Dataset | 2vcs.pdb

Galaxy Dataset ' 2vcs.pdb'


HEADER    OXIDOREDUCTASE                          26-SEP-07   2VCS              
TITLE     STRUCTURE OF ISONIAZID (INH) BOUND TO CYTOSOLIC SOYBEAN               
TITLE    2 ASCORBATE PEROXIDASE MUTANT H42A                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASCORBATE PEROXIDASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 2-250;                                            
COMPND   5 SYNONYM: CYTOSOLIC ASCORBATE PEROXIDASE 1;                           
COMPND   6 EC: 1.11.1.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GLYCINE MAX;                                    
SOURCE   3 ORGANISM_COMMON: SOYBEAN;                                            
SOURCE   4 ORGANISM_TAXID: 3847;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SG13009;                                   
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: SAPX6                                     
KEYWDS    ASCORBATE PEROXIDASE, PEROXIDASE, INH, APX, ISONIAZID,                
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.L.METCALFE,I.K.MACDONALD,K.A.BROWN,E.L.RAVEN,P.C.E.MOODY            
REVDAT   3   24-FEB-09 2VCS    1       VERSN                                    
REVDAT   2   11-MAR-08 2VCS    1       JRNL   REMARK FORMUL HETATM              
REVDAT   2 2                           CONECT MASTER                            
REVDAT   1   04-DEC-07 2VCS    0                                                
JRNL        AUTH   C.L.METCALFE,I.K.MACDONALD,E.J.MURPHY,K.A.BROWN,             
JRNL        AUTH 2 E.L.RAVEN,P.C.E.MOODY                                        
JRNL        TITL   THE TUBERCULOSIS PRODRUG ISONIAZID BOUND TO                  
JRNL        TITL 2 ACTIVATING PEROXIDASES.                                      
JRNL        REF    J.BIOL.CHEM.                  V. 283  6193 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18056997                                                     
JRNL        DOI    10.1074/JBC.M707412200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23523                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1260                            
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) : 1.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.73                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 314                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 13                           
REMARK   3   BIN FREE R VALUE                    : 0.5490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1946                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 299                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.12000                                              
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): 0.223         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.063         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.600         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2079 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2844 ; 1.179 ; 2.055       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   263 ; 5.242 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;37.374 ;24.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   324 ;12.844 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;20.063 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   289 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1643 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1110 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1430 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   229 ; 0.238 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    63 ; 0.277 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    42 ; 0.556 ; 0.200       
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):  1295 ; 1.025 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2032 ; 1.546 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   877 ; 2.512 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   803 ; 3.580 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VCS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33978.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU2HB                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : XENOCS MULTI-LAYER                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24816                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.68                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.62                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY                : 4.18                               
REMARK 200  R MERGE                    (I) : 0.03                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 26.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.21                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OAF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5M LISO4, PH 8.3                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.86750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.86750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.46850            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.86750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.86750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       37.46850            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.86750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.86750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.46850            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.86750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.86750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.46850            
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        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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      HOH A2057  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2100  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, HIS 42 TO ALA                         
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     MET A   -10                                                      
REMARK 465     ARG A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2064  -  O    HOH A  2297              2.09            
REMARK 500   O    HOH A  2228  -  O    HOH A  2230              1.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                                                                      
REMARK 500   O    HOH A  2015     O    HOH A  2208     6565      1.75           
REMARK 500   O    HOH A  2036     O    HOH A  2231     8666      2.19           
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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 172      -85.40   -102.13                                   
REMARK 500    ASP A 249       94.45     85.36                                   
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 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ISZ A 1252                                                       
REMARK 610     ISZ A 1253                                                       
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                             HEM A1251  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM A1251   NB                                                     
REMARK 620 2 HIS A 163   NE2  96.3                                              
REMARK 620 3 HEM A1251   NA   87.3  95.9                                        
REMARK 620 4 HEM A1251   NC   92.0  92.1 172.0                                  
REMARK 620 5 HOH A2295   O    81.8 171.6  75.9  96.1                            
REMARK 620 6 HEM A1251   ND  169.2  94.1  88.7  90.6  87.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A1251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ISZ A1252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ISZ A1253                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1254                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OAF   RELATED DB: PDB                                   
REMARK 900  ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN                         
REMARK 900  COMPLEX WITH ASCORBATE                                              
REMARK 900 RELATED ID: 2GHC   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL MOBILITY IN THE ACTIVE SITE                          
REMARK 900  OF A HEMEPEROXIDASE                                                 
REMARK 900 RELATED ID: 2GHD   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL MOBILITY IN THE ACTIVE SITE                          
REMARK 900  OF A HEMEPEROXIDASE                                                 
REMARK 900 RELATED ID: 2GHH   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL MOBILITY IN THE ACTIVE SITE                          
REMARK 900  OF A HEMEPEROXIDASE                                                 
REMARK 900 RELATED ID: 2GHK   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL MOBILITY IN THE ACTIVE SITE                          
REMARK 900  OF A HEMEPEROXIDASE                                                 
REMARK 900 RELATED ID: 2VCN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ISONIAZID (INH) BOUND TO                               
REMARK 900  CYTOSOLIC SOYBEAN ASCORBATE PEROXIDASE MUTANT                       
REMARK 900  W41A                                                                
REMARK 900 RELATED ID: 1OAG   RELATED DB: PDB                                   
REMARK 900  ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL                            
REMARK 900 RELATED ID: 1V0H   RELATED DB: PDB                                   
REMARK 900  ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN                         
REMARK 900  COMPLEX WITH SALICYLHYDROXAMIC ACID                                 
REMARK 900 RELATED ID: 2CL4   RELATED DB: PDB                                   
REMARK 900  ASCORBATE PEROXIDASE R172A MUTANT                                   
REMARK 900 RELATED ID: 2GGN   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL MOBILITY IN THE ACTIVE SITE                          
REMARK 900  OF A HEMEPEROXIDASE                                                 
REMARK 900 RELATED ID: 2GHE   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL MOBILITY IN THE ACTIVE SITE                          
REMARK 900  OF A HEMEPEROXIDASE                                                 
REMARK 900 RELATED ID: 2VCF   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ISONIAZID (INH) BOUND TO                               
REMARK 900  CYTOSOLIC SOYBEAN ASCORBATE PEROXIDASE                              
DBREF  2VCS A  -10     1  PDB    2VCS     2VCS           -10      1             
DBREF  2VCS A    2   250  UNP    Q43758   Q43758_SOYBN     2    250             
SEQADV 2VCS ALA A   42  UNP  Q43758    HIS    42 ENGINEERED MUTATION            
SEQRES   1 A  261  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLY          
SEQRES   2 A  261  LYS SER TYR PRO THR VAL SER ALA ASP TYR GLN LYS ALA          
SEQRES   3 A  261  VAL GLU LYS ALA LYS LYS LYS LEU ARG GLY PHE ILE ALA          
SEQRES   4 A  261  GLU LYS ARG CYS ALA PRO LEU MET LEU ARG LEU ALA TRP          
SEQRES   5 A  261  ALA SER ALA GLY THR PHE ASP LYS GLY THR LYS THR GLY          
SEQRES   6 A  261  GLY PRO PHE GLY THR ILE LYS HIS PRO ALA GLU LEU ALA          
SEQRES   7 A  261  HIS SER ALA ASN ASN GLY LEU ASP ILE ALA VAL ARG LEU          
SEQRES   8 A  261  LEU GLU PRO LEU LYS ALA GLU PHE PRO ILE LEU SER TYR          
SEQRES   9 A  261  ALA ASP PHE TYR GLN LEU ALA GLY VAL VAL ALA VAL GLU          
SEQRES  10 A  261  VAL THR GLY GLY PRO GLU VAL PRO PHE HIS PRO GLY ARG          
SEQRES  11 A  261  GLU ASP LYS PRO GLU PRO PRO PRO GLU GLY ARG LEU PRO          
SEQRES  12 A  261  ASP ALA THR LYS GLY SER ASP HIS LEU ARG ASP VAL PHE          
SEQRES  13 A  261  GLY LYS ALA MET GLY LEU THR ASP GLN ASP ILE VAL ALA          
SEQRES  14 A  261  LEU SER GLY GLY HIS THR ILE GLY ALA ALA HIS LYS GLU          
SEQRES  15 A  261  ARG SER GLY PHE GLU GLY PRO TRP THR SER ASN PRO LEU          
SEQRES  16 A  261  ILE PHE ASP ASN SER TYR PHE THR GLU LEU LEU SER GLY          
SEQRES  17 A  261  GLU LYS GLU GLY LEU LEU GLN LEU PRO SER ASP LYS ALA          
SEQRES  18 A  261  LEU LEU SER ASP PRO VAL PHE ARG PRO LEU VAL ASP LYS          
SEQRES  19 A  261  TYR ALA ALA ASP GLU ASP ALA PHE PHE ALA ASP TYR ALA          
SEQRES  20 A  261  GLU ALA HIS GLN LYS LEU SER GLU LEU GLY PHE ALA ASP          
SEQRES  21 A  261  ALA                                                          
HET    HEM  A1251      43                                                       
HET    ISZ  A1252      10                                                       
HET    ISZ  A1253      10                                                       
HET    SO4  A1254       5                                                       
HETNAM     ISZ 4-(DIAZENYLCARBONYL)PYRIDINE                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  ISZ    2(C6 H5 N3 O)                                                
FORMUL   3  HEM    C34 H32 FE N4 O4                                             
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *299(H2 O1)                                                   
HELIX    1   1 SER A    9  ARG A   31  1                                  23    
HELIX    2   2 CYS A   32  GLY A   45  1                                  14    
HELIX    3   3 GLY A   58  LYS A   61  5                                   4    
HELIX    4   4 HIS A   62  ALA A   67  1                                   6    
HELIX    5   5 HIS A   68  ASN A   72  5                                   5    
HELIX    6   6 GLY A   73  GLU A   87  1                                  15    
HELIX    7   7 SER A   92  THR A  108  1                                  17    
HELIX    8   8 GLY A  137  GLY A  146  1                                  10    
HELIX    9   9 THR A  152  GLY A  161  1                                  10    
HELIX   10  10 GLY A  162  ILE A  165  5                                   4    
HELIX   11  11 ASN A  188  GLY A  197  1                                  10    
HELIX   12  12 LEU A  205  ASP A  214  1                                  10    
HELIX   13  13 VAL A  216  ASP A  227  1                                  12    
HELIX   14  14 ASP A  227  GLU A  244  1                                  18    
SHEET    1  AA 2 ALA A 167  ALA A 168  0                                        
SHEET    2  AA 2 GLY A 177  PRO A 178 -1  O  GLY A 177   N  ALA A 168           
LINK        FE   HEM A1251                 NE2 HIS A 163     1555   1555  2.04  
LINK        FE   HEM A1251                 O   HOH A2295     1555   1555  2.38  
SITE     1 AC1 24 PRO A  34  TRP A  41  PRO A 132  ALA A 134                    
SITE     2 AC1 24 PHE A 145  LEU A 159  SER A 160  HIS A 163                    
SITE     3 AC1 24 ILE A 165  GLY A 166  ALA A 167  ALA A 168                    
SITE     4 AC1 24 HIS A 169  ARG A 172  SER A 173  TRP A 179                    
SITE     5 AC1 24 LEU A 205  SER A 207  TYR A 235  ISZ A1252                    
SITE     6 AC1 24 HOH A2292  HOH A2293  HOH A2294  HOH A2295                    
SITE     1 AC2  9 ARG A  38  TRP A  41  ALA A  70  PRO A 132                    
SITE     2 AC2  9 SER A 173  HEM A1251  HOH A2098  HOH A2295                    
SITE     3 AC2  9 HOH A2296                                                     
SITE     1 AC3  7 LYS A  30  CYS A  32  ARG A  79  ARG A 172                    
SITE     2 AC3  7 HOH A2293  HOH A2297  HOH A2298                               
SITE     1 AC4  7 LYS A 136  GLY A 137  SER A 138  ASP A 139                    
SITE     2 AC4  7 HIS A 140  HOH A2299  HOH A2300                               
CRYST1   81.735   81.735   74.937  90.00  90.00  90.00 P 42 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      0.012235  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012235  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013345        0.00000                         
ATOM      1  N   GLY A   2      35.259  38.537  16.817  1.00 30.55           N  
ANISOU    1  N   GLY A   2     3945   3493   4170     78    220   -263       N  
ATOM      2  CA  GLY A   2      35.919  39.084  15.596  1.00 30.30           C  
ANISOU    2  CA  GLY A   2     3906   3501   4102    106    245   -280       C  
ATOM      3  C   GLY A   2      36.635  40.408  15.809  1.00 29.96           C  
ANISOU    3  C   GLY A   2     3848   3459   4074    104    245   -261       C  
ATOM      4  O   GLY A   2      37.109  41.023  14.854  1.00 30.60           O  
ANISOU    4  O   GLY A   2     3980   3544   4101    101    288   -302       O  
ATOM      5  N   LYS A   3      36.742  40.840  17.065  1.00 29.25           N  
ANISOU    5  N   LYS A   3     3694   3381   4038    139    233   -244       N  
ATOM      6  CA  LYS A   3      37.296  42.161  17.377  1.00 27.98           C  
ANISOU    6  CA  LYS A   3     3421   3251   3957    134    248   -185       C  
ATOM      7  C   LYS A   3      38.767  42.155  17.787  1.00 27.26           C  
ANISOU    7  C   LYS A   3     3325   3121   3908    146    270   -177       C  
ATOM      8  O   LYS A   3      39.188  41.380  18.634  1.00 27.48           O  
ANISOU    8  O   LYS A   3     3236   3221   3983    162    245   -128       O  
ATOM      9  CB  LYS A   3      36.463  42.862  18.455  1.00 28.09           C  
ANISOU    9  CB  LYS A   3     3459   3248   3964    156    238   -193       C  
ATOM     10  CG  LYS A   3      35.019  43.161  18.059  1.00 27.40           C  
ANISOU   10  CG  LYS A   3     3259   3316   3834    206    318   -102       C  
ATOM     11  CD  LYS A   3      34.938  44.234  16.985  1.00 26.55           C  
ANISOU   11  CD  LYS A   3     2985   3548   3553    261    460    262       C  
ATOM     12  CE  LYS A   3      33.497  44.539  16.635  1.00 26.73           C  
ANISOU   12  CE  LYS A   3     2895   3758   3499    262    644    413       C  
ATOM     13  NZ  LYS A   3      33.331  45.206  15.307  1.00 25.20           N  
ANISOU   13  NZ  LYS A   3     2468   3673   3432    258   1012    674       N  
ATOM     14  N   SER A   4      39.531  43.047  17.168  1.00 26.05           N  
ANISOU   14  N   SER A   4     3153   2924   3819    122    269   -216       N  
ATOM     15  CA  SER A   4      40.904  43.292  17.537  1.00 24.61           C  
ANISOU   15  CA  SER A   4     2978   2692   3680    128    294   -221       C  
ATOM     16  C   SER A   4      41.020  44.777  17.878  1.00 23.52           C  
ANISOU   16  C   SER A   4     2830   2607   3496    110    302   -222       C  
ATOM     17  O   SER A   4      41.208  45.603  16.987  1.00 23.44           O  
ANISOU   17  O   SER A   4     2903   2493   3510    170    335   -250       O  
ATOM     18  CB  SER A   4      41.813  42.951  16.363  1.00 25.06           C  
ANISOU   18  CB  SER A   4     3017   2802   3702     88    275   -199       C  
ATOM     19  OG  SER A   4      43.164  43.074  16.751  1.00 26.61           O  
ANISOU   19  OG  SER A   4     3205   2943   3961      7    292   -209       O  
ATOM     20  N   TYR A   5      40.893  45.114  19.158  1.00 21.44           N  
ANISOU   20  N   TYR A   5     2481   2469   3196    142    306   -196       N  
ATOM     21  CA  TYR A   5      40.828  46.518  19.558  1.00 19.95           C  
ANISOU   21  CA  TYR A   5     2232   2391   2953     55    314   -187       C  
ATOM     22  C   TYR A   5      42.193  47.198  19.470  1.00 19.91           C  
ANISOU   22  C   TYR A   5     2205   2388   2968     89    350   -179       C  
ATOM     23  O   TYR A   5      43.211  46.583  19.791  1.00 19.79           O  
ANISOU   23  O   TYR A   5     2160   2378   2980     84    434   -178       O  
ATOM     24  CB  TYR A   5      40.237  46.658  20.962  1.00 19.68           C  
ANISOU   24  CB  TYR A   5     2126   2447   2903     68    321   -184       C  
ATOM     25  CG  TYR A   5      38.865  46.038  21.085  1.00 17.78           C  
ANISOU   25  CG  TYR A   5     1887   2296   2571     21    281   -167       C  
ATOM     26  CD1 TYR A   5      37.752  46.642  20.496  1.00 15.68           C  
ANISOU   26  CD1 TYR A   5     1461   2228   2269     58    128   -153       C  
ATOM     27  CD2 TYR A   5      38.683  44.841  21.766  1.00 18.08           C  
ANISOU   27  CD2 TYR A   5     1917   2482   2468    -50    172   -171       C  
ATOM     28  CE1 TYR A   5      36.491  46.079  20.607  1.00 15.31           C  
ANISOU   28  CE1 TYR A   5     1438   2196   2181     43    -44    -85       C  
ATOM     29  CE2 TYR A   5      37.419  44.271  21.890  1.00 17.22           C  
ANISOU   29  CE2 TYR A   5     1704   2361   2477     -6    132    -78       C  
ATOM     30  CZ  TYR A   5      36.330  44.888  21.290  1.00 16.52           C  
ANISOU   30  CZ  TYR A   5     1633   2281   2363     50    165   -161       C  
ATOM     31  OH  TYR A   5      35.083  44.326  21.398  1.00 16.14           O  
ANISOU   31  OH  TYR A   5     1748   1941   2442     30    217    -30       O  
ATOM     32  N   PRO A   6      42.213  48.468  19.028  1.00 19.29           N  
ANISOU   32  N   PRO A   6     2137   2260   2932     93    340   -199       N  
ATOM     33  CA  PRO A   6      43.488  49.160  18.877  1.00 19.32           C  
ANISOU   33  CA  PRO A   6     2144   2239   2955    133    317   -172       C  
ATOM     34  C   PRO A   6      44.110  49.530  20.228  1.00 19.13           C  
ANISOU   34  C   PRO A   6     2113   2202   2952    124    270   -138       C  
ATOM     35  O   PRO A   6      43.416  49.656  21.239  1.00 18.92           O  
ANISOU   35  O   PRO A   6     2072   2226   2891    177    226   -128       O  
ATOM     36  CB  PRO A   6      43.108  50.418  18.093  1.00 19.35           C  
ANISOU   36  CB  PRO A   6     2096   2247   3006    134    338   -170       C  
ATOM     37  CG  PRO A   6      41.692  50.689  18.500  1.00 19.66           C  
ANISOU   37  CG  PRO A   6     2191   2249   3027    158    384   -220       C  
ATOM     38  CD  PRO A   6      41.069  49.326  18.655  1.00 19.47           C  
ANISOU   38  CD  PRO A   6     2142   2284   2969     72    422   -194       C  
ATOM     39  N   THR A   7      45.424  49.685  20.235  1.00 18.83           N  
ANISOU   39  N   THR A   7     2104   2150   2900    117    200   -107       N  
ATOM     40  CA  THR A   7      46.113  50.224  21.386  1.00 18.73           C  
ANISOU   40  CA  THR A   7     2180   2153   2783     80    177    -52       C  
ATOM     41  C   THR A   7      45.872  51.735  21.418  1.00 17.61           C  
ANISOU   41  C   THR A   7     2103   2013   2574     42    159     26       C  
ATOM     42  O   THR A   7      45.934  52.414  20.370  1.00 17.00           O  
ANISOU   42  O   THR A   7     2135   1984   2339     -2    140     60       O  
ATOM     43  CB  THR A   7      47.626  49.935  21.301  1.00 19.15           C  
ANISOU   43  CB  THR A   7     2206   2184   2884    111    146    -62       C  
ATOM     44  OG1 THR A   7      47.834  48.518  21.343  1.00 21.36           O  
ANISOU   44  OG1 THR A   7     2393   2397   3324    175    174   -107       O  
ATOM     45  CG2 THR A   7      48.384  50.593  22.455  1.00 20.23           C  
ANISOU   45  CG2 THR A   7     2362   2414   2910     59    145    -76       C  
ATOM     46  N   VAL A   8      45.550  52.235  22.609  1.00 15.80           N  
ANISOU   46  N   VAL A   8     1943   1866   2194    -36    121     75       N  
ATOM     47  CA  VAL A   8      45.543  53.671  22.884  1.00 15.09           C  
ANISOU   47  CA  VAL A   8     1807   1877   2048   -106    159     96       C  
ATOM     48  C   VAL A   8      46.491  53.965  24.052  1.00 14.95           C  
ANISOU   48  C   VAL A   8     1760   1888   2032   -125     93    132       C  
ATOM     49  O   VAL A   8      46.751  53.088  24.899  1.00 15.53           O  
ANISOU   49  O   VAL A   8     1820   1972   2109   -210     68    137       O  
ATOM     50  CB  VAL A   8      44.122  54.226  23.147  1.00 14.98           C  
ANISOU   50  CB  VAL A   8     1811   1853   2025    -97    114    137       C  
ATOM     51  CG1 VAL A   8      43.197  53.984  21.923  1.00 13.64           C  
ANISOU   51  CG1 VAL A   8     1567   1673   1941   -154    157     18       C  
ATOM     52  CG2 VAL A   8      43.525  53.630  24.427  1.00 13.52           C  
ANISOU   52  CG2 VAL A   8     1630   1800   1705     18    386     59       C  
ATOM     53  N   SER A   9      46.996  55.196  24.112  1.00 14.69           N  
ANISOU   53  N   SER A   9     1709   1952   1919   -155     31     76       N  
ATOM     54  CA  SER A   9      47.986  55.563  25.128  1.00 14.04           C  
ANISOU   54  CA  SER A   9     1585   1958   1790   -103    -43    130       C  
ATOM     55  C   SER A   9      47.352  55.522  26.518  1.00 14.18           C  
ANISOU   55  C   SER A   9     1608   2057   1720   -100    -89     98       C  
ATOM     56  O   SER A   9      46.121  55.561  26.650  1.00 12.84           O  
ANISOU   56  O   SER A   9     1386   1908   1581    -75    -42    107       O  
ATOM     57  CB  SER A   9      48.511  56.972  24.867  1.00 14.01           C  
ANISOU   57  CB  SER A   9     1619   1922   1781   -146     -6    159       C  
ATOM     58  OG  SER A   9      47.491  57.926  25.137  1.00 12.47           O  
ANISOU   58  OG  SER A   9     1222   1800   1714    -61    -52    252       O  
ATOM     59  N   ALA A  10      48.200  55.475  27.543  1.00 14.43           N  
ANISOU   59  N   ALA A  10     1612   2206   1664    -22   -188     93       N  
ATOM     60  CA  ALA A  10      47.739  55.572  28.926  1.00 14.82           C  
ANISOU   60  CA  ALA A  10     1671   2293   1665    -31   -297     82       C  
ATOM     61  C   ALA A  10      46.946  56.870  29.150  1.00 14.87           C  
ANISOU   61  C   ALA A  10     1656   2310   1682    -55   -330     89       C  
ATOM     62  O   ALA A  10      45.911  56.858  29.835  1.00 14.80           O  
ANISOU   62  O   ALA A  10     1642   2318   1662     86   -285     44       O  
ATOM     63  CB  ALA A  10      48.931  55.498  29.884  1.00 15.41           C  
ANISOU   63  CB  ALA A  10     1710   2399   1744    -23   -377    148       C  
ATOM     64  N   ASP A  11      47.410  57.974  28.557  1.00 14.36           N  
ANISOU   64  N   ASP A  11     1598   2244   1611   -116   -328     31       N  
ATOM     65  CA  ASP A  11      46.715  59.257  28.691  1.00 13.84           C  
ANISOU   65  CA  ASP A  11     1636   2105   1515   -237   -330     16       C  
ATOM     66  C   ASP A  11      45.322  59.168  28.091  1.00 12.60           C  
ANISOU   66  C   ASP A  11     1518   1947   1321   -197   -329      4       C  
ATOM     67  O   ASP A  11      44.361  59.705  28.649  1.00 12.55           O  
ANISOU   67  O   ASP A  11     1635   1929   1203   -288   -251    -86       O  
ATOM     68  CB  ASP A  11      47.516  60.410  28.076  1.00 14.56           C  
ANISOU   68  CB  ASP A  11     1639   2289   1603   -245   -339     17       C  
ATOM     69  CG  ASP A  11      48.697  60.834  28.951  1.00 16.38           C  
ANISOU   69  CG  ASP A  11     1946   2451   1827   -473   -319    -73       C  
ATOM     70  OD1 ASP A  11      48.722  60.505  30.159  1.00 20.25           O  
ANISOU   70  OD1 ASP A  11     2179   3104   2411   -346   -463    -56       O  
ATOM     71  OD2 ASP A  11      49.604  61.505  28.432  1.00 19.43           O  
ANISOU   71  OD2 ASP A  11     2184   2810   2387   -707   -494   -363       O  
ATOM     72  N   TYR A  12      45.204  58.468  26.960  1.00 11.65           N  
ANISOU   72  N   TYR A  12     1450   1824   1150   -192   -307    -34       N  
ATOM     73  CA  TYR A  12      43.878  58.268  26.352  1.00 10.62           C  
ANISOU   73  CA  TYR A  12     1358   1709    968   -133   -278    -67       C  
ATOM     74  C   TYR A  12      42.953  57.501  27.321  1.00 11.06           C  
ANISOU   74  C   TYR A  12     1487   1712   1001    -44   -290    -26       C  
ATOM     75  O   TYR A  12      41.804  57.912  27.562  1.00  9.92           O  
ANISOU   75  O   TYR A  12     1378   1602    786     12   -325     53       O  
ATOM     76  CB  TYR A  12      43.986  57.535  25.012  1.00 10.68           C  
ANISOU   76  CB  TYR A  12     1416   1769    872   -161   -241    -42       C  
ATOM     77  CG  TYR A  12      42.756  57.699  24.138  1.00 10.46           C  
ANISOU   77  CG  TYR A  12     1316   1750    907   -114   -121   -147       C  
ATOM     78  CD1 TYR A  12      41.569  57.009  24.421  1.00 11.80           C  
ANISOU   78  CD1 TYR A  12     1543   1897   1042   -122    -79    -98       C  
ATOM     79  CD2 TYR A  12      42.778  58.546  23.023  1.00 10.97           C  
ANISOU   79  CD2 TYR A  12     1523   1742    903    -25   -114   -167       C  
ATOM     80  CE1 TYR A  12      40.431  57.161  23.614  1.00 10.47           C  
ANISOU   80  CE1 TYR A  12     1324   1729    924     11   -313   -135       C  
ATOM     81  CE2 TYR A  12      41.654  58.707  22.214  1.00 10.55           C  
ANISOU   81  CE2 TYR A  12     1511   1608    890   -175   -104   -165       C  
ATOM     82  CZ  TYR A  12      40.485  58.015  22.504  1.00 10.71           C  
ANISOU   82  CZ  TYR A  12     1387   1918    764   -112    -82    -80       C  
ATOM     83  OH  TYR A  12      39.386  58.201  21.690  1.00 10.11           O  
ANISOU   83  OH  TYR A  12     1320   1612    905   -168    -30    -46       O  
ATOM     84  N   GLN A  13      43.453  56.401  27.878  1.00 11.35           N  
ANISOU   84  N   GLN A  13     1538   1660   1112     41   -274    -22       N  
ATOM     85  C   GLN A  13      42.255  56.343  30.054  1.00 12.53           C  
ANISOU   85  C   GLN A  13     1727   1791   1241     96   -252      1       C  
ATOM     86  O   GLN A  13      41.125  56.208  30.529  1.00 13.05           O  
ANISOU   86  O   GLN A  13     1789   1798   1370     54   -231    -93       O  
ATOM     87  CA AGLN A  13      42.608  55.609  28.778  0.50 12.60           C  
ANISOU   87  CA AGLN A  13     1757   1768   1262    100   -286    -29       C  
ATOM     88  CB AGLN A  13      43.144  54.200  29.072  0.50 13.18           C  
ANISOU   88  CB AGLN A  13     1868   1807   1330    131   -308    -35       C  
ATOM     89  CG AGLN A  13      42.278  53.049  28.477  0.50 15.49           C  
ANISOU   89  CG AGLN A  13     2306   1931   1648    263   -326    -23       C  
ATOM     90  CD AGLN A  13      40.783  53.067  28.891  0.50 17.24           C  
ANISOU   90  CD AGLN A  13     2795   2083   1672    206   -385   -127       C  
ATOM     91  OE1AGLN A  13      39.908  52.751  28.083  0.50 17.67           O  
ANISOU   91  OE1AGLN A  13     3119   1962   1632    391   -415   -167       O  
ATOM     92  NE2AGLN A  13      40.496  53.440  30.147  0.50 17.75           N  
ANISOU   92  NE2AGLN A  13     3197   2129   1415    194   -435    139       N  
ATOM     93  CA BGLN A  13      42.704  55.561  28.813  0.50 12.23           C  
ANISOU   93  CA BGLN A  13     1669   1766   1210    107   -239     -2       C  
ATOM     94  CB BGLN A  13      43.557  54.342  29.193  0.50 12.23           C  
ANISOU   94  CB BGLN A  13     1684   1760   1200    135   -231      7       C  
ATOM     95  CG BGLN A  13      43.752  53.346  28.034  0.50 12.63           C  
ANISOU   95  CG BGLN A  13     1643   1833   1322    218   -109     67       C  
ATOM     96  CD BGLN A  13      44.732  52.216  28.361  0.50 13.95           C  
ANISOU   96  CD BGLN A  13     1922   2005   1371    327    -63    169       C  
ATOM     97  OE1BGLN A  13      44.691  51.639  29.444  0.50 16.21           O  
ANISOU   97  OE1BGLN A  13     2276   2182   1701    523     62    387       O  
ATOM     98  NE2BGLN A  13      45.616  51.897  27.411  0.50 14.69           N  
ANISOU   98  NE2BGLN A  13     1822   2216   1542    519     75    226       N  
ATOM     99  N   LYS A  14      43.173  57.160  30.573  1.00 12.71           N  
ANISOU   99  N   LYS A  14     1770   1842   1215     64   -251    -33       N  
ATOM    100  CA  LYS A  14      42.876  58.028  31.725  1.00 13.61           C  
ANISOU  100  CA  LYS A  14     1846   2060   1264    -48   -211    -12       C  
ATOM    101  C   LYS A  14      41.702  58.958  31.406  1.00 12.99           C  
ANISOU  101  C   LYS A  14     1808   1971   1155    -45   -183     23       C  
ATOM    102  O   LYS A  14      40.772  59.125  32.213  1.00 12.37           O  
ANISOU  102  O   LYS A  14     1645   2025   1027    -19   -179     83       O  
ATOM    103  CB  LYS A  14      44.088  58.877  32.081  1.00 14.83           C  
ANISOU  103  CB  LYS A  14     1995   2238   1401    -53   -275    -28       C  
ATOM    104  CG  LYS A  14      45.106  58.197  32.965  1.00 18.15           C  
ANISOU  104  CG  LYS A  14     2560   2593   1742   -135   -302      1       C  
ATOM    105  CD  LYS A  14      46.041  59.245  33.584  1.00 22.84           C  
ANISOU  105  CD  LYS A  14     3346   3138   2194   -304   -510   -310       C  
ATOM    106  CE  LYS A  14      45.247  60.520  33.962  1.00 26.88           C  
ANISOU  106  CE  LYS A  14     3907   3541   2763   -301   -525   -301       C  
ATOM    107  NZ  LYS A  14      45.922  61.458  34.919  1.00 30.37           N  
ANISOU  107  NZ  LYS A  14     4680   3806   3050   -291   -504   -670       N  
ATOM    108  N   ALA A  15      41.753  59.557  30.221  1.00 12.30           N  
ANISOU  108  N   ALA A  15     1762   1897   1011    -50   -165     59       N  
ATOM    109  CA  ALA A  15      40.704  60.448  29.759  1.00 11.83           C  
ANISOU  109  CA  ALA A  15     1715   1792    987    -57    -80     59       C  
ATOM    110  C   ALA A  15      39.361  59.731  29.623  1.00 11.71           C  
ANISOU  110  C   ALA A  15     1710   1756    983    -54    -91     47       C  
ATOM    111  O   ALA A  15      38.333  60.311  29.970  1.00 10.64           O  
ANISOU  111  O   ALA A  15     1503   1581    959    -74      6    -35       O  
ATOM    112  CB  ALA A  15      41.102  61.108  28.432  1.00 12.32           C  
ANISOU  112  CB  ALA A  15     1777   1829   1076    -48     -4    143       C  
ATOM    113  N   VAL A  16      39.367  58.493  29.108  1.00 10.45           N  
ANISOU  113  N   VAL A  16     1625   1519    827    -45   -131     32       N  
ATOM    114  CA  VAL A  16      38.137  57.697  29.016  1.00 11.14           C  
ANISOU  114  CA  VAL A  16     1793   1627    811    -41    -94    -14       C  
ATOM    115  C   VAL A  16      37.522  57.544  30.415  1.00 10.83           C  
ANISOU  115  C   VAL A  16     1758   1519    838    -77   -123     19       C  
ATOM    116  O   VAL A  16      36.317  57.769  30.613  1.00  9.84           O  
ANISOU  116  O   VAL A  16     1594   1506    639   -133   -149    -13       O  
ATOM    117  CB  VAL A  16      38.357  56.309  28.381  1.00 10.83           C  
ANISOU  117  CB  VAL A  16     1754   1573    787   -108    -46    -40       C  
ATOM    118  CG1 VAL A  16      37.092  55.425  28.528  1.00 12.42           C  
ANISOU  118  CG1 VAL A  16     2013   1873    832   -142     63   -315       C  
ATOM    119  CG2 VAL A  16      38.790  56.427  26.889  1.00 11.86           C  
ANISOU  119  CG2 VAL A  16     1940   1810    755     71   -178   -179       C  
ATOM    120  N   GLU A  17      38.373  57.204  31.379  1.00 10.93           N  
ANISOU  120  N   GLU A  17     1822   1542    785    -76   -137    106       N  
ATOM    121  CA  GLU A  17      37.908  56.930  32.728  1.00 12.15           C  
ANISOU  121  CA  GLU A  17     1955   1676    985     10   -181     17       C  
ATOM    122  C   GLU A  17      37.327  58.172  33.364  1.00 11.71           C  
ANISOU  122  C   GLU A  17     1866   1555   1027     -3   -227      9       C  
ATOM    123  O   GLU A  17      36.226  58.127  33.925  1.00 11.77           O  
ANISOU  123  O   GLU A  17     1851   1540   1078    -62   -165    -25       O  
ATOM    124  CB  GLU A  17      39.028  56.313  33.566  1.00 13.05           C  
ANISOU  124  CB  GLU A  17     2132   1723   1101     62   -134     98       C  
ATOM    125  CG  GLU A  17      39.246  54.831  33.195  1.00 16.76           C  
ANISOU  125  CG  GLU A  17     2740   2137   1490    -21   -102    144       C  
ATOM    126  CD  GLU A  17      37.911  54.054  33.080  1.00 23.06           C  
ANISOU  126  CD  GLU A  17     3607   3069   2083   -212     22     72       C  
ATOM    127  OE1 GLU A  17      37.198  53.932  34.109  1.00 25.19           O  
ANISOU  127  OE1 GLU A  17     4032   3322   2215   -234    230    243       O  
ATOM    128  OE2 GLU A  17      37.564  53.589  31.960  1.00 25.58           O  
ANISOU  128  OE2 GLU A  17     3941   3196   2581   -183    112     59       O  
ATOM    129  N   LYS A  18      38.042  59.287  33.208  1.00 11.57           N  
ANISOU  129  N   LYS A  18     1791   1506   1097     -1   -253    -67       N  
ATOM    130  C   LYS A  18      36.321  61.067  33.033  1.00 11.15           C  
ANISOU  130  C   LYS A  18     1726   1486   1022    -19   -193    -91       C  
ATOM    131  O   LYS A  18      35.391  61.570  33.683  1.00 10.37           O  
ANISOU  131  O   LYS A  18     1597   1557    783     61   -183    -70       O  
ATOM    132  CA ALYS A  18      37.598  60.583  33.728  0.50 11.68           C  
ANISOU  132  CA ALYS A  18     1804   1551   1083    -34   -195    -57       C  
ATOM    133  CB ALYS A  18      38.702  61.624  33.554  0.50 12.08           C  
ANISOU  133  CB ALYS A  18     1812   1595   1181   -101   -251   -119       C  
ATOM    134  CG ALYS A  18      39.596  61.799  34.750  0.50 14.64           C  
ANISOU  134  CG ALYS A  18     2131   1937   1492   -217    -99     -9       C  
ATOM    135  CD ALYS A  18      40.349  63.143  34.699  0.50 16.68           C  
ANISOU  135  CD ALYS A  18     2409   1928   1999   -494   -126   -231       C  
ATOM    136  CE ALYS A  18      39.402  64.330  34.541  0.50 18.70           C  
ANISOU  136  CE ALYS A  18     2574   2254   2274   -491   -180   -115       C  
ATOM    137  NZ ALYS A  18      40.080  65.643  34.742  0.50 21.45           N  
ANISOU  137  NZ ALYS A  18     2973   2544   2629   -367   -187   -260       N  
ATOM    138  CA BLYS A  18      37.595  60.566  33.738  0.50 10.95           C  
ANISOU  138  CA BLYS A  18     1742   1426    990      0   -193    -93       C  
ATOM    139  CB BLYS A  18      38.726  61.596  33.640  0.50 11.06           C  
ANISOU  139  CB BLYS A  18     1728   1432   1042    -53   -239   -173       C  
ATOM    140  CG BLYS A  18      38.432  62.919  34.327  0.50  9.49           C  
ANISOU  140  CG BLYS A  18     1692   1057    857     41   -113   -239       C  
ATOM    141  CD BLYS A  18      38.442  62.772  35.840  0.50 13.14           C  
ANISOU  141  CD BLYS A  18     2199   1311   1481    -84    218   -365       C  
ATOM    142  CE BLYS A  18      37.168  62.113  36.377  0.50 13.58           C  
ANISOU  142  CE BLYS A  18     2302   1469   1388    -99    289   -485       C  
ATOM    143  NZ BLYS A  18      35.947  62.901  36.111  0.50 14.31           N  
ANISOU  143  NZ BLYS A  18     2264   1788   1382   -191    453   -544       N  
ATOM    144  N   ALA A  19      36.278  60.924  31.712  1.00 10.27           N  
ANISOU  144  N   ALA A  19     1694   1416    790     -6   -169    -27       N  
ATOM    145  CA  ALA A  19      35.099  61.302  30.931  1.00 10.43           C  
ANISOU  145  CA  ALA A  19     1741   1448    771    -53    -74    -35       C  
ATOM    146  C   ALA A  19      33.886  60.478  31.346  1.00 10.61           C  
ANISOU  146  C   ALA A  19     1828   1461    741    -70   -102    -48       C  
ATOM    147  O   ALA A  19      32.781  61.012  31.424  1.00  9.66           O  
ANISOU  147  O   ALA A  19     1686   1375    606    -55     -8      6       O  
ATOM    148  CB  ALA A  19      35.365  61.161  29.438  1.00 10.67           C  
ANISOU  148  CB  ALA A  19     1741   1606    706      4   -108    -31       C  
ATOM    149  N   LYS A  20      34.108  59.196  31.640  1.00 10.14           N  
ANISOU  149  N   LYS A  20     1854   1354    642    -84    -93     88       N  
ATOM    150  CA  LYS A  20      33.014  58.300  32.037  1.00 11.05           C  
ANISOU  150  CA  LYS A  20     1981   1348    869    -99    -86     97       C  
ATOM    151  C   LYS A  20      32.328  58.847  33.296  1.00 10.83           C  
ANISOU  151  C   LYS A  20     1877   1378    859    -36    -57    109       C  
ATOM    152  O   LYS A  20      31.099  58.968  33.340  1.00 10.15           O  
ANISOU  152  O   LYS A  20     1719   1306    830     10   -125     70       O  
ATOM    153  CB  LYS A  20      33.524  56.877  32.270  1.00 11.02           C  
ANISOU  153  CB  LYS A  20     1937   1336    913   -156    -72    118       C  
ATOM    154  CG  LYS A  20      32.406  55.867  32.574  1.00 13.05           C  
ANISOU  154  CG  LYS A  20     2333   1333   1291   -226   -110    200       C  
ATOM    155  CD  LYS A  20      32.949  54.448  32.628  1.00 15.18           C  
ANISOU  155  CD  LYS A  20     2640   1386   1740   -207    122    338       C  
ATOM    156  CE  LYS A  20      31.862  53.464  33.058  1.00 20.43           C  
ANISOU  156  CE  LYS A  20     3293   1567   2899     -8    281    440       C  
ATOM    157  NZ  LYS A  20      32.426  52.129  33.409  1.00 24.17           N  
ANISOU  157  NZ  LYS A  20     3832   1744   3603     23    407    376       N  
ATOM    158  N   LYS A  21      33.144  59.195  34.292  1.00 10.24           N  
ANISOU  158  N   LYS A  21     1868   1338    681    -39    -84     60       N  
ATOM    159  CA  LYS A  21      32.654  59.764  35.557  1.00 11.11           C  
ANISOU  159  CA  LYS A  21     1835   1639    746     -4   -106     49       C  
ATOM    160  C   LYS A  21      31.920  61.079  35.317  1.00 11.20           C  
ANISOU  160  C   LYS A  21     1811   1669    775    -42   -120     32       C  
ATOM    161  O   LYS A  21      30.771  61.234  35.744  1.00 11.10           O  
ANISOU  161  O   LYS A  21     1783   1785    649     71    -64     65       O  
ATOM    162  CB  LYS A  21      33.801  59.965  36.542  1.00 11.42           C  
ANISOU  162  CB  LYS A  21     1858   1732    747     43    -65    107       C  
ATOM    163  CG  LYS A  21      34.483  58.676  36.954  1.00 12.74           C  
ANISOU  163  CG  LYS A  21     2112   2059    669    148    -95     41       C  
ATOM    164  CD  LYS A  21      35.466  58.989  38.090  1.00 16.22           C  
ANISOU  164  CD  LYS A  21     2522   2592   1048    200   -378     -6       C  
ATOM    165  CE  LYS A  21      36.202  57.753  38.540  1.00 20.87           C  
ANISOU  165  CE  LYS A  21     2992   3346   1590    385   -158   -213       C  
ATOM    166  NZ  LYS A  21      36.940  57.106  37.430  1.00 22.52           N  
ANISOU  166  NZ  LYS A  21     3160   3558   1836    503   -184   -398       N  
ATOM    167  N   LYS A  22      32.549  61.995  34.581  1.00 11.10           N  
ANISOU  167  N   LYS A  22     1791   1693    733    -56   -145     79       N  
ATOM    168  CA  LYS A  22      31.919  63.280  34.291  1.00 11.76           C  
ANISOU  168  CA  LYS A  22     1828   1754    885   -111   -161    105       C  
ATOM    169  C   LYS A  22      30.589  63.115  33.540  1.00 10.86           C  
ANISOU  169  C   LYS A  22     1677   1689    757   -143   -116     89       C  
ATOM    170  O   LYS A  22      29.639  63.845  33.804  1.00 11.37           O  
ANISOU  170  O   LYS A  22     1846   1692    779   -151   -179     51       O  
ATOM    171  CB  LYS A  22      32.858  64.186  33.498  1.00 12.54           C  
ANISOU  171  CB  LYS A  22     1878   1821   1063   -152   -127    112       C  
ATOM    172  CG  LYS A  22      34.102  64.660  34.257  1.00 16.03           C  
ANISOU  172  CG  LYS A  22     2326   2211   1552     -1   -304     40       C  
ATOM    173  CD  LYS A  22      33.888  65.917  35.093  1.00 23.38           C  
ANISOU  173  CD  LYS A  22     3321   3086   2474   -123   -452     31       C  
ATOM    174  CE  LYS A  22      33.512  67.125  34.236  1.00 26.90           C  
ANISOU  174  CE  LYS A  22     3870   3380   2969   -251   -348    -31       C  
ATOM    175  NZ  LYS A  22      34.099  68.428  34.705  1.00 27.18           N  
ANISOU  175  NZ  LYS A  22     3996   3375   2953   -470   -462   -316       N  
ATOM    176  N   LEU A  23      30.541  62.178  32.592  1.00 10.49           N  
ANISOU  176  N   LEU A  23     1587   1623    774   -154   -133     76       N  
ATOM    177  CA  LEU A  23      29.311  61.894  31.843  1.00  9.58           C  
ANISOU  177  CA  LEU A  23     1528   1603    508    -64   -122     28       C  
ATOM    178  C   LEU A  23      28.209  61.381  32.772  1.00  9.85           C  
ANISOU  178  C   LEU A  23     1631   1516    594    -82   -130      0       C  
ATOM    179  O   LEU A  23      27.042  61.740  32.601  1.00  9.56           O  
ANISOU  179  O   LEU A  23     1584   1634    413     36   -145     -8       O  
ATOM    180  CB  LEU A  23      29.555  60.899  30.701  1.00  9.80           C  
ANISOU  180  CB  LEU A  23     1534   1652    537    -94    -52     59       C  
ATOM    181  CG  LEU A  23      30.192  61.513  29.439  1.00  9.03           C  
ANISOU  181  CG  LEU A  23     1315   1754    361     77   -109    189       C  
ATOM    182  CD1 LEU A  23      30.797  60.382  28.597  1.00 10.24           C  
ANISOU  182  CD1 LEU A  23     1466   1998    427    144     89    -31       C  
ATOM    183  CD2 LEU A  23      29.173  62.328  28.609  1.00 11.17           C  
ANISOU  183  CD2 LEU A  23     1601   2094    547    230   -158    300       C  
ATOM    184  N   ARG A  24      28.572  60.564  33.765  1.00 10.19           N  
ANISOU  184  N   ARG A  24     1761   1499    612    -33   -158    -46       N  
ATOM    185  CA  ARG A  24      27.551  60.048  34.683  1.00 10.43           C  
ANISOU  185  CA  ARG A  24     1856   1358    747    -25   -153      4       C  
ATOM    186  C   ARG A  24      26.852  61.216  35.385  1.00 10.37           C  
ANISOU  186  C   ARG A  24     1899   1336    703    -28   -136    -60       C  
ATOM    187  O   ARG A  24      25.621  61.323  35.360  1.00  9.56           O  
ANISOU  187  O   ARG A  24     1660   1212    757   -166   -164   -289       O  
ATOM    188  CB  ARG A  24      28.151  59.129  35.742  1.00 10.88           C  
ANISOU  188  CB  ARG A  24     1922   1292    918     32   -198     56       C  
ATOM    189  CG  ARG A  24      28.487  57.727  35.290  1.00 10.81           C  
ANISOU  189  CG  ARG A  24     1844   1351    910    219    -79    112       C  
ATOM    190  CD  ARG A  24      29.338  57.115  36.415  1.00 11.23           C  
ANISOU  190  CD  ARG A  24     1991   1530    743    383    -90    -46       C  
ATOM    191  NE  ARG A  24      29.724  55.733  36.155  1.00 12.10           N  
ANISOU  191  NE  ARG A  24     1934   1617   1045    374     49   -183       N  
ATOM    192  CZ  ARG A  24      30.821  55.148  36.633  1.00 12.44           C  
ANISOU  192  CZ  ARG A  24     1835   1933    955    375    -30   -383       C  
ATOM    193  NH1 ARG A  24      31.710  55.838  37.358  1.00 10.61           N  
ANISOU  193  NH1 ARG A  24     1409   1816    806    150   -233   -529       N  
ATOM    194  NH2 ARG A  24      31.047  53.868  36.359  1.00 14.40           N  
ANISOU  194  NH2 ARG A  24     1825   2244   1399    388   -210   -488       N  
ATOM    195  N   GLY A  25      27.646  62.085  36.008  1.00 10.12           N  
ANISOU  195  N   GLY A  25     1876   1270    696   -115    -92    -23       N  
ATOM    196  CA  GLY A  25      27.112  63.238  36.767  1.00 10.87           C  
ANISOU  196  CA  GLY A  25     2001   1410    716     -7   -158      3       C  
ATOM    197  C   GLY A  25      26.279  64.147  35.873  1.00 10.77           C  
ANISOU  197  C   GLY A  25     1980   1435    677    -79   -171     11       C  
ATOM    198  O   GLY A  25      25.175  64.554  36.233  1.00 10.54           O  
ANISOU  198  O   GLY A  25     1996   1480    526    -14    -68     32       O  
ATOM    199  N   PHE A  26      26.807  64.432  34.685  1.00 10.43           N  
ANISOU  199  N   PHE A  26     1910   1474    579   -141   -158     45       N  
ATOM    200  CA  PHE A  26      26.153  65.336  33.748  1.00 11.11           C  
ANISOU  200  CA  PHE A  26     1932   1648    640   -125   -199     58       C  
ATOM    201  C   PHE A  26      24.813  64.808  33.211  1.00 10.66           C  
ANISOU  201  C   PHE A  26     1828   1624    596   -106   -176     11       C  
ATOM    202  O   PHE A  26      23.819  65.518  33.206  1.00 10.90           O  
ANISOU  202  O   PHE A  26     1884   1606    652    -57   -250    -36       O  
ATOM    203  CB  PHE A  26      27.065  65.627  32.560  1.00 11.28           C  
ANISOU  203  CB  PHE A  26     1999   1675    609   -121   -216    160       C  
ATOM    204  CG  PHE A  26      26.452  66.563  31.573  1.00 11.06           C  
ANISOU  204  CG  PHE A  26     2038   1643    518    -11   -395    361       C  
ATOM    205  CD1 PHE A  26      26.423  67.929  31.820  1.00 13.42           C  
ANISOU  205  CD1 PHE A  26     2215   2093    789    -34   -434    494       C  
ATOM    206  CD2 PHE A  26      25.848  66.068  30.410  1.00 12.54           C  
ANISOU  206  CD2 PHE A  26     2317   1846    599     91   -577    463       C  
ATOM    207  CE1 PHE A  26      25.830  68.808  30.896  1.00 13.43           C  
ANISOU  207  CE1 PHE A  26     2344   2153    605    -76   -631    552       C  
ATOM    208  CE2 PHE A  26      25.269  66.941  29.480  1.00 13.78           C  
ANISOU  208  CE2 PHE A  26     2673   1742    819    223   -422    690       C  
ATOM    209  CZ  PHE A  26      25.253  68.313  29.737  1.00 13.48           C  
ANISOU  209  CZ  PHE A  26     2369   1974    778   -306   -311    320       C  
ATOM    210  N   ILE A  27      24.822  63.561  32.752  1.00 10.36           N  
ANISOU  210  N   ILE A  27     1732   1616    588   -123   -166   -109       N  
ATOM    211  CA  ILE A  27      23.648  62.916  32.181  1.00 10.13           C  
ANISOU  211  CA  ILE A  27     1702   1590    555    -88   -134   -239       C  
ATOM    212  C   ILE A  27      22.568  62.765  33.268  1.00 10.81           C  
ANISOU  212  C   ILE A  27     1700   1749    656    -68   -142   -197       C  
ATOM    213  O   ILE A  27      21.390  63.041  33.025  1.00 10.76           O  
ANISOU  213  O   ILE A  27     1711   1781    593     45   -200   -185       O  
ATOM    214  CB  ILE A  27      24.043  61.567  31.516  1.00 10.09           C  
ANISOU  214  CB  ILE A  27     1597   1630    604    -25   -164   -181       C  
ATOM    215  CG1 ILE A  27      24.918  61.852  30.268  1.00  8.86           C  
ANISOU  215  CG1 ILE A  27     1503   1483    378   -151   -166   -317       C  
ATOM    216  CG2 ILE A  27      22.815  60.768  31.163  1.00 10.06           C  
ANISOU  216  CG2 ILE A  27     1859   1363    600   -134   -174   -584       C  
ATOM    217  CD1 ILE A  27      25.511  60.608  29.610  1.00 11.03           C  
ANISOU  217  CD1 ILE A  27     1836   1745    610    -54    -33   -221       C  
ATOM    218  N   ALA A  28      22.979  62.361  34.474  1.00 10.45           N  
ANISOU  218  N   ALA A  28     1672   1739    557    -99    -70   -216       N  
ATOM    219  CA  ALA A  28      22.027  62.216  35.570  1.00 11.32           C  
ANISOU  219  CA  ALA A  28     1763   1873    666   -139   -100   -248       C  
ATOM    220  C   ALA A  28      21.396  63.576  35.893  1.00 11.79           C  
ANISOU  220  C   ALA A  28     1755   1966    756   -142   -121   -259       C  
ATOM    221  O   ALA A  28      20.167  63.689  35.987  1.00 12.10           O  
ANISOU  221  O   ALA A  28     1729   2035    831   -246   -107   -338       O  
ATOM    222  CB  ALA A  28      22.703  61.622  36.782  1.00 10.90           C  
ANISOU  222  CB  ALA A  28     1651   1874    613   -128    -96   -157       C  
ATOM    223  N   GLU A  29      22.233  64.604  36.044  1.00 12.33           N  
ANISOU  223  N   GLU A  29     1903   1951    831   -172   -140   -248       N  
ATOM    224  CA  GLU A  29      21.747  65.940  36.417  1.00 13.67           C  
ANISOU  224  CA  GLU A  29     2011   2070   1111   -179   -181   -263       C  
ATOM    225  C   GLU A  29      20.829  66.523  35.364  1.00 13.82           C  
ANISOU  225  C   GLU A  29     1969   2109   1173   -202   -159   -304       C  
ATOM    226  O   GLU A  29      19.797  67.132  35.683  1.00 13.67           O  
ANISOU  226  O   GLU A  29     2002   2158   1033   -213   -168   -324       O  
ATOM    227  CB  GLU A  29      22.896  66.915  36.665  1.00 13.51           C  
ANISOU  227  CB  GLU A  29     1926   2046   1161   -162   -228   -259       C  
ATOM    228  CG  GLU A  29      22.455  68.182  37.437  1.00 16.39           C  
ANISOU  228  CG  GLU A  29     2355   2164   1709    -59   -422    -17       C  
ATOM    229  CD  GLU A  29      21.744  69.223  36.569  1.00 19.98           C  
ANISOU  229  CD  GLU A  29     2807   2570   2215    -89   -441    125       C  
ATOM    230  OE1 GLU A  29      20.833  69.915  37.098  1.00 20.22           O  
ANISOU  230  OE1 GLU A  29     2914   2410   2358    228   -465    355       O  
ATOM    231  OE2 GLU A  29      22.099  69.350  35.369  1.00 21.19           O  
ANISOU  231  OE2 GLU A  29     3127   2594   2329     35   -372    277       O  
ATOM    232  N   LYS A  30      21.222  66.335  34.108  1.00 14.11           N  
ANISOU  232  N   LYS A  30     1993   2219   1149   -178   -111   -346       N  
ATOM    233  CA  LYS A  30      20.494  66.909  32.987  1.00 15.45           C  
ANISOU  233  CA  LYS A  30     2078   2409   1383   -128    -26   -384       C  
ATOM    234  C   LYS A  30      19.236  66.111  32.591  1.00 15.06           C  
ANISOU  234  C   LYS A  30     2004   2379   1339   -163     -5   -435       C  
ATOM    235  O   LYS A  30      18.414  66.599  31.807  1.00 14.92           O  
ANISOU  235  O   LYS A  30     1971   2283   1413    -95     29   -485       O  
ATOM    236  CB  LYS A  30      21.447  67.081  31.801  1.00 15.92           C  
ANISOU  236  CB  LYS A  30     2093   2531   1424    -81    -31   -312       C  
ATOM    237  CG  LYS A  30      21.040  68.144  30.785  1.00 19.99           C  
ANISOU  237  CG  LYS A  30     2601   2937   2057   -141    156   -379       C  
ATOM    238  CD  LYS A  30      21.263  69.573  31.311  1.00 24.53           C  
ANISOU  238  CD  LYS A  30     3151   3561   2609   -324    146   -601       C  
ATOM    239  CE  LYS A  30      22.695  69.772  31.771  1.00 26.77           C  
ANISOU  239  CE  LYS A  30     3326   3971   2874   -266    -22   -551       C  
ATOM    240  NZ  LYS A  30      23.062  71.183  32.045  1.00 28.34           N  
ANISOU  240  NZ  LYS A  30     3483   4233   3051   -519     54   -697       N  
ATOM    241  N   ARG A  31      19.083  64.901  33.137  1.00 14.55           N  
ANISOU  241  N   ARG A  31     1914   2326   1286   -216     50   -488       N  
ATOM    242  CA  ARG A  31      17.949  63.997  32.830  1.00 15.35           C  
ANISOU  242  CA  ARG A  31     1949   2480   1403   -239     95   -445       C  
ATOM    243  C   ARG A  31      17.876  63.671  31.341  1.00 14.90           C  
ANISOU  243  C   ARG A  31     1869   2360   1429   -309     67   -408       C  
ATOM    244  O   ARG A  31      16.802  63.490  30.771  1.00 15.78           O  
ANISOU  244  O   ARG A  31     1873   2661   1462   -250     95   -438       O  
ATOM    245  CB  ARG A  31      16.614  64.568  33.326  1.00 15.24           C  
ANISOU  245  CB  ARG A  31     1920   2442   1428   -301     87   -479       C  
ATOM    246  CG  ARG A  31      16.676  65.097  34.740  1.00 17.03           C  
ANISOU  246  CG  ARG A  31     2205   2787   1476   -223    254   -402       C  
ATOM    247  CD  ARG A  31      15.398  65.792  35.165  1.00 19.86           C  
ANISOU  247  CD  ARG A  31     2533   3077   1933   -238    367   -338       C  
ATOM    248  NE  ARG A  31      14.243  64.898  35.286  1.00 22.73           N  
ANISOU  248  NE  ARG A  31     3216   3287   2133    -80    397   -187       N  
ATOM    249  CZ  ARG A  31      14.103  63.931  36.195  1.00 24.46           C  
ANISOU  249  CZ  ARG A  31     3539   3197   2558     23    344   -214       C  
ATOM    250  NH1 ARG A  31      12.984  63.218  36.211  1.00 24.10           N  
ANISOU  250  NH1 ARG A  31     3591   3010   2555     69    512   -215       N  
ATOM    251  NH2 ARG A  31      15.067  63.668  37.082  1.00 25.27           N  
ANISOU  251  NH2 ARG A  31     3676   3286   2638    140    322    -19       N  
ATOM    252  N   CYS A  32      19.036  63.578  30.711  1.00 13.95           N  
ANISOU  252  N   CYS A  32     1736   2242   1318   -302     52   -358       N  
ATOM    253  CA  CYS A  32      19.066  63.421  29.277  1.00 13.61           C  
ANISOU  253  CA  CYS A  32     1776   2142   1252   -361      0   -257       C  
ATOM    254  C   CYS A  32      19.575  62.060  28.854  1.00 12.10           C  
ANISOU  254  C   CYS A  32     1558   1917   1121   -344    -51   -275       C  
ATOM    255  O   CYS A  32      19.962  61.894  27.698  1.00 10.64           O  
ANISOU  255  O   CYS A  32     1456   1698    889   -356    -37   -233       O  
ATOM    256  CB  CYS A  32      19.906  64.522  28.641  1.00 14.20           C  
ANISOU  256  CB  CYS A  32     1833   2213   1349   -404      9   -225       C  
ATOM    257  SG  CYS A  32      21.612  64.594  29.185  1.00 14.72           S  
ANISOU  257  SG  CYS A  32     2133   2392   1065   -357   -173     76       S  
ATOM    258  N   ALA A  33      19.566  61.076  29.764  1.00 11.35           N  
ANISOU  258  N   ALA A  33     1410   1972    927   -309   -134   -311       N  
ATOM    259  CA  ALA A  33      20.017  59.731  29.359  1.00 10.77           C  
ANISOU  259  CA  ALA A  33     1290   1938    861   -253   -171   -281       C  
ATOM    260  C   ALA A  33      19.365  59.217  28.060  1.00 10.54           C  
ANISOU  260  C   ALA A  33     1142   2008    851   -204   -208   -285       C  
ATOM    261  O   ALA A  33      20.075  58.722  27.194  1.00  9.16           O  
ANISOU  261  O   ALA A  33      907   1953    618   -173   -177   -286       O  
ATOM    262  CB  ALA A  33      19.886  58.713  30.472  1.00 10.85           C  
ANISOU  262  CB  ALA A  33     1298   2000    822   -284   -115   -197       C  
ATOM    263  N   PRO A  34      18.023  59.307  27.936  1.00 10.91           N  
ANISOU  263  N   PRO A  34     1150   2095    897   -111   -238   -395       N  
ATOM    264  CA  PRO A  34      17.422  58.756  26.722  1.00 11.20           C  
ANISOU  264  CA  PRO A  34     1213   2134    908    -71   -201   -362       C  
ATOM    265  C   PRO A  34      17.950  59.410  25.455  1.00 11.34           C  
ANISOU  265  C   PRO A  34     1295   2033    978    -50   -178   -312       C  
ATOM    266  O   PRO A  34      18.256  58.715  24.474  1.00 10.92           O  
ANISOU  266  O   PRO A  34     1323   1960    866     70    -44   -428       O  
ATOM    267  CB  PRO A  34      15.925  59.054  26.885  1.00 11.61           C  
ANISOU  267  CB  PRO A  34     1188   2291    932    -68   -163   -391       C  
ATOM    268  CG  PRO A  34      15.713  59.360  28.306  1.00 12.25           C  
ANISOU  268  CG  PRO A  34     1302   2261   1089   -225   -242   -593       C  
ATOM    269  CD  PRO A  34      17.012  59.835  28.873  1.00 11.05           C  
ANISOU  269  CD  PRO A  34      952   2273    971   -102   -249   -349       C  
ATOM    270  N   LEU A  35      18.059  60.730  25.474  1.00 11.38           N  
ANISOU  270  N   LEU A  35     1398   1945    980      4   -192   -183       N  
ATOM    271  CA  LEU A  35      18.540  61.470  24.305  1.00 12.02           C  
ANISOU  271  CA  LEU A  35     1639   1883   1043    -25   -232   -122       C  
ATOM    272  C   LEU A  35      19.969  61.066  23.967  1.00 11.80           C  
ANISOU  272  C   LEU A  35     1665   1813   1005    -73   -182    -80       C  
ATOM    273  O   LEU A  35      20.327  60.959  22.802  1.00 11.68           O  
ANISOU  273  O   LEU A  35     1734   1833    869    -33   -254   -101       O  
ATOM    274  CB  LEU A  35      18.454  62.962  24.574  1.00 12.37           C  
ANISOU  274  CB  LEU A  35     1676   1915   1108     14   -222    -46       C  
ATOM    275  CG  LEU A  35      18.707  63.889  23.391  1.00 14.27           C  
ANISOU  275  CG  LEU A  35     2083   2000   1336    -91   -227    -40       C  
ATOM    276  CD1 LEU A  35      17.641  63.697  22.307  1.00 13.73           C  
ANISOU  276  CD1 LEU A  35     2192   1981   1043    -71   -367      8       C  
ATOM    277  CD2 LEU A  35      18.752  65.348  23.890  1.00 14.79           C  
ANISOU  277  CD2 LEU A  35     2240   1927   1452    101   -285   -191       C  
ATOM    278  N   MET A  36      20.776  60.817  24.996  1.00 11.03           N  
ANISOU  278  N   MET A  36     1612   1670    907    -62   -225    -42       N  
ATOM    279  CA  MET A  36      22.168  60.392  24.799  1.00 11.03           C  
ANISOU  279  CA  MET A  36     1673   1583    934   -208   -174     24       C  
ATOM    280  C   MET A  36      22.226  58.970  24.233  1.00 10.23           C  
ANISOU  280  C   MET A  36     1588   1495    801   -154   -208     87       C  
ATOM    281  O   MET A  36      23.065  58.666  23.385  1.00  9.44           O  
ANISOU  281  O   MET A  36     1579   1363    645   -322    -98      3       O  
ATOM    282  CB  MET A  36      22.956  60.501  26.111  1.00 11.33           C  
ANISOU  282  CB  MET A  36     1707   1612    985   -245   -101     14       C  
ATOM    283  CG  MET A  36      23.155  61.953  26.590  1.00 13.55           C  
ANISOU  283  CG  MET A  36     2024   1817   1304   -371    -61   -126       C  
ATOM    284  SD  MET A  36      23.791  63.036  25.281  1.00 18.36           S  
ANISOU  284  SD  MET A  36     2906   2137   1931   -573    600   -259       S  
ATOM    285  CE  MET A  36      23.356  64.685  25.838  1.00 16.91           C  
ANISOU  285  CE  MET A  36     2423   1961   2037   -538    211    -42       C  
ATOM    286  N   LEU A  37      21.339  58.100  24.704  1.00 10.25           N  
ANISOU  286  N   LEU A  37     1563   1543    788   -111   -231    161       N  
ATOM    287  CA  LEU A  37      21.258  56.750  24.137  1.00 10.17           C  
ANISOU  287  CA  LEU A  37     1635   1536    691   -110   -118    170       C  
ATOM    288  C   LEU A  37      20.841  56.821  22.668  1.00 10.75           C  
ANISOU  288  C   LEU A  37     1629   1637    815    -75   -140    176       C  
ATOM    289  O   LEU A  37      21.451  56.143  21.816  1.00 10.43           O  
ANISOU  289  O   LEU A  37     1619   1730    613    -77      0    136       O  
ATOM    290  CB  LEU A  37      20.337  55.824  24.944  1.00 10.68           C  
ANISOU  290  CB  LEU A  37     1726   1511    818   -102   -106    153       C  
ATOM    291  CG  LEU A  37      20.174  54.388  24.407  1.00 10.66           C  
ANISOU  291  CG  LEU A  37     1698   1585    767   -129   -184    222       C  
ATOM    292  CD1 LEU A  37      21.535  53.700  24.113  1.00 11.63           C  
ANISOU  292  CD1 LEU A  37     2132   1536    750     94   -426    247       C  
ATOM    293  CD2 LEU A  37      19.288  53.539  25.318  1.00 11.77           C  
ANISOU  293  CD2 LEU A  37     2040   1553    878   -151     22    307       C  
ATOM    294  N   ARG A  38      19.829  57.640  22.379  1.00 10.48           N  
ANISOU  294  N   ARG A  38     1574   1713    693    -24   -227    225       N  
ATOM    295  CA  ARG A  38      19.424  57.890  20.992  1.00 11.13           C  
ANISOU  295  CA  ARG A  38     1539   1774    916     95   -276    227       C  
ATOM    296  C   ARG A  38      20.596  58.381  20.137  1.00 10.94           C  
ANISOU  296  C   ARG A  38     1553   1748    854     61   -250    183       C  
ATOM    297  O   ARG A  38      20.797  57.904  19.012  1.00 10.72           O  
ANISOU  297  O   ARG A  38     1412   1642   1018    235   -151     70       O  
ATOM    298  CB  ARG A  38      18.245  58.878  20.922  1.00 11.56           C  
ANISOU  298  CB  ARG A  38     1598   1833    961    161   -361    307       C  
ATOM    299  CG  ARG A  38      17.585  58.913  19.527  1.00 11.82           C  
ANISOU  299  CG  ARG A  38     1694   1900    896    336   -413    453       C  
ATOM    300  CD  ARG A  38      16.595  60.059  19.447  1.00 13.84           C  
ANISOU  300  CD  ARG A  38     1866   1983   1410    554   -596    489       C  
ATOM    301  NE  ARG A  38      16.397  60.467  18.052  1.00 13.74           N  
ANISOU  301  NE  ARG A  38     2183   1789   1246    395   -654    284       N  
ATOM    302  CZ  ARG A  38      15.962  61.659  17.654  1.00 14.22           C  
ANISOU  302  CZ  ARG A  38     1998   1869   1536    247   -562    245       C  
ATOM    303  NH1 ARG A  38      15.646  62.591  18.540  1.00 13.74           N  
ANISOU  303  NH1 ARG A  38     2201   1556   1463    187    -63    143       N  
ATOM    304  NH2 ARG A  38      15.843  61.919  16.351  1.00 14.31           N  
ANISOU  304  NH2 ARG A  38     1873   1903   1659    288   -421    286       N  
ATOM    305  N   LEU A  39      21.353  59.343  20.666  1.00 10.67           N  
ANISOU  305  N   LEU A  39     1548   1655    850    -55   -229    149       N  
ATOM    306  CA  LEU A  39      22.505  59.895  19.951  1.00 11.16           C  
ANISOU  306  CA  LEU A  39     1639   1725    875    -72   -237     71       C  
ATOM    307  C   LEU A  39      23.540  58.808  19.612  1.00 11.25           C  
ANISOU  307  C   LEU A  39     1714   1677    883    -20   -202     50       C  
ATOM    308  O   LEU A  39      24.047  58.763  18.486  1.00 11.82           O  
ANISOU  308  O   LEU A  39     1938   1704    848     55   -173     31       O  
ATOM    309  CB  LEU A  39      23.165  61.020  20.765  1.00 10.82           C  
ANISOU  309  CB  LEU A  39     1602   1702    804   -162   -265     64       C  
ATOM    310  CG  LEU A  39      24.362  61.681  20.072  1.00 11.07           C  
ANISOU  310  CG  LEU A  39     1674   1923    609   -274   -268    220       C  
ATOM    311  CD1 LEU A  39      23.884  62.588  18.910  1.00 13.61           C  
ANISOU  311  CD1 LEU A  39     2108   2155    906   -213   -432    532       C  
ATOM    312  CD2 LEU A  39      25.219  62.460  21.070  1.00 12.19           C  
ANISOU  312  CD2 LEU A  39     1564   2113    951   -317   -151   -117       C  
ATOM    313  N   ALA A  40      23.866  57.958  20.591  1.00 11.17           N  
ANISOU  313  N   ALA A  40     1643   1661    940     13   -252      4       N  
ATOM    314  CA  ALA A  40      24.794  56.838  20.360  1.00 10.99           C  
ANISOU  314  CA  ALA A  40     1653   1635    885    -22   -235    -23       C  
ATOM    315  C   ALA A  40      24.246  55.849  19.313  1.00 11.39           C  
ANISOU  315  C   ALA A  40     1673   1802    853    -40   -205     -8       C  
ATOM    316  O   ALA A  40      24.974  55.381  18.427  1.00 11.31           O  
ANISOU  316  O   ALA A  40     1638   1821    837   -101   -184    -75       O  
ATOM    317  CB  ALA A  40      25.096  56.119  21.690  1.00 10.82           C  
ANISOU  317  CB  ALA A  40     1656   1570    883     32   -178     79       C  
ATOM    318  N   TRP A  41      22.965  55.515  19.443  1.00 11.92           N  
ANISOU  318  N   TRP A  41     1680   1958    891    -96   -253    -93       N  
ATOM    319  CA  TRP A  41      22.313  54.594  18.513  1.00 13.30           C  
ANISOU  319  CA  TRP A  41     1850   2121   1079    -76   -140    -42       C  
ATOM    320  C   TRP A  41      22.291  55.176  17.086  1.00 13.34           C  
ANISOU  320  C   TRP A  41     1879   2132   1055    -13   -114    -14       C  
ATOM    321  O   TRP A  41      22.644  54.479  16.132  1.00 13.08           O  
ANISOU  321  O   TRP A  41     1781   2245    945     10     12     -2       O  
ATOM    322  CB  TRP A  41      20.902  54.250  19.030  1.00 14.22           C  
ANISOU  322  CB  TRP A  41     1957   2217   1229   -130   -176   -122       C  
ATOM    323  CG  TRP A  41      19.833  54.134  17.980  1.00 16.03           C  
ANISOU  323  CG  TRP A  41     2219   2286   1585    -92   -195   -163       C  
ATOM    324  CD1 TRP A  41      18.737  54.944  17.833  1.00 16.69           C  
ANISOU  324  CD1 TRP A  41     2242   2394   1704   -162   -323   -160       C  
ATOM    325  CD2 TRP A  41      19.751  53.155  16.943  1.00 17.31           C  
ANISOU  325  CD2 TRP A  41     2405   2501   1669   -126   -149   -196       C  
ATOM    326  NE1 TRP A  41      17.983  54.529  16.762  1.00 18.68           N  
ANISOU  326  NE1 TRP A  41     2594   2520   1981    -82   -246   -137       N  
ATOM    327  CE2 TRP A  41      18.576  53.431  16.199  1.00 17.77           C  
ANISOU  327  CE2 TRP A  41     2447   2526   1778    -84   -149   -271       C  
ATOM    328  CE3 TRP A  41      20.546  52.062  16.576  1.00 16.97           C  
ANISOU  328  CE3 TRP A  41     2441   2320   1687    -96      8   -470       C  
ATOM    329  CZ2 TRP A  41      18.180  52.661  15.103  1.00 18.23           C  
ANISOU  329  CZ2 TRP A  41     2442   2581   1904   -100    -66   -234       C  
ATOM    330  CZ3 TRP A  41      20.144  51.283  15.461  1.00 16.51           C  
ANISOU  330  CZ3 TRP A  41     2381   2415   1476   -340   -200   -196       C  
ATOM    331  CH2 TRP A  41      18.975  51.591  14.753  1.00 16.76           C  
ANISOU  331  CH2 TRP A  41     2404   2301   1661    -92     16   -275       C  
ATOM    332  N   ALA A  42      21.894  56.445  16.951  1.00 13.11           N  
ANISOU  332  N   ALA A  42     1911   2074    994     48    -45     74       N  
ATOM    333  CA  ALA A  42      21.815  57.091  15.628  1.00 13.59           C  
ANISOU  333  CA  ALA A  42     2019   2031   1111    135    -68    101       C  
ATOM    334  C   ALA A  42      23.192  57.215  14.971  1.00 13.57           C  
ANISOU  334  C   ALA A  42     2052   2059   1044    153    -54     95       C  
ATOM    335  O   ALA A  42      23.303  57.161  13.738  1.00 14.31           O  
ANISOU  335  O   ALA A  42     2043   2223   1168    189    -90    239       O  
ATOM    336  CB  ALA A  42      21.148  58.457  15.740  1.00 13.36           C  
ANISOU  336  CB  ALA A  42     2060   1977   1038    207    -30     92       C  
ATOM    337  N   SER A  43      24.231  57.360  15.802  1.00 13.68           N  
ANISOU  337  N   SER A  43     2083   2050   1064    123    -67     82       N  
ATOM    338  CA  SER A  43      25.622  57.401  15.353  1.00 13.78           C  
ANISOU  338  CA  SER A  43     2142   2056   1037     96    -64    110       C  
ATOM    339  C   SER A  43      26.002  56.044  14.766  1.00 13.74           C  
ANISOU  339  C   SER A  43     2209   1985   1024    102    -26     83       C  
ATOM    340  O   SER A  43      26.571  55.959  13.670  1.00 14.09           O  
ANISOU  340  O   SER A  43     2298   2039   1014     61    106    206       O  
ATOM    341  CB  SER A  43      26.573  57.711  16.520  1.00 13.27           C  
ANISOU  341  CB  SER A  43     2066   1960   1013     57   -100     28       C  
ATOM    342  OG  SER A  43      26.372  59.006  17.051  1.00 15.57           O  
ANISOU  342  OG  SER A  43     2249   2422   1242    -39   -183    182       O  
ATOM    343  N   ALA A  44      25.672  54.981  15.494  1.00 13.33           N  
ANISOU  343  N   ALA A  44     2167   1977    917     52     76    104       N  
ATOM    344  CA  ALA A  44      26.126  53.637  15.133  1.00 13.67           C  
ANISOU  344  CA  ALA A  44     2181   1976   1037     67     41     94       C  
ATOM    345  C   ALA A  44      25.277  52.963  14.059  1.00 13.95           C  
ANISOU  345  C   ALA A  44     2193   2069   1038     60     40     55       C  
ATOM    346  O   ALA A  44      25.794  52.146  13.274  1.00 14.77           O  
ANISOU  346  O   ALA A  44     2236   2105   1269     39     -5    -63       O  
ATOM    347  CB  ALA A  44      26.178  52.755  16.380  1.00 13.53           C  
ANISOU  347  CB  ALA A  44     2219   2026    896    129     46    171       C  
ATOM    348  N   GLY A  45      23.984  53.301  14.020  1.00 14.05           N  
ANISOU  348  N   GLY A  45     2200   2098   1039     56     -7     31       N  
ATOM    349  CA  GLY A  45      22.993  52.534  13.259  1.00 14.37           C  
ANISOU  349  CA  GLY A  45     2266   2141   1051     -3    -87     50       C  
ATOM    350  C   GLY A  45      23.051  52.716  11.757  1.00 14.91           C  
ANISOU  350  C   GLY A  45     2350   2193   1122    -20    -89      2       C  
ATOM    351  O   GLY A  45      22.307  52.068  11.009  1.00 15.42           O  
ANISOU  351  O   GLY A  45     2429   2336   1094   -144   -198     26       O  
ATOM    352  N   THR A  46      23.936  53.610  11.320  1.00 15.17           N  
ANISOU  352  N   THR A  46     2434   2212   1114     51    -96     49       N  
ATOM    353  CA  THR A  46      24.131  53.899   9.905  1.00 15.01           C  
ANISOU  353  CA  THR A  46     2488   2118   1096    112    -20    -58       C  
ATOM    354  C   THR A  46      25.162  52.968   9.271  1.00 15.19           C  
ANISOU  354  C   THR A  46     2512   2116   1141    156    -20    -94       C  
ATOM    355  O   THR A  46      25.467  53.109   8.087  1.00 15.14           O  
ANISOU  355  O   THR A  46     2593   2067   1092    239    -44   -164       O  
ATOM    356  CB  THR A  46      24.628  55.352   9.696  1.00 14.96           C  
ANISOU  356  CB  THR A  46     2520   2078   1082     84    -31    -51       C  
ATOM    357  OG1 THR A  46      25.872  55.537  10.388  1.00 14.65           O  
ANISOU  357  OG1 THR A  46     2488   2046   1031     19   -127      9       O  
ATOM    358  CG2 THR A  46      23.610  56.366  10.183  1.00 15.62           C  
ANISOU  358  CG2 THR A  46     2533   2201   1198    101   -104    -63       C  
ATOM    359  N   PHE A  47      25.720  52.039  10.051  1.00 14.38           N  
ANISOU  359  N   PHE A  47     2383   2026   1053    225    -24   -141       N  
ATOM    360  CA  PHE A  47      26.729  51.133   9.499  1.00 14.89           C  
ANISOU  360  CA  PHE A  47     2370   2220   1065    179    -24   -203       C  
ATOM    361  C   PHE A  47      26.192  50.224   8.392  1.00 15.18           C  
ANISOU  361  C   PHE A  47     2417   2267   1083    133     33   -250       C  
ATOM    362  O   PHE A  47      25.153  49.568   8.553  1.00 15.04           O  
ANISOU  362  O   PHE A  47     2445   2264   1005     46     63   -280       O  
ATOM    363  CB  PHE A  47      27.388  50.277  10.581  1.00 14.68           C  
ANISOU  363  CB  PHE A  47     2282   2211   1082    237    -73   -191       C  
ATOM    364  CG  PHE A  47      28.536  49.469  10.065  1.00 15.07           C  
ANISOU  364  CG  PHE A  47     2234   2407   1081    178   -152   -229       C  
ATOM    365  CD1 PHE A  47      29.711  50.105   9.650  1.00 16.38           C  
ANISOU  365  CD1 PHE A  47     2355   2687   1179    227    -86   -135       C  
ATOM    366  CD2 PHE A  47      28.451  48.080   9.970  1.00 14.98           C  
ANISOU  366  CD2 PHE A  47     2139   2442   1110    171   -223   -288       C  
ATOM    367  CE1 PHE A  47      30.782  49.370   9.152  1.00 14.70           C  
ANISOU  367  CE1 PHE A  47     2052   2502   1030    319   -280   -188       C  
ATOM    368  CE2 PHE A  47      29.523  47.339   9.483  1.00 15.34           C  
ANISOU  368  CE2 PHE A  47     2199   2660    967     40   -137   -334       C  
ATOM    369  CZ  PHE A  47      30.689  47.991   9.071  1.00 16.16           C  
ANISOU  369  CZ  PHE A  47     2343   2618   1178    233   -241   -238       C  
ATOM    370  N   ASP A  48      26.902  50.200   7.265  1.00 15.69           N  
ANISOU  370  N   ASP A  48     2452   2392   1115     99    113   -368       N  
ATOM    371  CA  ASP A  48      26.591  49.249   6.194  1.00 16.49           C  
ANISOU  371  CA  ASP A  48     2550   2508   1207     43    201   -380       C  
ATOM    372  C   ASP A  48      27.769  48.303   6.033  1.00 17.08           C  
ANISOU  372  C   ASP A  48     2643   2573   1273     20    270   -408       C  
ATOM    373  O   ASP A  48      28.846  48.729   5.618  1.00 16.78           O  
ANISOU  373  O   ASP A  48     2474   2642   1260     89    310   -399       O  
ATOM    374  CB  ASP A  48      26.294  49.961   4.867  1.00 16.95           C  
ANISOU  374  CB  ASP A  48     2595   2620   1224    -11    144   -441       C  
ATOM    375  CG  ASP A  48      25.933  48.987   3.772  1.00 18.30           C  
ANISOU  375  CG  ASP A  48     2707   2856   1389      0    260   -460       C  
ATOM    376  OD1 ASP A  48      24.832  48.410   3.856  1.00 19.63           O  
ANISOU  376  OD1 ASP A  48     2838   3081   1541   -246    392   -536       O  
ATOM    377  OD2 ASP A  48      26.758  48.772   2.852  1.00 20.12           O  
ANISOU  377  OD2 ASP A  48     3117   3136   1389     -5    314   -592       O  
ATOM    378  N   LYS A  49      27.558  47.028   6.371  1.00 17.67           N  
ANISOU  378  N   LYS A  49     2791   2624   1297     42    377   -420       N  
ATOM    379  CA  LYS A  49      28.643  46.041   6.417  1.00 19.09           C  
ANISOU  379  CA  LYS A  49     2972   2766   1516    -41    426   -422       C  
ATOM    380  C   LYS A  49      29.279  45.802   5.040  1.00 19.49           C  
ANISOU  380  C   LYS A  49     3041   2835   1526    -37    465   -460       C  
ATOM    381  O   LYS A  49      30.499  45.673   4.938  1.00 19.71           O  
ANISOU  381  O   LYS A  49     3112   2887   1486    -29    483   -531       O  
ATOM    382  CB  LYS A  49      28.171  44.720   7.049  1.00 19.04           C  
ANISOU  382  CB  LYS A  49     2993   2718   1522    -30    414   -407       C  
ATOM    383  CG  LYS A  49      27.117  43.946   6.254  1.00 20.39           C  
ANISOU  383  CG  LYS A  49     3076   2860   1808   -135    351   -388       C  
ATOM    384  CD  LYS A  49      26.451  42.853   7.100  1.00 20.88           C  
ANISOU  384  CD  LYS A  49     3116   2890   1926   -165    378   -414       C  
ATOM    385  CE  LYS A  49      25.670  41.868   6.217  1.00 22.65           C  
ANISOU  385  CE  LYS A  49     3221   3049   2336   -327    313   -246       C  
ATOM    386  NZ  LYS A  49      24.718  41.018   6.995  1.00 24.80           N  
ANISOU  386  NZ  LYS A  49     3353   3366   2704   -258    205   -337       N  
ATOM    387  N   GLY A  50      28.450  45.789   3.997  1.00 20.21           N  
ANISOU  387  N   GLY A  50     3172   2910   1596    -85    512   -409       N  
ATOM    388  CA  GLY A  50      28.903  45.474   2.638  1.00 21.36           C  
ANISOU  388  CA  GLY A  50     3312   3060   1742   -119    480   -349       C  
ATOM    389  C   GLY A  50      29.899  46.492   2.110  1.00 22.00           C  
ANISOU  389  C   GLY A  50     3361   3157   1839   -115    509   -288       C  
ATOM    390  O   GLY A  50      30.850  46.138   1.391  1.00 22.96           O  
ANISOU  390  O   GLY A  50     3451   3174   2096    -86    518   -313       O  
ATOM    391  N   THR A  51      29.685  47.754   2.479  1.00 21.64           N  
ANISOU  391  N   THR A  51     3325   3120   1776   -143    456   -245       N  
ATOM    392  CA  THR A  51      30.525  48.857   2.009  1.00 21.68           C  
ANISOU  392  CA  THR A  51     3253   3199   1785   -150    430   -230       C  
ATOM    393  C   THR A  51      31.507  49.361   3.072  1.00 21.99           C  
ANISOU  393  C   THR A  51     3237   3236   1882   -162    396   -219       C  
ATOM    394  O   THR A  51      32.460  50.073   2.749  1.00 21.72           O  
ANISOU  394  O   THR A  51     3169   3294   1788   -258    518   -256       O  
ATOM    395  CB  THR A  51      29.673  50.042   1.484  1.00 21.63           C  
ANISOU  395  CB  THR A  51     3251   3191   1776   -155    422   -182       C  
ATOM    396  OG1 THR A  51      28.834  50.553   2.535  1.00 19.20           O  
ANISOU  396  OG1 THR A  51     3016   3020   1258    -47    518   -223       O  
ATOM    397  CG2 THR A  51      28.819  49.599   0.292  1.00 21.67           C  
ANISOU  397  CG2 THR A  51     3306   3180   1745   -214    418   -168       C  
ATOM    398  N   LYS A  52      31.262  48.980   4.327  1.00 21.47           N  
ANISOU  398  N   LYS A  52     3139   3221   1794   -128    349   -183       N  
ATOM    399  CA  LYS A  52      32.046  49.448   5.480  1.00 22.20           C  
ANISOU  399  CA  LYS A  52     3160   3271   2001    -65    286   -115       C  
ATOM    400  C   LYS A  52      31.942  50.967   5.652  1.00 21.46           C  
ANISOU  400  C   LYS A  52     3096   3181   1874    -90    231    -79       C  
ATOM    401  O   LYS A  52      32.916  51.652   5.990  1.00 22.69           O  
ANISOU  401  O   LYS A  52     3249   3285   2087   -107    207    -51       O  
ATOM    402  CB  LYS A  52      33.506  48.969   5.398  1.00 22.12           C  
ANISOU  402  CB  LYS A  52     3135   3286   1984    -72    271   -124       C  
ATOM    403  CG  LYS A  52      33.647  47.461   5.481  1.00 23.26           C  
ANISOU  403  CG  LYS A  52     3151   3401   2282     70    272   -160       C  
ATOM    404  CD  LYS A  52      35.100  47.004   5.397  1.00 25.34           C  
ANISOU  404  CD  LYS A  52     3387   3606   2633     92    447   -124       C  
ATOM    405  CE  LYS A  52      35.173  45.479   5.455  1.00 27.47           C  
ANISOU  405  CE  LYS A  52     3493   3874   3070    310    567   -134       C  
ATOM    406  NZ  LYS A  52      36.540  44.987   5.111  1.00 30.62           N  
ANISOU  406  NZ  LYS A  52     3817   4258   3559    331    613   -135       N  
ATOM    407  N   THR A  53      30.749  51.493   5.409  1.00 20.13           N  
ANISOU  407  N   THR A  53     2972   3050   1625    -60    203    -27       N  
ATOM    408  CA  THR A  53      30.524  52.933   5.509  1.00 18.86           C  
ANISOU  408  CA  THR A  53     2842   2882   1439   -107    173     37       C  
ATOM    409  C   THR A  53      29.563  53.243   6.641  1.00 18.05           C  
ANISOU  409  C   THR A  53     2778   2767   1310    -79    116     49       C  
ATOM    410  O   THR A  53      28.789  52.384   7.069  1.00 17.63           O  
ANISOU  410  O   THR A  53     2702   2661   1334   -139     54      5       O  
ATOM    411  CB  THR A  53      29.955  53.517   4.206  1.00 19.17           C  
ANISOU  411  CB  THR A  53     2892   2963   1427    -91    183     53       C  
ATOM    412  OG1 THR A  53      28.762  52.810   3.849  1.00 17.94           O  
ANISOU  412  OG1 THR A  53     2584   2904   1329   -233    371    103       O  
ATOM    413  CG2 THR A  53      30.987  53.431   3.064  1.00 18.56           C  
ANISOU  413  CG2 THR A  53     2814   2998   1237   -156    279    -12       C  
ATOM    414  N   GLY A  54      29.596  54.482   7.116  1.00 17.38           N  
ANISOU  414  N   GLY A  54     2707   2692   1202   -112    127     52       N  
ATOM    415  CA  GLY A  54      28.781  54.863   8.258  1.00 16.93           C  
ANISOU  415  CA  GLY A  54     2735   2620   1078    -88    149     38       C  
ATOM    416  C   GLY A  54      29.264  54.198   9.532  1.00 16.29           C  
ANISOU  416  C   GLY A  54     2625   2543   1020   -106    138     -3       C  
ATOM    417  O   GLY A  54      30.392  53.705   9.612  1.00 16.31           O  
ANISOU  417  O   GLY A  54     2586   2640    968   -132    131     11       O  
ATOM    418  N   GLY A  55      28.396  54.160  10.533  1.00 15.56           N  
ANISOU  418  N   GLY A  55     2586   2465    858   -109    170    -15       N  
ATOM    419  CA  GLY A  55      28.800  53.626  11.818  1.00 14.84           C  
ANISOU  419  CA  GLY A  55     2521   2283    831   -113    153    -72       C  
ATOM    420  C   GLY A  55      29.290  54.691  12.792  1.00 14.62           C  
ANISOU  420  C   GLY A  55     2430   2170    951   -127    187    -96       C  
ATOM    421  O   GLY A  55      29.311  55.888  12.475  1.00 13.79           O  
ANISOU  421  O   GLY A  55     2325   2057    857   -121    232    -65       O  
ATOM    422  N   PRO A  56      29.689  54.246  13.991  1.00 13.69           N  
ANISOU  422  N   PRO A  56     2368   2027    805   -114    132   -123       N  
ATOM    423  CA  PRO A  56      29.975  55.093  15.164  1.00 14.20           C  
ANISOU  423  CA  PRO A  56     2421   2000    974   -155    115   -146       C  
ATOM    424  C   PRO A  56      31.327  55.819  15.076  1.00 14.32           C  
ANISOU  424  C   PRO A  56     2435   1938   1068   -136     52   -170       C  
ATOM    425  O   PRO A  56      32.252  55.530  15.839  1.00 14.74           O  
ANISOU  425  O   PRO A  56     2477   1933   1187   -244     15    -84       O  
ATOM    426  CB  PRO A  56      29.933  54.099  16.327  1.00 14.23           C  
ANISOU  426  CB  PRO A  56     2431   1993    982   -134    111   -147       C  
ATOM    427  CG  PRO A  56      30.277  52.781  15.744  1.00 13.64           C  
ANISOU  427  CG  PRO A  56     2416   2010    754    -58    124   -169       C  
ATOM    428  CD  PRO A  56      29.877  52.809  14.278  1.00 13.82           C  
ANISOU  428  CD  PRO A  56     2430   2031    788    -86    151   -194       C  
ATOM    429  N   PHE A  57      31.426  56.760  14.140  1.00 14.44           N  
ANISOU  429  N   PHE A  57     2445   1772   1267   -103     70   -195       N  
ATOM    430  CA  PHE A  57      32.708  57.415  13.858  1.00 14.14           C  
ANISOU  430  CA  PHE A  57     2338   1813   1222     27     57   -218       C  
ATOM    431  C   PHE A  57      32.641  58.927  13.922  1.00 14.74           C  
ANISOU  431  C   PHE A  57     2436   1896   1266     26      1   -158       C  
ATOM    432  O   PHE A  57      33.324  59.623  13.180  1.00 15.24           O  
ANISOU  432  O   PHE A  57     2556   1974   1261     57    116   -146       O  
ATOM    433  CB  PHE A  57      33.303  56.875  12.550  1.00 13.83           C  
ANISOU  433  CB  PHE A  57     2330   1784   1138    -25    -35   -205       C  
ATOM    434  CG  PHE A  57      33.496  55.393  12.587  1.00 13.63           C  
ANISOU  434  CG  PHE A  57     2243   1769   1165     45     78   -284       C  
ATOM    435  CD1 PHE A  57      34.498  54.836  13.374  1.00 13.40           C  
ANISOU  435  CD1 PHE A  57     2169   1661   1261     44     14   -250       C  
ATOM    436  CD2 PHE A  57      32.626  54.552  11.908  1.00 15.04           C  
ANISOU  436  CD2 PHE A  57     2260   1828   1624     79    159   -258       C  
ATOM    437  CE1 PHE A  57      34.654  53.451  13.456  1.00 14.53           C  
ANISOU  437  CE1 PHE A  57     2388   1757   1374    -50    -74   -196       C  
ATOM    438  CE2 PHE A  57      32.763  53.182  11.980  1.00 15.05           C  
ANISOU  438  CE2 PHE A  57     2348   1728   1643    296    167   -229       C  
ATOM    439  CZ  PHE A  57      33.789  52.625  12.756  1.00 15.21           C  
ANISOU  439  CZ  PHE A  57     2416   1925   1437     66   -143   -276       C  
ATOM    440  N   GLY A  58      31.824  59.425  14.847  1.00 14.44           N  
ANISOU  440  N   GLY A  58     2423   1885   1175    167    -30   -160       N  
ATOM    441  CA  GLY A  58      31.831  60.851  15.178  1.00 15.41           C  
ANISOU  441  CA  GLY A  58     2519   1969   1366    101    -43   -124       C  
ATOM    442  C   GLY A  58      31.090  61.760  14.209  1.00 15.48           C  
ANISOU  442  C   GLY A  58     2498   2026   1358    128    -99   -151       C  
ATOM    443  O   GLY A  58      31.028  62.979  14.423  1.00 15.76           O  
ANISOU  443  O   GLY A  58     2529   1978   1480      6   -124   -106       O  
ATOM    444  N   THR A  59      30.509  61.185  13.157  1.00 15.95           N  
ANISOU  444  N   THR A  59     2519   2038   1502     81   -105   -118       N  
ATOM    445  CA  THR A  59      29.929  61.993  12.078  1.00 16.50           C  
ANISOU  445  CA  THR A  59     2595   2237   1435     97   -172   -191       C  
ATOM    446  C   THR A  59      28.606  62.677  12.453  1.00 17.06           C  
ANISOU  446  C   THR A  59     2674   2192   1615     58   -145   -132       C  
ATOM    447  O   THR A  59      28.207  63.647  11.814  1.00 17.11           O  
ANISOU  447  O   THR A  59     2707   2220   1574     40    -65    -73       O  
ATOM    448  CB  THR A  59      29.753  61.173  10.780  1.00 16.50           C  
ANISOU  448  CB  THR A  59     2597   2228   1444     94   -171   -213       C  
ATOM    449  OG1 THR A  59      28.848  60.091  11.024  1.00 16.16           O  
ANISOU  449  OG1 THR A  59     2579   2327   1231     65   -438   -297       O  
ATOM    450  CG2 THR A  59      31.110  60.629  10.293  1.00 15.56           C  
ANISOU  450  CG2 THR A  59     2503   2413    996    172   -199   -131       C  
ATOM    451  N   ILE A  60      27.950  62.193  13.507  1.00 17.53           N  
ANISOU  451  N   ILE A  60     2715   2133   1812     -8   -107    -66       N  
ATOM    452  CA  ILE A  60      26.660  62.742  13.932  1.00 18.48           C  
ANISOU  452  CA  ILE A  60     2859   2165   1996     36    -73    -18       C  
ATOM    453  C   ILE A  60      26.755  64.217  14.332  1.00 19.17           C  
ANISOU  453  C   ILE A  60     2924   2270   2090     61    -63     75       C  
ATOM    454  O   ILE A  60      25.764  64.921  14.270  1.00 19.91           O  
ANISOU  454  O   ILE A  60     3012   2316   2234     83    -29    120       O  
ATOM    455  CB  ILE A  60      25.981  61.889  15.062  1.00 18.65           C  
ANISOU  455  CB  ILE A  60     2815   2174   2096     43    -60    -34       C  
ATOM    456  CG1 ILE A  60      24.482  62.206  15.200  1.00 19.60           C  
ANISOU  456  CG1 ILE A  60     2915   2294   2236     17   -130   -142       C  
ATOM    457  CG2 ILE A  60      26.667  62.087  16.396  1.00 17.53           C  
ANISOU  457  CG2 ILE A  60     2905   1965   1788    -30     14   -180       C  
ATOM    458  CD1 ILE A  60      23.621  61.614  14.142  1.00 21.02           C  
ANISOU  458  CD1 ILE A  60     3112   2585   2286    121   -184   -510       C  
ATOM    459  N   LYS A  61      27.945  64.684  14.715  1.00 19.99           N  
ANISOU  459  N   LYS A  61     3052   2369   2171     32    -87    166       N  
ATOM    460  CA  LYS A  61      28.128  66.099  15.058  1.00 21.50           C  
ANISOU  460  CA  LYS A  61     3140   2571   2457     57   -150    215       C  
ATOM    461  C   LYS A  61      28.033  67.016  13.822  1.00 21.79           C  
ANISOU  461  C   LYS A  61     3147   2583   2546     82   -164    255       C  
ATOM    462  O   LYS A  61      27.830  68.227  13.948  1.00 22.03           O  
ANISOU  462  O   LYS A  61     3237   2592   2541     93   -159    241       O  
ATOM    463  CB  LYS A  61      29.453  66.310  15.804  1.00 22.00           C  
ANISOU  463  CB  LYS A  61     3181   2617   2561     41   -149    231       C  
ATOM    464  CG  LYS A  61      30.646  66.416  14.889  1.00 24.48           C  
ANISOU  464  CG  LYS A  61     3332   3060   2909     94   -204    215       C  
ATOM    465  CD  LYS A  61      31.956  66.530  15.631  1.00 28.49           C  
ANISOU  465  CD  LYS A  61     3671   3790   3364    -41   -397    335       C  
ATOM    466  CE  LYS A  61      33.091  66.365  14.632  1.00 31.81           C  
ANISOU  466  CE  LYS A  61     3836   4371   3877    -15   -495    313       C  
ATOM    467  NZ  LYS A  61      34.452  66.518  15.221  1.00 34.07           N  
ANISOU  467  NZ  LYS A  61     4114   4666   4164   -229   -811    284       N  
ATOM    468  N   HIS A  62      28.199  66.434  12.636  1.00 22.17           N  
ANISOU  468  N   HIS A  62     3181   2636   2606    101   -255    322       N  
ATOM    469  CA  HIS A  62      28.128  67.179  11.378  1.00 23.22           C  
ANISOU  469  CA  HIS A  62     3243   2802   2777    138   -242    403       C  
ATOM    470  C   HIS A  62      26.698  67.701  11.145  1.00 23.02           C  
ANISOU  470  C   HIS A  62     3254   2730   2762    141   -321    470       C  
ATOM    471  O   HIS A  62      25.744  66.913  11.164  1.00 23.00           O  
ANISOU  471  O   HIS A  62     3275   2802   2661    173   -346    534       O  
ATOM    472  CB  HIS A  62      28.553  66.289  10.204  1.00 23.35           C  
ANISOU  472  CB  HIS A  62     3167   2868   2833    209   -233    368       C  
ATOM    473  CG  HIS A  62      30.005  65.908  10.202  1.00 26.38           C  
ANISOU  473  CG  HIS A  62     3357   3478   3187    225    -79    350       C  
ATOM    474  ND1 HIS A  62      30.709  65.601  11.348  1.00 28.18           N  
ANISOU  474  ND1 HIS A  62     3302   3722   3682    393    -17    274       N  
ATOM    475  CD2 HIS A  62      30.875  65.749   9.176  1.00 29.21           C  
ANISOU  475  CD2 HIS A  62     3409   3969   3720    263     21    277       C  
ATOM    476  CE1 HIS A  62      31.952  65.286  11.031  1.00 28.93           C  
ANISOU  476  CE1 HIS A  62     3297   4001   3692    204     27    370       C  
ATOM    477  NE2 HIS A  62      32.078  65.360   9.718  1.00 30.23           N  
ANISOU  477  NE2 HIS A  62     3339   4301   3845    323    -37    343       N  
ATOM    478  N   PRO A  63      26.537  69.031  10.955  1.00 23.36           N  
ANISOU  478  N   PRO A  63     3298   2702   2875    129   -354    526       N  
ATOM    479  CA  PRO A  63      25.226  69.588  10.591  1.00 23.41           C  
ANISOU  479  CA  PRO A  63     3352   2635   2908    125   -352    562       C  
ATOM    480  C   PRO A  63      24.483  68.763   9.525  1.00 22.86           C  
ANISOU  480  C   PRO A  63     3336   2579   2768    125   -358    564       C  
ATOM    481  O   PRO A  63      23.280  68.546   9.663  1.00 22.80           O  
ANISOU  481  O   PRO A  63     3383   2538   2741    138   -341    541       O  
ATOM    482  CB  PRO A  63      25.580  70.983  10.060  1.00 23.64           C  
ANISOU  482  CB  PRO A  63     3362   2633   2985    119   -393    591       C  
ATOM    483  CG  PRO A  63      26.741  71.386  10.900  1.00 24.08           C  
ANISOU  483  CG  PRO A  63     3368   2691   3087    111   -409    538       C  
ATOM    484  CD  PRO A  63      27.550  70.099  11.092  1.00 23.75           C  
ANISOU  484  CD  PRO A  63     3362   2710   2952    154   -365    504       C  
ATOM    485  N   ALA A  64      25.205  68.286   8.504  1.00 22.56           N  
ANISOU  485  N   ALA A  64     3372   2559   2639    109   -336    578       N  
ATOM    486  CA  ALA A  64      24.625  67.469   7.423  1.00 22.38           C  
ANISOU  486  CA  ALA A  64     3372   2621   2509    131   -326    606       C  
ATOM    487  C   ALA A  64      23.922  66.208   7.932  1.00 22.18           C  
ANISOU  487  C   ALA A  64     3347   2658   2421    138   -364    579       C  
ATOM    488  O   ALA A  64      22.836  65.858   7.458  1.00 22.00           O  
ANISOU  488  O   ALA A  64     3328   2704   2327     90   -447    660       O  
ATOM    489  CB  ALA A  64      25.696  67.100   6.394  1.00 22.91           C  
ANISOU  489  CB  ALA A  64     3421   2667   2615    156   -297    571       C  
ATOM    490  N   GLU A  65      24.532  65.540   8.910  1.00 20.85           N  
ANISOU  490  N   GLU A  65     3213   2570   2137    201   -381    603       N  
ATOM    491  CA  GLU A  65      23.931  64.332   9.480  1.00 20.38           C  
ANISOU  491  CA  GLU A  65     3156   2576   2011    224   -399    485       C  
ATOM    492  C   GLU A  65      22.819  64.658  10.480  1.00 20.41           C  
ANISOU  492  C   GLU A  65     3172   2634   1947    234   -443    478       C  
ATOM    493  O   GLU A  65      21.813  63.950  10.553  1.00 20.40           O  
ANISOU  493  O   GLU A  65     3159   2694   1898    234   -508    428       O  
ATOM    494  CB  GLU A  65      24.985  63.424  10.105  1.00 19.51           C  
ANISOU  494  CB  GLU A  65     3104   2495   1813    271   -377    510       C  
ATOM    495  CG  GLU A  65      24.397  62.076  10.556  1.00 18.46           C  
ANISOU  495  CG  GLU A  65     2934   2315   1765    230   -386    458       C  
ATOM    496  CD  GLU A  65      25.442  61.016  10.820  1.00 18.25           C  
ANISOU  496  CD  GLU A  65     2909   2460   1566     96   -299    412       C  
ATOM    497  OE1 GLU A  65      26.607  61.212  10.416  1.00 16.89           O  
ANISOU  497  OE1 GLU A  65     2653   2373   1390   -108   -200    390       O  
ATOM    498  OE2 GLU A  65      25.088  59.974  11.420  1.00 18.66           O  
ANISOU  498  OE2 GLU A  65     2988   2382   1719     56   -123    365       O  
ATOM    499  N   LEU A  66      22.996  65.741  11.233  1.00 20.46           N  
ANISOU  499  N   LEU A  66     3169   2643   1963    246   -475    395       N  
ATOM    500  CA  LEU A  66      21.963  66.197  12.173  1.00 21.09           C  
ANISOU  500  CA  LEU A  66     3152   2792   2066    244   -528    359       C  
ATOM    501  C   LEU A  66      20.696  66.583  11.423  1.00 21.53           C  
ANISOU  501  C   LEU A  66     3174   2856   2148    280   -526    343       C  
ATOM    502  O   LEU A  66      19.584  66.463  11.950  1.00 21.64           O  
ANISOU  502  O   LEU A  66     3120   2922   2180    327   -521    295       O  
ATOM    503  CB  LEU A  66      22.465  67.381  13.002  1.00 20.84           C  
ANISOU  503  CB  LEU A  66     3159   2723   2035    217   -548    308       C  
ATOM    504  CG  LEU A  66      23.517  67.021  14.056  1.00 20.90           C  
ANISOU  504  CG  LEU A  66     3230   2779   1932     78   -627    366       C  
ATOM    505  CD1 LEU A  66      24.108  68.281  14.670  1.00 20.92           C  
ANISOU  505  CD1 LEU A  66     3104   2846   1998    -88   -612    300       C  
ATOM    506  CD2 LEU A  66      22.926  66.105  15.142  1.00 20.26           C  
ANISOU  506  CD2 LEU A  66     2971   2805   1920   -140   -462    244       C  
ATOM    507  N   ALA A  67      20.883  66.994  10.174  1.00 21.70           N  
ANISOU  507  N   ALA A  67     3195   2911   2137    278   -530    397       N  
ATOM    508  CA  ALA A  67      19.794  67.414   9.312  1.00 22.65           C  
ANISOU  508  CA  ALA A  67     3306   3117   2182    221   -608    411       C  
ATOM    509  C   ALA A  67      18.942  66.255   8.785  1.00 22.97           C  
ANISOU  509  C   ALA A  67     3332   3197   2197    193   -648    424       C  
ATOM    510  O   ALA A  67      17.829  66.484   8.282  1.00 23.17           O  
ANISOU  510  O   ALA A  67     3319   3302   2181    156   -714    476       O  
ATOM    511  CB  ALA A  67      20.335  68.261   8.158  1.00 23.04           C  
ANISOU  511  CB  ALA A  67     3366   3158   2229    238   -568    429       C  
ATOM    512  N   HIS A  68      19.448  65.022   8.891  1.00 22.64           N  
ANISOU  512  N   HIS A  68     3340   3211   2051    138   -710    418       N  
ATOM    513  CA  HIS A  68      18.661  63.853   8.488  1.00 22.57           C  
ANISOU  513  CA  HIS A  68     3289   3269   2017     99   -756    375       C  
ATOM    514  C   HIS A  68      17.356  63.832   9.277  1.00 22.64           C  
ANISOU  514  C   HIS A  68     3253   3256   2092    112   -768    373       C  
ATOM    515  O   HIS A  68      17.362  64.070  10.482  1.00 22.11           O  
ANISOU  515  O   HIS A  68     3121   3254   2026    112   -818    438       O  
ATOM    516  CB  HIS A  68      19.433  62.544   8.673  1.00 22.42           C  
ANISOU  516  CB  HIS A  68     3343   3299   1874     71   -773    350       C  
ATOM    517  CG  HIS A  68      20.676  62.440   7.841  1.00 22.29           C  
ANISOU  517  CG  HIS A  68     3427   3368   1673    -21   -888    288       C  
ATOM    518  ND1 HIS A  68      21.547  61.376   7.945  1.00 22.91           N  
ANISOU  518  ND1 HIS A  68     3798   3470   1435   -210   -911    328       N  
ATOM    519  CD2 HIS A  68      21.191  63.256   6.889  1.00 22.73           C  
ANISOU  519  CD2 HIS A  68     3591   3420   1622    -42   -934    250       C  
ATOM    520  CE1 HIS A  68      22.545  61.539   7.093  1.00 24.06           C  
ANISOU  520  CE1 HIS A  68     3815   3644   1683   -191   -854    149       C  
ATOM    521  NE2 HIS A  68      22.353  62.673   6.441  1.00 23.37           N  
ANISOU  521  NE2 HIS A  68     3922   3646   1310   -138   -885    287       N  
ATOM    522  N   SER A  69      16.233  63.591   8.589  1.00 22.75           N  
ANISOU  522  N   SER A  69     3207   3275   2160    129   -769    374       N  
ATOM    523  CA  SER A  69      14.923  63.664   9.238  1.00 22.90           C  
ANISOU  523  CA  SER A  69     3193   3283   2225    133   -729    306       C  
ATOM    524  C   SER A  69      14.827  62.728  10.448  1.00 22.01           C  
ANISOU  524  C   SER A  69     3054   3182   2125    173   -714    287       C  
ATOM    525  O   SER A  69      14.200  63.080  11.447  1.00 22.84           O  
ANISOU  525  O   SER A  69     3138   3303   2236    200   -690    347       O  
ATOM    526  CB  SER A  69      13.772  63.410   8.256  1.00 23.24           C  
ANISOU  526  CB  SER A  69     3287   3254   2285    133   -767    303       C  
ATOM    527  OG  SER A  69      13.818  62.094   7.734  1.00 26.54           O  
ANISOU  527  OG  SER A  69     3712   3634   2738     59   -739    126       O  
ATOM    528  N   ALA A  70      15.473  61.566  10.362  1.00 21.03           N  
ANISOU  528  N   ALA A  70     2895   3077   2018    180   -663    183       N  
ATOM    529  CA  ALA A  70      15.467  60.585  11.456  1.00 20.23           C  
ANISOU  529  CA  ALA A  70     2731   2961   1993    247   -621     95       C  
ATOM    530  C   ALA A  70      16.164  61.128  12.700  1.00 19.29           C  
ANISOU  530  C   ALA A  70     2595   2836   1897    276   -581     59       C  
ATOM    531  O   ALA A  70      15.958  60.612  13.801  1.00 19.25           O  
ANISOU  531  O   ALA A  70     2570   2860   1883    225   -529    -33       O  
ATOM    532  CB  ALA A  70      16.114  59.266  11.019  1.00 20.56           C  
ANISOU  532  CB  ALA A  70     2767   3017   2026    222   -644     48       C  
ATOM    533  N   ASN A  71      16.983  62.164  12.507  1.00 18.52           N  
ANISOU  533  N   ASN A  71     2435   2770   1829    333   -540     68       N  
ATOM    534  CA  ASN A  71      17.815  62.725  13.570  1.00 17.93           C  
ANISOU  534  CA  ASN A  71     2332   2652   1828    393   -478    138       C  
ATOM    535  C   ASN A  71      17.311  64.033  14.173  1.00 17.95           C  
ANISOU  535  C   ASN A  71     2314   2646   1860    409   -422    156       C  
ATOM    536  O   ASN A  71      18.073  64.718  14.866  1.00 17.82           O  
ANISOU  536  O   ASN A  71     2305   2667   1799    477   -414    142       O  
ATOM    537  CB  ASN A  71      19.259  62.888  13.061  1.00 17.22           C  
ANISOU  537  CB  ASN A  71     2207   2615   1718    468   -484    122       C  
ATOM    538  CG  ASN A  71      19.965  61.562  12.888  1.00 17.04           C  
ANISOU  538  CG  ASN A  71     2266   2583   1624    460   -453    153       C  
ATOM    539  OD1 ASN A  71      19.594  60.559  13.504  1.00 16.66           O  
ANISOU  539  OD1 ASN A  71     2468   2430   1432    799   -227    385       O  
ATOM    540  ND2 ASN A  71      20.998  61.548  12.048  1.00 14.59           N  
ANISOU  540  ND2 ASN A  71     1729   2303   1511    886   -265    315       N  
ATOM    541  N   ASN A  72      16.043  64.378  13.906  1.00 17.88           N  
ANISOU  541  N   ASN A  72     2287   2591   1915    414   -442    171       N  
ATOM    542  C   ASN A  72      15.596  65.623  15.990  1.00 18.20           C  
ANISOU  542  C   ASN A  72     2326   2532   2056    399   -395    186       C  
ATOM    543  O   ASN A  72      15.250  64.668  16.685  1.00 18.02           O  
ANISOU  543  O   ASN A  72     2401   2477   1968    405   -343    271       O  
ATOM    544  CA AASN A  72      15.418  65.581  14.483  0.50 18.02           C  
ANISOU  544  CA AASN A  72     2295   2555   1994    410   -430    220       C  
ATOM    545  CB AASN A  72      13.911  65.625  14.201  0.50 18.00           C  
ANISOU  545  CB AASN A  72     2265   2563   2012    438   -470    236       C  
ATOM    546  CG AASN A  72      13.571  66.121  12.811  0.50 18.24           C  
ANISOU  546  CG AASN A  72     2252   2614   2064    430   -599    274       C  
ATOM    547  OD1AASN A  72      14.426  66.600  12.062  0.50 17.49           O  
ANISOU  547  OD1AASN A  72     2288   2618   1737    312   -782    504       O  
ATOM    548  ND2AASN A  72      12.293  66.014  12.462  0.50 19.41           N  
ANISOU  548  ND2AASN A  72     2298   2684   2391    416   -822    339       N  
ATOM    549  CA BASN A  72      15.424  65.574  14.468  0.50 18.31           C  
ANISOU  549  CA BASN A  72     2366   2585   2006    399   -401    203       C  
ATOM    550  CB BASN A  72      13.937  65.591  14.096  0.50 18.58           C  
ANISOU  550  CB BASN A  72     2396   2626   2035    423   -410    204       C  
ATOM    551  CG BASN A  72      13.312  66.955  14.223  0.50 19.83           C  
ANISOU  551  CG BASN A  72     2678   2750   2104    357   -431    176       C  
ATOM    552  OD1BASN A  72      12.751  67.481  13.263  0.50 21.87           O  
ANISOU  552  OD1BASN A  72     3122   2952   2234    461   -500    170       O  
ATOM    553  ND2BASN A  72      13.376  67.530  15.416  0.50 20.78           N  
ANISOU  553  ND2BASN A  72     2729   3079   2087    276   -470    295       N  
ATOM    554  N   GLY A  73      16.119  66.739  16.492  1.00 18.34           N  
ANISOU  554  N   GLY A  73     2376   2513   2077    360   -362    168       N  
ATOM    555  CA  GLY A  73      16.333  66.924  17.927  1.00 17.99           C  
ANISOU  555  CA  GLY A  73     2370   2357   2105    355   -392    153       C  
ATOM    556  C   GLY A  73      17.692  66.484  18.453  1.00 17.69           C  
ANISOU  556  C   GLY A  73     2434   2230   2056    321   -383    144       C  
ATOM    557  O   GLY A  73      18.055  66.833  19.570  1.00 18.58           O  
ANISOU  557  O   GLY A  73     2546   2342   2170    351   -390     71       O  
ATOM    558  N   LEU A  74      18.455  65.728  17.667  1.00 16.84           N  
ANISOU  558  N   LEU A  74     2398   2063   1937    302   -333    141       N  
ATOM    559  CA  LEU A  74      19.770  65.286  18.138  1.00 16.79           C  
ANISOU  559  CA  LEU A  74     2541   1955   1881    292   -265    192       C  
ATOM    560  C   LEU A  74      20.814  66.402  18.190  1.00 16.89           C  
ANISOU  560  C   LEU A  74     2561   1932   1924    308   -259    222       C  
ATOM    561  O   LEU A  74      21.848  66.254  18.847  1.00 16.59           O  
ANISOU  561  O   LEU A  74     2536   1845   1920    235   -236    226       O  
ATOM    562  CB  LEU A  74      20.281  64.075  17.347  1.00 16.29           C  
ANISOU  562  CB  LEU A  74     2529   1860   1800    331   -278    168       C  
ATOM    563  CG  LEU A  74      19.600  62.734  17.667  1.00 15.66           C  
ANISOU  563  CG  LEU A  74     2633   1832   1485    216   -158    264       C  
ATOM    564  CD1 LEU A  74      20.212  61.628  16.840  1.00 15.09           C  
ANISOU  564  CD1 LEU A  74     2709   1776   1246    300     91    228       C  
ATOM    565  CD2 LEU A  74      19.656  62.350  19.164  1.00 14.73           C  
ANISOU  565  CD2 LEU A  74     2991   1675    930    247   -111    386       C  
ATOM    566  N   ASP A  75      20.532  67.522  17.520  1.00 17.52           N  
ANISOU  566  N   ASP A  75     2653   1982   2021    303   -258    269       N  
ATOM    567  CA  ASP A  75      21.360  68.721  17.641  1.00 18.15           C  
ANISOU  567  CA  ASP A  75     2728   2068   2098    322   -280    308       C  
ATOM    568  C   ASP A  75      21.422  69.193  19.103  1.00 17.65           C  
ANISOU  568  C   ASP A  75     2661   2086   1957    298   -246    335       C  
ATOM    569  O   ASP A  75      22.445  69.714  19.548  1.00 17.89           O  
ANISOU  569  O   ASP A  75     2683   2187   1927    297   -262    340       O  
ATOM    570  CB  ASP A  75      20.857  69.843  16.709  1.00 18.79           C  
ANISOU  570  CB  ASP A  75     2802   2130   2206    316   -290    311       C  
ATOM    571  CG  ASP A  75      19.466  70.349  17.073  1.00 21.44           C  
ANISOU  571  CG  ASP A  75     3108   2270   2768    351   -364    388       C  
ATOM    572  OD1 ASP A  75      18.580  69.545  17.458  1.00 21.65           O  
ANISOU  572  OD1 ASP A  75     2820   2580   2824    332   -530    396       O  
ATOM    573  OD2 ASP A  75      19.257  71.580  16.950  1.00 26.69           O  
ANISOU  573  OD2 ASP A  75     3602   2895   3641    518   -317    233       O  
ATOM    574  N   ILE A  76      20.322  69.002  19.832  1.00 16.89           N  
ANISOU  574  N   ILE A  76     2556   2027   1831    318   -196    351       N  
ATOM    575  CA  ILE A  76      20.276  69.279  21.271  1.00 16.60           C  
ANISOU  575  CA  ILE A  76     2428   2150   1729    282   -103    301       C  
ATOM    576  C   ILE A  76      21.304  68.431  22.040  1.00 15.71           C  
ANISOU  576  C   ILE A  76     2334   1997   1637    238    -61    306       C  
ATOM    577  O   ILE A  76      22.018  68.950  22.925  1.00 15.50           O  
ANISOU  577  O   ILE A  76     2212   2022   1654    234   -238    233       O  
ATOM    578  CB  ILE A  76      18.863  68.998  21.859  1.00 17.24           C  
ANISOU  578  CB  ILE A  76     2444   2236   1868    278   -149    273       C  
ATOM    579  CG1 ILE A  76      17.790  69.822  21.143  1.00 18.04           C  
ANISOU  579  CG1 ILE A  76     2571   2345   1937    381   -131    218       C  
ATOM    580  CG2 ILE A  76      18.839  69.229  23.394  1.00 16.59           C  
ANISOU  580  CG2 ILE A  76     2364   2399   1539    197     12    321       C  
ATOM    581  CD1 ILE A  76      16.374  69.434  21.532  1.00 18.12           C  
ANISOU  581  CD1 ILE A  76     2430   2390   2064    329   -124    311       C  
ATOM    582  N   ALA A  77      21.364  67.139  21.711  1.00 15.05           N  
ANISOU  582  N   ALA A  77     2278   1932   1508    158     46    315       N  
ATOM    583  CA  ALA A  77      22.300  66.190  22.339  1.00 14.22           C  
ANISOU  583  CA  ALA A  77     2256   1727   1418    105    116    348       C  
ATOM    584  C   ALA A  77      23.737  66.609  22.105  1.00 13.81           C  
ANISOU  584  C   ALA A  77     2246   1629   1373     94    124    336       C  
ATOM    585  O   ALA A  77      24.542  66.677  23.034  1.00 12.70           O  
ANISOU  585  O   ALA A  77     2180   1442   1203     69    100    404       O  
ATOM    586  CB  ALA A  77      22.065  64.761  21.817  1.00 14.76           C  
ANISOU  586  CB  ALA A  77     2321   1816   1471     97    119    317       C  
ATOM    587  N   VAL A  78      24.036  66.925  20.845  1.00 12.99           N  
ANISOU  587  N   VAL A  78     2140   1585   1209     35    179    262       N  
ATOM    588  CA  VAL A  78      25.368  67.333  20.450  1.00 12.93           C  
ANISOU  588  CA  VAL A  78     2189   1514   1206     -7    184    257       C  
ATOM    589  C   VAL A  78      25.776  68.609  21.200  1.00 12.72           C  
ANISOU  589  C   VAL A  78     2182   1465   1184     68    170    201       C  
ATOM    590  O   VAL A  78      26.869  68.671  21.775  1.00 12.72           O  
ANISOU  590  O   VAL A  78     2169   1390   1273    188     93    165       O  
ATOM    591  CB  VAL A  78      25.460  67.492  18.908  1.00 12.76           C  
ANISOU  591  CB  VAL A  78     2162   1508   1177    -22    184    251       C  
ATOM    592  CG1 VAL A  78      26.765  68.171  18.514  1.00 13.40           C  
ANISOU  592  CG1 VAL A  78     2120   1692   1278   -168    280    364       C  
ATOM    593  CG2 VAL A  78      25.315  66.114  18.224  1.00 12.57           C  
ANISOU  593  CG2 VAL A  78     2266   1521    987    -40    262    214       C  
ATOM    594  N   ARG A  79      24.886  69.599  21.221  1.00 13.19           N  
ANISOU  594  N   ARG A  79     2251   1499   1260    105     72    171       N  
ATOM    595  CA  ARG A  79      25.118  70.866  21.927  1.00 14.80           C  
ANISOU  595  CA  ARG A  79     2403   1660   1557    198     91    164       C  
ATOM    596  C   ARG A  79      25.350  70.638  23.433  1.00 14.16           C  
ANISOU  596  C   ARG A  79     2325   1638   1417    149    129    125       C  
ATOM    597  O   ARG A  79      26.285  71.207  24.018  1.00 14.07           O  
ANISOU  597  O   ARG A  79     2311   1653   1381     97    180    186       O  
ATOM    598  CB  ARG A  79      23.934  71.811  21.681  1.00 15.30           C  
ANISOU  598  CB  ARG A  79     2494   1644   1674    249     13    151       C  
ATOM    599  CG  ARG A  79      23.988  73.173  22.367  1.00 19.79           C  
ANISOU  599  CG  ARG A  79     2881   2213   2425    330      8    242       C  
ATOM    600  CD  ARG A  79      22.569  73.767  22.442  1.00 26.35           C  
ANISOU  600  CD  ARG A  79     3710   2961   3338    405    137    459       C  
ATOM    601  NE  ARG A  79      21.863  73.299  23.641  1.00 31.43           N  
ANISOU  601  NE  ARG A  79     4297   3577   4068    346     63    534       N  
ATOM    602  CZ  ARG A  79      20.551  73.082  23.730  1.00 33.53           C  
ANISOU  602  CZ  ARG A  79     4740   3777   4221    173    -29    694       C  
ATOM    603  NH1 ARG A  79      19.758  73.259  22.681  1.00 33.30           N  
ANISOU  603  NH1 ARG A  79     4818   3825   4006    280   -329    799       N  
ATOM    604  NH2 ARG A  79      20.030  72.675  24.881  1.00 34.52           N  
ANISOU  604  NH2 ARG A  79     5076   3893   4145    201    -35    865       N  
ATOM    605  N   LEU A  80      24.509  69.798  24.045  1.00 14.00           N  
ANISOU  605  N   LEU A  80     2311   1624   1384    186    140    124       N  
ATOM    606  CA  LEU A  80      24.623  69.468  25.478  1.00 13.75           C  
ANISOU  606  CA  LEU A  80     2241   1611   1371    123    243     77       C  
ATOM    607  C   LEU A  80      26.001  68.910  25.835  1.00 12.92           C  
ANISOU  607  C   LEU A  80     2195   1444   1267     79    219    146       C  
ATOM    608  O   LEU A  80      26.565  69.261  26.858  1.00 12.86           O  
ANISOU  608  O   LEU A  80     2223   1405   1257    -25    249     63       O  
ATOM    609  CB  LEU A  80      23.526  68.482  25.916  1.00 13.98           C  
ANISOU  609  CB  LEU A  80     2192   1736   1381    191    284     28       C  
ATOM    610  CG  LEU A  80      22.141  69.080  26.171  1.00 15.69           C  
ANISOU  610  CG  LEU A  80     2131   2116   1714     40    399   -147       C  
ATOM    611  CD1 LEU A  80      21.145  67.954  26.434  1.00 18.13           C  
ANISOU  611  CD1 LEU A  80     2205   2620   2061     21    420     11       C  
ATOM    612  CD2 LEU A  80      22.197  70.028  27.365  1.00 17.11           C  
ANISOU  612  CD2 LEU A  80     2367   2429   1704     58    544   -251       C  
ATOM    613  N   LEU A  81      26.540  68.054  24.974  1.00 12.17           N  
ANISOU  613  N   LEU A  81     2193   1262   1167     82    156    138       N  
ATOM    614  CA  LEU A  81      27.828  67.392  25.228  1.00 12.16           C  
ANISOU  614  CA  LEU A  81     2268   1209   1141     62    164    120       C  
ATOM    615  C   LEU A  81      29.075  68.216  24.897  1.00 12.85           C  
ANISOU  615  C   LEU A  81     2315   1317   1248    107    147     51       C  
ATOM    616  O   LEU A  81      30.177  67.892  25.363  1.00 12.27           O  
ANISOU  616  O   LEU A  81     2259   1330   1071    -32    129    -40       O  
ATOM    617  CB  LEU A  81      27.871  66.054  24.485  1.00 11.58           C  
ANISOU  617  CB  LEU A  81     2206   1105   1086     41    107    180       C  
ATOM    618  CG  LEU A  81      26.871  64.985  24.946  1.00 10.98           C  
ANISOU  618  CG  LEU A  81     2366    953    851     -3    139    299       C  
ATOM    619  CD1 LEU A  81      27.100  63.762  24.079  1.00 12.47           C  
ANISOU  619  CD1 LEU A  81     2672   1204    860    -31    333     74       C  
ATOM    620  CD2 LEU A  81      26.987  64.632  26.451  1.00 12.01           C  
ANISOU  620  CD2 LEU A  81     2427   1142    993     60   -118    201       C  
ATOM    621  N   GLU A  82      28.910  69.281  24.106  1.00 13.29           N  
ANISOU  621  N   GLU A  82     2342   1350   1356     78    173     62       N  
ATOM    622  CA  GLU A  82      30.069  70.011  23.603  1.00 14.71           C  
ANISOU  622  CA  GLU A  82     2437   1549   1603    128    140     58       C  
ATOM    623  C   GLU A  82      30.990  70.579  24.713  1.00 13.95           C  
ANISOU  623  C   GLU A  82     2326   1482   1491     79    115     11       C  
ATOM    624  O   GLU A  82      32.211  70.387  24.637  1.00 13.83           O  
ANISOU  624  O   GLU A  82     2349   1525   1381     29     -4     24       O  
ATOM    625  CB  GLU A  82      29.658  71.066  22.559  1.00 15.45           C  
ANISOU  625  CB  GLU A  82     2481   1630   1756    130    251    158       C  
ATOM    626  CG  GLU A  82      30.748  71.425  21.559  1.00 19.78           C  
ANISOU  626  CG  GLU A  82     2953   2118   2444    234    374     63       C  
ATOM    627  CD  GLU A  82      31.373  70.229  20.841  1.00 23.35           C  
ANISOU  627  CD  GLU A  82     3233   2563   3074    140    422     12       C  
ATOM    628  OE1 GLU A  82      30.640  69.410  20.268  1.00 24.91           O  
ANISOU  628  OE1 GLU A  82     3463   2784   3216    -94    683     59       O  
ATOM    629  OE2 GLU A  82      32.620  70.138  20.820  1.00 27.44           O  
ANISOU  629  OE2 GLU A  82     3586   2982   3855    383    502    -39       O  
ATOM    630  N   PRO A  83      30.419  71.257  25.739  1.00 13.91           N  
ANISOU  630  N   PRO A  83     2283   1479   1523     84     81    -33       N  
ATOM    631  CA  PRO A  83      31.284  71.725  26.848  1.00 13.45           C  
ANISOU  631  CA  PRO A  83     2224   1418   1466     65    118    -29       C  
ATOM    632  C   PRO A  83      32.073  70.595  27.531  1.00 13.70           C  
ANISOU  632  C   PRO A  83     2283   1385   1537     45    183      0       C  
ATOM    633  O   PRO A  83      33.279  70.751  27.776  1.00 12.38           O  
ANISOU  633  O   PRO A  83     2044   1171   1486     10    306     18       O  
ATOM    634  CB  PRO A  83      30.287  72.378  27.820  1.00 13.45           C  
ANISOU  634  CB  PRO A  83     2182   1423   1503    173     26    -54       C  
ATOM    635  CG  PRO A  83      29.172  72.873  26.893  1.00 14.03           C  
ANISOU  635  CG  PRO A  83     2264   1480   1586     65     16    -67       C  
ATOM    636  CD  PRO A  83      29.022  71.703  25.931  1.00 13.44           C  
ANISOU  636  CD  PRO A  83     2170   1480   1454     69    136   -138       C  
ATOM    637  N   LEU A  84      31.405  69.473  27.823  1.00 13.45           N  
ANISOU  637  N   LEU A  84     2309   1299   1502     -7    278     68       N  
ATOM    638  CA  LEU A  84      32.092  68.305  28.396  1.00 14.49           C  
ANISOU  638  CA  LEU A  84     2396   1492   1617    -45    283    120       C  
ATOM    639  C   LEU A  84      33.170  67.744  27.487  1.00 13.99           C  
ANISOU  639  C   LEU A  84     2333   1443   1538     -3    265    140       C  
ATOM    640  O   LEU A  84      34.283  67.479  27.940  1.00 14.32           O  
ANISOU  640  O   LEU A  84     2319   1580   1540    -46    190     90       O  
ATOM    641  CB  LEU A  84      31.109  67.185  28.757  1.00 14.82           C  
ANISOU  641  CB  LEU A  84     2474   1467   1690   -138    302    121       C  
ATOM    642  CG  LEU A  84      30.903  66.898  30.244  1.00 18.59           C  
ANISOU  642  CG  LEU A  84     2904   1999   2158   -253    303    114       C  
ATOM    643  CD1 LEU A  84      30.244  65.518  30.461  1.00 19.54           C  
ANISOU  643  CD1 LEU A  84     3184   2042   2195   -460    526    195       C  
ATOM    644  CD2 LEU A  84      32.221  67.003  31.051  1.00 18.85           C  
ANISOU  644  CD2 LEU A  84     2855   2175   2130    -24    264    355       C  
ATOM    645  N   LYS A  85      32.837  67.564  26.205  1.00 13.96           N  
ANISOU  645  N   LYS A  85     2287   1502   1515     44    254    131       N  
ATOM    646  CA  LYS A  85      33.790  67.047  25.227  1.00 13.54           C  
ANISOU  646  CA  LYS A  85     2233   1529   1379    189    273    161       C  
ATOM    647  C   LYS A  85      35.070  67.909  25.190  1.00 13.78           C  
ANISOU  647  C   LYS A  85     2259   1514   1459    211    310    126       C  
ATOM    648  O   LYS A  85      36.192  67.393  25.081  1.00 12.83           O  
ANISOU  648  O   LYS A  85     2207   1475   1191    248    341    194       O  
ATOM    649  CB  LYS A  85      33.136  66.952  23.830  1.00 13.59           C  
ANISOU  649  CB  LYS A  85     2165   1600   1397    216    230    146       C  
ATOM    650  CG  LYS A  85      34.095  66.565  22.698  1.00 12.83           C  
ANISOU  650  CG  LYS A  85     2040   1545   1287    259    169    213       C  
ATOM    651  CD  LYS A  85      34.720  65.179  22.883  1.00 13.40           C  
ANISOU  651  CD  LYS A  85     2208   1478   1403    240    389    268       C  
ATOM    652  CE  LYS A  85      35.811  64.934  21.835  1.00 13.12           C  
ANISOU  652  CE  LYS A  85     1760   1657   1568    365    221    335       C  
ATOM    653  NZ  LYS A  85      37.041  65.739  22.143  1.00 15.04           N  
ANISOU  653  NZ  LYS A  85     2324   1930   1460    272    229    151       N  
ATOM    654  N   ALA A  86      34.882  69.220  25.309  1.00 14.26           N  
ANISOU  654  N   ALA A  86     2290   1467   1661    202    387     74       N  
ATOM    655  CA  ALA A  86      35.986  70.190  25.286  1.00 15.01           C  
ANISOU  655  CA  ALA A  86     2287   1489   1926    237    515     -2       C  
ATOM    656  C   ALA A  86      36.971  69.988  26.426  1.00 14.97           C  
ANISOU  656  C   ALA A  86     2259   1519   1910    217    577    -79       C  
ATOM    657  O   ALA A  86      38.139  70.355  26.298  1.00 15.30           O  
ANISOU  657  O   ALA A  86     2279   1575   1959    155    677   -125       O  
ATOM    658  CB  ALA A  86      35.450  71.619  25.291  1.00 15.21           C  
ANISOU  658  CB  ALA A  86     2338   1466   1973    326    521     46       C  
ATOM    659  N   GLU A  87      36.507  69.389  27.525  1.00 15.31           N  
ANISOU  659  N   GLU A  87     2216   1615   1984    214    642   -115       N  
ATOM    660  CA  GLU A  87      37.383  69.022  28.640  1.00 15.69           C  
ANISOU  660  CA  GLU A  87     2188   1807   1965    196    722    -83       C  
ATOM    661  C   GLU A  87      38.240  67.795  28.316  1.00 14.90           C  
ANISOU  661  C   GLU A  87     1975   1754   1930    108    765     17       C  
ATOM    662  O   GLU A  87      39.176  67.476  29.050  1.00 15.12           O  
ANISOU  662  O   GLU A  87     1936   1907   1901    119    729    -36       O  
ATOM    663  CB  GLU A  87      36.577  68.775  29.918  1.00 16.08           C  
ANISOU  663  CB  GLU A  87     2221   1867   2019    198    670    -94       C  
ATOM    664  CG  GLU A  87      35.731  69.983  30.357  1.00 17.15           C  
ANISOU  664  CG  GLU A  87     2449   2201   1865    355    868   -186       C  
ATOM    665  CD  GLU A  87      35.026  69.772  31.694  1.00 19.88           C  
ANISOU  665  CD  GLU A  87     2807   2393   2351    403    806   -107       C  
ATOM    666  OE1 GLU A  87      35.346  68.797  32.401  1.00 23.81           O  
ANISOU  666  OE1 GLU A  87     3552   2947   2547    374    885    -87       O  
ATOM    667  OE2 GLU A  87      34.161  70.601  32.042  1.00 22.49           O  
ANISOU  667  OE2 GLU A  87     2734   3253   2558    506    896   -211       O  
ATOM    668  N   PHE A  88      37.900  67.093  27.241  1.00 13.45           N  
ANISOU  668  N   PHE A  88     1785   1637   1687     64    823     47       N  
ATOM    669  CA  PHE A  88      38.620  65.870  26.860  1.00 13.80           C  
ANISOU  669  CA  PHE A  88     1757   1713   1773    -82    784    111       C  
ATOM    670  C   PHE A  88      39.046  65.933  25.398  1.00 13.90           C  
ANISOU  670  C   PHE A  88     1693   1777   1808   -104    758     57       C  
ATOM    671  O   PHE A  88      38.591  65.139  24.571  1.00 13.23           O  
ANISOU  671  O   PHE A  88     1501   1746   1780   -264    697     84       O  
ATOM    672  CB  PHE A  88      37.769  64.630  27.161  1.00 13.68           C  
ANISOU  672  CB  PHE A  88     1786   1675   1736    -15    821    136       C  
ATOM    673  CG  PHE A  88      37.367  64.537  28.593  1.00 14.01           C  
ANISOU  673  CG  PHE A  88     1946   1734   1643    -81    823    274       C  
ATOM    674  CD1 PHE A  88      38.279  64.104  29.550  1.00 14.95           C  
ANISOU  674  CD1 PHE A  88     2177   1824   1679   -168    879    347       C  
ATOM    675  CD2 PHE A  88      36.099  64.951  29.000  1.00 13.07           C  
ANISOU  675  CD2 PHE A  88     1798   1580   1585   -141    893    403       C  
ATOM    676  CE1 PHE A  88      37.914  64.029  30.899  1.00 14.72           C  
ANISOU  676  CE1 PHE A  88     2241   2114   1235     -8   1256    165       C  
ATOM    677  CE2 PHE A  88      35.719  64.887  30.343  1.00 15.07           C  
ANISOU  677  CE2 PHE A  88     2128   1933   1664     46    743    171       C  
ATOM    678  CZ  PHE A  88      36.631  64.423  31.297  1.00 16.31           C  
ANISOU  678  CZ  PHE A  88     2248   2035   1912     -7    740    206       C  
ATOM    679  N   PRO A  89      39.933  66.893  25.077  1.00 14.59           N  
ANISOU  679  N   PRO A  89     1799   1899   1844   -155    679     42       N  
ATOM    680  CA  PRO A  89      40.374  67.064  23.696  1.00 14.56           C  
ANISOU  680  CA  PRO A  89     1837   1963   1730   -173    636     12       C  
ATOM    681  C   PRO A  89      41.036  65.811  23.110  1.00 14.05           C  
ANISOU  681  C   PRO A  89     1763   1956   1617   -119    548    -18       C  
ATOM    682  O   PRO A  89      40.953  65.593  21.899  1.00 14.81           O  
ANISOU  682  O   PRO A  89     2061   1995   1571    -93    458    -10       O  
ATOM    683  CB  PRO A  89      41.367  68.230  23.777  1.00 15.49           C  
ANISOU  683  CB  PRO A  89     1961   2072   1850   -214    590    -14       C  
ATOM    684  CG  PRO A  89      41.787  68.296  25.224  1.00 15.68           C  
ANISOU  684  CG  PRO A  89     1973   2171   1813   -194    756     78       C  
ATOM    685  CD  PRO A  89      40.563  67.874  25.983  1.00 14.79           C  
ANISOU  685  CD  PRO A  89     1804   1952   1863   -272    680     22       C  
ATOM    686  N   ILE A  90      41.663  64.987  23.951  1.00 12.48           N  
ANISOU  686  N   ILE A  90     1550   1834   1358   -115    487    -17       N  
ATOM    687  CA  ILE A  90      42.340  63.768  23.466  1.00 11.77           C  
ANISOU  687  CA  ILE A  90     1431   1897   1142    -14    361    -93       C  
ATOM    688  C   ILE A  90      41.364  62.711  22.909  1.00 11.26           C  
ANISOU  688  C   ILE A  90     1408   1865   1003    -29    247    -52       C  
ATOM    689  O   ILE A  90      41.746  61.931  22.058  1.00 10.97           O  
ANISOU  689  O   ILE A  90     1328   2006    833    -22    268    -44       O  
ATOM    690  CB  ILE A  90      43.228  63.123  24.564  1.00 11.61           C  
ANISOU  690  CB  ILE A  90     1353   1822   1235     17    324   -148       C  
ATOM    691  CG1 ILE A  90      44.394  62.305  23.966  1.00 11.49           C  
ANISOU  691  CG1 ILE A  90     1321   1976   1066    121    175   -272       C  
ATOM    692  CG2 ILE A  90      42.379  62.312  25.546  1.00 10.71           C  
ANISOU  692  CG2 ILE A  90     1070   1960   1039    149    599   -190       C  
ATOM    693  CD1 ILE A  90      45.491  61.918  25.009  1.00 12.06           C  
ANISOU  693  CD1 ILE A  90     1394   2114   1071    200    175    -76       C  
ATOM    694  N   LEU A  91      40.128  62.667  23.417  1.00 10.48           N  
ANISOU  694  N   LEU A  91     1373   1776    832    -61    176    -34       N  
ATOM    695  CA  LEU A  91      39.148  61.661  22.975  1.00 11.24           C  
ANISOU  695  CA  LEU A  91     1538   1759    970    -14    173     61       C  
ATOM    696  C   LEU A  91      38.562  61.991  21.599  1.00 11.18           C  
ANISOU  696  C   LEU A  91     1578   1689    978    -41    116     27       C  
ATOM    697  O   LEU A  91      38.288  63.146  21.309  1.00 11.07           O  
ANISOU  697  O   LEU A  91     1574   1567   1065     46    137    -18       O  
ATOM    698  CB  LEU A  91      38.011  61.541  23.979  1.00 10.33           C  
ANISOU  698  CB  LEU A  91     1382   1713    830    -40    187    125       C  
ATOM    699  CG  LEU A  91      38.416  61.083  25.379  1.00 10.75           C  
ANISOU  699  CG  LEU A  91     1471   1800    812     27    334    272       C  
ATOM    700  CD1 LEU A  91      37.191  60.989  26.311  1.00 12.23           C  
ANISOU  700  CD1 LEU A  91     1063   2237   1344   -209    335    229       C  
ATOM    701  CD2 LEU A  91      39.131  59.769  25.281  1.00  9.53           C  
ANISOU  701  CD2 LEU A  91     1329   1789    499    299    377    408       C  
ATOM    702  N   SER A  92      38.375  60.970  20.759  1.00 11.26           N  
ANISOU  702  N   SER A  92     1693   1619    965    -47     73     -7       N  
ATOM    703  CA  SER A  92      37.596  61.139  19.532  1.00 10.62           C  
ANISOU  703  CA  SER A  92     1666   1484    883    -53     98     47       C  
ATOM    704  C   SER A  92      36.141  61.453  19.899  1.00 10.71           C  
ANISOU  704  C   SER A  92     1679   1475    914    -43      8    106       C  
ATOM    705  O   SER A  92      35.638  61.020  20.963  1.00 10.68           O  
ANISOU  705  O   SER A  92     1745   1427    884    -52     67    122       O  
ATOM    706  CB  SER A  92      37.679  59.898  18.642  1.00 10.05           C  
ANISOU  706  CB  SER A  92     1608   1398    811   -123    106     30       C  
ATOM    707  OG  SER A  92      37.120  58.744  19.271  1.00 10.47           O  
ANISOU  707  OG  SER A  92     1746   1550    682   -151    240    -41       O  
ATOM    708  N   TYR A  93      35.477  62.240  19.056  1.00 11.33           N  
ANISOU  708  N   TYR A  93     1851   1467    985    -26     19    124       N  
ATOM    709  CA  TYR A  93      34.029  62.390  19.178  1.00 11.55           C  
ANISOU  709  CA  TYR A  93     1866   1510   1010     23   -104    241       C  
ATOM    710  C   TYR A  93      33.352  61.027  19.102  1.00 10.93           C  
ANISOU  710  C   TYR A  93     1843   1430    877     31    -71    211       C  
ATOM    711  O   TYR A  93      32.385  60.770  19.825  1.00 10.58           O  
ANISOU  711  O   TYR A  93     1903   1378    736    -74   -114    159       O  
ATOM    712  CB  TYR A  93      33.481  63.330  18.099  1.00 12.45           C  
ANISOU  712  CB  TYR A  93     1995   1561   1173     37   -135    303       C  
ATOM    713  CG  TYR A  93      33.683  64.784  18.427  1.00 14.08           C  
ANISOU  713  CG  TYR A  93     2132   1691   1524     27   -303    480       C  
ATOM    714  CD1 TYR A  93      34.892  65.428  18.138  1.00 14.29           C  
ANISOU  714  CD1 TYR A  93     2110   1656   1661    -52   -174    582       C  
ATOM    715  CD2 TYR A  93      32.679  65.517  19.064  1.00 14.69           C  
ANISOU  715  CD2 TYR A  93     2114   1670   1798    139   -324    488       C  
ATOM    716  CE1 TYR A  93      35.078  66.787  18.447  1.00 15.87           C  
ANISOU  716  CE1 TYR A  93     2353   1721   1952    -46   -267    530       C  
ATOM    717  CE2 TYR A  93      32.851  66.877  19.366  1.00 15.95           C  
ANISOU  717  CE2 TYR A  93     2249   1865   1946   -109   -386    490       C  
ATOM    718  CZ  TYR A  93      34.056  67.493  19.073  1.00 15.32           C  
ANISOU  718  CZ  TYR A  93     2381   1551   1888    -55   -257    534       C  
ATOM    719  OH  TYR A  93      34.220  68.826  19.380  1.00 18.41           O  
ANISOU  719  OH  TYR A  93     2661   2042   2291   -180   -183    445       O  
ATOM    720  N   ALA A  94      33.868  60.167  18.218  1.00 10.65           N  
ANISOU  720  N   ALA A  94     1873   1434    739     -9    -45    203       N  
ATOM    721  CA  ALA A  94      33.360  58.814  18.014  1.00 10.54           C  
ANISOU  721  CA  ALA A  94     1857   1423    723     52    -29    158       C  
ATOM    722  C   ALA A  94      33.277  58.066  19.337  1.00 10.25           C  
ANISOU  722  C   ALA A  94     1763   1381    750     52    -16    154       C  
ATOM    723  O   ALA A  94      32.207  57.582  19.724  1.00 10.58           O  
ANISOU  723  O   ALA A  94     1682   1522    815     72   -109     43       O  
ATOM    724  CB  ALA A  94      34.245  58.059  17.027  1.00 10.91           C  
ANISOU  724  CB  ALA A  94     1887   1495    762      7     46    192       C  
ATOM    725  N   ASP A  95      34.411  57.985  20.029  1.00  9.73           N  
ANISOU  725  N   ASP A  95     1678   1376    643     65   -104    132       N  
ATOM    726  CA  ASP A  95      34.461  57.353  21.359  1.00  9.63           C  
ANISOU  726  CA  ASP A  95     1570   1405    684     39     -7    171       C  
ATOM    727  C   ASP A  95      33.558  58.065  22.355  1.00  9.72           C  
ANISOU  727  C   ASP A  95     1591   1383    717     29    -42    134       C  
ATOM    728  O   ASP A  95      32.846  57.415  23.133  1.00  9.88           O  
ANISOU  728  O   ASP A  95     1435   1550    767     57    132    160       O  
ATOM    729  CB  ASP A  95      35.895  57.355  21.903  1.00  9.55           C  
ANISOU  729  CB  ASP A  95     1521   1430    674     34    -48    151       C  
ATOM    730  CG  ASP A  95      36.730  56.208  21.370  1.00 10.32           C  
ANISOU  730  CG  ASP A  95     1507   1608    807   -102      4    136       C  
ATOM    731  OD1 ASP A  95      36.192  55.348  20.636  1.00 10.99           O  
ANISOU  731  OD1 ASP A  95     1488   1873    814   -154     89    247       O  
ATOM    732  OD2 ASP A  95      37.938  56.172  21.699  1.00 11.15           O  
ANISOU  732  OD2 ASP A  95     1465   1865    905     41    -73    142       O  
ATOM    733  N   PHE A  96      33.595  59.397  22.338  1.00  9.36           N  
ANISOU  733  N   PHE A  96     1566   1341    648    136    -82     93       N  
ATOM    734  CA  PHE A  96      32.881  60.172  23.348  1.00  9.42           C  
ANISOU  734  CA  PHE A  96     1567   1288    722    105    -93      9       C  
ATOM    735  C   PHE A  96      31.379  59.909  23.304  1.00  8.78           C  
ANISOU  735  C   PHE A  96     1546   1160    627    131   -102     50       C  
ATOM    736  O   PHE A  96      30.750  59.681  24.328  1.00  8.90           O  
ANISOU  736  O   PHE A  96     1593   1167    619    110   -168    122       O  
ATOM    737  CB  PHE A  96      33.186  61.662  23.203  1.00  9.75           C  
ANISOU  737  CB  PHE A  96     1649   1318    738    101    -20     31       C  
ATOM    738  CG  PHE A  96      32.785  62.479  24.403  1.00 11.09           C  
ANISOU  738  CG  PHE A  96     1795   1542    874     76    134    -29       C  
ATOM    739  CD1 PHE A  96      33.571  62.482  25.557  1.00 11.68           C  
ANISOU  739  CD1 PHE A  96     1921   1623    894    199    237    -74       C  
ATOM    740  CD2 PHE A  96      31.624  63.257  24.373  1.00 12.71           C  
ANISOU  740  CD2 PHE A  96     2063   1789    976    106    319    -93       C  
ATOM    741  CE1 PHE A  96      33.200  63.257  26.678  1.00 12.98           C  
ANISOU  741  CE1 PHE A  96     2152   1852    927    113    211     -8       C  
ATOM    742  CE2 PHE A  96      31.246  64.026  25.487  1.00 14.92           C  
ANISOU  742  CE2 PHE A  96     2435   2085   1146     90    150    -68       C  
ATOM    743  CZ  PHE A  96      32.035  64.017  26.636  1.00 13.31           C  
ANISOU  743  CZ  PHE A  96     2301   1844    908     61    186     31       C  
ATOM    744  N   TYR A  97      30.820  59.915  22.099  1.00  8.38           N  
ANISOU  744  N   TYR A  97     1445   1193    544     97   -210    126       N  
ATOM    745  CA  TYR A  97      29.396  59.699  21.920  1.00  9.18           C  
ANISOU  745  CA  TYR A  97     1611   1266    612     46   -193    152       C  
ATOM    746  C   TYR A  97      28.995  58.280  22.291  1.00  9.16           C  
ANISOU  746  C   TYR A  97     1587   1305    586     81   -201    101       C  
ATOM    747  O   TYR A  97      27.950  58.077  22.899  1.00  8.84           O  
ANISOU  747  O   TYR A  97     1448   1272    637    203    -41    146       O  
ATOM    748  CB  TYR A  97      28.983  60.041  20.477  1.00  8.95           C  
ANISOU  748  CB  TYR A  97     1626   1209    566     14   -225    268       C  
ATOM    749  CG  TYR A  97      29.074  61.532  20.156  1.00  9.75           C  
ANISOU  749  CG  TYR A  97     1633   1186    883    -18   -137    272       C  
ATOM    750  CD1 TYR A  97      28.984  62.503  21.160  1.00  8.28           C  
ANISOU  750  CD1 TYR A  97     1491    814    839   -253    -34    302       C  
ATOM    751  CD2 TYR A  97      29.201  61.969  18.839  1.00  9.45           C  
ANISOU  751  CD2 TYR A  97     1776   1070    742    -26   -178    231       C  
ATOM    752  CE1 TYR A  97      29.052  63.873  20.856  1.00 10.07           C  
ANISOU  752  CE1 TYR A  97     1450   1206   1167   -111   -178    478       C  
ATOM    753  CE2 TYR A  97      29.261  63.328  18.528  1.00 10.84           C  
ANISOU  753  CE2 TYR A  97     2049   1278    790   -148   -156    342       C  
ATOM    754  CZ  TYR A  97      29.185  64.273  19.536  1.00  9.59           C  
ANISOU  754  CZ  TYR A  97     1608   1076    959   -176   -165    331       C  
ATOM    755  OH  TYR A  97      29.248  65.611  19.200  1.00 11.57           O  
ANISOU  755  OH  TYR A  97     1774   1378   1242   -305    -79    325       O  
ATOM    756  N   GLN A  98      29.817  57.298  21.929  1.00  9.44           N  
ANISOU  756  N   GLN A  98     1552   1420    613     82   -174     29       N  
ATOM    757  CA  GLN A  98      29.531  55.919  22.336  1.00  9.26           C  
ANISOU  757  CA  GLN A  98     1563   1419    533     17   -173    -59       C  
ATOM    758  C   GLN A  98      29.638  55.738  23.850  1.00  8.97           C  
ANISOU  758  C   GLN A  98     1466   1428    513     -8   -241     23       C  
ATOM    759  O   GLN A  98      28.828  55.016  24.457  1.00  9.09           O  
ANISOU  759  O   GLN A  98     1401   1673    381    -20   -267    -31       O  
ATOM    760  CB  GLN A  98      30.412  54.910  21.594  1.00  9.11           C  
ANISOU  760  CB  GLN A  98     1575   1390    495     38   -124    -96       C  
ATOM    761  CG  GLN A  98      30.064  54.817  20.094  1.00  9.31           C  
ANISOU  761  CG  GLN A  98     1514   1504    519   -123   -225   -350       C  
ATOM    762  CD  GLN A  98      28.573  54.635  19.850  1.00 10.35           C  
ANISOU  762  CD  GLN A  98     1704   1529    699   -231   -183   -335       C  
ATOM    763  OE1 GLN A  98      27.925  53.763  20.450  1.00 10.19           O  
ANISOU  763  OE1 GLN A  98     1615   1604    652   -487   -270   -216       O  
ATOM    764  NE2 GLN A  98      28.012  55.482  18.980  1.00  9.48           N  
ANISOU  764  NE2 GLN A  98     1381   1602    617   -180    -14     83       N  
ATOM    765  N   LEU A  99      30.634  56.394  24.448  1.00  8.98           N  
ANISOU  765  N   LEU A  99     1456   1465    489    -73   -269     53       N  
ATOM    766  CA  LEU A  99      30.777  56.405  25.898  1.00  8.93           C  
ANISOU  766  CA  LEU A  99     1404   1420    566   -112   -258    -24       C  
ATOM    767  C   LEU A  99      29.534  57.009  26.555  1.00  9.39           C  
ANISOU  767  C   LEU A  99     1446   1461    659    -86   -233     -7       C  
ATOM    768  O   LEU A  99      29.017  56.436  27.508  1.00  9.47           O  
ANISOU  768  O   LEU A  99     1412   1377    807   -150    -94     18       O  
ATOM    769  CB  LEU A  99      32.041  57.140  26.323  1.00  9.86           C  
ANISOU  769  CB  LEU A  99     1451   1711    583    -52   -344     27       C  
ATOM    770  CG  LEU A  99      32.399  57.023  27.811  1.00  9.03           C  
ANISOU  770  CG  LEU A  99     1552   1439    438   -144   -486    110       C  
ATOM    771  CD1 LEU A  99      32.463  55.564  28.280  1.00 10.74           C  
ANISOU  771  CD1 LEU A  99     1889   1589    601    -55   -695    289       C  
ATOM    772  CD2 LEU A  99      33.702  57.756  28.060  1.00 11.68           C  
ANISOU  772  CD2 LEU A  99     1836   1885    717   -310   -427    241       C  
ATOM    773  N   ALA A 100      29.037  58.127  26.016  1.00  9.16           N  
ANISOU  773  N   ALA A 100     1431   1302    745    -17   -153    -44       N  
ATOM    774  CA  ALA A 100      27.800  58.742  26.506  1.00  9.69           C  
ANISOU  774  CA  ALA A 100     1507   1394    778     15   -183     32       C  
ATOM    775  C   ALA A 100      26.630  57.747  26.478  1.00  9.69           C  
ANISOU  775  C   ALA A 100     1496   1398    787     69   -168     26       C  
ATOM    776  O   ALA A 100      25.831  57.691  27.426  1.00  9.20           O  
ANISOU  776  O   ALA A 100     1495   1338    662     37   -113    -31       O  
ATOM    777  CB  ALA A 100      27.464  59.996  25.717  1.00  9.79           C  
ANISOU  777  CB  ALA A 100     1518   1339    861     32   -129    -21       C  
ATOM    778  N   GLY A 101      26.549  56.950  25.407  1.00  9.09           N  
ANISOU  778  N   GLY A 101     1423   1354    677    101   -136      7       N  
ATOM    779  CA  GLY A 101      25.475  55.959  25.267  1.00  9.59           C  
ANISOU  779  CA  GLY A 101     1434   1559    650    153     -5     45       C  
ATOM    780  C   GLY A 101      25.580  54.888  26.344  1.00  9.09           C  
ANISOU  780  C   GLY A 101     1352   1473    625    212     36     -2       C  
ATOM    781  O   GLY A 101      24.582  54.508  26.954  1.00  9.49           O  
ANISOU  781  O   GLY A 101     1385   1705    515    241     56     13       O  
ATOM    782  N   VAL A 102      26.796  54.386  26.554  1.00  8.89           N  
ANISOU  782  N   VAL A 102     1256   1540    582    242     52    -13       N  
ATOM    783  CA  VAL A 102      27.073  53.363  27.569  1.00  9.40           C  
ANISOU  783  CA  VAL A 102     1272   1529    769    244    113    -64       C  
ATOM    784  C   VAL A 102      26.712  53.925  28.951  1.00  8.40           C  
ANISOU  784  C   VAL A 102     1113   1456    620    199     19    -73       C  
ATOM    785  O   VAL A 102      25.988  53.279  29.729  1.00  8.84           O  
ANISOU  785  O   VAL A 102     1097   1452    809    189    122    -39       O  
ATOM    786  CB  VAL A 102      28.554  52.887  27.493  1.00  9.13           C  
ANISOU  786  CB  VAL A 102     1258   1533    679    281    141    -47       C  
ATOM    787  CG1 VAL A 102      29.013  52.189  28.790  1.00 10.72           C  
ANISOU  787  CG1 VAL A 102     1402   1730    941    271     80    -39       C  
ATOM    788  CG2 VAL A 102      28.740  51.954  26.266  1.00  9.37           C  
ANISOU  788  CG2 VAL A 102     1484   1330    745    291    152   -313       C  
ATOM    789  N   VAL A 103      27.157  55.152  29.229  1.00  8.51           N  
ANISOU  789  N   VAL A 103     1122   1414    695    180     44    -88       N  
ATOM    790  CA  VAL A 103      26.852  55.800  30.519  1.00  8.70           C  
ANISOU  790  CA  VAL A 103     1236   1424    644     67    -94   -151       C  
ATOM    791  C   VAL A 103      25.333  56.002  30.706  1.00  8.39           C  
ANISOU  791  C   VAL A 103     1225   1368    594    -90    -44    -89       C  
ATOM    792  O   VAL A 103      24.799  55.790  31.798  1.00  7.79           O  
ANISOU  792  O   VAL A 103     1143   1452    363   -103   -243    -22       O  
ATOM    793  CB  VAL A 103      27.641  57.128  30.674  1.00  9.17           C  
ANISOU  793  CB  VAL A 103     1340   1449    693     61     11   -198       C  
ATOM    794  CG1 VAL A 103      27.126  57.975  31.878  1.00  9.63           C  
ANISOU  794  CG1 VAL A 103     1423   1413    821    256     -2   -309       C  
ATOM    795  CG2 VAL A 103      29.125  56.828  30.852  1.00  9.39           C  
ANISOU  795  CG2 VAL A 103     1407   1536    624    101   -123   -258       C  
ATOM    796  N   ALA A 104      24.655  56.427  29.640  1.00  7.73           N  
ANISOU  796  N   ALA A 104     1188   1364    386   -198   -131    -64       N  
ATOM    797  CA  ALA A 104      23.202  56.599  29.650  1.00  8.32           C  
ANISOU  797  CA  ALA A 104     1350   1387    424   -185    -61    -46       C  
ATOM    798  C   ALA A 104      22.471  55.361  30.151  1.00  8.63           C  
ANISOU  798  C   ALA A 104     1415   1404    457   -168    -90    -30       C  
ATOM    799  O   ALA A 104      21.561  55.466  30.967  1.00  8.76           O  
ANISOU  799  O   ALA A 104     1522   1405    402   -242     21    -10       O  
ATOM    800  CB  ALA A 104      22.670  57.005  28.276  1.00  8.70           C  
ANISOU  800  CB  ALA A 104     1376   1471    458   -193     -5     19       C  
ATOM    801  N   VAL A 105      22.860  54.199  29.639  1.00  8.67           N  
ANISOU  801  N   VAL A 105     1466   1447    381   -143   -100    -46       N  
ATOM    802  CA  VAL A 105      22.281  52.939  30.070  1.00  9.29           C  
ANISOU  802  CA  VAL A 105     1527   1544    459   -117   -112     11       C  
ATOM    803  C   VAL A 105      22.634  52.683  31.546  1.00  9.39           C  
ANISOU  803  C   VAL A 105     1459   1631    475   -151   -185     19       C  
ATOM    804  O   VAL A 105      21.770  52.270  32.336  1.00 10.19           O  
ANISOU  804  O   VAL A 105     1474   1767    628   -176   -248     52       O  
ATOM    805  CB  VAL A 105      22.746  51.779  29.150  1.00  9.40           C  
ANISOU  805  CB  VAL A 105     1631   1464    473   -116    -22    -10       C  
ATOM    806  CG1 VAL A 105      22.303  50.406  29.674  1.00 10.04           C  
ANISOU  806  CG1 VAL A 105     1718   1480    615   -166    107     27       C  
ATOM    807  CG2 VAL A 105      22.241  51.998  27.715  1.00  8.86           C  
ANISOU  807  CG2 VAL A 105     1609   1440    317   -136     82    -95       C  
ATOM    808  N   GLU A 106      23.895  52.909  31.910  1.00  9.78           N  
ANISOU  808  N   GLU A 106     1447   1716    550   -212   -315     68       N  
ATOM    809  CA  GLU A 106      24.330  52.665  33.293  1.00 10.39           C  
ANISOU  809  CA  GLU A 106     1392   1893    661   -262   -319     28       C  
ATOM    810  C   GLU A 106      23.586  53.513  34.323  1.00 11.04           C  
ANISOU  810  C   GLU A 106     1407   1992    794   -284   -310     22       C  
ATOM    811  O   GLU A 106      23.074  52.985  35.323  1.00 10.70           O  
ANISOU  811  O   GLU A 106     1426   2012    625   -298   -261    109       O  
ATOM    812  CB  GLU A 106      25.838  52.878  33.435  1.00 11.20           C  
ANISOU  812  CB  GLU A 106     1435   2040    778   -198   -479     67       C  
ATOM    813  CG  GLU A 106      26.410  52.324  34.765  1.00 12.93           C  
ANISOU  813  CG  GLU A 106     1693   2187   1030   -341   -547      7       C  
ATOM    814  CD  GLU A 106      27.787  52.890  35.066  1.00 18.20           C  
ANISOU  814  CD  GLU A 106     2093   2741   2078   -122   -330     -9       C  
ATOM    815  OE1 GLU A 106      27.876  54.041  35.531  1.00 21.74           O  
ANISOU  815  OE1 GLU A 106     2282   3338   2639   -418   -455   -385       O  
ATOM    816  OE2 GLU A 106      28.781  52.196  34.826  1.00 21.66           O  
ANISOU  816  OE2 GLU A 106     2409   3175   2643    -98   -258    183       O  
ATOM    817  N   VAL A 107      23.521  54.820  34.091  1.00 11.17           N  
ANISOU  817  N   VAL A 107     1421   1980    843   -283   -175      9       N  
ATOM    818  CA  VAL A 107      22.996  55.730  35.116  1.00 12.04           C  
ANISOU  818  CA  VAL A 107     1577   2032    965   -229   -141   -133       C  
ATOM    819  C   VAL A 107      21.500  55.579  35.327  1.00 12.41           C  
ANISOU  819  C   VAL A 107     1600   2139    974   -273    -55   -165       C  
ATOM    820  O   VAL A 107      20.983  55.968  36.378  1.00 13.20           O  
ANISOU  820  O   VAL A 107     1659   2341   1014   -371    -21   -381       O  
ATOM    821  CB  VAL A 107      23.315  57.211  34.852  1.00 12.28           C  
ANISOU  821  CB  VAL A 107     1530   2073   1060   -254    -72    -43       C  
ATOM    822  CG1 VAL A 107      24.830  57.448  34.807  1.00 14.89           C  
ANISOU  822  CG1 VAL A 107     1894   2188   1572   -194   -110    -88       C  
ATOM    823  CG2 VAL A 107      22.595  57.718  33.604  1.00 11.94           C  
ANISOU  823  CG2 VAL A 107     1952   1730    854   -188   -165   -152       C  
ATOM    824  N   THR A 108      20.819  55.007  34.333  1.00 12.08           N  
ANISOU  824  N   THR A 108     1597   2118    873   -224    -81   -126       N  
ATOM    825  CA  THR A 108      19.382  54.749  34.422  1.00 11.92           C  
ANISOU  825  CA  THR A 108     1607   2085    834   -137    -72    -76       C  
ATOM    826  C   THR A 108      19.076  53.358  35.035  1.00 11.67           C  
ANISOU  826  C   THR A 108     1660   2021    752   -218     -4    -42       C  
ATOM    827  O   THR A 108      17.914  52.955  35.123  1.00 11.48           O  
ANISOU  827  O   THR A 108     1541   2098    722   -179     43     -3       O  
ATOM    828  CB  THR A 108      18.663  54.926  33.039  1.00 12.08           C  
ANISOU  828  CB  THR A 108     1618   2076    895    -67    -62    -11       C  
ATOM    829  OG1 THR A 108      19.252  54.076  32.053  1.00 10.83           O  
ANISOU  829  OG1 THR A 108     1322   1981    809    232    -91     32       O  
ATOM    830  CG2 THR A 108      18.728  56.355  32.569  1.00 12.95           C  
ANISOU  830  CG2 THR A 108     1671   2190   1059     -5   -103    -18       C  
ATOM    831  N   GLY A 109      20.124  52.639  35.441  1.00 11.43           N  
ANISOU  831  N   GLY A 109     1732   1931    676   -281     -4     10       N  
ATOM    832  CA  GLY A 109      19.997  51.339  36.128  1.00 11.48           C  
ANISOU  832  CA  GLY A 109     1867   1879    613   -267     -7    -33       C  
ATOM    833  C   GLY A 109      20.177  50.111  35.250  1.00 11.90           C  
ANISOU  833  C   GLY A 109     1904   1885    731   -307      1     40       C  
ATOM    834  O   GLY A 109      19.818  48.994  35.646  1.00 11.37           O  
ANISOU  834  O   GLY A 109     1982   1774    562   -369     61      9       O  
ATOM    835  N   GLY A 110      20.719  50.326  34.050  1.00 11.45           N  
ANISOU  835  N   GLY A 110     1864   1834    651   -299     49     70       N  
ATOM    836  CA  GLY A 110      20.869  49.264  33.065  1.00 12.20           C  
ANISOU  836  CA  GLY A 110     1857   1924    853   -390     16     58       C  
ATOM    837  C   GLY A 110      22.168  48.491  33.239  1.00 12.29           C  
ANISOU  837  C   GLY A 110     1842   1919    908   -394     86     53       C  
ATOM    838  O   GLY A 110      22.967  48.790  34.147  1.00 11.39           O  
ANISOU  838  O   GLY A 110     1685   1837    805   -404     99     67       O  
ATOM    839  N   PRO A 111      22.400  47.490  32.367  1.00 12.85           N  
ANISOU  839  N   PRO A 111     1874   1968   1039   -436     49     88       N  
ATOM    840  CA  PRO A 111      23.619  46.704  32.456  1.00 13.22           C  
ANISOU  840  CA  PRO A 111     1824   2059   1138   -417     15     55       C  
ATOM    841  C   PRO A 111      24.829  47.581  32.150  1.00 13.59           C  
ANISOU  841  C   PRO A 111     1807   2127   1229   -369     37     91       C  
ATOM    842  O   PRO A 111      24.689  48.655  31.532  1.00 13.88           O  
ANISOU  842  O   PRO A 111     1732   2076   1465   -389     -6     91       O  
ATOM    843  CB  PRO A 111      23.440  45.638  31.364  1.00 13.62           C  
ANISOU  843  CB  PRO A 111     1853   2073   1248   -438    -17     52       C  
ATOM    844  CG  PRO A 111      22.519  46.275  30.381  1.00 13.65           C  
ANISOU  844  CG  PRO A 111     1967   2110   1109   -306    -79     85       C  
ATOM    845  CD  PRO A 111      21.559  47.075  31.231  1.00 12.49           C  
ANISOU  845  CD  PRO A 111     1871   1987    887   -445     27     20       C  
ATOM    846  N   GLU A 112      25.993  47.123  32.586  1.00 13.54           N  
ANISOU  846  N   GLU A 112     1775   2181   1188   -235    -24     99       N  
ATOM    847  CA  GLU A 112      27.254  47.790  32.282  1.00 14.54           C  
ANISOU  847  CA  GLU A 112     1844   2366   1312    -76     -4    100       C  
ATOM    848  C   GLU A 112      27.765  47.226  30.957  1.00 13.98           C  
ANISOU  848  C   GLU A 112     1758   2196   1357    -68     61    163       C  
ATOM    849  O   GLU A 112      28.192  46.075  30.872  1.00 15.19           O  
ANISOU  849  O   GLU A 112     2010   2300   1458    -45    157    174       O  
ATOM    850  CB  GLU A 112      28.258  47.579  33.432  1.00 15.09           C  
ANISOU  850  CB  GLU A 112     1950   2393   1388    -57    -26     68       C  
ATOM    851  CG  GLU A 112      27.851  48.323  34.708  1.00 17.74           C  
ANISOU  851  CG  GLU A 112     2261   2938   1540    145   -185     33       C  
ATOM    852  CD  GLU A 112      28.591  47.862  35.949  1.00 20.54           C  
ANISOU  852  CD  GLU A 112     2570   3225   2008    184    -45   -104       C  
ATOM    853  OE1 GLU A 112      29.676  47.253  35.819  1.00 24.06           O  
ANISOU  853  OE1 GLU A 112     2846   3871   2425    611    -39   -375       O  
ATOM    854  OE2 GLU A 112      28.075  48.110  37.062  1.00 22.69           O  
ANISOU  854  OE2 GLU A 112     3109   3432   2080    359   -178   -656       O  
ATOM    855  N   VAL A 113      27.680  48.035  29.911  1.00 12.75           N  
ANISOU  855  N   VAL A 113     1553   2036   1256    -80     91    201       N  
ATOM    856  CA  VAL A 113      28.051  47.601  28.576  1.00 11.96           C  
ANISOU  856  CA  VAL A 113     1428   1852   1262    -97    157    220       C  
ATOM    857  C   VAL A 113      29.561  47.790  28.438  1.00 12.59           C  
ANISOU  857  C   VAL A 113     1505   1878   1399   -104    175    195       C  
ATOM    858  O   VAL A 113      30.048  48.913  28.620  1.00 13.04           O  
ANISOU  858  O   VAL A 113     1577   1930   1445   -204    169    129       O  
ATOM    859  CB  VAL A 113      27.335  48.465  27.507  1.00 11.57           C  
ANISOU  859  CB  VAL A 113     1373   1855   1167    -71    121    236       C  
ATOM    860  CG1 VAL A 113      27.793  48.064  26.090  1.00 10.26           C  
ANISOU  860  CG1 VAL A 113     1328   1648    922    -68    394    286       C  
ATOM    861  CG2 VAL A 113      25.787  48.382  27.661  1.00 11.68           C  
ANISOU  861  CG2 VAL A 113     1495   1642   1299    -75    139    318       C  
ATOM    862  N   PRO A 114      30.305  46.707  28.115  1.00 13.03           N  
ANISOU  862  N   PRO A 114     1551   1839   1560   -116    133    226       N  
ATOM    863  CA  PRO A 114      31.754  46.870  27.965  1.00 12.61           C  
ANISOU  863  CA  PRO A 114     1495   1758   1535    -52    196    238       C  
ATOM    864  C   PRO A 114      32.089  47.965  26.954  1.00 12.69           C  
ANISOU  864  C   PRO A 114     1555   1686   1580    -15    169    274       C  
ATOM    865  O   PRO A 114      31.372  48.152  25.963  1.00 12.08           O  
ANISOU  865  O   PRO A 114     1468   1654   1466    -77    243    304       O  
ATOM    866  CB  PRO A 114      32.216  45.507  27.449  1.00 13.48           C  
ANISOU  866  CB  PRO A 114     1683   1844   1595    -48     87    273       C  
ATOM    867  CG  PRO A 114      31.185  44.547  27.950  1.00 13.51           C  
ANISOU  867  CG  PRO A 114     1521   1901   1709    -92    135    204       C  
ATOM    868  CD  PRO A 114      29.884  45.313  27.868  1.00 13.60           C  
ANISOU  868  CD  PRO A 114     1631   1874   1662    -28    193    155       C  
ATOM    869  N   PHE A 115      33.163  48.695  27.220  1.00 12.29           N  
ANISOU  869  N   PHE A 115     1501   1589   1578     10    154    289       N  
ATOM    870  CA  PHE A 115      33.560  49.788  26.343  1.00 12.49           C  
ANISOU  870  CA  PHE A 115     1612   1566   1567     38    181    265       C  
ATOM    871  C   PHE A 115      35.035  49.670  26.015  1.00 12.79           C  
ANISOU  871  C   PHE A 115     1627   1616   1615     57    129    284       C  
ATOM    872  O   PHE A 115      35.865  49.527  26.920  1.00 13.87           O  
ANISOU  872  O   PHE A 115     1761   1891   1616     67     89    307       O  
ATOM    873  CB  PHE A 115      33.289  51.163  26.978  1.00 12.68           C  
ANISOU  873  CB  PHE A 115     1630   1622   1567    120    108    269       C  
ATOM    874  CG  PHE A 115      33.705  52.319  26.095  1.00 11.02           C  
ANISOU  874  CG  PHE A 115     1552   1326   1309     98    272    332       C  
ATOM    875  CD1 PHE A 115      32.872  52.742  25.049  1.00 10.62           C  
ANISOU  875  CD1 PHE A 115     1626   1236   1172    249    265    557       C  
ATOM    876  CD2 PHE A 115      34.939  52.964  26.272  1.00 10.50           C  
ANISOU  876  CD2 PHE A 115     1771   1068   1151     20    414    318       C  
ATOM    877  CE1 PHE A 115      33.254  53.818  24.203  1.00 11.70           C  
ANISOU  877  CE1 PHE A 115     1688   1519   1237     11    652    510       C  
ATOM    878  CE2 PHE A 115      35.327  54.043  25.430  1.00 11.62           C  
ANISOU  878  CE2 PHE A 115     1981   1339   1094    457    228    508       C  
ATOM    879  CZ  PHE A 115      34.484  54.461  24.400  1.00 12.15           C  
ANISOU  879  CZ  PHE A 115     1842   1506   1267    285    296    247       C  
ATOM    880  N   HIS A 116      35.347  49.766  24.726  1.00 12.42           N  
ANISOU  880  N   HIS A 116     1656   1541   1522     51    157    280       N  
ATOM    881  CA  HIS A 116      36.723  49.753  24.239  1.00 12.53           C  
ANISOU  881  CA  HIS A 116     1745   1523   1490    -81    184    251       C  
ATOM    882  C   HIS A 116      36.992  51.019  23.429  1.00 12.69           C  
ANISOU  882  C   HIS A 116     1784   1578   1457    -72    217    188       C  
ATOM    883  O   HIS A 116      36.246  51.313  22.476  1.00 12.12           O  
ANISOU  883  O   HIS A 116     1776   1598   1229   -110    166    144       O  
ATOM    884  CB  HIS A 116      36.964  48.520  23.364  1.00 13.39           C  
ANISOU  884  CB  HIS A 116     1824   1557   1706    -96    191    299       C  
ATOM    885  CG  HIS A 116      36.848  47.230  24.103  1.00 14.50           C  
ANISOU  885  CG  HIS A 116     1944   1572   1991   -104     58    359       C  
ATOM    886  ND1 HIS A 116      35.660  46.535  24.188  1.00 17.29           N  
ANISOU  886  ND1 HIS A 116     2356   1784   2428   -160    242    448       N  
ATOM    887  CD2 HIS A 116      37.756  46.519  24.812  1.00 15.84           C  
ANISOU  887  CD2 HIS A 116     2290   1591   2136   -224    -14    487       C  
ATOM    888  CE1 HIS A 116      35.842  45.450  24.919  1.00 12.88           C  
ANISOU  888  CE1 HIS A 116     1668   1158   2066    212    -13    581       C  
ATOM    889  NE2 HIS A 116      37.108  45.408  25.294  1.00 17.85           N  
ANISOU  889  NE2 HIS A 116     2636   1978   2167   -199   -146    537       N  
ATOM    890  N   PRO A 117      38.043  51.776  23.800  1.00 12.42           N  
ANISOU  890  N   PRO A 117     1795   1598   1325    -96    207    167       N  
ATOM    891  CA  PRO A 117      38.342  53.029  23.086  1.00 12.38           C  
ANISOU  891  CA  PRO A 117     1795   1654   1253   -141    258    148       C  
ATOM    892  C   PRO A 117      39.062  52.797  21.761  1.00 12.31           C  
ANISOU  892  C   PRO A 117     1787   1732   1158   -168    200    114       C  
ATOM    893  O   PRO A 117      39.543  51.688  21.502  1.00 11.84           O  
ANISOU  893  O   PRO A 117     1810   1692    994   -130    341      2       O  
ATOM    894  CB  PRO A 117      39.281  53.759  24.052  1.00 11.96           C  
ANISOU  894  CB  PRO A 117     1738   1564   1240    -97    184    149       C  
ATOM    895  CG  PRO A 117      40.030  52.628  24.737  1.00 13.12           C  
ANISOU  895  CG  PRO A 117     1930   1704   1350   -214    216    253       C  
ATOM    896  CD  PRO A 117      38.997  51.520  24.898  1.00 13.23           C  
ANISOU  896  CD  PRO A 117     1821   1707   1496   -144    215     52       C  
ATOM    897  N   GLY A 118      39.164  53.856  20.959  1.00 12.05           N  
ANISOU  897  N   GLY A 118     1736   1878    961   -161    197    151       N  
ATOM    898  CA  GLY A 118      39.989  53.820  19.755  1.00 12.79           C  
ANISOU  898  CA  GLY A 118     1790   1991   1079   -182    229    230       C  
ATOM    899  C   GLY A 118      39.301  54.121  18.437  1.00 12.63           C  
ANISOU  899  C   GLY A 118     1667   2060   1069   -205    179    159       C  
ATOM    900  O   GLY A 118      39.954  54.120  17.390  1.00 12.32           O  
ANISOU  900  O   GLY A 118     1612   2161    906   -149    268    204       O  
ATOM    901  N   ARG A 119      38.003  54.412  18.467  1.00 12.53           N  
ANISOU  901  N   ARG A 119     1618   2080   1060   -192    186    168       N  
ATOM    902  CA  ARG A 119      37.303  54.788  17.229  1.00 13.03           C  
ANISOU  902  CA  ARG A 119     1689   2145   1116   -231    153    160       C  
ATOM    903  C   ARG A 119      37.889  56.092  16.726  1.00 14.07           C  
ANISOU  903  C   ARG A 119     1800   2297   1247   -198    204    192       C  
ATOM    904  O   ARG A 119      38.110  56.998  17.513  1.00 14.10           O  
ANISOU  904  O   ARG A 119     1854   2159   1342   -233    239    133       O  
ATOM    905  CB  ARG A 119      35.811  55.001  17.467  1.00 11.93           C  
ANISOU  905  CB  ARG A 119     1466   2077    987   -172    159     94       C  
ATOM    906  CG  ARG A 119      35.053  53.796  17.957  1.00 10.25           C  
ANISOU  906  CG  ARG A 119     1260   1876    758   -324    -26     14       C  
ATOM    907  CD  ARG A 119      33.712  54.202  18.620  1.00 11.15           C  
ANISOU  907  CD  ARG A 119     1183   1931   1121   -296     58    119       C  
ATOM    908  NE  ARG A 119      33.068  53.020  19.202  1.00 10.93           N  
ANISOU  908  NE  ARG A 119     1106   1773   1274   -352     69    200       N  
ATOM    909  CZ  ARG A 119      33.484  52.423  20.320  1.00 10.74           C  
ANISOU  909  CZ  ARG A 119     1076   1772   1229   -328     37    226       C  
ATOM    910  NH1 ARG A 119      34.525  52.924  20.999  1.00  9.83           N  
ANISOU  910  NH1 ARG A 119      795   1908   1030    -18   -184    106       N  
ATOM    911  NH2 ARG A 119      32.868  51.330  20.765  1.00 11.61           N  
ANISOU  911  NH2 ARG A 119     1452   1644   1315   -132     63    212       N  
ATOM    912  N   GLU A 120      38.154  56.176  15.426  1.00 15.57           N  
ANISOU  912  N   GLU A 120     2089   2536   1287   -204    257    230       N  
ATOM    913  CA  GLU A 120      38.637  57.428  14.844  1.00 17.87           C  
ANISOU  913  CA  GLU A 120     2426   2966   1395   -121    345    283       C  
ATOM    914  C   GLU A 120      37.486  58.246  14.273  1.00 18.31           C  
ANISOU  914  C   GLU A 120     2535   3034   1386   -155    371    321       C  
ATOM    915  O   GLU A 120      36.467  57.695  13.824  1.00 19.92           O  
ANISOU  915  O   GLU A 120     2810   3167   1588   -112    235    392       O  
ATOM    916  CB  GLU A 120      39.734  57.163  13.797  1.00 18.76           C  
ANISOU  916  CB  GLU A 120     2470   3033   1623   -110    358    287       C  
ATOM    917  CG  GLU A 120      41.031  56.632  14.433  1.00 19.35           C  
ANISOU  917  CG  GLU A 120     2615   3323   1412     -3    354    291       C  
ATOM    918  CD  GLU A 120      42.041  56.126  13.438  1.00 22.60           C  
ANISOU  918  CD  GLU A 120     2949   3649   1986     95    350    404       C  
ATOM    919  OE1 GLU A 120      41.890  56.400  12.231  1.00 24.38           O  
ANISOU  919  OE1 GLU A 120     3208   4204   1850    125    670    454       O  
ATOM    920  OE2 GLU A 120      42.993  55.440  13.870  1.00 26.36           O  
ANISOU  920  OE2 GLU A 120     3144   4321   2548    272    415    301       O  
ATOM    921  N   ASP A 121      37.627  59.563  14.309  1.00 18.68           N  
ANISOU  921  N   ASP A 121     2654   3138   1304   -127    427    296       N  
ATOM    922  CA  ASP A 121      36.616  60.430  13.721  1.00 19.25           C  
ANISOU  922  CA  ASP A 121     2782   3241   1291   -141    496    321       C  
ATOM    923  C   ASP A 121      36.787  60.441  12.215  1.00 20.59           C  
ANISOU  923  C   ASP A 121     2966   3392   1463    -95    482    271       C  
ATOM    924  O   ASP A 121      37.856  60.788  11.710  1.00 21.42           O  
ANISOU  924  O   ASP A 121     3078   3561   1499   -164    539    265       O  
ATOM    925  CB  ASP A 121      36.692  61.838  14.303  1.00 18.78           C  
ANISOU  925  CB  ASP A 121     2750   3167   1215   -129    538    344       C  
ATOM    926  CG  ASP A 121      36.177  61.900  15.732  1.00 18.38           C  
ANISOU  926  CG  ASP A 121     2712   3082   1188   -147    536    362       C  
ATOM    927  OD1 ASP A 121      35.285  61.078  16.083  1.00 15.99           O  
ANISOU  927  OD1 ASP A 121     2615   2718    741   -564    547    320       O  
ATOM    928  OD2 ASP A 121      36.665  62.766  16.503  1.00 16.62           O  
ANISOU  928  OD2 ASP A 121     2509   2672   1133   -169    659    514       O  
ATOM    929  N   LYS A 122      35.744  60.029  11.505  1.00 21.55           N  
ANISOU  929  N   LYS A 122     3153   3499   1533    -56    431    236       N  
ATOM    930  CA  LYS A 122      35.796  60.015  10.032  1.00 22.91           C  
ANISOU  930  CA  LYS A 122     3311   3610   1783    -23    396    246       C  
ATOM    931  C   LYS A 122      35.246  61.310   9.433  1.00 23.75           C  
ANISOU  931  C   LYS A 122     3379   3685   1957      0    319    251       C  
ATOM    932  O   LYS A 122      34.355  61.937  10.016  1.00 23.36           O  
ANISOU  932  O   LYS A 122     3352   3631   1892      0    293    268       O  
ATOM    933  CB  LYS A 122      35.091  58.778   9.477  1.00 22.94           C  
ANISOU  933  CB  LYS A 122     3394   3591   1728     -7    421    207       C  
ATOM    934  CG  LYS A 122      35.859  57.499   9.804  1.00 24.36           C  
ANISOU  934  CG  LYS A 122     3440   3693   2120     14    483    118       C  
ATOM    935  CD  LYS A 122      35.164  56.247   9.316  1.00 26.62           C  
ANISOU  935  CD  LYS A 122     3599   3647   2867    -54    425    -75       C  
ATOM    936  CE  LYS A 122      35.848  55.012   9.908  1.00 28.63           C  
ANISOU  936  CE  LYS A 122     3655   3871   3352    -34    401   -218       C  
ATOM    937  NZ  LYS A 122      35.421  53.735   9.260  1.00 28.45           N  
ANISOU  937  NZ  LYS A 122     3567   3663   3578    -83    514   -385       N  
ATOM    938  N   PRO A 123      35.796  61.725   8.275  1.00 24.97           N  
ANISOU  938  N   PRO A 123     3503   3794   2191     24    242    274       N  
ATOM    939  CA  PRO A 123      35.416  62.994   7.647  1.00 25.92           C  
ANISOU  939  CA  PRO A 123     3572   3878   2397     18    175    248       C  
ATOM    940  C   PRO A 123      34.003  63.060   7.059  1.00 26.70           C  
ANISOU  940  C   PRO A 123     3671   3946   2526     10     91    206       C  
ATOM    941  O   PRO A 123      33.391  64.131   7.096  1.00 27.31           O  
ANISOU  941  O   PRO A 123     3709   4029   2639     33     62    226       O  
ATOM    942  CB  PRO A 123      36.454  63.157   6.525  1.00 26.00           C  
ANISOU  942  CB  PRO A 123     3618   3891   2366     30    206    270       C  
ATOM    943  CG  PRO A 123      36.879  61.759   6.191  1.00 25.70           C  
ANISOU  943  CG  PRO A 123     3625   3853   2287     34    267    290       C  
ATOM    944  CD  PRO A 123      36.847  61.019   7.508  1.00 24.95           C  
ANISOU  944  CD  PRO A 123     3494   3813   2171     41    260    274       C  
ATOM    945  N   GLU A 124      33.479  61.938   6.560  1.00 26.87           N  
ANISOU  945  N   GLU A 124     3678   3978   2552    -28     20    153       N  
ATOM    946  C   GLU A 124      31.087  61.194   6.437  1.00 26.61           C  
ANISOU  946  C   GLU A 124     3684   3903   2521    -84    -49    109       C  
ATOM    947  O   GLU A 124      31.199  59.987   6.700  1.00 26.50           O  
ANISOU  947  O   GLU A 124     3683   3945   2438    -86      0    144       O  
ATOM    948  CA AGLU A 124      32.232  61.975   5.798  0.50 27.01           C  
ANISOU  948  CA AGLU A 124     3691   3975   2596    -60     -7    125       C  
ATOM    949  CB AGLU A 124      32.458  61.560   4.332  0.50 27.19           C  
ANISOU  949  CB AGLU A 124     3696   4016   2617    -41    -17    144       C  
ATOM    950  CG AGLU A 124      33.127  60.203   4.135  0.50 28.30           C  
ANISOU  950  CG AGLU A 124     3781   4193   2776    -59      6    109       C  
ATOM    951  CD AGLU A 124      34.146  60.207   3.008  0.50 29.14           C  
ANISOU  951  CD AGLU A 124     3804   4410   2855    -60     23    152       C  
ATOM    952  OE1AGLU A 124      33.764  60.465   1.848  0.50 29.48           O  
ANISOU  952  OE1AGLU A 124     3891   4459   2847    -47    106    261       O  
ATOM    953  OE2AGLU A 124      35.334  59.939   3.286  0.50 29.55           O  
ANISOU  953  OE2AGLU A 124     3810   4506   2911    -58     23    103       O  
ATOM    954  CA BGLU A 124      32.241  61.952   5.780  0.50 27.05           C  
ANISOU  954  CA BGLU A 124     3707   3961   2609    -62     -6    126       C  
ATOM    955  CB BGLU A 124      32.499  61.386   4.376  0.50 27.26           C  
ANISOU  955  CB BGLU A 124     3724   3989   2645    -42    -12    137       C  
ATOM    956  CG BGLU A 124      31.579  61.933   3.296  0.50 28.56           C  
ANISOU  956  CG BGLU A 124     3878   4115   2856    -70     -1    124       C  
ATOM    957  CD BGLU A 124      31.851  63.391   2.978  0.50 29.83           C  
ANISOU  957  CD BGLU A 124     4010   4182   3141    -89      9    105       C  
ATOM    958  OE1BGLU A 124      33.035  63.795   2.992  0.50 31.24           O  
ANISOU  958  OE1BGLU A 124     4144   4367   3357   -115     76     83       O  
ATOM    959  OE2BGLU A 124      30.881  64.131   2.715  0.50 30.69           O  
ANISOU  959  OE2BGLU A 124     4151   4258   3251    -59    -18     96       O  
ATOM    960  N   PRO A 125      29.976  61.897   6.695  1.00 26.11           N  
ANISOU  960  N   PRO A 125     3657   3816   2448   -117   -123     97       N  
ATOM    961  C   PRO A 125      28.219  60.309   6.101  1.00 25.28           C  
ANISOU  961  C   PRO A 125     3630   3670   2306   -151   -195     90       C  
ATOM    962  O   PRO A 125      28.424  60.545   4.892  1.00 25.13           O  
ANISOU  962  O   PRO A 125     3646   3713   2190   -177   -227     88       O  
ATOM    963  CA APRO A 125      28.744  61.276   7.159  0.50 25.74           C  
ANISOU  963  CA APRO A 125     3652   3757   2371   -138   -163     98       C  
ATOM    964  CB APRO A 125      27.780  62.458   7.311  0.50 25.47           C  
ANISOU  964  CB APRO A 125     3638   3718   2320   -148   -162     86       C  
ATOM    965  CG APRO A 125      28.637  63.665   7.365  0.50 26.24           C  
ANISOU  965  CG APRO A 125     3669   3828   2470   -125   -151     91       C  
ATOM    966  CD APRO A 125      29.841  63.355   6.546  0.50 26.23           C  
ANISOU  966  CD APRO A 125     3680   3821   2463   -121   -107     76       C  
ATOM    967  CA BPRO A 125      28.744  61.276   7.160  0.50 25.74           C  
ANISOU  967  CA BPRO A 125     3652   3757   2371   -138   -164     98       C  
ATOM    968  CB BPRO A 125      27.780  62.458   7.312  0.50 25.47           C  
ANISOU  968  CB BPRO A 125     3638   3718   2320   -148   -162     86       C  
ATOM    969  CG BPRO A 125      28.637  63.664   7.366  0.50 26.24           C  
ANISOU  969  CG BPRO A 125     3669   3828   2470   -125   -151     91       C  
ATOM    970  CD BPRO A 125      29.840  63.355   6.545  0.50 26.23           C  
ANISOU  970  CD BPRO A 125     3680   3821   2463   -121   -107     76       C  
ATOM    971  N   PRO A 126      27.541  59.231   6.534  1.00 24.91           N  
ANISOU  971  N   PRO A 126     3620   3587   2256   -122   -265    107       N  
ATOM    972  CA  PRO A 126      26.975  58.318   5.548  1.00 24.31           C  
ANISOU  972  CA  PRO A 126     3583   3498   2154   -126   -322    129       C  
ATOM    973  C   PRO A 126      25.792  58.993   4.851  1.00 23.70           C  
ANISOU  973  C   PRO A 126     3522   3401   2080   -110   -366    150       C  
ATOM    974  O   PRO A 126      25.330  60.039   5.308  1.00 23.43           O  
ANISOU  974  O   PRO A 126     3502   3377   2021    -83   -413    243       O  
ATOM    975  CB  PRO A 126      26.474  57.147   6.405  1.00 24.43           C  
ANISOU  975  CB  PRO A 126     3598   3487   2196   -128   -304    117       C  
ATOM    976  CG  PRO A 126      26.162  57.770   7.718  1.00 25.04           C  
ANISOU  976  CG  PRO A 126     3691   3619   2201   -124   -288    142       C  
ATOM    977  CD  PRO A 126      27.227  58.805   7.913  1.00 24.60           C  
ANISOU  977  CD  PRO A 126     3630   3561   2154   -162   -250    116       C  
ATOM    978  N   PRO A 127      25.302  58.395   3.757  1.00 23.53           N  
ANISOU  978  N   PRO A 127     3515   3387   2039   -104   -412    136       N  
ATOM    979  CA  PRO A 127      24.094  58.902   3.095  1.00 23.39           C  
ANISOU  979  CA  PRO A 127     3524   3357   2004   -100   -433    100       C  
ATOM    980  C   PRO A 127      22.892  58.837   4.036  1.00 22.91           C  
ANISOU  980  C   PRO A 127     3494   3288   1923    -82   -428     52       C  
ATOM    981  O   PRO A 127      22.826  57.944   4.900  1.00 22.07           O  
ANISOU  981  O   PRO A 127     3427   3175   1780   -120   -431    139       O  
ATOM    982  CB  PRO A 127      23.879  57.929   1.933  1.00 23.55           C  
ANISOU  982  CB  PRO A 127     3535   3419   1993    -95   -406     31       C  
ATOM    983  CG  PRO A 127      25.171  57.167   1.787  1.00 23.89           C  
ANISOU  983  CG  PRO A 127     3573   3493   2012    -82   -547    104       C  
ATOM    984  CD  PRO A 127      25.857  57.198   3.109  1.00 23.76           C  
ANISOU  984  CD  PRO A 127     3572   3420   2036    -83   -400    121       C  
ATOM    985  N   GLU A 128      21.962  59.776   3.882  1.00 22.39           N  
ANISOU  985  N   GLU A 128     3514   3177   1813    -50   -451     64       N  
ATOM    986  CA  GLU A 128      20.712  59.733   4.639  1.00 22.71           C  
ANISOU  986  CA  GLU A 128     3565   3164   1897      6   -418     15       C  
ATOM    987  C   GLU A 128      19.877  58.501   4.266  1.00 22.40           C  
ANISOU  987  C   GLU A 128     3513   3105   1892     23   -411      7       C  
ATOM    988  O   GLU A 128      19.957  58.000   3.133  1.00 22.28           O  
ANISOU  988  O   GLU A 128     3651   3090   1724      2   -363    -64       O  
ATOM    989  CB  GLU A 128      19.899  61.016   4.427  1.00 22.78           C  
ANISOU  989  CB  GLU A 128     3619   3162   1873      2   -407     60       C  
ATOM    990  CG  GLU A 128      18.624  61.083   5.266  1.00 24.26           C  
ANISOU  990  CG  GLU A 128     3768   3273   2176     98   -380     94       C  
ATOM    991  CD  GLU A 128      17.903  62.424   5.188  1.00 25.45           C  
ANISOU  991  CD  GLU A 128     3886   3511   2270     41   -408    178       C  
ATOM    992  OE1 GLU A 128      18.417  63.359   4.522  1.00 26.12           O  
ANISOU  992  OE1 GLU A 128     4156   3469   2297     64   -388    438       O  
ATOM    993  OE2 GLU A 128      16.815  62.538   5.808  1.00 25.78           O  
ANISOU  993  OE2 GLU A 128     3857   3760   2178     57   -372    270       O  
ATOM    994  N   GLY A 129      19.095  58.007   5.222  1.00 21.45           N  
ANISOU  994  N   GLY A 129     3396   2976   1776     45   -430     10       N  
ATOM    995  CA  GLY A 129      18.080  56.993   4.942  1.00 20.98           C  
ANISOU  995  CA  GLY A 129     3277   2878   1813     81   -417    -11       C  
ATOM    996  C   GLY A 129      18.349  55.598   5.466  1.00 20.35           C  
ANISOU  996  C   GLY A 129     3159   2800   1773     67   -397    -43       C  
ATOM    997  O   GLY A 129      17.572  54.679   5.186  1.00 20.43           O  
ANISOU  997  O   GLY A 129     3116   2834   1811     68   -529    -45       O  
ATOM    998  N   ARG A 130      19.436  55.425   6.222  1.00 18.96           N  
ANISOU  998  N   ARG A 130     3004   2657   1543     86   -391    -67       N  
ATOM    999  CA  ARG A 130      19.804  54.086   6.705  1.00 18.17           C  
ANISOU  999  CA  ARG A 130     2871   2620   1410     61   -286    -79       C  
ATOM   1000  C   ARG A 130      19.141  53.741   8.030  1.00 17.98           C  
ANISOU 1000  C   ARG A 130     2780   2589   1462     66   -337   -143       C  
ATOM   1001  O   ARG A 130      18.926  52.562   8.340  1.00 17.34           O  
ANISOU 1001  O   ARG A 130     2763   2476   1346    129   -350   -162       O  
ATOM   1002  CB  ARG A 130      21.313  53.926   6.822  1.00 17.76           C  
ANISOU 1002  CB  ARG A 130     2854   2565   1327     64   -209    -49       C  
ATOM   1003  CG  ARG A 130      22.028  54.034   5.494  1.00 18.01           C  
ANISOU 1003  CG  ARG A 130     2816   2714   1310     74     66     42       C  
ATOM   1004  CD  ARG A 130      23.487  53.744   5.664  1.00 18.55           C  
ANISOU 1004  CD  ARG A 130     2975   2867   1206     66    134    158       C  
ATOM   1005  NE  ARG A 130      24.180  53.750   4.373  1.00 18.67           N  
ANISOU 1005  NE  ARG A 130     3025   2946   1122     57    250    174       N  
ATOM   1006  CZ  ARG A 130      25.492  53.585   4.234  1.00 18.20           C  
ANISOU 1006  CZ  ARG A 130     3073   2810   1030    -12    333    251       C  
ATOM   1007  NH1 ARG A 130      26.265  53.395   5.300  1.00 15.88           N  
ANISOU 1007  NH1 ARG A 130     2812   2630    590   -139     93    338       N  
ATOM   1008  NH2 ARG A 130      26.029  53.597   3.025  1.00 18.57           N  
ANISOU 1008  NH2 ARG A 130     3496   2929    627     23    180    524       N  
ATOM   1009  N   LEU A 131      18.806  54.765   8.808  1.00 17.78           N  
ANISOU 1009  N   LEU A 131     2728   2540   1487     41   -436   -222       N  
ATOM   1010  CA  LEU A 131      18.127  54.507  10.073  1.00 17.96           C  
ANISOU 1010  CA  LEU A 131     2608   2536   1678    -13   -461   -247       C  
ATOM   1011  C   LEU A 131      16.727  53.954   9.797  1.00 17.61           C  
ANISOU 1011  C   LEU A 131     2496   2535   1659     16   -530   -268       C  
ATOM   1012  O   LEU A 131      16.105  54.318   8.789  1.00 17.39           O  
ANISOU 1012  O   LEU A 131     2466   2568   1572    -69   -483   -162       O  
ATOM   1013  CB  LEU A 131      18.102  55.755  10.971  1.00 18.13           C  
ANISOU 1013  CB  LEU A 131     2627   2558   1704    -25   -515   -333       C  
ATOM   1014  CG  LEU A 131      19.481  56.239  11.465  1.00 18.43           C  
ANISOU 1014  CG  LEU A 131     2689   2411   1902    -20   -571   -328       C  
ATOM   1015  CD1 LEU A 131      19.332  57.544  12.256  1.00 17.14           C  
ANISOU 1015  CD1 LEU A 131     2517   2186   1809    -54   -306   -476       C  
ATOM   1016  CD2 LEU A 131      20.220  55.164  12.287  1.00 18.33           C  
ANISOU 1016  CD2 LEU A 131     2603   2313   2046   -106   -620   -402       C  
ATOM   1017  N   PRO A 132      16.253  53.029  10.657  1.00 17.41           N  
ANISOU 1017  N   PRO A 132     2426   2544   1644     37   -539   -277       N  
ATOM   1018  CA  PRO A 132      14.964  52.383  10.408  1.00 17.51           C  
ANISOU 1018  CA  PRO A 132     2412   2503   1738     90   -591   -310       C  
ATOM   1019  C   PRO A 132      13.775  53.341  10.516  1.00 17.67           C  
ANISOU 1019  C   PRO A 132     2404   2496   1814    145   -607   -347       C  
ATOM   1020  O   PRO A 132      13.839  54.361  11.224  1.00 17.51           O  
ANISOU 1020  O   PRO A 132     2347   2404   1899    123   -646   -416       O  
ATOM   1021  CB  PRO A 132      14.892  51.285  11.478  1.00 17.84           C  
ANISOU 1021  CB  PRO A 132     2415   2556   1806    114   -557   -280       C  
ATOM   1022  CG  PRO A 132      15.757  51.767  12.576  1.00 17.43           C  
ANISOU 1022  CG  PRO A 132     2479   2485   1658     24   -593   -322       C  
ATOM   1023  CD  PRO A 132      16.873  52.546  11.907  1.00 17.51           C  
ANISOU 1023  CD  PRO A 132     2403   2579   1670     71   -558   -225       C  
ATOM   1024  N   ASP A 133      12.733  52.997   9.763  1.00 17.08           N  
ANISOU 1024  N   ASP A 133     2312   2381   1796    158   -676   -377       N  
ATOM   1025  CA  ASP A 133      11.481  53.723   9.633  1.00 17.76           C  
ANISOU 1025  CA  ASP A 133     2386   2555   1807    206   -695   -374       C  
ATOM   1026  C   ASP A 133      10.502  53.123  10.646  1.00 17.45           C  
ANISOU 1026  C   ASP A 133     2333   2463   1834    236   -719   -401       C  
ATOM   1027  O   ASP A 133      10.201  51.931  10.599  1.00 17.35           O  
ANISOU 1027  O   ASP A 133     2308   2467   1815    221   -691   -455       O  
ATOM   1028  CB  ASP A 133      10.983  53.553   8.183  1.00 18.02           C  
ANISOU 1028  CB  ASP A 133     2372   2643   1829    224   -732   -345       C  
ATOM   1029  CG  ASP A 133       9.634  54.214   7.912  1.00 19.64           C  
ANISOU 1029  CG  ASP A 133     2647   2929   1886    311   -789   -298       C  
ATOM   1030  OD1 ASP A 133       8.846  54.452   8.850  1.00 19.07           O  
ANISOU 1030  OD1 ASP A 133     2793   2646   1805    534   -847   -534       O  
ATOM   1031  OD2 ASP A 133       9.344  54.461   6.714  1.00 23.11           O  
ANISOU 1031  OD2 ASP A 133     3067   3439   2275    362   -810   -144       O  
ATOM   1032  N   ALA A 134      10.044  53.952  11.580  1.00 17.22           N  
ANISOU 1032  N   ALA A 134     2410   2320   1813    237   -689   -463       N  
ATOM   1033  CA  ALA A 134       9.175  53.505  12.677  1.00 17.36           C  
ANISOU 1033  CA  ALA A 134     2478   2264   1852    277   -699   -464       C  
ATOM   1034  C   ALA A 134       7.805  52.969  12.246  1.00 17.52           C  
ANISOU 1034  C   ALA A 134     2541   2215   1897    287   -705   -432       C  
ATOM   1035  O   ALA A 134       7.099  52.332  13.048  1.00 17.12           O  
ANISOU 1035  O   ALA A 134     2509   2162   1833    264   -732   -433       O  
ATOM   1036  CB  ALA A 134       9.015  54.624  13.704  1.00 17.15           C  
ANISOU 1036  CB  ALA A 134     2499   2173   1845    210   -682   -550       C  
ATOM   1037  N   THR A 135       7.437  53.215  10.987  1.00 17.85           N  
ANISOU 1037  N   THR A 135     2664   2170   1947    340   -696   -370       N  
ATOM   1038  CA  THR A 135       6.132  52.799  10.467  1.00 17.97           C  
ANISOU 1038  CA  THR A 135     2722   2121   1985    347   -782   -315       C  
ATOM   1039  C   THR A 135       6.198  51.438   9.763  1.00 18.22           C  
ANISOU 1039  C   THR A 135     2782   2106   2035    350   -749   -286       C  
ATOM   1040  O   THR A 135       5.170  50.900   9.329  1.00 18.21           O  
ANISOU 1040  O   THR A 135     2753   2049   2117    362   -765   -327       O  
ATOM   1041  CB  THR A 135       5.532  53.849   9.480  1.00 18.47           C  
ANISOU 1041  CB  THR A 135     2810   2175   2031    342   -727   -293       C  
ATOM   1042  OG1 THR A 135       6.349  53.935   8.304  1.00 19.37           O  
ANISOU 1042  OG1 THR A 135     2878   2475   2005    332   -820   -259       O  
ATOM   1043  CG2 THR A 135       5.403  55.230  10.141  1.00 19.46           C  
ANISOU 1043  CG2 THR A 135     2955   2195   2243    414   -881   -288       C  
ATOM   1044  N   LYS A 136       7.404  50.896   9.625  1.00 18.23           N  
ANISOU 1044  N   LYS A 136     2818   2099   2007    312   -778   -287       N  
ATOM   1045  CA  LYS A 136       7.578  49.619   8.922  1.00 18.88           C  
ANISOU 1045  CA  LYS A 136     2888   2153   2132    287   -716   -253       C  
ATOM   1046  C   LYS A 136       7.664  48.432   9.883  1.00 18.91           C  
ANISOU 1046  C   LYS A 136     2923   2139   2122    223   -659   -296       C  
ATOM   1047  O   LYS A 136       7.532  48.596  11.107  1.00 19.60           O  
ANISOU 1047  O   LYS A 136     3084   2191   2171    206   -631   -309       O  
ATOM   1048  CB  LYS A 136       8.752  49.693   7.948  1.00 18.78           C  
ANISOU 1048  CB  LYS A 136     2926   2067   2140    276   -766   -252       C  
ATOM   1049  CG  LYS A 136       8.541  50.731   6.846  1.00 20.48           C  
ANISOU 1049  CG  LYS A 136     3124   2404   2254    294   -826   -168       C  
ATOM   1050  CD  LYS A 136       9.724  50.775   5.888  1.00 23.53           C  
ANISOU 1050  CD  LYS A 136     3553   2716   2669    262   -893     89       C  
ATOM   1051  CE  LYS A 136       9.501  51.798   4.786  1.00 25.71           C  
ANISOU 1051  CE  LYS A 136     3739   2976   3053    352  -1125     86       C  
ATOM   1052  NZ  LYS A 136       8.239  51.542   4.020  1.00 28.12           N  
ANISOU 1052  NZ  LYS A 136     4225   3260   3199    117  -1230     20       N  
ATOM   1053  N   GLY A 137       7.868  47.237   9.336  1.00 18.63           N  
ANISOU 1053  N   GLY A 137     2917   2105   2054    208   -591   -292       N  
ATOM   1054  CA  GLY A 137       7.786  46.027  10.146  1.00 18.58           C  
ANISOU 1054  CA  GLY A 137     2986   2065   2008    161   -524   -335       C  
ATOM   1055  C   GLY A 137       9.042  45.190  10.177  1.00 18.35           C  
ANISOU 1055  C   GLY A 137     3002   2088   1882    118   -463   -340       C  
ATOM   1056  O   GLY A 137      10.156  45.694   9.994  1.00 17.86           O  
ANISOU 1056  O   GLY A 137     2982   2016   1785    120   -467   -366       O  
ATOM   1057  N   SER A 138       8.835  43.894  10.385  1.00 18.00           N  
ANISOU 1057  N   SER A 138     3035   2037   1764     75   -393   -403       N  
ATOM   1058  CA  SER A 138       9.912  42.936  10.601  1.00 18.66           C  
ANISOU 1058  CA  SER A 138     3114   2171   1803     37   -387   -349       C  
ATOM   1059  C   SER A 138      10.895  42.807   9.440  1.00 18.23           C  
ANISOU 1059  C   SER A 138     3085   2153   1687     47   -384   -380       C  
ATOM   1060  O   SER A 138      12.103  42.743   9.669  1.00 18.50           O  
ANISOU 1060  O   SER A 138     3193   2197   1638     16   -402   -419       O  
ATOM   1061  CB  SER A 138       9.333  41.569  10.978  1.00 18.80           C  
ANISOU 1061  CB  SER A 138     3144   2159   1838     27   -286   -329       C  
ATOM   1062  OG  SER A 138       8.780  41.643  12.280  1.00 21.21           O  
ANISOU 1062  OG  SER A 138     3320   2553   2184     12   -314   -190       O  
ATOM   1063  N  AASP A 139      10.377  42.776   8.210  0.50 18.45           N  
ANISOU 1063  N  AASP A 139     3123   2195   1691     31   -404   -387       N  
ATOM   1064  CA AASP A 139      11.210  42.710   7.004  0.50 18.64           C  
ANISOU 1064  CA AASP A 139     3106   2262   1712     55   -399   -373       C  
ATOM   1065  C  AASP A 139      12.187  43.881   6.963  0.50 17.94           C  
ANISOU 1065  C  AASP A 139     3025   2233   1558     42   -422   -383       C  
ATOM   1066  O  AASP A 139      13.382  43.694   6.730  0.50 17.82           O  
ANISOU 1066  O  AASP A 139     2994   2255   1519     37   -421   -383       O  
ATOM   1067  CB AASP A 139      10.337  42.714   5.740  0.50 19.10           C  
ANISOU 1067  CB AASP A 139     3162   2338   1753     38   -403   -396       C  
ATOM   1068  CG AASP A 139      11.155  42.710   4.452  0.50 21.30           C  
ANISOU 1068  CG AASP A 139     3416   2495   2180    100   -387   -383       C  
ATOM   1069  OD1AASP A 139      11.628  41.625   4.055  0.50 23.85           O  
ANISOU 1069  OD1AASP A 139     3670   2727   2663    153   -364   -464       O  
ATOM   1070  OD2AASP A 139      11.313  43.788   3.826  0.50 23.60           O  
ANISOU 1070  OD2AASP A 139     3707   2920   2337    154   -437   -287       O  
ATOM   1071  N  BASP A 139      10.376  42.768   8.211  0.50 18.09           N  
ANISOU 1071  N  BASP A 139     3092   2161   1619      2   -420   -404       N  
ATOM   1072  CA BASP A 139      11.215  42.699   7.013  0.50 17.96           C  
ANISOU 1072  CA BASP A 139     3048   2201   1575      4   -428   -401       C  
ATOM   1073  C  BASP A 139      12.188  43.877   6.972  0.50 17.54           C  
ANISOU 1073  C  BASP A 139     2990   2197   1476     12   -440   -402       C  
ATOM   1074  O  BASP A 139      13.385  43.692   6.745  0.50 17.43           O  
ANISOU 1074  O  BASP A 139     2961   2224   1438      9   -438   -399       O  
ATOM   1075  CB BASP A 139      10.363  42.702   5.733  0.50 18.04           C  
ANISOU 1075  CB BASP A 139     3071   2237   1543    -48   -446   -451       C  
ATOM   1076  CG BASP A 139       9.662  41.371   5.466  0.50 18.67           C  
ANISOU 1076  CG BASP A 139     3185   2261   1645    -83   -504   -477       C  
ATOM   1077  OD1BASP A 139       9.731  40.442   6.299  0.50 19.50           O  
ANISOU 1077  OD1BASP A 139     3282   2358   1769   -324   -591   -683       O  
ATOM   1078  OD2BASP A 139       9.025  41.262   4.395  0.50 19.88           O  
ANISOU 1078  OD2BASP A 139     3426   2401   1725   -182   -493   -615       O  
ATOM   1079  N   HIS A 140      11.659  45.082   7.192  1.00 17.08           N  
ANISOU 1079  N   HIS A 140     2948   2134   1407     24   -445   -376       N  
ATOM   1080  CA  HIS A 140      12.461  46.298   7.235  1.00 16.87           C  
ANISOU 1080  CA  HIS A 140     2909   2106   1394     55   -405   -334       C  
ATOM   1081  C   HIS A 140      13.512  46.261   8.348  1.00 15.83           C  
ANISOU 1081  C   HIS A 140     2816   1988   1211     34   -365   -317       C  
ATOM   1082  O   HIS A 140      14.678  46.614   8.126  1.00 15.47           O  
ANISOU 1082  O   HIS A 140     2756   2100   1018     67   -387   -306       O  
ATOM   1083  CB  HIS A 140      11.569  47.516   7.433  1.00 16.84           C  
ANISOU 1083  CB  HIS A 140     2952   2076   1370     67   -448   -307       C  
ATOM   1084  CG  HIS A 140      12.325  48.805   7.464  1.00 17.16           C  
ANISOU 1084  CG  HIS A 140     2940   2041   1538     39   -570   -375       C  
ATOM   1085  ND1 HIS A 140      12.366  49.620   8.576  1.00 19.73           N  
ANISOU 1085  ND1 HIS A 140     3221   2424   1851    120   -513   -138       N  
ATOM   1086  CD2 HIS A 140      13.085  49.410   6.522  1.00 15.63           C  
ANISOU 1086  CD2 HIS A 140     2754   1897   1286     18   -637   -361       C  
ATOM   1087  CE1 HIS A 140      13.112  50.678   8.312  1.00 17.07           C  
ANISOU 1087  CE1 HIS A 140     2957   2035   1493    -16   -640   -318       C  
ATOM   1088  NE2 HIS A 140      13.555  50.577   7.071  1.00 19.79           N  
ANISOU 1088  NE2 HIS A 140     3212   2302   2003     70   -471   -260       N  
ATOM   1089  N   LEU A 141      13.102  45.854   9.546  1.00 15.35           N  
ANISOU 1089  N   LEU A 141     2728   1872   1229     10   -260   -290       N  
ATOM   1090  CA  LEU A 141      14.055  45.731  10.640  1.00 15.18           C  
ANISOU 1090  CA  LEU A 141     2643   1843   1282     -7   -204   -293       C  
ATOM   1091  C   LEU A 141      15.230  44.812  10.278  1.00 15.46           C  
ANISOU 1091  C   LEU A 141     2708   1886   1280    -30   -174   -259       C  
ATOM   1092  O   LEU A 141      16.389  45.145  10.564  1.00 15.17           O  
ANISOU 1092  O   LEU A 141     2549   1852   1362    -63    -96   -223       O  
ATOM   1093  CB  LEU A 141      13.375  45.281  11.935  1.00 14.68           C  
ANISOU 1093  CB  LEU A 141     2587   1824   1166     11   -190   -335       C  
ATOM   1094  CG  LEU A 141      12.351  46.261  12.523  1.00 14.44           C  
ANISOU 1094  CG  LEU A 141     2496   1745   1243    -49   -141   -468       C  
ATOM   1095  CD1 LEU A 141      11.588  45.575  13.656  1.00 15.86           C  
ANISOU 1095  CD1 LEU A 141     2522   2035   1468     53     45   -475       C  
ATOM   1096  CD2 LEU A 141      12.979  47.614  12.996  1.00 16.36           C  
ANISOU 1096  CD2 LEU A 141     2630   1920   1663    138     -8   -735       C  
ATOM   1097  N   ARG A 142      14.935  43.678   9.642  1.00 15.49           N  
ANISOU 1097  N   ARG A 142     2711   1796   1375    -59   -182   -216       N  
ATOM   1098  CA  ARG A 142      15.990  42.754   9.200  1.00 15.96           C  
ANISOU 1098  CA  ARG A 142     2801   1854   1409    -53   -271   -228       C  
ATOM   1099  C   ARG A 142      16.888  43.348   8.111  1.00 16.53           C  
ANISOU 1099  C   ARG A 142     2859   1983   1437    -24   -314   -252       C  
ATOM   1100  O   ARG A 142      18.099  43.150   8.133  1.00 16.80           O  
ANISOU 1100  O   ARG A 142     2884   2126   1373    -65   -392   -242       O  
ATOM   1101  CB  ARG A 142      15.408  41.400   8.781  1.00 16.16           C  
ANISOU 1101  CB  ARG A 142     2791   1840   1506    -52   -233   -208       C  
ATOM   1102  CG  ARG A 142      14.949  40.566   9.975  1.00 15.96           C  
ANISOU 1102  CG  ARG A 142     2829   1799   1437    -23   -351   -111       C  
ATOM   1103  CD  ARG A 142      14.635  39.130   9.599  1.00 16.19           C  
ANISOU 1103  CD  ARG A 142     2644   1789   1718    -11   -427   -102       C  
ATOM   1104  NE  ARG A 142      14.294  38.359  10.796  1.00 16.17           N  
ANISOU 1104  NE  ARG A 142     2494   1971   1677   -206   -610   -154       N  
ATOM   1105  CZ  ARG A 142      13.054  38.147  11.231  1.00 17.17           C  
ANISOU 1105  CZ  ARG A 142     2739   1913   1869    -50   -537   -242       C  
ATOM   1106  NH1 ARG A 142      12.012  38.611  10.548  1.00 18.08           N  
ANISOU 1106  NH1 ARG A 142     2725   1927   2215    -11   -586   -136       N  
ATOM   1107  NH2 ARG A 142      12.858  37.431  12.335  1.00 17.83           N  
ANISOU 1107  NH2 ARG A 142     2770   2089   1915     57   -512   -128       N  
ATOM   1108  N   ASP A 143      16.299  44.088   7.172  1.00 16.89           N  
ANISOU 1108  N   ASP A 143     2947   2061   1410    -59   -350   -219       N  
ATOM   1109  CA  ASP A 143      17.078  44.828   6.175  1.00 17.44           C  
ANISOU 1109  CA  ASP A 143     2966   2122   1536    -93   -411   -278       C  
ATOM   1110  C   ASP A 143      18.109  45.774   6.827  1.00 16.76           C  
ANISOU 1110  C   ASP A 143     2870   2029   1469    -81   -410   -290       C  
ATOM   1111  O   ASP A 143      19.278  45.790   6.432  1.00 16.64           O  
ANISOU 1111  O   ASP A 143     2856   2013   1451   -111   -394   -339       O  
ATOM   1112  CB  ASP A 143      16.142  45.642   5.275  1.00 17.90           C  
ANISOU 1112  CB  ASP A 143     3044   2210   1547    -89   -450   -274       C  
ATOM   1113  CG  ASP A 143      15.393  44.789   4.265  1.00 20.37           C  
ANISOU 1113  CG  ASP A 143     3309   2544   1884    -29   -513   -338       C  
ATOM   1114  OD1 ASP A 143      15.740  43.600   4.064  1.00 22.29           O  
ANISOU 1114  OD1 ASP A 143     3680   2755   2035   -125   -513   -681       O  
ATOM   1115  OD2 ASP A 143      14.448  45.329   3.655  1.00 22.89           O  
ANISOU 1115  OD2 ASP A 143     3569   3220   1907    -90   -630   -373       O  
ATOM   1116  N   VAL A 144      17.670  46.520   7.842  1.00 15.88           N  
ANISOU 1116  N   VAL A 144     2760   1921   1349    -59   -437   -234       N  
ATOM   1117  CA  VAL A 144      18.470  47.589   8.443  1.00 15.26           C  
ANISOU 1117  CA  VAL A 144     2666   1854   1275    -10   -395   -238       C  
ATOM   1118  C   VAL A 144      19.488  47.003   9.427  1.00 14.97           C  
ANISOU 1118  C   VAL A 144     2544   1898   1245     21   -360   -247       C  
ATOM   1119  O   VAL A 144      20.711  47.199   9.286  1.00 14.98           O  
ANISOU 1119  O   VAL A 144     2544   2012   1134    -34   -382   -132       O  
ATOM   1120  CB  VAL A 144      17.537  48.635   9.135  1.00 15.14           C  
ANISOU 1120  CB  VAL A 144     2662   1819   1271     19   -427   -271       C  
ATOM   1121  CG1 VAL A 144      18.335  49.662   9.927  1.00 14.85           C  
ANISOU 1121  CG1 VAL A 144     2580   1786   1276    -83   -337   -263       C  
ATOM   1122  CG2 VAL A 144      16.654  49.334   8.104  1.00 16.46           C  
ANISOU 1122  CG2 VAL A 144     2768   1689   1796    -18   -483   -266       C  
ATOM   1123  N   PHE A 145      18.984  46.265  10.409  1.00 14.43           N  
ANISOU 1123  N   PHE A 145     2441   1820   1218     39   -305   -276       N  
ATOM   1124  CA  PHE A 145      19.849  45.657  11.423  1.00 14.21           C  
ANISOU 1124  CA  PHE A 145     2344   1849   1206    159   -271   -360       C  
ATOM   1125  C   PHE A 145      20.669  44.482  10.913  1.00 14.72           C  
ANISOU 1125  C   PHE A 145     2390   1880   1320    134   -264   -385       C  
ATOM   1126  O   PHE A 145      21.803  44.299  11.345  1.00 15.13           O  
ANISOU 1126  O   PHE A 145     2377   1887   1482    192   -332   -427       O  
ATOM   1127  CB  PHE A 145      19.035  45.214  12.631  1.00 13.46           C  
ANISOU 1127  CB  PHE A 145     2272   1780   1059    160   -273   -363       C  
ATOM   1128  CG  PHE A 145      18.554  46.354  13.498  1.00 15.00           C  
ANISOU 1128  CG  PHE A 145     2450   2060   1187    210   -179   -446       C  
ATOM   1129  CD1 PHE A 145      17.382  47.041  13.190  1.00 14.61           C  
ANISOU 1129  CD1 PHE A 145     2623   1867   1061    341    -97   -522       C  
ATOM   1130  CD2 PHE A 145      19.263  46.711  14.649  1.00 13.71           C  
ANISOU 1130  CD2 PHE A 145     2293   1969    943    149   -368   -657       C  
ATOM   1131  CE1 PHE A 145      16.921  48.085  14.018  1.00 16.59           C  
ANISOU 1131  CE1 PHE A 145     2724   2301   1278    209   -158   -602       C  
ATOM   1132  CE2 PHE A 145      18.820  47.760  15.478  1.00 15.40           C  
ANISOU 1132  CE2 PHE A 145     2336   2180   1336    151   -255   -475       C  
ATOM   1133  CZ  PHE A 145      17.645  48.448  15.158  1.00 14.65           C  
ANISOU 1133  CZ  PHE A 145     2361   2154   1049    153   -180   -452       C  
ATOM   1134  N   GLY A 146      20.094  43.695  10.003  1.00 15.29           N  
ANISOU 1134  N   GLY A 146     2416   1986   1404    153   -259   -441       N  
ATOM   1135  CA  GLY A 146      20.720  42.458   9.554  1.00 16.22           C  
ANISOU 1135  CA  GLY A 146     2577   2128   1456     88   -165   -503       C  
ATOM   1136  C   GLY A 146      21.551  42.681   8.311  1.00 17.29           C  
ANISOU 1136  C   GLY A 146     2701   2272   1593     70   -159   -493       C  
ATOM   1137  O   GLY A 146      22.773  42.536   8.337  1.00 17.74           O  
ANISOU 1137  O   GLY A 146     2677   2496   1567    119   -154   -483       O  
ATOM   1138  N   LYS A 147      20.889  43.063   7.224  1.00 17.73           N  
ANISOU 1138  N   LYS A 147     2838   2342   1553     13   -113   -475       N  
ATOM   1139  CA  LYS A 147      21.564  43.194   5.930  1.00 18.89           C  
ANISOU 1139  CA  LYS A 147     2951   2427   1800    -26    -66   -469       C  
ATOM   1140  C   LYS A 147      22.578  44.343   5.919  1.00 18.33           C  
ANISOU 1140  C   LYS A 147     2882   2379   1703      9    -28   -413       C  
ATOM   1141  O   LYS A 147      23.663  44.204   5.343  1.00 18.22           O  
ANISOU 1141  O   LYS A 147     2789   2301   1831     12      1   -404       O  
ATOM   1142  CB  LYS A 147      20.538  43.354   4.803  1.00 18.61           C  
ANISOU 1142  CB  LYS A 147     2920   2426   1722    -55   -110   -463       C  
ATOM   1143  CG  LYS A 147      19.638  42.125   4.603  1.00 21.91           C  
ANISOU 1143  CG  LYS A 147     3379   2803   2140     -5   -121   -423       C  
ATOM   1144  CD  LYS A 147      18.856  42.192   3.285  1.00 22.84           C  
ANISOU 1144  CD  LYS A 147     3404   2888   2384   -168   -124   -697       C  
ATOM   1145  CE  LYS A 147      18.043  40.920   3.056  1.00 26.58           C  
ANISOU 1145  CE  LYS A 147     3867   3160   3070     -9      2   -768       C  
ATOM   1146  NZ  LYS A 147      18.885  39.852   2.471  1.00 29.17           N  
ANISOU 1146  NZ  LYS A 147     4247   3436   3399   -105   -142   -883       N  
ATOM   1147  N   ALA A 148      22.221  45.468   6.544  1.00 17.12           N  
ANISOU 1147  N   ALA A 148     2809   2267   1428     16     27   -462       N  
ATOM   1148  CA  ALA A 148      23.136  46.608   6.617  1.00 16.51           C  
ANISOU 1148  CA  ALA A 148     2769   2215   1287     57     88   -408       C  
ATOM   1149  C   ALA A 148      24.091  46.483   7.803  1.00 16.37           C  
ANISOU 1149  C   ALA A 148     2705   2195   1317     67    135   -407       C  
ATOM   1150  O   ALA A 148      25.293  46.315   7.624  1.00 15.49           O  
ANISOU 1150  O   ALA A 148     2667   2152   1064    132    305   -459       O  
ATOM   1151  CB  ALA A 148      22.375  47.935   6.656  1.00 16.66           C  
ANISOU 1151  CB  ALA A 148     2775   2246   1307     61    110   -427       C  
ATOM   1152  N   MET A 149      23.562  46.558   9.018  1.00 15.77           N  
ANISOU 1152  N   MET A 149     2596   2208   1186     87    176   -372       N  
ATOM   1153  CA  MET A 149      24.445  46.596  10.187  1.00 16.59           C  
ANISOU 1153  CA  MET A 149     2668   2246   1386    126    191   -304       C  
ATOM   1154  C   MET A 149      25.204  45.301  10.442  1.00 16.29           C  
ANISOU 1154  C   MET A 149     2552   2200   1438    122    197   -293       C  
ATOM   1155  O   MET A 149      26.344  45.342  10.909  1.00 17.19           O  
ANISOU 1155  O   MET A 149     2630   2245   1656    162    104   -251       O  
ATOM   1156  CB  MET A 149      23.679  46.999  11.442  1.00 16.32           C  
ANISOU 1156  CB  MET A 149     2651   2213   1335    165    273   -384       C  
ATOM   1157  CG  MET A 149      23.283  48.453  11.481  1.00 17.23           C  
ANISOU 1157  CG  MET A 149     2830   2253   1463    104    183   -348       C  
ATOM   1158  SD  MET A 149      22.342  48.741  12.986  1.00 17.11           S  
ANISOU 1158  SD  MET A 149     2952   2273   1275    131    152   -189       S  
ATOM   1159  CE  MET A 149      20.744  49.164  12.301  1.00 17.27           C  
ANISOU 1159  CE  MET A 149     2956   2345   1262    283     90   -271       C  
ATOM   1160  N   GLY A 150      24.571  44.161  10.162  1.00 15.80           N  
ANISOU 1160  N   GLY A 150     2425   2151   1424    103    127   -309       N  
ATOM   1161  CA  GLY A 150      25.178  42.860  10.434  1.00 15.82           C  
ANISOU 1161  CA  GLY A 150     2405   2065   1537     -6     90   -222       C  
ATOM   1162  C   GLY A 150      24.907  42.308  11.822  1.00 15.67           C  
ANISOU 1162  C   GLY A 150     2318   2023   1610      1     35   -201       C  
ATOM   1163  O   GLY A 150      25.650  41.453  12.301  1.00 15.88           O  
ANISOU 1163  O   GLY A 150     2289   2124   1619     39     11   -148       O  
ATOM   1164  N   LEU A 151      23.834  42.791  12.451  1.00 15.31           N  
ANISOU 1164  N   LEU A 151     2257   1968   1591    -49      0   -183       N  
ATOM   1165  CA  LEU A 151      23.384  42.335  13.768  1.00 14.88           C  
ANISOU 1165  CA  LEU A 151     2184   1881   1589    -82    -52   -141       C  
ATOM   1166  C   LEU A 151      22.373  41.197  13.632  1.00 15.19           C  
ANISOU 1166  C   LEU A 151     2167   1917   1685    -82   -114   -141       C  
ATOM   1167  O   LEU A 151      21.809  40.987  12.552  1.00 15.80           O  
ANISOU 1167  O   LEU A 151     2339   2001   1660   -116    -80   -116       O  
ATOM   1168  CB  LEU A 151      22.750  43.505  14.533  1.00 14.74           C  
ANISOU 1168  CB  LEU A 151     2245   1900   1453   -125    -47   -173       C  
ATOM   1169  CG  LEU A 151      23.668  44.696  14.837  1.00 13.67           C  
ANISOU 1169  CG  LEU A 151     2133   1810   1250    -53    -73   -108       C  
ATOM   1170  CD1 LEU A 151      22.909  45.734  15.617  1.00 15.10           C  
ANISOU 1170  CD1 LEU A 151     2355   1770   1612     47   -197    -97       C  
ATOM   1171  CD2 LEU A 151      24.897  44.222  15.612  1.00 14.20           C  
ANISOU 1171  CD2 LEU A 151     2223   1769   1401     79   -158    187       C  
ATOM   1172  N   THR A 152      22.137  40.482  14.735  1.00 15.08           N  
ANISOU 1172  N   THR A 152     2059   1919   1752    -64   -145   -146       N  
ATOM   1173  CA  THR A 152      21.293  39.275  14.731  1.00 15.14           C  
ANISOU 1173  CA  THR A 152     1924   1917   1912     19   -195   -121       C  
ATOM   1174  C   THR A 152      19.839  39.594  15.080  1.00 14.67           C  
ANISOU 1174  C   THR A 152     1895   1829   1849      1   -238   -162       C  
ATOM   1175  O   THR A 152      19.542  40.693  15.565  1.00 13.81           O  
ANISOU 1175  O   THR A 152     1812   1604   1829     -8   -246   -298       O  
ATOM   1176  CB  THR A 152      21.780  38.216  15.743  1.00 15.04           C  
ANISOU 1176  CB  THR A 152     1851   1962   1900     42   -192    -81       C  
ATOM   1177  OG1 THR A 152      21.599  38.719  17.073  1.00 14.77           O  
ANISOU 1177  OG1 THR A 152     1705   1899   2007    189   -194     49       O  
ATOM   1178  CG2 THR A 152      23.249  37.836  15.503  1.00 15.94           C  
ANISOU 1178  CG2 THR A 152     1832   2076   2149     98   -156   -143       C  
ATOM   1179  N   ASP A 153      18.946  38.628  14.854  1.00 13.95           N  
ANISOU 1179  N   ASP A 153     1884   1706   1710    -15   -333   -226       N  
ATOM   1180  CA  ASP A 153      17.544  38.787  15.250  1.00 14.37           C  
ANISOU 1180  CA  ASP A 153     2015   1720   1724   -108   -386   -180       C  
ATOM   1181  C   ASP A 153      17.425  39.034  16.748  1.00 13.57           C  
ANISOU 1181  C   ASP A 153     1928   1568   1660   -117   -369   -193       C  
ATOM   1182  O   ASP A 153      16.646  39.881  17.178  1.00 14.17           O  
ANISOU 1182  O   ASP A 153     2040   1635   1708   -107   -427   -199       O  
ATOM   1183  CB  ASP A 153      16.713  37.568  14.855  1.00 14.35           C  
ANISOU 1183  CB  ASP A 153     2050   1726   1674   -100   -459   -232       C  
ATOM   1184  CG  ASP A 153      16.359  37.566  13.371  1.00 16.07           C  
ANISOU 1184  CG  ASP A 153     2421   1978   1704   -163   -480   -141       C  
ATOM   1185  OD1 ASP A 153      16.760  38.516  12.652  1.00 17.36           O  
ANISOU 1185  OD1 ASP A 153     2854   1948   1792    151   -609     54       O  
ATOM   1186  OD2 ASP A 153      15.683  36.612  12.935  1.00 17.62           O  
ANISOU 1186  OD2 ASP A 153     2750   2189   1753    -76   -475   -314       O  
ATOM   1187  N   GLN A 154      18.217  38.307  17.530  1.00 13.45           N  
ANISOU 1187  N   GLN A 154     2028   1472   1609    -86   -314   -119       N  
ATOM   1188  CA  GLN A 154      18.258  38.531  18.971  1.00 13.41           C  
ANISOU 1188  CA  GLN A 154     2023   1474   1598      5   -328    -54       C  
ATOM   1189  C   GLN A 154      18.640  39.973  19.287  1.00 13.12           C  
ANISOU 1189  C   GLN A 154     1952   1447   1585     14   -249   -117       C  
ATOM   1190  O   GLN A 154      17.984  40.616  20.119  1.00 12.64           O  
ANISOU 1190  O   GLN A 154     1913   1378   1509     65   -188   -129       O  
ATOM   1191  CB  GLN A 154      19.231  37.568  19.651  1.00 13.92           C  
ANISOU 1191  CB  GLN A 154     2068   1550   1668     66   -316    -15       C  
ATOM   1192  CG  GLN A 154      19.321  37.783  21.162  1.00 14.60           C  
ANISOU 1192  CG  GLN A 154     2300   1618   1629     79   -313    162       C  
ATOM   1193  CD  GLN A 154      20.326  36.848  21.795  1.00 16.48           C  
ANISOU 1193  CD  GLN A 154     2596   1906   1760    -14   -314    246       C  
ATOM   1194  OE1 GLN A 154      20.108  35.640  21.864  1.00 16.27           O  
ANISOU 1194  OE1 GLN A 154     2712   1706   1760     60     -5    445       O  
ATOM   1195  NE2 GLN A 154      21.450  37.398  22.232  1.00 18.25           N  
ANISOU 1195  NE2 GLN A 154     2796   2082   2055    -47   -499    139       N  
ATOM   1196  N   ASP A 155      19.685  40.477  18.619  1.00 12.35           N  
ANISOU 1196  N   ASP A 155     1853   1386   1453     12   -193   -131       N  
ATOM   1197  CA  ASP A 155      20.132  41.872  18.807  1.00 11.77           C  
ANISOU 1197  CA  ASP A 155     1784   1381   1306     23   -130   -191       C  
ATOM   1198  C   ASP A 155      18.992  42.846  18.504  1.00 11.34           C  
ANISOU 1198  C   ASP A 155     1682   1417   1207      4   -143   -217       C  
ATOM   1199  O   ASP A 155      18.835  43.846  19.192  1.00 10.49           O  
ANISOU 1199  O   ASP A 155     1640   1271   1074     39   -148   -314       O  
ATOM   1200  CB  ASP A 155      21.327  42.217  17.910  1.00 12.09           C  
ANISOU 1200  CB  ASP A 155     1710   1449   1435     22   -135   -158       C  
ATOM   1201  CG  ASP A 155      22.591  41.416  18.251  1.00 13.37           C  
ANISOU 1201  CG  ASP A 155     1957   1612   1507    104    -34   -136       C  
ATOM   1202  OD1 ASP A 155      22.777  41.014  19.426  1.00 12.22           O  
ANISOU 1202  OD1 ASP A 155     1896   1547   1199    -37     88   -301       O  
ATOM   1203  OD2 ASP A 155      23.415  41.201  17.327  1.00 15.93           O  
ANISOU 1203  OD2 ASP A 155     2678   1756   1617    227   -154   -303       O  
ATOM   1204  N   ILE A 156      18.209  42.569  17.461  1.00 11.24           N  
ANISOU 1204  N   ILE A 156     1655   1467   1149    -40   -146   -317       N  
ATOM   1205  CA  ILE A 156      17.092  43.472  17.113  1.00 11.31           C  
ANISOU 1205  CA  ILE A 156     1659   1583   1055    -69   -156   -339       C  
ATOM   1206  C   ILE A 156      16.098  43.639  18.274  1.00 11.55           C  
ANISOU 1206  C   ILE A 156     1646   1565   1177    -98   -149   -331       C  
ATOM   1207  O   ILE A 156      15.736  44.764  18.634  1.00 11.34           O  
ANISOU 1207  O   ILE A 156     1607   1521   1180      2   -121   -358       O  
ATOM   1208  CB  ILE A 156      16.331  43.008  15.856  1.00 11.15           C  
ANISOU 1208  CB  ILE A 156     1742   1564    930    -72   -140   -385       C  
ATOM   1209  CG1 ILE A 156      17.257  43.055  14.632  1.00 11.67           C  
ANISOU 1209  CG1 ILE A 156     1724   1715    993   -101    -36   -464       C  
ATOM   1210  CG2 ILE A 156      15.095  43.890  15.632  1.00 10.65           C  
ANISOU 1210  CG2 ILE A 156     1611   1791    642    -43   -185   -421       C  
ATOM   1211  CD1 ILE A 156      16.669  42.363  13.388  1.00 13.20           C  
ANISOU 1211  CD1 ILE A 156     1970   1855   1190     -8   -203   -426       C  
ATOM   1212  N   VAL A 157      15.673  42.518  18.857  1.00 10.92           N  
ANISOU 1212  N   VAL A 157     1534   1511   1102   -123    -99   -209       N  
ATOM   1213  CA  VAL A 157      14.667  42.554  19.918  1.00 10.42           C  
ANISOU 1213  CA  VAL A 157     1441   1423   1093   -206    -97   -159       C  
ATOM   1214  C   VAL A 157      15.269  43.221  21.168  1.00 10.10           C  
ANISOU 1214  C   VAL A 157     1403   1415   1017   -178    -89   -142       C  
ATOM   1215  O   VAL A 157      14.679  44.161  21.717  1.00 10.44           O  
ANISOU 1215  O   VAL A 157     1400   1461   1104   -260   -137   -120       O  
ATOM   1216  CB  VAL A 157      14.116  41.160  20.252  1.00 10.83           C  
ANISOU 1216  CB  VAL A 157     1489   1516   1106   -188   -166   -181       C  
ATOM   1217  CG1 VAL A 157      13.041  41.271  21.346  1.00  9.90           C  
ANISOU 1217  CG1 VAL A 157     1271   1331   1160   -331     50   -145       C  
ATOM   1218  CG2 VAL A 157      13.575  40.457  18.975  1.00 10.89           C  
ANISOU 1218  CG2 VAL A 157     1664   1228   1245   -349     -1   -223       C  
ATOM   1219  N   ALA A 158      16.455  42.767  21.575  1.00 10.25           N  
ANISOU 1219  N   ALA A 158     1418   1475   1000   -238    -75    -90       N  
ATOM   1220  CA  ALA A 158      17.117  43.333  22.754  1.00 10.16           C  
ANISOU 1220  CA  ALA A 158     1352   1471   1036   -134    -76    -79       C  
ATOM   1221  C   ALA A 158      17.311  44.855  22.619  1.00 10.34           C  
ANISOU 1221  C   ALA A 158     1387   1498   1043    -37    -26    -14       C  
ATOM   1222  O   ALA A 158      16.954  45.612  23.529  1.00  9.71           O  
ANISOU 1222  O   ALA A 158     1434   1434    820      6     54      8       O  
ATOM   1223  CB  ALA A 158      18.442  42.632  23.036  1.00 10.06           C  
ANISOU 1223  CB  ALA A 158     1472   1305   1042    -41    -93    -44       C  
ATOM   1224  N   LEU A 159      17.855  45.297  21.482  1.00 10.57           N  
ANISOU 1224  N   LEU A 159     1360   1601   1053     -4     12    -83       N  
ATOM   1225  CA  LEU A 159      18.086  46.730  21.247  1.00 10.17           C  
ANISOU 1225  CA  LEU A 159     1252   1651    959    -19      6    -65       C  
ATOM   1226  C   LEU A 159      16.811  47.573  21.208  1.00 10.62           C  
ANISOU 1226  C   LEU A 159     1370   1727    937    -12      2   -108       C  
ATOM   1227  O   LEU A 159      16.840  48.738  21.614  1.00 11.18           O  
ANISOU 1227  O   LEU A 159     1454   1885    906    -32    -50   -228       O  
ATOM   1228  CB  LEU A 159      18.914  46.967  19.973  1.00  9.92           C  
ANISOU 1228  CB  LEU A 159     1152   1687    927     37     60   -267       C  
ATOM   1229  CG  LEU A 159      20.378  46.519  20.071  1.00  8.90           C  
ANISOU 1229  CG  LEU A 159      854   1550    974    -92    116   -295       C  
ATOM   1230  CD1 LEU A 159      21.021  46.641  18.699  1.00  9.76           C  
ANISOU 1230  CD1 LEU A 159      845   1844   1017    -75    229   -408       C  
ATOM   1231  CD2 LEU A 159      21.183  47.299  21.122  1.00  8.97           C  
ANISOU 1231  CD2 LEU A 159     1047   1507    853    -18     63   -705       C  
ATOM   1232  N   SER A 160      15.721  46.996  20.691  1.00 10.68           N  
ANISOU 1232  N   SER A 160     1370   1817    868     63   -146    -74       N  
ATOM   1233  CA  SER A 160      14.403  47.640  20.720  1.00 10.89           C  
ANISOU 1233  CA  SER A 160     1422   1806    908     -9   -246   -126       C  
ATOM   1234  C   SER A 160      14.020  47.984  22.170  1.00 11.18           C  
ANISOU 1234  C   SER A 160     1437   1806   1004     -3   -224   -105       C  
ATOM   1235  O   SER A 160      13.335  48.975  22.422  1.00 11.42           O  
ANISOU 1235  O   SER A 160     1488   1823   1027     47   -267    -57       O  
ATOM   1236  CB  SER A 160      13.348  46.757  20.048  1.00 10.87           C  
ANISOU 1236  CB  SER A 160     1436   1741    951     59   -267   -164       C  
ATOM   1237  OG  SER A 160      13.630  46.623  18.653  1.00 10.87           O  
ANISOU 1237  OG  SER A 160     1498   1962    668      2   -546   -372       O  
ATOM   1238  N   GLY A 161      14.513  47.168  23.105  1.00 10.88           N  
ANISOU 1238  N   GLY A 161     1435   1811    885      2   -353   -106       N  
ATOM   1239  CA  GLY A 161      14.373  47.419  24.552  1.00 11.49           C  
ANISOU 1239  CA  GLY A 161     1511   1853    999     32   -263   -116       C  
ATOM   1240  C   GLY A 161      14.973  48.735  25.048  1.00 11.39           C  
ANISOU 1240  C   GLY A 161     1497   1875    956    103   -316   -152       C  
ATOM   1241  O   GLY A 161      14.666  49.174  26.154  1.00 12.73           O  
ANISOU 1241  O   GLY A 161     1653   2022   1158     85   -248   -117       O  
ATOM   1242  N   GLY A 162      15.803  49.376  24.227  1.00 11.56           N  
ANISOU 1242  N   GLY A 162     1491   1836   1062     44   -312   -161       N  
ATOM   1243  CA  GLY A 162      16.335  50.714  24.519  1.00 12.33           C  
ANISOU 1243  CA  GLY A 162     1597   2030   1056     51   -187   -123       C  
ATOM   1244  C   GLY A 162      15.221  51.730  24.752  1.00 12.24           C  
ANISOU 1244  C   GLY A 162     1539   2120    989     23   -163    -90       C  
ATOM   1245  O   GLY A 162      15.412  52.733  25.453  1.00 12.41           O  
ANISOU 1245  O   GLY A 162     1450   2210   1053     65   -164   -135       O  
ATOM   1246  N   HIS A 163      14.050  51.460  24.170  1.00 11.48           N  
ANISOU 1246  N   HIS A 163     1483   2090    787    -48   -116    -42       N  
ATOM   1247  CA  HIS A 163      12.877  52.299  24.334  1.00 12.03           C  
ANISOU 1247  CA  HIS A 163     1627   2119    823    -31   -157      0       C  
ATOM   1248  C   HIS A 163      12.287  52.186  25.745  1.00 12.16           C  
ANISOU 1248  C   HIS A 163     1636   2134    848     17   -141     -4       C  
ATOM   1249  O   HIS A 163      11.305  52.852  26.089  1.00 12.75           O  
ANISOU 1249  O   HIS A 163     1768   2244    831     86   -130    -12       O  
ATOM   1250  CB  HIS A 163      11.838  51.978  23.242  1.00 11.95           C  
ANISOU 1250  CB  HIS A 163     1643   2122    774    -12   -196    -52       C  
ATOM   1251  CG  HIS A 163      12.264  52.428  21.873  1.00 12.33           C  
ANISOU 1251  CG  HIS A 163     1773   2099    812    -73   -181     10       C  
ATOM   1252  ND1 HIS A 163      11.743  51.899  20.712  1.00 14.12           N  
ANISOU 1252  ND1 HIS A 163     1989   2265   1108    -64    -74    -22       N  
ATOM   1253  CD2 HIS A 163      13.185  53.347  21.487  1.00 11.28           C  
ANISOU 1253  CD2 HIS A 163     1805   2036    445    -49    -68     91       C  
ATOM   1254  CE1 HIS A 163      12.307  52.486  19.669  1.00 12.34           C  
ANISOU 1254  CE1 HIS A 163     1616   1955   1117   -379   -185    -17       C  
ATOM   1255  NE2 HIS A 163      13.189  53.364  20.112  1.00 13.89           N  
ANISOU 1255  NE2 HIS A 163     2181   2016   1079    -98   -110    -86       N  
ATOM   1256  N   THR A 164      12.902  51.350  26.573  1.00 11.93           N  
ANISOU 1256  N   THR A 164     1625   2005    901     55    -84     30       N  
ATOM   1257  CA  THR A 164      12.549  51.325  27.987  1.00 12.23           C  
ANISOU 1257  CA  THR A 164     1699   2008    939     94    -16    104       C  
ATOM   1258  C   THR A 164      12.880  52.659  28.697  1.00 12.72           C  
ANISOU 1258  C   THR A 164     1737   2117    980    115    -52     69       C  
ATOM   1259  O   THR A 164      12.370  52.952  29.794  1.00 13.35           O  
ANISOU 1259  O   THR A 164     1868   2142   1062     44    -41     50       O  
ATOM   1260  CB  THR A 164      13.170  50.121  28.696  1.00 12.26           C  
ANISOU 1260  CB  THR A 164     1778   1983    895    132     70    125       C  
ATOM   1261  OG1 THR A 164      12.470  49.903  29.921  1.00 15.63           O  
ANISOU 1261  OG1 THR A 164     2418   2189   1330    269    289    312       O  
ATOM   1262  CG2 THR A 164      14.662  50.346  28.973  1.00 10.27           C  
ANISOU 1262  CG2 THR A 164     1485   1709    708    155     45    109       C  
ATOM   1263  N   ILE A 165      13.723  53.471  28.056  1.00 12.26           N  
ANISOU 1263  N   ILE A 165     1631   2090    934     99   -171     74       N  
ATOM   1264  CA  ILE A 165      13.939  54.844  28.506  1.00 11.87           C  
ANISOU 1264  CA  ILE A 165     1522   2092    895    201   -174     55       C  
ATOM   1265  C   ILE A 165      13.569  55.829  27.400  1.00 12.84           C  
ANISOU 1265  C   ILE A 165     1609   2131   1135    196   -242    -35       C  
ATOM   1266  O   ILE A 165      13.717  55.534  26.209  1.00 13.03           O  
ANISOU 1266  O   ILE A 165     1704   2165   1079    243   -197     34       O  
ATOM   1267  CB  ILE A 165      15.388  55.084  29.042  1.00 11.98           C  
ANISOU 1267  CB  ILE A 165     1584   2099    865    208   -136     -8       C  
ATOM   1268  CG1 ILE A 165      16.457  54.912  27.939  1.00 11.81           C  
ANISOU 1268  CG1 ILE A 165     1340   2133   1012    193   -151     34       C  
ATOM   1269  CG2 ILE A 165      15.646  54.174  30.260  1.00 11.84           C  
ANISOU 1269  CG2 ILE A 165     1483   2325    687    140   -231    171       C  
ATOM   1270  CD1 ILE A 165      17.854  55.394  28.345  1.00 12.36           C  
ANISOU 1270  CD1 ILE A 165     1550   2310    835    306   -184    167       C  
ATOM   1271  N   GLY A 166      13.059  56.986  27.809  1.00 12.51           N  
ANISOU 1271  N   GLY A 166     1528   2079   1145    254   -307    -90       N  
ATOM   1272  CA  GLY A 166      12.772  58.061  26.886  1.00 12.80           C  
ANISOU 1272  CA  GLY A 166     1517   2095   1249    198   -399   -116       C  
ATOM   1273  C   GLY A 166      11.357  58.087  26.359  1.00 12.91           C  
ANISOU 1273  C   GLY A 166     1531   2087   1285    240   -416   -130       C  
ATOM   1274  O   GLY A 166      10.462  57.388  26.860  1.00 13.28           O  
ANISOU 1274  O   GLY A 166     1611   2273   1162    276   -408   -165       O  
ATOM   1275  N   ALA A 167      11.180  58.909  25.331  1.00 12.96           N  
ANISOU 1275  N   ALA A 167     1517   2128   1277    249   -449   -128       N  
ATOM   1276  CA  ALA A 167       9.885  59.247  24.783  1.00 13.15           C  
ANISOU 1276  CA  ALA A 167     1628   2063   1305    285   -445   -130       C  
ATOM   1277  C   ALA A 167      10.078  59.801  23.386  1.00 12.93           C  
ANISOU 1277  C   ALA A 167     1632   1971   1309    268   -482   -134       C  
ATOM   1278  O   ALA A 167      11.156  60.322  23.049  1.00 12.97           O  
ANISOU 1278  O   ALA A 167     1596   2121   1211    173   -550    -84       O  
ATOM   1279  CB  ALA A 167       9.214  60.302  25.662  1.00 13.11           C  
ANISOU 1279  CB  ALA A 167     1652   1938   1388    439   -422   -174       C  
ATOM   1280  N   ALA A 168       9.029  59.674  22.583  1.00 12.45           N  
ANISOU 1280  N   ALA A 168     1643   1808   1277    340   -504   -137       N  
ATOM   1281  CA  ALA A 168       8.965  60.335  21.297  1.00 12.91           C  
ANISOU 1281  CA  ALA A 168     1666   1826   1411    312   -506   -164       C  
ATOM   1282  C   ALA A 168       8.371  61.721  21.515  1.00 13.01           C  
ANISOU 1282  C   ALA A 168     1625   1811   1506    304   -544   -205       C  
ATOM   1283  O   ALA A 168       7.709  61.977  22.536  1.00 13.93           O  
ANISOU 1283  O   ALA A 168     1675   2044   1573    267   -477   -163       O  
ATOM   1284  CB  ALA A 168       8.105  59.544  20.347  1.00 12.95           C  
ANISOU 1284  CB  ALA A 168     1732   1721   1467    307   -520   -239       C  
ATOM   1285  N   HIS A 169       8.598  62.608  20.553  1.00 13.36           N  
ANISOU 1285  N   HIS A 169     1570   1833   1671    228   -525   -217       N  
ATOM   1286  CA  HIS A 169       8.136  63.993  20.655  1.00 13.49           C  
ANISOU 1286  CA  HIS A 169     1537   1839   1748    295   -550   -230       C  
ATOM   1287  C   HIS A 169       7.535  64.369  19.319  1.00 13.69           C  
ANISOU 1287  C   HIS A 169     1554   1828   1816    290   -507   -268       C  
ATOM   1288  O   HIS A 169       8.162  64.139  18.282  1.00 12.93           O  
ANISOU 1288  O   HIS A 169     1469   1675   1767    348   -410   -282       O  
ATOM   1289  CB  HIS A 169       9.295  64.939  20.957  1.00 14.03           C  
ANISOU 1289  CB  HIS A 169     1718   1883   1730    312   -643   -321       C  
ATOM   1290  CG  HIS A 169      10.122  64.525  22.130  1.00 14.82           C  
ANISOU 1290  CG  HIS A 169     1853   2022   1752    383   -857   -307       C  
ATOM   1291  ND1 HIS A 169      11.009  63.468  22.083  1.00 15.62           N  
ANISOU 1291  ND1 HIS A 169     2059   2169   1705    529  -1004   -410       N  
ATOM   1292  CD2 HIS A 169      10.186  65.017  23.389  1.00 16.84           C  
ANISOU 1292  CD2 HIS A 169     2253   2119   2024    434   -934   -395       C  
ATOM   1293  CE1 HIS A 169      11.595  63.338  23.263  1.00 16.45           C  
ANISOU 1293  CE1 HIS A 169     2326   2093   1829    431   -927   -418       C  
ATOM   1294  NE2 HIS A 169      11.104  64.258  24.074  1.00 16.68           N  
ANISOU 1294  NE2 HIS A 169     2180   2392   1763    340  -1182   -391       N  
ATOM   1295  N   LYS A 170       6.336  64.950  19.344  1.00 13.72           N  
ANISOU 1295  N   LYS A 170     1475   1872   1863    350   -451   -296       N  
ATOM   1296  CA  LYS A 170       5.595  65.234  18.106  1.00 14.30           C  
ANISOU 1296  CA  LYS A 170     1472   1993   1966    412   -413   -275       C  
ATOM   1297  C   LYS A 170       6.325  66.233  17.202  1.00 14.45           C  
ANISOU 1297  C   LYS A 170     1482   2087   1919    385   -374   -301       C  
ATOM   1298  O   LYS A 170       6.087  66.259  15.992  1.00 14.64           O  
ANISOU 1298  O   LYS A 170     1568   2110   1883    299   -347   -436       O  
ATOM   1299  CB  LYS A 170       4.150  65.689  18.412  1.00 14.52           C  
ANISOU 1299  CB  LYS A 170     1569   2039   1906    373   -414   -295       C  
ATOM   1300  CG  LYS A 170       4.025  67.033  19.094  1.00 16.17           C  
ANISOU 1300  CG  LYS A 170     1587   2314   2240    621   -352   -291       C  
ATOM   1301  CD  LYS A 170       2.600  67.205  19.659  1.00 16.77           C  
ANISOU 1301  CD  LYS A 170     1674   2459   2237    692   -328   -289       C  
ATOM   1302  CE  LYS A 170       2.455  68.528  20.385  1.00 21.62           C  
ANISOU 1302  CE  LYS A 170     2371   3156   2684    491   -631   -325       C  
ATOM   1303  NZ  LYS A 170       3.339  68.620  21.574  1.00 24.27           N  
ANISOU 1303  NZ  LYS A 170     2798   3610   2813    732   -423   -425       N  
ATOM   1304  N   GLU A 171       7.195  67.058  17.792  1.00 14.70           N  
ANISOU 1304  N   GLU A 171     1556   2099   1929    340   -330   -325       N  
ATOM   1305  CA  GLU A 171       8.013  68.005  17.024  1.00 15.41           C  
ANISOU 1305  CA  GLU A 171     1661   2228   1964    308   -351   -308       C  
ATOM   1306  C   GLU A 171       9.290  67.385  16.440  1.00 15.74           C  
ANISOU 1306  C   GLU A 171     1748   2293   1938    266   -351   -226       C  
ATOM   1307  O   GLU A 171       9.962  68.017  15.614  1.00 16.67           O  
ANISOU 1307  O   GLU A 171     1794   2428   2109    287   -235   -188       O  
ATOM   1308  CB  GLU A 171       8.350  69.262  17.852  1.00 15.99           C  
ANISOU 1308  CB  GLU A 171     1732   2316   2024    269   -367   -257       C  
ATOM   1309  CG  GLU A 171       9.415  69.074  18.911  1.00 18.15           C  
ANISOU 1309  CG  GLU A 171     2000   2636   2259    263   -297   -393       C  
ATOM   1310  CD  GLU A 171       8.894  68.481  20.222  1.00 20.23           C  
ANISOU 1310  CD  GLU A 171     2325   2905   2457    222   -395   -344       C  
ATOM   1311  OE1 GLU A 171       7.685  68.124  20.329  1.00 19.81           O  
ANISOU 1311  OE1 GLU A 171     2161   3045   2319    306   -309   -563       O  
ATOM   1312  OE2 GLU A 171       9.724  68.376  21.156  1.00 22.92           O  
ANISOU 1312  OE2 GLU A 171     2671   3151   2887     90   -399   -369       O  
ATOM   1313  N   ARG A 172       9.629  66.170  16.883  1.00 15.03           N  
ANISOU 1313  N   ARG A 172     1702   2205   1801    268   -436   -260       N  
ATOM   1314  CA  ARG A 172      10.810  65.473  16.376  1.00 15.21           C  
ANISOU 1314  CA  ARG A 172     1758   2243   1777    182   -509   -155       C  
ATOM   1315  C   ARG A 172      10.398  64.405  15.367  1.00 14.25           C  
ANISOU 1315  C   ARG A 172     1693   2073   1645    186   -526   -174       C  
ATOM   1316  O   ARG A 172      10.379  64.677  14.159  1.00 14.74           O  
ANISOU 1316  O   ARG A 172     1777   2104   1716    165   -459    -83       O  
ATOM   1317  CB  ARG A 172      11.675  64.911  17.508  1.00 14.75           C  
ANISOU 1317  CB  ARG A 172     1681   2268   1652    167   -570   -200       C  
ATOM   1318  CG  ARG A 172      12.278  66.018  18.401  1.00 16.27           C  
ANISOU 1318  CG  ARG A 172     1890   2439   1852    116   -729   -131       C  
ATOM   1319  CD  ARG A 172      13.147  65.497  19.527  1.00 16.84           C  
ANISOU 1319  CD  ARG A 172     1904   2603   1889    -23   -645   -222       C  
ATOM   1320  NE  ARG A 172      13.339  66.556  20.530  1.00 18.51           N  
ANISOU 1320  NE  ARG A 172     2243   2865   1922    -86   -700   -514       N  
ATOM   1321  CZ  ARG A 172      13.738  66.352  21.781  1.00 18.69           C  
ANISOU 1321  CZ  ARG A 172     2372   2912   1816   -297   -629   -595       C  
ATOM   1322  NH1 ARG A 172      14.010  65.119  22.198  1.00 18.40           N  
ANISOU 1322  NH1 ARG A 172     2234   3047   1709   -353   -631   -547       N  
ATOM   1323  NH2 ARG A 172      13.869  67.385  22.620  1.00 18.29           N  
ANISOU 1323  NH2 ARG A 172     2107   2934   1908   -437   -422   -622       N  
ATOM   1324  N   SER A 173      10.047  63.203  15.834  1.00 13.52           N  
ANISOU 1324  N   SER A 173     1644   1934   1557    140   -518   -130       N  
ATOM   1325  CA  SER A 173       9.533  62.184  14.905  1.00 13.59           C  
ANISOU 1325  CA  SER A 173     1663   1861   1636    188   -553   -108       C  
ATOM   1326  C   SER A 173       8.095  62.470  14.459  1.00 13.31           C  
ANISOU 1326  C   SER A 173     1676   1820   1561    123   -493    -84       C  
ATOM   1327  O   SER A 173       7.755  62.246  13.307  1.00 13.47           O  
ANISOU 1327  O   SER A 173     1659   1922   1536    102   -467   -198       O  
ATOM   1328  CB  SER A 173       9.632  60.765  15.481  1.00 13.33           C  
ANISOU 1328  CB  SER A 173     1655   1809   1600    210   -530   -103       C  
ATOM   1329  OG  SER A 173       8.817  60.595  16.628  1.00 14.74           O  
ANISOU 1329  OG  SER A 173     1769   1851   1980    379   -629    -85       O  
ATOM   1330  N   GLY A 174       7.269  62.975  15.373  1.00 12.67           N  
ANISOU 1330  N   GLY A 174     1683   1681   1450    149   -436    -42       N  
ATOM   1331  CA  GLY A 174       5.831  63.076  15.141  1.00 12.88           C  
ANISOU 1331  CA  GLY A 174     1817   1728   1346    122   -371    -17       C  
ATOM   1332  C   GLY A 174       5.085  62.188  16.115  1.00 13.12           C  
ANISOU 1332  C   GLY A 174     1919   1730   1335    158   -393    -36       C  
ATOM   1333  O   GLY A 174       3.973  62.514  16.528  1.00 12.68           O  
ANISOU 1333  O   GLY A 174     1786   1767   1265    180   -330     -1       O  
ATOM   1334  N   PHE A 175       5.701  61.064  16.479  1.00 12.92           N  
ANISOU 1334  N   PHE A 175     2030   1655   1224    186   -381    -57       N  
ATOM   1335  CA  PHE A 175       5.191  60.215  17.560  1.00 13.39           C  
ANISOU 1335  CA  PHE A 175     2143   1667   1276    207   -381    -91       C  
ATOM   1336  C   PHE A 175       5.357  60.950  18.882  1.00 13.44           C  
ANISOU 1336  C   PHE A 175     2082   1754   1270    236   -386    -82       C  
ATOM   1337  O   PHE A 175       6.130  61.899  18.939  1.00 13.13           O  
ANISOU 1337  O   PHE A 175     2023   1598   1366    121   -431   -197       O  
ATOM   1338  CB  PHE A 175       5.894  58.860  17.545  1.00 14.04           C  
ANISOU 1338  CB  PHE A 175     2266   1764   1305    223   -367    -42       C  
ATOM   1339  CG  PHE A 175       5.560  58.046  16.336  1.00 13.80           C  
ANISOU 1339  CG  PHE A 175     2299   1857   1088    309   -438    -77       C  
ATOM   1340  CD1 PHE A 175       6.429  58.013  15.242  1.00 16.03           C  
ANISOU 1340  CD1 PHE A 175     2484   2101   1502    423   -459    -75       C  
ATOM   1341  CD2 PHE A 175       4.353  57.334  16.270  1.00 14.51           C  
ANISOU 1341  CD2 PHE A 175     2536   1821   1156    436   -411   -137       C  
ATOM   1342  CE1 PHE A 175       6.101  57.272  14.098  1.00 15.73           C  
ANISOU 1342  CE1 PHE A 175     2582   1947   1448    328   -543   -111       C  
ATOM   1343  CE2 PHE A 175       4.026  56.590  15.142  1.00 16.46           C  
ANISOU 1343  CE2 PHE A 175     2624   2182   1445    412   -512   -116       C  
ATOM   1344  CZ  PHE A 175       4.904  56.554  14.059  1.00 15.81           C  
ANISOU 1344  CZ  PHE A 175     2374   2285   1349    340   -412   -132       C  
ATOM   1345  N   GLU A 176       4.615  60.548  19.921  1.00 13.33           N  
ANISOU 1345  N   GLU A 176     2055   1825   1185    227   -335   -109       N  
ATOM   1346  CA  GLU A 176       4.564  61.341  21.149  1.00 14.01           C  
ANISOU 1346  CA  GLU A 176     2112   2069   1141    262   -278    -92       C  
ATOM   1347  C   GLU A 176       4.362  60.499  22.396  1.00 14.47           C  
ANISOU 1347  C   GLU A 176     2143   2188   1167    244   -250   -140       C  
ATOM   1348  O   GLU A 176       3.420  59.703  22.478  1.00 14.78           O  
ANISOU 1348  O   GLU A 176     2358   2258    998    118   -281    -62       O  
ATOM   1349  CB  GLU A 176       3.476  62.433  21.058  1.00 14.31           C  
ANISOU 1349  CB  GLU A 176     2166   2071   1199    276   -226   -150       C  
ATOM   1350  CG  GLU A 176       3.233  63.239  22.361  1.00 16.11           C  
ANISOU 1350  CG  GLU A 176     2317   2481   1320    250   -233   -201       C  
ATOM   1351  CD  GLU A 176       4.404  64.133  22.750  1.00 16.72           C  
ANISOU 1351  CD  GLU A 176     2417   2719   1213    220   -180   -249       C  
ATOM   1352  OE1 GLU A 176       4.716  64.213  23.956  1.00 18.94           O  
ANISOU 1352  OE1 GLU A 176     2626   3196   1371    184   -284    -48       O  
ATOM   1353  OE2 GLU A 176       5.010  64.766  21.862  1.00 16.55           O  
ANISOU 1353  OE2 GLU A 176     2217   2880   1188    186    -25   -383       O  
ATOM   1354  N   GLY A 177       5.248  60.713  23.363  1.00 14.28           N  
ANISOU 1354  N   GLY A 177     2018   2268   1137    374   -240   -165       N  
ATOM   1355  CA  GLY A 177       5.147  60.069  24.651  1.00 14.74           C  
ANISOU 1355  CA  GLY A 177     1956   2379   1262    379   -239   -173       C  
ATOM   1356  C   GLY A 177       6.109  58.924  24.912  1.00 14.64           C  
ANISOU 1356  C   GLY A 177     1905   2415   1241    362   -260   -214       C  
ATOM   1357  O   GLY A 177       6.774  58.415  23.985  1.00 13.19           O  
ANISOU 1357  O   GLY A 177     1577   2225   1210    489   -241   -249       O  
ATOM   1358  N   PRO A 178       6.176  58.501  26.187  1.00 14.98           N  
ANISOU 1358  N   PRO A 178     1949   2504   1235    356   -233   -191       N  
ATOM   1359  CA  PRO A 178       7.086  57.455  26.624  1.00 15.02           C  
ANISOU 1359  CA  PRO A 178     1914   2566   1227    278   -286   -214       C  
ATOM   1360  C   PRO A 178       6.509  56.074  26.336  1.00 15.09           C  
ANISOU 1360  C   PRO A 178     1934   2560   1237    236   -270   -231       C  
ATOM   1361  O   PRO A 178       5.282  55.919  26.236  1.00 15.24           O  
ANISOU 1361  O   PRO A 178     1816   2565   1409    180   -340   -299       O  
ATOM   1362  CB  PRO A 178       7.164  57.684  28.131  1.00 15.05           C  
ANISOU 1362  CB  PRO A 178     1974   2614   1130    331   -191   -216       C  
ATOM   1363  CG  PRO A 178       5.785  58.216  28.491  1.00 15.21           C  
ANISOU 1363  CG  PRO A 178     1998   2617   1161    383   -300   -164       C  
ATOM   1364  CD  PRO A 178       5.326  59.005  27.293  1.00 15.45           C  
ANISOU 1364  CD  PRO A 178     2038   2575   1253    416   -267   -186       C  
ATOM   1365  N   TRP A 179       7.391  55.093  26.206  1.00 14.64           N  
ANISOU 1365  N   TRP A 179     1864   2590   1106    214   -236   -245       N  
ATOM   1366  CA  TRP A 179       6.996  53.692  26.062  1.00 14.38           C  
ANISOU 1366  CA  TRP A 179     1812   2560   1088    145   -200   -215       C  
ATOM   1367  C   TRP A 179       6.613  53.076  27.413  1.00 14.78           C  
ANISOU 1367  C   TRP A 179     1815   2650   1151    123   -178   -156       C  
ATOM   1368  O   TRP A 179       5.876  52.085  27.468  1.00 14.97           O  
ANISOU 1368  O   TRP A 179     1900   2670   1115     37   -166    -87       O  
ATOM   1369  CB  TRP A 179       8.152  52.880  25.470  1.00 14.01           C  
ANISOU 1369  CB  TRP A 179     1778   2523   1022    161   -193   -246       C  
ATOM   1370  CG  TRP A 179       8.407  53.139  24.020  1.00 13.96           C  
ANISOU 1370  CG  TRP A 179     1803   2465   1034    167   -274   -303       C  
ATOM   1371  CD1 TRP A 179       7.952  52.402  22.959  1.00 13.42           C  
ANISOU 1371  CD1 TRP A 179     1777   2389    931    421   -259   -275       C  
ATOM   1372  CD2 TRP A 179       9.188  54.202  23.466  1.00 13.25           C  
ANISOU 1372  CD2 TRP A 179     1840   2469    726    177    -97   -276       C  
ATOM   1373  NE1 TRP A 179       8.396  52.950  21.783  1.00 14.41           N  
ANISOU 1373  NE1 TRP A 179     2038   2418   1018    282   -183   -402       N  
ATOM   1374  CE2 TRP A 179       9.163  54.051  22.062  1.00 15.29           C  
ANISOU 1374  CE2 TRP A 179     2039   2606   1162    170   -195   -289       C  
ATOM   1375  CE3 TRP A 179       9.919  55.265  24.021  1.00 13.71           C  
ANISOU 1375  CE3 TRP A 179     1718   2441   1050    117     34   -311       C  
ATOM   1376  CZ2 TRP A 179       9.837  54.924  21.202  1.00 14.59           C  
ANISOU 1376  CZ2 TRP A 179     1974   2628    940    251   -191   -189       C  
ATOM   1377  CZ3 TRP A 179      10.585  56.143  23.155  1.00 13.15           C  
ANISOU 1377  CZ3 TRP A 179     1894   2356    746    236    -51   -249       C  
ATOM   1378  CH2 TRP A 179      10.533  55.959  21.761  1.00 14.24           C  
ANISOU 1378  CH2 TRP A 179     1899   2551    958    267   -264   -295       C  
ATOM   1379  N   THR A 180       7.128  53.654  28.495  1.00 14.40           N  
ANISOU 1379  N   THR A 180     1661   2688   1122     72   -190   -118       N  
ATOM   1380  CA  THR A 180       6.952  53.061  29.835  1.00 15.43           C  
ANISOU 1380  CA  THR A 180     1708   2850   1301    131   -195   -150       C  
ATOM   1381  C   THR A 180       6.511  54.103  30.865  1.00 15.32           C  
ANISOU 1381  C   THR A 180     1660   2857   1302     23   -220   -160       C  
ATOM   1382  O   THR A 180       6.598  55.313  30.629  1.00 14.87           O  
ANISOU 1382  O   THR A 180     1605   2852   1191     41   -268   -159       O  
ATOM   1383  CB  THR A 180       8.243  52.364  30.346  1.00 15.37           C  
ANISOU 1383  CB  THR A 180     1692   2815   1331    120   -165   -178       C  
ATOM   1384  OG1 THR A 180       9.229  53.356  30.655  1.00 17.04           O  
ANISOU 1384  OG1 THR A 180     1649   3154   1671    360   -339   -287       O  
ATOM   1385  CG2 THR A 180       8.803  51.358  29.303  1.00 14.84           C  
ANISOU 1385  CG2 THR A 180     1766   2773   1096    325   -189    -70       C  
ATOM   1386  N   SER A 181       6.049  53.613  32.009  1.00 15.89           N  
ANISOU 1386  N   SER A 181     1623   2940   1471    -84   -172   -156       N  
ATOM   1387  CA  SER A 181       5.665  54.464  33.131  1.00 17.08           C  
ANISOU 1387  CA  SER A 181     1788   3005   1697   -172   -150   -153       C  
ATOM   1388  C   SER A 181       6.879  55.061  33.820  1.00 17.00           C  
ANISOU 1388  C   SER A 181     1854   2913   1691   -170   -207   -162       C  
ATOM   1389  O   SER A 181       6.740  55.999  34.597  1.00 17.63           O  
ANISOU 1389  O   SER A 181     1931   2991   1775   -147   -181   -214       O  
ATOM   1390  CB  SER A 181       4.853  53.664  34.151  1.00 16.98           C  
ANISOU 1390  CB  SER A 181     1784   3005   1661   -214   -155   -153       C  
ATOM   1391  OG  SER A 181       3.688  53.154  33.537  1.00 19.43           O  
ANISOU 1391  OG  SER A 181     1979   3375   2027   -163     59    -13       O  
ATOM   1392  N   ASN A 182       8.056  54.494  33.549  1.00 16.77           N  
ANISOU 1392  N   ASN A 182     1809   2880   1683   -225   -190   -169       N  
ATOM   1393  C   ASN A 182      10.373  55.230  33.078  1.00 16.72           C  
ANISOU 1393  C   ASN A 182     1857   2777   1718   -177   -160   -188       C  
ATOM   1394  O   ASN A 182      11.333  54.455  32.948  1.00 16.65           O  
ANISOU 1394  O   ASN A 182     1853   2674   1795   -197   -248   -269       O  
ATOM   1395  CA AASN A 182       9.304  54.974  34.138  0.50 16.76           C  
ANISOU 1395  CA AASN A 182     1849   2820   1698   -181   -187   -157       C  
ATOM   1396  CB AASN A 182       9.784  54.004  35.213  0.50 16.69           C  
ANISOU 1396  CB AASN A 182     1811   2834   1696   -220   -190   -135       C  
ATOM   1397  CG AASN A 182       8.735  53.775  36.273  0.50 15.67           C  
ANISOU 1397  CG AASN A 182     1742   2799   1412   -152   -149   -103       C  
ATOM   1398  OD1AASN A 182       8.581  54.577  37.188  0.50 16.04           O  
ANISOU 1398  OD1AASN A 182     1820   2852   1422   -182   -127   -166       O  
ATOM   1399  ND2AASN A 182       7.985  52.697  36.134  0.50 13.51           N  
ANISOU 1399  ND2AASN A 182     1346   2717   1070   -310   -172    -67       N  
ATOM   1400  CA BASN A 182       9.306  54.984  34.141  0.50 17.36           C  
ANISOU 1400  CA BASN A 182     1946   2872   1776   -175   -177   -149       C  
ATOM   1401  CB BASN A 182       9.819  54.086  35.286  0.50 17.81           C  
ANISOU 1401  CB BASN A 182     1997   2939   1830   -202   -164   -120       C  
ATOM   1402  CG BASN A 182       9.565  52.602  35.052  0.50 19.34           C  
ANISOU 1402  CG BASN A 182     2314   3112   1921   -128   -109    -67       C  
ATOM   1403  OD1BASN A 182       9.395  51.836  36.009  0.50 22.80           O  
ANISOU 1403  OD1BASN A 182     2854   3636   2171   -244     38    -31       O  
ATOM   1404  ND2BASN A 182       9.526  52.184  33.789  0.50 20.09           N  
ANISOU 1404  ND2BASN A 182     2377   3323   1932     33     86     13       N  
ATOM   1405  N   PRO A 183      10.205  56.326  32.308  1.00 16.79           N  
ANISOU 1405  N   PRO A 183     1942   2732   1703    -85   -108   -186       N  
ATOM   1406  CA  PRO A 183      11.081  56.600  31.158  1.00 16.06           C  
ANISOU 1406  CA  PRO A 183     1949   2649   1503    -22    -56   -246       C  
ATOM   1407  C   PRO A 183      12.517  57.001  31.499  1.00 15.29           C  
ANISOU 1407  C   PRO A 183     1918   2552   1340     20    -68   -296       C  
ATOM   1408  O   PRO A 183      13.324  57.198  30.587  1.00 14.40           O  
ANISOU 1408  O   PRO A 183     1964   2536    968     -4    -55   -356       O  
ATOM   1409  CB  PRO A 183      10.364  57.745  30.439  1.00 16.68           C  
ANISOU 1409  CB  PRO A 183     2000   2706   1631      9    -56   -211       C  
ATOM   1410  CG  PRO A 183       9.655  58.472  31.535  1.00 17.12           C  
ANISOU 1410  CG  PRO A 183     2081   2789   1632      8    -41   -169       C  
ATOM   1411  CD  PRO A 183       9.180  57.382  32.467  1.00 16.92           C  
ANISOU 1411  CD  PRO A 183     1996   2736   1694    -69     19   -166       C  
ATOM   1412  N   LEU A 184      12.847  57.134  32.784  1.00 14.21           N  
ANISOU 1412  N   LEU A 184     1858   2437   1103     44    -39   -399       N  
ATOM   1413  CA  LEU A 184      14.247  57.337  33.136  1.00 13.90           C  
ANISOU 1413  CA  LEU A 184     1858   2424    998    -11    -16   -345       C  
ATOM   1414  C   LEU A 184      14.829  56.139  33.881  1.00 14.01           C  
ANISOU 1414  C   LEU A 184     1823   2462   1035    -17     18   -395       C  
ATOM   1415  O   LEU A 184      15.909  56.226  34.468  1.00 13.16           O  
ANISOU 1415  O   LEU A 184     1722   2531    745    -14    -69   -450       O  
ATOM   1416  CB  LEU A 184      14.429  58.627  33.941  1.00 14.57           C  
ANISOU 1416  CB  LEU A 184     1912   2453   1169     16     -8   -382       C  
ATOM   1417  CG  LEU A 184      14.384  59.952  33.159  1.00 13.81           C  
ANISOU 1417  CG  LEU A 184     1941   2381    923     80     46   -282       C  
ATOM   1418  CD1 LEU A 184      14.484  61.111  34.119  1.00 16.42           C  
ANISOU 1418  CD1 LEU A 184     2074   2562   1600    230    137   -253       C  
ATOM   1419  CD2 LEU A 184      15.496  60.068  32.094  1.00 15.16           C  
ANISOU 1419  CD2 LEU A 184     2032   2592   1135    199     -1   -515       C  
ATOM   1420  N   ILE A 185      14.097  55.026  33.863  1.00 13.38           N  
ANISOU 1420  N   ILE A 185     1811   2359    911   -109    -18   -366       N  
ATOM   1421  CA  ILE A 185      14.559  53.800  34.506  1.00 12.91           C  
ANISOU 1421  CA  ILE A 185     1749   2313    842   -120    -34   -292       C  
ATOM   1422  C   ILE A 185      14.734  52.730  33.450  1.00 13.13           C  
ANISOU 1422  C   ILE A 185     1705   2322    962   -144    -26   -192       C  
ATOM   1423  O   ILE A 185      13.812  52.434  32.708  1.00 13.15           O  
ANISOU 1423  O   ILE A 185     1706   2400    890    -94   -164   -197       O  
ATOM   1424  CB  ILE A 185      13.558  53.300  35.591  1.00 13.17           C  
ANISOU 1424  CB  ILE A 185     1790   2325    889    -59    -32   -218       C  
ATOM   1425  CG1 ILE A 185      13.389  54.360  36.684  1.00 11.36           C  
ANISOU 1425  CG1 ILE A 185     1508   2205    604   -224   -270   -525       C  
ATOM   1426  CG2 ILE A 185      14.001  51.937  36.169  1.00 14.57           C  
ANISOU 1426  CG2 ILE A 185     2127   2451    957    -51    -75   -307       C  
ATOM   1427  CD1 ILE A 185      14.694  54.793  37.437  1.00 12.54           C  
ANISOU 1427  CD1 ILE A 185     1427   2486    849   -314   -448   -505       C  
ATOM   1428  N   PHE A 186      15.929  52.153  33.402  1.00 12.93           N  
ANISOU 1428  N   PHE A 186     1530   2363   1018   -139    -84   -123       N  
ATOM   1429  CA  PHE A 186      16.237  51.100  32.445  1.00 12.71           C  
ANISOU 1429  CA  PHE A 186     1437   2308   1082   -148    -24    -48       C  
ATOM   1430  C   PHE A 186      15.843  49.745  33.021  1.00 13.15           C  
ANISOU 1430  C   PHE A 186     1522   2304   1171   -182    -43    -13       C  
ATOM   1431  O   PHE A 186      16.454  49.248  33.963  1.00 13.42           O  
ANISOU 1431  O   PHE A 186     1539   2279   1281   -265    -79     35       O  
ATOM   1432  CB  PHE A 186      17.719  51.137  32.054  1.00 13.39           C  
ANISOU 1432  CB  PHE A 186     1528   2439   1120   -178    -22     16       C  
ATOM   1433  CG  PHE A 186      18.021  50.397  30.771  1.00 11.24           C  
ANISOU 1433  CG  PHE A 186     1227   2302    741    -22     70    -72       C  
ATOM   1434  CD1 PHE A 186      18.163  49.011  30.766  1.00 12.78           C  
ANISOU 1434  CD1 PHE A 186     1339   2629    888    -67      8    168       C  
ATOM   1435  CD2 PHE A 186      18.140  51.096  29.566  1.00 12.71           C  
ANISOU 1435  CD2 PHE A 186     1411   2425    992    -69   -108     68       C  
ATOM   1436  CE1 PHE A 186      18.442  48.310  29.569  1.00 12.55           C  
ANISOU 1436  CE1 PHE A 186     1452   2445    871    206     82     53       C  
ATOM   1437  CE2 PHE A 186      18.414  50.428  28.362  1.00 12.29           C  
ANISOU 1437  CE2 PHE A 186     1514   2400    752    107   -111    176       C  
ATOM   1438  CZ  PHE A 186      18.564  49.025  28.355  1.00 13.03           C  
ANISOU 1438  CZ  PHE A 186     1590   2432    927     29   -113    171       C  
ATOM   1439  N   ASP A 187      14.779  49.166  32.479  1.00 13.76           N  
ANISOU 1439  N   ASP A 187     1748   2271   1206   -212    -36     13       N  
ATOM   1440  CA  ASP A 187      14.331  47.849  32.925  1.00 14.15           C  
ANISOU 1440  CA  ASP A 187     1844   2243   1288   -218     30    -99       C  
ATOM   1441  C   ASP A 187      13.650  47.136  31.770  1.00 14.04           C  
ANISOU 1441  C   ASP A 187     1907   2160   1265   -184     20    -67       C  
ATOM   1442  O   ASP A 187      13.691  47.636  30.639  1.00 13.46           O  
ANISOU 1442  O   ASP A 187     2030   1969   1116   -270     69   -112       O  
ATOM   1443  CB  ASP A 187      13.441  47.956  34.174  1.00 15.14           C  
ANISOU 1443  CB  ASP A 187     1938   2385   1427   -206     18    -86       C  
ATOM   1444  CG  ASP A 187      12.169  48.770  33.951  1.00 17.39           C  
ANISOU 1444  CG  ASP A 187     2136   2899   1570   -143    186   -300       C  
ATOM   1445  OD1 ASP A 187      11.703  48.966  32.795  1.00 16.63           O  
ANISOU 1445  OD1 ASP A 187     1981   2640   1696   -110     57   -265       O  
ATOM   1446  OD2 ASP A 187      11.611  49.208  34.983  1.00 23.40           O  
ANISOU 1446  OD2 ASP A 187     2921   3843   2127   -247    171   -627       O  
ATOM   1447  N   ASN A 188      13.028  45.991  32.042  1.00 13.49           N  
ANISOU 1447  N   ASN A 188     1912   2043   1167   -184     76     16       N  
ATOM   1448  CA  ASN A 188      12.355  45.233  30.980  1.00 14.40           C  
ANISOU 1448  CA  ASN A 188     2100   2078   1290   -214    129     53       C  
ATOM   1449  C   ASN A 188      10.895  45.646  30.721  1.00 14.67           C  
ANISOU 1449  C   ASN A 188     2114   2199   1258   -208    115     70       C  
ATOM   1450  O   ASN A 188      10.164  44.917  30.043  1.00 14.95           O  
ANISOU 1450  O   ASN A 188     2119   2147   1413   -171    119     40       O  
ATOM   1451  CB  ASN A 188      12.428  43.729  31.267  1.00 14.86           C  
ANISOU 1451  CB  ASN A 188     2243   2071   1329   -229    133    145       C  
ATOM   1452  CG  ASN A 188      11.521  43.314  32.421  1.00 14.73           C  
ANISOU 1452  CG  ASN A 188     2391   1944   1262   -415    275    205       C  
ATOM   1453  OD1 ASN A 188      11.120  44.141  33.241  1.00 16.46           O  
ANISOU 1453  OD1 ASN A 188     2677   1933   1642   -751    540    391       O  
ATOM   1454  ND2 ASN A 188      11.183  42.035  32.477  1.00 15.96           N  
ANISOU 1454  ND2 ASN A 188     2705   1980   1379   -717    314    377       N  
ATOM   1455  N   SER A 189      10.490  46.809  31.242  1.00 14.73           N  
ANISOU 1455  N   SER A 189     2100   2287   1207   -169    155     38       N  
ATOM   1456  CA  SER A 189       9.100  47.283  31.168  1.00 16.00           C  
ANISOU 1456  CA  SER A 189     2241   2487   1349   -144    115     11       C  
ATOM   1457  C   SER A 189       8.603  47.488  29.739  1.00 15.34           C  
ANISOU 1457  C   SER A 189     2104   2443   1278   -161    104    -90       C  
ATOM   1458  O   SER A 189       7.403  47.348  29.466  1.00 15.65           O  
ANISOU 1458  O   SER A 189     2116   2463   1365   -122    165    -89       O  
ATOM   1459  CB  SER A 189       8.915  48.592  31.944  1.00 16.17           C  
ANISOU 1459  CB  SER A 189     2238   2672   1233   -119     83    -59       C  
ATOM   1460  OG  SER A 189       8.978  48.364  33.346  1.00 20.49           O  
ANISOU 1460  OG  SER A 189     2902   3062   1818   -110    275    177       O  
ATOM   1461  N   TYR A 190       9.522  47.837  28.840  1.00 15.13           N  
ANISOU 1461  N   TYR A 190     2031   2416   1299   -206     59    -79       N  
ATOM   1462  CA  TYR A 190       9.204  47.954  27.419  1.00 15.07           C  
ANISOU 1462  CA  TYR A 190     1977   2442   1306   -242    135   -161       C  
ATOM   1463  C   TYR A 190       8.486  46.701  26.903  1.00 15.19           C  
ANISOU 1463  C   TYR A 190     1952   2411   1405   -212    154   -167       C  
ATOM   1464  O   TYR A 190       7.451  46.801  26.232  1.00 15.79           O  
ANISOU 1464  O   TYR A 190     1982   2440   1575   -212     68   -181       O  
ATOM   1465  CB  TYR A 190      10.481  48.259  26.614  1.00 14.35           C  
ANISOU 1465  CB  TYR A 190     1895   2326   1229   -267     51   -155       C  
ATOM   1466  CG  TYR A 190      10.331  48.095  25.112  1.00 13.69           C  
ANISOU 1466  CG  TYR A 190     1766   2275   1158   -255     11   -200       C  
ATOM   1467  CD1 TYR A 190       9.747  49.098  24.331  1.00 13.48           C  
ANISOU 1467  CD1 TYR A 190     1777   2222   1121   -227   -159   -104       C  
ATOM   1468  CD2 TYR A 190      10.807  46.958  24.474  1.00 12.86           C  
ANISOU 1468  CD2 TYR A 190     1686   2020   1177   -408   -171   -317       C  
ATOM   1469  CE1 TYR A 190       9.622  48.952  22.944  1.00 12.86           C  
ANISOU 1469  CE1 TYR A 190     1862   2058    965    -74    -34   -283       C  
ATOM   1470  CE2 TYR A 190      10.705  46.806  23.092  1.00 11.62           C  
ANISOU 1470  CE2 TYR A 190     1568   2023    822   -228    -62   -236       C  
ATOM   1471  CZ  TYR A 190      10.104  47.801  22.333  1.00 12.74           C  
ANISOU 1471  CZ  TYR A 190     1674   2061   1104   -269    -33   -209       C  
ATOM   1472  OH  TYR A 190       9.996  47.639  20.968  1.00 13.01           O  
ANISOU 1472  OH  TYR A 190     1708   1994   1241   -161   -290   -356       O  
ATOM   1473  N   PHE A 191       9.020  45.525  27.234  1.00 15.43           N  
ANISOU 1473  N   PHE A 191     1935   2434   1491   -258    201   -188       N  
ATOM   1474  CA  PHE A 191       8.448  44.254  26.768  1.00 15.60           C  
ANISOU 1474  CA  PHE A 191     1937   2407   1583   -225    229   -228       C  
ATOM   1475  C   PHE A 191       7.160  43.905  27.496  1.00 16.71           C  
ANISOU 1475  C   PHE A 191     2055   2607   1686   -222    241   -246       C  
ATOM   1476  O   PHE A 191       6.233  43.379  26.893  1.00 16.73           O  
ANISOU 1476  O   PHE A 191     2073   2704   1578   -260    262   -366       O  
ATOM   1477  CB  PHE A 191       9.483  43.136  26.877  1.00 14.99           C  
ANISOU 1477  CB  PHE A 191     1868   2227   1600   -229    128   -215       C  
ATOM   1478  CG  PHE A 191      10.779  43.472  26.196  1.00 13.47           C  
ANISOU 1478  CG  PHE A 191     1816   1867   1434   -251    104    -74       C  
ATOM   1479  CD1 PHE A 191      10.897  43.368  24.806  1.00 13.11           C  
ANISOU 1479  CD1 PHE A 191     1763   1746   1469    -17    -89    -80       C  
ATOM   1480  CD2 PHE A 191      11.867  43.945  26.938  1.00 12.81           C  
ANISOU 1480  CD2 PHE A 191     1623   1801   1442   -234   -129    220       C  
ATOM   1481  CE1 PHE A 191      12.088  43.703  24.162  1.00 12.34           C  
ANISOU 1481  CE1 PHE A 191     1667   1752   1267    -67     46   -219       C  
ATOM   1482  CE2 PHE A 191      13.065  44.293  26.303  1.00 11.28           C  
ANISOU 1482  CE2 PHE A 191     1464   1726   1092   -360    109    -41       C  
ATOM   1483  CZ  PHE A 191      13.182  44.168  24.915  1.00 12.15           C  
ANISOU 1483  CZ  PHE A 191     1789   1547   1280   -274    -61   -217       C  
ATOM   1484  N   THR A 192       7.105  44.234  28.784  1.00 17.55           N  
ANISOU 1484  N   THR A 192     2131   2871   1665   -206    338   -237       N  
ATOM   1485  CA  THR A 192       5.887  44.079  29.578  1.00 19.53           C  
ANISOU 1485  CA  THR A 192     2283   3218   1918   -204    280   -240       C  
ATOM   1486  C   THR A 192       4.738  44.892  28.972  1.00 19.74           C  
ANISOU 1486  C   THR A 192     2267   3308   1923   -171    223   -274       C  
ATOM   1487  O   THR A 192       3.632  44.373  28.799  1.00 19.06           O  
ANISOU 1487  O   THR A 192     2065   3234   1944   -285    208   -184       O  
ATOM   1488  CB  THR A 192       6.123  44.515  31.039  1.00 18.98           C  
ANISOU 1488  CB  THR A 192     2237   3258   1714   -125    368   -140       C  
ATOM   1489  OG1 THR A 192       7.214  43.758  31.577  1.00 22.57           O  
ANISOU 1489  OG1 THR A 192     2755   3978   1841   -279    439   -195       O  
ATOM   1490  CG2 THR A 192       4.863  44.269  31.882  1.00 22.35           C  
ANISOU 1490  CG2 THR A 192     2658   3571   2260   -184    307    -82       C  
ATOM   1491  N   GLU A 193       5.016  46.154  28.644  1.00 20.21           N  
ANISOU 1491  N   GLU A 193     2253   3376   2047   -166    164   -360       N  
ATOM   1492  CA  GLU A 193       4.020  47.052  28.067  1.00 21.16           C  
ANISOU 1492  CA  GLU A 193     2286   3594   2159    -16    165   -463       C  
ATOM   1493  C   GLU A 193       3.601  46.574  26.679  1.00 22.45           C  
ANISOU 1493  C   GLU A 193     2367   3753   2410     26    130   -517       C  
ATOM   1494  O   GLU A 193       2.406  46.537  26.351  1.00 22.38           O  
ANISOU 1494  O   GLU A 193     2309   3771   2421    115     70   -512       O  
ATOM   1495  CB  GLU A 193       4.556  48.493  27.994  1.00 20.81           C  
ANISOU 1495  CB  GLU A 193     2189   3599   2118    -70    191   -468       C  
ATOM   1496  CG  GLU A 193       4.825  49.187  29.358  1.00 20.62           C  
ANISOU 1496  CG  GLU A 193     2224   3763   1845    -44    268   -418       C  
ATOM   1497  CD  GLU A 193       3.655  49.107  30.359  1.00 23.17           C  
ANISOU 1497  CD  GLU A 193     2643   4183   1975   -186    235   -251       C  
ATOM   1498  OE1 GLU A 193       2.487  48.887  29.957  1.00 23.65           O  
ANISOU 1498  OE1 GLU A 193     2436   4455   2094   -343    506     66       O  
ATOM   1499  OE2 GLU A 193       3.914  49.280  31.570  1.00 22.76           O  
ANISOU 1499  OE2 GLU A 193     2894   4189   1562   -165    303    -63       O  
ATOM   1500  N   LEU A 194       4.591  46.178  25.882  1.00 23.59           N  
ANISOU 1500  N   LEU A 194     2474   3911   2576    110     98   -609       N  
ATOM   1501  CA  LEU A 194       4.351  45.674  24.529  1.00 24.83           C  
ANISOU 1501  CA  LEU A 194     2610   4026   2795    153     75   -672       C  
ATOM   1502  C   LEU A 194       3.352  44.508  24.556  1.00 25.74           C  
ANISOU 1502  C   LEU A 194     2720   4107   2951    163     24   -749       C  
ATOM   1503  O   LEU A 194       2.423  44.465  23.741  1.00 26.77           O  
ANISOU 1503  O   LEU A 194     2790   4281   3100    204    -47   -743       O  
ATOM   1504  CB  LEU A 194       5.683  45.286  23.865  1.00 24.71           C  
ANISOU 1504  CB  LEU A 194     2655   4009   2724    190     62   -675       C  
ATOM   1505  CG  LEU A 194       5.786  45.164  22.341  1.00 25.38           C  
ANISOU 1505  CG  LEU A 194     2745   4000   2899    171    163   -616       C  
ATOM   1506  CD1 LEU A 194       5.236  46.387  21.609  1.00 25.64           C  
ANISOU 1506  CD1 LEU A 194     2815   4043   2883    313    172   -681       C  
ATOM   1507  CD2 LEU A 194       7.237  44.886  21.939  1.00 24.27           C  
ANISOU 1507  CD2 LEU A 194     2539   3911   2771    265    156   -602       C  
ATOM   1508  N   LEU A 195       3.513  43.613  25.531  1.00 26.38           N  
ANISOU 1508  N   LEU A 195     2762   4164   3096    140     23   -790       N  
ATOM   1509  CA  LEU A 195       2.661  42.434  25.696  1.00 27.47           C  
ANISOU 1509  CA  LEU A 195     2875   4240   3321    131     83   -787       C  
ATOM   1510  C   LEU A 195       1.232  42.725  26.193  1.00 28.61           C  
ANISOU 1510  C   LEU A 195     3008   4369   3490     80     68   -787       C  
ATOM   1511  O   LEU A 195       0.266  42.158  25.685  1.00 29.29           O  
ANISOU 1511  O   LEU A 195     3070   4421   3637     74    148   -818       O  
ATOM   1512  CB  LEU A 195       3.351  41.412  26.615  1.00 27.40           C  
ANISOU 1512  CB  LEU A 195     2878   4249   3281     69     79   -812       C  
ATOM   1513  CG  LEU A 195       4.563  40.689  26.008  1.00 26.98           C  
ANISOU 1513  CG  LEU A 195     2870   4081   3297    106    -19   -786       C  
ATOM   1514  CD1 LEU A 195       5.191  39.735  27.008  1.00 27.64           C  
ANISOU 1514  CD1 LEU A 195     3047   4205   3249    -25    -14   -780       C  
ATOM   1515  CD2 LEU A 195       4.157  39.933  24.755  1.00 26.70           C  
ANISOU 1515  CD2 LEU A 195     3037   4113   2994     11    147   -767       C  
ATOM   1516  N   SER A 196       1.105  43.631  27.155  1.00 29.08           N  
ANISOU 1516  N   SER A 196     3102   4419   3527    106    121   -773       N  
ATOM   1517  CA  SER A 196      -0.162  43.901  27.827  1.00 29.91           C  
ANISOU 1517  CA  SER A 196     3218   4492   3652     89     84   -729       C  
ATOM   1518  C   SER A 196      -1.194  44.607  26.945  1.00 30.79           C  
ANISOU 1518  C   SER A 196     3355   4559   3782     92     64   -689       C  
ATOM   1519  O   SER A 196      -2.359  44.735  27.331  1.00 31.01           O  
ANISOU 1519  O   SER A 196     3394   4599   3789     49     33   -690       O  
ATOM   1520  CB  SER A 196       0.100  44.762  29.057  1.00 29.76           C  
ANISOU 1520  CB  SER A 196     3231   4476   3599     96    127   -758       C  
ATOM   1521  OG  SER A 196       0.491  46.061  28.661  1.00 28.84           O  
ANISOU 1521  OG  SER A 196     3092   4463   3401     43    233   -785       O  
ATOM   1522  N   GLY A 197      -0.752  45.081  25.783  1.00 32.04           N  
ANISOU 1522  N   GLY A 197     3520   4700   3954    112     44   -625       N  
ATOM   1523  CA  GLY A 197      -1.587  45.876  24.883  1.00 33.63           C  
ANISOU 1523  CA  GLY A 197     3746   4876   4157     99     22   -553       C  
ATOM   1524  C   GLY A 197      -1.333  47.367  25.000  1.00 34.66           C  
ANISOU 1524  C   GLY A 197     3899   4973   4296     81      0   -506       C  
ATOM   1525  O   GLY A 197      -0.414  47.798  25.703  1.00 34.74           O  
ANISOU 1525  O   GLY A 197     3841   5068   4290     92     23   -494       O  
ATOM   1526  N   GLU A 198      -2.154  48.157  24.309  1.00 35.73           N  
ANISOU 1526  N   GLU A 198     4062   5075   4439     61    -33   -472       N  
ATOM   1527  CA  GLU A 198      -2.073  49.615  24.402  1.00 36.51           C  
ANISOU 1527  CA  GLU A 198     4198   5139   4532     46    -37   -447       C  
ATOM   1528  C   GLU A 198      -2.691  50.098  25.715  1.00 36.48           C  
ANISOU 1528  C   GLU A 198     4175   5095   4588     45    -13   -416       C  
ATOM   1529  O   GLU A 198      -3.814  49.740  26.074  1.00 37.08           O  
ANISOU 1529  O   GLU A 198     4252   5156   4678     55      1   -414       O  
ATOM   1530  CB  GLU A 198      -2.726  50.307  23.194  1.00 36.88           C  
ANISOU 1530  CB  GLU A 198     4243   5218   4549     48    -32   -455       C  
ATOM   1531  CG  GLU A 198      -2.091  49.977  21.836  1.00 38.62           C  
ANISOU 1531  CG  GLU A 198     4566   5497   4609      0   -115   -510       C  
ATOM   1532  CD  GLU A 198      -1.090  51.026  21.343  1.00 40.56           C  
ANISOU 1532  CD  GLU A 198     4840   5891   4679    -69   -224   -658       C  
ATOM   1533  OE1 GLU A 198      -1.044  51.274  20.116  1.00 41.94           O  
ANISOU 1533  OE1 GLU A 198     5049   6082   4801    -64   -273   -653       O  
ATOM   1534  OE2 GLU A 198      -0.348  51.604  22.163  1.00 41.65           O  
ANISOU 1534  OE2 GLU A 198     5100   6041   4683    -37   -227   -882       O  
ATOM   1535  N   LYS A 199      -1.916  50.884  26.446  1.00 36.21           N  
ANISOU 1535  N   LYS A 199     4170   5006   4581     47      2   -387       N  
ATOM   1536  CA  LYS A 199      -2.365  51.517  27.673  1.00 35.66           C  
ANISOU 1536  CA  LYS A 199     4110   4886   4552     53     34   -314       C  
ATOM   1537  C   LYS A 199      -2.294  53.004  27.380  1.00 34.83           C  
ANISOU 1537  C   LYS A 199     3999   4749   4486     83     49   -283       C  
ATOM   1538  O   LYS A 199      -1.324  53.466  26.766  1.00 34.64           O  
ANISOU 1538  O   LYS A 199     3891   4762   4506     54    107   -314       O  
ATOM   1539  CB  LYS A 199      -1.429  51.137  28.822  1.00 35.72           C  
ANISOU 1539  CB  LYS A 199     4142   4907   4523     42     22   -319       C  
ATOM   1540  CG  LYS A 199      -1.706  51.809  30.157  1.00 36.30           C  
ANISOU 1540  CG  LYS A 199     4280   4908   4603      9     11   -290       C  
ATOM   1541  CD  LYS A 199      -0.664  51.371  31.195  1.00 36.97           C  
ANISOU 1541  CD  LYS A 199     4390   4975   4682    -12    -55   -311       C  
ATOM   1542  CE  LYS A 199      -0.856  52.074  32.526  1.00 38.33           C  
ANISOU 1542  CE  LYS A 199     4715   5059   4787    -70   -120   -260       C  
ATOM   1543  NZ  LYS A 199      -0.633  53.546  32.417  1.00 39.33           N  
ANISOU 1543  NZ  LYS A 199     4872   5177   4894   -172   -164   -195       N  
ATOM   1544  N   GLU A 200      -3.323  53.750  27.787  1.00 33.94           N  
ANISOU 1544  N   GLU A 200     3860   4633   4402    109     66   -220       N  
ATOM   1545  C   GLU A 200      -2.138  55.876  28.150  1.00 32.43           C  
ANISOU 1545  C   GLU A 200     3673   4466   4181    148     65   -151       C  
ATOM   1546  O   GLU A 200      -1.677  55.505  29.238  1.00 32.38           O  
ANISOU 1546  O   GLU A 200     3651   4489   4159    150     96   -162       O  
ATOM   1547  CA AGLU A 200      -3.347  55.183  27.516  0.50 33.11           C  
ANISOU 1547  CA AGLU A 200     3764   4519   4297    133     62   -172       C  
ATOM   1548  CB AGLU A 200      -4.672  55.823  27.955  0.50 33.33           C  
ANISOU 1548  CB AGLU A 200     3787   4524   4350    136     60   -161       C  
ATOM   1549  CG AGLU A 200      -4.885  57.257  27.456  0.50 33.39           C  
ANISOU 1549  CG AGLU A 200     3780   4462   4444    129     50   -139       C  
ATOM   1550  CD AGLU A 200      -4.606  57.433  25.971  0.50 34.12           C  
ANISOU 1550  CD AGLU A 200     3858   4470   4633     81    -45   -106       C  
ATOM   1551  OE1AGLU A 200      -3.588  58.075  25.628  0.50 33.96           O  
ANISOU 1551  OE1AGLU A 200     3886   4364   4650     31    -63    -53       O  
ATOM   1552  OE2AGLU A 200      -5.396  56.923  25.147  0.50 34.48           O  
ANISOU 1552  OE2AGLU A 200     3810   4507   4782     56    -73   -113       O  
ATOM   1553  CA BGLU A 200      -3.374  55.200  27.567  0.50 33.29           C  
ANISOU 1553  CA BGLU A 200     3792   4544   4309    129     66   -166       C  
ATOM   1554  CB BGLU A 200      -4.639  55.814  28.189  0.50 33.59           C  
ANISOU 1554  CB BGLU A 200     3832   4560   4369    132     69   -154       C  
ATOM   1555  CG BGLU A 200      -5.917  54.985  28.048  0.50 34.45           C  
ANISOU 1555  CG BGLU A 200     3964   4618   4507    106     73    -98       C  
ATOM   1556  CD BGLU A 200      -6.184  54.526  26.626  0.50 36.08           C  
ANISOU 1556  CD BGLU A 200     4262   4711   4735     76     75      0       C  
ATOM   1557  OE1BGLU A 200      -6.383  53.309  26.429  0.50 37.01           O  
ANISOU 1557  OE1BGLU A 200     4429   4741   4891     24     86     21       O  
ATOM   1558  OE2BGLU A 200      -6.188  55.373  25.706  0.50 37.19           O  
ANISOU 1558  OE2BGLU A 200     4413   4819   4898     21    142     70       O  
ATOM   1559  N   GLY A 201      -1.609  56.862  27.434  1.00 30.90           N  
ANISOU 1559  N   GLY A 201     3481   4331   3929    176     49   -119       N  
ATOM   1560  CA  GLY A 201      -0.440  57.595  27.883  1.00 28.84           C  
ANISOU 1560  CA  GLY A 201     3282   4119   3554    195     63   -109       C  
ATOM   1561  C   GLY A 201       0.878  56.961  27.470  1.00 27.01           C  
ANISOU 1561  C   GLY A 201     3047   3974   3241    206     38   -115       C  
ATOM   1562  O   GLY A 201       1.925  57.599  27.601  1.00 27.66           O  
ANISOU 1562  O   GLY A 201     3148   4026   3333    273     76   -123       O  
ATOM   1563  N   LEU A 202       0.832  55.717  26.980  1.00 25.08           N  
ANISOU 1563  N   LEU A 202     2873   3856   2800    193     -7    -91       N  
ATOM   1564  CA  LEU A 202       2.048  54.997  26.565  1.00 22.93           C  
ANISOU 1564  CA  LEU A 202     2707   3643   2362    140    -13   -115       C  
ATOM   1565  C   LEU A 202       2.117  54.735  25.058  1.00 22.21           C  
ANISOU 1565  C   LEU A 202     2601   3546   2290    121    -52    -95       C  
ATOM   1566  O   LEU A 202       1.108  54.450  24.410  1.00 22.26           O  
ANISOU 1566  O   LEU A 202     2570   3692   2195     81    -72   -115       O  
ATOM   1567  CB  LEU A 202       2.228  53.685  27.344  1.00 22.53           C  
ANISOU 1567  CB  LEU A 202     2643   3644   2271    131    -49   -152       C  
ATOM   1568  CG  LEU A 202       2.346  53.793  28.869  1.00 21.40           C  
ANISOU 1568  CG  LEU A 202     2700   3587   1843    103    -55   -107       C  
ATOM   1569  CD1 LEU A 202       2.613  52.431  29.473  1.00 21.38           C  
ANISOU 1569  CD1 LEU A 202     2824   3671   1626     53    -69   -278       C  
ATOM   1570  CD2 LEU A 202       3.443  54.789  29.268  1.00 20.55           C  
ANISOU 1570  CD2 LEU A 202     2791   3703   1313    -31     63   -109       C  
ATOM   1571  N   LEU A 203       3.329  54.831  24.525  1.00 20.06           N  
ANISOU 1571  N   LEU A 203     2369   3214   2036    113    -29    -76       N  
ATOM   1572  CA  LEU A 203       3.575  54.711  23.091  1.00 18.53           C  
ANISOU 1572  CA  LEU A 203     2244   2912   1884     90    -83    -28       C  
ATOM   1573  C   LEU A 203       3.969  53.297  22.665  1.00 18.15           C  
ANISOU 1573  C   LEU A 203     2211   2828   1857     62   -116    -37       C  
ATOM   1574  O   LEU A 203       4.745  52.617  23.344  1.00 17.34           O  
ANISOU 1574  O   LEU A 203     2184   2780   1624    -17   -167     32       O  
ATOM   1575  CB  LEU A 203       4.675  55.694  22.679  1.00 18.18           C  
ANISOU 1575  CB  LEU A 203     2194   2864   1849     95    -56     -3       C  
ATOM   1576  CG  LEU A 203       5.143  55.676  21.216  1.00 17.64           C  
ANISOU 1576  CG  LEU A 203     2189   2746   1766    154    -87     18       C  
ATOM   1577  CD1 LEU A 203       4.053  56.194  20.271  1.00 17.86           C  
ANISOU 1577  CD1 LEU A 203     2099   2759   1927     33   -157    -54       C  
ATOM   1578  CD2 LEU A 203       6.427  56.462  21.067  1.00 16.31           C  
ANISOU 1578  CD2 LEU A 203     1958   2536   1700    230    -33     36       C  
ATOM   1579  N   GLN A 204       3.439  52.876  21.516  1.00 17.82           N  
ANISOU 1579  N   GLN A 204     2192   2678   1900     60   -212    -66       N  
ATOM   1580  CA  GLN A 204       3.967  51.734  20.780  1.00 18.06           C  
ANISOU 1580  CA  GLN A 204     2260   2654   1946     -3   -265    -96       C  
ATOM   1581  C   GLN A 204       4.061  52.167  19.325  1.00 17.46           C  
ANISOU 1581  C   GLN A 204     2176   2509   1948     29   -332   -175       C  
ATOM   1582  O   GLN A 204       3.052  52.536  18.723  1.00 18.15           O  
ANISOU 1582  O   GLN A 204     2122   2699   2072     29   -316   -170       O  
ATOM   1583  CB  GLN A 204       3.052  50.511  20.912  1.00 18.49           C  
ANISOU 1583  CB  GLN A 204     2381   2659   1985     25   -240    -51       C  
ATOM   1584  CG  GLN A 204       2.941  49.937  22.335  1.00 19.37           C  
ANISOU 1584  CG  GLN A 204     2513   2725   2119      7   -190     23       C  
ATOM   1585  CD  GLN A 204       2.154  48.636  22.382  1.00 20.18           C  
ANISOU 1585  CD  GLN A 204     2601   2918   2146   -119   -217    -79       C  
ATOM   1586  OE1 GLN A 204       1.906  48.003  21.348  1.00 21.33           O  
ANISOU 1586  OE1 GLN A 204     2698   3070   2334   -211   -310   -199       O  
ATOM   1587  NE2 GLN A 204       1.765  48.223  23.589  1.00 20.37           N  
ANISOU 1587  NE2 GLN A 204     2797   2889   2052   -178   -132     58       N  
ATOM   1588  N   LEU A 205       5.275  52.175  18.783  1.00 16.45           N  
ANISOU 1588  N   LEU A 205     2009   2336   1904     37   -384   -251       N  
ATOM   1589  CA  LEU A 205       5.486  52.402  17.347  1.00 15.93           C  
ANISOU 1589  CA  LEU A 205     1924   2244   1882     91   -471   -300       C  
ATOM   1590  C   LEU A 205       5.100  51.136  16.580  1.00 16.04           C  
ANISOU 1590  C   LEU A 205     1878   2305   1911    105   -455   -332       C  
ATOM   1591  O   LEU A 205       5.156  50.040  17.140  1.00 15.54           O  
ANISOU 1591  O   LEU A 205     1840   2185   1878    209   -450   -282       O  
ATOM   1592  CB  LEU A 205       6.956  52.709  17.051  1.00 15.52           C  
ANISOU 1592  CB  LEU A 205     1824   2178   1892    144   -537   -273       C  
ATOM   1593  CG  LEU A 205       7.605  53.861  17.821  1.00 13.77           C  
ANISOU 1593  CG  LEU A 205     1691   1924   1613    150   -639   -399       C  
ATOM   1594  CD1 LEU A 205       9.089  53.878  17.583  1.00 14.11           C  
ANISOU 1594  CD1 LEU A 205     1723   2217   1418     69   -736   -484       C  
ATOM   1595  CD2 LEU A 205       6.963  55.219  17.462  1.00 14.49           C  
ANISOU 1595  CD2 LEU A 205     1767   2191   1547    315   -705   -345       C  
ATOM   1596  N   PRO A 206       4.705  51.278  15.300  1.00 15.78           N  
ANISOU 1596  N   PRO A 206     1845   2308   1843    127   -503   -364       N  
ATOM   1597  CA  PRO A 206       4.513  50.064  14.482  1.00 15.77           C  
ANISOU 1597  CA  PRO A 206     1866   2291   1835    177   -507   -372       C  
ATOM   1598  C   PRO A 206       5.745  49.143  14.489  1.00 15.52           C  
ANISOU 1598  C   PRO A 206     1892   2283   1722    187   -534   -347       C  
ATOM   1599  O   PRO A 206       5.596  47.919  14.515  1.00 15.56           O  
ANISOU 1599  O   PRO A 206     1848   2301   1762    144   -639   -371       O  
ATOM   1600  CB  PRO A 206       4.256  50.625  13.080  1.00 15.57           C  
ANISOU 1600  CB  PRO A 206     1885   2205   1826    199   -506   -355       C  
ATOM   1601  CG  PRO A 206       3.647  51.980  13.333  1.00 17.22           C  
ANISOU 1601  CG  PRO A 206     2130   2416   1995    170   -485   -418       C  
ATOM   1602  CD  PRO A 206       4.373  52.509  14.551  1.00 15.76           C  
ANISOU 1602  CD  PRO A 206     1833   2326   1826    124   -505   -412       C  
ATOM   1603  N   SER A 207       6.941  49.733  14.508  1.00 15.01           N  
ANISOU 1603  N   SER A 207     1811   2328   1563    259   -523   -305       N  
ATOM   1604  CA  SER A 207       8.187  48.960  14.594  1.00 14.73           C  
ANISOU 1604  CA  SER A 207     1868   2270   1457    274   -436   -284       C  
ATOM   1605  C   SER A 207       8.311  48.138  15.893  1.00 14.59           C  
ANISOU 1605  C   SER A 207     1829   2266   1445    332   -424   -296       C  
ATOM   1606  O   SER A 207       8.884  47.041  15.884  1.00 14.35           O  
ANISOU 1606  O   SER A 207     1982   2200   1270    349   -296   -364       O  
ATOM   1607  CB  SER A 207       9.401  49.870  14.368  1.00 14.34           C  
ANISOU 1607  CB  SER A 207     1834   2177   1436    285   -524   -278       C  
ATOM   1608  OG  SER A 207       9.423  50.950  15.292  1.00 14.51           O  
ANISOU 1608  OG  SER A 207     2082   2158   1273    167   -501   -238       O  
ATOM   1609  N   ASP A 208       7.750  48.653  16.993  1.00 14.63           N  
ANISOU 1609  N   ASP A 208     1773   2266   1520    304   -355   -295       N  
ATOM   1610  CA  ASP A 208       7.707  47.928  18.265  1.00 15.00           C  
ANISOU 1610  CA  ASP A 208     1740   2313   1646    257   -310   -330       C  
ATOM   1611  C   ASP A 208       6.714  46.767  18.129  1.00 15.30           C  
ANISOU 1611  C   ASP A 208     1695   2366   1753    240   -314   -365       C  
ATOM   1612  O   ASP A 208       7.013  45.617  18.501  1.00 14.57           O  
ANISOU 1612  O   ASP A 208     1498   2327   1710    258   -353   -404       O  
ATOM   1613  CB  ASP A 208       7.258  48.832  19.428  1.00 14.94           C  
ANISOU 1613  CB  ASP A 208     1794   2304   1577    172   -324   -357       C  
ATOM   1614  CG  ASP A 208       8.194  50.017  19.683  1.00 14.94           C  
ANISOU 1614  CG  ASP A 208     1890   2263   1523    183   -182    -98       C  
ATOM   1615  OD1 ASP A 208       9.436  49.843  19.789  1.00 13.07           O  
ANISOU 1615  OD1 ASP A 208     1658   1871   1436   -254   -288      0       O  
ATOM   1616  OD2 ASP A 208       7.672  51.137  19.807  1.00 15.40           O  
ANISOU 1616  OD2 ASP A 208     2391   1906   1553    281   -295    142       O  
ATOM   1617  N   LYS A 209       5.531  47.080  17.602  1.00 15.96           N  
ANISOU 1617  N   LYS A 209     1742   2427   1894    242   -362   -361       N  
ATOM   1618  CA  LYS A 209       4.455  46.089  17.451  1.00 17.36           C  
ANISOU 1618  CA  LYS A 209     1841   2563   2190    252   -424   -356       C  
ATOM   1619  C   LYS A 209       4.850  44.930  16.548  1.00 17.50           C  
ANISOU 1619  C   LYS A 209     1898   2467   2281    204   -467   -336       C  
ATOM   1620  O   LYS A 209       4.358  43.808  16.712  1.00 18.69           O  
ANISOU 1620  O   LYS A 209     2058   2634   2410    153   -423   -322       O  
ATOM   1621  CB  LYS A 209       3.181  46.744  16.914  1.00 17.81           C  
ANISOU 1621  CB  LYS A 209     1895   2596   2275    337   -434   -322       C  
ATOM   1622  CG  LYS A 209       2.523  47.711  17.865  1.00 19.16           C  
ANISOU 1622  CG  LYS A 209     1940   2876   2464    331   -412   -372       C  
ATOM   1623  CD  LYS A 209       1.247  48.267  17.233  1.00 22.12           C  
ANISOU 1623  CD  LYS A 209     2177   3172   3056    581   -270   -258       C  
ATOM   1624  CE  LYS A 209       0.769  49.510  17.945  1.00 24.59           C  
ANISOU 1624  CE  LYS A 209     2418   3577   3346    616   -303   -244       C  
ATOM   1625  NZ  LYS A 209      -0.656  49.798  17.575  1.00 26.08           N  
ANISOU 1625  NZ  LYS A 209     2672   3738   3499    709   -267    -89       N  
ATOM   1626  N   ALA A 210       5.748  45.210  15.606  1.00 17.61           N  
ANISOU 1626  N   ALA A 210     1992   2413   2285    187   -499   -313       N  
ATOM   1627  CA  ALA A 210       6.245  44.217  14.651  1.00 17.74           C  
ANISOU 1627  CA  ALA A 210     1982   2369   2388    176   -457   -284       C  
ATOM   1628  C   ALA A 210       6.960  43.051  15.353  1.00 17.98           C  
ANISOU 1628  C   ALA A 210     2028   2336   2467    125   -435   -312       C  
ATOM   1629  O   ALA A 210       6.957  41.918  14.858  1.00 18.82           O  
ANISOU 1629  O   ALA A 210     2229   2447   2475    123   -466   -331       O  
ATOM   1630  CB  ALA A 210       7.164  44.882  13.655  1.00 17.87           C  
ANISOU 1630  CB  ALA A 210     2070   2356   2364    175   -482   -286       C  
ATOM   1631  N   LEU A 211       7.556  43.329  16.510  1.00 17.25           N  
ANISOU 1631  N   LEU A 211     1852   2269   2430     68   -408   -311       N  
ATOM   1632  CA  LEU A 211       8.219  42.286  17.299  1.00 17.23           C  
ANISOU 1632  CA  LEU A 211     1835   2194   2517     11   -368   -351       C  
ATOM   1633  C   LEU A 211       7.238  41.229  17.798  1.00 17.59           C  
ANISOU 1633  C   LEU A 211     1895   2210   2576      2   -346   -361       C  
ATOM   1634  O   LEU A 211       7.612  40.064  17.996  1.00 18.15           O  
ANISOU 1634  O   LEU A 211     1925   2237   2731     54   -194   -390       O  
ATOM   1635  CB  LEU A 211       8.960  42.900  18.494  1.00 16.75           C  
ANISOU 1635  CB  LEU A 211     1684   2151   2527      0   -421   -351       C  
ATOM   1636  CG  LEU A 211       9.945  44.030  18.185  1.00 16.29           C  
ANISOU 1636  CG  LEU A 211     1616   2096   2476   -147   -385   -318       C  
ATOM   1637  CD1 LEU A 211      10.567  44.554  19.493  1.00 17.12           C  
ANISOU 1637  CD1 LEU A 211     1599   2381   2522    -20   -589   -225       C  
ATOM   1638  CD2 LEU A 211      11.021  43.565  17.197  1.00 15.56           C  
ANISOU 1638  CD2 LEU A 211     1440   1970   2501   -223   -308   -291       C  
ATOM   1639  N   LEU A 212       5.992  41.639  18.004  1.00 17.63           N  
ANISOU 1639  N   LEU A 212     1906   2202   2587     10   -386   -412       N  
ATOM   1640  CA  LEU A 212       4.962  40.772  18.590  1.00 18.59           C  
ANISOU 1640  CA  LEU A 212     2038   2349   2674     -6   -444   -468       C  
ATOM   1641  C   LEU A 212       4.442  39.704  17.637  1.00 19.15           C  
ANISOU 1641  C   LEU A 212     2090   2358   2827      2   -445   -490       C  
ATOM   1642  O   LEU A 212       4.036  38.614  18.068  1.00 20.17           O  
ANISOU 1642  O   LEU A 212     2196   2502   2963    -24   -476   -544       O  
ATOM   1643  CB  LEU A 212       3.790  41.607  19.103  1.00 18.22           C  
ANISOU 1643  CB  LEU A 212     1977   2311   2632     -1   -425   -489       C  
ATOM   1644  CG  LEU A 212       4.003  42.499  20.326  1.00 18.85           C  
ANISOU 1644  CG  LEU A 212     2096   2471   2594      5   -406   -549       C  
ATOM   1645  CD1 LEU A 212       2.811  43.428  20.529  1.00 19.65           C  
ANISOU 1645  CD1 LEU A 212     2264   2731   2469     21   -258   -757       C  
ATOM   1646  CD2 LEU A 212       4.292  41.660  21.577  1.00 20.14           C  
ANISOU 1646  CD2 LEU A 212     2372   2611   2666   -107   -442   -732       C  
ATOM   1647  N   SER A 213       4.469  40.011  16.347  1.00 19.46           N  
ANISOU 1647  N   SER A 213     2145   2404   2843     51   -509   -541       N  
ATOM   1648  CA  SER A 213       3.890  39.126  15.344  1.00 20.38           C  
ANISOU 1648  CA  SER A 213     2308   2523   2911     39   -519   -525       C  
ATOM   1649  C   SER A 213       4.937  38.276  14.608  1.00 19.84           C  
ANISOU 1649  C   SER A 213     2271   2396   2871     34   -514   -530       C  
ATOM   1650  O   SER A 213       4.583  37.342  13.886  1.00 20.78           O  
ANISOU 1650  O   SER A 213     2386   2553   2956     32   -508   -580       O  
ATOM   1651  CB  SER A 213       3.054  39.934  14.345  1.00 20.86           C  
ANISOU 1651  CB  SER A 213     2370   2554   3000     61   -533   -491       C  
ATOM   1652  OG  SER A 213       3.861  40.884  13.679  1.00 22.34           O  
ANISOU 1652  OG  SER A 213     2603   2841   3044   -107   -593   -621       O  
ATOM   1653  N   ASP A 214       6.214  38.606  14.776  1.00 19.08           N  
ANISOU 1653  N   ASP A 214     2177   2300   2770    -19   -507   -546       N  
ATOM   1654  CA  ASP A 214       7.267  37.841  14.109  1.00 18.59           C  
ANISOU 1654  CA  ASP A 214     2125   2206   2730    -85   -511   -555       C  
ATOM   1655  C   ASP A 214       7.575  36.545  14.851  1.00 18.59           C  
ANISOU 1655  C   ASP A 214     2169   2144   2748   -109   -461   -602       C  
ATOM   1656  O   ASP A 214       7.773  36.560  16.063  1.00 18.70           O  
ANISOU 1656  O   ASP A 214     2191   2187   2725    -99   -480   -598       O  
ATOM   1657  CB  ASP A 214       8.548  38.660  13.949  1.00 18.56           C  
ANISOU 1657  CB  ASP A 214     2160   2183   2709    -99   -475   -488       C  
ATOM   1658  CG  ASP A 214       9.601  37.910  13.160  1.00 17.78           C  
ANISOU 1658  CG  ASP A 214     2088   2087   2580   -157   -520   -459       C  
ATOM   1659  OD1 ASP A 214      10.513  37.300  13.776  1.00 16.32           O  
ANISOU 1659  OD1 ASP A 214     2265   1796   2139   -235   -660   -372       O  
ATOM   1660  OD2 ASP A 214       9.478  37.888  11.917  1.00 17.11           O  
ANISOU 1660  OD2 ASP A 214     2102   2097   2300   -125   -766   -466       O  
ATOM   1661  N   PRO A 215       7.616  35.413  14.125  1.00 18.57           N  
ANISOU 1661  N   PRO A 215     2244   2066   2745    -96   -452   -629       N  
ATOM   1662  CA  PRO A 215       7.920  34.112  14.736  1.00 18.40           C  
ANISOU 1662  CA  PRO A 215     2278   2004   2708   -101   -417   -619       C  
ATOM   1663  C   PRO A 215       9.243  34.041  15.518  1.00 18.17           C  
ANISOU 1663  C   PRO A 215     2279   1948   2676    -99   -362   -585       C  
ATOM   1664  O   PRO A 215       9.327  33.308  16.506  1.00 19.02           O  
ANISOU 1664  O   PRO A 215     2364   2178   2682   -143   -364   -558       O  
ATOM   1665  CB  PRO A 215       7.942  33.151  13.533  1.00 18.68           C  
ANISOU 1665  CB  PRO A 215     2338   1997   2759    -91   -445   -659       C  
ATOM   1666  CG  PRO A 215       7.160  33.822  12.484  1.00 18.42           C  
ANISOU 1666  CG  PRO A 215     2255   2002   2739   -127   -435   -697       C  
ATOM   1667  CD  PRO A 215       7.343  35.293  12.679  1.00 19.05           C  
ANISOU 1667  CD  PRO A 215     2356   2083   2798    -92   -418   -635       C  
ATOM   1668  N   VAL A 216      10.264  34.775  15.084  1.00 17.43           N  
ANISOU 1668  N   VAL A 216     2199   1821   2603   -133   -365   -554       N  
ATOM   1669  CA  VAL A 216      11.549  34.786  15.787  1.00 17.28           C  
ANISOU 1669  CA  VAL A 216     2205   1825   2534   -131   -282   -520       C  
ATOM   1670  C   VAL A 216      11.558  35.853  16.898  1.00 17.00           C  
ANISOU 1670  C   VAL A 216     2129   1830   2497   -134   -275   -450       C  
ATOM   1671  O   VAL A 216      12.040  35.598  18.009  1.00 16.68           O  
ANISOU 1671  O   VAL A 216     2111   1821   2402   -147   -295   -452       O  
ATOM   1672  CB  VAL A 216      12.744  34.961  14.801  1.00 17.06           C  
ANISOU 1672  CB  VAL A 216     2150   1826   2505   -133   -259   -567       C  
ATOM   1673  CG1 VAL A 216      14.083  34.985  15.539  1.00 17.42           C  
ANISOU 1673  CG1 VAL A 216     2289   1868   2460   -122   -202   -585       C  
ATOM   1674  CG2 VAL A 216      12.737  33.836  13.729  1.00 17.41           C  
ANISOU 1674  CG2 VAL A 216     2208   1844   2562   -172   -315   -579       C  
ATOM   1675  N   PHE A 217      11.011  37.036  16.609  1.00 16.72           N  
ANISOU 1675  N   PHE A 217     2085   1819   2446   -124   -234   -346       N  
ATOM   1676  CA  PHE A 217      11.054  38.126  17.592  1.00 16.30           C  
ANISOU 1676  CA  PHE A 217     1934   1813   2446   -142   -180   -224       C  
ATOM   1677  C   PHE A 217      10.173  37.843  18.814  1.00 16.74           C  
ANISOU 1677  C   PHE A 217     1960   1876   2521   -141   -158   -184       C  
ATOM   1678  O   PHE A 217      10.574  38.133  19.942  1.00 16.91           O  
ANISOU 1678  O   PHE A 217     1881   1912   2630   -286    -87   -119       O  
ATOM   1679  CB  PHE A 217      10.695  39.492  16.974  1.00 16.20           C  
ANISOU 1679  CB  PHE A 217     1932   1845   2377   -144   -217   -217       C  
ATOM   1680  CG  PHE A 217      11.608  39.932  15.846  1.00 14.73           C  
ANISOU 1680  CG  PHE A 217     1834   1700   2061   -112   -167   -157       C  
ATOM   1681  CD1 PHE A 217      12.950  39.539  15.796  1.00 13.61           C  
ANISOU 1681  CD1 PHE A 217     1740   1636   1795   -313   -265   -266       C  
ATOM   1682  CD2 PHE A 217      11.122  40.776  14.844  1.00 14.44           C  
ANISOU 1682  CD2 PHE A 217     1822   1679   1983   -168   -207   -408       C  
ATOM   1683  CE1 PHE A 217      13.785  39.968  14.758  1.00 14.44           C  
ANISOU 1683  CE1 PHE A 217     2010   1753   1723   -143   -274   -331       C  
ATOM   1684  CE2 PHE A 217      11.940  41.214  13.808  1.00 14.08           C  
ANISOU 1684  CE2 PHE A 217     2023   1746   1577   -138   -213   -243       C  
ATOM   1685  CZ  PHE A 217      13.273  40.808  13.755  1.00 13.91           C  
ANISOU 1685  CZ  PHE A 217     1825   1746   1714   -152   -312   -254       C  
ATOM   1686  N   ARG A 218       8.989  37.273  18.594  1.00 17.19           N  
ANISOU 1686  N   ARG A 218     1952   1971   2607   -159   -102   -145       N  
ATOM   1687  CA  ARG A 218       8.025  37.086  19.691  1.00 18.44           C  
ANISOU 1687  CA  ARG A 218     2025   2200   2781   -144   -123   -170       C  
ATOM   1688  C   ARG A 218       8.547  36.296  20.909  1.00 18.25           C  
ANISOU 1688  C   ARG A 218     2014   2160   2760   -163   -125   -134       C  
ATOM   1689  O   ARG A 218       8.420  36.777  22.036  1.00 19.03           O  
ANISOU 1689  O   ARG A 218     2034   2311   2885    -75   -100   -109       O  
ATOM   1690  CB  ARG A 218       6.670  36.547  19.196  1.00 18.78           C  
ANISOU 1690  CB  ARG A 218     2022   2316   2796   -157   -106   -135       C  
ATOM   1691  CG  ARG A 218       5.612  36.405  20.303  1.00 20.63           C  
ANISOU 1691  CG  ARG A 218     2252   2621   2963   -174    -89   -182       C  
ATOM   1692  CD  ARG A 218       5.577  37.639  21.230  1.00 21.96           C  
ANISOU 1692  CD  ARG A 218     2391   2962   2989   -103   -160   -112       C  
ATOM   1693  NE  ARG A 218       4.583  37.510  22.290  1.00 23.91           N  
ANISOU 1693  NE  ARG A 218     2616   3397   3068     -3   -260    -83       N  
ATOM   1694  CZ  ARG A 218       3.286  37.740  22.112  1.00 25.87           C  
ANISOU 1694  CZ  ARG A 218     2810   3758   3258      1   -163    -50       C  
ATOM   1695  NH1 ARG A 218       2.831  38.112  20.926  1.00 25.31           N  
ANISOU 1695  NH1 ARG A 218     2926   3713   2975     60   -452     81       N  
ATOM   1696  NH2 ARG A 218       2.442  37.606  23.119  1.00 27.97           N  
ANISOU 1696  NH2 ARG A 218     2973   4136   3515    -19   -172     79       N  
ATOM   1697  N   PRO A 219       9.153  35.109  20.698  1.00 18.42           N  
ANISOU 1697  N   PRO A 219     2059   2139   2800   -191   -150   -147       N  
ATOM   1698  CA  PRO A 219       9.700  34.391  21.866  1.00 18.02           C  
ANISOU 1698  CA  PRO A 219     1995   2112   2737   -187   -184   -122       C  
ATOM   1699  C   PRO A 219      10.732  35.185  22.669  1.00 17.77           C  
ANISOU 1699  C   PRO A 219     1909   2093   2748   -230   -167    -94       C  
ATOM   1700  O   PRO A 219      10.864  34.978  23.880  1.00 17.43           O  
ANISOU 1700  O   PRO A 219     1805   2125   2692   -363   -136    -68       O  
ATOM   1701  CB  PRO A 219      10.359  33.146  21.252  1.00 18.60           C  
ANISOU 1701  CB  PRO A 219     2162   2121   2781   -173   -235   -152       C  
ATOM   1702  CG  PRO A 219       9.696  32.965  19.918  1.00 18.90           C  
ANISOU 1702  CG  PRO A 219     2241   2161   2777   -192   -297   -170       C  
ATOM   1703  CD  PRO A 219       9.353  34.354  19.444  1.00 18.71           C  
ANISOU 1703  CD  PRO A 219     2137   2180   2791   -185   -174   -115       C  
ATOM   1704  N   LEU A 220      11.465  36.071  22.000  1.00 17.20           N  
ANISOU 1704  N   LEU A 220     1754   2061   2719   -288   -179    -55       N  
ATOM   1705  CA  LEU A 220      12.444  36.938  22.660  1.00 17.43           C  
ANISOU 1705  CA  LEU A 220     1729   2157   2735   -242   -228    -75       C  
ATOM   1706  C   LEU A 220      11.759  38.025  23.483  1.00 16.92           C  
ANISOU 1706  C   LEU A 220     1633   2085   2709   -278   -272    -22       C  
ATOM   1707  O   LEU A 220      12.159  38.300  24.614  1.00 16.48           O  
ANISOU 1707  O   LEU A 220     1520   2100   2640   -251   -316     -3       O  
ATOM   1708  CB  LEU A 220      13.406  37.548  21.633  1.00 17.40           C  
ANISOU 1708  CB  LEU A 220     1670   2155   2784   -204   -165    -85       C  
ATOM   1709  CG  LEU A 220      14.455  36.582  21.053  1.00 19.26           C  
ANISOU 1709  CG  LEU A 220     1903   2484   2929    -56   -136   -211       C  
ATOM   1710  CD1 LEU A 220      14.928  37.058  19.704  1.00 19.85           C  
ANISOU 1710  CD1 LEU A 220     1975   2632   2935   -120    -43   -351       C  
ATOM   1711  CD2 LEU A 220      15.642  36.413  21.998  1.00 20.16           C  
ANISOU 1711  CD2 LEU A 220     1847   2764   3049    291    -22   -289       C  
ATOM   1712  N   VAL A 221      10.724  38.644  22.915  1.00 16.42           N  
ANISOU 1712  N   VAL A 221     1561   2037   2638   -342   -323      1       N  
ATOM   1713  CA  VAL A 221       9.870  39.547  23.680  1.00 16.08           C  
ANISOU 1713  CA  VAL A 221     1617   1948   2544   -391   -364     51       C  
ATOM   1714  C   VAL A 221       9.351  38.832  24.939  1.00 16.31           C  
ANISOU 1714  C   VAL A 221     1671   1933   2590   -473   -358     74       C  
ATOM   1715  O   VAL A 221       9.442  39.368  26.046  1.00 16.33           O  
ANISOU 1715  O   VAL A 221     1737   1989   2479   -510   -306     66       O  
ATOM   1716  CB  VAL A 221       8.697  40.089  22.812  1.00 15.93           C  
ANISOU 1716  CB  VAL A 221     1583   1896   2570   -342   -371     73       C  
ATOM   1717  CG1 VAL A 221       7.648  40.813  23.683  1.00 15.42           C  
ANISOU 1717  CG1 VAL A 221     1535   1913   2409   -397   -424    107       C  
ATOM   1718  CG2 VAL A 221       9.238  41.009  21.722  1.00 14.44           C  
ANISOU 1718  CG2 VAL A 221     1401   1876   2206   -308   -363     85       C  
ATOM   1719  N   ASP A 222       8.836  37.617  24.768  1.00 17.24           N  
ANISOU 1719  N   ASP A 222     1871   2014   2664   -504   -340     83       N  
ATOM   1720  CA  ASP A 222       8.324  36.821  25.879  1.00 18.14           C  
ANISOU 1720  CA  ASP A 222     2050   2028   2815   -630   -366    135       C  
ATOM   1721  C   ASP A 222       9.411  36.570  26.916  1.00 18.33           C  
ANISOU 1721  C   ASP A 222     2061   2074   2827   -623   -320    173       C  
ATOM   1722  O   ASP A 222       9.187  36.737  28.122  1.00 18.95           O  
ANISOU 1722  O   ASP A 222     2118   2287   2794   -653   -315    183       O  
ATOM   1723  CB  ASP A 222       7.771  35.490  25.355  1.00 18.44           C  
ANISOU 1723  CB  ASP A 222     2128   2009   2868   -716   -406    128       C  
ATOM   1724  CG  ASP A 222       6.459  35.659  24.591  1.00 20.59           C  
ANISOU 1724  CG  ASP A 222     2443   2188   3191   -759   -344     76       C  
ATOM   1725  OD1 ASP A 222       5.811  36.725  24.688  1.00 23.08           O  
ANISOU 1725  OD1 ASP A 222     2715   2587   3467   -735   -259     28       O  
ATOM   1726  OD2 ASP A 222       6.069  34.711  23.879  1.00 25.70           O  
ANISOU 1726  OD2 ASP A 222     3178   2922   3663   -802   -547     30       O  
ATOM   1727  N   LYS A 223      10.590  36.186  26.437  1.00 18.08           N  
ANISOU 1727  N   LYS A 223     1958   2064   2848   -576   -275    255       N  
ATOM   1728  CA  LYS A 223      11.724  35.879  27.309  1.00 18.13           C  
ANISOU 1728  CA  LYS A 223     1974   2114   2798   -525   -267    302       C  
ATOM   1729  C   LYS A 223      12.103  37.083  28.165  1.00 17.88           C  
ANISOU 1729  C   LYS A 223     1959   2140   2693   -479   -237    286       C  
ATOM   1730  O   LYS A 223      12.244  36.965  29.396  1.00 17.27           O  
ANISOU 1730  O   LYS A 223     1895   2148   2519   -499   -212    349       O  
ATOM   1731  CB  LYS A 223      12.925  35.393  26.484  1.00 17.81           C  
ANISOU 1731  CB  LYS A 223     1876   2063   2826   -464   -255    318       C  
ATOM   1732  CG  LYS A 223      14.179  35.084  27.321  1.00 19.44           C  
ANISOU 1732  CG  LYS A 223     2090   2259   3038   -479   -282    315       C  
ATOM   1733  CD  LYS A 223      15.320  34.464  26.489  1.00 20.95           C  
ANISOU 1733  CD  LYS A 223     2226   2336   3396   -328   -239    404       C  
ATOM   1734  CE  LYS A 223      16.168  35.514  25.773  1.00 24.30           C  
ANISOU 1734  CE  LYS A 223     2474   2776   3981   -262   -274    340       C  
ATOM   1735  NZ  LYS A 223      17.570  35.041  25.432  1.00 25.22           N  
ANISOU 1735  NZ  LYS A 223     2583   2654   4342     15   -448    522       N  
ATOM   1736  N   TYR A 224      12.251  38.232  27.507  1.00 16.88           N  
ANISOU 1736  N   TYR A 224     1868   2042   2501   -519   -211    297       N  
ATOM   1737  CA  TYR A 224      12.676  39.474  28.162  1.00 17.10           C  
ANISOU 1737  CA  TYR A 224     1889   2160   2448   -447   -154    277       C  
ATOM   1738  C   TYR A 224      11.634  40.000  29.144  1.00 17.22           C  
ANISOU 1738  C   TYR A 224     1879   2218   2445   -440   -134    302       C  
ATOM   1739  O   TYR A 224      11.991  40.476  30.229  1.00 17.33           O  
ANISOU 1739  O   TYR A 224     1881   2207   2495   -435   -102    337       O  
ATOM   1740  CB  TYR A 224      13.042  40.544  27.127  1.00 16.43           C  
ANISOU 1740  CB  TYR A 224     1833   2088   2322   -446   -127    256       C  
ATOM   1741  CG  TYR A 224      14.192  40.160  26.214  1.00 15.27           C  
ANISOU 1741  CG  TYR A 224     1788   1913   2100   -500   -181     52       C  
ATOM   1742  CD1 TYR A 224      15.204  39.295  26.644  1.00 14.38           C  
ANISOU 1742  CD1 TYR A 224     1807   1916   1737   -402   -138    -31       C  
ATOM   1743  CD2 TYR A 224      14.275  40.675  24.925  1.00 14.32           C  
ANISOU 1743  CD2 TYR A 224     1790   1841   1809   -502   -301     29       C  
ATOM   1744  CE1 TYR A 224      16.264  38.950  25.810  1.00 14.69           C  
ANISOU 1744  CE1 TYR A 224     1713   1911   1955   -346   -137     19       C  
ATOM   1745  CE2 TYR A 224      15.335  40.352  24.087  1.00 13.96           C  
ANISOU 1745  CE2 TYR A 224     1515   1865   1922   -262   -230    -72       C  
ATOM   1746  CZ  TYR A 224      16.317  39.480  24.531  1.00 14.98           C  
ANISOU 1746  CZ  TYR A 224     1713   2020   1959   -342    -91     96       C  
ATOM   1747  OH  TYR A 224      17.350  39.135  23.694  1.00 15.26           O  
ANISOU 1747  OH  TYR A 224     1703   2263   1830   -481     54    116       O  
ATOM   1748  N   ALA A 225      10.353  39.899  28.774  1.00 17.54           N  
ANISOU 1748  N   ALA A 225     1850   2394   2420   -472    -82    299       N  
ATOM   1749  CA  ALA A 225       9.277  40.272  29.706  1.00 18.63           C  
ANISOU 1749  CA  ALA A 225     1953   2586   2540   -465   -166    265       C  
ATOM   1750  C   ALA A 225       9.275  39.386  30.964  1.00 19.13           C  
ANISOU 1750  C   ALA A 225     2028   2720   2519   -498   -161    260       C  
ATOM   1751  O   ALA A 225       8.982  39.863  32.064  1.00 19.63           O  
ANISOU 1751  O   ALA A 225     2082   2815   2562   -462   -194    195       O  
ATOM   1752  CB  ALA A 225       7.930  40.248  29.012  1.00 18.87           C  
ANISOU 1752  CB  ALA A 225     1913   2667   2587   -489   -120    221       C  
ATOM   1753  N   ALA A 226       9.620  38.108  30.807  1.00 19.43           N  
ANISOU 1753  N   ALA A 226     2111   2803   2468   -470   -201    323       N  
ATOM   1754  CA  ALA A 226       9.639  37.171  31.941  1.00 20.01           C  
ANISOU 1754  CA  ALA A 226     2200   2865   2535   -554   -187    378       C  
ATOM   1755  C   ALA A 226      10.940  37.223  32.764  1.00 20.47           C  
ANISOU 1755  C   ALA A 226     2285   2952   2538   -552   -171    429       C  
ATOM   1756  O   ALA A 226      10.948  36.886  33.960  1.00 20.46           O  
ANISOU 1756  O   ALA A 226     2251   3087   2432   -653   -147    468       O  
ATOM   1757  CB  ALA A 226       9.361  35.741  31.457  1.00 20.52           C  
ANISOU 1757  CB  ALA A 226     2254   2947   2594   -470   -167    375       C  
ATOM   1758  N   ASP A 227      12.037  37.632  32.124  1.00 19.85           N  
ANISOU 1758  N   ASP A 227     2309   2753   2478   -640   -191    491       N  
ATOM   1759  CA  ASP A 227      13.370  37.472  32.706  1.00 19.71           C  
ANISOU 1759  CA  ASP A 227     2415   2638   2436   -567   -158    471       C  
ATOM   1760  C   ASP A 227      14.212  38.720  32.399  1.00 19.22           C  
ANISOU 1760  C   ASP A 227     2401   2572   2329   -552   -147    431       C  
ATOM   1761  O   ASP A 227      14.825  38.828  31.328  1.00 18.06           O  
ANISOU 1761  O   ASP A 227     2276   2458   2124   -627    -59    479       O  
ATOM   1762  CB  ASP A 227      14.004  36.183  32.149  1.00 19.96           C  
ANISOU 1762  CB  ASP A 227     2401   2663   2520   -560   -194    519       C  
ATOM   1763  CG  ASP A 227      15.332  35.812  32.817  1.00 21.78           C  
ANISOU 1763  CG  ASP A 227     2823   2732   2716   -453   -303    577       C  
ATOM   1764  OD1 ASP A 227      15.921  36.625  33.557  1.00 21.92           O  
ANISOU 1764  OD1 ASP A 227     2840   2684   2801   -557   -542    773       O  
ATOM   1765  OD2 ASP A 227      15.798  34.676  32.569  1.00 23.96           O  
ANISOU 1765  OD2 ASP A 227     3179   2939   2985   -116   -436    768       O  
ATOM   1766  N   GLU A 228      14.223  39.672  33.335  1.00 18.64           N  
ANISOU 1766  N   GLU A 228     2431   2462   2188   -464   -124    415       N  
ATOM   1767  CA  GLU A 228      14.947  40.931  33.127  1.00 18.52           C  
ANISOU 1767  CA  GLU A 228     2515   2461   2059   -350   -149    327       C  
ATOM   1768  C   GLU A 228      16.463  40.714  33.074  1.00 17.86           C  
ANISOU 1768  C   GLU A 228     2503   2297   1983   -304   -187    315       C  
ATOM   1769  O   GLU A 228      17.161  41.410  32.347  1.00 17.10           O  
ANISOU 1769  O   GLU A 228     2418   2344   1734   -238   -122    324       O  
ATOM   1770  CB  GLU A 228      14.561  41.971  34.180  1.00 18.54           C  
ANISOU 1770  CB  GLU A 228     2557   2472   2013   -339   -122    373       C  
ATOM   1771  CG  GLU A 228      15.333  43.279  34.072  1.00 19.24           C  
ANISOU 1771  CG  GLU A 228     2644   2709   1955   -309      7    198       C  
ATOM   1772  CD  GLU A 228      14.831  44.339  35.019  1.00 21.30           C  
ANISOU 1772  CD  GLU A 228     2931   3041   2119   -254    -71    231       C  
ATOM   1773  OE1 GLU A 228      15.497  44.542  36.054  1.00 23.33           O  
ANISOU 1773  OE1 GLU A 228     3415   3475   1972   -244     74    -28       O  
ATOM   1774  OE2 GLU A 228      13.764  44.945  34.741  1.00 22.59           O  
ANISOU 1774  OE2 GLU A 228     3328   3365   1889   -127    124    454       O  
ATOM   1775  N   ASP A 229      16.954  39.738  33.839  1.00 17.42           N  
ANISOU 1775  N   ASP A 229     2508   2243   1868   -219   -262    323       N  
ATOM   1776  CA  ASP A 229      18.368  39.344  33.797  1.00 17.23           C  
ANISOU 1776  CA  ASP A 229     2545   2157   1842   -211   -271    348       C  
ATOM   1777  C   ASP A 229      18.782  38.927  32.378  1.00 16.57           C  
ANISOU 1777  C   ASP A 229     2447   2025   1822   -199   -294    329       C  
ATOM   1778  O   ASP A 229      19.818  39.363  31.873  1.00 15.57           O  
ANISOU 1778  O   ASP A 229     2266   1967   1680   -256   -258    366       O  
ATOM   1779  CB  ASP A 229      18.629  38.193  34.778  1.00 17.63           C  
ANISOU 1779  CB  ASP A 229     2658   2204   1835   -202   -336    350       C  
ATOM   1780  CG  ASP A 229      18.480  38.610  36.244  1.00 20.54           C  
ANISOU 1780  CG  ASP A 229     3155   2475   2171   -214   -203    430       C  
ATOM   1781  OD1 ASP A 229      18.466  39.825  36.549  1.00 22.71           O  
ANISOU 1781  OD1 ASP A 229     3465   2879   2282   -373   -335    382       O  
ATOM   1782  OD2 ASP A 229      18.392  37.700  37.098  1.00 23.98           O  
ANISOU 1782  OD2 ASP A 229     3834   2978   2296   -395   -190    563       O  
ATOM   1783  N   ALA A 230      17.954  38.090  31.750  1.00 15.74           N  
ANISOU 1783  N   ALA A 230     2342   1951   1685   -227   -329    284       N  
ATOM   1784  CA  ALA A 230      18.162  37.649  30.365  1.00 15.47           C  
ANISOU 1784  CA  ALA A 230     2278   1837   1761   -235   -312    228       C  
ATOM   1785  C   ALA A 230      18.179  38.839  29.406  1.00 14.43           C  
ANISOU 1785  C   ALA A 230     2124   1717   1642   -190   -323    225       C  
ATOM   1786  O   ALA A 230      19.049  38.929  28.524  1.00 14.75           O  
ANISOU 1786  O   ALA A 230     2188   1627   1786   -206   -255    290       O  
ATOM   1787  CB  ALA A 230      17.077  36.641  29.956  1.00 15.12           C  
ANISOU 1787  CB  ALA A 230     2257   1763   1723   -311   -317    251       C  
ATOM   1788  N   PHE A 231      17.218  39.746  29.572  1.00 13.30           N  
ANISOU 1788  N   PHE A 231     1955   1582   1516   -182   -355    169       N  
ATOM   1789  CA  PHE A 231      17.204  40.993  28.803  1.00 12.56           C  
ANISOU 1789  CA  PHE A 231     1756   1685   1331    -70   -403    174       C  
ATOM   1790  C   PHE A 231      18.508  41.772  28.983  1.00 12.77           C  
ANISOU 1790  C   PHE A 231     1850   1673   1326   -124   -342    170       C  
ATOM   1791  O   PHE A 231      19.151  42.134  27.998  1.00 12.06           O  
ANISOU 1791  O   PHE A 231     1656   1673   1251   -135   -368    218       O  
ATOM   1792  CB  PHE A 231      16.007  41.861  29.189  1.00 13.09           C  
ANISOU 1792  CB  PHE A 231     1833   1714   1424    -42   -440    119       C  
ATOM   1793  CG  PHE A 231      16.054  43.244  28.608  1.00 11.52           C  
ANISOU 1793  CG  PHE A 231     1568   1727   1079    181   -521    305       C  
ATOM   1794  CD1 PHE A 231      16.306  43.446  27.242  1.00 12.74           C  
ANISOU 1794  CD1 PHE A 231     1454   1994   1390    251   -329    249       C  
ATOM   1795  CD2 PHE A 231      15.847  44.350  29.420  1.00 11.54           C  
ANISOU 1795  CD2 PHE A 231     1365   1820   1200     -4   -692    140       C  
ATOM   1796  CE1 PHE A 231      16.342  44.737  26.714  1.00 10.28           C  
ANISOU 1796  CE1 PHE A 231     1331   1411   1162    229   -482    166       C  
ATOM   1797  CE2 PHE A 231      15.865  45.638  28.900  1.00 11.56           C  
ANISOU 1797  CE2 PHE A 231     1516   1857   1017    -29   -511      1       C  
ATOM   1798  CZ  PHE A 231      16.127  45.839  27.549  1.00 11.95           C  
ANISOU 1798  CZ  PHE A 231     1566   1979    992     17   -574     87       C  
ATOM   1799  N   PHE A 232      18.898  42.006  30.235  1.00 12.30           N  
ANISOU 1799  N   PHE A 232     1823   1654   1197   -154   -367    116       N  
ATOM   1800  CA  PHE A 232      20.111  42.761  30.519  1.00 12.70           C  
ANISOU 1800  CA  PHE A 232     1916   1700   1206    -97   -247     91       C  
ATOM   1801  C   PHE A 232      21.356  42.153  29.856  1.00 12.91           C  
ANISOU 1801  C   PHE A 232     2005   1670   1228    -32   -245     82       C  
ATOM   1802  O   PHE A 232      22.183  42.896  29.319  1.00 12.44           O  
ANISOU 1802  O   PHE A 232     1979   1705   1041     31    -36    104       O  
ATOM   1803  CB  PHE A 232      20.326  42.920  32.029  1.00 12.57           C  
ANISOU 1803  CB  PHE A 232     1963   1643   1169   -165   -287    109       C  
ATOM   1804  CG  PHE A 232      19.627  44.116  32.628  1.00 13.02           C  
ANISOU 1804  CG  PHE A 232     1995   1716   1233   -231   -269     64       C  
ATOM   1805  CD1 PHE A 232      18.417  44.598  32.110  1.00 13.15           C  
ANISOU 1805  CD1 PHE A 232     2010   1692   1294   -301   -218     -8       C  
ATOM   1806  CD2 PHE A 232      20.166  44.742  33.741  1.00 13.75           C  
ANISOU 1806  CD2 PHE A 232     2013   1916   1294   -431   -286      3       C  
ATOM   1807  CE1 PHE A 232      17.787  45.696  32.676  1.00 13.11           C  
ANISOU 1807  CE1 PHE A 232     2016   1656   1306   -356   -309    117       C  
ATOM   1808  CE2 PHE A 232      19.544  45.861  34.316  1.00 14.17           C  
ANISOU 1808  CE2 PHE A 232     2091   1840   1453   -283   -187    170       C  
ATOM   1809  CZ  PHE A 232      18.355  46.328  33.804  1.00 11.69           C  
ANISOU 1809  CZ  PHE A 232     1949   1370   1120   -446   -441    375       C  
ATOM   1810  N   ALA A 233      21.472  40.821  29.891  1.00 12.63           N  
ANISOU 1810  N   ALA A 233     2002   1592   1202     24   -203     86       N  
ATOM   1811  CA  ALA A 233      22.608  40.136  29.293  1.00 13.74           C  
ANISOU 1811  CA  ALA A 233     2194   1530   1494     -8   -261    136       C  
ATOM   1812  C   ALA A 233      22.591  40.338  27.774  1.00 13.22           C  
ANISOU 1812  C   ALA A 233     2125   1385   1510    -23   -246     99       C  
ATOM   1813  O   ALA A 233      23.594  40.731  27.176  1.00 13.59           O  
ANISOU 1813  O   ALA A 233     2169   1403   1589    -64   -312    184       O  
ATOM   1814  CB  ALA A 233      22.584  38.659  29.644  1.00 13.52           C  
ANISOU 1814  CB  ALA A 233     2174   1482   1479     20   -222    152       C  
ATOM   1815  N   ASP A 234      21.436  40.103  27.169  1.00 12.85           N  
ANISOU 1815  N   ASP A 234     2014   1296   1570    -82   -329    129       N  
ATOM   1816  CA  ASP A 234      21.311  40.144  25.718  1.00 12.81           C  
ANISOU 1816  CA  ASP A 234     1951   1243   1671    -68   -283     16       C  
ATOM   1817  C   ASP A 234      21.431  41.592  25.247  1.00 12.50           C  
ANISOU 1817  C   ASP A 234     1878   1248   1623    -69   -266    -35       C  
ATOM   1818  O   ASP A 234      22.029  41.849  24.203  1.00 12.24           O  
ANISOU 1818  O   ASP A 234     1867   1116   1665    -73   -247    -58       O  
ATOM   1819  CB  ASP A 234      19.968  39.553  25.270  1.00 13.16           C  
ANISOU 1819  CB  ASP A 234     2040   1212   1745   -189   -322     23       C  
ATOM   1820  CG  ASP A 234      19.959  38.012  25.280  1.00 13.60           C  
ANISOU 1820  CG  ASP A 234     2257   1094   1815   -188   -399     85       C  
ATOM   1821  OD1 ASP A 234      20.918  37.395  25.792  1.00 14.80           O  
ANISOU 1821  OD1 ASP A 234     2800    826   1997   -140   -563    167       O  
ATOM   1822  OD2 ASP A 234      18.998  37.416  24.750  1.00 15.27           O  
ANISOU 1822  OD2 ASP A 234     2497   1134   2172   -459   -130    119       O  
ATOM   1823  N   TYR A 235      20.866  42.518  26.031  1.00 11.96           N  
ANISOU 1823  N   TYR A 235     1760   1252   1533     70   -229   -126       N  
ATOM   1824  CA  TYR A 235      20.979  43.944  25.747  1.00 11.63           C  
ANISOU 1824  CA  TYR A 235     1675   1358   1384     63   -190   -192       C  
ATOM   1825  C   TYR A 235      22.457  44.392  25.772  1.00 11.65           C  
ANISOU 1825  C   TYR A 235     1630   1414   1379     66   -225   -212       C  
ATOM   1826  O   TYR A 235      22.922  45.062  24.856  1.00 11.43           O  
ANISOU 1826  O   TYR A 235     1590   1502   1247     42   -245   -215       O  
ATOM   1827  CB  TYR A 235      20.138  44.841  26.695  1.00 11.70           C  
ANISOU 1827  CB  TYR A 235     1681   1294   1467    228   -191   -163       C  
ATOM   1828  CG  TYR A 235      20.318  46.278  26.257  1.00 10.40           C  
ANISOU 1828  CG  TYR A 235     1715   1135   1101    165   -126   -133       C  
ATOM   1829  CD1 TYR A 235      21.390  47.042  26.734  1.00  9.73           C  
ANISOU 1829  CD1 TYR A 235     1740    982    975    324    -33   -305       C  
ATOM   1830  CD2 TYR A 235      19.486  46.839  25.280  1.00  8.76           C  
ANISOU 1830  CD2 TYR A 235     1260    970   1096    525   -380   -167       C  
ATOM   1831  CE1 TYR A 235      21.619  48.336  26.278  1.00 10.48           C  
ANISOU 1831  CE1 TYR A 235     1779   1018   1183    136   -255    -48       C  
ATOM   1832  CE2 TYR A 235      19.700  48.152  24.823  1.00  9.21           C  
ANISOU 1832  CE2 TYR A 235     1495    706   1298    586   -188   -223       C  
ATOM   1833  CZ  TYR A 235      20.783  48.884  25.312  1.00  9.26           C  
ANISOU 1833  CZ  TYR A 235     1447    751   1321    585   -206   -257       C  
ATOM   1834  OH  TYR A 235      21.026  50.172  24.877  1.00 11.59           O  
ANISOU 1834  OH  TYR A 235     1837   1540   1027    170    -39   -101       O  
ATOM   1835  N   ALA A 236      23.180  44.026  26.826  1.00 11.17           N  
ANISOU 1835  N   ALA A 236     1585   1438   1220     63   -249   -243       N  
ATOM   1836  CA  ALA A 236      24.591  44.397  26.942  1.00 12.24           C  
ANISOU 1836  CA  ALA A 236     1704   1614   1333     -5   -246   -132       C  
ATOM   1837  C   ALA A 236      25.409  43.904  25.743  1.00 12.65           C  
ANISOU 1837  C   ALA A 236     1769   1593   1445    -12   -267    -95       C  
ATOM   1838  O   ALA A 236      26.229  44.644  25.202  1.00 12.55           O  
ANISOU 1838  O   ALA A 236     1776   1589   1402    -97   -205    -81       O  
ATOM   1839  CB  ALA A 236      25.175  43.883  28.256  1.00 12.19           C  
ANISOU 1839  CB  ALA A 236     1591   1675   1363    -15   -300    -26       C  
ATOM   1840  N   GLU A 237      25.159  42.666  25.327  1.00 13.17           N  
ANISOU 1840  N   GLU A 237     1920   1566   1515    -32   -218   -138       N  
ATOM   1841  CA  GLU A 237      25.823  42.078  24.170  1.00 14.56           C  
ANISOU 1841  CA  GLU A 237     2138   1625   1768    -68   -156   -139       C  
ATOM   1842  C   GLU A 237      25.539  42.893  22.913  1.00 13.57           C  
ANISOU 1842  C   GLU A 237     1925   1572   1658   -102   -143   -152       C  
ATOM   1843  O   GLU A 237      26.456  43.261  22.170  1.00 13.74           O  
ANISOU 1843  O   GLU A 237     1884   1643   1693    -95   -124   -145       O  
ATOM   1844  CB  GLU A 237      25.326  40.648  23.980  1.00 14.94           C  
ANISOU 1844  CB  GLU A 237     2268   1609   1799    -68   -101   -163       C  
ATOM   1845  CG  GLU A 237      26.044  39.853  22.909  1.00 17.87           C  
ANISOU 1845  CG  GLU A 237     2757   1830   2200   -145    -68   -138       C  
ATOM   1846  CD  GLU A 237      25.535  38.417  22.822  1.00 19.99           C  
ANISOU 1846  CD  GLU A 237     3272   2033   2287   -123     14   -204       C  
ATOM   1847  OE1 GLU A 237      25.178  37.832  23.868  1.00 22.78           O  
ANISOU 1847  OE1 GLU A 237     3773   2178   2702   -162    563   -153       O  
ATOM   1848  OE2 GLU A 237      25.503  37.867  21.706  1.00 25.09           O  
ANISOU 1848  OE2 GLU A 237     3992   2716   2824   -128     47   -443       O  
ATOM   1849  N   ALA A 238      24.256  43.165  22.688  1.00 12.45           N  
ANISOU 1849  N   ALA A 238     1695   1440   1593     -9    -98   -134       N  
ATOM   1850  CA  ALA A 238      23.800  43.840  21.478  1.00 11.46           C  
ANISOU 1850  CA  ALA A 238     1446   1375   1530   -101    -91    -94       C  
ATOM   1851  C   ALA A 238      24.306  45.295  21.426  1.00 10.85           C  
ANISOU 1851  C   ALA A 238     1361   1312   1449    -66    -92   -118       C  
ATOM   1852  O   ALA A 238      24.766  45.749  20.386  1.00 10.34           O  
ANISOU 1852  O   ALA A 238     1278   1270   1377   -227    -52    -72       O  
ATOM   1853  CB  ALA A 238      22.277  43.772  21.381  1.00 11.15           C  
ANISOU 1853  CB  ALA A 238     1371   1369   1496    -72   -135    -94       C  
ATOM   1854  N   HIS A 239      24.251  46.004  22.551  1.00 10.25           N  
ANISOU 1854  N   HIS A 239     1213   1399   1282    -56   -129   -121       N  
ATOM   1855  CA  HIS A 239      24.685  47.397  22.599  1.00 10.00           C  
ANISOU 1855  CA  HIS A 239     1226   1373   1199    -12   -111   -144       C  
ATOM   1856  C   HIS A 239      26.194  47.447  22.333  1.00  9.95           C  
ANISOU 1856  C   HIS A 239     1249   1377   1152     39    -73   -177       C  
ATOM   1857  O   HIS A 239      26.675  48.293  21.571  1.00  9.21           O  
ANISOU 1857  O   HIS A 239     1041   1352   1103     97   -165   -147       O  
ATOM   1858  CB  HIS A 239      24.368  47.986  23.982  1.00 10.03           C  
ANISOU 1858  CB  HIS A 239     1310   1368   1133    -70    -39   -166       C  
ATOM   1859  CG  HIS A 239      24.566  49.470  24.103  1.00 10.32           C  
ANISOU 1859  CG  HIS A 239     1406   1374   1139   -160    -69    282       C  
ATOM   1860  ND1 HIS A 239      25.675  50.137  23.614  1.00 12.82           N  
ANISOU 1860  ND1 HIS A 239     1965   1488   1417   -175    -43    328       N  
ATOM   1861  CD2 HIS A 239      23.839  50.398  24.768  1.00  7.96           C  
ANISOU 1861  CD2 HIS A 239     1237    989    796    -84   -187    355       C  
ATOM   1862  CE1 HIS A 239      25.584  51.419  23.920  1.00 10.04           C  
ANISOU 1862  CE1 HIS A 239     1394   1381   1038      0     13    410       C  
ATOM   1863  NE2 HIS A 239      24.481  51.603  24.622  1.00 13.03           N  
ANISOU 1863  NE2 HIS A 239     1917   1761   1271     51   -430    377       N  
ATOM   1864  N   GLN A 240      26.941  46.545  22.962  1.00  9.60           N  
ANISOU 1864  N   GLN A 240     1299   1424    924     30   -147   -172       N  
ATOM   1865  CA  GLN A 240      28.369  46.489  22.671  1.00 10.34           C  
ANISOU 1865  CA  GLN A 240     1423   1415   1090     55   -132   -101       C  
ATOM   1866  C   GLN A 240      28.615  46.341  21.157  1.00 10.42           C  
ANISOU 1866  C   GLN A 240     1534   1385   1039    -60   -146   -118       C  
ATOM   1867  O   GLN A 240      29.374  47.120  20.562  1.00 11.16           O  
ANISOU 1867  O   GLN A 240     1761   1378   1098   -156   -159   -202       O  
ATOM   1868  CB  GLN A 240      29.081  45.373  23.414  1.00 10.78           C  
ANISOU 1868  CB  GLN A 240     1500   1544   1051     29   -119    -37       C  
ATOM   1869  CG  GLN A 240      30.580  45.490  23.181  1.00 11.16           C  
ANISOU 1869  CG  GLN A 240     1244   1614   1381    168   -201    106       C  
ATOM   1870  CD  GLN A 240      31.403  44.415  23.862  1.00 13.88           C  
ANISOU 1870  CD  GLN A 240     1716   1791   1766    263    -74    438       C  
ATOM   1871  OE1 GLN A 240      30.888  43.600  24.629  1.00 14.35           O  
ANISOU 1871  OE1 GLN A 240     1867   1928   1656    482    132    708       O  
ATOM   1872  NE2 GLN A 240      32.700  44.404  23.565  1.00 13.82           N  
ANISOU 1872  NE2 GLN A 240     1533   1907   1810     19   -102    573       N  
ATOM   1873  N   LYS A 241      27.972  45.348  20.546  1.00 10.67           N  
ANISOU 1873  N   LYS A 241     1644   1311   1098    -77   -154   -109       N  
ATOM   1874  CA  LYS A 241      28.137  45.107  19.108  1.00 11.15           C  
ANISOU 1874  CA  LYS A 241     1734   1356   1147   -115   -215    -46       C  
ATOM   1875  C   LYS A 241      27.768  46.344  18.295  1.00 11.21           C  
ANISOU 1875  C   LYS A 241     1664   1448   1147    -69   -217    -19       C  
ATOM   1876  O   LYS A 241      28.543  46.775  17.432  1.00 10.74           O  
ANISOU 1876  O   LYS A 241     1626   1484    970    -22   -144     40       O  
ATOM   1877  CB  LYS A 241      27.333  43.881  18.650  1.00 11.94           C  
ANISOU 1877  CB  LYS A 241     1867   1370   1300   -209   -195    -68       C  
ATOM   1878  CG  LYS A 241      27.875  42.578  19.224  1.00 12.82           C  
ANISOU 1878  CG  LYS A 241     2083   1420   1365    -84   -218    -37       C  
ATOM   1879  CD  LYS A 241      27.557  41.359  18.366  1.00 20.78           C  
ANISOU 1879  CD  LYS A 241     2834   2269   2790   -147   -258    156       C  
ATOM   1880  CE  LYS A 241      26.105  41.035  18.385  1.00 20.79           C  
ANISOU 1880  CE  LYS A 241     2790   2166   2941    -45   -284    182       C  
ATOM   1881  NZ  LYS A 241      25.755  39.940  17.405  1.00 16.94           N  
ANISOU 1881  NZ  LYS A 241     2772   1796   1868    252   -273   -283       N  
ATOM   1882  N   LEU A 242      26.622  46.942  18.617  1.00 10.97           N  
ANISOU 1882  N   LEU A 242     1580   1514   1072    -32   -184     29       N  
ATOM   1883  CA  LEU A 242      26.163  48.161  17.945  1.00 11.14           C  
ANISOU 1883  CA  LEU A 242     1544   1641   1046     48   -206     -4       C  
ATOM   1884  C   LEU A 242      27.214  49.289  18.038  1.00 11.04           C  
ANISOU 1884  C   LEU A 242     1578   1694    922     -7   -199     34       C  
ATOM   1885  O   LEU A 242      27.586  49.897  17.033  1.00 10.29           O  
ANISOU 1885  O   LEU A 242     1502   1759    648     36   -216     -4       O  
ATOM   1886  CB  LEU A 242      24.835  48.618  18.555  1.00 10.93           C  
ANISOU 1886  CB  LEU A 242     1440   1642   1068     70   -219     22       C  
ATOM   1887  CG  LEU A 242      24.293  49.975  18.087  1.00 10.18           C  
ANISOU 1887  CG  LEU A 242     1239   1680    946    209   -231    -23       C  
ATOM   1888  CD1 LEU A 242      23.767  49.859  16.645  1.00 11.95           C  
ANISOU 1888  CD1 LEU A 242     1331   2198   1011    151   -316    -85       C  
ATOM   1889  CD2 LEU A 242      23.204  50.455  19.049  1.00 11.47           C  
ANISOU 1889  CD2 LEU A 242     1446   1852   1058    258   -130    -59       C  
ATOM   1890  N   SER A 243      27.700  49.535  19.255  1.00 11.02           N  
ANISOU 1890  N   SER A 243     1656   1760    771    -55   -191     15       N  
ATOM   1891  CA  SER A 243      28.673  50.581  19.517  1.00 10.90           C  
ANISOU 1891  CA  SER A 243     1705   1779    657   -131   -135      4       C  
ATOM   1892  C   SER A 243      30.017  50.341  18.800  1.00 10.78           C  
ANISOU 1892  C   SER A 243     1679   1835    581   -151   -104    -11       C  
ATOM   1893  O   SER A 243      30.812  51.259  18.670  1.00 10.34           O  
ANISOU 1893  O   SER A 243     1680   1809    438   -167    -15      0       O  
ATOM   1894  CB  SER A 243      28.888  50.732  21.034  1.00 11.02           C  
ANISOU 1894  CB  SER A 243     1746   1797    642   -117   -231     27       C  
ATOM   1895  OG  SER A 243      29.715  49.704  21.547  1.00 10.90           O  
ANISOU 1895  OG  SER A 243     1999   1557    585   -249    -80    348       O  
ATOM   1896  N   GLU A 244      30.250  49.104  18.350  1.00 10.61           N  
ANISOU 1896  N   GLU A 244     1589   1834    605   -129    -46    -30       N  
ATOM   1897  CA  GLU A 244      31.521  48.713  17.734  1.00 11.56           C  
ANISOU 1897  CA  GLU A 244     1613   1928    850   -198    -45    -58       C  
ATOM   1898  C   GLU A 244      31.412  48.334  16.247  1.00 11.82           C  
ANISOU 1898  C   GLU A 244     1615   1976    897   -203     -5    -72       C  
ATOM   1899  O   GLU A 244      32.365  47.818  15.652  1.00 11.34           O  
ANISOU 1899  O   GLU A 244     1591   1995    722   -146    -21   -142       O  
ATOM   1900  CB  GLU A 244      32.166  47.585  18.555  1.00 11.15           C  
ANISOU 1900  CB  GLU A 244     1475   1846    915   -168    -78    -62       C  
ATOM   1901  CG  GLU A 244      32.568  48.001  19.973  1.00 11.26           C  
ANISOU 1901  CG  GLU A 244     1458   1918    902   -206     15    -60       C  
ATOM   1902  CD  GLU A 244      33.058  46.837  20.829  1.00 12.27           C  
ANISOU 1902  CD  GLU A 244     1633   1964   1062   -321    -47    -80       C  
ATOM   1903  OE1 GLU A 244      33.143  45.696  20.324  1.00 13.76           O  
ANISOU 1903  OE1 GLU A 244     1756   1907   1564   -297    -83   -210       O  
ATOM   1904  OE2 GLU A 244      33.389  47.069  22.009  1.00 13.38           O  
ANISOU 1904  OE2 GLU A 244     1986   2144    951   -228     -8    -67       O  
ATOM   1905  N   LEU A 245      30.256  48.584  15.649  1.00 12.42           N  
ANISOU 1905  N   LEU A 245     1732   2033    954   -175     10    -57       N  
ATOM   1906  CA  LEU A 245      30.076  48.334  14.202  1.00 13.49           C  
ANISOU 1906  CA  LEU A 245     1860   2125   1141   -180     69    -46       C  
ATOM   1907  C   LEU A 245      31.158  49.041  13.375  1.00 13.85           C  
ANISOU 1907  C   LEU A 245     1892   2165   1205   -136     86    -99       C  
ATOM   1908  O   LEU A 245      31.398  50.243  13.544  1.00 13.81           O  
ANISOU 1908  O   LEU A 245     1988   2115   1143   -197    151    -23       O  
ATOM   1909  CB  LEU A 245      28.670  48.742  13.745  1.00 13.55           C  
ANISOU 1909  CB  LEU A 245     1851   2089   1208   -206    120    -33       C  
ATOM   1910  CG  LEU A 245      27.480  47.924  14.275  1.00 13.74           C  
ANISOU 1910  CG  LEU A 245     1784   2075   1357   -276     97    -59       C  
ATOM   1911  CD1 LEU A 245      26.139  48.562  13.881  1.00 15.76           C  
ANISOU 1911  CD1 LEU A 245     2324   2146   1518   -237    156   -178       C  
ATOM   1912  CD2 LEU A 245      27.568  46.475  13.766  1.00 15.46           C  
ANISOU 1912  CD2 LEU A 245     2293   2127   1453   -418     61   -100       C  
ATOM   1913  N   GLY A 246      31.840  48.283  12.512  1.00 15.05           N  
ANISOU 1913  N   GLY A 246     2050   2281   1384   -143     77   -138       N  
ATOM   1914  CA  GLY A 246      32.901  48.843  11.672  1.00 15.95           C  
ANISOU 1914  CA  GLY A 246     2134   2360   1567    -46    124   -231       C  
ATOM   1915  C   GLY A 246      34.192  49.181  12.398  1.00 16.79           C  
ANISOU 1915  C   GLY A 246     2278   2359   1741      6    109   -240       C  
ATOM   1916  O   GLY A 246      35.135  49.709  11.794  1.00 17.40           O  
ANISOU 1916  O   GLY A 246     2302   2492   1818     46    102   -209       O  
ATOM   1917  N   PHE A 247      34.235  48.872  13.691  1.00 17.53           N  
ANISOU 1917  N   PHE A 247     2387   2386   1885     60     97   -338       N  
ATOM   1918  CA  PHE A 247      35.337  49.268  14.549  1.00 18.22           C  
ANISOU 1918  CA  PHE A 247     2504   2380   2036     46     41   -343       C  
ATOM   1919  C   PHE A 247      36.045  48.018  15.047  1.00 19.63           C  
ANISOU 1919  C   PHE A 247     2716   2513   2227     35      8   -373       C  
ATOM   1920  O   PHE A 247      35.411  47.138  15.618  1.00 18.82           O  
ANISOU 1920  O   PHE A 247     2602   2354   2192      6    -94   -390       O  
ATOM   1921  CB  PHE A 247      34.812  50.100  15.736  1.00 17.60           C  
ANISOU 1921  CB  PHE A 247     2428   2266   1993     57     72   -378       C  
ATOM   1922  CG  PHE A 247      35.826  50.314  16.841  1.00 17.11           C  
ANISOU 1922  CG  PHE A 247     2333   2232   1936    125     65   -374       C  
ATOM   1923  CD1 PHE A 247      37.058  50.939  16.579  1.00 16.80           C  
ANISOU 1923  CD1 PHE A 247     2232   2027   2124    249    -82   -421       C  
ATOM   1924  CD2 PHE A 247      35.536  49.931  18.154  1.00 17.00           C  
ANISOU 1924  CD2 PHE A 247     2447   2039   1973    209    -46   -298       C  
ATOM   1925  CE1 PHE A 247      38.000  51.151  17.606  1.00 16.27           C  
ANISOU 1925  CE1 PHE A 247     2100   2011   2068    210    -77   -467       C  
ATOM   1926  CE2 PHE A 247      36.468  50.150  19.197  1.00 16.31           C  
ANISOU 1926  CE2 PHE A 247     2235   2003   1958     72   -118   -424       C  
ATOM   1927  CZ  PHE A 247      37.702  50.757  18.915  1.00 16.17           C  
ANISOU 1927  CZ  PHE A 247     2167   2045   1931    245   -188   -447       C  
ATOM   1928  N   ALA A 248      37.362  47.970  14.851  1.00 21.63           N  
ANISOU 1928  N   ALA A 248     2970   2746   2501    -19     33   -336       N  
ATOM   1929  CA  ALA A 248      38.187  46.845  15.302  1.00 24.46           C  
ANISOU 1929  CA  ALA A 248     3334   3068   2891    -44     50   -303       C  
ATOM   1930  C   ALA A 248      37.742  45.541  14.622  1.00 26.70           C  
ANISOU 1930  C   ALA A 248     3595   3318   3231    -46     73   -277       C  
ATOM   1931  O   ALA A 248      37.758  44.466  15.235  1.00 26.57           O  
ANISOU 1931  O   ALA A 248     3661   3282   3151    -32     86   -207       O  
ATOM   1932  CB  ALA A 248      38.135  46.728  16.837  1.00 24.28           C  
ANISOU 1932  CB  ALA A 248     3348   3037   2840    -19     31   -320       C  
ATOM   1933  N   ASP A 249      37.354  45.690  13.346  1.00 29.09           N  
ANISOU 1933  N   ASP A 249     3892   3652   3507   -111     67   -265       N  
ATOM   1934  CA  ASP A 249      36.711  44.675  12.469  1.00 31.75           C  
ANISOU 1934  CA  ASP A 249     4186   3912   3965   -131    120   -245       C  
ATOM   1935  C   ASP A 249      35.172  44.534  12.559  1.00 32.90           C  
ANISOU 1935  C   ASP A 249     4333   4067   4097   -159     59   -230       C  
ATOM   1936  O   ASP A 249      34.644  43.836  13.432  1.00 33.24           O  
ANISOU 1936  O   ASP A 249     4344   4110   4173   -158    133   -197       O  
ATOM   1937  CB  ASP A 249      37.426  43.321  12.509  1.00 32.59           C  
ANISOU 1937  CB  ASP A 249     4263   4037   4080   -124    133   -266       C  
ATOM   1938  CG  ASP A 249      38.742  43.342  11.759  1.00 33.92           C  
ANISOU 1938  CG  ASP A 249     4434   4122   4330   -118    181   -337       C  
ATOM   1939  OD1 ASP A 249      39.352  44.431  11.667  1.00 35.08           O  
ANISOU 1939  OD1 ASP A 249     4587   4228   4511    -81    176   -505       O  
ATOM   1940  OD2 ASP A 249      39.166  42.270  11.255  1.00 38.34           O  
ANISOU 1940  OD2 ASP A 249     5060   4558   4947   -160     14   -256       O  
ATOM   1941  N   ALA A 250      34.469  45.236  11.669  1.00 33.88           N  
ANISOU 1941  N   ALA A 250     4475   4223   4174   -190     12   -245       N  
ATOM   1942  CA  ALA A 250      33.121  44.832  11.235  1.00 35.19           C  
ANISOU 1942  CA  ALA A 250     4646   4376   4346   -187    -13   -243       C  
ATOM   1943  C   ALA A 250      32.907  45.156   9.755  1.00 35.73           C  
ANISOU 1943  C   ALA A 250     4727   4450   4397   -206    -38   -267       C  
ATOM   1944  O   ALA A 250      33.611  46.000   9.171  1.00 36.37           O  
ANISOU 1944  O   ALA A 250     4817   4541   4458   -198    -29   -264       O  
ATOM   1945  CB  ALA A 250      31.993  45.441  12.112  1.00 34.32           C  
ANISOU 1945  CB  ALA A 250     4623   4226   4191   -177    -23   -285       C  
ATOM   1946  OXT ALA A 250      32.027  44.561   9.113  1.00 36.65           O  
ANISOU 1946  OXT ALA A 250     4811   4510   4604   -180    -66   -306       O  
TER    1947      ALA A 250                                                      
HETATM 1948 FE   HEM A1251      14.524  54.445  19.011  1.00 13.74          FE  
ANISOU 1948 FE   HEM A1251     1764   2391   1064    210   -278   -167      FE  
HETATM 1949  CHA HEM A1251      13.369  57.471  20.249  1.00 10.17           C  
ANISOU 1949  CHA HEM A1251     1358   1913    593    144   -463   -511       C  
HETATM 1950  CHB HEM A1251      12.386  54.832  16.273  1.00 11.63           C  
ANISOU 1950  CHB HEM A1251     1536   1926    956    217   -227   -542       C  
HETATM 1951  CHC HEM A1251      15.775  51.657  17.645  1.00  9.55           C  
ANISOU 1951  CHC HEM A1251     1170   1918    537    287   -440   -477       C  
HETATM 1952  CHD HEM A1251      16.808  54.285  21.519  1.00 11.66           C  
ANISOU 1952  CHD HEM A1251     1557   2050    822    264   -298   -325       C  
HETATM 1953  NA  HEM A1251      13.147  55.895  18.366  1.00 12.36           N  
ANISOU 1953  NA  HEM A1251     1598   2108    987    192   -279   -647       N  
HETATM 1954  C1A HEM A1251      12.834  57.046  19.045  1.00 12.49           C  
ANISOU 1954  C1A HEM A1251     1541   2073   1129    252   -321   -576       C  
HETATM 1955  C2A HEM A1251      11.838  57.753  18.286  1.00 12.55           C  
ANISOU 1955  C2A HEM A1251     1638   2123   1004    212   -345   -530       C  
HETATM 1956  C3A HEM A1251      11.548  57.042  17.178  1.00 11.81           C  
ANISOU 1956  C3A HEM A1251     1519   2052    914    223   -320   -725       C  
HETATM 1957  C4A HEM A1251      12.367  55.844  17.221  1.00 11.28           C  
ANISOU 1957  C4A HEM A1251     1456   2045    785    274   -368   -515       C  
HETATM 1958  CMA HEM A1251      10.533  57.410  16.066  1.00 12.41           C  
ANISOU 1958  CMA HEM A1251     1481   2246    988    294   -447   -603       C  
HETATM 1959  CAA HEM A1251      11.249  59.107  18.717  1.00 11.99           C  
ANISOU 1959  CAA HEM A1251     1499   1911   1144    252   -224   -611       C  
HETATM 1960  CBA HEM A1251      12.142  60.289  18.354  1.00 11.65           C  
ANISOU 1960  CBA HEM A1251     1305   2017   1103    296   -198   -302       C  
HETATM 1961  CGA HEM A1251      11.440  61.493  18.932  1.00 12.33           C  
ANISOU 1961  CGA HEM A1251     1445   1963   1274    131   -178   -330       C  
HETATM 1962  O1A HEM A1251      10.330  61.818  18.444  1.00 11.83           O  
ANISOU 1962  O1A HEM A1251     1504   1836   1153    126   -231   -152       O  
HETATM 1963  O2A HEM A1251      11.946  62.104  19.916  1.00 12.78           O  
ANISOU 1963  O2A HEM A1251     1327   2216   1311    244   -227   -340       O  
HETATM 1964  NB  HEM A1251      14.189  53.478  17.236  1.00 11.05           N  
ANISOU 1964  NB  HEM A1251     1256   2024    917    273   -367   -418       N  
HETATM 1965  C1B HEM A1251      13.157  53.692  16.338  1.00 11.30           C  
ANISOU 1965  C1B HEM A1251     1502   1940    852    170   -528   -434       C  
HETATM 1966  C2B HEM A1251      13.054  52.533  15.472  1.00 12.09           C  
ANISOU 1966  C2B HEM A1251     1578   2016   1000    181   -637   -290       C  
HETATM 1967  C3B HEM A1251      13.986  51.648  15.852  1.00 12.19           C  
ANISOU 1967  C3B HEM A1251     1466   1974   1192      3   -463   -401       C  
HETATM 1968  C4B HEM A1251      14.707  52.230  16.995  1.00 11.89           C  
ANISOU 1968  C4B HEM A1251     1643   1977    895    142   -335   -466       C  
HETATM 1969  CMB HEM A1251      12.025  52.407  14.329  1.00 12.90           C  
ANISOU 1969  CMB HEM A1251     1677   2176   1046    346   -718   -458       C  
HETATM 1970  CAB HEM A1251      14.264  50.249  15.263  1.00 12.03           C  
ANISOU 1970  CAB HEM A1251     1600   1802   1169    -13   -175   -156       C  
HETATM 1971  CBB HEM A1251      14.280  49.181  16.088  1.00 11.23           C  
ANISOU 1971  CBB HEM A1251     1378   1496   1389   -602     42    -45       C  
HETATM 1972  NC  HEM A1251      16.043  53.196  19.487  1.00 11.32           N  
ANISOU 1972  NC  HEM A1251     1545   1984    773    172   -455   -468       N  
HETATM 1973  C1C HEM A1251      16.445  52.118  18.745  1.00 10.48           C  
ANISOU 1973  C1C HEM A1251     1127   2123    729    398   -156   -307       C  
HETATM 1974  C2C HEM A1251      17.625  51.536  19.354  1.00 11.03           C  
ANISOU 1974  C2C HEM A1251     1329   2090    772    312   -356   -321       C  
HETATM 1975  C3C HEM A1251      17.917  52.275  20.452  1.00 11.21           C  
ANISOU 1975  C3C HEM A1251     1389   2111    758    397   -369   -258       C  
HETATM 1976  C4C HEM A1251      16.909  53.326  20.541  1.00 11.45           C  
ANISOU 1976  C4C HEM A1251     1432   1978    938    245   -490   -324       C  
HETATM 1977  CMC HEM A1251      18.355  50.309  18.780  1.00 11.77           C  
ANISOU 1977  CMC HEM A1251     1731   2010    730    215   -447   -255       C  
HETATM 1978  CAC HEM A1251      19.078  52.123  21.472  1.00  9.25           C  
ANISOU 1978  CAC HEM A1251     1031   1740    742    543   -245   -190       C  
HETATM 1979  CBC HEM A1251      19.507  50.920  21.890  1.00 11.10           C  
ANISOU 1979  CBC HEM A1251     1506   2161    548    802   -169    358       C  
HETATM 1980  ND  HEM A1251      15.040  55.717  20.609  1.00 10.45           N  
ANISOU 1980  ND  HEM A1251     1251   1949    768    319   -376   -295       N  
HETATM 1981  C1D HEM A1251      15.924  55.329  21.609  1.00 11.38           C  
ANISOU 1981  C1D HEM A1251     1556   2064    702     85   -288   -405       C  
HETATM 1982  C2D HEM A1251      15.753  56.193  22.764  1.00 11.39           C  
ANISOU 1982  C2D HEM A1251     1425   1958    943    210   -219   -573       C  
HETATM 1983  C3D HEM A1251      14.683  57.188  22.350  1.00 11.84           C  
ANISOU 1983  C3D HEM A1251     1487   2072    938    150   -433   -484       C  
HETATM 1984  C4D HEM A1251      14.310  56.821  21.001  1.00 11.04           C  
ANISOU 1984  C4D HEM A1251     1510   1988    695    235   -240   -702       C  
HETATM 1985  CMD HEM A1251      16.484  56.116  24.119  1.00 10.01           C  
ANISOU 1985  CMD HEM A1251     1305   1878    617    194   -401   -653       C  
HETATM 1986  CAD HEM A1251      14.093  58.325  23.192  1.00 11.99           C  
ANISOU 1986  CAD HEM A1251     1663   1975    917     58   -172   -594       C  
HETATM 1987  CBD HEM A1251      14.821  59.642  22.933  1.00 12.59           C  
ANISOU 1987  CBD HEM A1251     2146   1746    890    120   -175   -445       C  
HETATM 1988  CGD HEM A1251      14.306  60.695  23.890  1.00 12.19           C  
ANISOU 1988  CGD HEM A1251     2005   1679    948    223   -327   -434       C  
HETATM 1989  O1D HEM A1251      13.716  60.356  24.959  1.00 12.07           O  
ANISOU 1989  O1D HEM A1251     1868   1656   1059    223   -303   -337       O  
HETATM 1990  O2D HEM A1251      14.486  61.890  23.567  1.00 10.66           O  
ANISOU 1990  O2D HEM A1251     1999   1315    736    219   -591   -394       O  
HETATM 1991  C2  ISZ A1252      14.337  56.641  14.006  0.90 24.00           C  
ANISOU 1991  C2  ISZ A1252     2747   4080   2289   -127    -80    238       C  
HETATM 1992  C4  ISZ A1252      15.182  55.740  14.665  0.90 25.24           C  
ANISOU 1992  C4  ISZ A1252     2976   4210   2404   -158      5    184       C  
HETATM 1993  N1  ISZ A1252      15.697  56.043  15.881  0.90 25.27           N  
ANISOU 1993  N1  ISZ A1252     2939   4139   2521   -123   -283    120       N  
HETATM 1994  C5  ISZ A1252      15.434  57.221  16.487  0.90 24.84           C  
ANISOU 1994  C5  ISZ A1252     2643   4233   2563   -130    -88    203       C  
HETATM 1995  C3  ISZ A1252      14.614  58.157  15.854  0.90 24.89           C  
ANISOU 1995  C3  ISZ A1252     2697   4072   2687   -148    -28    100       C  
HETATM 1996  C1  ISZ A1252      14.054  57.874  14.605  0.90 24.58           C  
ANISOU 1996  C1  ISZ A1252     2776   4165   2395   -125   -129    224       C  
HETATM 1997  C6  ISZ A1252      13.157  58.880  13.921  0.90 25.92           C  
ANISOU 1997  C6  ISZ A1252     2954   4241   2653   -157   -226    158       C  
HETATM 1998  O1  ISZ A1252      12.785  59.872  14.537  0.90 27.11           O  
ANISOU 1998  O1  ISZ A1252     3078   4400   2820   -193   -349    238       O  
HETATM 1999  N2  ISZ A1252      12.774  58.672  12.659  0.90 26.23           N  
ANISOU 1999  N2  ISZ A1252     3128   4342   2494    -68   -411    140       N  
HETATM 2000  N3  ISZ A1252      11.965  59.615  11.988  0.90 28.77           N  
ANISOU 2000  N3  ISZ A1252     3397   4742   2790    -59   -461    -22       N  
HETATM 2001  C2  ISZ A1253      17.986  69.868  26.949  0.90 34.94           C  
ANISOU 2001  C2  ISZ A1253     4187   5349   3736    238     54   -710       C  
HETATM 2002  C4  ISZ A1253      18.581  70.874  27.710  0.90 36.04           C  
ANISOU 2002  C4  ISZ A1253     4313   5531   3846    189     88   -675       C  
HETATM 2003  N1  ISZ A1253      18.737  70.720  29.037  0.90 36.04           N  
ANISOU 2003  N1  ISZ A1253     4355   5527   3809    165     59   -562       N  
HETATM 2004  C5  ISZ A1253      18.318  69.607  29.665  0.90 36.55           C  
ANISOU 2004  C5  ISZ A1253     4451   5575   3859    181     -2   -632       C  
HETATM 2005  C3  ISZ A1253      17.720  68.565  28.959  0.90 35.40           C  
ANISOU 2005  C3  ISZ A1253     4352   5367   3731    188     37   -682       C  
HETATM 2006  C1  ISZ A1253      17.550  68.708  27.585  0.90 34.72           C  
ANISOU 2006  C1  ISZ A1253     4186   5329   3677    181    101   -753       C  
HETATM 2007  C6  ISZ A1253      16.908  67.604  26.808  0.90 33.80           C  
ANISOU 2007  C6  ISZ A1253     4133   5227   3481    185    145   -810       C  
HETATM 2008  O1  ISZ A1253      17.225  66.464  27.083  0.50 33.20           O  
ANISOU 2008  O1  ISZ A1253     4101   5093   3421    194    186   -888       O  
HETATM 2009  N2  ISZ A1253      16.023  67.901  25.859  0.90 34.10           N  
ANISOU 2009  N2  ISZ A1253     4253   5215   3486    123    227   -800       N  
HETATM 2010  N3  ISZ A1253      15.153  66.952  25.311  0.90 31.55           N  
ANISOU 2010  N3  ISZ A1253     3954   5003   3028    -91     66  -1002       N  
HETATM 2011  S   SO4 A1254       7.871  45.876   6.242  1.00 42.33           S  
HETATM 2012  O1  SO4 A1254       8.497  46.165   4.955  1.00 41.87           O  
HETATM 2013  O2  SO4 A1254       6.956  44.742   6.122  1.00 42.47           O  
HETATM 2014  O3  SO4 A1254       8.919  45.540   7.201  1.00 39.76           O  
HETATM 2015  O4  SO4 A1254       7.105  47.054   6.660  1.00 40.67           O  
HETATM 2016  O   HOH A2001      36.829  36.495  17.876  1.00 39.83           O  
HETATM 2017  O   HOH A2002      39.847  41.945  20.868  1.00 36.65           O  
HETATM 2018  O   HOH A2003      41.436  44.750  24.423  1.00 41.78           O  
HETATM 2019  O   HOH A2004      42.565  47.307  15.446  1.00 39.30           O  
HETATM 2020  O   HOH A2005      40.401  47.860  24.434  1.00 25.53           O  
HETATM 2021  O   HOH A2006      46.009  46.089  20.238  1.00 41.14           O  
HETATM 2022  O   HOH A2007      41.874  43.251  21.146  1.00 34.97           O  
HETATM 2023  O   HOH A2008      33.982  41.724  21.799  1.00 42.22           O  
HETATM 2024  O   HOH A2009      41.878  63.270  31.174  1.00 25.00           O  
HETATM 2025  O   HOH A2010      41.142  49.669  22.666  1.00 13.99           O  
HETATM 2026  O   HOH A2011      44.015  47.033  22.765  1.00 36.21           O  
HETATM 2027  O   HOH A2012      43.427  54.698  33.345  1.00 31.30           O  
HETATM 2028  O   HOH A2013      46.574  49.962  17.655  1.00 33.45           O  
HETATM 2029  O   HOH A2014      47.306  47.724  18.508  1.00 45.97           O  
HETATM 2030  O   HOH A2015      46.642  52.392  17.979  1.00 34.00           O  
HETATM 2031  O   HOH A2016      45.054  50.331  24.815  1.00 27.66           O  
HETATM 2032  O   HOH A2017      49.128  51.842  25.697  1.00 33.02           O  
HETATM 2033  O   HOH A2018      50.978  55.123  26.988  1.00 22.75           O  
HETATM 2034  O   HOH A2019      46.014  54.961  31.902  1.00 31.86           O  
HETATM 2035  O   HOH A2020      44.364  62.097  29.999  1.00 16.93           O  
HETATM 2036  O   HOH A2021      49.425  62.219  25.935  1.00 22.57           O  
HETATM 2037  O   HOH A2022      49.101  58.797  32.089  1.00 39.98           O  
HETATM 2038  O   HOH A2023      46.568  62.527  31.676  1.00 30.86           O  
HETATM 2039  O   HOH A2024      50.165  58.322  27.601  1.00 19.82           O  
HETATM 2040  O   HOH A2025      51.414  58.662  30.174  1.00 36.53           O  
HETATM 2041  O   HOH A2026      47.315  64.112  27.513  1.00 29.19           O  
HETATM 2042  O   HOH A2027      18.191  60.080  34.975  1.00 24.10           O  
HETATM 2043  O   HOH A2028      19.363  59.333  34.887  1.00 25.70           O  
HETATM 2044  O   HOH A2029      26.207  69.602  34.963  1.00 23.02           O  
HETATM 2045  O   HOH A2030      20.243  71.424  41.853  1.00 36.97           O  
HETATM 2046  O   HOH A2031      41.329  52.539  32.505  1.00 42.05           O  
HETATM 2047  O   HOH A2032      47.189  52.548  31.391  1.00 35.72           O  
HETATM 2048  O   HOH A2033      11.873  62.020  31.082  1.00 33.71           O  
HETATM 2049  O   HOH A2034      41.259  59.092  34.940  1.00 19.50           O  
HETATM 2050  O   HOH A2035      35.591  55.632  35.382  1.00 27.58           O  
HETATM 2051  O   HOH A2036      33.873  63.439  37.453  1.00 36.32           O  
HETATM 2052  O   HOH A2037      33.345  51.497  31.054  1.00 31.43           O  
HETATM 2053  O   HOH A2038      38.830  59.291  36.837  1.00 25.58           O  
HETATM 2054  O   HOH A2039      29.936  66.172  35.178  1.00 20.61           O  
HETATM 2055  O   HOH A2040      33.171  68.651  37.283  1.00 31.26           O  
HETATM 2056  O   HOH A2041      29.519  67.201   6.767  1.00 34.37           O  
HETATM 2057  O   HOH A2042      23.230  71.582  13.541  1.00 33.04           O  
HETATM 2058  O   HOH A2043      19.354  61.090  32.666  1.00 12.04           O  
HETATM 2059  O   HOH A2044      25.303  71.230  15.755  1.00 35.13           O  
HETATM 2060  O   HOH A2045      26.905  72.030  19.307  1.00 32.66           O  
HETATM 2061  O   HOH A2046      17.925  62.185  35.897  1.00 28.58           O  
HETATM 2062  O   HOH A2047      24.121  68.366  34.050  1.00 29.32           O  
HETATM 2063  O   HOH A2048      18.145  69.553  34.816  1.00 45.29           O  
HETATM 2064  O   HOH A2049      21.557  70.853  39.582  1.00 26.47           O  
HETATM 2065  O   HOH A2050      27.581  71.861  30.592  1.00 24.31           O  
HETATM 2066  O   HOH A2051      29.351  69.974  31.322  1.00 27.25           O  
HETATM 2067  O   HOH A2052      21.654  71.687  34.199  1.00 35.04           O  
HETATM 2068  O   HOH A2053      23.724  72.183  29.729  1.00 29.29           O  
HETATM 2069  O   HOH A2054      16.614  68.479  32.314  1.00 39.18           O  
HETATM 2070  O   HOH A2055      26.271  71.998  33.182  1.00 30.29           O  
HETATM 2071  O   HOH A2056      32.420  75.515  28.345  1.00 21.20           O  
HETATM 2072  O   HOH A2057      17.788  63.941  37.470  0.50 39.48           O  
HETATM 2073  O   HOH A2058      13.980  64.084  31.064  1.00 34.83           O  
HETATM 2074  O   HOH A2059      14.428  62.200  29.284  1.00 34.99           O  
HETATM 2075  O   HOH A2060      12.309  67.013  37.613  1.00 41.58           O  
HETATM 2076  O   HOH A2061      44.630  64.065  28.095  1.00 20.56           O  
HETATM 2077  O   HOH A2062      41.409  59.652  18.016  1.00 24.62           O  
HETATM 2078  O   HOH A2063      41.705  58.633  17.671  1.00 27.79           O  
HETATM 2079  O   HOH A2064      16.352  62.782  27.302  1.00 23.17           O  
HETATM 2080  O   HOH A2065      32.257  48.190  32.254  1.00 35.83           O  
HETATM 2081  O   HOH A2066      25.270  41.970  31.209  1.00 37.81           O  
HETATM 2082  O   HOH A2067      23.678  43.077  33.727  1.00 33.46           O  
HETATM 2083  O   HOH A2068      29.044  59.539  16.043  1.00 15.50           O  
HETATM 2084  O   HOH A2069      22.599  50.846   8.575  1.00 17.19           O  
HETATM 2085  O   HOH A2070      26.579  57.767  11.534  1.00 17.32           O  
HETATM 2086  O   HOH A2071      22.572  50.425   3.647  1.00 41.57           O  
HETATM 2087  O   HOH A2072      22.277  47.090   2.859  1.00 38.71           O  
HETATM 2088  O   HOH A2073      26.058  47.358   0.835  1.00 27.28           O  
HETATM 2089  O   HOH A2074      20.236  50.304   4.617  1.00 26.12           O  
HETATM 2090  O   HOH A2075      32.588  44.598   3.241  1.00 37.66           O  
HETATM 2091  O   HOH A2076      34.407  52.200   2.875  1.00 34.12           O  
HETATM 2092  O   HOH A2077      37.230  44.781   7.976  1.00 39.66           O  
HETATM 2093  O   HOH A2078      36.284  42.241   5.232  1.00 49.17           O  
HETATM 2094  O   HOH A2079      12.376  33.601   7.195  1.00 25.70           O  
HETATM 2095  O   HOH A2080      32.763  53.798   8.516  1.00 35.81           O  
HETATM 2096  O   HOH A2081      30.808  56.731   5.666  1.00 34.24           O  
HETATM 2097  O   HOH A2082      29.659  57.448  10.217  1.00 16.15           O  
HETATM 2098  O   HOH A2083      28.716  58.552  13.576  1.00 14.88           O  
HETATM 2099  O   HOH A2084      16.233  35.786   8.661  1.00 32.98           O  
HETATM 2100  O   HOH A2085      28.523  70.454  15.345  1.00 35.21           O  
HETATM 2101  O   HOH A2086       8.406  61.117  29.087  1.00 27.10           O  
HETATM 2102  O   HOH A2087      21.612  70.338  11.180  1.00 34.45           O  
HETATM 2103  O   HOH A2088       6.845  62.507  27.182  1.00 30.77           O  
HETATM 2104  O   HOH A2089      28.073  69.554   7.604  1.00 34.62           O  
HETATM 2105  O   HOH A2090      21.467  66.660   5.293  1.00 32.13           O  
HETATM 2106  O   HOH A2091      22.662  59.149  11.706  1.00 16.30           O  
HETATM 2107  O   HOH A2092      17.040  66.907  11.725  1.00 33.18           O  
HETATM 2108  O   HOH A2093      19.544  69.861  13.030  1.00 28.62           O  
HETATM 2109  O   HOH A2094      16.701  65.864   5.720  1.00 45.46           O  
HETATM 2110  O   HOH A2095      24.617  62.744   4.714  1.00 32.52           O  
HETATM 2111  O   HOH A2096      21.155  58.844   9.298  1.00 19.12           O  
HETATM 2112  O   HOH A2097       6.623  60.590  31.085  1.00 31.73           O  
HETATM 2113  O   HOH A2098      12.473  60.203   9.299  1.00 39.13           O  
HETATM 2114  O   HOH A2099      17.720  59.250  15.437  1.00 16.21           O  
HETATM 2115  O   HOH A2100       0.008  40.856  30.525  0.50 26.65           O  
HETATM 2116  O   HOH A2101       4.672  40.443  30.761  1.00 34.29           O  
HETATM 2117  O   HOH A2102      12.858  69.250  16.101  1.00 33.38           O  
HETATM 2118  O   HOH A2103      16.736  69.069  14.974  1.00 31.94           O  
HETATM 2119  O   HOH A2104       4.124  61.414  30.212  1.00 39.65           O  
HETATM 2120  O   HOH A2105      19.176  67.606  14.779  1.00 23.73           O  
HETATM 2121  O   HOH A2106      24.243  71.106  18.084  1.00 25.46           O  
HETATM 2122  O   HOH A2107      16.083  70.463  17.846  1.00 27.67           O  
HETATM 2123  O   HOH A2108       3.639  44.403  11.929  1.00 29.44           O  
HETATM 2124  O   HOH A2109      18.667  74.090  26.945  1.00 50.52           O  
HETATM 2125  O   HOH A2110      20.373  72.928  19.978  1.00 37.65           O  
HETATM 2126  O   HOH A2111      16.867  72.777  23.214  1.00 32.31           O  
HETATM 2127  O   HOH A2112      25.698  72.987  26.195  1.00 16.21           O  
HETATM 2128  O   HOH A2113      18.521  76.071  24.259  1.00 33.93           O  
HETATM 2129  O   HOH A2114      23.127  73.600  25.973  1.00 31.41           O  
HETATM 2130  O   HOH A2115      17.160  34.411  18.162  1.00 34.10           O  
HETATM 2131  O   HOH A2116      28.697  69.218  28.538  1.00 24.34           O  
HETATM 2132  O   HOH A2117      25.954  71.465  28.404  1.00 17.79           O  
HETATM 2133  O   HOH A2118      34.863  70.283  22.182  1.00 37.87           O  
HETATM 2134  O   HOH A2119      28.876  71.151  18.033  1.00 38.28           O  
HETATM 2135  O   HOH A2120       5.455  37.838  30.906  1.00 37.40           O  
HETATM 2136  O   HOH A2121      34.217  73.204  28.339  1.00 19.75           O  
HETATM 2137  O   HOH A2122      13.587  40.206  37.630  1.00 34.00           O  
HETATM 2138  O   HOH A2123      37.189  68.339  21.487  1.00 29.50           O  
HETATM 2139  O   HOH A2124      40.274  71.290  27.617  1.00 37.08           O  
HETATM 2140  O   HOH A2125      28.129  41.967  28.331  1.00 25.62           O  
HETATM 2141  O   HOH A2126      21.474  35.231  30.586  1.00 35.88           O  
HETATM 2142  O   HOH A2127      37.473  67.459  33.418  1.00 37.32           O  
HETATM 2143  O   HOH A2128      31.723  71.130  31.106  1.00 37.03           O  
HETATM 2144  O   HOH A2129      39.382  66.943  31.924  1.00 33.14           O  
HETATM 2145  O   HOH A2130      41.423  65.475  29.442  1.00 36.72           O  
HETATM 2146  O   HOH A2131      42.218  65.947  19.390  1.00 19.74           O  
HETATM 2147  O   HOH A2132      42.391  65.435  26.878  1.00 16.65           O  
HETATM 2148  O   HOH A2133      42.674  61.154  19.616  1.00 12.85           O  
HETATM 2149  O   HOH A2134      38.963  65.366  19.597  1.00 33.79           O  
HETATM 2150  O   HOH A2135      32.075  69.694  16.757  1.00 36.88           O  
HETATM 2151  O   HOH A2136      29.976  57.447  17.805  1.00 14.90           O  
HETATM 2152  O   HOH A2137      29.253  67.289  21.144  1.00 14.94           O  
HETATM 2153  O   HOH A2138      27.010  53.631  23.057  1.00 11.81           O  
HETATM 2154  O   HOH A2139      30.850  50.651  34.886  1.00 29.68           O  
HETATM 2155  O   HOH A2140      28.775  51.000  32.119  1.00 19.39           O  
HETATM 2156  O   HOH A2141      26.338  55.122  37.421  0.50 26.88           O  
HETATM 2157  O   HOH A2142      16.919  51.244  37.543  1.00 31.10           O  
HETATM 2158  O   HOH A2143      23.414  50.283  36.303  1.00 13.87           O  
HETATM 2159  O   HOH A2144      26.399  50.626  30.532  1.00 11.96           O  
HETATM 2160  O   HOH A2145      27.441  43.543  30.902  1.00 27.24           O  
HETATM 2161  O   HOH A2147      26.077  44.489  34.160  1.00 42.35           O  
HETATM 2162  O   HOH A2148      31.581  47.395  37.772  1.00 43.95           O  
HETATM 2163  O   HOH A2149      28.981  47.387  39.419  1.00 29.85           O  
HETATM 2164  O   HOH A2150      30.694  45.276  31.756  1.00 25.03           O  
HETATM 2165  O   HOH A2151      31.006  50.101  30.822  1.00 19.90           O  
HETATM 2166  O   HOH A2152      36.795  47.119  28.288  1.00 32.69           O  
HETATM 2167  O   HOH A2153      37.277  51.228  28.710  1.00 22.20           O  
HETATM 2168  O   HOH A2154      34.328  48.355  29.861  1.00 24.84           O  
HETATM 2169  O   HOH A2155      37.115  43.865  27.157  1.00 37.02           O  
HETATM 2170  O   HOH A2156      40.370  52.545  15.081  1.00 28.69           O  
HETATM 2171  O   HOH A2157      40.447  57.085  19.201  1.00 12.52           O  
HETATM 2172  O   HOH A2158      33.184  49.646  22.865  1.00 17.17           O  
HETATM 2173  O   HOH A2159      38.105  53.885  13.763  1.00 19.35           O  
HETATM 2174  O   HOH A2160      45.236  55.904  12.437  1.00 28.70           O  
HETATM 2175  O   HOH A2161      39.175  63.021  16.905  1.00 24.30           O  
HETATM 2176  O   HOH A2162      40.220  60.447  15.712  1.00 16.91           O  
HETATM 2177  O   HOH A2163      34.054  63.059  12.329  1.00 33.22           O  
HETATM 2178  O   HOH A2164      34.549  51.172   9.467  1.00 38.20           O  
HETATM 2179  O   HOH A2165      36.679  62.330   2.582  1.00 45.13           O  
HETATM 2180  O   HOH A2166      35.087  58.098   5.861  1.00 41.63           O  
HETATM 2181  O   HOH A2167      29.531  59.532   2.532  1.00 36.03           O  
HETATM 2182  O   HOH A2168      21.646  57.125   7.129  1.00 18.43           O  
HETATM 2183  O   HOH A2169      16.545  60.227   7.789  1.00 29.54           O  
HETATM 2184  O   HOH A2170      22.549  62.307   2.478  1.00 36.00           O  
HETATM 2185  O   HOH A2171      20.077  55.214   2.380  1.00 32.16           O  
HETATM 2186  O   HOH A2172      20.625  64.165   3.281  1.00 37.79           O  
HETATM 2187  O   HOH A2173      20.301  59.408   0.576  1.00 37.78           O  
HETATM 2188  O   HOH A2174      18.614  58.219   8.092  1.00 26.84           O  
HETATM 2189  O   HOH A2175      18.715  52.243   3.427  1.00 35.78           O  
HETATM 2190  O   HOH A2176      20.218  50.475   7.150  1.00 14.77           O  
HETATM 2191  O   HOH A2177      15.843  56.883   8.115  1.00 28.69           O  
HETATM 2192  O   HOH A2178      15.535  52.937   6.471  1.00 32.21           O  
HETATM 2193  O   HOH A2179       8.628  57.214   9.066  1.00 29.53           O  
HETATM 2194  O   HOH A2180      10.610  56.703  11.222  1.00 29.58           O  
HETATM 2195  O   HOH A2181       2.401  51.787  10.007  1.00 28.16           O  
HETATM 2196  O   HOH A2182       4.378  48.170  10.164  1.00 36.22           O  
HETATM 2197  O   HOH A2183       5.589  52.776   5.938  1.00 34.10           O  
HETATM 2198  O   HOH A2184       9.308  53.023   1.292  1.00 40.88           O  
HETATM 2199  O   HOH A2185       6.001  43.037  10.459  1.00 24.74           O  
HETATM 2200  O   HOH A2186      11.631  39.373   7.631  1.00 34.37           O  
HETATM 2201  O   HOH A2187      14.393  41.320   5.359  1.00 38.45           O  
HETATM 2202  O   HOH A2188      12.589  35.194   9.568  1.00 22.62           O  
HETATM 2203  O   HOH A2189      19.659  47.368   3.976  1.00 29.06           O  
HETATM 2204  O   HOH A2190      13.430  47.914   4.039  1.00 26.91           O  
HETATM 2205  O   HOH A2191      25.470  45.590   3.729  1.00 22.60           O  
HETATM 2206  O   HOH A2192      28.537  43.968  11.410  1.00 26.37           O  
HETATM 2207  O   HOH A2193      26.291  39.821  14.495  1.00 20.47           O  
HETATM 2208  O   HOH A2194      23.166  39.527  10.611  1.00 28.84           O  
HETATM 2209  O   HOH A2195      22.780  36.880  18.720  1.00 30.01           O  
HETATM 2210  O   HOH A2196      17.521  37.491  10.144  1.00 33.54           O  
HETATM 2211  O   HOH A2197      15.097  34.714  10.909  1.00 30.85           O  
HETATM 2212  O   HOH A2198      18.948  40.180  11.642  1.00 27.17           O  
HETATM 2213  O   HOH A2199      22.086  34.719  20.215  1.00 37.44           O  
HETATM 2214  O   HOH A2200      18.269  33.994  21.034  1.00 28.03           O  
HETATM 2215  O   HOH A2201      19.387  35.712  16.739  1.00 20.37           O  
HETATM 2216  O   HOH A2202      21.790  40.209  21.923  1.00 18.16           O  
HETATM 2217  O   HOH A2203      11.549  47.587  17.041  1.00 15.46           O  
HETATM 2218  O   HOH A2204      10.067  54.821  27.854  1.00 12.83           O  
HETATM 2219  O   HOH A2205      11.041  60.845  28.405  1.00 30.13           O  
HETATM 2220  O   HOH A2206       7.275  63.504  24.774  1.00 17.98           O  
HETATM 2221  O   HOH A2207       2.239  70.966  22.882  1.00 33.77           O  
HETATM 2222  O   HOH A2208       5.571  69.650  21.131  1.00 35.14           O  
HETATM 2223  O   HOH A2209      10.128  69.699  13.260  1.00 43.77           O  
HETATM 2224  O   HOH A2210       9.107  68.431  23.829  1.00 34.82           O  
HETATM 2225  O   HOH A2211      12.374  69.447  20.501  1.00 26.70           O  
HETATM 2226  O   HOH A2212      13.662  69.081  18.613  1.00 33.69           O  
HETATM 2227  O   HOH A2213      11.030  63.332  11.841  1.00 32.41           O  
HETATM 2228  O   HOH A2214       1.474  58.004  23.971  1.00 39.49           O  
HETATM 2229  O   HOH A2215       2.437  58.884  19.044  1.00 20.34           O  
HETATM 2230  O   HOH A2216       1.515  59.413  19.574  1.00 29.72           O  
HETATM 2231  O   HOH A2217       3.199  63.014  25.890  1.00 34.57           O  
HETATM 2232  O   HOH A2218       6.632  66.707  22.558  1.00 25.34           O  
HETATM 2233  O   HOH A2219       4.599  50.995  25.446  1.00 15.38           O  
HETATM 2234  O   HOH A2220       5.442  57.605  31.680  1.00 19.55           O  
HETATM 2235  O   HOH A2221       1.913  55.515  33.032  1.00 32.18           O  
HETATM 2236  O   HOH A2222       2.431  50.803  33.461  1.00 31.73           O  
HETATM 2237  O   HOH A2223       7.679  50.533  34.289  1.00 37.76           O  
HETATM 2238  O   HOH A2224      11.106  51.537  31.998  1.00 17.01           O  
HETATM 2239  O   HOH A2225      10.897  51.709  38.621  1.00 35.10           O  
HETATM 2240  O   HOH A2226      10.610  56.356  37.721  1.00 22.61           O  
HETATM 2241  O   HOH A2227       5.952  51.411  37.428  1.00 46.67           O  
HETATM 2242  O   HOH A2228      16.795  57.916  36.250  1.00 29.96           O  
HETATM 2243  O   HOH A2229      11.264  57.402  35.216  1.00 14.02           O  
HETATM 2244  O   HOH A2230      17.823  57.603  35.969  1.00 14.99           O  
HETATM 2245  O   HOH A2231      16.633  48.859  36.467  1.00 28.18           O  
HETATM 2246  O   HOH A2232       6.288  49.119  24.340  1.00 32.48           O  
HETATM 2247  O   HOH A2233       2.750  42.129  30.350  1.00 37.14           O  
HETATM 2248  O   HOH A2234       8.257  45.086  33.820  1.00 29.72           O  
HETATM 2249  O   HOH A2235       0.673  47.418  31.176  1.00 32.15           O  
HETATM 2250  O   HOH A2236       5.935  50.728  32.297  1.00 23.60           O  
HETATM 2251  O   HOH A2237       0.947  48.909  27.960  1.00 23.78           O  
HETATM 2252  O   HOH A2238      -0.103  41.348  23.527  0.50 19.90           O  
HETATM 2253  O   HOH A2239      -4.407  46.085  27.000  1.00 36.78           O  
HETATM 2254  O   HOH A2240      -2.722  48.292  29.751  1.00 47.76           O  
HETATM 2255  O   HOH A2241       0.200  52.038  24.652  1.00 33.96           O  
HETATM 2256  O   HOH A2242      -5.197  52.116  31.144  1.00 41.55           O  
HETATM 2257  O   HOH A2243       2.627  58.110  30.555  1.00 35.40           O  
HETATM 2258  O   HOH A2244       2.064  54.233  16.943  1.00 26.30           O  
HETATM 2259  O   HOH A2245       0.113  45.993  20.424  1.00 37.17           O  
HETATM 2260  O   HOH A2246       1.975  50.332  25.636  1.00 24.40           O  
HETATM 2261  O   HOH A2247       0.839  53.992  20.617  1.00 27.53           O  
HETATM 2262  O   HOH A2248       3.831  46.955  12.512  1.00 25.91           O  
HETATM 2263  O   HOH A2249      10.976  50.224  17.404  1.00 17.06           O  
HETATM 2264  O   HOH A2250       1.883  43.154  16.313  1.00 30.47           O  
HETATM 2265  O   HOH A2251       3.637  35.956  17.324  1.00 32.84           O  
HETATM 2266  O   HOH A2252       4.315  34.273  15.200  1.00 35.08           O  
HETATM 2267  O   HOH A2253       6.185  40.886  12.415  1.00 27.97           O  
HETATM 2268  O   HOH A2254       7.306  38.526  10.504  1.00 27.85           O  
HETATM 2269  O   HOH A2255      10.312  35.324  11.101  1.00 19.67           O  
HETATM 2270  O   HOH A2256       7.364  31.715  17.404  1.00 24.72           O  
HETATM 2271  O   HOH A2257      13.969  33.699  18.889  1.00 24.23           O  
HETATM 2272  O   HOH A2258      -0.097  37.727  22.325  1.00 45.80           O  
HETATM 2273  O   HOH A2259      10.485  32.596  24.965  1.00 31.76           O  
HETATM 2274  O   HOH A2260       6.530  32.887  22.163  1.00 32.08           O  
HETATM 2275  O   HOH A2261       4.047  34.459  22.669  1.00 28.07           O  
HETATM 2276  O   HOH A2262       6.730  36.313  29.072  1.00 20.97           O  
HETATM 2277  O   HOH A2263      12.979  34.739  35.366  1.00 46.50           O  
HETATM 2278  O   HOH A2264      18.495  34.988  33.240  1.00 38.63           O  
HETATM 2279  O   HOH A2265      15.091  33.147  30.064  1.00 26.65           O  
HETATM 2280  O   HOH A2266      15.545  46.671  37.204  1.00 38.98           O  
HETATM 2281  O   HOH A2267      17.804  44.184  36.652  1.00 33.74           O  
HETATM 2282  O   HOH A2268      12.374  39.491  35.640  1.00 30.21           O  
HETATM 2283  O   HOH A2269      20.682  39.360  38.878  1.00 38.36           O  
HETATM 2284  O   HOH A2270      19.436  42.195  35.785  1.00 37.51           O  
HETATM 2285  O   HOH A2271      22.157  39.522  33.208  1.00 23.61           O  
HETATM 2286  O   HOH A2272      20.628  36.083  32.508  1.00 35.83           O  
HETATM 2287  O   HOH A2273      26.067  40.048  28.184  1.00 20.17           O  
HETATM 2288  O   HOH A2274      21.000  34.940  24.522  1.00 35.24           O  
HETATM 2289  O   HOH A2275      20.127  36.122  28.132  1.00 40.93           O  
HETATM 2290  O   HOH A2276      23.600  37.356  26.317  1.00 30.07           O  
HETATM 2291  O   HOH A2277      24.251  38.769  19.742  1.00 30.31           O  
HETATM 2292  O   HOH A2278      23.399  35.792  23.467  1.00 31.79           O  
HETATM 2293  O   HOH A2279      28.985  41.780  22.319  1.00 28.25           O  
HETATM 2294  O   HOH A2280      32.198  41.229  25.869  1.00 35.08           O  
HETATM 2295  O   HOH A2281      34.757  42.780  25.879  1.00 32.94           O  
HETATM 2296  O   HOH A2282      28.579  42.780  25.874  1.00 28.49           O  
HETATM 2297  O   HOH A2283      27.085  37.473  17.691  1.00 33.02           O  
HETATM 2298  O   HOH A2284      30.450  45.101  16.402  1.00 14.72           O  
HETATM 2299  O   HOH A2285      30.771  50.109  24.048  1.00 13.09           O  
HETATM 2300  O   HOH A2286      31.342  43.933  19.234  1.00 23.42           O  
HETATM 2301  O   HOH A2287      37.090  51.733  12.158  1.00 35.46           O  
HETATM 2302  O   HOH A2288      41.018  41.611  13.079  0.50 27.65           O  
HETATM 2303  O   HOH A2289      32.819  41.309  14.713  1.00 43.93           O  
HETATM 2304  O   HOH A2290      37.330  47.700  11.365  1.00 27.50           O  
HETATM 2305  O   HOH A2291      34.870  48.742   8.901  1.00 36.76           O  
HETATM 2306  O   HOH A2292      12.995  61.718  26.990  1.00 21.90           O  
HETATM 2307  O   HOH A2293      14.619  64.045  25.018  1.00 15.55           O  
HETATM 2308  O   HOH A2294      14.381  62.587  20.998  1.00 12.77           O  
HETATM 2309  O   HOH A2295      15.804  55.873  17.599  0.10 18.07           O  
HETATM 2310  O   HOH A2296      13.179  62.453  14.453  1.00 25.18           O  
HETATM 2311  O   HOH A2297      16.453  64.873  27.352  1.00 43.53           O  
HETATM 2312  O   HOH A2298      15.296  70.255  25.024  1.00 36.49           O  
HETATM 2313  O   HOH A2299       7.051  42.711   7.666  1.00 28.37           O  
HETATM 2314  O   HOH A2300      10.580  46.700   3.970  1.00 43.75           O  
CONECT 1255 1948                                                                
CONECT 1948 1255 1964 1972 2309                                                 
CONECT 1949 1954 1984                                                           
CONECT 1950 1957 1965                                                           
CONECT 1951 1968 1973                                                           
CONECT 1952 1976 1981                                                           
CONECT 1953 1954 1957                                                           
CONECT 1954 1949 1953 1955                                                      
CONECT 1955 1954 1956 1959                                                      
CONECT 1956 1955 1957 1958                                                      
CONECT 1957 1950 1953 1956                                                      
CONECT 1958 1956                                                                
CONECT 1959 1955 1960                                                           
CONECT 1960 1959 1961                                                           
CONECT 1961 1960 1962 1963                                                      
CONECT 1962 1961                                                                
CONECT 1963 1961                                                                
CONECT 1964 1948 1965 1968                                                      
CONECT 1965 1950 1964 1966                                                      
CONECT 1966 1965 1967 1969                                                      
CONECT 1967 1966 1968 1970                                                      
CONECT 1968 1951 1964 1967                                                      
CONECT 1969 1966                                                                
CONECT 1970 1967 1971                                                           
CONECT 1971 1970                                                                
CONECT 1972 1948 1973 1976                                                      
CONECT 1973 1951 1972 1974                                                      
CONECT 1974 1973 1975 1977                                                      
CONECT 1975 1974 1976 1978                                                      
CONECT 1976 1952 1972 1975                                                      
CONECT 1977 1974                                                                
CONECT 1978 1975 1979                                                           
CONECT 1979 1978                                                                
CONECT 1980 1981 1984                                                           
CONECT 1981 1952 1980 1982                                                      
CONECT 1982 1981 1983 1985                                                      
CONECT 1983 1982 1984 1986                                                      
CONECT 1984 1949 1980 1983                                                      
CONECT 1985 1982                                                                
CONECT 1986 1983 1987                                                           
CONECT 1987 1986 1988                                                           
CONECT 1988 1987 1989 1990                                                      
CONECT 1989 1988                                                                
CONECT 1990 1988                                                                
CONECT 1991 1992 1996                                                           
CONECT 1992 1991 1993                                                           
CONECT 1993 1992 1994                                                           
CONECT 1994 1993 1995                                                           
CONECT 1995 1994 1996                                                           
CONECT 1996 1991 1995 1997                                                      
CONECT 1997 1996 1998 1999                                                      
CONECT 1998 1997                                                                
CONECT 1999 1997 2000                                                           
CONECT 2000 1999                                                                
CONECT 2001 2002 2006                                                           
CONECT 2002 2001 2003                                                           
CONECT 2003 2002 2004                                                           
CONECT 2004 2003 2005                                                           
CONECT 2005 2004 2006                                                           
CONECT 2006 2001 2005 2007                                                      
CONECT 2007 2006 2008 2009                                                      
CONECT 2008 2007                                                                
CONECT 2009 2007 2010                                                           
CONECT 2010 2009                                                                
CONECT 2011 2012 2013 2014 2015                                                 
CONECT 2012 2011                                                                
CONECT 2013 2011                                                                
CONECT 2014 2011                                                                
CONECT 2015 2011                                                                
CONECT 2309 1948                                                                
MASTER      409    0    4   14    2    0   13    6 2313    1   70   21          
END