATOM   2424  CD ALYS A 309      -7.852 -14.679 -34.130  0.50 44.97           C
ANISOU 2424  CD ALYS A 309     6606   4882   5600   1678    786   -252       C
ATOM   2425  CD BLYS A 309      -8.869 -13.103 -35.298  0.50 43.71           C
ANISOU 2425  CD BLYS A 309     8177   5078   3351   1148   -837   -602       C
ATOM   2426  CE ALYS A 309      -9.204 -15.277 -33.795  0.50 48.14           C
ANISOU 2426  CE ALYS A 309     6921   5189   6182   1920    626    156       C
ATOM   2427  CE BLYS A 309      -9.923 -13.572 -34.324  0.50 45.67           C
ANISOU 2427  CE BLYS A 309     8473   5094   3786   1556   -456   -768       C
ATOM   2428  NZ ALYS A 309     -10.371 -14.393 -33.607  0.50 45.72           N
ANISOU 2428  NZ ALYS A 309     6527   4594   6251   2789    358      5       N
ATOM   2429  NZ BLYS A 309      -9.539 -14.767 -33.557  0.50 51.70           N
ANISOU 2429  NZ BLYS A 309    10317   5396   3930    458   -500   -110       N
TER    2430      LYS A 309
HETATM 2431 ZN   ZN  A 466     -20.015  -6.504 -14.504  1.00 24.60          Zn
ANISOU 2431 ZN   ZN  A 466     3016   3133   3197    133   -121    171      Zn
HETATM 2432 ZN   ZN  A 467     -19.253  -5.732 -11.469  1.00 23.80          Zn
ANISOU 2432 ZN   ZN  A 467     2798   3009   3235   -142   -217    152      Zn
HETATM 2433  O   HOH A 501     -19.800  -7.403 -12.519  1.00 26.60           O
ANISOU 2433  O   HOH A 501     3363   3525   3219    238   -848   -284       O
HETATM 2434  O   HOH A 502     -36.477  -1.793  13.149  1.00 40.83           O
ANISOU 2434  O   HOH A 502     4858   4149   6508  -1495     98  -3064       O
HETATM 2435  O   HOH A 503     -17.655 -16.545   1.650  1.00 23.57           O
ANISOU 2435  O   HOH A 503     3100   2616   3240    449   -401    280       O
HETATM 2436  O   HOH A 504     -33.524 -14.416 -25.862  1.00 49.42           O
ANISOU 2436  O   HOH A 504     4554   7273   6951    783   -443    984       O
HETATM 2437  O   HOH A 505     -39.475  -7.685   1.700  1.00 38.51           O
ANISOU 2437  O   HOH A 505     5272   4136   5223   -167   -288   -520       O
HETATM 2438  O   HOH A 506     -29.871 -25.292 -13.876  1.00 43.37           O
ANISOU 2438  O   HOH A 506     5599   3896   6985    -58    315    651       O
HETATM 2439  O   HOH A 507     -20.858   3.005 -14.266  1.00 27.96           O
ANISOU 2439  O   HOH A 507     3907   2980   3736   -538   -203    195       O
HETATM 2440  O   HOH A 508     -34.959   7.005 -22.102  1.00 39.61           O
ANISOU 2440  O   HOH A 508     4461   3304   7285    863    266     81       O
HETATM 2441  O   HOH A 509     -30.292  -3.473 -24.209  1.00 33.92           O
ANISOU 2441  O   HOH A 509     4542   4322   4022   1094  -1017   -804       O
HETATM 2442  O   HOH A 510     -36.765   4.089   5.487  1.00 40.80           O
ANISOU 2442  O   HOH A 510     5489   5837   4175   1657   -461   -997       O
HETATM 2443  O   HOH A 511     -28.270 -27.780 -17.976  1.00 49.99           O
ANISOU 2443  O   HOH A 511     5737   5481   7774    518    717   -803       O
HETATM 2444  O   HOH A 512     -23.486 -18.596  -0.034  1.00 46.49           O
ANISOU 2444  O   HOH A 512     4140   7836   5688   -308     98  -1848       O
HETATM 2445  O   HOH A 513     -30.666 -21.953 -30.876  1.00 82.17           O
ANISOU 2445  O   HOH A 513    10986   8105  12129  -2923  -3546    516       O
HETATM 2446  O   HOH A 514     -19.728  14.367 -15.660  1.00 42.75           O
ANISOU 2446  O   HOH A 514     5333   5000   5911   -567    180   -577       O
HETATM 2447  O   HOH A 515     -28.640 -15.948  -3.827  1.00 25.45           O
ANISOU 2447  O   HOH A 515     3081   2751   3839   -240   -101    300       O
HETATM 2448  O   HOH A 516     -36.809   3.086  -2.861  1.00 26.78           O
ANISOU 2448  O   HOH A 516     3599   3301   3276    582    244   -104       O
HETATM 2449  O   HOH A 517     -40.322   2.900 -22.020  1.00 46.03           O
ANISOU 2449  O   HOH A 517     4917   6257   6315    530  -1156    787       O
HETATM 2450  O   HOH A 518     -27.674  10.312 -27.418  1.00 62.50           O
ANISOU 2450  O   HOH A 518    12106   5375   6265    598  -1142    595       O
HETATM 2451  O   HOH A 519     -12.893   1.066 -22.596  1.00 47.87           O
ANISOU 2451  O   HOH A 519     5965   6161   6064  -1724    341    685       O
HETATM 2452  O   HOH A 520     -43.856   5.446  -8.259  1.00 51.14           O
ANISOU 2452  O   HOH A 520     5186   5632   8612    959    149    418       O
HETATM 2453  O   HOH A 521     -28.681  -6.358 -25.145  1.00 47.57           O
ANISOU 2453  O   HOH A 521     8909   5425   3739     88  -1134    700       O
HETATM 2454  O   HOH A 522     -19.064   5.064  -7.268  1.00 32.68           O
ANISOU 2454  O   HOH A 522     3894   4160   4361  -1025   -857    286       O
HETATM 2455  O   HOH A 523     -40.396 -14.919   2.116  1.00 46.62           O
ANISOU 2455  O   HOH A 523     5885   6058   5770  -1488    950   3009       O
HETATM 2456  O   HOH A 524     -24.000   0.569   7.324  1.00 38.35           O
ANISOU 2456  O   HOH A 524     4878   3076   6619   -709    415     59       O
HETATM 2457  O   HOH A 525     -39.778 -12.215  -5.665  1.00 28.36           O
ANISOU 2457  O   HOH A 525     3604   3625   3547   -171    180    167       O
HETATM 2458  O   HOH A 526     -36.215  -8.792   1.163  1.00 24.54           O
ANISOU 2458  O   HOH A 526     3067   2897   3361   -256    -45   -182       O
HETATM 2459  O   HOH A 527     -37.466   6.299  -4.037  1.00 39.31           O
ANISOU 2459  O   HOH A 527     4573   5034   5327   -286   -172  -1004       O
HETATM 2460  O   HOH A 528     -17.378 -12.576  -1.158  1.00 26.50           O
ANISOU 2460  O   HOH A 528     3689   2948   3432   -435   -141    426       O
HETATM 2461  O   HOH A 529     -30.347 -18.809 -24.518  1.00 43.89           O
ANISOU 2461  O   HOH A 529     5744   5059   5873   -784  -1263    821       O
HETATM 2462  O   HOH A 530     -16.615  -3.924   2.608  1.00 44.27           O
ANISOU 2462  O   HOH A 530     4901   6036   5882   -656  -1636    195       O
HETATM 2463  O   HOH A 531     -38.391 -13.684  -7.586  1.00 26.20           O
ANISOU 2463  O   HOH A 531     3265   3566   3125   -329    116     66       O
HETATM 2464  O   HOH A 532     -28.474  -3.637 -22.216  1.00 24.44           O
ANISOU 2464  O   HOH A 532     3450   2831   3005     -2   -536    132       O
HETATM 2465  O   HOH A 533     -30.473  -2.428  13.513  1.00 40.96           O
ANISOU 2465  O   HOH A 533     4748   5016   5799   -990   1236  -1322       O
HETATM 2466  O   HOH A 534     -24.072  -0.964  -8.527  1.00 24.15           O
ANISOU 2466  O   HOH A 534     3383   2667   3124   -331   -477    317       O
HETATM 2467  O   HOH A 535     -24.105   1.408  -9.937  1.00 24.69           O
ANISOU 2467  O   HOH A 535     3492   2694   3197     96   -331     88       O
HETATM 2468  O   HOH A 536      -4.374   1.256 -24.904  1.00 49.63           O
ANISOU 2468  O   HOH A 536     5314   6930   6614   1086    359    216       O
HETATM 2469  O   HOH A 537     -39.361  -4.776 -20.534  1.00 28.21           O
ANISOU 2469  O   HOH A 537     3784   3685   3248    411   -743    379       O
HETATM 2470  O   HOH A 538     -16.151  -6.862 -29.665  1.00 37.12           O
ANISOU 2470  O   HOH A 538     3889   4740   5474   1027   -554   -515       O
HETATM 2471  O   HOH A 539     -24.093  -3.856  12.172  1.00 36.97           O
ANISOU 2471  O   HOH A 539     5205   4980   3862   1065  -1072   -651       O
HETATM 2472  O   HOH A 540     -18.281 -10.596   5.587  1.00 27.42           O
ANISOU 2472  O   HOH A 540     3144   3581   3693   -102   -797   -121       O
HETATM 2473  O   HOH A 541     -44.030  -8.106 -14.413  1.00 38.48           O
ANISOU 2473  O   HOH A 541     3016   6084   5521    -13   -815   1740       O
HETATM 2474  O   HOH A 542     -34.456   9.934  -5.773  1.00 32.71           O
ANISOU 2474  O   HOH A 542     4857   3595   3975    690    454   -180       O
HETATM 2475  O   HOH A 543     -35.381 -12.061   3.512  1.00 39.05           O
ANISOU 2475  O   HOH A 543     5619   5002   4217    840    477     24       O
HETATM 2476  O   HOH A 544     -35.734  13.255 -11.835  1.00 34.77           O
ANISOU 2476  O   HOH A 544     5248   3193   4768    882     -1   -399       O
HETATM 2477  O   HOH A 545     -24.497 -11.047 -25.890  1.00 38.07           O
ANISOU 2477  O   HOH A 545     4775   5414   4275   1119    438   -444       O
HETATM 2478  O   HOH A 546     -21.843  -1.101 -20.958  1.00 24.40           O
ANISOU 2478  O   HOH A 546     2961   3082   3227    -69     11    198       O
HETATM 2479  O   HOH A 547     -37.740   3.287   3.123  1.00 33.23           O
ANISOU 2479  O   HOH A 547     4361   3879   4387    -66    246   -359       O
HETATM 2480  O   HOH A 548     -39.689  -1.075   2.193  1.00 37.59           O
ANISOU 2480  O   HOH A 548     5591   4272   4419   -932   1369   -282       O
HETATM 2481  O   HOH A 549     -20.396  11.658 -27.067  1.00 50.73           O
ANISOU 2481  O   HOH A 549     9525   4477   5272     44    166   2107       O
HETATM 2482  O   HOH A 550     -20.211 -11.358 -26.094  1.00 42.18           O
ANISOU 2482  O   HOH A 550     5002   5994   5029   1113    177    768       O
HETATM 2483  O   HOH A 551     -14.589  -1.603  -6.126  1.00 41.79           O
ANISOU 2483  O   HOH A 551     4850   4910   6119   -643  -1304    773       O
HETATM 2484  O   HOH A 552      -4.543 -29.983 -27.082  1.00 46.07           O
ANISOU 2484  O   HOH A 552     4718   5361   7427    108   -425    500       O
HETATM 2485  O   HOH A 553     -40.685  -1.179  -7.274  1.00 30.35           O
ANISOU 2485  O   HOH A 553     3218   4045   4269     65   -255     90       O
HETATM 2486  O   HOH A 554     -24.491  15.353  -8.337  1.00 42.64           O
ANISOU 2486  O   HOH A 554     6642   4693   4864   -658   -609   -254       O
HETATM 2487  O   HOH A 555     -13.543   7.963 -10.544  1.00 50.97           O
ANISOU 2487  O   HOH A 555     4255   8149   6961   -450    192    920       O
HETATM 2488  O   HOH A 556     -20.865 -13.380 -13.597  1.00 39.88           O
ANISOU 2488  O   HOH A 556     6043   5338   3770   2297    368     81       O
HETATM 2489  O   HOH A 557     -23.338 -28.685 -22.556  1.00 57.68           O
ANISOU 2489  O   HOH A 557     6671   6130   9114   -728   2049   -714       O
HETATM 2490  O   HOH A 558      -6.497 -20.874 -41.645  1.00 64.13           O
ANISOU 2490  O   HOH A 558    10451   6583   7331   2798    504  -1170       O
HETATM 2491  O   HOH A 559     -15.476 -15.476  -0.000  0.50 27.98           O
ANISOU 2491  O   HOH A 559     2896   2896   4840   -370    327   -327       O
HETATM 2492  O   HOH A 560     -31.567  14.191  -3.599  1.00 51.59           O
ANISOU 2492  O   HOH A 560     6453   7824   5324   1447    165   -115       O
HETATM 2493  O   HOH A 561     -24.969 -20.876  -7.977  1.00 45.70           O
ANISOU 2493  O   HOH A 561     4813   4578   7971    273  -1231   1036       O
HETATM 2494  O   HOH A 562     -27.108 -17.079   1.062  1.00 37.24           O
ANISOU 2494  O   HOH A 562     5144   4154   4852    -68   -112   -484       O
HETATM 2495  O   HOH A 563     -19.137  -5.341   6.043  1.00 38.98           O
ANISOU 2495  O   HOH A 563     5461   5109   4239   -225   -703   -555       O
HETATM 2496  O   HOH A 564     -26.150  17.405 -14.453  1.00 51.14           O
ANISOU 2496  O   HOH A 564     9093   4605   5734   1323    670    511       O
HETATM 2497  O   HOH A 565     -36.553   7.938  -6.480  1.00 27.65           O
ANISOU 2497  O   HOH A 565     3873   3065   3566    253     23    -35       O
HETATM 2498  O   HOH A 566     -37.466 -13.348   4.328  1.00 51.05           O
ANISOU 2498  O   HOH A 566     6140   7773   5482   -774   1009    507       O
HETATM 2499  O   HOH A 567     -19.020  -8.907   7.571  1.00 37.55           O
ANISOU 2499  O   HOH A 567     4659   4988   4621    451  -1040   -968       O
HETATM 2500  O   HOH A 568     -39.334   1.140   4.027  1.00 41.87           O
ANISOU 2500  O   HOH A 568     5276   5683   4951   1289    395     21       O
HETATM 2501  O   HOH A 569     -17.852  -1.745   6.171  1.00 61.33           O
ANISOU 2501  O   HOH A 569     8145   5791   9366    -31  -1073   1191       O
HETATM 2502  O   HOH A 570     -17.744  10.789 -26.759  1.00 46.70           O
ANISOU 2502  O   HOH A 570     5948   5313   6483    640    315   1605       O
HETATM 2503  O   HOH A 571     -39.468 -16.086  -7.364  1.00 39.39           O
ANISOU 2503  O   HOH A 571     4638   4286   6041   -298      0  -1061       O
HETATM 2504  O   HOH A 572     -16.679  -9.583 -29.028  1.00 43.06           O
ANISOU 2504  O   HOH A 572     5078   5628   5655   1085    489    682       O
HETATM 2505  O   HOH A 573     -38.381  -0.572   6.086  1.00 48.75           O
ANISOU 2505  O   HOH A 573     7484   5684   5354      5   -273  -1548       O
HETATM 2506  O   HOH A 574     -41.944  -6.541   1.768  1.00 65.35           O
ANISOU 2506  O   HOH A 574     7297  10113   7420   2558  -1112  -2352       O
HETATM 2507  O   HOH A 575     -42.012  -2.247   1.983  1.00 43.08           O
ANISOU 2507  O   HOH A 575     4229   5196   6941   -150    103   -161       O
HETATM 2508  O   HOH A 576     -16.698  -6.169   4.700  1.00 44.60           O
ANISOU 2508  O   HOH A 576     5955   4865   6125    111  -1115   -404       O
HETATM 2509  O   HOH A 577      -2.745  -0.414 -44.815  1.00102.99           O
ANISOU 2509  O   HOH A 577    10971  11525  16635  -2703   1151  -4430       O
HETATM 2510  O   HOH A 578     -17.071 -12.917   6.847  1.00 35.78           O
ANISOU 2510  O   HOH A 578     6134   2891   4572   -186  -1821    524       O
HETATM 2511  O   HOH A 579     -18.501   8.193   2.214  1.00 51.76           O
ANISOU 2511  O   HOH A 579     5337   7667   6661   -218    323  -1671       O
CONECT  504 2431
CONECT  521 2431
CONECT  537 2432
CONECT  547 2432
CONECT 1319 2431
CONECT 1459 2431 2432
CONECT 1838 2432
CONECT 2431 1459  504  521 1319
CONECT 2432 1838 1459  537  547
END



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